data_6SPI
# 
_entry.id   6SPI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.322 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6SPI         
WWPDB D_1292104079 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6SPI 
_pdbx_database_status.recvd_initial_deposition_date   2019-09-01 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chantadul, V.'   1 0000-0001-8257-4582 
'Amporndanai, K.' 2 0000-0001-8527-9394 
'Wright, G.'      3 0000-0002-3756-9634 
'Antonyuk, S.'    4 0000-0002-2779-9946 
'Hasnain, S.'     5 0000-0002-2854-4718 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            3 
_citation.language                  ? 
_citation.page_first                97 
_citation.page_last                 97 
_citation.title                     'Ebselen as template for stabilization of A4V mutant dimer for motor neuron disease therapy.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-020-0826-3 
_citation.pdbx_database_id_PubMed   32139772 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chantadul, V.'   1  ?                   
primary 'Wright, G.S.A.'  2  0000-0002-3756-9634 
primary 'Amporndanai, K.' 3  ?                   
primary 'Shahid, M.'      4  ?                   
primary 'Antonyuk, S.V.'  5  0000-0002-2779-9946 
primary 'Washbourn, G.'   6  ?                   
primary 'Rogers, M.'      7  ?                   
primary 'Roberts, N.'     8  ?                   
primary 'Pye, M.'         9  ?                   
primary 
;O'Neill, P.M.
;
10 ?                   
primary 'Hasnain, S.S.'   11 0000-0002-2854-4718 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.440 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6SPI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.526 
_cell.length_a_esd                 ? 
_cell.length_b                     194.671 
_cell.length_b_esd                 ? 
_cell.length_c                     146.526 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         6SPI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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]'                      15986.812 12  1.15.1.1 A4V ? ? 
2 non-polymer syn '~{N}-[(4-chlorophenyl)methyl]-2-selanyl-benzamide' 324.664   12  ?        ?   ? ? 
3 non-polymer syn 'ZINC ION'                                          65.409    12  ?        ?   ? ? 
4 non-polymer syn 'SULFATE ION'                                       96.063    18  ?        ?   ? ? 
5 water       nat water                                               18.015    230 ?        ?   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MATKVVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKVVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J,K,L 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   VAL n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 CYS n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   154 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET303C 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           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 6SPI A 1 ? 154 ? P00441 1 ? 154 ? 0 153 
2  1 6SPI B 1 ? 154 ? P00441 1 ? 154 ? 0 153 
3  1 6SPI C 1 ? 154 ? P00441 1 ? 154 ? 0 153 
4  1 6SPI D 1 ? 154 ? P00441 1 ? 154 ? 0 153 
5  1 6SPI E 1 ? 154 ? P00441 1 ? 154 ? 0 153 
6  1 6SPI F 1 ? 154 ? P00441 1 ? 154 ? 0 153 
7  1 6SPI G 1 ? 154 ? P00441 1 ? 154 ? 0 153 
8  1 6SPI H 1 ? 154 ? P00441 1 ? 154 ? 0 153 
9  1 6SPI I 1 ? 154 ? P00441 1 ? 154 ? 0 153 
10 1 6SPI J 1 ? 154 ? P00441 1 ? 154 ? 0 153 
11 1 6SPI K 1 ? 154 ? P00441 1 ? 154 ? 0 153 
12 1 6SPI L 1 ? 154 ? P00441 1 ? 154 ? 0 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1  6SPI VAL A 5 ? UNP P00441 ALA 5 'engineered mutation' 4 1  
2  6SPI VAL B 5 ? UNP P00441 ALA 5 'engineered mutation' 4 2  
3  6SPI VAL C 5 ? UNP P00441 ALA 5 'engineered mutation' 4 3  
4  6SPI VAL D 5 ? UNP P00441 ALA 5 'engineered mutation' 4 4  
5  6SPI VAL E 5 ? UNP P00441 ALA 5 'engineered mutation' 4 5  
6  6SPI VAL F 5 ? UNP P00441 ALA 5 'engineered mutation' 4 6  
7  6SPI VAL G 5 ? UNP P00441 ALA 5 'engineered mutation' 4 7  
8  6SPI VAL H 5 ? UNP P00441 ALA 5 'engineered mutation' 4 8  
9  6SPI VAL I 5 ? UNP P00441 ALA 5 'engineered mutation' 4 9  
10 6SPI VAL J 5 ? UNP P00441 ALA 5 'engineered mutation' 4 10 
11 6SPI VAL K 5 ? UNP P00441 ALA 5 'engineered mutation' 4 11 
12 6SPI VAL L 5 ? UNP P00441 ALA 5 'engineered mutation' 4 12 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                             ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                            ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                          ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                     ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                            ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                           ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                     ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                             ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                           ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                               ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                          ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                             ? 'C6 H13 N O2'       131.173 
LQW non-polymer         . '~{N}-[(4-chlorophenyl)methyl]-2-selanyl-benzamide' ? 'C14 H12 Cl N O Se' 324.664 
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 
SO4 non-polymer         . 'SULFATE ION'                                       ? 'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE                                           ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                          ? 'C11 H12 N2 O2'     204.225 
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                   6SPI 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            4.25 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         71.06 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 7.8, 2.6 M ammonium sulphate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-06-29 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double crystal InSb(111) and InSb(220)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            25.1 
_reflns.entry_id                         6SPI 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.800 
_reflns.d_resolution_low                 58.540 
_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                       77624 
_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             99.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.100 
_reflns.pdbx_Rmerge_I_obs                0.202 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            3.700 
_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                  0.245 
_reflns.pdbx_Rpim_I_all                  0.136 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.965 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.800 
_reflns_shell.d_res_low                   2.860 
_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           4567 
_reflns_shell.percent_possible_all        99.700 
_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                0.724 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             3.000 
_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             0.890 
_reflns_shell.pdbx_Rpim_I_all             0.510 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.538 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            -2.9900 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -1.6000 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            4.5500 
_refine.B_iso_max                                136.490 
_refine.B_iso_mean                               32.7090 
_refine.B_iso_min                                2.570 
_refine.correlation_coeff_Fo_to_Fc               0.9200 
_refine.correlation_coeff_Fo_to_Fc_free          0.9030 
_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                                 6SPI 
_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                            2.8000 
_refine.ls_d_res_low                             58.540 
_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                     73673 
_refine.ls_number_reflns_R_free                  3867 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.5000 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2146 
_refine.ls_R_factor_R_free                       0.2411 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2132 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1UXM 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.5350 
_refine.pdbx_overall_ESU_R_Free                  0.2990 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             14.7590 
_refine.overall_SU_ML                            0.2660 
_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                       2.8000 
_refine_hist.d_res_low                        58.540 
_refine_hist.number_atoms_solvent             230 
_refine_hist.number_atoms_total               13892 
_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       1836 
_refine_hist.pdbx_B_iso_mean_ligand           83.23 
_refine_hist.pdbx_B_iso_mean_solvent          18.21 
_refine_hist.pdbx_number_atoms_protein        13344 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         318 
_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' ? 0.008  0.012  13967 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.353  1.650  18864 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.047  5.000  1835  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.333 24.459 628   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 16.004 15.000 2229  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 15.481 15.000 48    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.094  0.200  1747  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  10732 ? r_gen_planes_refined   ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 1   'interatomic distance' ? A 4620 ? ? 1  
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 2   'interatomic distance' ? B 4620 ? ? 1  
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 3   'interatomic distance' ? A 4592 ? ? 2  
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 4   'interatomic distance' ? C 4592 ? ? 2  
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 5   'interatomic distance' ? A 4614 ? ? 3  
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 6   'interatomic distance' ? D 4614 ? ? 3  
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 7   'interatomic distance' ? A 4611 ? ? 4  
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 8   'interatomic distance' ? E 4611 ? ? 4  
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 9   'interatomic distance' ? A 4639 ? ? 5  
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 10  'interatomic distance' ? F 4639 ? ? 5  
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 11  'interatomic distance' ? A 4639 ? ? 6  
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 12  'interatomic distance' ? G 4639 ? ? 6  
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 13  'interatomic distance' ? A 4612 ? ? 7  
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 14  'interatomic distance' ? H 4612 ? ? 7  
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 15  'interatomic distance' ? A 4567 ? ? 8  
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 16  'interatomic distance' ? I 4567 ? ? 8  
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 17  'interatomic distance' ? A 4629 ? ? 9  
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 18  'interatomic distance' ? J 4629 ? ? 9  
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 19  'interatomic distance' ? A 4634 ? ? 10 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 20  'interatomic distance' ? K 4634 ? ? 10 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 21  'interatomic distance' ? A 4610 ? ? 11 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 22  'interatomic distance' ? L 4610 ? ? 11 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 23  'interatomic distance' ? B 4630 ? ? 12 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 24  'interatomic distance' ? C 4630 ? ? 12 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 25  'interatomic distance' ? B 4658 ? ? 13 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 26  'interatomic distance' ? D 4658 ? ? 13 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 27  'interatomic distance' ? B 4629 ? ? 14 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 28  'interatomic distance' ? E 4629 ? ? 14 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 29  'interatomic distance' ? B 4657 ? ? 15 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 30  'interatomic distance' ? F 4657 ? ? 15 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 31  'interatomic distance' ? B 4669 ? ? 16 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 32  'interatomic distance' ? G 4669 ? ? 16 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 33  'interatomic distance' ? B 4653 ? ? 17 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 34  'interatomic distance' ? H 4653 ? ? 17 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 35  'interatomic distance' ? B 4611 ? ? 18 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 36  'interatomic distance' ? I 4611 ? ? 18 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 37  'interatomic distance' ? B 4678 ? ? 19 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 38  'interatomic distance' ? J 4678 ? ? 19 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 39  'interatomic distance' ? B 4672 ? ? 20 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 40  'interatomic distance' ? K 4672 ? ? 20 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 41  'interatomic distance' ? B 4641 ? ? 21 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 42  'interatomic distance' ? L 4641 ? ? 21 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 43  'interatomic distance' ? C 4634 ? ? 22 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 44  'interatomic distance' ? D 4634 ? ? 22 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 45  'interatomic distance' ? C 4618 ? ? 23 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 46  'interatomic distance' ? E 4618 ? ? 23 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 47  'interatomic distance' ? C 4649 ? ? 24 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 48  'interatomic distance' ? F 4649 ? ? 24 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 49  'interatomic distance' ? C 4639 ? ? 25 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 50  'interatomic distance' ? G 4639 ? ? 25 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 51  'interatomic distance' ? C 4640 ? ? 26 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 52  'interatomic distance' ? H 4640 ? ? 26 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 53  'interatomic distance' ? C 4585 ? ? 27 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 54  'interatomic distance' ? I 4585 ? ? 27 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 55  'interatomic distance' ? C 4637 ? ? 28 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 56  'interatomic distance' ? J 4637 ? ? 28 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 57  'interatomic distance' ? C 4648 ? ? 29 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 58  'interatomic distance' ? K 4648 ? ? 29 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 59  'interatomic distance' ? C 4644 ? ? 30 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 60  'interatomic distance' ? L 4644 ? ? 30 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 61  'interatomic distance' ? D 4601 ? ? 31 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 62  'interatomic distance' ? E 4601 ? ? 31 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 63  'interatomic distance' ? D 4635 ? ? 32 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 64  'interatomic distance' ? F 4635 ? ? 32 
'X-RAY DIFFRACTION' 1 ? ? 0.030 ? 0.050 65  'interatomic distance' ? D 4636 ? ? 33 
'X-RAY DIFFRACTION' 2 ? ? 0.030 ? 0.050 66  'interatomic distance' ? G 4636 ? ? 33 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 67  'interatomic distance' ? D 4621 ? ? 34 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 68  'interatomic distance' ? H 4621 ? ? 34 
'X-RAY DIFFRACTION' 1 ? ? 0.030 ? 0.050 69  'interatomic distance' ? D 4596 ? ? 35 
'X-RAY DIFFRACTION' 2 ? ? 0.030 ? 0.050 70  'interatomic distance' ? I 4596 ? ? 35 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 71  'interatomic distance' ? D 4640 ? ? 36 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 72  'interatomic distance' ? J 4640 ? ? 36 
'X-RAY DIFFRACTION' 1 ? ? 0.030 ? 0.050 73  'interatomic distance' ? D 4647 ? ? 37 
'X-RAY DIFFRACTION' 2 ? ? 0.030 ? 0.050 74  'interatomic distance' ? K 4647 ? ? 37 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 75  'interatomic distance' ? D 4606 ? ? 38 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 76  'interatomic distance' ? L 4606 ? ? 38 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 77  'interatomic distance' ? E 4630 ? ? 39 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 78  'interatomic distance' ? F 4630 ? ? 39 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 79  'interatomic distance' ? E 4616 ? ? 40 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 80  'interatomic distance' ? G 4616 ? ? 40 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 81  'interatomic distance' ? E 4620 ? ? 41 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 82  'interatomic distance' ? H 4620 ? ? 41 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 83  'interatomic distance' ? E 4573 ? ? 42 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 84  'interatomic distance' ? I 4573 ? ? 42 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 85  'interatomic distance' ? E 4626 ? ? 43 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 86  'interatomic distance' ? J 4626 ? ? 43 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 87  'interatomic distance' ? E 4611 ? ? 44 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 88  'interatomic distance' ? K 4611 ? ? 44 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 89  'interatomic distance' ? E 4593 ? ? 45 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 90  'interatomic distance' ? L 4593 ? ? 45 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 91  'interatomic distance' ? F 4671 ? ? 46 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 92  'interatomic distance' ? G 4671 ? ? 46 
'X-RAY DIFFRACTION' 1 ? ? 0.060 ? 0.050 93  'interatomic distance' ? F 4639 ? ? 47 
'X-RAY DIFFRACTION' 2 ? ? 0.060 ? 0.050 94  'interatomic distance' ? H 4639 ? ? 47 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 95  'interatomic distance' ? F 4607 ? ? 48 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 96  'interatomic distance' ? I 4607 ? ? 48 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 97  'interatomic distance' ? F 4655 ? ? 49 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 98  'interatomic distance' ? J 4655 ? ? 49 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 99  'interatomic distance' ? F 4655 ? ? 50 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 100 'interatomic distance' ? K 4655 ? ? 50 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 101 'interatomic distance' ? F 4634 ? ? 51 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 102 'interatomic distance' ? L 4634 ? ? 51 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 103 'interatomic distance' ? G 4651 ? ? 52 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 104 'interatomic distance' ? H 4651 ? ? 52 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 105 'interatomic distance' ? G 4601 ? ? 53 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 106 'interatomic distance' ? I 4601 ? ? 53 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 107 'interatomic distance' ? G 4665 ? ? 54 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 108 'interatomic distance' ? J 4665 ? ? 54 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 109 'interatomic distance' ? G 4663 ? ? 55 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 110 'interatomic distance' ? K 4663 ? ? 55 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 111 'interatomic distance' ? G 4625 ? ? 56 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 112 'interatomic distance' ? L 4625 ? ? 56 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 113 'interatomic distance' ? H 4591 ? ? 57 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 114 'interatomic distance' ? I 4591 ? ? 57 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 115 'interatomic distance' ? H 4647 ? ? 58 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 116 'interatomic distance' ? J 4647 ? ? 58 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 117 'interatomic distance' ? H 4646 ? ? 59 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 118 'interatomic distance' ? K 4646 ? ? 59 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 119 'interatomic distance' ? H 4629 ? ? 60 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 120 'interatomic distance' ? L 4629 ? ? 60 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 121 'interatomic distance' ? I 4644 ? ? 61 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 122 'interatomic distance' ? J 4644 ? ? 61 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 123 'interatomic distance' ? I 4649 ? ? 62 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 124 'interatomic distance' ? K 4649 ? ? 62 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 125 'interatomic distance' ? I 4630 ? ? 63 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 126 'interatomic distance' ? L 4630 ? ? 63 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 127 'interatomic distance' ? J 4669 ? ? 64 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 128 'interatomic distance' ? K 4669 ? ? 64 
'X-RAY DIFFRACTION' 1 ? ? 0.050 ? 0.050 129 'interatomic distance' ? J 4616 ? ? 65 
'X-RAY DIFFRACTION' 2 ? ? 0.050 ? 0.050 130 'interatomic distance' ? L 4616 ? ? 65 
'X-RAY DIFFRACTION' 1 ? ? 0.040 ? 0.050 131 'interatomic distance' ? K 4626 ? ? 66 
'X-RAY DIFFRACTION' 2 ? ? 0.040 ? 0.050 132 'interatomic distance' ? L 4626 ? ? 66 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.8000 
_refine_ls_shell.d_res_low                        2.8730 
_refine_ls_shell.number_reflns_all                5680 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             294 
_refine_ls_shell.number_reflns_R_work             5386 
_refine_ls_shell.percent_reflns_obs               99.3500 
_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                  0.4000 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3470 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1  1 A 
1  2 B 
2  1 A 
2  2 C 
3  1 A 
3  2 D 
4  1 A 
4  2 E 
5  1 A 
5  2 F 
6  1 A 
6  2 G 
7  1 A 
7  2 H 
8  1 A 
8  2 I 
9  1 A 
9  2 J 
10 1 A 
10 2 K 
11 1 A 
11 2 L 
12 1 B 
12 2 C 
13 1 B 
13 2 D 
14 1 B 
14 2 E 
15 1 B 
15 2 F 
16 1 B 
16 2 G 
17 1 B 
17 2 H 
18 1 B 
18 2 I 
19 1 B 
19 2 J 
20 1 B 
20 2 K 
21 1 B 
21 2 L 
22 1 C 
22 2 D 
23 1 C 
23 2 E 
24 1 C 
24 2 F 
25 1 C 
25 2 G 
26 1 C 
26 2 H 
27 1 C 
27 2 I 
28 1 C 
28 2 J 
29 1 C 
29 2 K 
30 1 C 
30 2 L 
31 1 D 
31 2 E 
32 1 D 
32 2 F 
33 1 D 
33 2 G 
34 1 D 
34 2 H 
35 1 D 
35 2 I 
36 1 D 
36 2 J 
37 1 D 
37 2 K 
38 1 D 
38 2 L 
39 1 E 
39 2 F 
40 1 E 
40 2 G 
41 1 E 
41 2 H 
42 1 E 
42 2 I 
43 1 E 
43 2 J 
44 1 E 
44 2 K 
45 1 E 
45 2 L 
46 1 F 
46 2 G 
47 1 F 
47 2 H 
48 1 F 
48 2 I 
49 1 F 
49 2 J 
50 1 F 
50 2 K 
51 1 F 
51 2 L 
52 1 G 
52 2 H 
53 1 G 
53 2 I 
54 1 G 
54 2 J 
55 1 G 
55 2 K 
56 1 G 
56 2 L 
57 1 H 
57 2 I 
58 1 H 
58 2 J 
59 1 H 
59 2 K 
60 1 H 
60 2 L 
61 1 I 
61 2 J 
62 1 I 
62 2 K 
63 1 I 
63 2 L 
64 1 J 
64 2 K 
65 1 J 
65 2 L 
66 1 K 
66 2 L 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
1  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
1  2 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
2  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
2  2 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
3  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
3  2 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
4  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
4  2 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
5  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
5  2 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
6  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
6  2 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
7  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
7  2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
8  1 0 0 A 1 A 151 ? ? ? ? ? ? ? ? ? 
8  2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
9  1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
9  2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
10 1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
10 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
11 1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
11 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
12 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
12 2 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
13 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
13 2 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
14 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
14 2 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
15 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
15 2 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
16 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
16 2 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
17 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
17 2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
18 1 0 0 B 1 B 151 ? ? ? ? ? ? ? ? ? 
18 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
19 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
19 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
20 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
20 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
21 1 0 0 B 1 B 153 ? ? ? ? ? ? ? ? ? 
21 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
22 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
22 2 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
23 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
23 2 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
24 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
24 2 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
25 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
25 2 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
26 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
26 2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
27 1 0 0 C 1 C 151 ? ? ? ? ? ? ? ? ? 
27 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
28 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
28 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
29 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
29 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
30 1 0 0 C 1 C 153 ? ? ? ? ? ? ? ? ? 
30 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
31 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
31 2 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
32 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
32 2 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
33 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
33 2 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
34 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
34 2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
35 1 0 0 D 1 D 151 ? ? ? ? ? ? ? ? ? 
35 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
36 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
36 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
37 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
37 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
38 1 0 0 D 1 D 153 ? ? ? ? ? ? ? ? ? 
38 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
39 1 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
39 2 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
40 1 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
40 2 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
41 1 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
41 2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
42 1 0 0 E 1 E 151 ? ? ? ? ? ? ? ? ? 
42 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
43 1 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
43 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
44 1 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
44 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
45 1 0 0 E 1 E 153 ? ? ? ? ? ? ? ? ? 
45 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
46 1 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
46 2 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
47 1 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
47 2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
48 1 0 0 F 1 F 151 ? ? ? ? ? ? ? ? ? 
48 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
49 1 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
49 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
50 1 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
50 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
51 1 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
51 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
52 1 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
52 2 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
53 1 0 0 G 1 G 151 ? ? ? ? ? ? ? ? ? 
53 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
54 1 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
54 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
55 1 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
55 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
56 1 0 0 G 1 G 153 ? ? ? ? ? ? ? ? ? 
56 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
57 1 0 0 H 1 H 151 ? ? ? ? ? ? ? ? ? 
57 2 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
58 1 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
58 2 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
59 1 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
59 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
60 1 0 0 H 1 H 153 ? ? ? ? ? ? ? ? ? 
60 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
61 1 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
61 2 0 0 J 1 J 151 ? ? ? ? ? ? ? ? ? 
62 1 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
62 2 0 0 K 1 K 151 ? ? ? ? ? ? ? ? ? 
63 1 0 0 I 1 I 151 ? ? ? ? ? ? ? ? ? 
63 2 0 0 L 1 L 151 ? ? ? ? ? ? ? ? ? 
64 1 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
64 2 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
65 1 0 0 J 1 J 153 ? ? ? ? ? ? ? ? ? 
65 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
66 1 0 0 K 1 K 153 ? ? ? ? ? ? ? ? ? 
66 2 0 0 L 1 L 153 ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1  ? 
2  ? 
3  ? 
4  ? 
5  ? 
6  ? 
7  ? 
8  ? 
9  ? 
10 ? 
11 ? 
12 ? 
13 ? 
14 ? 
15 ? 
16 ? 
17 ? 
18 ? 
19 ? 
20 ? 
21 ? 
22 ? 
23 ? 
24 ? 
25 ? 
26 ? 
27 ? 
28 ? 
29 ? 
30 ? 
31 ? 
32 ? 
33 ? 
34 ? 
35 ? 
36 ? 
37 ? 
38 ? 
39 ? 
40 ? 
41 ? 
42 ? 
43 ? 
44 ? 
45 ? 
46 ? 
47 ? 
48 ? 
49 ? 
50 ? 
51 ? 
52 ? 
53 ? 
54 ? 
55 ? 
56 ? 
57 ? 
58 ? 
59 ? 
60 ? 
61 ? 
62 ? 
63 ? 
64 ? 
65 ? 
66 ? 
# 
_struct.entry_id                     6SPI 
_struct.title                        'A4V MUTANT OF HUMAN SOD1 WITH EBSELEN DERIVATIVE 4' 
_struct.pdbx_descriptor              'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_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        6SPI 
_struct_keywords.text            'A4V SOD1 mutant, ebselen, ebselen derivatives, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 1 ? 
L  N N 1 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 4 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 4 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 4 ? 
HA N N 4 ? 
IA N N 2 ? 
JA N N 3 ? 
KA N N 4 ? 
LA N N 2 ? 
MA N N 3 ? 
NA N N 4 ? 
OA N N 2 ? 
PA N N 3 ? 
QA N N 2 ? 
RA N N 3 ? 
SA N N 4 ? 
TA N N 4 ? 
UA N N 2 ? 
VA N N 3 ? 
WA N N 4 ? 
XA N N 4 ? 
YA N N 4 ? 
ZA N N 2 ? 
AB N N 3 ? 
BB N N 4 ? 
CB N N 5 ? 
DB N N 5 ? 
EB N N 5 ? 
FB N N 5 ? 
GB N N 5 ? 
HB N N 5 ? 
IB N N 5 ? 
JB N N 5 ? 
KB N N 5 ? 
LB N N 5 ? 
MB N N 5 ? 
NB N N 5 ? 
# 
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 ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  AA2 GLU A 134 ? GLY A 139 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P3  AA3 ALA B 56  ? GLY B 62  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  AA4 GLU B 134 ? GLY B 139 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5  AA5 ALA C 56  ? GLY C 62  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  AA6 SER C 108 ? CYS C 112 ? SER C 107 CYS C 111 5 ? 5 
HELX_P HELX_P7  AA7 GLU C 134 ? GLY C 139 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P8  AA8 ALA D 56  ? GLY D 62  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P9  AA9 SER D 108 ? CYS D 112 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P10 AB1 GLU D 134 ? GLY D 139 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P11 AB2 ALA E 56  ? GLY E 62  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P12 AB3 SER E 108 ? CYS E 112 ? SER E 107 CYS E 111 5 ? 5 
HELX_P HELX_P13 AB4 GLU E 134 ? GLY E 139 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P14 AB5 ALA F 56  ? GLY F 62  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P15 AB6 SER F 108 ? CYS F 112 ? SER F 107 CYS F 111 5 ? 5 
HELX_P HELX_P16 AB7 GLU F 134 ? GLY F 139 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P17 AB8 ALA G 56  ? GLY G 62  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P18 AB9 SER G 108 ? CYS G 112 ? SER G 107 CYS G 111 5 ? 5 
HELX_P HELX_P19 AC1 GLU G 134 ? GLY G 139 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P20 AC2 ALA H 56  ? GLY H 62  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P21 AC3 GLU H 134 ? GLY H 139 ? GLU H 133 GLY H 138 1 ? 6 
HELX_P HELX_P22 AC4 ALA I 56  ? GLY I 62  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P23 AC5 SER I 108 ? CYS I 112 ? SER I 107 CYS I 111 5 ? 5 
HELX_P HELX_P24 AC6 GLU I 134 ? GLY I 139 ? GLU I 133 GLY I 138 1 ? 6 
HELX_P HELX_P25 AC7 ALA J 56  ? GLY J 62  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P26 AC8 SER J 108 ? CYS J 112 ? SER J 107 CYS J 111 5 ? 5 
HELX_P HELX_P27 AC9 GLU J 134 ? GLY J 139 ? GLU J 133 GLY J 138 1 ? 6 
HELX_P HELX_P28 AD1 ALA K 56  ? GLY K 62  ? ALA K 55  GLY K 61  5 ? 7 
HELX_P HELX_P29 AD2 GLU K 134 ? GLY K 139 ? GLU K 133 GLY K 138 1 ? 6 
HELX_P HELX_P30 AD3 ALA L 56  ? GLY L 62  ? ALA L 55  GLY L 61  5 ? 7 
HELX_P HELX_P31 AD4 SER L 108 ? CYS L 112 ? SER L 107 CYS L 111 5 ? 5 
HELX_P HELX_P32 AD5 GLU L 134 ? GLY L 139 ? GLU L 133 GLY L 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ?    ? A CYS 58  SG  ? ? ? 1_555 A  CYS 147 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.077 ? 
disulf2  disulf ?    ? B CYS 58  SG  ? ? ? 1_555 B  CYS 147 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.105 ? 
disulf3  disulf ?    ? C CYS 58  SG  ? ? ? 1_555 C  CYS 147 SG ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.076 ? 
disulf4  disulf ?    ? D CYS 58  SG  ? ? ? 1_555 D  CYS 147 SG ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.075 ? 
disulf5  disulf ?    ? E CYS 58  SG  ? ? ? 1_555 E  CYS 147 SG ? ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.076 ? 
disulf6  disulf ?    ? F CYS 58  SG  ? ? ? 1_555 F  CYS 147 SG ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.095 ? 
disulf7  disulf ?    ? G CYS 58  SG  ? ? ? 1_555 G  CYS 147 SG ? ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.085 ? 
disulf8  disulf ?    ? H CYS 58  SG  ? ? ? 1_555 H  CYS 147 SG ? ? H CYS 57  H CYS 146 1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf9  disulf ?    ? I CYS 58  SG  ? ? ? 1_555 I  CYS 147 SG ? ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.076 ? 
disulf10 disulf ?    ? J CYS 58  SG  ? ? ? 1_555 J  CYS 147 SG ? ? J CYS 57  J CYS 146 1_555 ? ? ? ? ? ? ? 2.106 ? 
disulf11 disulf ?    ? K CYS 58  SG  ? ? ? 1_555 K  CYS 147 SG ? ? K CYS 57  K CYS 146 1_555 ? ? ? ? ? ? ? 2.083 ? 
disulf12 disulf ?    ? L CYS 58  SG  ? ? ? 1_555 L  CYS 147 SG ? ? L CYS 57  L CYS 146 1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc1  metalc ?    ? A HIS 64  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 63  A ZN  202 1_555 ? ? ? ? ? ? ? 2.015 ? 
metalc2  metalc ?    ? A HIS 72  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 71  A ZN  202 1_555 ? ? ? ? ? ? ? 2.004 ? 
metalc3  metalc ?    ? A HIS 81  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 80  A ZN  202 1_555 ? ? ? ? ? ? ? 1.975 ? 
metalc4  metalc ?    ? A ASP 84  OD1 ? ? ? 1_555 N  ZN  .   ZN ? ? A ASP 83  A ZN  202 1_555 ? ? ? ? ? ? ? 1.800 ? 
metalc5  metalc ?    ? B HIS 64  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? B HIS 63  B ZN  202 1_555 ? ? ? ? ? ? ? 2.039 ? 
metalc6  metalc ?    ? B HIS 72  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? B HIS 71  B ZN  202 1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc7  metalc ?    ? B HIS 81  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? B HIS 80  B ZN  202 1_555 ? ? ? ? ? ? ? 1.932 ? 
metalc8  metalc ?    ? B ASP 84  OD1 ? ? ? 1_555 R  ZN  .   ZN ? ? B ASP 83  B ZN  202 1_555 ? ? ? ? ? ? ? 1.833 ? 
covale1  covale none ? B CYS 112 SG  ? ? ? 1_555 Q  LQW .   SE ? ? B CYS 111 B LQW 201 1_555 ? ? ? ? ? ? ? 1.966 ? 
metalc9  metalc ?    ? C HIS 64  ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? C HIS 63  C ZN  202 1_555 ? ? ? ? ? ? ? 1.972 ? 
metalc10 metalc ?    ? C HIS 72  ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? C HIS 71  C ZN  202 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc11 metalc ?    ? C HIS 81  ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? C HIS 80  C ZN  202 1_555 ? ? ? ? ? ? ? 1.956 ? 
metalc12 metalc ?    ? C ASP 84  OD1 ? ? ? 1_555 V  ZN  .   ZN ? ? C ASP 83  C ZN  202 1_555 ? ? ? ? ? ? ? 1.829 ? 
covale2  covale none ? C CYS 112 SG  ? ? ? 1_555 U  LQW .   SE ? ? C CYS 111 C LQW 201 1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc13 metalc ?    ? D HIS 64  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? D HIS 63  D ZN  202 1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc14 metalc ?    ? D HIS 72  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? D HIS 71  D ZN  202 1_555 ? ? ? ? ? ? ? 1.991 ? 
metalc15 metalc ?    ? D HIS 81  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? D HIS 80  D ZN  202 1_555 ? ? ? ? ? ? ? 1.953 ? 
metalc16 metalc ?    ? D ASP 84  OD1 ? ? ? 1_555 Y  ZN  .   ZN ? ? D ASP 83  D ZN  202 1_555 ? ? ? ? ? ? ? 1.827 ? 
covale3  covale none ? D CYS 112 SG  ? ? ? 1_555 X  LQW .   SE ? ? D CYS 111 D LQW 201 1_555 ? ? ? ? ? ? ? 2.004 ? 
metalc17 metalc ?    ? E HIS 64  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? E HIS 63  E ZN  202 1_555 ? ? ? ? ? ? ? 1.977 ? 
metalc18 metalc ?    ? E HIS 72  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? E HIS 71  E ZN  202 1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc19 metalc ?    ? E HIS 81  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? E HIS 80  E ZN  202 1_555 ? ? ? ? ? ? ? 1.978 ? 
metalc20 metalc ?    ? E ASP 84  OD1 ? ? ? 1_555 CA ZN  .   ZN ? ? E ASP 83  E ZN  202 1_555 ? ? ? ? ? ? ? 1.800 ? 
covale4  covale none ? E CYS 112 SG  ? ? ? 1_555 BA LQW .   SE ? ? E CYS 111 E LQW 201 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc21 metalc ?    ? F HIS 64  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? F HIS 63  F ZN  202 1_555 ? ? ? ? ? ? ? 2.012 ? 
metalc22 metalc ?    ? F HIS 72  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? F HIS 71  F ZN  202 1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc23 metalc ?    ? F HIS 81  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? F HIS 80  F ZN  202 1_555 ? ? ? ? ? ? ? 1.913 ? 
metalc24 metalc ?    ? F ASP 84  OD1 ? ? ? 1_555 FA ZN  .   ZN ? ? F ASP 83  F ZN  202 1_555 ? ? ? ? ? ? ? 1.838 ? 
covale5  covale none ? F CYS 112 SG  ? ? ? 1_555 EA LQW .   SE ? ? F CYS 111 F LQW 201 1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc25 metalc ?    ? G HIS 64  ND1 ? ? ? 1_555 JA ZN  .   ZN ? ? G HIS 63  G ZN  202 1_555 ? ? ? ? ? ? ? 2.026 ? 
metalc26 metalc ?    ? G HIS 72  ND1 ? ? ? 1_555 JA ZN  .   ZN ? ? G HIS 71  G ZN  202 1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc27 metalc ?    ? G HIS 81  ND1 ? ? ? 1_555 JA ZN  .   ZN ? ? G HIS 80  G ZN  202 1_555 ? ? ? ? ? ? ? 1.908 ? 
metalc28 metalc ?    ? G ASP 84  OD1 ? ? ? 1_555 JA ZN  .   ZN ? ? G ASP 83  G ZN  202 1_555 ? ? ? ? ? ? ? 1.850 ? 
covale6  covale none ? G CYS 112 SG  ? ? ? 1_555 IA LQW .   SE ? ? G CYS 111 G LQW 201 1_555 ? ? ? ? ? ? ? 2.024 ? 
metalc29 metalc ?    ? H HIS 64  ND1 ? ? ? 1_555 MA ZN  .   ZN ? ? H HIS 63  H ZN  202 1_555 ? ? ? ? ? ? ? 2.015 ? 
metalc30 metalc ?    ? H HIS 72  ND1 ? ? ? 1_555 MA ZN  .   ZN ? ? H HIS 71  H ZN  202 1_555 ? ? ? ? ? ? ? 1.979 ? 
metalc31 metalc ?    ? H HIS 81  ND1 ? ? ? 1_555 MA ZN  .   ZN ? ? H HIS 80  H ZN  202 1_555 ? ? ? ? ? ? ? 1.976 ? 
metalc32 metalc ?    ? H ASP 84  OD1 ? ? ? 1_555 MA ZN  .   ZN ? ? H ASP 83  H ZN  202 1_555 ? ? ? ? ? ? ? 1.824 ? 
covale7  covale none ? H CYS 112 SG  ? ? ? 1_555 LA LQW .   SE ? ? H CYS 111 H LQW 201 1_555 ? ? ? ? ? ? ? 2.039 ? 
metalc33 metalc ?    ? I HIS 64  ND1 ? ? ? 1_555 PA ZN  .   ZN ? ? I HIS 63  I ZN  202 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc34 metalc ?    ? I HIS 72  ND1 ? ? ? 1_555 PA ZN  .   ZN ? ? I HIS 71  I ZN  202 1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc35 metalc ?    ? I HIS 81  ND1 ? ? ? 1_555 PA ZN  .   ZN ? ? I HIS 80  I ZN  202 1_555 ? ? ? ? ? ? ? 1.983 ? 
metalc36 metalc ?    ? I ASP 84  OD1 ? ? ? 1_555 PA ZN  .   ZN ? ? I ASP 83  I ZN  202 1_555 ? ? ? ? ? ? ? 1.771 ? 
metalc37 metalc ?    ? I ASP 84  OD2 ? ? ? 1_555 PA ZN  .   ZN ? ? I ASP 83  I ZN  202 1_555 ? ? ? ? ? ? ? 2.664 ? 
covale8  covale none ? I CYS 112 SG  ? ? ? 1_555 OA LQW .   SE ? ? I CYS 111 I LQW 201 1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc38 metalc ?    ? J HIS 64  ND1 ? ? ? 1_555 RA ZN  .   ZN ? ? J HIS 63  J ZN  202 1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc39 metalc ?    ? J HIS 72  ND1 ? ? ? 1_555 RA ZN  .   ZN ? ? J HIS 71  J ZN  202 1_555 ? ? ? ? ? ? ? 2.100 ? 
metalc40 metalc ?    ? J HIS 81  ND1 ? ? ? 1_555 RA ZN  .   ZN ? ? J HIS 80  J ZN  202 1_555 ? ? ? ? ? ? ? 1.873 ? 
metalc41 metalc ?    ? J ASP 84  OD1 ? ? ? 1_555 RA ZN  .   ZN ? ? J ASP 83  J ZN  202 1_555 ? ? ? ? ? ? ? 1.832 ? 
metalc42 metalc ?    ? K HIS 64  ND1 ? ? ? 1_555 VA ZN  .   ZN ? ? K HIS 63  K ZN  202 1_555 ? ? ? ? ? ? ? 2.043 ? 
metalc43 metalc ?    ? K HIS 72  ND1 ? ? ? 1_555 VA ZN  .   ZN ? ? K HIS 71  K ZN  202 1_555 ? ? ? ? ? ? ? 1.981 ? 
metalc44 metalc ?    ? K HIS 81  ND1 ? ? ? 1_555 VA ZN  .   ZN ? ? K HIS 80  K ZN  202 1_555 ? ? ? ? ? ? ? 1.921 ? 
metalc45 metalc ?    ? K ASP 84  OD1 ? ? ? 1_555 VA ZN  .   ZN ? ? K ASP 83  K ZN  202 1_555 ? ? ? ? ? ? ? 1.856 ? 
covale9  covale none ? K CYS 112 SG  ? ? ? 1_555 UA LQW .   SE ? ? K CYS 111 K LQW 201 1_555 ? ? ? ? ? ? ? 1.966 ? 
metalc46 metalc ?    ? L HIS 64  ND1 ? ? ? 1_555 AB ZN  .   ZN ? ? L HIS 63  L ZN  202 1_555 ? ? ? ? ? ? ? 1.941 ? 
metalc47 metalc ?    ? L HIS 72  ND1 ? ? ? 1_555 AB ZN  .   ZN ? ? L HIS 71  L ZN  202 1_555 ? ? ? ? ? ? ? 1.989 ? 
metalc48 metalc ?    ? L HIS 81  ND1 ? ? ? 1_555 AB ZN  .   ZN ? ? L HIS 80  L ZN  202 1_555 ? ? ? ? ? ? ? 2.031 ? 
metalc49 metalc ?    ? L ASP 84  OD1 ? ? ? 1_555 AB ZN  .   ZN ? ? L ASP 83  L ZN  202 1_555 ? ? ? ? ? ? ? 1.804 ? 
covale10 covale none ? L CYS 112 SG  ? ? ? 1_555 ZA LQW .   SE ? ? L CYS 111 L LQW 201 1_555 ? ? ? ? ? ? ? 2.039 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 4 ? 
AC1 ? 5 ? 
AC2 ? 4 ? 
AC3 ? 5 ? 
AC4 ? 4 ? 
AC5 ? 5 ? 
AC6 ? 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 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC3 4 5 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 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 96  ? ASP A 102 ? ALA A 95  ASP A 101 
AA1 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
AA1 3 GLN A 16  ? GLN A 23  ? GLN A 15  GLN A 22  
AA1 4 THR A 3   ? LEU A 9   ? THR A 2   LEU A 8   
AA1 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
AA2 1 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
AA2 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
AA2 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
AA2 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
AA3 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
AA3 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
AA3 3 GLN B 16  ? GLN B 23  ? GLN B 15  GLN B 22  
AA3 4 THR B 3   ? LEU B 9   ? THR B 2   LEU B 8   
AA3 5 GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
AA4 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
AA4 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
AA4 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
AA4 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
AA5 1 ALA C 96  ? ASP C 102 ? ALA C 95  ASP C 101 
AA5 2 VAL C 30  ? LYS C 37  ? VAL C 29  LYS C 36  
AA5 3 GLN C 16  ? GLN C 23  ? GLN C 15  GLN C 22  
AA5 4 THR C 3   ? LEU C 9   ? THR C 2   LEU C 8   
AA5 5 GLY C 151 ? ILE C 152 ? GLY C 150 ILE C 151 
AA6 1 ASP C 84  ? ALA C 90  ? ASP C 83  ALA C 89  
AA6 2 GLY C 42  ? HIS C 49  ? GLY C 41  HIS C 48  
AA6 3 THR C 117 ? HIS C 121 ? THR C 116 HIS C 120 
AA6 4 ARG C 144 ? VAL C 149 ? ARG C 143 VAL C 148 
AA7 1 ALA D 96  ? ASP D 102 ? ALA D 95  ASP D 101 
AA7 2 VAL D 30  ? LYS D 37  ? VAL D 29  LYS D 36  
AA7 3 GLN D 16  ? GLN D 23  ? GLN D 15  GLN D 22  
AA7 4 THR D 3   ? LEU D 9   ? THR D 2   LEU D 8   
AA7 5 GLY D 151 ? ILE D 152 ? GLY D 150 ILE D 151 
AA8 1 ASP D 84  ? ALA D 90  ? ASP D 83  ALA D 89  
AA8 2 GLY D 42  ? HIS D 49  ? GLY D 41  HIS D 48  
AA8 3 THR D 117 ? HIS D 121 ? THR D 116 HIS D 120 
AA8 4 ARG D 144 ? VAL D 149 ? ARG D 143 VAL D 148 
AA9 1 ALA E 96  ? ASP E 102 ? ALA E 95  ASP E 101 
AA9 2 VAL E 30  ? LYS E 37  ? VAL E 29  LYS E 36  
AA9 3 GLN E 16  ? GLN E 23  ? GLN E 15  GLN E 22  
AA9 4 THR E 3   ? LEU E 9   ? THR E 2   LEU E 8   
AA9 5 GLY E 151 ? ILE E 152 ? GLY E 150 ILE E 151 
AB1 1 ASP E 84  ? ALA E 90  ? ASP E 83  ALA E 89  
AB1 2 GLY E 42  ? HIS E 49  ? GLY E 41  HIS E 48  
AB1 3 THR E 117 ? HIS E 121 ? THR E 116 HIS E 120 
AB1 4 ARG E 144 ? VAL E 149 ? ARG E 143 VAL E 148 
AB2 1 ALA F 96  ? ASP F 102 ? ALA F 95  ASP F 101 
AB2 2 VAL F 30  ? LYS F 37  ? VAL F 29  LYS F 36  
AB2 3 GLN F 16  ? GLN F 23  ? GLN F 15  GLN F 22  
AB2 4 THR F 3   ? LEU F 9   ? THR F 2   LEU F 8   
AB2 5 GLY F 151 ? ILE F 152 ? GLY F 150 ILE F 151 
AB3 1 ASP F 84  ? ALA F 90  ? ASP F 83  ALA F 89  
AB3 2 GLY F 42  ? HIS F 49  ? GLY F 41  HIS F 48  
AB3 3 THR F 117 ? HIS F 121 ? THR F 116 HIS F 120 
AB3 4 ARG F 144 ? VAL F 149 ? ARG F 143 VAL F 148 
AB4 1 ALA G 96  ? ASP G 102 ? ALA G 95  ASP G 101 
AB4 2 VAL G 30  ? LYS G 37  ? VAL G 29  LYS G 36  
AB4 3 GLN G 16  ? GLN G 23  ? GLN G 15  GLN G 22  
AB4 4 THR G 3   ? LEU G 9   ? THR G 2   LEU G 8   
AB4 5 GLY G 151 ? ILE G 152 ? GLY G 150 ILE G 151 
AB5 1 ASP G 84  ? ALA G 90  ? ASP G 83  ALA G 89  
AB5 2 GLY G 42  ? HIS G 49  ? GLY G 41  HIS G 48  
AB5 3 THR G 117 ? HIS G 121 ? THR G 116 HIS G 120 
AB5 4 ARG G 144 ? VAL G 149 ? ARG G 143 VAL G 148 
AB6 1 ALA H 96  ? ASP H 102 ? ALA H 95  ASP H 101 
AB6 2 VAL H 30  ? LYS H 37  ? VAL H 29  LYS H 36  
AB6 3 GLN H 16  ? GLN H 23  ? GLN H 15  GLN H 22  
AB6 4 THR H 3   ? LEU H 9   ? THR H 2   LEU H 8   
AB6 5 GLY H 151 ? ILE H 152 ? GLY H 150 ILE H 151 
AB7 1 ASP H 84  ? ALA H 90  ? ASP H 83  ALA H 89  
AB7 2 GLY H 42  ? HIS H 49  ? GLY H 41  HIS H 48  
AB7 3 THR H 117 ? HIS H 121 ? THR H 116 HIS H 120 
AB7 4 ARG H 144 ? VAL H 149 ? ARG H 143 VAL H 148 
AB8 1 ALA I 96  ? ASP I 102 ? ALA I 95  ASP I 101 
AB8 2 VAL I 30  ? LYS I 37  ? VAL I 29  LYS I 36  
AB8 3 GLN I 16  ? GLN I 23  ? GLN I 15  GLN I 22  
AB8 4 THR I 3   ? LEU I 9   ? THR I 2   LEU I 8   
AB8 5 GLY I 151 ? ILE I 152 ? GLY I 150 ILE I 151 
AB9 1 ASP I 84  ? ALA I 90  ? ASP I 83  ALA I 89  
AB9 2 GLY I 42  ? HIS I 49  ? GLY I 41  HIS I 48  
AB9 3 THR I 117 ? HIS I 121 ? THR I 116 HIS I 120 
AB9 4 ARG I 144 ? VAL I 149 ? ARG I 143 VAL I 148 
AC1 1 ALA J 96  ? ASP J 102 ? ALA J 95  ASP J 101 
AC1 2 VAL J 30  ? LYS J 37  ? VAL J 29  LYS J 36  
AC1 3 GLN J 16  ? GLN J 23  ? GLN J 15  GLN J 22  
AC1 4 THR J 3   ? LEU J 9   ? THR J 2   LEU J 8   
AC1 5 GLY J 151 ? ILE J 152 ? GLY J 150 ILE J 151 
AC2 1 ASP J 84  ? ALA J 90  ? ASP J 83  ALA J 89  
AC2 2 GLY J 42  ? HIS J 49  ? GLY J 41  HIS J 48  
AC2 3 THR J 117 ? HIS J 121 ? THR J 116 HIS J 120 
AC2 4 ARG J 144 ? VAL J 149 ? ARG J 143 VAL J 148 
AC3 1 ALA K 96  ? ASP K 102 ? ALA K 95  ASP K 101 
AC3 2 VAL K 30  ? LYS K 37  ? VAL K 29  LYS K 36  
AC3 3 GLN K 16  ? GLN K 23  ? GLN K 15  GLN K 22  
AC3 4 THR K 3   ? LEU K 9   ? THR K 2   LEU K 8   
AC3 5 GLY K 151 ? ILE K 152 ? GLY K 150 ILE K 151 
AC4 1 ASP K 84  ? ALA K 90  ? ASP K 83  ALA K 89  
AC4 2 GLY K 42  ? HIS K 49  ? GLY K 41  HIS K 48  
AC4 3 THR K 117 ? HIS K 121 ? THR K 116 HIS K 120 
AC4 4 ARG K 144 ? VAL K 149 ? ARG K 143 VAL K 148 
AC5 1 ALA L 96  ? ASP L 102 ? ALA L 95  ASP L 101 
AC5 2 VAL L 30  ? LYS L 37  ? VAL L 29  LYS L 36  
AC5 3 GLN L 16  ? GLN L 23  ? GLN L 15  GLN L 22  
AC5 4 THR L 3   ? LEU L 9   ? THR L 2   LEU L 8   
AC5 5 GLY L 151 ? ILE L 152 ? GLY L 150 ILE L 151 
AC6 1 ASP L 84  ? ALA L 90  ? ASP L 83  ALA L 89  
AC6 2 GLY L 42  ? HIS L 49  ? GLY L 41  HIS L 48  
AC6 3 THR L 117 ? HIS L 121 ? THR L 116 HIS L 120 
AC6 4 ARG L 144 ? VAL L 149 ? ARG L 143 VAL L 148 
# 
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 ILE A 100 ? O ILE A 99  N VAL A 32  ? N VAL A 31  
AA1 2 3 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
AA1 3 4 O GLY A 17  ? O GLY A 16  N LEU A 9   ? N LEU A 8   
AA1 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
AA2 1 2 O ALA A 90  ? O ALA A 89  N GLY A 42  ? N GLY A 41  
AA2 2 3 N GLY A 45  ? N GLY A 44  O HIS A 121 ? O HIS A 120 
AA2 3 4 N VAL A 120 ? N VAL A 119 O ALA A 146 ? O ALA A 145 
AA3 1 2 O ILE B 100 ? O ILE B 99  N VAL B 32  ? N VAL B 31  
AA3 2 3 O TRP B 33  ? O TRP B 32  N ASN B 20  ? N ASN B 19  
AA3 3 4 O GLY B 17  ? O GLY B 16  N LEU B 9   ? N LEU B 8   
AA3 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
AA4 1 2 O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
AA4 2 3 N GLY B 45  ? N GLY B 44  O HIS B 121 ? O HIS B 120 
AA4 3 4 N VAL B 120 ? N VAL B 119 O ALA B 146 ? O ALA B 145 
AA5 1 2 O ILE C 100 ? O ILE C 99  N VAL C 32  ? N VAL C 31  
AA5 2 3 O TRP C 33  ? O TRP C 32  N ASN C 20  ? N ASN C 19  
AA5 3 4 O GLY C 17  ? O GLY C 16  N LEU C 9   ? N LEU C 8   
AA5 4 5 N VAL C 6   ? N VAL C 5   O GLY C 151 ? O GLY C 150 
AA6 1 2 O ALA C 90  ? O ALA C 89  N GLY C 42  ? N GLY C 41  
AA6 2 3 N GLY C 45  ? N GLY C 44  O HIS C 121 ? O HIS C 120 
AA6 3 4 N VAL C 120 ? N VAL C 119 O ALA C 146 ? O ALA C 145 
AA7 1 2 O ILE D 100 ? O ILE D 99  N VAL D 32  ? N VAL D 31  
AA7 2 3 O TRP D 33  ? O TRP D 32  N ASN D 20  ? N ASN D 19  
AA7 3 4 O GLY D 17  ? O GLY D 16  N LEU D 9   ? N LEU D 8   
AA7 4 5 N VAL D 6   ? N VAL D 5   O GLY D 151 ? O GLY D 150 
AA8 1 2 O ALA D 90  ? O ALA D 89  N GLY D 42  ? N GLY D 41  
AA8 2 3 N GLY D 45  ? N GLY D 44  O HIS D 121 ? O HIS D 120 
AA8 3 4 N VAL D 120 ? N VAL D 119 O ALA D 146 ? O ALA D 145 
AA9 1 2 O ILE E 100 ? O ILE E 99  N VAL E 32  ? N VAL E 31  
AA9 2 3 O TRP E 33  ? O TRP E 32  N ASN E 20  ? N ASN E 19  
AA9 3 4 O GLY E 17  ? O GLY E 16  N LEU E 9   ? N LEU E 8   
AA9 4 5 N VAL E 6   ? N VAL E 5   O GLY E 151 ? O GLY E 150 
AB1 1 2 O ALA E 90  ? O ALA E 89  N GLY E 42  ? N GLY E 41  
AB1 2 3 N GLY E 45  ? N GLY E 44  O HIS E 121 ? O HIS E 120 
AB1 3 4 N VAL E 120 ? N VAL E 119 O ALA E 146 ? O ALA E 145 
AB2 1 2 O ILE F 100 ? O ILE F 99  N VAL F 32  ? N VAL F 31  
AB2 2 3 O TRP F 33  ? O TRP F 32  N ASN F 20  ? N ASN F 19  
AB2 3 4 O GLY F 17  ? O GLY F 16  N LEU F 9   ? N LEU F 8   
AB2 4 5 N VAL F 6   ? N VAL F 5   O GLY F 151 ? O GLY F 150 
AB3 1 2 O ALA F 90  ? O ALA F 89  N GLY F 42  ? N GLY F 41  
AB3 2 3 N GLY F 45  ? N GLY F 44  O HIS F 121 ? O HIS F 120 
AB3 3 4 N VAL F 120 ? N VAL F 119 O ALA F 146 ? O ALA F 145 
AB4 1 2 O ILE G 100 ? O ILE G 99  N VAL G 32  ? N VAL G 31  
AB4 2 3 O TRP G 33  ? O TRP G 32  N ASN G 20  ? N ASN G 19  
AB4 3 4 O GLY G 17  ? O GLY G 16  N LEU G 9   ? N LEU G 8   
AB4 4 5 N VAL G 6   ? N VAL G 5   O GLY G 151 ? O GLY G 150 
AB5 1 2 O ALA G 90  ? O ALA G 89  N GLY G 42  ? N GLY G 41  
AB5 2 3 N GLY G 45  ? N GLY G 44  O HIS G 121 ? O HIS G 120 
AB5 3 4 N VAL G 120 ? N VAL G 119 O ALA G 146 ? O ALA G 145 
AB6 1 2 O ILE H 100 ? O ILE H 99  N VAL H 32  ? N VAL H 31  
AB6 2 3 O TRP H 33  ? O TRP H 32  N ASN H 20  ? N ASN H 19  
AB6 3 4 O GLY H 17  ? O GLY H 16  N LEU H 9   ? N LEU H 8   
AB6 4 5 N VAL H 6   ? N VAL H 5   O GLY H 151 ? O GLY H 150 
AB7 1 2 O ALA H 90  ? O ALA H 89  N GLY H 42  ? N GLY H 41  
AB7 2 3 N GLY H 45  ? N GLY H 44  O HIS H 121 ? O HIS H 120 
AB7 3 4 N VAL H 120 ? N VAL H 119 O ALA H 146 ? O ALA H 145 
AB8 1 2 O ILE I 100 ? O ILE I 99  N VAL I 32  ? N VAL I 31  
AB8 2 3 O TRP I 33  ? O TRP I 32  N ASN I 20  ? N ASN I 19  
AB8 3 4 O GLY I 17  ? O GLY I 16  N LEU I 9   ? N LEU I 8   
AB8 4 5 N VAL I 6   ? N VAL I 5   O GLY I 151 ? O GLY I 150 
AB9 1 2 O ALA I 90  ? O ALA I 89  N GLY I 42  ? N GLY I 41  
AB9 2 3 N GLY I 45  ? N GLY I 44  O HIS I 121 ? O HIS I 120 
AB9 3 4 N VAL I 120 ? N VAL I 119 O ALA I 146 ? O ALA I 145 
AC1 1 2 O ILE J 100 ? O ILE J 99  N VAL J 32  ? N VAL J 31  
AC1 2 3 O TRP J 33  ? O TRP J 32  N ASN J 20  ? N ASN J 19  
AC1 3 4 O GLY J 17  ? O GLY J 16  N LEU J 9   ? N LEU J 8   
AC1 4 5 N VAL J 6   ? N VAL J 5   O GLY J 151 ? O GLY J 150 
AC2 1 2 O ALA J 90  ? O ALA J 89  N GLY J 42  ? N GLY J 41  
AC2 2 3 N GLY J 45  ? N GLY J 44  O HIS J 121 ? O HIS J 120 
AC2 3 4 N VAL J 120 ? N VAL J 119 O ALA J 146 ? O ALA J 145 
AC3 1 2 O ILE K 100 ? O ILE K 99  N VAL K 32  ? N VAL K 31  
AC3 2 3 O TRP K 33  ? O TRP K 32  N ASN K 20  ? N ASN K 19  
AC3 3 4 O GLY K 17  ? O GLY K 16  N LEU K 9   ? N LEU K 8   
AC3 4 5 N VAL K 6   ? N VAL K 5   O GLY K 151 ? O GLY K 150 
AC4 1 2 O ALA K 90  ? O ALA K 89  N GLY K 42  ? N GLY K 41  
AC4 2 3 N GLY K 45  ? N GLY K 44  O HIS K 121 ? O HIS K 120 
AC4 3 4 N VAL K 120 ? N VAL K 119 O ALA K 146 ? O ALA K 145 
AC5 1 2 O ILE L 100 ? O ILE L 99  N VAL L 32  ? N VAL L 31  
AC5 2 3 O TRP L 33  ? O TRP L 32  N ASN L 20  ? N ASN L 19  
AC5 3 4 O GLY L 17  ? O GLY L 16  N LEU L 9   ? N LEU L 8   
AC5 4 5 N VAL L 6   ? N VAL L 5   O GLY L 151 ? O GLY L 150 
AC6 1 2 O ALA L 90  ? O ALA L 89  N GLY L 42  ? N GLY L 41  
AC6 2 3 N GLY L 45  ? N GLY L 44  O HIS L 121 ? O HIS L 120 
AC6 3 4 N VAL L 120 ? N VAL L 119 O ALA L 146 ? O ALA L 145 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A LQW 201 ? 5  'binding site for residue LQW A 201'                  
AC2 Software A ZN  202 ? 4  'binding site for residue ZN A 202'                   
AC3 Software A SO4 203 ? 3  'binding site for residue SO4 A 203'                  
AC4 Software A SO4 204 ? 6  'binding site for residue SO4 A 204'                  
AC5 Software B ZN  202 ? 4  'binding site for residue ZN B 202'                   
AC6 Software B SO4 203 ? 5  'binding site for residue SO4 B 203'                  
AC7 Software B SO4 204 ? 3  'binding site for residue SO4 B 204'                  
AC8 Software C ZN  202 ? 4  'binding site for residue ZN C 202'                   
AC9 Software C SO4 203 ? 4  'binding site for residue SO4 C 203'                  
AD1 Software D ZN  202 ? 4  'binding site for residue ZN D 202'                   
AD2 Software D SO4 203 ? 4  'binding site for residue SO4 D 203'                  
AD3 Software D SO4 204 ? 6  'binding site for residue SO4 D 204'                  
AD4 Software E ZN  202 ? 4  'binding site for residue ZN E 202'                   
AD5 Software E SO4 203 ? 3  'binding site for residue SO4 E 203'                  
AD6 Software F ZN  202 ? 4  'binding site for residue ZN F 202'                   
AD7 Software F SO4 203 ? 4  'binding site for residue SO4 F 203'                  
AD8 Software F SO4 204 ? 4  'binding site for residue SO4 F 204'                  
AD9 Software G ZN  202 ? 4  'binding site for residue ZN G 202'                   
AE1 Software G SO4 203 ? 3  'binding site for residue SO4 G 203'                  
AE2 Software H ZN  202 ? 4  'binding site for residue ZN H 202'                   
AE3 Software H SO4 203 ? 5  'binding site for residue SO4 H 203'                  
AE4 Software I ZN  202 ? 4  'binding site for residue ZN I 202'                   
AE5 Software J LQW 201 ? 8  'binding site for residue LQW J 201'                  
AE6 Software J ZN  202 ? 4  'binding site for residue ZN J 202'                   
AE7 Software J SO4 203 ? 4  'binding site for residue SO4 J 203'                  
AE8 Software J SO4 204 ? 4  'binding site for residue SO4 J 204'                  
AE9 Software K ZN  202 ? 4  'binding site for residue ZN K 202'                   
AF1 Software K SO4 203 ? 3  'binding site for residue SO4 K 203'                  
AF2 Software K SO4 204 ? 6  'binding site for residue SO4 K 204'                  
AF3 Software K SO4 205 ? 6  'binding site for residue SO4 K 205'                  
AF4 Software L ZN  202 ? 4  'binding site for residue ZN L 202'                   
AF5 Software L SO4 203 ? 3  'binding site for residue SO4 L 203'                  
AF6 Software B LQW 201 ? 11 'binding site for Di-peptide LQW B 201 and CYS B 111' 
AF7 Software C LQW 201 ? 12 'binding site for Di-peptide LQW C 201 and CYS C 111' 
AF8 Software D LQW 201 ? 12 'binding site for Di-peptide LQW D 201 and CYS D 111' 
AF9 Software E LQW 201 ? 13 'binding site for Di-peptide LQW E 201 and CYS E 111' 
AG1 Software F LQW 201 ? 12 'binding site for Di-peptide LQW F 201 and CYS F 111' 
AG2 Software G LQW 201 ? 10 'binding site for Di-peptide LQW G 201 and CYS G 111' 
AG3 Software H LQW 201 ? 10 'binding site for Di-peptide LQW H 201 and CYS H 111' 
AG4 Software I LQW 201 ? 10 'binding site for Di-peptide LQW I 201 and CYS I 111' 
AG5 Software K LQW 201 ? 10 'binding site for Di-peptide LQW K 201 and CYS K 111' 
AG6 Software L LQW 201 ? 9  'binding site for Di-peptide LQW L 201 and CYS L 111' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 5  THR A  3   ? THR A 2   . ? 1_555 ? 
2   AC1 5  GLY A  109 ? GLY A 108 . ? 1_555 ? 
3   AC1 5  CYS A  112 ? CYS A 111 . ? 1_555 ? 
4   AC1 5  ILE A  152 ? ILE A 151 . ? 1_555 ? 
5   AC1 5  LQW QA .   ? LQW J 201 . ? 1_555 ? 
6   AC2 4  HIS A  64  ? HIS A 63  . ? 1_555 ? 
7   AC2 4  HIS A  72  ? HIS A 71  . ? 1_555 ? 
8   AC2 4  HIS A  81  ? HIS A 80  . ? 1_555 ? 
9   AC2 4  ASP A  84  ? ASP A 83  . ? 1_555 ? 
10  AC3 3  THR A  59  ? THR A 58  . ? 1_555 ? 
11  AC3 3  SER A  143 ? SER A 142 . ? 1_555 ? 
12  AC3 3  ARG A  144 ? ARG A 143 . ? 1_555 ? 
13  AC4 6  HIS A  49  ? HIS A 48  . ? 1_555 ? 
14  AC4 6  HIS A  121 ? HIS A 120 . ? 1_555 ? 
15  AC4 6  THR A  138 ? THR A 137 . ? 1_555 ? 
16  AC4 6  ARG A  144 ? ARG A 143 . ? 1_555 ? 
17  AC4 6  HOH CB .   ? HOH A 303 . ? 1_555 ? 
18  AC4 6  HOH CB .   ? HOH A 308 . ? 1_555 ? 
19  AC5 4  HIS B  64  ? HIS B 63  . ? 1_555 ? 
20  AC5 4  HIS B  72  ? HIS B 71  . ? 1_555 ? 
21  AC5 4  HIS B  81  ? HIS B 80  . ? 1_555 ? 
22  AC5 4  ASP B  84  ? ASP B 83  . ? 1_555 ? 
23  AC6 5  HIS B  121 ? HIS B 120 . ? 1_555 ? 
24  AC6 5  THR B  138 ? THR B 137 . ? 1_555 ? 
25  AC6 5  GLY B  142 ? GLY B 141 . ? 1_555 ? 
26  AC6 5  ARG B  144 ? ARG B 143 . ? 1_555 ? 
27  AC6 5  HOH DB .   ? HOH B 304 . ? 1_555 ? 
28  AC7 3  THR B  59  ? THR B 58  . ? 1_555 ? 
29  AC7 3  SER B  143 ? SER B 142 . ? 1_555 ? 
30  AC7 3  ARG B  144 ? ARG B 143 . ? 1_555 ? 
31  AC8 4  HIS C  64  ? HIS C 63  . ? 1_555 ? 
32  AC8 4  HIS C  72  ? HIS C 71  . ? 1_555 ? 
33  AC8 4  HIS C  81  ? HIS C 80  . ? 1_555 ? 
34  AC8 4  ASP C  84  ? ASP C 83  . ? 1_555 ? 
35  AC9 4  HIS C  49  ? HIS C 48  . ? 1_555 ? 
36  AC9 4  HIS C  121 ? HIS C 120 . ? 1_555 ? 
37  AC9 4  GLY C  142 ? GLY C 141 . ? 1_555 ? 
38  AC9 4  ARG C  144 ? ARG C 143 . ? 1_555 ? 
39  AD1 4  HIS D  64  ? HIS D 63  . ? 1_555 ? 
40  AD1 4  HIS D  72  ? HIS D 71  . ? 1_555 ? 
41  AD1 4  HIS D  81  ? HIS D 80  . ? 1_555 ? 
42  AD1 4  ASP D  84  ? ASP D 83  . ? 1_555 ? 
43  AD2 4  LYS B  129 ? LYS B 128 . ? 1_555 ? 
44  AD2 4  LYS D  76  ? LYS D 75  . ? 1_555 ? 
45  AD2 4  LYS D  129 ? LYS D 128 . ? 1_555 ? 
46  AD2 4  LYS F  129 ? LYS F 128 . ? 1_555 ? 
47  AD3 6  HIS D  49  ? HIS D 48  . ? 1_555 ? 
48  AD3 6  HIS D  121 ? HIS D 120 . ? 1_555 ? 
49  AD3 6  THR D  138 ? THR D 137 . ? 1_555 ? 
50  AD3 6  GLY D  142 ? GLY D 141 . ? 1_555 ? 
51  AD3 6  ARG D  144 ? ARG D 143 . ? 1_555 ? 
52  AD3 6  HOH FB .   ? HOH D 311 . ? 1_555 ? 
53  AD4 4  HIS E  64  ? HIS E 63  . ? 1_555 ? 
54  AD4 4  HIS E  72  ? HIS E 71  . ? 1_555 ? 
55  AD4 4  HIS E  81  ? HIS E 80  . ? 1_555 ? 
56  AD4 4  ASP E  84  ? ASP E 83  . ? 1_555 ? 
57  AD5 3  LYS A  129 ? LYS A 128 . ? 1_555 ? 
58  AD5 3  LYS C  129 ? LYS C 128 . ? 1_555 ? 
59  AD5 3  LYS E  129 ? LYS E 128 . ? 1_555 ? 
60  AD6 4  HIS F  64  ? HIS F 63  . ? 1_555 ? 
61  AD6 4  HIS F  72  ? HIS F 71  . ? 1_555 ? 
62  AD6 4  HIS F  81  ? HIS F 80  . ? 1_555 ? 
63  AD6 4  ASP F  84  ? ASP F 83  . ? 1_555 ? 
64  AD7 4  THR F  59  ? THR F 58  . ? 1_555 ? 
65  AD7 4  SER F  143 ? SER F 142 . ? 1_555 ? 
66  AD7 4  ARG F  144 ? ARG F 143 . ? 1_555 ? 
67  AD7 4  SO4 HA .   ? SO4 F 204 . ? 1_555 ? 
68  AD8 4  HIS F  121 ? HIS F 120 . ? 1_555 ? 
69  AD8 4  GLY F  142 ? GLY F 141 . ? 1_555 ? 
70  AD8 4  ARG F  144 ? ARG F 143 . ? 1_555 ? 
71  AD8 4  SO4 GA .   ? SO4 F 203 . ? 1_555 ? 
72  AD9 4  HIS G  64  ? HIS G 63  . ? 1_555 ? 
73  AD9 4  HIS G  72  ? HIS G 71  . ? 1_555 ? 
74  AD9 4  HIS G  81  ? HIS G 80  . ? 1_555 ? 
75  AD9 4  ASP G  84  ? ASP G 83  . ? 1_555 ? 
76  AE1 3  THR G  59  ? THR G 58  . ? 1_555 ? 
77  AE1 3  SER G  143 ? SER G 142 . ? 1_555 ? 
78  AE1 3  ARG G  144 ? ARG G 143 . ? 1_555 ? 
79  AE2 4  HIS H  64  ? HIS H 63  . ? 1_555 ? 
80  AE2 4  HIS H  72  ? HIS H 71  . ? 1_555 ? 
81  AE2 4  HIS H  81  ? HIS H 80  . ? 1_555 ? 
82  AE2 4  ASP H  84  ? ASP H 83  . ? 1_555 ? 
83  AE3 5  HIS H  121 ? HIS H 120 . ? 1_555 ? 
84  AE3 5  THR H  138 ? THR H 137 . ? 1_555 ? 
85  AE3 5  GLY H  142 ? GLY H 141 . ? 1_555 ? 
86  AE3 5  ARG H  144 ? ARG H 143 . ? 1_555 ? 
87  AE3 5  HOH JB .   ? HOH H 310 . ? 1_555 ? 
88  AE4 4  HIS I  64  ? HIS I 63  . ? 1_555 ? 
89  AE4 4  HIS I  72  ? HIS I 71  . ? 1_555 ? 
90  AE4 4  HIS I  81  ? HIS I 80  . ? 1_555 ? 
91  AE4 4  ASP I  84  ? ASP I 83  . ? 1_555 ? 
92  AE5 8  LQW M  .   ? LQW A 201 . ? 1_555 ? 
93  AE5 8  THR J  3   ? THR J 2   . ? 1_555 ? 
94  AE5 8  LYS J  4   ? LYS J 3   . ? 1_555 ? 
95  AE5 8  LEU J  107 ? LEU J 106 . ? 1_555 ? 
96  AE5 8  ASP J  110 ? ASP J 109 . ? 2_656 ? 
97  AE5 8  CYS J  112 ? CYS J 111 . ? 1_555 ? 
98  AE5 8  ILE J  114 ? ILE J 113 . ? 1_555 ? 
99  AE5 8  ILE J  152 ? ILE J 151 . ? 1_555 ? 
100 AE6 4  HIS J  64  ? HIS J 63  . ? 1_555 ? 
101 AE6 4  HIS J  72  ? HIS J 71  . ? 1_555 ? 
102 AE6 4  HIS J  81  ? HIS J 80  . ? 1_555 ? 
103 AE6 4  ASP J  84  ? ASP J 83  . ? 1_555 ? 
104 AE7 4  THR J  59  ? THR J 58  . ? 1_555 ? 
105 AE7 4  SER J  143 ? SER J 142 . ? 1_555 ? 
106 AE7 4  ARG J  144 ? ARG J 143 . ? 1_555 ? 
107 AE7 4  HOH LB .   ? HOH J 312 . ? 1_555 ? 
108 AE8 4  GLU J  134 ? GLU J 133 . ? 1_555 ? 
109 AE8 4  THR J  138 ? THR J 137 . ? 1_555 ? 
110 AE8 4  ASN J  140 ? ASN J 139 . ? 1_555 ? 
111 AE8 4  GLY J  142 ? GLY J 141 . ? 1_555 ? 
112 AE9 4  HIS K  64  ? HIS K 63  . ? 1_555 ? 
113 AE9 4  HIS K  72  ? HIS K 71  . ? 1_555 ? 
114 AE9 4  HIS K  81  ? HIS K 80  . ? 1_555 ? 
115 AE9 4  ASP K  84  ? ASP K 83  . ? 1_555 ? 
116 AF1 3  THR K  59  ? THR K 58  . ? 1_555 ? 
117 AF1 3  SER K  143 ? SER K 142 . ? 1_555 ? 
118 AF1 3  ARG K  144 ? ARG K 143 . ? 1_555 ? 
119 AF2 6  GLU K  134 ? GLU K 133 . ? 1_555 ? 
120 AF2 6  THR K  138 ? THR K 137 . ? 1_555 ? 
121 AF2 6  ASN K  140 ? ASN K 139 . ? 1_555 ? 
122 AF2 6  ALA K  141 ? ALA K 140 . ? 1_555 ? 
123 AF2 6  GLY K  142 ? GLY K 141 . ? 1_555 ? 
124 AF2 6  SO4 YA .   ? SO4 K 205 . ? 1_555 ? 
125 AF3 6  HIS K  49  ? HIS K 48  . ? 1_555 ? 
126 AF3 6  HIS K  121 ? HIS K 120 . ? 1_555 ? 
127 AF3 6  THR K  138 ? THR K 137 . ? 1_555 ? 
128 AF3 6  ARG K  144 ? ARG K 143 . ? 1_555 ? 
129 AF3 6  SO4 XA .   ? SO4 K 204 . ? 1_555 ? 
130 AF3 6  HOH MB .   ? HOH K 305 . ? 1_555 ? 
131 AF4 4  HIS L  64  ? HIS L 63  . ? 1_555 ? 
132 AF4 4  HIS L  72  ? HIS L 71  . ? 1_555 ? 
133 AF4 4  HIS L  81  ? HIS L 80  . ? 1_555 ? 
134 AF4 4  ASP L  84  ? ASP L 83  . ? 1_555 ? 
135 AF5 3  THR L  59  ? THR L 58  . ? 1_555 ? 
136 AF5 3  SER L  143 ? SER L 142 . ? 1_555 ? 
137 AF5 3  ARG L  144 ? ARG L 143 . ? 1_555 ? 
138 AF6 11 SER B  106 ? SER B 105 . ? 1_555 ? 
139 AF6 11 LEU B  107 ? LEU B 106 . ? 1_555 ? 
140 AF6 11 GLY B  109 ? GLY B 108 . ? 1_555 ? 
141 AF6 11 ASP B  110 ? ASP B 109 . ? 2_555 ? 
142 AF6 11 ASP B  110 ? ASP B 109 . ? 1_555 ? 
143 AF6 11 HIS B  111 ? HIS B 110 . ? 1_555 ? 
144 AF6 11 ILE B  113 ? ILE B 112 . ? 1_555 ? 
145 AF6 11 ILE B  114 ? ILE B 113 . ? 1_555 ? 
146 AF6 11 ARG B  116 ? ARG B 115 . ? 1_555 ? 
147 AF6 11 ILE B  152 ? ILE B 151 . ? 1_555 ? 
148 AF6 11 LQW UA .   ? LQW K 201 . ? 1_555 ? 
149 AF7 12 THR C  3   ? THR C 2   . ? 1_555 ? 
150 AF7 12 LYS C  4   ? LYS C 3   . ? 1_555 ? 
151 AF7 12 SER C  106 ? SER C 105 . ? 1_555 ? 
152 AF7 12 LEU C  107 ? LEU C 106 . ? 1_555 ? 
153 AF7 12 GLY C  109 ? GLY C 108 . ? 1_555 ? 
154 AF7 12 ASP C  110 ? ASP C 109 . ? 1_555 ? 
155 AF7 12 HIS C  111 ? HIS C 110 . ? 1_555 ? 
156 AF7 12 ILE C  113 ? ILE C 112 . ? 1_555 ? 
157 AF7 12 ILE C  114 ? ILE C 113 . ? 1_555 ? 
158 AF7 12 ARG C  116 ? ARG C 115 . ? 1_555 ? 
159 AF7 12 ALA C  153 ? ALA C 152 . ? 1_555 ? 
160 AF7 12 LQW OA .   ? LQW I 201 . ? 1_555 ? 
161 AF8 12 SER D  106 ? SER D 105 . ? 1_555 ? 
162 AF8 12 LEU D  107 ? LEU D 106 . ? 1_555 ? 
163 AF8 12 GLY D  109 ? GLY D 108 . ? 1_555 ? 
164 AF8 12 ASP D  110 ? ASP D 109 . ? 1_555 ? 
165 AF8 12 HIS D  111 ? HIS D 110 . ? 1_555 ? 
166 AF8 12 ILE D  113 ? ILE D 112 . ? 1_555 ? 
167 AF8 12 ILE D  114 ? ILE D 113 . ? 1_555 ? 
168 AF8 12 ARG D  116 ? ARG D 115 . ? 1_555 ? 
169 AF8 12 ILE D  152 ? ILE D 151 . ? 1_555 ? 
170 AF8 12 ALA D  153 ? ALA D 152 . ? 1_555 ? 
171 AF8 12 ARG L  116 ? ARG L 115 . ? 1_555 ? 
172 AF8 12 LQW ZA .   ? LQW L 201 . ? 1_555 ? 
173 AF9 13 SER E  106 ? SER E 105 . ? 1_555 ? 
174 AF9 13 LEU E  107 ? LEU E 106 . ? 1_555 ? 
175 AF9 13 SER E  108 ? SER E 107 . ? 1_555 ? 
176 AF9 13 GLY E  109 ? GLY E 108 . ? 1_555 ? 
177 AF9 13 ASP E  110 ? ASP E 109 . ? 1_555 ? 
178 AF9 13 HIS E  111 ? HIS E 110 . ? 1_555 ? 
179 AF9 13 ILE E  113 ? ILE E 112 . ? 1_555 ? 
180 AF9 13 ILE E  114 ? ILE E 113 . ? 1_555 ? 
181 AF9 13 ARG E  116 ? ARG E 115 . ? 1_555 ? 
182 AF9 13 HOH GB .   ? HOH E 309 . ? 1_555 ? 
183 AF9 13 GLY G  109 ? GLY G 108 . ? 1_555 ? 
184 AF9 13 ASP G  110 ? ASP G 109 . ? 1_555 ? 
185 AF9 13 LQW IA .   ? LQW G 201 . ? 1_555 ? 
186 AG1 12 THR F  3   ? THR F 2   . ? 1_555 ? 
187 AG1 12 SER F  106 ? SER F 105 . ? 1_555 ? 
188 AG1 12 LEU F  107 ? LEU F 106 . ? 1_555 ? 
189 AG1 12 GLY F  109 ? GLY F 108 . ? 1_555 ? 
190 AG1 12 ASP F  110 ? ASP F 109 . ? 1_555 ? 
191 AG1 12 HIS F  111 ? HIS F 110 . ? 1_555 ? 
192 AG1 12 ILE F  113 ? ILE F 112 . ? 1_555 ? 
193 AG1 12 ILE F  114 ? ILE F 113 . ? 1_555 ? 
194 AG1 12 ARG F  116 ? ARG F 115 . ? 1_555 ? 
195 AG1 12 ILE F  152 ? ILE F 151 . ? 1_555 ? 
196 AG1 12 ARG H  116 ? ARG H 115 . ? 1_555 ? 
197 AG1 12 LQW LA .   ? LQW H 201 . ? 1_555 ? 
198 AG2 10 LQW BA .   ? LQW E 201 . ? 1_555 ? 
199 AG2 10 SER G  106 ? SER G 105 . ? 1_555 ? 
200 AG2 10 LEU G  107 ? LEU G 106 . ? 1_555 ? 
201 AG2 10 GLY G  109 ? GLY G 108 . ? 1_555 ? 
202 AG2 10 ASP G  110 ? ASP G 109 . ? 1_555 ? 
203 AG2 10 HIS G  111 ? HIS G 110 . ? 1_555 ? 
204 AG2 10 ILE G  113 ? ILE G 112 . ? 1_555 ? 
205 AG2 10 ILE G  114 ? ILE G 113 . ? 1_555 ? 
206 AG2 10 ARG G  116 ? ARG G 115 . ? 1_555 ? 
207 AG2 10 ILE G  152 ? ILE G 151 . ? 1_555 ? 
208 AG3 10 LQW EA .   ? LQW F 201 . ? 1_555 ? 
209 AG3 10 SER H  106 ? SER H 105 . ? 1_555 ? 
210 AG3 10 LEU H  107 ? LEU H 106 . ? 1_555 ? 
211 AG3 10 SER H  108 ? SER H 107 . ? 1_555 ? 
212 AG3 10 GLY H  109 ? GLY H 108 . ? 1_555 ? 
213 AG3 10 ASP H  110 ? ASP H 109 . ? 1_555 ? 
214 AG3 10 HIS H  111 ? HIS H 110 . ? 1_555 ? 
215 AG3 10 ILE H  113 ? ILE H 112 . ? 1_555 ? 
216 AG3 10 ILE H  114 ? ILE H 113 . ? 1_555 ? 
217 AG3 10 ARG H  116 ? ARG H 115 . ? 1_555 ? 
218 AG4 10 LQW U  .   ? LQW C 201 . ? 1_555 ? 
219 AG4 10 SER I  106 ? SER I 105 . ? 1_555 ? 
220 AG4 10 LEU I  107 ? LEU I 106 . ? 1_555 ? 
221 AG4 10 GLY I  109 ? GLY I 108 . ? 1_555 ? 
222 AG4 10 ASP I  110 ? ASP I 109 . ? 1_555 ? 
223 AG4 10 HIS I  111 ? HIS I 110 . ? 1_555 ? 
224 AG4 10 ILE I  113 ? ILE I 112 . ? 1_555 ? 
225 AG4 10 ILE I  114 ? ILE I 113 . ? 1_555 ? 
226 AG4 10 ARG I  116 ? ARG I 115 . ? 1_555 ? 
227 AG4 10 ILE I  152 ? ILE I 151 . ? 1_555 ? 
228 AG5 10 LQW Q  .   ? LQW B 201 . ? 1_555 ? 
229 AG5 10 SER K  106 ? SER K 105 . ? 1_555 ? 
230 AG5 10 SER K  108 ? SER K 107 . ? 1_555 ? 
231 AG5 10 GLY K  109 ? GLY K 108 . ? 1_555 ? 
232 AG5 10 ASP K  110 ? ASP K 109 . ? 1_555 ? 
233 AG5 10 HIS K  111 ? HIS K 110 . ? 1_555 ? 
234 AG5 10 ILE K  113 ? ILE K 112 . ? 1_555 ? 
235 AG5 10 ILE K  114 ? ILE K 113 . ? 1_555 ? 
236 AG5 10 ARG K  116 ? ARG K 115 . ? 1_555 ? 
237 AG5 10 ILE K  152 ? ILE K 151 . ? 1_555 ? 
238 AG6 9  LQW X  .   ? LQW D 201 . ? 1_555 ? 
239 AG6 9  SER L  106 ? SER L 105 . ? 1_555 ? 
240 AG6 9  LEU L  107 ? LEU L 106 . ? 1_555 ? 
241 AG6 9  GLY L  109 ? GLY L 108 . ? 1_555 ? 
242 AG6 9  ASP L  110 ? ASP L 109 . ? 1_555 ? 
243 AG6 9  HIS L  111 ? HIS L 110 . ? 1_555 ? 
244 AG6 9  ILE L  113 ? ILE L 112 . ? 1_555 ? 
245 AG6 9  ILE L  114 ? ILE L 113 . ? 1_555 ? 
246 AG6 9  ARG L  116 ? ARG L 115 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6SPI 
_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]   0.008809 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000529 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005137 
_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]   0.006837 
_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  
CL 
N  
O  
S  
SE 
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 2   ? 55.824  -19.444 69.391 1.00 98.69  ? 1   ALA A N   1 
ATOM   2     C  CA  . ALA A  1 2   ? 54.679  -20.116 68.739 1.00 94.77  ? 1   ALA A CA  1 
ATOM   3     C  C   . ALA A  1 2   ? 54.996  -21.612 68.535 1.00 90.33  ? 1   ALA A C   1 
ATOM   4     O  O   . ALA A  1 2   ? 56.134  -22.028 68.326 1.00 86.67  ? 1   ALA A O   1 
ATOM   5     C  CB  . ALA A  1 2   ? 54.439  -19.387 67.427 1.00 87.82  ? 1   ALA A CB  1 
ATOM   6     N  N   . THR A  1 3   ? 53.935  -22.418 68.351 1.00 78.39  ? 2   THR A N   1 
ATOM   7     C  CA  . THR A  1 3   ? 53.978  -23.683 67.624 1.00 62.66  ? 2   THR A CA  1 
ATOM   8     C  C   . THR A  1 3   ? 53.446  -23.483 66.197 1.00 52.37  ? 2   THR A C   1 
ATOM   9     O  O   . THR A  1 3   ? 52.360  -22.936 65.993 1.00 48.43  ? 2   THR A O   1 
ATOM   10    C  CB  . THR A  1 3   ? 53.311  -24.769 68.468 1.00 61.77  ? 2   THR A CB  1 
ATOM   11    O  OG1 . THR A  1 3   ? 53.414  -26.071 67.894 1.00 64.30  ? 2   THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 3   ? 51.838  -24.568 68.750 1.00 69.14  ? 2   THR A CG2 1 
ATOM   13    N  N   . LYS A  1 4   ? 54.280  -23.816 65.202 1.00 45.30  ? 3   LYS A N   1 
ATOM   14    C  CA  . LYS A  1 4   ? 53.997  -23.554 63.800 1.00 39.75  ? 3   LYS A CA  1 
ATOM   15    C  C   . LYS A  1 4   ? 53.883  -24.883 63.059 1.00 38.38  ? 3   LYS A C   1 
ATOM   16    O  O   . LYS A  1 4   ? 54.721  -25.782 63.197 1.00 40.15  ? 3   LYS A O   1 
ATOM   17    C  CB  . LYS A  1 4   ? 55.078  -22.714 63.113 1.00 37.61  ? 3   LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 4   ? 54.958  -21.200 63.260 1.00 41.52  ? 3   LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 4   ? 56.089  -20.424 62.614 0.20 39.32  ? 3   LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 4   ? 56.503  -19.199 63.404 0.20 39.29  ? 3   LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 4   ? 57.773  -18.641 62.894 0.20 39.12  ? 3   LYS A NZ  1 
ATOM   22    N  N   . VAL A  1 5   ? 52.852  -24.961 62.218 1.00 34.82  ? 4   VAL A N   1 
ATOM   23    C  CA  . VAL A  1 5   ? 52.545  -26.149 61.449 1.00 28.74  ? 4   VAL A CA  1 
ATOM   24    C  C   . VAL A  1 5   ? 52.260  -25.704 60.018 1.00 25.72  ? 4   VAL A C   1 
ATOM   25    O  O   . VAL A  1 5   ? 51.885  -24.559 59.771 1.00 28.19  ? 4   VAL A O   1 
ATOM   26    C  CB  . VAL A  1 5   ? 51.343  -26.858 62.091 1.00 28.40  ? 4   VAL A CB  1 
ATOM   27    C  CG1 . VAL A  1 5   ? 50.732  -27.892 61.184 1.00 30.07  ? 4   VAL A CG1 1 
ATOM   28    C  CG2 . VAL A  1 5   ? 51.713  -27.479 63.425 1.00 28.06  ? 4   VAL A CG2 1 
ATOM   29    N  N   . VAL A  1 6   ? 52.462  -26.608 59.065 1.00 23.29  ? 5   VAL A N   1 
ATOM   30    C  CA  . VAL A  1 6   ? 52.242  -26.225 57.683 1.00 23.56  ? 5   VAL A CA  1 
ATOM   31    C  C   . VAL A  1 6   ? 51.629  -27.390 56.908 1.00 24.31  ? 5   VAL A C   1 
ATOM   32    O  O   . VAL A  1 6   ? 51.689  -28.543 57.331 1.00 24.30  ? 5   VAL A O   1 
ATOM   33    C  CB  . VAL A  1 6   ? 53.541  -25.723 57.033 1.00 23.38  ? 5   VAL A CB  1 
ATOM   34    C  CG1 . VAL A  1 6   ? 54.527  -26.861 56.794 1.00 22.84  ? 5   VAL A CG1 1 
ATOM   35    C  CG2 . VAL A  1 6   ? 53.258  -24.969 55.744 1.00 23.99  ? 5   VAL A CG2 1 
ATOM   36    N  N   . CYS A  1 7   ? 51.045  -27.062 55.758 1.00 24.41  ? 6   CYS A N   1 
ATOM   37    C  CA  . CYS A  1 7   ? 50.384  -28.067 54.956 1.00 24.59  ? 6   CYS A CA  1 
ATOM   38    C  C   . CYS A  1 7   ? 50.446  -27.638 53.498 1.00 24.98  ? 6   CYS A C   1 
ATOM   39    O  O   . CYS A  1 7   ? 50.083  -26.509 53.178 1.00 27.05  ? 6   CYS A O   1 
ATOM   40    C  CB  . CYS A  1 7   ? 48.938  -28.180 55.405 1.00 23.97  ? 6   CYS A CB  1 
ATOM   41    S  SG  . CYS A  1 7   ? 48.018  -29.445 54.506 1.00 28.42  ? 6   CYS A SG  1 
ATOM   42    N  N   . VAL A  1 8   ? 50.916  -28.535 52.636 1.00 24.44  ? 7   VAL A N   1 
ATOM   43    C  CA  . VAL A  1 8   ? 50.970  -28.257 51.208 1.00 25.49  ? 7   VAL A CA  1 
ATOM   44    C  C   . VAL A  1 8   ? 49.819  -29.012 50.551 1.00 26.48  ? 7   VAL A C   1 
ATOM   45    O  O   . VAL A  1 8   ? 49.760  -30.234 50.660 1.00 27.93  ? 7   VAL A O   1 
ATOM   46    C  CB  . VAL A  1 8   ? 52.313  -28.710 50.598 1.00 23.77  ? 7   VAL A CB  1 
ATOM   47    C  CG1 . VAL A  1 8   ? 52.323  -28.523 49.095 1.00 22.70  ? 7   VAL A CG1 1 
ATOM   48    C  CG2 . VAL A  1 8   ? 53.514  -28.058 51.246 1.00 24.12  ? 7   VAL A CG2 1 
ATOM   49    N  N   . LEU A  1 9   ? 48.911  -28.293 49.885 1.00 26.61  ? 8   LEU A N   1 
ATOM   50    C  CA  . LEU A  1 9   ? 47.765  -28.944 49.274 1.00 26.65  ? 8   LEU A CA  1 
ATOM   51    C  C   . LEU A  1 9   ? 48.090  -29.251 47.817 1.00 27.18  ? 8   LEU A C   1 
ATOM   52    O  O   . LEU A  1 9   ? 48.451  -28.344 47.073 1.00 29.48  ? 8   LEU A O   1 
ATOM   53    C  CB  . LEU A  1 9   ? 46.547  -28.025 49.372 1.00 25.44  ? 8   LEU A CB  1 
ATOM   54    C  CG  . LEU A  1 9   ? 46.142  -27.582 50.772 1.00 25.83  ? 8   LEU A CG  1 
ATOM   55    C  CD1 . LEU A  1 9   ? 45.102  -26.485 50.673 1.00 26.09  ? 8   LEU A CD1 1 
ATOM   56    C  CD2 . LEU A  1 9   ? 45.545  -28.730 51.563 1.00 26.55  ? 8   LEU A CD2 1 
ATOM   57    N  N   . LYS A  1 10  ? 47.937  -30.528 47.429 1.00 27.42  ? 9   LYS A N   1 
ATOM   58    C  CA  . LYS A  1 10  ? 48.011  -30.973 46.043 1.00 28.40  ? 9   LYS A CA  1 
ATOM   59    C  C   . LYS A  1 10  ? 46.849  -31.921 45.760 1.00 27.43  ? 9   LYS A C   1 
ATOM   60    O  O   . LYS A  1 10  ? 46.281  -32.482 46.690 1.00 25.08  ? 9   LYS A O   1 
ATOM   61    C  CB  . LYS A  1 10  ? 49.350  -31.666 45.751 1.00 28.13  ? 9   LYS A CB  1 
ATOM   62    C  CG  . LYS A  1 10  ? 50.499  -30.715 45.441 1.00 30.52  ? 9   LYS A CG  1 
ATOM   63    C  CD  . LYS A  1 10  ? 51.832  -31.360 45.181 0.40 30.09  ? 9   LYS A CD  1 
ATOM   64    C  CE  . LYS A  1 10  ? 52.877  -30.294 45.349 0.40 29.29  ? 9   LYS A CE  1 
ATOM   65    N  NZ  . LYS A  1 10  ? 53.912  -30.748 46.303 0.40 29.90  ? 9   LYS A NZ  1 
ATOM   66    N  N   . GLY A  1 11  ? 46.504  -32.065 44.483 1.00 28.39  ? 10  GLY A N   1 
ATOM   67    C  CA  . GLY A  1 11  ? 45.479  -33.015 44.080 1.00 32.81  ? 10  GLY A CA  1 
ATOM   68    C  C   . GLY A  1 11  ? 45.540  -33.322 42.595 1.00 39.55  ? 10  GLY A C   1 
ATOM   69    O  O   . GLY A  1 11  ? 46.541  -33.033 41.971 1.00 44.53  ? 10  GLY A O   1 
ATOM   70    N  N   . ASP A  1 12  ? 44.468  -33.898 42.056 1.00 43.26  ? 11  ASP A N   1 
ATOM   71    C  CA  . ASP A  1 12  ? 44.470  -34.395 40.691 1.00 42.90  ? 11  ASP A CA  1 
ATOM   72    C  C   . ASP A  1 12  ? 44.386  -33.250 39.690 1.00 41.93  ? 11  ASP A C   1 
ATOM   73    O  O   . ASP A  1 12  ? 44.858  -33.383 38.564 1.00 39.95  ? 11  ASP A O   1 
ATOM   74    C  CB  . ASP A  1 12  ? 43.292  -35.347 40.465 1.00 43.12  ? 11  ASP A CB  1 
ATOM   75    C  CG  . ASP A  1 12  ? 43.437  -36.603 41.277 1.00 44.19  ? 11  ASP A CG  1 
ATOM   76    O  OD1 . ASP A  1 12  ? 44.593  -37.058 41.429 1.00 45.36  ? 11  ASP A OD1 1 
ATOM   77    O  OD2 . ASP A  1 12  ? 42.404  -37.097 41.735 1.00 43.50  ? 11  ASP A OD2 1 
ATOM   78    N  N   . GLY A  1 13  ? 43.750  -32.144 40.101 1.00 46.95  ? 12  GLY A N   1 
ATOM   79    C  CA  . GLY A  1 13  ? 43.467  -31.055 39.186 1.00 50.87  ? 12  GLY A CA  1 
ATOM   80    C  C   . GLY A  1 13  ? 44.531  -29.970 39.297 1.00 51.97  ? 12  GLY A C   1 
ATOM   81    O  O   . GLY A  1 13  ? 45.635  -30.234 39.773 1.00 53.07  ? 12  GLY A O   1 
ATOM   82    N  N   . PRO A  1 14  ? 44.198  -28.708 38.943 1.00 51.12  ? 13  PRO A N   1 
ATOM   83    C  CA  . PRO A  1 14  ? 45.134  -27.599 39.091 1.00 51.94  ? 13  PRO A CA  1 
ATOM   84    C  C   . PRO A  1 14  ? 45.167  -26.968 40.486 1.00 51.78  ? 13  PRO A C   1 
ATOM   85    O  O   . PRO A  1 14  ? 45.886  -25.992 40.701 1.00 50.05  ? 13  PRO A O   1 
ATOM   86    C  CB  . PRO A  1 14  ? 44.559  -26.606 38.061 1.00 53.76  ? 13  PRO A CB  1 
ATOM   87    C  CG  . PRO A  1 14  ? 43.050  -26.819 38.112 1.00 50.18  ? 13  PRO A CG  1 
ATOM   88    C  CD  . PRO A  1 14  ? 42.889  -28.292 38.405 1.00 50.12  ? 13  PRO A CD  1 
ATOM   89    N  N   . VAL A  1 15  ? 44.385  -27.495 41.434 1.00 49.84  ? 14  VAL A N   1 
ATOM   90    C  CA  . VAL A  1 15  ? 44.304  -26.838 42.729 1.00 45.91  ? 14  VAL A CA  1 
ATOM   91    C  C   . VAL A  1 15  ? 45.560  -27.138 43.537 1.00 44.16  ? 14  VAL A C   1 
ATOM   92    O  O   . VAL A  1 15  ? 45.930  -28.303 43.696 1.00 44.14  ? 14  VAL A O   1 
ATOM   93    C  CB  . VAL A  1 15  ? 43.024  -27.211 43.496 1.00 43.19  ? 14  VAL A CB  1 
ATOM   94    C  CG1 . VAL A  1 15  ? 42.987  -26.551 44.860 1.00 39.77  ? 14  VAL A CG1 1 
ATOM   95    C  CG2 . VAL A  1 15  ? 41.803  -26.771 42.708 1.00 42.88  ? 14  VAL A CG2 1 
ATOM   96    N  N   . GLN A  1 16  ? 46.207  -26.080 44.034 1.00 43.79  ? 15  GLN A N   1 
ATOM   97    C  CA  . GLN A  1 16  ? 47.365  -26.262 44.902 1.00 39.97  ? 15  GLN A CA  1 
ATOM   98    C  C   . GLN A  1 16  ? 47.549  -25.033 45.788 1.00 34.44  ? 15  GLN A C   1 
ATOM   99    O  O   . GLN A  1 16  ? 47.101  -23.942 45.422 1.00 33.83  ? 15  GLN A O   1 
ATOM   100   C  CB  . GLN A  1 16  ? 48.619  -26.581 44.094 1.00 44.44  ? 15  GLN A CB  1 
ATOM   101   C  CG  . GLN A  1 16  ? 49.044  -25.472 43.127 1.00 46.15  ? 15  GLN A CG  1 
ATOM   102   C  CD  . GLN A  1 16  ? 50.321  -25.865 42.421 1.00 48.67  ? 15  GLN A CD  1 
ATOM   103   O  OE1 . GLN A  1 16  ? 50.654  -27.039 42.305 1.00 47.65  ? 15  GLN A OE1 1 
ATOM   104   N  NE2 . GLN A  1 16  ? 51.069  -24.884 41.946 1.00 56.45  ? 15  GLN A NE2 1 
ATOM   105   N  N   . GLY A  1 17  ? 48.192  -25.231 46.945 1.00 29.12  ? 16  GLY A N   1 
ATOM   106   C  CA  . GLY A  1 17  ? 48.373  -24.137 47.875 1.00 26.47  ? 16  GLY A CA  1 
ATOM   107   C  C   . GLY A  1 17  ? 49.193  -24.537 49.102 1.00 25.61  ? 16  GLY A C   1 
ATOM   108   O  O   . GLY A  1 17  ? 49.527  -25.707 49.303 1.00 28.91  ? 16  GLY A O   1 
ATOM   109   N  N   . ILE A  1 18  ? 49.515  -23.530 49.919 1.00 21.26  ? 17  ILE A N   1 
ATOM   110   C  CA  . ILE A  1 18  ? 50.236  -23.720 51.162 1.00 19.23  ? 17  ILE A CA  1 
ATOM   111   C  C   . ILE A  1 18  ? 49.385  -23.101 52.260 1.00 18.44  ? 17  ILE A C   1 
ATOM   112   O  O   . ILE A  1 18  ? 48.957  -21.965 52.120 1.00 19.30  ? 17  ILE A O   1 
ATOM   113   C  CB  . ILE A  1 18  ? 51.618  -23.036 51.081 1.00 18.05  ? 17  ILE A CB  1 
ATOM   114   C  CG1 . ILE A  1 18  ? 52.488  -23.642 49.982 1.00 17.88  ? 17  ILE A CG1 1 
ATOM   115   C  CG2 . ILE A  1 18  ? 52.316  -23.041 52.433 1.00 17.03  ? 17  ILE A CG2 1 
ATOM   116   C  CD1 . ILE A  1 18  ? 53.810  -22.944 49.801 1.00 19.11  ? 17  ILE A CD1 1 
ATOM   117   N  N   . ILE A  1 19  ? 49.155  -23.834 53.350 1.00 17.76  ? 18  ILE A N   1 
ATOM   118   C  CA  . ILE A  1 19  ? 48.415  -23.260 54.458 1.00 19.58  ? 18  ILE A CA  1 
ATOM   119   C  C   . ILE A  1 19  ? 49.260  -23.375 55.717 1.00 21.34  ? 18  ILE A C   1 
ATOM   120   O  O   . ILE A  1 19  ? 49.747  -24.453 56.030 1.00 24.18  ? 18  ILE A O   1 
ATOM   121   C  CB  . ILE A  1 19  ? 47.048  -23.946 54.633 1.00 18.97  ? 18  ILE A CB  1 
ATOM   122   C  CG1 . ILE A  1 19  ? 46.151  -23.789 53.394 1.00 18.53  ? 18  ILE A CG1 1 
ATOM   123   C  CG2 . ILE A  1 19  ? 46.347  -23.452 55.891 1.00 18.68  ? 18  ILE A CG2 1 
ATOM   124   C  CD1 . ILE A  1 19  ? 45.744  -22.369 53.050 1.00 16.74  ? 18  ILE A CD1 1 
ATOM   125   N  N   . ASN A  1 20  ? 49.399  -22.259 56.435 1.00 22.00  ? 19  ASN A N   1 
ATOM   126   C  CA  . ASN A  1 20  ? 50.144  -22.238 57.684 1.00 24.04  ? 19  ASN A CA  1 
ATOM   127   C  C   . ASN A  1 20  ? 49.179  -22.243 58.860 1.00 25.87  ? 19  ASN A C   1 
ATOM   128   O  O   . ASN A  1 20  ? 48.089  -21.684 58.778 1.00 29.71  ? 19  ASN A O   1 
ATOM   129   C  CB  . ASN A  1 20  ? 51.022  -20.997 57.792 1.00 24.57  ? 19  ASN A CB  1 
ATOM   130   C  CG  . ASN A  1 20  ? 51.890  -20.842 56.555 1.00 26.76  ? 19  ASN A CG  1 
ATOM   131   O  OD1 . ASN A  1 20  ? 51.547  -20.105 55.641 1.00 25.53  ? 19  ASN A OD1 1 
ATOM   132   N  ND2 . ASN A  1 20  ? 52.984  -21.578 56.472 1.00 30.29  ? 19  ASN A ND2 1 
ATOM   133   N  N   . PHE A  1 21  ? 49.605  -22.867 59.958 1.00 26.94  ? 20  PHE A N   1 
ATOM   134   C  CA  . PHE A  1 21  ? 48.846  -22.853 61.197 1.00 29.92  ? 20  PHE A CA  1 
ATOM   135   C  C   . PHE A  1 21  ? 49.780  -22.391 62.303 1.00 33.09  ? 20  PHE A C   1 
ATOM   136   O  O   . PHE A  1 21  ? 50.902  -22.876 62.397 1.00 33.42  ? 20  PHE A O   1 
ATOM   137   C  CB  . PHE A  1 21  ? 48.371  -24.252 61.568 1.00 29.88  ? 20  PHE A CB  1 
ATOM   138   C  CG  . PHE A  1 21  ? 47.447  -24.913 60.587 1.00 31.14  ? 20  PHE A CG  1 
ATOM   139   C  CD1 . PHE A  1 21  ? 47.901  -25.331 59.343 1.00 30.69  ? 20  PHE A CD1 1 
ATOM   140   C  CD2 . PHE A  1 21  ? 46.128  -25.179 60.940 1.00 32.13  ? 20  PHE A CD2 1 
ATOM   141   C  CE1 . PHE A  1 21  ? 47.051  -25.975 58.456 1.00 31.32  ? 20  PHE A CE1 1 
ATOM   142   C  CE2 . PHE A  1 21  ? 45.268  -25.801 60.041 1.00 30.96  ? 20  PHE A CE2 1 
ATOM   143   C  CZ  . PHE A  1 21  ? 45.733  -26.204 58.805 1.00 30.06  ? 20  PHE A CZ  1 
ATOM   144   N  N   . GLU A  1 22  ? 49.302  -21.457 63.127 1.00 39.49  ? 21  GLU A N   1 
ATOM   145   C  CA  . GLU A  1 22  ? 50.122  -20.962 64.215 1.00 44.06  ? 21  GLU A CA  1 
ATOM   146   C  C   . GLU A  1 22  ? 49.256  -20.835 65.461 1.00 45.45  ? 21  GLU A C   1 
ATOM   147   O  O   . GLU A  1 22  ? 48.103  -20.417 65.378 1.00 50.19  ? 21  GLU A O   1 
ATOM   148   C  CB  . GLU A  1 22  ? 50.762  -19.639 63.814 1.00 45.53  ? 21  GLU A CB  1 
ATOM   149   C  CG  . GLU A  1 22  ? 51.917  -19.246 64.721 1.00 56.91  ? 21  GLU A CG  1 
ATOM   150   C  CD  . GLU A  1 22  ? 52.624  -17.947 64.344 1.00 61.79  ? 21  GLU A CD  1 
ATOM   151   O  OE1 . GLU A  1 22  ? 53.086  -17.824 63.192 1.00 57.20  ? 21  GLU A OE1 1 
ATOM   152   O  OE2 . GLU A  1 22  ? 52.668  -17.029 65.205 1.00 68.66  ? 21  GLU A OE2 1 
ATOM   153   N  N   . GLN A  1 23  ? 49.823  -21.215 66.612 1.00 48.51  ? 22  GLN A N   1 
ATOM   154   C  CA  . GLN A  1 23  ? 49.100  -21.182 67.875 1.00 56.25  ? 22  GLN A CA  1 
ATOM   155   C  C   . GLN A  1 23  ? 50.026  -20.631 68.957 1.00 71.65  ? 22  GLN A C   1 
ATOM   156   O  O   . GLN A  1 23  ? 50.936  -21.324 69.405 1.00 80.92  ? 22  GLN A O   1 
ATOM   157   C  CB  . GLN A  1 23  ? 48.624  -22.595 68.216 1.00 48.49  ? 22  GLN A CB  1 
ATOM   158   C  CG  . GLN A  1 23  ? 47.677  -22.647 69.390 1.00 44.13  ? 22  GLN A CG  1 
ATOM   159   C  CD  . GLN A  1 23  ? 47.271  -24.059 69.760 1.00 43.84  ? 22  GLN A CD  1 
ATOM   160   O  OE1 . GLN A  1 23  ? 48.031  -25.016 69.605 1.00 44.80  ? 22  GLN A OE1 1 
ATOM   161   N  NE2 . GLN A  1 23  ? 46.058  -24.200 70.273 1.00 41.40  ? 22  GLN A NE2 1 
ATOM   162   N  N   . LYS A  1 24  ? 49.775  -19.383 69.383 1.00 88.43  ? 23  LYS A N   1 
ATOM   163   C  CA  . LYS A  1 24  ? 50.673  -18.673 70.290 1.00 87.77  ? 23  LYS A CA  1 
ATOM   164   C  C   . LYS A  1 24  ? 50.591  -19.271 71.697 1.00 92.80  ? 23  LYS A C   1 
ATOM   165   O  O   . LYS A  1 24  ? 51.616  -19.607 72.279 1.00 108.44 ? 23  LYS A O   1 
ATOM   166   C  CB  . LYS A  1 24  ? 50.503  -17.148 70.216 1.00 77.77  ? 23  LYS A CB  1 
ATOM   167   C  CG  . LYS A  1 24  ? 51.137  -16.489 68.995 0.70 74.35  ? 23  LYS A CG  1 
ATOM   168   C  CD  . LYS A  1 24  ? 50.935  -14.997 68.905 0.70 68.91  ? 23  LYS A CD  1 
ATOM   169   C  CE  . LYS A  1 24  ? 51.567  -14.412 67.659 0.70 62.59  ? 23  LYS A CE  1 
ATOM   170   N  NZ  . LYS A  1 24  ? 51.097  -13.031 67.433 0.70 56.01  ? 23  LYS A NZ  1 
ATOM   171   N  N   . GLU A  1 25  ? 49.371  -19.419 72.253 1.00 94.61  ? 24  GLU A N   1 
ATOM   172   C  CA  . GLU A  1 25  ? 49.192  -20.044 73.550 1.00 99.67  ? 24  GLU A CA  1 
ATOM   173   C  C   . GLU A  1 25  ? 48.745  -21.488 73.363 1.00 99.92  ? 24  GLU A C   1 
ATOM   174   O  O   . GLU A  1 25  ? 48.103  -21.800 72.370 1.00 96.72  ? 24  GLU A O   1 
ATOM   175   C  CB  . GLU A  1 25  ? 48.187  -19.249 74.382 1.00 100.38 ? 24  GLU A CB  1 
ATOM   176   C  CG  . GLU A  1 25  ? 48.723  -17.848 74.658 1.00 97.73  ? 24  GLU A CG  1 
ATOM   177   C  CD  . GLU A  1 25  ? 47.780  -16.833 75.246 1.00 91.87  ? 24  GLU A CD  1 
ATOM   178   O  OE1 . GLU A  1 25  ? 46.563  -17.027 75.123 1.00 97.56  ? 24  GLU A OE1 1 
ATOM   179   O  OE2 . GLU A  1 25  ? 48.281  -15.863 75.820 1.00 81.79  ? 24  GLU A OE2 1 
ATOM   180   N  N   . SER A  1 26  ? 49.055  -22.334 74.349 1.00 104.67 ? 25  SER A N   1 
ATOM   181   C  CA  . SER A  1 26  ? 48.940  -23.773 74.165 1.00 105.93 ? 25  SER A CA  1 
ATOM   182   C  C   . SER A  1 26  ? 47.488  -24.233 74.020 1.00 107.77 ? 25  SER A C   1 
ATOM   183   O  O   . SER A  1 26  ? 47.230  -25.201 73.314 1.00 113.06 ? 25  SER A O   1 
ATOM   184   C  CB  . SER A  1 26  ? 49.681  -24.551 75.231 0.20 102.04 ? 25  SER A CB  1 
ATOM   185   O  OG  . SER A  1 26  ? 49.192  -25.878 75.302 0.20 98.75  ? 25  SER A OG  1 
ATOM   186   N  N   . ASN A  1 27  ? 46.544  -23.576 74.699 1.00 101.46 ? 26  ASN A N   1 
ATOM   187   C  CA  . ASN A  1 27  ? 45.158  -23.969 74.499 1.00 95.00  ? 26  ASN A CA  1 
ATOM   188   C  C   . ASN A  1 27  ? 44.383  -22.870 73.776 1.00 88.42  ? 26  ASN A C   1 
ATOM   189   O  O   . ASN A  1 27  ? 43.155  -22.871 73.758 1.00 87.60  ? 26  ASN A O   1 
ATOM   190   C  CB  . ASN A  1 27  ? 44.495  -24.531 75.763 1.00 94.10  ? 26  ASN A CB  1 
ATOM   191   C  CG  . ASN A  1 27  ? 44.411  -23.556 76.915 1.00 95.40  ? 26  ASN A CG  1 
ATOM   192   O  OD1 . ASN A  1 27  ? 45.273  -22.703 77.083 1.00 94.15  ? 26  ASN A OD1 1 
ATOM   193   N  ND2 . ASN A  1 27  ? 43.349  -23.658 77.696 1.00 97.67  ? 26  ASN A ND2 1 
ATOM   194   N  N   . GLY A  1 28  ? 45.113  -21.919 73.202 1.00 78.70  ? 27  GLY A N   1 
ATOM   195   C  CA  . GLY A  1 28  ? 44.531  -20.712 72.630 1.00 67.19  ? 27  GLY A CA  1 
ATOM   196   C  C   . GLY A  1 28  ? 44.146  -20.882 71.162 1.00 60.63  ? 27  GLY A C   1 
ATOM   197   O  O   . GLY A  1 28  ? 44.315  -21.956 70.591 1.00 65.06  ? 27  GLY A O   1 
ATOM   198   N  N   . PRO A  1 29  ? 43.638  -19.816 70.504 1.00 52.10  ? 28  PRO A N   1 
ATOM   199   C  CA  . PRO A  1 29  ? 43.164  -19.908 69.122 1.00 45.47  ? 28  PRO A CA  1 
ATOM   200   C  C   . PRO A  1 29  ? 44.298  -20.199 68.140 1.00 36.69  ? 28  PRO A C   1 
ATOM   201   O  O   . PRO A  1 29  ? 45.461  -19.922 68.439 1.00 34.48  ? 28  PRO A O   1 
ATOM   202   C  CB  . PRO A  1 29  ? 42.575  -18.508 68.855 1.00 44.64  ? 28  PRO A CB  1 
ATOM   203   C  CG  . PRO A  1 29  ? 43.321  -17.617 69.804 1.00 43.58  ? 28  PRO A CG  1 
ATOM   204   C  CD  . PRO A  1 29  ? 43.514  -18.457 71.050 1.00 47.51  ? 28  PRO A CD  1 
ATOM   205   N  N   . VAL A  1 30  ? 43.934  -20.759 66.977 1.00 30.65  ? 29  VAL A N   1 
ATOM   206   C  CA  . VAL A  1 30  ? 44.882  -21.111 65.933 1.00 27.53  ? 29  VAL A CA  1 
ATOM   207   C  C   . VAL A  1 30  ? 44.641  -20.204 64.732 1.00 26.69  ? 29  VAL A C   1 
ATOM   208   O  O   . VAL A  1 30  ? 43.525  -20.137 64.227 1.00 27.88  ? 29  VAL A O   1 
ATOM   209   C  CB  . VAL A  1 30  ? 44.733  -22.588 65.521 1.00 26.28  ? 29  VAL A CB  1 
ATOM   210   C  CG1 . VAL A  1 30  ? 45.738  -22.964 64.429 1.00 27.09  ? 29  VAL A CG1 1 
ATOM   211   C  CG2 . VAL A  1 30  ? 44.812  -23.546 66.706 1.00 24.82  ? 29  VAL A CG2 1 
ATOM   212   N  N   . LYS A  1 31  ? 45.685  -19.501 64.281 1.00 25.11  ? 30  LYS A N   1 
ATOM   213   C  CA  . LYS A  1 31  ? 45.573  -18.710 63.071 1.00 24.37  ? 30  LYS A CA  1 
ATOM   214   C  C   . LYS A  1 31  ? 45.875  -19.621 61.888 1.00 24.77  ? 30  LYS A C   1 
ATOM   215   O  O   . LYS A  1 31  ? 46.901  -20.294 61.855 1.00 27.62  ? 30  LYS A O   1 
ATOM   216   C  CB  . LYS A  1 31  ? 46.510  -17.495 63.098 1.00 24.05  ? 30  LYS A CB  1 
ATOM   217   C  CG  . LYS A  1 31  ? 45.972  -16.264 63.833 0.40 24.97  ? 30  LYS A CG  1 
ATOM   218   C  CD  . LYS A  1 31  ? 46.642  -14.954 63.412 0.40 24.80  ? 30  LYS A CD  1 
ATOM   219   C  CE  . LYS A  1 31  ? 45.647  -13.848 63.129 0.40 24.03  ? 30  LYS A CE  1 
ATOM   220   N  NZ  . LYS A  1 31  ? 46.316  -12.639 62.605 0.40 23.12  ? 30  LYS A NZ  1 
ATOM   221   N  N   . VAL A  1 32  ? 44.961  -19.643 60.918 1.00 23.89  ? 31  VAL A N   1 
ATOM   222   C  CA  . VAL A  1 32  ? 45.155  -20.444 59.722 1.00 23.29  ? 31  VAL A CA  1 
ATOM   223   C  C   . VAL A  1 32  ? 45.215  -19.502 58.530 1.00 21.99  ? 31  VAL A C   1 
ATOM   224   O  O   . VAL A  1 32  ? 44.233  -18.831 58.240 1.00 22.47  ? 31  VAL A O   1 
ATOM   225   C  CB  . VAL A  1 32  ? 44.009  -21.463 59.567 1.00 22.60  ? 31  VAL A CB  1 
ATOM   226   C  CG1 . VAL A  1 32  ? 44.247  -22.394 58.396 1.00 21.12  ? 31  VAL A CG1 1 
ATOM   227   C  CG2 . VAL A  1 32  ? 43.821  -22.283 60.830 1.00 21.68  ? 31  VAL A CG2 1 
ATOM   228   N  N   . TRP A  1 33  ? 46.360  -19.435 57.848 1.00 22.35  ? 32  TRP A N   1 
ATOM   229   C  CA  . TRP A  1 33  ? 46.433  -18.545 56.704 1.00 23.46  ? 32  TRP A CA  1 
ATOM   230   C  C   . TRP A  1 33  ? 47.297  -19.135 55.600 1.00 23.36  ? 32  TRP A C   1 
ATOM   231   O  O   . TRP A  1 33  ? 48.175  -19.957 55.840 1.00 24.52  ? 32  TRP A O   1 
ATOM   232   C  CB  . TRP A  1 33  ? 46.955  -17.165 57.108 1.00 26.11  ? 32  TRP A CB  1 
ATOM   233   C  CG  . TRP A  1 33  ? 48.445  -17.096 57.233 1.00 29.27  ? 32  TRP A CG  1 
ATOM   234   C  CD1 . TRP A  1 33  ? 49.361  -16.643 56.316 1.00 28.98  ? 32  TRP A CD1 1 
ATOM   235   C  CD2 . TRP A  1 33  ? 49.204  -17.528 58.374 1.00 31.63  ? 32  TRP A CD2 1 
ATOM   236   N  NE1 . TRP A  1 33  ? 50.637  -16.762 56.804 1.00 28.78  ? 32  TRP A NE1 1 
ATOM   237   C  CE2 . TRP A  1 33  ? 50.573  -17.295 58.069 1.00 31.19  ? 32  TRP A CE2 1 
ATOM   238   C  CE3 . TRP A  1 33  ? 48.856  -18.094 59.610 1.00 33.30  ? 32  TRP A CE3 1 
ATOM   239   C  CZ2 . TRP A  1 33  ? 51.590  -17.607 58.971 1.00 31.13  ? 32  TRP A CZ2 1 
ATOM   240   C  CZ3 . TRP A  1 33  ? 49.868  -18.394 60.496 1.00 37.28  ? 32  TRP A CZ3 1 
ATOM   241   C  CH2 . TRP A  1 33  ? 51.215  -18.149 60.182 1.00 35.42  ? 32  TRP A CH2 1 
ATOM   242   N  N   . GLY A  1 34  ? 47.060  -18.644 54.387 1.00 21.84  ? 33  GLY A N   1 
ATOM   243   C  CA  . GLY A  1 34  ? 47.886  -18.981 53.247 1.00 21.02  ? 33  GLY A CA  1 
ATOM   244   C  C   . GLY A  1 34  ? 47.111  -18.731 51.972 1.00 21.62  ? 33  GLY A C   1 
ATOM   245   O  O   . GLY A  1 34  ? 46.155  -17.978 51.957 1.00 23.25  ? 33  GLY A O   1 
ATOM   246   N  N   . SER A  1 35  ? 47.514  -19.405 50.909 1.00 23.21  ? 34  SER A N   1 
ATOM   247   C  CA  . SER A  1 35  ? 46.952  -19.105 49.614 1.00 25.13  ? 34  SER A CA  1 
ATOM   248   C  C   . SER A  1 35  ? 46.679  -20.416 48.866 1.00 28.33  ? 34  SER A C   1 
ATOM   249   O  O   . SER A  1 35  ? 47.477  -21.351 48.942 1.00 32.28  ? 34  SER A O   1 
ATOM   250   C  CB  . SER A  1 35  ? 47.916  -18.217 48.919 1.00 25.20  ? 34  SER A CB  1 
ATOM   251   O  OG  . SER A  1 35  ? 47.557  -18.085 47.563 1.00 29.60  ? 34  SER A OG  1 
ATOM   252   N  N   . ILE A  1 36  ? 45.519  -20.509 48.196 1.00 25.58  ? 35  ILE A N   1 
ATOM   253   C  CA  . ILE A  1 36  ? 45.239  -21.640 47.328 1.00 22.62  ? 35  ILE A CA  1 
ATOM   254   C  C   . ILE A  1 36  ? 44.890  -21.085 45.952 1.00 25.53  ? 35  ILE A C   1 
ATOM   255   O  O   . ILE A  1 36  ? 44.142  -20.118 45.847 1.00 28.87  ? 35  ILE A O   1 
ATOM   256   C  CB  . ILE A  1 36  ? 44.089  -22.493 47.886 1.00 19.94  ? 35  ILE A CB  1 
ATOM   257   C  CG1 . ILE A  1 36  ? 44.284  -22.811 49.367 1.00 18.22  ? 35  ILE A CG1 1 
ATOM   258   C  CG2 . ILE A  1 36  ? 43.882  -23.741 47.041 1.00 19.85  ? 35  ILE A CG2 1 
ATOM   259   C  CD1 . ILE A  1 36  ? 43.090  -23.458 50.018 1.00 16.55  ? 35  ILE A CD1 1 
ATOM   260   N  N   . LYS A  1 37  ? 45.432  -21.705 44.899 1.00 27.54  ? 36  LYS A N   1 
ATOM   261   C  CA  . LYS A  1 37  ? 45.169  -21.230 43.551 1.00 29.19  ? 36  LYS A CA  1 
ATOM   262   C  C   . LYS A  1 37  ? 44.550  -22.352 42.720 1.00 29.76  ? 36  LYS A C   1 
ATOM   263   O  O   . LYS A  1 37  ? 44.583  -23.510 43.123 1.00 33.28  ? 36  LYS A O   1 
ATOM   264   C  CB  . LYS A  1 37  ? 46.440  -20.636 42.934 1.00 31.31  ? 36  LYS A CB  1 
ATOM   265   C  CG  . LYS A  1 37  ? 47.560  -21.622 42.660 1.00 35.20  ? 36  LYS A CG  1 
ATOM   266   C  CD  . LYS A  1 37  ? 48.684  -20.965 41.868 1.00 37.88  ? 36  LYS A CD  1 
ATOM   267   C  CE  . LYS A  1 37  ? 49.791  -21.922 41.486 1.00 38.14  ? 36  LYS A CE  1 
ATOM   268   N  NZ  . LYS A  1 37  ? 51.069  -21.204 41.221 1.00 40.24  ? 36  LYS A NZ  1 
ATOM   269   N  N   . GLY A  1 38  ? 43.962  -21.979 41.577 1.00 30.48  ? 37  GLY A N   1 
ATOM   270   C  CA  . GLY A  1 38  ? 43.356  -22.928 40.650 1.00 29.85  ? 37  GLY A CA  1 
ATOM   271   C  C   . GLY A  1 38  ? 41.907  -23.283 40.994 1.00 31.61  ? 37  GLY A C   1 
ATOM   272   O  O   . GLY A  1 38  ? 41.362  -24.240 40.439 1.00 32.58  ? 37  GLY A O   1 
ATOM   273   N  N   . LEU A  1 39  ? 41.284  -22.534 41.916 1.00 29.68  ? 38  LEU A N   1 
ATOM   274   C  CA  . LEU A  1 39  ? 39.921  -22.807 42.348 1.00 28.13  ? 38  LEU A CA  1 
ATOM   275   C  C   . LEU A  1 39  ? 38.940  -22.069 41.443 1.00 26.91  ? 38  LEU A C   1 
ATOM   276   O  O   . LEU A  1 39  ? 39.283  -21.055 40.845 1.00 25.92  ? 38  LEU A O   1 
ATOM   277   C  CB  . LEU A  1 39  ? 39.749  -22.327 43.790 1.00 28.01  ? 38  LEU A CB  1 
ATOM   278   C  CG  . LEU A  1 39  ? 40.476  -23.163 44.843 1.00 29.21  ? 38  LEU A CG  1 
ATOM   279   C  CD1 . LEU A  1 39  ? 40.539  -22.431 46.165 1.00 28.33  ? 38  LEU A CD1 1 
ATOM   280   C  CD2 . LEU A  1 39  ? 39.805  -24.507 45.046 1.00 28.63  ? 38  LEU A CD2 1 
ATOM   281   N  N   . THR A  1 40  ? 37.711  -22.588 41.351 1.00 26.71  ? 39  THR A N   1 
ATOM   282   C  CA  . THR A  1 40  ? 36.632  -21.858 40.710 1.00 27.31  ? 39  THR A CA  1 
ATOM   283   C  C   . THR A  1 40  ? 36.208  -20.732 41.639 1.00 29.12  ? 39  THR A C   1 
ATOM   284   O  O   . THR A  1 40  ? 36.292  -20.872 42.858 1.00 29.98  ? 39  THR A O   1 
ATOM   285   C  CB  . THR A  1 40  ? 35.431  -22.759 40.403 1.00 25.21  ? 39  THR A CB  1 
ATOM   286   O  OG1 . THR A  1 40  ? 35.151  -23.449 41.618 1.00 25.30  ? 39  THR A OG1 1 
ATOM   287   C  CG2 . THR A  1 40  ? 35.685  -23.737 39.277 1.00 22.77  ? 39  THR A CG2 1 
ATOM   288   N  N   . GLU A  1 41  ? 35.758  -19.615 41.049 1.00 32.41  ? 40  GLU A N   1 
ATOM   289   C  CA  . GLU A  1 41  ? 35.377  -18.458 41.843 1.00 33.68  ? 40  GLU A CA  1 
ATOM   290   C  C   . GLU A  1 41  ? 34.283  -18.878 42.826 1.00 31.49  ? 40  GLU A C   1 
ATOM   291   O  O   . GLU A  1 41  ? 33.421  -19.685 42.482 1.00 30.78  ? 40  GLU A O   1 
ATOM   292   C  CB  . GLU A  1 41  ? 34.885  -17.345 40.923 1.00 36.24  ? 40  GLU A CB  1 
ATOM   293   C  CG  . GLU A  1 41  ? 34.576  -16.072 41.683 1.00 38.44  ? 40  GLU A CG  1 
ATOM   294   C  CD  . GLU A  1 41  ? 34.157  -14.870 40.862 1.00 42.73  ? 40  GLU A CD  1 
ATOM   295   O  OE1 . GLU A  1 41  ? 33.954  -15.023 39.630 1.00 45.12  ? 40  GLU A OE1 1 
ATOM   296   O  OE2 . GLU A  1 41  ? 34.044  -13.781 41.461 1.00 46.06  ? 40  GLU A OE2 1 
ATOM   297   N  N   . GLY A  1 42  ? 34.341  -18.355 44.054 1.00 28.77  ? 41  GLY A N   1 
ATOM   298   C  CA  . GLY A  1 42  ? 33.290  -18.624 45.023 1.00 28.48  ? 41  GLY A CA  1 
ATOM   299   C  C   . GLY A  1 42  ? 33.749  -19.430 46.238 1.00 26.76  ? 41  GLY A C   1 
ATOM   300   O  O   . GLY A  1 42  ? 34.950  -19.532 46.495 1.00 30.63  ? 41  GLY A O   1 
ATOM   301   N  N   . LEU A  1 43  ? 32.772  -19.973 46.980 1.00 23.93  ? 42  LEU A N   1 
ATOM   302   C  CA  . LEU A  1 43  ? 33.012  -20.633 48.258 1.00 23.53  ? 42  LEU A CA  1 
ATOM   303   C  C   . LEU A  1 43  ? 33.480  -22.068 48.040 1.00 23.78  ? 42  LEU A C   1 
ATOM   304   O  O   . LEU A  1 43  ? 32.979  -22.745 47.150 1.00 26.42  ? 42  LEU A O   1 
ATOM   305   C  CB  . LEU A  1 43  ? 31.725  -20.633 49.087 1.00 21.69  ? 42  LEU A CB  1 
ATOM   306   C  CG  . LEU A  1 43  ? 31.234  -19.270 49.558 1.00 20.43  ? 42  LEU A CG  1 
ATOM   307   C  CD1 . LEU A  1 43  ? 29.854  -19.388 50.160 1.00 19.73  ? 42  LEU A CD1 1 
ATOM   308   C  CD2 . LEU A  1 43  ? 32.180  -18.676 50.580 1.00 20.41  ? 42  LEU A CD2 1 
ATOM   309   N  N   . HIS A  1 44  ? 34.432  -22.508 48.874 1.00 23.04  ? 43  HIS A N   1 
ATOM   310   C  CA  . HIS A  1 44  ? 34.913  -23.882 48.894 1.00 21.94  ? 43  HIS A CA  1 
ATOM   311   C  C   . HIS A  1 44  ? 35.042  -24.362 50.337 1.00 22.20  ? 43  HIS A C   1 
ATOM   312   O  O   . HIS A  1 44  ? 35.579  -23.657 51.200 1.00 21.28  ? 43  HIS A O   1 
ATOM   313   C  CB  . HIS A  1 44  ? 36.240  -24.007 48.150 1.00 20.59  ? 43  HIS A CB  1 
ATOM   314   C  CG  . HIS A  1 44  ? 36.135  -23.734 46.688 1.00 20.63  ? 43  HIS A CG  1 
ATOM   315   N  ND1 . HIS A  1 44  ? 35.967  -24.748 45.754 1.00 20.83  ? 43  HIS A ND1 1 
ATOM   316   C  CD2 . HIS A  1 44  ? 36.200  -22.576 45.990 1.00 19.98  ? 43  HIS A CD2 1 
ATOM   317   C  CE1 . HIS A  1 44  ? 35.935  -24.223 44.544 1.00 21.05  ? 43  HIS A CE1 1 
ATOM   318   N  NE2 . HIS A  1 44  ? 36.075  -22.892 44.664 1.00 20.67  ? 43  HIS A NE2 1 
ATOM   319   N  N   . GLY A  1 45  ? 34.509  -25.569 50.577 1.00 20.52  ? 44  GLY A N   1 
ATOM   320   C  CA  . GLY A  1 45  ? 34.577  -26.196 51.885 1.00 19.23  ? 44  GLY A CA  1 
ATOM   321   C  C   . GLY A  1 45  ? 36.023  -26.489 52.273 1.00 18.39  ? 44  GLY A C   1 
ATOM   322   O  O   . GLY A  1 45  ? 36.847  -26.869 51.435 1.00 17.10  ? 44  GLY A O   1 
ATOM   323   N  N   . PHE A  1 46  ? 36.310  -26.321 53.563 1.00 18.40  ? 45  PHE A N   1 
ATOM   324   C  CA  . PHE A  1 46  ? 37.675  -26.311 54.048 1.00 17.97  ? 45  PHE A CA  1 
ATOM   325   C  C   . PHE A  1 46  ? 37.696  -27.046 55.378 1.00 18.13  ? 45  PHE A C   1 
ATOM   326   O  O   . PHE A  1 46  ? 37.196  -26.512 56.367 1.00 18.05  ? 45  PHE A O   1 
ATOM   327   C  CB  . PHE A  1 46  ? 38.092  -24.851 54.235 1.00 17.42  ? 45  PHE A CB  1 
ATOM   328   C  CG  . PHE A  1 46  ? 39.561  -24.592 54.423 1.00 17.37  ? 45  PHE A CG  1 
ATOM   329   C  CD1 . PHE A  1 46  ? 40.473  -24.851 53.408 1.00 16.84  ? 45  PHE A CD1 1 
ATOM   330   C  CD2 . PHE A  1 46  ? 40.021  -24.036 55.607 1.00 17.72  ? 45  PHE A CD2 1 
ATOM   331   C  CE1 . PHE A  1 46  ? 41.828  -24.597 53.590 1.00 16.60  ? 45  PHE A CE1 1 
ATOM   332   C  CE2 . PHE A  1 46  ? 41.370  -23.757 55.778 1.00 17.28  ? 45  PHE A CE2 1 
ATOM   333   C  CZ  . PHE A  1 46  ? 42.272  -24.046 54.770 1.00 16.81  ? 45  PHE A CZ  1 
ATOM   334   N  N   . HIS A  1 47  ? 38.247  -28.271 55.388 1.00 18.46  ? 46  HIS A N   1 
ATOM   335   C  CA  . HIS A  1 47  ? 38.119  -29.116 56.562 1.00 18.04  ? 46  HIS A CA  1 
ATOM   336   C  C   . HIS A  1 47  ? 39.410  -29.851 56.879 1.00 18.33  ? 46  HIS A C   1 
ATOM   337   O  O   . HIS A  1 47  ? 40.219  -30.141 55.993 1.00 17.70  ? 46  HIS A O   1 
ATOM   338   C  CB  . HIS A  1 47  ? 37.006  -30.144 56.375 1.00 18.37  ? 46  HIS A CB  1 
ATOM   339   C  CG  . HIS A  1 47  ? 35.780  -29.592 55.738 1.00 19.16  ? 46  HIS A CG  1 
ATOM   340   N  ND1 . HIS A  1 47  ? 35.418  -29.912 54.444 1.00 18.58  ? 46  HIS A ND1 1 
ATOM   341   C  CD2 . HIS A  1 47  ? 34.846  -28.729 56.203 1.00 19.86  ? 46  HIS A CD2 1 
ATOM   342   C  CE1 . HIS A  1 47  ? 34.311  -29.268 54.133 1.00 18.81  ? 46  HIS A CE1 1 
ATOM   343   N  NE2 . HIS A  1 47  ? 33.940  -28.530 55.193 1.00 19.48  ? 46  HIS A NE2 1 
ATOM   344   N  N   . VAL A  1 48  ? 39.564  -30.166 58.172 1.00 18.61  ? 47  VAL A N   1 
ATOM   345   C  CA  . VAL A  1 48  ? 40.547  -31.142 58.596 1.00 19.10  ? 47  VAL A CA  1 
ATOM   346   C  C   . VAL A  1 48  ? 39.863  -32.506 58.643 1.00 21.04  ? 47  VAL A C   1 
ATOM   347   O  O   . VAL A  1 48  ? 38.938  -32.708 59.430 1.00 22.68  ? 47  VAL A O   1 
ATOM   348   C  CB  . VAL A  1 48  ? 41.162  -30.787 59.961 1.00 18.26  ? 47  VAL A CB  1 
ATOM   349   C  CG1 . VAL A  1 48  ? 42.244  -31.804 60.350 1.00 18.20  ? 47  VAL A CG1 1 
ATOM   350   C  CG2 . VAL A  1 48  ? 41.750  -29.388 59.958 1.00 17.17  ? 47  VAL A CG2 1 
ATOM   351   N  N   . HIS A  1 49  ? 40.330  -33.432 57.798 1.00 21.76  ? 48  HIS A N   1 
ATOM   352   C  CA  . HIS A  1 49  ? 39.885  -34.818 57.837 1.00 22.25  ? 48  HIS A CA  1 
ATOM   353   C  C   . HIS A  1 49  ? 40.741  -35.633 58.812 1.00 21.20  ? 48  HIS A C   1 
ATOM   354   O  O   . HIS A  1 49  ? 41.784  -35.170 59.263 1.00 19.86  ? 48  HIS A O   1 
ATOM   355   C  CB  . HIS A  1 49  ? 39.869  -35.398 56.420 1.00 23.60  ? 48  HIS A CB  1 
ATOM   356   C  CG  . HIS A  1 49  ? 38.857  -34.761 55.534 1.00 24.25  ? 48  HIS A CG  1 
ATOM   357   N  ND1 . HIS A  1 49  ? 37.841  -35.483 54.939 1.00 24.21  ? 48  HIS A ND1 1 
ATOM   358   C  CD2 . HIS A  1 49  ? 38.696  -33.479 55.136 1.00 24.80  ? 48  HIS A CD2 1 
ATOM   359   C  CE1 . HIS A  1 49  ? 37.107  -34.667 54.194 1.00 25.46  ? 48  HIS A CE1 1 
ATOM   360   N  NE2 . HIS A  1 49  ? 37.606  -33.433 54.296 1.00 25.62  ? 48  HIS A NE2 1 
ATOM   361   N  N   . GLU A  1 50  ? 40.305  -36.865 59.090 1.00 22.28  ? 49  GLU A N   1 
ATOM   362   C  CA  . GLU A  1 50  ? 40.781  -37.653 60.223 1.00 23.88  ? 49  GLU A CA  1 
ATOM   363   C  C   . GLU A  1 50  ? 42.205  -38.175 60.028 1.00 22.85  ? 49  GLU A C   1 
ATOM   364   O  O   . GLU A  1 50  ? 42.991  -38.153 60.962 1.00 23.24  ? 49  GLU A O   1 
ATOM   365   C  CB  . GLU A  1 50  ? 39.859  -38.848 60.471 1.00 23.91  ? 49  GLU A CB  1 
ATOM   366   C  CG  . GLU A  1 50  ? 40.071  -39.470 61.828 1.00 23.41  ? 49  GLU A CG  1 
ATOM   367   C  CD  . GLU A  1 50  ? 39.189  -40.656 62.160 1.00 24.85  ? 49  GLU A CD  1 
ATOM   368   O  OE1 . GLU A  1 50  ? 38.131  -40.837 61.493 1.00 24.41  ? 49  GLU A OE1 1 
ATOM   369   O  OE2 . GLU A  1 50  ? 39.573  -41.410 63.082 1.00 25.49  ? 49  GLU A OE2 1 
ATOM   370   N  N   . PHE A  1 51  ? 42.521  -38.666 58.826 1.00 22.28  ? 50  PHE A N   1 
ATOM   371   C  CA  . PHE A  1 51  ? 43.744  -39.428 58.614 1.00 22.15  ? 50  PHE A CA  1 
ATOM   372   C  C   . PHE A  1 51  ? 44.732  -38.680 57.735 1.00 22.81  ? 50  PHE A C   1 
ATOM   373   O  O   . PHE A  1 51  ? 44.361  -38.187 56.673 1.00 27.02  ? 50  PHE A O   1 
ATOM   374   C  CB  . PHE A  1 51  ? 43.432  -40.768 57.950 1.00 21.09  ? 50  PHE A CB  1 
ATOM   375   C  CG  . PHE A  1 51  ? 42.425  -41.581 58.714 1.00 21.83  ? 50  PHE A CG  1 
ATOM   376   C  CD1 . PHE A  1 51  ? 42.655  -41.908 60.048 1.00 20.92  ? 50  PHE A CD1 1 
ATOM   377   C  CD2 . PHE A  1 51  ? 41.242  -41.995 58.118 1.00 21.60  ? 50  PHE A CD2 1 
ATOM   378   C  CE1 . PHE A  1 51  ? 41.729  -42.642 60.773 1.00 20.08  ? 50  PHE A CE1 1 
ATOM   379   C  CE2 . PHE A  1 51  ? 40.317  -42.735 58.840 1.00 21.40  ? 50  PHE A CE2 1 
ATOM   380   C  CZ  . PHE A  1 51  ? 40.564  -43.056 60.163 1.00 20.91  ? 50  PHE A CZ  1 
ATOM   381   N  N   . GLY A  1 52  ? 45.988  -38.644 58.192 1.00 22.86  ? 51  GLY A N   1 
ATOM   382   C  CA  . GLY A  1 52  ? 47.122  -38.215 57.384 1.00 23.82  ? 51  GLY A CA  1 
ATOM   383   C  C   . GLY A  1 52  ? 47.542  -39.315 56.414 1.00 23.96  ? 51  GLY A C   1 
ATOM   384   O  O   . GLY A  1 52  ? 48.691  -39.755 56.407 1.00 22.67  ? 51  GLY A O   1 
ATOM   385   N  N   . ASP A  1 53  ? 46.582  -39.767 55.607 1.00 23.68  ? 52  ASP A N   1 
ATOM   386   C  CA  . ASP A  1 53  ? 46.804  -40.923 54.765 1.00 23.73  ? 52  ASP A CA  1 
ATOM   387   C  C   . ASP A  1 53  ? 46.461  -40.542 53.334 1.00 24.82  ? 52  ASP A C   1 
ATOM   388   O  O   . ASP A  1 53  ? 45.313  -40.243 53.030 1.00 25.86  ? 52  ASP A O   1 
ATOM   389   C  CB  . ASP A  1 53  ? 45.979  -42.102 55.273 1.00 22.84  ? 52  ASP A CB  1 
ATOM   390   C  CG  . ASP A  1 53  ? 46.146  -43.378 54.482 1.00 24.58  ? 52  ASP A CG  1 
ATOM   391   O  OD1 . ASP A  1 53  ? 46.523  -43.295 53.285 1.00 22.93  ? 52  ASP A OD1 1 
ATOM   392   O  OD2 . ASP A  1 53  ? 45.891  -44.454 55.078 1.00 27.29  ? 52  ASP A OD2 1 
ATOM   393   N  N   . ASN A  1 54  ? 47.474  -40.549 52.466 1.00 25.65  ? 53  ASN A N   1 
ATOM   394   C  CA  . ASN A  1 54  ? 47.276  -40.117 51.094 1.00 25.55  ? 53  ASN A CA  1 
ATOM   395   C  C   . ASN A  1 54  ? 47.491  -41.307 50.157 1.00 22.57  ? 53  ASN A C   1 
ATOM   396   O  O   . ASN A  1 54  ? 47.681  -41.135 48.960 1.00 21.69  ? 53  ASN A O   1 
ATOM   397   C  CB  . ASN A  1 54  ? 48.146  -38.889 50.804 1.00 30.31  ? 53  ASN A CB  1 
ATOM   398   C  CG  . ASN A  1 54  ? 47.997  -38.336 49.398 1.00 37.64  ? 53  ASN A CG  1 
ATOM   399   O  OD1 . ASN A  1 54  ? 46.886  -38.035 48.956 1.00 40.32  ? 53  ASN A OD1 1 
ATOM   400   N  ND2 . ASN A  1 54  ? 49.109  -38.180 48.688 1.00 40.92  ? 53  ASN A ND2 1 
ATOM   401   N  N   . THR A  1 55  ? 47.417  -42.525 50.705 1.00 20.73  ? 54  THR A N   1 
ATOM   402   C  CA  . THR A  1 55  ? 47.781  -43.721 49.955 1.00 21.49  ? 54  THR A CA  1 
ATOM   403   C  C   . THR A  1 55  ? 46.898  -43.890 48.722 1.00 21.55  ? 54  THR A C   1 
ATOM   404   O  O   . THR A  1 55  ? 47.351  -44.413 47.713 1.00 20.54  ? 54  THR A O   1 
ATOM   405   C  CB  . THR A  1 55  ? 47.724  -44.989 50.807 1.00 21.31  ? 54  THR A CB  1 
ATOM   406   O  OG1 . THR A  1 55  ? 46.402  -45.096 51.318 1.00 22.53  ? 54  THR A OG1 1 
ATOM   407   C  CG2 . THR A  1 55  ? 48.704  -44.983 51.960 1.00 22.33  ? 54  THR A CG2 1 
ATOM   408   N  N   . ALA A  1 56  ? 45.640  -43.450 48.816 1.00 22.85  ? 55  ALA A N   1 
ATOM   409   C  CA  . ALA A  1 56  ? 44.697  -43.580 47.721 1.00 23.29  ? 55  ALA A CA  1 
ATOM   410   C  C   . ALA A  1 56  ? 44.179  -42.200 47.346 1.00 25.02  ? 55  ALA A C   1 
ATOM   411   O  O   . ALA A  1 56  ? 42.982  -42.015 47.141 1.00 30.19  ? 55  ALA A O   1 
ATOM   412   C  CB  . ALA A  1 56  ? 43.574  -44.494 48.138 1.00 22.40  ? 55  ALA A CB  1 
ATOM   413   N  N   . GLY A  1 57  ? 45.086  -41.221 47.279 1.00 25.47  ? 56  GLY A N   1 
ATOM   414   C  CA  . GLY A  1 57  ? 44.700  -39.840 47.034 1.00 26.72  ? 56  GLY A CA  1 
ATOM   415   C  C   . GLY A  1 57  ? 44.016  -39.234 48.255 1.00 28.08  ? 56  GLY A C   1 
ATOM   416   O  O   . GLY A  1 57  ? 44.186  -39.718 49.381 1.00 27.95  ? 56  GLY A O   1 
ATOM   417   N  N   . CYS A  1 58  ? 43.219  -38.181 48.021 1.00 28.49  ? 57  CYS A N   1 
ATOM   418   C  CA  . CYS A  1 58  ? 42.597  -37.473 49.127 1.00 27.08  ? 57  CYS A CA  1 
ATOM   419   C  C   . CYS A  1 58  ? 41.529  -38.328 49.801 1.00 27.02  ? 57  CYS A C   1 
ATOM   420   O  O   . CYS A  1 58  ? 41.225  -38.099 50.967 1.00 25.48  ? 57  CYS A O   1 
ATOM   421   C  CB  . CYS A  1 58  ? 42.014  -36.149 48.662 1.00 27.22  ? 57  CYS A CB  1 
ATOM   422   S  SG  . CYS A  1 58  ? 43.278  -34.947 48.167 1.00 27.88  ? 57  CYS A SG  1 
ATOM   423   N  N   . THR A  1 59  ? 40.996  -39.324 49.077 1.00 27.56  ? 58  THR A N   1 
ATOM   424   C  CA  . THR A  1 59  ? 39.937  -40.187 49.583 1.00 27.15  ? 58  THR A CA  1 
ATOM   425   C  C   . THR A  1 59  ? 40.351  -40.845 50.892 1.00 25.65  ? 58  THR A C   1 
ATOM   426   O  O   . THR A  1 59  ? 39.528  -41.000 51.793 1.00 27.73  ? 58  THR A O   1 
ATOM   427   C  CB  . THR A  1 59  ? 39.623  -41.352 48.643 1.00 26.93  ? 58  THR A CB  1 
ATOM   428   O  OG1 . THR A  1 59  ? 39.467  -40.800 47.336 1.00 29.06  ? 58  THR A OG1 1 
ATOM   429   C  CG2 . THR A  1 59  ? 38.385  -42.121 49.056 1.00 24.08  ? 58  THR A CG2 1 
ATOM   430   N  N   . SER A  1 60  ? 41.617  -41.252 50.979 1.00 21.92  ? 59  SER A N   1 
ATOM   431   C  CA  . SER A  1 60  ? 42.030  -42.100 52.082 1.00 19.98  ? 59  SER A CA  1 
ATOM   432   C  C   . SER A  1 60  ? 42.211  -41.288 53.362 1.00 18.21  ? 59  SER A C   1 
ATOM   433   O  O   . SER A  1 60  ? 42.538  -41.837 54.408 1.00 16.77  ? 59  SER A O   1 
ATOM   434   C  CB  . SER A  1 60  ? 43.207  -42.980 51.726 1.00 20.98  ? 59  SER A CB  1 
ATOM   435   O  OG  . SER A  1 60  ? 44.279  -42.205 51.234 1.00 24.43  ? 59  SER A OG  1 
ATOM   436   N  N   . ALA A  1 61  ? 41.920  -39.981 53.276 1.00 18.91  ? 60  ALA A N   1 
ATOM   437   C  CA  . ALA A  1 61  ? 42.005  -39.070 54.409 1.00 19.09  ? 60  ALA A CA  1 
ATOM   438   C  C   . ALA A  1 61  ? 40.853  -39.330 55.376 1.00 20.06  ? 60  ALA A C   1 
ATOM   439   O  O   . ALA A  1 61  ? 40.907  -38.918 56.536 1.00 21.48  ? 60  ALA A O   1 
ATOM   440   C  CB  . ALA A  1 61  ? 41.999  -37.649 53.930 1.00 17.91  ? 60  ALA A CB  1 
ATOM   441   N  N   . GLY A  1 62  ? 39.813  -40.010 54.880 1.00 18.53  ? 61  GLY A N   1 
ATOM   442   C  CA  . GLY A  1 62  ? 38.655  -40.357 55.680 1.00 18.20  ? 61  GLY A CA  1 
ATOM   443   C  C   . GLY A  1 62  ? 37.712  -39.173 55.867 1.00 18.46  ? 61  GLY A C   1 
ATOM   444   O  O   . GLY A  1 62  ? 37.755  -38.204 55.100 1.00 17.92  ? 61  GLY A O   1 
ATOM   445   N  N   . PRO A  1 63  ? 36.837  -39.217 56.913 1.00 18.20  ? 62  PRO A N   1 
ATOM   446   C  CA  . PRO A  1 63  ? 35.806  -38.190 57.110 1.00 17.42  ? 62  PRO A CA  1 
ATOM   447   C  C   . PRO A  1 63  ? 36.376  -36.950 57.797 1.00 17.82  ? 62  PRO A C   1 
ATOM   448   O  O   . PRO A  1 63  ? 37.560  -36.921 58.148 1.00 17.19  ? 62  PRO A O   1 
ATOM   449   C  CB  . PRO A  1 63  ? 34.846  -38.913 58.058 1.00 16.20  ? 62  PRO A CB  1 
ATOM   450   C  CG  . PRO A  1 63  ? 35.752  -39.758 58.920 1.00 16.21  ? 62  PRO A CG  1 
ATOM   451   C  CD  . PRO A  1 63  ? 36.817  -40.245 57.967 1.00 16.88  ? 62  PRO A CD  1 
ATOM   452   N  N   . HIS A  1 64  ? 35.524  -35.931 57.998 1.00 18.73  ? 63  HIS A N   1 
ATOM   453   C  CA  . HIS A  1 64  ? 35.946  -34.772 58.775 1.00 19.30  ? 63  HIS A CA  1 
ATOM   454   C  C   . HIS A  1 64  ? 36.413  -35.259 60.146 1.00 18.77  ? 63  HIS A C   1 
ATOM   455   O  O   . HIS A  1 64  ? 35.755  -36.111 60.740 1.00 19.51  ? 63  HIS A O   1 
ATOM   456   C  CB  . HIS A  1 64  ? 34.795  -33.769 58.932 1.00 17.97  ? 63  HIS A CB  1 
ATOM   457   C  CG  . HIS A  1 64  ? 34.304  -33.161 57.662 1.00 17.48  ? 63  HIS A CG  1 
ATOM   458   N  ND1 . HIS A  1 64  ? 33.179  -32.361 57.620 1.00 17.98  ? 63  HIS A ND1 1 
ATOM   459   C  CD2 . HIS A  1 64  ? 34.763  -33.226 56.399 1.00 16.26  ? 63  HIS A CD2 1 
ATOM   460   C  CE1 . HIS A  1 64  ? 32.974  -31.952 56.390 1.00 17.08  ? 63  HIS A CE1 1 
ATOM   461   N  NE2 . HIS A  1 64  ? 33.934  -32.472 55.620 1.00 16.01  ? 63  HIS A NE2 1 
ATOM   462   N  N   . PHE A  1 65  ? 37.532  -34.713 60.636 1.00 17.87  ? 64  PHE A N   1 
ATOM   463   C  CA  . PHE A  1 65  ? 38.048  -35.064 61.951 1.00 18.93  ? 64  PHE A CA  1 
ATOM   464   C  C   . PHE A  1 65  ? 36.981  -34.810 63.020 1.00 18.65  ? 64  PHE A C   1 
ATOM   465   O  O   . PHE A  1 65  ? 36.571  -33.674 63.235 1.00 18.16  ? 64  PHE A O   1 
ATOM   466   C  CB  . PHE A  1 65  ? 39.349  -34.302 62.232 1.00 19.19  ? 64  PHE A CB  1 
ATOM   467   C  CG  . PHE A  1 65  ? 39.975  -34.598 63.573 1.00 20.28  ? 64  PHE A CG  1 
ATOM   468   C  CD1 . PHE A  1 65  ? 40.049  -35.896 64.072 1.00 19.25  ? 64  PHE A CD1 1 
ATOM   469   C  CD2 . PHE A  1 65  ? 40.510  -33.564 64.336 1.00 22.12  ? 64  PHE A CD2 1 
ATOM   470   C  CE1 . PHE A  1 65  ? 40.632  -36.148 65.311 1.00 19.98  ? 64  PHE A CE1 1 
ATOM   471   C  CE2 . PHE A  1 65  ? 41.111  -33.816 65.567 1.00 23.45  ? 64  PHE A CE2 1 
ATOM   472   C  CZ  . PHE A  1 65  ? 41.165  -35.112 66.055 1.00 21.73  ? 64  PHE A CZ  1 
ATOM   473   N  N   . ASN A  1 66  ? 36.543  -35.870 63.703 1.00 18.62  ? 65  ASN A N   1 
ATOM   474   C  CA  . ASN A  1 66  ? 35.343  -35.764 64.516 1.00 19.23  ? 65  ASN A CA  1 
ATOM   475   C  C   . ASN A  1 66  ? 35.516  -36.464 65.869 1.00 20.57  ? 65  ASN A C   1 
ATOM   476   O  O   . ASN A  1 66  ? 34.719  -37.320 66.233 1.00 20.23  ? 65  ASN A O   1 
ATOM   477   C  CB  . ASN A  1 66  ? 34.120  -36.261 63.730 1.00 18.74  ? 65  ASN A CB  1 
ATOM   478   C  CG  . ASN A  1 66  ? 32.815  -36.072 64.480 1.00 19.01  ? 65  ASN A CG  1 
ATOM   479   O  OD1 . ASN A  1 66  ? 32.721  -35.262 65.393 1.00 20.09  ? 65  ASN A OD1 1 
ATOM   480   N  ND2 . ASN A  1 66  ? 31.799  -36.816 64.110 1.00 18.15  ? 65  ASN A ND2 1 
ATOM   481   N  N   . PRO A  1 67  ? 36.510  -36.100 66.705 1.00 22.70  ? 66  PRO A N   1 
ATOM   482   C  CA  . PRO A  1 67  ? 36.771  -36.846 67.938 1.00 23.93  ? 66  PRO A CA  1 
ATOM   483   C  C   . PRO A  1 67  ? 35.642  -36.806 68.963 1.00 26.90  ? 66  PRO A C   1 
ATOM   484   O  O   . PRO A  1 67  ? 35.611  -37.653 69.855 1.00 29.10  ? 66  PRO A O   1 
ATOM   485   C  CB  . PRO A  1 67  ? 38.024  -36.185 68.531 1.00 22.73  ? 66  PRO A CB  1 
ATOM   486   C  CG  . PRO A  1 67  ? 38.061  -34.820 67.920 1.00 22.37  ? 66  PRO A CG  1 
ATOM   487   C  CD  . PRO A  1 67  ? 37.424  -34.959 66.550 1.00 23.23  ? 66  PRO A CD  1 
ATOM   488   N  N   . LEU A  1 68  ? 34.719  -35.843 68.834 1.00 28.54  ? 67  LEU A N   1 
ATOM   489   C  CA  . LEU A  1 68  ? 33.661  -35.713 69.832 1.00 28.88  ? 67  LEU A CA  1 
ATOM   490   C  C   . LEU A  1 68  ? 32.336  -36.301 69.341 1.00 30.09  ? 67  LEU A C   1 
ATOM   491   O  O   . LEU A  1 68  ? 31.325  -36.164 70.021 1.00 33.91  ? 67  LEU A O   1 
ATOM   492   C  CB  . LEU A  1 68  ? 33.494  -34.243 70.224 1.00 29.24  ? 67  LEU A CB  1 
ATOM   493   C  CG  . LEU A  1 68  ? 34.632  -33.595 70.996 1.00 30.74  ? 67  LEU A CG  1 
ATOM   494   C  CD1 . LEU A  1 68  ? 34.186  -32.216 71.486 1.00 32.44  ? 67  LEU A CD1 1 
ATOM   495   C  CD2 . LEU A  1 68  ? 35.039  -34.430 72.189 1.00 31.78  ? 67  LEU A CD2 1 
ATOM   496   N  N   . SER A  1 69  ? 32.345  -36.939 68.163 1.00 28.68  ? 68  SER A N   1 
ATOM   497   C  CA  . SER A  1 69  ? 31.184  -37.618 67.597 1.00 27.70  ? 68  SER A CA  1 
ATOM   498   C  C   . SER A  1 69  ? 29.971  -36.696 67.489 1.00 27.48  ? 68  SER A C   1 
ATOM   499   O  O   . SER A  1 69  ? 28.903  -37.054 67.974 1.00 27.79  ? 68  SER A O   1 
ATOM   500   C  CB  . SER A  1 69  ? 30.818  -38.834 68.401 1.00 25.22  ? 68  SER A CB  1 
ATOM   501   O  OG  . SER A  1 69  ? 31.828  -39.808 68.299 1.00 27.06  ? 68  SER A OG  1 
ATOM   502   N  N   . ARG A  1 70  ? 30.132  -35.533 66.853 1.00 27.35  ? 69  ARG A N   1 
ATOM   503   C  CA  . ARG A  1 70  ? 29.028  -34.607 66.646 1.00 28.39  ? 69  ARG A CA  1 
ATOM   504   C  C   . ARG A  1 70  ? 28.658  -34.590 65.165 1.00 29.37  ? 69  ARG A C   1 
ATOM   505   O  O   . ARG A  1 70  ? 29.340  -35.206 64.344 1.00 28.62  ? 69  ARG A O   1 
ATOM   506   C  CB  . ARG A  1 70  ? 29.384  -33.195 67.133 1.00 29.93  ? 69  ARG A CB  1 
ATOM   507   C  CG  . ARG A  1 70  ? 29.934  -33.120 68.543 1.00 33.15  ? 69  ARG A CG  1 
ATOM   508   C  CD  . ARG A  1 70  ? 28.903  -32.908 69.622 1.00 38.61  ? 69  ARG A CD  1 
ATOM   509   N  NE  . ARG A  1 70  ? 29.540  -32.544 70.875 1.00 47.15  ? 69  ARG A NE  1 
ATOM   510   C  CZ  . ARG A  1 70  ? 29.929  -31.319 71.239 1.00 47.24  ? 69  ARG A CZ  1 
ATOM   511   N  NH1 . ARG A  1 70  ? 29.733  -30.293 70.434 1.00 46.52  ? 69  ARG A NH1 1 
ATOM   512   N  NH2 . ARG A  1 70  ? 30.471  -31.114 72.433 1.00 44.30  ? 69  ARG A NH2 1 
ATOM   513   N  N   . LYS A  1 71  ? 27.568  -33.877 64.842 1.00 30.86  ? 70  LYS A N   1 
ATOM   514   C  CA  . LYS A  1 71  ? 27.135  -33.702 63.461 1.00 31.59  ? 70  LYS A CA  1 
ATOM   515   C  C   . LYS A  1 71  ? 27.888  -32.506 62.866 1.00 29.00  ? 70  LYS A C   1 
ATOM   516   O  O   . LYS A  1 71  ? 28.436  -31.673 63.605 1.00 27.75  ? 70  LYS A O   1 
ATOM   517   C  CB  . LYS A  1 71  ? 25.610  -33.618 63.368 1.00 35.61  ? 70  LYS A CB  1 
ATOM   518   C  CG  . LYS A  1 71  ? 24.870  -34.791 64.003 1.00 41.77  ? 70  LYS A CG  1 
ATOM   519   C  CD  . LYS A  1 71  ? 23.369  -34.708 63.894 1.00 45.58  ? 70  LYS A CD  1 
ATOM   520   C  CE  . LYS A  1 71  ? 22.738  -36.093 63.810 1.00 47.08  ? 70  LYS A CE  1 
ATOM   521   N  NZ  . LYS A  1 71  ? 21.326  -36.124 64.254 1.00 50.08  ? 70  LYS A NZ  1 
ATOM   522   N  N   . HIS A  1 72  ? 27.936  -32.441 61.527 1.00 26.02  ? 71  HIS A N   1 
ATOM   523   C  CA  . HIS A  1 72  ? 28.677  -31.402 60.832 1.00 25.47  ? 71  HIS A CA  1 
ATOM   524   C  C   . HIS A  1 72  ? 28.024  -30.037 61.046 1.00 24.56  ? 71  HIS A C   1 
ATOM   525   O  O   . HIS A  1 72  ? 26.805  -29.924 61.036 1.00 24.74  ? 71  HIS A O   1 
ATOM   526   C  CB  . HIS A  1 72  ? 28.787  -31.769 59.346 1.00 26.71  ? 71  HIS A CB  1 
ATOM   527   C  CG  . HIS A  1 72  ? 29.423  -30.709 58.516 1.00 26.25  ? 71  HIS A CG  1 
ATOM   528   N  ND1 . HIS A  1 72  ? 30.800  -30.583 58.374 1.00 26.39  ? 71  HIS A ND1 1 
ATOM   529   C  CD2 . HIS A  1 72  ? 28.868  -29.726 57.781 1.00 26.62  ? 71  HIS A CD2 1 
ATOM   530   C  CE1 . HIS A  1 72  ? 31.060  -29.562 57.589 1.00 28.61  ? 71  HIS A CE1 1 
ATOM   531   N  NE2 . HIS A  1 72  ? 29.889  -29.012 57.219 1.00 28.28  ? 71  HIS A NE2 1 
ATOM   532   N  N   . GLY A  1 73  ? 28.849  -29.005 61.244 1.00 25.50  ? 72  GLY A N   1 
ATOM   533   C  CA  . GLY A  1 73  ? 28.360  -27.640 61.363 1.00 24.92  ? 72  GLY A CA  1 
ATOM   534   C  C   . GLY A  1 73  ? 29.285  -26.647 60.656 1.00 25.63  ? 72  GLY A C   1 
ATOM   535   O  O   . GLY A  1 73  ? 30.273  -27.055 60.030 1.00 25.62  ? 72  GLY A O   1 
ATOM   536   N  N   . GLY A  1 74  ? 28.935  -25.356 60.753 1.00 24.81  ? 73  GLY A N   1 
ATOM   537   C  CA  . GLY A  1 74  ? 29.868  -24.279 60.452 1.00 23.55  ? 73  GLY A CA  1 
ATOM   538   C  C   . GLY A  1 74  ? 30.808  -24.050 61.636 1.00 24.30  ? 73  GLY A C   1 
ATOM   539   O  O   . GLY A  1 74  ? 30.507  -24.468 62.753 1.00 21.60  ? 73  GLY A O   1 
ATOM   540   N  N   . PRO A  1 75  ? 31.987  -23.416 61.439 1.00 26.39  ? 74  PRO A N   1 
ATOM   541   C  CA  . PRO A  1 75  ? 32.957  -23.235 62.521 1.00 26.61  ? 74  PRO A CA  1 
ATOM   542   C  C   . PRO A  1 75  ? 32.364  -22.555 63.752 1.00 27.88  ? 74  PRO A C   1 
ATOM   543   O  O   . PRO A  1 75  ? 32.805  -22.811 64.864 1.00 24.86  ? 74  PRO A O   1 
ATOM   544   C  CB  . PRO A  1 75  ? 34.077  -22.375 61.911 1.00 26.03  ? 74  PRO A CB  1 
ATOM   545   C  CG  . PRO A  1 75  ? 33.495  -21.823 60.628 1.00 27.16  ? 74  PRO A CG  1 
ATOM   546   C  CD  . PRO A  1 75  ? 32.455  -22.830 60.175 1.00 27.33  ? 74  PRO A CD  1 
ATOM   547   N  N   . LYS A  1 76  ? 31.331  -21.734 63.542 1.00 31.17  ? 75  LYS A N   1 
ATOM   548   C  CA  . LYS A  1 76  ? 30.785  -20.914 64.611 1.00 33.16  ? 75  LYS A CA  1 
ATOM   549   C  C   . LYS A  1 76  ? 29.740  -21.675 65.425 1.00 31.80  ? 75  LYS A C   1 
ATOM   550   O  O   . LYS A  1 76  ? 29.362  -21.206 66.490 1.00 32.14  ? 75  LYS A O   1 
ATOM   551   C  CB  . LYS A  1 76  ? 30.246  -19.599 64.052 1.00 37.23  ? 75  LYS A CB  1 
ATOM   552   C  CG  . LYS A  1 76  ? 31.300  -18.555 63.720 1.00 48.44  ? 75  LYS A CG  1 
ATOM   553   C  CD  . LYS A  1 76  ? 30.821  -17.503 62.706 1.00 53.10  ? 75  LYS A CD  1 
ATOM   554   C  CE  . LYS A  1 76  ? 29.901  -16.434 63.275 1.00 51.92  ? 75  LYS A CE  1 
ATOM   555   N  NZ  . LYS A  1 76  ? 28.750  -16.163 62.379 1.00 53.78  ? 75  LYS A NZ  1 
ATOM   556   N  N   . ASP A  1 77  ? 29.307  -22.860 64.954 1.00 30.92  ? 76  ASP A N   1 
ATOM   557   C  CA  . ASP A  1 77  ? 28.269  -23.652 65.596 1.00 31.05  ? 76  ASP A CA  1 
ATOM   558   C  C   . ASP A  1 77  ? 28.841  -24.375 66.809 1.00 31.91  ? 76  ASP A C   1 
ATOM   559   O  O   . ASP A  1 77  ? 30.016  -24.716 66.838 1.00 33.40  ? 76  ASP A O   1 
ATOM   560   C  CB  . ASP A  1 77  ? 27.642  -24.636 64.605 1.00 30.96  ? 76  ASP A CB  1 
ATOM   561   C  CG  . ASP A  1 77  ? 26.784  -23.956 63.563 1.00 33.33  ? 76  ASP A CG  1 
ATOM   562   O  OD1 . ASP A  1 77  ? 26.178  -22.928 63.931 1.00 36.00  ? 76  ASP A OD1 1 
ATOM   563   O  OD2 . ASP A  1 77  ? 26.730  -24.438 62.396 1.00 32.04  ? 76  ASP A OD2 1 
ATOM   564   N  N   . GLU A  1 78  ? 27.997  -24.626 67.814 1.00 33.93  ? 77  GLU A N   1 
ATOM   565   C  CA  . GLU A  1 78  ? 28.432  -25.466 68.911 1.00 35.50  ? 77  GLU A CA  1 
ATOM   566   C  C   . GLU A  1 78  ? 28.432  -26.917 68.433 1.00 34.70  ? 77  GLU A C   1 
ATOM   567   O  O   . GLU A  1 78  ? 29.312  -27.685 68.805 1.00 37.04  ? 77  GLU A O   1 
ATOM   568   C  CB  . GLU A  1 78  ? 27.581  -25.209 70.159 1.00 42.40  ? 77  GLU A CB  1 
ATOM   569   C  CG  . GLU A  1 78  ? 28.127  -25.811 71.421 1.00 51.77  ? 77  GLU A CG  1 
ATOM   570   C  CD  . GLU A  1 78  ? 27.728  -27.235 71.811 1.00 57.98  ? 77  GLU A CD  1 
ATOM   571   O  OE1 . GLU A  1 78  ? 26.909  -27.931 71.129 1.00 59.63  ? 77  GLU A OE1 1 
ATOM   572   O  OE2 . GLU A  1 78  ? 28.282  -27.657 72.787 1.00 58.49  ? 77  GLU A OE2 1 
ATOM   573   N  N   . GLU A  1 79  ? 27.446  -27.283 67.611 1.00 33.48  ? 78  GLU A N   1 
ATOM   574   C  CA  . GLU A  1 79  ? 27.367  -28.601 67.006 1.00 31.97  ? 78  GLU A CA  1 
ATOM   575   C  C   . GLU A  1 79  ? 28.186  -28.602 65.710 1.00 31.99  ? 78  GLU A C   1 
ATOM   576   O  O   . GLU A  1 79  ? 27.702  -28.209 64.634 1.00 29.97  ? 78  GLU A O   1 
ATOM   577   C  CB  . GLU A  1 79  ? 25.889  -28.997 66.862 1.00 34.92  ? 78  GLU A CB  1 
ATOM   578   C  CG  . GLU A  1 79  ? 25.621  -30.426 66.393 1.00 39.45  ? 78  GLU A CG  1 
ATOM   579   C  CD  . GLU A  1 79  ? 25.923  -31.572 67.346 1.00 44.82  ? 78  GLU A CD  1 
ATOM   580   O  OE1 . GLU A  1 79  ? 26.272  -31.295 68.544 1.00 47.00  ? 78  GLU A OE1 1 
ATOM   581   O  OE2 . GLU A  1 79  ? 25.842  -32.750 66.892 1.00 48.42  ? 78  GLU A OE2 1 
ATOM   582   N  N   . ARG A  1 80  ? 29.453  -29.032 65.831 1.00 31.09  ? 79  ARG A N   1 
ATOM   583   C  CA  . ARG A  1 80  ? 30.354  -29.142 64.689 1.00 28.24  ? 79  ARG A CA  1 
ATOM   584   C  C   . ARG A  1 80  ? 31.372  -30.258 64.917 1.00 26.93  ? 79  ARG A C   1 
ATOM   585   O  O   . ARG A  1 80  ? 31.627  -30.679 66.044 1.00 28.84  ? 79  ARG A O   1 
ATOM   586   C  CB  . ARG A  1 80  ? 31.129  -27.842 64.467 1.00 26.44  ? 79  ARG A CB  1 
ATOM   587   C  CG  . ARG A  1 80  ? 31.943  -27.385 65.674 1.00 23.77  ? 79  ARG A CG  1 
ATOM   588   C  CD  . ARG A  1 80  ? 32.819  -26.200 65.308 1.00 24.44  ? 79  ARG A CD  1 
ATOM   589   N  NE  . ARG A  1 80  ? 34.131  -26.612 64.824 1.00 23.55  ? 79  ARG A NE  1 
ATOM   590   C  CZ  . ARG A  1 80  ? 35.183  -25.802 64.666 1.00 24.60  ? 79  ARG A CZ  1 
ATOM   591   N  NH1 . ARG A  1 80  ? 35.093  -24.511 64.948 1.00 24.66  ? 79  ARG A NH1 1 
ATOM   592   N  NH2 . ARG A  1 80  ? 36.329  -26.286 64.222 1.00 24.28  ? 79  ARG A NH2 1 
ATOM   593   N  N   . HIS A  1 81  ? 31.952  -30.725 63.809 1.00 23.62  ? 80  HIS A N   1 
ATOM   594   C  CA  . HIS A  1 81  ? 33.166  -31.516 63.825 1.00 21.80  ? 80  HIS A CA  1 
ATOM   595   C  C   . HIS A  1 81  ? 34.327  -30.610 64.209 1.00 21.63  ? 80  HIS A C   1 
ATOM   596   O  O   . HIS A  1 81  ? 34.347  -29.442 63.830 1.00 21.03  ? 80  HIS A O   1 
ATOM   597   C  CB  . HIS A  1 81  ? 33.418  -32.092 62.434 1.00 20.42  ? 80  HIS A CB  1 
ATOM   598   C  CG  . HIS A  1 81  ? 32.317  -32.966 61.936 1.00 19.51  ? 80  HIS A CG  1 
ATOM   599   N  ND1 . HIS A  1 81  ? 31.961  -33.025 60.600 1.00 19.78  ? 80  HIS A ND1 1 
ATOM   600   C  CD2 . HIS A  1 81  ? 31.510  -33.827 62.591 1.00 18.90  ? 80  HIS A CD2 1 
ATOM   601   C  CE1 . HIS A  1 81  ? 30.993  -33.899 60.444 1.00 19.31  ? 80  HIS A CE1 1 
ATOM   602   N  NE2 . HIS A  1 81  ? 30.686  -34.396 61.659 1.00 20.48  ? 80  HIS A NE2 1 
ATOM   603   N  N   . VAL A  1 82  ? 35.304  -31.156 64.943 1.00 22.64  ? 81  VAL A N   1 
ATOM   604   C  CA  . VAL A  1 82  ? 36.505  -30.393 65.250 1.00 22.75  ? 81  VAL A CA  1 
ATOM   605   C  C   . VAL A  1 82  ? 37.118  -29.876 63.947 1.00 22.12  ? 81  VAL A C   1 
ATOM   606   O  O   . VAL A  1 82  ? 37.586  -28.746 63.895 1.00 23.60  ? 81  VAL A O   1 
ATOM   607   C  CB  . VAL A  1 82  ? 37.515  -31.194 66.092 1.00 23.16  ? 81  VAL A CB  1 
ATOM   608   C  CG1 . VAL A  1 82  ? 38.913  -30.559 66.082 1.00 23.98  ? 81  VAL A CG1 1 
ATOM   609   C  CG2 . VAL A  1 82  ? 37.005  -31.381 67.518 1.00 21.38  ? 81  VAL A CG2 1 
ATOM   610   N  N   . GLY A  1 83  ? 37.076  -30.677 62.882 1.00 20.40  ? 82  GLY A N   1 
ATOM   611   C  CA  . GLY A  1 83  ? 37.737  -30.307 61.644 1.00 20.53  ? 82  GLY A CA  1 
ATOM   612   C  C   . GLY A  1 83  ? 36.938  -29.330 60.783 1.00 21.13  ? 82  GLY A C   1 
ATOM   613   O  O   . GLY A  1 83  ? 37.375  -29.012 59.672 1.00 23.07  ? 82  GLY A O   1 
ATOM   614   N  N   . ASP A  1 84  ? 35.789  -28.855 61.293 1.00 20.25  ? 83  ASP A N   1 
ATOM   615   C  CA  . ASP A  1 84  ? 34.859  -28.042 60.522 1.00 21.35  ? 83  ASP A CA  1 
ATOM   616   C  C   . ASP A  1 84  ? 35.317  -26.581 60.496 1.00 22.72  ? 83  ASP A C   1 
ATOM   617   O  O   . ASP A  1 84  ? 35.029  -25.816 61.416 1.00 24.00  ? 83  ASP A O   1 
ATOM   618   C  CB  . ASP A  1 84  ? 33.423  -28.195 61.033 1.00 22.14  ? 83  ASP A CB  1 
ATOM   619   C  CG  . ASP A  1 84  ? 32.759  -29.511 60.635 1.00 22.88  ? 83  ASP A CG  1 
ATOM   620   O  OD1 . ASP A  1 84  ? 33.263  -30.177 59.715 1.00 22.73  ? 83  ASP A OD1 1 
ATOM   621   O  OD2 . ASP A  1 84  ? 31.727  -29.858 61.246 1.00 22.71  ? 83  ASP A OD2 1 
ATOM   622   N  N   . LEU A  1 85  ? 36.005  -26.184 59.416 1.00 21.90  ? 84  LEU A N   1 
ATOM   623   C  CA  . LEU A  1 85  ? 36.564  -24.843 59.345 1.00 21.76  ? 84  LEU A CA  1 
ATOM   624   C  C   . LEU A  1 85  ? 35.766  -23.966 58.384 1.00 22.44  ? 84  LEU A C   1 
ATOM   625   O  O   . LEU A  1 85  ? 36.201  -22.864 58.060 1.00 26.17  ? 84  LEU A O   1 
ATOM   626   C  CB  . LEU A  1 85  ? 38.040  -24.917 58.924 1.00 21.84  ? 84  LEU A CB  1 
ATOM   627   C  CG  . LEU A  1 85  ? 39.018  -25.470 59.959 1.00 21.45  ? 84  LEU A CG  1 
ATOM   628   C  CD1 . LEU A  1 85  ? 40.437  -25.387 59.435 1.00 20.32  ? 84  LEU A CD1 1 
ATOM   629   C  CD2 . LEU A  1 85  ? 38.897  -24.730 61.274 1.00 21.69  ? 84  LEU A CD2 1 
ATOM   630   N  N   . GLY A  1 86  ? 34.605  -24.447 57.923 1.00 21.31  ? 85  GLY A N   1 
ATOM   631   C  CA  . GLY A  1 86  ? 33.732  -23.623 57.095 1.00 20.52  ? 85  GLY A CA  1 
ATOM   632   C  C   . GLY A  1 86  ? 34.230  -23.497 55.654 1.00 19.85  ? 85  GLY A C   1 
ATOM   633   O  O   . GLY A  1 86  ? 34.661  -24.489 55.062 1.00 19.66  ? 85  GLY A O   1 
ATOM   634   N  N   . ASN A  1 87  ? 34.143  -22.277 55.099 1.00 19.54  ? 86  ASN A N   1 
ATOM   635   C  CA  . ASN A  1 87  ? 34.475  -22.050 53.701 1.00 19.96  ? 86  ASN A CA  1 
ATOM   636   C  C   . ASN A  1 87  ? 35.658  -21.096 53.558 1.00 20.42  ? 86  ASN A C   1 
ATOM   637   O  O   . ASN A  1 87  ? 35.979  -20.311 54.456 1.00 20.58  ? 86  ASN A O   1 
ATOM   638   C  CB  . ASN A  1 87  ? 33.306  -21.469 52.908 1.00 20.52  ? 86  ASN A CB  1 
ATOM   639   C  CG  . ASN A  1 87  ? 32.172  -22.452 52.769 1.00 21.86  ? 86  ASN A CG  1 
ATOM   640   O  OD1 . ASN A  1 87  ? 32.251  -23.403 51.995 1.00 24.03  ? 86  ASN A OD1 1 
ATOM   641   N  ND2 . ASN A  1 87  ? 31.125  -22.248 53.542 1.00 22.15  ? 86  ASN A ND2 1 
ATOM   642   N  N   . VAL A  1 88  ? 36.306  -21.197 52.397 1.00 19.62  ? 87  VAL A N   1 
ATOM   643   C  CA  . VAL A  1 88  ? 37.250  -20.192 51.951 1.00 19.46  ? 87  VAL A CA  1 
ATOM   644   C  C   . VAL A  1 88  ? 36.695  -19.639 50.639 1.00 22.57  ? 87  VAL A C   1 
ATOM   645   O  O   . VAL A  1 88  ? 35.880  -20.301 49.983 1.00 24.87  ? 87  VAL A O   1 
ATOM   646   C  CB  . VAL A  1 88  ? 38.675  -20.776 51.815 1.00 18.56  ? 87  VAL A CB  1 
ATOM   647   C  CG1 . VAL A  1 88  ? 39.191  -21.351 53.128 1.00 17.98  ? 87  VAL A CG1 1 
ATOM   648   C  CG2 . VAL A  1 88  ? 38.800  -21.809 50.708 1.00 17.07  ? 87  VAL A CG2 1 
ATOM   649   N  N   . THR A  1 89  ? 37.115  -18.423 50.265 1.00 23.34  ? 88  THR A N   1 
ATOM   650   C  CA  . THR A  1 89  ? 36.540  -17.785 49.093 1.00 22.31  ? 88  THR A CA  1 
ATOM   651   C  C   . THR A  1 89  ? 37.618  -17.573 48.036 1.00 22.60  ? 88  THR A C   1 
ATOM   652   O  O   . THR A  1 89  ? 38.636  -16.946 48.298 1.00 22.96  ? 88  THR A O   1 
ATOM   653   C  CB  . THR A  1 89  ? 35.923  -16.433 49.458 1.00 22.28  ? 88  THR A CB  1 
ATOM   654   O  OG1 . THR A  1 89  ? 34.980  -16.598 50.520 1.00 22.62  ? 88  THR A OG1 1 
ATOM   655   C  CG2 . THR A  1 89  ? 35.241  -15.784 48.280 1.00 21.19  ? 88  THR A CG2 1 
ATOM   656   N  N   . ALA A  1 90  ? 37.356  -18.063 46.827 1.00 23.31  ? 89  ALA A N   1 
ATOM   657   C  CA  . ALA A  1 90  ? 38.233  -17.803 45.697 1.00 24.97  ? 89  ALA A CA  1 
ATOM   658   C  C   . ALA A  1 90  ? 37.738  -16.593 44.907 1.00 27.54  ? 89  ALA A C   1 
ATOM   659   O  O   . ALA A  1 90  ? 36.553  -16.508 44.588 1.00 27.94  ? 89  ALA A O   1 
ATOM   660   C  CB  . ALA A  1 90  ? 38.332  -19.034 44.830 1.00 23.18  ? 89  ALA A CB  1 
ATOM   661   N  N   . ASP A  1 91  ? 38.685  -15.689 44.577 1.00 29.79  ? 90  ASP A N   1 
ATOM   662   C  CA  A ASP A  1 91  ? 38.427  -14.489 43.798 0.50 29.46  ? 90  ASP A CA  1 
ATOM   663   C  CA  B ASP A  1 91  ? 38.414  -14.493 43.797 0.50 31.75  ? 90  ASP A CA  1 
ATOM   664   C  C   . ASP A  1 91  ? 38.291  -14.855 42.320 1.00 31.64  ? 90  ASP A C   1 
ATOM   665   O  O   . ASP A  1 91  ? 38.385  -16.022 41.958 1.00 28.38  ? 90  ASP A O   1 
ATOM   666   C  CB  A ASP A  1 91  ? 39.518  -13.433 44.036 0.50 27.67  ? 90  ASP A CB  1 
ATOM   667   C  CB  B ASP A  1 91  ? 39.464  -13.420 44.077 0.50 33.92  ? 90  ASP A CB  1 
ATOM   668   C  CG  A ASP A  1 91  ? 40.928  -13.805 43.580 0.50 23.99  ? 90  ASP A CG  1 
ATOM   669   C  CG  B ASP A  1 91  ? 39.212  -12.753 45.420 0.50 33.41  ? 90  ASP A CG  1 
ATOM   670   O  OD1 A ASP A  1 91  ? 41.068  -14.686 42.704 0.50 22.83  ? 90  ASP A OD1 1 
ATOM   671   O  OD1 B ASP A  1 91  ? 38.079  -12.865 45.934 0.50 30.67  ? 90  ASP A OD1 1 
ATOM   672   O  OD2 A ASP A  1 91  ? 41.884  -13.207 44.100 0.50 21.04  ? 90  ASP A OD2 1 
ATOM   673   O  OD2 B ASP A  1 91  ? 40.150  -12.125 45.938 0.50 34.22  ? 90  ASP A OD2 1 
ATOM   674   N  N   . LYS A  1 92  ? 38.076  -13.834 41.473 1.00 38.60  ? 91  LYS A N   1 
ATOM   675   C  CA  . LYS A  1 92  ? 37.810  -14.040 40.053 1.00 47.36  ? 91  LYS A CA  1 
ATOM   676   C  C   . LYS A  1 92  ? 38.990  -14.728 39.369 1.00 50.71  ? 91  LYS A C   1 
ATOM   677   O  O   . LYS A  1 92  ? 38.823  -15.257 38.277 1.00 51.69  ? 91  LYS A O   1 
ATOM   678   C  CB  . LYS A  1 92  ? 37.426  -12.741 39.331 1.00 53.68  ? 91  LYS A CB  1 
ATOM   679   C  CG  . LYS A  1 92  ? 38.512  -11.678 39.201 1.00 62.78  ? 91  LYS A CG  1 
ATOM   680   C  CD  . LYS A  1 92  ? 37.983  -10.271 38.987 1.00 63.11  ? 91  LYS A CD  1 
ATOM   681   C  CE  . LYS A  1 92  ? 38.890  -9.228  39.616 1.00 64.72  ? 91  LYS A CE  1 
ATOM   682   N  NZ  . LYS A  1 92  ? 39.003  -8.028  38.760 1.00 63.76  ? 91  LYS A NZ  1 
ATOM   683   N  N   . ASP A  1 93  ? 40.166  -14.720 40.008 1.00 54.10  ? 92  ASP A N   1 
ATOM   684   C  CA  . ASP A  1 93  ? 41.373  -15.299 39.432 1.00 55.53  ? 92  ASP A CA  1 
ATOM   685   C  C   . ASP A  1 93  ? 41.571  -16.735 39.906 1.00 49.78  ? 92  ASP A C   1 
ATOM   686   O  O   . ASP A  1 93  ? 42.523  -17.389 39.504 1.00 49.73  ? 92  ASP A O   1 
ATOM   687   C  CB  . ASP A  1 93  ? 42.618  -14.499 39.811 1.00 63.74  ? 92  ASP A CB  1 
ATOM   688   C  CG  . ASP A  1 93  ? 42.624  -13.104 39.233 1.00 76.77  ? 92  ASP A CG  1 
ATOM   689   O  OD1 . ASP A  1 93  ? 42.241  -12.950 38.048 1.00 86.71  ? 92  ASP A OD1 1 
ATOM   690   O  OD2 . ASP A  1 93  ? 43.032  -12.190 39.975 1.00 81.43  ? 92  ASP A OD2 1 
ATOM   691   N  N   . GLY A  1 94  ? 40.677  -17.216 40.772 1.00 46.91  ? 93  GLY A N   1 
ATOM   692   C  CA  . GLY A  1 94  ? 40.771  -18.576 41.268 1.00 40.16  ? 93  GLY A CA  1 
ATOM   693   C  C   . GLY A  1 94  ? 41.759  -18.695 42.426 1.00 35.92  ? 93  GLY A C   1 
ATOM   694   O  O   . GLY A  1 94  ? 42.266  -19.780 42.707 1.00 37.03  ? 93  GLY A O   1 
ATOM   695   N  N   . VAL A  1 95  ? 41.995  -17.570 43.111 1.00 30.72  ? 94  VAL A N   1 
ATOM   696   C  CA  . VAL A  1 95  ? 42.889  -17.582 44.258 1.00 29.26  ? 94  VAL A CA  1 
ATOM   697   C  C   . VAL A  1 95  ? 42.078  -17.332 45.521 1.00 27.86  ? 94  VAL A C   1 
ATOM   698   O  O   . VAL A  1 95  ? 41.332  -16.365 45.610 1.00 30.53  ? 94  VAL A O   1 
ATOM   699   C  CB  . VAL A  1 95  ? 44.032  -16.561 44.099 1.00 29.71  ? 94  VAL A CB  1 
ATOM   700   C  CG1 . VAL A  1 95  ? 44.899  -16.488 45.336 1.00 27.36  ? 94  VAL A CG1 1 
ATOM   701   C  CG2 . VAL A  1 95  ? 44.858  -16.834 42.847 1.00 28.01  ? 94  VAL A CG2 1 
ATOM   702   N  N   . ALA A  1 96  ? 42.255  -18.194 46.521 1.00 26.48  ? 95  ALA A N   1 
ATOM   703   C  CA  . ALA A  1 96  ? 41.675  -17.950 47.832 1.00 27.61  ? 95  ALA A CA  1 
ATOM   704   C  C   . ALA A  1 96  ? 42.781  -17.502 48.785 1.00 28.68  ? 95  ALA A C   1 
ATOM   705   O  O   . ALA A  1 96  ? 43.713  -18.260 49.038 1.00 28.08  ? 95  ALA A O   1 
ATOM   706   C  CB  . ALA A  1 96  ? 41.005  -19.197 48.333 1.00 26.09  ? 95  ALA A CB  1 
ATOM   707   N  N   . ASP A  1 97  ? 42.679  -16.262 49.291 1.00 28.01  ? 96  ASP A N   1 
ATOM   708   C  CA  . ASP A  1 97  ? 43.601  -15.821 50.316 1.00 28.90  ? 96  ASP A CA  1 
ATOM   709   C  C   . ASP A  1 97  ? 43.009  -16.204 51.657 1.00 27.07  ? 96  ASP A C   1 
ATOM   710   O  O   . ASP A  1 97  ? 42.209  -15.458 52.210 1.00 32.23  ? 96  ASP A O   1 
ATOM   711   C  CB  . ASP A  1 97  ? 43.988  -14.343 50.199 1.00 31.27  ? 96  ASP A CB  1 
ATOM   712   C  CG  . ASP A  1 97  ? 44.823  -14.065 48.953 1.00 36.28  ? 96  ASP A CG  1 
ATOM   713   O  OD1 . ASP A  1 97  ? 45.838  -14.773 48.748 1.00 38.30  ? 96  ASP A OD1 1 
ATOM   714   O  OD2 . ASP A  1 97  ? 44.442  -13.178 48.165 1.00 38.01  ? 96  ASP A OD2 1 
ATOM   715   N  N   . VAL A  1 98  ? 43.423  -17.364 52.163 1.00 23.31  ? 97  VAL A N   1 
ATOM   716   C  CA  . VAL A  1 98  ? 42.817  -17.930 53.344 1.00 21.38  ? 97  VAL A CA  1 
ATOM   717   C  C   . VAL A  1 98  ? 43.327  -17.186 54.571 1.00 21.46  ? 97  VAL A C   1 
ATOM   718   O  O   . VAL A  1 98  ? 44.518  -16.913 54.712 1.00 22.70  ? 97  VAL A O   1 
ATOM   719   C  CB  . VAL A  1 98  ? 43.138  -19.432 53.450 1.00 20.76  ? 97  VAL A CB  1 
ATOM   720   C  CG1 . VAL A  1 98  ? 42.525  -20.051 54.689 1.00 19.64  ? 97  VAL A CG1 1 
ATOM   721   C  CG2 . VAL A  1 98  ? 42.722  -20.178 52.206 1.00 20.47  ? 97  VAL A CG2 1 
ATOM   722   N  N   . SER A  1 99  ? 42.393  -16.885 55.470 1.00 20.89  ? 98  SER A N   1 
ATOM   723   C  CA  . SER A  1 99  ? 42.729  -16.324 56.761 1.00 21.80  ? 98  SER A CA  1 
ATOM   724   C  C   . SER A  1 99  ? 41.583  -16.614 57.720 1.00 22.61  ? 98  SER A C   1 
ATOM   725   O  O   . SER A  1 99  ? 40.489  -16.077 57.561 1.00 23.73  ? 98  SER A O   1 
ATOM   726   C  CB  . SER A  1 99  ? 42.989  -14.859 56.638 1.00 21.50  ? 98  SER A CB  1 
ATOM   727   O  OG  . SER A  1 99  ? 43.223  -14.309 57.925 1.00 21.73  ? 98  SER A OG  1 
ATOM   728   N  N   . ILE A  1 100 ? 41.845  -17.496 58.689 1.00 23.92  ? 99  ILE A N   1 
ATOM   729   C  CA  . ILE A  1 100 ? 40.815  -17.987 59.584 1.00 25.68  ? 99  ILE A CA  1 
ATOM   730   C  C   . ILE A  1 100 ? 41.406  -18.016 60.982 1.00 27.60  ? 99  ILE A C   1 
ATOM   731   O  O   . ILE A  1 100 ? 42.604  -18.221 61.151 1.00 26.48  ? 99  ILE A O   1 
ATOM   732   C  CB  . ILE A  1 100 ? 40.347  -19.396 59.152 1.00 25.35  ? 99  ILE A CB  1 
ATOM   733   C  CG1 . ILE A  1 100 ? 39.414  -19.321 57.942 1.00 23.83  ? 99  ILE A CG1 1 
ATOM   734   C  CG2 . ILE A  1 100 ? 39.714  -20.175 60.306 1.00 24.14  ? 99  ILE A CG2 1 
ATOM   735   C  CD1 . ILE A  1 100 ? 39.120  -20.639 57.317 1.00 24.58  ? 99  ILE A CD1 1 
ATOM   736   N  N   . GLU A  1 101 ? 40.544  -17.852 61.979 1.00 29.17  ? 100 GLU A N   1 
ATOM   737   C  CA  . GLU A  1 101 ? 40.968  -18.090 63.342 1.00 31.12  ? 100 GLU A CA  1 
ATOM   738   C  C   . GLU A  1 101 ? 39.976  -19.065 63.958 1.00 29.33  ? 100 GLU A C   1 
ATOM   739   O  O   . GLU A  1 101 ? 38.776  -18.898 63.805 1.00 32.33  ? 100 GLU A O   1 
ATOM   740   C  CB  . GLU A  1 101 ? 41.081  -16.753 64.059 1.00 36.20  ? 100 GLU A CB  1 
ATOM   741   C  CG  . GLU A  1 101 ? 41.275  -16.882 65.551 1.00 47.62  ? 100 GLU A CG  1 
ATOM   742   C  CD  . GLU A  1 101 ? 41.696  -15.578 66.205 1.00 55.60  ? 100 GLU A CD  1 
ATOM   743   O  OE1 . GLU A  1 101 ? 41.181  -15.290 67.313 1.00 60.14  ? 100 GLU A OE1 1 
ATOM   744   O  OE2 . GLU A  1 101 ? 42.516  -14.817 65.577 1.00 55.38  ? 100 GLU A OE2 1 
ATOM   745   N  N   . ASP A  1 102 ? 40.479  -20.117 64.597 1.00 28.00  ? 101 ASP A N   1 
ATOM   746   C  CA  . ASP A  1 102 ? 39.584  -21.117 65.145 1.00 29.42  ? 101 ASP A CA  1 
ATOM   747   C  C   . ASP A  1 102 ? 40.057  -21.499 66.539 1.00 31.21  ? 101 ASP A C   1 
ATOM   748   O  O   . ASP A  1 102 ? 41.258  -21.557 66.782 1.00 33.73  ? 101 ASP A O   1 
ATOM   749   C  CB  . ASP A  1 102 ? 39.508  -22.345 64.245 1.00 29.34  ? 101 ASP A CB  1 
ATOM   750   C  CG  . ASP A  1 102 ? 38.349  -23.247 64.620 1.00 31.86  ? 101 ASP A CG  1 
ATOM   751   O  OD1 . ASP A  1 102 ? 37.200  -22.817 64.394 1.00 34.92  ? 101 ASP A OD1 1 
ATOM   752   O  OD2 . ASP A  1 102 ? 38.605  -24.347 65.163 1.00 32.76  ? 101 ASP A OD2 1 
ATOM   753   N  N   . SER A  1 103 ? 39.110  -21.773 67.436 1.00 32.93  ? 102 SER A N   1 
ATOM   754   C  CA  . SER A  1 103 ? 39.454  -22.091 68.808 1.00 35.64  ? 102 SER A CA  1 
ATOM   755   C  C   . SER A  1 103 ? 39.134  -23.539 69.160 1.00 35.42  ? 102 SER A C   1 
ATOM   756   O  O   . SER A  1 103 ? 39.268  -23.938 70.311 1.00 37.07  ? 102 SER A O   1 
ATOM   757   C  CB  . SER A  1 103 ? 38.800  -21.134 69.752 1.00 38.91  ? 102 SER A CB  1 
ATOM   758   O  OG  . SER A  1 103 ? 39.664  -20.014 69.921 1.00 50.65  ? 102 SER A OG  1 
ATOM   759   N  N   . VAL A  1 104 ? 38.720  -24.319 68.164 1.00 33.43  ? 103 VAL A N   1 
ATOM   760   C  CA  . VAL A  1 104 ? 38.308  -25.691 68.416 1.00 29.56  ? 103 VAL A CA  1 
ATOM   761   C  C   . VAL A  1 104 ? 39.441  -26.621 68.002 1.00 29.84  ? 103 VAL A C   1 
ATOM   762   O  O   . VAL A  1 104 ? 39.772  -27.542 68.738 1.00 35.52  ? 103 VAL A O   1 
ATOM   763   C  CB  . VAL A  1 104 ? 36.966  -26.036 67.734 1.00 27.72  ? 103 VAL A CB  1 
ATOM   764   C  CG1 . VAL A  1 104 ? 36.635  -27.514 67.820 1.00 26.40  ? 103 VAL A CG1 1 
ATOM   765   C  CG2 . VAL A  1 104 ? 35.832  -25.215 68.309 1.00 26.80  ? 103 VAL A CG2 1 
ATOM   766   N  N   . ILE A  1 105 ? 40.017  -26.384 66.820 1.00 27.68  ? 104 ILE A N   1 
ATOM   767   C  CA  . ILE A  1 105 ? 41.217  -27.109 66.444 1.00 26.15  ? 104 ILE A CA  1 
ATOM   768   C  C   . ILE A  1 105 ? 42.339  -26.695 67.396 1.00 27.46  ? 104 ILE A C   1 
ATOM   769   O  O   . ILE A  1 105 ? 42.257  -25.636 68.021 1.00 28.29  ? 104 ILE A O   1 
ATOM   770   C  CB  . ILE A  1 105 ? 41.599  -26.867 64.974 1.00 24.16  ? 104 ILE A CB  1 
ATOM   771   C  CG1 . ILE A  1 105 ? 41.957  -25.402 64.716 1.00 22.15  ? 104 ILE A CG1 1 
ATOM   772   C  CG2 . ILE A  1 105 ? 40.494  -27.362 64.050 1.00 23.62  ? 104 ILE A CG2 1 
ATOM   773   C  CD1 . ILE A  1 105 ? 42.616  -25.150 63.383 1.00 21.73  ? 104 ILE A CD1 1 
ATOM   774   N  N   . SER A  1 106 ? 43.360  -27.546 67.523 1.00 29.19  ? 105 SER A N   1 
ATOM   775   C  CA  . SER A  1 106 ? 44.526  -27.209 68.318 1.00 30.13  ? 105 SER A CA  1 
ATOM   776   C  C   . SER A  1 106 ? 45.786  -27.794 67.689 1.00 30.81  ? 105 SER A C   1 
ATOM   777   O  O   . SER A  1 106 ? 45.714  -28.756 66.915 1.00 30.18  ? 105 SER A O   1 
ATOM   778   C  CB  . SER A  1 106 ? 44.378  -27.705 69.730 1.00 29.73  ? 105 SER A CB  1 
ATOM   779   O  OG  . SER A  1 106 ? 45.372  -27.103 70.559 1.00 34.39  ? 105 SER A OG  1 
ATOM   780   N  N   . LEU A  1 107 ? 46.939  -27.205 68.042 1.00 31.87  ? 106 LEU A N   1 
ATOM   781   C  CA  . LEU A  1 107 ? 48.210  -27.770 67.623 1.00 33.10  ? 106 LEU A CA  1 
ATOM   782   C  C   . LEU A  1 107 ? 48.909  -28.458 68.788 1.00 37.41  ? 106 LEU A C   1 
ATOM   783   O  O   . LEU A  1 107 ? 50.074  -28.833 68.658 1.00 39.53  ? 106 LEU A O   1 
ATOM   784   C  CB  . LEU A  1 107 ? 49.080  -26.657 67.017 1.00 29.83  ? 106 LEU A CB  1 
ATOM   785   C  CG  . LEU A  1 107 ? 48.458  -25.877 65.866 1.00 26.93  ? 106 LEU A CG  1 
ATOM   786   C  CD1 . LEU A  1 107 ? 49.519  -24.924 65.321 1.00 25.92  ? 106 LEU A CD1 1 
ATOM   787   C  CD2 . LEU A  1 107 ? 47.972  -26.831 64.798 1.00 26.82  ? 106 LEU A CD2 1 
ATOM   788   N  N   . SER A  1 108 ? 48.208  -28.613 69.925 1.00 40.83  ? 107 SER A N   1 
ATOM   789   C  CA  . SER A  1 108 ? 48.789  -29.289 71.083 1.00 49.72  ? 107 SER A CA  1 
ATOM   790   C  C   . SER A  1 108 ? 47.668  -29.667 72.038 1.00 53.99  ? 107 SER A C   1 
ATOM   791   O  O   . SER A  1 108 ? 46.798  -28.814 72.224 1.00 62.55  ? 107 SER A O   1 
ATOM   792   C  CB  . SER A  1 108 ? 49.812  -28.409 71.814 1.00 56.04  ? 107 SER A CB  1 
ATOM   793   O  OG  . SER A  1 108 ? 49.192  -27.204 72.281 1.00 67.06  ? 107 SER A OG  1 
ATOM   794   N  N   . GLY A  1 109 ? 47.725  -30.853 72.668 1.00 51.62  ? 108 GLY A N   1 
ATOM   795   C  CA  . GLY A  1 109 ? 46.569  -31.321 73.407 1.00 52.80  ? 108 GLY A CA  1 
ATOM   796   C  C   . GLY A  1 109 ? 45.906  -32.493 72.699 1.00 49.63  ? 108 GLY A C   1 
ATOM   797   O  O   . GLY A  1 109 ? 46.381  -32.974 71.663 1.00 57.41  ? 108 GLY A O   1 
ATOM   798   N  N   . ASP A  1 110 ? 44.779  -32.931 73.261 1.00 46.99  ? 109 ASP A N   1 
ATOM   799   C  CA  . ASP A  1 110 ? 44.253  -34.268 72.970 1.00 51.40  ? 109 ASP A CA  1 
ATOM   800   C  C   . ASP A  1 110 ? 43.900  -34.404 71.484 1.00 55.23  ? 109 ASP A C   1 
ATOM   801   O  O   . ASP A  1 110 ? 44.152  -35.412 70.826 1.00 68.67  ? 109 ASP A O   1 
ATOM   802   C  CB  . ASP A  1 110 ? 43.125  -34.672 73.920 1.00 54.83  ? 109 ASP A CB  1 
ATOM   803   C  CG  . ASP A  1 110 ? 43.652  -34.949 75.320 1.00 63.03  ? 109 ASP A CG  1 
ATOM   804   O  OD1 . ASP A  1 110 ? 44.888  -35.104 75.463 1.00 64.26  ? 109 ASP A OD1 1 
ATOM   805   O  OD2 . ASP A  1 110 ? 42.837  -34.986 76.283 1.00 76.99  ? 109 ASP A OD2 1 
ATOM   806   N  N   . HIS A  1 111 ? 43.324  -33.345 70.943 1.00 45.95  ? 110 HIS A N   1 
ATOM   807   C  CA  . HIS A  1 111 ? 42.727  -33.484 69.617 1.00 46.21  ? 110 HIS A CA  1 
ATOM   808   C  C   . HIS A  1 111 ? 43.444  -32.512 68.699 1.00 51.79  ? 110 HIS A C   1 
ATOM   809   O  O   . HIS A  1 111 ? 42.847  -31.713 67.943 1.00 61.30  ? 110 HIS A O   1 
ATOM   810   C  CB  . HIS A  1 111 ? 41.178  -33.318 69.647 1.00 46.53  ? 110 HIS A CB  1 
ATOM   811   C  CG  . HIS A  1 111 ? 40.498  -34.159 70.696 1.00 47.64  ? 110 HIS A CG  1 
ATOM   812   N  ND1 . HIS A  1 111 ? 39.773  -33.665 71.792 1.00 43.41  ? 110 HIS A ND1 1 
ATOM   813   C  CD2 . HIS A  1 111 ? 40.728  -35.461 70.976 1.00 45.94  ? 110 HIS A CD2 1 
ATOM   814   C  CE1 . HIS A  1 111 ? 39.484  -34.670 72.590 1.00 42.19  ? 110 HIS A CE1 1 
ATOM   815   N  NE2 . HIS A  1 111 ? 40.066  -35.786 72.130 1.00 43.43  ? 110 HIS A NE2 1 
ATOM   816   N  N   . CYS A  1 112 ? 44.773  -32.577 68.776 1.00 45.42  ? 111 CYS A N   1 
ATOM   817   C  CA  . CYS A  1 112 ? 45.772  -32.045 67.863 1.00 42.03  ? 111 CYS A CA  1 
ATOM   818   C  C   . CYS A  1 112 ? 45.438  -32.464 66.428 1.00 38.06  ? 111 CYS A C   1 
ATOM   819   O  O   . CYS A  1 112 ? 44.941  -33.581 66.172 1.00 34.59  ? 111 CYS A O   1 
ATOM   820   C  CB  . CYS A  1 112 ? 47.077  -32.763 68.281 1.00 44.12  ? 111 CYS A CB  1 
ATOM   821   S  SG  . CYS A  1 112 ? 48.608  -31.846 68.021 1.00 60.52  ? 111 CYS A SG  1 
ATOM   822   N  N   . ILE A  1 113 ? 45.705  -31.577 65.453 1.00 36.21  ? 112 ILE A N   1 
ATOM   823   C  CA  . ILE A  1 113 ? 45.443  -31.837 64.048 1.00 33.45  ? 112 ILE A CA  1 
ATOM   824   C  C   . ILE A  1 113 ? 46.736  -32.200 63.317 1.00 32.11  ? 112 ILE A C   1 
ATOM   825   O  O   . ILE A  1 113 ? 46.718  -32.432 62.099 1.00 33.78  ? 112 ILE A O   1 
ATOM   826   C  CB  . ILE A  1 113 ? 44.728  -30.656 63.358 1.00 32.99  ? 112 ILE A CB  1 
ATOM   827   C  CG1 . ILE A  1 113 ? 45.498  -29.343 63.496 1.00 28.04  ? 112 ILE A CG1 1 
ATOM   828   C  CG2 . ILE A  1 113 ? 43.286  -30.516 63.835 1.00 35.23  ? 112 ILE A CG2 1 
ATOM   829   C  CD1 . ILE A  1 113 ? 45.151  -28.322 62.418 1.00 26.96  ? 112 ILE A CD1 1 
ATOM   830   N  N   . ILE A  1 114 ? 47.854  -32.234 64.051 1.00 30.20  ? 113 ILE A N   1 
ATOM   831   C  CA  . ILE A  1 114 ? 49.131  -32.606 63.461 1.00 27.74  ? 113 ILE A CA  1 
ATOM   832   C  C   . ILE A  1 114 ? 49.037  -34.044 62.980 1.00 26.31  ? 113 ILE A C   1 
ATOM   833   O  O   . ILE A  1 114 ? 48.526  -34.908 63.697 1.00 24.67  ? 113 ILE A O   1 
ATOM   834   C  CB  . ILE A  1 114 ? 50.294  -32.423 64.445 1.00 28.61  ? 113 ILE A CB  1 
ATOM   835   C  CG1 . ILE A  1 114 ? 50.312  -30.982 64.961 1.00 30.48  ? 113 ILE A CG1 1 
ATOM   836   C  CG2 . ILE A  1 114 ? 51.618  -32.813 63.804 1.00 27.85  ? 113 ILE A CG2 1 
ATOM   837   C  CD1 . ILE A  1 114 ? 51.662  -30.534 65.484 1.00 32.62  ? 113 ILE A CD1 1 
ATOM   838   N  N   . GLY A  1 115 ? 49.504  -34.256 61.744 1.00 25.22  ? 114 GLY A N   1 
ATOM   839   C  CA  . GLY A  1 115 ? 49.556  -35.582 61.158 1.00 23.54  ? 114 GLY A CA  1 
ATOM   840   C  C   . GLY A  1 115 ? 48.204  -36.020 60.605 1.00 23.90  ? 114 GLY A C   1 
ATOM   841   O  O   . GLY A  1 115 ? 48.025  -37.200 60.301 1.00 26.62  ? 114 GLY A O   1 
ATOM   842   N  N   . ARG A  1 116 ? 47.267  -35.063 60.481 1.00 21.95  ? 115 ARG A N   1 
ATOM   843   C  CA  . ARG A  1 116 ? 45.989  -35.294 59.829 1.00 19.96  ? 115 ARG A CA  1 
ATOM   844   C  C   . ARG A  1 116 ? 45.984  -34.581 58.478 1.00 20.40  ? 115 ARG A C   1 
ATOM   845   O  O   . ARG A  1 116 ? 47.030  -34.098 58.040 1.00 21.56  ? 115 ARG A O   1 
ATOM   846   C  CB  . ARG A  1 116 ? 44.855  -34.944 60.792 1.00 18.80  ? 115 ARG A CB  1 
ATOM   847   C  CG  . ARG A  1 116 ? 45.017  -35.641 62.138 1.00 17.90  ? 115 ARG A CG  1 
ATOM   848   C  CD  . ARG A  1 116 ? 43.787  -35.480 63.024 1.00 18.08  ? 115 ARG A CD  1 
ATOM   849   N  NE  . ARG A  1 116 ? 43.945  -36.166 64.307 1.00 17.44  ? 115 ARG A NE  1 
ATOM   850   C  CZ  . ARG A  1 116 ? 43.632  -37.426 64.554 1.00 17.83  ? 115 ARG A CZ  1 
ATOM   851   N  NH1 . ARG A  1 116 ? 43.120  -38.184 63.601 1.00 18.15  ? 115 ARG A NH1 1 
ATOM   852   N  NH2 . ARG A  1 116 ? 43.823  -37.927 65.762 1.00 17.36  ? 115 ARG A NH2 1 
ATOM   853   N  N   . THR A  1 117 ? 44.831  -34.545 57.791 1.00 20.26  ? 116 THR A N   1 
ATOM   854   C  CA  . THR A  1 117 ? 44.804  -33.963 56.456 1.00 18.95  ? 116 THR A CA  1 
ATOM   855   C  C   . THR A  1 117 ? 43.934  -32.714 56.406 1.00 17.74  ? 116 THR A C   1 
ATOM   856   O  O   . THR A  1 117 ? 42.858  -32.659 56.998 1.00 18.73  ? 116 THR A O   1 
ATOM   857   C  CB  . THR A  1 117 ? 44.336  -34.970 55.403 1.00 19.22  ? 116 THR A CB  1 
ATOM   858   O  OG1 . THR A  1 117 ? 45.305  -36.014 55.393 1.00 20.83  ? 116 THR A OG1 1 
ATOM   859   C  CG2 . THR A  1 117 ? 44.240  -34.379 54.014 1.00 19.47  ? 116 THR A CG2 1 
ATOM   860   N  N   . LEU A  1 118 ? 44.410  -31.714 55.672 1.00 16.97  ? 117 LEU A N   1 
ATOM   861   C  CA  . LEU A  1 118 ? 43.582  -30.572 55.345 1.00 16.58  ? 117 LEU A CA  1 
ATOM   862   C  C   . LEU A  1 118 ? 43.110  -30.753 53.907 1.00 16.87  ? 117 LEU A C   1 
ATOM   863   O  O   . LEU A  1 118 ? 43.905  -31.118 53.037 1.00 16.05  ? 117 LEU A O   1 
ATOM   864   C  CB  . LEU A  1 118 ? 44.446  -29.317 55.496 1.00 16.28  ? 117 LEU A CB  1 
ATOM   865   C  CG  . LEU A  1 118 ? 43.761  -28.011 55.122 1.00 16.43  ? 117 LEU A CG  1 
ATOM   866   C  CD1 . LEU A  1 118 ? 42.638  -27.716 56.102 1.00 17.78  ? 117 LEU A CD1 1 
ATOM   867   C  CD2 . LEU A  1 118 ? 44.750  -26.886 55.089 1.00 15.43  ? 117 LEU A CD2 1 
ATOM   868   N  N   . VAL A  1 119 ? 41.810  -30.524 53.676 1.00 16.94  ? 118 VAL A N   1 
ATOM   869   C  CA  . VAL A  1 119 ? 41.220  -30.713 52.358 1.00 16.49  ? 118 VAL A CA  1 
ATOM   870   C  C   . VAL A  1 119 ? 40.448  -29.462 51.946 1.00 16.30  ? 118 VAL A C   1 
ATOM   871   O  O   . VAL A  1 119 ? 39.676  -28.905 52.723 1.00 15.53  ? 118 VAL A O   1 
ATOM   872   C  CB  . VAL A  1 119 ? 40.281  -31.937 52.316 1.00 16.08  ? 118 VAL A CB  1 
ATOM   873   C  CG1 . VAL A  1 119 ? 39.699  -32.144 50.928 1.00 16.26  ? 118 VAL A CG1 1 
ATOM   874   C  CG2 . VAL A  1 119 ? 40.932  -33.215 52.818 1.00 15.94  ? 118 VAL A CG2 1 
ATOM   875   N  N   . VAL A  1 120 ? 40.631  -29.058 50.691 1.00 16.91  ? 119 VAL A N   1 
ATOM   876   C  CA  . VAL A  1 120 ? 39.793  -28.030 50.109 1.00 17.88  ? 119 VAL A CA  1 
ATOM   877   C  C   . VAL A  1 120 ? 38.884  -28.695 49.082 1.00 19.26  ? 119 VAL A C   1 
ATOM   878   O  O   . VAL A  1 120 ? 39.352  -29.423 48.207 1.00 20.55  ? 119 VAL A O   1 
ATOM   879   C  CB  . VAL A  1 120 ? 40.630  -26.879 49.510 1.00 18.26  ? 119 VAL A CB  1 
ATOM   880   C  CG1 . VAL A  1 120 ? 41.611  -27.352 48.435 1.00 17.15  ? 119 VAL A CG1 1 
ATOM   881   C  CG2 . VAL A  1 120 ? 39.752  -25.748 48.987 1.00 17.17  ? 119 VAL A CG2 1 
ATOM   882   N  N   . HIS A  1 121 ? 37.577  -28.429 49.211 1.00 20.69  ? 120 HIS A N   1 
ATOM   883   C  CA  . HIS A  1 121 ? 36.538  -29.157 48.494 1.00 22.43  ? 120 HIS A CA  1 
ATOM   884   C  C   . HIS A  1 121 ? 36.034  -28.407 47.264 1.00 24.23  ? 120 HIS A C   1 
ATOM   885   O  O   . HIS A  1 121 ? 36.340  -27.231 47.060 1.00 24.64  ? 120 HIS A O   1 
ATOM   886   C  CB  . HIS A  1 121 ? 35.379  -29.474 49.437 1.00 21.57  ? 120 HIS A CB  1 
ATOM   887   C  CG  . HIS A  1 121 ? 35.693  -30.536 50.428 1.00 21.50  ? 120 HIS A CG  1 
ATOM   888   N  ND1 . HIS A  1 121 ? 35.416  -31.863 50.184 1.00 22.42  ? 120 HIS A ND1 1 
ATOM   889   C  CD2 . HIS A  1 121 ? 36.229  -30.473 51.668 1.00 21.20  ? 120 HIS A CD2 1 
ATOM   890   C  CE1 . HIS A  1 121 ? 35.770  -32.577 51.240 1.00 23.66  ? 120 HIS A CE1 1 
ATOM   891   N  NE2 . HIS A  1 121 ? 36.266  -31.748 52.169 1.00 23.01  ? 120 HIS A NE2 1 
ATOM   892   N  N   . GLU A  1 122 ? 35.191  -29.103 46.492 1.00 26.61  ? 121 GLU A N   1 
ATOM   893   C  CA  . GLU A  1 122 ? 34.770  -28.698 45.161 1.00 28.31  ? 121 GLU A CA  1 
ATOM   894   C  C   . GLU A  1 122 ? 33.775  -27.543 45.215 1.00 28.42  ? 121 GLU A C   1 
ATOM   895   O  O   . GLU A  1 122 ? 33.880  -26.623 44.416 1.00 28.97  ? 121 GLU A O   1 
ATOM   896   C  CB  . GLU A  1 122 ? 34.205  -29.938 44.476 1.00 33.06  ? 121 GLU A CB  1 
ATOM   897   C  CG  . GLU A  1 122 ? 33.275  -29.662 43.322 1.00 35.43  ? 121 GLU A CG  1 
ATOM   898   C  CD  . GLU A  1 122 ? 32.467  -30.903 42.973 1.00 38.63  ? 121 GLU A CD  1 
ATOM   899   O  OE1 . GLU A  1 122 ? 32.179  -31.087 41.783 1.00 39.37  ? 121 GLU A OE1 1 
ATOM   900   O  OE2 . GLU A  1 122 ? 32.121  -31.681 43.896 1.00 37.19  ? 121 GLU A OE2 1 
ATOM   901   N  N   . LYS A  1 123 ? 32.833  -27.598 46.169 1.00 27.32  ? 122 LYS A N   1 
ATOM   902   C  CA  . LYS A  1 123 ? 31.696  -26.693 46.275 1.00 24.54  ? 122 LYS A CA  1 
ATOM   903   C  C   . LYS A  1 123 ? 31.634  -26.070 47.665 1.00 23.03  ? 122 LYS A C   1 
ATOM   904   O  O   . LYS A  1 123 ? 32.448  -26.376 48.532 1.00 23.57  ? 122 LYS A O   1 
ATOM   905   C  CB  . LYS A  1 123 ? 30.390  -27.476 46.096 1.00 27.96  ? 122 LYS A CB  1 
ATOM   906   C  CG  . LYS A  1 123 ? 30.168  -28.119 44.733 1.00 31.21  ? 122 LYS A CG  1 
ATOM   907   C  CD  . LYS A  1 123 ? 28.841  -28.843 44.579 1.00 31.53  ? 122 LYS A CD  1 
ATOM   908   C  CE  . LYS A  1 123 ? 28.781  -30.171 45.297 1.00 30.27  ? 122 LYS A CE  1 
ATOM   909   N  NZ  . LYS A  1 123 ? 27.526  -30.904 45.007 1.00 30.55  ? 122 LYS A NZ  1 
ATOM   910   N  N   . ALA A  1 124 ? 30.629  -25.214 47.880 1.00 21.42  ? 123 ALA A N   1 
ATOM   911   C  CA  . ALA A  1 124 ? 30.407  -24.574 49.168 1.00 21.29  ? 123 ALA A CA  1 
ATOM   912   C  C   . ALA A  1 124 ? 30.042  -25.617 50.218 1.00 21.41  ? 123 ALA A C   1 
ATOM   913   O  O   . ALA A  1 124 ? 29.380  -26.601 49.917 1.00 22.44  ? 123 ALA A O   1 
ATOM   914   C  CB  . ALA A  1 124 ? 29.310  -23.552 49.046 1.00 21.66  ? 123 ALA A CB  1 
ATOM   915   N  N   . ASP A  1 125 ? 30.488  -25.386 51.451 1.00 20.46  ? 124 ASP A N   1 
ATOM   916   C  CA  . ASP A  1 125 ? 30.029  -26.133 52.602 1.00 19.30  ? 124 ASP A CA  1 
ATOM   917   C  C   . ASP A  1 125 ? 28.745  -25.462 53.093 1.00 20.72  ? 124 ASP A C   1 
ATOM   918   O  O   . ASP A  1 125 ? 28.754  -24.271 53.412 1.00 21.65  ? 124 ASP A O   1 
ATOM   919   C  CB  . ASP A  1 125 ? 31.135  -26.157 53.657 1.00 18.80  ? 124 ASP A CB  1 
ATOM   920   C  CG  . ASP A  1 125 ? 30.742  -26.767 54.995 1.00 20.44  ? 124 ASP A CG  1 
ATOM   921   O  OD1 . ASP A  1 125 ? 29.554  -27.124 55.168 1.00 22.06  ? 124 ASP A OD1 1 
ATOM   922   O  OD2 . ASP A  1 125 ? 31.628  -26.882 55.864 1.00 20.60  ? 124 ASP A OD2 1 
ATOM   923   N  N   . ASP A  1 126 ? 27.643  -26.223 53.168 1.00 19.84  ? 125 ASP A N   1 
ATOM   924   C  CA  . ASP A  1 126 ? 26.353  -25.647 53.526 1.00 19.29  ? 125 ASP A CA  1 
ATOM   925   C  C   . ASP A  1 126 ? 26.214  -25.511 55.041 1.00 18.76  ? 125 ASP A C   1 
ATOM   926   O  O   . ASP A  1 126 ? 25.149  -25.143 55.526 1.00 18.08  ? 125 ASP A O   1 
ATOM   927   C  CB  . ASP A  1 126 ? 25.183  -26.357 52.836 1.00 20.82  ? 125 ASP A CB  1 
ATOM   928   C  CG  . ASP A  1 126 ? 24.866  -27.759 53.357 1.00 22.72  ? 125 ASP A CG  1 
ATOM   929   O  OD1 . ASP A  1 126 ? 25.222  -28.063 54.534 1.00 22.05  ? 125 ASP A OD1 1 
ATOM   930   O  OD2 . ASP A  1 126 ? 24.240  -28.539 52.589 1.00 23.45  ? 125 ASP A OD2 1 
ATOM   931   N  N   . LEU A  1 127 ? 27.294  -25.794 55.778 1.00 18.76  ? 126 LEU A N   1 
ATOM   932   C  CA  . LEU A  1 127 ? 27.361  -25.582 57.218 1.00 19.13  ? 126 LEU A CA  1 
ATOM   933   C  C   . LEU A  1 127 ? 26.266  -26.369 57.945 1.00 20.35  ? 126 LEU A C   1 
ATOM   934   O  O   . LEU A  1 127 ? 25.903  -26.023 59.071 1.00 23.17  ? 126 LEU A O   1 
ATOM   935   C  CB  . LEU A  1 127 ? 27.273  -24.086 57.554 1.00 17.61  ? 126 LEU A CB  1 
ATOM   936   C  CG  . LEU A  1 127 ? 28.179  -23.148 56.750 1.00 17.28  ? 126 LEU A CG  1 
ATOM   937   C  CD1 . LEU A  1 127 ? 28.077  -21.730 57.330 1.00 16.11  ? 126 LEU A CD1 1 
ATOM   938   C  CD2 . LEU A  1 127 ? 29.641  -23.609 56.767 1.00 16.92  ? 126 LEU A CD2 1 
ATOM   939   N  N   . GLY A  1 128 ? 25.759  -27.431 57.292 1.00 19.72  ? 127 GLY A N   1 
ATOM   940   C  CA  . GLY A  1 128 ? 24.880  -28.402 57.917 1.00 18.90  ? 127 GLY A CA  1 
ATOM   941   C  C   . GLY A  1 128 ? 23.410  -27.987 57.853 1.00 20.99  ? 127 GLY A C   1 
ATOM   942   O  O   . GLY A  1 128 ? 22.574  -28.536 58.571 1.00 20.58  ? 127 GLY A O   1 
ATOM   943   N  N   . LYS A  1 129 ? 23.092  -27.037 56.970 1.00 22.46  ? 128 LYS A N   1 
ATOM   944   C  CA  . LYS A  1 129 ? 21.763  -26.457 56.891 1.00 22.52  ? 128 LYS A CA  1 
ATOM   945   C  C   . LYS A  1 129 ? 21.127  -26.774 55.542 1.00 21.38  ? 128 LYS A C   1 
ATOM   946   O  O   . LYS A  1 129 ? 20.337  -25.990 55.034 1.00 20.21  ? 128 LYS A O   1 
ATOM   947   C  CB  . LYS A  1 129 ? 21.848  -24.941 57.070 1.00 25.34  ? 128 LYS A CB  1 
ATOM   948   C  CG  . LYS A  1 129 ? 22.604  -24.460 58.304 1.00 27.75  ? 128 LYS A CG  1 
ATOM   949   C  CD  . LYS A  1 129 ? 22.837  -22.948 58.144 1.00 28.99  ? 128 LYS A CD  1 
ATOM   950   C  CE  . LYS A  1 129 ? 22.700  -22.087 59.377 1.00 33.37  ? 128 LYS A CE  1 
ATOM   951   N  NZ  . LYS A  1 129 ? 21.929  -20.883 58.988 1.00 41.86  ? 128 LYS A NZ  1 
ATOM   952   N  N   . GLY A  1 130 ? 21.452  -27.938 54.987 1.00 22.41  ? 129 GLY A N   1 
ATOM   953   C  CA  . GLY A  1 130 ? 21.002  -28.312 53.652 1.00 21.87  ? 129 GLY A CA  1 
ATOM   954   C  C   . GLY A  1 130 ? 19.796  -29.242 53.670 1.00 21.50  ? 129 GLY A C   1 
ATOM   955   O  O   . GLY A  1 130 ? 19.249  -29.548 52.613 1.00 21.93  ? 129 GLY A O   1 
ATOM   956   N  N   . GLY A  1 131 ? 19.445  -29.720 54.865 1.00 21.23  ? 130 GLY A N   1 
ATOM   957   C  CA  . GLY A  1 131 ? 18.230  -30.485 55.095 1.00 23.68  ? 130 GLY A CA  1 
ATOM   958   C  C   . GLY A  1 131 ? 18.256  -31.883 54.484 1.00 26.42  ? 130 GLY A C   1 
ATOM   959   O  O   . GLY A  1 131 ? 17.205  -32.459 54.221 1.00 29.80  ? 130 GLY A O   1 
ATOM   960   N  N   . ASN A  1 132 ? 19.448  -32.425 54.237 1.00 27.89  ? 131 ASN A N   1 
ATOM   961   C  CA  . ASN A  1 132 ? 19.580  -33.818 53.838 1.00 27.69  ? 131 ASN A CA  1 
ATOM   962   C  C   . ASN A  1 132 ? 20.635  -34.483 54.709 1.00 30.02  ? 131 ASN A C   1 
ATOM   963   O  O   . ASN A  1 132 ? 21.276  -33.832 55.534 1.00 27.46  ? 131 ASN A O   1 
ATOM   964   C  CB  . ASN A  1 132 ? 19.816  -33.996 52.333 1.00 27.93  ? 131 ASN A CB  1 
ATOM   965   C  CG  . ASN A  1 132 ? 21.042  -33.301 51.796 1.00 28.19  ? 131 ASN A CG  1 
ATOM   966   O  OD1 . ASN A  1 132 ? 21.954  -32.965 52.548 1.00 29.58  ? 131 ASN A OD1 1 
ATOM   967   N  ND2 . ASN A  1 132 ? 21.062  -33.074 50.495 1.00 30.22  ? 131 ASN A ND2 1 
ATOM   968   N  N   . GLU A  1 133 ? 20.805  -35.797 54.520 1.00 37.13  ? 132 GLU A N   1 
ATOM   969   C  CA  . GLU A  1 133 ? 21.660  -36.559 55.410 1.00 39.01  ? 132 GLU A CA  1 
ATOM   970   C  C   . GLU A  1 133 ? 23.106  -36.154 55.163 1.00 37.22  ? 132 GLU A C   1 
ATOM   971   O  O   . GLU A  1 133 ? 23.886  -36.008 56.105 1.00 39.04  ? 132 GLU A O   1 
ATOM   972   C  CB  . GLU A  1 133 ? 21.413  -38.049 55.218 1.00 44.26  ? 132 GLU A CB  1 
ATOM   973   C  CG  . GLU A  1 133 ? 22.087  -38.886 56.290 1.00 54.13  ? 132 GLU A CG  1 
ATOM   974   C  CD  . GLU A  1 133 ? 22.124  -40.374 55.931 1.00 60.86  ? 132 GLU A CD  1 
ATOM   975   O  OE1 . GLU A  1 133 ? 22.526  -40.663 54.785 1.00 58.37  ? 132 GLU A OE1 1 
ATOM   976   O  OE2 . GLU A  1 133 ? 21.780  -41.263 56.796 1.00 73.07  ? 132 GLU A OE2 1 
ATOM   977   N  N   . GLU A  1 134 ? 23.411  -35.926 53.875 1.00 33.81  ? 133 GLU A N   1 
ATOM   978   C  CA  . GLU A  1 134 ? 24.718  -35.502 53.415 1.00 31.64  ? 133 GLU A CA  1 
ATOM   979   C  C   . GLU A  1 134 ? 25.148  -34.223 54.138 1.00 28.89  ? 133 GLU A C   1 
ATOM   980   O  O   . GLU A  1 134 ? 26.296  -34.106 54.558 1.00 27.84  ? 133 GLU A O   1 
ATOM   981   C  CB  . GLU A  1 134 ? 24.649  -35.330 51.895 1.00 36.41  ? 133 GLU A CB  1 
ATOM   982   C  CG  . GLU A  1 134 ? 25.994  -35.384 51.192 1.00 43.36  ? 133 GLU A CG  1 
ATOM   983   C  CD  . GLU A  1 134 ? 26.982  -36.465 51.605 1.00 46.12  ? 133 GLU A CD  1 
ATOM   984   O  OE1 . GLU A  1 134 ? 26.555  -37.594 51.940 1.00 49.45  ? 133 GLU A OE1 1 
ATOM   985   O  OE2 . GLU A  1 134 ? 28.195  -36.173 51.586 1.00 47.02  ? 133 GLU A OE2 1 
ATOM   986   N  N   . SER A  1 135 ? 24.214  -33.278 54.293 1.00 27.67  ? 134 SER A N   1 
ATOM   987   C  CA  . SER A  1 135 ? 24.509  -31.989 54.895 1.00 26.45  ? 134 SER A CA  1 
ATOM   988   C  C   . SER A  1 135 ? 25.107  -32.174 56.289 1.00 26.16  ? 134 SER A C   1 
ATOM   989   O  O   . SER A  1 135 ? 26.038  -31.464 56.654 1.00 25.03  ? 134 SER A O   1 
ATOM   990   C  CB  . SER A  1 135 ? 23.295  -31.098 54.937 1.00 25.94  ? 134 SER A CB  1 
ATOM   991   O  OG  . SER A  1 135 ? 23.616  -29.806 55.452 1.00 23.88  ? 134 SER A OG  1 
ATOM   992   N  N   . THR A  1 136 ? 24.586  -33.131 57.061 1.00 27.55  ? 135 THR A N   1 
ATOM   993   C  CA  . THR A  1 136 ? 25.015  -33.238 58.448 1.00 29.46  ? 135 THR A CA  1 
ATOM   994   C  C   . THR A  1 136 ? 26.277  -34.089 58.574 1.00 29.34  ? 135 THR A C   1 
ATOM   995   O  O   . THR A  1 136 ? 26.753  -34.306 59.692 1.00 29.90  ? 135 THR A O   1 
ATOM   996   C  CB  . THR A  1 136 ? 23.910  -33.797 59.354 1.00 29.35  ? 135 THR A CB  1 
ATOM   997   O  OG1 . THR A  1 136 ? 23.675  -35.134 58.908 1.00 30.72  ? 135 THR A OG1 1 
ATOM   998   C  CG2 . THR A  1 136 ? 22.640  -32.981 59.318 1.00 27.20  ? 135 THR A CG2 1 
ATOM   999   N  N   . LYS A  1 137 ? 26.808  -34.554 57.431 1.00 29.74  ? 136 LYS A N   1 
ATOM   1000  C  CA  . LYS A  1 137 ? 28.052  -35.305 57.415 1.00 30.82  ? 136 LYS A CA  1 
ATOM   1001  C  C   . LYS A  1 137 ? 29.171  -34.473 56.797 1.00 29.15  ? 136 LYS A C   1 
ATOM   1002  O  O   . LYS A  1 137 ? 30.221  -34.302 57.412 1.00 30.74  ? 136 LYS A O   1 
ATOM   1003  C  CB  . LYS A  1 137 ? 27.884  -36.618 56.650 1.00 36.67  ? 136 LYS A CB  1 
ATOM   1004  C  CG  . LYS A  1 137 ? 27.211  -37.754 57.417 1.00 43.90  ? 136 LYS A CG  1 
ATOM   1005  C  CD  . LYS A  1 137 ? 26.804  -38.903 56.500 1.00 50.74  ? 136 LYS A CD  1 
ATOM   1006  C  CE  . LYS A  1 137 ? 26.745  -40.257 57.172 1.00 54.84  ? 136 LYS A CE  1 
ATOM   1007  N  NZ  . LYS A  1 137 ? 26.130  -41.195 56.219 1.00 60.17  ? 136 LYS A NZ  1 
ATOM   1008  N  N   . THR A  1 138 ? 28.940  -33.950 55.585 1.00 26.02  ? 137 THR A N   1 
ATOM   1009  C  CA  . THR A  1 138 ? 30.003  -33.354 54.796 1.00 23.74  ? 137 THR A CA  1 
ATOM   1010  C  C   . THR A  1 138 ? 29.698  -31.916 54.399 1.00 23.40  ? 137 THR A C   1 
ATOM   1011  O  O   . THR A  1 138 ? 30.504  -31.282 53.724 1.00 22.44  ? 137 THR A O   1 
ATOM   1012  C  CB  . THR A  1 138 ? 30.241  -34.153 53.512 1.00 23.56  ? 137 THR A CB  1 
ATOM   1013  O  OG1 . THR A  1 138 ? 29.157  -33.933 52.610 1.00 22.20  ? 137 THR A OG1 1 
ATOM   1014  C  CG2 . THR A  1 138 ? 30.404  -35.629 53.789 1.00 25.02  ? 137 THR A CG2 1 
ATOM   1015  N  N   . GLY A  1 139 ? 28.517  -31.428 54.780 1.00 24.30  ? 138 GLY A N   1 
ATOM   1016  C  CA  . GLY A  1 139 ? 28.050  -30.115 54.361 1.00 24.59  ? 138 GLY A CA  1 
ATOM   1017  C  C   . GLY A  1 139 ? 27.877  -29.996 52.847 1.00 24.04  ? 138 GLY A C   1 
ATOM   1018  O  O   . GLY A  1 139 ? 27.732  -28.888 52.338 1.00 24.16  ? 138 GLY A O   1 
ATOM   1019  N  N   . ASN A  1 140 ? 27.903  -31.123 52.127 1.00 24.22  ? 139 ASN A N   1 
ATOM   1020  C  CA  . ASN A  1 140 ? 27.598  -31.141 50.702 1.00 25.42  ? 139 ASN A CA  1 
ATOM   1021  C  C   . ASN A  1 140 ? 28.687  -30.420 49.918 1.00 25.97  ? 139 ASN A C   1 
ATOM   1022  O  O   . ASN A  1 140 ? 28.430  -29.899 48.832 1.00 26.09  ? 139 ASN A O   1 
ATOM   1023  C  CB  . ASN A  1 140 ? 26.227  -30.534 50.372 1.00 25.07  ? 139 ASN A CB  1 
ATOM   1024  C  CG  . ASN A  1 140 ? 25.063  -31.445 50.684 1.00 26.18  ? 139 ASN A CG  1 
ATOM   1025  O  OD1 . ASN A  1 140 ? 24.888  -32.478 50.041 1.00 25.83  ? 139 ASN A OD1 1 
ATOM   1026  N  ND2 . ASN A  1 140 ? 24.275  -31.085 51.679 1.00 27.64  ? 139 ASN A ND2 1 
ATOM   1027  N  N   . ALA A  1 141 ? 29.913  -30.431 50.468 1.00 25.52  ? 140 ALA A N   1 
ATOM   1028  C  CA  . ALA A  1 141 ? 31.012  -29.665 49.907 1.00 25.30  ? 140 ALA A CA  1 
ATOM   1029  C  C   . ALA A  1 141 ? 31.556  -30.324 48.641 1.00 26.41  ? 140 ALA A C   1 
ATOM   1030  O  O   . ALA A  1 141 ? 32.391  -29.750 47.951 1.00 27.40  ? 140 ALA A O   1 
ATOM   1031  C  CB  . ALA A  1 141 ? 32.075  -29.485 50.953 1.00 26.01  ? 140 ALA A CB  1 
ATOM   1032  N  N   . GLY A  1 142 ? 31.075  -31.535 48.339 1.00 25.47  ? 141 GLY A N   1 
ATOM   1033  C  CA  . GLY A  1 142 ? 31.473  -32.213 47.121 1.00 25.83  ? 141 GLY A CA  1 
ATOM   1034  C  C   . GLY A  1 142 ? 32.869  -32.804 47.259 1.00 25.98  ? 141 GLY A C   1 
ATOM   1035  O  O   . GLY A  1 142 ? 33.331  -33.056 48.374 1.00 26.09  ? 141 GLY A O   1 
ATOM   1036  N  N   . SER A  1 143 ? 33.533  -32.981 46.107 1.00 25.15  ? 142 SER A N   1 
ATOM   1037  C  CA  . SER A  1 143 ? 34.758  -33.758 46.026 1.00 22.75  ? 142 SER A CA  1 
ATOM   1038  C  C   . SER A  1 143 ? 35.930  -33.007 46.652 1.00 23.30  ? 142 SER A C   1 
ATOM   1039  O  O   . SER A  1 143 ? 35.814  -31.827 46.999 1.00 23.71  ? 142 SER A O   1 
ATOM   1040  C  CB  . SER A  1 143 ? 35.054  -34.166 44.609 1.00 20.80  ? 142 SER A CB  1 
ATOM   1041  O  OG  . SER A  1 143 ? 35.308  -33.031 43.810 1.00 19.76  ? 142 SER A OG  1 
ATOM   1042  N  N   . ARG A  1 144 ? 37.058  -33.723 46.773 1.00 23.23  ? 143 ARG A N   1 
ATOM   1043  C  CA  . ARG A  1 144 ? 38.273  -33.241 47.408 1.00 22.56  ? 143 ARG A CA  1 
ATOM   1044  C  C   . ARG A  1 144 ? 39.222  -32.765 46.309 1.00 23.14  ? 143 ARG A C   1 
ATOM   1045  O  O   . ARG A  1 144 ? 39.765  -33.574 45.564 1.00 24.35  ? 143 ARG A O   1 
ATOM   1046  C  CB  . ARG A  1 144 ? 38.875  -34.378 48.240 1.00 22.44  ? 143 ARG A CB  1 
ATOM   1047  C  CG  . ARG A  1 144 ? 37.920  -34.934 49.287 1.00 21.73  ? 143 ARG A CG  1 
ATOM   1048  C  CD  . ARG A  1 144 ? 38.368  -36.202 49.985 1.00 22.56  ? 143 ARG A CD  1 
ATOM   1049  N  NE  . ARG A  1 144 ? 37.346  -36.693 50.902 1.00 23.17  ? 143 ARG A NE  1 
ATOM   1050  C  CZ  . ARG A  1 144 ? 37.573  -37.444 51.986 1.00 23.99  ? 143 ARG A CZ  1 
ATOM   1051  N  NH1 . ARG A  1 144 ? 38.797  -37.816 52.317 1.00 27.25  ? 143 ARG A NH1 1 
ATOM   1052  N  NH2 . ARG A  1 144 ? 36.584  -37.826 52.766 1.00 22.94  ? 143 ARG A NH2 1 
ATOM   1053  N  N   . LEU A  1 145 ? 39.396  -31.447 46.180 1.00 23.35  ? 144 LEU A N   1 
ATOM   1054  C  CA  . LEU A  1 145 ? 40.132  -30.915 45.049 1.00 23.00  ? 144 LEU A CA  1 
ATOM   1055  C  C   . LEU A  1 145 ? 41.629  -31.042 45.306 1.00 23.25  ? 144 LEU A C   1 
ATOM   1056  O  O   . LEU A  1 145 ? 42.390  -31.300 44.379 1.00 24.69  ? 144 LEU A O   1 
ATOM   1057  C  CB  . LEU A  1 145 ? 39.718  -29.454 44.844 1.00 24.13  ? 144 LEU A CB  1 
ATOM   1058  C  CG  . LEU A  1 145 ? 38.328  -29.249 44.256 1.00 24.06  ? 144 LEU A CG  1 
ATOM   1059  C  CD1 . LEU A  1 145 ? 38.058  -27.771 43.977 1.00 24.16  ? 144 LEU A CD1 1 
ATOM   1060  C  CD2 . LEU A  1 145 ? 38.124  -30.082 42.991 1.00 22.47  ? 144 LEU A CD2 1 
ATOM   1061  N  N   . ALA A  1 146 ? 42.028  -30.828 46.565 1.00 23.19  ? 145 ALA A N   1 
ATOM   1062  C  CA  . ALA A  1 146 ? 43.413  -30.905 46.976 1.00 23.32  ? 145 ALA A CA  1 
ATOM   1063  C  C   . ALA A  1 146 ? 43.502  -31.123 48.483 1.00 24.28  ? 145 ALA A C   1 
ATOM   1064  O  O   . ALA A  1 146 ? 42.624  -30.699 49.233 1.00 24.01  ? 145 ALA A O   1 
ATOM   1065  C  CB  . ALA A  1 146 ? 44.150  -29.674 46.532 1.00 23.31  ? 145 ALA A CB  1 
ATOM   1066  N  N   . CYS A  1 147 ? 44.584  -31.777 48.907 1.00 23.27  ? 146 CYS A N   1 
ATOM   1067  C  CA  . CYS A  1 147 ? 44.786  -32.051 50.312 1.00 23.48  ? 146 CYS A CA  1 
ATOM   1068  C  C   . CYS A  1 147 ? 46.283  -32.181 50.576 1.00 24.40  ? 146 CYS A C   1 
ATOM   1069  O  O   . CYS A  1 147 ? 47.081  -32.195 49.633 1.00 24.36  ? 146 CYS A O   1 
ATOM   1070  C  CB  . CYS A  1 147 ? 44.079  -33.335 50.714 1.00 24.90  ? 146 CYS A CB  1 
ATOM   1071  S  SG  . CYS A  1 147 ? 44.604  -34.791 49.758 1.00 26.12  ? 146 CYS A SG  1 
ATOM   1072  N  N   . GLY A  1 148 ? 46.633  -32.243 51.865 1.00 22.35  ? 147 GLY A N   1 
ATOM   1073  C  CA  . GLY A  1 148 ? 47.988  -32.474 52.312 1.00 21.58  ? 147 GLY A CA  1 
ATOM   1074  C  C   . GLY A  1 148 ? 48.011  -32.920 53.772 1.00 22.34  ? 147 GLY A C   1 
ATOM   1075  O  O   . GLY A  1 148 ? 47.062  -32.674 54.524 1.00 22.48  ? 147 GLY A O   1 
ATOM   1076  N  N   . VAL A  1 149 ? 49.108  -33.574 54.166 1.00 21.08  ? 148 VAL A N   1 
ATOM   1077  C  CA  . VAL A  1 149 ? 49.258  -33.920 55.566 1.00 19.49  ? 148 VAL A CA  1 
ATOM   1078  C  C   . VAL A  1 149 ? 49.764  -32.694 56.317 1.00 19.36  ? 148 VAL A C   1 
ATOM   1079  O  O   . VAL A  1 149 ? 50.581  -31.940 55.804 1.00 19.56  ? 148 VAL A O   1 
ATOM   1080  C  CB  . VAL A  1 149 ? 50.141  -35.168 55.755 1.00 17.82  ? 148 VAL A CB  1 
ATOM   1081  C  CG1 . VAL A  1 149 ? 50.199  -35.593 57.218 1.00 17.81  ? 148 VAL A CG1 1 
ATOM   1082  C  CG2 . VAL A  1 149 ? 49.658  -36.305 54.871 1.00 16.38  ? 148 VAL A CG2 1 
ATOM   1083  N  N   . ILE A  1 150 ? 49.234  -32.501 57.524 1.00 19.38  ? 149 ILE A N   1 
ATOM   1084  C  CA  . ILE A  1 150 ? 49.547  -31.345 58.343 1.00 20.02  ? 149 ILE A CA  1 
ATOM   1085  C  C   . ILE A  1 150 ? 50.786  -31.682 59.160 1.00 21.18  ? 149 ILE A C   1 
ATOM   1086  O  O   . ILE A  1 150 ? 50.730  -32.553 60.030 1.00 21.42  ? 149 ILE A O   1 
ATOM   1087  C  CB  . ILE A  1 150 ? 48.341  -31.029 59.255 1.00 19.15  ? 149 ILE A CB  1 
ATOM   1088  C  CG1 . ILE A  1 150 ? 47.104  -30.620 58.444 1.00 18.71  ? 149 ILE A CG1 1 
ATOM   1089  C  CG2 . ILE A  1 150 ? 48.704  -29.998 60.313 1.00 18.30  ? 149 ILE A CG2 1 
ATOM   1090  C  CD1 . ILE A  1 150 ? 45.830  -30.673 59.240 1.00 19.21  ? 149 ILE A CD1 1 
ATOM   1091  N  N   . GLY A  1 151 ? 51.886  -30.977 58.879 1.00 22.35  ? 150 GLY A N   1 
ATOM   1092  C  CA  . GLY A  1 151 ? 53.190  -31.332 59.420 1.00 24.03  ? 150 GLY A CA  1 
ATOM   1093  C  C   . GLY A  1 151 ? 53.860  -30.199 60.198 1.00 23.32  ? 150 GLY A C   1 
ATOM   1094  O  O   . GLY A  1 151 ? 53.467  -29.037 60.083 1.00 22.04  ? 150 GLY A O   1 
ATOM   1095  N  N   . ILE A  1 152 ? 54.882  -30.572 60.986 1.00 22.54  ? 151 ILE A N   1 
ATOM   1096  C  CA  . ILE A  1 152 ? 55.567  -29.651 61.881 1.00 22.02  ? 151 ILE A CA  1 
ATOM   1097  C  C   . ILE A  1 152 ? 56.495  -28.786 61.042 1.00 24.62  ? 151 ILE A C   1 
ATOM   1098  O  O   . ILE A  1 152 ? 57.203  -29.315 60.187 1.00 23.29  ? 151 ILE A O   1 
ATOM   1099  C  CB  . ILE A  1 152 ? 56.346  -30.431 62.950 1.00 19.22  ? 151 ILE A CB  1 
ATOM   1100  C  CG1 . ILE A  1 152 ? 55.404  -31.244 63.846 1.00 19.65  ? 151 ILE A CG1 1 
ATOM   1101  C  CG2 . ILE A  1 152 ? 57.232  -29.498 63.743 1.00 17.28  ? 151 ILE A CG2 1 
ATOM   1102  C  CD1 . ILE A  1 152 ? 56.100  -32.390 64.551 1.00 19.28  ? 151 ILE A CD1 1 
ATOM   1103  N  N   . ALA A  1 153 ? 56.462  -27.462 61.290 1.00 28.93  ? 152 ALA A N   1 
ATOM   1104  C  CA  . ALA A  1 153 ? 57.279  -26.501 60.564 1.00 32.60  ? 152 ALA A CA  1 
ATOM   1105  C  C   . ALA A  1 153 ? 58.254  -25.836 61.529 1.00 37.71  ? 152 ALA A C   1 
ATOM   1106  O  O   . ALA A  1 153 ? 58.111  -25.963 62.749 1.00 37.74  ? 152 ALA A O   1 
ATOM   1107  C  CB  . ALA A  1 153 ? 56.408  -25.486 59.875 1.00 29.22  ? 152 ALA A CB  1 
ATOM   1108  N  N   . GLN A  1 154 ? 59.239  -25.120 60.966 1.00 46.10  ? 153 GLN A N   1 
ATOM   1109  C  CA  . GLN A  1 154 ? 60.282  -24.492 61.767 1.00 53.77  ? 153 GLN A CA  1 
ATOM   1110  C  C   . GLN A  1 154 ? 59.736  -23.299 62.564 1.00 56.96  ? 153 GLN A C   1 
ATOM   1111  O  O   . GLN A  1 154 ? 59.084  -22.383 62.045 1.00 60.85  ? 153 GLN A O   1 
ATOM   1112  C  CB  . GLN A  1 154 ? 61.461  -24.035 60.911 1.00 53.37  ? 153 GLN A CB  1 
ATOM   1113  C  CG  . GLN A  1 154 ? 62.557  -23.410 61.760 1.00 55.44  ? 153 GLN A CG  1 
ATOM   1114  C  CD  . GLN A  1 154 ? 63.874  -23.352 61.037 1.00 57.90  ? 153 GLN A CD  1 
ATOM   1115  O  OE1 . GLN A  1 154 ? 63.984  -22.816 59.933 1.00 59.21  ? 153 GLN A OE1 1 
ATOM   1116  N  NE2 . GLN A  1 154 ? 64.897  -23.890 61.680 1.00 55.77  ? 153 GLN A NE2 1 
ATOM   1117  O  OXT . GLN A  1 154 ? 59.980  -23.229 63.773 1.00 63.30  ? 153 GLN A OXT 1 
ATOM   1118  N  N   . ALA B  1 2   ? -4.709  -26.322 3.189  1.00 34.37  ? 1   ALA B N   1 
ATOM   1119  C  CA  . ALA B  1 2   ? -3.813  -26.781 4.278  1.00 36.60  ? 1   ALA B CA  1 
ATOM   1120  C  C   . ALA B  1 2   ? -4.220  -28.166 4.822  1.00 38.83  ? 1   ALA B C   1 
ATOM   1121  O  O   . ALA B  1 2   ? -5.389  -28.487 4.982  1.00 42.88  ? 1   ALA B O   1 
ATOM   1122  C  CB  . ALA B  1 2   ? -3.692  -25.734 5.368  1.00 32.53  ? 1   ALA B CB  1 
ATOM   1123  N  N   . THR B  1 3   ? -3.178  -28.925 5.223  1.00 35.58  ? 2   THR B N   1 
ATOM   1124  C  CA  . THR B  1 3   ? -3.367  -30.147 5.997  1.00 36.41  ? 2   THR B CA  1 
ATOM   1125  C  C   . THR B  1 3   ? -3.001  -29.881 7.461  1.00 34.17  ? 2   THR B C   1 
ATOM   1126  O  O   . THR B  1 3   ? -1.937  -29.332 7.737  1.00 33.91  ? 2   THR B O   1 
ATOM   1127  C  CB  . THR B  1 3   ? -2.726  -31.365 5.311  1.00 34.31  ? 2   THR B CB  1 
ATOM   1128  O  OG1 . THR B  1 3   ? -1.349  -31.083 5.148  1.00 43.17  ? 2   THR B OG1 1 
ATOM   1129  C  CG2 . THR B  1 3   ? -3.313  -31.660 3.952  1.00 34.17  ? 2   THR B CG2 1 
ATOM   1130  N  N   . LYS B  1 4   ? -3.921  -30.216 8.378  1.00 31.71  ? 3   LYS B N   1 
ATOM   1131  C  CA  . LYS B  1 4   ? -3.672  -30.080 9.811  1.00 30.01  ? 3   LYS B CA  1 
ATOM   1132  C  C   . LYS B  1 4   ? -3.592  -31.454 10.480 1.00 30.32  ? 3   LYS B C   1 
ATOM   1133  O  O   . LYS B  1 4   ? -4.423  -32.335 10.250 1.00 34.00  ? 3   LYS B O   1 
ATOM   1134  C  CB  . LYS B  1 4   ? -4.776  -29.282 10.512 1.00 27.17  ? 3   LYS B CB  1 
ATOM   1135  C  CG  . LYS B  1 4   ? -4.706  -27.772 10.426 0.40 26.55  ? 3   LYS B CG  1 
ATOM   1136  C  CD  . LYS B  1 4   ? -5.954  -27.068 10.931 0.40 25.91  ? 3   LYS B CD  1 
ATOM   1137  C  CE  . LYS B  1 4   ? -6.239  -25.770 10.212 0.40 24.66  ? 3   LYS B CE  1 
ATOM   1138  N  NZ  . LYS B  1 4   ? -7.592  -25.284 10.559 0.40 23.88  ? 3   LYS B NZ  1 
ATOM   1139  N  N   . VAL B  1 5   ? -2.597  -31.593 11.354 1.00 27.53  ? 4   VAL B N   1 
ATOM   1140  C  CA  . VAL B  1 5   ? -2.330  -32.824 12.072 1.00 25.44  ? 4   VAL B CA  1 
ATOM   1141  C  C   . VAL B  1 5   ? -2.103  -32.468 13.537 1.00 23.23  ? 4   VAL B C   1 
ATOM   1142  O  O   . VAL B  1 5   ? -1.746  -31.336 13.868 1.00 24.16  ? 4   VAL B O   1 
ATOM   1143  C  CB  . VAL B  1 5   ? -1.107  -33.508 11.444 1.00 26.90  ? 4   VAL B CB  1 
ATOM   1144  C  CG1 . VAL B  1 5   ? -0.516  -34.594 12.329 1.00 29.15  ? 4   VAL B CG1 1 
ATOM   1145  C  CG2 . VAL B  1 5   ? -1.434  -34.051 10.068 1.00 26.01  ? 4   VAL B CG2 1 
ATOM   1146  N  N   . VAL B  1 6   ? -2.326  -33.426 14.432 1.00 21.16  ? 5   VAL B N   1 
ATOM   1147  C  CA  . VAL B  1 6   ? -2.179  -33.111 15.843 1.00 20.85  ? 5   VAL B CA  1 
ATOM   1148  C  C   . VAL B  1 6   ? -1.601  -34.311 16.589 1.00 21.06  ? 5   VAL B C   1 
ATOM   1149  O  O   . VAL B  1 6   ? -1.635  -35.445 16.104 1.00 19.79  ? 5   VAL B O   1 
ATOM   1150  C  CB  . VAL B  1 6   ? -3.515  -32.645 16.448 1.00 19.37  ? 5   VAL B CB  1 
ATOM   1151  C  CG1 . VAL B  1 6   ? -4.502  -33.789 16.585 1.00 18.49  ? 5   VAL B CG1 1 
ATOM   1152  C  CG2 . VAL B  1 6   ? -3.289  -31.930 17.766 1.00 21.20  ? 5   VAL B CG2 1 
ATOM   1153  N  N   . CYS B  1 7   ? -1.080  -34.038 17.786 1.00 21.60  ? 6   CYS B N   1 
ATOM   1154  C  CA  . CYS B  1 7   ? -0.468  -35.088 18.571 1.00 22.53  ? 6   CYS B CA  1 
ATOM   1155  C  C   . CYS B  1 7   ? -0.590  -34.722 20.042 1.00 23.26  ? 6   CYS B C   1 
ATOM   1156  O  O   . CYS B  1 7   ? -0.234  -33.606 20.431 1.00 24.56  ? 6   CYS B O   1 
ATOM   1157  C  CB  . CYS B  1 7   ? 1.003   -35.186 18.200 1.00 23.71  ? 6   CYS B CB  1 
ATOM   1158  S  SG  . CYS B  1 7   ? 1.871   -36.508 19.075 1.00 26.30  ? 6   CYS B SG  1 
ATOM   1159  N  N   . VAL B  1 8   ? -1.113  -35.652 20.848 1.00 22.88  ? 7   VAL B N   1 
ATOM   1160  C  CA  . VAL B  1 8   ? -1.202  -35.436 22.284 1.00 24.02  ? 7   VAL B CA  1 
ATOM   1161  C  C   . VAL B  1 8   ? -0.078  -36.227 22.942 1.00 26.89  ? 7   VAL B C   1 
ATOM   1162  O  O   . VAL B  1 8   ? -0.022  -37.443 22.778 1.00 31.79  ? 7   VAL B O   1 
ATOM   1163  C  CB  . VAL B  1 8   ? -2.573  -35.874 22.830 1.00 22.84  ? 7   VAL B CB  1 
ATOM   1164  C  CG1 . VAL B  1 8   ? -2.628  -35.797 24.342 1.00 23.48  ? 7   VAL B CG1 1 
ATOM   1165  C  CG2 . VAL B  1 8   ? -3.697  -35.042 22.249 1.00 22.43  ? 7   VAL B CG2 1 
ATOM   1166  N  N   . LEU B  1 9   ? 0.804   -35.543 23.679 1.00 26.64  ? 8   LEU B N   1 
ATOM   1167  C  CA  . LEU B  1 9   ? 1.910   -36.243 24.319 1.00 27.25  ? 8   LEU B CA  1 
ATOM   1168  C  C   . LEU B  1 9   ? 1.514   -36.616 25.746 1.00 28.69  ? 8   LEU B C   1 
ATOM   1169  O  O   . LEU B  1 9   ? 1.108   -35.742 26.508 1.00 27.80  ? 8   LEU B O   1 
ATOM   1170  C  CB  . LEU B  1 9   ? 3.141   -35.330 24.335 1.00 24.64  ? 8   LEU B CB  1 
ATOM   1171  C  CG  . LEU B  1 9   ? 3.620   -34.837 22.975 1.00 23.15  ? 8   LEU B CG  1 
ATOM   1172  C  CD1 . LEU B  1 9   ? 4.635   -33.737 23.157 1.00 23.10  ? 8   LEU B CD1 1 
ATOM   1173  C  CD2 . LEU B  1 9   ? 4.238   -35.952 22.152 1.00 22.67  ? 8   LEU B CD2 1 
ATOM   1174  N  N   . LYS B  1 10  ? 1.639   -37.910 26.075 1.00 31.03  ? 9   LYS B N   1 
ATOM   1175  C  CA  . LYS B  1 10  ? 1.489   -38.424 27.428 1.00 32.81  ? 9   LYS B CA  1 
ATOM   1176  C  C   . LYS B  1 10  ? 2.627   -39.399 27.715 1.00 33.83  ? 9   LYS B C   1 
ATOM   1177  O  O   . LYS B  1 10  ? 3.231   -39.930 26.790 1.00 33.63  ? 9   LYS B O   1 
ATOM   1178  C  CB  . LYS B  1 10  ? 0.130   -39.102 27.657 1.00 31.79  ? 9   LYS B CB  1 
ATOM   1179  C  CG  . LYS B  1 10  ? -0.999  -38.142 27.987 0.40 31.12  ? 9   LYS B CG  1 
ATOM   1180  C  CD  . LYS B  1 10  ? -2.361  -38.751 28.187 0.40 29.45  ? 9   LYS B CD  1 
ATOM   1181  C  CE  . LYS B  1 10  ? -3.357  -37.632 28.030 0.40 28.13  ? 9   LYS B CE  1 
ATOM   1182  N  NZ  . LYS B  1 10  ? -4.403  -37.984 27.049 0.40 26.43  ? 9   LYS B NZ  1 
ATOM   1183  N  N   . GLY B  1 11  ? 2.904   -39.609 29.006 1.00 32.78  ? 10  GLY B N   1 
ATOM   1184  C  CA  . GLY B  1 11  ? 3.876   -40.598 29.435 1.00 34.66  ? 10  GLY B CA  1 
ATOM   1185  C  C   . GLY B  1 11  ? 3.609   -41.052 30.867 1.00 36.06  ? 10  GLY B C   1 
ATOM   1186  O  O   . GLY B  1 11  ? 2.566   -40.729 31.428 1.00 35.97  ? 10  GLY B O   1 
ATOM   1187  N  N   . ASP B  1 12  ? 4.584   -41.725 31.476 1.00 38.28  ? 11  ASP B N   1 
ATOM   1188  C  CA  . ASP B  1 12  ? 4.413   -42.245 32.825 1.00 40.57  ? 11  ASP B CA  1 
ATOM   1189  C  C   . ASP B  1 12  ? 4.523   -41.127 33.859 1.00 40.73  ? 11  ASP B C   1 
ATOM   1190  O  O   . ASP B  1 12  ? 3.959   -41.226 34.947 1.00 40.17  ? 11  ASP B O   1 
ATOM   1191  C  CB  . ASP B  1 12  ? 5.445   -43.321 33.146 1.00 47.04  ? 11  ASP B CB  1 
ATOM   1192  C  CG  . ASP B  1 12  ? 5.282   -44.531 32.271 1.00 50.71  ? 11  ASP B CG  1 
ATOM   1193  O  OD1 . ASP B  1 12  ? 4.116   -44.870 32.002 1.00 53.90  ? 11  ASP B OD1 1 
ATOM   1194  O  OD2 . ASP B  1 12  ? 6.318   -45.101 31.868 1.00 51.81  ? 11  ASP B OD2 1 
ATOM   1195  N  N   . GLY B  1 13  ? 5.273   -40.069 33.520 1.00 39.81  ? 12  GLY B N   1 
ATOM   1196  C  CA  . GLY B  1 13  ? 5.565   -38.998 34.454 1.00 37.60  ? 12  GLY B CA  1 
ATOM   1197  C  C   . GLY B  1 13  ? 4.595   -37.843 34.261 1.00 38.48  ? 12  GLY B C   1 
ATOM   1198  O  O   . GLY B  1 13  ? 3.507   -38.028 33.715 1.00 39.01  ? 12  GLY B O   1 
ATOM   1199  N  N   . PRO B  1 14  ? 4.949   -36.620 34.714 1.00 39.10  ? 13  PRO B N   1 
ATOM   1200  C  CA  . PRO B  1 14  ? 4.047   -35.472 34.613 1.00 36.69  ? 13  PRO B CA  1 
ATOM   1201  C  C   . PRO B  1 14  ? 4.091   -34.742 33.270 1.00 34.73  ? 13  PRO B C   1 
ATOM   1202  O  O   . PRO B  1 14  ? 3.368   -33.771 33.087 1.00 36.25  ? 13  PRO B O   1 
ATOM   1203  C  CB  . PRO B  1 14  ? 4.553   -34.570 35.747 1.00 35.07  ? 13  PRO B CB  1 
ATOM   1204  C  CG  . PRO B  1 14  ? 6.048   -34.822 35.770 1.00 37.92  ? 13  PRO B CG  1 
ATOM   1205  C  CD  . PRO B  1 14  ? 6.218   -36.276 35.369 1.00 40.33  ? 13  PRO B CD  1 
ATOM   1206  N  N   . VAL B  1 15  ? 4.908   -35.216 32.329 1.00 32.11  ? 14  VAL B N   1 
ATOM   1207  C  CA  . VAL B  1 15  ? 5.041   -34.491 31.077 1.00 30.74  ? 14  VAL B CA  1 
ATOM   1208  C  C   . VAL B  1 15  ? 3.821   -34.740 30.198 1.00 29.93  ? 14  VAL B C   1 
ATOM   1209  O  O   . VAL B  1 15  ? 3.457   -35.883 29.960 1.00 28.88  ? 14  VAL B O   1 
ATOM   1210  C  CB  . VAL B  1 15  ? 6.348   -34.829 30.345 1.00 29.23  ? 14  VAL B CB  1 
ATOM   1211  C  CG1 . VAL B  1 15  ? 6.444   -34.101 29.019 1.00 27.54  ? 14  VAL B CG1 1 
ATOM   1212  C  CG2 . VAL B  1 15  ? 7.560   -34.550 31.197 1.00 29.76  ? 14  VAL B CG2 1 
ATOM   1213  N  N   . GLN B  1 16  ? 3.195   -33.653 29.739 1.00 31.46  ? 15  GLN B N   1 
ATOM   1214  C  CA  . GLN B  1 16  ? 2.073   -33.769 28.824 1.00 34.70  ? 15  GLN B CA  1 
ATOM   1215  C  C   . GLN B  1 16  ? 1.928   -32.496 27.999 1.00 31.58  ? 15  GLN B C   1 
ATOM   1216  O  O   . GLN B  1 16  ? 2.353   -31.429 28.439 1.00 31.26  ? 15  GLN B O   1 
ATOM   1217  C  CB  . GLN B  1 16  ? 0.782   -34.128 29.554 1.00 42.36  ? 15  GLN B CB  1 
ATOM   1218  C  CG  . GLN B  1 16  ? 0.322   -33.080 30.555 1.00 48.00  ? 15  GLN B CG  1 
ATOM   1219  C  CD  . GLN B  1 16  ? -0.913  -33.533 31.289 1.00 54.50  ? 15  GLN B CD  1 
ATOM   1220  O  OE1 . GLN B  1 16  ? -1.322  -34.693 31.220 1.00 60.87  ? 15  GLN B OE1 1 
ATOM   1221  N  NE2 . GLN B  1 16  ? -1.511  -32.614 32.023 1.00 57.15  ? 15  GLN B NE2 1 
ATOM   1222  N  N   . GLY B  1 17  ? 1.359   -32.639 26.795 1.00 28.87  ? 16  GLY B N   1 
ATOM   1223  C  CA  . GLY B  1 17  ? 1.215   -31.493 25.917 1.00 26.84  ? 16  GLY B CA  1 
ATOM   1224  C  C   . GLY B  1 17  ? 0.454   -31.823 24.638 1.00 25.77  ? 16  GLY B C   1 
ATOM   1225  O  O   . GLY B  1 17  ? 0.172   -32.989 24.348 1.00 27.85  ? 16  GLY B O   1 
ATOM   1226  N  N   . ILE B  1 18  ? 0.153   -30.772 23.870 1.00 23.75  ? 17  ILE B N   1 
ATOM   1227  C  CA  . ILE B  1 18  ? -0.490  -30.909 22.574 1.00 23.67  ? 17  ILE B CA  1 
ATOM   1228  C  C   . ILE B  1 18  ? 0.417   -30.236 21.552 1.00 25.22  ? 17  ILE B C   1 
ATOM   1229  O  O   . ILE B  1 18  ? 0.842   -29.107 21.773 1.00 27.25  ? 17  ILE B O   1 
ATOM   1230  C  CB  . ILE B  1 18  ? -1.881  -30.246 22.608 1.00 21.79  ? 17  ILE B CB  1 
ATOM   1231  C  CG1 . ILE B  1 18  ? -2.808  -30.973 23.587 1.00 20.93  ? 17  ILE B CG1 1 
ATOM   1232  C  CG2 . ILE B  1 18  ? -2.490  -30.160 21.207 1.00 20.59  ? 17  ILE B CG2 1 
ATOM   1233  C  CD1 . ILE B  1 18  ? -4.199  -30.395 23.687 1.00 19.65  ? 17  ILE B CD1 1 
ATOM   1234  N  N   . ILE B  1 19  ? 0.705   -30.933 20.448 1.00 25.13  ? 18  ILE B N   1 
ATOM   1235  C  CA  . ILE B  1 19  ? 1.496   -30.305 19.404 1.00 25.56  ? 18  ILE B CA  1 
ATOM   1236  C  C   . ILE B  1 19  ? 0.703   -30.359 18.106 1.00 26.27  ? 18  ILE B C   1 
ATOM   1237  O  O   . ILE B  1 19  ? 0.222   -31.420 17.717 1.00 26.47  ? 18  ILE B O   1 
ATOM   1238  C  CB  . ILE B  1 19  ? 2.868   -30.986 19.262 1.00 25.39  ? 18  ILE B CB  1 
ATOM   1239  C  CG1 . ILE B  1 19  ? 3.708   -30.894 20.543 1.00 24.47  ? 18  ILE B CG1 1 
ATOM   1240  C  CG2 . ILE B  1 19  ? 3.626   -30.456 18.061 1.00 23.23  ? 18  ILE B CG2 1 
ATOM   1241  C  CD1 . ILE B  1 19  ? 4.093   -29.500 20.977 1.00 23.22  ? 18  ILE B CD1 1 
ATOM   1242  N  N   . ASN B  1 20  ? 0.607   -29.209 17.438 1.00 27.47  ? 19  ASN B N   1 
ATOM   1243  C  CA  . ASN B  1 20  ? -0.084  -29.125 16.159 1.00 30.00  ? 19  ASN B CA  1 
ATOM   1244  C  C   . ASN B  1 20  ? 0.936   -29.084 15.031 1.00 32.76  ? 19  ASN B C   1 
ATOM   1245  O  O   . ASN B  1 20  ? 2.034   -28.544 15.191 1.00 37.14  ? 19  ASN B O   1 
ATOM   1246  C  CB  . ASN B  1 20  ? -0.932  -27.857 16.079 1.00 29.44  ? 19  ASN B CB  1 
ATOM   1247  C  CG  . ASN B  1 20  ? -1.864  -27.758 17.268 1.00 28.81  ? 19  ASN B CG  1 
ATOM   1248  O  OD1 . ASN B  1 20  ? -1.550  -27.063 18.228 1.00 29.75  ? 19  ASN B OD1 1 
ATOM   1249  N  ND2 . ASN B  1 20  ? -2.965  -28.501 17.258 1.00 28.59  ? 19  ASN B ND2 1 
ATOM   1250  N  N   . PHE B  1 21  ? 0.544   -29.650 13.887 1.00 33.11  ? 20  PHE B N   1 
ATOM   1251  C  CA  . PHE B  1 21  ? 1.355   -29.577 12.682 1.00 32.86  ? 20  PHE B CA  1 
ATOM   1252  C  C   . PHE B  1 21  ? 0.478   -29.040 11.567 1.00 31.94  ? 20  PHE B C   1 
ATOM   1253  O  O   . PHE B  1 21  ? -0.643  -29.509 11.396 1.00 32.67  ? 20  PHE B O   1 
ATOM   1254  C  CB  . PHE B  1 21  ? 1.839   -30.961 12.257 1.00 31.25  ? 20  PHE B CB  1 
ATOM   1255  C  CG  . PHE B  1 21  ? 2.704   -31.690 13.246 1.00 29.70  ? 20  PHE B CG  1 
ATOM   1256  C  CD1 . PHE B  1 21  ? 2.195   -32.163 14.445 1.00 28.46  ? 20  PHE B CD1 1 
ATOM   1257  C  CD2 . PHE B  1 21  ? 4.043   -31.923 12.957 1.00 30.13  ? 20  PHE B CD2 1 
ATOM   1258  C  CE1 . PHE B  1 21  ? 2.998   -32.852 15.343 1.00 30.25  ? 20  PHE B CE1 1 
ATOM   1259  C  CE2 . PHE B  1 21  ? 4.854   -32.608 13.854 1.00 30.80  ? 20  PHE B CE2 1 
ATOM   1260  C  CZ  . PHE B  1 21  ? 4.326   -33.074 15.043 1.00 32.01  ? 20  PHE B CZ  1 
ATOM   1261  N  N   . GLU B  1 22  ? 0.998   -28.069 10.821 1.00 35.42  ? 21  GLU B N   1 
ATOM   1262  C  CA  . GLU B  1 22  ? 0.228   -27.498 9.735  1.00 36.67  ? 21  GLU B CA  1 
ATOM   1263  C  C   . GLU B  1 22  ? 1.151   -27.299 8.543  1.00 37.68  ? 21  GLU B C   1 
ATOM   1264  O  O   . GLU B  1 22  ? 2.304   -26.894 8.702  1.00 40.28  ? 21  GLU B O   1 
ATOM   1265  C  CB  . GLU B  1 22  ? -0.430  -26.199 10.168 1.00 41.75  ? 21  GLU B CB  1 
ATOM   1266  C  CG  . GLU B  1 22  ? -1.550  -25.754 9.260  1.00 53.60  ? 21  GLU B CG  1 
ATOM   1267  C  CD  . GLU B  1 22  ? -2.294  -24.495 9.702  1.00 58.27  ? 21  GLU B CD  1 
ATOM   1268  O  OE1 . GLU B  1 22  ? -2.825  -24.482 10.819 1.00 63.62  ? 21  GLU B OE1 1 
ATOM   1269  O  OE2 . GLU B  1 22  ? -2.347  -23.519 8.933  1.00 62.93  ? 21  GLU B OE2 1 
ATOM   1270  N  N   . GLN B  1 23  ? 0.633   -27.609 7.343  1.00 37.78  ? 22  GLN B N   1 
ATOM   1271  C  CA  . GLN B  1 23  ? 1.419   -27.498 6.127  1.00 38.83  ? 22  GLN B CA  1 
ATOM   1272  C  C   . GLN B  1 23  ? 0.624   -26.755 5.061  1.00 41.74  ? 22  GLN B C   1 
ATOM   1273  O  O   . GLN B  1 23  ? -0.273  -27.326 4.485  1.00 48.23  ? 22  GLN B O   1 
ATOM   1274  C  CB  . GLN B  1 23  ? 1.856   -28.889 5.692  1.00 36.95  ? 22  GLN B CB  1 
ATOM   1275  C  CG  . GLN B  1 23  ? 2.865   -28.877 4.552  1.00 36.12  ? 22  GLN B CG  1 
ATOM   1276  C  CD  . GLN B  1 23  ? 3.259   -30.262 4.096  1.00 37.02  ? 22  GLN B CD  1 
ATOM   1277  O  OE1 . GLN B  1 23  ? 2.514   -31.221 4.182  1.00 34.47  ? 22  GLN B OE1 1 
ATOM   1278  N  NE2 . GLN B  1 23  ? 4.477   -30.406 3.623  1.00 38.29  ? 22  GLN B NE2 1 
ATOM   1279  N  N   . LYS B  1 24  ? 0.990   -25.478 4.838  1.00 40.86  ? 23  LYS B N   1 
ATOM   1280  C  CA  . LYS B  1 24  ? 0.224   -24.597 3.960  1.00 39.04  ? 23  LYS B CA  1 
ATOM   1281  C  C   . LYS B  1 24  ? 0.402   -25.009 2.497  1.00 40.68  ? 23  LYS B C   1 
ATOM   1282  O  O   . LYS B  1 24  ? -0.596  -25.179 1.809  1.00 45.96  ? 23  LYS B O   1 
ATOM   1283  C  CB  . LYS B  1 24  ? 0.452   -23.115 4.275  1.00 41.18  ? 23  LYS B CB  1 
ATOM   1284  C  CG  . LYS B  1 24  ? -0.353  -22.604 5.460  1.00 45.90  ? 23  LYS B CG  1 
ATOM   1285  C  CD  . LYS B  1 24  ? -0.322  -21.091 5.669  1.00 51.21  ? 23  LYS B CD  1 
ATOM   1286  C  CE  . LYS B  1 24  ? -1.247  -20.641 6.790  1.00 51.13  ? 23  LYS B CE  1 
ATOM   1287  N  NZ  . LYS B  1 24  ? -0.690  -19.610 7.726  1.00 45.57  ? 23  LYS B NZ  1 
ATOM   1288  N  N   . GLU B  1 25  ? 1.648   -25.190 2.034  1.00 42.19  ? 24  GLU B N   1 
ATOM   1289  C  CA  . GLU B  1 25  ? 1.883   -25.648 0.673  1.00 46.96  ? 24  GLU B CA  1 
ATOM   1290  C  C   . GLU B  1 25  ? 2.194   -27.143 0.673  1.00 47.43  ? 24  GLU B C   1 
ATOM   1291  O  O   . GLU B  1 25  ? 2.721   -27.647 1.675  1.00 48.67  ? 24  GLU B O   1 
ATOM   1292  C  CB  . GLU B  1 25  ? 3.028   -24.875 0.029  1.00 51.60  ? 24  GLU B CB  1 
ATOM   1293  C  CG  . GLU B  1 25  ? 2.881   -23.369 0.120  1.00 52.88  ? 24  GLU B CG  1 
ATOM   1294  C  CD  . GLU B  1 25  ? 4.166   -22.558 0.106  1.00 58.19  ? 24  GLU B CD  1 
ATOM   1295  O  OE1 . GLU B  1 25  ? 5.260   -23.142 0.271  1.00 62.73  ? 24  GLU B OE1 1 
ATOM   1296  O  OE2 . GLU B  1 25  ? 4.059   -21.342 -0.057 1.00 60.42  ? 24  GLU B OE2 1 
ATOM   1297  N  N   . SER B  1 26  ? 1.873   -27.828 -0.432 1.00 48.71  ? 25  SER B N   1 
ATOM   1298  C  CA  . SER B  1 26  ? 1.801   -29.289 -0.379 1.00 58.24  ? 25  SER B CA  1 
ATOM   1299  C  C   . SER B  1 26  ? 3.167   -29.951 -0.179 1.00 56.10  ? 25  SER B C   1 
ATOM   1300  O  O   . SER B  1 26  ? 3.264   -31.002 0.452  1.00 58.37  ? 25  SER B O   1 
ATOM   1301  C  CB  . SER B  1 26  ? 1.026   -29.900 -1.525 1.00 59.27  ? 25  SER B CB  1 
ATOM   1302  O  OG  . SER B  1 26  ? 1.279   -29.166 -2.709 1.00 55.20  ? 25  SER B OG  1 
ATOM   1303  N  N   . ASN B  1 27  ? 4.212   -29.360 -0.754 1.00 51.08  ? 26  ASN B N   1 
ATOM   1304  C  CA  . ASN B  1 27  ? 5.530   -29.927 -0.524 1.00 55.38  ? 26  ASN B CA  1 
ATOM   1305  C  C   . ASN B  1 27  ? 6.378   -28.978 0.322  1.00 53.06  ? 26  ASN B C   1 
ATOM   1306  O  O   . ASN B  1 27  ? 7.575   -29.160 0.463  1.00 58.49  ? 26  ASN B O   1 
ATOM   1307  C  CB  . ASN B  1 27  ? 6.193   -30.411 -1.813 1.00 63.88  ? 26  ASN B CB  1 
ATOM   1308  C  CG  . ASN B  1 27  ? 7.241   -31.472 -1.578 1.00 70.69  ? 26  ASN B CG  1 
ATOM   1309  O  OD1 . ASN B  1 27  ? 7.279   -32.164 -0.556 1.00 76.35  ? 26  ASN B OD1 1 
ATOM   1310  N  ND2 . ASN B  1 27  ? 8.064   -31.668 -2.590 1.00 76.42  ? 26  ASN B ND2 1 
ATOM   1311  N  N   . GLY B  1 28  ? 5.728   -27.996 0.924  1.00 48.98  ? 27  GLY B N   1 
ATOM   1312  C  CA  . GLY B  1 28  ? 6.390   -26.877 1.564  1.00 43.76  ? 27  GLY B CA  1 
ATOM   1313  C  C   . GLY B  1 28  ? 6.569   -27.129 3.058  1.00 39.03  ? 27  GLY B C   1 
ATOM   1314  O  O   . GLY B  1 28  ? 6.328   -28.224 3.573  1.00 37.88  ? 27  GLY B O   1 
ATOM   1315  N  N   . PRO B  1 29  ? 7.004   -26.084 3.807  1.00 36.55  ? 28  PRO B N   1 
ATOM   1316  C  CA  . PRO B  1 29  ? 7.406   -26.258 5.201  1.00 35.64  ? 28  PRO B CA  1 
ATOM   1317  C  C   . PRO B  1 29  ? 6.224   -26.595 6.102  1.00 33.42  ? 28  PRO B C   1 
ATOM   1318  O  O   . PRO B  1 29  ? 5.085   -26.289 5.766  1.00 34.34  ? 28  PRO B O   1 
ATOM   1319  C  CB  . PRO B  1 29  ? 7.997   -24.892 5.549  1.00 35.82  ? 28  PRO B CB  1 
ATOM   1320  C  CG  . PRO B  1 29  ? 7.282   -23.931 4.629  1.00 35.16  ? 28  PRO B CG  1 
ATOM   1321  C  CD  . PRO B  1 29  ? 7.173   -24.702 3.340  1.00 34.12  ? 28  PRO B CD  1 
ATOM   1322  N  N   . VAL B  1 30  ? 6.526   -27.227 7.246  1.00 30.59  ? 29  VAL B N   1 
ATOM   1323  C  CA  . VAL B  1 30  ? 5.526   -27.628 8.222  1.00 29.78  ? 29  VAL B CA  1 
ATOM   1324  C  C   . VAL B  1 30  ? 5.738   -26.797 9.485  1.00 29.36  ? 29  VAL B C   1 
ATOM   1325  O  O   . VAL B  1 30  ? 6.837   -26.780 10.038 1.00 30.56  ? 29  VAL B O   1 
ATOM   1326  C  CB  . VAL B  1 30  ? 5.634   -29.128 8.548  1.00 29.20  ? 29  VAL B CB  1 
ATOM   1327  C  CG1 . VAL B  1 30  ? 4.592   -29.552 9.584  1.00 28.75  ? 29  VAL B CG1 1 
ATOM   1328  C  CG2 . VAL B  1 30  ? 5.590   -30.008 7.298  1.00 29.13  ? 29  VAL B CG2 1 
ATOM   1329  N  N   . LYS B  1 31  ? 4.688   -26.102 9.937  1.00 26.50  ? 30  LYS B N   1 
ATOM   1330  C  CA  . LYS B  1 31  ? 4.763   -25.399 11.200 1.00 27.13  ? 30  LYS B CA  1 
ATOM   1331  C  C   . LYS B  1 31  ? 4.404   -26.377 12.306 1.00 27.88  ? 30  LYS B C   1 
ATOM   1332  O  O   . LYS B  1 31  ? 3.371   -27.028 12.256 1.00 30.33  ? 30  LYS B O   1 
ATOM   1333  C  CB  . LYS B  1 31  ? 3.868   -24.149 11.222 1.00 27.99  ? 30  LYS B CB  1 
ATOM   1334  C  CG  . LYS B  1 31  ? 4.498   -22.888 10.635 0.40 27.77  ? 30  LYS B CG  1 
ATOM   1335  C  CD  . LYS B  1 31  ? 3.960   -21.582 11.224 0.40 26.73  ? 30  LYS B CD  1 
ATOM   1336  C  CE  . LYS B  1 31  ? 4.087   -20.512 10.182 0.40 26.55  ? 30  LYS B CE  1 
ATOM   1337  N  NZ  . LYS B  1 31  ? 2.787   -19.844 9.939  0.40 26.67  ? 30  LYS B NZ  1 
ATOM   1338  N  N   . VAL B  1 32  ? 5.276   -26.458 13.311 1.00 27.83  ? 31  VAL B N   1 
ATOM   1339  C  CA  . VAL B  1 32  ? 5.023   -27.316 14.455 1.00 27.68  ? 31  VAL B CA  1 
ATOM   1340  C  C   . VAL B  1 32  ? 4.922   -26.427 15.688 1.00 28.74  ? 31  VAL B C   1 
ATOM   1341  O  O   . VAL B  1 32  ? 5.903   -25.777 16.054 1.00 31.17  ? 31  VAL B O   1 
ATOM   1342  C  CB  . VAL B  1 32  ? 6.151   -28.346 14.607 1.00 27.23  ? 31  VAL B CB  1 
ATOM   1343  C  CG1 . VAL B  1 32  ? 5.859   -29.325 15.724 1.00 26.58  ? 31  VAL B CG1 1 
ATOM   1344  C  CG2 . VAL B  1 32  ? 6.397   -29.094 13.303 1.00 26.95  ? 31  VAL B CG2 1 
ATOM   1345  N  N   . TRP B  1 33  ? 3.744   -26.379 16.321 1.00 28.91  ? 32  TRP B N   1 
ATOM   1346  C  CA  . TRP B  1 33  ? 3.633   -25.535 17.497 1.00 30.49  ? 32  TRP B CA  1 
ATOM   1347  C  C   . TRP B  1 33  ? 2.706   -26.161 18.528 1.00 31.42  ? 32  TRP B C   1 
ATOM   1348  O  O   . TRP B  1 33  ? 1.825   -26.954 18.204 1.00 30.83  ? 32  TRP B O   1 
ATOM   1349  C  CB  . TRP B  1 33  ? 3.154   -24.125 17.129 1.00 32.15  ? 32  TRP B CB  1 
ATOM   1350  C  CG  . TRP B  1 33  ? 1.671   -24.024 16.940 1.00 33.74  ? 32  TRP B CG  1 
ATOM   1351  C  CD1 . TRP B  1 33  ? 0.719   -23.598 17.831 1.00 32.64  ? 32  TRP B CD1 1 
ATOM   1352  C  CD2 . TRP B  1 33  ? 0.959   -24.393 15.751 1.00 35.40  ? 32  TRP B CD2 1 
ATOM   1353  N  NE1 . TRP B  1 33  ? -0.533  -23.675 17.290 1.00 31.12  ? 32  TRP B NE1 1 
ATOM   1354  C  CE2 . TRP B  1 33  ? -0.418  -24.153 16.007 1.00 35.35  ? 32  TRP B CE2 1 
ATOM   1355  C  CE3 . TRP B  1 33  ? 1.353   -24.906 14.508 1.00 36.01  ? 32  TRP B CE3 1 
ATOM   1356  C  CZ2 . TRP B  1 33  ? -1.397  -24.400 15.042 1.00 36.28  ? 32  TRP B CZ2 1 
ATOM   1357  C  CZ3 . TRP B  1 33  ? 0.377   -25.141 13.566 1.00 39.09  ? 32  TRP B CZ3 1 
ATOM   1358  C  CH2 . TRP B  1 33  ? -0.979  -24.893 13.830 1.00 36.76  ? 32  TRP B CH2 1 
ATOM   1359  N  N   . GLY B  1 34  ? 2.886   -25.718 19.773 1.00 30.13  ? 33  GLY B N   1 
ATOM   1360  C  CA  . GLY B  1 34  ? 1.992   -26.088 20.854 1.00 29.05  ? 33  GLY B CA  1 
ATOM   1361  C  C   . GLY B  1 34  ? 2.708   -25.905 22.176 1.00 30.63  ? 33  GLY B C   1 
ATOM   1362  O  O   . GLY B  1 34  ? 3.690   -25.177 22.270 1.00 40.90  ? 33  GLY B O   1 
ATOM   1363  N  N   . SER B  1 35  ? 2.230   -26.613 23.187 1.00 30.08  ? 34  SER B N   1 
ATOM   1364  C  CA  . SER B  1 35  ? 2.747   -26.370 24.521 1.00 30.63  ? 34  SER B CA  1 
ATOM   1365  C  C   . SER B  1 35  ? 2.955   -27.712 25.232 1.00 34.07  ? 34  SER B C   1 
ATOM   1366  O  O   . SER B  1 35  ? 2.140   -28.630 25.077 1.00 40.70  ? 34  SER B O   1 
ATOM   1367  C  CB  . SER B  1 35  ? 1.792   -25.467 25.212 1.00 26.89  ? 34  SER B CB  1 
ATOM   1368  O  OG  . SER B  1 35  ? 2.085   -25.400 26.581 1.00 27.77  ? 34  SER B OG  1 
ATOM   1369  N  N   . ILE B  1 36  ? 4.088   -27.856 25.936 1.00 32.73  ? 35  ILE B N   1 
ATOM   1370  C  CA  . ILE B  1 36  ? 4.315   -29.041 26.754 1.00 28.51  ? 35  ILE B CA  1 
ATOM   1371  C  C   . ILE B  1 36  ? 4.606   -28.561 28.174 1.00 29.44  ? 35  ILE B C   1 
ATOM   1372  O  O   . ILE B  1 36  ? 5.362   -27.607 28.365 1.00 30.21  ? 35  ILE B O   1 
ATOM   1373  C  CB  . ILE B  1 36  ? 5.482   -29.871 26.202 1.00 26.91  ? 35  ILE B CB  1 
ATOM   1374  C  CG1 . ILE B  1 36  ? 5.335   -30.125 24.705 1.00 26.16  ? 35  ILE B CG1 1 
ATOM   1375  C  CG2 . ILE B  1 36  ? 5.640   -31.164 26.984 1.00 25.14  ? 35  ILE B CG2 1 
ATOM   1376  C  CD1 . ILE B  1 36  ? 6.582   -30.761 24.080 1.00 27.45  ? 35  ILE B CD1 1 
ATOM   1377  N  N   . LYS B  1 37  ? 4.001   -29.229 29.161 1.00 27.94  ? 36  LYS B N   1 
ATOM   1378  C  CA  . LYS B  1 37  ? 4.210   -28.838 30.544 1.00 28.41  ? 36  LYS B CA  1 
ATOM   1379  C  C   . LYS B  1 37  ? 4.777   -30.020 31.334 1.00 31.68  ? 36  LYS B C   1 
ATOM   1380  O  O   . LYS B  1 37  ? 4.748   -31.153 30.858 1.00 31.67  ? 36  LYS B O   1 
ATOM   1381  C  CB  . LYS B  1 37  ? 2.915   -28.270 31.132 1.00 25.27  ? 36  LYS B CB  1 
ATOM   1382  C  CG  . LYS B  1 37  ? 1.772   -29.263 31.304 1.00 21.90  ? 36  LYS B CG  1 
ATOM   1383  C  CD  . LYS B  1 37  ? 0.748   -28.416 32.074 0.00 58.91  ? 36  LYS B CD  1 
ATOM   1384  C  CE  . LYS B  1 37  ? -0.530  -29.212 32.275 0.00 65.37  ? 36  LYS B CE  1 
ATOM   1385  N  NZ  . LYS B  1 37  ? -1.671  -28.526 32.958 0.00 62.58  ? 36  LYS B NZ  1 
ATOM   1386  N  N   . GLY B  1 38  ? 5.325   -29.727 32.521 1.00 32.82  ? 37  GLY B N   1 
ATOM   1387  C  CA  . GLY B  1 38  ? 5.888   -30.735 33.408 1.00 33.46  ? 37  GLY B CA  1 
ATOM   1388  C  C   . GLY B  1 38  ? 7.330   -31.143 33.076 1.00 35.84  ? 37  GLY B C   1 
ATOM   1389  O  O   . GLY B  1 38  ? 7.815   -32.145 33.600 1.00 39.65  ? 37  GLY B O   1 
ATOM   1390  N  N   . LEU B  1 39  ? 8.013   -30.361 32.228 1.00 32.99  ? 38  LEU B N   1 
ATOM   1391  C  CA  . LEU B  1 39  ? 9.395   -30.636 31.865 1.00 33.52  ? 38  LEU B CA  1 
ATOM   1392  C  C   . LEU B  1 39  ? 10.341  -29.983 32.866 1.00 36.96  ? 38  LEU B C   1 
ATOM   1393  O  O   . LEU B  1 39  ? 9.984   -29.000 33.506 1.00 41.40  ? 38  LEU B O   1 
ATOM   1394  C  CB  . LEU B  1 39  ? 9.665   -30.080 30.467 1.00 30.27  ? 38  LEU B CB  1 
ATOM   1395  C  CG  . LEU B  1 39  ? 8.991   -30.833 29.328 1.00 30.08  ? 38  LEU B CG  1 
ATOM   1396  C  CD1 . LEU B  1 39  ? 8.968   -29.989 28.064 1.00 28.87  ? 38  LEU B CD1 1 
ATOM   1397  C  CD2 . LEU B  1 39  ? 9.686   -32.177 29.097 1.00 29.81  ? 38  LEU B CD2 1 
ATOM   1398  N  N   . THR B  1 40  ? 11.555  -30.530 32.987 1.00 36.52  ? 39  THR B N   1 
ATOM   1399  C  CA  . THR B  1 40  ? 12.606  -29.849 33.729 1.00 33.41  ? 39  THR B CA  1 
ATOM   1400  C  C   . THR B  1 40  ? 13.100  -28.678 32.890 1.00 33.58  ? 39  THR B C   1 
ATOM   1401  O  O   . THR B  1 40  ? 13.077  -28.743 31.667 1.00 30.78  ? 39  THR B O   1 
ATOM   1402  C  CB  . THR B  1 40  ? 13.763  -30.790 34.069 1.00 31.90  ? 39  THR B CB  1 
ATOM   1403  O  OG1 . THR B  1 40  ? 14.114  -31.415 32.830 1.00 31.73  ? 39  THR B OG1 1 
ATOM   1404  C  CG2 . THR B  1 40  ? 13.398  -31.769 35.171 1.00 28.26  ? 39  THR B CG2 1 
ATOM   1405  N  N   . GLU B  1 41  ? 13.541  -27.611 33.562 1.00 36.60  ? 40  GLU B N   1 
ATOM   1406  C  CA  . GLU B  1 41  ? 14.001  -26.420 32.870 1.00 37.02  ? 40  GLU B CA  1 
ATOM   1407  C  C   . GLU B  1 41  ? 15.119  -26.800 31.905 1.00 35.49  ? 40  GLU B C   1 
ATOM   1408  O  O   . GLU B  1 41  ? 15.946  -27.646 32.229 1.00 36.55  ? 40  GLU B O   1 
ATOM   1409  C  CB  . GLU B  1 41  ? 14.469  -25.377 33.879 1.00 40.38  ? 40  GLU B CB  1 
ATOM   1410  C  CG  . GLU B  1 41  ? 14.835  -24.069 33.213 1.00 51.21  ? 40  GLU B CG  1 
ATOM   1411  C  CD  . GLU B  1 41  ? 15.243  -22.925 34.127 1.00 57.36  ? 40  GLU B CD  1 
ATOM   1412  O  OE1 . GLU B  1 41  ? 15.406  -23.161 35.341 1.00 63.14  ? 40  GLU B OE1 1 
ATOM   1413  O  OE2 . GLU B  1 41  ? 15.387  -21.795 33.614 1.00 57.00  ? 40  GLU B OE2 1 
ATOM   1414  N  N   . GLY B  1 42  ? 15.117  -26.198 30.712 1.00 31.51  ? 41  GLY B N   1 
ATOM   1415  C  CA  . GLY B  1 42  ? 16.214  -26.399 29.778 1.00 30.39  ? 41  GLY B CA  1 
ATOM   1416  C  C   . GLY B  1 42  ? 15.801  -27.109 28.490 1.00 32.30  ? 41  GLY B C   1 
ATOM   1417  O  O   . GLY B  1 42  ? 14.611  -27.200 28.180 1.00 32.83  ? 41  GLY B O   1 
ATOM   1418  N  N   . LEU B  1 43  ? 16.808  -27.611 27.758 1.00 33.68  ? 42  LEU B N   1 
ATOM   1419  C  CA  . LEU B  1 43  ? 16.634  -28.197 26.436 1.00 33.38  ? 42  LEU B CA  1 
ATOM   1420  C  C   . LEU B  1 43  ? 16.163  -29.644 26.556 1.00 33.40  ? 42  LEU B C   1 
ATOM   1421  O  O   . LEU B  1 43  ? 16.622  -30.373 27.431 1.00 31.13  ? 42  LEU B O   1 
ATOM   1422  C  CB  . LEU B  1 43  ? 17.955  -28.155 25.663 1.00 34.03  ? 42  LEU B CB  1 
ATOM   1423  C  CG  . LEU B  1 43  ? 18.469  -26.759 25.319 1.00 33.67  ? 42  LEU B CG  1 
ATOM   1424  C  CD1 . LEU B  1 43  ? 19.925  -26.799 24.894 1.00 31.02  ? 42  LEU B CD1 1 
ATOM   1425  C  CD2 . LEU B  1 43  ? 17.575  -26.119 24.266 1.00 34.63  ? 42  LEU B CD2 1 
ATOM   1426  N  N   . HIS B  1 44  ? 15.251  -30.032 25.653 1.00 34.41  ? 43  HIS B N   1 
ATOM   1427  C  CA  . HIS B  1 44  ? 14.768  -31.398 25.533 1.00 34.30  ? 43  HIS B CA  1 
ATOM   1428  C  C   . HIS B  1 44  ? 14.698  -31.793 24.062 1.00 35.38  ? 43  HIS B C   1 
ATOM   1429  O  O   . HIS B  1 44  ? 14.200  -31.042 23.220 1.00 38.54  ? 43  HIS B O   1 
ATOM   1430  C  CB  . HIS B  1 44  ? 13.410  -31.557 26.212 1.00 32.96  ? 43  HIS B CB  1 
ATOM   1431  C  CG  . HIS B  1 44  ? 13.441  -31.360 27.690 1.00 34.00  ? 43  HIS B CG  1 
ATOM   1432  N  ND1 . HIS B  1 44  ? 13.559  -32.418 28.579 1.00 34.63  ? 43  HIS B ND1 1 
ATOM   1433  C  CD2 . HIS B  1 44  ? 13.347  -30.252 28.446 1.00 34.27  ? 43  HIS B CD2 1 
ATOM   1434  C  CE1 . HIS B  1 44  ? 13.533  -31.974 29.815 1.00 34.97  ? 43  HIS B CE1 1 
ATOM   1435  N  NE2 . HIS B  1 44  ? 13.395  -30.647 29.762 1.00 37.99  ? 43  HIS B NE2 1 
ATOM   1436  N  N   . GLY B  1 45  ? 15.239  -32.981 23.767 1.00 33.97  ? 44  GLY B N   1 
ATOM   1437  C  CA  . GLY B  1 45  ? 15.223  -33.536 22.424 1.00 32.94  ? 44  GLY B CA  1 
ATOM   1438  C  C   . GLY B  1 45  ? 13.790  -33.795 21.959 1.00 30.59  ? 44  GLY B C   1 
ATOM   1439  O  O   . GLY B  1 45  ? 12.932  -34.215 22.738 1.00 27.31  ? 44  GLY B O   1 
ATOM   1440  N  N   . PHE B  1 46  ? 13.558  -33.556 20.671 1.00 30.24  ? 45  PHE B N   1 
ATOM   1441  C  CA  . PHE B  1 46  ? 12.217  -33.506 20.126 1.00 30.88  ? 45  PHE B CA  1 
ATOM   1442  C  C   . PHE B  1 46  ? 12.250  -34.164 18.757 1.00 30.29  ? 45  PHE B C   1 
ATOM   1443  O  O   . PHE B  1 46  ? 12.791  -33.584 17.820 1.00 31.49  ? 45  PHE B O   1 
ATOM   1444  C  CB  . PHE B  1 46  ? 11.813  -32.035 20.004 1.00 32.18  ? 45  PHE B CB  1 
ATOM   1445  C  CG  . PHE B  1 46  ? 10.355  -31.755 19.766 1.00 32.35  ? 45  PHE B CG  1 
ATOM   1446  C  CD1 . PHE B  1 46  ? 9.397   -32.065 20.726 1.00 33.52  ? 45  PHE B CD1 1 
ATOM   1447  C  CD2 . PHE B  1 46  ? 9.952   -31.126 18.600 1.00 31.98  ? 45  PHE B CD2 1 
ATOM   1448  C  CE1 . PHE B  1 46  ? 8.055   -31.760 20.522 1.00 33.29  ? 45  PHE B CE1 1 
ATOM   1449  C  CE2 . PHE B  1 46  ? 8.615   -30.819 18.389 1.00 31.88  ? 45  PHE B CE2 1 
ATOM   1450  C  CZ  . PHE B  1 46  ? 7.665   -31.144 19.351 1.00 32.98  ? 45  PHE B CZ  1 
ATOM   1451  N  N   . HIS B  1 47  ? 11.697  -35.381 18.659 1.00 28.97  ? 46  HIS B N   1 
ATOM   1452  C  CA  . HIS B  1 47  ? 11.865  -36.159 17.443 1.00 27.12  ? 46  HIS B CA  1 
ATOM   1453  C  C   . HIS B  1 47  ? 10.576  -36.861 17.039 1.00 27.85  ? 46  HIS B C   1 
ATOM   1454  O  O   . HIS B  1 47  ? 9.733   -37.194 17.880 1.00 27.00  ? 46  HIS B O   1 
ATOM   1455  C  CB  . HIS B  1 47  ? 12.968  -37.208 17.613 1.00 26.31  ? 46  HIS B CB  1 
ATOM   1456  C  CG  . HIS B  1 47  ? 14.165  -36.705 18.338 1.00 26.14  ? 46  HIS B CG  1 
ATOM   1457  N  ND1 . HIS B  1 47  ? 14.470  -37.097 19.626 1.00 25.36  ? 46  HIS B ND1 1 
ATOM   1458  C  CD2 . HIS B  1 47  ? 15.122  -35.826 17.961 1.00 27.96  ? 46  HIS B CD2 1 
ATOM   1459  C  CE1 . HIS B  1 47  ? 15.564  -36.480 20.017 1.00 27.82  ? 46  HIS B CE1 1 
ATOM   1460  N  NE2 . HIS B  1 47  ? 15.984  -35.686 19.013 1.00 27.91  ? 46  HIS B NE2 1 
ATOM   1461  N  N   . VAL B  1 48  ? 10.473  -37.098 15.728 1.00 26.75  ? 47  VAL B N   1 
ATOM   1462  C  CA  . VAL B  1 48  ? 9.509   -38.057 15.215 1.00 25.88  ? 47  VAL B CA  1 
ATOM   1463  C  C   . VAL B  1 48  ? 10.201  -39.419 15.128 1.00 24.82  ? 47  VAL B C   1 
ATOM   1464  O  O   . VAL B  1 48  ? 11.157  -39.587 14.374 1.00 23.46  ? 47  VAL B O   1 
ATOM   1465  C  CB  . VAL B  1 48  ? 8.953   -37.632 13.843 1.00 24.92  ? 47  VAL B CB  1 
ATOM   1466  C  CG1 . VAL B  1 48  ? 7.903   -38.614 13.348 1.00 22.74  ? 47  VAL B CG1 1 
ATOM   1467  C  CG2 . VAL B  1 48  ? 8.375   -36.228 13.883 1.00 24.39  ? 47  VAL B CG2 1 
ATOM   1468  N  N   . HIS B  1 49  ? 9.699   -40.383 15.902 1.00 24.36  ? 48  HIS B N   1 
ATOM   1469  C  CA  . HIS B  1 49  ? 10.144  -41.767 15.818 1.00 24.27  ? 48  HIS B CA  1 
ATOM   1470  C  C   . HIS B  1 49  ? 9.325   -42.524 14.773 1.00 25.00  ? 48  HIS B C   1 
ATOM   1471  O  O   . HIS B  1 49  ? 8.304   -42.031 14.294 1.00 27.04  ? 48  HIS B O   1 
ATOM   1472  C  CB  . HIS B  1 49  ? 10.095  -42.426 17.198 1.00 24.34  ? 48  HIS B CB  1 
ATOM   1473  C  CG  . HIS B  1 49  ? 11.071  -41.840 18.161 1.00 24.98  ? 48  HIS B CG  1 
ATOM   1474  N  ND1 . HIS B  1 49  ? 12.061  -42.599 18.760 1.00 24.42  ? 48  HIS B ND1 1 
ATOM   1475  C  CD2 . HIS B  1 49  ? 11.219  -40.579 18.629 1.00 24.70  ? 48  HIS B CD2 1 
ATOM   1476  C  CE1 . HIS B  1 49  ? 12.765  -41.828 19.563 1.00 25.10  ? 48  HIS B CE1 1 
ATOM   1477  N  NE2 . HIS B  1 49  ? 12.271  -40.593 19.508 1.00 24.49  ? 48  HIS B NE2 1 
ATOM   1478  N  N   . GLU B  1 50  ? 9.768   -43.742 14.448 1.00 25.11  ? 49  GLU B N   1 
ATOM   1479  C  CA  . GLU B  1 50  ? 9.341   -44.466 13.259 1.00 22.96  ? 49  GLU B CA  1 
ATOM   1480  C  C   . GLU B  1 50  ? 7.914   -44.991 13.367 1.00 22.00  ? 49  GLU B C   1 
ATOM   1481  O  O   . GLU B  1 50  ? 7.160   -44.906 12.394 1.00 22.98  ? 49  GLU B O   1 
ATOM   1482  C  CB  . GLU B  1 50  ? 10.276  -45.640 12.989 1.00 22.23  ? 49  GLU B CB  1 
ATOM   1483  C  CG  . GLU B  1 50  ? 10.134  -46.167 11.581 1.00 23.08  ? 49  GLU B CG  1 
ATOM   1484  C  CD  . GLU B  1 50  ? 11.063  -47.325 11.230 1.00 23.09  ? 49  GLU B CD  1 
ATOM   1485  O  OE1 . GLU B  1 50  ? 12.077  -47.534 11.917 1.00 21.82  ? 49  GLU B OE1 1 
ATOM   1486  O  OE2 . GLU B  1 50  ? 10.756  -48.028 10.260 1.00 24.97  ? 49  GLU B OE2 1 
ATOM   1487  N  N   . PHE B  1 51  ? 7.559   -45.547 14.532 1.00 20.61  ? 50  PHE B N   1 
ATOM   1488  C  CA  . PHE B  1 51  ? 6.329   -46.316 14.652 1.00 23.01  ? 50  PHE B CA  1 
ATOM   1489  C  C   . PHE B  1 51  ? 5.308   -45.600 15.529 1.00 23.80  ? 50  PHE B C   1 
ATOM   1490  O  O   . PHE B  1 51  ? 5.639   -45.163 16.632 1.00 26.76  ? 50  PHE B O   1 
ATOM   1491  C  CB  . PHE B  1 51  ? 6.607   -47.693 15.260 1.00 22.04  ? 50  PHE B CB  1 
ATOM   1492  C  CG  . PHE B  1 51  ? 7.650   -48.461 14.486 1.00 23.10  ? 50  PHE B CG  1 
ATOM   1493  C  CD1 . PHE B  1 51  ? 7.491   -48.713 13.122 1.00 22.07  ? 50  PHE B CD1 1 
ATOM   1494  C  CD2 . PHE B  1 51  ? 8.802   -48.918 15.124 1.00 22.97  ? 50  PHE B CD2 1 
ATOM   1495  C  CE1 . PHE B  1 51  ? 8.471   -49.392 12.407 1.00 20.37  ? 50  PHE B CE1 1 
ATOM   1496  C  CE2 . PHE B  1 51  ? 9.785   -49.576 14.386 1.00 21.85  ? 50  PHE B CE2 1 
ATOM   1497  C  CZ  . PHE B  1 51  ? 9.609   -49.833 13.041 1.00 19.71  ? 50  PHE B CZ  1 
ATOM   1498  N  N   . GLY B  1 52  ? 4.070   -45.535 15.024 1.00 22.85  ? 51  GLY B N   1 
ATOM   1499  C  CA  . GLY B  1 52  ? 2.909   -45.143 15.799 1.00 24.33  ? 51  GLY B CA  1 
ATOM   1500  C  C   . GLY B  1 52  ? 2.451   -46.282 16.707 1.00 24.58  ? 51  GLY B C   1 
ATOM   1501  O  O   . GLY B  1 52  ? 1.299   -46.713 16.648 1.00 25.66  ? 51  GLY B O   1 
ATOM   1502  N  N   . ASP B  1 53  ? 3.377   -46.770 17.534 1.00 24.20  ? 52  ASP B N   1 
ATOM   1503  C  CA  . ASP B  1 53  ? 3.114   -47.947 18.330 1.00 28.07  ? 52  ASP B CA  1 
ATOM   1504  C  C   . ASP B  1 53  ? 3.397   -47.619 19.788 1.00 29.79  ? 52  ASP B C   1 
ATOM   1505  O  O   . ASP B  1 53  ? 4.525   -47.354 20.154 1.00 29.48  ? 52  ASP B O   1 
ATOM   1506  C  CB  . ASP B  1 53  ? 3.946   -49.119 17.810 1.00 28.63  ? 52  ASP B CB  1 
ATOM   1507  C  CG  . ASP B  1 53  ? 3.710   -50.424 18.553 1.00 29.59  ? 52  ASP B CG  1 
ATOM   1508  O  OD1 . ASP B  1 53  ? 3.279   -50.375 19.734 1.00 28.26  ? 52  ASP B OD1 1 
ATOM   1509  O  OD2 . ASP B  1 53  ? 3.945   -51.496 17.932 1.00 30.62  ? 52  ASP B OD2 1 
ATOM   1510  N  N   . ASN B  1 54  ? 2.354   -47.636 20.612 1.00 31.79  ? 53  ASN B N   1 
ATOM   1511  C  CA  . ASN B  1 54  ? 2.487   -47.261 22.007 1.00 31.14  ? 53  ASN B CA  1 
ATOM   1512  C  C   . ASN B  1 54  ? 2.201   -48.481 22.882 1.00 28.52  ? 53  ASN B C   1 
ATOM   1513  O  O   . ASN B  1 54  ? 1.956   -48.351 24.075 1.00 27.04  ? 53  ASN B O   1 
ATOM   1514  C  CB  . ASN B  1 54  ? 1.637   -46.022 22.302 1.00 39.85  ? 53  ASN B CB  1 
ATOM   1515  C  CG  . ASN B  1 54  ? 1.704   -45.534 23.733 1.00 51.52  ? 53  ASN B CG  1 
ATOM   1516  O  OD1 . ASN B  1 54  ? 2.782   -45.293 24.268 1.00 62.98  ? 53  ASN B OD1 1 
ATOM   1517  N  ND2 . ASN B  1 54  ? 0.547   -45.377 24.364 1.00 57.02  ? 53  ASN B ND2 1 
ATOM   1518  N  N   . THR B  1 55  ? 2.273   -49.679 22.292 1.00 28.43  ? 54  THR B N   1 
ATOM   1519  C  CA  . THR B  1 55  ? 1.849   -50.894 22.978 1.00 28.46  ? 54  THR B CA  1 
ATOM   1520  C  C   . THR B  1 55  ? 2.667   -51.122 24.247 1.00 29.05  ? 54  THR B C   1 
ATOM   1521  O  O   . THR B  1 55  ? 2.148   -51.668 25.215 1.00 29.41  ? 54  THR B O   1 
ATOM   1522  C  CB  . THR B  1 55  ? 1.932   -52.138 22.087 1.00 27.19  ? 54  THR B CB  1 
ATOM   1523  O  OG1 . THR B  1 55  ? 3.277   -52.252 21.638 1.00 27.06  ? 54  THR B OG1 1 
ATOM   1524  C  CG2 . THR B  1 55  ? 1.017   -52.084 20.890 1.00 26.43  ? 54  THR B CG2 1 
ATOM   1525  N  N   . ALA B  1 56  ? 3.940   -50.713 24.227 1.00 30.30  ? 55  ALA B N   1 
ATOM   1526  C  CA  . ALA B  1 56  ? 4.823   -50.909 25.362 1.00 29.80  ? 55  ALA B CA  1 
ATOM   1527  C  C   . ALA B  1 56  ? 5.353   -49.555 25.817 1.00 33.13  ? 55  ALA B C   1 
ATOM   1528  O  O   . ALA B  1 56  ? 6.550   -49.404 26.066 1.00 39.92  ? 55  ALA B O   1 
ATOM   1529  C  CB  . ALA B  1 56  ? 5.943   -51.828 24.951 1.00 28.38  ? 55  ALA B CB  1 
ATOM   1530  N  N   . GLY B  1 57  ? 4.462   -48.559 25.883 1.00 33.00  ? 56  GLY B N   1 
ATOM   1531  C  CA  . GLY B  1 57  ? 4.864   -47.196 26.196 1.00 29.78  ? 56  GLY B CA  1 
ATOM   1532  C  C   . GLY B  1 57  ? 5.613   -46.562 25.025 1.00 29.91  ? 56  GLY B C   1 
ATOM   1533  O  O   . GLY B  1 57  ? 5.487   -46.996 23.878 1.00 31.60  ? 56  GLY B O   1 
ATOM   1534  N  N   . CYS B  1 58  ? 6.416   -45.538 25.325 1.00 28.61  ? 57  CYS B N   1 
ATOM   1535  C  CA  . CYS B  1 58  ? 7.089   -44.800 24.272 1.00 28.94  ? 57  CYS B CA  1 
ATOM   1536  C  C   . CYS B  1 58  ? 8.178   -45.640 23.616 1.00 28.76  ? 57  CYS B C   1 
ATOM   1537  O  O   . CYS B  1 58  ? 8.534   -45.367 22.469 1.00 26.83  ? 57  CYS B O   1 
ATOM   1538  C  CB  . CYS B  1 58  ? 7.656   -43.501 24.800 1.00 31.48  ? 57  CYS B CB  1 
ATOM   1539  S  SG  . CYS B  1 58  ? 6.392   -42.315 25.309 1.00 33.33  ? 57  CYS B SG  1 
ATOM   1540  N  N   . THR B  1 59  ? 8.664   -46.673 24.323 1.00 30.69  ? 58  THR B N   1 
ATOM   1541  C  CA  . THR B  1 59  ? 9.734   -47.528 23.822 1.00 28.67  ? 58  THR B CA  1 
ATOM   1542  C  C   . THR B  1 59  ? 9.372   -48.122 22.462 1.00 27.73  ? 58  THR B C   1 
ATOM   1543  O  O   . THR B  1 59  ? 10.230  -48.251 21.587 1.00 26.64  ? 58  THR B O   1 
ATOM   1544  C  CB  . THR B  1 59  ? 9.975   -48.750 24.714 1.00 25.63  ? 58  THR B CB  1 
ATOM   1545  O  OG1 . THR B  1 59  ? 10.080  -48.281 26.050 1.00 24.68  ? 58  THR B OG1 1 
ATOM   1546  C  CG2 . THR B  1 59  ? 11.242  -49.482 24.335 1.00 26.10  ? 58  THR B CG2 1 
ATOM   1547  N  N   . SER B  1 60  ? 8.098   -48.501 22.310 1.00 25.74  ? 59  SER B N   1 
ATOM   1548  C  CA  . SER B  1 60  ? 7.729   -49.297 21.157 1.00 26.99  ? 59  SER B CA  1 
ATOM   1549  C  C   . SER B  1 60  ? 7.615   -48.432 19.898 1.00 25.65  ? 59  SER B C   1 
ATOM   1550  O  O   . SER B  1 60  ? 7.333   -48.937 18.811 1.00 24.60  ? 59  SER B O   1 
ATOM   1551  C  CB  . SER B  1 60  ? 6.524   -50.172 21.446 1.00 27.06  ? 59  SER B CB  1 
ATOM   1552  O  OG  . SER B  1 60  ? 5.445   -49.399 21.924 1.00 28.80  ? 59  SER B OG  1 
ATOM   1553  N  N   . ALA B  1 61  ? 7.918   -47.139 20.051 1.00 26.00  ? 60  ALA B N   1 
ATOM   1554  C  CA  . ALA B  1 61  ? 7.887   -46.181 18.951 1.00 26.36  ? 60  ALA B CA  1 
ATOM   1555  C  C   . ALA B  1 61  ? 9.073   -46.409 18.019 1.00 27.51  ? 60  ALA B C   1 
ATOM   1556  O  O   . ALA B  1 61  ? 9.070   -45.935 16.875 1.00 30.09  ? 60  ALA B O   1 
ATOM   1557  C  CB  . ALA B  1 61  ? 7.880   -44.774 19.495 1.00 25.51  ? 60  ALA B CB  1 
ATOM   1558  N  N   . GLY B  1 62  ? 10.087  -47.120 18.532 1.00 25.08  ? 61  GLY B N   1 
ATOM   1559  C  CA  . GLY B  1 62  ? 11.280  -47.428 17.766 1.00 24.82  ? 61  GLY B CA  1 
ATOM   1560  C  C   . GLY B  1 62  ? 12.233  -46.239 17.660 1.00 24.67  ? 61  GLY B C   1 
ATOM   1561  O  O   . GLY B  1 62  ? 12.159  -45.308 18.466 1.00 24.72  ? 61  GLY B O   1 
ATOM   1562  N  N   . PRO B  1 63  ? 13.143  -46.232 16.650 1.00 23.79  ? 62  PRO B N   1 
ATOM   1563  C  CA  . PRO B  1 63  ? 14.174  -45.196 16.535 1.00 22.95  ? 62  PRO B CA  1 
ATOM   1564  C  C   . PRO B  1 63  ? 13.635  -43.922 15.888 1.00 22.40  ? 62  PRO B C   1 
ATOM   1565  O  O   . PRO B  1 63  ? 12.475  -43.867 15.502 1.00 21.96  ? 62  PRO B O   1 
ATOM   1566  C  CB  . PRO B  1 63  ? 15.183  -45.873 15.596 1.00 21.78  ? 62  PRO B CB  1 
ATOM   1567  C  CG  . PRO B  1 63  ? 14.316  -46.677 14.668 1.00 21.53  ? 62  PRO B CG  1 
ATOM   1568  C  CD  . PRO B  1 63  ? 13.191  -47.203 15.540 1.00 22.58  ? 62  PRO B CD  1 
ATOM   1569  N  N   . HIS B  1 64  ? 14.490  -42.900 15.762 1.00 22.39  ? 63  HIS B N   1 
ATOM   1570  C  CA  . HIS B  1 64  ? 14.112  -41.706 15.022 1.00 21.27  ? 63  HIS B CA  1 
ATOM   1571  C  C   . HIS B  1 64  ? 13.690  -42.124 13.617 1.00 20.94  ? 63  HIS B C   1 
ATOM   1572  O  O   . HIS B  1 64  ? 14.359  -42.953 13.005 1.00 21.30  ? 63  HIS B O   1 
ATOM   1573  C  CB  . HIS B  1 64  ? 15.276  -40.713 14.968 1.00 19.53  ? 63  HIS B CB  1 
ATOM   1574  C  CG  . HIS B  1 64  ? 15.719  -40.176 16.287 1.00 19.49  ? 63  HIS B CG  1 
ATOM   1575  N  ND1 . HIS B  1 64  ? 16.851  -39.399 16.414 1.00 20.47  ? 63  HIS B ND1 1 
ATOM   1576  C  CD2 . HIS B  1 64  ? 15.202  -40.300 17.527 1.00 18.93  ? 63  HIS B CD2 1 
ATOM   1577  C  CE1 . HIS B  1 64  ? 17.000  -39.049 17.677 1.00 19.91  ? 63  HIS B CE1 1 
ATOM   1578  N  NE2 . HIS B  1 64  ? 16.005  -39.599 18.380 1.00 18.82  ? 63  HIS B NE2 1 
ATOM   1579  N  N   . PHE B  1 65  ? 12.597  -41.541 13.115 1.00 21.51  ? 64  PHE B N   1 
ATOM   1580  C  CA  . PHE B  1 65  ? 12.127  -41.806 11.762 1.00 23.13  ? 64  PHE B CA  1 
ATOM   1581  C  C   . PHE B  1 65  ? 13.237  -41.510 10.750 1.00 24.26  ? 64  PHE B C   1 
ATOM   1582  O  O   . PHE B  1 65  ? 13.664  -40.366 10.612 1.00 23.88  ? 64  PHE B O   1 
ATOM   1583  C  CB  . PHE B  1 65  ? 10.846  -41.017 11.475 1.00 23.32  ? 64  PHE B CB  1 
ATOM   1584  C  CG  . PHE B  1 65  ? 10.273  -41.212 10.092 1.00 23.49  ? 64  PHE B CG  1 
ATOM   1585  C  CD1 . PHE B  1 65  ? 10.211  -42.476 9.518  1.00 23.58  ? 64  PHE B CD1 1 
ATOM   1586  C  CD2 . PHE B  1 65  ? 9.779   -40.136 9.365  1.00 23.34  ? 64  PHE B CD2 1 
ATOM   1587  C  CE1 . PHE B  1 65  ? 9.679   -42.658 8.250  1.00 23.31  ? 64  PHE B CE1 1 
ATOM   1588  C  CE2 . PHE B  1 65  ? 9.234   -40.319 8.098  1.00 23.17  ? 64  PHE B CE2 1 
ATOM   1589  C  CZ  . PHE B  1 65  ? 9.185   -41.579 7.542  1.00 23.12  ? 64  PHE B CZ  1 
ATOM   1590  N  N   . ASN B  1 66  ? 13.686  -42.542 10.026 1.00 24.13  ? 65  ASN B N   1 
ATOM   1591  C  CA  . ASN B  1 66  ? 14.917  -42.404 9.266  1.00 23.74  ? 65  ASN B CA  1 
ATOM   1592  C  C   . ASN B  1 66  ? 14.789  -43.033 7.874  1.00 23.51  ? 65  ASN B C   1 
ATOM   1593  O  O   . ASN B  1 66  ? 15.599  -43.874 7.495  1.00 23.60  ? 65  ASN B O   1 
ATOM   1594  C  CB  . ASN B  1 66  ? 16.109  -42.941 10.067 1.00 23.99  ? 65  ASN B CB  1 
ATOM   1595  C  CG  . ASN B  1 66  ? 17.438  -42.716 9.373  1.00 24.62  ? 65  ASN B CG  1 
ATOM   1596  O  OD1 . ASN B  1 66  ? 17.564  -41.857 8.507  1.00 25.38  ? 65  ASN B OD1 1 
ATOM   1597  N  ND2 . ASN B  1 66  ? 18.437  -43.490 9.741  1.00 23.46  ? 65  ASN B ND2 1 
ATOM   1598  N  N   . PRO B  1 67  ? 13.826  -42.613 7.022  1.00 22.88  ? 66  PRO B N   1 
ATOM   1599  C  CA  . PRO B  1 67  ? 13.611  -43.287 5.742  1.00 24.24  ? 66  PRO B CA  1 
ATOM   1600  C  C   . PRO B  1 67  ? 14.781  -43.217 4.760  1.00 25.74  ? 66  PRO B C   1 
ATOM   1601  O  O   . PRO B  1 67  ? 14.846  -44.018 3.833  1.00 26.41  ? 66  PRO B O   1 
ATOM   1602  C  CB  . PRO B  1 67  ? 12.396  -42.579 5.133  1.00 23.55  ? 66  PRO B CB  1 
ATOM   1603  C  CG  . PRO B  1 67  ? 12.359  -41.251 5.820  1.00 22.81  ? 66  PRO B CG  1 
ATOM   1604  C  CD  . PRO B  1 67  ? 12.941  -41.462 7.201  1.00 21.40  ? 66  PRO B CD  1 
ATOM   1605  N  N   . LEU B  1 68  ? 15.701  -42.266 4.968  1.00 27.15  ? 67  LEU B N   1 
ATOM   1606  C  CA  . LEU B  1 68  ? 16.795  -42.075 4.028  1.00 28.61  ? 67  LEU B CA  1 
ATOM   1607  C  C   . LEU B  1 68  ? 18.099  -42.694 4.529  1.00 30.63  ? 67  LEU B C   1 
ATOM   1608  O  O   . LEU B  1 68  ? 19.139  -42.511 3.897  1.00 33.44  ? 67  LEU B O   1 
ATOM   1609  C  CB  . LEU B  1 68  ? 16.960  -40.585 3.716  1.00 27.04  ? 67  LEU B CB  1 
ATOM   1610  C  CG  . LEU B  1 68  ? 15.843  -39.953 2.890  1.00 26.66  ? 67  LEU B CG  1 
ATOM   1611  C  CD1 . LEU B  1 68  ? 16.121  -38.496 2.588  1.00 25.46  ? 67  LEU B CD1 1 
ATOM   1612  C  CD2 . LEU B  1 68  ? 15.596  -40.751 1.624  1.00 25.49  ? 67  LEU B CD2 1 
ATOM   1613  N  N   . SER B  1 69  ? 18.045  -43.388 5.672  1.00 29.50  ? 68  SER B N   1 
ATOM   1614  C  CA  . SER B  1 69  ? 19.181  -44.104 6.243  1.00 28.54  ? 68  SER B CA  1 
ATOM   1615  C  C   . SER B  1 69  ? 20.390  -43.197 6.446  1.00 28.93  ? 68  SER B C   1 
ATOM   1616  O  O   . SER B  1 69  ? 21.475  -43.535 5.987  1.00 30.85  ? 68  SER B O   1 
ATOM   1617  C  CB  . SER B  1 69  ? 19.567  -45.274 5.390  1.00 26.90  ? 68  SER B CB  1 
ATOM   1618  O  OG  . SER B  1 69  ? 18.551  -46.249 5.413  1.00 28.77  ? 68  SER B OG  1 
ATOM   1619  N  N   . ARG B  1 70  ? 20.204  -42.062 7.133  1.00 28.77  ? 69  ARG B N   1 
ATOM   1620  C  CA  . ARG B  1 70  ? 21.299  -41.157 7.431  1.00 26.94  ? 69  ARG B CA  1 
ATOM   1621  C  C   . ARG B  1 70  ? 21.613  -41.223 8.926  1.00 26.83  ? 69  ARG B C   1 
ATOM   1622  O  O   . ARG B  1 70  ? 20.905  -41.879 9.688  1.00 25.03  ? 69  ARG B O   1 
ATOM   1623  C  CB  . ARG B  1 70  ? 20.961  -39.726 7.021  1.00 27.94  ? 69  ARG B CB  1 
ATOM   1624  C  CG  . ARG B  1 70  ? 20.449  -39.568 5.605  1.00 30.37  ? 69  ARG B CG  1 
ATOM   1625  C  CD  . ARG B  1 70  ? 21.457  -39.201 4.590  1.00 33.12  ? 69  ARG B CD  1 
ATOM   1626  N  NE  . ARG B  1 70  ? 20.804  -38.766 3.355  1.00 35.51  ? 69  ARG B NE  1 
ATOM   1627  C  CZ  . ARG B  1 70  ? 20.346  -37.533 3.090  1.00 34.07  ? 69  ARG B CZ  1 
ATOM   1628  N  NH1 . ARG B  1 70  ? 20.428  -36.577 3.987  1.00 32.72  ? 69  ARG B NH1 1 
ATOM   1629  N  NH2 . ARG B  1 70  ? 19.831  -37.243 1.910  1.00 31.42  ? 69  ARG B NH2 1 
ATOM   1630  N  N   . LYS B  1 71  ? 22.693  -40.540 9.327  1.00 28.73  ? 70  LYS B N   1 
ATOM   1631  C  CA  . LYS B  1 71  ? 23.079  -40.439 10.729 1.00 27.83  ? 70  LYS B CA  1 
ATOM   1632  C  C   . LYS B  1 71  ? 22.320  -39.276 11.366 1.00 26.42  ? 70  LYS B C   1 
ATOM   1633  O  O   . LYS B  1 71  ? 21.808  -38.403 10.660 1.00 26.42  ? 70  LYS B O   1 
ATOM   1634  C  CB  . LYS B  1 71  ? 24.613  -40.393 10.870 1.00 27.99  ? 70  LYS B CB  1 
ATOM   1635  C  CG  . LYS B  1 71  ? 25.363  -41.528 10.162 0.60 26.87  ? 70  LYS B CG  1 
ATOM   1636  C  CD  . LYS B  1 71  ? 26.532  -42.221 10.846 0.60 26.18  ? 70  LYS B CD  1 
ATOM   1637  C  CE  . LYS B  1 71  ? 26.494  -43.712 10.584 0.60 24.02  ? 70  LYS B CE  1 
ATOM   1638  N  NZ  . LYS B  1 71  ? 27.358  -44.451 11.531 0.60 22.89  ? 70  LYS B NZ  1 
ATOM   1639  N  N   . HIS B  1 72  ? 22.225  -39.284 12.701 1.00 25.52  ? 71  HIS B N   1 
ATOM   1640  C  CA  . HIS B  1 72  ? 21.462  -38.279 13.430 1.00 26.29  ? 71  HIS B CA  1 
ATOM   1641  C  C   . HIS B  1 72  ? 22.132  -36.910 13.321 1.00 27.24  ? 71  HIS B C   1 
ATOM   1642  O  O   . HIS B  1 72  ? 23.355  -36.807 13.381 1.00 28.54  ? 71  HIS B O   1 
ATOM   1643  C  CB  . HIS B  1 72  ? 21.301  -38.721 14.887 1.00 27.68  ? 71  HIS B CB  1 
ATOM   1644  C  CG  . HIS B  1 72  ? 20.633  -37.707 15.750 1.00 27.37  ? 71  HIS B CG  1 
ATOM   1645  N  ND1 . HIS B  1 72  ? 19.252  -37.585 15.848 1.00 27.40  ? 71  HIS B ND1 1 
ATOM   1646  C  CD2 . HIS B  1 72  ? 21.159  -36.768 16.562 1.00 28.42  ? 71  HIS B CD2 1 
ATOM   1647  C  CE1 . HIS B  1 72  ? 18.960  -36.607 16.680 1.00 29.17  ? 71  HIS B CE1 1 
ATOM   1648  N  NE2 . HIS B  1 72  ? 20.117  -36.084 17.126 1.00 30.22  ? 71  HIS B NE2 1 
ATOM   1649  N  N   . GLY B  1 73  ? 21.320  -35.861 13.151 1.00 28.34  ? 72  GLY B N   1 
ATOM   1650  C  CA  . GLY B  1 73  ? 21.819  -34.492 13.125 1.00 26.33  ? 72  GLY B CA  1 
ATOM   1651  C  C   . GLY B  1 73  ? 20.865  -33.536 13.835 1.00 26.20  ? 72  GLY B C   1 
ATOM   1652  O  O   . GLY B  1 73  ? 19.854  -33.973 14.407 1.00 26.47  ? 72  GLY B O   1 
ATOM   1653  N  N   . GLY B  1 74  ? 21.220  -32.241 13.826 1.00 24.03  ? 73  GLY B N   1 
ATOM   1654  C  CA  . GLY B  1 74  ? 20.282  -31.177 14.151 1.00 23.98  ? 73  GLY B CA  1 
ATOM   1655  C  C   . GLY B  1 74  ? 19.389  -30.874 12.950 1.00 23.89  ? 73  GLY B C   1 
ATOM   1656  O  O   . GLY B  1 74  ? 19.735  -31.229 11.826 1.00 21.98  ? 73  GLY B O   1 
ATOM   1657  N  N   . PRO B  1 75  ? 18.206  -30.241 13.139 1.00 24.53  ? 74  PRO B N   1 
ATOM   1658  C  CA  . PRO B  1 75  ? 17.279  -30.001 12.032 1.00 25.71  ? 74  PRO B CA  1 
ATOM   1659  C  C   . PRO B  1 75  ? 17.922  -29.259 10.863 1.00 26.90  ? 74  PRO B C   1 
ATOM   1660  O  O   . PRO B  1 75  ? 17.525  -29.454 9.720  1.00 28.01  ? 74  PRO B O   1 
ATOM   1661  C  CB  . PRO B  1 75  ? 16.138  -29.171 12.640 1.00 24.74  ? 74  PRO B CB  1 
ATOM   1662  C  CG  . PRO B  1 75  ? 16.673  -28.701 13.977 1.00 25.52  ? 74  PRO B CG  1 
ATOM   1663  C  CD  . PRO B  1 75  ? 17.692  -29.733 14.417 1.00 24.40  ? 74  PRO B CD  1 
ATOM   1664  N  N   . LYS B  1 76  ? 18.945  -28.445 11.158 1.00 26.23  ? 75  LYS B N   1 
ATOM   1665  C  CA  . LYS B  1 76  ? 19.530  -27.579 10.144 1.00 24.04  ? 75  LYS B CA  1 
ATOM   1666  C  C   . LYS B  1 76  ? 20.607  -28.299 9.337  1.00 24.21  ? 75  LYS B C   1 
ATOM   1667  O  O   . LYS B  1 76  ? 21.014  -27.777 8.308  1.00 24.06  ? 75  LYS B O   1 
ATOM   1668  C  CB  . LYS B  1 76  ? 19.998  -26.260 10.756 1.00 22.66  ? 75  LYS B CB  1 
ATOM   1669  C  CG  . LYS B  1 76  ? 18.877  -25.255 11.000 0.40 23.03  ? 75  LYS B CG  1 
ATOM   1670  C  CD  . LYS B  1 76  ? 19.189  -24.146 11.977 0.40 23.03  ? 75  LYS B CD  1 
ATOM   1671  C  CE  . LYS B  1 76  ? 18.215  -22.992 11.833 0.40 23.21  ? 75  LYS B CE  1 
ATOM   1672  N  NZ  . LYS B  1 76  ? 18.168  -22.151 13.048 0.40 22.08  ? 75  LYS B NZ  1 
ATOM   1673  N  N   . ASP B  1 77  ? 21.023  -29.499 9.768  1.00 26.43  ? 76  ASP B N   1 
ATOM   1674  C  CA  . ASP B  1 77  ? 22.089  -30.262 9.129  1.00 29.65  ? 76  ASP B CA  1 
ATOM   1675  C  C   . ASP B  1 77  ? 21.569  -30.927 7.861  1.00 32.84  ? 76  ASP B C   1 
ATOM   1676  O  O   . ASP B  1 77  ? 20.395  -31.263 7.760  1.00 35.60  ? 76  ASP B O   1 
ATOM   1677  C  CB  . ASP B  1 77  ? 22.678  -31.306 10.086 1.00 30.30  ? 76  ASP B CB  1 
ATOM   1678  C  CG  . ASP B  1 77  ? 23.485  -30.679 11.205 1.00 32.83  ? 76  ASP B CG  1 
ATOM   1679  O  OD1 . ASP B  1 77  ? 24.092  -29.636 10.940 1.00 37.04  ? 76  ASP B OD1 1 
ATOM   1680  O  OD2 . ASP B  1 77  ? 23.493  -31.228 12.339 1.00 36.25  ? 76  ASP B OD2 1 
ATOM   1681  N  N   . GLU B  1 78  ? 22.455  -31.124 6.875  1.00 37.45  ? 77  GLU B N   1 
ATOM   1682  C  CA  . GLU B  1 78  ? 22.077  -31.904 5.714  1.00 40.13  ? 77  GLU B CA  1 
ATOM   1683  C  C   . GLU B  1 78  ? 22.034  -33.381 6.114  1.00 40.82  ? 77  GLU B C   1 
ATOM   1684  O  O   . GLU B  1 78  ? 21.176  -34.107 5.658  1.00 38.35  ? 77  GLU B O   1 
ATOM   1685  C  CB  . GLU B  1 78  ? 23.032  -31.561 4.564  1.00 45.74  ? 77  GLU B CB  1 
ATOM   1686  C  CG  . GLU B  1 78  ? 22.895  -32.309 3.266  1.00 56.02  ? 77  GLU B CG  1 
ATOM   1687  C  CD  . GLU B  1 78  ? 21.533  -32.463 2.618  1.00 69.24  ? 77  GLU B CD  1 
ATOM   1688  O  OE1 . GLU B  1 78  ? 20.663  -31.584 2.770  1.00 78.42  ? 77  GLU B OE1 1 
ATOM   1689  O  OE2 . GLU B  1 78  ? 21.358  -33.465 1.952  1.00 74.01  ? 77  GLU B OE2 1 
ATOM   1690  N  N   . GLU B  1 79  ? 22.983  -33.798 6.962  1.00 38.64  ? 78  GLU B N   1 
ATOM   1691  C  CA  . GLU B  1 79  ? 23.031  -35.150 7.489  1.00 32.01  ? 78  GLU B CA  1 
ATOM   1692  C  C   . GLU B  1 79  ? 22.160  -35.213 8.748  1.00 31.36  ? 78  GLU B C   1 
ATOM   1693  O  O   . GLU B  1 79  ? 22.601  -34.886 9.858  1.00 30.83  ? 78  GLU B O   1 
ATOM   1694  C  CB  . GLU B  1 79  ? 24.496  -35.578 7.659  1.00 29.14  ? 78  GLU B CB  1 
ATOM   1695  C  CG  . GLU B  1 79  ? 24.725  -37.034 8.044  1.00 30.89  ? 78  GLU B CG  1 
ATOM   1696  C  CD  . GLU B  1 79  ? 24.438  -38.118 7.011  1.00 33.37  ? 78  GLU B CD  1 
ATOM   1697  O  OE1 . GLU B  1 79  ? 24.136  -37.774 5.828  1.00 35.74  ? 78  GLU B OE1 1 
ATOM   1698  O  OE2 . GLU B  1 79  ? 24.490  -39.321 7.386  1.00 31.67  ? 78  GLU B OE2 1 
ATOM   1699  N  N   . ARG B  1 80  ? 20.898  -35.625 8.555  1.00 30.88  ? 79  ARG B N   1 
ATOM   1700  C  CA  . ARG B  1 80  ? 19.952  -35.798 9.650  1.00 29.50  ? 79  ARG B CA  1 
ATOM   1701  C  C   . ARG B  1 80  ? 18.939  -36.892 9.320  1.00 27.91  ? 79  ARG B C   1 
ATOM   1702  O  O   . ARG B  1 80  ? 18.724  -37.241 8.164  1.00 27.78  ? 79  ARG B O   1 
ATOM   1703  C  CB  . ARG B  1 80  ? 19.175  -34.505 9.912  1.00 29.05  ? 79  ARG B CB  1 
ATOM   1704  C  CG  . ARG B  1 80  ? 18.414  -33.976 8.700  1.00 26.54  ? 79  ARG B CG  1 
ATOM   1705  C  CD  . ARG B  1 80  ? 17.530  -32.814 9.095  1.00 28.31  ? 79  ARG B CD  1 
ATOM   1706  N  NE  . ARG B  1 80  ? 16.195  -33.246 9.498  1.00 28.82  ? 79  ARG B NE  1 
ATOM   1707  C  CZ  . ARG B  1 80  ? 15.143  -32.444 9.657  1.00 30.25  ? 79  ARG B CZ  1 
ATOM   1708  N  NH1 . ARG B  1 80  ? 15.252  -31.142 9.449  1.00 28.62  ? 79  ARG B NH1 1 
ATOM   1709  N  NH2 . ARG B  1 80  ? 13.979  -32.945 10.028 1.00 29.81  ? 79  ARG B NH2 1 
ATOM   1710  N  N   . HIS B  1 81  ? 18.316  -37.422 10.374 1.00 25.55  ? 80  HIS B N   1 
ATOM   1711  C  CA  . HIS B  1 81  ? 17.096  -38.204 10.266 1.00 23.47  ? 80  HIS B CA  1 
ATOM   1712  C  C   . HIS B  1 81  ? 15.953  -37.271 9.888  1.00 22.32  ? 80  HIS B C   1 
ATOM   1713  O  O   . HIS B  1 81  ? 15.925  -36.123 10.332 1.00 21.81  ? 80  HIS B O   1 
ATOM   1714  C  CB  . HIS B  1 81  ? 16.785  -38.852 11.610 1.00 23.60  ? 80  HIS B CB  1 
ATOM   1715  C  CG  . HIS B  1 81  ? 17.862  -39.761 12.103 1.00 22.95  ? 80  HIS B CG  1 
ATOM   1716  N  ND1 . HIS B  1 81  ? 18.170  -39.895 13.450 1.00 22.28  ? 80  HIS B ND1 1 
ATOM   1717  C  CD2 . HIS B  1 81  ? 18.685  -40.593 11.435 1.00 21.78  ? 80  HIS B CD2 1 
ATOM   1718  C  CE1 . HIS B  1 81  ? 19.127  -40.781 13.590 1.00 21.77  ? 80  HIS B CE1 1 
ATOM   1719  N  NE2 . HIS B  1 81  ? 19.470  -41.214 12.365 1.00 22.79  ? 80  HIS B NE2 1 
ATOM   1720  N  N   . VAL B  1 82  ? 15.007  -37.765 9.084  1.00 21.00  ? 81  VAL B N   1 
ATOM   1721  C  CA  . VAL B  1 82  ? 13.822  -36.983 8.775  1.00 20.38  ? 81  VAL B CA  1 
ATOM   1722  C  C   . VAL B  1 82  ? 13.157  -36.534 10.077 1.00 21.26  ? 81  VAL B C   1 
ATOM   1723  O  O   . VAL B  1 82  ? 12.692  -35.404 10.174 1.00 23.59  ? 81  VAL B O   1 
ATOM   1724  C  CB  . VAL B  1 82  ? 12.840  -37.730 7.851  1.00 19.28  ? 81  VAL B CB  1 
ATOM   1725  C  CG1 . VAL B  1 82  ? 11.461  -37.076 7.826  1.00 17.20  ? 81  VAL B CG1 1 
ATOM   1726  C  CG2 . VAL B  1 82  ? 13.407  -37.843 6.435  1.00 18.18  ? 81  VAL B CG2 1 
ATOM   1727  N  N   . GLY B  1 83  ? 13.152  -37.390 11.098 1.00 20.87  ? 82  GLY B N   1 
ATOM   1728  C  CA  . GLY B  1 83  ? 12.444  -37.080 12.328 1.00 21.32  ? 82  GLY B CA  1 
ATOM   1729  C  C   . GLY B  1 83  ? 13.210  -36.157 13.273 1.00 23.15  ? 82  GLY B C   1 
ATOM   1730  O  O   . GLY B  1 83  ? 12.721  -35.888 14.371 1.00 24.34  ? 82  GLY B O   1 
ATOM   1731  N  N   . ASP B  1 84  ? 14.383  -35.669 12.838 1.00 24.84  ? 83  ASP B N   1 
ATOM   1732  C  CA  . ASP B  1 84  ? 15.286  -34.902 13.689 1.00 26.02  ? 83  ASP B CA  1 
ATOM   1733  C  C   . ASP B  1 84  ? 14.838  -33.440 13.778 1.00 26.67  ? 83  ASP B C   1 
ATOM   1734  O  O   . ASP B  1 84  ? 15.164  -32.630 12.910 1.00 28.46  ? 83  ASP B O   1 
ATOM   1735  C  CB  . ASP B  1 84  ? 16.741  -35.040 13.224 1.00 24.90  ? 83  ASP B CB  1 
ATOM   1736  C  CG  . ASP B  1 84  ? 17.382  -36.380 13.576 1.00 25.38  ? 83  ASP B CG  1 
ATOM   1737  O  OD1 . ASP B  1 84  ? 16.838  -37.094 14.441 1.00 24.78  ? 83  ASP B OD1 1 
ATOM   1738  O  OD2 . ASP B  1 84  ? 18.438  -36.696 12.987 1.00 25.06  ? 83  ASP B OD2 1 
ATOM   1739  N  N   . LEU B  1 85  ? 14.106  -33.098 14.845 1.00 26.58  ? 84  LEU B N   1 
ATOM   1740  C  CA  . LEU B  1 85  ? 13.548  -31.757 14.964 1.00 28.29  ? 84  LEU B CA  1 
ATOM   1741  C  C   . LEU B  1 85  ? 14.309  -30.942 16.015 1.00 28.96  ? 84  LEU B C   1 
ATOM   1742  O  O   . LEU B  1 85  ? 13.863  -29.858 16.388 1.00 31.00  ? 84  LEU B O   1 
ATOM   1743  C  CB  . LEU B  1 85  ? 12.057  -31.841 15.320 1.00 26.48  ? 84  LEU B CB  1 
ATOM   1744  C  CG  . LEU B  1 85  ? 11.124  -32.327 14.214 1.00 25.53  ? 84  LEU B CG  1 
ATOM   1745  C  CD1 . LEU B  1 85  ? 9.686   -32.329 14.707 1.00 23.69  ? 84  LEU B CD1 1 
ATOM   1746  C  CD2 . LEU B  1 85  ? 11.306  -31.542 12.918 1.00 25.39  ? 84  LEU B CD2 1 
ATOM   1747  N  N   . GLY B  1 86  ? 15.450  -31.454 16.494 1.00 27.09  ? 85  GLY B N   1 
ATOM   1748  C  CA  . GLY B  1 86  ? 16.285  -30.682 17.405 1.00 24.31  ? 85  GLY B CA  1 
ATOM   1749  C  C   . GLY B  1 86  ? 15.730  -30.634 18.832 1.00 23.75  ? 85  GLY B C   1 
ATOM   1750  O  O   . GLY B  1 86  ? 15.281  -31.656 19.346 1.00 22.29  ? 85  GLY B O   1 
ATOM   1751  N  N   . ASN B  1 87  ? 15.788  -29.454 19.464 1.00 23.71  ? 86  ASN B N   1 
ATOM   1752  C  CA  . ASN B  1 87  ? 15.403  -29.302 20.858 1.00 23.44  ? 86  ASN B CA  1 
ATOM   1753  C  C   . ASN B  1 87  ? 14.221  -28.351 21.014 1.00 23.86  ? 86  ASN B C   1 
ATOM   1754  O  O   . ASN B  1 87  ? 13.942  -27.513 20.154 1.00 21.49  ? 86  ASN B O   1 
ATOM   1755  C  CB  . ASN B  1 87  ? 16.541  -28.774 21.738 1.00 24.19  ? 86  ASN B CB  1 
ATOM   1756  C  CG  . ASN B  1 87  ? 17.671  -29.768 21.857 1.00 24.58  ? 86  ASN B CG  1 
ATOM   1757  O  OD1 . ASN B  1 87  ? 17.559  -30.755 22.573 1.00 25.12  ? 86  ASN B OD1 1 
ATOM   1758  N  ND2 . ASN B  1 87  ? 18.745  -29.534 21.123 1.00 24.71  ? 86  ASN B ND2 1 
ATOM   1759  N  N   . VAL B  1 88  ? 13.527  -28.511 22.141 1.00 25.51  ? 87  VAL B N   1 
ATOM   1760  C  CA  . VAL B  1 88  ? 12.567  -27.534 22.611 1.00 27.29  ? 87  VAL B CA  1 
ATOM   1761  C  C   . VAL B  1 88  ? 13.060  -27.057 23.975 1.00 29.21  ? 87  VAL B C   1 
ATOM   1762  O  O   . VAL B  1 88  ? 13.841  -27.758 24.620 1.00 29.29  ? 87  VAL B O   1 
ATOM   1763  C  CB  . VAL B  1 88  ? 11.131  -28.114 22.648 1.00 26.93  ? 87  VAL B CB  1 
ATOM   1764  C  CG1 . VAL B  1 88  ? 10.671  -28.605 21.284 1.00 25.41  ? 87  VAL B CG1 1 
ATOM   1765  C  CG2 . VAL B  1 88  ? 10.959  -29.210 23.688 1.00 25.73  ? 87  VAL B CG2 1 
ATOM   1766  N  N   . THR B  1 89  ? 12.633  -25.860 24.394 1.00 31.73  ? 88  THR B N   1 
ATOM   1767  C  CA  . THR B  1 89  ? 13.159  -25.287 25.619 1.00 33.39  ? 88  THR B CA  1 
ATOM   1768  C  C   . THR B  1 89  ? 12.043  -25.112 26.641 1.00 32.80  ? 88  THR B C   1 
ATOM   1769  O  O   . THR B  1 89  ? 11.054  -24.446 26.371 1.00 33.82  ? 88  THR B O   1 
ATOM   1770  C  CB  . THR B  1 89  ? 13.818  -23.927 25.359 1.00 36.80  ? 88  THR B CB  1 
ATOM   1771  O  OG1 . THR B  1 89  ? 14.788  -24.044 24.310 1.00 34.40  ? 88  THR B OG1 1 
ATOM   1772  C  CG2 . THR B  1 89  ? 14.448  -23.352 26.610 1.00 36.92  ? 88  THR B CG2 1 
ATOM   1773  N  N   . ALA B  1 90  ? 12.237  -25.681 27.828 1.00 34.49  ? 89  ALA B N   1 
ATOM   1774  C  CA  . ALA B  1 90  ? 11.306  -25.472 28.929 1.00 37.36  ? 89  ALA B CA  1 
ATOM   1775  C  C   . ALA B  1 90  ? 11.789  -24.330 29.823 1.00 40.70  ? 89  ALA B C   1 
ATOM   1776  O  O   . ALA B  1 90  ? 12.963  -24.286 30.200 1.00 43.45  ? 89  ALA B O   1 
ATOM   1777  C  CB  . ALA B  1 90  ? 11.147  -26.750 29.710 1.00 35.77  ? 89  ALA B CB  1 
ATOM   1778  N  N   . ASP B  1 91  ? 10.855  -23.430 30.174 1.00 40.90  ? 90  ASP B N   1 
ATOM   1779  C  CA  . ASP B  1 91  ? 11.102  -22.291 31.049 1.00 40.50  ? 90  ASP B CA  1 
ATOM   1780  C  C   . ASP B  1 91  ? 11.167  -22.758 32.503 1.00 39.79  ? 90  ASP B C   1 
ATOM   1781  O  O   . ASP B  1 91  ? 11.032  -23.947 32.774 1.00 38.41  ? 90  ASP B O   1 
ATOM   1782  C  CB  . ASP B  1 91  ? 10.059  -21.187 30.832 1.00 41.89  ? 90  ASP B CB  1 
ATOM   1783  C  CG  . ASP B  1 91  ? 8.622   -21.554 31.205 1.00 42.90  ? 90  ASP B CG  1 
ATOM   1784  O  OD1 . ASP B  1 91  ? 8.414   -22.492 32.012 1.00 42.26  ? 90  ASP B OD1 1 
ATOM   1785  O  OD2 . ASP B  1 91  ? 7.710   -20.890 30.695 1.00 42.75  ? 90  ASP B OD2 1 
ATOM   1786  N  N   . LYS B  1 92  ? 11.361  -21.809 33.431 1.00 41.09  ? 91  LYS B N   1 
ATOM   1787  C  CA  . LYS B  1 92  ? 11.563  -22.124 34.841 1.00 44.08  ? 91  LYS B CA  1 
ATOM   1788  C  C   . LYS B  1 92  ? 10.345  -22.846 35.422 1.00 45.45  ? 91  LYS B C   1 
ATOM   1789  O  O   . LYS B  1 92  ? 10.454  -23.461 36.475 1.00 46.70  ? 91  LYS B O   1 
ATOM   1790  C  CB  . LYS B  1 92  ? 11.922  -20.883 35.675 1.00 42.38  ? 91  LYS B CB  1 
ATOM   1791  C  CG  . LYS B  1 92  ? 10.831  -19.820 35.819 0.50 38.88  ? 91  LYS B CG  1 
ATOM   1792  C  CD  . LYS B  1 92  ? 10.907  -18.950 37.041 0.50 35.66  ? 91  LYS B CD  1 
ATOM   1793  C  CE  . LYS B  1 92  ? 9.533   -18.415 37.359 0.50 32.79  ? 91  LYS B CE  1 
ATOM   1794  N  NZ  . LYS B  1 92  ? 9.623   -17.176 38.151 0.50 32.04  ? 91  LYS B NZ  1 
ATOM   1795  N  N   . ASP B  1 93  ? 9.195   -22.761 34.739 1.00 46.21  ? 92  ASP B N   1 
ATOM   1796  C  CA  . ASP B  1 93  ? 7.952   -23.351 35.217 1.00 43.56  ? 92  ASP B CA  1 
ATOM   1797  C  C   . ASP B  1 93  ? 7.737   -24.734 34.616 1.00 41.06  ? 92  ASP B C   1 
ATOM   1798  O  O   . ASP B  1 93  ? 6.742   -25.389 34.907 1.00 37.73  ? 92  ASP B O   1 
ATOM   1799  C  CB  . ASP B  1 93  ? 6.746   -22.483 34.859 1.00 48.21  ? 92  ASP B CB  1 
ATOM   1800  C  CG  . ASP B  1 93  ? 6.758   -21.148 35.570 1.00 55.15  ? 92  ASP B CG  1 
ATOM   1801  O  OD1 . ASP B  1 93  ? 7.065   -21.142 36.789 1.00 57.47  ? 92  ASP B OD1 1 
ATOM   1802  O  OD2 . ASP B  1 93  ? 6.445   -20.127 34.915 1.00 58.64  ? 92  ASP B OD2 1 
ATOM   1803  N  N   . GLY B  1 94  ? 8.660   -25.163 33.755 1.00 43.21  ? 93  GLY B N   1 
ATOM   1804  C  CA  . GLY B  1 94  ? 8.562   -26.479 33.151 1.00 41.46  ? 93  GLY B CA  1 
ATOM   1805  C  C   . GLY B  1 94  ? 7.645   -26.485 31.935 1.00 37.71  ? 93  GLY B C   1 
ATOM   1806  O  O   . GLY B  1 94  ? 7.138   -27.536 31.556 1.00 34.32  ? 93  GLY B O   1 
ATOM   1807  N  N   . VAL B  1 95  ? 7.449   -25.310 31.330 1.00 34.67  ? 94  VAL B N   1 
ATOM   1808  C  CA  . VAL B  1 95  ? 6.612   -25.211 30.150 1.00 35.61  ? 94  VAL B CA  1 
ATOM   1809  C  C   . VAL B  1 95  ? 7.476   -24.892 28.935 1.00 35.05  ? 94  VAL B C   1 
ATOM   1810  O  O   . VAL B  1 95  ? 8.248   -23.937 28.946 1.00 36.76  ? 94  VAL B O   1 
ATOM   1811  C  CB  . VAL B  1 95  ? 5.484   -24.176 30.331 1.00 35.22  ? 94  VAL B CB  1 
ATOM   1812  C  CG1 . VAL B  1 95  ? 4.670   -23.992 29.050 1.00 33.47  ? 94  VAL B CG1 1 
ATOM   1813  C  CG2 . VAL B  1 95  ? 4.596   -24.529 31.515 1.00 31.78  ? 94  VAL B CG2 1 
ATOM   1814  N  N   . ALA B  1 96  ? 7.317   -25.691 27.874 1.00 31.61  ? 95  ALA B N   1 
ATOM   1815  C  CA  . ALA B  1 96  ? 7.973   -25.387 26.614 1.00 30.10  ? 95  ALA B CA  1 
ATOM   1816  C  C   . ALA B  1 96  ? 6.916   -24.877 25.637 1.00 31.40  ? 95  ALA B C   1 
ATOM   1817  O  O   . ALA B  1 96  ? 5.981   -25.612 25.296 1.00 31.50  ? 95  ALA B O   1 
ATOM   1818  C  CB  . ALA B  1 96  ? 8.639   -26.623 26.081 1.00 28.40  ? 95  ALA B CB  1 
ATOM   1819  N  N   . ASP B  1 97  ? 7.066   -23.622 25.188 1.00 31.57  ? 96  ASP B N   1 
ATOM   1820  C  CA  . ASP B  1 97  ? 6.194   -23.132 24.131 1.00 32.71  ? 96  ASP B CA  1 
ATOM   1821  C  C   . ASP B  1 97  ? 6.845   -23.467 22.802 1.00 31.43  ? 96  ASP B C   1 
ATOM   1822  O  O   . ASP B  1 97  ? 7.687   -22.714 22.321 1.00 33.57  ? 96  ASP B O   1 
ATOM   1823  C  CB  . ASP B  1 97  ? 5.813   -21.654 24.269 1.00 35.37  ? 96  ASP B CB  1 
ATOM   1824  C  CG  . ASP B  1 97  ? 4.963   -21.383 25.497 1.00 41.52  ? 96  ASP B CG  1 
ATOM   1825  O  OD1 . ASP B  1 97  ? 3.937   -22.079 25.680 1.00 42.34  ? 96  ASP B OD1 1 
ATOM   1826  O  OD2 . ASP B  1 97  ? 5.347   -20.495 26.282 1.00 49.22  ? 96  ASP B OD2 1 
ATOM   1827  N  N   . VAL B  1 98  ? 6.436   -24.599 22.229 1.00 28.65  ? 97  VAL B N   1 
ATOM   1828  C  CA  . VAL B  1 98  ? 7.084   -25.114 21.043 1.00 29.34  ? 97  VAL B CA  1 
ATOM   1829  C  C   . VAL B  1 98  ? 6.647   -24.307 19.829 1.00 29.36  ? 97  VAL B C   1 
ATOM   1830  O  O   . VAL B  1 98  ? 5.464   -24.015 19.650 1.00 30.65  ? 97  VAL B O   1 
ATOM   1831  C  CB  . VAL B  1 98  ? 6.755   -26.604 20.848 1.00 30.01  ? 97  VAL B CB  1 
ATOM   1832  C  CG1 . VAL B  1 98  ? 7.447   -27.163 19.623 1.00 27.73  ? 97  VAL B CG1 1 
ATOM   1833  C  CG2 . VAL B  1 98  ? 7.112   -27.408 22.083 1.00 31.14  ? 97  VAL B CG2 1 
ATOM   1834  N  N   . SER B  1 99  ? 7.629   -23.976 18.990 1.00 29.09  ? 98  SER B N   1 
ATOM   1835  C  CA  . SER B  1 99  ? 7.347   -23.355 17.710 1.00 29.57  ? 98  SER B CA  1 
ATOM   1836  C  C   . SER B  1 99  ? 8.533   -23.599 16.785 1.00 29.51  ? 98  SER B C   1 
ATOM   1837  O  O   . SER B  1 99  ? 9.625   -23.070 17.008 1.00 32.24  ? 98  SER B O   1 
ATOM   1838  C  CB  . SER B  1 99  ? 7.083   -21.891 17.891 1.00 29.46  ? 98  SER B CB  1 
ATOM   1839  O  OG  . SER B  1 99  ? 6.918   -21.266 16.639 1.00 30.48  ? 98  SER B OG  1 
ATOM   1840  N  N   . ILE B  1 100 ? 8.309   -24.431 15.768 1.00 28.67  ? 99  ILE B N   1 
ATOM   1841  C  CA  . ILE B  1 100 ? 9.375   -24.881 14.888 1.00 29.51  ? 99  ILE B CA  1 
ATOM   1842  C  C   . ILE B  1 100 ? 8.842   -24.851 13.469 1.00 29.52  ? 99  ILE B C   1 
ATOM   1843  O  O   . ILE B  1 100 ? 7.657   -25.051 13.248 1.00 33.72  ? 99  ILE B O   1 
ATOM   1844  C  CB  . ILE B  1 100 ? 9.832   -26.309 15.271 1.00 29.04  ? 99  ILE B CB  1 
ATOM   1845  C  CG1 . ILE B  1 100 ? 10.715  -26.293 16.517 1.00 28.40  ? 99  ILE B CG1 1 
ATOM   1846  C  CG2 . ILE B  1 100 ? 10.534  -27.011 14.110 1.00 27.99  ? 99  ILE B CG2 1 
ATOM   1847  C  CD1 . ILE B  1 100 ? 10.937  -27.646 17.101 1.00 30.64  ? 99  ILE B CD1 1 
ATOM   1848  N  N   . GLU B  1 101 ? 9.736   -24.639 12.515 1.00 28.75  ? 100 GLU B N   1 
ATOM   1849  C  CA  . GLU B  1 101 ? 9.364   -24.796 11.128 1.00 30.22  ? 100 GLU B CA  1 
ATOM   1850  C  C   . GLU B  1 101 ? 10.375  -25.736 10.492 1.00 28.51  ? 100 GLU B C   1 
ATOM   1851  O  O   . GLU B  1 101 ? 11.567  -25.583 10.696 1.00 27.89  ? 100 GLU B O   1 
ATOM   1852  C  CB  . GLU B  1 101 ? 9.272   -23.416 10.486 1.00 34.68  ? 100 GLU B CB  1 
ATOM   1853  C  CG  . GLU B  1 101 ? 9.141   -23.459 8.985  1.00 42.39  ? 100 GLU B CG  1 
ATOM   1854  C  CD  . GLU B  1 101 ? 8.747   -22.137 8.375  1.00 47.57  ? 100 GLU B CD  1 
ATOM   1855  O  OE1 . GLU B  1 101 ? 9.333   -21.780 7.325  1.00 48.79  ? 100 GLU B OE1 1 
ATOM   1856  O  OE2 . GLU B  1 101 ? 7.836   -21.490 8.937  1.00 54.77  ? 100 GLU B OE2 1 
ATOM   1857  N  N   . ASP B  1 102 ? 9.891   -26.740 9.766  1.00 29.41  ? 101 ASP B N   1 
ATOM   1858  C  CA  . ASP B  1 102 ? 10.799  -27.720 9.205  1.00 30.12  ? 101 ASP B CA  1 
ATOM   1859  C  C   . ASP B  1 102 ? 10.373  -28.029 7.781  1.00 30.12  ? 101 ASP B C   1 
ATOM   1860  O  O   . ASP B  1 102 ? 9.179   -28.077 7.495  1.00 31.51  ? 101 ASP B O   1 
ATOM   1861  C  CB  . ASP B  1 102 ? 10.824  -28.996 10.049 1.00 29.25  ? 101 ASP B CB  1 
ATOM   1862  C  CG  . ASP B  1 102 ? 11.992  -29.883 9.677  1.00 29.93  ? 101 ASP B CG  1 
ATOM   1863  O  OD1 . ASP B  1 102 ? 13.141  -29.459 9.975  1.00 32.34  ? 101 ASP B OD1 1 
ATOM   1864  O  OD2 . ASP B  1 102 ? 11.752  -30.954 9.068  1.00 26.27  ? 101 ASP B OD2 1 
ATOM   1865  N  N   . SER B  1 103 ? 11.350  -28.266 6.905  1.00 30.23  ? 102 SER B N   1 
ATOM   1866  C  CA  . SER B  1 103 ? 11.045  -28.512 5.502  1.00 28.00  ? 102 SER B CA  1 
ATOM   1867  C  C   . SER B  1 103 ? 11.392  -29.937 5.090  1.00 25.47  ? 102 SER B C   1 
ATOM   1868  O  O   . SER B  1 103 ? 11.314  -30.280 3.913  1.00 22.74  ? 102 SER B O   1 
ATOM   1869  C  CB  . SER B  1 103 ? 11.734  -27.517 4.628  1.00 30.70  ? 102 SER B CB  1 
ATOM   1870  O  OG  . SER B  1 103 ? 10.924  -26.374 4.504  1.00 35.00  ? 102 SER B OG  1 
ATOM   1871  N  N   . VAL B  1 104 ? 11.762  -30.769 6.064  1.00 24.52  ? 103 VAL B N   1 
ATOM   1872  C  CA  . VAL B  1 104 ? 12.179  -32.130 5.764  1.00 21.75  ? 103 VAL B CA  1 
ATOM   1873  C  C   . VAL B  1 104 ? 11.023  -33.071 6.081  1.00 20.83  ? 103 VAL B C   1 
ATOM   1874  O  O   . VAL B  1 104 ? 10.715  -33.951 5.284  1.00 20.95  ? 103 VAL B O   1 
ATOM   1875  C  CB  . VAL B  1 104 ? 13.488  -32.509 6.499  1.00 20.76  ? 103 VAL B CB  1 
ATOM   1876  C  CG1 . VAL B  1 104 ? 13.820  -33.976 6.353  1.00 19.07  ? 103 VAL B CG1 1 
ATOM   1877  C  CG2 . VAL B  1 104 ? 14.646  -31.648 6.027  1.00 19.46  ? 103 VAL B CG2 1 
ATOM   1878  N  N   . ILE B  1 105 ? 10.396  -32.887 7.249  1.00 20.06  ? 104 ILE B N   1 
ATOM   1879  C  CA  . ILE B  1 105 ? 9.170   -33.612 7.529  1.00 20.64  ? 104 ILE B CA  1 
ATOM   1880  C  C   . ILE B  1 105 ? 8.100   -33.118 6.556  1.00 23.08  ? 104 ILE B C   1 
ATOM   1881  O  O   . ILE B  1 105 ? 8.216   -32.033 5.995  1.00 24.19  ? 104 ILE B O   1 
ATOM   1882  C  CB  . ILE B  1 105 ? 8.733   -33.437 8.994  1.00 19.17  ? 104 ILE B CB  1 
ATOM   1883  C  CG1 . ILE B  1 105 ? 8.369   -31.985 9.318  1.00 19.35  ? 104 ILE B CG1 1 
ATOM   1884  C  CG2 . ILE B  1 105 ? 9.787   -33.998 9.940  1.00 18.43  ? 104 ILE B CG2 1 
ATOM   1885  C  CD1 . ILE B  1 105 ? 7.656   -31.812 10.629 1.00 19.18  ? 104 ILE B CD1 1 
ATOM   1886  N  N   . SER B  1 106 ? 7.064   -33.924 6.344  1.00 25.03  ? 105 SER B N   1 
ATOM   1887  C  CA  . SER B  1 106 ? 5.940   -33.537 5.502  1.00 26.43  ? 105 SER B CA  1 
ATOM   1888  C  C   . SER B  1 106 ? 4.646   -34.131 6.053  1.00 25.38  ? 105 SER B C   1 
ATOM   1889  O  O   . SER B  1 106 ? 4.672   -35.119 6.801  1.00 26.27  ? 105 SER B O   1 
ATOM   1890  C  CB  . SER B  1 106 ? 6.145   -33.961 4.090  1.00 28.88  ? 105 SER B CB  1 
ATOM   1891  O  OG  . SER B  1 106 ? 5.221   -33.258 3.269  1.00 34.78  ? 105 SER B OG  1 
ATOM   1892  N  N   . LEU B  1 107 ? 3.520   -33.501 5.678  1.00 25.55  ? 106 LEU B N   1 
ATOM   1893  C  CA  . LEU B  1 107 ? 2.224   -34.071 5.993  1.00 26.83  ? 106 LEU B CA  1 
ATOM   1894  C  C   . LEU B  1 107 ? 1.579   -34.685 4.752  1.00 28.76  ? 106 LEU B C   1 
ATOM   1895  O  O   . LEU B  1 107 ? 0.411   -35.067 4.804  1.00 29.30  ? 106 LEU B O   1 
ATOM   1896  C  CB  . LEU B  1 107 ? 1.329   -32.997 6.622  1.00 24.79  ? 106 LEU B CB  1 
ATOM   1897  C  CG  . LEU B  1 107 ? 1.896   -32.304 7.854  1.00 24.01  ? 106 LEU B CG  1 
ATOM   1898  C  CD1 . LEU B  1 107 ? 0.833   -31.388 8.412  1.00 24.46  ? 106 LEU B CD1 1 
ATOM   1899  C  CD2 . LEU B  1 107 ? 2.336   -33.334 8.893  1.00 23.10  ? 106 LEU B CD2 1 
ATOM   1900  N  N   . SER B  1 108 ? 2.347   -34.806 3.660  1.00 32.51  ? 107 SER B N   1 
ATOM   1901  C  CA  . SER B  1 108 ? 1.928   -35.569 2.495  1.00 35.58  ? 107 SER B CA  1 
ATOM   1902  C  C   . SER B  1 108 ? 3.148   -35.941 1.658  1.00 36.62  ? 107 SER B C   1 
ATOM   1903  O  O   . SER B  1 108 ? 4.210   -35.324 1.778  1.00 40.26  ? 107 SER B O   1 
ATOM   1904  C  CB  . SER B  1 108 ? 0.918   -34.799 1.660  1.00 38.14  ? 107 SER B CB  1 
ATOM   1905  O  OG  . SER B  1 108 ? 1.492   -33.592 1.154  1.00 43.41  ? 107 SER B OG  1 
ATOM   1906  N  N   . GLY B  1 109 ? 3.022   -37.006 0.857  1.00 35.47  ? 108 GLY B N   1 
ATOM   1907  C  CA  . GLY B  1 109 ? 4.125   -37.480 0.031  1.00 35.93  ? 108 GLY B CA  1 
ATOM   1908  C  C   . GLY B  1 109 ? 5.115   -38.336 0.826  1.00 37.55  ? 108 GLY B C   1 
ATOM   1909  O  O   . GLY B  1 109 ? 4.716   -38.924 1.820  1.00 39.50  ? 108 GLY B O   1 
ATOM   1910  N  N   . ASP B  1 110 ? 6.384   -38.321 0.408  1.00 38.78  ? 109 ASP B N   1 
ATOM   1911  C  CA  . ASP B  1 110 ? 7.310   -39.382 0.748  1.00 44.78  ? 109 ASP B CA  1 
ATOM   1912  C  C   . ASP B  1 110 ? 7.649   -39.383 2.235  1.00 46.93  ? 109 ASP B C   1 
ATOM   1913  O  O   . ASP B  1 110 ? 7.970   -40.440 2.801  1.00 54.51  ? 109 ASP B O   1 
ATOM   1914  C  CB  . ASP B  1 110 ? 8.583   -39.331 -0.096 1.00 47.92  ? 109 ASP B CB  1 
ATOM   1915  C  CG  . ASP B  1 110 ? 8.307   -39.441 -1.595 1.00 46.71  ? 109 ASP B CG  1 
ATOM   1916  O  OD1 . ASP B  1 110 ? 7.433   -40.253 -2.004 1.00 50.17  ? 109 ASP B OD1 1 
ATOM   1917  O  OD2 . ASP B  1 110 ? 8.960   -38.721 -2.354 1.00 48.31  ? 109 ASP B OD2 1 
ATOM   1918  N  N   . HIS B  1 111 ? 7.623   -38.207 2.869  1.00 39.56  ? 110 HIS B N   1 
ATOM   1919  C  CA  . HIS B  1 111 ? 8.116   -38.184 4.236  1.00 39.45  ? 110 HIS B CA  1 
ATOM   1920  C  C   . HIS B  1 111 ? 6.964   -37.908 5.194  1.00 36.66  ? 110 HIS B C   1 
ATOM   1921  O  O   . HIS B  1 111 ? 7.124   -37.201 6.195  1.00 40.05  ? 110 HIS B O   1 
ATOM   1922  C  CB  . HIS B  1 111 ? 9.305   -37.221 4.372  1.00 47.75  ? 110 HIS B CB  1 
ATOM   1923  C  CG  . HIS B  1 111 ? 10.469  -37.540 3.489  1.00 51.36  ? 110 HIS B CG  1 
ATOM   1924  N  ND1 . HIS B  1 111 ? 11.336  -36.552 3.029  1.00 52.07  ? 110 HIS B ND1 1 
ATOM   1925  C  CD2 . HIS B  1 111 ? 10.907  -38.716 2.963  1.00 45.81  ? 110 HIS B CD2 1 
ATOM   1926  C  CE1 . HIS B  1 111 ? 12.264  -37.117 2.273  1.00 54.09  ? 110 HIS B CE1 1 
ATOM   1927  N  NE2 . HIS B  1 111 ? 12.030  -38.462 2.240  1.00 48.86  ? 110 HIS B NE2 1 
ATOM   1928  N  N   . CYS B  1 112 ? 5.800   -38.486 4.885  1.00 32.52  ? 111 CYS B N   1 
ATOM   1929  C  CA  . CYS B  1 112 ? 4.631   -38.285 5.723  1.00 29.75  ? 111 CYS B CA  1 
ATOM   1930  C  C   . CYS B  1 112 ? 4.911   -38.843 7.122  1.00 29.17  ? 111 CYS B C   1 
ATOM   1931  O  O   . CYS B  1 112 ? 5.475   -39.941 7.279  1.00 29.88  ? 111 CYS B O   1 
ATOM   1932  C  CB  . CYS B  1 112 ? 3.429   -38.940 5.074  1.00 32.26  ? 111 CYS B CB  1 
ATOM   1933  S  SG  . CYS B  1 112 ? 1.856   -38.099 5.443  1.00 31.99  ? 111 CYS B SG  1 
ATOM   1934  N  N   . ILE B  1 113 ? 4.620   -38.026 8.143  1.00 27.09  ? 112 ILE B N   1 
ATOM   1935  C  CA  . ILE B  1 113 ? 4.855   -38.394 9.530  1.00 26.36  ? 112 ILE B CA  1 
ATOM   1936  C  C   . ILE B  1 113 ? 3.543   -38.822 10.192 1.00 27.43  ? 112 ILE B C   1 
ATOM   1937  O  O   . ILE B  1 113 ? 3.514   -39.120 11.391 1.00 28.22  ? 112 ILE B O   1 
ATOM   1938  C  CB  . ILE B  1 113 ? 5.526   -37.241 10.312 1.00 25.69  ? 112 ILE B CB  1 
ATOM   1939  C  CG1 . ILE B  1 113 ? 4.739   -35.925 10.201 1.00 24.04  ? 112 ILE B CG1 1 
ATOM   1940  C  CG2 . ILE B  1 113 ? 6.991   -37.098 9.920  1.00 24.10  ? 112 ILE B CG2 1 
ATOM   1941  C  CD1 . ILE B  1 113 ? 5.030   -34.974 11.336 1.00 22.41  ? 112 ILE B CD1 1 
ATOM   1942  N  N   . ILE B  1 114 ? 2.449   -38.815 9.416  1.00 26.74  ? 113 ILE B N   1 
ATOM   1943  C  CA  . ILE B  1 114 ? 1.152   -39.221 9.930  1.00 25.66  ? 113 ILE B CA  1 
ATOM   1944  C  C   . ILE B  1 114 ? 1.234   -40.682 10.339 1.00 25.05  ? 113 ILE B C   1 
ATOM   1945  O  O   . ILE B  1 114 ? 1.778   -41.505 9.603  1.00 25.33  ? 113 ILE B O   1 
ATOM   1946  C  CB  . ILE B  1 114 ? 0.038   -38.980 8.903  1.00 26.81  ? 113 ILE B CB  1 
ATOM   1947  C  CG1 . ILE B  1 114 ? 0.031   -37.505 8.498  1.00 28.80  ? 113 ILE B CG1 1 
ATOM   1948  C  CG2 . ILE B  1 114 ? -1.313  -39.410 9.456  1.00 25.37  ? 113 ILE B CG2 1 
ATOM   1949  C  CD1 . ILE B  1 114 ? -1.279  -36.995 7.943  1.00 28.23  ? 113 ILE B CD1 1 
ATOM   1950  N  N   . GLY B  1 115 ? 0.715   -40.961 11.537 1.00 24.45  ? 114 GLY B N   1 
ATOM   1951  C  CA  . GLY B  1 115 ? 0.637   -42.318 12.054 1.00 23.93  ? 114 GLY B CA  1 
ATOM   1952  C  C   . GLY B  1 115 ? 1.967   -42.782 12.642 1.00 25.12  ? 114 GLY B C   1 
ATOM   1953  O  O   . GLY B  1 115 ? 2.137   -43.979 12.890 1.00 25.92  ? 114 GLY B O   1 
ATOM   1954  N  N   . ARG B  1 116 ? 2.896   -41.828 12.854 1.00 24.09  ? 115 ARG B N   1 
ATOM   1955  C  CA  . ARG B  1 116 ? 4.145   -42.103 13.551 1.00 22.18  ? 115 ARG B CA  1 
ATOM   1956  C  C   . ARG B  1 116 ? 4.090   -41.462 14.941 1.00 22.90  ? 115 ARG B C   1 
ATOM   1957  O  O   . ARG B  1 116 ? 3.028   -40.995 15.357 1.00 24.78  ? 115 ARG B O   1 
ATOM   1958  C  CB  . ARG B  1 116 ? 5.311   -41.694 12.658 1.00 20.28  ? 115 ARG B CB  1 
ATOM   1959  C  CG  . ARG B  1 116 ? 5.213   -42.312 11.275 1.00 20.50  ? 115 ARG B CG  1 
ATOM   1960  C  CD  . ARG B  1 116 ? 6.435   -42.093 10.419 1.00 20.18  ? 115 ARG B CD  1 
ATOM   1961  N  NE  . ARG B  1 116 ? 6.331   -42.704 9.106  1.00 20.99  ? 115 ARG B NE  1 
ATOM   1962  C  CZ  . ARG B  1 116 ? 6.666   -43.977 8.823  1.00 20.55  ? 115 ARG B CZ  1 
ATOM   1963  N  NH1 . ARG B  1 116 ? 7.142   -44.785 9.762  1.00 20.57  ? 115 ARG B NH1 1 
ATOM   1964  N  NH2 . ARG B  1 116 ? 6.546   -44.429 7.587  1.00 19.19  ? 115 ARG B NH2 1 
ATOM   1965  N  N   . THR B  1 117 ? 5.207   -41.468 15.678 1.00 21.33  ? 116 THR B N   1 
ATOM   1966  C  CA  . THR B  1 117 ? 5.176   -40.955 17.041 1.00 20.45  ? 116 THR B CA  1 
ATOM   1967  C  C   . THR B  1 117 ? 6.044   -39.707 17.188 1.00 21.00  ? 116 THR B C   1 
ATOM   1968  O  O   . THR B  1 117 ? 7.147   -39.630 16.646 1.00 22.47  ? 116 THR B O   1 
ATOM   1969  C  CB  . THR B  1 117 ? 5.607   -42.011 18.060 1.00 19.49  ? 116 THR B CB  1 
ATOM   1970  O  OG1 . THR B  1 117 ? 4.643   -43.047 17.978 1.00 19.56  ? 116 THR B OG1 1 
ATOM   1971  C  CG2 . THR B  1 117 ? 5.626   -41.492 19.478 1.00 19.91  ? 116 THR B CG2 1 
ATOM   1972  N  N   . LEU B  1 118 ? 5.531   -38.742 17.947 1.00 19.95  ? 117 LEU B N   1 
ATOM   1973  C  CA  . LEU B  1 118 ? 6.344   -37.620 18.370 1.00 19.60  ? 117 LEU B CA  1 
ATOM   1974  C  C   . LEU B  1 118 ? 6.757   -37.878 19.817 1.00 19.20  ? 117 LEU B C   1 
ATOM   1975  O  O   . LEU B  1 118 ? 5.928   -38.280 20.631 1.00 17.82  ? 117 LEU B O   1 
ATOM   1976  C  CB  . LEU B  1 118 ? 5.483   -36.360 18.247 1.00 18.67  ? 117 LEU B CB  1 
ATOM   1977  C  CG  . LEU B  1 118 ? 6.161   -35.072 18.709 1.00 18.78  ? 117 LEU B CG  1 
ATOM   1978  C  CD1 . LEU B  1 118 ? 7.341   -34.734 17.808 1.00 17.92  ? 117 LEU B CD1 1 
ATOM   1979  C  CD2 . LEU B  1 118 ? 5.175   -33.928 18.760 1.00 17.74  ? 117 LEU B CD2 1 
ATOM   1980  N  N   . VAL B  1 119 ? 8.045   -37.671 20.113 1.00 19.68  ? 118 VAL B N   1 
ATOM   1981  C  CA  . VAL B  1 119 ? 8.579   -37.946 21.439 1.00 20.95  ? 118 VAL B CA  1 
ATOM   1982  C  C   . VAL B  1 119 ? 9.343   -36.730 21.950 1.00 21.64  ? 118 VAL B C   1 
ATOM   1983  O  O   . VAL B  1 119 ? 10.156  -36.144 21.230 1.00 23.37  ? 118 VAL B O   1 
ATOM   1984  C  CB  . VAL B  1 119 ? 9.514   -39.176 21.450 1.00 21.79  ? 118 VAL B CB  1 
ATOM   1985  C  CG1 . VAL B  1 119 ? 10.036  -39.468 22.844 1.00 22.19  ? 118 VAL B CG1 1 
ATOM   1986  C  CG2 . VAL B  1 119 ? 8.881   -40.414 20.852 1.00 21.94  ? 118 VAL B CG2 1 
ATOM   1987  N  N   . VAL B  1 120 ? 9.107   -36.399 23.219 1.00 20.78  ? 119 VAL B N   1 
ATOM   1988  C  CA  . VAL B  1 120 ? 9.927   -35.412 23.888 1.00 21.73  ? 119 VAL B CA  1 
ATOM   1989  C  C   . VAL B  1 120 ? 10.789  -36.145 24.911 1.00 23.12  ? 119 VAL B C   1 
ATOM   1990  O  O   . VAL B  1 120 ? 10.276  -36.914 25.734 1.00 21.89  ? 119 VAL B O   1 
ATOM   1991  C  CB  . VAL B  1 120 ? 9.069   -34.291 24.509 1.00 21.87  ? 119 VAL B CB  1 
ATOM   1992  C  CG1 . VAL B  1 120 ? 8.054   -34.810 25.524 1.00 22.03  ? 119 VAL B CG1 1 
ATOM   1993  C  CG2 . VAL B  1 120 ? 9.928   -33.196 25.107 1.00 21.10  ? 119 VAL B CG2 1 
ATOM   1994  N  N   . HIS B  1 121 ? 12.104  -35.879 24.847 1.00 25.74  ? 120 HIS B N   1 
ATOM   1995  C  CA  . HIS B  1 121 ? 13.107  -36.652 25.566 1.00 27.30  ? 120 HIS B CA  1 
ATOM   1996  C  C   . HIS B  1 121 ? 13.558  -35.979 26.862 1.00 28.76  ? 120 HIS B C   1 
ATOM   1997  O  O   . HIS B  1 121 ? 13.246  -34.825 27.122 1.00 26.04  ? 120 HIS B O   1 
ATOM   1998  C  CB  . HIS B  1 121 ? 14.303  -36.924 24.660 1.00 26.03  ? 120 HIS B CB  1 
ATOM   1999  C  CG  . HIS B  1 121 ? 14.032  -37.926 23.598 1.00 27.49  ? 120 HIS B CG  1 
ATOM   2000  N  ND1 . HIS B  1 121 ? 14.296  -39.263 23.783 1.00 28.93  ? 120 HIS B ND1 1 
ATOM   2001  C  CD2 . HIS B  1 121 ? 13.548  -37.795 22.342 1.00 27.46  ? 120 HIS B CD2 1 
ATOM   2002  C  CE1 . HIS B  1 121 ? 13.982  -39.914 22.674 1.00 30.14  ? 120 HIS B CE1 1 
ATOM   2003  N  NE2 . HIS B  1 121 ? 13.523  -39.038 21.775 1.00 28.30  ? 120 HIS B NE2 1 
ATOM   2004  N  N   . GLU B  1 122 ? 14.363  -36.718 27.631 1.00 31.96  ? 121 GLU B N   1 
ATOM   2005  C  CA  . GLU B  1 122 ? 14.730  -36.392 28.997 1.00 32.07  ? 121 GLU B CA  1 
ATOM   2006  C  C   . GLU B  1 122 ? 15.739  -35.246 29.039 1.00 34.09  ? 121 GLU B C   1 
ATOM   2007  O  O   . GLU B  1 122 ? 15.609  -34.362 29.882 1.00 36.32  ? 121 GLU B O   1 
ATOM   2008  C  CB  . GLU B  1 122 ? 15.257  -37.668 29.639 1.00 36.39  ? 121 GLU B CB  1 
ATOM   2009  C  CG  . GLU B  1 122 ? 16.129  -37.457 30.850 1.00 39.26  ? 121 GLU B CG  1 
ATOM   2010  C  CD  . GLU B  1 122 ? 16.923  -38.719 31.165 1.00 43.00  ? 121 GLU B CD  1 
ATOM   2011  O  OE1 . GLU B  1 122 ? 17.200  -38.921 32.348 1.00 44.46  ? 121 GLU B OE1 1 
ATOM   2012  O  OE2 . GLU B  1 122 ? 17.312  -39.460 30.212 1.00 41.23  ? 121 GLU B OE2 1 
ATOM   2013  N  N   . LYS B  1 123 ? 16.720  -35.268 28.123 1.00 34.60  ? 122 LYS B N   1 
ATOM   2014  C  CA  . LYS B  1 123 ? 17.867  -34.366 28.115 1.00 34.65  ? 122 LYS B CA  1 
ATOM   2015  C  C   . LYS B  1 123 ? 17.987  -33.662 26.763 1.00 33.38  ? 122 LYS B C   1 
ATOM   2016  O  O   . LYS B  1 123 ? 17.211  -33.915 25.847 1.00 31.38  ? 122 LYS B O   1 
ATOM   2017  C  CB  . LYS B  1 123 ? 19.161  -35.172 28.302 1.00 37.44  ? 122 LYS B CB  1 
ATOM   2018  C  CG  . LYS B  1 123 ? 19.317  -35.880 29.639 1.00 41.18  ? 122 LYS B CG  1 
ATOM   2019  C  CD  . LYS B  1 123 ? 20.635  -36.629 29.813 1.00 49.15  ? 122 LYS B CD  1 
ATOM   2020  C  CE  . LYS B  1 123 ? 20.732  -37.915 29.014 1.00 55.44  ? 122 LYS B CE  1 
ATOM   2021  N  NZ  . LYS B  1 123 ? 21.699  -38.896 29.582 1.00 53.74  ? 122 LYS B NZ  1 
ATOM   2022  N  N   . ALA B  1 124 ? 19.002  -32.800 26.639 1.00 32.18  ? 123 ALA B N   1 
ATOM   2023  C  CA  . ALA B  1 124 ? 19.281  -32.090 25.402 1.00 29.57  ? 123 ALA B CA  1 
ATOM   2024  C  C   . ALA B  1 124 ? 19.697  -33.075 24.311 1.00 28.28  ? 123 ALA B C   1 
ATOM   2025  O  O   . ALA B  1 124 ? 20.336  -34.081 24.582 1.00 26.71  ? 123 ALA B O   1 
ATOM   2026  C  CB  . ALA B  1 124 ? 20.370  -31.079 25.627 1.00 29.61  ? 123 ALA B CB  1 
ATOM   2027  N  N   . ASP B  1 125 ? 19.300  -32.774 23.075 1.00 29.52  ? 124 ASP B N   1 
ATOM   2028  C  CA  . ASP B  1 125 ? 19.800  -33.460 21.900 1.00 27.17  ? 124 ASP B CA  1 
ATOM   2029  C  C   . ASP B  1 125 ? 21.100  -32.772 21.494 1.00 27.34  ? 124 ASP B C   1 
ATOM   2030  O  O   . ASP B  1 125 ? 21.102  -31.568 21.239 1.00 28.58  ? 124 ASP B O   1 
ATOM   2031  C  CB  . ASP B  1 125 ? 18.735  -33.427 20.802 1.00 27.22  ? 124 ASP B CB  1 
ATOM   2032  C  CG  . ASP B  1 125 ? 19.178  -33.972 19.450 1.00 28.31  ? 124 ASP B CG  1 
ATOM   2033  O  OD1 . ASP B  1 125 ? 20.364  -34.316 19.299 1.00 31.11  ? 124 ASP B OD1 1 
ATOM   2034  O  OD2 . ASP B  1 125 ? 18.331  -34.032 18.541 1.00 28.51  ? 124 ASP B OD2 1 
ATOM   2035  N  N   . ASP B  1 126 ? 22.203  -33.533 21.420 1.00 25.28  ? 125 ASP B N   1 
ATOM   2036  C  CA  . ASP B  1 126 ? 23.504  -32.942 21.140 1.00 24.58  ? 125 ASP B CA  1 
ATOM   2037  C  C   . ASP B  1 126 ? 23.699  -32.719 19.639 1.00 23.53  ? 125 ASP B C   1 
ATOM   2038  O  O   . ASP B  1 126 ? 24.781  -32.324 19.213 1.00 21.61  ? 125 ASP B O   1 
ATOM   2039  C  CB  . ASP B  1 126 ? 24.644  -33.697 21.834 1.00 26.60  ? 125 ASP B CB  1 
ATOM   2040  C  CG  . ASP B  1 126 ? 24.984  -35.063 21.245 1.00 29.38  ? 125 ASP B CG  1 
ATOM   2041  O  OD1 . ASP B  1 126 ? 24.672  -35.299 20.041 1.00 30.42  ? 125 ASP B OD1 1 
ATOM   2042  O  OD2 . ASP B  1 126 ? 25.583  -35.887 21.994 1.00 26.37  ? 125 ASP B OD2 1 
ATOM   2043  N  N   . LEU B  1 127 ? 22.646  -32.962 18.848 1.00 23.52  ? 126 LEU B N   1 
ATOM   2044  C  CA  . LEU B  1 127 ? 22.626  -32.674 17.421 1.00 25.11  ? 126 LEU B CA  1 
ATOM   2045  C  C   . LEU B  1 127 ? 23.748  -33.417 16.692 1.00 27.90  ? 126 LEU B C   1 
ATOM   2046  O  O   . LEU B  1 127 ? 24.158  -33.004 15.602 1.00 31.66  ? 126 LEU B O   1 
ATOM   2047  C  CB  . LEU B  1 127 ? 22.719  -31.163 17.177 1.00 24.76  ? 126 LEU B CB  1 
ATOM   2048  C  CG  . LEU B  1 127 ? 21.783  -30.270 17.997 1.00 24.05  ? 126 LEU B CG  1 
ATOM   2049  C  CD1 . LEU B  1 127 ? 21.881  -28.816 17.523 1.00 22.84  ? 126 LEU B CD1 1 
ATOM   2050  C  CD2 . LEU B  1 127 ? 20.339  -30.725 17.883 1.00 22.90  ? 126 LEU B CD2 1 
ATOM   2051  N  N   . GLY B  1 128 ? 24.234  -34.507 17.304 1.00 28.79  ? 127 GLY B N   1 
ATOM   2052  C  CA  . GLY B  1 128 ? 25.139  -35.441 16.654 1.00 29.00  ? 127 GLY B CA  1 
ATOM   2053  C  C   . GLY B  1 128 ? 26.606  -35.033 16.795 1.00 31.95  ? 127 GLY B C   1 
ATOM   2054  O  O   . GLY B  1 128 ? 27.459  -35.541 16.072 1.00 31.99  ? 127 GLY B O   1 
ATOM   2055  N  N   . LYS B  1 129 ? 26.891  -34.130 17.741 1.00 32.71  ? 128 LYS B N   1 
ATOM   2056  C  CA  . LYS B  1 129 ? 28.216  -33.549 17.883 1.00 30.52  ? 128 LYS B CA  1 
ATOM   2057  C  C   . LYS B  1 129 ? 28.819  -33.940 19.227 1.00 30.21  ? 128 LYS B C   1 
ATOM   2058  O  O   . LYS B  1 129 ? 29.605  -33.182 19.789 1.00 30.71  ? 128 LYS B O   1 
ATOM   2059  C  CB  . LYS B  1 129 ? 28.135  -32.023 17.781 1.00 31.00  ? 128 LYS B CB  1 
ATOM   2060  C  CG  . LYS B  1 129 ? 27.420  -31.495 16.555 1.00 34.85  ? 128 LYS B CG  1 
ATOM   2061  C  CD  . LYS B  1 129 ? 27.737  -30.056 16.276 1.00 37.53  ? 128 LYS B CD  1 
ATOM   2062  C  CE  . LYS B  1 129 ? 26.894  -29.617 15.109 1.00 44.39  ? 128 LYS B CE  1 
ATOM   2063  N  NZ  . LYS B  1 129 ? 27.583  -28.577 14.312 1.00 52.61  ? 128 LYS B NZ  1 
ATOM   2064  N  N   . GLY B  1 130 ? 28.461  -35.129 19.726 1.00 29.90  ? 129 GLY B N   1 
ATOM   2065  C  CA  . GLY B  1 130 ? 28.871  -35.569 21.050 1.00 27.53  ? 129 GLY B CA  1 
ATOM   2066  C  C   . GLY B  1 130 ? 30.099  -36.482 21.013 1.00 28.72  ? 129 GLY B C   1 
ATOM   2067  O  O   . GLY B  1 130 ? 30.664  -36.799 22.060 1.00 26.61  ? 129 GLY B O   1 
ATOM   2068  N  N   . GLY B  1 131 ? 30.487  -36.904 19.798 1.00 29.27  ? 130 GLY B N   1 
ATOM   2069  C  CA  . GLY B  1 131 ? 31.709  -37.653 19.567 1.00 30.42  ? 130 GLY B CA  1 
ATOM   2070  C  C   . GLY B  1 131 ? 31.673  -39.078 20.133 1.00 32.97  ? 130 GLY B C   1 
ATOM   2071  O  O   . GLY B  1 131 ? 32.716  -39.670 20.412 1.00 32.26  ? 130 GLY B O   1 
ATOM   2072  N  N   . ASN B  1 132 ? 30.469  -39.628 20.316 1.00 33.04  ? 131 ASN B N   1 
ATOM   2073  C  CA  . ASN B  1 132 ? 30.322  -41.038 20.633 1.00 30.18  ? 131 ASN B CA  1 
ATOM   2074  C  C   . ASN B  1 132 ? 29.309  -41.657 19.676 1.00 30.65  ? 131 ASN B C   1 
ATOM   2075  O  O   . ASN B  1 132 ? 28.698  -40.962 18.861 1.00 27.22  ? 131 ASN B O   1 
ATOM   2076  C  CB  . ASN B  1 132 ? 30.029  -41.288 22.115 1.00 29.55  ? 131 ASN B CB  1 
ATOM   2077  C  CG  . ASN B  1 132 ? 28.769  -40.632 22.632 1.00 28.31  ? 131 ASN B CG  1 
ATOM   2078  O  OD1 . ASN B  1 132 ? 27.884  -40.270 21.863 1.00 29.53  ? 131 ASN B OD1 1 
ATOM   2079  N  ND2 . ASN B  1 132 ? 28.705  -40.437 23.944 1.00 26.60  ? 131 ASN B ND2 1 
ATOM   2080  N  N   . GLU B  1 133 ? 29.143  -42.978 19.788 1.00 34.61  ? 132 GLU B N   1 
ATOM   2081  C  CA  . GLU B  1 133 ? 28.335  -43.692 18.818 1.00 37.38  ? 132 GLU B CA  1 
ATOM   2082  C  C   . GLU B  1 133 ? 26.872  -43.308 19.020 1.00 36.65  ? 132 GLU B C   1 
ATOM   2083  O  O   . GLU B  1 133 ? 26.124  -43.116 18.059 1.00 37.69  ? 132 GLU B O   1 
ATOM   2084  C  CB  . GLU B  1 133 ? 28.582  -45.193 18.925 1.00 41.21  ? 132 GLU B CB  1 
ATOM   2085  C  CG  . GLU B  1 133 ? 27.968  -45.945 17.767 1.00 47.43  ? 132 GLU B CG  1 
ATOM   2086  C  CD  . GLU B  1 133 ? 27.824  -47.442 17.971 1.00 49.35  ? 132 GLU B CD  1 
ATOM   2087  O  OE1 . GLU B  1 133 ? 28.654  -48.040 18.702 1.00 50.35  ? 132 GLU B OE1 1 
ATOM   2088  O  OE2 . GLU B  1 133 ? 26.884  -48.013 17.383 1.00 52.40  ? 132 GLU B OE2 1 
ATOM   2089  N  N   . GLU B  1 134 ? 26.514  -43.157 20.303 1.00 36.86  ? 133 GLU B N   1 
ATOM   2090  C  CA  . GLU B  1 134 ? 25.183  -42.776 20.732 1.00 37.82  ? 133 GLU B CA  1 
ATOM   2091  C  C   . GLU B  1 134 ? 24.769  -41.460 20.070 1.00 35.92  ? 133 GLU B C   1 
ATOM   2092  O  O   . GLU B  1 134 ? 23.631  -41.315 19.619 1.00 31.70  ? 133 GLU B O   1 
ATOM   2093  C  CB  . GLU B  1 134 ? 25.184  -42.706 22.259 1.00 43.00  ? 133 GLU B CB  1 
ATOM   2094  C  CG  . GLU B  1 134 ? 23.807  -42.820 22.893 1.00 47.80  ? 133 GLU B CG  1 
ATOM   2095  C  CD  . GLU B  1 134 ? 22.839  -43.872 22.359 1.00 55.35  ? 133 GLU B CD  1 
ATOM   2096  O  OE1 . GLU B  1 134 ? 23.278  -44.961 21.923 1.00 56.67  ? 133 GLU B OE1 1 
ATOM   2097  O  OE2 . GLU B  1 134 ? 21.628  -43.586 22.359 1.00 60.47  ? 133 GLU B OE2 1 
ATOM   2098  N  N   . SER B  1 135 ? 25.704  -40.503 20.009 1.00 35.47  ? 134 SER B N   1 
ATOM   2099  C  CA  . SER B  1 135 ? 25.425  -39.183 19.470 1.00 35.71  ? 134 SER B CA  1 
ATOM   2100  C  C   . SER B  1 135 ? 24.875  -39.288 18.051 1.00 36.11  ? 134 SER B C   1 
ATOM   2101  O  O   . SER B  1 135 ? 23.951  -38.563 17.695 1.00 39.39  ? 134 SER B O   1 
ATOM   2102  C  CB  . SER B  1 135 ? 26.638  -38.288 19.530 1.00 33.42  ? 134 SER B CB  1 
ATOM   2103  O  OG  . SER B  1 135 ? 26.323  -36.973 19.085 1.00 30.19  ? 134 SER B OG  1 
ATOM   2104  N  N   . THR B  1 136 ? 25.434  -40.195 17.244 1.00 34.90  ? 135 THR B N   1 
ATOM   2105  C  CA  . THR B  1 136 ? 25.052  -40.223 15.838 1.00 33.78  ? 135 THR B CA  1 
ATOM   2106  C  C   . THR B  1 136 ? 23.802  -41.070 15.617 1.00 31.13  ? 135 THR B C   1 
ATOM   2107  O  O   . THR B  1 136 ? 23.372  -41.227 14.475 1.00 28.54  ? 135 THR B O   1 
ATOM   2108  C  CB  . THR B  1 136 ? 26.199  -40.722 14.948 1.00 35.09  ? 135 THR B CB  1 
ATOM   2109  O  OG1 . THR B  1 136 ? 26.421  -42.086 15.319 1.00 34.84  ? 135 THR B OG1 1 
ATOM   2110  C  CG2 . THR B  1 136 ? 27.458  -39.893 15.078 1.00 31.78  ? 135 THR B CG2 1 
ATOM   2111  N  N   . LYS B  1 137 ? 23.231  -41.601 16.711 1.00 31.49  ? 136 LYS B N   1 
ATOM   2112  C  CA  . LYS B  1 137 ? 21.991  -42.358 16.640 1.00 31.28  ? 136 LYS B CA  1 
ATOM   2113  C  C   . LYS B  1 137 ? 20.841  -41.564 17.256 1.00 28.27  ? 136 LYS B C   1 
ATOM   2114  O  O   . LYS B  1 137 ? 19.810  -41.357 16.611 1.00 28.62  ? 136 LYS B O   1 
ATOM   2115  C  CB  . LYS B  1 137 ? 22.139  -43.711 17.337 1.00 35.96  ? 136 LYS B CB  1 
ATOM   2116  C  CG  . LYS B  1 137 ? 22.849  -44.795 16.530 1.00 40.46  ? 136 LYS B CG  1 
ATOM   2117  C  CD  . LYS B  1 137 ? 23.084  -46.066 17.309 1.00 46.73  ? 136 LYS B CD  1 
ATOM   2118  C  CE  . LYS B  1 137 ? 23.220  -47.292 16.428 1.00 53.42  ? 136 LYS B CE  1 
ATOM   2119  N  NZ  . LYS B  1 137 ? 23.851  -48.392 17.186 1.00 60.80  ? 136 LYS B NZ  1 
ATOM   2120  N  N   . THR B  1 138 ? 21.022  -41.113 18.505 1.00 25.37  ? 137 THR B N   1 
ATOM   2121  C  CA  . THR B  1 138 ? 19.918  -40.566 19.279 1.00 24.94  ? 137 THR B CA  1 
ATOM   2122  C  C   . THR B  1 138 ? 20.206  -39.152 19.775 1.00 25.46  ? 137 THR B C   1 
ATOM   2123  O  O   . THR B  1 138 ? 19.366  -38.563 20.465 1.00 26.29  ? 137 THR B O   1 
ATOM   2124  C  CB  . THR B  1 138 ? 19.641  -41.444 20.502 1.00 24.03  ? 137 THR B CB  1 
ATOM   2125  O  OG1 . THR B  1 138 ? 20.693  -41.272 21.462 1.00 23.85  ? 137 THR B OG1 1 
ATOM   2126  C  CG2 . THR B  1 138 ? 19.477  -42.900 20.127 1.00 21.86  ? 137 THR B CG2 1 
ATOM   2127  N  N   . GLY B  1 139 ? 21.404  -38.639 19.471 1.00 25.75  ? 138 GLY B N   1 
ATOM   2128  C  CA  . GLY B  1 139 ? 21.845  -37.354 19.984 1.00 25.55  ? 138 GLY B CA  1 
ATOM   2129  C  C   . GLY B  1 139 ? 21.945  -37.315 21.511 1.00 25.62  ? 138 GLY B C   1 
ATOM   2130  O  O   . GLY B  1 139 ? 22.071  -36.238 22.088 1.00 25.28  ? 138 GLY B O   1 
ATOM   2131  N  N   . ASN B  1 140 ? 21.886  -38.485 22.165 1.00 25.75  ? 139 ASN B N   1 
ATOM   2132  C  CA  . ASN B  1 140 ? 22.137  -38.582 23.599 1.00 26.82  ? 139 ASN B CA  1 
ATOM   2133  C  C   . ASN B  1 140 ? 21.014  -37.900 24.377 1.00 26.49  ? 139 ASN B C   1 
ATOM   2134  O  O   . ASN B  1 140 ? 21.227  -37.442 25.500 1.00 28.36  ? 139 ASN B O   1 
ATOM   2135  C  CB  . ASN B  1 140 ? 23.496  -38.000 24.015 1.00 26.88  ? 139 ASN B CB  1 
ATOM   2136  C  CG  . ASN B  1 140 ? 24.666  -38.903 23.677 1.00 27.66  ? 139 ASN B CG  1 
ATOM   2137  O  OD1 . ASN B  1 140 ? 24.826  -39.976 24.251 1.00 27.89  ? 139 ASN B OD1 1 
ATOM   2138  N  ND2 . ASN B  1 140 ? 25.498  -38.477 22.742 1.00 26.22  ? 139 ASN B ND2 1 
ATOM   2139  N  N   . ALA B  1 141 ? 19.812  -37.876 23.786 1.00 25.22  ? 140 ALA B N   1 
ATOM   2140  C  CA  . ALA B  1 141 ? 18.694  -37.133 24.340 1.00 25.88  ? 140 ALA B CA  1 
ATOM   2141  C  C   . ALA B  1 141 ? 18.090  -37.852 25.549 1.00 27.14  ? 140 ALA B C   1 
ATOM   2142  O  O   . ALA B  1 141 ? 17.224  -37.309 26.241 1.00 27.89  ? 140 ALA B O   1 
ATOM   2143  C  CB  . ALA B  1 141 ? 17.674  -36.884 23.263 1.00 25.53  ? 140 ALA B CB  1 
ATOM   2144  N  N   . GLY B  1 142 ? 18.552  -39.080 25.809 1.00 26.38  ? 141 GLY B N   1 
ATOM   2145  C  CA  . GLY B  1 142 ? 18.097  -39.811 26.979 1.00 25.20  ? 141 GLY B CA  1 
ATOM   2146  C  C   . GLY B  1 142 ? 16.701  -40.379 26.763 1.00 25.37  ? 141 GLY B C   1 
ATOM   2147  O  O   . GLY B  1 142 ? 16.285  -40.573 25.616 1.00 27.58  ? 141 GLY B O   1 
ATOM   2148  N  N   . SER B  1 143 ? 15.990  -40.613 27.872 1.00 24.54  ? 142 SER B N   1 
ATOM   2149  C  CA  . SER B  1 143 ? 14.759  -41.390 27.858 1.00 25.62  ? 142 SER B CA  1 
ATOM   2150  C  C   . SER B  1 143 ? 13.614  -40.599 27.226 1.00 25.80  ? 142 SER B C   1 
ATOM   2151  O  O   . SER B  1 143 ? 13.750  -39.403 26.946 1.00 26.09  ? 142 SER B O   1 
ATOM   2152  C  CB  . SER B  1 143 ? 14.396  -41.880 29.234 1.00 24.76  ? 142 SER B CB  1 
ATOM   2153  O  OG  . SER B  1 143 ? 14.116  -40.786 30.084 1.00 26.68  ? 142 SER B OG  1 
ATOM   2154  N  N   . ARG B  1 144 ? 12.491  -41.301 27.019 1.00 24.80  ? 143 ARG B N   1 
ATOM   2155  C  CA  . ARG B  1 144 ? 11.310  -40.770 26.358 1.00 24.68  ? 143 ARG B CA  1 
ATOM   2156  C  C   . ARG B  1 144 ? 10.304  -40.359 27.434 1.00 26.55  ? 143 ARG B C   1 
ATOM   2157  O  O   . ARG B  1 144 ? 9.722   -41.211 28.093 1.00 25.70  ? 143 ARG B O   1 
ATOM   2158  C  CB  . ARG B  1 144 ? 10.748  -41.842 25.425 1.00 22.24  ? 143 ARG B CB  1 
ATOM   2159  C  CG  . ARG B  1 144 ? 11.741  -42.347 24.402 1.00 22.09  ? 143 ARG B CG  1 
ATOM   2160  C  CD  . ARG B  1 144 ? 11.376  -43.589 23.650 1.00 22.29  ? 143 ARG B CD  1 
ATOM   2161  N  NE  . ARG B  1 144 ? 12.424  -44.020 22.738 1.00 23.13  ? 143 ARG B NE  1 
ATOM   2162  C  CZ  . ARG B  1 144 ? 12.231  -44.715 21.612 1.00 24.08  ? 143 ARG B CZ  1 
ATOM   2163  N  NH1 . ARG B  1 144 ? 11.013  -45.060 21.228 1.00 24.68  ? 143 ARG B NH1 1 
ATOM   2164  N  NH2 . ARG B  1 144 ? 13.255  -45.048 20.853 1.00 24.16  ? 143 ARG B NH2 1 
ATOM   2165  N  N   . LEU B  1 145 ? 10.127  -39.048 27.635 1.00 27.75  ? 144 LEU B N   1 
ATOM   2166  C  CA  . LEU B  1 145 ? 9.343   -38.587 28.765 1.00 27.93  ? 144 LEU B CA  1 
ATOM   2167  C  C   . LEU B  1 145 ? 7.856   -38.685 28.438 1.00 29.42  ? 144 LEU B C   1 
ATOM   2168  O  O   . LEU B  1 145 ? 7.045   -39.014 29.302 1.00 29.34  ? 144 LEU B O   1 
ATOM   2169  C  CB  . LEU B  1 145 ? 9.752   -37.149 29.080 1.00 29.86  ? 144 LEU B CB  1 
ATOM   2170  C  CG  . LEU B  1 145 ? 11.128  -36.976 29.719 1.00 31.75  ? 144 LEU B CG  1 
ATOM   2171  C  CD1 . LEU B  1 145 ? 11.373  -35.515 30.079 1.00 32.19  ? 144 LEU B CD1 1 
ATOM   2172  C  CD2 . LEU B  1 145 ? 11.276  -37.870 30.944 1.00 28.73  ? 144 LEU B CD2 1 
ATOM   2173  N  N   . ALA B  1 146 ? 7.515   -38.388 27.179 1.00 29.68  ? 145 ALA B N   1 
ATOM   2174  C  CA  . ALA B  1 146 ? 6.137   -38.405 26.719 1.00 27.98  ? 145 ALA B CA  1 
ATOM   2175  C  C   . ALA B  1 146 ? 6.110   -38.504 25.199 1.00 27.30  ? 145 ALA B C   1 
ATOM   2176  O  O   . ALA B  1 146 ? 7.043   -38.087 24.507 1.00 26.73  ? 145 ALA B O   1 
ATOM   2177  C  CB  . ALA B  1 146 ? 5.397   -37.182 27.193 1.00 29.48  ? 145 ALA B CB  1 
ATOM   2178  N  N   . CYS B  1 147 ? 5.047   -39.134 24.694 1.00 27.48  ? 146 CYS B N   1 
ATOM   2179  C  CA  . CYS B  1 147 ? 4.908   -39.338 23.266 1.00 28.02  ? 146 CYS B CA  1 
ATOM   2180  C  C   . CYS B  1 147 ? 3.427   -39.438 22.930 1.00 27.65  ? 146 CYS B C   1 
ATOM   2181  O  O   . CYS B  1 147 ? 2.591   -39.483 23.831 1.00 28.50  ? 146 CYS B O   1 
ATOM   2182  C  CB  . CYS B  1 147 ? 5.638   -40.597 22.819 1.00 30.05  ? 146 CYS B CB  1 
ATOM   2183  S  SG  . CYS B  1 147 ? 5.090   -42.088 23.671 1.00 31.11  ? 146 CYS B SG  1 
ATOM   2184  N  N   . GLY B  1 148 ? 3.140   -39.440 21.625 1.00 25.02  ? 147 GLY B N   1 
ATOM   2185  C  CA  . GLY B  1 148 ? 1.803   -39.631 21.104 1.00 22.85  ? 147 GLY B CA  1 
ATOM   2186  C  C   . GLY B  1 148 ? 1.856   -40.012 19.625 1.00 22.14  ? 147 GLY B C   1 
ATOM   2187  O  O   . GLY B  1 148 ? 2.839   -39.745 18.932 1.00 20.50  ? 147 GLY B O   1 
ATOM   2188  N  N   . VAL B  1 149 ? 0.779   -40.641 19.149 1.00 21.47  ? 148 VAL B N   1 
ATOM   2189  C  CA  . VAL B  1 149 ? 0.688   -40.922 17.732 1.00 20.79  ? 148 VAL B CA  1 
ATOM   2190  C  C   . VAL B  1 149 ? 0.221   -39.658 17.019 1.00 20.63  ? 148 VAL B C   1 
ATOM   2191  O  O   . VAL B  1 149 ? -0.613  -38.923 17.531 1.00 20.90  ? 148 VAL B O   1 
ATOM   2192  C  CB  . VAL B  1 149 ? -0.186  -42.158 17.444 1.00 19.70  ? 148 VAL B CB  1 
ATOM   2193  C  CG1 . VAL B  1 149 ? -0.165  -42.518 15.962 1.00 19.71  ? 148 VAL B CG1 1 
ATOM   2194  C  CG2 . VAL B  1 149 ? 0.271   -43.337 18.281 1.00 17.49  ? 148 VAL B CG2 1 
ATOM   2195  N  N   . ILE B  1 150 ? 0.806   -39.413 15.847 1.00 20.69  ? 149 ILE B N   1 
ATOM   2196  C  CA  . ILE B  1 150 ? 0.535   -38.218 15.069 1.00 20.77  ? 149 ILE B CA  1 
ATOM   2197  C  C   . ILE B  1 150 ? -0.674  -38.513 14.186 1.00 21.68  ? 149 ILE B C   1 
ATOM   2198  O  O   . ILE B  1 150 ? -0.583  -39.348 13.284 1.00 22.76  ? 149 ILE B O   1 
ATOM   2199  C  CB  . ILE B  1 150 ? 1.776   -37.864 14.227 1.00 18.65  ? 149 ILE B CB  1 
ATOM   2200  C  CG1 . ILE B  1 150 ? 2.975   -37.503 15.108 1.00 18.94  ? 149 ILE B CG1 1 
ATOM   2201  C  CG2 . ILE B  1 150 ? 1.458   -36.772 13.216 1.00 17.34  ? 149 ILE B CG2 1 
ATOM   2202  C  CD1 . ILE B  1 150 ? 4.288   -37.521 14.363 1.00 19.24  ? 149 ILE B CD1 1 
ATOM   2203  N  N   . GLY B  1 151 ? -1.780  -37.806 14.443 1.00 21.60  ? 150 GLY B N   1 
ATOM   2204  C  CA  . GLY B  1 151 ? -3.055  -38.126 13.818 1.00 22.27  ? 150 GLY B CA  1 
ATOM   2205  C  C   . GLY B  1 151 ? -3.668  -36.954 13.053 1.00 23.66  ? 150 GLY B C   1 
ATOM   2206  O  O   . GLY B  1 151 ? -3.282  -35.800 13.248 1.00 24.13  ? 150 GLY B O   1 
ATOM   2207  N  N   . ILE B  1 152 ? -4.648  -37.281 12.202 1.00 24.59  ? 151 ILE B N   1 
ATOM   2208  C  CA  . ILE B  1 152 ? -5.303  -36.319 11.331 1.00 26.56  ? 151 ILE B CA  1 
ATOM   2209  C  C   . ILE B  1 152 ? -6.258  -35.486 12.172 1.00 28.71  ? 151 ILE B C   1 
ATOM   2210  O  O   . ILE B  1 152 ? -7.003  -36.055 12.985 1.00 26.21  ? 151 ILE B O   1 
ATOM   2211  C  CB  . ILE B  1 152 ? -6.053  -37.061 10.208 1.00 25.40  ? 151 ILE B CB  1 
ATOM   2212  C  CG1 . ILE B  1 152 ? -5.092  -37.849 9.312  1.00 24.84  ? 151 ILE B CG1 1 
ATOM   2213  C  CG2 . ILE B  1 152 ? -6.935  -36.103 9.427  1.00 23.72  ? 151 ILE B CG2 1 
ATOM   2214  C  CD1 . ILE B  1 152 ? -5.775  -38.949 8.539  1.00 24.50  ? 151 ILE B CD1 1 
ATOM   2215  N  N   . ALA B  1 153 ? -6.225  -34.158 11.976 1.00 35.81  ? 152 ALA B N   1 
ATOM   2216  C  CA  . ALA B  1 153 ? -7.100  -33.235 12.700 1.00 41.66  ? 152 ALA B CA  1 
ATOM   2217  C  C   . ALA B  1 153 ? -8.035  -32.535 11.714 1.00 45.94  ? 152 ALA B C   1 
ATOM   2218  O  O   . ALA B  1 153 ? -7.812  -32.615 10.504 1.00 40.09  ? 152 ALA B O   1 
ATOM   2219  C  CB  . ALA B  1 153 ? -6.271  -32.249 13.498 1.00 39.13  ? 152 ALA B CB  1 
ATOM   2220  N  N   . GLN B  1 154 ? -9.052  -31.848 12.240 1.00 56.61  ? 153 GLN B N   1 
ATOM   2221  C  CA  . GLN B  1 154 ? -10.074 -31.250 11.378 1.00 69.09  ? 153 GLN B CA  1 
ATOM   2222  C  C   . GLN B  1 154 ? -9.534  -30.020 10.631 1.00 70.84  ? 153 GLN B C   1 
ATOM   2223  O  O   . GLN B  1 154 ? -8.982  -29.093 11.210 1.00 69.77  ? 153 GLN B O   1 
ATOM   2224  C  CB  . GLN B  1 154 ? -11.371 -30.877 12.088 1.00 72.15  ? 153 GLN B CB  1 
ATOM   2225  C  CG  . GLN B  1 154 ? -12.401 -30.447 11.067 1.00 75.68  ? 153 GLN B CG  1 
ATOM   2226  C  CD  . GLN B  1 154 ? -13.695 -29.986 11.670 1.00 78.25  ? 153 GLN B CD  1 
ATOM   2227  O  OE1 . GLN B  1 154 ? -14.314 -30.655 12.495 1.00 81.58  ? 153 GLN B OE1 1 
ATOM   2228  N  NE2 . GLN B  1 154 ? -14.124 -28.819 11.237 1.00 76.53  ? 153 GLN B NE2 1 
ATOM   2229  O  OXT . GLN B  1 154 ? -9.657  -29.906 9.407  1.00 70.57  ? 153 GLN B OXT 1 
ATOM   2230  N  N   . ALA C  1 2   ? 10.387  8.444   69.080 1.00 56.52  ? 1   ALA C N   1 
ATOM   2231  C  CA  . ALA C  1 2   ? 10.715  9.852   69.305 1.00 56.28  ? 1   ALA C CA  1 
ATOM   2232  C  C   . ALA C  1 2   ? 11.495  10.422  68.116 1.00 54.82  ? 1   ALA C C   1 
ATOM   2233  O  O   . ALA C  1 2   ? 11.210  11.560  67.744 1.00 63.85  ? 1   ALA C O   1 
ATOM   2234  C  CB  . ALA C  1 2   ? 11.404  10.059  70.651 1.00 52.36  ? 1   ALA C CB  1 
ATOM   2235  N  N   . THR C  1 3   ? 12.558  9.726   67.673 1.00 43.22  ? 2   THR C N   1 
ATOM   2236  C  CA  . THR C  1 3   ? 13.502  10.310  66.731 1.00 38.54  ? 2   THR C CA  1 
ATOM   2237  C  C   . THR C  1 3   ? 13.316  9.657   65.357 1.00 33.41  ? 2   THR C C   1 
ATOM   2238  O  O   . THR C  1 3   ? 13.351  8.432   65.235 1.00 36.36  ? 2   THR C O   1 
ATOM   2239  C  CB  . THR C  1 3   ? 14.933  10.364  67.304 1.00 40.22  ? 2   THR C CB  1 
ATOM   2240  O  OG1 . THR C  1 3   ? 15.285  9.043   67.684 1.00 54.41  ? 2   THR C OG1 1 
ATOM   2241  C  CG2 . THR C  1 3   ? 15.042  11.201  68.561 1.00 38.72  ? 2   THR C CG2 1 
ATOM   2242  N  N   . LYS C  1 4   ? 13.086  10.478  64.325 1.00 27.85  ? 3   LYS C N   1 
ATOM   2243  C  CA  . LYS C  1 4   ? 13.008  10.010  62.947 1.00 25.73  ? 3   LYS C CA  1 
ATOM   2244  C  C   . LYS C  1 4   ? 14.169  10.581  62.138 1.00 26.85  ? 3   LYS C C   1 
ATOM   2245  O  O   . LYS C  1 4   ? 14.490  11.773  62.203 1.00 30.81  ? 3   LYS C O   1 
ATOM   2246  C  CB  . LYS C  1 4   ? 11.714  10.441  62.248 1.00 23.63  ? 3   LYS C CB  1 
ATOM   2247  C  CG  . LYS C  1 4   ? 10.465  9.611   62.490 0.50 22.62  ? 3   LYS C CG  1 
ATOM   2248  C  CD  . LYS C  1 4   ? 9.346   10.006  61.513 0.50 21.45  ? 3   LYS C CD  1 
ATOM   2249  C  CE  . LYS C  1 4   ? 9.283   9.086   60.314 0.50 20.11  ? 3   LYS C CE  1 
ATOM   2250  N  NZ  . LYS C  1 4   ? 8.798   9.813   59.120 0.50 19.16  ? 3   LYS C NZ  1 
ATOM   2251  N  N   . VAL C  1 5   ? 14.785  9.705   61.344 1.00 24.06  ? 4   VAL C N   1 
ATOM   2252  C  CA  . VAL C  1 5   ? 15.963  10.023  60.563 1.00 22.46  ? 4   VAL C CA  1 
ATOM   2253  C  C   . VAL C  1 5   ? 15.746  9.475   59.156 1.00 21.39  ? 4   VAL C C   1 
ATOM   2254  O  O   . VAL C  1 5   ? 14.967  8.557   58.955 1.00 21.38  ? 4   VAL C O   1 
ATOM   2255  C  CB  . VAL C  1 5   ? 17.195  9.407   61.245 1.00 22.85  ? 4   VAL C CB  1 
ATOM   2256  C  CG1 . VAL C  1 5   ? 18.408  9.370   60.335 1.00 22.71  ? 4   VAL C CG1 1 
ATOM   2257  C  CG2 . VAL C  1 5   ? 17.505  10.123  62.546 1.00 22.43  ? 4   VAL C CG2 1 
ATOM   2258  N  N   . VAL C  1 6   ? 16.419  10.054  58.170 1.00 19.77  ? 5   VAL C N   1 
ATOM   2259  C  CA  . VAL C  1 6   ? 16.213  9.598   56.808 1.00 18.93  ? 5   VAL C CA  1 
ATOM   2260  C  C   . VAL C  1 6   ? 17.529  9.642   56.041 1.00 19.32  ? 5   VAL C C   1 
ATOM   2261  O  O   . VAL C  1 6   ? 18.474  10.319  56.428 1.00 21.65  ? 5   VAL C O   1 
ATOM   2262  C  CB  . VAL C  1 6   ? 15.113  10.421  56.108 1.00 18.96  ? 5   VAL C CB  1 
ATOM   2263  C  CG1 . VAL C  1 6   ? 15.572  11.842  55.802 1.00 18.99  ? 5   VAL C CG1 1 
ATOM   2264  C  CG2 . VAL C  1 6   ? 14.639  9.745   54.836 1.00 18.17  ? 5   VAL C CG2 1 
ATOM   2265  N  N   . CYS C  1 7   ? 17.563  8.933   54.920 1.00 19.17  ? 6   CYS C N   1 
ATOM   2266  C  CA  . CYS C  1 7   ? 18.754  8.885   54.105 1.00 19.91  ? 6   CYS C CA  1 
ATOM   2267  C  C   . CYS C  1 7   ? 18.347  8.660   52.659 1.00 20.98  ? 6   CYS C C   1 
ATOM   2268  O  O   . CYS C  1 7   ? 17.575  7.752   52.376 1.00 21.95  ? 6   CYS C O   1 
ATOM   2269  C  CB  . CYS C  1 7   ? 19.616  7.735   54.580 1.00 20.67  ? 6   CYS C CB  1 
ATOM   2270  S  SG  . CYS C  1 7   ? 21.178  7.613   53.681 1.00 22.23  ? 6   CYS C SG  1 
ATOM   2271  N  N   . VAL C  1 8   ? 18.853  9.516   51.767 1.00 21.68  ? 7   VAL C N   1 
ATOM   2272  C  CA  . VAL C  1 8   ? 18.607  9.361   50.347 1.00 23.18  ? 7   VAL C CA  1 
ATOM   2273  C  C   . VAL C  1 8   ? 19.857  8.761   49.718 1.00 23.81  ? 7   VAL C C   1 
ATOM   2274  O  O   . VAL C  1 8   ? 20.926  9.352   49.805 1.00 26.05  ? 7   VAL C O   1 
ATOM   2275  C  CB  . VAL C  1 8   ? 18.263  10.713  49.689 1.00 23.52  ? 7   VAL C CB  1 
ATOM   2276  C  CG1 . VAL C  1 8   ? 18.164  10.595  48.171 1.00 23.29  ? 7   VAL C CG1 1 
ATOM   2277  C  CG2 . VAL C  1 8   ? 16.997  11.325  50.275 1.00 21.81  ? 7   VAL C CG2 1 
ATOM   2278  N  N   . LEU C  1 9   ? 19.721  7.594   49.085 1.00 23.80  ? 8   LEU C N   1 
ATOM   2279  C  CA  . LEU C  1 9   ? 20.873  6.943   48.487 1.00 24.66  ? 8   LEU C CA  1 
ATOM   2280  C  C   . LEU C  1 9   ? 20.967  7.337   47.019 1.00 25.74  ? 8   LEU C C   1 
ATOM   2281  O  O   . LEU C  1 9   ? 19.997  7.173   46.291 1.00 26.34  ? 8   LEU C O   1 
ATOM   2282  C  CB  . LEU C  1 9   ? 20.729  5.425   48.620 1.00 25.19  ? 8   LEU C CB  1 
ATOM   2283  C  CG  . LEU C  1 9   ? 20.562  4.887   50.036 1.00 26.14  ? 8   LEU C CG  1 
ATOM   2284  C  CD1 . LEU C  1 9   ? 20.117  3.435   49.991 1.00 27.01  ? 8   LEU C CD1 1 
ATOM   2285  C  CD2 . LEU C  1 9   ? 21.856  5.016   50.824 1.00 27.29  ? 8   LEU C CD2 1 
ATOM   2286  N  N   . LYS C  1 10  ? 22.136  7.858   46.615 1.00 27.70  ? 9   LYS C N   1 
ATOM   2287  C  CA  . LYS C  1 10  ? 22.476  8.120   45.225 1.00 29.65  ? 9   LYS C CA  1 
ATOM   2288  C  C   . LYS C  1 10  ? 23.890  7.621   44.957 1.00 29.44  ? 9   LYS C C   1 
ATOM   2289  O  O   . LYS C  1 10  ? 24.675  7.462   45.886 1.00 28.12  ? 9   LYS C O   1 
ATOM   2290  C  CB  . LYS C  1 10  ? 22.370  9.613   44.880 1.00 33.65  ? 9   LYS C CB  1 
ATOM   2291  C  CG  . LYS C  1 10  ? 20.965  10.097  44.566 1.00 41.19  ? 9   LYS C CG  1 
ATOM   2292  C  CD  . LYS C  1 10  ? 20.858  11.570  44.240 1.00 48.21  ? 9   LYS C CD  1 
ATOM   2293  C  CE  . LYS C  1 10  ? 19.417  11.970  44.423 1.00 48.76  ? 9   LYS C CE  1 
ATOM   2294  N  NZ  . LYS C  1 10  ? 19.299  13.093  45.379 1.00 52.41  ? 9   LYS C NZ  1 
ATOM   2295  N  N   . GLY C  1 11  ? 24.191  7.369   43.681 1.00 30.55  ? 10  GLY C N   1 
ATOM   2296  C  CA  . GLY C  1 11  ? 25.532  7.001   43.257 1.00 29.61  ? 10  GLY C CA  1 
ATOM   2297  C  C   . GLY C  1 11  ? 25.729  7.281   41.768 1.00 30.65  ? 10  GLY C C   1 
ATOM   2298  O  O   . GLY C  1 11  ? 24.908  7.946   41.149 1.00 28.90  ? 10  GLY C O   1 
ATOM   2299  N  N   . ASP C  1 12  ? 26.797  6.722   41.194 1.00 33.54  ? 11  ASP C N   1 
ATOM   2300  C  CA  . ASP C  1 12  ? 27.134  6.969   39.802 1.00 33.05  ? 11  ASP C CA  1 
ATOM   2301  C  C   . ASP C  1 12  ? 26.207  6.207   38.865 1.00 31.90  ? 11  ASP C C   1 
ATOM   2302  O  O   . ASP C  1 12  ? 26.005  6.624   37.733 1.00 31.93  ? 11  ASP C O   1 
ATOM   2303  C  CB  . ASP C  1 12  ? 28.582  6.588   39.515 1.00 37.69  ? 11  ASP C CB  1 
ATOM   2304  C  CG  . ASP C  1 12  ? 29.538  7.498   40.251 1.00 45.41  ? 11  ASP C CG  1 
ATOM   2305  O  OD1 . ASP C  1 12  ? 29.217  8.697   40.362 1.00 48.48  ? 11  ASP C OD1 1 
ATOM   2306  O  OD2 . ASP C  1 12  ? 30.574  6.998   40.729 1.00 51.94  ? 11  ASP C OD2 1 
ATOM   2307  N  N   . GLY C  1 13  ? 25.671  5.079   39.334 1.00 32.45  ? 12  GLY C N   1 
ATOM   2308  C  CA  . GLY C  1 13  ? 24.875  4.202   38.497 1.00 32.47  ? 12  GLY C CA  1 
ATOM   2309  C  C   . GLY C  1 13  ? 23.390  4.484   38.669 1.00 32.99  ? 12  GLY C C   1 
ATOM   2310  O  O   . GLY C  1 13  ? 23.016  5.564   39.113 1.00 35.66  ? 12  GLY C O   1 
ATOM   2311  N  N   . PRO C  1 14  ? 22.509  3.516   38.341 1.00 32.20  ? 13  PRO C N   1 
ATOM   2312  C  CA  . PRO C  1 14  ? 21.065  3.719   38.467 1.00 29.25  ? 13  PRO C CA  1 
ATOM   2313  C  C   . PRO C  1 14  ? 20.504  3.445   39.862 1.00 27.90  ? 13  PRO C C   1 
ATOM   2314  O  O   . PRO C  1 14  ? 19.302  3.570   40.069 1.00 26.18  ? 13  PRO C O   1 
ATOM   2315  C  CB  . PRO C  1 14  ? 20.524  2.689   37.458 1.00 29.63  ? 13  PRO C CB  1 
ATOM   2316  C  CG  . PRO C  1 14  ? 21.514  1.533   37.533 1.00 29.40  ? 13  PRO C CG  1 
ATOM   2317  C  CD  . PRO C  1 14  ? 22.855  2.173   37.833 1.00 31.50  ? 13  PRO C CD  1 
ATOM   2318  N  N   . VAL C  1 15  ? 21.358  3.082   40.823 1.00 28.37  ? 14  VAL C N   1 
ATOM   2319  C  CA  . VAL C  1 15  ? 20.838  2.704   42.124 1.00 29.16  ? 14  VAL C CA  1 
ATOM   2320  C  C   . VAL C  1 15  ? 20.457  3.963   42.894 1.00 31.38  ? 14  VAL C C   1 
ATOM   2321  O  O   . VAL C  1 15  ? 21.264  4.889   43.018 1.00 33.53  ? 14  VAL C O   1 
ATOM   2322  C  CB  . VAL C  1 15  ? 21.817  1.831   42.923 1.00 28.13  ? 14  VAL C CB  1 
ATOM   2323  C  CG1 . VAL C  1 15  ? 21.270  1.519   44.308 1.00 27.80  ? 14  VAL C CG1 1 
ATOM   2324  C  CG2 . VAL C  1 15  ? 22.150  0.556   42.170 1.00 27.20  ? 14  VAL C CG2 1 
ATOM   2325  N  N   . GLN C  1 16  ? 19.211  3.994   43.386 1.00 31.77  ? 15  GLN C N   1 
ATOM   2326  C  CA  . GLN C  1 16  ? 18.765  5.102   44.205 1.00 31.01  ? 15  GLN C CA  1 
ATOM   2327  C  C   . GLN C  1 16  ? 17.618  4.652   45.100 1.00 28.51  ? 15  GLN C C   1 
ATOM   2328  O  O   . GLN C  1 16  ? 16.913  3.702   44.773 1.00 30.01  ? 15  GLN C O   1 
ATOM   2329  C  CB  . GLN C  1 16  ? 18.402  6.314   43.357 1.00 33.83  ? 15  GLN C CB  1 
ATOM   2330  C  CG  . GLN C  1 16  ? 17.249  6.102   42.406 1.00 41.20  ? 15  GLN C CG  1 
ATOM   2331  C  CD  . GLN C  1 16  ? 16.870  7.408   41.739 1.00 49.03  ? 15  GLN C CD  1 
ATOM   2332  O  OE1 . GLN C  1 16  ? 17.468  8.472   41.958 1.00 52.26  ? 15  GLN C OE1 1 
ATOM   2333  N  NE2 . GLN C  1 16  ? 15.852  7.342   40.899 1.00 54.59  ? 15  GLN C NE2 1 
ATOM   2334  N  N   . GLY C  1 17  ? 17.456  5.337   46.240 1.00 24.28  ? 16  GLY C N   1 
ATOM   2335  C  CA  . GLY C  1 17  ? 16.431  4.937   47.189 1.00 21.79  ? 16  GLY C CA  1 
ATOM   2336  C  C   . GLY C  1 17  ? 16.362  5.857   48.395 1.00 20.89  ? 16  GLY C C   1 
ATOM   2337  O  O   . GLY C  1 17  ? 17.185  6.758   48.555 1.00 22.08  ? 16  GLY C O   1 
ATOM   2338  N  N   . ILE C  1 18  ? 15.325  5.647   49.202 1.00 19.03  ? 17  ILE C N   1 
ATOM   2339  C  CA  . ILE C  1 18  ? 15.087  6.423   50.406 1.00 18.58  ? 17  ILE C CA  1 
ATOM   2340  C  C   . ILE C  1 18  ? 14.964  5.425   51.546 1.00 18.07  ? 17  ILE C C   1 
ATOM   2341  O  O   . ILE C  1 18  ? 14.206  4.473   51.442 1.00 17.86  ? 17  ILE C O   1 
ATOM   2342  C  CB  . ILE C  1 18  ? 13.788  7.241   50.255 1.00 18.20  ? 17  ILE C CB  1 
ATOM   2343  C  CG1 . ILE C  1 18  ? 13.837  8.210   49.069 1.00 19.14  ? 17  ILE C CG1 1 
ATOM   2344  C  CG2 . ILE C  1 18  ? 13.435  7.930   51.552 1.00 17.46  ? 17  ILE C CG2 1 
ATOM   2345  C  CD1 . ILE C  1 18  ? 12.526  8.904   48.815 1.00 18.79  ? 17  ILE C CD1 1 
ATOM   2346  N  N   . ILE C  1 19  ? 15.702  5.634   52.636 1.00 18.00  ? 18  ILE C N   1 
ATOM   2347  C  CA  . ILE C  1 19  ? 15.604  4.722   53.766 1.00 18.06  ? 18  ILE C CA  1 
ATOM   2348  C  C   . ILE C  1 19  ? 15.299  5.531   55.008 1.00 18.51  ? 18  ILE C C   1 
ATOM   2349  O  O   . ILE C  1 19  ? 15.998  6.496   55.281 1.00 20.72  ? 18  ILE C O   1 
ATOM   2350  C  CB  . ILE C  1 19  ? 16.902  3.890   53.947 1.00 16.78  ? 18  ILE C CB  1 
ATOM   2351  C  CG1 . ILE C  1 19  ? 17.248  3.050   52.715 1.00 14.95  ? 18  ILE C CG1 1 
ATOM   2352  C  CG2 . ILE C  1 19  ? 16.851  3.070   55.245 1.00 16.55  ? 18  ILE C CG2 1 
ATOM   2353  C  CD1 . ILE C  1 19  ? 16.234  1.966   52.439 1.00 14.75  ? 18  ILE C CD1 1 
ATOM   2354  N  N   . ASN C  1 20  ? 14.277  5.111   55.757 1.00 18.63  ? 19  ASN C N   1 
ATOM   2355  C  CA  . ASN C  1 20  ? 13.886  5.790   56.983 1.00 19.93  ? 19  ASN C CA  1 
ATOM   2356  C  C   . ASN C  1 20  ? 14.385  5.020   58.194 1.00 21.02  ? 19  ASN C C   1 
ATOM   2357  O  O   . ASN C  1 20  ? 14.463  3.798   58.154 1.00 23.86  ? 19  ASN C O   1 
ATOM   2358  C  CB  . ASN C  1 20  ? 12.373  5.923   57.087 1.00 19.18  ? 19  ASN C CB  1 
ATOM   2359  C  CG  . ASN C  1 20  ? 11.791  6.547   55.838 1.00 19.72  ? 19  ASN C CG  1 
ATOM   2360  O  OD1 . ASN C  1 20  ? 11.322  5.835   54.955 1.00 19.26  ? 19  ASN C OD1 1 
ATOM   2361  N  ND2 . ASN C  1 20  ? 11.868  7.861   55.722 1.00 18.40  ? 19  ASN C ND2 1 
ATOM   2362  N  N   . PHE C  1 21  ? 14.700  5.750   59.265 1.00 21.81  ? 20  PHE C N   1 
ATOM   2363  C  CA  . PHE C  1 21  ? 15.082  5.153   60.533 1.00 24.15  ? 20  PHE C CA  1 
ATOM   2364  C  C   . PHE C  1 21  ? 14.220  5.758   61.626 1.00 26.41  ? 20  PHE C C   1 
ATOM   2365  O  O   . PHE C  1 21  ? 14.052  6.966   61.672 1.00 27.02  ? 20  PHE C O   1 
ATOM   2366  C  CB  . PHE C  1 21  ? 16.534  5.481   60.888 1.00 22.90  ? 20  PHE C CB  1 
ATOM   2367  C  CG  . PHE C  1 21  ? 17.563  4.959   59.913 1.00 23.92  ? 20  PHE C CG  1 
ATOM   2368  C  CD1 . PHE C  1 21  ? 17.687  5.512   58.643 1.00 24.03  ? 20  PHE C CD1 1 
ATOM   2369  C  CD2 . PHE C  1 21  ? 18.431  3.938   60.274 1.00 23.06  ? 20  PHE C CD2 1 
ATOM   2370  C  CE1 . PHE C  1 21  ? 18.646  5.041   57.758 1.00 23.25  ? 20  PHE C CE1 1 
ATOM   2371  C  CE2 . PHE C  1 21  ? 19.399  3.481   59.394 1.00 22.92  ? 20  PHE C CE2 1 
ATOM   2372  C  CZ  . PHE C  1 21  ? 19.508  4.032   58.131 1.00 23.58  ? 20  PHE C CZ  1 
ATOM   2373  N  N   . GLU C  1 22  ? 13.670  4.918   62.502 1.00 30.75  ? 21  GLU C N   1 
ATOM   2374  C  CA  . GLU C  1 22  ? 12.837  5.415   63.583 1.00 33.90  ? 21  GLU C CA  1 
ATOM   2375  C  C   . GLU C  1 22  ? 13.182  4.673   64.869 1.00 33.82  ? 21  GLU C C   1 
ATOM   2376  O  O   . GLU C  1 22  ? 13.407  3.468   64.822 1.00 36.92  ? 21  GLU C O   1 
ATOM   2377  C  CB  . GLU C  1 22  ? 11.367  5.261   63.191 1.00 37.82  ? 21  GLU C CB  1 
ATOM   2378  C  CG  . GLU C  1 22  ? 10.432  6.067   64.081 1.00 45.11  ? 21  GLU C CG  1 
ATOM   2379  C  CD  . GLU C  1 22  ? 8.957   5.946   63.726 1.00 52.36  ? 21  GLU C CD  1 
ATOM   2380  O  OE1 . GLU C  1 22  ? 8.597   6.228   62.562 1.00 54.73  ? 21  GLU C OE1 1 
ATOM   2381  O  OE2 . GLU C  1 22  ? 8.163   5.513   64.614 1.00 62.41  ? 21  GLU C OE2 1 
ATOM   2382  N  N   . GLN C  1 23  ? 13.219  5.397   65.994 1.00 31.96  ? 22  GLN C N   1 
ATOM   2383  C  CA  . GLN C  1 23  ? 13.586  4.818   67.276 1.00 33.10  ? 22  GLN C CA  1 
ATOM   2384  C  C   . GLN C  1 23  ? 12.663  5.359   68.362 1.00 37.45  ? 22  GLN C C   1 
ATOM   2385  O  O   . GLN C  1 23  ? 12.800  6.525   68.742 1.00 38.78  ? 22  GLN C O   1 
ATOM   2386  C  CB  . GLN C  1 23  ? 15.049  5.134   67.597 1.00 31.57  ? 22  GLN C CB  1 
ATOM   2387  C  CG  . GLN C  1 23  ? 15.587  4.387   68.814 1.00 33.43  ? 22  GLN C CG  1 
ATOM   2388  C  CD  . GLN C  1 23  ? 17.015  4.756   69.140 1.00 35.63  ? 22  GLN C CD  1 
ATOM   2389  O  OE1 . GLN C  1 23  ? 17.442  5.907   68.981 1.00 37.22  ? 22  GLN C OE1 1 
ATOM   2390  N  NE2 . GLN C  1 23  ? 17.753  3.784   69.656 1.00 35.57  ? 22  GLN C NE2 1 
ATOM   2391  N  N   . LYS C  1 24  ? 11.745  4.522   68.879 1.00 43.57  ? 23  LYS C N   1 
ATOM   2392  C  CA  . LYS C  1 24  ? 10.757  4.962   69.856 1.00 47.11  ? 23  LYS C CA  1 
ATOM   2393  C  C   . LYS C  1 24  ? 11.401  5.281   71.211 1.00 49.43  ? 23  LYS C C   1 
ATOM   2394  O  O   . LYS C  1 24  ? 11.192  6.365   71.739 1.00 52.57  ? 23  LYS C O   1 
ATOM   2395  C  CB  . LYS C  1 24  ? 9.521   4.054   69.898 1.00 46.49  ? 23  LYS C CB  1 
ATOM   2396  C  CG  . LYS C  1 24  ? 8.546   4.234   68.734 0.40 45.45  ? 23  LYS C CG  1 
ATOM   2397  C  CD  . LYS C  1 24  ? 7.570   3.079   68.532 0.40 45.52  ? 23  LYS C CD  1 
ATOM   2398  C  CE  . LYS C  1 24  ? 7.009   2.978   67.127 0.40 44.05  ? 23  LYS C CE  1 
ATOM   2399  N  NZ  . LYS C  1 24  ? 5.608   2.501   67.150 0.40 43.84  ? 23  LYS C NZ  1 
ATOM   2400  N  N   . GLU C  1 25  ? 12.178  4.356   71.768 1.00 55.95  ? 24  GLU C N   1 
ATOM   2401  C  CA  . GLU C  1 25  ? 12.801  4.568   73.074 1.00 58.86  ? 24  GLU C CA  1 
ATOM   2402  C  C   . GLU C  1 25  ? 14.272  4.859   72.866 1.00 58.85  ? 24  GLU C C   1 
ATOM   2403  O  O   . GLU C  1 25  ? 14.850  4.421   71.898 1.00 63.09  ? 24  GLU C O   1 
ATOM   2404  C  CB  . GLU C  1 25  ? 12.644  3.353   74.005 1.00 65.67  ? 24  GLU C CB  1 
ATOM   2405  C  CG  . GLU C  1 25  ? 11.267  2.715   74.019 1.00 78.20  ? 24  GLU C CG  1 
ATOM   2406  C  CD  . GLU C  1 25  ? 10.171  3.510   74.711 1.00 84.51  ? 24  GLU C CD  1 
ATOM   2407  O  OE1 . GLU C  1 25  ? 10.484  4.450   75.482 1.00 85.56  ? 24  GLU C OE1 1 
ATOM   2408  O  OE2 . GLU C  1 25  ? 8.999   3.188   74.474 1.00 87.96  ? 24  GLU C OE2 1 
ATOM   2409  N  N   . SER C  1 26  ? 14.905  5.583   73.811 1.00 59.62  ? 25  SER C N   1 
ATOM   2410  C  CA  . SER C  1 26  ? 16.348  5.775   73.774 1.00 62.26  ? 25  SER C CA  1 
ATOM   2411  C  C   . SER C  1 26  ? 17.031  4.437   74.031 1.00 63.08  ? 25  SER C C   1 
ATOM   2412  O  O   . SER C  1 26  ? 16.696  3.690   74.952 1.00 64.74  ? 25  SER C O   1 
ATOM   2413  C  CB  . SER C  1 26  ? 16.862  6.817   74.704 1.00 61.44  ? 25  SER C CB  1 
ATOM   2414  O  OG  . SER C  1 26  ? 16.004  7.932   74.753 1.00 67.15  ? 25  SER C OG  1 
ATOM   2415  N  N   . ASN C  1 27  ? 17.908  4.044   73.120 1.00 59.02  ? 26  ASN C N   1 
ATOM   2416  C  CA  . ASN C  1 27  ? 18.626  2.790   73.278 1.00 54.08  ? 26  ASN C CA  1 
ATOM   2417  C  C   . ASN C  1 27  ? 17.672  1.612   73.150 1.00 51.54  ? 26  ASN C C   1 
ATOM   2418  O  O   . ASN C  1 27  ? 18.130  0.473   73.230 1.00 53.51  ? 26  ASN C O   1 
ATOM   2419  C  CB  . ASN C  1 27  ? 19.535  2.722   74.511 0.20 49.91  ? 26  ASN C CB  1 
ATOM   2420  C  CG  . ASN C  1 27  ? 20.598  3.805   74.529 0.20 46.93  ? 26  ASN C CG  1 
ATOM   2421  O  OD1 . ASN C  1 27  ? 21.101  4.209   73.484 0.20 43.72  ? 26  ASN C OD1 1 
ATOM   2422  N  ND2 . ASN C  1 27  ? 20.936  4.303   75.709 0.20 46.04  ? 26  ASN C ND2 1 
ATOM   2423  N  N   . GLY C  1 28  ? 16.425  1.865   72.694 1.00 45.09  ? 27  GLY C N   1 
ATOM   2424  C  CA  . GLY C  1 28  ? 15.585  0.793   72.161 1.00 37.87  ? 27  GLY C CA  1 
ATOM   2425  C  C   . GLY C  1 28  ? 15.861  0.509   70.681 1.00 37.56  ? 27  GLY C C   1 
ATOM   2426  O  O   . GLY C  1 28  ? 16.713  1.158   70.068 1.00 41.30  ? 27  GLY C O   1 
ATOM   2427  N  N   . PRO C  1 29  ? 15.186  -0.482  70.072 1.00 34.74  ? 28  PRO C N   1 
ATOM   2428  C  CA  . PRO C  1 29  ? 15.489  -0.896  68.701 1.00 32.44  ? 28  PRO C CA  1 
ATOM   2429  C  C   . PRO C  1 29  ? 15.156  0.191   67.679 1.00 29.88  ? 28  PRO C C   1 
ATOM   2430  O  O   . PRO C  1 29  ? 14.341  1.068   67.956 1.00 29.78  ? 28  PRO C O   1 
ATOM   2431  C  CB  . PRO C  1 29  ? 14.575  -2.115  68.502 1.00 35.40  ? 28  PRO C CB  1 
ATOM   2432  C  CG  . PRO C  1 29  ? 13.408  -1.863  69.445 1.00 34.92  ? 28  PRO C CG  1 
ATOM   2433  C  CD  . PRO C  1 29  ? 14.065  -1.231  70.662 1.00 37.02  ? 28  PRO C CD  1 
ATOM   2434  N  N   . VAL C  1 30  ? 15.805  0.116   66.511 1.00 27.96  ? 29  VAL C N   1 
ATOM   2435  C  CA  . VAL C  1 30  ? 15.623  1.067   65.429 1.00 26.94  ? 29  VAL C CA  1 
ATOM   2436  C  C   . VAL C  1 30  ? 14.945  0.351   64.263 1.00 27.76  ? 29  VAL C C   1 
ATOM   2437  O  O   . VAL C  1 30  ? 15.445  -0.670  63.794 1.00 30.81  ? 29  VAL C O   1 
ATOM   2438  C  CB  . VAL C  1 30  ? 16.969  1.669   64.977 1.00 26.38  ? 29  VAL C CB  1 
ATOM   2439  C  CG1 . VAL C  1 30  ? 16.782  2.670   63.850 1.00 25.59  ? 29  VAL C CG1 1 
ATOM   2440  C  CG2 . VAL C  1 30  ? 17.741  2.295   66.123 1.00 25.15  ? 29  VAL C CG2 1 
ATOM   2441  N  N   . LYS C  1 31  ? 13.816  0.888   63.797 1.00 25.47  ? 30  LYS C N   1 
ATOM   2442  C  CA  . LYS C  1 31  ? 13.174  0.329   62.619 1.00 25.74  ? 30  LYS C CA  1 
ATOM   2443  C  C   . LYS C  1 31  ? 13.798  0.986   61.392 1.00 25.77  ? 30  LYS C C   1 
ATOM   2444  O  O   . LYS C  1 31  ? 13.878  2.215   61.311 1.00 26.39  ? 30  LYS C O   1 
ATOM   2445  C  CB  . LYS C  1 31  ? 11.654  0.571   62.640 1.00 27.47  ? 30  LYS C CB  1 
ATOM   2446  C  CG  . LYS C  1 31  ? 10.791  -0.290  63.540 1.00 31.36  ? 30  LYS C CG  1 
ATOM   2447  C  CD  . LYS C  1 31  ? 9.348   -0.325  63.105 1.00 36.20  ? 30  LYS C CD  1 
ATOM   2448  C  CE  . LYS C  1 31  ? 8.539   -0.844  64.258 1.00 38.62  ? 30  LYS C CE  1 
ATOM   2449  N  NZ  . LYS C  1 31  ? 7.318   -0.026  64.394 1.00 39.77  ? 30  LYS C NZ  1 
ATOM   2450  N  N   . VAL C  1 32  ? 14.273  0.172   60.451 1.00 23.87  ? 31  VAL C N   1 
ATOM   2451  C  CA  . VAL C  1 32  ? 14.867  0.695   59.233 1.00 23.24  ? 31  VAL C CA  1 
ATOM   2452  C  C   . VAL C  1 32  ? 14.020  0.215   58.062 1.00 24.37  ? 31  VAL C C   1 
ATOM   2453  O  O   . VAL C  1 32  ? 13.937  -0.988  57.815 1.00 28.33  ? 31  VAL C O   1 
ATOM   2454  C  CB  . VAL C  1 32  ? 16.322  0.206   59.085 1.00 22.18  ? 31  VAL C CB  1 
ATOM   2455  C  CG1 . VAL C  1 32  ? 17.000  0.804   57.856 1.00 21.31  ? 31  VAL C CG1 1 
ATOM   2456  C  CG2 . VAL C  1 32  ? 17.125  0.486   60.337 1.00 21.97  ? 31  VAL C CG2 1 
ATOM   2457  N  N   . TRP C  1 33  ? 13.389  1.138   57.336 1.00 23.97  ? 32  TRP C N   1 
ATOM   2458  C  CA  . TRP C  1 33  ? 12.582  0.697   56.207 1.00 24.15  ? 32  TRP C CA  1 
ATOM   2459  C  C   . TRP C  1 33  ? 12.640  1.694   55.061 1.00 23.74  ? 32  TRP C C   1 
ATOM   2460  O  O   . TRP C  1 33  ? 12.907  2.873   55.259 1.00 26.87  ? 32  TRP C O   1 
ATOM   2461  C  CB  . TRP C  1 33  ? 11.127  0.454   56.624 1.00 25.81  ? 32  TRP C CB  1 
ATOM   2462  C  CG  . TRP C  1 33  ? 10.318  1.713   56.722 1.00 27.60  ? 32  TRP C CG  1 
ATOM   2463  C  CD1 . TRP C  1 33  ? 9.458   2.231   55.789 1.00 28.62  ? 32  TRP C CD1 1 
ATOM   2464  C  CD2 . TRP C  1 33  ? 10.313  2.631   57.828 1.00 27.85  ? 32  TRP C CD2 1 
ATOM   2465  N  NE1 . TRP C  1 33  ? 8.913   3.406   56.245 1.00 30.65  ? 32  TRP C NE1 1 
ATOM   2466  C  CE2 . TRP C  1 33  ? 9.417   3.673   57.496 1.00 28.97  ? 32  TRP C CE2 1 
ATOM   2467  C  CE3 . TRP C  1 33  ? 10.982  2.674   59.057 1.00 28.10  ? 32  TRP C CE3 1 
ATOM   2468  C  CZ2 . TRP C  1 33  ? 9.177   4.743   58.358 1.00 28.47  ? 32  TRP C CZ2 1 
ATOM   2469  C  CZ3 . TRP C  1 33  ? 10.743  3.733   59.910 1.00 29.07  ? 32  TRP C CZ3 1 
ATOM   2470  C  CH2 . TRP C  1 33  ? 9.849   4.749   59.566 1.00 28.95  ? 32  TRP C CH2 1 
ATOM   2471  N  N   . GLY C  1 34  ? 12.334  1.200   53.863 1.00 21.17  ? 33  GLY C N   1 
ATOM   2472  C  CA  . GLY C  1 34  ? 12.222  2.043   52.691 1.00 21.00  ? 33  GLY C CA  1 
ATOM   2473  C  C   . GLY C  1 34  ? 12.407  1.218   51.432 1.00 21.50  ? 33  GLY C C   1 
ATOM   2474  O  O   . GLY C  1 34  ? 12.276  0.008   51.462 1.00 24.84  ? 33  GLY C O   1 
ATOM   2475  N  N   . SER C  1 35  ? 12.765  1.872   50.339 1.00 22.21  ? 34  SER C N   1 
ATOM   2476  C  CA  . SER C  1 35  ? 12.814  1.188   49.069 1.00 22.48  ? 34  SER C CA  1 
ATOM   2477  C  C   . SER C  1 35  ? 14.065  1.617   48.294 1.00 22.78  ? 34  SER C C   1 
ATOM   2478  O  O   . SER C  1 35  ? 14.444  2.781   48.323 1.00 22.57  ? 34  SER C O   1 
ATOM   2479  C  CB  . SER C  1 35  ? 11.541  1.491   48.362 1.00 22.04  ? 34  SER C CB  1 
ATOM   2480  O  OG  . SER C  1 35  ? 11.614  1.078   47.015 1.00 25.49  ? 34  SER C OG  1 
ATOM   2481  N  N   . ILE C  1 36  ? 14.746  0.665   47.643 1.00 21.49  ? 35  ILE C N   1 
ATOM   2482  C  CA  . ILE C  1 36  ? 15.858  0.980   46.759 1.00 21.12  ? 35  ILE C CA  1 
ATOM   2483  C  C   . ILE C  1 36  ? 15.567  0.363   45.400 1.00 21.68  ? 35  ILE C C   1 
ATOM   2484  O  O   . ILE C  1 36  ? 15.118  -0.775  45.332 1.00 21.95  ? 35  ILE C O   1 
ATOM   2485  C  CB  . ILE C  1 36  ? 17.184  0.442   47.337 1.00 20.16  ? 35  ILE C CB  1 
ATOM   2486  C  CG1 . ILE C  1 36  ? 17.351  0.814   48.810 1.00 18.25  ? 35  ILE C CG1 1 
ATOM   2487  C  CG2 . ILE C  1 36  ? 18.367  0.889   46.486 1.00 19.39  ? 35  ILE C CG2 1 
ATOM   2488  C  CD1 . ILE C  1 36  ? 18.526  0.149   49.472 1.00 18.47  ? 35  ILE C CD1 1 
ATOM   2489  N  N   . LYS C  1 37  ? 15.833  1.109   44.329 1.00 23.44  ? 36  LYS C N   1 
ATOM   2490  C  CA  . LYS C  1 37  ? 15.574  0.598   42.992 1.00 25.58  ? 36  LYS C CA  1 
ATOM   2491  C  C   . LYS C  1 37  ? 16.863  0.619   42.174 1.00 25.14  ? 36  LYS C C   1 
ATOM   2492  O  O   . LYS C  1 37  ? 17.838  1.258   42.565 1.00 24.57  ? 36  LYS C O   1 
ATOM   2493  C  CB  . LYS C  1 37  ? 14.422  1.370   42.338 1.00 30.07  ? 36  LYS C CB  1 
ATOM   2494  C  CG  . LYS C  1 37  ? 14.708  2.842   42.033 1.00 33.19  ? 36  LYS C CG  1 
ATOM   2495  C  CD  . LYS C  1 37  ? 13.888  3.476   40.931 1.00 37.98  ? 36  LYS C CD  1 
ATOM   2496  C  CE  . LYS C  1 37  ? 13.649  4.960   41.168 1.00 40.68  ? 36  LYS C CE  1 
ATOM   2497  N  NZ  . LYS C  1 37  ? 12.620  5.525   40.260 1.00 40.76  ? 36  LYS C NZ  1 
ATOM   2498  N  N   . GLY C  1 38  ? 16.854  -0.115  41.052 1.00 25.99  ? 37  GLY C N   1 
ATOM   2499  C  CA  . GLY C  1 38  ? 17.976  -0.171  40.126 1.00 26.76  ? 37  GLY C CA  1 
ATOM   2500  C  C   . GLY C  1 38  ? 19.064  -1.179  40.517 1.00 27.08  ? 37  GLY C C   1 
ATOM   2501  O  O   . GLY C  1 38  ? 20.161  -1.146  39.963 1.00 25.24  ? 37  GLY C O   1 
ATOM   2502  N  N   . LEU C  1 39  ? 18.756  -2.078  41.464 1.00 27.73  ? 38  LEU C N   1 
ATOM   2503  C  CA  . LEU C  1 39  ? 19.711  -3.076  41.920 1.00 28.50  ? 38  LEU C CA  1 
ATOM   2504  C  C   . LEU C  1 39  ? 19.603  -4.322  41.046 1.00 29.11  ? 38  LEU C C   1 
ATOM   2505  O  O   . LEU C  1 39  ? 18.551  -4.578  40.456 1.00 28.94  ? 38  LEU C O   1 
ATOM   2506  C  CB  . LEU C  1 39  ? 19.404  -3.436  43.376 1.00 26.07  ? 38  LEU C CB  1 
ATOM   2507  C  CG  . LEU C  1 39  ? 19.741  -2.354  44.396 1.00 25.24  ? 38  LEU C CG  1 
ATOM   2508  C  CD1 . LEU C  1 39  ? 19.056  -2.647  45.722 1.00 24.74  ? 38  LEU C CD1 1 
ATOM   2509  C  CD2 . LEU C  1 39  ? 21.252  -2.240  44.585 1.00 24.78  ? 38  LEU C CD2 1 
ATOM   2510  N  N   . THR C  1 40  ? 20.694  -5.100  40.984 1.00 29.55  ? 39  THR C N   1 
ATOM   2511  C  CA  . THR C  1 40  ? 20.624  -6.422  40.378 1.00 28.81  ? 39  THR C CA  1 
ATOM   2512  C  C   . THR C  1 40  ? 19.879  -7.342  41.334 1.00 30.06  ? 39  THR C C   1 
ATOM   2513  O  O   . THR C  1 40  ? 19.956  -7.159  42.551 1.00 31.29  ? 39  THR C O   1 
ATOM   2514  C  CB  . THR C  1 40  ? 22.011  -6.999  40.084 1.00 27.21  ? 39  THR C CB  1 
ATOM   2515  O  OG1 . THR C  1 40  ? 22.751  -6.842  41.291 1.00 26.81  ? 39  THR C OG1 1 
ATOM   2516  C  CG2 . THR C  1 40  ? 22.727  -6.299  38.952 1.00 26.86  ? 39  THR C CG2 1 
ATOM   2517  N  N   . GLU C  1 41  ? 19.158  -8.326  40.774 1.00 30.63  ? 40  GLU C N   1 
ATOM   2518  C  CA  . GLU C  1 41  ? 18.384  -9.240  41.591 1.00 29.51  ? 40  GLU C CA  1 
ATOM   2519  C  C   . GLU C  1 41  ? 19.314  -9.912  42.602 1.00 28.26  ? 40  GLU C C   1 
ATOM   2520  O  O   . GLU C  1 41  ? 20.457  -10.234 42.271 1.00 28.79  ? 40  GLU C O   1 
ATOM   2521  C  CB  . GLU C  1 41  ? 17.698  -10.274 40.701 1.00 32.66  ? 40  GLU C CB  1 
ATOM   2522  C  CG  . GLU C  1 41  ? 16.786  -11.191 41.504 1.00 37.41  ? 40  GLU C CG  1 
ATOM   2523  C  CD  . GLU C  1 41  ? 15.985  -12.224 40.743 1.00 37.36  ? 40  GLU C CD  1 
ATOM   2524  O  OE1 . GLU C  1 41  ? 16.226  -12.385 39.542 1.00 40.79  ? 40  GLU C OE1 1 
ATOM   2525  O  OE2 . GLU C  1 41  ? 15.121  -12.852 41.361 1.00 35.36  ? 40  GLU C OE2 1 
ATOM   2526  N  N   . GLY C  1 42  ? 18.831  -10.090 43.836 1.00 25.48  ? 41  GLY C N   1 
ATOM   2527  C  CA  . GLY C  1 42  ? 19.599  -10.824 44.825 1.00 26.84  ? 41  GLY C CA  1 
ATOM   2528  C  C   . GLY C  1 42  ? 20.034  -9.967  46.015 1.00 28.21  ? 41  GLY C C   1 
ATOM   2529  O  O   . GLY C  1 42  ? 19.503  -8.876  46.241 1.00 29.48  ? 41  GLY C O   1 
ATOM   2530  N  N   . LEU C  1 43  ? 21.008  -10.499 46.774 1.00 26.80  ? 42  LEU C N   1 
ATOM   2531  C  CA  . LEU C  1 43  ? 21.441  -9.924  48.041 1.00 25.49  ? 42  LEU C CA  1 
ATOM   2532  C  C   . LEU C  1 43  ? 22.440  -8.803  47.785 1.00 25.25  ? 42  LEU C C   1 
ATOM   2533  O  O   . LEU C  1 43  ? 23.287  -8.916  46.898 1.00 23.40  ? 42  LEU C O   1 
ATOM   2534  C  CB  . LEU C  1 43  ? 22.095  -11.008 48.902 1.00 25.08  ? 42  LEU C CB  1 
ATOM   2535  C  CG  . LEU C  1 43  ? 21.151  -12.112 49.383 1.00 23.97  ? 42  LEU C CG  1 
ATOM   2536  C  CD1 . LEU C  1 43  ? 21.908  -13.330 49.872 1.00 23.08  ? 42  LEU C CD1 1 
ATOM   2537  C  CD2 . LEU C  1 43  ? 20.169  -11.561 50.400 1.00 23.95  ? 42  LEU C CD2 1 
ATOM   2538  N  N   . HIS C  1 44  ? 22.322  -7.730  48.589 1.00 24.39  ? 43  HIS C N   1 
ATOM   2539  C  CA  . HIS C  1 44  ? 23.258  -6.617  48.574 1.00 22.24  ? 43  HIS C CA  1 
ATOM   2540  C  C   . HIS C  1 44  ? 23.588  -6.210  50.004 1.00 22.51  ? 43  HIS C C   1 
ATOM   2541  O  O   . HIS C  1 44  ? 22.701  -6.083  50.854 1.00 23.14  ? 43  HIS C O   1 
ATOM   2542  C  CB  . HIS C  1 44  ? 22.692  -5.443  47.786 1.00 20.33  ? 43  HIS C CB  1 
ATOM   2543  C  CG  . HIS C  1 44  ? 22.514  -5.719  46.332 1.00 20.77  ? 43  HIS C CG  1 
ATOM   2544  N  ND1 . HIS C  1 44  ? 23.472  -5.377  45.390 1.00 21.45  ? 43  HIS C ND1 1 
ATOM   2545  C  CD2 . HIS C  1 44  ? 21.486  -6.274  45.651 1.00 20.32  ? 43  HIS C CD2 1 
ATOM   2546  C  CE1 . HIS C  1 44  ? 23.040  -5.707  44.184 1.00 21.88  ? 43  HIS C CE1 1 
ATOM   2547  N  NE2 . HIS C  1 44  ? 21.811  -6.258  44.324 1.00 20.97  ? 43  HIS C NE2 1 
ATOM   2548  N  N   . GLY C  1 45  ? 24.891  -6.043  50.261 1.00 22.02  ? 44  GLY C N   1 
ATOM   2549  C  CA  . GLY C  1 45  ? 25.374  -5.616  51.561 1.00 21.59  ? 44  GLY C CA  1 
ATOM   2550  C  C   . GLY C  1 45  ? 24.876  -4.214  51.896 1.00 22.40  ? 44  GLY C C   1 
ATOM   2551  O  O   . GLY C  1 45  ? 24.798  -3.344  51.031 1.00 24.32  ? 44  GLY C O   1 
ATOM   2552  N  N   . PHE C  1 46  ? 24.563  -4.007  53.173 1.00 21.36  ? 45  PHE C N   1 
ATOM   2553  C  CA  . PHE C  1 46  ? 23.841  -2.830  53.614 1.00 19.87  ? 45  PHE C CA  1 
ATOM   2554  C  C   . PHE C  1 46  ? 24.449  -2.392  54.937 1.00 19.82  ? 45  PHE C C   1 
ATOM   2555  O  O   . PHE C  1 46  ? 24.239  -3.053  55.947 1.00 19.92  ? 45  PHE C O   1 
ATOM   2556  C  CB  . PHE C  1 46  ? 22.376  -3.219  53.794 1.00 19.14  ? 45  PHE C CB  1 
ATOM   2557  C  CG  . PHE C  1 46  ? 21.390  -2.092  53.955 1.00 19.03  ? 45  PHE C CG  1 
ATOM   2558  C  CD1 . PHE C  1 46  ? 21.138  -1.220  52.905 1.00 18.51  ? 45  PHE C CD1 1 
ATOM   2559  C  CD2 . PHE C  1 46  ? 20.664  -1.947  55.135 1.00 18.59  ? 45  PHE C CD2 1 
ATOM   2560  C  CE1 . PHE C  1 46  ? 20.199  -0.204  53.036 1.00 18.06  ? 45  PHE C CE1 1 
ATOM   2561  C  CE2 . PHE C  1 46  ? 19.722  -0.936  55.266 1.00 18.72  ? 45  PHE C CE2 1 
ATOM   2562  C  CZ  . PHE C  1 46  ? 19.491  -0.070  54.209 1.00 18.53  ? 45  PHE C CZ  1 
ATOM   2563  N  N   . HIS C  1 47  ? 25.215  -1.295  54.916 1.00 20.75  ? 46  HIS C N   1 
ATOM   2564  C  CA  . HIS C  1 47  ? 25.992  -0.923  56.086 1.00 21.54  ? 46  HIS C CA  1 
ATOM   2565  C  C   . HIS C  1 47  ? 25.948  0.575   56.344 1.00 20.72  ? 46  HIS C C   1 
ATOM   2566  O  O   . HIS C  1 47  ? 25.791  1.379   55.423 1.00 19.61  ? 46  HIS C O   1 
ATOM   2567  C  CB  . HIS C  1 47  ? 27.454  -1.356  55.937 1.00 24.00  ? 46  HIS C CB  1 
ATOM   2568  C  CG  . HIS C  1 47  ? 27.618  -2.713  55.341 1.00 24.52  ? 46  HIS C CG  1 
ATOM   2569  N  ND1 . HIS C  1 47  ? 28.092  -2.899  54.053 1.00 24.01  ? 46  HIS C ND1 1 
ATOM   2570  C  CD2 . HIS C  1 47  ? 27.353  -3.938  55.844 1.00 23.26  ? 46  HIS C CD2 1 
ATOM   2571  C  CE1 . HIS C  1 47  ? 28.114  -4.189  53.787 1.00 24.34  ? 46  HIS C CE1 1 
ATOM   2572  N  NE2 . HIS C  1 47  ? 27.660  -4.844  54.871 1.00 24.31  ? 46  HIS C NE2 1 
ATOM   2573  N  N   . VAL C  1 48  ? 26.131  0.912   57.621 1.00 20.35  ? 47  VAL C N   1 
ATOM   2574  C  CA  . VAL C  1 48  ? 26.460  2.270   57.999 1.00 22.27  ? 47  VAL C CA  1 
ATOM   2575  C  C   . VAL C  1 48  ? 27.981  2.388   58.047 1.00 23.33  ? 47  VAL C C   1 
ATOM   2576  O  O   . VAL C  1 48  ? 28.620  1.729   58.861 1.00 24.28  ? 47  VAL C O   1 
ATOM   2577  C  CB  . VAL C  1 48  ? 25.837  2.671   59.352 1.00 21.58  ? 47  VAL C CB  1 
ATOM   2578  C  CG1 . VAL C  1 48  ? 26.142  4.131   59.675 1.00 21.17  ? 47  VAL C CG1 1 
ATOM   2579  C  CG2 . VAL C  1 48  ? 24.346  2.390   59.413 1.00 19.81  ? 47  VAL C CG2 1 
ATOM   2580  N  N   . HIS C  1 49  ? 28.541  3.237   57.171 1.00 23.11  ? 48  HIS C N   1 
ATOM   2581  C  CA  . HIS C  1 49  ? 29.954  3.572   57.205 1.00 22.86  ? 48  HIS C CA  1 
ATOM   2582  C  C   . HIS C  1 49  ? 30.201  4.763   58.133 1.00 22.21  ? 48  HIS C C   1 
ATOM   2583  O  O   . HIS C  1 49  ? 29.264  5.434   58.551 1.00 20.92  ? 48  HIS C O   1 
ATOM   2584  C  CB  . HIS C  1 49  ? 30.473  3.802   55.788 1.00 23.04  ? 48  HIS C CB  1 
ATOM   2585  C  CG  . HIS C  1 49  ? 30.457  2.568   54.952 1.00 24.81  ? 48  HIS C CG  1 
ATOM   2586  N  ND1 . HIS C  1 49  ? 31.603  2.056   54.380 1.00 25.48  ? 48  HIS C ND1 1 
ATOM   2587  C  CD2 . HIS C  1 49  ? 29.446  1.754   54.579 1.00 25.21  ? 48  HIS C CD2 1 
ATOM   2588  C  CE1 . HIS C  1 49  ? 31.295  0.978   53.686 1.00 28.21  ? 48  HIS C CE1 1 
ATOM   2589  N  NE2 . HIS C  1 49  ? 29.981  0.772   53.788 1.00 27.54  ? 48  HIS C NE2 1 
ATOM   2590  N  N   . GLU C  1 50  ? 31.484  5.037   58.414 1.00 23.15  ? 49  GLU C N   1 
ATOM   2591  C  CA  . GLU C  1 50  ? 31.901  5.890   59.517 1.00 23.80  ? 49  GLU C CA  1 
ATOM   2592  C  C   . GLU C  1 50  ? 31.617  7.368   59.260 1.00 24.56  ? 49  GLU C C   1 
ATOM   2593  O  O   . GLU C  1 50  ? 31.179  8.067   60.169 1.00 23.82  ? 49  GLU C O   1 
ATOM   2594  C  CB  . GLU C  1 50  ? 33.395  5.726   59.778 1.00 25.44  ? 49  GLU C CB  1 
ATOM   2595  C  CG  . GLU C  1 50  ? 33.815  6.286   61.121 1.00 26.81  ? 49  GLU C CG  1 
ATOM   2596  C  CD  . GLU C  1 50  ? 35.287  6.149   61.455 1.00 28.52  ? 49  GLU C CD  1 
ATOM   2597  O  OE1 . GLU C  1 50  ? 35.983  5.311   60.828 1.00 28.00  ? 49  GLU C OE1 1 
ATOM   2598  O  OE2 . GLU C  1 50  ? 35.735  6.888   62.349 1.00 29.38  ? 49  GLU C OE2 1 
ATOM   2599  N  N   . PHE C  1 51  ? 31.884  7.843   58.038 1.00 25.77  ? 50  PHE C N   1 
ATOM   2600  C  CA  . PHE C  1 51  ? 31.905  9.273   57.771 1.00 27.35  ? 50  PHE C CA  1 
ATOM   2601  C  C   . PHE C  1 51  ? 30.753  9.693   56.870 1.00 28.56  ? 50  PHE C C   1 
ATOM   2602  O  O   . PHE C  1 51  ? 30.533  9.082   55.825 1.00 28.22  ? 50  PHE C O   1 
ATOM   2603  C  CB  . PHE C  1 51  ? 33.218  9.674   57.099 1.00 26.99  ? 50  PHE C CB  1 
ATOM   2604  C  CG  . PHE C  1 51  ? 34.433  9.258   57.884 1.00 26.49  ? 50  PHE C CG  1 
ATOM   2605  C  CD1 . PHE C  1 51  ? 34.591  9.669   59.200 1.00 26.13  ? 50  PHE C CD1 1 
ATOM   2606  C  CD2 . PHE C  1 51  ? 35.404  8.444   57.320 1.00 26.06  ? 50  PHE C CD2 1 
ATOM   2607  C  CE1 . PHE C  1 51  ? 35.703  9.288   59.938 1.00 26.11  ? 50  PHE C CE1 1 
ATOM   2608  C  CE2 . PHE C  1 51  ? 36.511  8.052   58.057 1.00 25.63  ? 50  PHE C CE2 1 
ATOM   2609  C  CZ  . PHE C  1 51  ? 36.656  8.472   59.362 1.00 26.39  ? 50  PHE C CZ  1 
ATOM   2610  N  N   . GLY C  1 52  ? 30.064  10.770  57.286 1.00 29.65  ? 51  GLY C N   1 
ATOM   2611  C  CA  . GLY C  1 52  ? 29.115  11.487  56.446 1.00 27.96  ? 51  GLY C CA  1 
ATOM   2612  C  C   . GLY C  1 52  ? 29.849  12.377  55.445 1.00 28.96  ? 51  GLY C C   1 
ATOM   2613  O  O   . GLY C  1 52  ? 29.630  13.586  55.391 1.00 30.88  ? 51  GLY C O   1 
ATOM   2614  N  N   . ASP C  1 53  ? 30.742  11.766  54.668 1.00 26.70  ? 52  ASP C N   1 
ATOM   2615  C  CA  . ASP C  1 53  ? 31.617  12.519  53.795 1.00 24.38  ? 52  ASP C CA  1 
ATOM   2616  C  C   . ASP C  1 53  ? 31.474  11.963  52.386 1.00 23.60  ? 52  ASP C C   1 
ATOM   2617  O  O   . ASP C  1 53  ? 31.819  10.821  52.126 1.00 24.03  ? 52  ASP C O   1 
ATOM   2618  C  CB  . ASP C  1 53  ? 33.051  12.444  54.309 1.00 24.84  ? 52  ASP C CB  1 
ATOM   2619  C  CG  . ASP C  1 53  ? 34.065  13.212  53.477 1.00 25.70  ? 52  ASP C CG  1 
ATOM   2620  O  OD1 . ASP C  1 53  ? 33.792  13.450  52.270 1.00 24.99  ? 52  ASP C OD1 1 
ATOM   2621  O  OD2 . ASP C  1 53  ? 35.158  13.463  54.030 1.00 23.87  ? 52  ASP C OD2 1 
ATOM   2622  N  N   . ASN C  1 54  ? 30.952  12.779  51.480 1.00 24.32  ? 53  ASN C N   1 
ATOM   2623  C  CA  . ASN C  1 54  ? 30.682  12.339  50.127 1.00 25.17  ? 53  ASN C CA  1 
ATOM   2624  C  C   . ASN C  1 54  ? 31.581  13.111  49.161 1.00 23.60  ? 53  ASN C C   1 
ATOM   2625  O  O   . ASN C  1 54  ? 31.333  13.141  47.964 1.00 23.74  ? 53  ASN C O   1 
ATOM   2626  C  CB  . ASN C  1 54  ? 29.180  12.423  49.836 1.00 31.35  ? 53  ASN C CB  1 
ATOM   2627  C  CG  . ASN C  1 54  ? 28.781  11.973  48.443 1.00 37.47  ? 53  ASN C CG  1 
ATOM   2628  O  OD1 . ASN C  1 54  ? 29.105  10.862  48.027 1.00 43.56  ? 53  ASN C OD1 1 
ATOM   2629  N  ND2 . ASN C  1 54  ? 28.065  12.821  47.713 1.00 37.61  ? 53  ASN C ND2 1 
ATOM   2630  N  N   . THR C  1 55  ? 32.660  13.704  49.681 1.00 23.29  ? 54  THR C N   1 
ATOM   2631  C  CA  . THR C  1 55  ? 33.487  14.613  48.895 1.00 24.29  ? 54  THR C CA  1 
ATOM   2632  C  C   . THR C  1 55  ? 34.085  13.905  47.686 1.00 25.72  ? 54  THR C C   1 
ATOM   2633  O  O   . THR C  1 55  ? 34.283  14.526  46.650 1.00 26.08  ? 54  THR C O   1 
ATOM   2634  C  CB  . THR C  1 55  ? 34.598  15.265  49.720 1.00 23.13  ? 54  THR C CB  1 
ATOM   2635  O  OG1 . THR C  1 55  ? 35.385  14.211  50.267 1.00 22.10  ? 54  THR C OG1 1 
ATOM   2636  C  CG2 . THR C  1 55  ? 34.066  16.144  50.834 1.00 23.73  ? 54  THR C CG2 1 
ATOM   2637  N  N   . ALA C  1 56  ? 34.372  12.608  47.831 1.00 28.29  ? 55  ALA C N   1 
ATOM   2638  C  CA  . ALA C  1 56  ? 34.975  11.834  46.759 1.00 28.98  ? 55  ALA C CA  1 
ATOM   2639  C  C   . ALA C  1 56  ? 34.067  10.655  46.430 1.00 30.29  ? 55  ALA C C   1 
ATOM   2640  O  O   . ALA C  1 56  ? 34.537  9.534   46.274 1.00 35.89  ? 55  ALA C O   1 
ATOM   2641  C  CB  . ALA C  1 56  ? 36.345  11.374  47.201 1.00 27.84  ? 55  ALA C CB  1 
ATOM   2642  N  N   . GLY C  1 57  ? 32.759  10.913  46.354 1.00 28.99  ? 56  GLY C N   1 
ATOM   2643  C  CA  . GLY C  1 57  ? 31.782  9.856   46.152 1.00 28.99  ? 56  GLY C CA  1 
ATOM   2644  C  C   . GLY C  1 57  ? 31.624  9.005   47.413 1.00 31.16  ? 56  GLY C C   1 
ATOM   2645  O  O   . GLY C  1 57  ? 31.949  9.441   48.521 1.00 31.90  ? 56  GLY C O   1 
ATOM   2646  N  N   . CYS C  1 58  ? 31.149  7.767   47.230 1.00 30.03  ? 57  CYS C N   1 
ATOM   2647  C  CA  . CYS C  1 58  ? 30.869  6.914   48.371 1.00 28.16  ? 57  CYS C CA  1 
ATOM   2648  C  C   . CYS C  1 58  ? 32.156  6.472   49.058 1.00 27.99  ? 57  CYS C C   1 
ATOM   2649  O  O   . CYS C  1 58  ? 32.113  6.135   50.242 1.00 28.87  ? 57  CYS C O   1 
ATOM   2650  C  CB  . CYS C  1 58  ? 30.036  5.716   47.963 1.00 28.48  ? 57  CYS C CB  1 
ATOM   2651  S  SG  . CYS C  1 58  ? 28.362  6.179   47.444 1.00 28.65  ? 57  CYS C SG  1 
ATOM   2652  N  N   . THR C  1 59  ? 33.285  6.512   48.332 1.00 26.91  ? 58  THR C N   1 
ATOM   2653  C  CA  . THR C  1 59  ? 34.569  6.074   48.862 1.00 26.11  ? 58  THR C CA  1 
ATOM   2654  C  C   . THR C  1 59  ? 34.910  6.816   50.151 1.00 25.88  ? 58  THR C C   1 
ATOM   2655  O  O   . THR C  1 59  ? 35.470  6.230   51.078 1.00 25.92  ? 58  THR C O   1 
ATOM   2656  C  CB  . THR C  1 59  ? 35.731  6.401   47.917 1.00 24.90  ? 58  THR C CB  1 
ATOM   2657  O  OG1 . THR C  1 59  ? 35.363  5.937   46.624 1.00 27.19  ? 58  THR C OG1 1 
ATOM   2658  C  CG2 . THR C  1 59  ? 37.036  5.774   48.343 1.00 23.41  ? 58  THR C CG2 1 
ATOM   2659  N  N   . SER C  1 60  ? 34.591  8.116   50.185 1.00 23.57  ? 59  SER C N   1 
ATOM   2660  C  CA  . SER C  1 60  ? 35.108  8.945   51.258 1.00 22.04  ? 59  SER C CA  1 
ATOM   2661  C  C   . SER C  1 60  ? 34.314  8.727   52.545 1.00 20.89  ? 59  SER C C   1 
ATOM   2662  O  O   . SER C  1 60  ? 34.611  9.333   53.570 1.00 20.79  ? 59  SER C O   1 
ATOM   2663  C  CB  . SER C  1 60  ? 35.245  10.393  50.831 1.00 23.01  ? 59  SER C CB  1 
ATOM   2664  O  OG  . SER C  1 60  ? 34.027  10.883  50.316 1.00 26.29  ? 59  SER C OG  1 
ATOM   2665  N  N   . ALA C  1 61  ? 33.351  7.795   52.493 1.00 19.89  ? 60  ALA C N   1 
ATOM   2666  C  CA  . ALA C  1 61  ? 32.525  7.439   53.639 1.00 19.19  ? 60  ALA C CA  1 
ATOM   2667  C  C   . ALA C  1 61  ? 33.341  6.627   54.642 1.00 19.68  ? 60  ALA C C   1 
ATOM   2668  O  O   . ALA C  1 61  ? 32.954  6.505   55.805 1.00 19.79  ? 60  ALA C O   1 
ATOM   2669  C  CB  . ALA C  1 61  ? 31.311  6.678   53.182 1.00 17.47  ? 60  ALA C CB  1 
ATOM   2670  N  N   . GLY C  1 62  ? 34.461  6.070   54.169 1.00 18.98  ? 61  GLY C N   1 
ATOM   2671  C  CA  . GLY C  1 62  ? 35.350  5.282   55.005 1.00 20.71  ? 61  GLY C CA  1 
ATOM   2672  C  C   . GLY C  1 62  ? 34.830  3.871   55.254 1.00 21.99  ? 61  GLY C C   1 
ATOM   2673  O  O   . GLY C  1 62  ? 33.982  3.382   54.507 1.00 22.61  ? 61  GLY C O   1 
ATOM   2674  N  N   . PRO C  1 63  ? 35.308  3.186   56.325 1.00 22.59  ? 62  PRO C N   1 
ATOM   2675  C  CA  . PRO C  1 63  ? 34.951  1.784   56.587 1.00 21.46  ? 62  PRO C CA  1 
ATOM   2676  C  C   . PRO C  1 63  ? 33.590  1.663   57.272 1.00 20.81  ? 62  PRO C C   1 
ATOM   2677  O  O   . PRO C  1 63  ? 32.954  2.674   57.575 1.00 19.91  ? 62  PRO C O   1 
ATOM   2678  C  CB  . PRO C  1 63  ? 36.057  1.365   57.568 1.00 19.83  ? 62  PRO C CB  1 
ATOM   2679  C  CG  . PRO C  1 63  ? 36.310  2.617   58.381 1.00 19.39  ? 62  PRO C CG  1 
ATOM   2680  C  CD  . PRO C  1 63  ? 36.185  3.744   57.375 1.00 21.32  ? 62  PRO C CD  1 
ATOM   2681  N  N   . HIS C  1 64  ? 33.149  0.423   57.521 1.00 20.27  ? 63  HIS C N   1 
ATOM   2682  C  CA  . HIS C  1 64  ? 31.935  0.215   58.298 1.00 19.16  ? 63  HIS C CA  1 
ATOM   2683  C  C   . HIS C  1 64  ? 32.098  0.919   59.640 1.00 18.13  ? 63  HIS C C   1 
ATOM   2684  O  O   . HIS C  1 64  ? 33.154  0.820   60.248 1.00 18.49  ? 63  HIS C O   1 
ATOM   2685  C  CB  . HIS C  1 64  ? 31.664  -1.282  58.513 1.00 18.53  ? 63  HIS C CB  1 
ATOM   2686  C  CG  . HIS C  1 64  ? 31.415  -2.066  57.273 1.00 19.42  ? 63  HIS C CG  1 
ATOM   2687  N  ND1 . HIS C  1 64  ? 31.322  -3.448  57.288 1.00 20.43  ? 63  HIS C ND1 1 
ATOM   2688  C  CD2 . HIS C  1 64  ? 31.250  -1.688  55.990 1.00 19.64  ? 63  HIS C CD2 1 
ATOM   2689  C  CE1 . HIS C  1 64  ? 31.083  -3.886  56.068 1.00 20.26  ? 63  HIS C CE1 1 
ATOM   2690  N  NE2 . HIS C  1 64  ? 31.042  -2.822  55.245 1.00 20.29  ? 63  HIS C NE2 1 
ATOM   2691  N  N   . PHE C  1 65  ? 31.056  1.616   60.093 1.00 19.25  ? 64  PHE C N   1 
ATOM   2692  C  CA  . PHE C  1 65  ? 31.068  2.294   61.382 1.00 22.00  ? 64  PHE C CA  1 
ATOM   2693  C  C   . PHE C  1 65  ? 31.385  1.293   62.496 1.00 23.35  ? 64  PHE C C   1 
ATOM   2694  O  O   . PHE C  1 65  ? 30.620  0.360   62.745 1.00 23.86  ? 64  PHE C O   1 
ATOM   2695  C  CB  . PHE C  1 65  ? 29.740  3.022   61.619 1.00 22.19  ? 64  PHE C CB  1 
ATOM   2696  C  CG  . PHE C  1 65  ? 29.648  3.763   62.926 1.00 23.38  ? 64  PHE C CG  1 
ATOM   2697  C  CD1 . PHE C  1 65  ? 30.718  4.516   63.407 1.00 23.27  ? 64  PHE C CD1 1 
ATOM   2698  C  CD2 . PHE C  1 65  ? 28.480  3.723   63.676 1.00 24.76  ? 64  PHE C CD2 1 
ATOM   2699  C  CE1 . PHE C  1 65  ? 30.629  5.193   64.615 1.00 22.80  ? 64  PHE C CE1 1 
ATOM   2700  C  CE2 . PHE C  1 65  ? 28.390  4.406   64.882 1.00 25.25  ? 64  PHE C CE2 1 
ATOM   2701  C  CZ  . PHE C  1 65  ? 29.462  5.141   65.349 1.00 24.79  ? 64  PHE C CZ  1 
ATOM   2702  N  N   . ASN C  1 66  ? 32.516  1.506   63.181 1.00 23.54  ? 65  ASN C N   1 
ATOM   2703  C  CA  . ASN C  1 66  ? 33.038  0.468   64.048 1.00 24.45  ? 65  ASN C CA  1 
ATOM   2704  C  C   . ASN C  1 66  ? 33.542  1.049   65.370 1.00 25.56  ? 65  ASN C C   1 
ATOM   2705  O  O   . ASN C  1 66  ? 34.680  0.816   65.752 1.00 23.48  ? 65  ASN C O   1 
ATOM   2706  C  CB  . ASN C  1 66  ? 34.093  -0.367  63.309 1.00 26.00  ? 65  ASN C CB  1 
ATOM   2707  C  CG  . ASN C  1 66  ? 34.582  -1.546  64.120 1.00 27.74  ? 65  ASN C CG  1 
ATOM   2708  O  OD1 . ASN C  1 66  ? 33.914  -1.994  65.057 1.00 29.42  ? 65  ASN C OD1 1 
ATOM   2709  N  ND2 . ASN C  1 66  ? 35.754  -2.047  63.777 1.00 27.06  ? 65  ASN C ND2 1 
ATOM   2710  N  N   . PRO C  1 67  ? 32.712  1.753   66.168 1.00 29.95  ? 66  PRO C N   1 
ATOM   2711  C  CA  . PRO C  1 67  ? 33.204  2.426   67.371 1.00 30.90  ? 66  PRO C CA  1 
ATOM   2712  C  C   . PRO C  1 67  ? 33.776  1.499   68.441 1.00 33.57  ? 66  PRO C C   1 
ATOM   2713  O  O   . PRO C  1 67  ? 34.533  1.954   69.301 1.00 36.42  ? 66  PRO C O   1 
ATOM   2714  C  CB  . PRO C  1 67  ? 31.983  3.154   67.945 1.00 27.77  ? 66  PRO C CB  1 
ATOM   2715  C  CG  . PRO C  1 67  ? 30.799  2.431   67.350 1.00 28.04  ? 66  PRO C CG  1 
ATOM   2716  C  CD  . PRO C  1 67  ? 31.254  1.893   66.006 1.00 31.27  ? 66  PRO C CD  1 
ATOM   2717  N  N   . LEU C  1 68  ? 33.416  0.203   68.396 1.00 34.37  ? 67  LEU C N   1 
ATOM   2718  C  CA  . LEU C  1 68  ? 33.834  -0.710  69.453 1.00 32.69  ? 67  LEU C CA  1 
ATOM   2719  C  C   . LEU C  1 68  ? 35.002  -1.589  68.994 1.00 32.89  ? 67  LEU C C   1 
ATOM   2720  O  O   . LEU C  1 68  ? 35.398  -2.495  69.717 1.00 32.84  ? 67  LEU C O   1 
ATOM   2721  C  CB  . LEU C  1 68  ? 32.649  -1.563  69.910 1.00 33.47  ? 67  LEU C CB  1 
ATOM   2722  C  CG  . LEU C  1 68  ? 31.544  -0.816  70.677 1.00 36.38  ? 67  LEU C CG  1 
ATOM   2723  C  CD1 . LEU C  1 68  ? 30.552  -1.801  71.248 1.00 37.34  ? 67  LEU C CD1 1 
ATOM   2724  C  CD2 . LEU C  1 68  ? 32.103  0.029   71.814 1.00 36.67  ? 67  LEU C CD2 1 
ATOM   2725  N  N   . SER C  1 69  ? 35.540  -1.327  67.799 1.00 33.80  ? 68  SER C N   1 
ATOM   2726  C  CA  . SER C  1 69  ? 36.722  -2.001  67.271 1.00 33.93  ? 68  SER C CA  1 
ATOM   2727  C  C   . SER C  1 69  ? 36.552  -3.514  67.239 1.00 32.63  ? 68  SER C C   1 
ATOM   2728  O  O   . SER C  1 69  ? 37.408  -4.217  67.756 1.00 33.08  ? 68  SER C O   1 
ATOM   2729  C  CB  . SER C  1 69  ? 37.950  -1.637  68.045 1.00 35.93  ? 68  SER C CB  1 
ATOM   2730  O  OG  . SER C  1 69  ? 38.260  -0.274  67.839 1.00 39.39  ? 68  SER C OG  1 
ATOM   2731  N  N   . ARG C  1 70  ? 35.469  -4.002  66.622 1.00 33.21  ? 69  ARG C N   1 
ATOM   2732  C  CA  . ARG C  1 70  ? 35.244  -5.434  66.481 1.00 33.43  ? 69  ARG C CA  1 
ATOM   2733  C  C   . ARG C  1 70  ? 35.425  -5.830  65.017 1.00 33.22  ? 69  ARG C C   1 
ATOM   2734  O  O   . ARG C  1 70  ? 35.624  -4.971  64.151 1.00 32.20  ? 69  ARG C O   1 
ATOM   2735  C  CB  . ARG C  1 70  ? 33.849  -5.816  66.953 1.00 35.10  ? 69  ARG C CB  1 
ATOM   2736  C  CG  . ARG C  1 70  ? 33.476  -5.302  68.349 1.00 40.21  ? 69  ARG C CG  1 
ATOM   2737  C  CD  . ARG C  1 70  ? 32.454  -6.361  68.792 1.00 49.38  ? 69  ARG C CD  1 
ATOM   2738  N  NE  . ARG C  1 70  ? 31.728  -6.014  70.042 1.00 56.73  ? 69  ARG C NE  1 
ATOM   2739  C  CZ  . ARG C  1 70  ? 32.242  -6.103  71.264 1.00 62.98  ? 69  ARG C CZ  1 
ATOM   2740  N  NH1 . ARG C  1 70  ? 33.443  -6.624  71.476 1.00 74.52  ? 69  ARG C NH1 1 
ATOM   2741  N  NH2 . ARG C  1 70  ? 31.498  -5.763  72.315 1.00 59.97  ? 69  ARG C NH2 1 
ATOM   2742  N  N   . LYS C  1 71  ? 35.380  -7.144  64.752 1.00 32.34  ? 70  LYS C N   1 
ATOM   2743  C  CA  . LYS C  1 71  ? 35.477  -7.669  63.394 1.00 32.42  ? 70  LYS C CA  1 
ATOM   2744  C  C   . LYS C  1 71  ? 34.077  -7.679  62.772 1.00 28.59  ? 70  LYS C C   1 
ATOM   2745  O  O   . LYS C  1 71  ? 33.084  -7.616  63.483 1.00 26.14  ? 70  LYS C O   1 
ATOM   2746  C  CB  . LYS C  1 71  ? 36.217  -9.014  63.379 1.00 40.93  ? 70  LYS C CB  1 
ATOM   2747  C  CG  . LYS C  1 71  ? 37.585  -9.005  64.063 1.00 47.32  ? 70  LYS C CG  1 
ATOM   2748  C  CD  . LYS C  1 71  ? 38.568  -10.046 63.616 1.00 55.69  ? 70  LYS C CD  1 
ATOM   2749  C  CE  . LYS C  1 71  ? 39.992  -9.518  63.659 1.00 58.53  ? 70  LYS C CE  1 
ATOM   2750  N  NZ  . LYS C  1 71  ? 40.988  -10.600 63.493 1.00 58.10  ? 70  LYS C NZ  1 
ATOM   2751  N  N   . HIS C  1 72  ? 34.009  -7.728  61.440 1.00 26.54  ? 71  HIS C N   1 
ATOM   2752  C  CA  . HIS C  1 72  ? 32.751  -7.656  60.710 1.00 26.91  ? 71  HIS C CA  1 
ATOM   2753  C  C   . HIS C  1 72  ? 31.922  -8.914  60.957 1.00 28.91  ? 71  HIS C C   1 
ATOM   2754  O  O   . HIS C  1 72  ? 32.461  -10.021 60.995 1.00 30.78  ? 71  HIS C O   1 
ATOM   2755  C  CB  . HIS C  1 72  ? 33.020  -7.436  59.218 1.00 24.15  ? 71  HIS C CB  1 
ATOM   2756  C  CG  . HIS C  1 72  ? 31.805  -7.473  58.366 1.00 23.12  ? 71  HIS C CG  1 
ATOM   2757  N  ND1 . HIS C  1 72  ? 30.994  -6.365  58.162 1.00 22.74  ? 71  HIS C ND1 1 
ATOM   2758  C  CD2 . HIS C  1 72  ? 31.253  -8.479  57.660 1.00 22.57  ? 71  HIS C CD2 1 
ATOM   2759  C  CE1 . HIS C  1 72  ? 29.994  -6.696  57.373 1.00 22.99  ? 71  HIS C CE1 1 
ATOM   2760  N  NE2 . HIS C  1 72  ? 30.126  -7.990  57.056 1.00 23.39  ? 71  HIS C NE2 1 
ATOM   2761  N  N   . GLY C  1 73  ? 30.606  -8.737  61.125 1.00 27.54  ? 72  GLY C N   1 
ATOM   2762  C  CA  . GLY C  1 73  ? 29.689  -9.854  61.276 1.00 25.46  ? 72  GLY C CA  1 
ATOM   2763  C  C   . GLY C  1 73  ? 28.371  -9.592  60.549 1.00 25.52  ? 72  GLY C C   1 
ATOM   2764  O  O   . GLY C  1 73  ? 28.224  -8.566  59.876 1.00 25.63  ? 72  GLY C O   1 
ATOM   2765  N  N   . GLY C  1 74  ? 27.435  -10.551 60.665 1.00 23.84  ? 73  GLY C N   1 
ATOM   2766  C  CA  . GLY C  1 74  ? 26.041  -10.322 60.325 1.00 21.56  ? 73  GLY C CA  1 
ATOM   2767  C  C   . GLY C  1 74  ? 25.339  -9.598  61.475 1.00 20.15  ? 73  GLY C C   1 
ATOM   2768  O  O   . GLY C  1 74  ? 25.838  -9.599  62.600 1.00 18.37  ? 73  GLY C O   1 
ATOM   2769  N  N   . PRO C  1 75  ? 24.181  -8.941  61.234 1.00 19.86  ? 74  PRO C N   1 
ATOM   2770  C  CA  . PRO C  1 75  ? 23.514  -8.165  62.277 1.00 21.64  ? 74  PRO C CA  1 
ATOM   2771  C  C   . PRO C  1 75  ? 23.221  -8.977  63.535 1.00 23.06  ? 74  PRO C C   1 
ATOM   2772  O  O   . PRO C  1 75  ? 23.200  -8.416  64.628 1.00 21.97  ? 74  PRO C O   1 
ATOM   2773  C  CB  . PRO C  1 75  ? 22.211  -7.669  61.632 1.00 21.36  ? 74  PRO C CB  1 
ATOM   2774  C  CG  . PRO C  1 75  ? 22.063  -8.490  60.369 1.00 20.56  ? 74  PRO C CG  1 
ATOM   2775  C  CD  . PRO C  1 75  ? 23.462  -8.884  59.953 1.00 20.00  ? 74  PRO C CD  1 
ATOM   2776  N  N   . LYS C  1 76  ? 23.053  -10.299 63.369 1.00 25.35  ? 75  LYS C N   1 
ATOM   2777  C  CA  . LYS C  1 76  ? 22.632  -11.163 64.455 1.00 26.10  ? 75  LYS C CA  1 
ATOM   2778  C  C   . LYS C  1 76  ? 23.812  -11.585 65.341 1.00 27.18  ? 75  LYS C C   1 
ATOM   2779  O  O   . LYS C  1 76  ? 23.589  -12.101 66.431 1.00 27.76  ? 75  LYS C O   1 
ATOM   2780  C  CB  . LYS C  1 76  ? 21.940  -12.401 63.874 1.00 25.53  ? 75  LYS C CB  1 
ATOM   2781  C  CG  . LYS C  1 76  ? 20.495  -12.245 63.460 1.00 32.55  ? 75  LYS C CG  1 
ATOM   2782  C  CD  . LYS C  1 76  ? 20.010  -13.327 62.530 1.00 39.04  ? 75  LYS C CD  1 
ATOM   2783  C  CE  . LYS C  1 76  ? 19.594  -14.605 63.233 1.00 39.61  ? 75  LYS C CE  1 
ATOM   2784  N  NZ  . LYS C  1 76  ? 19.646  -15.719 62.269 1.00 35.34  ? 75  LYS C NZ  1 
ATOM   2785  N  N   . ASP C  1 77  ? 25.058  -11.359 64.873 1.00 28.45  ? 76  ASP C N   1 
ATOM   2786  C  CA  . ASP C  1 77  ? 26.262  -11.822 65.542 1.00 28.98  ? 76  ASP C CA  1 
ATOM   2787  C  C   . ASP C  1 77  ? 26.578  -10.909 66.727 1.00 29.53  ? 76  ASP C C   1 
ATOM   2788  O  O   . ASP C  1 77  ? 26.258  -9.721  66.704 1.00 29.15  ? 76  ASP C O   1 
ATOM   2789  C  CB  . ASP C  1 77  ? 27.441  -11.886 64.568 1.00 27.87  ? 76  ASP C CB  1 
ATOM   2790  C  CG  . ASP C  1 77  ? 27.297  -13.015 63.559 1.00 30.52  ? 76  ASP C CG  1 
ATOM   2791  O  OD1 . ASP C  1 77  ? 26.703  -14.043 63.930 1.00 30.44  ? 76  ASP C OD1 1 
ATOM   2792  O  OD2 . ASP C  1 77  ? 27.750  -12.860 62.395 1.00 33.55  ? 76  ASP C OD2 1 
ATOM   2793  N  N   . GLU C  1 78  ? 27.212  -11.462 67.761 1.00 30.34  ? 77  GLU C N   1 
ATOM   2794  C  CA  . GLU C  1 78  ? 27.685  -10.599 68.825 1.00 32.77  ? 77  GLU C CA  1 
ATOM   2795  C  C   . GLU C  1 78  ? 28.945  -9.876  68.354 1.00 32.86  ? 77  GLU C C   1 
ATOM   2796  O  O   . GLU C  1 78  ? 29.148  -8.701  68.657 1.00 33.33  ? 77  GLU C O   1 
ATOM   2797  C  CB  . GLU C  1 78  ? 27.842  -11.321 70.161 1.00 41.52  ? 77  GLU C CB  1 
ATOM   2798  C  CG  . GLU C  1 78  ? 27.724  -10.310 71.306 1.00 50.16  ? 77  GLU C CG  1 
ATOM   2799  C  CD  . GLU C  1 78  ? 28.793  -10.383 72.381 1.00 59.15  ? 77  GLU C CD  1 
ATOM   2800  O  OE1 . GLU C  1 78  ? 28.921  -11.490 72.943 1.00 68.05  ? 77  GLU C OE1 1 
ATOM   2801  O  OE2 . GLU C  1 78  ? 29.477  -9.338  72.681 1.00 61.64  ? 77  GLU C OE2 1 
ATOM   2802  N  N   . GLU C  1 79  ? 29.771  -10.576 67.571 1.00 32.91  ? 78  GLU C N   1 
ATOM   2803  C  CA  . GLU C  1 79  ? 30.948  -9.993  66.942 1.00 33.03  ? 78  GLU C CA  1 
ATOM   2804  C  C   . GLU C  1 79  ? 30.550  -9.342  65.612 1.00 31.09  ? 78  GLU C C   1 
ATOM   2805  O  O   . GLU C  1 79  ? 30.481  -9.998  64.572 1.00 30.48  ? 78  GLU C O   1 
ATOM   2806  C  CB  . GLU C  1 79  ? 32.068  -11.043 66.878 1.00 36.11  ? 78  GLU C CB  1 
ATOM   2807  C  CG  . GLU C  1 79  ? 33.435  -10.540 66.417 1.00 39.55  ? 78  GLU C CG  1 
ATOM   2808  C  CD  . GLU C  1 79  ? 34.222  -9.621  67.351 1.00 45.90  ? 78  GLU C CD  1 
ATOM   2809  O  OE1 . GLU C  1 79  ? 33.762  -9.382  68.524 1.00 45.23  ? 78  GLU C OE1 1 
ATOM   2810  O  OE2 . GLU C  1 79  ? 35.275  -9.097  66.900 1.00 50.93  ? 78  GLU C OE2 1 
ATOM   2811  N  N   . ARG C  1 80  ? 30.262  -8.036  65.669 1.00 29.33  ? 79  ARG C N   1 
ATOM   2812  C  CA  . ARG C  1 80  ? 29.913  -7.245  64.498 1.00 26.97  ? 79  ARG C CA  1 
ATOM   2813  C  C   . ARG C  1 80  ? 30.340  -5.791  64.677 1.00 26.34  ? 79  ARG C C   1 
ATOM   2814  O  O   . ARG C  1 80  ? 30.548  -5.316  65.795 1.00 26.28  ? 79  ARG C O   1 
ATOM   2815  C  CB  . ARG C  1 80  ? 28.405  -7.264  64.251 1.00 26.27  ? 79  ARG C CB  1 
ATOM   2816  C  CG  . ARG C  1 80  ? 27.573  -6.759  65.420 1.00 26.17  ? 79  ARG C CG  1 
ATOM   2817  C  CD  . ARG C  1 80  ? 26.115  -6.648  65.026 1.00 27.33  ? 79  ARG C CD  1 
ATOM   2818  N  NE  . ARG C  1 80  ? 25.805  -5.342  64.476 1.00 27.03  ? 79  ARG C NE  1 
ATOM   2819  C  CZ  . ARG C  1 80  ? 24.575  -4.860  64.298 1.00 26.86  ? 79  ARG C CZ  1 
ATOM   2820  N  NH1 . ARG C  1 80  ? 23.520  -5.595  64.603 1.00 26.45  ? 79  ARG C NH1 1 
ATOM   2821  N  NH2 . ARG C  1 80  ? 24.402  -3.639  63.821 1.00 27.19  ? 79  ARG C NH2 1 
ATOM   2822  N  N   . HIS C  1 81  ? 30.460  -5.096  63.542 1.00 26.25  ? 80  HIS C N   1 
ATOM   2823  C  CA  . HIS C  1 81  ? 30.515  -3.646  63.504 1.00 25.59  ? 80  HIS C CA  1 
ATOM   2824  C  C   . HIS C  1 81  ? 29.136  -3.104  63.854 1.00 26.99  ? 80  HIS C C   1 
ATOM   2825  O  O   . HIS C  1 81  ? 28.128  -3.706  63.483 1.00 29.97  ? 80  HIS C O   1 
ATOM   2826  C  CB  . HIS C  1 81  ? 30.891  -3.181  62.097 1.00 22.66  ? 80  HIS C CB  1 
ATOM   2827  C  CG  . HIS C  1 81  ? 32.209  -3.685  61.637 1.00 22.63  ? 80  HIS C CG  1 
ATOM   2828  N  ND1 . HIS C  1 81  ? 32.460  -4.016  60.311 1.00 22.19  ? 80  HIS C ND1 1 
ATOM   2829  C  CD2 . HIS C  1 81  ? 33.358  -3.906  62.318 1.00 22.03  ? 80  HIS C CD2 1 
ATOM   2830  C  CE1 . HIS C  1 81  ? 33.713  -4.407  60.195 1.00 21.65  ? 80  HIS C CE1 1 
ATOM   2831  N  NE2 . HIS C  1 81  ? 34.285  -4.361  61.416 1.00 21.47  ? 80  HIS C NE2 1 
ATOM   2832  N  N   . VAL C  1 82  ? 29.100  -1.956  64.548 1.00 26.85  ? 81  VAL C N   1 
ATOM   2833  C  CA  . VAL C  1 82  ? 27.828  -1.304  64.809 1.00 26.00  ? 81  VAL C CA  1 
ATOM   2834  C  C   . VAL C  1 82  ? 27.075  -1.106  63.493 1.00 25.97  ? 81  VAL C C   1 
ATOM   2835  O  O   . VAL C  1 82  ? 25.869  -1.302  63.445 1.00 27.06  ? 81  VAL C O   1 
ATOM   2836  C  CB  . VAL C  1 82  ? 27.985  0.009   65.600 1.00 25.65  ? 81  VAL C CB  1 
ATOM   2837  C  CG1 . VAL C  1 82  ? 26.740  0.882   65.527 1.00 24.41  ? 81  VAL C CG1 1 
ATOM   2838  C  CG2 . VAL C  1 82  ? 28.379  -0.250  67.045 1.00 24.29  ? 81  VAL C CG2 1 
ATOM   2839  N  N   . GLY C  1 83  ? 27.797  -0.769  62.415 1.00 23.44  ? 82  GLY C N   1 
ATOM   2840  C  CA  . GLY C  1 83  ? 27.147  -0.444  61.162 1.00 22.43  ? 82  GLY C CA  1 
ATOM   2841  C  C   . GLY C  1 83  ? 26.718  -1.662  60.344 1.00 22.14  ? 82  GLY C C   1 
ATOM   2842  O  O   . GLY C  1 83  ? 26.228  -1.492  59.226 1.00 22.20  ? 82  GLY C O   1 
ATOM   2843  N  N   . ASP C  1 84  ? 26.907  -2.868  60.897 1.00 21.98  ? 83  ASP C N   1 
ATOM   2844  C  CA  . ASP C  1 84  ? 26.704  -4.115  60.165 1.00 22.77  ? 83  ASP C CA  1 
ATOM   2845  C  C   . ASP C  1 84  ? 25.219  -4.490  60.135 1.00 24.25  ? 83  ASP C C   1 
ATOM   2846  O  O   . ASP C  1 84  ? 24.706  -5.108  61.065 1.00 23.18  ? 83  ASP C O   1 
ATOM   2847  C  CB  . ASP C  1 84  ? 27.578  -5.240  60.722 1.00 21.17  ? 83  ASP C CB  1 
ATOM   2848  C  CG  . ASP C  1 84  ? 29.043  -5.143  60.349 1.00 21.11  ? 83  ASP C CG  1 
ATOM   2849  O  OD1 . ASP C  1 84  ? 29.364  -4.402  59.402 1.00 21.23  ? 83  ASP C OD1 1 
ATOM   2850  O  OD2 . ASP C  1 84  ? 29.858  -5.826  60.999 1.00 20.37  ? 83  ASP C OD2 1 
ATOM   2851  N  N   . LEU C  1 85  ? 24.532  -4.138  59.038 1.00 25.21  ? 84  LEU C N   1 
ATOM   2852  C  CA  . LEU C  1 85  ? 23.096  -4.353  58.953 1.00 24.15  ? 84  LEU C CA  1 
ATOM   2853  C  C   . LEU C  1 85  ? 22.768  -5.521  58.023 1.00 23.58  ? 84  LEU C C   1 
ATOM   2854  O  O   . LEU C  1 85  ? 21.607  -5.723  57.683 1.00 24.75  ? 84  LEU C O   1 
ATOM   2855  C  CB  . LEU C  1 85  ? 22.411  -3.064  58.491 1.00 22.92  ? 84  LEU C CB  1 
ATOM   2856  C  CG  . LEU C  1 85  ? 22.351  -1.926  59.505 1.00 23.47  ? 84  LEU C CG  1 
ATOM   2857  C  CD1 . LEU C  1 85  ? 21.543  -0.762  58.944 1.00 22.99  ? 84  LEU C CD1 1 
ATOM   2858  C  CD2 . LEU C  1 85  ? 21.755  -2.398  60.839 1.00 23.08  ? 84  LEU C CD2 1 
ATOM   2859  N  N   . GLY C  1 86  ? 23.783  -6.283  57.607 1.00 22.89  ? 85  GLY C N   1 
ATOM   2860  C  CA  . GLY C  1 86  ? 23.541  -7.482  56.821 1.00 23.86  ? 85  GLY C CA  1 
ATOM   2861  C  C   . GLY C  1 86  ? 23.214  -7.177  55.358 1.00 24.92  ? 85  GLY C C   1 
ATOM   2862  O  O   . GLY C  1 86  ? 23.844  -6.316  54.744 1.00 24.16  ? 85  GLY C O   1 
ATOM   2863  N  N   . ASN C  1 87  ? 22.217  -7.897  54.812 1.00 23.51  ? 86  ASN C N   1 
ATOM   2864  C  CA  . ASN C  1 87  ? 21.865  -7.768  53.408 1.00 21.56  ? 86  ASN C CA  1 
ATOM   2865  C  C   . ASN C  1 87  ? 20.442  -7.242  53.241 1.00 21.58  ? 86  ASN C C   1 
ATOM   2866  O  O   . ASN C  1 87  ? 19.595  -7.352  54.136 1.00 22.13  ? 86  ASN C O   1 
ATOM   2867  C  CB  . ASN C  1 87  ? 21.970  -9.093  52.660 1.00 22.33  ? 86  ASN C CB  1 
ATOM   2868  C  CG  . ASN C  1 87  ? 23.399  -9.568  52.550 1.00 23.67  ? 86  ASN C CG  1 
ATOM   2869  O  OD1 . ASN C  1 87  ? 24.182  -9.044  51.766 1.00 24.07  ? 86  ASN C OD1 1 
ATOM   2870  N  ND2 . ASN C  1 87  ? 23.752  -10.545 53.361 1.00 23.45  ? 86  ASN C ND2 1 
ATOM   2871  N  N   . VAL C  1 88  ? 20.210  -6.657  52.066 1.00 19.62  ? 87  VAL C N   1 
ATOM   2872  C  CA  . VAL C  1 88  ? 18.869  -6.383  51.596 1.00 19.17  ? 87  VAL C CA  1 
ATOM   2873  C  C   . VAL C  1 88  ? 18.690  -7.180  50.306 1.00 20.15  ? 87  VAL C C   1 
ATOM   2874  O  O   . VAL C  1 88  ? 19.672  -7.559  49.670 1.00 20.33  ? 87  VAL C O   1 
ATOM   2875  C  CB  . VAL C  1 88  ? 18.623  -4.871  51.424 1.00 19.74  ? 87  VAL C CB  1 
ATOM   2876  C  CG1 . VAL C  1 88  ? 18.791  -4.117  52.737 1.00 19.07  ? 87  VAL C CG1 1 
ATOM   2877  C  CG2 . VAL C  1 88  ? 19.467  -4.257  50.309 1.00 19.92  ? 87  VAL C CG2 1 
ATOM   2878  N  N   . THR C  1 89  ? 17.434  -7.464  49.947 1.00 21.35  ? 88  THR C N   1 
ATOM   2879  C  CA  . THR C  1 89  ? 17.175  -8.333  48.815 1.00 21.41  ? 88  THR C CA  1 
ATOM   2880  C  C   . THR C  1 89  ? 16.437  -7.562  47.730 1.00 21.44  ? 88  THR C C   1 
ATOM   2881  O  O   . THR C  1 89  ? 15.361  -7.019  47.978 1.00 22.15  ? 88  THR C O   1 
ATOM   2882  C  CB  . THR C  1 89  ? 16.329  -9.543  49.231 1.00 20.44  ? 88  THR C CB  1 
ATOM   2883  O  OG1 . THR C  1 89  ? 16.966  -10.219 50.318 1.00 21.03  ? 88  THR C OG1 1 
ATOM   2884  C  CG2 . THR C  1 89  ? 16.079  -10.502 48.089 1.00 18.47  ? 88  THR C CG2 1 
ATOM   2885  N  N   . ALA C  1 90  ? 17.000  -7.571  46.520 1.00 21.40  ? 89  ALA C N   1 
ATOM   2886  C  CA  . ALA C  1 90  ? 16.316  -6.997  45.376 1.00 23.61  ? 89  ALA C CA  1 
ATOM   2887  C  C   . ALA C  1 90  ? 15.557  -8.087  44.617 1.00 26.23  ? 89  ALA C C   1 
ATOM   2888  O  O   . ALA C  1 90  ? 16.106  -9.156  44.336 1.00 29.36  ? 89  ALA C O   1 
ATOM   2889  C  CB  . ALA C  1 90  ? 17.311  -6.306  44.488 1.00 23.75  ? 89  ALA C CB  1 
ATOM   2890  N  N   . ASP C  1 91  ? 14.294  -7.788  44.271 1.00 26.70  ? 90  ASP C N   1 
ATOM   2891  C  CA  . ASP C  1 91  ? 13.412  -8.670  43.523 1.00 27.26  ? 90  ASP C CA  1 
ATOM   2892  C  C   . ASP C  1 91  ? 13.800  -8.648  42.044 1.00 28.32  ? 90  ASP C C   1 
ATOM   2893  O  O   . ASP C  1 91  ? 14.743  -7.962  41.666 1.00 26.62  ? 90  ASP C O   1 
ATOM   2894  C  CB  . ASP C  1 91  ? 11.942  -8.312  43.751 1.00 28.59  ? 90  ASP C CB  1 
ATOM   2895  C  CG  . ASP C  1 91  ? 11.512  -6.936  43.245 1.00 32.52  ? 90  ASP C CG  1 
ATOM   2896  O  OD1 . ASP C  1 91  ? 12.191  -6.367  42.343 1.00 31.53  ? 90  ASP C OD1 1 
ATOM   2897  O  OD2 . ASP C  1 91  ? 10.486  -6.438  43.764 1.00 34.58  ? 90  ASP C OD2 1 
ATOM   2898  N  N   . LYS C  1 92  ? 13.055  -9.396  41.213 1.00 30.66  ? 91  LYS C N   1 
ATOM   2899  C  CA  . LYS C  1 92  ? 13.389  -9.561  39.801 1.00 31.23  ? 91  LYS C CA  1 
ATOM   2900  C  C   . LYS C  1 92  ? 13.359  -8.218  39.073 1.00 29.55  ? 91  LYS C C   1 
ATOM   2901  O  O   . LYS C  1 92  ? 13.906  -8.115  37.984 1.00 29.38  ? 91  LYS C O   1 
ATOM   2902  C  CB  . LYS C  1 92  ? 12.492  -10.589 39.103 0.80 35.81  ? 91  LYS C CB  1 
ATOM   2903  C  CG  . LYS C  1 92  ? 11.015  -10.228 38.950 0.80 40.76  ? 91  LYS C CG  1 
ATOM   2904  C  CD  . LYS C  1 92  ? 10.229  -11.324 38.267 0.80 41.89  ? 91  LYS C CD  1 
ATOM   2905  C  CE  . LYS C  1 92  ? 8.800   -11.483 38.754 0.80 41.79  ? 91  LYS C CE  1 
ATOM   2906  N  NZ  . LYS C  1 92  ? 8.469   -12.919 38.938 0.80 43.54  ? 91  LYS C NZ  1 
ATOM   2907  N  N   . ASP C  1 93  ? 12.726  -7.201  39.672 1.00 29.12  ? 92  ASP C N   1 
ATOM   2908  C  CA  . ASP C  1 93  ? 12.584  -5.890  39.054 1.00 29.15  ? 92  ASP C CA  1 
ATOM   2909  C  C   . ASP C  1 93  ? 13.692  -4.947  39.518 1.00 29.10  ? 92  ASP C C   1 
ATOM   2910  O  O   . ASP C  1 93  ? 13.737  -3.796  39.100 1.00 29.22  ? 92  ASP C O   1 
ATOM   2911  C  CB  . ASP C  1 93  ? 11.238  -5.254  39.398 1.00 30.10  ? 92  ASP C CB  1 
ATOM   2912  C  CG  . ASP C  1 93  ? 10.063  -6.011  38.818 1.00 32.71  ? 92  ASP C CG  1 
ATOM   2913  O  OD1 . ASP C  1 93  ? 10.154  -6.434  37.640 1.00 33.59  ? 92  ASP C OD1 1 
ATOM   2914  O  OD2 . ASP C  1 93  ? 9.060   -6.160  39.540 1.00 35.07  ? 92  ASP C OD2 1 
ATOM   2915  N  N   . GLY C  1 94  ? 14.564  -5.426  40.409 1.00 28.58  ? 93  GLY C N   1 
ATOM   2916  C  CA  . GLY C  1 94  ? 15.666  -4.615  40.892 1.00 26.95  ? 93  GLY C CA  1 
ATOM   2917  C  C   . GLY C  1 94  ? 15.238  -3.685  42.027 1.00 26.77  ? 93  GLY C C   1 
ATOM   2918  O  O   . GLY C  1 94  ? 15.898  -2.679  42.288 1.00 26.32  ? 93  GLY C O   1 
ATOM   2919  N  N   . VAL C  1 95  ? 14.144  -4.047  42.708 1.00 25.94  ? 94  VAL C N   1 
ATOM   2920  C  CA  . VAL C  1 95  ? 13.668  -3.248  43.823 1.00 27.37  ? 94  VAL C CA  1 
ATOM   2921  C  C   . VAL C  1 95  ? 13.868  -4.018  45.125 1.00 26.57  ? 94  VAL C C   1 
ATOM   2922  O  O   . VAL C  1 95  ? 13.443  -5.161  45.246 1.00 28.97  ? 94  VAL C O   1 
ATOM   2923  C  CB  . VAL C  1 95  ? 12.194  -2.828  43.632 1.00 26.59  ? 94  VAL C CB  1 
ATOM   2924  C  CG1 . VAL C  1 95  ? 11.646  -2.098  44.860 1.00 24.08  ? 94  VAL C CG1 1 
ATOM   2925  C  CG2 . VAL C  1 95  ? 12.030  -1.992  42.374 1.00 25.76  ? 94  VAL C CG2 1 
ATOM   2926  N  N   . ALA C  1 96  ? 14.492  -3.368  46.105 1.00 23.95  ? 95  ALA C N   1 
ATOM   2927  C  CA  . ALA C  1 96  ? 14.601  -3.941  47.433 1.00 24.23  ? 95  ALA C CA  1 
ATOM   2928  C  C   . ALA C  1 96  ? 13.643  -3.224  48.374 1.00 25.31  ? 95  ALA C C   1 
ATOM   2929  O  O   . ALA C  1 96  ? 13.803  -2.028  48.594 1.00 26.28  ? 95  ALA C O   1 
ATOM   2930  C  CB  . ALA C  1 96  ? 16.023  -3.827  47.919 1.00 23.00  ? 95  ALA C CB  1 
ATOM   2931  N  N   . ASP C  1 97  ? 12.653  -3.950  48.910 1.00 26.58  ? 96  ASP C N   1 
ATOM   2932  C  CA  . ASP C  1 97  ? 11.789  -3.348  49.917 1.00 27.21  ? 96  ASP C CA  1 
ATOM   2933  C  C   . ASP C  1 97  ? 12.409  -3.599  51.278 1.00 25.84  ? 96  ASP C C   1 
ATOM   2934  O  O   . ASP C  1 97  ? 12.180  -4.643  51.865 1.00 30.72  ? 96  ASP C O   1 
ATOM   2935  C  CB  . ASP C  1 97  ? 10.316  -3.774  49.825 1.00 27.92  ? 96  ASP C CB  1 
ATOM   2936  C  CG  . ASP C  1 97  ? 9.648   -3.311  48.550 1.00 30.20  ? 96  ASP C CG  1 
ATOM   2937  O  OD1 . ASP C  1 97  ? 9.712   -2.101  48.278 1.00 35.65  ? 96  ASP C OD1 1 
ATOM   2938  O  OD2 . ASP C  1 97  ? 9.082   -4.156  47.840 1.00 30.42  ? 96  ASP C OD2 1 
ATOM   2939  N  N   . VAL C  1 98  ? 13.185  -2.632  51.753 1.00 22.60  ? 97  VAL C N   1 
ATOM   2940  C  CA  . VAL C  1 98  ? 13.967  -2.810  52.956 1.00 22.76  ? 97  VAL C CA  1 
ATOM   2941  C  C   . VAL C  1 98  ? 13.064  -2.731  54.181 1.00 22.75  ? 97  VAL C C   1 
ATOM   2942  O  O   . VAL C  1 98  ? 12.203  -1.860  54.294 1.00 24.30  ? 97  VAL C O   1 
ATOM   2943  C  CB  . VAL C  1 98  ? 15.080  -1.752  53.036 1.00 23.15  ? 97  VAL C CB  1 
ATOM   2944  C  CG1 . VAL C  1 98  ? 15.929  -1.926  54.292 1.00 23.62  ? 97  VAL C CG1 1 
ATOM   2945  C  CG2 . VAL C  1 98  ? 15.940  -1.770  51.776 1.00 22.43  ? 97  VAL C CG2 1 
ATOM   2946  N  N   . SER C  1 99  ? 13.297  -3.660  55.109 1.00 21.66  ? 98  SER C N   1 
ATOM   2947  C  CA  . SER C  1 99  ? 12.649  -3.635  56.401 1.00 21.40  ? 98  SER C CA  1 
ATOM   2948  C  C   . SER C  1 99  ? 13.500  -4.419  57.393 1.00 21.77  ? 98  SER C C   1 
ATOM   2949  O  O   . SER C  1 99  ? 13.639  -5.641  57.268 1.00 22.82  ? 98  SER C O   1 
ATOM   2950  C  CB  . SER C  1 99  ? 11.274  -4.197  56.289 1.00 22.44  ? 98  SER C CB  1 
ATOM   2951  O  OG  . SER C  1 99  ? 10.668  -4.294  57.570 1.00 22.80  ? 98  SER C OG  1 
ATOM   2952  N  N   . ILE C  1 100 ? 14.081  -3.697  58.357 1.00 21.03  ? 99  ILE C N   1 
ATOM   2953  C  CA  . ILE C  1 100 ? 15.019  -4.279  59.300 1.00 20.80  ? 99  ILE C CA  1 
ATOM   2954  C  C   . ILE C  1 100 ? 14.694  -3.714  60.671 1.00 22.04  ? 99  ILE C C   1 
ATOM   2955  O  O   . ILE C  1 100 ? 14.243  -2.576  60.793 1.00 23.15  ? 99  ILE C O   1 
ATOM   2956  C  CB  . ILE C  1 100 ? 16.472  -3.937  58.894 1.00 18.55  ? 99  ILE C CB  1 
ATOM   2957  C  CG1 . ILE C  1 100 ? 16.942  -4.808  57.733 1.00 17.30  ? 99  ILE C CG1 1 
ATOM   2958  C  CG2 . ILE C  1 100 ? 17.439  -4.029  60.057 1.00 16.88  ? 99  ILE C CG2 1 
ATOM   2959  C  CD1 . ILE C  1 100 ? 18.198  -4.310  57.084 1.00 18.69  ? 99  ILE C CD1 1 
ATOM   2960  N  N   . GLU C  1 101 ? 14.983  -4.493  61.703 1.00 24.36  ? 100 GLU C N   1 
ATOM   2961  C  CA  . GLU C  1 101 ? 14.965  -3.944  63.045 1.00 27.95  ? 100 GLU C CA  1 
ATOM   2962  C  C   . GLU C  1 101 ? 16.302  -4.287  63.686 1.00 29.61  ? 100 GLU C C   1 
ATOM   2963  O  O   . GLU C  1 101 ? 16.765  -5.417  63.582 1.00 31.53  ? 100 GLU C O   1 
ATOM   2964  C  CB  . GLU C  1 101 ? 13.755  -4.483  63.790 1.00 32.58  ? 100 GLU C CB  1 
ATOM   2965  C  CG  . GLU C  1 101 ? 13.770  -4.179  65.276 1.00 40.45  ? 100 GLU C CG  1 
ATOM   2966  C  CD  . GLU C  1 101 ? 12.392  -4.258  65.913 1.00 48.60  ? 100 GLU C CD  1 
ATOM   2967  O  OE1 . GLU C  1 101 ? 11.387  -3.948  65.209 1.00 50.28  ? 100 GLU C OE1 1 
ATOM   2968  O  OE2 . GLU C  1 101 ? 12.344  -4.583  67.127 1.00 52.17  ? 100 GLU C OE2 1 
ATOM   2969  N  N   . ASP C  1 102 ? 16.966  -3.290  64.266 1.00 29.89  ? 101 ASP C N   1 
ATOM   2970  C  CA  . ASP C  1 102 ? 18.296  -3.525  64.796 1.00 29.65  ? 101 ASP C CA  1 
ATOM   2971  C  C   . ASP C  1 102 ? 18.401  -2.864  66.162 1.00 28.36  ? 101 ASP C C   1 
ATOM   2972  O  O   . ASP C  1 102 ? 17.847  -1.788  66.367 1.00 28.41  ? 101 ASP C O   1 
ATOM   2973  C  CB  . ASP C  1 102 ? 19.370  -2.995  63.846 1.00 30.13  ? 101 ASP C CB  1 
ATOM   2974  C  CG  . ASP C  1 102 ? 20.747  -3.499  64.227 1.00 31.41  ? 101 ASP C CG  1 
ATOM   2975  O  OD1 . ASP C  1 102 ? 20.974  -4.712  64.044 1.00 33.40  ? 101 ASP C OD1 1 
ATOM   2976  O  OD2 . ASP C  1 102 ? 21.565  -2.695  64.741 1.00 31.88  ? 101 ASP C OD2 1 
ATOM   2977  N  N   . SER C  1 103 ? 19.129  -3.508  67.074 1.00 28.62  ? 102 SER C N   1 
ATOM   2978  C  CA  . SER C  1 103 ? 19.238  -2.992  68.428 1.00 30.83  ? 102 SER C CA  1 
ATOM   2979  C  C   . SER C  1 103 ? 20.648  -2.508  68.749 1.00 29.50  ? 102 SER C C   1 
ATOM   2980  O  O   . SER C  1 103 ? 20.927  -2.138  69.881 1.00 29.43  ? 102 SER C O   1 
ATOM   2981  C  CB  . SER C  1 103 ? 18.758  -3.997  69.420 1.00 34.55  ? 102 SER C CB  1 
ATOM   2982  O  OG  . SER C  1 103 ? 17.357  -3.831  69.589 1.00 45.41  ? 102 SER C OG  1 
ATOM   2983  N  N   . VAL C  1 104 ? 21.524  -2.511  67.741 1.00 27.99  ? 103 VAL C N   1 
ATOM   2984  C  CA  . VAL C  1 104 ? 22.909  -2.150  67.968 1.00 26.47  ? 103 VAL C CA  1 
ATOM   2985  C  C   . VAL C  1 104 ? 23.131  -0.722  67.489 1.00 26.50  ? 103 VAL C C   1 
ATOM   2986  O  O   . VAL C  1 104 ? 23.756  0.070   68.201 1.00 31.78  ? 103 VAL C O   1 
ATOM   2987  C  CB  . VAL C  1 104 ? 23.888  -3.149  67.328 1.00 25.57  ? 103 VAL C CB  1 
ATOM   2988  C  CG1 . VAL C  1 104 ? 25.336  -2.671  67.399 1.00 25.11  ? 103 VAL C CG1 1 
ATOM   2989  C  CG2 . VAL C  1 104 ? 23.754  -4.530  67.944 1.00 24.72  ? 103 VAL C CG2 1 
ATOM   2990  N  N   . ILE C  1 105 ? 22.625  -0.398  66.296 1.00 25.20  ? 104 ILE C N   1 
ATOM   2991  C  CA  . ILE C  1 105 ? 22.621  0.988   65.867 1.00 26.63  ? 104 ILE C CA  1 
ATOM   2992  C  C   . ILE C  1 105 ? 21.700  1.769   66.794 1.00 29.48  ? 104 ILE C C   1 
ATOM   2993  O  O   . ILE C  1 105 ? 20.835  1.187   67.446 1.00 31.91  ? 104 ILE C O   1 
ATOM   2994  C  CB  . ILE C  1 105 ? 22.216  1.146   64.392 1.00 25.47  ? 104 ILE C CB  1 
ATOM   2995  C  CG1 . ILE C  1 105 ? 20.777  0.692   64.151 1.00 24.29  ? 104 ILE C CG1 1 
ATOM   2996  C  CG2 . ILE C  1 105 ? 23.198  0.434   63.489 1.00 24.89  ? 104 ILE C CG2 1 
ATOM   2997  C  CD1 . ILE C  1 105 ? 20.233  1.114   62.801 1.00 24.16  ? 104 ILE C CD1 1 
ATOM   2998  N  N   . SER C  1 106 ? 21.917  3.090   66.860 1.00 30.74  ? 105 SER C N   1 
ATOM   2999  C  CA  . SER C  1 106 ? 21.052  3.948   67.647 1.00 28.91  ? 105 SER C CA  1 
ATOM   3000  C  C   . SER C  1 106 ? 20.891  5.303   66.975 1.00 29.18  ? 105 SER C C   1 
ATOM   3001  O  O   . SER C  1 106 ? 21.710  5.685   66.150 1.00 28.29  ? 105 SER C O   1 
ATOM   3002  C  CB  . SER C  1 106 ? 21.595  4.097   69.041 1.00 28.80  ? 105 SER C CB  1 
ATOM   3003  O  OG  . SER C  1 106 ? 20.608  4.661   69.879 1.00 27.51  ? 105 SER C OG  1 
ATOM   3004  N  N   . LEU C  1 107 ? 19.837  6.028   67.344 1.00 28.96  ? 106 LEU C N   1 
ATOM   3005  C  CA  . LEU C  1 107 ? 19.670  7.407   66.914 1.00 29.38  ? 106 LEU C CA  1 
ATOM   3006  C  C   . LEU C  1 107 ? 19.950  8.363   68.076 1.00 32.01  ? 106 LEU C C   1 
ATOM   3007  O  O   . LEU C  1 107 ? 19.648  9.547   67.988 1.00 35.32  ? 106 LEU C O   1 
ATOM   3008  C  CB  . LEU C  1 107 ? 18.265  7.607   66.337 1.00 27.71  ? 106 LEU C CB  1 
ATOM   3009  C  CG  . LEU C  1 107 ? 17.880  6.664   65.194 1.00 27.04  ? 106 LEU C CG  1 
ATOM   3010  C  CD1 . LEU C  1 107 ? 16.529  7.001   64.600 1.00 27.02  ? 106 LEU C CD1 1 
ATOM   3011  C  CD2 . LEU C  1 107 ? 18.922  6.684   64.095 1.00 26.85  ? 106 LEU C CD2 1 
ATOM   3012  N  N   . SER C  1 108 ? 20.526  7.854   69.171 1.00 35.69  ? 107 SER C N   1 
ATOM   3013  C  CA  . SER C  1 108 ? 21.049  8.684   70.249 1.00 39.75  ? 107 SER C CA  1 
ATOM   3014  C  C   . SER C  1 108 ? 22.122  7.920   71.027 1.00 43.70  ? 107 SER C C   1 
ATOM   3015  O  O   . SER C  1 108 ? 22.204  6.696   70.959 1.00 49.27  ? 107 SER C O   1 
ATOM   3016  C  CB  . SER C  1 108 ? 19.942  9.168   71.140 1.00 40.69  ? 107 SER C CB  1 
ATOM   3017  O  OG  . SER C  1 108 ? 19.297  8.079   71.774 1.00 46.06  ? 107 SER C OG  1 
ATOM   3018  N  N   . GLY C  1 109 ? 22.978  8.665   71.742 1.00 45.46  ? 108 GLY C N   1 
ATOM   3019  C  CA  . GLY C  1 109 ? 23.991  8.067   72.598 1.00 49.61  ? 108 GLY C CA  1 
ATOM   3020  C  C   . GLY C  1 109 ? 25.247  7.707   71.815 1.00 56.59  ? 108 GLY C C   1 
ATOM   3021  O  O   . GLY C  1 109 ? 25.484  8.241   70.736 1.00 60.27  ? 108 GLY C O   1 
ATOM   3022  N  N   . ASP C  1 110 ? 25.990  6.721   72.318 1.00 64.42  ? 109 ASP C N   1 
ATOM   3023  C  CA  . ASP C  1 110 ? 27.315  6.403   71.812 1.00 71.39  ? 109 ASP C CA  1 
ATOM   3024  C  C   . ASP C  1 110 ? 27.256  5.842   70.389 1.00 65.37  ? 109 ASP C C   1 
ATOM   3025  O  O   . ASP C  1 110 ? 28.235  5.908   69.661 1.00 51.86  ? 109 ASP C O   1 
ATOM   3026  C  CB  . ASP C  1 110 ? 28.040  5.428   72.744 1.00 91.46  ? 109 ASP C CB  1 
ATOM   3027  C  CG  . ASP C  1 110 ? 29.509  5.253   72.364 1.00 101.46 ? 109 ASP C CG  1 
ATOM   3028  O  OD1 . ASP C  1 110 ? 30.190  6.290   72.275 1.00 112.39 ? 109 ASP C OD1 1 
ATOM   3029  O  OD2 . ASP C  1 110 ? 29.965  4.097   72.120 1.00 91.46  ? 109 ASP C OD2 1 
ATOM   3030  N  N   . HIS C  1 111 ? 26.137  5.255   69.985 1.00 66.86  ? 110 HIS C N   1 
ATOM   3031  C  CA  . HIS C  1 111 ? 26.145  4.582   68.698 1.00 69.24  ? 110 HIS C CA  1 
ATOM   3032  C  C   . HIS C  1 111 ? 25.309  5.353   67.685 1.00 63.72  ? 110 HIS C C   1 
ATOM   3033  O  O   . HIS C  1 111 ? 24.774  4.758   66.768 1.00 65.35  ? 110 HIS C O   1 
ATOM   3034  C  CB  . HIS C  1 111 ? 25.791  3.087   68.830 1.00 79.43  ? 110 HIS C CB  1 
ATOM   3035  C  CG  . HIS C  1 111 ? 26.630  2.340   69.816 1.00 89.71  ? 110 HIS C CG  1 
ATOM   3036  N  ND1 . HIS C  1 111 ? 26.134  1.231   70.499 1.00 79.31  ? 110 HIS C ND1 1 
ATOM   3037  C  CD2 . HIS C  1 111 ? 27.909  2.508   70.234 1.00 101.50 ? 110 HIS C CD2 1 
ATOM   3038  C  CE1 . HIS C  1 111 ? 27.064  0.774   71.322 1.00 83.96  ? 110 HIS C CE1 1 
ATOM   3039  N  NE2 . HIS C  1 111 ? 28.159  1.559   71.193 1.00 95.56  ? 110 HIS C NE2 1 
ATOM   3040  N  N   . CYS C  1 112 ? 25.223  6.677   67.864 1.00 52.67  ? 111 CYS C N   1 
ATOM   3041  C  CA  . CYS C  1 112 ? 24.412  7.505   66.992 1.00 46.26  ? 111 CYS C CA  1 
ATOM   3042  C  C   . CYS C  1 112 ? 24.965  7.410   65.571 1.00 41.68  ? 111 CYS C C   1 
ATOM   3043  O  O   . CYS C  1 112 ? 26.166  7.492   65.368 1.00 40.75  ? 111 CYS C O   1 
ATOM   3044  C  CB  . CYS C  1 112 ? 24.427  8.935   67.506 1.00 44.75  ? 111 CYS C CB  1 
ATOM   3045  S  SG  . CYS C  1 112 ? 22.945  9.892   67.123 1.00 59.49  ? 111 CYS C SG  1 
ATOM   3046  N  N   . ILE C  1 113 ? 24.080  7.140   64.607 1.00 37.86  ? 112 ILE C N   1 
ATOM   3047  C  CA  . ILE C  1 113 ? 24.465  6.984   63.209 1.00 34.06  ? 112 ILE C CA  1 
ATOM   3048  C  C   . ILE C  1 113 ? 24.111  8.252   62.435 1.00 34.56  ? 112 ILE C C   1 
ATOM   3049  O  O   . ILE C  1 113 ? 24.334  8.319   61.224 1.00 36.31  ? 112 ILE C O   1 
ATOM   3050  C  CB  . ILE C  1 113 ? 23.807  5.740   62.567 1.00 33.50  ? 112 ILE C CB  1 
ATOM   3051  C  CG1 . ILE C  1 113 ? 22.285  5.737   62.718 1.00 31.74  ? 112 ILE C CG1 1 
ATOM   3052  C  CG2 . ILE C  1 113 ? 24.419  4.449   63.093 1.00 31.74  ? 112 ILE C CG2 1 
ATOM   3053  C  CD1 . ILE C  1 113 ? 21.570  4.911   61.690 1.00 31.57  ? 112 ILE C CD1 1 
ATOM   3054  N  N   . ILE C  1 114 ? 23.547  9.253   63.132 1.00 32.10  ? 113 ILE C N   1 
ATOM   3055  C  CA  . ILE C  1 114 ? 23.197  10.514  62.498 1.00 27.86  ? 113 ILE C CA  1 
ATOM   3056  C  C   . ILE C  1 114 ? 24.479  11.170  62.013 1.00 28.38  ? 113 ILE C C   1 
ATOM   3057  O  O   . ILE C  1 114 ? 25.473  11.211  62.734 1.00 32.51  ? 113 ILE C O   1 
ATOM   3058  C  CB  . ILE C  1 114 ? 22.431  11.428  63.459 1.00 27.11  ? 113 ILE C CB  1 
ATOM   3059  C  CG1 . ILE C  1 114 ? 21.226  10.696  64.055 1.00 27.81  ? 113 ILE C CG1 1 
ATOM   3060  C  CG2 . ILE C  1 114 ? 22.046  12.725  62.770 1.00 25.30  ? 113 ILE C CG2 1 
ATOM   3061  C  CD1 . ILE C  1 114 ? 20.142  11.592  64.563 1.00 27.25  ? 113 ILE C CD1 1 
ATOM   3062  N  N   . GLY C  1 115 ? 24.444  11.641  60.768 1.00 26.56  ? 114 GLY C N   1 
ATOM   3063  C  CA  . GLY C  1 115 ? 25.556  12.348  60.162 1.00 24.58  ? 114 GLY C CA  1 
ATOM   3064  C  C   . GLY C  1 115 ? 26.642  11.402  59.655 1.00 24.29  ? 114 GLY C C   1 
ATOM   3065  O  O   . GLY C  1 115 ? 27.752  11.847  59.345 1.00 25.36  ? 114 GLY C O   1 
ATOM   3066  N  N   . ARG C  1 116 ? 26.308  10.105  59.571 1.00 22.60  ? 115 ARG C N   1 
ATOM   3067  C  CA  . ARG C  1 116 ? 27.178  9.107   58.961 1.00 20.14  ? 115 ARG C CA  1 
ATOM   3068  C  C   . ARG C  1 116 ? 26.575  8.678   57.625 1.00 18.96  ? 115 ARG C C   1 
ATOM   3069  O  O   . ARG C  1 116 ? 25.625  9.300   57.158 1.00 19.39  ? 115 ARG C O   1 
ATOM   3070  C  CB  . ARG C  1 116 ? 27.469  7.993   59.968 1.00 19.95  ? 115 ARG C CB  1 
ATOM   3071  C  CG  . ARG C  1 116 ? 27.961  8.542   61.302 1.00 19.50  ? 115 ARG C CG  1 
ATOM   3072  C  CD  . ARG C  1 116 ? 28.445  7.465   62.236 1.00 19.45  ? 115 ARG C CD  1 
ATOM   3073  N  NE  . ARG C  1 116 ? 28.941  8.000   63.501 1.00 19.74  ? 115 ARG C NE  1 
ATOM   3074  C  CZ  . ARG C  1 116 ? 30.195  8.386   63.733 1.00 18.43  ? 115 ARG C CZ  1 
ATOM   3075  N  NH1 . ARG C  1 116 ? 31.113  8.295   62.790 1.00 16.97  ? 115 ARG C NH1 1 
ATOM   3076  N  NH2 . ARG C  1 116 ? 30.528  8.848   64.921 1.00 18.16  ? 115 ARG C NH2 1 
ATOM   3077  N  N   . THR C  1 117 ? 27.151  7.659   56.983 1.00 18.20  ? 116 THR C N   1 
ATOM   3078  C  CA  . THR C  1 117 ? 26.680  7.282   55.656 1.00 17.77  ? 116 THR C CA  1 
ATOM   3079  C  C   . THR C  1 117 ? 26.061  5.885   55.660 1.00 17.33  ? 116 THR C C   1 
ATOM   3080  O  O   . THR C  1 117 ? 26.573  4.959   56.285 1.00 17.83  ? 116 THR C O   1 
ATOM   3081  C  CB  . THR C  1 117 ? 27.797  7.354   54.609 1.00 17.05  ? 116 THR C CB  1 
ATOM   3082  O  OG1 . THR C  1 117 ? 28.193  8.717   54.552 1.00 17.80  ? 116 THR C OG1 1 
ATOM   3083  C  CG2 . THR C  1 117 ? 27.350  6.925   53.236 1.00 16.22  ? 116 THR C CG2 1 
ATOM   3084  N  N   . LEU C  1 118 ? 24.963  5.750   54.924 1.00 16.03  ? 117 LEU C N   1 
ATOM   3085  C  CA  . LEU C  1 118 ? 24.416  4.443   54.641 1.00 15.96  ? 117 LEU C CA  1 
ATOM   3086  C  C   . LEU C  1 118 ? 24.832  4.080   53.219 1.00 16.39  ? 117 LEU C C   1 
ATOM   3087  O  O   . LEU C  1 118 ? 24.741  4.915   52.319 1.00 15.97  ? 117 LEU C O   1 
ATOM   3088  C  CB  . LEU C  1 118 ? 22.895  4.530   54.776 1.00 15.94  ? 117 LEU C CB  1 
ATOM   3089  C  CG  . LEU C  1 118 ? 22.126  3.261   54.439 1.00 15.79  ? 117 LEU C CG  1 
ATOM   3090  C  CD1 . LEU C  1 118 ? 22.454  2.184   55.459 1.00 15.90  ? 117 LEU C CD1 1 
ATOM   3091  C  CD2 . LEU C  1 118 ? 20.631  3.530   54.407 1.00 15.48  ? 117 LEU C CD2 1 
ATOM   3092  N  N   . VAL C  1 119 ? 25.311  2.843   53.037 1.00 16.65  ? 118 VAL C N   1 
ATOM   3093  C  CA  . VAL C  1 119 ? 25.807  2.395   51.743 1.00 16.73  ? 118 VAL C CA  1 
ATOM   3094  C  C   . VAL C  1 119 ? 25.144  1.074   51.371 1.00 16.81  ? 118 VAL C C   1 
ATOM   3095  O  O   . VAL C  1 119 ? 25.069  0.152   52.185 1.00 18.17  ? 118 VAL C O   1 
ATOM   3096  C  CB  . VAL C  1 119 ? 27.340  2.218   51.728 1.00 16.16  ? 118 VAL C CB  1 
ATOM   3097  C  CG1 . VAL C  1 119 ? 27.838  1.776   50.358 1.00 15.98  ? 118 VAL C CG1 1 
ATOM   3098  C  CG2 . VAL C  1 119 ? 28.079  3.453   52.200 1.00 16.08  ? 118 VAL C CG2 1 
ATOM   3099  N  N   . VAL C  1 120 ? 24.716  0.987   50.114 1.00 16.55  ? 119 VAL C N   1 
ATOM   3100  C  CA  . VAL C  1 120 ? 24.272  -0.281  49.573 1.00 17.36  ? 119 VAL C CA  1 
ATOM   3101  C  C   . VAL C  1 120 ? 25.329  -0.755  48.575 1.00 18.65  ? 119 VAL C C   1 
ATOM   3102  O  O   . VAL C  1 120 ? 25.713  -0.007  47.669 1.00 18.23  ? 119 VAL C O   1 
ATOM   3103  C  CB  . VAL C  1 120 ? 22.863  -0.171  48.966 1.00 17.08  ? 119 VAL C CB  1 
ATOM   3104  C  CG1 . VAL C  1 120 ? 22.776  0.862   47.851 1.00 16.95  ? 119 VAL C CG1 1 
ATOM   3105  C  CG2 . VAL C  1 120 ? 22.352  -1.520  48.501 1.00 18.05  ? 119 VAL C CG2 1 
ATOM   3106  N  N   . HIS C  1 121 ? 25.774  -2.006  48.758 1.00 19.63  ? 120 HIS C N   1 
ATOM   3107  C  CA  . HIS C  1 121 ? 26.940  -2.544  48.074 1.00 22.03  ? 120 HIS C CA  1 
ATOM   3108  C  C   . HIS C  1 121 ? 26.570  -3.406  46.867 1.00 24.00  ? 120 HIS C C   1 
ATOM   3109  O  O   . HIS C  1 121 ? 25.410  -3.751  46.660 1.00 24.48  ? 120 HIS C O   1 
ATOM   3110  C  CB  . HIS C  1 121 ? 27.800  -3.342  49.048 1.00 21.85  ? 120 HIS C CB  1 
ATOM   3111  C  CG  . HIS C  1 121 ? 28.544  -2.495  50.018 1.00 21.93  ? 120 HIS C CG  1 
ATOM   3112  N  ND1 . HIS C  1 121 ? 29.827  -2.063  49.774 1.00 20.86  ? 120 HIS C ND1 1 
ATOM   3113  C  CD2 . HIS C  1 121 ? 28.204  -2.024  51.237 1.00 23.28  ? 120 HIS C CD2 1 
ATOM   3114  C  CE1 . HIS C  1 121 ? 30.248  -1.357  50.811 1.00 21.86  ? 120 HIS C CE1 1 
ATOM   3115  N  NE2 . HIS C  1 121 ? 29.277  -1.322  51.723 1.00 22.88  ? 120 HIS C NE2 1 
ATOM   3116  N  N   . GLU C  1 122 ? 27.604  -3.792  46.113 1.00 25.23  ? 121 GLU C N   1 
ATOM   3117  C  CA  . GLU C  1 122 ? 27.482  -4.402  44.803 1.00 28.70  ? 121 GLU C CA  1 
ATOM   3118  C  C   . GLU C  1 122 ? 27.007  -5.853  44.908 1.00 30.28  ? 121 GLU C C   1 
ATOM   3119  O  O   . GLU C  1 122 ? 26.167  -6.270  44.118 1.00 30.80  ? 121 GLU C O   1 
ATOM   3120  C  CB  . GLU C  1 122 ? 28.841  -4.271  44.128 1.00 31.73  ? 121 GLU C CB  1 
ATOM   3121  C  CG  . GLU C  1 122 ? 29.081  -5.236  42.991 1.00 32.52  ? 121 GLU C CG  1 
ATOM   3122  C  CD  . GLU C  1 122 ? 30.568  -5.280  42.645 1.00 34.28  ? 121 GLU C CD  1 
ATOM   3123  O  OE1 . GLU C  1 122 ? 30.892  -5.329  41.427 1.00 34.88  ? 121 GLU C OE1 1 
ATOM   3124  O  OE2 . GLU C  1 122 ? 31.419  -5.172  43.591 1.00 32.31  ? 121 GLU C OE2 1 
ATOM   3125  N  N   . LYS C  1 123 ? 27.547  -6.595  45.890 1.00 31.46  ? 122 LYS C N   1 
ATOM   3126  C  CA  . LYS C  1 123 ? 27.360  -8.034  46.044 1.00 30.06  ? 122 LYS C CA  1 
ATOM   3127  C  C   . LYS C  1 123 ? 26.830  -8.354  47.445 1.00 28.60  ? 122 LYS C C   1 
ATOM   3128  O  O   . LYS C  1 123 ? 26.667  -7.470  48.284 1.00 27.90  ? 122 LYS C O   1 
ATOM   3129  C  CB  . LYS C  1 123 ? 28.705  -8.752  45.910 1.00 32.84  ? 122 LYS C CB  1 
ATOM   3130  C  CG  . LYS C  1 123 ? 29.379  -8.642  44.540 1.00 38.75  ? 122 LYS C CG  1 
ATOM   3131  C  CD  . LYS C  1 123 ? 30.693  -9.404  44.390 1.00 39.53  ? 122 LYS C CD  1 
ATOM   3132  C  CE  . LYS C  1 123 ? 31.852  -8.779  45.142 1.00 39.08  ? 122 LYS C CE  1 
ATOM   3133  N  NZ  . LYS C  1 123 ? 33.102  -9.544  44.916 1.00 38.71  ? 122 LYS C NZ  1 
ATOM   3134  N  N   . ALA C  1 124 ? 26.605  -9.648  47.699 1.00 26.15  ? 123 ALA C N   1 
ATOM   3135  C  CA  . ALA C  1 124 ? 26.159  -10.123 48.997 1.00 24.64  ? 123 ALA C CA  1 
ATOM   3136  C  C   . ALA C  1 124 ? 27.237  -9.876  50.054 1.00 23.32  ? 123 ALA C C   1 
ATOM   3137  O  O   . ALA C  1 124 ? 28.425  -9.949  49.772 1.00 23.85  ? 123 ALA C O   1 
ATOM   3138  C  CB  . ALA C  1 124 ? 25.845  -11.589 48.910 1.00 24.68  ? 123 ALA C CB  1 
ATOM   3139  N  N   . ASP C  1 125 ? 26.795  -9.561  51.270 1.00 22.44  ? 124 ASP C N   1 
ATOM   3140  C  CA  . ASP C  1 125 ? 27.658  -9.528  52.433 1.00 21.70  ? 124 ASP C CA  1 
ATOM   3141  C  C   . ASP C  1 125 ? 27.729  -10.954 52.984 1.00 22.89  ? 124 ASP C C   1 
ATOM   3142  O  O   . ASP C  1 125 ? 26.699  -11.538 53.314 1.00 24.25  ? 124 ASP C O   1 
ATOM   3143  C  CB  . ASP C  1 125 ? 27.103  -8.520  53.443 1.00 20.25  ? 124 ASP C CB  1 
ATOM   3144  C  CG  . ASP C  1 125 ? 27.809  -8.495  54.793 1.00 20.55  ? 124 ASP C CG  1 
ATOM   3145  O  OD1 . ASP C  1 125 ? 28.708  -9.321  55.017 1.00 21.85  ? 124 ASP C OD1 1 
ATOM   3146  O  OD2 . ASP C  1 125 ? 27.442  -7.656  55.625 1.00 20.26  ? 124 ASP C OD2 1 
ATOM   3147  N  N   . ASP C  1 126 ? 28.939  -11.511 53.102 1.00 21.62  ? 125 ASP C N   1 
ATOM   3148  C  CA  . ASP C  1 126 ? 29.094  -12.896 53.527 1.00 20.04  ? 125 ASP C CA  1 
ATOM   3149  C  C   . ASP C  1 126 ? 29.015  -13.024 55.051 1.00 19.66  ? 125 ASP C C   1 
ATOM   3150  O  O   . ASP C  1 126 ? 29.227  -14.109 55.590 1.00 20.76  ? 125 ASP C O   1 
ATOM   3151  C  CB  . ASP C  1 126 ? 30.318  -13.566 52.889 1.00 19.45  ? 125 ASP C CB  1 
ATOM   3152  C  CG  . ASP C  1 126 ? 31.670  -13.103 53.421 1.00 19.71  ? 125 ASP C CG  1 
ATOM   3153  O  OD1 . ASP C  1 126 ? 31.723  -12.593 54.580 1.00 19.09  ? 125 ASP C OD1 1 
ATOM   3154  O  OD2 . ASP C  1 126 ? 32.679  -13.277 52.676 1.00 18.88  ? 125 ASP C OD2 1 
ATOM   3155  N  N   . LEU C  1 127 ? 28.698  -11.922 55.736 1.00 19.48  ? 126 LEU C N   1 
ATOM   3156  C  CA  . LEU C  1 127 ? 28.456  -11.903 57.173 1.00 20.49  ? 126 LEU C CA  1 
ATOM   3157  C  C   . LEU C  1 127 ? 29.672  -12.420 57.946 1.00 21.45  ? 126 LEU C C   1 
ATOM   3158  O  O   . LEU C  1 127 ? 29.539  -12.866 59.089 1.00 23.17  ? 126 LEU C O   1 
ATOM   3159  C  CB  . LEU C  1 127 ? 27.203  -12.722 57.516 1.00 20.69  ? 126 LEU C CB  1 
ATOM   3160  C  CG  . LEU C  1 127 ? 25.956  -12.458 56.669 1.00 19.73  ? 126 LEU C CG  1 
ATOM   3161  C  CD1 . LEU C  1 127 ? 24.788  -13.304 57.149 1.00 19.00  ? 126 LEU C CD1 1 
ATOM   3162  C  CD2 . LEU C  1 127 ? 25.615  -10.981 56.643 1.00 19.17  ? 126 LEU C CD2 1 
ATOM   3163  N  N   . GLY C  1 128 ? 30.852  -12.342 57.313 1.00 20.91  ? 127 GLY C N   1 
ATOM   3164  C  CA  . GLY C  1 128 ? 32.121  -12.584 57.980 1.00 20.86  ? 127 GLY C CA  1 
ATOM   3165  C  C   . GLY C  1 128 ? 32.513  -14.059 57.987 1.00 22.05  ? 127 GLY C C   1 
ATOM   3166  O  O   . GLY C  1 128 ? 33.392  -14.463 58.741 1.00 23.14  ? 127 GLY C O   1 
ATOM   3167  N  N   . LYS C  1 129 ? 31.871  -14.853 57.128 1.00 22.98  ? 128 LYS C N   1 
ATOM   3168  C  CA  . LYS C  1 129 ? 32.037  -16.298 57.132 1.00 23.83  ? 128 LYS C CA  1 
ATOM   3169  C  C   . LYS C  1 129 ? 32.655  -16.747 55.811 1.00 23.94  ? 128 LYS C C   1 
ATOM   3170  O  O   . LYS C  1 129 ? 32.399  -17.860 55.361 1.00 23.37  ? 128 LYS C O   1 
ATOM   3171  C  CB  . LYS C  1 129 ? 30.685  -16.984 57.314 1.00 25.13  ? 128 LYS C CB  1 
ATOM   3172  C  CG  . LYS C  1 129 ? 29.893  -16.520 58.534 1.00 26.10  ? 128 LYS C CG  1 
ATOM   3173  C  CD  . LYS C  1 129 ? 28.440  -16.875 58.529 1.00 26.99  ? 128 LYS C CD  1 
ATOM   3174  C  CE  . LYS C  1 129 ? 27.848  -17.870 59.520 1.00 28.31  ? 128 LYS C CE  1 
ATOM   3175  N  NZ  . LYS C  1 129 ? 26.919  -18.716 58.735 1.00 29.82  ? 128 LYS C NZ  1 
ATOM   3176  N  N   . GLY C  1 130 ? 33.494  -15.892 55.217 1.00 24.41  ? 129 GLY C N   1 
ATOM   3177  C  CA  . GLY C  1 130 ? 34.079  -16.157 53.912 1.00 23.53  ? 129 GLY C CA  1 
ATOM   3178  C  C   . GLY C  1 130 ? 35.490  -16.728 54.012 1.00 24.20  ? 129 GLY C C   1 
ATOM   3179  O  O   . GLY C  1 130 ? 36.054  -17.133 52.996 1.00 23.94  ? 129 GLY C O   1 
ATOM   3180  N  N   . GLY C  1 131 ? 36.052  -16.714 55.235 1.00 23.97  ? 130 GLY C N   1 
ATOM   3181  C  CA  . GLY C  1 131 ? 37.320  -17.346 55.538 1.00 26.28  ? 130 GLY C CA  1 
ATOM   3182  C  C   . GLY C  1 131 ? 38.523  -16.662 54.891 1.00 29.82  ? 130 GLY C C   1 
ATOM   3183  O  O   . GLY C  1 131 ? 39.561  -17.289 54.695 1.00 34.42  ? 130 GLY C O   1 
ATOM   3184  N  N   . ASN C  1 132 ? 38.390  -15.374 54.561 1.00 30.34  ? 131 ASN C N   1 
ATOM   3185  C  CA  . ASN C  1 132 ? 39.536  -14.574 54.161 1.00 30.41  ? 131 ASN C CA  1 
ATOM   3186  C  C   . ASN C  1 132 ? 39.564  -13.293 54.984 1.00 32.83  ? 131 ASN C C   1 
ATOM   3187  O  O   . ASN C  1 132 ? 38.651  -13.039 55.780 1.00 32.27  ? 131 ASN C O   1 
ATOM   3188  C  CB  . ASN C  1 132 ? 39.612  -14.354 52.649 1.00 29.34  ? 131 ASN C CB  1 
ATOM   3189  C  CG  . ASN C  1 132 ? 38.407  -13.656 52.055 1.00 30.81  ? 131 ASN C CG  1 
ATOM   3190  O  OD1 . ASN C  1 132 ? 37.634  -13.008 52.755 1.00 30.64  ? 131 ASN C OD1 1 
ATOM   3191  N  ND2 . ASN C  1 132 ? 38.256  -13.756 50.752 1.00 31.11  ? 131 ASN C ND2 1 
ATOM   3192  N  N   . GLU C  1 133 ? 40.618  -12.499 54.787 1.00 36.03  ? 132 GLU C N   1 
ATOM   3193  C  CA  . GLU C  1 133 ? 40.813  -11.342 55.644 1.00 37.43  ? 132 GLU C CA  1 
ATOM   3194  C  C   . GLU C  1 133 ? 39.741  -10.305 55.323 1.00 34.87  ? 132 GLU C C   1 
ATOM   3195  O  O   . GLU C  1 133 ? 39.194  -9.665  56.218 1.00 32.87  ? 132 GLU C O   1 
ATOM   3196  C  CB  . GLU C  1 133 ? 42.235  -10.799 55.563 1.00 45.04  ? 132 GLU C CB  1 
ATOM   3197  C  CG  . GLU C  1 133 ? 42.485  -9.877  56.731 1.00 58.71  ? 132 GLU C CG  1 
ATOM   3198  C  CD  . GLU C  1 133 ? 43.858  -9.299  56.904 1.00 69.71  ? 132 GLU C CD  1 
ATOM   3199  O  OE1 . GLU C  1 133 ? 44.825  -9.960  56.481 1.00 79.21  ? 132 GLU C OE1 1 
ATOM   3200  O  OE2 . GLU C  1 133 ? 43.934  -8.188  57.463 1.00 74.33  ? 132 GLU C OE2 1 
ATOM   3201  N  N   . GLU C  1 134 ? 39.436  -10.207 54.032 1.00 32.17  ? 133 GLU C N   1 
ATOM   3202  C  CA  . GLU C  1 134 ? 38.419  -9.317  53.496 1.00 32.64  ? 133 GLU C CA  1 
ATOM   3203  C  C   . GLU C  1 134 ? 37.077  -9.560  54.192 1.00 31.82  ? 133 GLU C C   1 
ATOM   3204  O  O   . GLU C  1 134 ? 36.376  -8.614  54.548 1.00 32.44  ? 133 GLU C O   1 
ATOM   3205  C  CB  . GLU C  1 134 ? 38.338  -9.519  51.979 1.00 34.79  ? 133 GLU C CB  1 
ATOM   3206  C  CG  . GLU C  1 134 ? 37.732  -8.360  51.217 1.00 42.33  ? 133 GLU C CG  1 
ATOM   3207  C  CD  . GLU C  1 134 ? 38.144  -6.942  51.588 1.00 48.62  ? 133 GLU C CD  1 
ATOM   3208  O  OE1 . GLU C  1 134 ? 39.305  -6.716  51.985 1.00 53.98  ? 133 GLU C OE1 1 
ATOM   3209  O  OE2 . GLU C  1 134 ? 37.276  -6.053  51.498 1.00 51.68  ? 133 GLU C OE2 1 
ATOM   3210  N  N   . SER C  1 135 ? 36.729  -10.836 54.392 1.00 28.50  ? 134 SER C N   1 
ATOM   3211  C  CA  . SER C  1 135 ? 35.454  -11.208 54.978 1.00 28.71  ? 134 SER C CA  1 
ATOM   3212  C  C   . SER C  1 135 ? 35.274  -10.539 56.335 1.00 29.47  ? 134 SER C C   1 
ATOM   3213  O  O   . SER C  1 135 ? 34.189  -10.082 56.653 1.00 32.60  ? 134 SER C O   1 
ATOM   3214  C  CB  . SER C  1 135 ? 35.299  -12.704 55.075 1.00 28.67  ? 134 SER C CB  1 
ATOM   3215  O  OG  . SER C  1 135 ? 34.020  -13.068 55.571 1.00 27.67  ? 134 SER C OG  1 
ATOM   3216  N  N   . THR C  1 136 ? 36.335  -10.471 57.135 1.00 30.96  ? 135 THR C N   1 
ATOM   3217  C  CA  . THR C  1 136 ? 36.183  -9.985  58.499 1.00 32.38  ? 135 THR C CA  1 
ATOM   3218  C  C   . THR C  1 136 ? 36.291  -8.461  58.553 1.00 32.21  ? 135 THR C C   1 
ATOM   3219  O  O   . THR C  1 136 ? 36.235  -7.885  59.640 1.00 33.40  ? 135 THR C O   1 
ATOM   3220  C  CB  . THR C  1 136 ? 37.185  -10.623 59.465 1.00 33.73  ? 135 THR C CB  1 
ATOM   3221  O  OG1 . THR C  1 136 ? 38.473  -10.193 59.023 1.00 39.81  ? 135 THR C OG1 1 
ATOM   3222  C  CG2 . THR C  1 136 ? 37.107  -12.130 59.490 1.00 35.60  ? 135 THR C CG2 1 
ATOM   3223  N  N   . LYS C  1 137 ? 36.445  -7.820  57.389 1.00 33.04  ? 136 LYS C N   1 
ATOM   3224  C  CA  . LYS C  1 137 ? 36.471  -6.366  57.303 1.00 35.44  ? 136 LYS C CA  1 
ATOM   3225  C  C   . LYS C  1 137 ? 35.194  -5.848  56.638 1.00 32.80  ? 136 LYS C C   1 
ATOM   3226  O  O   . LYS C  1 137 ? 34.504  -5.001  57.203 1.00 32.06  ? 136 LYS C O   1 
ATOM   3227  C  CB  . LYS C  1 137 ? 37.704  -5.876  56.538 1.00 44.10  ? 136 LYS C CB  1 
ATOM   3228  C  CG  . LYS C  1 137 ? 39.002  -5.847  57.326 1.00 50.44  ? 136 LYS C CG  1 
ATOM   3229  C  CD  . LYS C  1 137 ? 40.201  -5.505  56.460 1.00 55.46  ? 136 LYS C CD  1 
ATOM   3230  C  CE  . LYS C  1 137 ? 41.440  -5.253  57.289 1.00 59.13  ? 136 LYS C CE  1 
ATOM   3231  N  NZ  . LYS C  1 137 ? 42.446  -4.480  56.528 1.00 62.29  ? 136 LYS C NZ  1 
ATOM   3232  N  N   . THR C  1 138 ? 34.882  -6.365  55.444 1.00 28.02  ? 137 THR C N   1 
ATOM   3233  C  CA  . THR C  1 138 ? 33.847  -5.779  54.609 1.00 24.34  ? 137 THR C CA  1 
ATOM   3234  C  C   . THR C  1 138 ? 32.771  -6.793  54.227 1.00 23.62  ? 137 THR C C   1 
ATOM   3235  O  O   . THR C  1 138 ? 31.832  -6.443  53.506 1.00 22.17  ? 137 THR C O   1 
ATOM   3236  C  CB  . THR C  1 138 ? 34.452  -5.228  53.314 1.00 22.45  ? 137 THR C CB  1 
ATOM   3237  O  OG1 . THR C  1 138 ? 34.830  -6.314  52.466 1.00 21.18  ? 137 THR C OG1 1 
ATOM   3238  C  CG2 . THR C  1 138 ? 35.628  -4.320  53.580 1.00 21.01  ? 137 THR C CG2 1 
ATOM   3239  N  N   . GLY C  1 139 ? 32.940  -8.046  54.663 1.00 22.73  ? 138 GLY C N   1 
ATOM   3240  C  CA  . GLY C  1 139 ? 32.058  -9.126  54.267 1.00 22.87  ? 138 GLY C CA  1 
ATOM   3241  C  C   . GLY C  1 139 ? 32.065  -9.393  52.757 1.00 24.48  ? 138 GLY C C   1 
ATOM   3242  O  O   . GLY C  1 139 ? 31.197  -10.105 52.256 1.00 23.56  ? 138 GLY C O   1 
ATOM   3243  N  N   . ASN C  1 140 ? 33.036  -8.820  52.031 1.00 25.62  ? 139 ASN C N   1 
ATOM   3244  C  CA  . ASN C  1 140 ? 33.230  -9.134  50.620 1.00 27.31  ? 139 ASN C CA  1 
ATOM   3245  C  C   . ASN C  1 140 ? 32.067  -8.589  49.788 1.00 27.63  ? 139 ASN C C   1 
ATOM   3246  O  O   . ASN C  1 140 ? 31.767  -9.110  48.716 1.00 27.19  ? 139 ASN C O   1 
ATOM   3247  C  CB  . ASN C  1 140 ? 33.417  -10.634 50.352 1.00 27.09  ? 139 ASN C CB  1 
ATOM   3248  C  CG  . ASN C  1 140 ? 34.794  -11.149 50.734 1.00 28.65  ? 139 ASN C CG  1 
ATOM   3249  O  OD1 . ASN C  1 140 ? 35.791  -10.803 50.107 1.00 28.72  ? 139 ASN C OD1 1 
ATOM   3250  N  ND2 . ASN C  1 140 ? 34.868  -11.975 51.768 1.00 31.45  ? 139 ASN C ND2 1 
ATOM   3251  N  N   . ALA C  1 141 ? 31.443  -7.511  50.277 1.00 29.05  ? 140 ALA C N   1 
ATOM   3252  C  CA  . ALA C  1 141 ? 30.224  -6.979  49.685 1.00 27.56  ? 140 ALA C CA  1 
ATOM   3253  C  C   . ALA C  1 141 ? 30.519  -6.214  48.392 1.00 29.32  ? 140 ALA C C   1 
ATOM   3254  O  O   . ALA C  1 141 ? 29.596  -5.812  47.672 1.00 33.45  ? 140 ALA C O   1 
ATOM   3255  C  CB  . ALA C  1 141 ? 29.504  -6.115  50.689 1.00 26.74  ? 140 ALA C CB  1 
ATOM   3256  N  N   . GLY C  1 142 ? 31.815  -6.012  48.094 1.00 26.75  ? 141 GLY C N   1 
ATOM   3257  C  CA  . GLY C  1 142 ? 32.182  -5.362  46.846 1.00 24.66  ? 141 GLY C CA  1 
ATOM   3258  C  C   . GLY C  1 142 ? 31.963  -3.857  46.921 1.00 25.87  ? 141 GLY C C   1 
ATOM   3259  O  O   . GLY C  1 142 ? 31.939  -3.290  48.018 1.00 27.06  ? 141 GLY C O   1 
ATOM   3260  N  N   . SER C  1 143 ? 31.777  -3.234  45.750 1.00 25.45  ? 142 SER C N   1 
ATOM   3261  C  CA  . SER C  1 143 ? 31.821  -1.783  45.623 1.00 25.57  ? 142 SER C CA  1 
ATOM   3262  C  C   . SER C  1 143 ? 30.565  -1.145  46.215 1.00 26.49  ? 142 SER C C   1 
ATOM   3263  O  O   . SER C  1 143 ? 29.612  -1.840  46.579 1.00 24.83  ? 142 SER C O   1 
ATOM   3264  C  CB  . SER C  1 143 ? 32.032  -1.355  44.194 1.00 24.32  ? 142 SER C CB  1 
ATOM   3265  O  OG  . SER C  1 143 ? 30.915  -1.742  43.395 1.00 25.13  ? 142 SER C OG  1 
ATOM   3266  N  N   . ARG C  1 144 ? 30.598  0.196   46.288 1.00 25.97  ? 143 ARG C N   1 
ATOM   3267  C  CA  . ARG C  1 144 ? 29.545  1.008   46.873 1.00 25.70  ? 143 ARG C CA  1 
ATOM   3268  C  C   . ARG C  1 144 ? 28.659  1.538   45.750 1.00 26.78  ? 143 ARG C C   1 
ATOM   3269  O  O   . ARG C  1 144 ? 29.086  2.389   44.983 1.00 29.59  ? 143 ARG C O   1 
ATOM   3270  C  CB  . ARG C  1 144 ? 30.200  2.134   47.678 1.00 23.38  ? 143 ARG C CB  1 
ATOM   3271  C  CG  . ARG C  1 144 ? 31.156  1.636   48.749 1.00 22.29  ? 143 ARG C CG  1 
ATOM   3272  C  CD  . ARG C  1 144 ? 32.027  2.682   49.383 1.00 23.25  ? 143 ARG C CD  1 
ATOM   3273  N  NE  . ARG C  1 144 ? 32.947  2.097   50.357 1.00 24.66  ? 143 ARG C NE  1 
ATOM   3274  C  CZ  . ARG C  1 144 ? 33.455  2.718   51.418 1.00 24.29  ? 143 ARG C CZ  1 
ATOM   3275  N  NH1 . ARG C  1 144 ? 33.132  3.970   51.685 1.00 28.25  ? 143 ARG C NH1 1 
ATOM   3276  N  NH2 . ARG C  1 144 ? 34.275  2.081   52.224 1.00 23.72  ? 143 ARG C NH2 1 
ATOM   3277  N  N   . LEU C  1 145 ? 27.441  1.013   45.628 1.00 26.40  ? 144 LEU C N   1 
ATOM   3278  C  CA  . LEU C  1 145 ? 26.616  1.339   44.475 1.00 26.18  ? 144 LEU C CA  1 
ATOM   3279  C  C   . LEU C  1 145 ? 25.960  2.702   44.681 1.00 27.79  ? 144 LEU C C   1 
ATOM   3280  O  O   . LEU C  1 145 ? 25.825  3.491   43.740 1.00 30.12  ? 144 LEU C O   1 
ATOM   3281  C  CB  . LEU C  1 145 ? 25.566  0.246   44.277 1.00 26.47  ? 144 LEU C CB  1 
ATOM   3282  C  CG  . LEU C  1 145 ? 26.109  -1.097  43.778 1.00 27.86  ? 144 LEU C CG  1 
ATOM   3283  C  CD1 . LEU C  1 145 ? 24.977  -2.083  43.542 1.00 28.97  ? 144 LEU C CD1 1 
ATOM   3284  C  CD2 . LEU C  1 145 ? 26.931  -0.910  42.514 1.00 27.16  ? 144 LEU C CD2 1 
ATOM   3285  N  N   . ALA C  1 146 ? 25.556  2.970   45.928 1.00 25.97  ? 145 ALA C N   1 
ATOM   3286  C  CA  . ALA C  1 146 ? 24.875  4.208   46.271 1.00 24.42  ? 145 ALA C CA  1 
ATOM   3287  C  C   . ALA C  1 146 ? 24.972  4.428   47.777 1.00 25.53  ? 145 ALA C C   1 
ATOM   3288  O  O   . ALA C  1 146 ? 25.099  3.484   48.567 1.00 26.27  ? 145 ALA C O   1 
ATOM   3289  C  CB  . ALA C  1 146 ? 23.432  4.168   45.823 1.00 23.79  ? 145 ALA C CB  1 
ATOM   3290  N  N   . CYS C  1 147 ? 24.965  5.709   48.159 1.00 26.13  ? 146 CYS C N   1 
ATOM   3291  C  CA  . CYS C  1 147 ? 25.089  6.071   49.557 1.00 24.94  ? 146 CYS C CA  1 
ATOM   3292  C  C   . CYS C  1 147 ? 24.416  7.417   49.769 1.00 23.09  ? 146 CYS C C   1 
ATOM   3293  O  O   . CYS C  1 147 ? 24.010  8.064   48.812 1.00 21.15  ? 146 CYS C O   1 
ATOM   3294  C  CB  . CYS C  1 147 ? 26.553  6.136   49.975 1.00 25.95  ? 146 CYS C CB  1 
ATOM   3295  S  SG  . CYS C  1 147 ? 27.531  7.291   48.988 1.00 26.79  ? 146 CYS C SG  1 
ATOM   3296  N  N   . GLY C  1 148 ? 24.289  7.792   51.042 1.00 21.58  ? 147 GLY C N   1 
ATOM   3297  C  CA  . GLY C  1 148 ? 23.782  9.087   51.442 1.00 20.56  ? 147 GLY C CA  1 
ATOM   3298  C  C   . GLY C  1 148 ? 24.152  9.384   52.887 1.00 21.66  ? 147 GLY C C   1 
ATOM   3299  O  O   . GLY C  1 148 ? 24.427  8.474   53.672 1.00 21.17  ? 147 GLY C O   1 
ATOM   3300  N  N   . VAL C  1 149 ? 24.142  10.675  53.229 1.00 21.82  ? 148 VAL C N   1 
ATOM   3301  C  CA  . VAL C  1 149 ? 24.345  11.033  54.621 1.00 21.83  ? 148 VAL C CA  1 
ATOM   3302  C  C   . VAL C  1 149 ? 23.023  10.861  55.363 1.00 21.25  ? 148 VAL C C   1 
ATOM   3303  O  O   . VAL C  1 149 ? 21.951  11.137  54.836 1.00 20.54  ? 148 VAL C O   1 
ATOM   3304  C  CB  . VAL C  1 149 ? 24.946  12.440  54.759 1.00 22.17  ? 148 VAL C CB  1 
ATOM   3305  C  CG1 . VAL C  1 149 ? 25.278  12.758  56.208 1.00 22.28  ? 148 VAL C CG1 1 
ATOM   3306  C  CG2 . VAL C  1 149 ? 26.184  12.580  53.886 1.00 21.47  ? 148 VAL C CG2 1 
ATOM   3307  N  N   . ILE C  1 150 ? 23.123  10.350  56.588 1.00 21.50  ? 149 ILE C N   1 
ATOM   3308  C  CA  . ILE C  1 150 ? 21.969  10.044  57.413 1.00 20.48  ? 149 ILE C CA  1 
ATOM   3309  C  C   . ILE C  1 150 ? 21.606  11.307  58.179 1.00 19.90  ? 149 ILE C C   1 
ATOM   3310  O  O   . ILE C  1 150 ? 22.370  11.743  59.024 1.00 20.52  ? 149 ILE C O   1 
ATOM   3311  C  CB  . ILE C  1 150 ? 22.303  8.878   58.359 1.00 20.26  ? 149 ILE C CB  1 
ATOM   3312  C  CG1 . ILE C  1 150 ? 22.600  7.584   57.598 1.00 19.33  ? 149 ILE C CG1 1 
ATOM   3313  C  CG2 . ILE C  1 150 ? 21.221  8.686   59.400 1.00 19.99  ? 149 ILE C CG2 1 
ATOM   3314  C  CD1 . ILE C  1 150 ? 23.301  6.543   58.445 1.00 19.16  ? 149 ILE C CD1 1 
ATOM   3315  N  N   . GLY C  1 151 ? 20.432  11.867  57.879 1.00 19.77  ? 150 GLY C N   1 
ATOM   3316  C  CA  . GLY C  1 151 ? 20.044  13.180  58.368 1.00 20.28  ? 150 GLY C CA  1 
ATOM   3317  C  C   . GLY C  1 151 ? 18.735  13.181  59.155 1.00 20.62  ? 150 GLY C C   1 
ATOM   3318  O  O   . GLY C  1 151 ? 17.954  12.236  59.084 1.00 18.48  ? 150 GLY C O   1 
ATOM   3319  N  N   . ILE C  1 152 ? 18.513  14.274  59.897 1.00 22.49  ? 151 ILE C N   1 
ATOM   3320  C  CA  . ILE C  1 152 ? 17.356  14.426  60.765 1.00 24.03  ? 151 ILE C CA  1 
ATOM   3321  C  C   . ILE C  1 152 ? 16.143  14.725  59.896 1.00 27.25  ? 151 ILE C C   1 
ATOM   3322  O  O   . ILE C  1 152 ? 16.240  15.558  58.994 1.00 27.56  ? 151 ILE C O   1 
ATOM   3323  C  CB  . ILE C  1 152 ? 17.603  15.545  61.788 1.00 21.37  ? 151 ILE C CB  1 
ATOM   3324  C  CG1 . ILE C  1 152 ? 18.768  15.198  62.721 1.00 20.62  ? 151 ILE C CG1 1 
ATOM   3325  C  CG2 . ILE C  1 152 ? 16.322  15.856  62.544 1.00 19.87  ? 151 ILE C CG2 1 
ATOM   3326  C  CD1 . ILE C  1 152 ? 19.366  16.405  63.396 1.00 21.81  ? 151 ILE C CD1 1 
ATOM   3327  N  N   . ALA C  1 153 ? 15.029  14.023  60.170 1.00 31.51  ? 152 ALA C N   1 
ATOM   3328  C  CA  . ALA C  1 153 ? 13.792  14.184  59.418 1.00 33.43  ? 152 ALA C CA  1 
ATOM   3329  C  C   . ALA C  1 153 ? 12.712  14.724  60.347 1.00 38.82  ? 152 ALA C C   1 
ATOM   3330  O  O   . ALA C  1 153 ? 12.856  14.702  61.574 1.00 36.97  ? 152 ALA C O   1 
ATOM   3331  C  CB  . ALA C  1 153 ? 13.380  12.873  58.805 1.00 29.90  ? 152 ALA C CB  1 
ATOM   3332  N  N   . GLN C  1 154 ? 11.606  15.189  59.743 1.00 48.33  ? 153 GLN C N   1 
ATOM   3333  C  CA  . GLN C  1 154 ? 10.477  15.699  60.514 1.00 54.09  ? 153 GLN C CA  1 
ATOM   3334  C  C   . GLN C  1 154 ? 9.739   14.567  61.243 1.00 56.67  ? 153 GLN C C   1 
ATOM   3335  O  O   . GLN C  1 154 ? 9.353   13.536  60.664 1.00 53.21  ? 153 GLN C O   1 
ATOM   3336  C  CB  . GLN C  1 154 ? 9.491   16.473  59.643 1.00 56.34  ? 153 GLN C CB  1 
ATOM   3337  C  CG  . GLN C  1 154 ? 8.343   17.033  60.473 1.00 60.42  ? 153 GLN C CG  1 
ATOM   3338  C  CD  . GLN C  1 154 ? 7.682   18.218  59.810 1.00 63.43  ? 153 GLN C CD  1 
ATOM   3339  O  OE1 . GLN C  1 154 ? 7.230   18.145  58.669 1.00 67.31  ? 153 GLN C OE1 1 
ATOM   3340  N  NE2 . GLN C  1 154 ? 7.627   19.328  60.528 1.00 63.55  ? 153 GLN C NE2 1 
ATOM   3341  O  OXT . GLN C  1 154 ? 9.490   14.688  62.448 1.00 59.50  ? 153 GLN C OXT 1 
ATOM   3342  N  N   . ALA D  1 2   ? 38.856  1.184   3.713  1.00 77.82  ? 1   ALA D N   1 
ATOM   3343  C  CA  . ALA D  1 2   ? 39.483  2.119   4.654  1.00 69.25  ? 1   ALA D CA  1 
ATOM   3344  C  C   . ALA D  1 2   ? 38.448  2.919   5.442  1.00 68.00  ? 1   ALA D C   1 
ATOM   3345  O  O   . ALA D  1 2   ? 38.720  4.078   5.730  1.00 73.18  ? 1   ALA D O   1 
ATOM   3346  C  CB  . ALA D  1 2   ? 40.451  3.019   3.905  1.00 63.72  ? 1   ALA D CB  1 
ATOM   3347  N  N   A THR D  1 3   ? 37.333  2.289   5.848  0.50 61.46  ? 2   THR D N   1 
ATOM   3348  N  N   B THR D  1 3   ? 37.334  2.289   5.846  0.50 61.45  ? 2   THR D N   1 
ATOM   3349  C  CA  A THR D  1 3   ? 36.395  2.910   6.769  0.50 55.33  ? 2   THR D CA  1 
ATOM   3350  C  CA  B THR D  1 3   ? 36.395  2.910   6.768  0.50 55.32  ? 2   THR D CA  1 
ATOM   3351  C  C   A THR D  1 3   ? 36.556  2.281   8.160  0.50 51.23  ? 2   THR D C   1 
ATOM   3352  C  C   B THR D  1 3   ? 36.556  2.281   8.160  0.50 51.22  ? 2   THR D C   1 
ATOM   3353  O  O   A THR D  1 3   ? 36.501  1.061   8.319  0.50 50.86  ? 2   THR D O   1 
ATOM   3354  O  O   B THR D  1 3   ? 36.501  1.061   8.319  0.50 50.86  ? 2   THR D O   1 
ATOM   3355  C  CB  A THR D  1 3   ? 34.973  2.972   6.176  0.50 55.90  ? 2   THR D CB  1 
ATOM   3356  C  CB  B THR D  1 3   ? 34.972  2.974   6.176  0.50 55.87  ? 2   THR D CB  1 
ATOM   3357  O  OG1 A THR D  1 3   ? 34.548  1.640   5.902  0.50 66.48  ? 2   THR D OG1 1 
ATOM   3358  O  OG1 B THR D  1 3   ? 34.547  1.641   5.908  0.50 66.42  ? 2   THR D OG1 1 
ATOM   3359  C  CG2 A THR D  1 3   ? 34.897  3.765   4.887  0.50 54.74  ? 2   THR D CG2 1 
ATOM   3360  C  CG2 B THR D  1 3   ? 34.896  3.763   4.885  0.50 54.71  ? 2   THR D CG2 1 
ATOM   3361  N  N   . LYS D  1 4   ? 36.798  3.130   9.170  1.00 49.45  ? 3   LYS D N   1 
ATOM   3362  C  CA  . LYS D  1 4   ? 36.906  2.702   10.558 1.00 46.13  ? 3   LYS D CA  1 
ATOM   3363  C  C   . LYS D  1 4   ? 35.749  3.291   11.365 1.00 42.69  ? 3   LYS D C   1 
ATOM   3364  O  O   . LYS D  1 4   ? 35.426  4.478   11.270 1.00 41.64  ? 3   LYS D O   1 
ATOM   3365  C  CB  . LYS D  1 4   ? 38.212  3.161   11.211 1.00 48.72  ? 3   LYS D CB  1 
ATOM   3366  C  CG  . LYS D  1 4   ? 39.437  2.296   10.981 1.00 59.55  ? 3   LYS D CG  1 
ATOM   3367  C  CD  . LYS D  1 4   ? 40.681  2.790   11.708 1.00 69.72  ? 3   LYS D CD  1 
ATOM   3368  C  CE  . LYS D  1 4   ? 41.961  2.533   10.931 1.00 75.67  ? 3   LYS D CE  1 
ATOM   3369  N  NZ  . LYS D  1 4   ? 43.158  2.532   11.808 1.00 71.36  ? 3   LYS D NZ  1 
ATOM   3370  N  N   . VAL D  1 5   ? 35.161  2.437   12.202 1.00 36.32  ? 4   VAL D N   1 
ATOM   3371  C  CA  . VAL D  1 5   ? 34.005  2.776   13.008 1.00 32.78  ? 4   VAL D CA  1 
ATOM   3372  C  C   . VAL D  1 5   ? 34.259  2.269   14.421 1.00 27.83  ? 4   VAL D C   1 
ATOM   3373  O  O   . VAL D  1 5   ? 35.045  1.355   14.622 1.00 28.22  ? 4   VAL D O   1 
ATOM   3374  C  CB  . VAL D  1 5   ? 32.752  2.143   12.377 1.00 34.99  ? 4   VAL D CB  1 
ATOM   3375  C  CG1 . VAL D  1 5   ? 31.570  2.124   13.325 1.00 32.69  ? 4   VAL D CG1 1 
ATOM   3376  C  CG2 . VAL D  1 5   ? 32.399  2.824   11.063 1.00 38.00  ? 4   VAL D CG2 1 
ATOM   3377  N  N   . VAL D  1 6   ? 33.610  2.876   15.407 1.00 24.47  ? 5   VAL D N   1 
ATOM   3378  C  CA  . VAL D  1 6   ? 33.863  2.473   16.778 1.00 22.39  ? 5   VAL D CA  1 
ATOM   3379  C  C   . VAL D  1 6   ? 32.572  2.552   17.589 1.00 22.31  ? 5   VAL D C   1 
ATOM   3380  O  O   . VAL D  1 6   ? 31.614  3.222   17.207 1.00 23.64  ? 5   VAL D O   1 
ATOM   3381  C  CB  . VAL D  1 6   ? 34.991  3.308   17.413 1.00 20.88  ? 5   VAL D CB  1 
ATOM   3382  C  CG1 . VAL D  1 6   ? 34.551  4.736   17.687 1.00 20.34  ? 5   VAL D CG1 1 
ATOM   3383  C  CG2 . VAL D  1 6   ? 35.508  2.661   18.683 1.00 20.69  ? 5   VAL D CG2 1 
ATOM   3384  N  N   . CYS D  1 7   ? 32.573  1.874   18.735 1.00 21.68  ? 6   CYS D N   1 
ATOM   3385  C  CA  . CYS D  1 7   ? 31.394  1.827   19.569 1.00 21.33  ? 6   CYS D CA  1 
ATOM   3386  C  C   . CYS D  1 7   ? 31.825  1.621   21.009 1.00 21.05  ? 6   CYS D C   1 
ATOM   3387  O  O   . CYS D  1 7   ? 32.609  0.725   21.292 1.00 21.22  ? 6   CYS D O   1 
ATOM   3388  C  CB  . CYS D  1 7   ? 30.524  0.661   19.131 1.00 22.46  ? 6   CYS D CB  1 
ATOM   3389  S  SG  . CYS D  1 7   ? 28.983  0.538   20.064 1.00 25.34  ? 6   CYS D SG  1 
ATOM   3390  N  N   . VAL D  1 8   ? 31.337  2.480   21.903 1.00 21.28  ? 7   VAL D N   1 
ATOM   3391  C  CA  . VAL D  1 8   ? 31.625  2.351   23.323 1.00 21.83  ? 7   VAL D CA  1 
ATOM   3392  C  C   . VAL D  1 8   ? 30.389  1.761   23.991 1.00 23.38  ? 7   VAL D C   1 
ATOM   3393  O  O   . VAL D  1 8   ? 29.317  2.353   23.917 1.00 23.83  ? 7   VAL D O   1 
ATOM   3394  C  CB  . VAL D  1 8   ? 31.969  3.715   23.944 1.00 22.26  ? 7   VAL D CB  1 
ATOM   3395  C  CG1 . VAL D  1 8   ? 32.139  3.610   25.451 1.00 23.30  ? 7   VAL D CG1 1 
ATOM   3396  C  CG2 . VAL D  1 8   ? 33.180  4.365   23.289 1.00 22.94  ? 7   VAL D CG2 1 
ATOM   3397  N  N   . LEU D  1 9   ? 30.535  0.601   24.635 1.00 24.52  ? 8   LEU D N   1 
ATOM   3398  C  CA  . LEU D  1 9   ? 29.391  -0.039  25.269 1.00 25.18  ? 8   LEU D CA  1 
ATOM   3399  C  C   . LEU D  1 9   ? 29.328  0.377   26.734 1.00 27.24  ? 8   LEU D C   1 
ATOM   3400  O  O   . LEU D  1 9   ? 30.309  0.219   27.449 1.00 27.78  ? 8   LEU D O   1 
ATOM   3401  C  CB  . LEU D  1 9   ? 29.522  -1.558  25.157 1.00 24.15  ? 8   LEU D CB  1 
ATOM   3402  C  CG  . LEU D  1 9   ? 29.655  -2.112  23.741 1.00 24.57  ? 8   LEU D CG  1 
ATOM   3403  C  CD1 . LEU D  1 9   ? 30.061  -3.566  23.781 1.00 23.57  ? 8   LEU D CD1 1 
ATOM   3404  C  CD2 . LEU D  1 9   ? 28.351  -1.999  22.980 1.00 26.85  ? 8   LEU D CD2 1 
ATOM   3405  N  N   . LYS D  1 10  ? 28.172  0.913   27.154 1.00 30.45  ? 9   LYS D N   1 
ATOM   3406  C  CA  . LYS D  1 10  ? 27.868  1.204   28.549 1.00 32.86  ? 9   LYS D CA  1 
ATOM   3407  C  C   . LYS D  1 10  ? 26.456  0.724   28.856 1.00 33.51  ? 9   LYS D C   1 
ATOM   3408  O  O   . LYS D  1 10  ? 25.646  0.549   27.945 1.00 36.64  ? 9   LYS D O   1 
ATOM   3409  C  CB  . LYS D  1 10  ? 27.979  2.705   28.850 1.00 36.79  ? 9   LYS D CB  1 
ATOM   3410  C  CG  . LYS D  1 10  ? 29.389  3.229   29.077 1.00 43.08  ? 9   LYS D CG  1 
ATOM   3411  C  CD  . LYS D  1 10  ? 29.365  4.752   29.372 1.00 49.83  ? 9   LYS D CD  1 
ATOM   3412  C  CE  . LYS D  1 10  ? 30.468  5.573   28.727 1.00 50.42  ? 9   LYS D CE  1 
ATOM   3413  N  NZ  . LYS D  1 10  ? 30.074  6.258   27.459 1.00 45.88  ? 9   LYS D NZ  1 
ATOM   3414  N  N   . GLY D  1 11  ? 26.190  0.489   30.145 1.00 32.06  ? 10  GLY D N   1 
ATOM   3415  C  CA  . GLY D  1 11  ? 24.865  0.124   30.617 1.00 32.46  ? 10  GLY D CA  1 
ATOM   3416  C  C   . GLY D  1 11  ? 24.714  0.424   32.109 1.00 33.83  ? 10  GLY D C   1 
ATOM   3417  O  O   . GLY D  1 11  ? 25.557  1.103   32.681 1.00 36.02  ? 10  GLY D O   1 
ATOM   3418  N  N   . ASP D  1 12  ? 23.660  -0.099  32.735 1.00 37.40  ? 11  ASP D N   1 
ATOM   3419  C  CA  . ASP D  1 12  ? 23.370  0.212   34.124 1.00 39.96  ? 11  ASP D CA  1 
ATOM   3420  C  C   . ASP D  1 12  ? 24.315  -0.521  35.069 1.00 42.33  ? 11  ASP D C   1 
ATOM   3421  O  O   . ASP D  1 12  ? 24.562  -0.053  36.178 1.00 44.81  ? 11  ASP D O   1 
ATOM   3422  C  CB  . ASP D  1 12  ? 21.927  -0.147  34.476 1.00 43.59  ? 11  ASP D CB  1 
ATOM   3423  C  CG  . ASP D  1 12  ? 20.953  0.737   33.739 1.00 44.79  ? 11  ASP D CG  1 
ATOM   3424  O  OD1 . ASP D  1 12  ? 21.275  1.926   33.550 1.00 41.80  ? 11  ASP D OD1 1 
ATOM   3425  O  OD2 . ASP D  1 12  ? 19.898  0.221   33.367 1.00 47.80  ? 11  ASP D OD2 1 
ATOM   3426  N  N   . GLY D  1 13  ? 24.819  -1.681  34.629 1.00 43.29  ? 12  GLY D N   1 
ATOM   3427  C  CA  . GLY D  1 13  ? 25.620  -2.535  35.485 1.00 39.82  ? 12  GLY D CA  1 
ATOM   3428  C  C   . GLY D  1 13  ? 27.103  -2.289  35.248 1.00 40.42  ? 12  GLY D C   1 
ATOM   3429  O  O   . GLY D  1 13  ? 27.483  -1.227  34.753 1.00 40.48  ? 12  GLY D O   1 
ATOM   3430  N  N   . PRO D  1 14  ? 27.978  -3.267  35.572 1.00 39.71  ? 13  PRO D N   1 
ATOM   3431  C  CA  . PRO D  1 14  ? 29.417  -3.101  35.389 1.00 36.26  ? 13  PRO D CA  1 
ATOM   3432  C  C   . PRO D  1 14  ? 29.927  -3.402  33.979 1.00 34.01  ? 13  PRO D C   1 
ATOM   3433  O  O   . PRO D  1 14  ? 31.116  -3.284  33.740 1.00 35.48  ? 13  PRO D O   1 
ATOM   3434  C  CB  . PRO D  1 14  ? 29.963  -4.126  36.398 1.00 36.51  ? 13  PRO D CB  1 
ATOM   3435  C  CG  . PRO D  1 14  ? 28.960  -5.262  36.370 1.00 37.18  ? 13  PRO D CG  1 
ATOM   3436  C  CD  . PRO D  1 14  ? 27.626  -4.588  36.119 1.00 39.04  ? 13  PRO D CD  1 
ATOM   3437  N  N   . VAL D  1 15  ? 29.042  -3.764  33.050 1.00 33.28  ? 14  VAL D N   1 
ATOM   3438  C  CA  . VAL D  1 15  ? 29.524  -4.158  31.736 1.00 35.02  ? 14  VAL D CA  1 
ATOM   3439  C  C   . VAL D  1 15  ? 29.902  -2.920  30.934 1.00 33.69  ? 14  VAL D C   1 
ATOM   3440  O  O   . VAL D  1 15  ? 29.107  -1.995  30.808 1.00 34.29  ? 14  VAL D O   1 
ATOM   3441  C  CB  . VAL D  1 15  ? 28.517  -5.040  30.976 1.00 36.26  ? 14  VAL D CB  1 
ATOM   3442  C  CG1 . VAL D  1 15  ? 29.028  -5.391  29.589 1.00 34.19  ? 14  VAL D CG1 1 
ATOM   3443  C  CG2 . VAL D  1 15  ? 28.214  -6.304  31.758 1.00 37.77  ? 14  VAL D CG2 1 
ATOM   3444  N  N   . GLN D  1 16  ? 31.134  -2.912  30.410 1.00 33.59  ? 15  GLN D N   1 
ATOM   3445  C  CA  . GLN D  1 16  ? 31.570  -1.820  29.557 1.00 35.46  ? 15  GLN D CA  1 
ATOM   3446  C  C   . GLN D  1 16  ? 32.692  -2.285  28.641 1.00 32.49  ? 15  GLN D C   1 
ATOM   3447  O  O   . GLN D  1 16  ? 33.395  -3.233  28.976 1.00 32.64  ? 15  GLN D O   1 
ATOM   3448  C  CB  . GLN D  1 16  ? 31.966  -0.595  30.379 1.00 40.80  ? 15  GLN D CB  1 
ATOM   3449  C  CG  . GLN D  1 16  ? 33.146  -0.819  31.316 1.00 44.11  ? 15  GLN D CG  1 
ATOM   3450  C  CD  . GLN D  1 16  ? 33.478  0.450   32.058 1.00 48.90  ? 15  GLN D CD  1 
ATOM   3451  O  OE1 . GLN D  1 16  ? 32.674  1.379   32.144 1.00 49.24  ? 15  GLN D OE1 1 
ATOM   3452  N  NE2 . GLN D  1 16  ? 34.687  0.512   32.593 1.00 57.21  ? 15  GLN D NE2 1 
ATOM   3453  N  N   . GLY D  1 17  ? 32.840  -1.618  27.488 1.00 28.52  ? 16  GLY D N   1 
ATOM   3454  C  CA  . GLY D  1 17  ? 33.872  -2.009  26.540 1.00 27.17  ? 16  GLY D CA  1 
ATOM   3455  C  C   . GLY D  1 17  ? 33.912  -1.113  25.308 1.00 26.33  ? 16  GLY D C   1 
ATOM   3456  O  O   . GLY D  1 17  ? 33.071  -0.236  25.134 1.00 27.03  ? 16  GLY D O   1 
ATOM   3457  N  N   . ILE D  1 18  ? 34.922  -1.346  24.468 1.00 24.20  ? 17  ILE D N   1 
ATOM   3458  C  CA  . ILE D  1 18  ? 35.114  -0.616  23.230 1.00 23.98  ? 17  ILE D CA  1 
ATOM   3459  C  C   . ILE D  1 18  ? 35.181  -1.641  22.105 1.00 24.35  ? 17  ILE D C   1 
ATOM   3460  O  O   . ILE D  1 18  ? 35.925  -2.595  22.211 1.00 24.59  ? 17  ILE D O   1 
ATOM   3461  C  CB  . ILE D  1 18  ? 36.409  0.216   23.303 1.00 22.36  ? 17  ILE D CB  1 
ATOM   3462  C  CG1 . ILE D  1 18  ? 36.361  1.258   24.423 1.00 21.45  ? 17  ILE D CG1 1 
ATOM   3463  C  CG2 . ILE D  1 18  ? 36.740  0.838   21.956 1.00 23.80  ? 17  ILE D CG2 1 
ATOM   3464  C  CD1 . ILE D  1 18  ? 37.641  2.048   24.580 1.00 19.92  ? 17  ILE D CD1 1 
ATOM   3465  N  N   . ILE D  1 19  ? 34.419  -1.444  21.030 1.00 24.48  ? 18  ILE D N   1 
ATOM   3466  C  CA  . ILE D  1 19  ? 34.491  -2.364  19.907 1.00 24.97  ? 18  ILE D CA  1 
ATOM   3467  C  C   . ILE D  1 19  ? 34.787  -1.570  18.646 1.00 23.91  ? 18  ILE D C   1 
ATOM   3468  O  O   . ILE D  1 19  ? 34.101  -0.599  18.369 1.00 24.69  ? 18  ILE D O   1 
ATOM   3469  C  CB  . ILE D  1 19  ? 33.184  -3.180  19.757 1.00 25.65  ? 18  ILE D CB  1 
ATOM   3470  C  CG1 . ILE D  1 19  ? 32.860  -4.015  20.998 1.00 25.11  ? 18  ILE D CG1 1 
ATOM   3471  C  CG2 . ILE D  1 19  ? 33.207  -4.028  18.488 1.00 25.94  ? 18  ILE D CG2 1 
ATOM   3472  C  CD1 . ILE D  1 19  ? 33.858  -5.098  21.308 1.00 24.93  ? 18  ILE D CD1 1 
ATOM   3473  N  N   . ASN D  1 20  ? 35.787  -2.013  17.885 1.00 24.06  ? 19  ASN D N   1 
ATOM   3474  C  CA  . ASN D  1 20  ? 36.150  -1.372  16.631 1.00 26.34  ? 19  ASN D CA  1 
ATOM   3475  C  C   . ASN D  1 20  ? 35.615  -2.171  15.450 1.00 27.66  ? 19  ASN D C   1 
ATOM   3476  O  O   . ASN D  1 20  ? 35.524  -3.394  15.521 1.00 30.24  ? 19  ASN D O   1 
ATOM   3477  C  CB  . ASN D  1 20  ? 37.664  -1.258  16.481 1.00 25.10  ? 19  ASN D CB  1 
ATOM   3478  C  CG  . ASN D  1 20  ? 38.278  -0.601  17.693 1.00 24.98  ? 19  ASN D CG  1 
ATOM   3479  O  OD1 . ASN D  1 20  ? 38.764  -1.289  18.589 1.00 24.52  ? 19  ASN D OD1 1 
ATOM   3480  N  ND2 . ASN D  1 20  ? 38.224  0.719   17.733 1.00 24.13  ? 19  ASN D ND2 1 
ATOM   3481  N  N   . PHE D  1 21  ? 35.288  -1.464  14.368 1.00 27.50  ? 20  PHE D N   1 
ATOM   3482  C  CA  . PHE D  1 21  ? 34.875  -2.091  13.127 1.00 29.47  ? 20  PHE D CA  1 
ATOM   3483  C  C   . PHE D  1 21  ? 35.715  -1.517  12.001 1.00 32.90  ? 20  PHE D C   1 
ATOM   3484  O  O   . PHE D  1 21  ? 35.887  -0.309  11.922 1.00 32.10  ? 20  PHE D O   1 
ATOM   3485  C  CB  . PHE D  1 21  ? 33.415  -1.766  12.797 1.00 29.51  ? 20  PHE D CB  1 
ATOM   3486  C  CG  . PHE D  1 21  ? 32.399  -2.232  13.806 1.00 28.05  ? 20  PHE D CG  1 
ATOM   3487  C  CD1 . PHE D  1 21  ? 32.309  -1.641  15.060 1.00 28.19  ? 20  PHE D CD1 1 
ATOM   3488  C  CD2 . PHE D  1 21  ? 31.534  -3.274  13.503 1.00 29.10  ? 20  PHE D CD2 1 
ATOM   3489  C  CE1 . PHE D  1 21  ? 31.366  -2.082  15.982 1.00 30.33  ? 20  PHE D CE1 1 
ATOM   3490  C  CE2 . PHE D  1 21  ? 30.577  -3.697  14.415 1.00 30.08  ? 20  PHE D CE2 1 
ATOM   3491  C  CZ  . PHE D  1 21  ? 30.492  -3.104  15.653 1.00 29.76  ? 20  PHE D CZ  1 
ATOM   3492  N  N   . GLU D  1 22  ? 36.231  -2.385  11.130 1.00 39.58  ? 21  GLU D N   1 
ATOM   3493  C  CA  . GLU D  1 22  ? 37.046  -1.922  10.021 1.00 44.64  ? 21  GLU D CA  1 
ATOM   3494  C  C   . GLU D  1 22  ? 36.663  -2.692  8.761  1.00 44.67  ? 21  GLU D C   1 
ATOM   3495  O  O   . GLU D  1 22  ? 36.432  -3.893  8.837  1.00 43.74  ? 21  GLU D O   1 
ATOM   3496  C  CB  . GLU D  1 22  ? 38.525  -2.076  10.376 1.00 49.39  ? 21  GLU D CB  1 
ATOM   3497  C  CG  . GLU D  1 22  ? 39.432  -1.281  9.446  1.00 59.77  ? 21  GLU D CG  1 
ATOM   3498  C  CD  . GLU D  1 22  ? 40.916  -1.358  9.745  1.00 67.11  ? 21  GLU D CD  1 
ATOM   3499  O  OE1 . GLU D  1 22  ? 41.306  -1.094  10.919 1.00 67.83  ? 21  GLU D OE1 1 
ATOM   3500  O  OE2 . GLU D  1 22  ? 41.663  -1.734  8.803  1.00 75.57  ? 21  GLU D OE2 1 
ATOM   3501  N  N   . GLN D  1 23  ? 36.602  -1.989  7.623  1.00 45.15  ? 22  GLN D N   1 
ATOM   3502  C  CA  . GLN D  1 23  ? 36.214  -2.594  6.360  1.00 47.77  ? 22  GLN D CA  1 
ATOM   3503  C  C   . GLN D  1 23  ? 37.116  -2.053  5.246  1.00 52.08  ? 22  GLN D C   1 
ATOM   3504  O  O   . GLN D  1 23  ? 36.955  -0.914  4.833  1.00 50.46  ? 22  GLN D O   1 
ATOM   3505  C  CB  . GLN D  1 23  ? 34.743  -2.280  6.066  1.00 44.94  ? 22  GLN D CB  1 
ATOM   3506  C  CG  . GLN D  1 23  ? 34.182  -3.058  4.880  1.00 44.90  ? 22  GLN D CG  1 
ATOM   3507  C  CD  . GLN D  1 23  ? 32.756  -2.687  4.554  1.00 45.19  ? 22  GLN D CD  1 
ATOM   3508  O  OE1 . GLN D  1 23  ? 32.340  -1.528  4.705  1.00 46.01  ? 22  GLN D OE1 1 
ATOM   3509  N  NE2 . GLN D  1 23  ? 32.005  -3.673  4.080  1.00 46.37  ? 22  GLN D NE2 1 
ATOM   3510  N  N   . LYS D  1 24  ? 38.037  -2.889  4.737  1.00 52.20  ? 23  LYS D N   1 
ATOM   3511  C  CA  . LYS D  1 24  ? 39.022  -2.451  3.754  1.00 51.74  ? 23  LYS D CA  1 
ATOM   3512  C  C   . LYS D  1 24  ? 38.372  -2.195  2.389  1.00 52.51  ? 23  LYS D C   1 
ATOM   3513  O  O   . LYS D  1 24  ? 38.564  -1.124  1.828  1.00 49.82  ? 23  LYS D O   1 
ATOM   3514  C  CB  . LYS D  1 24  ? 40.279  -3.333  3.754  1.00 48.83  ? 23  LYS D CB  1 
ATOM   3515  C  CG  . LYS D  1 24  ? 41.243  -3.061  4.910  0.20 46.01  ? 23  LYS D CG  1 
ATOM   3516  C  CD  . LYS D  1 24  ? 42.549  -3.815  4.835  0.20 44.42  ? 23  LYS D CD  1 
ATOM   3517  C  CE  . LYS D  1 24  ? 43.435  -3.538  6.030  0.20 42.86  ? 23  LYS D CE  1 
ATOM   3518  N  NZ  . LYS D  1 24  ? 44.772  -4.155  5.877  0.20 41.92  ? 23  LYS D NZ  1 
ATOM   3519  N  N   . GLU D  1 25  ? 37.605  -3.148  1.865  1.00 62.22  ? 24  GLU D N   1 
ATOM   3520  C  CA  . GLU D  1 25  ? 36.954  -2.973  0.565  1.00 67.43  ? 24  GLU D CA  1 
ATOM   3521  C  C   . GLU D  1 25  ? 35.472  -2.687  0.794  1.00 66.09  ? 24  GLU D C   1 
ATOM   3522  O  O   . GLU D  1 25  ? 34.934  -3.111  1.807  1.00 66.48  ? 24  GLU D O   1 
ATOM   3523  C  CB  . GLU D  1 25  ? 37.111  -4.174  -0.371 1.00 78.93  ? 24  GLU D CB  1 
ATOM   3524  C  CG  . GLU D  1 25  ? 38.517  -4.734  -0.433 1.00 95.65  ? 24  GLU D CG  1 
ATOM   3525  C  CD  . GLU D  1 25  ? 38.791  -5.870  0.544  1.00 107.56 ? 24  GLU D CD  1 
ATOM   3526  O  OE1 . GLU D  1 25  ? 38.103  -5.968  1.595  1.00 117.70 ? 24  GLU D OE1 1 
ATOM   3527  O  OE2 . GLU D  1 25  ? 39.699  -6.691  0.251  1.00 111.20 ? 24  GLU D OE2 1 
ATOM   3528  N  N   . SER D  1 26  ? 34.825  -2.006  -0.163 1.00 66.10  ? 25  SER D N   1 
ATOM   3529  C  CA  . SER D  1 26  ? 33.519  -1.424  0.081  1.00 66.41  ? 25  SER D CA  1 
ATOM   3530  C  C   . SER D  1 26  ? 32.427  -2.476  0.273  1.00 66.51  ? 25  SER D C   1 
ATOM   3531  O  O   . SER D  1 26  ? 31.498  -2.233  1.045  1.00 66.95  ? 25  SER D O   1 
ATOM   3532  C  CB  . SER D  1 26  ? 33.097  -0.378  -0.939 1.00 62.90  ? 25  SER D CB  1 
ATOM   3533  O  OG  . SER D  1 26  ? 34.096  -0.035  -1.888 1.00 69.29  ? 25  SER D OG  1 
ATOM   3534  N  N   . ASN D  1 27  ? 32.524  -3.621  -0.407 1.00 66.25  ? 26  ASN D N   1 
ATOM   3535  C  CA  . ASN D  1 27  ? 31.514  -4.637  -0.159 1.00 68.65  ? 26  ASN D CA  1 
ATOM   3536  C  C   . ASN D  1 27  ? 32.107  -5.840  0.566  1.00 63.67  ? 26  ASN D C   1 
ATOM   3537  O  O   . ASN D  1 27  ? 31.489  -6.901  0.638  1.00 57.39  ? 26  ASN D O   1 
ATOM   3538  C  CB  . ASN D  1 27  ? 30.650  -4.956  -1.383 1.00 82.67  ? 26  ASN D CB  1 
ATOM   3539  C  CG  . ASN D  1 27  ? 29.232  -4.420  -1.257 1.00 91.35  ? 26  ASN D CG  1 
ATOM   3540  O  OD1 . ASN D  1 27  ? 28.706  -4.200  -0.155 1.00 90.76  ? 26  ASN D OD1 1 
ATOM   3541  N  ND2 . ASN D  1 27  ? 28.597  -4.208  -2.395 1.00 89.52  ? 26  ASN D ND2 1 
ATOM   3542  N  N   . GLY D  1 28  ? 33.327  -5.664  1.078  1.00 62.93  ? 27  GLY D N   1 
ATOM   3543  C  CA  . GLY D  1 28  ? 34.105  -6.766  1.624  1.00 58.71  ? 27  GLY D CA  1 
ATOM   3544  C  C   . GLY D  1 28  ? 33.838  -7.000  3.108  1.00 53.80  ? 27  GLY D C   1 
ATOM   3545  O  O   . GLY D  1 28  ? 33.022  -6.307  3.712  1.00 56.20  ? 27  GLY D O   1 
ATOM   3546  N  N   . PRO D  1 29  ? 34.532  -7.971  3.738  1.00 47.46  ? 28  PRO D N   1 
ATOM   3547  C  CA  . PRO D  1 29  ? 34.246  -8.343  5.126  1.00 43.86  ? 28  PRO D CA  1 
ATOM   3548  C  C   . PRO D  1 29  ? 34.597  -7.224  6.104  1.00 41.62  ? 28  PRO D C   1 
ATOM   3549  O  O   . PRO D  1 29  ? 35.413  -6.359  5.788  1.00 45.38  ? 28  PRO D O   1 
ATOM   3550  C  CB  . PRO D  1 29  ? 35.146  -9.565  5.355  1.00 44.24  ? 28  PRO D CB  1 
ATOM   3551  C  CG  . PRO D  1 29  ? 36.286  -9.356  4.382  1.00 48.71  ? 28  PRO D CG  1 
ATOM   3552  C  CD  . PRO D  1 29  ? 35.645  -8.737  3.151  1.00 48.83  ? 28  PRO D CD  1 
ATOM   3553  N  N   . VAL D  1 30  ? 33.971  -7.265  7.286  1.00 38.81  ? 29  VAL D N   1 
ATOM   3554  C  CA  . VAL D  1 30  ? 34.185  -6.291  8.341  1.00 38.84  ? 29  VAL D CA  1 
ATOM   3555  C  C   . VAL D  1 30  ? 34.884  -6.987  9.506  1.00 37.20  ? 29  VAL D C   1 
ATOM   3556  O  O   . VAL D  1 30  ? 34.386  -7.991  10.007 1.00 37.18  ? 29  VAL D O   1 
ATOM   3557  C  CB  . VAL D  1 30  ? 32.855  -5.663  8.807  1.00 38.34  ? 29  VAL D CB  1 
ATOM   3558  C  CG1 . VAL D  1 30  ? 33.073  -4.640  9.906  1.00 36.51  ? 29  VAL D CG1 1 
ATOM   3559  C  CG2 . VAL D  1 30  ? 32.062  -5.058  7.662  1.00 35.85  ? 29  VAL D CG2 1 
ATOM   3560  N  N   . LYS D  1 31  ? 36.033  -6.450  9.934  1.00 34.15  ? 30  LYS D N   1 
ATOM   3561  C  CA  . LYS D  1 31  ? 36.686  -6.970  11.121 1.00 32.67  ? 30  LYS D CA  1 
ATOM   3562  C  C   . LYS D  1 31  ? 36.078  -6.280  12.338 1.00 31.60  ? 30  LYS D C   1 
ATOM   3563  O  O   . LYS D  1 31  ? 36.016  -5.058  12.391 1.00 31.41  ? 30  LYS D O   1 
ATOM   3564  C  CB  . LYS D  1 31  ? 38.202  -6.741  11.065 1.00 34.31  ? 30  LYS D CB  1 
ATOM   3565  C  CG  . LYS D  1 31  ? 39.025  -7.752  10.278 0.60 37.51  ? 30  LYS D CG  1 
ATOM   3566  C  CD  . LYS D  1 31  ? 40.490  -7.855  10.771 0.60 38.55  ? 30  LYS D CD  1 
ATOM   3567  C  CE  . LYS D  1 31  ? 40.979  -9.252  11.128 0.60 38.47  ? 30  LYS D CE  1 
ATOM   3568  N  NZ  . LYS D  1 31  ? 41.886  -9.828  10.103 0.60 40.61  ? 30  LYS D NZ  1 
ATOM   3569  N  N   . VAL D  1 32  ? 35.623  -7.073  13.306 1.00 29.65  ? 31  VAL D N   1 
ATOM   3570  C  CA  . VAL D  1 32  ? 35.061  -6.524  14.527 1.00 27.80  ? 31  VAL D CA  1 
ATOM   3571  C  C   . VAL D  1 32  ? 35.938  -6.979  15.687 1.00 28.96  ? 31  VAL D C   1 
ATOM   3572  O  O   . VAL D  1 32  ? 36.024  -8.175  15.950 1.00 32.82  ? 31  VAL D O   1 
ATOM   3573  C  CB  . VAL D  1 32  ? 33.609  -7.001  14.721 1.00 24.77  ? 31  VAL D CB  1 
ATOM   3574  C  CG1 . VAL D  1 32  ? 32.969  -6.363  15.951 1.00 23.78  ? 31  VAL D CG1 1 
ATOM   3575  C  CG2 . VAL D  1 32  ? 32.778  -6.751  13.474 1.00 23.91  ? 31  VAL D CG2 1 
ATOM   3576  N  N   . TRP D  1 33  ? 36.594  -6.045  16.377 1.00 27.19  ? 32  TRP D N   1 
ATOM   3577  C  CA  . TRP D  1 33  ? 37.422  -6.466  17.495 1.00 26.37  ? 32  TRP D CA  1 
ATOM   3578  C  C   . TRP D  1 33  ? 37.395  -5.438  18.618 1.00 27.05  ? 32  TRP D C   1 
ATOM   3579  O  O   . TRP D  1 33  ? 37.143  -4.256  18.398 1.00 25.32  ? 32  TRP D O   1 
ATOM   3580  C  CB  . TRP D  1 33  ? 38.867  -6.731  17.052 1.00 26.51  ? 32  TRP D CB  1 
ATOM   3581  C  CG  . TRP D  1 33  ? 39.685  -5.485  16.903 1.00 27.38  ? 32  TRP D CG  1 
ATOM   3582  C  CD1 . TRP D  1 33  ? 40.566  -4.946  17.804 1.00 27.67  ? 32  TRP D CD1 1 
ATOM   3583  C  CD2 . TRP D  1 33  ? 39.672  -4.595  15.776 1.00 29.13  ? 32  TRP D CD2 1 
ATOM   3584  N  NE1 . TRP D  1 33  ? 41.113  -3.789  17.309 1.00 28.10  ? 32  TRP D NE1 1 
ATOM   3585  C  CE2 . TRP D  1 33  ? 40.582  -3.548  16.066 1.00 30.27  ? 32  TRP D CE2 1 
ATOM   3586  C  CE3 . TRP D  1 33  ? 38.974  -4.576  14.561 1.00 29.22  ? 32  TRP D CE3 1 
ATOM   3587  C  CZ2 . TRP D  1 33  ? 40.814  -2.501  15.169 1.00 30.86  ? 32  TRP D CZ2 1 
ATOM   3588  C  CZ3 . TRP D  1 33  ? 39.203  -3.536  13.679 1.00 30.68  ? 32  TRP D CZ3 1 
ATOM   3589  C  CH2 . TRP D  1 33  ? 40.116  -2.518  13.975 1.00 30.92  ? 32  TRP D CH2 1 
ATOM   3590  N  N   . GLY D  1 34  ? 37.725  -5.913  19.817 1.00 26.16  ? 33  GLY D N   1 
ATOM   3591  C  CA  . GLY D  1 34  ? 37.870  -5.049  20.969 1.00 26.26  ? 33  GLY D CA  1 
ATOM   3592  C  C   . GLY D  1 34  ? 37.704  -5.861  22.246 1.00 27.03  ? 33  GLY D C   1 
ATOM   3593  O  O   . GLY D  1 34  ? 37.841  -7.072  22.240 1.00 29.49  ? 33  GLY D O   1 
ATOM   3594  N  N   . SER D  1 35  ? 37.362  -5.189  23.333 1.00 25.89  ? 34  SER D N   1 
ATOM   3595  C  CA  . SER D  1 35  ? 37.340  -5.843  24.614 1.00 26.42  ? 34  SER D CA  1 
ATOM   3596  C  C   . SER D  1 35  ? 36.112  -5.394  25.408 1.00 26.70  ? 34  SER D C   1 
ATOM   3597  O  O   . SER D  1 35  ? 35.735  -4.235  25.360 1.00 27.22  ? 34  SER D O   1 
ATOM   3598  C  CB  . SER D  1 35  ? 38.634  -5.527  25.289 1.00 28.28  ? 34  SER D CB  1 
ATOM   3599  O  OG  . SER D  1 35  ? 38.592  -5.917  26.644 1.00 33.46  ? 34  SER D OG  1 
ATOM   3600  N  N   . ILE D  1 36  ? 35.446  -6.324  26.101 1.00 25.53  ? 35  ILE D N   1 
ATOM   3601  C  CA  . ILE D  1 36  ? 34.359  -5.986  27.007 1.00 24.84  ? 35  ILE D CA  1 
ATOM   3602  C  C   . ILE D  1 36  ? 34.689  -6.584  28.368 1.00 26.99  ? 35  ILE D C   1 
ATOM   3603  O  O   . ILE D  1 36  ? 35.138  -7.722  28.451 1.00 30.16  ? 35  ILE D O   1 
ATOM   3604  C  CB  . ILE D  1 36  ? 33.018  -6.528  26.478 1.00 23.54  ? 35  ILE D CB  1 
ATOM   3605  C  CG1 . ILE D  1 36  ? 32.808  -6.182  25.000 1.00 22.55  ? 35  ILE D CG1 1 
ATOM   3606  C  CG2 . ILE D  1 36  ? 31.866  -6.064  27.350 1.00 22.00  ? 35  ILE D CG2 1 
ATOM   3607  C  CD1 . ILE D  1 36  ? 31.618  -6.850  24.370 1.00 21.58  ? 35  ILE D CD1 1 
ATOM   3608  N  N   . LYS D  1 37  ? 34.463  -5.820  29.438 1.00 27.64  ? 36  LYS D N   1 
ATOM   3609  C  CA  . LYS D  1 37  ? 34.745  -6.314  30.775 1.00 27.88  ? 36  LYS D CA  1 
ATOM   3610  C  C   . LYS D  1 37  ? 33.479  -6.272  31.627 1.00 26.70  ? 36  LYS D C   1 
ATOM   3611  O  O   . LYS D  1 37  ? 32.501  -5.638  31.249 1.00 26.84  ? 36  LYS D O   1 
ATOM   3612  C  CB  . LYS D  1 37  ? 35.918  -5.539  31.389 1.00 30.55  ? 36  LYS D CB  1 
ATOM   3613  C  CG  . LYS D  1 37  ? 35.666  -4.078  31.695 1.00 34.76  ? 36  LYS D CG  1 
ATOM   3614  C  CD  . LYS D  1 37  ? 36.690  -3.533  32.691 1.00 39.52  ? 36  LYS D CD  1 
ATOM   3615  C  CE  . LYS D  1 37  ? 36.303  -2.216  33.324 1.00 40.59  ? 36  LYS D CE  1 
ATOM   3616  N  NZ  . LYS D  1 37  ? 37.499  -1.586  33.949 1.00 37.93  ? 36  LYS D NZ  1 
ATOM   3617  N  N   . GLY D  1 38  ? 33.511  -6.986  32.757 1.00 26.42  ? 37  GLY D N   1 
ATOM   3618  C  CA  . GLY D  1 38  ? 32.414  -7.023  33.712 1.00 28.52  ? 37  GLY D CA  1 
ATOM   3619  C  C   . GLY D  1 38  ? 31.321  -8.038  33.369 1.00 28.55  ? 37  GLY D C   1 
ATOM   3620  O  O   . GLY D  1 38  ? 30.237  -7.995  33.949 1.00 28.80  ? 37  GLY D O   1 
ATOM   3621  N  N   . LEU D  1 39  ? 31.610  -8.956  32.433 1.00 27.56  ? 38  LEU D N   1 
ATOM   3622  C  CA  . LEU D  1 39  ? 30.647  -9.965  32.018 1.00 26.82  ? 38  LEU D CA  1 
ATOM   3623  C  C   . LEU D  1 39  ? 30.784  -11.195 32.905 1.00 27.93  ? 38  LEU D C   1 
ATOM   3624  O  O   . LEU D  1 39  ? 31.844  -11.439 33.470 1.00 27.97  ? 38  LEU D O   1 
ATOM   3625  C  CB  . LEU D  1 39  ? 30.922  -10.344 30.563 1.00 25.02  ? 38  LEU D CB  1 
ATOM   3626  C  CG  . LEU D  1 39  ? 30.563  -9.272  29.534 1.00 24.35  ? 38  LEU D CG  1 
ATOM   3627  C  CD1 . LEU D  1 39  ? 31.208  -9.585  28.200 1.00 23.50  ? 38  LEU D CD1 1 
ATOM   3628  C  CD2 . LEU D  1 39  ? 29.055  -9.154  29.379 1.00 24.15  ? 38  LEU D CD2 1 
ATOM   3629  N  N   . THR D  1 40  ? 29.700  -11.973 33.023 1.00 30.45  ? 39  THR D N   1 
ATOM   3630  C  CA  . THR D  1 40  ? 29.787  -13.285 33.645 1.00 30.80  ? 39  THR D CA  1 
ATOM   3631  C  C   . THR D  1 40  ? 30.498  -14.226 32.679 1.00 31.52  ? 39  THR D C   1 
ATOM   3632  O  O   . THR D  1 40  ? 30.385  -14.062 31.463 1.00 30.59  ? 39  THR D O   1 
ATOM   3633  C  CB  . THR D  1 40  ? 28.401  -13.846 33.981 1.00 31.76  ? 39  THR D CB  1 
ATOM   3634  O  OG1 . THR D  1 40  ? 27.626  -13.701 32.792 1.00 31.46  ? 39  THR D OG1 1 
ATOM   3635  C  CG2 . THR D  1 40  ? 27.736  -13.154 35.149 1.00 29.74  ? 39  THR D CG2 1 
ATOM   3636  N  N   . GLU D  1 41  ? 31.231  -15.198 33.233 1.00 32.10  ? 40  GLU D N   1 
ATOM   3637  C  CA  . GLU D  1 41  ? 31.993  -16.127 32.416 1.00 34.13  ? 40  GLU D CA  1 
ATOM   3638  C  C   . GLU D  1 41  ? 31.048  -16.819 31.439 1.00 34.22  ? 40  GLU D C   1 
ATOM   3639  O  O   . GLU D  1 41  ? 29.919  -17.140 31.801 1.00 36.88  ? 40  GLU D O   1 
ATOM   3640  C  CB  . GLU D  1 41  ? 32.706  -17.147 33.303 1.00 36.66  ? 40  GLU D CB  1 
ATOM   3641  C  CG  . GLU D  1 41  ? 33.607  -18.067 32.500 1.00 43.00  ? 40  GLU D CG  1 
ATOM   3642  C  CD  . GLU D  1 41  ? 34.427  -19.081 33.266 1.00 48.79  ? 40  GLU D CD  1 
ATOM   3643  O  OE1 . GLU D  1 41  ? 34.212  -19.219 34.485 1.00 53.11  ? 40  GLU D OE1 1 
ATOM   3644  O  OE2 . GLU D  1 41  ? 35.285  -19.726 32.639 1.00 50.24  ? 40  GLU D OE2 1 
ATOM   3645  N  N   . GLY D  1 42  ? 31.499  -17.018 30.195 1.00 30.53  ? 41  GLY D N   1 
ATOM   3646  C  CA  . GLY D  1 42  ? 30.711  -17.764 29.228 1.00 28.74  ? 41  GLY D CA  1 
ATOM   3647  C  C   . GLY D  1 42  ? 30.229  -16.921 28.045 1.00 30.58  ? 41  GLY D C   1 
ATOM   3648  O  O   . GLY D  1 42  ? 30.756  -15.833 27.796 1.00 32.60  ? 41  GLY D O   1 
ATOM   3649  N  N   . LEU D  1 43  ? 29.227  -17.458 27.325 1.00 28.87  ? 42  LEU D N   1 
ATOM   3650  C  CA  . LEU D  1 43  ? 28.764  -16.894 26.063 1.00 26.18  ? 42  LEU D CA  1 
ATOM   3651  C  C   . LEU D  1 43  ? 27.777  -15.762 26.330 1.00 25.93  ? 42  LEU D C   1 
ATOM   3652  O  O   . LEU D  1 43  ? 26.950  -15.859 27.241 1.00 25.24  ? 42  LEU D O   1 
ATOM   3653  C  CB  . LEU D  1 43  ? 28.076  -17.989 25.246 1.00 24.47  ? 42  LEU D CB  1 
ATOM   3654  C  CG  . LEU D  1 43  ? 28.989  -19.088 24.711 1.00 23.57  ? 42  LEU D CG  1 
ATOM   3655  C  CD1 . LEU D  1 43  ? 28.149  -20.192 24.080 1.00 21.74  ? 42  LEU D CD1 1 
ATOM   3656  C  CD2 . LEU D  1 43  ? 30.015  -18.557 23.713 1.00 22.32  ? 42  LEU D CD2 1 
ATOM   3657  N  N   . HIS D  1 44  ? 27.875  -14.704 25.509 1.00 24.93  ? 43  HIS D N   1 
ATOM   3658  C  CA  . HIS D  1 44  ? 26.940  -13.591 25.527 1.00 24.05  ? 43  HIS D CA  1 
ATOM   3659  C  C   . HIS D  1 44  ? 26.571  -13.203 24.098 1.00 24.76  ? 43  HIS D C   1 
ATOM   3660  O  O   . HIS D  1 44  ? 27.434  -13.093 23.222 1.00 23.49  ? 43  HIS D O   1 
ATOM   3661  C  CB  . HIS D  1 44  ? 27.526  -12.404 26.283 1.00 23.61  ? 43  HIS D CB  1 
ATOM   3662  C  CG  . HIS D  1 44  ? 27.744  -12.655 27.732 1.00 25.06  ? 43  HIS D CG  1 
ATOM   3663  N  ND1 . HIS D  1 44  ? 26.805  -12.289 28.689 1.00 26.35  ? 43  HIS D ND1 1 
ATOM   3664  C  CD2 . HIS D  1 44  ? 28.792  -13.209 28.394 1.00 25.82  ? 43  HIS D CD2 1 
ATOM   3665  C  CE1 . HIS D  1 44  ? 27.267  -12.600 29.893 1.00 27.70  ? 43  HIS D CE1 1 
ATOM   3666  N  NE2 . HIS D  1 44  ? 28.495  -13.175 29.731 1.00 26.73  ? 43  HIS D NE2 1 
ATOM   3667  N  N   . GLY D  1 45  ? 25.264  -13.029 23.877 1.00 24.86  ? 44  GLY D N   1 
ATOM   3668  C  CA  . GLY D  1 45  ? 24.742  -12.630 22.580 1.00 24.07  ? 44  GLY D CA  1 
ATOM   3669  C  C   . GLY D  1 45  ? 25.231  -11.242 22.199 1.00 25.75  ? 44  GLY D C   1 
ATOM   3670  O  O   . GLY D  1 45  ? 25.333  -10.356 23.043 1.00 26.87  ? 44  GLY D O   1 
ATOM   3671  N  N   . PHE D  1 46  ? 25.511  -11.065 20.908 1.00 25.61  ? 45  PHE D N   1 
ATOM   3672  C  CA  . PHE D  1 46  ? 26.226  -9.899  20.423 1.00 23.13  ? 45  PHE D CA  1 
ATOM   3673  C  C   . PHE D  1 46  ? 25.583  -9.491  19.106 1.00 23.37  ? 45  PHE D C   1 
ATOM   3674  O  O   . PHE D  1 46  ? 25.764  -10.177 18.106 1.00 24.02  ? 45  PHE D O   1 
ATOM   3675  C  CB  . PHE D  1 46  ? 27.684  -10.291 20.213 1.00 20.91  ? 45  PHE D CB  1 
ATOM   3676  C  CG  . PHE D  1 46  ? 28.664  -9.169  19.998 1.00 20.63  ? 45  PHE D CG  1 
ATOM   3677  C  CD1 . PHE D  1 46  ? 28.942  -8.267  21.013 1.00 20.04  ? 45  PHE D CD1 1 
ATOM   3678  C  CD2 . PHE D  1 46  ? 29.360  -9.052  18.797 1.00 20.26  ? 45  PHE D CD2 1 
ATOM   3679  C  CE1 . PHE D  1 46  ? 29.887  -7.263  20.835 1.00 18.63  ? 45  PHE D CE1 1 
ATOM   3680  C  CE2 . PHE D  1 46  ? 30.302  -8.050  18.619 1.00 19.01  ? 45  PHE D CE2 1 
ATOM   3681  C  CZ  . PHE D  1 46  ? 30.564  -7.160  19.640 1.00 18.15  ? 45  PHE D CZ  1 
ATOM   3682  N  N   . HIS D  1 47  ? 24.818  -8.389  19.126 1.00 22.19  ? 46  HIS D N   1 
ATOM   3683  C  CA  . HIS D  1 47  ? 24.018  -8.042  17.966 1.00 21.60  ? 46  HIS D CA  1 
ATOM   3684  C  C   . HIS D  1 47  ? 24.074  -6.551  17.674 1.00 22.58  ? 46  HIS D C   1 
ATOM   3685  O  O   . HIS D  1 47  ? 24.257  -5.724  18.575 1.00 22.94  ? 46  HIS D O   1 
ATOM   3686  C  CB  . HIS D  1 47  ? 22.562  -8.462  18.157 1.00 22.39  ? 46  HIS D CB  1 
ATOM   3687  C  CG  . HIS D  1 47  ? 22.404  -9.800  18.791 1.00 22.96  ? 46  HIS D CG  1 
ATOM   3688  N  ND1 . HIS D  1 47  ? 21.959  -9.958  20.094 1.00 23.54  ? 46  HIS D ND1 1 
ATOM   3689  C  CD2 . HIS D  1 47  ? 22.649  -11.038 18.318 1.00 23.00  ? 46  HIS D CD2 1 
ATOM   3690  C  CE1 . HIS D  1 47  ? 21.938  -11.241 20.390 1.00 24.43  ? 46  HIS D CE1 1 
ATOM   3691  N  NE2 . HIS D  1 47  ? 22.362  -11.926 19.318 1.00 23.67  ? 46  HIS D NE2 1 
ATOM   3692  N  N   . VAL D  1 48  ? 23.877  -6.239  16.390 1.00 22.76  ? 47  VAL D N   1 
ATOM   3693  C  CA  . VAL D  1 48  ? 23.544  -4.886  15.991 1.00 23.80  ? 47  VAL D CA  1 
ATOM   3694  C  C   . VAL D  1 48  ? 22.022  -4.762  15.973 1.00 24.99  ? 47  VAL D C   1 
ATOM   3695  O  O   . VAL D  1 48  ? 21.360  -5.440  15.187 1.00 22.95  ? 47  VAL D O   1 
ATOM   3696  C  CB  . VAL D  1 48  ? 24.141  -4.523  14.621 1.00 23.38  ? 47  VAL D CB  1 
ATOM   3697  C  CG1 . VAL D  1 48  ? 23.839  -3.073  14.265 1.00 24.16  ? 47  VAL D CG1 1 
ATOM   3698  C  CG2 . VAL D  1 48  ? 25.637  -4.771  14.575 1.00 22.41  ? 47  VAL D CG2 1 
ATOM   3699  N  N   . HIS D  1 49  ? 21.489  -3.890  16.841 1.00 27.42  ? 48  HIS D N   1 
ATOM   3700  C  CA  . HIS D  1 49  ? 20.076  -3.550  16.832 1.00 30.69  ? 48  HIS D CA  1 
ATOM   3701  C  C   . HIS D  1 49  ? 19.815  -2.382  15.878 1.00 32.86  ? 48  HIS D C   1 
ATOM   3702  O  O   . HIS D  1 49  ? 20.752  -1.726  15.420 1.00 35.04  ? 48  HIS D O   1 
ATOM   3703  C  CB  . HIS D  1 49  ? 19.594  -3.282  18.256 1.00 31.08  ? 48  HIS D CB  1 
ATOM   3704  C  CG  . HIS D  1 49  ? 19.620  -4.492  19.124 1.00 31.89  ? 48  HIS D CG  1 
ATOM   3705  N  ND1 . HIS D  1 49  ? 18.481  -4.990  19.732 1.00 31.42  ? 48  HIS D ND1 1 
ATOM   3706  C  CD2 . HIS D  1 49  ? 20.632  -5.305  19.495 1.00 31.22  ? 48  HIS D CD2 1 
ATOM   3707  C  CE1 . HIS D  1 49  ? 18.796  -6.056  20.446 1.00 31.60  ? 48  HIS D CE1 1 
ATOM   3708  N  NE2 . HIS D  1 49  ? 20.108  -6.268  20.327 1.00 32.19  ? 48  HIS D NE2 1 
ATOM   3709  N  N   . GLU D  1 50  ? 18.528  -2.105  15.619 1.00 32.88  ? 49  GLU D N   1 
ATOM   3710  C  CA  . GLU D  1 50  ? 18.094  -1.273  14.506 1.00 31.55  ? 49  GLU D CA  1 
ATOM   3711  C  C   . GLU D  1 50  ? 18.398  0.213   14.723 1.00 33.08  ? 49  GLU D C   1 
ATOM   3712  O  O   . GLU D  1 50  ? 18.819  0.889   13.789 1.00 31.08  ? 49  GLU D O   1 
ATOM   3713  C  CB  . GLU D  1 50  ? 16.593  -1.429  14.285 1.00 32.27  ? 49  GLU D CB  1 
ATOM   3714  C  CG  . GLU D  1 50  ? 16.147  -0.897  12.941 1.00 33.28  ? 49  GLU D CG  1 
ATOM   3715  C  CD  . GLU D  1 50  ? 14.664  -1.028  12.642 1.00 33.85  ? 49  GLU D CD  1 
ATOM   3716  O  OE1 . GLU D  1 50  ? 13.969  -1.843  13.311 1.00 32.96  ? 49  GLU D OE1 1 
ATOM   3717  O  OE2 . GLU D  1 50  ? 14.206  -0.306  11.735 1.00 35.02  ? 49  GLU D OE2 1 
ATOM   3718  N  N   . PHE D  1 51  ? 18.162  0.719   15.939 1.00 33.36  ? 50  PHE D N   1 
ATOM   3719  C  CA  . PHE D  1 51  ? 18.154  2.155   16.169 1.00 32.72  ? 50  PHE D CA  1 
ATOM   3720  C  C   . PHE D  1 51  ? 19.324  2.592   17.038 1.00 31.98  ? 50  PHE D C   1 
ATOM   3721  O  O   . PHE D  1 51  ? 19.563  2.009   18.093 1.00 33.06  ? 50  PHE D O   1 
ATOM   3722  C  CB  . PHE D  1 51  ? 16.859  2.585   16.862 1.00 33.01  ? 50  PHE D CB  1 
ATOM   3723  C  CG  . PHE D  1 51  ? 15.626  2.159   16.110 1.00 33.56  ? 50  PHE D CG  1 
ATOM   3724  C  CD1 . PHE D  1 51  ? 15.446  2.543   14.784 1.00 32.71  ? 50  PHE D CD1 1 
ATOM   3725  C  CD2 . PHE D  1 51  ? 14.662  1.362   16.717 1.00 31.60  ? 50  PHE D CD2 1 
ATOM   3726  C  CE1 . PHE D  1 51  ? 14.317  2.154   14.079 1.00 31.17  ? 50  PHE D CE1 1 
ATOM   3727  C  CE2 . PHE D  1 51  ? 13.530  0.977   16.010 1.00 30.90  ? 50  PHE D CE2 1 
ATOM   3728  C  CZ  . PHE D  1 51  ? 13.364  1.367   14.694 1.00 31.30  ? 50  PHE D CZ  1 
ATOM   3729  N  N   . GLY D  1 52  ? 20.007  3.651   16.581 1.00 29.22  ? 51  GLY D N   1 
ATOM   3730  C  CA  . GLY D  1 52  ? 20.972  4.384   17.376 1.00 26.10  ? 51  GLY D CA  1 
ATOM   3731  C  C   . GLY D  1 52  ? 20.265  5.310   18.361 1.00 26.07  ? 51  GLY D C   1 
ATOM   3732  O  O   . GLY D  1 52  ? 20.490  6.520   18.376 1.00 26.35  ? 51  GLY D O   1 
ATOM   3733  N  N   . ASP D  1 53  ? 19.397  4.723   19.181 1.00 24.65  ? 52  ASP D N   1 
ATOM   3734  C  CA  . ASP D  1 53  ? 18.555  5.504   20.061 1.00 24.77  ? 52  ASP D CA  1 
ATOM   3735  C  C   . ASP D  1 53  ? 18.739  4.987   21.479 1.00 25.50  ? 52  ASP D C   1 
ATOM   3736  O  O   . ASP D  1 53  ? 18.389  3.845   21.772 1.00 29.68  ? 52  ASP D O   1 
ATOM   3737  C  CB  . ASP D  1 53  ? 17.103  5.422   19.591 1.00 25.34  ? 52  ASP D CB  1 
ATOM   3738  C  CG  . ASP D  1 53  ? 16.127  6.228   20.431 1.00 25.19  ? 52  ASP D CG  1 
ATOM   3739  O  OD1 . ASP D  1 53  ? 16.432  6.485   21.623 1.00 23.40  ? 52  ASP D OD1 1 
ATOM   3740  O  OD2 . ASP D  1 53  ? 15.065  6.596   19.878 1.00 24.89  ? 52  ASP D OD2 1 
ATOM   3741  N  N   . ASN D  1 54  ? 19.292  5.829   22.348 1.00 24.66  ? 53  ASN D N   1 
ATOM   3742  C  CA  A ASN D  1 54  ? 19.595  5.412   23.704 0.50 23.99  ? 53  ASN D CA  1 
ATOM   3743  C  CA  B ASN D  1 54  ? 19.591  5.409   23.705 0.50 24.75  ? 53  ASN D CA  1 
ATOM   3744  C  C   . ASN D  1 54  ? 18.730  6.210   24.679 1.00 24.13  ? 53  ASN D C   1 
ATOM   3745  O  O   . ASN D  1 54  ? 19.012  6.269   25.870 1.00 24.00  ? 53  ASN D O   1 
ATOM   3746  C  CB  A ASN D  1 54  ? 21.106  5.491   23.961 0.50 23.52  ? 53  ASN D CB  1 
ATOM   3747  C  CB  B ASN D  1 54  ? 21.100  5.366   23.991 0.50 25.55  ? 53  ASN D CB  1 
ATOM   3748  C  CG  A ASN D  1 54  ? 21.539  5.075   25.355 0.50 22.03  ? 53  ASN D CG  1 
ATOM   3749  C  CG  B ASN D  1 54  ? 21.850  4.286   23.200 0.50 25.56  ? 53  ASN D CG  1 
ATOM   3750  O  OD1 A ASN D  1 54  ? 21.228  3.976   25.808 0.50 21.27  ? 53  ASN D OD1 1 
ATOM   3751  O  OD1 B ASN D  1 54  ? 21.246  3.362   22.643 0.50 24.67  ? 53  ASN D OD1 1 
ATOM   3752  N  ND2 A ASN D  1 54  ? 22.279  5.938   26.037 0.50 21.00  ? 53  ASN D ND2 1 
ATOM   3753  N  ND2 B ASN D  1 54  ? 23.177  4.366   23.136 0.50 23.33  ? 53  ASN D ND2 1 
ATOM   3754  N  N   . THR D  1 55  ? 17.647  6.799   24.173 1.00 24.79  ? 54  THR D N   1 
ATOM   3755  C  CA  . THR D  1 55  ? 16.839  7.726   24.961 1.00 26.63  ? 54  THR D CA  1 
ATOM   3756  C  C   . THR D  1 55  ? 16.270  7.046   26.200 1.00 27.23  ? 54  THR D C   1 
ATOM   3757  O  O   . THR D  1 55  ? 16.092  7.691   27.226 1.00 29.43  ? 54  THR D O   1 
ATOM   3758  C  CB  . THR D  1 55  ? 15.704  8.363   24.151 1.00 26.21  ? 54  THR D CB  1 
ATOM   3759  O  OG1 . THR D  1 55  ? 14.898  7.301   23.650 1.00 26.36  ? 54  THR D OG1 1 
ATOM   3760  C  CG2 . THR D  1 55  ? 16.200  9.211   23.000 1.00 26.55  ? 54  THR D CG2 1 
ATOM   3761  N  N   . ALA D  1 56  ? 15.975  5.749   26.090 1.00 28.94  ? 55  ALA D N   1 
ATOM   3762  C  CA  . ALA D  1 56  ? 15.395  5.002   27.194 1.00 28.94  ? 55  ALA D CA  1 
ATOM   3763  C  C   . ALA D  1 56  ? 16.307  3.827   27.526 1.00 30.47  ? 55  ALA D C   1 
ATOM   3764  O  O   . ALA D  1 56  ? 15.838  2.717   27.721 1.00 33.71  ? 55  ALA D O   1 
ATOM   3765  C  CB  . ALA D  1 56  ? 14.013  4.541   26.803 1.00 27.17  ? 55  ALA D CB  1 
ATOM   3766  N  N   . GLY D  1 57  ? 17.619  4.080   27.561 1.00 30.67  ? 56  GLY D N   1 
ATOM   3767  C  CA  . GLY D  1 57  ? 18.597  3.019   27.755 1.00 30.46  ? 56  GLY D CA  1 
ATOM   3768  C  C   . GLY D  1 57  ? 18.715  2.140   26.509 1.00 32.53  ? 56  GLY D C   1 
ATOM   3769  O  O   . GLY D  1 57  ? 18.363  2.553   25.402 1.00 32.05  ? 56  GLY D O   1 
ATOM   3770  N  N   . CYS D  1 58  ? 19.180  0.906   26.713 1.00 30.67  ? 57  CYS D N   1 
ATOM   3771  C  CA  . CYS D  1 58  ? 19.420  0.009   25.593 1.00 28.66  ? 57  CYS D CA  1 
ATOM   3772  C  C   . CYS D  1 58  ? 18.114  -0.438  24.945 1.00 27.71  ? 57  CYS D C   1 
ATOM   3773  O  O   . CYS D  1 58  ? 18.117  -0.805  23.776 1.00 25.76  ? 57  CYS D O   1 
ATOM   3774  C  CB  . CYS D  1 58  ? 20.249  -1.189  26.018 1.00 28.28  ? 57  CYS D CB  1 
ATOM   3775  S  SG  . CYS D  1 58  ? 21.939  -0.703  26.477 1.00 30.65  ? 57  CYS D SG  1 
ATOM   3776  N  N   . THR D  1 59  ? 17.006  -0.368  25.700 1.00 27.22  ? 58  THR D N   1 
ATOM   3777  C  CA  . THR D  1 59  ? 15.703  -0.808  25.220 1.00 27.62  ? 58  THR D CA  1 
ATOM   3778  C  C   . THR D  1 59  ? 15.331  -0.096  23.925 1.00 27.91  ? 58  THR D C   1 
ATOM   3779  O  O   . THR D  1 59  ? 14.742  -0.703  23.030 1.00 25.98  ? 58  THR D O   1 
ATOM   3780  C  CB  . THR D  1 59  ? 14.577  -0.445  26.193 1.00 27.51  ? 58  THR D CB  1 
ATOM   3781  O  OG1 . THR D  1 59  ? 14.984  -0.874  27.489 1.00 30.78  ? 58  THR D OG1 1 
ATOM   3782  C  CG2 . THR D  1 59  ? 13.248  -1.060  25.818 1.00 27.68  ? 58  THR D CG2 1 
ATOM   3783  N  N   . SER D  1 60  ? 15.658  1.202   23.851 1.00 29.57  ? 59  SER D N   1 
ATOM   3784  C  CA  . SER D  1 60  ? 15.108  2.007   22.771 1.00 29.30  ? 59  SER D CA  1 
ATOM   3785  C  C   . SER D  1 60  ? 15.870  1.751   21.468 1.00 28.21  ? 59  SER D C   1 
ATOM   3786  O  O   . SER D  1 60  ? 15.553  2.336   20.436 1.00 28.91  ? 59  SER D O   1 
ATOM   3787  C  CB  . SER D  1 60  ? 15.000  3.470   23.166 1.00 28.40  ? 59  SER D CB  1 
ATOM   3788  O  OG  . SER D  1 60  ? 16.239  3.968   23.635 1.00 31.83  ? 59  SER D OG  1 
ATOM   3789  N  N   . ALA D  1 61  ? 16.828  0.816   21.517 1.00 27.65  ? 60  ALA D N   1 
ATOM   3790  C  CA  . ALA D  1 61  ? 17.620  0.428   20.360 1.00 28.02  ? 60  ALA D CA  1 
ATOM   3791  C  C   . ALA D  1 61  ? 16.776  -0.402  19.397 1.00 29.09  ? 60  ALA D C   1 
ATOM   3792  O  O   . ALA D  1 61  ? 17.137  -0.557  18.228 1.00 29.50  ? 60  ALA D O   1 
ATOM   3793  C  CB  . ALA D  1 61  ? 18.838  -0.333  20.807 1.00 27.04  ? 60  ALA D CB  1 
ATOM   3794  N  N   . GLY D  1 62  ? 15.661  -0.937  19.911 1.00 28.55  ? 61  GLY D N   1 
ATOM   3795  C  CA  . GLY D  1 62  ? 14.744  -1.736  19.117 1.00 28.51  ? 61  GLY D CA  1 
ATOM   3796  C  C   . GLY D  1 62  ? 15.252  -3.156  18.890 1.00 30.25  ? 61  GLY D C   1 
ATOM   3797  O  O   . GLY D  1 62  ? 16.114  -3.637  19.631 1.00 32.00  ? 61  GLY D O   1 
ATOM   3798  N  N   . PRO D  1 63  ? 14.743  -3.861  17.847 1.00 30.72  ? 62  PRO D N   1 
ATOM   3799  C  CA  . PRO D  1 63  ? 15.082  -5.269  17.607 1.00 29.50  ? 62  PRO D CA  1 
ATOM   3800  C  C   . PRO D  1 63  ? 16.425  -5.424  16.894 1.00 27.40  ? 62  PRO D C   1 
ATOM   3801  O  O   . PRO D  1 63  ? 17.061  -4.430  16.554 1.00 23.99  ? 62  PRO D O   1 
ATOM   3802  C  CB  . PRO D  1 63  ? 13.945  -5.703  16.672 1.00 27.39  ? 62  PRO D CB  1 
ATOM   3803  C  CG  . PRO D  1 63  ? 13.684  -4.474  15.839 1.00 27.76  ? 62  PRO D CG  1 
ATOM   3804  C  CD  . PRO D  1 63  ? 13.844  -3.322  16.810 1.00 29.73  ? 62  PRO D CD  1 
ATOM   3805  N  N   . HIS D  1 64  ? 16.850  -6.673  16.666 1.00 28.38  ? 63  HIS D N   1 
ATOM   3806  C  CA  . HIS D  1 64  ? 18.044  -6.919  15.869 1.00 28.77  ? 63  HIS D CA  1 
ATOM   3807  C  C   . HIS D  1 64  ? 17.855  -6.242  14.515 1.00 27.66  ? 63  HIS D C   1 
ATOM   3808  O  O   . HIS D  1 64  ? 16.776  -6.338  13.933 1.00 30.69  ? 63  HIS D O   1 
ATOM   3809  C  CB  . HIS D  1 64  ? 18.277  -8.435  15.673 1.00 27.87  ? 63  HIS D CB  1 
ATOM   3810  C  CG  . HIS D  1 64  ? 18.554  -9.187  16.930 1.00 27.82  ? 63  HIS D CG  1 
ATOM   3811  N  ND1 . HIS D  1 64  ? 18.638  -10.572 16.942 1.00 28.92  ? 63  HIS D ND1 1 
ATOM   3812  C  CD2 . HIS D  1 64  ? 18.762  -8.772  18.205 1.00 27.25  ? 63  HIS D CD2 1 
ATOM   3813  C  CE1 . HIS D  1 64  ? 18.908  -10.978 18.174 1.00 31.20  ? 63  HIS D CE1 1 
ATOM   3814  N  NE2 . HIS D  1 64  ? 18.979  -9.890  18.974 1.00 28.02  ? 63  HIS D NE2 1 
ATOM   3815  N  N   . PHE D  1 65  ? 18.898  -5.570  14.020 1.00 25.07  ? 64  PHE D N   1 
ATOM   3816  C  CA  . PHE D  1 65  ? 18.855  -4.930  12.714 1.00 26.16  ? 64  PHE D CA  1 
ATOM   3817  C  C   . PHE D  1 65  ? 18.510  -5.961  11.637 1.00 26.74  ? 64  PHE D C   1 
ATOM   3818  O  O   . PHE D  1 65  ? 19.263  -6.906  11.398 1.00 25.01  ? 64  PHE D O   1 
ATOM   3819  C  CB  . PHE D  1 65  ? 20.180  -4.219  12.426 1.00 27.92  ? 64  PHE D CB  1 
ATOM   3820  C  CG  . PHE D  1 65  ? 20.250  -3.516  11.095 1.00 27.92  ? 64  PHE D CG  1 
ATOM   3821  C  CD1 . PHE D  1 65  ? 19.177  -2.763  10.626 1.00 28.71  ? 64  PHE D CD1 1 
ATOM   3822  C  CD2 . PHE D  1 65  ? 21.400  -3.580  10.322 1.00 28.06  ? 64  PHE D CD2 1 
ATOM   3823  C  CE1 . PHE D  1 65  ? 19.245  -2.109  9.402  1.00 27.81  ? 64  PHE D CE1 1 
ATOM   3824  C  CE2 . PHE D  1 65  ? 21.469  -2.923  9.100  1.00 28.69  ? 64  PHE D CE2 1 
ATOM   3825  C  CZ  . PHE D  1 65  ? 20.391  -2.191  8.641  1.00 28.85  ? 64  PHE D CZ  1 
ATOM   3826  N  N   . ASN D  1 66  ? 17.364  -5.770  10.973 1.00 28.86  ? 65  ASN D N   1 
ATOM   3827  C  CA  . ASN D  1 66  ? 16.814  -6.838  10.152 1.00 30.34  ? 65  ASN D CA  1 
ATOM   3828  C  C   . ASN D  1 66  ? 16.273  -6.288  8.829  1.00 31.83  ? 65  ASN D C   1 
ATOM   3829  O  O   . ASN D  1 66  ? 15.120  -6.527  8.479  1.00 31.39  ? 65  ASN D O   1 
ATOM   3830  C  CB  . ASN D  1 66  ? 15.775  -7.647  10.937 1.00 31.38  ? 65  ASN D CB  1 
ATOM   3831  C  CG  . ASN D  1 66  ? 15.252  -8.845  10.163 1.00 34.47  ? 65  ASN D CG  1 
ATOM   3832  O  OD1 . ASN D  1 66  ? 15.891  -9.319  9.225  1.00 36.57  ? 65  ASN D OD1 1 
ATOM   3833  N  ND2 . ASN D  1 66  ? 14.089  -9.344  10.540 1.00 34.16  ? 65  ASN D ND2 1 
ATOM   3834  N  N   . PRO D  1 67  ? 17.082  -5.592  7.993  1.00 31.08  ? 66  PRO D N   1 
ATOM   3835  C  CA  . PRO D  1 67  ? 16.550  -4.955  6.790  1.00 31.21  ? 66  PRO D CA  1 
ATOM   3836  C  C   . PRO D  1 67  ? 15.972  -5.918  5.752  1.00 34.65  ? 66  PRO D C   1 
ATOM   3837  O  O   . PRO D  1 67  ? 15.220  -5.502  4.883  1.00 36.86  ? 66  PRO D O   1 
ATOM   3838  C  CB  . PRO D  1 67  ? 17.758  -4.226  6.184  1.00 30.35  ? 66  PRO D CB  1 
ATOM   3839  C  CG  . PRO D  1 67  ? 18.961  -4.940  6.757  1.00 30.76  ? 66  PRO D CG  1 
ATOM   3840  C  CD  . PRO D  1 67  ? 18.542  -5.440  8.119  1.00 30.33  ? 66  PRO D CD  1 
ATOM   3841  N  N   . LEU D  1 68  ? 16.325  -7.205  5.834  1.00 38.10  ? 67  LEU D N   1 
ATOM   3842  C  CA  . LEU D  1 68  ? 15.910  -8.166  4.821  1.00 36.07  ? 67  LEU D CA  1 
ATOM   3843  C  C   . LEU D  1 68  ? 14.741  -9.024  5.308  1.00 36.94  ? 67  LEU D C   1 
ATOM   3844  O  O   . LEU D  1 68  ? 14.340  -9.950  4.613  1.00 36.54  ? 67  LEU D O   1 
ATOM   3845  C  CB  . LEU D  1 68  ? 17.100  -9.043  4.423  1.00 38.36  ? 67  LEU D CB  1 
ATOM   3846  C  CG  . LEU D  1 68  ? 18.231  -8.338  3.670  1.00 40.92  ? 67  LEU D CG  1 
ATOM   3847  C  CD1 . LEU D  1 68  ? 19.324  -9.323  3.290  1.00 43.49  ? 67  LEU D CD1 1 
ATOM   3848  C  CD2 . LEU D  1 68  ? 17.702  -7.560  2.473  1.00 39.84  ? 67  LEU D CD2 1 
ATOM   3849  N  N   . SER D  1 69  ? 14.207  -8.720  6.502  1.00 38.78  ? 68  SER D N   1 
ATOM   3850  C  CA  . SER D  1 69  ? 13.040  -9.384  7.069  1.00 38.74  ? 68  SER D CA  1 
ATOM   3851  C  C   . SER D  1 69  ? 13.215  -10.899 7.136  1.00 41.60  ? 68  SER D C   1 
ATOM   3852  O  O   . SER D  1 69  ? 12.351  -11.623 6.646  1.00 43.25  ? 68  SER D O   1 
ATOM   3853  C  CB  . SER D  1 69  ? 11.801  -9.057  6.287  1.00 35.58  ? 68  SER D CB  1 
ATOM   3854  O  OG  . SER D  1 69  ? 11.473  -7.692  6.398  1.00 31.99  ? 68  SER D OG  1 
ATOM   3855  N  N   . ARG D  1 70  ? 14.314  -11.373 7.742  1.00 41.53  ? 69  ARG D N   1 
ATOM   3856  C  CA  . ARG D  1 70  ? 14.537  -12.802 7.912  1.00 38.94  ? 69  ARG D CA  1 
ATOM   3857  C  C   . ARG D  1 70  ? 14.383  -13.162 9.387  1.00 38.91  ? 69  ARG D C   1 
ATOM   3858  O  O   . ARG D  1 70  ? 14.214  -12.280 10.230 1.00 38.10  ? 69  ARG D O   1 
ATOM   3859  C  CB  . ARG D  1 70  ? 15.923  -13.212 7.409  1.00 40.46  ? 69  ARG D CB  1 
ATOM   3860  C  CG  . ARG D  1 70  ? 16.247  -12.746 5.998  1.00 45.13  ? 69  ARG D CG  1 
ATOM   3861  C  CD  . ARG D  1 70  ? 15.891  -13.728 4.889  1.00 57.44  ? 69  ARG D CD  1 
ATOM   3862  N  NE  . ARG D  1 70  ? 16.602  -13.266 3.685  1.00 79.38  ? 69  ARG D NE  1 
ATOM   3863  C  CZ  . ARG D  1 70  ? 17.858  -13.571 3.339  1.00 85.60  ? 69  ARG D CZ  1 
ATOM   3864  N  NH1 . ARG D  1 70  ? 18.566  -14.393 4.093  1.00 98.63  ? 69  ARG D NH1 1 
ATOM   3865  N  NH2 . ARG D  1 70  ? 18.406  -13.030 2.264  1.00 80.77  ? 69  ARG D NH2 1 
ATOM   3866  N  N   . LYS D  1 71  ? 14.432  -14.471 9.678  1.00 39.85  ? 70  LYS D N   1 
ATOM   3867  C  CA  . LYS D  1 71  ? 14.389  -14.965 11.046 1.00 37.12  ? 70  LYS D CA  1 
ATOM   3868  C  C   . LYS D  1 71  ? 15.796  -14.954 11.637 1.00 32.88  ? 70  LYS D C   1 
ATOM   3869  O  O   . LYS D  1 71  ? 16.768  -14.906 10.908 1.00 32.10  ? 70  LYS D O   1 
ATOM   3870  C  CB  . LYS D  1 71  ? 13.645  -16.313 11.111 1.00 39.64  ? 70  LYS D CB  1 
ATOM   3871  C  CG  . LYS D  1 71  ? 12.255  -16.328 10.483 1.00 44.96  ? 70  LYS D CG  1 
ATOM   3872  C  CD  . LYS D  1 71  ? 11.090  -16.976 11.304 1.00 50.47  ? 70  LYS D CD  1 
ATOM   3873  C  CE  . LYS D  1 71  ? 10.220  -17.907 10.483 1.00 54.46  ? 70  LYS D CE  1 
ATOM   3874  N  NZ  . LYS D  1 71  ? 8.777   -17.790 10.821 1.00 53.59  ? 70  LYS D NZ  1 
ATOM   3875  N  N   . HIS D  1 72  ? 15.890  -14.969 12.967 1.00 30.87  ? 71  HIS D N   1 
ATOM   3876  C  CA  . HIS D  1 72  ? 17.161  -14.879 13.672 1.00 32.50  ? 71  HIS D CA  1 
ATOM   3877  C  C   . HIS D  1 72  ? 17.983  -16.147 13.445 1.00 36.01  ? 71  HIS D C   1 
ATOM   3878  O  O   . HIS D  1 72  ? 17.441  -17.258 13.452 1.00 38.17  ? 71  HIS D O   1 
ATOM   3879  C  CB  . HIS D  1 72  ? 16.917  -14.624 15.154 1.00 31.03  ? 71  HIS D CB  1 
ATOM   3880  C  CG  . HIS D  1 72  ? 18.149  -14.633 15.986 1.00 32.36  ? 71  HIS D CG  1 
ATOM   3881  N  ND1 . HIS D  1 72  ? 18.958  -13.515 16.145 1.00 31.70  ? 71  HIS D ND1 1 
ATOM   3882  C  CD2 . HIS D  1 72  ? 18.714  -15.632 16.709 1.00 34.47  ? 71  HIS D CD2 1 
ATOM   3883  C  CE1 . HIS D  1 72  ? 19.972  -13.826 16.921 1.00 33.82  ? 71  HIS D CE1 1 
ATOM   3884  N  NE2 . HIS D  1 72  ? 19.847  -15.119 17.277 1.00 36.12  ? 71  HIS D NE2 1 
ATOM   3885  N  N   . GLY D  1 73  ? 19.298  -15.972 13.243 1.00 35.24  ? 72  GLY D N   1 
ATOM   3886  C  CA  . GLY D  1 73  ? 20.211  -17.100 13.110 1.00 35.34  ? 72  GLY D CA  1 
ATOM   3887  C  C   . GLY D  1 73  ? 21.542  -16.824 13.814 1.00 34.81  ? 72  GLY D C   1 
ATOM   3888  O  O   . GLY D  1 73  ? 21.706  -15.765 14.440 1.00 34.89  ? 72  GLY D O   1 
ATOM   3889  N  N   . GLY D  1 74  ? 22.480  -17.784 13.700 1.00 31.52  ? 73  GLY D N   1 
ATOM   3890  C  CA  . GLY D  1 74  ? 23.883  -17.541 13.990 1.00 29.28  ? 73  GLY D CA  1 
ATOM   3891  C  C   . GLY D  1 74  ? 24.556  -16.846 12.808 1.00 30.76  ? 73  GLY D C   1 
ATOM   3892  O  O   . GLY D  1 74  ? 24.029  -16.878 11.698 1.00 32.06  ? 73  GLY D O   1 
ATOM   3893  N  N   . PRO D  1 75  ? 25.718  -16.180 12.993 1.00 31.81  ? 74  PRO D N   1 
ATOM   3894  C  CA  . PRO D  1 75  ? 26.356  -15.430 11.910 1.00 32.05  ? 74  PRO D CA  1 
ATOM   3895  C  C   . PRO D  1 75  ? 26.619  -16.278 10.672 1.00 32.70  ? 74  PRO D C   1 
ATOM   3896  O  O   . PRO D  1 75  ? 26.613  -15.753 9.567  1.00 33.91  ? 74  PRO D O   1 
ATOM   3897  C  CB  . PRO D  1 75  ? 27.681  -14.916 12.501 1.00 32.51  ? 74  PRO D CB  1 
ATOM   3898  C  CG  . PRO D  1 75  ? 27.868  -15.707 13.784 1.00 32.93  ? 74  PRO D CG  1 
ATOM   3899  C  CD  . PRO D  1 75  ? 26.476  -16.093 14.249 1.00 33.16  ? 74  PRO D CD  1 
ATOM   3900  N  N   . LYS D  1 76  ? 26.791  -17.590 10.872 1.00 34.65  ? 75  LYS D N   1 
ATOM   3901  C  CA  . LYS D  1 76  ? 27.190  -18.492 9.811  1.00 38.23  ? 75  LYS D CA  1 
ATOM   3902  C  C   . LYS D  1 76  ? 25.992  -18.945 8.971  1.00 37.50  ? 75  LYS D C   1 
ATOM   3903  O  O   . LYS D  1 76  ? 26.190  -19.498 7.895  1.00 36.47  ? 75  LYS D O   1 
ATOM   3904  C  CB  . LYS D  1 76  ? 27.888  -19.713 10.427 1.00 39.19  ? 75  LYS D CB  1 
ATOM   3905  C  CG  . LYS D  1 76  ? 29.333  -19.541 10.856 1.00 44.67  ? 75  LYS D CG  1 
ATOM   3906  C  CD  . LYS D  1 76  ? 29.756  -20.544 11.930 1.00 45.91  ? 75  LYS D CD  1 
ATOM   3907  C  CE  . LYS D  1 76  ? 30.076  -21.940 11.420 1.00 47.14  ? 75  LYS D CE  1 
ATOM   3908  N  NZ  . LYS D  1 76  ? 29.488  -23.001 12.275 1.00 42.50  ? 75  LYS D NZ  1 
ATOM   3909  N  N   . ASP D  1 77  ? 24.754  -18.701 9.457  1.00 38.46  ? 76  ASP D N   1 
ATOM   3910  C  CA  . ASP D  1 77  ? 23.535  -19.180 8.831  1.00 37.04  ? 76  ASP D CA  1 
ATOM   3911  C  C   . ASP D  1 77  ? 23.195  -18.307 7.627  1.00 37.33  ? 76  ASP D C   1 
ATOM   3912  O  O   . ASP D  1 77  ? 23.515  -17.119 7.609  1.00 36.37  ? 76  ASP D O   1 
ATOM   3913  C  CB  . ASP D  1 77  ? 22.380  -19.218 9.834  1.00 37.05  ? 76  ASP D CB  1 
ATOM   3914  C  CG  . ASP D  1 77  ? 22.547  -20.319 10.869 1.00 39.61  ? 76  ASP D CG  1 
ATOM   3915  O  OD1 . ASP D  1 77  ? 23.121  -21.353 10.504 1.00 40.34  ? 76  ASP D OD1 1 
ATOM   3916  O  OD2 . ASP D  1 77  ? 22.130  -20.137 12.040 1.00 40.01  ? 76  ASP D OD2 1 
ATOM   3917  N  N   . GLU D  1 78  ? 22.534  -18.899 6.627  1.00 36.72  ? 77  GLU D N   1 
ATOM   3918  C  CA  . GLU D  1 78  ? 22.045  -18.067 5.542  1.00 35.67  ? 77  GLU D CA  1 
ATOM   3919  C  C   . GLU D  1 78  ? 20.801  -17.315 6.017  1.00 37.44  ? 77  GLU D C   1 
ATOM   3920  O  O   . GLU D  1 78  ? 20.598  -16.147 5.686  1.00 38.98  ? 77  GLU D O   1 
ATOM   3921  C  CB  . GLU D  1 78  ? 21.852  -18.806 4.222  0.60 35.74  ? 77  GLU D CB  1 
ATOM   3922  C  CG  . GLU D  1 78  ? 22.030  -17.829 3.072  0.60 37.55  ? 77  GLU D CG  1 
ATOM   3923  C  CD  . GLU D  1 78  ? 20.991  -17.775 1.975  0.60 38.83  ? 77  GLU D CD  1 
ATOM   3924  O  OE1 . GLU D  1 78  ? 19.786  -18.009 2.234  0.60 37.99  ? 77  GLU D OE1 1 
ATOM   3925  O  OE2 . GLU D  1 78  ? 21.404  -17.447 0.874  0.60 38.96  ? 77  GLU D OE2 1 
ATOM   3926  N  N   . GLU D  1 79  ? 19.987  -17.986 6.839  1.00 37.57  ? 78  GLU D N   1 
ATOM   3927  C  CA  . GLU D  1 79  ? 18.819  -17.380 7.467  1.00 37.00  ? 78  GLU D CA  1 
ATOM   3928  C  C   . GLU D  1 79  ? 19.251  -16.698 8.773  1.00 35.91  ? 78  GLU D C   1 
ATOM   3929  O  O   . GLU D  1 79  ? 19.344  -17.328 9.832  1.00 33.62  ? 78  GLU D O   1 
ATOM   3930  C  CB  . GLU D  1 79  ? 17.704  -18.427 7.590  1.00 39.66  ? 78  GLU D CB  1 
ATOM   3931  C  CG  . GLU D  1 79  ? 16.349  -17.906 8.063  1.00 45.00  ? 78  GLU D CG  1 
ATOM   3932  C  CD  . GLU D  1 79  ? 15.535  -17.018 7.126  1.00 53.29  ? 78  GLU D CD  1 
ATOM   3933  O  OE1 . GLU D  1 79  ? 15.938  -16.840 5.949  1.00 59.08  ? 78  GLU D OE1 1 
ATOM   3934  O  OE2 . GLU D  1 79  ? 14.492  -16.484 7.584  1.00 55.14  ? 78  GLU D OE2 1 
ATOM   3935  N  N   . ARG D  1 80  ? 19.541  -15.392 8.674  1.00 35.76  ? 79  ARG D N   1 
ATOM   3936  C  CA  . ARG D  1 80  ? 19.911  -14.571 9.817  1.00 33.62  ? 79  ARG D CA  1 
ATOM   3937  C  C   . ARG D  1 80  ? 19.481  -13.120 9.603  1.00 33.18  ? 79  ARG D C   1 
ATOM   3938  O  O   . ARG D  1 80  ? 19.253  -12.677 8.477  1.00 32.05  ? 79  ARG D O   1 
ATOM   3939  C  CB  . ARG D  1 80  ? 21.426  -14.588 10.032 1.00 32.67  ? 79  ARG D CB  1 
ATOM   3940  C  CG  . ARG D  1 80  ? 22.231  -14.116 8.832  1.00 31.97  ? 79  ARG D CG  1 
ATOM   3941  C  CD  . ARG D  1 80  ? 23.692  -13.997 9.184  1.00 31.75  ? 79  ARG D CD  1 
ATOM   3942  N  NE  . ARG D  1 80  ? 24.012  -12.668 9.678  1.00 33.71  ? 79  ARG D NE  1 
ATOM   3943  C  CZ  . ARG D  1 80  ? 25.246  -12.182 9.812  1.00 33.57  ? 79  ARG D CZ  1 
ATOM   3944  N  NH1 . ARG D  1 80  ? 26.296  -12.926 9.499  1.00 34.00  ? 79  ARG D NH1 1 
ATOM   3945  N  NH2 . ARG D  1 80  ? 25.427  -10.950 10.256 1.00 31.30  ? 79  ARG D NH2 1 
ATOM   3946  N  N   . HIS D  1 81  ? 19.385  -12.392 10.722 1.00 33.36  ? 80  HIS D N   1 
ATOM   3947  C  CA  . HIS D  1 81  ? 19.332  -10.940 10.723 1.00 30.21  ? 80  HIS D CA  1 
ATOM   3948  C  C   . HIS D  1 81  ? 20.701  -10.408 10.331 1.00 29.54  ? 80  HIS D C   1 
ATOM   3949  O  O   . HIS D  1 81  ? 21.718  -11.003 10.695 1.00 30.32  ? 80  HIS D O   1 
ATOM   3950  C  CB  . HIS D  1 81  ? 18.988  -10.438 12.126 1.00 27.74  ? 80  HIS D CB  1 
ATOM   3951  C  CG  . HIS D  1 81  ? 17.681  -10.934 12.631 1.00 27.38  ? 80  HIS D CG  1 
ATOM   3952  N  ND1 . HIS D  1 81  ? 17.458  -11.228 13.965 1.00 28.59  ? 80  HIS D ND1 1 
ATOM   3953  C  CD2 . HIS D  1 81  ? 16.520  -11.168 11.984 1.00 27.26  ? 80  HIS D CD2 1 
ATOM   3954  C  CE1 . HIS D  1 81  ? 16.207  -11.615 14.110 1.00 29.64  ? 80  HIS D CE1 1 
ATOM   3955  N  NE2 . HIS D  1 81  ? 15.616  -11.600 12.916 1.00 30.24  ? 80  HIS D NE2 1 
ATOM   3956  N  N   . VAL D  1 82  ? 20.721  -9.280  9.610  1.00 29.23  ? 81  VAL D N   1 
ATOM   3957  C  CA  . VAL D  1 82  ? 21.985  -8.637  9.299  1.00 30.74  ? 81  VAL D CA  1 
ATOM   3958  C  C   . VAL D  1 82  ? 22.777  -8.409  10.588 1.00 32.86  ? 81  VAL D C   1 
ATOM   3959  O  O   . VAL D  1 82  ? 23.985  -8.603  10.611 1.00 32.00  ? 81  VAL D O   1 
ATOM   3960  C  CB  . VAL D  1 82  ? 21.807  -7.341  8.480  1.00 30.30  ? 81  VAL D CB  1 
ATOM   3961  C  CG1 . VAL D  1 82  ? 23.063  -6.478  8.490  1.00 29.44  ? 81  VAL D CG1 1 
ATOM   3962  C  CG2 . VAL D  1 82  ? 21.367  -7.633  7.059  1.00 28.01  ? 81  VAL D CG2 1 
ATOM   3963  N  N   . GLY D  1 83  ? 22.087  -8.041  11.673 1.00 32.58  ? 82  GLY D N   1 
ATOM   3964  C  CA  . GLY D  1 83  ? 22.782  -7.675  12.899 1.00 29.81  ? 82  GLY D CA  1 
ATOM   3965  C  C   . GLY D  1 83  ? 23.203  -8.876  13.742 1.00 29.55  ? 82  GLY D C   1 
ATOM   3966  O  O   . GLY D  1 83  ? 23.718  -8.678  14.841 1.00 34.54  ? 82  GLY D O   1 
ATOM   3967  N  N   . ASP D  1 84  ? 22.993  -10.101 13.230 1.00 28.18  ? 83  ASP D N   1 
ATOM   3968  C  CA  . ASP D  1 84  ? 23.212  -11.323 13.993 1.00 27.09  ? 83  ASP D CA  1 
ATOM   3969  C  C   . ASP D  1 84  ? 24.701  -11.701 13.982 1.00 30.52  ? 83  ASP D C   1 
ATOM   3970  O  O   . ASP D  1 84  ? 25.195  -12.343 13.053 1.00 29.53  ? 83  ASP D O   1 
ATOM   3971  C  CB  . ASP D  1 84  ? 22.331  -12.459 13.478 1.00 26.94  ? 83  ASP D CB  1 
ATOM   3972  C  CG  . ASP D  1 84  ? 20.872  -12.353 13.888 1.00 29.19  ? 83  ASP D CG  1 
ATOM   3973  O  OD1 . ASP D  1 84  ? 20.568  -11.578 14.824 1.00 29.31  ? 83  ASP D OD1 1 
ATOM   3974  O  OD2 . ASP D  1 84  ? 20.043  -13.061 13.270 1.00 28.50  ? 83  ASP D OD2 1 
ATOM   3975  N  N   . LEU D  1 85  ? 25.424  -11.319 15.045 1.00 29.99  ? 84  LEU D N   1 
ATOM   3976  C  CA  . LEU D  1 85  ? 26.860  -11.537 15.098 1.00 27.36  ? 84  LEU D CA  1 
ATOM   3977  C  C   . LEU D  1 85  ? 27.210  -12.675 16.058 1.00 28.09  ? 84  LEU D C   1 
ATOM   3978  O  O   . LEU D  1 85  ? 28.376  -12.872 16.385 1.00 28.89  ? 84  LEU D O   1 
ATOM   3979  C  CB  . LEU D  1 85  ? 27.545  -10.235 15.515 1.00 27.17  ? 84  LEU D CB  1 
ATOM   3980  C  CG  . LEU D  1 85  ? 27.587  -9.118  14.466 1.00 26.95  ? 84  LEU D CG  1 
ATOM   3981  C  CD1 . LEU D  1 85  ? 28.432  -7.958  14.964 1.00 24.64  ? 84  LEU D CD1 1 
ATOM   3982  C  CD2 . LEU D  1 85  ? 28.135  -9.611  13.136 1.00 25.78  ? 84  LEU D CD2 1 
ATOM   3983  N  N   . GLY D  1 86  ? 26.201  -13.428 16.513 1.00 27.96  ? 85  GLY D N   1 
ATOM   3984  C  CA  . GLY D  1 86  ? 26.437  -14.607 17.325 1.00 29.02  ? 85  GLY D CA  1 
ATOM   3985  C  C   . GLY D  1 86  ? 26.809  -14.282 18.764 1.00 28.23  ? 85  GLY D C   1 
ATOM   3986  O  O   . GLY D  1 86  ? 26.190  -13.409 19.371 1.00 26.91  ? 85  GLY D O   1 
ATOM   3987  N  N   . ASN D  1 87  ? 27.817  -15.003 19.297 1.00 27.03  ? 86  ASN D N   1 
ATOM   3988  C  CA  . ASN D  1 87  ? 28.208  -14.843 20.690 1.00 24.89  ? 86  ASN D CA  1 
ATOM   3989  C  C   . ASN D  1 87  ? 29.634  -14.321 20.811 1.00 24.33  ? 86  ASN D C   1 
ATOM   3990  O  O   . ASN D  1 87  ? 30.456  -14.454 19.903 1.00 24.63  ? 86  ASN D O   1 
ATOM   3991  C  CB  . ASN D  1 87  ? 28.111  -16.146 21.474 1.00 24.72  ? 86  ASN D CB  1 
ATOM   3992  C  CG  . ASN D  1 87  ? 26.682  -16.607 21.628 1.00 25.68  ? 86  ASN D CG  1 
ATOM   3993  O  OD1 . ASN D  1 87  ? 25.920  -16.066 22.417 1.00 25.98  ? 86  ASN D OD1 1 
ATOM   3994  N  ND2 . ASN D  1 87  ? 26.305  -17.600 20.863 1.00 26.72  ? 86  ASN D ND2 1 
ATOM   3995  N  N   . VAL D  1 88  ? 29.892  -13.706 21.964 1.00 23.58  ? 87  VAL D N   1 
ATOM   3996  C  CA  . VAL D  1 88  ? 31.245  -13.413 22.395 1.00 24.14  ? 87  VAL D CA  1 
ATOM   3997  C  C   . VAL D  1 88  ? 31.465  -14.179 23.699 1.00 25.50  ? 87  VAL D C   1 
ATOM   3998  O  O   . VAL D  1 88  ? 30.499  -14.548 24.365 1.00 25.24  ? 87  VAL D O   1 
ATOM   3999  C  CB  . VAL D  1 88  ? 31.489  -11.896 22.525 1.00 23.20  ? 87  VAL D CB  1 
ATOM   4000  C  CG1 . VAL D  1 88  ? 31.276  -11.176 21.204 1.00 21.15  ? 87  VAL D CG1 1 
ATOM   4001  C  CG2 . VAL D  1 88  ? 30.681  -11.261 23.646 1.00 22.44  ? 87  VAL D CG2 1 
ATOM   4002  N  N   . THR D  1 89  ? 32.731  -14.458 24.027 1.00 26.41  ? 88  THR D N   1 
ATOM   4003  C  CA  . THR D  1 89  ? 33.018  -15.328 25.154 1.00 27.57  ? 88  THR D CA  1 
ATOM   4004  C  C   . THR D  1 89  ? 33.792  -14.557 26.212 1.00 27.72  ? 88  THR D C   1 
ATOM   4005  O  O   . THR D  1 89  ? 34.858  -14.017 25.934 1.00 25.12  ? 88  THR D O   1 
ATOM   4006  C  CB  . THR D  1 89  ? 33.847  -16.543 24.722 1.00 28.00  ? 88  THR D CB  1 
ATOM   4007  O  OG1 . THR D  1 89  ? 33.205  -17.203 23.627 1.00 29.32  ? 88  THR D OG1 1 
ATOM   4008  C  CG2 . THR D  1 89  ? 34.125  -17.493 25.870 1.00 27.63  ? 88  THR D CG2 1 
ATOM   4009  N  N   . ALA D  1 90  ? 33.264  -14.553 27.436 1.00 30.41  ? 89  ALA D N   1 
ATOM   4010  C  CA  . ALA D  1 90  ? 33.971  -13.959 28.558 1.00 32.71  ? 89  ALA D CA  1 
ATOM   4011  C  C   . ALA D  1 90  ? 34.758  -15.035 29.310 1.00 34.40  ? 89  ALA D C   1 
ATOM   4012  O  O   . ALA D  1 90  ? 34.217  -16.093 29.619 1.00 36.77  ? 89  ALA D O   1 
ATOM   4013  C  CB  . ALA D  1 90  ? 32.989  -13.240 29.455 1.00 30.66  ? 89  ALA D CB  1 
ATOM   4014  N  N   . ASP D  1 91  ? 35.999  -14.709 29.640 1.00 34.88  ? 90  ASP D N   1 
ATOM   4015  C  CA  . ASP D  1 91  ? 36.944  -15.564 30.359 1.00 38.50  ? 90  ASP D CA  1 
ATOM   4016  C  C   . ASP D  1 91  ? 36.575  -15.525 31.850 1.00 39.54  ? 90  ASP D C   1 
ATOM   4017  O  O   . ASP D  1 91  ? 35.625  -14.835 32.246 1.00 35.93  ? 90  ASP D O   1 
ATOM   4018  C  CB  . ASP D  1 91  ? 38.413  -15.135 30.173 1.00 43.52  ? 90  ASP D CB  1 
ATOM   4019  C  CG  . ASP D  1 91  ? 38.921  -14.930 28.762 1.00 49.63  ? 90  ASP D CG  1 
ATOM   4020  O  OD1 . ASP D  1 91  ? 38.469  -15.717 27.917 1.00 48.33  ? 90  ASP D OD1 1 
ATOM   4021  O  OD2 . ASP D  1 91  ? 39.813  -14.045 28.552 1.00 54.57  ? 90  ASP D OD2 1 
ATOM   4022  N  N   . LYS D  1 92  ? 37.338  -16.255 32.682 1.00 43.52  ? 91  LYS D N   1 
ATOM   4023  C  CA  . LYS D  1 92  ? 37.038  -16.402 34.099 1.00 45.55  ? 91  LYS D CA  1 
ATOM   4024  C  C   . LYS D  1 92  ? 37.063  -15.048 34.806 1.00 43.24  ? 91  LYS D C   1 
ATOM   4025  O  O   . LYS D  1 92  ? 36.510  -14.942 35.902 1.00 41.16  ? 91  LYS D O   1 
ATOM   4026  C  CB  . LYS D  1 92  ? 37.957  -17.415 34.796 1.00 49.97  ? 91  LYS D CB  1 
ATOM   4027  C  CG  . LYS D  1 92  ? 37.695  -18.859 34.419 0.80 57.68  ? 91  LYS D CG  1 
ATOM   4028  C  CD  . LYS D  1 92  ? 38.364  -19.923 35.228 0.80 62.64  ? 91  LYS D CD  1 
ATOM   4029  C  CE  . LYS D  1 92  ? 38.282  -21.219 34.445 0.80 66.25  ? 91  LYS D CE  1 
ATOM   4030  N  NZ  . LYS D  1 92  ? 38.103  -22.427 35.295 0.80 66.46  ? 91  LYS D NZ  1 
ATOM   4031  N  N   . ASP D  1 93  ? 37.683  -14.038 34.188 1.00 46.52  ? 92  ASP D N   1 
ATOM   4032  C  CA  . ASP D  1 93  ? 37.816  -12.725 34.813 1.00 47.78  ? 92  ASP D CA  1 
ATOM   4033  C  C   . ASP D  1 93  ? 36.715  -11.781 34.328 1.00 44.94  ? 92  ASP D C   1 
ATOM   4034  O  O   . ASP D  1 93  ? 36.669  -10.617 34.727 1.00 43.85  ? 92  ASP D O   1 
ATOM   4035  C  CB  . ASP D  1 93  ? 39.166  -12.072 34.495 1.00 46.72  ? 92  ASP D CB  1 
ATOM   4036  C  CG  . ASP D  1 93  ? 39.532  -12.054 33.022 1.00 52.46  ? 92  ASP D CG  1 
ATOM   4037  O  OD1 . ASP D  1 93  ? 38.635  -12.306 32.138 1.00 53.04  ? 92  ASP D OD1 1 
ATOM   4038  O  OD2 . ASP D  1 93  ? 40.675  -11.973 32.804 1.00 57.22  ? 92  ASP D OD2 1 
ATOM   4039  N  N   . GLY D  1 94  ? 35.840  -12.274 33.452 1.00 41.53  ? 93  GLY D N   1 
ATOM   4040  C  CA  . GLY D  1 94  ? 34.722  -11.473 32.978 1.00 32.74  ? 93  GLY D CA  1 
ATOM   4041  C  C   . GLY D  1 94  ? 35.121  -10.564 31.822 1.00 29.40  ? 93  GLY D C   1 
ATOM   4042  O  O   . GLY D  1 94  ? 34.453  -9.566  31.559 1.00 26.33  ? 93  GLY D O   1 
ATOM   4043  N  N   . VAL D  1 95  ? 36.199  -10.933 31.124 1.00 29.50  ? 94  VAL D N   1 
ATOM   4044  C  CA  . VAL D  1 95  ? 36.644  -10.160 29.977 1.00 29.52  ? 94  VAL D CA  1 
ATOM   4045  C  C   . VAL D  1 95  ? 36.413  -10.959 28.699 1.00 28.51  ? 94  VAL D C   1 
ATOM   4046  O  O   . VAL D  1 95  ? 36.838  -12.099 28.588 1.00 30.35  ? 94  VAL D O   1 
ATOM   4047  C  CB  . VAL D  1 95  ? 38.116  -9.731  30.119 1.00 29.88  ? 94  VAL D CB  1 
ATOM   4048  C  CG1 . VAL D  1 95  ? 38.630  -9.027  28.865 1.00 28.83  ? 94  VAL D CG1 1 
ATOM   4049  C  CG2 . VAL D  1 95  ? 38.319  -8.880  31.366 1.00 28.69  ? 94  VAL D CG2 1 
ATOM   4050  N  N   . ALA D  1 96  ? 35.756  -10.332 27.724 1.00 28.94  ? 95  ALA D N   1 
ATOM   4051  C  CA  . ALA D  1 96  ? 35.608  -10.926 26.412 1.00 29.31  ? 95  ALA D CA  1 
ATOM   4052  C  C   . ALA D  1 96  ? 36.535  -10.222 25.433 1.00 29.76  ? 95  ALA D C   1 
ATOM   4053  O  O   . ALA D  1 96  ? 36.364  -9.041  25.185 1.00 27.64  ? 95  ALA D O   1 
ATOM   4054  C  CB  . ALA D  1 96  ? 34.173  -10.828 25.964 1.00 29.34  ? 95  ALA D CB  1 
ATOM   4055  N  N   . ASP D  1 97  ? 37.504  -10.957 24.877 1.00 31.64  ? 96  ASP D N   1 
ATOM   4056  C  CA  . ASP D  1 97  ? 38.336  -10.398 23.827 1.00 33.98  ? 96  ASP D CA  1 
ATOM   4057  C  C   . ASP D  1 97  ? 37.658  -10.682 22.499 1.00 32.56  ? 96  ASP D C   1 
ATOM   4058  O  O   . ASP D  1 97  ? 37.805  -11.756 21.940 1.00 37.83  ? 96  ASP D O   1 
ATOM   4059  C  CB  . ASP D  1 97  ? 39.796  -10.855 23.878 1.00 37.60  ? 96  ASP D CB  1 
ATOM   4060  C  CG  . ASP D  1 97  ? 40.521  -10.357 25.117 1.00 41.22  ? 96  ASP D CG  1 
ATOM   4061  O  OD1 . ASP D  1 97  ? 40.467  -9.117  25.377 1.00 43.21  ? 96  ASP D OD1 1 
ATOM   4062  O  OD2 . ASP D  1 97  ? 41.086  -11.215 25.845 1.00 43.41  ? 96  ASP D OD2 1 
ATOM   4063  N  N   . VAL D  1 98  ? 36.892  -9.705  22.022 1.00 29.86  ? 97  VAL D N   1 
ATOM   4064  C  CA  . VAL D  1 98  ? 36.084  -9.889  20.835 1.00 29.16  ? 97  VAL D CA  1 
ATOM   4065  C  C   . VAL D  1 98  ? 36.967  -9.848  19.597 1.00 28.67  ? 97  VAL D C   1 
ATOM   4066  O  O   . VAL D  1 98  ? 37.827  -8.979  19.461 1.00 29.41  ? 97  VAL D O   1 
ATOM   4067  C  CB  . VAL D  1 98  ? 34.978  -8.828  20.758 1.00 29.25  ? 97  VAL D CB  1 
ATOM   4068  C  CG1 . VAL D  1 98  ? 34.103  -9.041  19.527 1.00 26.99  ? 97  VAL D CG1 1 
ATOM   4069  C  CG2 . VAL D  1 98  ? 34.153  -8.810  22.043 1.00 29.47  ? 97  VAL D CG2 1 
ATOM   4070  N  N   . SER D  1 99  ? 36.713  -10.793 18.688 1.00 27.92  ? 98  SER D N   1 
ATOM   4071  C  CA  . SER D  1 99  ? 37.354  -10.781 17.388 1.00 27.85  ? 98  SER D CA  1 
ATOM   4072  C  C   . SER D  1 99  ? 36.509  -11.586 16.411 1.00 28.19  ? 98  SER D C   1 
ATOM   4073  O  O   . SER D  1 99  ? 36.417  -12.800 16.540 1.00 30.98  ? 98  SER D O   1 
ATOM   4074  C  CB  . SER D  1 99  ? 38.754  -11.300 17.468 1.00 26.77  ? 98  SER D CB  1 
ATOM   4075  O  OG  . SER D  1 99  ? 39.323  -11.274 16.179 1.00 26.67  ? 98  SER D OG  1 
ATOM   4076  N  N   . ILE D  1 100 ? 35.878  -10.890 15.462 1.00 26.29  ? 99  ILE D N   1 
ATOM   4077  C  CA  . ILE D  1 100 ? 34.908  -11.498 14.567 1.00 26.90  ? 99  ILE D CA  1 
ATOM   4078  C  C   . ILE D  1 100 ? 35.165  -10.957 13.172 1.00 27.74  ? 99  ILE D C   1 
ATOM   4079  O  O   . ILE D  1 100 ? 35.621  -9.826  13.018 1.00 28.30  ? 99  ILE D O   1 
ATOM   4080  C  CB  . ILE D  1 100 ? 33.472  -11.167 15.026 1.00 25.48  ? 99  ILE D CB  1 
ATOM   4081  C  CG1 . ILE D  1 100 ? 33.058  -12.029 16.219 1.00 24.56  ? 99  ILE D CG1 1 
ATOM   4082  C  CG2 . ILE D  1 100 ? 32.460  -11.283 13.895 1.00 22.87  ? 99  ILE D CG2 1 
ATOM   4083  C  CD1 . ILE D  1 100 ? 31.815  -11.492 16.912 1.00 26.52  ? 99  ILE D CD1 1 
ATOM   4084  N  N   . GLU D  1 101 ? 34.844  -11.768 12.171 1.00 30.06  ? 100 GLU D N   1 
ATOM   4085  C  CA  . GLU D  1 101 ? 34.863  -11.254 10.816 1.00 33.56  ? 100 GLU D CA  1 
ATOM   4086  C  C   . GLU D  1 101 ? 33.521  -11.602 10.191 1.00 34.89  ? 100 GLU D C   1 
ATOM   4087  O  O   . GLU D  1 101 ? 33.072  -12.739 10.279 1.00 38.87  ? 100 GLU D O   1 
ATOM   4088  C  CB  . GLU D  1 101 ? 36.077  -11.812 10.080 1.00 36.68  ? 100 GLU D CB  1 
ATOM   4089  C  CG  . GLU D  1 101 ? 36.074  -11.524 8.608  1.00 44.29  ? 100 GLU D CG  1 
ATOM   4090  C  CD  . GLU D  1 101 ? 37.399  -11.799 7.927  1.00 48.73  ? 100 GLU D CD  1 
ATOM   4091  O  OE1 . GLU D  1 101 ? 38.477  -11.684 8.608  1.00 48.24  ? 100 GLU D OE1 1 
ATOM   4092  O  OE2 . GLU D  1 101 ? 37.345  -12.095 6.694  1.00 53.00  ? 100 GLU D OE2 1 
ATOM   4093  N  N   . ASP D  1 102 ? 32.850  -10.613 9.609  1.00 34.35  ? 101 ASP D N   1 
ATOM   4094  C  CA  . ASP D  1 102 ? 31.499  -10.846 9.130  1.00 34.82  ? 101 ASP D CA  1 
ATOM   4095  C  C   . ASP D  1 102 ? 31.356  -10.208 7.755  1.00 34.17  ? 101 ASP D C   1 
ATOM   4096  O  O   . ASP D  1 102 ? 31.905  -9.138  7.513  1.00 33.78  ? 101 ASP D O   1 
ATOM   4097  C  CB  . ASP D  1 102 ? 30.455  -10.301 10.101 1.00 33.65  ? 101 ASP D CB  1 
ATOM   4098  C  CG  . ASP D  1 102 ? 29.064  -10.808 9.761  1.00 34.29  ? 101 ASP D CG  1 
ATOM   4099  O  OD1 . ASP D  1 102 ? 28.843  -12.015 9.982  1.00 34.08  ? 101 ASP D OD1 1 
ATOM   4100  O  OD2 . ASP D  1 102 ? 28.229  -10.015 9.244  1.00 33.12  ? 101 ASP D OD2 1 
ATOM   4101  N  N   . SER D  1 103 ? 30.608  -10.884 6.876  1.00 34.82  ? 102 SER D N   1 
ATOM   4102  C  CA  . SER D  1 103 ? 30.472  -10.407 5.511  1.00 37.51  ? 102 SER D CA  1 
ATOM   4103  C  C   . SER D  1 103 ? 29.054  -9.941  5.208  1.00 38.06  ? 102 SER D C   1 
ATOM   4104  O  O   . SER D  1 103 ? 28.747  -9.598  4.071  1.00 38.65  ? 102 SER D O   1 
ATOM   4105  C  CB  . SER D  1 103 ? 30.935  -11.432 4.538  1.00 40.61  ? 102 SER D CB  1 
ATOM   4106  O  OG  . SER D  1 103 ? 32.329  -11.270 4.335  1.00 47.58  ? 102 SER D OG  1 
ATOM   4107  N  N   . VAL D  1 104 ? 28.205  -9.910  6.236  1.00 39.90  ? 103 VAL D N   1 
ATOM   4108  C  CA  . VAL D  1 104 ? 26.814  -9.544  6.033  1.00 39.10  ? 103 VAL D CA  1 
ATOM   4109  C  C   . VAL D  1 104 ? 26.617  -8.100  6.479  1.00 37.80  ? 103 VAL D C   1 
ATOM   4110  O  O   . VAL D  1 104 ? 25.984  -7.328  5.768  1.00 38.74  ? 103 VAL D O   1 
ATOM   4111  C  CB  . VAL D  1 104 ? 25.850  -10.525 6.729  1.00 38.52  ? 103 VAL D CB  1 
ATOM   4112  C  CG1 . VAL D  1 104 ? 24.413  -10.049 6.681  1.00 37.43  ? 103 VAL D CG1 1 
ATOM   4113  C  CG2 . VAL D  1 104 ? 25.953  -11.918 6.138  1.00 34.34  ? 103 VAL D CG2 1 
ATOM   4114  N  N   . ILE D  1 105 ? 27.156  -7.750  7.652  1.00 35.74  ? 104 ILE D N   1 
ATOM   4115  C  CA  . ILE D  1 105 ? 27.178  -6.351  8.044  1.00 32.46  ? 104 ILE D CA  1 
ATOM   4116  C  C   . ILE D  1 105 ? 28.092  -5.607  7.080  1.00 34.14  ? 104 ILE D C   1 
ATOM   4117  O  O   . ILE D  1 105 ? 28.939  -6.215  6.427  1.00 35.06  ? 104 ILE D O   1 
ATOM   4118  C  CB  . ILE D  1 105 ? 27.621  -6.164  9.507  1.00 28.10  ? 104 ILE D CB  1 
ATOM   4119  C  CG1 . ILE D  1 105 ? 29.063  -6.618  9.731  1.00 25.56  ? 104 ILE D CG1 1 
ATOM   4120  C  CG2 . ILE D  1 105 ? 26.647  -6.841  10.445 1.00 27.16  ? 104 ILE D CG2 1 
ATOM   4121  C  CD1 . ILE D  1 105 ? 29.634  -6.159  11.047 1.00 23.24  ? 104 ILE D CD1 1 
ATOM   4122  N  N   . SER D  1 106 ? 27.887  -4.287  6.984  1.00 34.81  ? 105 SER D N   1 
ATOM   4123  C  CA  . SER D  1 106 ? 28.738  -3.451  6.158  1.00 35.08  ? 105 SER D CA  1 
ATOM   4124  C  C   . SER D  1 106 ? 28.929  -2.084  6.804  1.00 36.29  ? 105 SER D C   1 
ATOM   4125  O  O   . SER D  1 106 ? 28.125  -1.678  7.639  1.00 36.69  ? 105 SER D O   1 
ATOM   4126  C  CB  . SER D  1 106 ? 28.172  -3.329  4.782  1.00 35.97  ? 105 SER D CB  1 
ATOM   4127  O  OG  . SER D  1 106 ? 29.148  -2.791  3.917  1.00 38.71  ? 105 SER D OG  1 
ATOM   4128  N  N   . LEU D  1 107 ? 29.983  -1.374  6.396  1.00 35.99  ? 106 LEU D N   1 
ATOM   4129  C  CA  . LEU D  1 107 ? 30.160  0.013   6.795  1.00 38.95  ? 106 LEU D CA  1 
ATOM   4130  C  C   . LEU D  1 107 ? 29.856  0.951   5.623  1.00 43.41  ? 106 LEU D C   1 
ATOM   4131  O  O   . LEU D  1 107 ? 30.161  2.139   5.689  1.00 49.12  ? 106 LEU D O   1 
ATOM   4132  C  CB  . LEU D  1 107 ? 31.580  0.219   7.333  1.00 34.64  ? 106 LEU D CB  1 
ATOM   4133  C  CG  . LEU D  1 107 ? 31.979  -0.689  8.494  1.00 33.59  ? 106 LEU D CG  1 
ATOM   4134  C  CD1 . LEU D  1 107 ? 33.337  -0.329  9.056  1.00 33.95  ? 106 LEU D CD1 1 
ATOM   4135  C  CD2 . LEU D  1 107 ? 30.964  -0.646  9.611  1.00 32.73  ? 106 LEU D CD2 1 
ATOM   4136  N  N   . SER D  1 108 ? 29.259  0.419   4.547  1.00 45.61  ? 107 SER D N   1 
ATOM   4137  C  CA  . SER D  1 108 ? 28.716  1.228   3.465  1.00 50.00  ? 107 SER D CA  1 
ATOM   4138  C  C   . SER D  1 108 ? 27.643  0.440   2.711  1.00 52.43  ? 107 SER D C   1 
ATOM   4139  O  O   . SER D  1 108 ? 27.572  -0.778  2.800  1.00 53.37  ? 107 SER D O   1 
ATOM   4140  C  CB  . SER D  1 108 ? 29.806  1.718   2.549  1.00 53.06  ? 107 SER D CB  1 
ATOM   4141  O  OG  . SER D  1 108 ? 30.452  0.628   1.922  1.00 63.11  ? 107 SER D OG  1 
ATOM   4142  N  N   . GLY D  1 109 ? 26.772  1.155   1.988  1.00 56.60  ? 108 GLY D N   1 
ATOM   4143  C  CA  . GLY D  1 109 ? 25.747  0.534   1.167  1.00 58.45  ? 108 GLY D CA  1 
ATOM   4144  C  C   . GLY D  1 109 ? 24.511  0.190   1.988  1.00 64.50  ? 108 GLY D C   1 
ATOM   4145  O  O   . GLY D  1 109 ? 24.292  0.751   3.055  1.00 70.44  ? 108 GLY D O   1 
ATOM   4146  N  N   . ASP D  1 110 ? 23.765  -0.812  1.522  1.00 74.31  ? 109 ASP D N   1 
ATOM   4147  C  CA  . ASP D  1 110 ? 22.446  -1.122  2.046  1.00 81.44  ? 109 ASP D CA  1 
ATOM   4148  C  C   . ASP D  1 110 ? 22.505  -1.621  3.487  1.00 78.78  ? 109 ASP D C   1 
ATOM   4149  O  O   . ASP D  1 110 ? 21.527  -1.510  4.209  1.00 64.56  ? 109 ASP D O   1 
ATOM   4150  C  CB  . ASP D  1 110 ? 21.729  -2.133  1.149  1.00 97.86  ? 109 ASP D CB  1 
ATOM   4151  C  CG  . ASP D  1 110 ? 21.532  -1.639  -0.272 1.00 109.70 ? 109 ASP D CG  1 
ATOM   4152  O  OD1 . ASP D  1 110 ? 21.096  -0.478  -0.434 1.00 112.35 ? 109 ASP D OD1 1 
ATOM   4153  O  OD2 . ASP D  1 110 ? 21.871  -2.398  -1.198 1.00 116.99 ? 109 ASP D OD2 1 
ATOM   4154  N  N   . HIS D  1 111 ? 23.623  -2.208  3.905  1.00 86.66  ? 110 HIS D N   1 
ATOM   4155  C  CA  . HIS D  1 111 ? 23.612  -2.829  5.218  1.00 79.55  ? 110 HIS D CA  1 
ATOM   4156  C  C   . HIS D  1 111 ? 24.482  -2.036  6.188  1.00 71.14  ? 110 HIS D C   1 
ATOM   4157  O  O   . HIS D  1 111 ? 25.043  -2.611  7.109  1.00 77.45  ? 110 HIS D O   1 
ATOM   4158  C  CB  . HIS D  1 111 ? 23.938  -4.331  5.133  1.00 84.26  ? 110 HIS D CB  1 
ATOM   4159  C  CG  . HIS D  1 111 ? 23.058  -5.103  4.202  1.00 91.77  ? 110 HIS D CG  1 
ATOM   4160  N  ND1 . HIS D  1 111 ? 23.498  -6.254  3.561  1.00 87.26  ? 110 HIS D ND1 1 
ATOM   4161  C  CD2 . HIS D  1 111 ? 21.779  -4.927  3.804  1.00 97.88  ? 110 HIS D CD2 1 
ATOM   4162  C  CE1 . HIS D  1 111 ? 22.535  -6.735  2.799  1.00 84.21  ? 110 HIS D CE1 1 
ATOM   4163  N  NE2 . HIS D  1 111 ? 21.493  -5.900  2.890  1.00 94.27  ? 110 HIS D NE2 1 
ATOM   4164  N  N   . CYS D  1 112 ? 24.569  -0.720  5.973  1.00 56.27  ? 111 CYS D N   1 
ATOM   4165  C  CA  . CYS D  1 112 ? 25.408  0.120   6.807  1.00 52.45  ? 111 CYS D CA  1 
ATOM   4166  C  C   . CYS D  1 112 ? 24.891  0.067   8.248  1.00 45.85  ? 111 CYS D C   1 
ATOM   4167  O  O   . CYS D  1 112 ? 23.692  0.157   8.479  1.00 43.08  ? 111 CYS D O   1 
ATOM   4168  C  CB  . CYS D  1 112 ? 25.397  1.534   6.254  1.00 57.23  ? 111 CYS D CB  1 
ATOM   4169  S  SG  . CYS D  1 112 ? 26.885  2.501   6.599  1.00 73.25  ? 111 CYS D SG  1 
ATOM   4170  N  N   . ILE D  1 113 ? 25.802  -0.180  9.195  1.00 39.13  ? 112 ILE D N   1 
ATOM   4171  C  CA  . ILE D  1 113 ? 25.451  -0.299  10.603 1.00 36.27  ? 112 ILE D CA  1 
ATOM   4172  C  C   . ILE D  1 113 ? 25.821  0.985   11.345 1.00 35.98  ? 112 ILE D C   1 
ATOM   4173  O  O   . ILE D  1 113 ? 25.631  1.079   12.564 1.00 36.00  ? 112 ILE D O   1 
ATOM   4174  C  CB  . ILE D  1 113 ? 26.111  -1.530  11.269 1.00 34.73  ? 112 ILE D CB  1 
ATOM   4175  C  CG1 . ILE D  1 113 ? 27.630  -1.543  11.083 1.00 33.38  ? 112 ILE D CG1 1 
ATOM   4176  C  CG2 . ILE D  1 113 ? 25.480  -2.828  10.793 1.00 33.23  ? 112 ILE D CG2 1 
ATOM   4177  C  CD1 . ILE D  1 113 ? 28.366  -2.327  12.127 1.00 30.42  ? 112 ILE D CD1 1 
ATOM   4178  N  N   . ILE D  1 114 ? 26.362  1.967   10.612 1.00 34.78  ? 113 ILE D N   1 
ATOM   4179  C  CA  . ILE D  1 114 ? 26.723  3.244   11.208 1.00 31.69  ? 113 ILE D CA  1 
ATOM   4180  C  C   . ILE D  1 114 ? 25.448  3.907   11.711 1.00 30.26  ? 113 ILE D C   1 
ATOM   4181  O  O   . ILE D  1 114 ? 24.435  3.930   11.014 1.00 28.17  ? 113 ILE D O   1 
ATOM   4182  C  CB  . ILE D  1 114 ? 27.457  4.144   10.206 1.00 31.61  ? 113 ILE D CB  1 
ATOM   4183  C  CG1 . ILE D  1 114 ? 28.654  3.406   9.607  1.00 35.00  ? 113 ILE D CG1 1 
ATOM   4184  C  CG2 . ILE D  1 114 ? 27.848  5.454   10.860 1.00 28.71  ? 113 ILE D CG2 1 
ATOM   4185  C  CD1 . ILE D  1 114 ? 29.729  4.292   9.060  1.00 37.93  ? 113 ILE D CD1 1 
ATOM   4186  N  N   . GLY D  1 115 ? 25.524  4.405   12.947 1.00 29.05  ? 114 GLY D N   1 
ATOM   4187  C  CA  . GLY D  1 115 ? 24.430  5.132   13.564 1.00 27.98  ? 114 GLY D CA  1 
ATOM   4188  C  C   . GLY D  1 115 ? 23.365  4.198   14.124 1.00 29.31  ? 114 GLY D C   1 
ATOM   4189  O  O   . GLY D  1 115 ? 22.270  4.656   14.451 1.00 29.34  ? 114 GLY D O   1 
ATOM   4190  N  N   . ARG D  1 116 ? 23.698  2.898   14.227 1.00 28.56  ? 115 ARG D N   1 
ATOM   4191  C  CA  . ARG D  1 116 ? 22.838  1.921   14.880 1.00 26.11  ? 115 ARG D CA  1 
ATOM   4192  C  C   . ARG D  1 116 ? 23.468  1.528   16.216 1.00 26.45  ? 115 ARG D C   1 
ATOM   4193  O  O   . ARG D  1 116 ? 24.435  2.157   16.648 1.00 26.79  ? 115 ARG D O   1 
ATOM   4194  C  CB  . ARG D  1 116 ? 22.534  0.784   13.911 1.00 24.86  ? 115 ARG D CB  1 
ATOM   4195  C  CG  . ARG D  1 116 ? 22.009  1.295   12.581 1.00 26.98  ? 115 ARG D CG  1 
ATOM   4196  C  CD  . ARG D  1 116 ? 21.500  0.190   11.681 1.00 28.53  ? 115 ARG D CD  1 
ATOM   4197  N  NE  . ARG D  1 116 ? 20.983  0.703   10.414 1.00 29.23  ? 115 ARG D NE  1 
ATOM   4198  C  CZ  . ARG D  1 116 ? 19.733  1.096   10.195 1.00 28.70  ? 115 ARG D CZ  1 
ATOM   4199  N  NH1 . ARG D  1 116 ? 18.830  1.039   11.157 1.00 27.82  ? 115 ARG D NH1 1 
ATOM   4200  N  NH2 . ARG D  1 116 ? 19.389  1.537   8.999  1.00 30.19  ? 115 ARG D NH2 1 
ATOM   4201  N  N   . THR D  1 117 ? 22.901  0.524   16.897 1.00 26.68  ? 116 THR D N   1 
ATOM   4202  C  CA  . THR D  1 117 ? 23.404  0.179   18.220 1.00 25.69  ? 116 THR D CA  1 
ATOM   4203  C  C   . THR D  1 117 ? 24.009  -1.220  18.239 1.00 24.08  ? 116 THR D C   1 
ATOM   4204  O  O   . THR D  1 117 ? 23.481  -2.156  17.641 1.00 24.09  ? 116 THR D O   1 
ATOM   4205  C  CB  . THR D  1 117 ? 22.317  0.293   19.293 1.00 26.31  ? 116 THR D CB  1 
ATOM   4206  O  OG1 . THR D  1 117 ? 21.930  1.663   19.327 1.00 29.05  ? 116 THR D OG1 1 
ATOM   4207  C  CG2 . THR D  1 117 ? 22.799  -0.110  20.667 1.00 26.19  ? 116 THR D CG2 1 
ATOM   4208  N  N   . LEU D  1 118 ? 25.125  -1.346  18.953 1.00 21.50  ? 117 LEU D N   1 
ATOM   4209  C  CA  . LEU D  1 118 ? 25.669  -2.650  19.254 1.00 20.31  ? 117 LEU D CA  1 
ATOM   4210  C  C   . LEU D  1 118 ? 25.288  -2.981  20.691 1.00 20.62  ? 117 LEU D C   1 
ATOM   4211  O  O   . LEU D  1 118 ? 25.412  -2.129  21.566 1.00 20.57  ? 117 LEU D O   1 
ATOM   4212  C  CB  . LEU D  1 118 ? 27.188  -2.567  19.081 1.00 19.32  ? 117 LEU D CB  1 
ATOM   4213  C  CG  . LEU D  1 118 ? 27.950  -3.841  19.415 1.00 18.92  ? 117 LEU D CG  1 
ATOM   4214  C  CD1 . LEU D  1 118 ? 27.584  -4.926  18.416 1.00 18.30  ? 117 LEU D CD1 1 
ATOM   4215  C  CD2 . LEU D  1 118 ? 29.447  -3.558  19.391 1.00 19.43  ? 117 LEU D CD2 1 
ATOM   4216  N  N   . VAL D  1 119 ? 24.797  -4.208  20.910 1.00 21.35  ? 118 VAL D N   1 
ATOM   4217  C  CA  . VAL D  1 119 ? 24.337  -4.621  22.228 1.00 22.57  ? 118 VAL D CA  1 
ATOM   4218  C  C   . VAL D  1 119 ? 24.998  -5.942  22.613 1.00 24.15  ? 118 VAL D C   1 
ATOM   4219  O  O   . VAL D  1 119 ? 25.046  -6.884  21.817 1.00 25.16  ? 118 VAL D O   1 
ATOM   4220  C  CB  . VAL D  1 119 ? 22.805  -4.783  22.291 1.00 22.66  ? 118 VAL D CB  1 
ATOM   4221  C  CG1 . VAL D  1 119 ? 22.335  -5.197  23.689 1.00 21.10  ? 118 VAL D CG1 1 
ATOM   4222  C  CG2 . VAL D  1 119 ? 22.058  -3.551  21.809 1.00 22.31  ? 118 VAL D CG2 1 
ATOM   4223  N  N   . VAL D  1 120 ? 25.462  -6.008  23.861 1.00 23.51  ? 119 VAL D N   1 
ATOM   4224  C  CA  . VAL D  1 120 ? 25.905  -7.268  24.419 1.00 24.01  ? 119 VAL D CA  1 
ATOM   4225  C  C   . VAL D  1 120 ? 24.872  -7.713  25.452 1.00 24.91  ? 119 VAL D C   1 
ATOM   4226  O  O   . VAL D  1 120 ? 24.507  -6.946  26.343 1.00 23.29  ? 119 VAL D O   1 
ATOM   4227  C  CB  . VAL D  1 120 ? 27.331  -7.161  24.992 1.00 24.60  ? 119 VAL D CB  1 
ATOM   4228  C  CG1 . VAL D  1 120 ? 27.453  -6.108  26.085 1.00 25.26  ? 119 VAL D CG1 1 
ATOM   4229  C  CG2 . VAL D  1 120 ? 27.849  -8.501  25.478 1.00 23.02  ? 119 VAL D CG2 1 
ATOM   4230  N  N   . HIS D  1 121 ? 24.418  -8.965  25.309 1.00 26.45  ? 120 HIS D N   1 
ATOM   4231  C  CA  . HIS D  1 121 ? 23.269  -9.488  26.034 1.00 27.11  ? 120 HIS D CA  1 
ATOM   4232  C  C   . HIS D  1 121 ? 23.677  -10.327 27.243 1.00 29.84  ? 120 HIS D C   1 
ATOM   4233  O  O   . HIS D  1 121 ? 24.846  -10.674 27.425 1.00 32.30  ? 120 HIS D O   1 
ATOM   4234  C  CB  . HIS D  1 121 ? 22.381  -10.302 25.100 1.00 25.33  ? 120 HIS D CB  1 
ATOM   4235  C  CG  . HIS D  1 121 ? 21.616  -9.471  24.130 1.00 24.81  ? 120 HIS D CG  1 
ATOM   4236  N  ND1 . HIS D  1 121 ? 20.341  -9.018  24.398 1.00 23.32  ? 120 HIS D ND1 1 
ATOM   4237  C  CD2 . HIS D  1 121 ? 21.928  -9.023  22.893 1.00 24.27  ? 120 HIS D CD2 1 
ATOM   4238  C  CE1 . HIS D  1 121 ? 19.904  -8.324  23.359 1.00 22.96  ? 120 HIS D CE1 1 
ATOM   4239  N  NE2 . HIS D  1 121 ? 20.856  -8.315  22.423 1.00 23.16  ? 120 HIS D NE2 1 
ATOM   4240  N  N   . GLU D  1 122 ? 22.661  -10.690 28.036 1.00 29.93  ? 121 GLU D N   1 
ATOM   4241  C  CA  . GLU D  1 122 ? 22.818  -11.266 29.358 1.00 29.15  ? 121 GLU D CA  1 
ATOM   4242  C  C   . GLU D  1 122 ? 23.283  -12.714 29.282 1.00 31.30  ? 121 GLU D C   1 
ATOM   4243  O  O   . GLU D  1 122 ? 24.145  -13.113 30.064 1.00 33.95  ? 121 GLU D O   1 
ATOM   4244  C  CB  . GLU D  1 122 ? 21.482  -11.115 30.069 1.00 30.13  ? 121 GLU D CB  1 
ATOM   4245  C  CG  . GLU D  1 122 ? 21.265  -12.057 31.231 1.00 32.06  ? 121 GLU D CG  1 
ATOM   4246  C  CD  . GLU D  1 122 ? 19.792  -12.107 31.604 1.00 36.67  ? 121 GLU D CD  1 
ATOM   4247  O  OE1 . GLU D  1 122 ? 19.504  -12.178 32.816 1.00 41.09  ? 121 GLU D OE1 1 
ATOM   4248  O  OE2 . GLU D  1 122 ? 18.925  -12.008 30.682 1.00 37.07  ? 121 GLU D OE2 1 
ATOM   4249  N  N   . LYS D  1 123 ? 22.715  -13.481 28.331 1.00 32.11  ? 122 LYS D N   1 
ATOM   4250  C  CA  . LYS D  1 123 ? 22.902  -14.919 28.206 1.00 30.81  ? 122 LYS D CA  1 
ATOM   4251  C  C   . LYS D  1 123 ? 23.393  -15.265 26.798 1.00 29.65  ? 122 LYS D C   1 
ATOM   4252  O  O   . LYS D  1 123 ? 23.527  -14.395 25.932 1.00 28.40  ? 122 LYS D O   1 
ATOM   4253  C  CB  . LYS D  1 123 ? 21.560  -15.626 28.398 1.00 34.05  ? 122 LYS D CB  1 
ATOM   4254  C  CG  . LYS D  1 123 ? 20.944  -15.510 29.793 1.00 37.53  ? 122 LYS D CG  1 
ATOM   4255  C  CD  . LYS D  1 123 ? 19.608  -16.167 30.041 1.00 40.17  ? 122 LYS D CD  1 
ATOM   4256  C  CE  . LYS D  1 123 ? 18.442  -15.633 29.227 1.00 43.69  ? 122 LYS D CE  1 
ATOM   4257  N  NZ  . LYS D  1 123 ? 17.194  -16.372 29.528 1.00 43.69  ? 122 LYS D NZ  1 
ATOM   4258  N  N   . ALA D  1 124 ? 23.599  -16.566 26.561 1.00 29.12  ? 123 ALA D N   1 
ATOM   4259  C  CA  . ALA D  1 124 ? 24.013  -17.067 25.260 1.00 27.64  ? 123 ALA D CA  1 
ATOM   4260  C  C   . ALA D  1 124 ? 22.903  -16.824 24.239 1.00 27.71  ? 123 ALA D C   1 
ATOM   4261  O  O   . ALA D  1 124 ? 21.708  -16.885 24.557 1.00 28.99  ? 123 ALA D O   1 
ATOM   4262  C  CB  . ALA D  1 124 ? 24.318  -18.535 25.360 1.00 26.74  ? 123 ALA D CB  1 
ATOM   4263  N  N   . ASP D  1 125 ? 23.320  -16.549 23.001 1.00 25.10  ? 124 ASP D N   1 
ATOM   4264  C  CA  . ASP D  1 125 ? 22.422  -16.542 21.864 1.00 23.05  ? 124 ASP D CA  1 
ATOM   4265  C  C   . ASP D  1 125 ? 22.335  -17.979 21.360 1.00 23.64  ? 124 ASP D C   1 
ATOM   4266  O  O   . ASP D  1 125 ? 23.357  -18.585 21.031 1.00 22.94  ? 124 ASP D O   1 
ATOM   4267  C  CB  . ASP D  1 125 ? 22.955  -15.572 20.811 1.00 23.18  ? 124 ASP D CB  1 
ATOM   4268  C  CG  . ASP D  1 125 ? 22.215  -15.579 19.482 1.00 23.86  ? 124 ASP D CG  1 
ATOM   4269  O  OD1 . ASP D  1 125 ? 21.309  -16.414 19.301 1.00 22.53  ? 124 ASP D OD1 1 
ATOM   4270  O  OD2 . ASP D  1 125 ? 22.566  -14.754 18.623 1.00 26.92  ? 124 ASP D OD2 1 
ATOM   4271  N  N   . ASP D  1 126 ? 21.114  -18.530 21.291 1.00 23.41  ? 125 ASP D N   1 
ATOM   4272  C  CA  . ASP D  1 126 ? 20.950  -19.930 20.921 1.00 23.60  ? 125 ASP D CA  1 
ATOM   4273  C  C   . ASP D  1 126 ? 21.010  -20.108 19.402 1.00 24.29  ? 125 ASP D C   1 
ATOM   4274  O  O   . ASP D  1 126 ? 20.800  -21.197 18.918 1.00 26.32  ? 125 ASP D O   1 
ATOM   4275  C  CB  . ASP D  1 126 ? 19.739  -20.573 21.606 1.00 24.17  ? 125 ASP D CB  1 
ATOM   4276  C  CG  . ASP D  1 126 ? 18.379  -20.124 21.081 1.00 25.77  ? 125 ASP D CG  1 
ATOM   4277  O  OD1 . ASP D  1 126 ? 18.306  -19.654 19.907 1.00 25.47  ? 125 ASP D OD1 1 
ATOM   4278  O  OD2 . ASP D  1 126 ? 17.381  -20.269 21.848 1.00 24.02  ? 125 ASP D OD2 1 
ATOM   4279  N  N   . LEU D  1 127 ? 21.315  -19.035 18.670 1.00 24.32  ? 126 LEU D N   1 
ATOM   4280  C  CA  . LEU D  1 127 ? 21.534  -19.072 17.231 1.00 24.54  ? 126 LEU D CA  1 
ATOM   4281  C  C   . LEU D  1 127 ? 20.302  -19.612 16.499 1.00 26.22  ? 126 LEU D C   1 
ATOM   4282  O  O   . LEU D  1 127 ? 20.411  -20.092 15.371 1.00 26.53  ? 126 LEU D O   1 
ATOM   4283  C  CB  . LEU D  1 127 ? 22.781  -19.898 16.889 1.00 23.38  ? 126 LEU D CB  1 
ATOM   4284  C  CG  . LEU D  1 127 ? 24.045  -19.592 17.702 1.00 22.30  ? 126 LEU D CG  1 
ATOM   4285  C  CD1 . LEU D  1 127 ? 25.237  -20.410 17.231 1.00 20.30  ? 126 LEU D CD1 1 
ATOM   4286  C  CD2 . LEU D  1 127 ? 24.374  -18.111 17.664 1.00 21.63  ? 126 LEU D CD2 1 
ATOM   4287  N  N   . GLY D  1 128 ? 19.133  -19.508 17.149 1.00 27.56  ? 127 GLY D N   1 
ATOM   4288  C  CA  . GLY D  1 128 ? 17.852  -19.789 16.518 1.00 30.28  ? 127 GLY D CA  1 
ATOM   4289  C  C   . GLY D  1 128 ? 17.477  -21.275 16.583 1.00 30.85  ? 127 GLY D C   1 
ATOM   4290  O  O   . GLY D  1 128 ? 16.596  -21.721 15.859 1.00 31.87  ? 127 GLY D O   1 
ATOM   4291  N  N   . LYS D  1 129 ? 18.133  -22.024 17.469 1.00 30.31  ? 128 LYS D N   1 
ATOM   4292  C  CA  . LYS D  1 129 ? 17.979  -23.463 17.548 1.00 31.38  ? 128 LYS D CA  1 
ATOM   4293  C  C   . LYS D  1 129 ? 17.371  -23.856 18.891 1.00 29.17  ? 128 LYS D C   1 
ATOM   4294  O  O   . LYS D  1 129 ? 17.636  -24.946 19.387 1.00 28.26  ? 128 LYS D O   1 
ATOM   4295  C  CB  . LYS D  1 129 ? 19.336  -24.149 17.386 1.00 34.72  ? 128 LYS D CB  1 
ATOM   4296  C  CG  . LYS D  1 129 ? 20.130  -23.734 16.149 1.00 41.62  ? 128 LYS D CG  1 
ATOM   4297  C  CD  . LYS D  1 129 ? 21.408  -24.521 16.059 1.00 42.18  ? 128 LYS D CD  1 
ATOM   4298  C  CE  . LYS D  1 129 ? 21.797  -24.755 14.613 1.00 51.60  ? 128 LYS D CE  1 
ATOM   4299  N  NZ  . LYS D  1 129 ? 23.259  -24.895 14.511 1.00 57.13  ? 128 LYS D NZ  1 
ATOM   4300  N  N   . GLY D  1 130 ? 16.521  -22.989 19.443 1.00 28.31  ? 129 GLY D N   1 
ATOM   4301  C  CA  . GLY D  1 130 ? 15.946  -23.197 20.763 1.00 28.01  ? 129 GLY D CA  1 
ATOM   4302  C  C   . GLY D  1 130 ? 14.540  -23.802 20.704 1.00 29.43  ? 129 GLY D C   1 
ATOM   4303  O  O   . GLY D  1 130 ? 13.987  -24.224 21.721 1.00 29.47  ? 129 GLY D O   1 
ATOM   4304  N  N   . GLY D  1 131 ? 13.973  -23.840 19.492 1.00 30.84  ? 130 GLY D N   1 
ATOM   4305  C  CA  . GLY D  1 131 ? 12.705  -24.502 19.210 1.00 29.77  ? 130 GLY D CA  1 
ATOM   4306  C  C   . GLY D  1 131 ? 11.498  -23.795 19.827 1.00 29.73  ? 130 GLY D C   1 
ATOM   4307  O  O   . GLY D  1 131 ? 10.460  -24.410 20.049 1.00 24.23  ? 130 GLY D O   1 
ATOM   4308  N  N   . ASN D  1 132 ? 11.640  -22.493 20.108 1.00 33.81  ? 131 ASN D N   1 
ATOM   4309  C  CA  . ASN D  1 132 ? 10.511  -21.679 20.513 1.00 34.58  ? 131 ASN D CA  1 
ATOM   4310  C  C   . ASN D  1 132 ? 10.480  -20.427 19.642 1.00 37.30  ? 131 ASN D C   1 
ATOM   4311  O  O   . ASN D  1 132 ? 11.375  -20.191 18.827 1.00 35.80  ? 131 ASN D O   1 
ATOM   4312  C  CB  . ASN D  1 132 ? 10.475  -21.416 22.019 1.00 34.16  ? 131 ASN D CB  1 
ATOM   4313  C  CG  . ASN D  1 132 ? 11.693  -20.696 22.564 1.00 36.84  ? 131 ASN D CG  1 
ATOM   4314  O  OD1 . ASN D  1 132 ? 12.438  -20.054 21.830 1.00 41.24  ? 131 ASN D OD1 1 
ATOM   4315  N  ND2 . ASN D  1 132 ? 11.931  -20.829 23.865 1.00 34.65  ? 131 ASN D ND2 1 
ATOM   4316  N  N   . GLU D  1 133 ? 9.425   -19.630 19.823 1.00 41.82  ? 132 GLU D N   1 
ATOM   4317  C  CA  . GLU D  1 133 ? 9.205   -18.503 18.932 1.00 39.36  ? 132 GLU D CA  1 
ATOM   4318  C  C   . GLU D  1 133 ? 10.270  -17.451 19.207 1.00 34.13  ? 132 GLU D C   1 
ATOM   4319  O  O   . GLU D  1 133 ? 10.793  -16.835 18.285 1.00 28.41  ? 132 GLU D O   1 
ATOM   4320  C  CB  . GLU D  1 133 ? 7.779   -17.976 19.097 1.00 43.97  ? 132 GLU D CB  1 
ATOM   4321  C  CG  . GLU D  1 133 ? 7.414   -16.955 18.043 1.00 52.29  ? 132 GLU D CG  1 
ATOM   4322  C  CD  . GLU D  1 133 ? 5.916   -16.820 17.784 1.00 61.48  ? 132 GLU D CD  1 
ATOM   4323  O  OE1 . GLU D  1 133 ? 5.125   -16.963 18.749 1.00 62.27  ? 132 GLU D OE1 1 
ATOM   4324  O  OE2 . GLU D  1 133 ? 5.534   -16.587 16.608 1.00 71.11  ? 132 GLU D OE2 1 
ATOM   4325  N  N   . GLU D  1 134 ? 10.603  -17.314 20.495 1.00 34.41  ? 133 GLU D N   1 
ATOM   4326  C  CA  . GLU D  1 134 ? 11.608  -16.389 20.980 1.00 36.12  ? 133 GLU D CA  1 
ATOM   4327  C  C   . GLU D  1 134 ? 12.941  -16.644 20.277 1.00 33.70  ? 133 GLU D C   1 
ATOM   4328  O  O   . GLU D  1 134 ? 13.639  -15.707 19.891 1.00 31.48  ? 133 GLU D O   1 
ATOM   4329  C  CB  . GLU D  1 134 ? 11.695  -16.539 22.501 1.00 40.15  ? 133 GLU D CB  1 
ATOM   4330  C  CG  . GLU D  1 134 ? 12.295  -15.339 23.213 1.00 46.72  ? 133 GLU D CG  1 
ATOM   4331  C  CD  . GLU D  1 134 ? 11.863  -13.937 22.784 1.00 50.83  ? 133 GLU D CD  1 
ATOM   4332  O  OE1 . GLU D  1 134 ? 10.678  -13.743 22.388 1.00 47.34  ? 133 GLU D OE1 1 
ATOM   4333  O  OE2 . GLU D  1 134 ? 12.729  -13.039 22.839 1.00 52.76  ? 133 GLU D OE2 1 
ATOM   4334  N  N   . SER D  1 135 ? 13.296  -17.924 20.111 1.00 31.16  ? 134 SER D N   1 
ATOM   4335  C  CA  . SER D  1 135 ? 14.566  -18.307 19.518 1.00 30.46  ? 134 SER D CA  1 
ATOM   4336  C  C   . SER D  1 135 ? 14.727  -17.676 18.144 1.00 31.98  ? 134 SER D C   1 
ATOM   4337  O  O   . SER D  1 135 ? 15.808  -17.223 17.798 1.00 33.22  ? 134 SER D O   1 
ATOM   4338  C  CB  . SER D  1 135 ? 14.721  -19.809 19.468 1.00 29.19  ? 134 SER D CB  1 
ATOM   4339  O  OG  . SER D  1 135 ? 15.996  -20.178 18.971 1.00 28.77  ? 134 SER D OG  1 
ATOM   4340  N  N   . THR D  1 136 ? 13.651  -17.640 17.359 1.00 34.63  ? 135 THR D N   1 
ATOM   4341  C  CA  . THR D  1 136 ? 13.782  -17.184 15.980 1.00 36.68  ? 135 THR D CA  1 
ATOM   4342  C  C   . THR D  1 136 ? 13.660  -15.663 15.891 1.00 35.87  ? 135 THR D C   1 
ATOM   4343  O  O   . THR D  1 136 ? 13.693  -15.115 14.800 1.00 34.16  ? 135 THR D O   1 
ATOM   4344  C  CB  . THR D  1 136 ? 12.773  -17.864 15.049 1.00 37.55  ? 135 THR D CB  1 
ATOM   4345  O  OG1 . THR D  1 136 ? 11.487  -17.427 15.493 1.00 39.31  ? 135 THR D OG1 1 
ATOM   4346  C  CG2 . THR D  1 136 ? 12.865  -19.374 15.071 1.00 33.89  ? 135 THR D CG2 1 
ATOM   4347  N  N   . LYS D  1 137 ? 13.521  -14.991 17.035 1.00 38.29  ? 136 LYS D N   1 
ATOM   4348  C  CA  . LYS D  1 137 ? 13.483  -13.534 17.088 1.00 41.50  ? 136 LYS D CA  1 
ATOM   4349  C  C   . LYS D  1 137 ? 14.767  -12.984 17.713 1.00 40.97  ? 136 LYS D C   1 
ATOM   4350  O  O   . LYS D  1 137 ? 15.448  -12.147 17.114 1.00 40.92  ? 136 LYS D O   1 
ATOM   4351  C  CB  . LYS D  1 137 ? 12.258  -13.031 17.863 1.00 49.63  ? 136 LYS D CB  1 
ATOM   4352  C  CG  . LYS D  1 137 ? 10.948  -13.042 17.097 1.00 56.90  ? 136 LYS D CG  1 
ATOM   4353  C  CD  . LYS D  1 137 ? 9.877   -12.106 17.640 1.00 63.55  ? 136 LYS D CD  1 
ATOM   4354  C  CE  . LYS D  1 137 ? 8.623   -12.227 16.803 1.00 66.03  ? 136 LYS D CE  1 
ATOM   4355  N  NZ  . LYS D  1 137 ? 7.794   -10.992 16.789 1.00 71.91  ? 136 LYS D NZ  1 
ATOM   4356  N  N   . THR D  1 138 ? 15.106  -13.470 18.915 1.00 36.91  ? 137 THR D N   1 
ATOM   4357  C  CA  . THR D  1 138 ? 16.155  -12.846 19.710 1.00 33.08  ? 137 THR D CA  1 
ATOM   4358  C  C   . THR D  1 138 ? 17.240  -13.844 20.104 1.00 32.87  ? 137 THR D C   1 
ATOM   4359  O  O   . THR D  1 138 ? 18.193  -13.462 20.807 1.00 37.67  ? 137 THR D O   1 
ATOM   4360  C  CB  . THR D  1 138 ? 15.558  -12.271 21.002 1.00 30.71  ? 137 THR D CB  1 
ATOM   4361  O  OG1 . THR D  1 138 ? 15.188  -13.337 21.881 1.00 29.09  ? 137 THR D OG1 1 
ATOM   4362  C  CG2 . THR D  1 138 ? 14.384  -11.366 20.727 1.00 28.50  ? 137 THR D CG2 1 
ATOM   4363  N  N   . GLY D  1 139 ? 17.066  -15.115 19.712 1.00 27.93  ? 138 GLY D N   1 
ATOM   4364  C  CA  . GLY D  1 139 ? 17.967  -16.175 20.122 1.00 25.98  ? 138 GLY D CA  1 
ATOM   4365  C  C   . GLY D  1 139 ? 18.000  -16.389 21.635 1.00 26.55  ? 138 GLY D C   1 
ATOM   4366  O  O   . GLY D  1 139 ? 18.876  -17.090 22.133 1.00 30.16  ? 138 GLY D O   1 
ATOM   4367  N  N   . ASN D  1 140 ? 17.049  -15.794 22.370 1.00 25.33  ? 139 ASN D N   1 
ATOM   4368  C  CA  . ASN D  1 140 ? 16.867  -16.064 23.790 1.00 25.93  ? 139 ASN D CA  1 
ATOM   4369  C  C   . ASN D  1 140 ? 18.055  -15.512 24.579 1.00 25.85  ? 139 ASN D C   1 
ATOM   4370  O  O   . ASN D  1 140 ? 18.374  -16.018 25.656 1.00 27.38  ? 139 ASN D O   1 
ATOM   4371  C  CB  . ASN D  1 140 ? 16.671  -17.552 24.090 1.00 28.08  ? 139 ASN D CB  1 
ATOM   4372  C  CG  . ASN D  1 140 ? 15.291  -18.072 23.732 1.00 31.30  ? 139 ASN D CG  1 
ATOM   4373  O  OD1 . ASN D  1 140 ? 14.295  -17.721 24.346 1.00 35.97  ? 139 ASN D OD1 1 
ATOM   4374  N  ND2 . ASN D  1 140 ? 15.213  -18.941 22.738 1.00 31.72  ? 139 ASN D ND2 1 
ATOM   4375  N  N   . ALA D  1 141 ? 18.680  -14.451 24.050 1.00 26.15  ? 140 ALA D N   1 
ATOM   4376  C  CA  . ALA D  1 141 ? 19.923  -13.920 24.600 1.00 26.88  ? 140 ALA D CA  1 
ATOM   4377  C  C   . ALA D  1 141 ? 19.678  -13.142 25.896 1.00 27.46  ? 140 ALA D C   1 
ATOM   4378  O  O   . ALA D  1 141 ? 20.620  -12.730 26.578 1.00 30.28  ? 140 ALA D O   1 
ATOM   4379  C  CB  . ALA D  1 141 ? 20.619  -13.090 23.558 1.00 25.68  ? 140 ALA D CB  1 
ATOM   4380  N  N   . GLY D  1 142 ? 18.399  -12.922 26.224 1.00 26.61  ? 141 GLY D N   1 
ATOM   4381  C  CA  . GLY D  1 142 ? 18.059  -12.249 27.463 1.00 27.26  ? 141 GLY D CA  1 
ATOM   4382  C  C   . GLY D  1 142 ? 18.284  -10.745 27.347 1.00 28.93  ? 141 GLY D C   1 
ATOM   4383  O  O   . GLY D  1 142 ? 18.279  -10.201 26.239 1.00 29.32  ? 141 GLY D O   1 
ATOM   4384  N  N   . SER D  1 143 ? 18.507  -10.101 28.504 1.00 29.36  ? 142 SER D N   1 
ATOM   4385  C  CA  . SER D  1 143 ? 18.469  -8.651  28.606 1.00 28.78  ? 142 SER D CA  1 
ATOM   4386  C  C   . SER D  1 143 ? 19.705  -8.028  27.964 1.00 29.46  ? 142 SER D C   1 
ATOM   4387  O  O   . SER D  1 143 ? 20.649  -8.732  27.588 1.00 31.59  ? 142 SER D O   1 
ATOM   4388  C  CB  . SER D  1 143 ? 18.301  -8.203  30.035 1.00 26.89  ? 142 SER D CB  1 
ATOM   4389  O  OG  . SER D  1 143 ? 19.425  -8.581  30.807 1.00 26.37  ? 142 SER D OG  1 
ATOM   4390  N  N   . ARG D  1 144 ? 19.668  -6.684  27.870 1.00 27.12  ? 143 ARG D N   1 
ATOM   4391  C  CA  . ARG D  1 144 ? 20.707  -5.886  27.240 1.00 24.51  ? 143 ARG D CA  1 
ATOM   4392  C  C   . ARG D  1 144 ? 21.630  -5.346  28.329 1.00 24.75  ? 143 ARG D C   1 
ATOM   4393  O  O   . ARG D  1 144 ? 21.233  -4.489  29.102 1.00 26.77  ? 143 ARG D O   1 
ATOM   4394  C  CB  . ARG D  1 144 ? 20.038  -4.776  26.431 1.00 22.53  ? 143 ARG D CB  1 
ATOM   4395  C  CG  . ARG D  1 144 ? 19.057  -5.294  25.388 1.00 21.95  ? 143 ARG D CG  1 
ATOM   4396  C  CD  . ARG D  1 144 ? 18.205  -4.244  24.715 1.00 23.40  ? 143 ARG D CD  1 
ATOM   4397  N  NE  . ARG D  1 144 ? 17.252  -4.848  23.789 1.00 22.69  ? 143 ARG D NE  1 
ATOM   4398  C  CZ  . ARG D  1 144 ? 16.721  -4.239  22.724 1.00 24.03  ? 143 ARG D CZ  1 
ATOM   4399  N  NH1 . ARG D  1 144 ? 17.044  -2.994  22.411 1.00 27.73  ? 143 ARG D NH1 1 
ATOM   4400  N  NH2 . ARG D  1 144 ? 15.864  -4.872  21.952 1.00 24.08  ? 143 ARG D NH2 1 
ATOM   4401  N  N   . LEU D  1 145 ? 22.852  -5.873  28.414 1.00 24.61  ? 144 LEU D N   1 
ATOM   4402  C  CA  . LEU D  1 145 ? 23.718  -5.532  29.531 1.00 24.10  ? 144 LEU D CA  1 
ATOM   4403  C  C   . LEU D  1 145 ? 24.376  -4.182  29.277 1.00 24.41  ? 144 LEU D C   1 
ATOM   4404  O  O   . LEU D  1 145 ? 24.559  -3.392  30.203 1.00 26.60  ? 144 LEU D O   1 
ATOM   4405  C  CB  . LEU D  1 145 ? 24.764  -6.636  29.713 1.00 25.73  ? 144 LEU D CB  1 
ATOM   4406  C  CG  . LEU D  1 145 ? 24.228  -7.955  30.268 1.00 26.55  ? 144 LEU D CG  1 
ATOM   4407  C  CD1 . LEU D  1 145 ? 25.362  -8.942  30.494 1.00 27.23  ? 144 LEU D CD1 1 
ATOM   4408  C  CD2 . LEU D  1 145 ? 23.435  -7.727  31.554 1.00 28.11  ? 144 LEU D CD2 1 
ATOM   4409  N  N   . ALA D  1 146 ? 24.732  -3.934  28.013 1.00 23.14  ? 145 ALA D N   1 
ATOM   4410  C  CA  . ALA D  1 146 ? 25.425  -2.712  27.628 1.00 23.10  ? 145 ALA D CA  1 
ATOM   4411  C  C   . ALA D  1 146 ? 25.293  -2.514  26.123 1.00 25.62  ? 145 ALA D C   1 
ATOM   4412  O  O   . ALA D  1 146 ? 25.145  -3.475  25.360 1.00 29.40  ? 145 ALA D O   1 
ATOM   4413  C  CB  . ALA D  1 146 ? 26.882  -2.750  28.045 1.00 21.62  ? 145 ALA D CB  1 
ATOM   4414  N  N   . CYS D  1 147 ? 25.308  -1.243  25.709 1.00 25.51  ? 146 CYS D N   1 
ATOM   4415  C  CA  . CYS D  1 147 ? 25.158  -0.911  24.309 1.00 23.21  ? 146 CYS D CA  1 
ATOM   4416  C  C   . CYS D  1 147 ? 25.829  0.424   24.051 1.00 22.13  ? 146 CYS D C   1 
ATOM   4417  O  O   . CYS D  1 147 ? 26.255  1.088   24.991 1.00 23.02  ? 146 CYS D O   1 
ATOM   4418  C  CB  . CYS D  1 147 ? 23.684  -0.841  23.920 1.00 24.77  ? 146 CYS D CB  1 
ATOM   4419  S  SG  . CYS D  1 147 ? 22.728  0.357   24.877 1.00 24.48  ? 146 CYS D SG  1 
ATOM   4420  N  N   . GLY D  1 148 ? 25.933  0.773   22.764 1.00 20.92  ? 147 GLY D N   1 
ATOM   4421  C  CA  . GLY D  1 148 ? 26.430  2.062   22.330 1.00 22.28  ? 147 GLY D CA  1 
ATOM   4422  C  C   . GLY D  1 148 ? 26.027  2.330   20.886 1.00 25.35  ? 147 GLY D C   1 
ATOM   4423  O  O   . GLY D  1 148 ? 25.723  1.399   20.123 1.00 26.47  ? 147 GLY D O   1 
ATOM   4424  N  N   . VAL D  1 149 ? 26.028  3.613   20.512 1.00 26.23  ? 148 VAL D N   1 
ATOM   4425  C  CA  . VAL D  1 149 ? 25.786  3.937   19.116 1.00 24.99  ? 148 VAL D CA  1 
ATOM   4426  C  C   . VAL D  1 149 ? 27.088  3.744   18.344 1.00 24.12  ? 148 VAL D C   1 
ATOM   4427  O  O   . VAL D  1 149 ? 28.170  4.038   18.840 1.00 22.78  ? 148 VAL D O   1 
ATOM   4428  C  CB  . VAL D  1 149 ? 25.181  5.342   18.954 1.00 24.40  ? 148 VAL D CB  1 
ATOM   4429  C  CG1 . VAL D  1 149 ? 24.817  5.626   17.510 1.00 24.32  ? 148 VAL D CG1 1 
ATOM   4430  C  CG2 . VAL D  1 149 ? 23.960  5.496   19.846 1.00 25.34  ? 148 VAL D CG2 1 
ATOM   4431  N  N   . ILE D  1 150 ? 26.954  3.203   17.135 1.00 23.80  ? 149 ILE D N   1 
ATOM   4432  C  CA  . ILE D  1 150 ? 28.090  2.875   16.293 1.00 22.87  ? 149 ILE D CA  1 
ATOM   4433  C  C   . ILE D  1 150 ? 28.425  4.120   15.482 1.00 21.61  ? 149 ILE D C   1 
ATOM   4434  O  O   . ILE D  1 150 ? 27.637  4.533   14.639 1.00 21.33  ? 149 ILE D O   1 
ATOM   4435  C  CB  . ILE D  1 150 ? 27.720  1.688   15.382 1.00 22.64  ? 149 ILE D CB  1 
ATOM   4436  C  CG1 . ILE D  1 150 ? 27.434  0.414   16.180 1.00 21.43  ? 149 ILE D CG1 1 
ATOM   4437  C  CG2 . ILE D  1 150 ? 28.767  1.470   14.310 1.00 22.80  ? 149 ILE D CG2 1 
ATOM   4438  C  CD1 . ILE D  1 150 ? 26.707  -0.640  15.375 1.00 20.80  ? 149 ILE D CD1 1 
ATOM   4439  N  N   . GLY D  1 151 ? 29.604  4.690   15.737 1.00 21.42  ? 150 GLY D N   1 
ATOM   4440  C  CA  . GLY D  1 151 ? 29.971  5.987   15.186 1.00 22.78  ? 150 GLY D CA  1 
ATOM   4441  C  C   . GLY D  1 151 ? 31.262  5.969   14.372 1.00 23.85  ? 150 GLY D C   1 
ATOM   4442  O  O   . GLY D  1 151 ? 32.050  5.035   14.470 1.00 25.93  ? 150 GLY D O   1 
ATOM   4443  N  N   . ILE D  1 152 ? 31.461  7.019   13.571 1.00 24.80  ? 151 ILE D N   1 
ATOM   4444  C  CA  . ILE D  1 152 ? 32.603  7.160   12.692 1.00 25.90  ? 151 ILE D CA  1 
ATOM   4445  C  C   . ILE D  1 152 ? 33.834  7.492   13.529 1.00 28.50  ? 151 ILE D C   1 
ATOM   4446  O  O   . ILE D  1 152 ? 33.760  8.351   14.401 1.00 28.40  ? 151 ILE D O   1 
ATOM   4447  C  CB  . ILE D  1 152 ? 32.318  8.243   11.637 1.00 24.07  ? 151 ILE D CB  1 
ATOM   4448  C  CG1 . ILE D  1 152 ? 31.197  7.781   10.698 1.00 23.77  ? 151 ILE D CG1 1 
ATOM   4449  C  CG2 . ILE D  1 152 ? 33.577  8.603   10.867 1.00 22.30  ? 151 ILE D CG2 1 
ATOM   4450  C  CD1 . ILE D  1 152 ? 30.518  8.901   9.952  1.00 24.92  ? 151 ILE D CD1 1 
ATOM   4451  N  N   . ALA D  1 153 ? 34.942  6.791   13.245 1.00 31.73  ? 152 ALA D N   1 
ATOM   4452  C  CA  . ALA D  1 153 ? 36.205  6.979   13.945 1.00 36.00  ? 152 ALA D CA  1 
ATOM   4453  C  C   . ALA D  1 153 ? 37.255  7.490   12.964 1.00 43.53  ? 152 ALA D C   1 
ATOM   4454  O  O   . ALA D  1 153 ? 37.045  7.450   11.748 1.00 45.23  ? 152 ALA D O   1 
ATOM   4455  C  CB  . ALA D  1 153 ? 36.636  5.686   14.587 1.00 33.88  ? 152 ALA D CB  1 
ATOM   4456  N  N   . GLN D  1 154 ? 38.398  7.946   13.503 1.00 52.02  ? 153 GLN D N   1 
ATOM   4457  C  CA  . GLN D  1 154 ? 39.465  8.492   12.670 1.00 56.07  ? 153 GLN D CA  1 
ATOM   4458  C  C   . GLN D  1 154 ? 40.169  7.389   11.864 1.00 59.69  ? 153 GLN D C   1 
ATOM   4459  O  O   . GLN D  1 154 ? 40.608  6.354   12.383 1.00 58.28  ? 153 GLN D O   1 
ATOM   4460  C  CB  . GLN D  1 154 ? 40.503  9.261   13.479 1.00 57.85  ? 153 GLN D CB  1 
ATOM   4461  C  CG  . GLN D  1 154 ? 41.571  9.865   12.575 1.00 58.08  ? 153 GLN D CG  1 
ATOM   4462  C  CD  . GLN D  1 154 ? 42.335  10.969  13.259 1.00 63.07  ? 153 GLN D CD  1 
ATOM   4463  O  OE1 . GLN D  1 154 ? 42.926  10.773  14.320 1.00 64.39  ? 153 GLN D OE1 1 
ATOM   4464  N  NE2 . GLN D  1 154 ? 42.333  12.149  12.650 1.00 61.84  ? 153 GLN D NE2 1 
ATOM   4465  O  OXT . GLN D  1 154 ? 40.333  7.534   10.647 1.00 61.64  ? 153 GLN D OXT 1 
ATOM   4466  N  N   . ALA E  1 2   ? 5.053   -45.698 68.071 1.00 79.35  ? 1   ALA E N   1 
ATOM   4467  C  CA  . ALA E  1 2   ? 5.483   -44.557 67.176 1.00 71.16  ? 1   ALA E CA  1 
ATOM   4468  C  C   . ALA E  1 2   ? 4.322   -44.070 66.308 1.00 62.31  ? 1   ALA E C   1 
ATOM   4469  O  O   . ALA E  1 2   ? 3.454   -44.847 65.908 1.00 69.00  ? 1   ALA E O   1 
ATOM   4470  C  CB  . ALA E  1 2   ? 6.682   -44.949 66.334 1.00 68.39  ? 1   ALA E CB  1 
ATOM   4471  N  N   . THR E  1 3   ? 4.312   -42.772 66.015 1.00 48.74  ? 2   THR E N   1 
ATOM   4472  C  CA  . THR E  1 3   ? 3.323   -42.160 65.135 1.00 41.53  ? 2   THR E CA  1 
ATOM   4473  C  C   . THR E  1 3   ? 3.972   -41.836 63.783 1.00 36.24  ? 2   THR E C   1 
ATOM   4474  O  O   . THR E  1 3   ? 5.005   -41.168 63.724 1.00 34.33  ? 2   THR E O   1 
ATOM   4475  C  CB  . THR E  1 3   ? 2.594   -41.014 65.857 1.00 40.98  ? 2   THR E CB  1 
ATOM   4476  O  OG1 . THR E  1 3   ? 1.529   -40.459 65.094 1.00 41.51  ? 2   THR E OG1 1 
ATOM   4477  C  CG2 . THR E  1 3   ? 3.515   -39.927 66.363 1.00 45.76  ? 2   THR E CG2 1 
ATOM   4478  N  N   . LYS E  1 4   ? 3.406   -42.377 62.700 1.00 31.16  ? 3   LYS E N   1 
ATOM   4479  C  CA  . LYS E  1 4   ? 3.960   -42.240 61.353 1.00 26.93  ? 3   LYS E CA  1 
ATOM   4480  C  C   . LYS E  1 4   ? 2.966   -41.495 60.472 1.00 25.26  ? 3   LYS E C   1 
ATOM   4481  O  O   . LYS E  1 4   ? 1.786   -41.797 60.455 1.00 26.20  ? 3   LYS E O   1 
ATOM   4482  C  CB  . LYS E  1 4   ? 4.315   -43.571 60.669 1.00 23.85  ? 3   LYS E CB  1 
ATOM   4483  C  CG  . LYS E  1 4   ? 5.473   -44.365 61.448 0.00 54.66  ? 3   LYS E CG  1 
ATOM   4484  C  CD  . LYS E  1 4   ? 5.603   -45.814 61.028 0.00 60.92  ? 3   LYS E CD  1 
ATOM   4485  C  CE  . LYS E  1 4   ? 6.861   -46.473 61.553 0.00 63.65  ? 3   LYS E CE  1 
ATOM   4486  N  NZ  . LYS E  1 4   ? 7.054   -47.825 60.977 0.00 64.31  ? 3   LYS E NZ  1 
ATOM   4487  N  N   . VAL E  1 5   ? 3.482   -40.539 59.704 1.00 24.52  ? 4   VAL E N   1 
ATOM   4488  C  CA  . VAL E  1 5   ? 2.692   -39.650 58.876 1.00 23.13  ? 4   VAL E CA  1 
ATOM   4489  C  C   . VAL E  1 5   ? 3.363   -39.570 57.510 1.00 20.60  ? 4   VAL E C   1 
ATOM   4490  O  O   . VAL E  1 5   ? 4.557   -39.798 57.390 1.00 19.52  ? 4   VAL E O   1 
ATOM   4491  C  CB  . VAL E  1 5   ? 2.590   -38.278 59.564 1.00 24.89  ? 4   VAL E CB  1 
ATOM   4492  C  CG1 . VAL E  1 5   ? 2.115   -37.188 58.625 1.00 27.54  ? 4   VAL E CG1 1 
ATOM   4493  C  CG2 . VAL E  1 5   ? 1.725   -38.353 60.808 1.00 27.18  ? 4   VAL E CG2 1 
ATOM   4494  N  N   . VAL E  1 6   ? 2.588   -39.256 56.477 1.00 18.74  ? 5   VAL E N   1 
ATOM   4495  C  CA  . VAL E  1 6   ? 3.164   -39.216 55.147 1.00 17.82  ? 5   VAL E CA  1 
ATOM   4496  C  C   . VAL E  1 6   ? 2.533   -38.086 54.339 1.00 17.40  ? 5   VAL E C   1 
ATOM   4497  O  O   . VAL E  1 6   ? 1.461   -37.580 54.668 1.00 17.96  ? 5   VAL E O   1 
ATOM   4498  C  CB  . VAL E  1 6   ? 3.027   -40.570 54.431 1.00 17.58  ? 5   VAL E CB  1 
ATOM   4499  C  CG1 . VAL E  1 6   ? 1.589   -40.856 54.033 1.00 17.56  ? 5   VAL E CG1 1 
ATOM   4500  C  CG2 . VAL E  1 6   ? 3.924   -40.651 53.213 1.00 17.27  ? 5   VAL E CG2 1 
ATOM   4501  N  N   . CYS E  1 7   ? 3.215   -37.709 53.257 1.00 16.43  ? 6   CYS E N   1 
ATOM   4502  C  CA  . CYS E  1 7   ? 2.737   -36.635 52.424 1.00 16.89  ? 6   CYS E CA  1 
ATOM   4503  C  C   . CYS E  1 7   ? 3.241   -36.872 51.008 1.00 17.09  ? 6   CYS E C   1 
ATOM   4504  O  O   . CYS E  1 7   ? 4.436   -37.099 50.814 1.00 18.22  ? 6   CYS E O   1 
ATOM   4505  C  CB  . CYS E  1 7   ? 3.295   -35.326 52.960 1.00 17.59  ? 6   CYS E CB  1 
ATOM   4506  S  SG  . CYS E  1 7   ? 2.725   -33.884 52.028 1.00 21.18  ? 6   CYS E SG  1 
ATOM   4507  N  N   . VAL E  1 8   ? 2.328   -36.815 50.036 1.00 17.39  ? 7   VAL E N   1 
ATOM   4508  C  CA  . VAL E  1 8   ? 2.707   -36.937 48.639 1.00 19.22  ? 7   VAL E CA  1 
ATOM   4509  C  C   . VAL E  1 8   ? 2.681   -35.538 48.031 1.00 20.90  ? 7   VAL E C   1 
ATOM   4510  O  O   . VAL E  1 8   ? 1.635   -34.884 48.046 1.00 21.66  ? 7   VAL E O   1 
ATOM   4511  C  CB  . VAL E  1 8   ? 1.738   -37.860 47.875 1.00 19.03  ? 7   VAL E CB  1 
ATOM   4512  C  CG1 . VAL E  1 8   ? 2.042   -37.878 46.378 1.00 19.50  ? 7   VAL E CG1 1 
ATOM   4513  C  CG2 . VAL E  1 8   ? 1.683   -39.265 48.450 1.00 18.83  ? 7   VAL E CG2 1 
ATOM   4514  N  N   . LEU E  1 9   ? 3.822   -35.080 47.503 1.00 21.68  ? 8   LEU E N   1 
ATOM   4515  C  CA  . LEU E  1 9   ? 3.876   -33.749 46.933 1.00 23.40  ? 8   LEU E CA  1 
ATOM   4516  C  C   . LEU E  1 9   ? 3.620   -33.833 45.437 1.00 25.40  ? 8   LEU E C   1 
ATOM   4517  O  O   . LEU E  1 9   ? 4.287   -34.598 44.738 1.00 25.80  ? 8   LEU E O   1 
ATOM   4518  C  CB  . LEU E  1 9   ? 5.254   -33.139 47.198 1.00 25.26  ? 8   LEU E CB  1 
ATOM   4519  C  CG  . LEU E  1 9   ? 5.690   -33.049 48.656 1.00 25.86  ? 8   LEU E CG  1 
ATOM   4520  C  CD1 . LEU E  1 9   ? 7.184   -32.733 48.708 1.00 27.44  ? 8   LEU E CD1 1 
ATOM   4521  C  CD2 . LEU E  1 9   ? 4.892   -31.972 49.375 1.00 25.38  ? 8   LEU E CD2 1 
ATOM   4522  N  N   . LYS E  1 10  ? 2.639   -33.052 44.961 1.00 29.09  ? 9   LYS E N   1 
ATOM   4523  C  CA  . LYS E  1 10  ? 2.368   -32.887 43.535 1.00 31.40  ? 9   LYS E CA  1 
ATOM   4524  C  C   . LYS E  1 10  ? 2.135   -31.404 43.266 1.00 31.62  ? 9   LYS E C   1 
ATOM   4525  O  O   . LYS E  1 10  ? 1.820   -30.631 44.177 1.00 31.35  ? 9   LYS E O   1 
ATOM   4526  C  CB  . LYS E  1 10  ? 1.106   -33.658 43.123 1.00 34.84  ? 9   LYS E CB  1 
ATOM   4527  C  CG  . LYS E  1 10  ? 1.212   -35.169 43.005 1.00 40.09  ? 9   LYS E CG  1 
ATOM   4528  C  CD  . LYS E  1 10  ? -0.168  -35.794 42.640 1.00 42.96  ? 9   LYS E CD  1 
ATOM   4529  C  CE  . LYS E  1 10  ? -0.830  -36.863 43.523 1.00 45.26  ? 9   LYS E CE  1 
ATOM   4530  N  NZ  . LYS E  1 10  ? -0.372  -38.266 43.317 1.00 45.62  ? 9   LYS E NZ  1 
ATOM   4531  N  N   . GLY E  1 11  ? 2.333   -31.024 42.004 1.00 32.45  ? 10  GLY E N   1 
ATOM   4532  C  CA  . GLY E  1 11  ? 2.087   -29.678 41.531 1.00 36.49  ? 10  GLY E CA  1 
ATOM   4533  C  C   . GLY E  1 11  ? 1.902   -29.681 40.011 1.00 37.49  ? 10  GLY E C   1 
ATOM   4534  O  O   . GLY E  1 11  ? 1.808   -30.729 39.382 1.00 34.85  ? 10  GLY E O   1 
ATOM   4535  N  N   . ASP E  1 12  ? 1.827   -28.482 39.428 1.00 41.87  ? 11  ASP E N   1 
ATOM   4536  C  CA  . ASP E  1 12  ? 1.526   -28.337 38.014 1.00 46.07  ? 11  ASP E CA  1 
ATOM   4537  C  C   . ASP E  1 12  ? 2.725   -28.700 37.152 1.00 48.62  ? 11  ASP E C   1 
ATOM   4538  O  O   . ASP E  1 12  ? 2.557   -29.090 36.004 1.00 52.12  ? 11  ASP E O   1 
ATOM   4539  C  CB  . ASP E  1 12  ? 1.065   -26.919 37.705 1.00 50.65  ? 11  ASP E CB  1 
ATOM   4540  C  CG  . ASP E  1 12  ? -0.282  -26.641 38.346 1.00 55.91  ? 11  ASP E CG  1 
ATOM   4541  O  OD1 . ASP E  1 12  ? -1.103  -27.574 38.395 1.00 59.90  ? 11  ASP E OD1 1 
ATOM   4542  O  OD2 . ASP E  1 12  ? -0.485  -25.514 38.825 1.00 63.29  ? 11  ASP E OD2 1 
ATOM   4543  N  N   . GLY E  1 13  ? 3.933   -28.543 37.702 1.00 51.01  ? 12  GLY E N   1 
ATOM   4544  C  CA  . GLY E  1 13  ? 5.164   -28.757 36.961 1.00 44.23  ? 12  GLY E CA  1 
ATOM   4545  C  C   . GLY E  1 13  ? 5.690   -30.167 37.188 1.00 43.37  ? 12  GLY E C   1 
ATOM   4546  O  O   . GLY E  1 13  ? 4.928   -31.073 37.513 1.00 43.24  ? 12  GLY E O   1 
ATOM   4547  N  N   . PRO E  1 14  ? 7.012   -30.398 37.013 1.00 42.99  ? 13  PRO E N   1 
ATOM   4548  C  CA  . PRO E  1 14  ? 7.578   -31.740 37.150 1.00 40.45  ? 13  PRO E CA  1 
ATOM   4549  C  C   . PRO E  1 14  ? 7.912   -32.158 38.582 1.00 37.30  ? 13  PRO E C   1 
ATOM   4550  O  O   . PRO E  1 14  ? 8.341   -33.274 38.804 1.00 36.16  ? 13  PRO E O   1 
ATOM   4551  C  CB  . PRO E  1 14  ? 8.849   -31.653 36.300 1.00 40.69  ? 13  PRO E CB  1 
ATOM   4552  C  CG  . PRO E  1 14  ? 9.276   -30.226 36.447 1.00 35.75  ? 13  PRO E CG  1 
ATOM   4553  C  CD  . PRO E  1 14  ? 8.027   -29.398 36.655 1.00 39.85  ? 13  PRO E CD  1 
ATOM   4554  N  N   . VAL E  1 15  ? 7.691   -31.268 39.554 1.00 35.09  ? 14  VAL E N   1 
ATOM   4555  C  CA  . VAL E  1 15  ? 8.157   -31.568 40.898 1.00 33.95  ? 14  VAL E CA  1 
ATOM   4556  C  C   . VAL E  1 15  ? 7.181   -32.528 41.558 1.00 33.12  ? 14  VAL E C   1 
ATOM   4557  O  O   . VAL E  1 15  ? 5.975   -32.274 41.583 1.00 33.31  ? 14  VAL E O   1 
ATOM   4558  C  CB  . VAL E  1 15  ? 8.372   -30.301 41.743 1.00 34.79  ? 14  VAL E CB  1 
ATOM   4559  C  CG1 . VAL E  1 15  ? 8.800   -30.657 43.156 1.00 33.67  ? 14  VAL E CG1 1 
ATOM   4560  C  CG2 . VAL E  1 15  ? 9.427   -29.422 41.079 1.00 34.12  ? 14  VAL E CG2 1 
ATOM   4561  N  N   . GLN E  1 16  ? 7.711   -33.638 42.084 1.00 31.95  ? 15  GLN E N   1 
ATOM   4562  C  CA  . GLN E  1 16  ? 6.880   -34.560 42.851 1.00 30.88  ? 15  GLN E CA  1 
ATOM   4563  C  C   . GLN E  1 16  ? 7.753   -35.366 43.810 1.00 27.52  ? 15  GLN E C   1 
ATOM   4564  O  O   . GLN E  1 16  ? 8.953   -35.523 43.565 1.00 28.99  ? 15  GLN E O   1 
ATOM   4565  C  CB  . GLN E  1 16  ? 6.073   -35.463 41.909 1.00 34.12  ? 15  GLN E CB  1 
ATOM   4566  C  CG  . GLN E  1 16  ? 6.906   -36.346 41.001 1.00 40.11  ? 15  GLN E CG  1 
ATOM   4567  C  CD  . GLN E  1 16  ? 6.102   -36.821 39.811 1.00 43.33  ? 15  GLN E CD  1 
ATOM   4568  O  OE1 . GLN E  1 16  ? 5.128   -36.188 39.420 1.00 46.48  ? 15  GLN E OE1 1 
ATOM   4569  N  NE2 . GLN E  1 16  ? 6.562   -37.907 39.195 1.00 42.72  ? 15  GLN E NE2 1 
ATOM   4570  N  N   . GLY E  1 17  ? 7.144   -35.868 44.889 1.00 22.71  ? 16  GLY E N   1 
ATOM   4571  C  CA  . GLY E  1 17  ? 7.901   -36.565 45.908 1.00 21.68  ? 16  GLY E CA  1 
ATOM   4572  C  C   . GLY E  1 17  ? 7.026   -37.154 47.009 1.00 21.52  ? 16  GLY E C   1 
ATOM   4573  O  O   . GLY E  1 17  ? 5.829   -36.872 47.084 1.00 24.42  ? 16  GLY E O   1 
ATOM   4574  N  N   . ILE E  1 18  ? 7.642   -37.971 47.863 1.00 20.34  ? 17  ILE E N   1 
ATOM   4575  C  CA  . ILE E  1 18  ? 6.987   -38.539 49.025 1.00 20.38  ? 17  ILE E CA  1 
ATOM   4576  C  C   . ILE E  1 18  ? 7.824   -38.164 50.237 1.00 20.04  ? 17  ILE E C   1 
ATOM   4577  O  O   . ILE E  1 18  ? 9.039   -38.365 50.224 1.00 20.84  ? 17  ILE E O   1 
ATOM   4578  C  CB  . ILE E  1 18  ? 6.893   -40.073 48.880 1.00 22.29  ? 17  ILE E CB  1 
ATOM   4579  C  CG1 . ILE E  1 18  ? 6.068   -40.494 47.662 1.00 21.70  ? 17  ILE E CG1 1 
ATOM   4580  C  CG2 . ILE E  1 18  ? 6.409   -40.730 50.162 1.00 22.07  ? 17  ILE E CG2 1 
ATOM   4581  C  CD1 . ILE E  1 18  ? 6.130   -41.994 47.418 1.00 20.35  ? 17  ILE E CD1 1 
ATOM   4582  N  N   . ILE E  1 19  ? 7.187   -37.628 51.283 1.00 19.11  ? 18  ILE E N   1 
ATOM   4583  C  CA  . ILE E  1 19  ? 7.938   -37.301 52.483 1.00 19.31  ? 18  ILE E CA  1 
ATOM   4584  C  C   . ILE E  1 19  ? 7.286   -37.993 53.665 1.00 19.34  ? 18  ILE E C   1 
ATOM   4585  O  O   . ILE E  1 19  ? 6.079   -37.871 53.849 1.00 21.13  ? 18  ILE E O   1 
ATOM   4586  C  CB  . ILE E  1 19  ? 8.020   -35.774 52.705 1.00 19.18  ? 18  ILE E CB  1 
ATOM   4587  C  CG1 . ILE E  1 19  ? 8.714   -35.046 51.549 1.00 18.71  ? 18  ILE E CG1 1 
ATOM   4588  C  CG2 . ILE E  1 19  ? 8.658   -35.441 54.046 1.00 19.22  ? 18  ILE E CG2 1 
ATOM   4589  C  CD1 . ILE E  1 19  ? 10.169  -35.405 51.358 1.00 17.17  ? 18  ILE E CD1 1 
ATOM   4590  N  N   . ASN E  1 20  ? 8.100   -38.686 54.462 1.00 19.77  ? 19  ASN E N   1 
ATOM   4591  C  CA  . ASN E  1 20  ? 7.615   -39.372 55.645 1.00 21.18  ? 19  ASN E CA  1 
ATOM   4592  C  C   . ASN E  1 20  ? 7.965   -38.569 56.892 1.00 23.17  ? 19  ASN E C   1 
ATOM   4593  O  O   . ASN E  1 20  ? 8.995   -37.905 56.942 1.00 25.72  ? 19  ASN E O   1 
ATOM   4594  C  CB  . ASN E  1 20  ? 8.236   -40.759 55.778 1.00 20.46  ? 19  ASN E CB  1 
ATOM   4595  C  CG  . ASN E  1 20  ? 8.064   -41.556 54.506 1.00 20.38  ? 19  ASN E CG  1 
ATOM   4596  O  OD1 . ASN E  1 20  ? 8.980   -41.609 53.693 1.00 20.58  ? 19  ASN E OD1 1 
ATOM   4597  N  ND2 . ASN E  1 20  ? 6.883   -42.123 54.290 1.00 19.45  ? 19  ASN E ND2 1 
ATOM   4598  N  N   . PHE E  1 21  ? 7.109   -38.663 57.909 1.00 23.94  ? 20  PHE E N   1 
ATOM   4599  C  CA  . PHE E  1 21  ? 7.359   -38.055 59.202 1.00 25.75  ? 20  PHE E CA  1 
ATOM   4600  C  C   . PHE E  1 21  ? 7.177   -39.118 60.272 1.00 28.67  ? 20  PHE E C   1 
ATOM   4601  O  O   . PHE E  1 21  ? 6.202   -39.853 60.238 1.00 29.69  ? 20  PHE E O   1 
ATOM   4602  C  CB  . PHE E  1 21  ? 6.348   -36.945 59.501 1.00 24.76  ? 20  PHE E CB  1 
ATOM   4603  C  CG  . PHE E  1 21  ? 6.361   -35.784 58.540 1.00 23.34  ? 20  PHE E CG  1 
ATOM   4604  C  CD1 . PHE E  1 21  ? 5.896   -35.935 57.235 1.00 23.77  ? 20  PHE E CD1 1 
ATOM   4605  C  CD2 . PHE E  1 21  ? 6.797   -34.536 58.946 1.00 21.84  ? 20  PHE E CD2 1 
ATOM   4606  C  CE1 . PHE E  1 21  ? 5.888   -34.858 56.360 1.00 22.87  ? 20  PHE E CE1 1 
ATOM   4607  C  CE2 . PHE E  1 21  ? 6.772   -33.457 58.073 1.00 22.08  ? 20  PHE E CE2 1 
ATOM   4608  C  CZ  . PHE E  1 21  ? 6.315   -33.617 56.782 1.00 21.82  ? 20  PHE E CZ  1 
ATOM   4609  N  N   . GLU E  1 22  ? 8.111   -39.185 61.220 1.00 32.33  ? 21  GLU E N   1 
ATOM   4610  C  CA  . GLU E  1 22  ? 8.010   -40.170 62.282 1.00 34.74  ? 21  GLU E CA  1 
ATOM   4611  C  C   . GLU E  1 22  ? 8.408   -39.517 63.599 1.00 33.73  ? 21  GLU E C   1 
ATOM   4612  O  O   . GLU E  1 22  ? 9.352   -38.735 63.634 1.00 31.96  ? 21  GLU E O   1 
ATOM   4613  C  CB  . GLU E  1 22  ? 8.880   -41.385 61.950 1.00 40.70  ? 21  GLU E CB  1 
ATOM   4614  C  CG  . GLU E  1 22  ? 8.515   -42.597 62.786 1.00 47.15  ? 21  GLU E CG  1 
ATOM   4615  C  CD  . GLU E  1 22  ? 9.290   -43.868 62.532 1.00 49.97  ? 21  GLU E CD  1 
ATOM   4616  O  OE1 . GLU E  1 22  ? 9.434   -44.278 61.345 1.00 52.51  ? 21  GLU E OE1 1 
ATOM   4617  O  OE2 . GLU E  1 22  ? 9.762   -44.416 63.531 1.00 58.04  ? 21  GLU E OE2 1 
ATOM   4618  N  N   . GLN E  1 23  ? 7.682   -39.845 64.673 1.00 35.81  ? 22  GLN E N   1 
ATOM   4619  C  CA  . GLN E  1 23  ? 7.928   -39.273 65.986 1.00 35.88  ? 22  GLN E CA  1 
ATOM   4620  C  C   . GLN E  1 23  ? 7.811   -40.362 67.050 1.00 37.24  ? 22  GLN E C   1 
ATOM   4621  O  O   . GLN E  1 23  ? 6.701   -40.802 67.347 1.00 35.62  ? 22  GLN E O   1 
ATOM   4622  C  CB  . GLN E  1 23  ? 6.904   -38.159 66.233 1.00 34.19  ? 22  GLN E CB  1 
ATOM   4623  C  CG  . GLN E  1 23  ? 7.200   -37.337 67.486 1.00 36.36  ? 22  GLN E CG  1 
ATOM   4624  C  CD  . GLN E  1 23  ? 6.151   -36.294 67.748 1.00 36.18  ? 22  GLN E CD  1 
ATOM   4625  O  OE1 . GLN E  1 23  ? 4.971   -36.470 67.493 1.00 34.77  ? 22  GLN E OE1 1 
ATOM   4626  N  NE2 . GLN E  1 23  ? 6.582   -35.192 68.302 1.00 36.41  ? 22  GLN E NE2 1 
ATOM   4627  N  N   . LYS E  1 24  ? 8.941   -40.778 67.645 1.00 40.64  ? 23  LYS E N   1 
ATOM   4628  C  CA  . LYS E  1 24  ? 8.960   -41.877 68.602 1.00 42.57  ? 23  LYS E CA  1 
ATOM   4629  C  C   . LYS E  1 24  ? 8.276   -41.481 69.916 1.00 47.25  ? 23  LYS E C   1 
ATOM   4630  O  O   . LYS E  1 24  ? 7.381   -42.188 70.374 1.00 51.98  ? 23  LYS E O   1 
ATOM   4631  C  CB  . LYS E  1 24  ? 10.350  -42.511 68.748 1.00 38.41  ? 23  LYS E CB  1 
ATOM   4632  C  CG  . LYS E  1 24  ? 10.784  -43.431 67.616 0.40 36.46  ? 23  LYS E CG  1 
ATOM   4633  C  CD  . LYS E  1 24  ? 12.138  -44.082 67.892 0.40 34.91  ? 23  LYS E CD  1 
ATOM   4634  C  CE  . LYS E  1 24  ? 12.459  -45.312 67.063 0.40 33.15  ? 23  LYS E CE  1 
ATOM   4635  N  NZ  . LYS E  1 24  ? 13.300  -46.258 67.835 0.40 31.36  ? 23  LYS E NZ  1 
ATOM   4636  N  N   . GLU E  1 25  ? 8.698   -40.372 70.535 1.00 51.81  ? 24  GLU E N   1 
ATOM   4637  C  CA  . GLU E  1 25  ? 8.094   -39.935 71.793 1.00 54.98  ? 24  GLU E CA  1 
ATOM   4638  C  C   . GLU E  1 25  ? 7.169   -38.766 71.515 1.00 55.00  ? 24  GLU E C   1 
ATOM   4639  O  O   . GLU E  1 25  ? 7.372   -38.036 70.580 1.00 63.05  ? 24  GLU E O   1 
ATOM   4640  C  CB  . GLU E  1 25  ? 9.146   -39.553 72.840 1.00 60.78  ? 24  GLU E CB  1 
ATOM   4641  C  CG  . GLU E  1 25  ? 10.005  -40.762 73.197 1.00 65.21  ? 24  GLU E CG  1 
ATOM   4642  C  CD  . GLU E  1 25  ? 11.238  -40.489 74.031 1.00 65.20  ? 24  GLU E CD  1 
ATOM   4643  O  OE1 . GLU E  1 25  ? 11.808  -39.409 73.853 1.00 64.64  ? 24  GLU E OE1 1 
ATOM   4644  O  OE2 . GLU E  1 25  ? 11.626  -41.360 74.848 1.00 69.00  ? 24  GLU E OE2 1 
ATOM   4645  N  N   . SER E  1 26  ? 6.138   -38.608 72.352 1.00 52.81  ? 25  SER E N   1 
ATOM   4646  C  CA  . SER E  1 26  ? 5.241   -37.464 72.259 1.00 53.49  ? 25  SER E CA  1 
ATOM   4647  C  C   . SER E  1 26  ? 6.015   -36.197 72.614 1.00 55.82  ? 25  SER E C   1 
ATOM   4648  O  O   . SER E  1 26  ? 6.746   -36.113 73.601 1.00 61.21  ? 25  SER E O   1 
ATOM   4649  C  CB  . SER E  1 26  ? 4.024   -37.609 73.119 1.00 51.94  ? 25  SER E CB  1 
ATOM   4650  O  OG  . SER E  1 26  ? 4.258   -38.382 74.281 1.00 50.99  ? 25  SER E OG  1 
ATOM   4651  N  N   . ASN E  1 27  ? 5.984   -35.232 71.720 1.00 57.10  ? 26  ASN E N   1 
ATOM   4652  C  CA  . ASN E  1 27  ? 6.657   -33.960 71.956 1.00 56.79  ? 26  ASN E CA  1 
ATOM   4653  C  C   . ASN E  1 27  ? 8.170   -34.112 71.894 1.00 50.78  ? 26  ASN E C   1 
ATOM   4654  O  O   . ASN E  1 27  ? 8.857   -33.096 71.947 1.00 45.61  ? 26  ASN E O   1 
ATOM   4655  C  CB  . ASN E  1 27  ? 6.187   -33.176 73.197 1.00 63.79  ? 26  ASN E CB  1 
ATOM   4656  C  CG  . ASN E  1 27  ? 4.715   -32.815 73.157 1.00 69.74  ? 26  ASN E CG  1 
ATOM   4657  O  OD1 . ASN E  1 27  ? 4.193   -32.515 72.087 1.00 70.44  ? 26  ASN E OD1 1 
ATOM   4658  N  ND2 . ASN E  1 27  ? 4.039   -32.869 74.300 1.00 66.14  ? 26  ASN E ND2 1 
ATOM   4659  N  N   . GLY E  1 28  ? 8.639   -35.332 71.497 1.00 45.41  ? 27  GLY E N   1 
ATOM   4660  C  CA  . GLY E  1 28  ? 10.030  -35.480 71.090 1.00 41.21  ? 27  GLY E CA  1 
ATOM   4661  C  C   . GLY E  1 28  ? 10.258  -35.162 69.613 1.00 37.06  ? 27  GLY E C   1 
ATOM   4662  O  O   . GLY E  1 28  ? 9.330   -34.756 68.915 1.00 35.30  ? 27  GLY E O   1 
ATOM   4663  N  N   . PRO E  1 29  ? 11.498  -35.294 69.104 1.00 34.69  ? 28  PRO E N   1 
ATOM   4664  C  CA  . PRO E  1 29  ? 11.833  -34.820 67.759 1.00 31.17  ? 28  PRO E CA  1 
ATOM   4665  C  C   . PRO E  1 29  ? 11.126  -35.628 66.674 1.00 29.32  ? 28  PRO E C   1 
ATOM   4666  O  O   . PRO E  1 29  ? 10.743  -36.772 66.912 1.00 29.79  ? 28  PRO E O   1 
ATOM   4667  C  CB  . PRO E  1 29  ? 13.349  -35.015 67.674 1.00 30.10  ? 28  PRO E CB  1 
ATOM   4668  C  CG  . PRO E  1 29  ? 13.622  -36.123 68.654 1.00 29.92  ? 28  PRO E CG  1 
ATOM   4669  C  CD  . PRO E  1 29  ? 12.646  -35.898 69.797 1.00 32.24  ? 28  PRO E CD  1 
ATOM   4670  N  N   . VAL E  1 30  ? 10.963  -35.008 65.493 1.00 26.39  ? 29  VAL E N   1 
ATOM   4671  C  CA  . VAL E  1 30  ? 10.302  -35.623 64.356 1.00 24.84  ? 29  VAL E CA  1 
ATOM   4672  C  C   . VAL E  1 30  ? 11.342  -35.842 63.262 1.00 23.49  ? 29  VAL E C   1 
ATOM   4673  O  O   . VAL E  1 30  ? 12.012  -34.899 62.856 1.00 21.32  ? 29  VAL E O   1 
ATOM   4674  C  CB  . VAL E  1 30  ? 9.154   -34.740 63.831 1.00 25.47  ? 29  VAL E CB  1 
ATOM   4675  C  CG1 . VAL E  1 30  ? 8.455   -35.385 62.644 1.00 26.21  ? 29  VAL E CG1 1 
ATOM   4676  C  CG2 . VAL E  1 30  ? 8.150   -34.386 64.908 1.00 25.53  ? 29  VAL E CG2 1 
ATOM   4677  N  N   . LYS E  1 31  ? 11.464  -37.087 62.789 1.00 23.64  ? 30  LYS E N   1 
ATOM   4678  C  CA  . LYS E  1 31  ? 12.344  -37.364 61.666 1.00 23.12  ? 30  LYS E CA  1 
ATOM   4679  C  C   . LYS E  1 31  ? 11.537  -37.128 60.390 1.00 22.48  ? 30  LYS E C   1 
ATOM   4680  O  O   . LYS E  1 31  ? 10.446  -37.668 60.221 1.00 24.40  ? 30  LYS E O   1 
ATOM   4681  C  CB  . LYS E  1 31  ? 12.889  -38.788 61.700 1.00 23.60  ? 30  LYS E CB  1 
ATOM   4682  C  CG  . LYS E  1 31  ? 14.055  -39.055 62.651 1.00 25.02  ? 30  LYS E CG  1 
ATOM   4683  C  CD  . LYS E  1 31  ? 14.823  -40.371 62.365 0.50 24.66  ? 30  LYS E CD  1 
ATOM   4684  C  CE  . LYS E  1 31  ? 14.683  -41.647 63.224 0.50 23.73  ? 30  LYS E CE  1 
ATOM   4685  N  NZ  . LYS E  1 31  ? 15.514  -41.714 64.456 0.50 22.18  ? 30  LYS E NZ  1 
ATOM   4686  N  N   . VAL E  1 32  ? 12.071  -36.300 59.492 1.00 20.30  ? 31  VAL E N   1 
ATOM   4687  C  CA  . VAL E  1 32  ? 11.414  -36.033 58.226 1.00 19.24  ? 31  VAL E CA  1 
ATOM   4688  C  C   . VAL E  1 32  ? 12.331  -36.529 57.116 1.00 20.34  ? 31  VAL E C   1 
ATOM   4689  O  O   . VAL E  1 32  ? 13.436  -36.012 56.972 1.00 22.72  ? 31  VAL E O   1 
ATOM   4690  C  CB  . VAL E  1 32  ? 11.130  -34.527 58.071 1.00 17.63  ? 31  VAL E CB  1 
ATOM   4691  C  CG1 . VAL E  1 32  ? 10.372  -34.220 56.790 1.00 16.66  ? 31  VAL E CG1 1 
ATOM   4692  C  CG2 . VAL E  1 32  ? 10.426  -33.964 59.285 1.00 16.81  ? 31  VAL E CG2 1 
ATOM   4693  N  N   . TRP E  1 33  ? 11.889  -37.527 56.346 1.00 20.00  ? 32  TRP E N   1 
ATOM   4694  C  CA  . TRP E  1 33  ? 12.749  -38.006 55.276 1.00 20.73  ? 32  TRP E CA  1 
ATOM   4695  C  C   . TRP E  1 33  ? 11.936  -38.428 54.062 1.00 20.82  ? 32  TRP E C   1 
ATOM   4696  O  O   . TRP E  1 33  ? 10.763  -38.776 54.160 1.00 22.50  ? 32  TRP E O   1 
ATOM   4697  C  CB  . TRP E  1 33  ? 13.630  -39.162 55.749 1.00 21.73  ? 32  TRP E CB  1 
ATOM   4698  C  CG  . TRP E  1 33  ? 12.925  -40.486 55.773 1.00 23.10  ? 32  TRP E CG  1 
ATOM   4699  C  CD1 . TRP E  1 33  ? 12.966  -41.480 54.831 1.00 23.19  ? 32  TRP E CD1 1 
ATOM   4700  C  CD2 . TRP E  1 33  ? 12.046  -40.952 56.808 1.00 24.13  ? 32  TRP E CD2 1 
ATOM   4701  N  NE1 . TRP E  1 33  ? 12.175  -42.533 55.210 1.00 23.22  ? 32  TRP E NE1 1 
ATOM   4702  C  CE2 . TRP E  1 33  ? 11.603  -42.240 56.423 1.00 24.07  ? 32  TRP E CE2 1 
ATOM   4703  C  CE3 . TRP E  1 33  ? 11.591  -40.401 58.014 1.00 24.92  ? 32  TRP E CE3 1 
ATOM   4704  C  CZ2 . TRP E  1 33  ? 10.724  -42.984 57.215 1.00 24.26  ? 32  TRP E CZ2 1 
ATOM   4705  C  CZ3 . TRP E  1 33  ? 10.724  -41.144 58.792 1.00 25.94  ? 32  TRP E CZ3 1 
ATOM   4706  C  CH2 . TRP E  1 33  ? 10.301  -42.422 58.404 1.00 24.62  ? 32  TRP E CH2 1 
ATOM   4707  N  N   . GLY E  1 34  ? 12.611  -38.440 52.915 1.00 19.55  ? 33  GLY E N   1 
ATOM   4708  C  CA  . GLY E  1 34  ? 12.026  -38.950 51.689 1.00 20.66  ? 33  GLY E CA  1 
ATOM   4709  C  C   . GLY E  1 34  ? 12.759  -38.363 50.496 1.00 22.45  ? 33  GLY E C   1 
ATOM   4710  O  O   . GLY E  1 34  ? 13.880  -37.880 50.624 1.00 25.44  ? 33  GLY E O   1 
ATOM   4711  N  N   . SER E  1 35  ? 12.095  -38.353 49.349 1.00 22.64  ? 34  SER E N   1 
ATOM   4712  C  CA  . SER E  1 35  ? 12.774  -37.957 48.137 1.00 22.94  ? 34  SER E CA  1 
ATOM   4713  C  C   . SER E  1 35  ? 11.856  -37.058 47.304 1.00 25.06  ? 34  SER E C   1 
ATOM   4714  O  O   . SER E  1 35  ? 10.652  -37.287 47.239 1.00 29.50  ? 34  SER E O   1 
ATOM   4715  C  CB  . SER E  1 35  ? 13.175  -39.205 47.444 1.00 22.62  ? 34  SER E CB  1 
ATOM   4716  O  OG  . SER E  1 35  ? 13.621  -38.916 46.141 1.00 27.61  ? 34  SER E OG  1 
ATOM   4717  N  N   . ILE E  1 36  ? 12.408  -35.989 46.715 1.00 25.43  ? 35  ILE E N   1 
ATOM   4718  C  CA  . ILE E  1 36  ? 11.667  -35.154 45.781 1.00 23.45  ? 35  ILE E CA  1 
ATOM   4719  C  C   . ILE E  1 36  ? 12.463  -35.096 44.484 1.00 23.91  ? 35  ILE E C   1 
ATOM   4720  O  O   . ILE E  1 36  ? 13.685  -34.940 44.513 1.00 25.01  ? 35  ILE E O   1 
ATOM   4721  C  CB  . ILE E  1 36  ? 11.457  -33.746 46.365 1.00 22.95  ? 35  ILE E CB  1 
ATOM   4722  C  CG1 . ILE E  1 36  ? 10.919  -33.799 47.793 1.00 22.04  ? 35  ILE E CG1 1 
ATOM   4723  C  CG2 . ILE E  1 36  ? 10.570  -32.915 45.450 1.00 23.24  ? 35  ILE E CG2 1 
ATOM   4724  C  CD1 . ILE E  1 36  ? 10.858  -32.453 48.480 1.00 21.72  ? 35  ILE E CD1 1 
ATOM   4725  N  N   . LYS E  1 37  ? 11.767  -35.210 43.350 1.00 24.25  ? 36  LYS E N   1 
ATOM   4726  C  CA  . LYS E  1 37  ? 12.452  -35.180 42.064 1.00 26.00  ? 36  LYS E CA  1 
ATOM   4727  C  C   . LYS E  1 37  ? 11.892  -34.043 41.212 1.00 25.57  ? 36  LYS E C   1 
ATOM   4728  O  O   . LYS E  1 37  ? 10.832  -33.499 41.524 1.00 25.72  ? 36  LYS E O   1 
ATOM   4729  C  CB  . LYS E  1 37  ? 12.398  -36.549 41.383 1.00 28.07  ? 36  LYS E CB  1 
ATOM   4730  C  CG  . LYS E  1 37  ? 10.998  -36.992 40.945 1.00 30.05  ? 36  LYS E CG  1 
ATOM   4731  C  CD  . LYS E  1 37  ? 10.887  -38.330 40.295 1.00 34.23  ? 36  LYS E CD  1 
ATOM   4732  C  CE  . LYS E  1 37  ? 9.804   -38.393 39.220 1.00 36.46  ? 36  LYS E CE  1 
ATOM   4733  N  NZ  . LYS E  1 37  ? 9.801   -39.666 38.466 1.00 38.87  ? 36  LYS E NZ  1 
ATOM   4734  N  N   . GLY E  1 38  ? 12.643  -33.685 40.161 1.00 26.10  ? 37  GLY E N   1 
ATOM   4735  C  CA  . GLY E  1 38  ? 12.234  -32.664 39.207 1.00 29.56  ? 37  GLY E CA  1 
ATOM   4736  C  C   . GLY E  1 38  ? 12.572  -31.236 39.646 1.00 31.93  ? 37  GLY E C   1 
ATOM   4737  O  O   . GLY E  1 38  ? 12.064  -30.278 39.071 1.00 36.82  ? 37  GLY E O   1 
ATOM   4738  N  N   . LEU E  1 39  ? 13.426  -31.092 40.671 1.00 29.77  ? 38  LEU E N   1 
ATOM   4739  C  CA  . LEU E  1 39  ? 13.808  -29.781 41.178 1.00 30.27  ? 38  LEU E CA  1 
ATOM   4740  C  C   . LEU E  1 39  ? 15.021  -29.267 40.413 1.00 33.12  ? 38  LEU E C   1 
ATOM   4741  O  O   . LEU E  1 39  ? 15.797  -30.056 39.878 1.00 36.50  ? 38  LEU E O   1 
ATOM   4742  C  CB  . LEU E  1 39  ? 14.139  -29.897 42.665 1.00 26.20  ? 38  LEU E CB  1 
ATOM   4743  C  CG  . LEU E  1 39  ? 12.928  -30.139 43.576 1.00 23.48  ? 38  LEU E CG  1 
ATOM   4744  C  CD1 . LEU E  1 39  ? 13.382  -30.602 44.942 1.00 22.61  ? 38  LEU E CD1 1 
ATOM   4745  C  CD2 . LEU E  1 39  ? 12.093  -28.888 43.719 1.00 21.89  ? 38  LEU E CD2 1 
ATOM   4746  N  N   . THR E  1 40  ? 15.180  -27.938 40.364 1.00 34.54  ? 39  THR E N   1 
ATOM   4747  C  CA  . THR E  1 40  ? 16.417  -27.355 39.861 1.00 32.71  ? 39  THR E CA  1 
ATOM   4748  C  C   . THR E  1 40  ? 17.494  -27.557 40.919 1.00 35.04  ? 39  THR E C   1 
ATOM   4749  O  O   . THR E  1 40  ? 17.190  -27.583 42.113 1.00 37.82  ? 39  THR E O   1 
ATOM   4750  C  CB  . THR E  1 40  ? 16.263  -25.859 39.565 1.00 30.04  ? 39  THR E CB  1 
ATOM   4751  O  OG1 . THR E  1 40  ? 15.675  -25.287 40.732 1.00 28.17  ? 39  THR E OG1 1 
ATOM   4752  C  CG2 . THR E  1 40  ? 15.405  -25.577 38.349 1.00 28.88  ? 39  THR E CG2 1 
ATOM   4753  N  N   . GLU E  1 41  ? 18.744  -27.710 40.466 1.00 38.15  ? 40  GLU E N   1 
ATOM   4754  C  CA  . GLU E  1 41  ? 19.845  -27.971 41.380 1.00 37.44  ? 40  GLU E CA  1 
ATOM   4755  C  C   . GLU E  1 41  ? 19.908  -26.845 42.410 1.00 36.45  ? 40  GLU E C   1 
ATOM   4756  O  O   . GLU E  1 41  ? 19.670  -25.683 42.074 1.00 34.56  ? 40  GLU E O   1 
ATOM   4757  C  CB  . GLU E  1 41  ? 21.150  -28.065 40.591 1.00 38.17  ? 40  GLU E CB  1 
ATOM   4758  C  CG  . GLU E  1 41  ? 22.319  -28.447 41.469 1.00 42.43  ? 40  GLU E CG  1 
ATOM   4759  C  CD  . GLU E  1 41  ? 23.652  -28.653 40.763 1.00 44.92  ? 40  GLU E CD  1 
ATOM   4760  O  OE1 . GLU E  1 41  ? 23.748  -28.375 39.528 1.00 43.34  ? 40  GLU E OE1 1 
ATOM   4761  O  OE2 . GLU E  1 41  ? 24.594  -29.106 41.464 1.00 40.54  ? 40  GLU E OE2 1 
ATOM   4762  N  N   . GLY E  1 42  ? 20.194  -27.195 43.668 1.00 33.36  ? 41  GLY E N   1 
ATOM   4763  C  CA  . GLY E  1 42  ? 20.375  -26.183 44.700 1.00 32.34  ? 41  GLY E CA  1 
ATOM   4764  C  C   . GLY E  1 42  ? 19.298  -26.217 45.792 1.00 33.67  ? 41  GLY E C   1 
ATOM   4765  O  O   . GLY E  1 42  ? 18.582  -27.213 45.937 1.00 35.29  ? 41  GLY E O   1 
ATOM   4766  N  N   . LEU E  1 43  ? 19.218  -25.114 46.555 1.00 30.83  ? 42  LEU E N   1 
ATOM   4767  C  CA  . LEU E  1 43  ? 18.393  -25.026 47.752 1.00 28.50  ? 42  LEU E CA  1 
ATOM   4768  C  C   . LEU E  1 43  ? 16.953  -24.701 47.375 1.00 28.19  ? 42  LEU E C   1 
ATOM   4769  O  O   . LEU E  1 43  ? 16.714  -23.894 46.475 1.00 31.02  ? 42  LEU E O   1 
ATOM   4770  C  CB  . LEU E  1 43  ? 18.945  -23.920 48.655 1.00 28.99  ? 42  LEU E CB  1 
ATOM   4771  C  CG  . LEU E  1 43  ? 20.304  -24.210 49.299 1.00 29.29  ? 42  LEU E CG  1 
ATOM   4772  C  CD1 . LEU E  1 43  ? 20.815  -22.981 50.022 1.00 28.67  ? 42  LEU E CD1 1 
ATOM   4773  C  CD2 . LEU E  1 43  ? 20.254  -25.398 50.263 1.00 29.59  ? 42  LEU E CD2 1 
ATOM   4774  N  N   . HIS E  1 44  ? 16.007  -25.333 48.085 1.00 26.73  ? 43  HIS E N   1 
ATOM   4775  C  CA  . HIS E  1 44  ? 14.582  -25.057 47.954 1.00 24.52  ? 43  HIS E CA  1 
ATOM   4776  C  C   . HIS E  1 44  ? 13.944  -24.983 49.339 1.00 25.23  ? 43  HIS E C   1 
ATOM   4777  O  O   . HIS E  1 44  ? 14.196  -25.825 50.207 1.00 25.42  ? 43  HIS E O   1 
ATOM   4778  C  CB  . HIS E  1 44  ? 13.899  -26.112 47.091 1.00 24.03  ? 43  HIS E CB  1 
ATOM   4779  C  CG  . HIS E  1 44  ? 14.351  -26.104 45.668 1.00 24.73  ? 43  HIS E CG  1 
ATOM   4780  N  ND1 . HIS E  1 44  ? 13.655  -25.425 44.677 1.00 23.67  ? 43  HIS E ND1 1 
ATOM   4781  C  CD2 . HIS E  1 44  ? 15.403  -26.718 45.064 1.00 23.92  ? 43  HIS E CD2 1 
ATOM   4782  C  CE1 . HIS E  1 44  ? 14.259  -25.624 43.510 1.00 23.29  ? 43  HIS E CE1 1 
ATOM   4783  N  NE2 . HIS E  1 44  ? 15.344  -26.417 43.733 1.00 22.97  ? 43  HIS E NE2 1 
ATOM   4784  N  N   . GLY E  1 45  ? 13.138  -23.934 49.533 1.00 25.44  ? 44  GLY E N   1 
ATOM   4785  C  CA  . GLY E  1 45  ? 12.429  -23.729 50.784 1.00 24.93  ? 44  GLY E CA  1 
ATOM   4786  C  C   . GLY E  1 45  ? 11.422  -24.850 51.034 1.00 23.45  ? 44  GLY E C   1 
ATOM   4787  O  O   . GLY E  1 45  ? 10.770  -25.336 50.111 1.00 24.76  ? 44  GLY E O   1 
ATOM   4788  N  N   . PHE E  1 46  ? 11.298  -25.228 52.303 1.00 21.53  ? 45  PHE E N   1 
ATOM   4789  C  CA  . PHE E  1 46  ? 10.586  -26.431 52.678 1.00 21.64  ? 45  PHE E CA  1 
ATOM   4790  C  C   . PHE E  1 46  ? 9.801   -26.131 53.946 1.00 20.95  ? 45  PHE E C   1 
ATOM   4791  O  O   . PHE E  1 46  ? 10.405  -26.001 55.009 1.00 19.82  ? 45  PHE E O   1 
ATOM   4792  C  CB  . PHE E  1 46  ? 11.626  -27.526 52.941 1.00 21.19  ? 45  PHE E CB  1 
ATOM   4793  C  CG  . PHE E  1 46  ? 11.103  -28.937 53.032 1.00 20.64  ? 45  PHE E CG  1 
ATOM   4794  C  CD1 . PHE E  1 46  ? 10.535  -29.561 51.925 1.00 20.60  ? 45  PHE E CD1 1 
ATOM   4795  C  CD2 . PHE E  1 46  ? 11.222  -29.656 54.212 1.00 20.15  ? 45  PHE E CD2 1 
ATOM   4796  C  CE1 . PHE E  1 46  ? 10.060  -30.860 52.010 1.00 20.68  ? 45  PHE E CE1 1 
ATOM   4797  C  CE2 . PHE E  1 46  ? 10.781  -30.966 54.289 1.00 20.29  ? 45  PHE E CE2 1 
ATOM   4798  C  CZ  . PHE E  1 46  ? 10.211  -31.570 53.186 1.00 21.02  ? 45  PHE E CZ  1 
ATOM   4799  N  N   . HIS E  1 47  ? 8.473   -26.002 53.816 1.00 20.67  ? 46  HIS E N   1 
ATOM   4800  C  CA  . HIS E  1 47  ? 7.682   -25.514 54.932 1.00 21.24  ? 46  HIS E CA  1 
ATOM   4801  C  C   . HIS E  1 47  ? 6.379   -26.284 55.078 1.00 21.65  ? 46  HIS E C   1 
ATOM   4802  O  O   . HIS E  1 47  ? 5.820   -26.806 54.108 1.00 23.31  ? 46  HIS E O   1 
ATOM   4803  C  CB  . HIS E  1 47  ? 7.351   -24.027 54.769 1.00 21.64  ? 46  HIS E CB  1 
ATOM   4804  C  CG  . HIS E  1 47  ? 8.500   -23.218 54.268 1.00 22.67  ? 46  HIS E CG  1 
ATOM   4805  N  ND1 . HIS E  1 47  ? 8.530   -22.703 52.982 1.00 22.20  ? 46  HIS E ND1 1 
ATOM   4806  C  CD2 . HIS E  1 47  ? 9.662   -22.855 54.861 1.00 22.42  ? 46  HIS E CD2 1 
ATOM   4807  C  CE1 . HIS E  1 47  ? 9.664   -22.057 52.814 1.00 23.38  ? 46  HIS E CE1 1 
ATOM   4808  N  NE2 . HIS E  1 47  ? 10.382  -22.137 53.954 1.00 21.86  ? 46  HIS E NE2 1 
ATOM   4809  N  N   . VAL E  1 48  ? 5.901   -26.302 56.326 1.00 21.15  ? 47  VAL E N   1 
ATOM   4810  C  CA  . VAL E  1 48  ? 4.523   -26.670 56.592 1.00 20.65  ? 47  VAL E CA  1 
ATOM   4811  C  C   . VAL E  1 48  ? 3.686   -25.391 56.586 1.00 21.01  ? 47  VAL E C   1 
ATOM   4812  O  O   . VAL E  1 48  ? 3.895   -24.513 57.423 1.00 19.95  ? 47  VAL E O   1 
ATOM   4813  C  CB  . VAL E  1 48  ? 4.377   -27.416 57.929 1.00 19.48  ? 47  VAL E CB  1 
ATOM   4814  C  CG1 . VAL E  1 48  ? 2.950   -27.862 58.147 1.00 19.16  ? 47  VAL E CG1 1 
ATOM   4815  C  CG2 . VAL E  1 48  ? 5.313   -28.606 58.022 1.00 18.94  ? 47  VAL E CG2 1 
ATOM   4816  N  N   . HIS E  1 49  ? 2.740   -25.310 55.643 1.00 22.07  ? 48  HIS E N   1 
ATOM   4817  C  CA  . HIS E  1 49  ? 1.757   -24.237 55.614 1.00 23.54  ? 48  HIS E CA  1 
ATOM   4818  C  C   . HIS E  1 49  ? 0.536   -24.606 56.461 1.00 24.42  ? 48  HIS E C   1 
ATOM   4819  O  O   . HIS E  1 49  ? 0.380   -25.757 56.864 1.00 24.65  ? 48  HIS E O   1 
ATOM   4820  C  CB  . HIS E  1 49  ? 1.397   -23.891 54.169 1.00 24.47  ? 48  HIS E CB  1 
ATOM   4821  C  CG  . HIS E  1 49  ? 2.537   -23.305 53.407 1.00 27.14  ? 48  HIS E CG  1 
ATOM   4822  N  ND1 . HIS E  1 49  ? 2.467   -22.043 52.839 1.00 27.42  ? 48  HIS E ND1 1 
ATOM   4823  C  CD2 . HIS E  1 49  ? 3.772   -23.795 53.121 1.00 29.50  ? 48  HIS E CD2 1 
ATOM   4824  C  CE1 . HIS E  1 49  ? 3.603   -21.779 52.220 1.00 29.35  ? 48  HIS E CE1 1 
ATOM   4825  N  NE2 . HIS E  1 49  ? 4.427   -22.842 52.385 1.00 29.69  ? 48  HIS E NE2 1 
ATOM   4826  N  N   . GLU E  1 50  ? -0.346  -23.622 56.692 1.00 25.10  ? 49  GLU E N   1 
ATOM   4827  C  CA  . GLU E  1 50  ? -1.361  -23.678 57.735 1.00 27.39  ? 49  GLU E CA  1 
ATOM   4828  C  C   . GLU E  1 50  ? -2.493  -24.648 57.410 1.00 27.63  ? 49  GLU E C   1 
ATOM   4829  O  O   . GLU E  1 50  ? -2.942  -25.374 58.292 1.00 25.85  ? 49  GLU E O   1 
ATOM   4830  C  CB  . GLU E  1 50  ? -1.954  -22.294 57.973 1.00 29.71  ? 49  GLU E CB  1 
ATOM   4831  C  CG  . GLU E  1 50  ? -2.713  -22.213 59.284 1.00 32.70  ? 49  GLU E CG  1 
ATOM   4832  C  CD  . GLU E  1 50  ? -3.321  -20.851 59.594 1.00 33.96  ? 49  GLU E CD  1 
ATOM   4833  O  OE1 . GLU E  1 50  ? -2.894  -19.831 58.994 1.00 34.76  ? 49  GLU E OE1 1 
ATOM   4834  O  OE2 . GLU E  1 50  ? -4.231  -20.813 60.435 1.00 32.62  ? 49  GLU E OE2 1 
ATOM   4835  N  N   . PHE E  1 51  ? -2.965  -24.636 56.159 1.00 27.34  ? 50  PHE E N   1 
ATOM   4836  C  CA  . PHE E  1 51  ? -4.205  -25.311 55.816 1.00 25.59  ? 50  PHE E CA  1 
ATOM   4837  C  C   . PHE E  1 51  ? -3.954  -26.517 54.919 1.00 24.25  ? 50  PHE E C   1 
ATOM   4838  O  O   . PHE E  1 51  ? -3.261  -26.414 53.910 1.00 22.98  ? 50  PHE E O   1 
ATOM   4839  C  CB  . PHE E  1 51  ? -5.151  -24.357 55.091 1.00 27.75  ? 50  PHE E CB  1 
ATOM   4840  C  CG  . PHE E  1 51  ? -5.426  -23.096 55.869 1.00 28.68  ? 50  PHE E CG  1 
ATOM   4841  C  CD1 . PHE E  1 51  ? -5.939  -23.167 57.166 1.00 27.19  ? 50  PHE E CD1 1 
ATOM   4842  C  CD2 . PHE E  1 51  ? -5.147  -21.846 55.322 1.00 27.68  ? 50  PHE E CD2 1 
ATOM   4843  C  CE1 . PHE E  1 51  ? -6.171  -22.017 57.903 1.00 25.41  ? 50  PHE E CE1 1 
ATOM   4844  C  CE2 . PHE E  1 51  ? -5.382  -20.697 56.069 1.00 26.57  ? 50  PHE E CE2 1 
ATOM   4845  C  CZ  . PHE E  1 51  ? -5.892  -20.785 57.350 1.00 26.26  ? 50  PHE E CZ  1 
ATOM   4846  N  N   . GLY E  1 52  ? -4.577  -27.643 55.300 1.00 23.70  ? 51  GLY E N   1 
ATOM   4847  C  CA  . GLY E  1 52  ? -4.700  -28.813 54.448 1.00 21.87  ? 51  GLY E CA  1 
ATOM   4848  C  C   . GLY E  1 52  ? -5.788  -28.617 53.414 1.00 20.67  ? 51  GLY E C   1 
ATOM   4849  O  O   . GLY E  1 52  ? -6.720  -29.403 53.309 1.00 20.49  ? 51  GLY E O   1 
ATOM   4850  N  N   . ASP E  1 53  ? -5.645  -27.548 52.636 1.00 20.71  ? 52  ASP E N   1 
ATOM   4851  C  CA  . ASP E  1 53  ? -6.683  -27.148 51.707 1.00 20.31  ? 52  ASP E CA  1 
ATOM   4852  C  C   . ASP E  1 53  ? -6.048  -27.016 50.332 1.00 20.48  ? 52  ASP E C   1 
ATOM   4853  O  O   . ASP E  1 53  ? -5.192  -26.159 50.121 1.00 22.04  ? 52  ASP E O   1 
ATOM   4854  C  CB  . ASP E  1 53  ? -7.336  -25.852 52.182 1.00 19.36  ? 52  ASP E CB  1 
ATOM   4855  C  CG  . ASP E  1 53  ? -8.452  -25.349 51.275 1.00 19.78  ? 52  ASP E CG  1 
ATOM   4856  O  OD1 . ASP E  1 53  ? -8.453  -25.699 50.067 1.00 18.04  ? 52  ASP E OD1 1 
ATOM   4857  O  OD2 . ASP E  1 53  ? -9.359  -24.652 51.793 1.00 21.37  ? 52  ASP E OD2 1 
ATOM   4858  N  N   . ASN E  1 54  ? -6.468  -27.878 49.410 1.00 20.93  ? 53  ASN E N   1 
ATOM   4859  C  CA  . ASN E  1 54  ? -5.863  -27.911 48.093 1.00 23.85  ? 53  ASN E CA  1 
ATOM   4860  C  C   . ASN E  1 54  ? -6.907  -27.505 47.058 1.00 22.91  ? 53  ASN E C   1 
ATOM   4861  O  O   . ASN E  1 54  ? -6.737  -27.748 45.869 1.00 22.00  ? 53  ASN E O   1 
ATOM   4862  C  CB  . ASN E  1 54  ? -5.201  -29.274 47.852 1.00 29.40  ? 53  ASN E CB  1 
ATOM   4863  C  CG  . ASN E  1 54  ? -4.502  -29.398 46.511 1.00 34.38  ? 53  ASN E CG  1 
ATOM   4864  O  OD1 . ASN E  1 54  ? -3.641  -28.573 46.175 1.00 40.96  ? 53  ASN E OD1 1 
ATOM   4865  N  ND2 . ASN E  1 54  ? -4.835  -30.435 45.755 1.00 33.94  ? 53  ASN E ND2 1 
ATOM   4866  N  N   . THR E  1 55  ? -7.984  -26.843 47.513 1.00 23.50  ? 54  THR E N   1 
ATOM   4867  C  CA  . THR E  1 55  ? -9.122  -26.550 46.650 1.00 23.68  ? 54  THR E CA  1 
ATOM   4868  C  C   . THR E  1 55  ? -8.706  -25.689 45.465 1.00 24.57  ? 54  THR E C   1 
ATOM   4869  O  O   . THR E  1 55  ? -9.285  -25.811 44.393 1.00 26.62  ? 54  THR E O   1 
ATOM   4870  C  CB  . THR E  1 55  ? -10.272 -25.869 47.403 1.00 22.40  ? 54  THR E CB  1 
ATOM   4871  O  OG1 . THR E  1 55  ? -9.756  -24.674 47.976 1.00 20.97  ? 54  THR E OG1 1 
ATOM   4872  C  CG2 . THR E  1 55  ? -10.868 -26.733 48.493 1.00 23.21  ? 54  THR E CG2 1 
ATOM   4873  N  N   . ALA E  1 56  ? -7.712  -24.818 45.668 1.00 25.53  ? 55  ALA E N   1 
ATOM   4874  C  CA  . ALA E  1 56  ? -7.254  -23.926 44.620 1.00 26.48  ? 55  ALA E CA  1 
ATOM   4875  C  C   . ALA E  1 56  ? -5.770  -24.162 44.382 1.00 26.34  ? 55  ALA E C   1 
ATOM   4876  O  O   . ALA E  1 56  ? -5.010  -23.212 44.256 1.00 30.55  ? 55  ALA E O   1 
ATOM   4877  C  CB  . ALA E  1 56  ? -7.535  -22.499 45.033 1.00 28.06  ? 55  ALA E CB  1 
ATOM   4878  N  N   . GLY E  1 57  ? -5.362  -25.431 44.344 1.00 25.02  ? 56  GLY E N   1 
ATOM   4879  C  CA  . GLY E  1 57  ? -3.956  -25.784 44.234 1.00 25.83  ? 56  GLY E CA  1 
ATOM   4880  C  C   . GLY E  1 57  ? -3.200  -25.485 45.529 1.00 28.51  ? 56  GLY E C   1 
ATOM   4881  O  O   . GLY E  1 57  ? -3.813  -25.407 46.605 1.00 27.63  ? 56  GLY E O   1 
ATOM   4882  N  N   . CYS E  1 58  ? -1.879  -25.283 45.401 1.00 27.64  ? 57  CYS E N   1 
ATOM   4883  C  CA  . CYS E  1 58  ? -1.045  -25.085 46.571 1.00 24.98  ? 57  CYS E CA  1 
ATOM   4884  C  C   . CYS E  1 58  ? -1.336  -23.759 47.261 1.00 24.67  ? 57  CYS E C   1 
ATOM   4885  O  O   . CYS E  1 58  ? -1.093  -23.622 48.456 1.00 23.40  ? 57  CYS E O   1 
ATOM   4886  C  CB  . CYS E  1 58  ? 0.435   -25.185 46.218 1.00 26.34  ? 57  CYS E CB  1 
ATOM   4887  S  SG  . CYS E  1 58  ? 0.915   -26.863 45.725 1.00 33.15  ? 57  CYS E SG  1 
ATOM   4888  N  N   . THR E  1 59  ? -1.898  -22.804 46.501 1.00 24.07  ? 58  THR E N   1 
ATOM   4889  C  CA  . THR E  1 59  ? -2.166  -21.463 47.006 1.00 22.64  ? 58  THR E CA  1 
ATOM   4890  C  C   . THR E  1 59  ? -3.051  -21.526 48.240 1.00 22.66  ? 58  THR E C   1 
ATOM   4891  O  O   . THR E  1 59  ? -2.864  -20.742 49.175 1.00 25.04  ? 58  THR E O   1 
ATOM   4892  C  CB  . THR E  1 59  ? -2.957  -20.621 46.001 1.00 20.89  ? 58  THR E CB  1 
ATOM   4893  O  OG1 . THR E  1 59  ? -2.296  -20.736 44.743 1.00 20.77  ? 58  THR E OG1 1 
ATOM   4894  C  CG2 . THR E  1 59  ? -3.071  -19.171 46.421 1.00 20.00  ? 58  THR E CG2 1 
ATOM   4895  N  N   . SER E  1 60  ? -4.032  -22.437 48.221 1.00 22.00  ? 59  SER E N   1 
ATOM   4896  C  CA  . SER E  1 60  ? -5.072  -22.378 49.233 1.00 23.15  ? 59  SER E CA  1 
ATOM   4897  C  C   . SER E  1 60  ? -4.573  -22.959 50.558 1.00 22.61  ? 59  SER E C   1 
ATOM   4898  O  O   . SER E  1 60  ? -5.315  -22.984 51.547 1.00 21.64  ? 59  SER E O   1 
ATOM   4899  C  CB  . SER E  1 60  ? -6.380  -22.963 48.743 1.00 23.10  ? 59  SER E CB  1 
ATOM   4900  O  OG  . SER E  1 60  ? -6.192  -24.277 48.246 1.00 23.51  ? 59  SER E OG  1 
ATOM   4901  N  N   . ALA E  1 61  ? -3.287  -23.352 50.581 1.00 21.57  ? 60  ALA E N   1 
ATOM   4902  C  CA  . ALA E  1 61  ? -2.647  -23.883 51.773 1.00 20.62  ? 60  ALA E CA  1 
ATOM   4903  C  C   . ALA E  1 61  ? -2.400  -22.769 52.793 1.00 20.51  ? 60  ALA E C   1 
ATOM   4904  O  O   . ALA E  1 61  ? -2.179  -23.044 53.972 1.00 19.57  ? 60  ALA E O   1 
ATOM   4905  C  CB  . ALA E  1 61  ? -1.360  -24.557 51.395 1.00 18.26  ? 60  ALA E CB  1 
ATOM   4906  N  N   . GLY E  1 62  ? -2.436  -21.520 52.312 1.00 21.48  ? 61  GLY E N   1 
ATOM   4907  C  CA  . GLY E  1 62  ? -2.234  -20.356 53.151 1.00 23.47  ? 61  GLY E CA  1 
ATOM   4908  C  C   . GLY E  1 62  ? -0.758  -20.127 53.497 1.00 25.99  ? 61  GLY E C   1 
ATOM   4909  O  O   . GLY E  1 62  ? 0.133   -20.629 52.805 1.00 25.64  ? 61  GLY E O   1 
ATOM   4910  N  N   . PRO E  1 63  ? -0.469  -19.380 54.599 1.00 25.83  ? 62  PRO E N   1 
ATOM   4911  C  CA  . PRO E  1 63  ? 0.907   -19.012 54.954 1.00 24.49  ? 62  PRO E CA  1 
ATOM   4912  C  C   . PRO E  1 63  ? 1.635   -20.135 55.692 1.00 23.42  ? 62  PRO E C   1 
ATOM   4913  O  O   . PRO E  1 63  ? 1.048   -21.183 55.945 1.00 24.47  ? 62  PRO E O   1 
ATOM   4914  C  CB  . PRO E  1 63  ? 0.667   -17.843 55.921 1.00 24.78  ? 62  PRO E CB  1 
ATOM   4915  C  CG  . PRO E  1 63  ? -0.609  -18.238 56.642 1.00 25.60  ? 62  PRO E CG  1 
ATOM   4916  C  CD  . PRO E  1 63  ? -1.466  -18.909 55.587 1.00 23.81  ? 62  PRO E CD  1 
ATOM   4917  N  N   . HIS E  1 64  ? 2.908   -19.913 56.043 1.00 23.22  ? 63  HIS E N   1 
ATOM   4918  C  CA  . HIS E  1 64  ? 3.619   -20.870 56.878 1.00 23.37  ? 63  HIS E CA  1 
ATOM   4919  C  C   . HIS E  1 64  ? 2.823   -21.087 58.163 1.00 23.12  ? 63  HIS E C   1 
ATOM   4920  O  O   . HIS E  1 64  ? 2.344   -20.120 58.742 1.00 24.53  ? 63  HIS E O   1 
ATOM   4921  C  CB  . HIS E  1 64  ? 5.043   -20.393 57.209 1.00 22.36  ? 63  HIS E CB  1 
ATOM   4922  C  CG  . HIS E  1 64  ? 5.943   -20.236 56.031 1.00 21.57  ? 63  HIS E CG  1 
ATOM   4923  N  ND1 . HIS E  1 64  ? 7.197   -19.655 56.149 1.00 20.69  ? 63  HIS E ND1 1 
ATOM   4924  C  CD2 . HIS E  1 64  ? 5.780   -20.556 54.725 1.00 21.56  ? 63  HIS E CD2 1 
ATOM   4925  C  CE1 . HIS E  1 64  ? 7.780   -19.636 54.974 1.00 20.77  ? 63  HIS E CE1 1 
ATOM   4926  N  NE2 . HIS E  1 64  ? 6.929   -20.186 54.075 1.00 22.24  ? 63  HIS E NE2 1 
ATOM   4927  N  N   . PHE E  1 65  ? 2.707   -22.345 58.599 1.00 22.04  ? 64  PHE E N   1 
ATOM   4928  C  CA  . PHE E  1 65  ? 2.039   -22.678 59.846 1.00 22.61  ? 64  PHE E CA  1 
ATOM   4929  C  C   . PHE E  1 65  ? 2.667   -21.910 61.010 1.00 23.81  ? 64  PHE E C   1 
ATOM   4930  O  O   . PHE E  1 65  ? 3.827   -22.124 61.339 1.00 23.58  ? 64  PHE E O   1 
ATOM   4931  C  CB  . PHE E  1 65  ? 2.039   -24.195 60.070 1.00 22.30  ? 64  PHE E CB  1 
ATOM   4932  C  CG  . PHE E  1 65  ? 1.360   -24.647 61.341 1.00 22.20  ? 64  PHE E CG  1 
ATOM   4933  C  CD1 . PHE E  1 65  ? 0.151   -24.086 61.745 1.00 22.07  ? 64  PHE E CD1 1 
ATOM   4934  C  CD2 . PHE E  1 65  ? 1.917   -25.646 62.131 1.00 21.40  ? 64  PHE E CD2 1 
ATOM   4935  C  CE1 . PHE E  1 65  ? -0.472  -24.507 62.913 1.00 21.94  ? 64  PHE E CE1 1 
ATOM   4936  C  CE2 . PHE E  1 65  ? 1.286   -26.068 63.295 1.00 20.58  ? 64  PHE E CE2 1 
ATOM   4937  C  CZ  . PHE E  1 65  ? 0.097   -25.502 63.685 1.00 21.11  ? 64  PHE E CZ  1 
ATOM   4938  N  N   . ASN E  1 66  ? 1.880   -21.035 61.648 1.00 25.61  ? 65  ASN E N   1 
ATOM   4939  C  CA  . ASN E  1 66  ? 2.464   -20.070 62.560 1.00 26.98  ? 65  ASN E CA  1 
ATOM   4940  C  C   . ASN E  1 66  ? 1.623   -19.921 63.833 1.00 28.58  ? 65  ASN E C   1 
ATOM   4941  O  O   . ASN E  1 66  ? 1.239   -18.814 64.196 1.00 28.00  ? 65  ASN E O   1 
ATOM   4942  C  CB  . ASN E  1 66  ? 2.726   -18.739 61.846 1.00 26.35  ? 65  ASN E CB  1 
ATOM   4943  C  CG  . ASN E  1 66  ? 3.456   -17.740 62.721 1.00 27.07  ? 65  ASN E CG  1 
ATOM   4944  O  OD1 . ASN E  1 66  ? 4.106   -18.103 63.705 1.00 26.82  ? 65  ASN E OD1 1 
ATOM   4945  N  ND2 . ASN E  1 66  ? 3.349   -16.472 62.374 1.00 26.96  ? 65  ASN E ND2 1 
ATOM   4946  N  N   . PRO E  1 67  ? 1.360   -20.995 64.611 1.00 31.07  ? 66  PRO E N   1 
ATOM   4947  C  CA  . PRO E  1 67  ? 0.453   -20.892 65.757 1.00 30.65  ? 66  PRO E CA  1 
ATOM   4948  C  C   . PRO E  1 67  ? 0.917   -19.957 66.872 1.00 32.32  ? 66  PRO E C   1 
ATOM   4949  O  O   . PRO E  1 67  ? 0.100   -19.533 67.680 1.00 34.77  ? 66  PRO E O   1 
ATOM   4950  C  CB  . PRO E  1 67  ? 0.365   -22.319 66.311 1.00 30.39  ? 66  PRO E CB  1 
ATOM   4951  C  CG  . PRO E  1 67  ? 1.621   -22.992 65.804 1.00 32.11  ? 66  PRO E CG  1 
ATOM   4952  C  CD  . PRO E  1 67  ? 1.961   -22.330 64.480 1.00 30.94  ? 66  PRO E CD  1 
ATOM   4953  N  N   . LEU E  1 68  ? 2.215   -19.630 66.909 1.00 35.61  ? 67  LEU E N   1 
ATOM   4954  C  CA  . LEU E  1 68  ? 2.741   -18.817 67.996 1.00 36.38  ? 67  LEU E CA  1 
ATOM   4955  C  C   . LEU E  1 68  ? 2.949   -17.361 67.568 1.00 36.40  ? 67  LEU E C   1 
ATOM   4956  O  O   . LEU E  1 68  ? 3.502   -16.581 68.338 1.00 36.14  ? 67  LEU E O   1 
ATOM   4957  C  CB  . LEU E  1 68  ? 4.048   -19.436 68.502 1.00 35.48  ? 67  LEU E CB  1 
ATOM   4958  C  CG  . LEU E  1 68  ? 3.913   -20.734 69.290 1.00 37.89  ? 67  LEU E CG  1 
ATOM   4959  C  CD1 . LEU E  1 68  ? 5.257   -21.124 69.929 1.00 40.10  ? 67  LEU E CD1 1 
ATOM   4960  C  CD2 . LEU E  1 68  ? 2.846   -20.642 70.376 1.00 36.59  ? 67  LEU E CD2 1 
ATOM   4961  N  N   . SER E  1 69  ? 2.529   -17.013 66.343 1.00 35.17  ? 68  SER E N   1 
ATOM   4962  C  CA  . SER E  1 69  ? 2.585   -15.655 65.823 1.00 36.63  ? 68  SER E CA  1 
ATOM   4963  C  C   . SER E  1 69  ? 3.990   -15.064 65.892 1.00 37.72  ? 68  SER E C   1 
ATOM   4964  O  O   . SER E  1 69  ? 4.155   -13.972 66.431 1.00 39.55  ? 68  SER E O   1 
ATOM   4965  C  CB  . SER E  1 69  ? 1.626   -14.754 66.549 1.00 37.61  ? 68  SER E CB  1 
ATOM   4966  O  OG  . SER E  1 69  ? 0.292   -15.131 66.307 1.00 37.18  ? 68  SER E OG  1 
ATOM   4967  N  N   . ARG E  1 70  ? 4.985   -15.770 65.342 1.00 36.75  ? 69  ARG E N   1 
ATOM   4968  C  CA  . ARG E  1 70  ? 6.352   -15.268 65.300 1.00 33.89  ? 69  ARG E CA  1 
ATOM   4969  C  C   . ARG E  1 70  ? 6.711   -14.908 63.862 1.00 32.75  ? 69  ARG E C   1 
ATOM   4970  O  O   . ARG E  1 70  ? 5.930   -15.159 62.940 1.00 30.38  ? 69  ARG E O   1 
ATOM   4971  C  CB  . ARG E  1 70  ? 7.339   -16.301 65.856 1.00 35.55  ? 69  ARG E CB  1 
ATOM   4972  C  CG  . ARG E  1 70  ? 6.976   -16.861 67.220 1.00 42.03  ? 69  ARG E CG  1 
ATOM   4973  C  CD  . ARG E  1 70  ? 7.560   -16.107 68.395 1.00 48.46  ? 69  ARG E CD  1 
ATOM   4974  N  NE  . ARG E  1 70  ? 7.430   -16.885 69.611 1.00 63.61  ? 69  ARG E NE  1 
ATOM   4975  C  CZ  . ARG E  1 70  ? 8.271   -17.844 70.027 1.00 73.28  ? 69  ARG E CZ  1 
ATOM   4976  N  NH1 . ARG E  1 70  ? 9.344   -18.161 69.310 1.00 73.94  ? 69  ARG E NH1 1 
ATOM   4977  N  NH2 . ARG E  1 70  ? 8.048   -18.464 71.190 1.00 77.64  ? 69  ARG E NH2 1 
ATOM   4978  N  N   . LYS E  1 71  ? 7.901   -14.307 63.689 1.00 30.63  ? 70  LYS E N   1 
ATOM   4979  C  CA  . LYS E  1 71  ? 8.410   -13.972 62.364 1.00 27.05  ? 70  LYS E CA  1 
ATOM   4980  C  C   . LYS E  1 71  ? 9.136   -15.197 61.796 1.00 25.31  ? 70  LYS E C   1 
ATOM   4981  O  O   . LYS E  1 71  ? 9.512   -16.103 62.544 1.00 24.24  ? 70  LYS E O   1 
ATOM   4982  C  CB  . LYS E  1 71  ? 9.232   -12.677 62.406 1.00 25.31  ? 70  LYS E CB  1 
ATOM   4983  C  CG  . LYS E  1 71  ? 8.526   -11.479 63.022 0.20 24.81  ? 70  LYS E CG  1 
ATOM   4984  C  CD  . LYS E  1 71  ? 9.313   -10.208 62.834 0.20 24.15  ? 70  LYS E CD  1 
ATOM   4985  C  CE  . LYS E  1 71  ? 8.962   -9.141  63.846 0.20 23.61  ? 70  LYS E CE  1 
ATOM   4986  N  NZ  . LYS E  1 71  ? 10.034  -8.124  63.946 0.20 22.94  ? 70  LYS E NZ  1 
ATOM   4987  N  N   . HIS E  1 72  ? 9.308   -15.227 60.469 1.00 23.58  ? 71  HIS E N   1 
ATOM   4988  C  CA  . HIS E  1 72  ? 9.911   -16.358 59.786 1.00 23.56  ? 71  HIS E CA  1 
ATOM   4989  C  C   . HIS E  1 72  ? 11.392  -16.477 60.150 1.00 26.37  ? 71  HIS E C   1 
ATOM   4990  O  O   . HIS E  1 72  ? 12.095  -15.475 60.246 1.00 28.18  ? 71  HIS E O   1 
ATOM   4991  C  CB  . HIS E  1 72  ? 9.694   -16.216 58.276 1.00 22.04  ? 71  HIS E CB  1 
ATOM   4992  C  CG  . HIS E  1 72  ? 10.380  -17.264 57.473 1.00 22.05  ? 71  HIS E CG  1 
ATOM   4993  N  ND1 . HIS E  1 72  ? 9.830   -18.512 57.223 1.00 22.30  ? 71  HIS E ND1 1 
ATOM   4994  C  CD2 . HIS E  1 72  ? 11.577  -17.254 56.858 1.00 22.64  ? 71  HIS E CD2 1 
ATOM   4995  C  CE1 . HIS E  1 72  ? 10.664  -19.218 56.495 1.00 22.47  ? 71  HIS E CE1 1 
ATOM   4996  N  NE2 . HIS E  1 72  ? 11.741  -18.476 56.263 1.00 23.06  ? 71  HIS E NE2 1 
ATOM   4997  N  N   . GLY E  1 73  ? 11.861  -17.711 60.349 1.00 27.25  ? 72  GLY E N   1 
ATOM   4998  C  CA  . GLY E  1 73  ? 13.269  -17.973 60.603 1.00 27.79  ? 72  GLY E CA  1 
ATOM   4999  C  C   . GLY E  1 73  ? 13.736  -19.249 59.906 1.00 28.11  ? 72  GLY E C   1 
ATOM   5000  O  O   . GLY E  1 73  ? 12.969  -19.868 59.169 1.00 31.50  ? 72  GLY E O   1 
ATOM   5001  N  N   . GLY E  1 74  ? 15.010  -19.600 60.116 1.00 27.39  ? 73  GLY E N   1 
ATOM   5002  C  CA  . GLY E  1 74  ? 15.517  -20.929 59.812 1.00 24.77  ? 73  GLY E CA  1 
ATOM   5003  C  C   . GLY E  1 74  ? 15.140  -21.901 60.922 1.00 23.49  ? 73  GLY E C   1 
ATOM   5004  O  O   . GLY E  1 74  ? 14.817  -21.472 62.026 1.00 21.64  ? 73  GLY E O   1 
ATOM   5005  N  N   . PRO E  1 75  ? 15.149  -23.232 60.673 1.00 23.68  ? 74  PRO E N   1 
ATOM   5006  C  CA  . PRO E  1 75  ? 14.716  -24.200 61.684 1.00 24.13  ? 74  PRO E CA  1 
ATOM   5007  C  C   . PRO E  1 75  ? 15.472  -24.066 63.004 1.00 25.81  ? 74  PRO E C   1 
ATOM   5008  O  O   . PRO E  1 75  ? 14.919  -24.359 64.053 1.00 25.54  ? 74  PRO E O   1 
ATOM   5009  C  CB  . PRO E  1 75  ? 14.962  -25.571 61.046 1.00 22.80  ? 74  PRO E CB  1 
ATOM   5010  C  CG  . PRO E  1 75  ? 15.861  -25.296 59.858 1.00 22.10  ? 74  PRO E CG  1 
ATOM   5011  C  CD  . PRO E  1 75  ? 15.556  -23.881 59.422 1.00 22.32  ? 74  PRO E CD  1 
ATOM   5012  N  N   . LYS E  1 76  ? 16.701  -23.565 62.936 1.00 29.15  ? 75  LYS E N   1 
ATOM   5013  C  CA  . LYS E  1 76  ? 17.594  -23.526 64.080 1.00 29.69  ? 75  LYS E CA  1 
ATOM   5014  C  C   . LYS E  1 76  ? 17.350  -22.286 64.936 1.00 28.94  ? 75  LYS E C   1 
ATOM   5015  O  O   . LYS E  1 76  ? 17.834  -22.228 66.056 1.00 29.77  ? 75  LYS E O   1 
ATOM   5016  C  CB  . LYS E  1 76  ? 19.054  -23.623 63.626 1.00 32.47  ? 75  LYS E CB  1 
ATOM   5017  C  CG  . LYS E  1 76  ? 19.507  -24.992 63.149 1.00 39.90  ? 75  LYS E CG  1 
ATOM   5018  C  CD  . LYS E  1 76  ? 20.908  -24.997 62.612 1.00 45.48  ? 75  LYS E CD  1 
ATOM   5019  C  CE  . LYS E  1 76  ? 21.937  -25.204 63.708 1.00 50.46  ? 75  LYS E CE  1 
ATOM   5020  N  NZ  . LYS E  1 76  ? 23.232  -24.592 63.345 1.00 49.88  ? 75  LYS E NZ  1 
ATOM   5021  N  N   . ASP E  1 77  ? 16.578  -21.307 64.426 1.00 28.58  ? 76  ASP E N   1 
ATOM   5022  C  CA  . ASP E  1 77  ? 16.332  -20.036 65.095 1.00 26.65  ? 76  ASP E CA  1 
ATOM   5023  C  C   . ASP E  1 77  ? 15.300  -20.221 66.205 1.00 26.45  ? 76  ASP E C   1 
ATOM   5024  O  O   . ASP E  1 77  ? 14.429  -21.069 66.110 1.00 26.37  ? 76  ASP E O   1 
ATOM   5025  C  CB  . ASP E  1 77  ? 15.887  -18.969 64.090 1.00 24.17  ? 76  ASP E CB  1 
ATOM   5026  C  CG  . ASP E  1 77  ? 17.005  -18.532 63.169 1.00 24.63  ? 76  ASP E CG  1 
ATOM   5027  O  OD1 . ASP E  1 77  ? 18.149  -18.529 63.648 1.00 26.23  ? 76  ASP E OD1 1 
ATOM   5028  O  OD2 . ASP E  1 77  ? 16.744  -18.210 61.984 1.00 24.20  ? 76  ASP E OD2 1 
ATOM   5029  N  N   . GLU E  1 78  ? 15.391  -19.407 67.248 1.00 29.49  ? 77  GLU E N   1 
ATOM   5030  C  CA  . GLU E  1 78  ? 14.332  -19.413 68.243 1.00 32.12  ? 77  GLU E CA  1 
ATOM   5031  C  C   . GLU E  1 78  ? 13.126  -18.666 67.683 1.00 32.69  ? 77  GLU E C   1 
ATOM   5032  O  O   . GLU E  1 78  ? 11.983  -19.062 67.906 1.00 32.53  ? 77  GLU E O   1 
ATOM   5033  C  CB  . GLU E  1 78  ? 14.785  -18.917 69.615 1.00 38.86  ? 77  GLU E CB  1 
ATOM   5034  C  CG  . GLU E  1 78  ? 13.893  -19.529 70.694 1.00 50.26  ? 77  GLU E CG  1 
ATOM   5035  C  CD  . GLU E  1 78  ? 13.343  -18.587 71.745 1.00 58.41  ? 77  GLU E CD  1 
ATOM   5036  O  OE1 . GLU E  1 78  ? 14.186  -17.893 72.362 1.00 65.03  ? 77  GLU E OE1 1 
ATOM   5037  O  OE2 . GLU E  1 78  ? 12.083  -18.574 71.972 1.00 57.78  ? 77  GLU E OE2 1 
ATOM   5038  N  N   . GLU E  1 79  ? 13.390  -17.597 66.920 1.00 32.49  ? 78  GLU E N   1 
ATOM   5039  C  CA  . GLU E  1 79  ? 12.355  -16.837 66.232 1.00 30.16  ? 78  GLU E CA  1 
ATOM   5040  C  C   . GLU E  1 79  ? 12.086  -17.493 64.870 1.00 29.83  ? 78  GLU E C   1 
ATOM   5041  O  O   . GLU E  1 79  ? 12.771  -17.229 63.874 1.00 29.25  ? 78  GLU E O   1 
ATOM   5042  C  CB  . GLU E  1 79  ? 12.744  -15.355 66.196 1.00 30.39  ? 78  GLU E CB  1 
ATOM   5043  C  CG  . GLU E  1 79  ? 11.692  -14.393 65.649 1.00 34.16  ? 78  GLU E CG  1 
ATOM   5044  C  CD  . GLU E  1 79  ? 10.440  -14.128 66.480 1.00 38.41  ? 78  GLU E CD  1 
ATOM   5045  O  OE1 . GLU E  1 79  ? 10.372  -14.605 67.652 1.00 37.64  ? 78  GLU E OE1 1 
ATOM   5046  O  OE2 . GLU E  1 79  ? 9.510   -13.455 65.949 1.00 39.74  ? 78  GLU E OE2 1 
ATOM   5047  N  N   . ARG E  1 80  ? 11.080  -18.382 64.848 1.00 28.23  ? 79  ARG E N   1 
ATOM   5048  C  CA  . ARG E  1 80  ? 10.650  -19.061 63.636 1.00 25.49  ? 79  ARG E CA  1 
ATOM   5049  C  C   . ARG E  1 80  ? 9.163   -19.394 63.702 1.00 25.11  ? 79  ARG E C   1 
ATOM   5050  O  O   . ARG E  1 80  ? 8.561   -19.448 64.777 1.00 24.79  ? 79  ARG E O   1 
ATOM   5051  C  CB  . ARG E  1 80  ? 11.418  -20.370 63.440 1.00 23.83  ? 79  ARG E CB  1 
ATOM   5052  C  CG  . ARG E  1 80  ? 11.295  -21.349 64.594 1.00 21.15  ? 79  ARG E CG  1 
ATOM   5053  C  CD  . ARG E  1 80  ? 11.934  -22.672 64.241 1.00 20.39  ? 79  ARG E CD  1 
ATOM   5054  N  NE  . ARG E  1 80  ? 10.983  -23.580 63.623 1.00 20.06  ? 79  ARG E NE  1 
ATOM   5055  C  CZ  . ARG E  1 80  ? 11.174  -24.886 63.450 1.00 20.16  ? 79  ARG E CZ  1 
ATOM   5056  N  NH1 . ARG E  1 80  ? 12.303  -25.452 63.836 1.00 19.84  ? 79  ARG E NH1 1 
ATOM   5057  N  NH2 . ARG E  1 80  ? 10.233  -25.627 62.891 1.00 19.78  ? 79  ARG E NH2 1 
ATOM   5058  N  N   . HIS E  1 81  ? 8.586   -19.623 62.515 1.00 24.07  ? 80  HIS E N   1 
ATOM   5059  C  CA  . HIS E  1 81  ? 7.301   -20.278 62.379 1.00 22.60  ? 80  HIS E CA  1 
ATOM   5060  C  C   . HIS E  1 81  ? 7.476   -21.751 62.729 1.00 22.61  ? 80  HIS E C   1 
ATOM   5061  O  O   . HIS E  1 81  ? 8.514   -22.338 62.430 1.00 23.94  ? 80  HIS E O   1 
ATOM   5062  C  CB  . HIS E  1 81  ? 6.825   -20.167 60.931 1.00 21.66  ? 80  HIS E CB  1 
ATOM   5063  C  CG  . HIS E  1 81  ? 6.653   -18.769 60.464 1.00 21.76  ? 80  HIS E CG  1 
ATOM   5064  N  ND1 . HIS E  1 81  ? 6.914   -18.386 59.161 1.00 21.88  ? 80  HIS E ND1 1 
ATOM   5065  C  CD2 . HIS E  1 81  ? 6.237   -17.661 61.121 1.00 22.41  ? 80  HIS E CD2 1 
ATOM   5066  C  CE1 . HIS E  1 81  ? 6.652   -17.100 59.028 1.00 22.08  ? 80  HIS E CE1 1 
ATOM   5067  N  NE2 . HIS E  1 81  ? 6.247   -16.627 60.221 1.00 22.76  ? 80  HIS E NE2 1 
ATOM   5068  N  N   . VAL E  1 82  ? 6.449   -22.348 63.336 1.00 21.76  ? 81  VAL E N   1 
ATOM   5069  C  CA  . VAL E  1 82  ? 6.482   -23.777 63.597 1.00 22.19  ? 81  VAL E CA  1 
ATOM   5070  C  C   . VAL E  1 82  ? 6.766   -24.525 62.297 1.00 21.50  ? 81  VAL E C   1 
ATOM   5071  O  O   . VAL E  1 82  ? 7.522   -25.485 62.299 1.00 20.75  ? 81  VAL E O   1 
ATOM   5072  C  CB  . VAL E  1 82  ? 5.205   -24.278 64.297 1.00 23.16  ? 81  VAL E CB  1 
ATOM   5073  C  CG1 . VAL E  1 82  ? 5.089   -25.790 64.243 1.00 22.98  ? 81  VAL E CG1 1 
ATOM   5074  C  CG2 . VAL E  1 82  ? 5.146   -23.791 65.741 1.00 23.84  ? 81  VAL E CG2 1 
ATOM   5075  N  N   . GLY E  1 83  ? 6.205   -24.055 61.183 1.00 21.74  ? 82  GLY E N   1 
ATOM   5076  C  CA  . GLY E  1 83  ? 6.324   -24.780 59.928 1.00 22.27  ? 82  GLY E CA  1 
ATOM   5077  C  C   . GLY E  1 83  ? 7.656   -24.554 59.206 1.00 21.82  ? 82  GLY E C   1 
ATOM   5078  O  O   . GLY E  1 83  ? 7.830   -25.065 58.096 1.00 21.14  ? 82  GLY E O   1 
ATOM   5079  N  N   . ASP E  1 84  ? 8.574   -23.800 59.836 1.00 20.76  ? 83  ASP E N   1 
ATOM   5080  C  CA  . ASP E  1 84  ? 9.812   -23.368 59.197 1.00 19.86  ? 83  ASP E CA  1 
ATOM   5081  C  C   . ASP E  1 84  ? 10.859  -24.481 59.245 1.00 20.51  ? 83  ASP E C   1 
ATOM   5082  O  O   . ASP E  1 84  ? 11.570  -24.636 60.233 1.00 22.40  ? 83  ASP E O   1 
ATOM   5083  C  CB  . ASP E  1 84  ? 10.326  -22.060 59.806 1.00 19.05  ? 83  ASP E CB  1 
ATOM   5084  C  CG  . ASP E  1 84  ? 9.557   -20.826 59.379 1.00 20.11  ? 83  ASP E CG  1 
ATOM   5085  O  OD1 . ASP E  1 84  ? 8.825   -20.903 58.378 1.00 21.20  ? 83  ASP E OD1 1 
ATOM   5086  O  OD2 . ASP E  1 84  ? 9.705   -19.782 60.049 1.00 21.41  ? 83  ASP E OD2 1 
ATOM   5087  N  N   . LEU E  1 85  ? 10.976  -25.247 58.155 1.00 20.27  ? 84  LEU E N   1 
ATOM   5088  C  CA  . LEU E  1 85  ? 11.868  -26.395 58.134 1.00 19.40  ? 84  LEU E CA  1 
ATOM   5089  C  C   . LEU E  1 85  ? 13.112  -26.109 57.295 1.00 19.28  ? 84  LEU E C   1 
ATOM   5090  O  O   . LEU E  1 85  ? 13.882  -27.026 57.003 1.00 19.09  ? 84  LEU E O   1 
ATOM   5091  C  CB  . LEU E  1 85  ? 11.118  -27.620 57.600 1.00 19.83  ? 84  LEU E CB  1 
ATOM   5092  C  CG  . LEU E  1 85  ? 10.074  -28.239 58.532 1.00 19.79  ? 84  LEU E CG  1 
ATOM   5093  C  CD1 . LEU E  1 85  ? 9.550   -29.545 57.938 1.00 18.87  ? 84  LEU E CD1 1 
ATOM   5094  C  CD2 . LEU E  1 85  ? 10.656  -28.523 59.908 1.00 18.85  ? 84  LEU E CD2 1 
ATOM   5095  N  N   . GLY E  1 86  ? 13.312  -24.845 56.903 1.00 18.04  ? 85  GLY E N   1 
ATOM   5096  C  CA  . GLY E  1 86  ? 14.533  -24.463 56.211 1.00 18.02  ? 85  GLY E CA  1 
ATOM   5097  C  C   . GLY E  1 86  ? 14.550  -24.882 54.751 1.00 17.44  ? 85  GLY E C   1 
ATOM   5098  O  O   . GLY E  1 86  ? 13.538  -24.751 54.057 1.00 18.29  ? 85  GLY E O   1 
ATOM   5099  N  N   . ASN E  1 87  ? 15.715  -25.393 54.301 1.00 17.42  ? 86  ASN E N   1 
ATOM   5100  C  CA  . ASN E  1 87  ? 15.882  -25.757 52.899 1.00 17.76  ? 86  ASN E CA  1 
ATOM   5101  C  C   . ASN E  1 87  ? 16.123  -27.255 52.741 1.00 17.69  ? 86  ASN E C   1 
ATOM   5102  O  O   . ASN E  1 87  ? 16.555  -27.949 53.663 1.00 17.45  ? 86  ASN E O   1 
ATOM   5103  C  CB  . ASN E  1 87  ? 17.036  -25.012 52.243 1.00 18.43  ? 86  ASN E CB  1 
ATOM   5104  C  CG  . ASN E  1 87  ? 16.759  -23.532 52.123 1.00 19.57  ? 86  ASN E CG  1 
ATOM   5105  O  OD1 . ASN E  1 87  ? 15.979  -23.098 51.282 1.00 20.62  ? 86  ASN E OD1 1 
ATOM   5106  N  ND2 . ASN E  1 87  ? 17.381  -22.751 52.979 1.00 19.49  ? 86  ASN E ND2 1 
ATOM   5107  N  N   . VAL E  1 88  ? 15.815  -27.727 51.535 1.00 17.20  ? 87  VAL E N   1 
ATOM   5108  C  CA  . VAL E  1 88  ? 16.255  -29.035 51.088 1.00 17.08  ? 87  VAL E CA  1 
ATOM   5109  C  C   . VAL E  1 88  ? 17.147  -28.790 49.869 1.00 18.18  ? 87  VAL E C   1 
ATOM   5110  O  O   . VAL E  1 88  ? 17.055  -27.741 49.233 1.00 17.47  ? 87  VAL E O   1 
ATOM   5111  C  CB  . VAL E  1 88  ? 15.067  -29.978 50.803 1.00 15.60  ? 87  VAL E CB  1 
ATOM   5112  C  CG1 . VAL E  1 88  ? 14.219  -30.197 52.036 1.00 15.20  ? 87  VAL E CG1 1 
ATOM   5113  C  CG2 . VAL E  1 88  ? 14.224  -29.532 49.621 1.00 13.96  ? 87  VAL E CG2 1 
ATOM   5114  N  N   . THR E  1 89  ? 18.030  -29.752 49.577 1.00 18.67  ? 88  THR E N   1 
ATOM   5115  C  CA  . THR E  1 89  ? 19.013  -29.545 48.535 1.00 20.63  ? 88  THR E CA  1 
ATOM   5116  C  C   . THR E  1 89  ? 18.794  -30.551 47.415 1.00 22.17  ? 88  THR E C   1 
ATOM   5117  O  O   . THR E  1 89  ? 18.802  -31.758 47.649 1.00 22.81  ? 88  THR E O   1 
ATOM   5118  C  CB  . THR E  1 89  ? 20.432  -29.711 49.091 1.00 21.37  ? 88  THR E CB  1 
ATOM   5119  O  OG1 . THR E  1 89  ? 20.611  -28.862 50.232 1.00 21.70  ? 88  THR E OG1 1 
ATOM   5120  C  CG2 . THR E  1 89  ? 21.505  -29.483 48.042 1.00 20.59  ? 88  THR E CG2 1 
ATOM   5121  N  N   . ALA E  1 90  ? 18.649  -30.042 46.192 1.00 24.89  ? 89  ALA E N   1 
ATOM   5122  C  CA  . ALA E  1 90  ? 18.570  -30.903 45.023 1.00 27.69  ? 89  ALA E CA  1 
ATOM   5123  C  C   . ALA E  1 90  ? 19.953  -31.039 44.384 1.00 31.26  ? 89  ALA E C   1 
ATOM   5124  O  O   . ALA E  1 90  ? 20.649  -30.041 44.174 1.00 33.64  ? 89  ALA E O   1 
ATOM   5125  C  CB  . ALA E  1 90  ? 17.565  -30.353 44.045 1.00 27.61  ? 89  ALA E CB  1 
ATOM   5126  N  N   . ASP E  1 91  ? 20.318  -32.289 44.053 1.00 34.56  ? 90  ASP E N   1 
ATOM   5127  C  CA  . ASP E  1 91  ? 21.577  -32.632 43.408 1.00 37.72  ? 90  ASP E CA  1 
ATOM   5128  C  C   . ASP E  1 91  ? 21.497  -32.290 41.920 1.00 40.11  ? 90  ASP E C   1 
ATOM   5129  O  O   . ASP E  1 91  ? 20.476  -31.787 41.455 1.00 38.68  ? 90  ASP E O   1 
ATOM   5130  C  CB  . ASP E  1 91  ? 21.942  -34.102 43.655 1.00 43.27  ? 90  ASP E CB  1 
ATOM   5131  C  CG  . ASP E  1 91  ? 20.986  -35.135 43.051 1.00 48.99  ? 90  ASP E CG  1 
ATOM   5132  O  OD1 . ASP E  1 91  ? 20.245  -34.801 42.091 1.00 51.13  ? 90  ASP E OD1 1 
ATOM   5133  O  OD2 . ASP E  1 91  ? 20.993  -36.277 43.540 1.00 47.75  ? 90  ASP E OD2 1 
ATOM   5134  N  N   . LYS E  1 92  ? 22.579  -32.585 41.177 1.00 47.09  ? 91  LYS E N   1 
ATOM   5135  C  CA  . LYS E  1 92  ? 22.683  -32.220 39.772 1.00 51.25  ? 91  LYS E CA  1 
ATOM   5136  C  C   . LYS E  1 92  ? 21.582  -32.865 38.941 1.00 50.63  ? 91  LYS E C   1 
ATOM   5137  O  O   . LYS E  1 92  ? 21.324  -32.423 37.830 1.00 50.06  ? 91  LYS E O   1 
ATOM   5138  C  CB  . LYS E  1 92  ? 24.072  -32.523 39.192 1.00 55.70  ? 91  LYS E CB  1 
ATOM   5139  C  CG  . LYS E  1 92  ? 25.174  -31.585 39.655 1.00 67.30  ? 91  LYS E CG  1 
ATOM   5140  C  CD  . LYS E  1 92  ? 26.354  -31.416 38.679 1.00 67.74  ? 91  LYS E CD  1 
ATOM   5141  C  CE  . LYS E  1 92  ? 26.889  -29.998 38.622 1.00 60.50  ? 91  LYS E CE  1 
ATOM   5142  N  NZ  . LYS E  1 92  ? 28.366  -29.969 38.728 1.00 55.70  ? 91  LYS E NZ  1 
ATOM   5143  N  N   . ASP E  1 93  ? 20.944  -33.911 39.481 1.00 51.54  ? 92  ASP E N   1 
ATOM   5144  C  CA  . ASP E  1 93  ? 19.924  -34.666 38.767 1.00 54.50  ? 92  ASP E CA  1 
ATOM   5145  C  C   . ASP E  1 93  ? 18.531  -34.154 39.114 1.00 53.38  ? 92  ASP E C   1 
ATOM   5146  O  O   . ASP E  1 93  ? 17.541  -34.667 38.601 1.00 58.57  ? 92  ASP E O   1 
ATOM   5147  C  CB  . ASP E  1 93  ? 19.987  -36.154 39.105 1.00 55.76  ? 92  ASP E CB  1 
ATOM   5148  C  CG  . ASP E  1 93  ? 21.267  -36.814 38.640 1.00 60.05  ? 92  ASP E CG  1 
ATOM   5149  O  OD1 . ASP E  1 93  ? 21.697  -36.522 37.503 1.00 66.84  ? 92  ASP E OD1 1 
ATOM   5150  O  OD2 . ASP E  1 93  ? 21.820  -37.621 39.416 1.00 58.12  ? 92  ASP E OD2 1 
ATOM   5151  N  N   . GLY E  1 94  ? 18.453  -33.160 40.006 1.00 50.35  ? 93  GLY E N   1 
ATOM   5152  C  CA  . GLY E  1 94  ? 17.172  -32.585 40.382 1.00 42.77  ? 93  GLY E CA  1 
ATOM   5153  C  C   . GLY E  1 94  ? 16.464  -33.417 41.446 1.00 37.17  ? 93  GLY E C   1 
ATOM   5154  O  O   . GLY E  1 94  ? 15.241  -33.329 41.601 1.00 40.69  ? 93  GLY E O   1 
ATOM   5155  N  N   . VAL E  1 95  ? 17.245  -34.205 42.194 1.00 32.37  ? 94  VAL E N   1 
ATOM   5156  C  CA  . VAL E  1 95  ? 16.677  -35.019 43.254 1.00 29.71  ? 94  VAL E CA  1 
ATOM   5157  C  C   . VAL E  1 95  ? 17.144  -34.475 44.599 1.00 28.96  ? 94  VAL E C   1 
ATOM   5158  O  O   . VAL E  1 95  ? 18.338  -34.301 44.828 1.00 30.47  ? 94  VAL E O   1 
ATOM   5159  C  CB  . VAL E  1 95  ? 17.034  -36.507 43.084 1.00 27.52  ? 94  VAL E CB  1 
ATOM   5160  C  CG1 . VAL E  1 95  ? 16.551  -37.341 44.260 1.00 24.79  ? 94  VAL E CG1 1 
ATOM   5161  C  CG2 . VAL E  1 95  ? 16.481  -37.047 41.774 1.00 26.59  ? 94  VAL E CG2 1 
ATOM   5162  N  N   . ALA E  1 96  ? 16.188  -34.245 45.502 1.00 27.19  ? 95  ALA E N   1 
ATOM   5163  C  CA  . ALA E  1 96  ? 16.523  -33.885 46.864 1.00 26.20  ? 95  ALA E CA  1 
ATOM   5164  C  C   . ALA E  1 96  ? 16.271  -35.082 47.766 1.00 25.67  ? 95  ALA E C   1 
ATOM   5165  O  O   . ALA E  1 96  ? 15.138  -35.519 47.890 1.00 27.19  ? 95  ALA E O   1 
ATOM   5166  C  CB  . ALA E  1 96  ? 15.706  -32.698 47.292 1.00 25.71  ? 95  ALA E CB  1 
ATOM   5167  N  N   . ASP E  1 97  ? 17.333  -35.606 48.390 1.00 25.98  ? 96  ASP E N   1 
ATOM   5168  C  CA  . ASP E  1 97  ? 17.161  -36.655 49.375 1.00 26.76  ? 96  ASP E CA  1 
ATOM   5169  C  C   . ASP E  1 97  ? 16.967  -35.984 50.718 1.00 26.50  ? 96  ASP E C   1 
ATOM   5170  O  O   . ASP E  1 97  ? 17.935  -35.638 51.384 1.00 32.83  ? 96  ASP E O   1 
ATOM   5171  C  CB  . ASP E  1 97  ? 18.277  -37.700 49.358 1.00 27.85  ? 96  ASP E CB  1 
ATOM   5172  C  CG  . ASP E  1 97  ? 18.275  -38.527 48.082 1.00 31.55  ? 96  ASP E CG  1 
ATOM   5173  O  OD1 . ASP E  1 97  ? 17.189  -39.066 47.727 1.00 31.96  ? 96  ASP E OD1 1 
ATOM   5174  O  OD2 . ASP E  1 97  ? 19.346  -38.598 47.435 1.00 32.92  ? 96  ASP E OD2 1 
ATOM   5175  N  N   . VAL E  1 98  ? 15.703  -35.802 51.096 1.00 24.31  ? 97  VAL E N   1 
ATOM   5176  C  CA  . VAL E  1 98  ? 15.375  -35.044 52.285 1.00 23.44  ? 97  VAL E CA  1 
ATOM   5177  C  C   . VAL E  1 98  ? 15.659  -35.890 53.519 1.00 23.12  ? 97  VAL E C   1 
ATOM   5178  O  O   . VAL E  1 98  ? 15.306  -37.069 53.579 1.00 25.51  ? 97  VAL E O   1 
ATOM   5179  C  CB  . VAL E  1 98  ? 13.910  -34.590 52.259 1.00 22.27  ? 97  VAL E CB  1 
ATOM   5180  C  CG1 . VAL E  1 98  ? 13.568  -33.770 53.489 1.00 21.53  ? 97  VAL E CG1 1 
ATOM   5181  C  CG2 . VAL E  1 98  ? 13.608  -33.816 50.985 1.00 22.50  ? 97  VAL E CG2 1 
ATOM   5182  N  N   . SER E  1 99  ? 16.288  -35.248 54.508 1.00 21.16  ? 98  SER E N   1 
ATOM   5183  C  CA  . SER E  1 99  ? 16.478  -35.865 55.804 1.00 20.70  ? 98  SER E CA  1 
ATOM   5184  C  C   . SER E  1 99  ? 16.687  -34.772 56.842 1.00 19.45  ? 98  SER E C   1 
ATOM   5185  O  O   . SER E  1 99  ? 17.708  -34.096 56.828 1.00 20.14  ? 98  SER E O   1 
ATOM   5186  C  CB  . SER E  1 99  ? 17.612  -36.832 55.781 1.00 21.07  ? 98  SER E CB  1 
ATOM   5187  O  OG  . SER E  1 99  ? 17.780  -37.376 57.080 1.00 22.55  ? 98  SER E OG  1 
ATOM   5188  N  N   . ILE E  1 100 ? 15.688  -34.588 57.706 1.00 18.42  ? 99  ILE E N   1 
ATOM   5189  C  CA  . ILE E  1 100 ? 15.672  -33.478 58.639 1.00 20.14  ? 99  ILE E CA  1 
ATOM   5190  C  C   . ILE E  1 100 ? 15.205  -34.010 59.982 1.00 21.43  ? 99  ILE E C   1 
ATOM   5191  O  O   . ILE E  1 100 ? 14.426  -34.949 60.035 1.00 23.20  ? 99  ILE E O   1 
ATOM   5192  C  CB  . ILE E  1 100 ? 14.736  -32.358 58.141 1.00 19.29  ? 99  ILE E CB  1 
ATOM   5193  C  CG1 . ILE E  1 100 ? 15.367  -31.562 56.998 1.00 18.21  ? 99  ILE E CG1 1 
ATOM   5194  C  CG2 . ILE E  1 100 ? 14.308  -31.434 59.280 1.00 17.22  ? 99  ILE E CG2 1 
ATOM   5195  C  CD1 . ILE E  1 100 ? 14.382  -30.670 56.298 1.00 18.59  ? 99  ILE E CD1 1 
ATOM   5196  N  N   . GLU E  1 101 ? 15.686  -33.386 61.048 1.00 23.02  ? 100 GLU E N   1 
ATOM   5197  C  CA  . GLU E  1 101 ? 15.135  -33.677 62.350 1.00 25.58  ? 100 GLU E CA  1 
ATOM   5198  C  C   . GLU E  1 101 ? 14.731  -32.350 62.971 1.00 26.02  ? 100 GLU E C   1 
ATOM   5199  O  O   . GLU E  1 101 ? 15.493  -31.389 62.931 1.00 27.66  ? 100 GLU E O   1 
ATOM   5200  C  CB  . GLU E  1 101 ? 16.149  -34.474 63.161 1.00 28.67  ? 100 GLU E CB  1 
ATOM   5201  C  CG  . GLU E  1 101 ? 15.781  -34.606 64.629 1.00 33.42  ? 100 GLU E CG  1 
ATOM   5202  C  CD  . GLU E  1 101 ? 16.530  -35.717 65.328 1.00 39.34  ? 100 GLU E CD  1 
ATOM   5203  O  OE1 . GLU E  1 101 ? 16.951  -35.487 66.486 1.00 41.34  ? 100 GLU E OE1 1 
ATOM   5204  O  OE2 . GLU E  1 101 ? 16.652  -36.814 64.721 1.00 43.42  ? 100 GLU E OE2 1 
ATOM   5205  N  N   . ASP E  1 102 ? 13.497  -32.285 63.474 1.00 26.60  ? 101 ASP E N   1 
ATOM   5206  C  CA  . ASP E  1 102 ? 13.022  -31.027 64.005 1.00 27.83  ? 101 ASP E CA  1 
ATOM   5207  C  C   . ASP E  1 102 ? 12.305  -31.283 65.318 1.00 28.28  ? 101 ASP E C   1 
ATOM   5208  O  O   . ASP E  1 102 ? 11.621  -32.294 65.452 1.00 29.34  ? 101 ASP E O   1 
ATOM   5209  C  CB  . ASP E  1 102 ? 12.103  -30.326 63.007 1.00 28.73  ? 101 ASP E CB  1 
ATOM   5210  C  CG  . ASP E  1 102 ? 11.854  -28.886 63.389 1.00 28.78  ? 101 ASP E CG  1 
ATOM   5211  O  OD1 . ASP E  1 102 ? 12.802  -28.099 63.291 1.00 30.28  ? 101 ASP E OD1 1 
ATOM   5212  O  OD2 . ASP E  1 102 ? 10.725  -28.575 63.821 1.00 28.55  ? 101 ASP E OD2 1 
ATOM   5213  N  N   . SER E  1 103 ? 12.447  -30.348 66.260 1.00 29.53  ? 102 SER E N   1 
ATOM   5214  C  CA  . SER E  1 103 ? 11.846  -30.528 67.571 1.00 30.32  ? 102 SER E CA  1 
ATOM   5215  C  C   . SER E  1 103 ? 10.724  -29.527 67.824 1.00 29.73  ? 102 SER E C   1 
ATOM   5216  O  O   . SER E  1 103 ? 10.181  -29.478 68.924 1.00 31.42  ? 102 SER E O   1 
ATOM   5217  C  CB  . SER E  1 103 ? 12.882  -30.477 68.640 1.00 30.88  ? 102 SER E CB  1 
ATOM   5218  O  OG  . SER E  1 103 ? 13.402  -31.778 68.833 1.00 33.09  ? 102 SER E OG  1 
ATOM   5219  N  N   . VAL E  1 104 ? 10.369  -28.750 66.799 1.00 26.62  ? 103 VAL E N   1 
ATOM   5220  C  CA  . VAL E  1 104 ? 9.361   -27.722 66.969 1.00 25.41  ? 103 VAL E CA  1 
ATOM   5221  C  C   . VAL E  1 104 ? 8.046   -28.226 66.387 1.00 24.97  ? 103 VAL E C   1 
ATOM   5222  O  O   . VAL E  1 104 ? 7.007   -28.083 67.021 1.00 26.82  ? 103 VAL E O   1 
ATOM   5223  C  CB  . VAL E  1 104 ? 9.796   -26.368 66.371 1.00 25.60  ? 103 VAL E CB  1 
ATOM   5224  C  CG1 . VAL E  1 104 ? 8.666   -25.344 66.362 1.00 24.22  ? 103 VAL E CG1 1 
ATOM   5225  C  CG2 . VAL E  1 104 ? 11.009  -25.814 67.085 1.00 24.22  ? 103 VAL E CG2 1 
ATOM   5226  N  N   . ILE E  1 105 ? 8.097   -28.807 65.185 1.00 23.86  ? 104 ILE E N   1 
ATOM   5227  C  CA  . ILE E  1 105 ? 6.924   -29.478 64.658 1.00 24.44  ? 104 ILE E CA  1 
ATOM   5228  C  C   . ILE E  1 105 ? 6.642   -30.685 65.545 1.00 26.11  ? 104 ILE E C   1 
ATOM   5229  O  O   . ILE E  1 105 ? 7.524   -31.166 66.251 1.00 25.21  ? 104 ILE E O   1 
ATOM   5230  C  CB  . ILE E  1 105 ? 7.100   -29.884 63.182 1.00 22.57  ? 104 ILE E CB  1 
ATOM   5231  C  CG1 . ILE E  1 105 ? 8.208   -30.920 62.998 1.00 21.18  ? 104 ILE E CG1 1 
ATOM   5232  C  CG2 . ILE E  1 105 ? 7.298   -28.667 62.317 1.00 21.50  ? 104 ILE E CG2 1 
ATOM   5233  C  CD1 . ILE E  1 105 ? 8.209   -31.580 61.647 1.00 19.71  ? 104 ILE E CD1 1 
ATOM   5234  N  N   . SER E  1 106 ? 5.388   -31.148 65.512 1.00 30.00  ? 105 SER E N   1 
ATOM   5235  C  CA  . SER E  1 106 ? 4.999   -32.326 66.258 1.00 30.90  ? 105 SER E CA  1 
ATOM   5236  C  C   . SER E  1 106 ? 3.950   -33.117 65.492 1.00 31.58  ? 105 SER E C   1 
ATOM   5237  O  O   . SER E  1 106 ? 3.277   -32.570 64.639 1.00 31.24  ? 105 SER E O   1 
ATOM   5238  C  CB  . SER E  1 106 ? 4.512   -31.953 67.631 1.00 30.63  ? 105 SER E CB  1 
ATOM   5239  O  OG  . SER E  1 106 ? 4.471   -33.114 68.432 1.00 33.46  ? 105 SER E OG  1 
ATOM   5240  N  N   . LEU E  1 107 ? 3.807   -34.397 65.821 1.00 32.16  ? 106 LEU E N   1 
ATOM   5241  C  CA  . LEU E  1 107 ? 2.719   -35.208 65.303 1.00 31.91  ? 106 LEU E CA  1 
ATOM   5242  C  C   . LEU E  1 107 ? 1.675   -35.452 66.396 1.00 33.81  ? 106 LEU E C   1 
ATOM   5243  O  O   . LEU E  1 107 ? 0.790   -36.275 66.217 1.00 34.25  ? 106 LEU E O   1 
ATOM   5244  C  CB  . LEU E  1 107 ? 3.265   -36.519 64.730 1.00 30.32  ? 106 LEU E CB  1 
ATOM   5245  C  CG  . LEU E  1 107 ? 4.357   -36.378 63.671 1.00 30.36  ? 106 LEU E CG  1 
ATOM   5246  C  CD1 . LEU E  1 107 ? 4.767   -37.713 63.091 1.00 29.20  ? 106 LEU E CD1 1 
ATOM   5247  C  CD2 . LEU E  1 107 ? 3.916   -35.456 62.555 1.00 29.47  ? 106 LEU E CD2 1 
ATOM   5248  N  N   . SER E  1 108 ? 1.777   -34.741 67.527 1.00 38.18  ? 107 SER E N   1 
ATOM   5249  C  CA  . SER E  1 108 ? 0.734   -34.723 68.546 1.00 43.72  ? 107 SER E CA  1 
ATOM   5250  C  C   . SER E  1 108 ? 0.860   -33.466 69.404 1.00 46.09  ? 107 SER E C   1 
ATOM   5251  O  O   . SER E  1 108 ? 1.903   -32.827 69.434 1.00 51.21  ? 107 SER E O   1 
ATOM   5252  C  CB  . SER E  1 108 ? 0.749   -35.978 69.386 1.00 43.24  ? 107 SER E CB  1 
ATOM   5253  O  OG  . SER E  1 108 ? 1.974   -36.081 70.089 1.00 49.77  ? 107 SER E OG  1 
ATOM   5254  N  N   . GLY E  1 109 ? -0.228  -33.070 70.073 1.00 49.84  ? 108 GLY E N   1 
ATOM   5255  C  CA  . GLY E  1 109 ? -0.233  -31.901 70.939 1.00 50.18  ? 108 GLY E CA  1 
ATOM   5256  C  C   . GLY E  1 109 ? -0.441  -30.613 70.143 1.00 56.91  ? 108 GLY E C   1 
ATOM   5257  O  O   . GLY E  1 109 ? -0.958  -30.644 69.033 1.00 62.99  ? 108 GLY E O   1 
ATOM   5258  N  N   . ASP E  1 110 ? 0.040   -29.501 70.697 1.00 62.16  ? 109 ASP E N   1 
ATOM   5259  C  CA  . ASP E  1 110 ? -0.315  -28.176 70.226 1.00 66.75  ? 109 ASP E CA  1 
ATOM   5260  C  C   . ASP E  1 110 ? 0.231   -27.901 68.829 1.00 65.28  ? 109 ASP E C   1 
ATOM   5261  O  O   . ASP E  1 110 ? -0.313  -27.066 68.118 1.00 67.47  ? 109 ASP E O   1 
ATOM   5262  C  CB  . ASP E  1 110 ? 0.154   -27.104 71.211 1.00 76.47  ? 109 ASP E CB  1 
ATOM   5263  C  CG  . ASP E  1 110 ? -0.548  -27.198 72.556 1.00 77.86  ? 109 ASP E CG  1 
ATOM   5264  O  OD1 . ASP E  1 110 ? -1.634  -26.585 72.695 1.00 76.09  ? 109 ASP E OD1 1 
ATOM   5265  O  OD2 . ASP E  1 110 ? 0.041   -27.776 73.495 1.00 81.78  ? 109 ASP E OD2 1 
ATOM   5266  N  N   . HIS E  1 111 ? 1.329   -28.558 68.444 1.00 59.45  ? 110 HIS E N   1 
ATOM   5267  C  CA  . HIS E  1 111 ? 1.934   -28.170 67.186 1.00 56.88  ? 110 HIS E CA  1 
ATOM   5268  C  C   . HIS E  1 111 ? 1.740   -29.258 66.135 1.00 50.20  ? 110 HIS E C   1 
ATOM   5269  O  O   . HIS E  1 111 ? 2.586   -29.430 65.265 1.00 50.64  ? 110 HIS E O   1 
ATOM   5270  C  CB  . HIS E  1 111 ? 3.386   -27.729 67.408 1.00 63.81  ? 110 HIS E CB  1 
ATOM   5271  C  CG  . HIS E  1 111 ? 3.551   -26.595 68.372 1.00 67.60  ? 110 HIS E CG  1 
ATOM   5272  N  ND1 . HIS E  1 111 ? 4.733   -26.403 69.063 1.00 61.62  ? 110 HIS E ND1 1 
ATOM   5273  C  CD2 . HIS E  1 111 ? 2.727   -25.587 68.753 1.00 68.84  ? 110 HIS E CD2 1 
ATOM   5274  C  CE1 . HIS E  1 111 ? 4.647   -25.326 69.821 1.00 66.63  ? 110 HIS E CE1 1 
ATOM   5275  N  NE2 . HIS E  1 111 ? 3.416   -24.811 69.651 1.00 72.17  ? 110 HIS E NE2 1 
ATOM   5276  N  N   . CYS E  1 112 ? 0.618   -29.978 66.232 1.00 43.83  ? 111 CYS E N   1 
ATOM   5277  C  CA  . CYS E  1 112 ? 0.348   -31.069 65.316 1.00 39.39  ? 111 CYS E CA  1 
ATOM   5278  C  C   . CYS E  1 112 ? 0.267   -30.529 63.887 1.00 33.43  ? 111 CYS E C   1 
ATOM   5279  O  O   . CYS E  1 112 ? -0.369  -29.521 63.651 1.00 31.96  ? 111 CYS E O   1 
ATOM   5280  C  CB  . CYS E  1 112 ? -0.932  -31.763 65.744 1.00 42.99  ? 111 CYS E CB  1 
ATOM   5281  S  SG  . CYS E  1 112 ? -1.028  -33.519 65.334 1.00 60.23  ? 111 CYS E SG  1 
ATOM   5282  N  N   . ILE E  1 113 ? 0.999   -31.162 62.967 1.00 28.79  ? 112 ILE E N   1 
ATOM   5283  C  CA  . ILE E  1 113 ? 1.049   -30.746 61.574 1.00 27.96  ? 112 ILE E CA  1 
ATOM   5284  C  C   . ILE E  1 113 ? 0.173   -31.662 60.721 1.00 27.94  ? 112 ILE E C   1 
ATOM   5285  O  O   . ILE E  1 113 ? 0.094   -31.494 59.496 1.00 28.10  ? 112 ILE E O   1 
ATOM   5286  C  CB  . ILE E  1 113 ? 2.489   -30.702 61.016 1.00 28.06  ? 112 ILE E CB  1 
ATOM   5287  C  CG1 . ILE E  1 113 ? 3.231   -32.025 61.206 1.00 26.11  ? 112 ILE E CG1 1 
ATOM   5288  C  CG2 . ILE E  1 113 ? 3.270   -29.542 61.603 1.00 30.67  ? 112 ILE E CG2 1 
ATOM   5289  C  CD1 . ILE E  1 113 ? 4.344   -32.249 60.224 1.00 24.79  ? 112 ILE E CD1 1 
ATOM   5290  N  N   . ILE E  1 114 ? -0.472  -32.647 61.372 1.00 26.22  ? 113 ILE E N   1 
ATOM   5291  C  CA  . ILE E  1 114 ? -1.367  -33.550 60.667 1.00 23.36  ? 113 ILE E CA  1 
ATOM   5292  C  C   . ILE E  1 114 ? -2.524  -32.736 60.111 1.00 22.16  ? 113 ILE E C   1 
ATOM   5293  O  O   . ILE E  1 114 ? -3.083  -31.887 60.804 1.00 20.50  ? 113 ILE E O   1 
ATOM   5294  C  CB  . ILE E  1 114 ? -1.861  -34.668 61.595 1.00 22.45  ? 113 ILE E CB  1 
ATOM   5295  C  CG1 . ILE E  1 114 ? -0.675  -35.385 62.250 1.00 23.21  ? 113 ILE E CG1 1 
ATOM   5296  C  CG2 . ILE E  1 114 ? -2.774  -35.614 60.832 1.00 22.54  ? 113 ILE E CG2 1 
ATOM   5297  C  CD1 . ILE E  1 114 ? -0.963  -36.779 62.684 1.00 22.27  ? 113 ILE E CD1 1 
ATOM   5298  N  N   . GLY E  1 115 ? -2.830  -32.995 58.836 1.00 22.10  ? 114 GLY E N   1 
ATOM   5299  C  CA  . GLY E  1 115 ? -3.947  -32.363 58.159 1.00 21.76  ? 114 GLY E CA  1 
ATOM   5300  C  C   . GLY E  1 115 ? -3.606  -30.957 57.685 1.00 22.85  ? 114 GLY E C   1 
ATOM   5301  O  O   . GLY E  1 115 ? -4.515  -30.202 57.328 1.00 24.80  ? 114 GLY E O   1 
ATOM   5302  N  N   . ARG E  1 116 ? -2.306  -30.618 57.685 1.00 21.72  ? 115 ARG E N   1 
ATOM   5303  C  CA  . ARG E  1 116 ? -1.821  -29.371 57.111 1.00 21.38  ? 115 ARG E CA  1 
ATOM   5304  C  C   . ARG E  1 116 ? -1.081  -29.673 55.811 1.00 21.13  ? 115 ARG E C   1 
ATOM   5305  O  O   . ARG E  1 116 ? -1.131  -30.802 55.331 1.00 22.28  ? 115 ARG E O   1 
ATOM   5306  C  CB  . ARG E  1 116 ? -1.055  -28.584 58.171 1.00 21.84  ? 115 ARG E CB  1 
ATOM   5307  C  CG  . ARG E  1 116 ? -1.849  -28.424 59.455 1.00 23.10  ? 115 ARG E CG  1 
ATOM   5308  C  CD  . ARG E  1 116 ? -1.217  -27.498 60.452 1.00 22.58  ? 115 ARG E CD  1 
ATOM   5309  N  NE  . ARG E  1 116 ? -2.010  -27.342 61.668 1.00 22.60  ? 115 ARG E NE  1 
ATOM   5310  C  CZ  . ARG E  1 116 ? -2.973  -26.441 61.848 1.00 22.35  ? 115 ARG E CZ  1 
ATOM   5311  N  NH1 . ARG E  1 116 ? -3.284  -25.579 60.886 1.00 22.15  ? 115 ARG E NH1 1 
ATOM   5312  N  NH2 . ARG E  1 116 ? -3.607  -26.397 63.008 1.00 23.29  ? 115 ARG E NH2 1 
ATOM   5313  N  N   . THR E  1 117 ? -0.431  -28.667 55.209 1.00 20.50  ? 116 THR E N   1 
ATOM   5314  C  CA  . THR E  1 117 ? 0.209   -28.890 53.918 1.00 19.44  ? 116 THR E CA  1 
ATOM   5315  C  C   . THR E  1 117 ? 1.723   -28.744 54.017 1.00 19.42  ? 116 THR E C   1 
ATOM   5316  O  O   . THR E  1 117 ? 2.243   -27.854 54.693 1.00 20.05  ? 116 THR E O   1 
ATOM   5317  C  CB  . THR E  1 117 ? -0.344  -27.965 52.831 1.00 18.56  ? 116 THR E CB  1 
ATOM   5318  O  OG1 . THR E  1 117 ? -1.734  -28.281 52.703 1.00 17.97  ? 116 THR E OG1 1 
ATOM   5319  C  CG2 . THR E  1 117 ? 0.372   -28.124 51.497 1.00 18.10  ? 116 THR E CG2 1 
ATOM   5320  N  N   . LEU E  1 118 ? 2.427   -29.638 53.321 1.00 18.27  ? 117 LEU E N   1 
ATOM   5321  C  CA  . LEU E  1 118 ? 3.857   -29.485 53.147 1.00 17.74  ? 117 LEU E CA  1 
ATOM   5322  C  C   . LEU E  1 118 ? 4.082   -28.935 51.746 1.00 17.66  ? 117 LEU E C   1 
ATOM   5323  O  O   . LEU E  1 118 ? 3.463   -29.413 50.793 1.00 18.01  ? 117 LEU E O   1 
ATOM   5324  C  CB  . LEU E  1 118 ? 4.499   -30.864 53.312 1.00 17.03  ? 117 LEU E CB  1 
ATOM   5325  C  CG  . LEU E  1 118 ? 6.009   -30.909 53.103 1.00 16.43  ? 117 LEU E CG  1 
ATOM   5326  C  CD1 . LEU E  1 118 ? 6.701   -30.122 54.199 1.00 16.81  ? 117 LEU E CD1 1 
ATOM   5327  C  CD2 . LEU E  1 118 ? 6.506   -32.342 53.085 1.00 16.87  ? 117 LEU E CD2 1 
ATOM   5328  N  N   . VAL E  1 119 ? 4.946   -27.914 51.641 1.00 17.71  ? 118 VAL E N   1 
ATOM   5329  C  CA  . VAL E  1 119 ? 5.204   -27.263 50.366 1.00 18.03  ? 118 VAL E CA  1 
ATOM   5330  C  C   . VAL E  1 119 ? 6.706   -27.201 50.116 1.00 18.42  ? 118 VAL E C   1 
ATOM   5331  O  O   . VAL E  1 119 ? 7.490   -26.827 51.000 1.00 19.61  ? 118 VAL E O   1 
ATOM   5332  C  CB  . VAL E  1 119 ? 4.616   -25.840 50.314 1.00 18.76  ? 118 VAL E CB  1 
ATOM   5333  C  CG1 . VAL E  1 119 ? 4.868   -25.182 48.963 1.00 19.98  ? 118 VAL E CG1 1 
ATOM   5334  C  CG2 . VAL E  1 119 ? 3.134   -25.793 50.666 1.00 18.28  ? 118 VAL E CG2 1 
ATOM   5335  N  N   . VAL E  1 120 ? 7.096   -27.520 48.883 1.00 18.45  ? 119 VAL E N   1 
ATOM   5336  C  CA  . VAL E  1 120 ? 8.462   -27.279 48.457 1.00 19.95  ? 119 VAL E CA  1 
ATOM   5337  C  C   . VAL E  1 120 ? 8.443   -26.121 47.463 1.00 22.21  ? 119 VAL E C   1 
ATOM   5338  O  O   . VAL E  1 120 ? 7.676   -26.138 46.498 1.00 22.72  ? 119 VAL E O   1 
ATOM   5339  C  CB  . VAL E  1 120 ? 9.120   -28.555 47.889 1.00 19.02  ? 119 VAL E CB  1 
ATOM   5340  C  CG1 . VAL E  1 120 ? 8.344   -29.132 46.711 1.00 19.27  ? 119 VAL E CG1 1 
ATOM   5341  C  CG2 . VAL E  1 120 ? 10.579  -28.331 47.529 1.00 18.08  ? 119 VAL E CG2 1 
ATOM   5342  N  N   . HIS E  1 121 ? 9.299   -25.123 47.722 1.00 25.36  ? 120 HIS E N   1 
ATOM   5343  C  CA  . HIS E  1 121 ? 9.256   -23.837 47.038 1.00 27.55  ? 120 HIS E CA  1 
ATOM   5344  C  C   . HIS E  1 121 ? 10.287  -23.731 45.912 1.00 30.05  ? 120 HIS E C   1 
ATOM   5345  O  O   . HIS E  1 121 ? 11.179  -24.574 45.768 1.00 31.23  ? 120 HIS E O   1 
ATOM   5346  C  CB  . HIS E  1 121 ? 9.448   -22.712 48.045 1.00 26.45  ? 120 HIS E CB  1 
ATOM   5347  C  CG  . HIS E  1 121 ? 8.266   -22.485 48.922 1.00 26.46  ? 120 HIS E CG  1 
ATOM   5348  N  ND1 . HIS E  1 121 ? 7.252   -21.598 48.590 1.00 25.84  ? 120 HIS E ND1 1 
ATOM   5349  C  CD2 . HIS E  1 121 ? 7.934   -23.019 50.117 1.00 27.72  ? 120 HIS E CD2 1 
ATOM   5350  C  CE1 . HIS E  1 121 ? 6.360   -21.572 49.549 1.00 28.78  ? 120 HIS E CE1 1 
ATOM   5351  N  NE2 . HIS E  1 121 ? 6.758   -22.436 50.513 1.00 28.93  ? 120 HIS E NE2 1 
ATOM   5352  N  N   . GLU E  1 122 ? 10.173  -22.629 45.159 1.00 31.11  ? 121 GLU E N   1 
ATOM   5353  C  CA  . GLU E  1 122 ? 10.868  -22.422 43.899 1.00 31.68  ? 121 GLU E CA  1 
ATOM   5354  C  C   . GLU E  1 122 ? 12.350  -22.125 44.118 1.00 30.34  ? 121 GLU E C   1 
ATOM   5355  O  O   . GLU E  1 122 ? 13.182  -22.642 43.384 1.00 29.83  ? 121 GLU E O   1 
ATOM   5356  C  CB  . GLU E  1 122 ? 10.142  -21.299 43.169 1.00 35.17  ? 121 GLU E CB  1 
ATOM   5357  C  CG  . GLU E  1 122 ? 10.956  -20.588 42.115 1.00 39.33  ? 121 GLU E CG  1 
ATOM   5358  C  CD  . GLU E  1 122 ? 10.317  -19.254 41.751 1.00 40.89  ? 121 GLU E CD  1 
ATOM   5359  O  OE1 . GLU E  1 122 ? 10.456  -18.850 40.597 1.00 46.43  ? 121 GLU E OE1 1 
ATOM   5360  O  OE2 . GLU E  1 122 ? 9.714   -18.604 42.636 1.00 36.75  ? 121 GLU E OE2 1 
ATOM   5361  N  N   . LYS E  1 123 ? 12.657  -21.306 45.137 1.00 29.29  ? 122 LYS E N   1 
ATOM   5362  C  CA  . LYS E  1 123 ? 13.986  -20.767 45.401 1.00 28.60  ? 122 LYS E CA  1 
ATOM   5363  C  C   . LYS E  1 123 ? 14.421  -21.089 46.832 1.00 28.64  ? 122 LYS E C   1 
ATOM   5364  O  O   . LYS E  1 123 ? 13.668  -21.673 47.608 1.00 28.48  ? 122 LYS E O   1 
ATOM   5365  C  CB  . LYS E  1 123 ? 13.960  -19.241 45.278 1.00 28.23  ? 122 LYS E CB  1 
ATOM   5366  C  CG  . LYS E  1 123 ? 13.669  -18.691 43.891 1.00 31.27  ? 122 LYS E CG  1 
ATOM   5367  C  CD  . LYS E  1 123 ? 13.696  -17.156 43.798 1.00 31.10  ? 122 LYS E CD  1 
ATOM   5368  C  CE  . LYS E  1 123 ? 12.498  -16.471 44.420 1.00 28.29  ? 122 LYS E CE  1 
ATOM   5369  N  NZ  . LYS E  1 123 ? 12.257  -15.118 43.855 1.00 25.48  ? 122 LYS E NZ  1 
ATOM   5370  N  N   . ALA E  1 124 ? 15.635  -20.649 47.186 1.00 26.71  ? 123 ALA E N   1 
ATOM   5371  C  CA  . ALA E  1 124 ? 16.166  -20.818 48.529 1.00 24.99  ? 123 ALA E CA  1 
ATOM   5372  C  C   . ALA E  1 124 ? 15.338  -20.018 49.528 1.00 23.83  ? 123 ALA E C   1 
ATOM   5373  O  O   . ALA E  1 124 ? 14.842  -18.945 49.214 1.00 26.59  ? 123 ALA E O   1 
ATOM   5374  C  CB  . ALA E  1 124 ? 17.600  -20.373 48.565 1.00 26.05  ? 123 ALA E CB  1 
ATOM   5375  N  N   . ASP E  1 125 ? 15.191  -20.566 50.733 1.00 21.67  ? 124 ASP E N   1 
ATOM   5376  C  CA  . ASP E  1 125 ? 14.653  -19.840 51.863 1.00 20.22  ? 124 ASP E CA  1 
ATOM   5377  C  C   . ASP E  1 125 ? 15.815  -19.086 52.507 1.00 20.54  ? 124 ASP E C   1 
ATOM   5378  O  O   . ASP E  1 125 ? 16.802  -19.694 52.908 1.00 19.42  ? 124 ASP E O   1 
ATOM   5379  C  CB  . ASP E  1 125 ? 13.973  -20.824 52.820 1.00 20.23  ? 124 ASP E CB  1 
ATOM   5380  C  CG  . ASP E  1 125 ? 13.501  -20.234 54.137 1.00 20.54  ? 124 ASP E CG  1 
ATOM   5381  O  OD1 . ASP E  1 125 ? 13.759  -19.044 54.384 1.00 20.08  ? 124 ASP E OD1 1 
ATOM   5382  O  OD2 . ASP E  1 125 ? 12.877  -20.971 54.913 1.00 21.22  ? 124 ASP E OD2 1 
ATOM   5383  N  N   . ASP E  1 126 ? 15.695  -17.759 52.622 1.00 21.92  ? 125 ASP E N   1 
ATOM   5384  C  CA  . ASP E  1 126 ? 16.789  -16.943 53.129 1.00 22.41  ? 125 ASP E CA  1 
ATOM   5385  C  C   . ASP E  1 126 ? 16.819  -16.957 54.659 1.00 24.01  ? 125 ASP E C   1 
ATOM   5386  O  O   . ASP E  1 126 ? 17.616  -16.248 55.258 1.00 24.99  ? 125 ASP E O   1 
ATOM   5387  C  CB  . ASP E  1 126 ? 16.821  -15.548 52.497 1.00 22.89  ? 125 ASP E CB  1 
ATOM   5388  C  CG  . ASP E  1 126 ? 15.713  -14.603 52.947 1.00 25.83  ? 125 ASP E CG  1 
ATOM   5389  O  OD1 . ASP E  1 126 ? 15.156  -14.808 54.067 1.00 24.33  ? 125 ASP E OD1 1 
ATOM   5390  O  OD2 . ASP E  1 126 ? 15.429  -13.635 52.178 1.00 26.78  ? 125 ASP E OD2 1 
ATOM   5391  N  N   . LEU E  1 127 ? 15.960  -17.778 55.279 1.00 23.62  ? 126 LEU E N   1 
ATOM   5392  C  CA  . LEU E  1 127 ? 15.949  -18.001 56.716 1.00 23.34  ? 126 LEU E CA  1 
ATOM   5393  C  C   . LEU E  1 127 ? 15.752  -16.692 57.481 1.00 25.49  ? 126 LEU E C   1 
ATOM   5394  O  O   . LEU E  1 127 ? 16.118  -16.594 58.650 1.00 27.98  ? 126 LEU E O   1 
ATOM   5395  C  CB  . LEU E  1 127 ? 17.244  -18.703 57.151 1.00 22.15  ? 126 LEU E CB  1 
ATOM   5396  C  CG  . LEU E  1 127 ? 17.693  -19.921 56.348 1.00 19.81  ? 126 LEU E CG  1 
ATOM   5397  C  CD1 . LEU E  1 127 ? 18.874  -20.586 57.039 1.00 18.79  ? 126 LEU E CD1 1 
ATOM   5398  C  CD2 . LEU E  1 127 ? 16.586  -20.935 56.219 1.00 19.37  ? 126 LEU E CD2 1 
ATOM   5399  N  N   . GLY E  1 128 ? 15.155  -15.699 56.804 1.00 27.96  ? 127 GLY E N   1 
ATOM   5400  C  CA  . GLY E  1 128 ? 14.698  -14.468 57.434 1.00 28.99  ? 127 GLY E CA  1 
ATOM   5401  C  C   . GLY E  1 128 ? 15.798  -13.411 57.535 1.00 28.53  ? 127 GLY E C   1 
ATOM   5402  O  O   . GLY E  1 128 ? 15.673  -12.458 58.292 1.00 25.92  ? 127 GLY E O   1 
ATOM   5403  N  N   . LYS E  1 129 ? 16.860  -13.579 56.746 1.00 30.68  ? 128 LYS E N   1 
ATOM   5404  C  CA  . LYS E  1 129 ? 18.031  -12.723 56.824 1.00 30.33  ? 128 LYS E CA  1 
ATOM   5405  C  C   . LYS E  1 129 ? 18.207  -11.955 55.517 1.00 28.53  ? 128 LYS E C   1 
ATOM   5406  O  O   . LYS E  1 129 ? 19.332  -11.647 55.126 1.00 30.59  ? 128 LYS E O   1 
ATOM   5407  C  CB  . LYS E  1 129 ? 19.279  -13.569 57.080 1.00 30.80  ? 128 LYS E CB  1 
ATOM   5408  C  CG  . LYS E  1 129 ? 19.195  -14.512 58.280 1.00 32.25  ? 128 LYS E CG  1 
ATOM   5409  C  CD  . LYS E  1 129 ? 20.407  -15.444 58.248 1.00 32.75  ? 128 LYS E CD  1 
ATOM   5410  C  CE  . LYS E  1 129 ? 21.304  -15.569 59.475 1.00 34.97  ? 128 LYS E CE  1 
ATOM   5411  N  NZ  . LYS E  1 129 ? 22.704  -15.467 59.003 1.00 34.21  ? 128 LYS E NZ  1 
ATOM   5412  N  N   . GLY E  1 130 ? 17.092  -11.638 54.854 1.00 25.25  ? 129 GLY E N   1 
ATOM   5413  C  CA  . GLY E  1 130 ? 17.131  -11.004 53.545 1.00 23.99  ? 129 GLY E CA  1 
ATOM   5414  C  C   . GLY E  1 130 ? 16.923  -9.495  53.615 1.00 23.58  ? 129 GLY E C   1 
ATOM   5415  O  O   . GLY E  1 130 ? 17.037  -8.816  52.596 1.00 23.09  ? 129 GLY E O   1 
ATOM   5416  N  N   . GLY E  1 131 ? 16.560  -9.010  54.808 1.00 23.10  ? 130 GLY E N   1 
ATOM   5417  C  CA  . GLY E  1 131 ? 16.471  -7.591  55.099 1.00 26.44  ? 130 GLY E CA  1 
ATOM   5418  C  C   . GLY E  1 131 ? 15.324  -6.883  54.391 1.00 28.51  ? 130 GLY E C   1 
ATOM   5419  O  O   . GLY E  1 131 ? 15.376  -5.671  54.208 1.00 29.92  ? 130 GLY E O   1 
ATOM   5420  N  N   . ASN E  1 132 ? 14.294  -7.635  53.994 1.00 30.67  ? 131 ASN E N   1 
ATOM   5421  C  CA  . ASN E  1 132 ? 13.078  -7.038  53.473 1.00 35.19  ? 131 ASN E CA  1 
ATOM   5422  C  C   . ASN E  1 132 ? 11.883  -7.633  54.198 1.00 37.78  ? 131 ASN E C   1 
ATOM   5423  O  O   . ASN E  1 132 ? 12.043  -8.548  55.011 1.00 37.86  ? 131 ASN E O   1 
ATOM   5424  C  CB  . ASN E  1 132 ? 12.981  -7.077  51.945 1.00 35.22  ? 131 ASN E CB  1 
ATOM   5425  C  CG  . ASN E  1 132 ? 13.002  -8.463  51.351 1.00 35.86  ? 131 ASN E CG  1 
ATOM   5426  O  OD1 . ASN E  1 132 ? 12.768  -9.456  52.037 1.00 35.60  ? 131 ASN E OD1 1 
ATOM   5427  N  ND2 . ASN E  1 132 ? 13.143  -8.533  50.044 1.00 33.53  ? 131 ASN E ND2 1 
ATOM   5428  N  N   . GLU E  1 133 ? 10.690  -7.107  53.894 1.00 43.39  ? 132 GLU E N   1 
ATOM   5429  C  CA  . GLU E  1 133 ? 9.513   -7.491  54.649 1.00 44.27  ? 132 GLU E CA  1 
ATOM   5430  C  C   . GLU E  1 133 ? 9.179   -8.944  54.315 1.00 41.01  ? 132 GLU E C   1 
ATOM   5431  O  O   . GLU E  1 133 ? 8.820   -9.730  55.194 1.00 39.56  ? 132 GLU E O   1 
ATOM   5432  C  CB  . GLU E  1 133 ? 8.346   -6.539  54.338 1.00 51.85  ? 132 GLU E CB  1 
ATOM   5433  C  CG  . GLU E  1 133 ? 8.695   -5.074  54.053 1.00 64.20  ? 132 GLU E CG  1 
ATOM   5434  C  CD  . GLU E  1 133 ? 7.870   -4.432  52.938 1.00 69.96  ? 132 GLU E CD  1 
ATOM   5435  O  OE1 . GLU E  1 133 ? 7.736   -5.098  51.910 1.00 80.96  ? 132 GLU E OE1 1 
ATOM   5436  O  OE2 . GLU E  1 133 ? 7.354   -3.286  53.092 1.00 67.66  ? 132 GLU E OE2 1 
ATOM   5437  N  N   . GLU E  1 134 ? 9.358   -9.272  53.027 1.00 37.05  ? 133 GLU E N   1 
ATOM   5438  C  CA  . GLU E  1 134 ? 9.119   -10.593 52.484 1.00 35.25  ? 133 GLU E CA  1 
ATOM   5439  C  C   . GLU E  1 134 ? 9.930   -11.637 53.251 1.00 34.50  ? 133 GLU E C   1 
ATOM   5440  O  O   . GLU E  1 134 ? 9.420   -12.707 53.574 1.00 36.01  ? 133 GLU E O   1 
ATOM   5441  C  CB  . GLU E  1 134 ? 9.449   -10.556 50.992 1.00 36.46  ? 133 GLU E CB  1 
ATOM   5442  C  CG  . GLU E  1 134 ? 8.795   -11.656 50.177 1.00 40.99  ? 133 GLU E CG  1 
ATOM   5443  C  CD  . GLU E  1 134 ? 7.334   -11.985 50.436 1.00 43.92  ? 133 GLU E CD  1 
ATOM   5444  O  OE1 . GLU E  1 134 ? 6.546   -11.070 50.742 1.00 40.90  ? 133 GLU E OE1 1 
ATOM   5445  O  OE2 . GLU E  1 134 ? 6.989   -13.179 50.324 1.00 54.91  ? 133 GLU E OE2 1 
ATOM   5446  N  N   . SER E  1 135 ? 11.192  -11.312 53.554 1.00 32.13  ? 134 SER E N   1 
ATOM   5447  C  CA  . SER E  1 135 ? 12.093  -12.238 54.216 1.00 31.64  ? 134 SER E CA  1 
ATOM   5448  C  C   . SER E  1 135 ? 11.495  -12.722 55.530 1.00 31.75  ? 134 SER E C   1 
ATOM   5449  O  O   . SER E  1 135 ? 11.606  -13.895 55.861 1.00 32.57  ? 134 SER E O   1 
ATOM   5450  C  CB  . SER E  1 135 ? 13.456  -11.641 54.427 1.00 30.20  ? 134 SER E CB  1 
ATOM   5451  O  OG  . SER E  1 135 ? 14.365  -12.579 55.005 1.00 25.47  ? 134 SER E OG  1 
ATOM   5452  N  N   . THR E  1 136 ? 10.850  -11.825 56.277 1.00 32.86  ? 135 THR E N   1 
ATOM   5453  C  CA  . THR E  1 136 ? 10.400  -12.195 57.610 1.00 34.77  ? 135 THR E CA  1 
ATOM   5454  C  C   . THR E  1 136 ? 9.024   -12.857 57.562 1.00 34.34  ? 135 THR E C   1 
ATOM   5455  O  O   . THR E  1 136 ? 8.478   -13.196 58.612 1.00 36.09  ? 135 THR E O   1 
ATOM   5456  C  CB  . THR E  1 136 ? 10.392  -11.004 58.572 1.00 35.07  ? 135 THR E CB  1 
ATOM   5457  O  OG1 . THR E  1 136 ? 9.417   -10.102 58.052 1.00 39.96  ? 135 THR E OG1 1 
ATOM   5458  C  CG2 . THR E  1 136 ? 11.744  -10.340 58.705 1.00 32.98  ? 135 THR E CG2 1 
ATOM   5459  N  N   . LYS E  1 137 ? 8.480   -13.036 56.350 1.00 32.56  ? 136 LYS E N   1 
ATOM   5460  C  CA  . LYS E  1 137 ? 7.212   -13.729 56.169 1.00 30.68  ? 136 LYS E CA  1 
ATOM   5461  C  C   . LYS E  1 137 ? 7.434   -15.094 55.520 1.00 27.48  ? 136 LYS E C   1 
ATOM   5462  O  O   . LYS E  1 137 ? 6.998   -16.111 56.053 1.00 26.60  ? 136 LYS E O   1 
ATOM   5463  C  CB  . LYS E  1 137 ? 6.238   -12.893 55.327 1.00 33.34  ? 136 LYS E CB  1 
ATOM   5464  C  CG  . LYS E  1 137 ? 5.523   -11.771 56.076 1.00 36.57  ? 136 LYS E CG  1 
ATOM   5465  C  CD  . LYS E  1 137 ? 4.115   -11.389 55.642 1.00 36.40  ? 136 LYS E CD  1 
ATOM   5466  C  CE  . LYS E  1 137 ? 3.440   -10.660 56.780 0.20 34.28  ? 136 LYS E CE  1 
ATOM   5467  N  NZ  . LYS E  1 137 ? 2.008   -10.415 56.507 0.20 33.15  ? 136 LYS E NZ  1 
ATOM   5468  N  N   . THR E  1 138 ? 8.124   -15.110 54.373 1.00 24.91  ? 137 THR E N   1 
ATOM   5469  C  CA  . THR E  1 138 ? 8.190   -16.299 53.542 1.00 23.62  ? 137 THR E CA  1 
ATOM   5470  C  C   . THR E  1 138 ? 9.627   -16.740 53.275 1.00 24.25  ? 137 THR E C   1 
ATOM   5471  O  O   . THR E  1 138 ? 9.842   -17.729 52.579 1.00 25.41  ? 137 THR E O   1 
ATOM   5472  C  CB  . THR E  1 138 ? 7.520   -16.047 52.189 1.00 23.39  ? 137 THR E CB  1 
ATOM   5473  O  OG1 . THR E  1 138 ? 8.344   -15.182 51.405 1.00 21.59  ? 137 THR E OG1 1 
ATOM   5474  C  CG2 . THR E  1 138 ? 6.136   -15.468 52.346 1.00 24.01  ? 137 THR E CG2 1 
ATOM   5475  N  N   . GLY E  1 139 ? 10.597  -15.979 53.789 1.00 22.96  ? 138 GLY E N   1 
ATOM   5476  C  CA  . GLY E  1 139 ? 12.002  -16.219 53.504 1.00 21.46  ? 138 GLY E CA  1 
ATOM   5477  C  C   . GLY E  1 139 ? 12.347  -16.072 52.023 1.00 21.47  ? 138 GLY E C   1 
ATOM   5478  O  O   . GLY E  1 139 ? 13.427  -16.479 51.607 1.00 22.92  ? 138 GLY E O   1 
ATOM   5479  N  N   . ASN E  1 140 ? 11.437  -15.507 51.227 1.00 20.56  ? 139 ASN E N   1 
ATOM   5480  C  CA  . ASN E  1 140 ? 11.722  -15.181 49.835 1.00 21.52  ? 139 ASN E CA  1 
ATOM   5481  C  C   . ASN E  1 140 ? 11.874  -16.455 49.013 1.00 22.72  ? 139 ASN E C   1 
ATOM   5482  O  O   . ASN E  1 140 ? 12.558  -16.452 47.992 1.00 22.92  ? 139 ASN E O   1 
ATOM   5483  C  CB  . ASN E  1 140 ? 12.955  -14.283 49.663 1.00 19.69  ? 139 ASN E CB  1 
ATOM   5484  C  CG  . ASN E  1 140 ? 12.701  -12.833 50.015 1.00 20.66  ? 139 ASN E CG  1 
ATOM   5485  O  OD1 . ASN E  1 140 ? 11.951  -12.147 49.318 1.00 19.87  ? 139 ASN E OD1 1 
ATOM   5486  N  ND2 . ASN E  1 140 ? 13.307  -12.363 51.097 1.00 20.96  ? 139 ASN E ND2 1 
ATOM   5487  N  N   . ALA E  1 141 ? 11.202  -17.525 49.453 1.00 23.75  ? 140 ALA E N   1 
ATOM   5488  C  CA  . ALA E  1 141 ? 11.382  -18.844 48.862 1.00 25.01  ? 140 ALA E CA  1 
ATOM   5489  C  C   . ALA E  1 141 ? 10.667  -18.948 47.514 1.00 27.10  ? 140 ALA E C   1 
ATOM   5490  O  O   . ALA E  1 141 ? 10.828  -19.934 46.794 1.00 28.28  ? 140 ALA E O   1 
ATOM   5491  C  CB  . ALA E  1 141 ? 10.915  -19.900 49.827 1.00 23.48  ? 140 ALA E CB  1 
ATOM   5492  N  N   . GLY E  1 142 ? 9.892   -17.922 47.161 1.00 28.14  ? 141 GLY E N   1 
ATOM   5493  C  CA  . GLY E  1 142 ? 9.242   -17.901 45.862 1.00 30.50  ? 141 GLY E CA  1 
ATOM   5494  C  C   . GLY E  1 142 ? 8.028   -18.824 45.833 1.00 30.88  ? 141 GLY E C   1 
ATOM   5495  O  O   . GLY E  1 142 ? 7.459   -19.129 46.879 1.00 29.59  ? 141 GLY E O   1 
ATOM   5496  N  N   . SER E  1 143 ? 7.669   -19.273 44.625 1.00 30.93  ? 142 SER E N   1 
ATOM   5497  C  CA  . SER E  1 143 ? 6.402   -19.943 44.380 1.00 30.08  ? 142 SER E CA  1 
ATOM   5498  C  C   . SER E  1 143 ? 6.406   -21.354 44.958 1.00 30.01  ? 142 SER E C   1 
ATOM   5499  O  O   . SER E  1 143 ? 7.449   -21.854 45.403 1.00 30.99  ? 142 SER E O   1 
ATOM   5500  C  CB  . SER E  1 143 ? 6.054   -19.949 42.916 1.00 31.09  ? 142 SER E CB  1 
ATOM   5501  O  OG  . SER E  1 143 ? 7.002   -20.712 42.186 1.00 32.89  ? 142 SER E OG  1 
ATOM   5502  N  N   . ARG E  1 144 ? 5.215   -21.978 44.923 1.00 28.86  ? 143 ARG E N   1 
ATOM   5503  C  CA  . ARG E  1 144 ? 4.965   -23.298 45.485 1.00 25.78  ? 143 ARG E CA  1 
ATOM   5504  C  C   . ARG E  1 144 ? 5.052   -24.322 44.354 1.00 24.39  ? 143 ARG E C   1 
ATOM   5505  O  O   . ARG E  1 144 ? 4.178   -24.364 43.500 1.00 25.58  ? 143 ARG E O   1 
ATOM   5506  C  CB  . ARG E  1 144 ? 3.593   -23.299 46.169 1.00 23.81  ? 143 ARG E CB  1 
ATOM   5507  C  CG  . ARG E  1 144 ? 3.462   -22.224 47.244 1.00 22.89  ? 143 ARG E CG  1 
ATOM   5508  C  CD  . ARG E  1 144 ? 2.041   -22.028 47.788 1.00 22.89  ? 143 ARG E CD  1 
ATOM   5509  N  NE  . ARG E  1 144 ? 2.040   -20.942 48.768 1.00 25.01  ? 143 ARG E NE  1 
ATOM   5510  C  CZ  . ARG E  1 144 ? 1.170   -20.795 49.774 1.00 25.49  ? 143 ARG E CZ  1 
ATOM   5511  N  NH1 . ARG E  1 144 ? 0.210   -21.674 49.985 1.00 27.26  ? 143 ARG E NH1 1 
ATOM   5512  N  NH2 . ARG E  1 144 ? 1.262   -19.760 50.581 1.00 25.03  ? 143 ARG E NH2 1 
ATOM   5513  N  N   . LEU E  1 145 ? 6.120   -25.124 44.325 1.00 21.93  ? 144 LEU E N   1 
ATOM   5514  C  CA  . LEU E  1 145 ? 6.347   -25.993 43.187 1.00 21.34  ? 144 LEU E CA  1 
ATOM   5515  C  C   . LEU E  1 145 ? 5.472   -27.235 43.305 1.00 21.57  ? 144 LEU E C   1 
ATOM   5516  O  O   . LEU E  1 145 ? 4.965   -27.738 42.305 1.00 23.17  ? 144 LEU E O   1 
ATOM   5517  C  CB  . LEU E  1 145 ? 7.834   -26.357 43.126 1.00 20.28  ? 144 LEU E CB  1 
ATOM   5518  C  CG  . LEU E  1 145 ? 8.758   -25.230 42.678 1.00 19.19  ? 144 LEU E CG  1 
ATOM   5519  C  CD1 . LEU E  1 145 ? 10.198  -25.722 42.550 1.00 18.25  ? 144 LEU E CD1 1 
ATOM   5520  C  CD2 . LEU E  1 145 ? 8.275   -24.593 41.375 1.00 18.27  ? 144 LEU E CD2 1 
ATOM   5521  N  N   . ALA E  1 146 ? 5.321   -27.726 44.540 1.00 21.50  ? 145 ALA E N   1 
ATOM   5522  C  CA  . ALA E  1 146 ? 4.528   -28.911 44.816 1.00 22.46  ? 145 ALA E CA  1 
ATOM   5523  C  C   . ALA E  1 146 ? 4.128   -28.911 46.294 1.00 24.90  ? 145 ALA E C   1 
ATOM   5524  O  O   . ALA E  1 146 ? 4.855   -28.386 47.148 1.00 25.11  ? 145 ALA E O   1 
ATOM   5525  C  CB  . ALA E  1 146 ? 5.305   -30.148 44.428 1.00 21.01  ? 145 ALA E CB  1 
ATOM   5526  N  N   . CYS E  1 147 ? 2.991   -29.556 46.576 1.00 24.28  ? 146 CYS E N   1 
ATOM   5527  C  CA  . CYS E  1 147 ? 2.507   -29.646 47.939 1.00 24.26  ? 146 CYS E CA  1 
ATOM   5528  C  C   . CYS E  1 147 ? 1.649   -30.896 48.077 1.00 23.45  ? 146 CYS E C   1 
ATOM   5529  O  O   . CYS E  1 147 ? 1.366   -31.555 47.078 1.00 23.34  ? 146 CYS E O   1 
ATOM   5530  C  CB  . CYS E  1 147 ? 1.698   -28.409 48.309 1.00 26.25  ? 146 CYS E CB  1 
ATOM   5531  S  SG  . CYS E  1 147 ? 0.264   -28.148 47.220 1.00 32.60  ? 146 CYS E SG  1 
ATOM   5532  N  N   . GLY E  1 148 ? 1.278   -31.205 49.327 1.00 22.94  ? 147 GLY E N   1 
ATOM   5533  C  CA  . GLY E  1 148 ? 0.352   -32.271 49.645 1.00 22.30  ? 147 GLY E CA  1 
ATOM   5534  C  C   . GLY E  1 148 ? -0.187  -32.107 51.070 1.00 23.95  ? 147 GLY E C   1 
ATOM   5535  O  O   . GLY E  1 148 ? 0.417   -31.427 51.907 1.00 23.61  ? 147 GLY E O   1 
ATOM   5536  N  N   . VAL E  1 149 ? -1.340  -32.723 51.345 1.00 24.04  ? 148 VAL E N   1 
ATOM   5537  C  CA  . VAL E  1 149 ? -1.837  -32.731 52.707 1.00 22.61  ? 148 VAL E CA  1 
ATOM   5538  C  C   . VAL E  1 149 ? -1.101  -33.812 53.498 1.00 21.70  ? 148 VAL E C   1 
ATOM   5539  O  O   . VAL E  1 149 ? -0.803  -34.882 52.977 1.00 21.48  ? 148 VAL E O   1 
ATOM   5540  C  CB  . VAL E  1 149 ? -3.370  -32.873 52.749 1.00 21.79  ? 148 VAL E CB  1 
ATOM   5541  C  CG1 . VAL E  1 149 ? -3.903  -32.770 54.182 1.00 21.34  ? 148 VAL E CG1 1 
ATOM   5542  C  CG2 . VAL E  1 149 ? -4.014  -31.822 51.854 1.00 20.45  ? 148 VAL E CG2 1 
ATOM   5543  N  N   . ILE E  1 150 ? -0.781  -33.490 54.745 1.00 21.85  ? 149 ILE E N   1 
ATOM   5544  C  CA  . ILE E  1 150 ? -0.009  -34.361 55.610 1.00 23.37  ? 149 ILE E CA  1 
ATOM   5545  C  C   . ILE E  1 150 ? -0.992  -35.288 56.317 1.00 22.78  ? 149 ILE E C   1 
ATOM   5546  O  O   . ILE E  1 150 ? -1.796  -34.832 57.134 1.00 23.00  ? 149 ILE E O   1 
ATOM   5547  C  CB  . ILE E  1 150 ? 0.774   -33.503 56.630 1.00 25.31  ? 149 ILE E CB  1 
ATOM   5548  C  CG1 . ILE E  1 150 ? 1.806   -32.605 55.949 1.00 24.02  ? 149 ILE E CG1 1 
ATOM   5549  C  CG2 . ILE E  1 150 ? 1.394   -34.362 57.723 1.00 25.93  ? 149 ILE E CG2 1 
ATOM   5550  C  CD1 . ILE E  1 150 ? 2.313   -31.496 56.835 1.00 24.67  ? 149 ILE E CD1 1 
ATOM   5551  N  N   . GLY E  1 151 ? -0.895  -36.586 56.010 1.00 21.55  ? 150 GLY E N   1 
ATOM   5552  C  CA  . GLY E  1 151 ? -1.889  -37.557 56.445 1.00 22.00  ? 150 GLY E CA  1 
ATOM   5553  C  C   . GLY E  1 151 ? -1.318  -38.714 57.256 1.00 21.62  ? 150 GLY E C   1 
ATOM   5554  O  O   . GLY E  1 151 ? -0.116  -38.952 57.225 1.00 22.70  ? 150 GLY E O   1 
ATOM   5555  N  N   . ILE E  1 152 ? -2.200  -39.424 57.974 1.00 21.90  ? 151 ILE E N   1 
ATOM   5556  C  CA  . ILE E  1 152 ? -1.811  -40.522 58.844 1.00 21.86  ? 151 ILE E CA  1 
ATOM   5557  C  C   . ILE E  1 152 ? -1.470  -41.731 57.983 1.00 23.35  ? 151 ILE E C   1 
ATOM   5558  O  O   . ILE E  1 152 ? -2.219  -42.041 57.068 1.00 23.63  ? 151 ILE E O   1 
ATOM   5559  C  CB  . ILE E  1 152 ? -2.926  -40.837 59.846 1.00 20.97  ? 151 ILE E CB  1 
ATOM   5560  C  CG1 . ILE E  1 152 ? -3.130  -39.675 60.805 1.00 21.97  ? 151 ILE E CG1 1 
ATOM   5561  C  CG2 . ILE E  1 152 ? -2.617  -42.092 60.616 1.00 19.57  ? 151 ILE E CG2 1 
ATOM   5562  C  CD1 . ILE E  1 152 ? -4.485  -39.627 61.470 1.00 26.04  ? 151 ILE E CD1 1 
ATOM   5563  N  N   . ALA E  1 153 ? -0.332  -42.381 58.292 1.00 24.24  ? 152 ALA E N   1 
ATOM   5564  C  CA  . ALA E  1 153 ? 0.144   -43.547 57.572 1.00 26.40  ? 152 ALA E CA  1 
ATOM   5565  C  C   . ALA E  1 153 ? 0.146   -44.760 58.502 1.00 30.34  ? 152 ALA E C   1 
ATOM   5566  O  O   . ALA E  1 153 ? 0.008   -44.614 59.719 1.00 28.84  ? 152 ALA E O   1 
ATOM   5567  C  CB  . ALA E  1 153 ? 1.516   -43.264 57.036 1.00 23.66  ? 152 ALA E CB  1 
ATOM   5568  N  N   . GLN E  1 154 ? 0.347   -45.953 57.924 1.00 38.02  ? 153 GLN E N   1 
ATOM   5569  C  CA  . GLN E  1 154 ? 0.374   -47.182 58.710 1.00 45.02  ? 153 GLN E CA  1 
ATOM   5570  C  C   . GLN E  1 154 ? 1.636   -47.273 59.586 1.00 49.38  ? 153 GLN E C   1 
ATOM   5571  O  O   . GLN E  1 154 ? 2.781   -47.117 59.113 1.00 48.55  ? 153 GLN E O   1 
ATOM   5572  C  CB  . GLN E  1 154 ? 0.269   -48.438 57.846 1.00 44.07  ? 153 GLN E CB  1 
ATOM   5573  C  CG  . GLN E  1 154 ? 0.235   -49.694 58.708 1.00 44.37  ? 153 GLN E CG  1 
ATOM   5574  C  CD  . GLN E  1 154 ? -0.413  -50.863 58.016 1.00 47.89  ? 153 GLN E CD  1 
ATOM   5575  O  OE1 . GLN E  1 154 ? 0.026   -51.277 56.951 1.00 52.73  ? 153 GLN E OE1 1 
ATOM   5576  N  NE2 . GLN E  1 154 ? -1.469  -51.398 58.610 1.00 52.08  ? 153 GLN E NE2 1 
ATOM   5577  O  OXT . GLN E  1 154 ? 1.507   -47.535 60.797 1.00 48.85  ? 153 GLN E OXT 1 
ATOM   5578  N  N   . ALA F  1 2   ? 44.116  -53.083 5.722  1.00 89.33  ? 1   ALA F N   1 
ATOM   5579  C  CA  . ALA F  1 2   ? 43.763  -51.924 6.610  1.00 80.93  ? 1   ALA F CA  1 
ATOM   5580  C  C   . ALA F  1 2   ? 44.965  -51.435 7.421  1.00 73.47  ? 1   ALA F C   1 
ATOM   5581  O  O   . ALA F  1 2   ? 45.850  -52.206 7.773  1.00 83.59  ? 1   ALA F O   1 
ATOM   5582  C  CB  . ALA F  1 2   ? 42.591  -52.269 7.498  1.00 79.52  ? 1   ALA F CB  1 
ATOM   5583  N  N   . THR F  1 3   ? 44.997  -50.136 7.698  1.00 59.24  ? 2   THR F N   1 
ATOM   5584  C  CA  . THR F  1 3   ? 46.044  -49.505 8.490  1.00 54.97  ? 2   THR F CA  1 
ATOM   5585  C  C   . THR F  1 3   ? 45.502  -49.162 9.882  1.00 47.23  ? 2   THR F C   1 
ATOM   5586  O  O   . THR F  1 3   ? 44.464  -48.513 10.015 1.00 49.58  ? 2   THR F O   1 
ATOM   5587  C  CB  . THR F  1 3   ? 46.706  -48.361 7.699  1.00 51.79  ? 2   THR F CB  1 
ATOM   5588  O  OG1 . THR F  1 3   ? 47.792  -47.726 8.370  1.00 51.53  ? 2   THR F OG1 1 
ATOM   5589  C  CG2 . THR F  1 3   ? 45.743  -47.298 7.223  1.00 56.25  ? 2   THR F CG2 1 
ATOM   5590  N  N   . LYS F  1 4   ? 46.154  -49.686 10.927 1.00 39.38  ? 3   LYS F N   1 
ATOM   5591  C  CA  . LYS F  1 4   ? 45.720  -49.523 12.309 1.00 37.74  ? 3   LYS F CA  1 
ATOM   5592  C  C   . LYS F  1 4   ? 46.777  -48.736 13.082 1.00 34.40  ? 3   LYS F C   1 
ATOM   5593  O  O   . LYS F  1 4   ? 47.977  -49.024 13.009 1.00 35.90  ? 3   LYS F O   1 
ATOM   5594  C  CB  . LYS F  1 4   ? 45.521  -50.867 13.023 1.00 43.52  ? 3   LYS F CB  1 
ATOM   5595  C  CG  . LYS F  1 4   ? 44.167  -51.536 12.840 1.00 51.35  ? 3   LYS F CG  1 
ATOM   5596  C  CD  . LYS F  1 4   ? 44.047  -52.935 13.433 1.00 53.95  ? 3   LYS F CD  1 
ATOM   5597  C  CE  . LYS F  1 4   ? 43.834  -53.038 14.940 1.00 54.56  ? 3   LYS F CE  1 
ATOM   5598  N  NZ  . LYS F  1 4   ? 42.546  -52.460 15.398 1.00 48.90  ? 3   LYS F NZ  1 
ATOM   5599  N  N   . VAL F  1 5   ? 46.300  -47.769 13.867 1.00 30.96  ? 4   VAL F N   1 
ATOM   5600  C  CA  . VAL F  1 5   ? 47.147  -46.868 14.624 1.00 28.27  ? 4   VAL F CA  1 
ATOM   5601  C  C   . VAL F  1 5   ? 46.569  -46.769 16.033 1.00 27.77  ? 4   VAL F C   1 
ATOM   5602  O  O   . VAL F  1 5   ? 45.380  -47.003 16.247 1.00 27.41  ? 4   VAL F O   1 
ATOM   5603  C  CB  . VAL F  1 5   ? 47.193  -45.505 13.915 1.00 27.26  ? 4   VAL F CB  1 
ATOM   5604  C  CG1 . VAL F  1 5   ? 47.725  -44.395 14.800 1.00 27.89  ? 4   VAL F CG1 1 
ATOM   5605  C  CG2 . VAL F  1 5   ? 47.969  -45.592 12.616 1.00 25.53  ? 4   VAL F CG2 1 
ATOM   5606  N  N   . VAL F  1 6   ? 47.416  -46.437 17.006 1.00 27.49  ? 5   VAL F N   1 
ATOM   5607  C  CA  . VAL F  1 6   ? 46.927  -46.371 18.371 1.00 26.37  ? 5   VAL F CA  1 
ATOM   5608  C  C   . VAL F  1 6   ? 47.601  -45.219 19.113 1.00 24.91  ? 5   VAL F C   1 
ATOM   5609  O  O   . VAL F  1 6   ? 48.646  -44.713 18.706 1.00 22.71  ? 5   VAL F O   1 
ATOM   5610  C  CB  . VAL F  1 6   ? 47.118  -47.710 19.101 1.00 25.45  ? 5   VAL F CB  1 
ATOM   5611  C  CG1 . VAL F  1 6   ? 48.594  -47.974 19.398 1.00 24.64  ? 5   VAL F CG1 1 
ATOM   5612  C  CG2 . VAL F  1 6   ? 46.283  -47.772 20.375 1.00 23.17  ? 5   VAL F CG2 1 
ATOM   5613  N  N   . CYS F  1 7   ? 46.989  -44.823 20.228 1.00 23.55  ? 6   CYS F N   1 
ATOM   5614  C  CA  . CYS F  1 7   ? 47.523  -43.736 21.014 1.00 23.37  ? 6   CYS F CA  1 
ATOM   5615  C  C   . CYS F  1 7   ? 47.118  -43.953 22.464 1.00 22.97  ? 6   CYS F C   1 
ATOM   5616  O  O   . CYS F  1 7   ? 45.941  -44.185 22.745 1.00 22.04  ? 6   CYS F O   1 
ATOM   5617  C  CB  . CYS F  1 7   ? 46.926  -42.434 20.507 1.00 23.89  ? 6   CYS F CB  1 
ATOM   5618  S  SG  . CYS F  1 7   ? 47.562  -40.979 21.371 1.00 25.76  ? 6   CYS F SG  1 
ATOM   5619  N  N   . VAL F  1 8   ? 48.106  -43.886 23.366 1.00 22.69  ? 7   VAL F N   1 
ATOM   5620  C  CA  . VAL F  1 8   ? 47.822  -43.975 24.791 1.00 23.09  ? 7   VAL F CA  1 
ATOM   5621  C  C   . VAL F  1 8   ? 47.886  -42.565 25.365 1.00 24.90  ? 7   VAL F C   1 
ATOM   5622  O  O   . VAL F  1 8   ? 48.930  -41.919 25.268 1.00 26.47  ? 7   VAL F O   1 
ATOM   5623  C  CB  . VAL F  1 8   ? 48.825  -44.897 25.504 1.00 21.27  ? 7   VAL F CB  1 
ATOM   5624  C  CG1 . VAL F  1 8   ? 48.626  -44.884 27.010 1.00 21.87  ? 7   VAL F CG1 1 
ATOM   5625  C  CG2 . VAL F  1 8   ? 48.774  -46.316 24.974 1.00 20.67  ? 7   VAL F CG2 1 
ATOM   5626  N  N   . LEU F  1 9   ? 46.784  -42.098 25.965 1.00 25.40  ? 8   LEU F N   1 
ATOM   5627  C  CA  . LEU F  1 9   ? 46.778  -40.757 26.527 1.00 26.21  ? 8   LEU F CA  1 
ATOM   5628  C  C   . LEU F  1 9   ? 47.149  -40.826 28.004 1.00 27.16  ? 8   LEU F C   1 
ATOM   5629  O  O   . LEU F  1 9   ? 46.511  -41.568 28.748 1.00 28.59  ? 8   LEU F O   1 
ATOM   5630  C  CB  . LEU F  1 9   ? 45.388  -40.141 26.359 1.00 26.07  ? 8   LEU F CB  1 
ATOM   5631  C  CG  . LEU F  1 9   ? 44.852  -40.065 24.935 1.00 27.13  ? 8   LEU F CG  1 
ATOM   5632  C  CD1 . LEU F  1 9   ? 43.366  -39.731 24.943 1.00 27.59  ? 8   LEU F CD1 1 
ATOM   5633  C  CD2 . LEU F  1 9   ? 45.595  -39.009 24.153 1.00 26.12  ? 8   LEU F CD2 1 
ATOM   5634  N  N   . LYS F  1 10  ? 48.173  -40.054 28.399 1.00 25.96  ? 9   LYS F N   1 
ATOM   5635  C  CA  . LYS F  1 10  ? 48.555  -39.855 29.789 1.00 27.01  ? 9   LYS F CA  1 
ATOM   5636  C  C   . LYS F  1 10  ? 48.802  -38.368 30.023 1.00 27.86  ? 9   LYS F C   1 
ATOM   5637  O  O   . LYS F  1 10  ? 49.058  -37.628 29.081 1.00 27.50  ? 9   LYS F O   1 
ATOM   5638  C  CB  . LYS F  1 10  ? 49.792  -40.680 30.176 1.00 25.69  ? 9   LYS F CB  1 
ATOM   5639  C  CG  . LYS F  1 10  ? 49.456  -42.109 30.586 0.60 28.43  ? 9   LYS F CG  1 
ATOM   5640  C  CD  . LYS F  1 10  ? 50.538  -43.064 30.936 0.60 29.51  ? 9   LYS F CD  1 
ATOM   5641  C  CE  . LYS F  1 10  ? 49.839  -44.397 30.988 0.60 27.63  ? 9   LYS F CE  1 
ATOM   5642  N  NZ  . LYS F  1 10  ? 50.658  -45.413 30.308 0.60 26.53  ? 9   LYS F NZ  1 
ATOM   5643  N  N   . GLY F  1 11  ? 48.719  -37.956 31.288 1.00 28.82  ? 10  GLY F N   1 
ATOM   5644  C  CA  . GLY F  1 11  ? 49.048  -36.593 31.675 1.00 32.49  ? 10  GLY F CA  1 
ATOM   5645  C  C   . GLY F  1 11  ? 49.419  -36.524 33.155 1.00 35.63  ? 10  GLY F C   1 
ATOM   5646  O  O   . GLY F  1 11  ? 49.616  -37.550 33.800 1.00 34.59  ? 10  GLY F O   1 
ATOM   5647  N  N   . ASP F  1 12  ? 49.454  -35.303 33.699 1.00 37.31  ? 11  ASP F N   1 
ATOM   5648  C  CA  . ASP F  1 12  ? 49.829  -35.102 35.087 1.00 38.51  ? 11  ASP F CA  1 
ATOM   5649  C  C   . ASP F  1 12  ? 48.713  -35.526 36.032 1.00 36.07  ? 11  ASP F C   1 
ATOM   5650  O  O   . ASP F  1 12  ? 48.988  -35.879 37.172 1.00 37.89  ? 11  ASP F O   1 
ATOM   5651  C  CB  . ASP F  1 12  ? 50.205  -33.644 35.333 1.00 45.69  ? 11  ASP F CB  1 
ATOM   5652  C  CG  . ASP F  1 12  ? 51.498  -33.304 34.614 1.00 54.45  ? 11  ASP F CG  1 
ATOM   5653  O  OD1 . ASP F  1 12  ? 52.383  -34.198 34.536 1.00 55.61  ? 11  ASP F OD1 1 
ATOM   5654  O  OD2 . ASP F  1 12  ? 51.600  -32.173 34.100 1.00 59.81  ? 11  ASP F OD2 1 
ATOM   5655  N  N   . GLY F  1 13  ? 47.466  -35.454 35.558 1.00 35.26  ? 12  GLY F N   1 
ATOM   5656  C  CA  . GLY F  1 13  ? 46.316  -35.704 36.407 1.00 36.09  ? 12  GLY F CA  1 
ATOM   5657  C  C   . GLY F  1 13  ? 45.839  -37.145 36.287 1.00 36.08  ? 12  GLY F C   1 
ATOM   5658  O  O   . GLY F  1 13  ? 46.595  -38.007 35.848 1.00 31.98  ? 12  GLY F O   1 
ATOM   5659  N  N   . PRO F  1 14  ? 44.563  -37.430 36.621 1.00 37.73  ? 13  PRO F N   1 
ATOM   5660  C  CA  . PRO F  1 14  ? 44.021  -38.781 36.508 1.00 35.68  ? 13  PRO F CA  1 
ATOM   5661  C  C   . PRO F  1 14  ? 43.507  -39.150 35.115 1.00 36.38  ? 13  PRO F C   1 
ATOM   5662  O  O   . PRO F  1 14  ? 43.011  -40.261 34.932 1.00 37.15  ? 13  PRO F O   1 
ATOM   5663  C  CB  . PRO F  1 14  ? 42.852  -38.704 37.511 1.00 36.17  ? 13  PRO F CB  1 
ATOM   5664  C  CG  . PRO F  1 14  ? 42.315  -37.271 37.382 1.00 36.99  ? 13  PRO F CG  1 
ATOM   5665  C  CD  . PRO F  1 14  ? 43.567  -36.457 37.112 1.00 39.32  ? 13  PRO F CD  1 
ATOM   5666  N  N   . VAL F  1 15  ? 43.614  -38.240 34.135 1.00 36.77  ? 14  VAL F N   1 
ATOM   5667  C  CA  . VAL F  1 15  ? 43.025  -38.545 32.839 1.00 36.89  ? 14  VAL F CA  1 
ATOM   5668  C  C   . VAL F  1 15  ? 43.927  -39.520 32.090 1.00 39.33  ? 14  VAL F C   1 
ATOM   5669  O  O   . VAL F  1 15  ? 45.126  -39.276 31.957 1.00 46.06  ? 14  VAL F O   1 
ATOM   5670  C  CB  . VAL F  1 15  ? 42.746  -37.282 32.010 1.00 34.89  ? 14  VAL F CB  1 
ATOM   5671  C  CG1 . VAL F  1 15  ? 42.200  -37.633 30.636 1.00 35.88  ? 14  VAL F CG1 1 
ATOM   5672  C  CG2 . VAL F  1 15  ? 41.763  -36.384 32.730 1.00 35.29  ? 14  VAL F CG2 1 
ATOM   5673  N  N   . GLN F  1 16  ? 43.340  -40.626 31.622 1.00 39.24  ? 15  GLN F N   1 
ATOM   5674  C  CA  . GLN F  1 16  ? 44.091  -41.579 30.825 1.00 36.75  ? 15  GLN F CA  1 
ATOM   5675  C  C   . GLN F  1 16  ? 43.140  -42.371 29.937 1.00 33.53  ? 15  GLN F C   1 
ATOM   5676  O  O   . GLN F  1 16  ? 41.962  -42.518 30.269 1.00 34.84  ? 15  GLN F O   1 
ATOM   5677  C  CB  . GLN F  1 16  ? 44.957  -42.482 31.698 1.00 41.76  ? 15  GLN F CB  1 
ATOM   5678  C  CG  . GLN F  1 16  ? 44.181  -43.358 32.666 1.00 50.08  ? 15  GLN F CG  1 
ATOM   5679  C  CD  . GLN F  1 16  ? 45.117  -44.044 33.633 1.00 55.93  ? 15  GLN F CD  1 
ATOM   5680  O  OE1 . GLN F  1 16  ? 46.320  -43.794 33.680 1.00 66.12  ? 15  GLN F OE1 1 
ATOM   5681  N  NE2 . GLN F  1 16  ? 44.582  -44.941 34.427 1.00 61.97  ? 15  GLN F NE2 1 
ATOM   5682  N  N   . GLY F  1 17  ? 43.669  -42.865 28.809 1.00 27.53  ? 16  GLY F N   1 
ATOM   5683  C  CA  . GLY F  1 17  ? 42.840  -43.606 27.882 1.00 25.58  ? 16  GLY F CA  1 
ATOM   5684  C  C   . GLY F  1 17  ? 43.634  -44.186 26.720 1.00 25.75  ? 16  GLY F C   1 
ATOM   5685  O  O   . GLY F  1 17  ? 44.814  -43.883 26.544 1.00 29.56  ? 16  GLY F O   1 
ATOM   5686  N  N   . ILE F  1 18  ? 42.952  -45.022 25.930 1.00 23.24  ? 17  ILE F N   1 
ATOM   5687  C  CA  . ILE F  1 18  ? 43.523  -45.609 24.732 1.00 21.79  ? 17  ILE F CA  1 
ATOM   5688  C  C   . ILE F  1 18  ? 42.600  -45.244 23.577 1.00 22.18  ? 17  ILE F C   1 
ATOM   5689  O  O   . ILE F  1 18  ? 41.390  -45.431 23.683 1.00 20.52  ? 17  ILE F O   1 
ATOM   5690  C  CB  . ILE F  1 18  ? 43.617  -47.139 24.899 1.00 21.20  ? 17  ILE F CB  1 
ATOM   5691  C  CG1 . ILE F  1 18  ? 44.550  -47.524 26.051 1.00 21.01  ? 17  ILE F CG1 1 
ATOM   5692  C  CG2 . ILE F  1 18  ? 43.985  -47.827 23.584 1.00 19.86  ? 17  ILE F CG2 1 
ATOM   5693  C  CD1 . ILE F  1 18  ? 44.645  -49.007 26.294 1.00 20.16  ? 17  ILE F CD1 1 
ATOM   5694  N  N   . ILE F  1 19  ? 43.166  -44.721 22.487 1.00 22.64  ? 18  ILE F N   1 
ATOM   5695  C  CA  . ILE F  1 19  ? 42.334  -44.403 21.336 1.00 23.10  ? 18  ILE F CA  1 
ATOM   5696  C  C   . ILE F  1 19  ? 42.903  -45.124 20.122 1.00 23.97  ? 18  ILE F C   1 
ATOM   5697  O  O   . ILE F  1 19  ? 44.098  -45.007 19.847 1.00 23.58  ? 18  ILE F O   1 
ATOM   5698  C  CB  . ILE F  1 19  ? 42.249  -42.882 21.096 1.00 21.85  ? 18  ILE F CB  1 
ATOM   5699  C  CG1 . ILE F  1 19  ? 41.639  -42.135 22.291 1.00 21.00  ? 18  ILE F CG1 1 
ATOM   5700  C  CG2 . ILE F  1 19  ? 41.508  -42.576 19.806 1.00 20.53  ? 18  ILE F CG2 1 
ATOM   5701  C  CD1 . ILE F  1 19  ? 40.197  -42.484 22.608 1.00 19.99  ? 18  ILE F CD1 1 
ATOM   5702  N  N   . ASN F  1 20  ? 42.033  -45.834 19.401 1.00 24.15  ? 19  ASN F N   1 
ATOM   5703  C  CA  . ASN F  1 20  ? 42.433  -46.533 18.194 1.00 25.48  ? 19  ASN F CA  1 
ATOM   5704  C  C   . ASN F  1 20  ? 41.997  -45.755 16.965 1.00 26.56  ? 19  ASN F C   1 
ATOM   5705  O  O   . ASN F  1 20  ? 40.965  -45.092 16.984 1.00 26.52  ? 19  ASN F O   1 
ATOM   5706  C  CB  . ASN F  1 20  ? 41.802  -47.923 18.122 1.00 24.86  ? 19  ASN F CB  1 
ATOM   5707  C  CG  . ASN F  1 20  ? 42.077  -48.707 19.372 1.00 24.28  ? 19  ASN F CG  1 
ATOM   5708  O  OD1 . ASN F  1 20  ? 41.229  -48.750 20.259 1.00 26.19  ? 19  ASN F OD1 1 
ATOM   5709  N  ND2 . ASN F  1 20  ? 43.275  -49.275 19.452 1.00 24.71  ? 19  ASN F ND2 1 
ATOM   5710  N  N   . PHE F  1 21  ? 42.795  -45.872 15.900 1.00 28.34  ? 20  PHE F N   1 
ATOM   5711  C  CA  . PHE F  1 21  ? 42.451  -45.289 14.617 1.00 31.68  ? 20  PHE F CA  1 
ATOM   5712  C  C   . PHE F  1 21  ? 42.556  -46.380 13.566 1.00 33.89  ? 20  PHE F C   1 
ATOM   5713  O  O   . PHE F  1 21  ? 43.538  -47.117 13.540 1.00 36.78  ? 20  PHE F O   1 
ATOM   5714  C  CB  . PHE F  1 21  ? 43.441  -44.191 14.234 1.00 30.20  ? 20  PHE F CB  1 
ATOM   5715  C  CG  . PHE F  1 21  ? 43.502  -43.012 15.168 1.00 31.65  ? 20  PHE F CG  1 
ATOM   5716  C  CD1 . PHE F  1 21  ? 44.053  -43.136 16.435 1.00 33.03  ? 20  PHE F CD1 1 
ATOM   5717  C  CD2 . PHE F  1 21  ? 43.020  -41.772 14.782 1.00 33.50  ? 20  PHE F CD2 1 
ATOM   5718  C  CE1 . PHE F  1 21  ? 44.121  -42.041 17.293 1.00 34.33  ? 20  PHE F CE1 1 
ATOM   5719  C  CE2 . PHE F  1 21  ? 43.105  -40.676 15.628 1.00 34.11  ? 20  PHE F CE2 1 
ATOM   5720  C  CZ  . PHE F  1 21  ? 43.656  -40.810 16.884 1.00 35.69  ? 20  PHE F CZ  1 
ATOM   5721  N  N   . GLU F  1 22  ? 41.550  -46.466 12.697 1.00 36.76  ? 21  GLU F N   1 
ATOM   5722  C  CA  . GLU F  1 22  ? 41.574  -47.468 11.649 1.00 39.75  ? 21  GLU F CA  1 
ATOM   5723  C  C   . GLU F  1 22  ? 41.083  -46.833 10.355 1.00 38.18  ? 21  GLU F C   1 
ATOM   5724  O  O   . GLU F  1 22  ? 40.136  -46.051 10.374 1.00 37.44  ? 21  GLU F O   1 
ATOM   5725  C  CB  . GLU F  1 22  ? 40.734  -48.674 12.063 1.00 47.29  ? 21  GLU F CB  1 
ATOM   5726  C  CG  . GLU F  1 22  ? 41.010  -49.905 11.211 1.00 52.58  ? 21  GLU F CG  1 
ATOM   5727  C  CD  . GLU F  1 22  ? 40.237  -51.154 11.616 1.00 58.79  ? 21  GLU F CD  1 
ATOM   5728  O  OE1 . GLU F  1 22  ? 40.320  -51.559 12.805 1.00 58.61  ? 21  GLU F OE1 1 
ATOM   5729  O  OE2 . GLU F  1 22  ? 39.531  -51.713 10.753 1.00 65.02  ? 21  GLU F OE2 1 
ATOM   5730  N  N   . GLN F  1 23  ? 41.739  -47.176 9.241  1.00 36.41  ? 22  GLN F N   1 
ATOM   5731  C  CA  . GLN F  1 23  ? 41.394  -46.629 7.939  1.00 35.93  ? 22  GLN F CA  1 
ATOM   5732  C  C   . GLN F  1 23  ? 41.423  -47.755 6.909  1.00 37.95  ? 22  GLN F C   1 
ATOM   5733  O  O   . GLN F  1 23  ? 42.502  -48.198 6.530  1.00 42.22  ? 22  GLN F O   1 
ATOM   5734  C  CB  . GLN F  1 23  ? 42.378  -45.520 7.574  1.00 33.78  ? 22  GLN F CB  1 
ATOM   5735  C  CG  . GLN F  1 23  ? 41.976  -44.735 6.341  1.00 35.79  ? 22  GLN F CG  1 
ATOM   5736  C  CD  . GLN F  1 23  ? 42.988  -43.687 5.940  1.00 38.48  ? 22  GLN F CD  1 
ATOM   5737  O  OE1 . GLN F  1 23  ? 44.197  -43.861 6.121  1.00 41.76  ? 22  GLN F OE1 1 
ATOM   5738  N  NE2 . GLN F  1 23  ? 42.496  -42.589 5.374  1.00 38.44  ? 22  GLN F NE2 1 
ATOM   5739  N  N   . LYS F  1 24  ? 40.239  -48.193 6.449  1.00 39.40  ? 23  LYS F N   1 
ATOM   5740  C  CA  . LYS F  1 24  ? 40.131  -49.374 5.596  1.00 42.73  ? 23  LYS F CA  1 
ATOM   5741  C  C   . LYS F  1 24  ? 40.677  -49.091 4.193  1.00 44.31  ? 23  LYS F C   1 
ATOM   5742  O  O   . LYS F  1 24  ? 41.515  -49.839 3.708  1.00 45.05  ? 23  LYS F O   1 
ATOM   5743  C  CB  . LYS F  1 24  ? 38.727  -49.999 5.636  1.00 42.61  ? 23  LYS F CB  1 
ATOM   5744  C  CG  . LYS F  1 24  ? 38.411  -50.805 6.892  1.00 40.80  ? 23  LYS F CG  1 
ATOM   5745  C  CD  . LYS F  1 24  ? 36.943  -51.159 7.049  0.40 39.99  ? 23  LYS F CD  1 
ATOM   5746  C  CE  . LYS F  1 24  ? 36.657  -51.890 8.343  0.40 38.01  ? 23  LYS F CE  1 
ATOM   5747  N  NZ  . LYS F  1 24  ? 35.431  -52.712 8.242  0.40 35.79  ? 23  LYS F NZ  1 
ATOM   5748  N  N   . GLU F  1 25  ? 40.241  -48.003 3.547  1.00 51.77  ? 24  GLU F N   1 
ATOM   5749  C  CA  . GLU F  1 25  ? 40.764  -47.628 2.239  1.00 57.22  ? 24  GLU F CA  1 
ATOM   5750  C  C   . GLU F  1 25  ? 41.740  -46.470 2.423  1.00 59.19  ? 24  GLU F C   1 
ATOM   5751  O  O   . GLU F  1 25  ? 41.621  -45.709 3.378  1.00 60.91  ? 24  GLU F O   1 
ATOM   5752  C  CB  . GLU F  1 25  ? 39.637  -47.222 1.280  1.00 60.93  ? 24  GLU F CB  1 
ATOM   5753  C  CG  . GLU F  1 25  ? 38.402  -48.110 1.294  1.00 61.29  ? 24  GLU F CG  1 
ATOM   5754  C  CD  . GLU F  1 25  ? 38.545  -49.517 0.729  1.00 61.76  ? 24  GLU F CD  1 
ATOM   5755  O  OE1 . GLU F  1 25  ? 39.479  -49.731 -0.057 1.00 61.83  ? 24  GLU F OE1 1 
ATOM   5756  O  OE2 . GLU F  1 25  ? 37.790  -50.407 1.165  1.00 58.11  ? 24  GLU F OE2 1 
ATOM   5757  N  N   . SER F  1 26  ? 42.671  -46.307 1.480  1.00 63.80  ? 25  SER F N   1 
ATOM   5758  C  CA  . SER F  1 26  ? 43.793  -45.400 1.671  1.00 70.55  ? 25  SER F CA  1 
ATOM   5759  C  C   . SER F  1 26  ? 43.361  -43.935 1.696  1.00 72.49  ? 25  SER F C   1 
ATOM   5760  O  O   . SER F  1 26  ? 43.994  -43.133 2.379  1.00 81.99  ? 25  SER F O   1 
ATOM   5761  C  CB  . SER F  1 26  ? 44.923  -45.643 0.697  1.00 65.97  ? 25  SER F CB  1 
ATOM   5762  O  OG  . SER F  1 26  ? 44.406  -45.999 -0.577 1.00 65.78  ? 25  SER F OG  1 
ATOM   5763  N  N   . ASN F  1 27  ? 42.307  -43.567 0.956  1.00 67.64  ? 26  ASN F N   1 
ATOM   5764  C  CA  . ASN F  1 27  ? 41.862  -42.189 1.028  1.00 67.85  ? 26  ASN F CA  1 
ATOM   5765  C  C   . ASN F  1 27  ? 40.522  -42.085 1.756  1.00 63.99  ? 26  ASN F C   1 
ATOM   5766  O  O   . ASN F  1 27  ? 39.854  -41.053 1.690  1.00 64.83  ? 26  ASN F O   1 
ATOM   5767  C  CB  . ASN F  1 27  ? 41.895  -41.561 -0.366 1.00 68.24  ? 26  ASN F CB  1 
ATOM   5768  C  CG  . ASN F  1 27  ? 41.826  -40.048 -0.377 1.00 67.24  ? 26  ASN F CG  1 
ATOM   5769  O  OD1 . ASN F  1 27  ? 42.280  -39.396 0.563  1.00 65.15  ? 26  ASN F OD1 1 
ATOM   5770  N  ND2 . ASN F  1 27  ? 41.223  -39.490 -1.415 1.00 67.61  ? 26  ASN F ND2 1 
ATOM   5771  N  N   . GLY F  1 28  ? 40.117  -43.179 2.418  1.00 55.64  ? 27  GLY F N   1 
ATOM   5772  C  CA  . GLY F  1 28  ? 38.786  -43.296 2.981  1.00 45.65  ? 27  GLY F CA  1 
ATOM   5773  C  C   . GLY F  1 28  ? 38.699  -42.729 4.394  1.00 38.66  ? 27  GLY F C   1 
ATOM   5774  O  O   . GLY F  1 28  ? 39.690  -42.263 4.954  1.00 39.40  ? 27  GLY F O   1 
ATOM   5775  N  N   . PRO F  1 29  ? 37.506  -42.765 5.028  1.00 35.49  ? 28  PRO F N   1 
ATOM   5776  C  CA  . PRO F  1 29  ? 37.330  -42.223 6.377  1.00 34.47  ? 28  PRO F CA  1 
ATOM   5777  C  C   . PRO F  1 29  ? 38.132  -43.006 7.416  1.00 32.61  ? 28  PRO F C   1 
ATOM   5778  O  O   . PRO F  1 29  ? 38.484  -44.163 7.184  1.00 34.03  ? 28  PRO F O   1 
ATOM   5779  C  CB  . PRO F  1 29  ? 35.822  -42.398 6.602  1.00 33.15  ? 28  PRO F CB  1 
ATOM   5780  C  CG  . PRO F  1 29  ? 35.436  -43.561 5.739  1.00 31.24  ? 28  PRO F CG  1 
ATOM   5781  C  CD  . PRO F  1 29  ? 36.275  -43.370 4.496  1.00 33.67  ? 28  PRO F CD  1 
ATOM   5782  N  N   . VAL F  1 30  ? 38.398  -42.357 8.555  1.00 28.63  ? 29  VAL F N   1 
ATOM   5783  C  CA  . VAL F  1 30  ? 39.139  -42.950 9.658  1.00 25.92  ? 29  VAL F CA  1 
ATOM   5784  C  C   . VAL F  1 30  ? 38.187  -43.145 10.834 1.00 25.29  ? 29  VAL F C   1 
ATOM   5785  O  O   . VAL F  1 30  ? 37.540  -42.198 11.266 1.00 26.13  ? 29  VAL F O   1 
ATOM   5786  C  CB  . VAL F  1 30  ? 40.325  -42.063 10.077 1.00 25.13  ? 29  VAL F CB  1 
ATOM   5787  C  CG1 . VAL F  1 30  ? 41.111  -42.687 11.222 1.00 24.44  ? 29  VAL F CG1 1 
ATOM   5788  C  CG2 . VAL F  1 30  ? 41.242  -41.729 8.911  1.00 24.76  ? 29  VAL F CG2 1 
ATOM   5789  N  N   . LYS F  1 31  ? 38.094  -44.382 11.336 1.00 24.84  ? 30  LYS F N   1 
ATOM   5790  C  CA  . LYS F  1 31  ? 37.304  -44.634 12.525 1.00 25.83  ? 30  LYS F CA  1 
ATOM   5791  C  C   . LYS F  1 31  ? 38.198  -44.375 13.734 1.00 28.11  ? 30  LYS F C   1 
ATOM   5792  O  O   . LYS F  1 31  ? 39.293  -44.916 13.829 1.00 28.01  ? 30  LYS F O   1 
ATOM   5793  C  CB  . LYS F  1 31  ? 36.717  -46.050 12.517 1.00 24.89  ? 30  LYS F CB  1 
ATOM   5794  C  CG  . LYS F  1 31  ? 35.396  -46.177 11.753 0.40 24.54  ? 30  LYS F CG  1 
ATOM   5795  C  CD  . LYS F  1 31  ? 34.936  -47.581 11.496 0.40 24.19  ? 30  LYS F CD  1 
ATOM   5796  C  CE  . LYS F  1 31  ? 34.075  -47.544 10.264 0.40 23.46  ? 30  LYS F CE  1 
ATOM   5797  N  NZ  . LYS F  1 31  ? 34.466  -48.600 9.308  0.40 22.95  ? 30  LYS F NZ  1 
ATOM   5798  N  N   . VAL F  1 32  ? 37.714  -43.537 14.650 1.00 28.40  ? 31  VAL F N   1 
ATOM   5799  C  CA  . VAL F  1 32  ? 38.461  -43.238 15.861 1.00 26.06  ? 31  VAL F CA  1 
ATOM   5800  C  C   . VAL F  1 32  ? 37.626  -43.713 17.044 1.00 25.92  ? 31  VAL F C   1 
ATOM   5801  O  O   . VAL F  1 32  ? 36.537  -43.193 17.268 1.00 26.08  ? 31  VAL F O   1 
ATOM   5802  C  CB  . VAL F  1 32  ? 38.750  -41.731 15.961 1.00 25.23  ? 31  VAL F CB  1 
ATOM   5803  C  CG1 . VAL F  1 32  ? 39.605  -41.405 17.173 1.00 25.31  ? 31  VAL F CG1 1 
ATOM   5804  C  CG2 . VAL F  1 32  ? 39.378  -41.198 14.687 1.00 25.01  ? 31  VAL F CG2 1 
ATOM   5805  N  N   . TRP F  1 33  ? 38.122  -44.698 17.795 1.00 26.92  ? 32  TRP F N   1 
ATOM   5806  C  CA  . TRP F  1 33  ? 37.343  -45.156 18.933 1.00 27.80  ? 32  TRP F CA  1 
ATOM   5807  C  C   . TRP F  1 33  ? 38.246  -45.557 20.092 1.00 27.07  ? 32  TRP F C   1 
ATOM   5808  O  O   . TRP F  1 33  ? 39.409  -45.915 19.907 1.00 30.75  ? 32  TRP F O   1 
ATOM   5809  C  CB  . TRP F  1 33  ? 36.425  -46.319 18.548 1.00 29.23  ? 32  TRP F CB  1 
ATOM   5810  C  CG  . TRP F  1 33  ? 37.126  -47.643 18.493 1.00 30.84  ? 32  TRP F CG  1 
ATOM   5811  C  CD1 . TRP F  1 33  ? 37.158  -48.620 19.451 1.00 30.73  ? 32  TRP F CD1 1 
ATOM   5812  C  CD2 . TRP F  1 33  ? 37.922  -48.128 17.402 1.00 32.44  ? 32  TRP F CD2 1 
ATOM   5813  N  NE1 . TRP F  1 33  ? 37.914  -49.681 19.030 1.00 32.26  ? 32  TRP F NE1 1 
ATOM   5814  C  CE2 . TRP F  1 33  ? 38.390  -49.412 17.770 1.00 32.38  ? 32  TRP F CE2 1 
ATOM   5815  C  CE3 . TRP F  1 33  ? 38.282  -47.600 16.155 1.00 35.33  ? 32  TRP F CE3 1 
ATOM   5816  C  CZ2 . TRP F  1 33  ? 39.198  -50.175 16.925 1.00 33.94  ? 32  TRP F CZ2 1 
ATOM   5817  C  CZ3 . TRP F  1 33  ? 39.085  -48.360 15.324 1.00 38.03  ? 32  TRP F CZ3 1 
ATOM   5818  C  CH2 . TRP F  1 33  ? 39.533  -49.631 15.703 1.00 35.41  ? 32  TRP F CH2 1 
ATOM   5819  N  N   . GLY F  1 34  ? 37.659  -45.546 21.283 1.00 23.90  ? 33  GLY F N   1 
ATOM   5820  C  CA  . GLY F  1 34  ? 38.317  -46.038 22.472 1.00 24.11  ? 33  GLY F CA  1 
ATOM   5821  C  C   . GLY F  1 34  ? 37.665  -45.437 23.703 1.00 24.74  ? 33  GLY F C   1 
ATOM   5822  O  O   . GLY F  1 34  ? 36.534  -44.978 23.658 1.00 26.09  ? 33  GLY F O   1 
ATOM   5823  N  N   . SER F  1 35  ? 38.412  -45.401 24.796 1.00 25.70  ? 34  SER F N   1 
ATOM   5824  C  CA  . SER F  1 35  ? 37.825  -44.981 26.047 1.00 26.74  ? 34  SER F CA  1 
ATOM   5825  C  C   . SER F  1 35  ? 38.802  -44.057 26.784 1.00 28.55  ? 34  SER F C   1 
ATOM   5826  O  O   . SER F  1 35  ? 40.008  -44.286 26.760 1.00 29.13  ? 34  SER F O   1 
ATOM   5827  C  CB  . SER F  1 35  ? 37.484  -46.219 26.800 1.00 26.70  ? 34  SER F CB  1 
ATOM   5828  O  OG  . SER F  1 35  ? 37.149  -45.909 28.129 1.00 32.30  ? 34  SER F OG  1 
ATOM   5829  N  N   . ILE F  1 36  ? 38.288  -42.979 27.393 1.00 27.79  ? 35  ILE F N   1 
ATOM   5830  C  CA  . ILE F  1 36  ? 39.096  -42.138 28.259 1.00 27.12  ? 35  ILE F CA  1 
ATOM   5831  C  C   . ILE F  1 36  ? 38.401  -42.060 29.614 1.00 30.23  ? 35  ILE F C   1 
ATOM   5832  O  O   . ILE F  1 36  ? 37.183  -41.902 29.673 1.00 29.55  ? 35  ILE F O   1 
ATOM   5833  C  CB  . ILE F  1 36  ? 39.275  -40.734 27.650 1.00 25.63  ? 35  ILE F CB  1 
ATOM   5834  C  CG1 . ILE F  1 36  ? 39.726  -40.810 26.192 1.00 24.84  ? 35  ILE F CG1 1 
ATOM   5835  C  CG2 . ILE F  1 36  ? 40.228  -39.896 28.497 1.00 24.43  ? 35  ILE F CG2 1 
ATOM   5836  C  CD1 . ILE F  1 36  ? 39.722  -39.480 25.480 1.00 25.00  ? 35  ILE F CD1 1 
ATOM   5837  N  N   . LYS F  1 37  ? 39.179  -42.168 30.696 1.00 32.10  ? 36  LYS F N   1 
ATOM   5838  C  CA  . LYS F  1 37  ? 38.597  -42.115 32.026 1.00 32.03  ? 36  LYS F CA  1 
ATOM   5839  C  C   . LYS F  1 37  ? 39.241  -40.986 32.825 1.00 30.31  ? 36  LYS F C   1 
ATOM   5840  O  O   . LYS F  1 37  ? 40.284  -40.459 32.430 1.00 29.06  ? 36  LYS F O   1 
ATOM   5841  C  CB  . LYS F  1 37  ? 38.689  -43.481 32.711 1.00 35.70  ? 36  LYS F CB  1 
ATOM   5842  C  CG  . LYS F  1 37  ? 40.093  -43.957 33.039 1.00 40.92  ? 36  LYS F CG  1 
ATOM   5843  C  CD  . LYS F  1 37  ? 40.060  -45.213 33.907 1.00 45.96  ? 36  LYS F CD  1 
ATOM   5844  C  CE  . LYS F  1 37  ? 41.410  -45.537 34.511 1.00 49.07  ? 36  LYS F CE  1 
ATOM   5845  N  NZ  . LYS F  1 37  ? 41.344  -46.290 35.792 1.00 54.85  ? 36  LYS F NZ  1 
ATOM   5846  N  N   . GLY F  1 38  ? 38.587  -40.609 33.935 1.00 29.73  ? 37  GLY F N   1 
ATOM   5847  C  CA  . GLY F  1 38  ? 39.092  -39.579 34.833 1.00 29.25  ? 37  GLY F CA  1 
ATOM   5848  C  C   . GLY F  1 38  ? 38.721  -38.154 34.413 1.00 29.40  ? 37  GLY F C   1 
ATOM   5849  O  O   . GLY F  1 38  ? 39.280  -37.191 34.947 1.00 28.80  ? 37  GLY F O   1 
ATOM   5850  N  N   . LEU F  1 39  ? 37.784  -38.017 33.466 1.00 29.64  ? 38  LEU F N   1 
ATOM   5851  C  CA  . LEU F  1 39  ? 37.373  -36.708 32.974 1.00 29.66  ? 38  LEU F CA  1 
ATOM   5852  C  C   . LEU F  1 39  ? 36.218  -36.185 33.825 1.00 30.71  ? 38  LEU F C   1 
ATOM   5853  O  O   . LEU F  1 39  ? 35.485  -36.963 34.428 1.00 29.87  ? 38  LEU F O   1 
ATOM   5854  C  CB  . LEU F  1 39  ? 36.912  -36.850 31.522 1.00 29.43  ? 38  LEU F CB  1 
ATOM   5855  C  CG  . LEU F  1 39  ? 38.009  -37.115 30.505 1.00 29.11  ? 38  LEU F CG  1 
ATOM   5856  C  CD1 . LEU F  1 39  ? 37.406  -37.620 29.203 1.00 29.04  ? 38  LEU F CD1 1 
ATOM   5857  C  CD2 . LEU F  1 39  ? 38.869  -35.882 30.283 1.00 29.24  ? 38  LEU F CD2 1 
ATOM   5858  N  N   . THR F  1 40  ? 36.059  -34.859 33.858 1.00 32.98  ? 39  THR F N   1 
ATOM   5859  C  CA  . THR F  1 40  ? 34.866  -34.259 34.437 1.00 33.55  ? 39  THR F CA  1 
ATOM   5860  C  C   . THR F  1 40  ? 33.704  -34.485 33.476 1.00 36.24  ? 39  THR F C   1 
ATOM   5861  O  O   . THR F  1 40  ? 33.910  -34.542 32.262 1.00 38.19  ? 39  THR F O   1 
ATOM   5862  C  CB  . THR F  1 40  ? 35.048  -32.757 34.688 1.00 30.00  ? 39  THR F CB  1 
ATOM   5863  O  OG1 . THR F  1 40  ? 35.546  -32.220 33.461 1.00 29.13  ? 39  THR F OG1 1 
ATOM   5864  C  CG2 . THR F  1 40  ? 35.984  -32.458 35.839 1.00 27.08  ? 39  THR F CG2 1 
ATOM   5865  N  N   . GLU F  1 41  ? 32.495  -34.616 34.030 1.00 36.76  ? 40  GLU F N   1 
ATOM   5866  C  CA  . GLU F  1 41  ? 31.319  -34.880 33.215 1.00 37.54  ? 40  GLU F CA  1 
ATOM   5867  C  C   . GLU F  1 41  ? 31.181  -33.776 32.169 1.00 33.54  ? 40  GLU F C   1 
ATOM   5868  O  O   . GLU F  1 41  ? 31.444  -32.617 32.469 1.00 34.16  ? 40  GLU F O   1 
ATOM   5869  C  CB  . GLU F  1 41  ? 30.071  -34.965 34.094 1.00 39.66  ? 40  GLU F CB  1 
ATOM   5870  C  CG  . GLU F  1 41  ? 28.844  -35.358 33.300 1.00 43.44  ? 40  GLU F CG  1 
ATOM   5871  C  CD  . GLU F  1 41  ? 27.549  -35.559 34.046 1.00 48.39  ? 40  GLU F CD  1 
ATOM   5872  O  OE1 . GLU F  1 41  ? 27.512  -35.243 35.245 1.00 52.59  ? 40  GLU F OE1 1 
ATOM   5873  O  OE2 . GLU F  1 41  ? 26.585  -36.039 33.416 1.00 50.03  ? 40  GLU F OE2 1 
ATOM   5874  N  N   . GLY F  1 42  ? 30.802  -34.146 30.941 1.00 29.48  ? 41  GLY F N   1 
ATOM   5875  C  CA  . GLY F  1 42  ? 30.542  -33.150 29.918 1.00 30.82  ? 41  GLY F CA  1 
ATOM   5876  C  C   . GLY F  1 42  ? 31.513  -33.218 28.737 1.00 33.94  ? 41  GLY F C   1 
ATOM   5877  O  O   . GLY F  1 42  ? 32.209  -34.218 28.547 1.00 36.23  ? 41  GLY F O   1 
ATOM   5878  N  N   . LEU F  1 43  ? 31.530  -32.138 27.936 1.00 33.06  ? 42  LEU F N   1 
ATOM   5879  C  CA  . LEU F  1 43  ? 32.258  -32.082 26.676 1.00 30.13  ? 42  LEU F CA  1 
ATOM   5880  C  C   . LEU F  1 43  ? 33.724  -31.756 26.930 1.00 28.73  ? 42  LEU F C   1 
ATOM   5881  O  O   . LEU F  1 43  ? 34.031  -30.943 27.795 1.00 27.10  ? 42  LEU F O   1 
ATOM   5882  C  CB  . LEU F  1 43  ? 31.637  -31.015 25.777 1.00 29.82  ? 42  LEU F CB  1 
ATOM   5883  C  CG  . LEU F  1 43  ? 30.226  -31.293 25.275 1.00 30.98  ? 42  LEU F CG  1 
ATOM   5884  C  CD1 . LEU F  1 43  ? 29.656  -30.063 24.593 1.00 32.30  ? 42  LEU F CD1 1 
ATOM   5885  C  CD2 . LEU F  1 43  ? 30.217  -32.461 24.308 1.00 31.71  ? 42  LEU F CD2 1 
ATOM   5886  N  N   . HIS F  1 44  ? 34.607  -32.402 26.156 1.00 28.12  ? 43  HIS F N   1 
ATOM   5887  C  CA  . HIS F  1 44  ? 36.038  -32.137 26.168 1.00 26.09  ? 43  HIS F CA  1 
ATOM   5888  C  C   . HIS F  1 44  ? 36.561  -32.082 24.737 1.00 26.31  ? 43  HIS F C   1 
ATOM   5889  O  O   . HIS F  1 44  ? 36.246  -32.939 23.906 1.00 27.55  ? 43  HIS F O   1 
ATOM   5890  C  CB  . HIS F  1 44  ? 36.783  -33.183 26.992 1.00 24.88  ? 43  HIS F CB  1 
ATOM   5891  C  CG  . HIS F  1 44  ? 36.442  -33.155 28.446 1.00 26.45  ? 43  HIS F CG  1 
ATOM   5892  N  ND1 . HIS F  1 44  ? 37.205  -32.463 29.377 1.00 25.20  ? 43  HIS F ND1 1 
ATOM   5893  C  CD2 . HIS F  1 44  ? 35.446  -33.750 29.146 1.00 26.03  ? 43  HIS F CD2 1 
ATOM   5894  C  CE1 . HIS F  1 44  ? 36.700  -32.637 30.585 1.00 23.89  ? 43  HIS F CE1 1 
ATOM   5895  N  NE2 . HIS F  1 44  ? 35.615  -33.421 30.468 1.00 24.70  ? 43  HIS F NE2 1 
ATOM   5896  N  N   . GLY F  1 45  ? 37.340  -31.032 24.463 1.00 25.41  ? 44  GLY F N   1 
ATOM   5897  C  CA  . GLY F  1 45  ? 37.955  -30.843 23.162 1.00 24.59  ? 44  GLY F CA  1 
ATOM   5898  C  C   . GLY F  1 45  ? 38.948  -31.964 22.865 1.00 23.60  ? 44  GLY F C   1 
ATOM   5899  O  O   . GLY F  1 45  ? 39.665  -32.437 23.753 1.00 21.70  ? 44  GLY F O   1 
ATOM   5900  N  N   . PHE F  1 46  ? 38.982  -32.362 21.592 1.00 23.83  ? 45  PHE F N   1 
ATOM   5901  C  CA  . PHE F  1 46  ? 39.673  -33.569 21.188 1.00 25.32  ? 45  PHE F CA  1 
ATOM   5902  C  C   . PHE F  1 46  ? 40.366  -33.282 19.864 1.00 25.27  ? 45  PHE F C   1 
ATOM   5903  O  O   . PHE F  1 46  ? 39.688  -33.162 18.840 1.00 26.60  ? 45  PHE F O   1 
ATOM   5904  C  CB  . PHE F  1 46  ? 38.619  -34.664 21.017 1.00 25.46  ? 45  PHE F CB  1 
ATOM   5905  C  CG  . PHE F  1 46  ? 39.124  -36.076 20.893 1.00 25.09  ? 45  PHE F CG  1 
ATOM   5906  C  CD1 . PHE F  1 46  ? 39.773  -36.696 21.956 1.00 24.02  ? 45  PHE F CD1 1 
ATOM   5907  C  CD2 . PHE F  1 46  ? 38.899  -36.800 19.731 1.00 24.76  ? 45  PHE F CD2 1 
ATOM   5908  C  CE1 . PHE F  1 46  ? 40.202  -38.010 21.849 1.00 23.99  ? 45  PHE F CE1 1 
ATOM   5909  C  CE2 . PHE F  1 46  ? 39.337  -38.110 19.629 1.00 25.35  ? 45  PHE F CE2 1 
ATOM   5910  C  CZ  . PHE F  1 46  ? 39.996  -38.711 20.686 1.00 24.66  ? 45  PHE F CZ  1 
ATOM   5911  N  N   . HIS F  1 47  ? 41.698  -33.146 19.899 1.00 24.19  ? 46  HIS F N   1 
ATOM   5912  C  CA  . HIS F  1 47  ? 42.405  -32.670 18.723 1.00 25.62  ? 46  HIS F CA  1 
ATOM   5913  C  C   . HIS F  1 47  ? 43.704  -33.422 18.500 1.00 26.55  ? 46  HIS F C   1 
ATOM   5914  O  O   . HIS F  1 47  ? 44.332  -33.927 19.437 1.00 26.94  ? 46  HIS F O   1 
ATOM   5915  C  CB  . HIS F  1 47  ? 42.742  -31.179 18.852 1.00 27.10  ? 46  HIS F CB  1 
ATOM   5916  C  CG  . HIS F  1 47  ? 41.624  -30.367 19.412 1.00 26.08  ? 46  HIS F CG  1 
ATOM   5917  N  ND1 . HIS F  1 47  ? 41.680  -29.834 20.679 1.00 24.88  ? 46  HIS F ND1 1 
ATOM   5918  C  CD2 . HIS F  1 47  ? 40.426  -30.019 18.890 1.00 26.28  ? 46  HIS F CD2 1 
ATOM   5919  C  CE1 . HIS F  1 47  ? 40.556  -29.189 20.919 1.00 26.44  ? 46  HIS F CE1 1 
ATOM   5920  N  NE2 . HIS F  1 47  ? 39.767  -29.289 19.836 1.00 26.39  ? 46  HIS F NE2 1 
ATOM   5921  N  N   . VAL F  1 48  ? 44.093  -33.464 17.217 1.00 25.09  ? 47  VAL F N   1 
ATOM   5922  C  CA  . VAL F  1 48  ? 45.448  -33.840 16.863 1.00 24.45  ? 47  VAL F CA  1 
ATOM   5923  C  C   . VAL F  1 48  ? 46.283  -32.569 16.790 1.00 24.47  ? 47  VAL F C   1 
ATOM   5924  O  O   . VAL F  1 48  ? 46.017  -31.711 15.952 1.00 25.57  ? 47  VAL F O   1 
ATOM   5925  C  CB  . VAL F  1 48  ? 45.497  -34.622 15.539 1.00 24.38  ? 47  VAL F CB  1 
ATOM   5926  C  CG1 . VAL F  1 48  ? 46.914  -35.060 15.215 1.00 23.88  ? 47  VAL F CG1 1 
ATOM   5927  C  CG2 . VAL F  1 48  ? 44.600  -35.851 15.591 1.00 23.23  ? 47  VAL F CG2 1 
ATOM   5928  N  N   . HIS F  1 49  ? 47.292  -32.470 17.665 1.00 23.90  ? 48  HIS F N   1 
ATOM   5929  C  CA  . HIS F  1 49  ? 48.272  -31.396 17.609 1.00 23.52  ? 48  HIS F CA  1 
ATOM   5930  C  C   . HIS F  1 49  ? 49.429  -31.780 16.688 1.00 24.14  ? 48  HIS F C   1 
ATOM   5931  O  O   . HIS F  1 49  ? 49.561  -32.936 16.297 1.00 24.97  ? 48  HIS F O   1 
ATOM   5932  C  CB  . HIS F  1 49  ? 48.723  -31.024 19.020 1.00 22.74  ? 48  HIS F CB  1 
ATOM   5933  C  CG  . HIS F  1 49  ? 47.643  -30.424 19.847 1.00 23.27  ? 48  HIS F CG  1 
ATOM   5934  N  ND1 . HIS F  1 49  ? 47.746  -29.150 20.383 1.00 23.53  ? 48  HIS F ND1 1 
ATOM   5935  C  CD2 . HIS F  1 49  ? 46.436  -30.904 20.224 1.00 25.25  ? 48  HIS F CD2 1 
ATOM   5936  C  CE1 . HIS F  1 49  ? 46.652  -28.874 21.070 1.00 25.51  ? 48  HIS F CE1 1 
ATOM   5937  N  NE2 . HIS F  1 49  ? 45.826  -29.939 20.987 1.00 27.06  ? 48  HIS F NE2 1 
ATOM   5938  N  N   . GLU F  1 50  ? 50.289  -30.801 16.381 1.00 25.15  ? 49  GLU F N   1 
ATOM   5939  C  CA  . GLU F  1 50  ? 51.235  -30.877 15.274 1.00 25.43  ? 49  GLU F CA  1 
ATOM   5940  C  C   . GLU F  1 50  ? 52.387  -31.841 15.547 1.00 25.02  ? 49  GLU F C   1 
ATOM   5941  O  O   . GLU F  1 50  ? 52.778  -32.584 14.650 1.00 26.06  ? 49  GLU F O   1 
ATOM   5942  C  CB  . GLU F  1 50  ? 51.811  -29.495 14.976 1.00 26.61  ? 49  GLU F CB  1 
ATOM   5943  C  CG  . GLU F  1 50  ? 52.488  -29.435 13.623 1.00 29.49  ? 49  GLU F CG  1 
ATOM   5944  C  CD  . GLU F  1 50  ? 53.073  -28.078 13.252 1.00 31.12  ? 49  GLU F CD  1 
ATOM   5945  O  OE1 . GLU F  1 50  ? 52.682  -27.058 13.851 1.00 32.14  ? 49  GLU F OE1 1 
ATOM   5946  O  OE2 . GLU F  1 50  ? 53.931  -28.039 12.363 1.00 34.53  ? 49  GLU F OE2 1 
ATOM   5947  N  N   . PHE F  1 51  ? 52.941  -31.804 16.766 1.00 23.56  ? 50  PHE F N   1 
ATOM   5948  C  CA  . PHE F  1 51  ? 54.204  -32.470 17.037 1.00 22.81  ? 50  PHE F CA  1 
ATOM   5949  C  C   . PHE F  1 51  ? 54.022  -33.657 17.975 1.00 24.15  ? 50  PHE F C   1 
ATOM   5950  O  O   . PHE F  1 51  ? 53.391  -33.533 19.028 1.00 22.43  ? 50  PHE F O   1 
ATOM   5951  C  CB  . PHE F  1 51  ? 55.187  -31.499 17.681 1.00 22.54  ? 50  PHE F CB  1 
ATOM   5952  C  CG  . PHE F  1 51  ? 55.413  -30.258 16.865 1.00 22.45  ? 50  PHE F CG  1 
ATOM   5953  C  CD1 . PHE F  1 51  ? 55.842  -30.353 15.545 1.00 21.63  ? 50  PHE F CD1 1 
ATOM   5954  C  CD2 . PHE F  1 51  ? 55.167  -29.000 17.403 1.00 22.02  ? 50  PHE F CD2 1 
ATOM   5955  C  CE1 . PHE F  1 51  ? 56.026  -29.213 14.776 1.00 21.89  ? 50  PHE F CE1 1 
ATOM   5956  C  CE2 . PHE F  1 51  ? 55.342  -27.862 16.633 1.00 22.60  ? 50  PHE F CE2 1 
ATOM   5957  C  CZ  . PHE F  1 51  ? 55.780  -27.969 15.327 1.00 22.62  ? 50  PHE F CZ  1 
ATOM   5958  N  N   . GLY F  1 52  ? 54.624  -34.789 17.578 1.00 25.60  ? 51  GLY F N   1 
ATOM   5959  C  CA  . GLY F  1 52  ? 54.798  -35.946 18.441 1.00 25.07  ? 51  GLY F CA  1 
ATOM   5960  C  C   . GLY F  1 52  ? 55.946  -35.714 19.420 1.00 25.37  ? 51  GLY F C   1 
ATOM   5961  O  O   . GLY F  1 52  ? 56.891  -36.491 19.485 1.00 26.69  ? 51  GLY F O   1 
ATOM   5962  N  N   . ASP F  1 53  ? 55.856  -34.619 20.172 1.00 25.21  ? 52  ASP F N   1 
ATOM   5963  C  CA  . ASP F  1 53  ? 56.954  -34.196 21.018 1.00 24.15  ? 52  ASP F CA  1 
ATOM   5964  C  C   . ASP F  1 53  ? 56.416  -34.020 22.434 1.00 23.75  ? 52  ASP F C   1 
ATOM   5965  O  O   . ASP F  1 53  ? 55.573  -33.162 22.683 1.00 23.59  ? 52  ASP F O   1 
ATOM   5966  C  CB  . ASP F  1 53  ? 57.569  -32.914 20.465 1.00 23.92  ? 52  ASP F CB  1 
ATOM   5967  C  CG  . ASP F  1 53  ? 58.729  -32.363 21.275 1.00 25.02  ? 52  ASP F CG  1 
ATOM   5968  O  OD1 . ASP F  1 53  ? 58.821  -32.678 22.490 1.00 24.07  ? 52  ASP F OD1 1 
ATOM   5969  O  OD2 . ASP F  1 53  ? 59.504  -31.588 20.682 1.00 26.57  ? 52  ASP F OD2 1 
ATOM   5970  N  N   . ASN F  1 54  ? 56.905  -34.851 23.349 1.00 24.68  ? 53  ASN F N   1 
ATOM   5971  C  CA  . ASN F  1 54  ? 56.400  -34.848 24.706 1.00 27.37  ? 53  ASN F CA  1 
ATOM   5972  C  C   . ASN F  1 54  ? 57.512  -34.399 25.655 1.00 27.26  ? 53  ASN F C   1 
ATOM   5973  O  O   . ASN F  1 54  ? 57.426  -34.604 26.860 1.00 25.84  ? 53  ASN F O   1 
ATOM   5974  C  CB  . ASN F  1 54  ? 55.779  -36.212 25.031 1.00 32.20  ? 53  ASN F CB  1 
ATOM   5975  C  CG  . ASN F  1 54  ? 55.186  -36.308 26.426 1.00 38.13  ? 53  ASN F CG  1 
ATOM   5976  O  OD1 . ASN F  1 54  ? 54.341  -35.480 26.805 1.00 44.55  ? 53  ASN F OD1 1 
ATOM   5977  N  ND2 . ASN F  1 54  ? 55.607  -37.328 27.176 1.00 35.87  ? 53  ASN F ND2 1 
ATOM   5978  N  N   . THR F  1 55  ? 58.547  -33.744 25.107 1.00 28.32  ? 54  THR F N   1 
ATOM   5979  C  CA  . THR F  1 55  ? 59.739  -33.420 25.879 1.00 27.19  ? 54  THR F CA  1 
ATOM   5980  C  C   . THR F  1 55  ? 59.400  -32.525 27.067 1.00 28.32  ? 54  THR F C   1 
ATOM   5981  O  O   . THR F  1 55  ? 60.054  -32.609 28.098 1.00 28.48  ? 54  THR F O   1 
ATOM   5982  C  CB  . THR F  1 55  ? 60.826  -32.753 25.030 1.00 25.87  ? 54  THR F CB  1 
ATOM   5983  O  OG1 . THR F  1 55  ? 60.262  -31.583 24.452 1.00 23.91  ? 54  THR F OG1 1 
ATOM   5984  C  CG2 . THR F  1 55  ? 61.356  -33.633 23.923 1.00 26.48  ? 54  THR F CG2 1 
ATOM   5985  N  N   . ALA F  1 56  ? 58.386  -31.669 26.912 1.00 30.21  ? 55  ALA F N   1 
ATOM   5986  C  CA  . ALA F  1 56  ? 57.992  -30.749 27.965 1.00 30.88  ? 55  ALA F CA  1 
ATOM   5987  C  C   . ALA F  1 56  ? 56.526  -30.990 28.307 1.00 32.94  ? 55  ALA F C   1 
ATOM   5988  O  O   . ALA F  1 56  ? 55.764  -30.045 28.458 1.00 35.02  ? 55  ALA F O   1 
ATOM   5989  C  CB  . ALA F  1 56  ? 58.226  -29.334 27.501 1.00 29.64  ? 55  ALA F CB  1 
ATOM   5990  N  N   . GLY F  1 57  ? 56.135  -32.264 28.412 1.00 32.92  ? 56  GLY F N   1 
ATOM   5991  C  CA  . GLY F  1 57  ? 54.738  -32.616 28.620 1.00 33.73  ? 56  GLY F CA  1 
ATOM   5992  C  C   . GLY F  1 57  ? 53.898  -32.367 27.366 1.00 36.48  ? 56  GLY F C   1 
ATOM   5993  O  O   . GLY F  1 57  ? 54.434  -32.316 26.257 1.00 36.11  ? 56  GLY F O   1 
ATOM   5994  N  N   . CYS F  1 58  ? 52.589  -32.189 27.558 1.00 36.62  ? 57  CYS F N   1 
ATOM   5995  C  CA  . CYS F  1 58  ? 51.679  -32.031 26.436 1.00 33.92  ? 57  CYS F CA  1 
ATOM   5996  C  C   . CYS F  1 58  ? 51.908  -30.699 25.723 1.00 33.40  ? 57  CYS F C   1 
ATOM   5997  O  O   . CYS F  1 58  ? 51.587  -30.592 24.543 1.00 33.13  ? 57  CYS F O   1 
ATOM   5998  C  CB  . CYS F  1 58  ? 50.222  -32.140 26.873 1.00 31.99  ? 57  CYS F CB  1 
ATOM   5999  S  SG  . CYS F  1 58  ? 49.801  -33.818 27.418 1.00 38.42  ? 57  CYS F SG  1 
ATOM   6000  N  N   . THR F  1 59  ? 52.504  -29.723 26.420 1.00 31.94  ? 58  THR F N   1 
ATOM   6001  C  CA  . THR F  1 59  ? 52.726  -28.395 25.864 1.00 29.54  ? 58  THR F CA  1 
ATOM   6002  C  C   . THR F  1 59  ? 53.536  -28.479 24.575 1.00 29.19  ? 58  THR F C   1 
ATOM   6003  O  O   . THR F  1 59  ? 53.287  -27.726 23.634 1.00 28.46  ? 58  THR F O   1 
ATOM   6004  C  CB  . THR F  1 59  ? 53.575  -27.514 26.790 1.00 28.02  ? 58  THR F CB  1 
ATOM   6005  O  OG1 . THR F  1 59  ? 53.014  -27.596 28.095 1.00 27.66  ? 58  THR F OG1 1 
ATOM   6006  C  CG2 . THR F  1 59  ? 53.647  -26.075 26.329 1.00 26.24  ? 58  THR F CG2 1 
ATOM   6007  N  N   . SER F  1 60  ? 54.524  -29.379 24.552 1.00 30.01  ? 59  SER F N   1 
ATOM   6008  C  CA  . SER F  1 60  ? 55.494  -29.349 23.473 1.00 30.35  ? 59  SER F CA  1 
ATOM   6009  C  C   . SER F  1 60  ? 54.911  -29.974 22.204 1.00 29.74  ? 59  SER F C   1 
ATOM   6010  O  O   . SER F  1 60  ? 55.582  -30.029 21.172 1.00 29.39  ? 59  SER F O   1 
ATOM   6011  C  CB  . SER F  1 60  ? 56.833  -29.915 23.890 1.00 32.70  ? 59  SER F CB  1 
ATOM   6012  O  OG  . SER F  1 60  ? 56.687  -31.218 24.432 1.00 35.35  ? 59  SER F OG  1 
ATOM   6013  N  N   . ALA F  1 61  ? 53.629  -30.375 22.277 1.00 28.14  ? 60  ALA F N   1 
ATOM   6014  C  CA  . ALA F  1 61  ? 52.914  -30.949 21.149 1.00 26.44  ? 60  ALA F CA  1 
ATOM   6015  C  C   . ALA F  1 61  ? 52.591  -29.866 20.120 1.00 26.09  ? 60  ALA F C   1 
ATOM   6016  O  O   . ALA F  1 61  ? 52.292  -30.172 18.966 1.00 24.27  ? 60  ALA F O   1 
ATOM   6017  C  CB  . ALA F  1 61  ? 51.661  -31.629 21.629 1.00 23.19  ? 60  ALA F CB  1 
ATOM   6018  N  N   . GLY F  1 62  ? 52.650  -28.603 20.562 1.00 26.86  ? 61  GLY F N   1 
ATOM   6019  C  CA  . GLY F  1 62  ? 52.398  -27.458 19.708 1.00 28.81  ? 61  GLY F CA  1 
ATOM   6020  C  C   . GLY F  1 62  ? 50.908  -27.241 19.456 1.00 30.63  ? 61  GLY F C   1 
ATOM   6021  O  O   . GLY F  1 62  ? 50.067  -27.728 20.220 1.00 29.80  ? 61  GLY F O   1 
ATOM   6022  N  N   . PRO F  1 63  ? 50.541  -26.515 18.363 1.00 29.98  ? 62  PRO F N   1 
ATOM   6023  C  CA  . PRO F  1 63  ? 49.142  -26.157 18.097 1.00 28.96  ? 62  PRO F CA  1 
ATOM   6024  C  C   . PRO F  1 63  ? 48.369  -27.298 17.441 1.00 27.19  ? 62  PRO F C   1 
ATOM   6025  O  O   . PRO F  1 63  ? 48.941  -28.349 17.168 1.00 28.85  ? 62  PRO F O   1 
ATOM   6026  C  CB  . PRO F  1 63  ? 49.312  -25.005 17.099 1.00 28.24  ? 62  PRO F CB  1 
ATOM   6027  C  CG  . PRO F  1 63  ? 50.528  -25.405 16.299 1.00 27.32  ? 62  PRO F CG  1 
ATOM   6028  C  CD  . PRO F  1 63  ? 51.456  -26.044 17.309 1.00 27.30  ? 62  PRO F CD  1 
ATOM   6029  N  N   . HIS F  1 64  ? 47.072  -27.084 17.181 1.00 26.82  ? 63  HIS F N   1 
ATOM   6030  C  CA  . HIS F  1 64  ? 46.305  -28.063 16.422 1.00 26.51  ? 63  HIS F CA  1 
ATOM   6031  C  C   . HIS F  1 64  ? 47.003  -28.300 15.085 1.00 26.05  ? 63  HIS F C   1 
ATOM   6032  O  O   . HIS F  1 64  ? 47.442  -27.342 14.457 1.00 27.65  ? 63  HIS F O   1 
ATOM   6033  C  CB  . HIS F  1 64  ? 44.868  -27.585 16.193 1.00 25.67  ? 63  HIS F CB  1 
ATOM   6034  C  CG  . HIS F  1 64  ? 44.054  -27.399 17.427 1.00 24.85  ? 63  HIS F CG  1 
ATOM   6035  N  ND1 . HIS F  1 64  ? 42.791  -26.838 17.383 1.00 24.98  ? 63  HIS F ND1 1 
ATOM   6036  C  CD2 . HIS F  1 64  ? 44.297  -27.701 18.720 1.00 24.76  ? 63  HIS F CD2 1 
ATOM   6037  C  CE1 . HIS F  1 64  ? 42.287  -26.796 18.601 1.00 25.67  ? 63  HIS F CE1 1 
ATOM   6038  N  NE2 . HIS F  1 64  ? 43.195  -27.326 19.447 1.00 25.64  ? 63  HIS F NE2 1 
ATOM   6039  N  N   . PHE F  1 65  ? 47.101  -29.564 14.663 1.00 24.07  ? 64  PHE F N   1 
ATOM   6040  C  CA  . PHE F  1 65  ? 47.691  -29.917 13.380 1.00 25.29  ? 64  PHE F CA  1 
ATOM   6041  C  C   . PHE F  1 65  ? 46.988  -29.171 12.247 1.00 26.48  ? 64  PHE F C   1 
ATOM   6042  O  O   . PHE F  1 65  ? 45.811  -29.390 11.997 1.00 27.71  ? 64  PHE F O   1 
ATOM   6043  C  CB  . PHE F  1 65  ? 47.684  -31.437 13.181 1.00 25.90  ? 64  PHE F CB  1 
ATOM   6044  C  CG  . PHE F  1 65  ? 48.272  -31.913 11.873 1.00 26.41  ? 64  PHE F CG  1 
ATOM   6045  C  CD1 . PHE F  1 65  ? 49.448  -31.360 11.382 1.00 26.87  ? 64  PHE F CD1 1 
ATOM   6046  C  CD2 . PHE F  1 65  ? 47.665  -32.926 11.139 1.00 26.21  ? 64  PHE F CD2 1 
ATOM   6047  C  CE1 . PHE F  1 65  ? 49.995  -31.792 10.185 1.00 26.46  ? 64  PHE F CE1 1 
ATOM   6048  C  CE2 . PHE F  1 65  ? 48.216  -33.363 9.940  1.00 25.67  ? 64  PHE F CE2 1 
ATOM   6049  C  CZ  . PHE F  1 65  ? 49.382  -32.797 9.468  1.00 26.60  ? 64  PHE F CZ  1 
ATOM   6050  N  N   . ASN F  1 66  ? 47.724  -28.305 11.546 1.00 28.13  ? 65  ASN F N   1 
ATOM   6051  C  CA  . ASN F  1 66  ? 47.080  -27.353 10.660 1.00 30.11  ? 65  ASN F CA  1 
ATOM   6052  C  C   . ASN F  1 66  ? 47.839  -27.217 9.339  1.00 32.45  ? 65  ASN F C   1 
ATOM   6053  O  O   . ASN F  1 66  ? 48.199  -26.110 8.941  1.00 31.67  ? 65  ASN F O   1 
ATOM   6054  C  CB  . ASN F  1 66  ? 46.867  -26.010 11.371 1.00 30.86  ? 65  ASN F CB  1 
ATOM   6055  C  CG  . ASN F  1 66  ? 46.078  -25.021 10.541 1.00 31.32  ? 65  ASN F CG  1 
ATOM   6056  O  OD1 . ASN F  1 66  ? 45.369  -25.397 9.609  1.00 32.98  ? 65  ASN F OD1 1 
ATOM   6057  N  ND2 . ASN F  1 66  ? 46.203  -23.750 10.863 1.00 32.04  ? 65  ASN F ND2 1 
ATOM   6058  N  N   . PRO F  1 67  ? 48.056  -28.303 8.560  1.00 33.76  ? 66  PRO F N   1 
ATOM   6059  C  CA  . PRO F  1 67  ? 48.899  -28.208 7.362  1.00 33.06  ? 66  PRO F CA  1 
ATOM   6060  C  C   . PRO F  1 67  ? 48.361  -27.287 6.267  1.00 35.76  ? 66  PRO F C   1 
ATOM   6061  O  O   . PRO F  1 67  ? 49.122  -26.865 5.402  1.00 33.71  ? 66  PRO F O   1 
ATOM   6062  C  CB  . PRO F  1 67  ? 48.944  -29.643 6.823  1.00 32.66  ? 66  PRO F CB  1 
ATOM   6063  C  CG  . PRO F  1 67  ? 47.715  -30.318 7.415  1.00 33.33  ? 66  PRO F CG  1 
ATOM   6064  C  CD  . PRO F  1 67  ? 47.462  -29.639 8.746  1.00 32.13  ? 66  PRO F CD  1 
ATOM   6065  N  N   . LEU F  1 68  ? 47.058  -26.962 6.308  1.00 40.50  ? 67  LEU F N   1 
ATOM   6066  C  CA  . LEU F  1 68  ? 46.459  -26.166 5.247  1.00 38.13  ? 67  LEU F CA  1 
ATOM   6067  C  C   . LEU F  1 68  ? 46.268  -24.708 5.669  1.00 36.68  ? 67  LEU F C   1 
ATOM   6068  O  O   . LEU F  1 68  ? 45.658  -23.941 4.928  1.00 37.35  ? 67  LEU F O   1 
ATOM   6069  C  CB  . LEU F  1 68  ? 45.128  -26.799 4.830  1.00 39.30  ? 67  LEU F CB  1 
ATOM   6070  C  CG  . LEU F  1 68  ? 45.228  -28.123 4.066  1.00 41.89  ? 67  LEU F CG  1 
ATOM   6071  C  CD1 . LEU F  1 68  ? 43.850  -28.555 3.564  1.00 42.30  ? 67  LEU F CD1 1 
ATOM   6072  C  CD2 . LEU F  1 68  ? 46.209  -28.023 2.901  1.00 40.13  ? 67  LEU F CD2 1 
ATOM   6073  N  N   . SER F  1 69  ? 46.765  -24.340 6.857  1.00 34.58  ? 68  SER F N   1 
ATOM   6074  C  CA  . SER F  1 69  ? 46.735  -22.973 7.361  1.00 34.46  ? 68  SER F CA  1 
ATOM   6075  C  C   . SER F  1 69  ? 45.325  -22.390 7.378  1.00 35.51  ? 68  SER F C   1 
ATOM   6076  O  O   . SER F  1 69  ? 45.116  -21.309 6.837  1.00 38.38  ? 68  SER F O   1 
ATOM   6077  C  CB  . SER F  1 69  ? 47.635  -22.078 6.560  1.00 34.61  ? 68  SER F CB  1 
ATOM   6078  O  OG  . SER F  1 69  ? 48.983  -22.441 6.738  1.00 40.71  ? 68  SER F OG  1 
ATOM   6079  N  N   . ARG F  1 70  ? 44.373  -23.092 8.003  1.00 34.95  ? 69  ARG F N   1 
ATOM   6080  C  CA  . ARG F  1 70  ? 43.010  -22.596 8.130  1.00 35.64  ? 69  ARG F CA  1 
ATOM   6081  C  C   . ARG F  1 70  ? 42.746  -22.217 9.584  1.00 34.43  ? 69  ARG F C   1 
ATOM   6082  O  O   . ARG F  1 70  ? 43.587  -22.450 10.454 1.00 33.29  ? 69  ARG F O   1 
ATOM   6083  C  CB  . ARG F  1 70  ? 41.997  -23.646 7.660  1.00 40.38  ? 69  ARG F CB  1 
ATOM   6084  C  CG  . ARG F  1 70  ? 42.272  -24.224 6.281  1.00 47.96  ? 69  ARG F CG  1 
ATOM   6085  C  CD  . ARG F  1 70  ? 41.600  -23.489 5.130  1.00 56.41  ? 69  ARG F CD  1 
ATOM   6086  N  NE  . ARG F  1 70  ? 41.659  -24.331 3.938  1.00 71.34  ? 69  ARG F NE  1 
ATOM   6087  C  CZ  . ARG F  1 70  ? 40.785  -25.298 3.618  1.00 72.46  ? 69  ARG F CZ  1 
ATOM   6088  N  NH1 . ARG F  1 70  ? 39.762  -25.567 4.409  1.00 78.43  ? 69  ARG F NH1 1 
ATOM   6089  N  NH2 . ARG F  1 70  ? 40.929  -26.011 2.513  1.00 65.43  ? 69  ARG F NH2 1 
ATOM   6090  N  N   . LYS F  1 71  ? 41.572  -21.620 9.829  1.00 33.40  ? 70  LYS F N   1 
ATOM   6091  C  CA  . LYS F  1 71  ? 41.147  -21.263 11.177 1.00 31.04  ? 70  LYS F CA  1 
ATOM   6092  C  C   . LYS F  1 71  ? 40.463  -22.476 11.811 1.00 27.41  ? 70  LYS F C   1 
ATOM   6093  O  O   . LYS F  1 71  ? 40.039  -23.389 11.106 1.00 24.76  ? 70  LYS F O   1 
ATOM   6094  C  CB  . LYS F  1 71  ? 40.331  -19.958 11.174 1.00 33.80  ? 70  LYS F CB  1 
ATOM   6095  C  CG  . LYS F  1 71  ? 40.978  -18.781 10.455 1.00 40.91  ? 70  LYS F CG  1 
ATOM   6096  C  CD  . LYS F  1 71  ? 40.927  -17.381 11.030 1.00 48.47  ? 70  LYS F CD  1 
ATOM   6097  C  CE  . LYS F  1 71  ? 42.144  -16.643 10.501 1.00 51.74  ? 70  LYS F CE  1 
ATOM   6098  N  NZ  . LYS F  1 71  ? 42.373  -15.313 11.126 1.00 53.42  ? 70  LYS F NZ  1 
ATOM   6099  N  N   . HIS F  1 72  ? 40.380  -22.486 13.145 1.00 26.59  ? 71  HIS F N   1 
ATOM   6100  C  CA  . HIS F  1 72  ? 39.827  -23.609 13.889 1.00 28.07  ? 71  HIS F CA  1 
ATOM   6101  C  C   . HIS F  1 72  ? 38.325  -23.734 13.632 1.00 31.30  ? 71  HIS F C   1 
ATOM   6102  O  O   . HIS F  1 72  ? 37.618  -22.734 13.566 1.00 32.87  ? 71  HIS F O   1 
ATOM   6103  C  CB  . HIS F  1 72  ? 40.145  -23.449 15.378 1.00 26.94  ? 71  HIS F CB  1 
ATOM   6104  C  CG  . HIS F  1 72  ? 39.515  -24.481 16.243 1.00 26.14  ? 71  HIS F CG  1 
ATOM   6105  N  ND1 . HIS F  1 72  ? 40.088  -25.725 16.473 1.00 26.15  ? 71  HIS F ND1 1 
ATOM   6106  C  CD2 . HIS F  1 72  ? 38.359  -24.462 16.937 1.00 25.85  ? 71  HIS F CD2 1 
ATOM   6107  C  CE1 . HIS F  1 72  ? 39.305  -26.420 17.267 1.00 25.31  ? 71  HIS F CE1 1 
ATOM   6108  N  NE2 . HIS F  1 72  ? 38.239  -25.672 17.562 1.00 26.58  ? 71  HIS F NE2 1 
ATOM   6109  N  N   . GLY F  1 73  ? 37.846  -24.976 13.481 1.00 30.13  ? 72  GLY F N   1 
ATOM   6110  C  CA  . GLY F  1 73  ? 36.425  -25.247 13.323 1.00 29.17  ? 72  GLY F CA  1 
ATOM   6111  C  C   . GLY F  1 73  ? 36.012  -26.514 14.063 1.00 30.95  ? 72  GLY F C   1 
ATOM   6112  O  O   . GLY F  1 73  ? 36.834  -27.118 14.756 1.00 31.71  ? 72  GLY F O   1 
ATOM   6113  N  N   . GLY F  1 74  ? 34.723  -26.873 13.947 1.00 30.18  ? 73  GLY F N   1 
ATOM   6114  C  CA  . GLY F  1 74  ? 34.248  -28.196 14.315 1.00 28.52  ? 73  GLY F CA  1 
ATOM   6115  C  C   . GLY F  1 74  ? 34.542  -29.184 13.185 1.00 28.75  ? 73  GLY F C   1 
ATOM   6116  O  O   . GLY F  1 74  ? 34.790  -28.772 12.053 1.00 28.54  ? 73  GLY F O   1 
ATOM   6117  N  N   . PRO F  1 75  ? 34.543  -30.513 13.447 1.00 28.73  ? 74  PRO F N   1 
ATOM   6118  C  CA  . PRO F  1 75  ? 34.917  -31.491 12.429 1.00 28.38  ? 74  PRO F CA  1 
ATOM   6119  C  C   . PRO F  1 75  ? 34.078  -31.377 11.162 1.00 30.81  ? 74  PRO F C   1 
ATOM   6120  O  O   . PRO F  1 75  ? 34.566  -31.684 10.077 1.00 34.57  ? 74  PRO F O   1 
ATOM   6121  C  CB  . PRO F  1 75  ? 34.716  -32.854 13.100 1.00 27.12  ? 74  PRO F CB  1 
ATOM   6122  C  CG  . PRO F  1 75  ? 33.913  -32.567 14.348 1.00 29.51  ? 74  PRO F CG  1 
ATOM   6123  C  CD  . PRO F  1 75  ? 34.234  -31.141 14.740 1.00 29.68  ? 74  PRO F CD  1 
ATOM   6124  N  N   . LYS F  1 76  ? 32.840  -30.887 11.303 1.00 32.59  ? 75  LYS F N   1 
ATOM   6125  C  CA  . LYS F  1 76  ? 31.911  -30.873 10.182 1.00 34.31  ? 75  LYS F CA  1 
ATOM   6126  C  C   . LYS F  1 76  ? 32.084  -29.634 9.307  1.00 34.77  ? 75  LYS F C   1 
ATOM   6127  O  O   . LYS F  1 76  ? 31.531  -29.598 8.216  1.00 34.63  ? 75  LYS F O   1 
ATOM   6128  C  CB  . LYS F  1 76  ? 30.474  -31.087 10.652 1.00 36.11  ? 75  LYS F CB  1 
ATOM   6129  C  CG  . LYS F  1 76  ? 30.125  -32.542 10.915 1.00 43.01  ? 75  LYS F CG  1 
ATOM   6130  C  CD  . LYS F  1 76  ? 28.598  -32.775 11.004 1.00 51.04  ? 75  LYS F CD  1 
ATOM   6131  C  CE  . LYS F  1 76  ? 27.919  -32.347 12.303 1.00 59.24  ? 75  LYS F CE  1 
ATOM   6132  N  NZ  . LYS F  1 76  ? 27.243  -33.433 13.083 1.00 57.95  ? 75  LYS F NZ  1 
ATOM   6133  N  N   . ASP F  1 77  ? 32.869  -28.649 9.768  1.00 38.33  ? 76  ASP F N   1 
ATOM   6134  C  CA  . ASP F  1 77  ? 33.070  -27.383 9.071  1.00 38.54  ? 76  ASP F CA  1 
ATOM   6135  C  C   . ASP F  1 77  ? 34.029  -27.571 7.900  1.00 39.18  ? 76  ASP F C   1 
ATOM   6136  O  O   . ASP F  1 77  ? 34.909  -28.419 7.946  1.00 37.97  ? 76  ASP F O   1 
ATOM   6137  C  CB  . ASP F  1 77  ? 33.570  -26.300 10.031 1.00 37.26  ? 76  ASP F CB  1 
ATOM   6138  C  CG  . ASP F  1 77  ? 32.512  -25.858 11.019 1.00 39.29  ? 76  ASP F CG  1 
ATOM   6139  O  OD1 . ASP F  1 77  ? 31.337  -25.867 10.614 1.00 42.00  ? 76  ASP F OD1 1 
ATOM   6140  O  OD2 . ASP F  1 77  ? 32.860  -25.519 12.180 1.00 39.47  ? 76  ASP F OD2 1 
ATOM   6141  N  N   . GLU F  1 78  ? 33.862  -26.766 6.852  1.00 43.68  ? 77  GLU F N   1 
ATOM   6142  C  CA  . GLU F  1 78  ? 34.854  -26.780 5.790  1.00 48.95  ? 77  GLU F CA  1 
ATOM   6143  C  C   . GLU F  1 78  ? 36.091  -26.024 6.273  1.00 48.08  ? 77  GLU F C   1 
ATOM   6144  O  O   . GLU F  1 78  ? 37.216  -26.415 5.975  1.00 45.59  ? 77  GLU F O   1 
ATOM   6145  C  CB  . GLU F  1 78  ? 34.293  -26.278 4.458  1.00 57.99  ? 77  GLU F CB  1 
ATOM   6146  C  CG  . GLU F  1 78  ? 35.143  -26.776 3.293  1.00 68.67  ? 77  GLU F CG  1 
ATOM   6147  C  CD  . GLU F  1 78  ? 35.589  -25.739 2.273  1.00 79.91  ? 77  GLU F CD  1 
ATOM   6148  O  OE1 . GLU F  1 78  ? 34.696  -25.035 1.772  1.00 94.96  ? 77  GLU F OE1 1 
ATOM   6149  O  OE2 . GLU F  1 78  ? 36.830  -25.634 1.979  1.00 82.07  ? 77  GLU F OE2 1 
ATOM   6150  N  N   . GLU F  1 79  ? 35.871  -24.949 7.037  1.00 48.01  ? 78  GLU F N   1 
ATOM   6151  C  CA  . GLU F  1 79  ? 36.941  -24.180 7.654  1.00 44.13  ? 78  GLU F CA  1 
ATOM   6152  C  C   . GLU F  1 79  ? 37.308  -24.821 8.997  1.00 42.86  ? 78  GLU F C   1 
ATOM   6153  O  O   . GLU F  1 79  ? 36.691  -24.548 10.028 1.00 39.32  ? 78  GLU F O   1 
ATOM   6154  C  CB  . GLU F  1 79  ? 36.551  -22.695 7.697  1.00 44.30  ? 78  GLU F CB  1 
ATOM   6155  C  CG  . GLU F  1 79  ? 37.645  -21.728 8.143  1.00 44.52  ? 78  GLU F CG  1 
ATOM   6156  C  CD  . GLU F  1 79  ? 38.844  -21.496 7.223  1.00 50.75  ? 78  GLU F CD  1 
ATOM   6157  O  OE1 . GLU F  1 79  ? 38.832  -21.997 6.073  1.00 49.66  ? 78  GLU F OE1 1 
ATOM   6158  O  OE2 . GLU F  1 79  ? 39.800  -20.822 7.668  1.00 53.46  ? 78  GLU F OE2 1 
ATOM   6159  N  N   . ARG F  1 80  ? 38.318  -25.704 8.957  1.00 39.86  ? 79  ARG F N   1 
ATOM   6160  C  CA  . ARG F  1 80  ? 38.835  -26.371 10.137 1.00 35.67  ? 79  ARG F CA  1 
ATOM   6161  C  C   . ARG F  1 80  ? 40.317  -26.697 9.970  1.00 34.07  ? 79  ARG F C   1 
ATOM   6162  O  O   . ARG F  1 80  ? 40.836  -26.767 8.858  1.00 34.80  ? 79  ARG F O   1 
ATOM   6163  C  CB  . ARG F  1 80  ? 38.084  -27.677 10.400 1.00 33.63  ? 79  ARG F CB  1 
ATOM   6164  C  CG  . ARG F  1 80  ? 38.135  -28.671 9.253  1.00 30.87  ? 79  ARG F CG  1 
ATOM   6165  C  CD  . ARG F  1 80  ? 37.520  -29.996 9.664  1.00 30.99  ? 79  ARG F CD  1 
ATOM   6166  N  NE  . ARG F  1 80  ? 38.516  -30.892 10.232 1.00 32.05  ? 79  ARG F NE  1 
ATOM   6167  C  CZ  . ARG F  1 80  ? 38.339  -32.198 10.444 1.00 28.81  ? 79  ARG F CZ  1 
ATOM   6168  N  NH1 . ARG F  1 80  ? 37.190  -32.774 10.149 1.00 26.08  ? 79  ARG F NH1 1 
ATOM   6169  N  NH2 . ARG F  1 80  ? 39.317  -32.929 10.950 1.00 28.68  ? 79  ARG F NH2 1 
ATOM   6170  N  N   . HIS F  1 81  ? 40.980  -26.903 11.114 1.00 31.74  ? 80  HIS F N   1 
ATOM   6171  C  CA  . HIS F  1 81  ? 42.273  -27.557 11.172 1.00 30.53  ? 80  HIS F CA  1 
ATOM   6172  C  C   . HIS F  1 81  ? 42.076  -29.036 10.853 1.00 31.62  ? 80  HIS F C   1 
ATOM   6173  O  O   . HIS F  1 81  ? 41.059  -29.623 11.231 1.00 34.17  ? 80  HIS F O   1 
ATOM   6174  C  CB  . HIS F  1 81  ? 42.850  -27.424 12.585 1.00 28.12  ? 80  HIS F CB  1 
ATOM   6175  C  CG  . HIS F  1 81  ? 43.046  -26.019 13.022 1.00 28.30  ? 80  HIS F CG  1 
ATOM   6176  N  ND1 . HIS F  1 81  ? 42.870  -25.613 14.337 1.00 27.72  ? 80  HIS F ND1 1 
ATOM   6177  C  CD2 . HIS F  1 81  ? 43.413  -24.919 12.328 1.00 28.64  ? 80  HIS F CD2 1 
ATOM   6178  C  CE1 . HIS F  1 81  ? 43.133  -24.325 14.438 1.00 27.64  ? 80  HIS F CE1 1 
ATOM   6179  N  NE2 . HIS F  1 81  ? 43.458  -23.871 13.212 1.00 28.15  ? 80  HIS F NE2 1 
ATOM   6180  N  N   . VAL F  1 82  ? 43.062  -29.641 10.186 1.00 30.75  ? 81  VAL F N   1 
ATOM   6181  C  CA  . VAL F  1 82  ? 43.013  -31.078 9.953  1.00 29.74  ? 81  VAL F CA  1 
ATOM   6182  C  C   . VAL F  1 82  ? 42.817  -31.804 11.284 1.00 28.30  ? 81  VAL F C   1 
ATOM   6183  O  O   . VAL F  1 82  ? 42.064  -32.762 11.356 1.00 29.55  ? 81  VAL F O   1 
ATOM   6184  C  CB  . VAL F  1 82  ? 44.238  -31.595 9.177  1.00 29.90  ? 81  VAL F CB  1 
ATOM   6185  C  CG1 . VAL F  1 82  ? 44.350  -33.110 9.241  1.00 29.52  ? 81  VAL F CG1 1 
ATOM   6186  C  CG2 . VAL F  1 82  ? 44.204  -31.141 7.725  1.00 31.29  ? 81  VAL F CG2 1 
ATOM   6187  N  N   . GLY F  1 83  ? 43.453  -31.316 12.347 1.00 27.35  ? 82  GLY F N   1 
ATOM   6188  C  CA  . GLY F  1 83  ? 43.424  -32.009 13.626 1.00 27.98  ? 82  GLY F CA  1 
ATOM   6189  C  C   . GLY F  1 83  ? 42.146  -31.771 14.432 1.00 28.27  ? 82  GLY F C   1 
ATOM   6190  O  O   . GLY F  1 83  ? 42.054  -32.243 15.571 1.00 29.02  ? 82  GLY F O   1 
ATOM   6191  N  N   . ASP F  1 84  ? 41.182  -31.034 13.849 1.00 25.77  ? 83  ASP F N   1 
ATOM   6192  C  CA  . ASP F  1 84  ? 39.990  -30.595 14.562 1.00 25.05  ? 83  ASP F CA  1 
ATOM   6193  C  C   . ASP F  1 84  ? 38.943  -31.712 14.610 1.00 25.34  ? 83  ASP F C   1 
ATOM   6194  O  O   . ASP F  1 84  ? 38.160  -31.887 13.675 1.00 25.69  ? 83  ASP F O   1 
ATOM   6195  C  CB  . ASP F  1 84  ? 39.435  -29.303 13.966 1.00 24.32  ? 83  ASP F CB  1 
ATOM   6196  C  CG  . ASP F  1 84  ? 40.228  -28.058 14.326 1.00 26.50  ? 83  ASP F CG  1 
ATOM   6197  O  OD1 . ASP F  1 84  ? 41.032  -28.116 15.287 1.00 27.52  ? 83  ASP F OD1 1 
ATOM   6198  O  OD2 . ASP F  1 84  ? 40.030  -27.026 13.653 1.00 25.44  ? 83  ASP F OD2 1 
ATOM   6199  N  N   . LEU F  1 85  ? 38.907  -32.457 15.724 1.00 23.83  ? 84  LEU F N   1 
ATOM   6200  C  CA  . LEU F  1 85  ? 38.026  -33.607 15.823 1.00 22.84  ? 84  LEU F CA  1 
ATOM   6201  C  C   . LEU F  1 85  ? 36.837  -33.315 16.739 1.00 23.41  ? 84  LEU F C   1 
ATOM   6202  O  O   . LEU F  1 85  ? 36.095  -34.236 17.094 1.00 24.59  ? 84  LEU F O   1 
ATOM   6203  C  CB  . LEU F  1 85  ? 38.820  -34.819 16.319 1.00 22.56  ? 84  LEU F CB  1 
ATOM   6204  C  CG  . LEU F  1 85  ? 39.810  -35.439 15.333 1.00 21.83  ? 84  LEU F CG  1 
ATOM   6205  C  CD1 . LEU F  1 85  ? 40.440  -36.682 15.942 1.00 20.45  ? 84  LEU F CD1 1 
ATOM   6206  C  CD2 . LEU F  1 85  ? 39.129  -35.770 14.009 1.00 21.22  ? 84  LEU F CD2 1 
ATOM   6207  N  N   . GLY F  1 86  ? 36.651  -32.045 17.124 1.00 21.42  ? 85  GLY F N   1 
ATOM   6208  C  CA  . GLY F  1 86  ? 35.474  -31.672 17.896 1.00 21.53  ? 85  GLY F CA  1 
ATOM   6209  C  C   . GLY F  1 86  ? 35.570  -32.077 19.369 1.00 21.28  ? 85  GLY F C   1 
ATOM   6210  O  O   . GLY F  1 86  ? 36.625  -31.925 19.989 1.00 21.09  ? 85  GLY F O   1 
ATOM   6211  N  N   . ASN F  1 87  ? 34.458  -32.585 19.917 1.00 21.59  ? 86  ASN F N   1 
ATOM   6212  C  CA  . ASN F  1 87  ? 34.383  -32.917 21.334 1.00 22.75  ? 86  ASN F CA  1 
ATOM   6213  C  C   . ASN F  1 87  ? 34.141  -34.408 21.543 1.00 23.18  ? 86  ASN F C   1 
ATOM   6214  O  O   . ASN F  1 87  ? 33.640  -35.121 20.666 1.00 23.05  ? 86  ASN F O   1 
ATOM   6215  C  CB  . ASN F  1 87  ? 33.269  -32.161 22.056 1.00 23.98  ? 86  ASN F CB  1 
ATOM   6216  C  CG  . ASN F  1 87  ? 33.546  -30.683 22.129 1.00 26.42  ? 86  ASN F CG  1 
ATOM   6217  O  OD1 . ASN F  1 87  ? 34.383  -30.235 22.912 1.00 29.10  ? 86  ASN F OD1 1 
ATOM   6218  N  ND2 . ASN F  1 87  ? 32.866  -29.924 21.289 1.00 26.49  ? 86  ASN F ND2 1 
ATOM   6219  N  N   . VAL F  1 88  ? 34.520  -34.857 22.739 1.00 22.37  ? 87  VAL F N   1 
ATOM   6220  C  CA  . VAL F  1 88  ? 34.101  -36.152 23.243 1.00 22.33  ? 87  VAL F CA  1 
ATOM   6221  C  C   . VAL F  1 88  ? 33.306  -35.878 24.516 1.00 22.53  ? 87  VAL F C   1 
ATOM   6222  O  O   . VAL F  1 88  ? 33.455  -34.816 25.124 1.00 23.14  ? 87  VAL F O   1 
ATOM   6223  C  CB  . VAL F  1 88  ? 35.303  -37.098 23.459 1.00 22.40  ? 87  VAL F CB  1 
ATOM   6224  C  CG1 . VAL F  1 88  ? 36.099  -37.318 22.167 1.00 22.07  ? 87  VAL F CG1 1 
ATOM   6225  C  CG2 . VAL F  1 88  ? 36.230  -36.633 24.576 1.00 21.08  ? 87  VAL F CG2 1 
ATOM   6226  N  N   . THR F  1 89  ? 32.441  -36.817 24.901 1.00 23.02  ? 88  THR F N   1 
ATOM   6227  C  CA  . THR F  1 89  ? 31.555  -36.576 26.028 1.00 23.98  ? 88  THR F CA  1 
ATOM   6228  C  C   . THR F  1 89  ? 31.857  -37.568 27.144 1.00 25.13  ? 88  THR F C   1 
ATOM   6229  O  O   . THR F  1 89  ? 31.807  -38.777 26.933 1.00 26.72  ? 88  THR F O   1 
ATOM   6230  C  CB  . THR F  1 89  ? 30.087  -36.726 25.617 1.00 24.33  ? 88  THR F CB  1 
ATOM   6231  O  OG1 . THR F  1 89  ? 29.818  -35.911 24.468 1.00 24.97  ? 88  THR F OG1 1 
ATOM   6232  C  CG2 . THR F  1 89  ? 29.145  -36.399 26.755 1.00 23.64  ? 88  THR F CG2 1 
ATOM   6233  N  N   . ALA F  1 90  ? 32.127  -37.042 28.340 1.00 25.57  ? 89  ALA F N   1 
ATOM   6234  C  CA  . ALA F  1 90  ? 32.298  -37.883 29.511 1.00 27.83  ? 89  ALA F CA  1 
ATOM   6235  C  C   . ALA F  1 90  ? 30.978  -38.002 30.272 1.00 29.83  ? 89  ALA F C   1 
ATOM   6236  O  O   . ALA F  1 90  ? 30.307  -37.000 30.523 1.00 29.60  ? 89  ALA F O   1 
ATOM   6237  C  CB  . ALA F  1 90  ? 33.388  -37.322 30.388 1.00 29.02  ? 89  ALA F CB  1 
ATOM   6238  N  N   . ASP F  1 91  ? 30.636  -39.246 30.647 1.00 32.19  ? 90  ASP F N   1 
ATOM   6239  C  CA  . ASP F  1 91  ? 29.431  -39.576 31.392 1.00 35.90  ? 90  ASP F CA  1 
ATOM   6240  C  C   . ASP F  1 91  ? 29.630  -39.210 32.864 1.00 37.40  ? 90  ASP F C   1 
ATOM   6241  O  O   . ASP F  1 91  ? 30.685  -38.698 33.240 1.00 36.13  ? 90  ASP F O   1 
ATOM   6242  C  CB  . ASP F  1 91  ? 29.046  -41.046 31.198 1.00 37.64  ? 90  ASP F CB  1 
ATOM   6243  C  CG  . ASP F  1 91  ? 30.042  -42.070 31.741 1.00 39.53  ? 90  ASP F CG  1 
ATOM   6244  O  OD1 . ASP F  1 91  ? 30.859  -41.722 32.634 1.00 38.80  ? 90  ASP F OD1 1 
ATOM   6245  O  OD2 . ASP F  1 91  ? 29.991  -43.222 31.261 1.00 39.31  ? 90  ASP F OD2 1 
ATOM   6246  N  N   . LYS F  1 92  ? 28.614  -39.491 33.690 1.00 39.42  ? 91  LYS F N   1 
ATOM   6247  C  CA  . LYS F  1 92  ? 28.611  -39.091 35.094 1.00 41.56  ? 91  LYS F CA  1 
ATOM   6248  C  C   . LYS F  1 92  ? 29.776  -39.730 35.848 1.00 39.68  ? 91  LYS F C   1 
ATOM   6249  O  O   . LYS F  1 92  ? 30.115  -39.280 36.929 1.00 36.99  ? 91  LYS F O   1 
ATOM   6250  C  CB  . LYS F  1 92  ? 27.268  -39.367 35.785 1.00 44.33  ? 91  LYS F CB  1 
ATOM   6251  C  CG  . LYS F  1 92  ? 26.886  -40.834 35.928 1.00 49.17  ? 91  LYS F CG  1 
ATOM   6252  C  CD  . LYS F  1 92  ? 25.843  -41.189 36.932 1.00 50.20  ? 91  LYS F CD  1 
ATOM   6253  C  CE  . LYS F  1 92  ? 25.248  -42.529 36.546 1.00 52.72  ? 91  LYS F CE  1 
ATOM   6254  N  NZ  . LYS F  1 92  ? 24.895  -43.380 37.713 1.00 57.67  ? 91  LYS F NZ  1 
ATOM   6255  N  N   . ASP F  1 93  ? 30.369  -40.785 35.280 1.00 42.32  ? 92  ASP F N   1 
ATOM   6256  C  CA  . ASP F  1 93  ? 31.443  -41.533 35.924 1.00 42.25  ? 92  ASP F CA  1 
ATOM   6257  C  C   . ASP F  1 93  ? 32.803  -41.028 35.457 1.00 39.38  ? 92  ASP F C   1 
ATOM   6258  O  O   . ASP F  1 93  ? 33.828  -41.525 35.899 1.00 41.44  ? 92  ASP F O   1 
ATOM   6259  C  CB  . ASP F  1 93  ? 31.352  -43.026 35.615 1.00 45.38  ? 92  ASP F CB  1 
ATOM   6260  C  CG  . ASP F  1 93  ? 30.106  -43.676 36.178 1.00 48.93  ? 92  ASP F CG  1 
ATOM   6261  O  OD1 . ASP F  1 93  ? 29.770  -43.371 37.344 1.00 51.16  ? 92  ASP F OD1 1 
ATOM   6262  O  OD2 . ASP F  1 93  ? 29.487  -44.489 35.444 1.00 47.78  ? 92  ASP F OD2 1 
ATOM   6263  N  N   . GLY F  1 94  ? 32.813  -40.052 34.546 1.00 37.31  ? 93  GLY F N   1 
ATOM   6264  C  CA  . GLY F  1 94  ? 34.059  -39.488 34.053 1.00 35.16  ? 93  GLY F CA  1 
ATOM   6265  C  C   . GLY F  1 94  ? 34.678  -40.339 32.946 1.00 32.56  ? 93  GLY F C   1 
ATOM   6266  O  O   . GLY F  1 94  ? 35.881  -40.256 32.695 1.00 36.38  ? 93  GLY F O   1 
ATOM   6267  N  N   . VAL F  1 95  ? 33.838  -41.137 32.278 1.00 27.85  ? 94  VAL F N   1 
ATOM   6268  C  CA  . VAL F  1 95  ? 34.315  -41.965 31.186 1.00 27.15  ? 94  VAL F CA  1 
ATOM   6269  C  C   . VAL F  1 95  ? 33.739  -41.453 29.872 1.00 27.42  ? 94  VAL F C   1 
ATOM   6270  O  O   . VAL F  1 95  ? 32.536  -41.281 29.742 1.00 27.67  ? 94  VAL F O   1 
ATOM   6271  C  CB  . VAL F  1 95  ? 33.975  -43.453 31.412 1.00 25.66  ? 94  VAL F CB  1 
ATOM   6272  C  CG1 . VAL F  1 95  ? 34.367  -44.315 30.219 1.00 24.63  ? 94  VAL F CG1 1 
ATOM   6273  C  CG2 . VAL F  1 95  ? 34.596  -43.973 32.695 1.00 24.64  ? 94  VAL F CG2 1 
ATOM   6274  N  N   . ALA F  1 96  ? 34.608  -41.242 28.886 1.00 28.34  ? 95  ALA F N   1 
ATOM   6275  C  CA  . ALA F  1 96  ? 34.149  -40.913 27.541 1.00 29.41  ? 95  ALA F CA  1 
ATOM   6276  C  C   . ALA F  1 96  ? 34.332  -42.132 26.646 1.00 30.57  ? 95  ALA F C   1 
ATOM   6277  O  O   . ALA F  1 96  ? 35.462  -42.569 26.444 1.00 33.81  ? 95  ALA F O   1 
ATOM   6278  C  CB  . ALA F  1 96  ? 34.926  -39.737 27.013 1.00 29.15  ? 95  ALA F CB  1 
ATOM   6279  N  N   . ASP F  1 97  ? 33.227  -42.674 26.120 1.00 32.62  ? 96  ASP F N   1 
ATOM   6280  C  CA  . ASP F  1 97  ? 33.352  -43.732 25.128 1.00 35.16  ? 96  ASP F CA  1 
ATOM   6281  C  C   . ASP F  1 97  ? 33.446  -43.080 23.760 1.00 31.21  ? 96  ASP F C   1 
ATOM   6282  O  O   . ASP F  1 97  ? 32.433  -42.753 23.157 1.00 35.42  ? 96  ASP F O   1 
ATOM   6283  C  CB  . ASP F  1 97  ? 32.268  -44.811 25.212 1.00 42.18  ? 96  ASP F CB  1 
ATOM   6284  C  CG  . ASP F  1 97  ? 32.344  -45.612 26.496 1.00 51.34  ? 96  ASP F CG  1 
ATOM   6285  O  OD1 . ASP F  1 97  ? 33.455  -46.118 26.835 1.00 53.20  ? 96  ASP F OD1 1 
ATOM   6286  O  OD2 . ASP F  1 97  ? 31.293  -45.710 27.153 1.00 58.42  ? 96  ASP F OD2 1 
ATOM   6287  N  N   . VAL F  1 98  ? 34.679  -42.897 23.294 1.00 25.94  ? 97  VAL F N   1 
ATOM   6288  C  CA  . VAL F  1 98  ? 34.921  -42.166 22.074 1.00 25.29  ? 97  VAL F CA  1 
ATOM   6289  C  C   . VAL F  1 98  ? 34.558  -43.032 20.876 1.00 26.71  ? 97  VAL F C   1 
ATOM   6290  O  O   . VAL F  1 98  ? 34.912  -44.207 20.807 1.00 30.05  ? 97  VAL F O   1 
ATOM   6291  C  CB  . VAL F  1 98  ? 36.384  -41.708 21.998 1.00 23.80  ? 97  VAL F CB  1 
ATOM   6292  C  CG1 . VAL F  1 98  ? 36.650  -40.917 20.725 1.00 23.56  ? 97  VAL F CG1 1 
ATOM   6293  C  CG2 . VAL F  1 98  ? 36.783  -40.922 23.237 1.00 22.26  ? 97  VAL F CG2 1 
ATOM   6294  N  N   . SER F  1 99  ? 33.862  -42.418 19.919 1.00 27.35  ? 98  SER F N   1 
ATOM   6295  C  CA  . SER F  1 99  ? 33.582  -43.060 18.652 1.00 26.64  ? 98  SER F CA  1 
ATOM   6296  C  C   . SER F  1 99  ? 33.285  -41.983 17.617 1.00 26.41  ? 98  SER F C   1 
ATOM   6297  O  O   . SER F  1 99  ? 32.259  -41.310 17.696 1.00 27.04  ? 98  SER F O   1 
ATOM   6298  C  CB  . SER F  1 99  ? 32.449  -44.026 18.785 1.00 27.70  ? 98  SER F CB  1 
ATOM   6299  O  OG  . SER F  1 99  ? 32.170  -44.594 17.519 1.00 31.28  ? 98  SER F OG  1 
ATOM   6300  N  N   . ILE F  1 100 ? 34.212  -41.810 16.673 1.00 26.18  ? 99  ILE F N   1 
ATOM   6301  C  CA  . ILE F  1 100 ? 34.152  -40.717 15.720 1.00 27.43  ? 99  ILE F CA  1 
ATOM   6302  C  C   . ILE F  1 100 ? 34.533  -41.275 14.360 1.00 29.27  ? 99  ILE F C   1 
ATOM   6303  O  O   . ILE F  1 100 ? 35.316  -42.212 14.263 1.00 33.03  ? 99  ILE F O   1 
ATOM   6304  C  CB  . ILE F  1 100 ? 35.109  -39.582 16.133 1.00 26.35  ? 99  ILE F CB  1 
ATOM   6305  C  CG1 . ILE F  1 100 ? 34.533  -38.753 17.284 1.00 24.77  ? 99  ILE F CG1 1 
ATOM   6306  C  CG2 . ILE F  1 100 ? 35.471  -38.687 14.955 1.00 25.09  ? 99  ILE F CG2 1 
ATOM   6307  C  CD1 . ILE F  1 100 ? 35.568  -37.851 17.926 1.00 25.31  ? 99  ILE F CD1 1 
ATOM   6308  N  N   . GLU F  1 101 ? 33.992  -40.669 13.313 1.00 29.31  ? 100 GLU F N   1 
ATOM   6309  C  CA  . GLU F  1 101 ? 34.455  -40.983 11.979 1.00 30.09  ? 100 GLU F CA  1 
ATOM   6310  C  C   . GLU F  1 101 ? 34.817  -39.663 11.311 1.00 29.31  ? 100 GLU F C   1 
ATOM   6311  O  O   . GLU F  1 101 ? 34.064  -38.704 11.389 1.00 30.45  ? 100 GLU F O   1 
ATOM   6312  C  CB  . GLU F  1 101 ? 33.383  -41.795 11.267 1.00 33.97  ? 100 GLU F CB  1 
ATOM   6313  C  CG  . GLU F  1 101 ? 33.634  -41.959 9.792  1.00 41.80  ? 100 GLU F CG  1 
ATOM   6314  C  CD  . GLU F  1 101 ? 32.778  -43.022 9.130  1.00 44.57  ? 100 GLU F CD  1 
ATOM   6315  O  OE1 . GLU F  1 101 ? 32.495  -44.057 9.777  1.00 45.05  ? 100 GLU F OE1 1 
ATOM   6316  O  OE2 . GLU F  1 101 ? 32.491  -42.852 7.920  1.00 44.79  ? 100 GLU F OE2 1 
ATOM   6317  N  N   . ASP F  1 102 ? 36.000  -39.601 10.709 1.00 28.51  ? 101 ASP F N   1 
ATOM   6318  C  CA  . ASP F  1 102 ? 36.450  -38.348 10.141 1.00 28.45  ? 101 ASP F CA  1 
ATOM   6319  C  C   . ASP F  1 102 ? 37.068  -38.625 8.780  1.00 31.54  ? 101 ASP F C   1 
ATOM   6320  O  O   . ASP F  1 102 ? 37.740  -39.642 8.606  1.00 33.20  ? 101 ASP F O   1 
ATOM   6321  C  CB  . ASP F  1 102 ? 37.445  -37.640 11.058 1.00 26.38  ? 101 ASP F CB  1 
ATOM   6322  C  CG  . ASP F  1 102 ? 37.668  -36.203 10.634 1.00 26.71  ? 101 ASP F CG  1 
ATOM   6323  O  OD1 . ASP F  1 102 ? 36.733  -35.411 10.784 1.00 27.53  ? 101 ASP F OD1 1 
ATOM   6324  O  OD2 . ASP F  1 102 ? 38.762  -35.897 10.111 1.00 24.91  ? 101 ASP F OD2 1 
ATOM   6325  N  N   . SER F  1 103 ? 36.852  -37.696 7.835  1.00 32.25  ? 102 SER F N   1 
ATOM   6326  C  CA  . SER F  1 103 ? 37.356  -37.898 6.488  1.00 32.00  ? 102 SER F CA  1 
ATOM   6327  C  C   . SER F  1 103 ? 38.457  -36.907 6.135  1.00 30.09  ? 102 SER F C   1 
ATOM   6328  O  O   . SER F  1 103 ? 38.917  -36.884 4.998  1.00 29.47  ? 102 SER F O   1 
ATOM   6329  C  CB  . SER F  1 103 ? 36.248  -37.873 5.494  1.00 34.39  ? 102 SER F CB  1 
ATOM   6330  O  OG  . SER F  1 103 ? 35.712  -39.185 5.371  1.00 36.87  ? 102 SER F OG  1 
ATOM   6331  N  N   . VAL F  1 104 ? 38.888  -36.113 7.120  1.00 29.30  ? 103 VAL F N   1 
ATOM   6332  C  CA  . VAL F  1 104 ? 39.883  -35.090 6.857  1.00 29.82  ? 103 VAL F CA  1 
ATOM   6333  C  C   . VAL F  1 104 ? 41.239  -35.584 7.347  1.00 32.26  ? 103 VAL F C   1 
ATOM   6334  O  O   . VAL F  1 104 ? 42.229  -35.453 6.633  1.00 34.50  ? 103 VAL F O   1 
ATOM   6335  C  CB  . VAL F  1 104 ? 39.502  -33.727 7.458  1.00 28.53  ? 103 VAL F CB  1 
ATOM   6336  C  CG1 . VAL F  1 104 ? 40.640  -32.704 7.375  1.00 27.71  ? 103 VAL F CG1 1 
ATOM   6337  C  CG2 . VAL F  1 104 ? 38.234  -33.182 6.822  1.00 27.35  ? 103 VAL F CG2 1 
ATOM   6338  N  N   . ILE F  1 105 ? 41.279  -36.146 8.563  1.00 28.96  ? 104 ILE F N   1 
ATOM   6339  C  CA  . ILE F  1 105 ? 42.492  -36.807 9.008  1.00 27.82  ? 104 ILE F CA  1 
ATOM   6340  C  C   . ILE F  1 105 ? 42.703  -38.032 8.119  1.00 31.24  ? 104 ILE F C   1 
ATOM   6341  O  O   . ILE F  1 105 ? 41.767  -38.521 7.487  1.00 33.62  ? 104 ILE F O   1 
ATOM   6342  C  CB  . ILE F  1 105 ? 42.427  -37.190 10.492 1.00 24.74  ? 104 ILE F CB  1 
ATOM   6343  C  CG1 . ILE F  1 105 ? 41.335  -38.228 10.775 1.00 24.83  ? 104 ILE F CG1 1 
ATOM   6344  C  CG2 . ILE F  1 105 ? 42.288  -35.956 11.352 1.00 23.83  ? 104 ILE F CG2 1 
ATOM   6345  C  CD1 . ILE F  1 105 ? 41.444  -38.872 12.133 1.00 24.37  ? 104 ILE F CD1 1 
ATOM   6346  N  N   . SER F  1 106 ? 43.949  -38.507 8.058  1.00 32.79  ? 105 SER F N   1 
ATOM   6347  C  CA  . SER F  1 106 ? 44.272  -39.703 7.305  1.00 33.68  ? 105 SER F CA  1 
ATOM   6348  C  C   . SER F  1 106 ? 45.372  -40.486 8.016  1.00 35.78  ? 105 SER F C   1 
ATOM   6349  O  O   . SER F  1 106 ? 46.114  -39.926 8.829  1.00 36.48  ? 105 SER F O   1 
ATOM   6350  C  CB  . SER F  1 106 ? 44.671  -39.356 5.915  1.00 32.51  ? 105 SER F CB  1 
ATOM   6351  O  OG  . SER F  1 106 ? 44.664  -40.531 5.115  1.00 33.44  ? 105 SER F OG  1 
ATOM   6352  N  N   . LEU F  1 107 ? 45.466  -41.782 7.693  1.00 36.53  ? 106 LEU F N   1 
ATOM   6353  C  CA  . LEU F  1 107 ? 46.589  -42.581 8.155  1.00 38.15  ? 106 LEU F CA  1 
ATOM   6354  C  C   . LEU F  1 107 ? 47.569  -42.856 7.014  1.00 40.76  ? 106 LEU F C   1 
ATOM   6355  O  O   . LEU F  1 107 ? 48.470  -43.680 7.150  1.00 46.66  ? 106 LEU F O   1 
ATOM   6356  C  CB  . LEU F  1 107 ? 46.070  -43.880 8.778  1.00 34.09  ? 106 LEU F CB  1 
ATOM   6357  C  CG  . LEU F  1 107 ? 45.075  -43.711 9.922  1.00 32.21  ? 106 LEU F CG  1 
ATOM   6358  C  CD1 . LEU F  1 107 ? 44.754  -45.040 10.555 1.00 29.32  ? 106 LEU F CD1 1 
ATOM   6359  C  CD2 . LEU F  1 107 ? 45.611  -42.771 10.982 1.00 30.83  ? 106 LEU F CD2 1 
ATOM   6360  N  N   . SER F  1 108 ? 47.403  -42.153 5.888  1.00 41.19  ? 107 SER F N   1 
ATOM   6361  C  CA  . SER F  1 108 ? 48.390  -42.138 4.816  1.00 44.84  ? 107 SER F CA  1 
ATOM   6362  C  C   . SER F  1 108 ? 48.254  -40.850 4.004  1.00 45.24  ? 107 SER F C   1 
ATOM   6363  O  O   . SER F  1 108 ? 47.219  -40.194 4.032  1.00 48.48  ? 107 SER F O   1 
ATOM   6364  C  CB  . SER F  1 108 ? 48.294  -43.374 3.973  1.00 44.60  ? 107 SER F CB  1 
ATOM   6365  O  OG  . SER F  1 108 ? 47.032  -43.435 3.333  1.00 53.65  ? 107 SER F OG  1 
ATOM   6366  N  N   . GLY F  1 109 ? 49.331  -40.476 3.308  1.00 46.07  ? 108 GLY F N   1 
ATOM   6367  C  CA  . GLY F  1 109 ? 49.307  -39.335 2.404  1.00 52.44  ? 108 GLY F CA  1 
ATOM   6368  C  C   . GLY F  1 109 ? 49.541  -38.020 3.133  1.00 54.34  ? 108 GLY F C   1 
ATOM   6369  O  O   . GLY F  1 109 ? 50.120  -38.020 4.200  1.00 54.34  ? 108 GLY F O   1 
ATOM   6370  N  N   . ASP F  1 110 ? 49.006  -36.927 2.588  1.00 65.22  ? 109 ASP F N   1 
ATOM   6371  C  CA  . ASP F  1 110 ? 49.363  -35.585 3.004  1.00 67.03  ? 109 ASP F CA  1 
ATOM   6372  C  C   . ASP F  1 110 ? 48.896  -35.291 4.429  1.00 63.01  ? 109 ASP F C   1 
ATOM   6373  O  O   . ASP F  1 110 ? 49.467  -34.442 5.103  1.00 60.46  ? 109 ASP F O   1 
ATOM   6374  C  CB  . ASP F  1 110 ? 48.792  -34.535 2.041  1.00 82.08  ? 109 ASP F CB  1 
ATOM   6375  C  CG  . ASP F  1 110 ? 49.353  -33.148 2.312  1.00 95.84  ? 109 ASP F CG  1 
ATOM   6376  O  OD1 . ASP F  1 110 ? 50.593  -33.043 2.333  1.00 109.10 ? 109 ASP F OD1 1 
ATOM   6377  O  OD2 . ASP F  1 110 ? 48.554  -32.192 2.541  1.00 102.64 ? 109 ASP F OD2 1 
ATOM   6378  N  N   . HIS F  1 111 ? 47.834  -35.953 4.889  1.00 60.51  ? 110 HIS F N   1 
ATOM   6379  C  CA  . HIS F  1 111 ? 47.289  -35.556 6.171  1.00 56.74  ? 110 HIS F CA  1 
ATOM   6380  C  C   . HIS F  1 111 ? 47.549  -36.635 7.213  1.00 54.48  ? 110 HIS F C   1 
ATOM   6381  O  O   . HIS F  1 111 ? 46.761  -36.795 8.139  1.00 55.01  ? 110 HIS F O   1 
ATOM   6382  C  CB  . HIS F  1 111 ? 45.819  -35.144 6.015  1.00 60.84  ? 110 HIS F CB  1 
ATOM   6383  C  CG  . HIS F  1 111 ? 45.589  -34.024 5.048  1.00 67.54  ? 110 HIS F CG  1 
ATOM   6384  N  ND1 . HIS F  1 111 ? 44.376  -33.871 4.394  1.00 63.52  ? 110 HIS F ND1 1 
ATOM   6385  C  CD2 . HIS F  1 111 ? 46.374  -33.000 4.641  1.00 69.93  ? 110 HIS F CD2 1 
ATOM   6386  C  CE1 . HIS F  1 111 ? 44.411  -32.795 3.633  1.00 64.69  ? 110 HIS F CE1 1 
ATOM   6387  N  NE2 . HIS F  1 111 ? 45.635  -32.244 3.763  1.00 69.69  ? 110 HIS F NE2 1 
ATOM   6388  N  N   . CYS F  1 112 ? 48.670  -37.349 7.063  1.00 49.61  ? 111 CYS F N   1 
ATOM   6389  C  CA  . CYS F  1 112 ? 48.989  -38.437 7.967  1.00 43.75  ? 111 CYS F CA  1 
ATOM   6390  C  C   . CYS F  1 112 ? 49.179  -37.861 9.367  1.00 39.47  ? 111 CYS F C   1 
ATOM   6391  O  O   . CYS F  1 112 ? 49.832  -36.829 9.542  1.00 37.85  ? 111 CYS F O   1 
ATOM   6392  C  CB  . CYS F  1 112 ? 50.236  -39.147 7.474  1.00 49.37  ? 111 CYS F CB  1 
ATOM   6393  S  SG  . CYS F  1 112 ? 50.331  -40.904 7.896  1.00 61.12  ? 111 CYS F SG  1 
ATOM   6394  N  N   . ILE F  1 113 ? 48.515  -38.479 10.351 1.00 34.43  ? 112 ILE F N   1 
ATOM   6395  C  CA  . ILE F  1 113 ? 48.575  -38.021 11.736 1.00 30.97  ? 112 ILE F CA  1 
ATOM   6396  C  C   . ILE F  1 113 ? 49.517  -38.919 12.538 1.00 32.14  ? 112 ILE F C   1 
ATOM   6397  O  O   . ILE F  1 113 ? 49.684  -38.717 13.743 1.00 33.37  ? 112 ILE F O   1 
ATOM   6398  C  CB  . ILE F  1 113 ? 47.167  -37.990 12.379 1.00 27.85  ? 112 ILE F CB  1 
ATOM   6399  C  CG1 . ILE F  1 113 ? 46.433  -39.329 12.250 1.00 24.57  ? 112 ILE F CG1 1 
ATOM   6400  C  CG2 . ILE F  1 113 ? 46.347  -36.827 11.840 1.00 28.16  ? 112 ILE F CG2 1 
ATOM   6401  C  CD1 . ILE F  1 113 ? 45.397  -39.538 13.301 1.00 24.47  ? 112 ILE F CD1 1 
ATOM   6402  N  N   . ILE F  1 114 ? 50.122  -39.914 11.864 1.00 29.90  ? 113 ILE F N   1 
ATOM   6403  C  CA  . ILE F  1 114 ? 51.071  -40.797 12.515 1.00 28.02  ? 113 ILE F CA  1 
ATOM   6404  C  C   . ILE F  1 114 ? 52.258  -39.958 12.974 1.00 28.87  ? 113 ILE F C   1 
ATOM   6405  O  O   . ILE F  1 114 ? 52.764  -39.114 12.225 1.00 28.04  ? 113 ILE F O   1 
ATOM   6406  C  CB  . ILE F  1 114 ? 51.522  -41.924 11.579 1.00 27.74  ? 113 ILE F CB  1 
ATOM   6407  C  CG1 . ILE F  1 114 ? 50.307  -42.676 11.040 1.00 28.11  ? 113 ILE F CG1 1 
ATOM   6408  C  CG2 . ILE F  1 114 ? 52.501  -42.844 12.285 1.00 27.04  ? 113 ILE F CG2 1 
ATOM   6409  C  CD1 . ILE F  1 114 ? 50.585  -44.084 10.581 1.00 28.38  ? 113 ILE F CD1 1 
ATOM   6410  N  N   . GLY F  1 115 ? 52.654  -40.193 14.230 1.00 27.37  ? 114 GLY F N   1 
ATOM   6411  C  CA  . GLY F  1 115 ? 53.811  -39.545 14.811 1.00 27.01  ? 114 GLY F CA  1 
ATOM   6412  C  C   . GLY F  1 115 ? 53.501  -38.132 15.290 1.00 27.39  ? 114 GLY F C   1 
ATOM   6413  O  O   . GLY F  1 115 ? 54.427  -37.366 15.577 1.00 27.51  ? 114 GLY F O   1 
ATOM   6414  N  N   . ARG F  1 116 ? 52.202  -37.799 15.371 1.00 27.09  ? 115 ARG F N   1 
ATOM   6415  C  CA  . ARG F  1 116 ? 51.755  -36.540 15.955 1.00 26.79  ? 115 ARG F CA  1 
ATOM   6416  C  C   . ARG F  1 116 ? 51.099  -36.830 17.305 1.00 26.24  ? 115 ARG F C   1 
ATOM   6417  O  O   . ARG F  1 116 ? 51.184  -37.953 17.797 1.00 26.53  ? 115 ARG F O   1 
ATOM   6418  C  CB  . ARG F  1 116 ? 50.908  -35.784 14.932 1.00 25.63  ? 115 ARG F CB  1 
ATOM   6419  C  CG  . ARG F  1 116 ? 51.613  -35.644 13.597 1.00 27.01  ? 115 ARG F CG  1 
ATOM   6420  C  CD  . ARG F  1 116 ? 50.919  -34.742 12.626 1.00 29.19  ? 115 ARG F CD  1 
ATOM   6421  N  NE  . ARG F  1 116 ? 51.629  -34.599 11.360 1.00 30.76  ? 115 ARG F NE  1 
ATOM   6422  C  CZ  . ARG F  1 116 ? 52.581  -33.688 11.110 1.00 28.20  ? 115 ARG F CZ  1 
ATOM   6423  N  NH1 . ARG F  1 116 ? 52.948  -32.819 12.039 1.00 26.32  ? 115 ARG F NH1 1 
ATOM   6424  N  NH2 . ARG F  1 116 ? 53.145  -33.632 9.918  1.00 26.78  ? 115 ARG F NH2 1 
ATOM   6425  N  N   . THR F  1 117 ? 50.494  -35.812 17.931 1.00 25.27  ? 116 THR F N   1 
ATOM   6426  C  CA  . THR F  1 117 ? 49.938  -36.013 19.264 1.00 24.11  ? 116 THR F CA  1 
ATOM   6427  C  C   . THR F  1 117 ? 48.420  -35.878 19.261 1.00 23.41  ? 116 THR F C   1 
ATOM   6428  O  O   . THR F  1 117 ? 47.856  -34.999 18.612 1.00 24.51  ? 116 THR F O   1 
ATOM   6429  C  CB  . THR F  1 117 ? 50.553  -35.061 20.289 1.00 22.84  ? 116 THR F CB  1 
ATOM   6430  O  OG1 . THR F  1 117 ? 51.943  -35.375 20.346 1.00 22.47  ? 116 THR F OG1 1 
ATOM   6431  C  CG2 . THR F  1 117 ? 49.947  -35.209 21.667 1.00 22.56  ? 116 THR F CG2 1 
ATOM   6432  N  N   . LEU F  1 118 ? 47.767  -36.758 20.018 1.00 21.04  ? 117 LEU F N   1 
ATOM   6433  C  CA  . LEU F  1 118 ? 46.353  -36.598 20.292 1.00 20.74  ? 117 LEU F CA  1 
ATOM   6434  C  C   . LEU F  1 118 ? 46.233  -36.020 21.695 1.00 21.85  ? 117 LEU F C   1 
ATOM   6435  O  O   . LEU F  1 118 ? 46.919  -36.481 22.607 1.00 23.54  ? 117 LEU F O   1 
ATOM   6436  C  CB  . LEU F  1 118 ? 45.693  -37.970 20.189 1.00 19.74  ? 117 LEU F CB  1 
ATOM   6437  C  CG  . LEU F  1 118 ? 44.201  -38.002 20.516 1.00 18.77  ? 117 LEU F CG  1 
ATOM   6438  C  CD1 . LEU F  1 118 ? 43.418  -37.227 19.482 1.00 17.69  ? 117 LEU F CD1 1 
ATOM   6439  C  CD2 . LEU F  1 118 ? 43.709  -39.447 20.560 1.00 20.26  ? 117 LEU F CD2 1 
ATOM   6440  N  N   . VAL F  1 119 ? 45.386  -34.994 21.848 1.00 23.05  ? 118 VAL F N   1 
ATOM   6441  C  CA  . VAL F  1 119 ? 45.216  -34.324 23.128 1.00 22.99  ? 118 VAL F CA  1 
ATOM   6442  C  C   . VAL F  1 119 ? 43.733  -34.268 23.482 1.00 23.71  ? 118 VAL F C   1 
ATOM   6443  O  O   . VAL F  1 119 ? 42.884  -33.916 22.650 1.00 25.22  ? 118 VAL F O   1 
ATOM   6444  C  CB  . VAL F  1 119 ? 45.795  -32.899 23.115 1.00 22.95  ? 118 VAL F CB  1 
ATOM   6445  C  CG1 . VAL F  1 119 ? 45.632  -32.221 24.460 1.00 21.47  ? 118 VAL F CG1 1 
ATOM   6446  C  CG2 . VAL F  1 119 ? 47.255  -32.858 22.669 1.00 23.69  ? 118 VAL F CG2 1 
ATOM   6447  N  N   . VAL F  1 120 ? 43.440  -34.572 24.745 1.00 23.55  ? 119 VAL F N   1 
ATOM   6448  C  CA  . VAL F  1 120 ? 42.107  -34.337 25.266 1.00 23.98  ? 119 VAL F CA  1 
ATOM   6449  C  C   . VAL F  1 120 ? 42.188  -33.159 26.234 1.00 25.22  ? 119 VAL F C   1 
ATOM   6450  O  O   . VAL F  1 120 ? 43.027  -33.158 27.143 1.00 27.84  ? 119 VAL F O   1 
ATOM   6451  C  CB  . VAL F  1 120 ? 41.512  -35.611 25.901 1.00 23.15  ? 119 VAL F CB  1 
ATOM   6452  C  CG1 . VAL F  1 120 ? 42.380  -36.157 27.031 1.00 21.80  ? 119 VAL F CG1 1 
ATOM   6453  C  CG2 . VAL F  1 120 ? 40.077  -35.391 26.360 1.00 24.24  ? 119 VAL F CG2 1 
ATOM   6454  N  N   . HIS F  1 121 ? 41.306  -32.171 26.019 1.00 25.49  ? 120 HIS F N   1 
ATOM   6455  C  CA  . HIS F  1 121 ? 41.394  -30.874 26.674 1.00 27.85  ? 120 HIS F CA  1 
ATOM   6456  C  C   . HIS F  1 121 ? 40.449  -30.756 27.870 1.00 30.53  ? 120 HIS F C   1 
ATOM   6457  O  O   . HIS F  1 121 ? 39.583  -31.606 28.093 1.00 34.38  ? 120 HIS F O   1 
ATOM   6458  C  CB  . HIS F  1 121 ? 41.115  -29.763 25.668 1.00 26.94  ? 120 HIS F CB  1 
ATOM   6459  C  CG  . HIS F  1 121 ? 42.223  -29.542 24.706 1.00 29.13  ? 120 HIS F CG  1 
ATOM   6460  N  ND1 . HIS F  1 121 ? 43.222  -28.617 24.935 1.00 29.10  ? 120 HIS F ND1 1 
ATOM   6461  C  CD2 . HIS F  1 121 ? 42.482  -30.100 23.500 1.00 31.07  ? 120 HIS F CD2 1 
ATOM   6462  C  CE1 . HIS F  1 121 ? 44.055  -28.610 23.905 1.00 29.80  ? 120 HIS F CE1 1 
ATOM   6463  N  NE2 . HIS F  1 121 ? 43.625  -29.505 23.006 1.00 30.46  ? 120 HIS F NE2 1 
ATOM   6464  N  N   . GLU F  1 122 ? 40.603  -29.643 28.597 1.00 29.70  ? 121 GLU F N   1 
ATOM   6465  C  CA  . GLU F  1 122 ? 40.000  -29.424 29.896 1.00 30.15  ? 121 GLU F CA  1 
ATOM   6466  C  C   . GLU F  1 122 ? 38.501  -29.136 29.770 1.00 30.69  ? 121 GLU F C   1 
ATOM   6467  O  O   . GLU F  1 122 ? 37.723  -29.650 30.569 1.00 30.68  ? 121 GLU F O   1 
ATOM   6468  C  CB  . GLU F  1 122 ? 40.760  -28.282 30.556 1.00 32.17  ? 121 GLU F CB  1 
ATOM   6469  C  CG  . GLU F  1 122 ? 40.008  -27.560 31.654 1.00 32.65  ? 121 GLU F CG  1 
ATOM   6470  C  CD  . GLU F  1 122 ? 40.652  -26.217 31.952 1.00 34.09  ? 121 GLU F CD  1 
ATOM   6471  O  OE1 . GLU F  1 122 ? 40.550  -25.795 33.100 1.00 35.59  ? 121 GLU F OE1 1 
ATOM   6472  O  OE2 . GLU F  1 122 ? 41.187  -25.573 31.019 1.00 32.16  ? 121 GLU F OE2 1 
ATOM   6473  N  N   . LYS F  1 123 ? 38.115  -28.340 28.763 1.00 29.35  ? 122 LYS F N   1 
ATOM   6474  C  CA  . LYS F  1 123 ? 36.767  -27.819 28.586 1.00 29.95  ? 122 LYS F CA  1 
ATOM   6475  C  C   . LYS F  1 123 ? 36.239  -28.146 27.190 1.00 30.04  ? 122 LYS F C   1 
ATOM   6476  O  O   . LYS F  1 123 ? 36.937  -28.737 26.374 1.00 32.07  ? 122 LYS F O   1 
ATOM   6477  C  CB  . LYS F  1 123 ? 36.782  -26.285 28.688 1.00 31.21  ? 122 LYS F CB  1 
ATOM   6478  C  CG  . LYS F  1 123 ? 37.163  -25.708 30.038 1.00 32.85  ? 122 LYS F CG  1 
ATOM   6479  C  CD  . LYS F  1 123 ? 37.098  -24.180 30.084 1.00 34.05  ? 122 LYS F CD  1 
ATOM   6480  C  CE  . LYS F  1 123 ? 38.261  -23.498 29.404 1.00 33.49  ? 122 LYS F CE  1 
ATOM   6481  N  NZ  . LYS F  1 123 ? 38.225  -22.033 29.622 1.00 35.41  ? 122 LYS F NZ  1 
ATOM   6482  N  N   . ALA F  1 124 ? 34.999  -27.719 26.917 1.00 28.25  ? 123 ALA F N   1 
ATOM   6483  C  CA  . ALA F  1 124 ? 34.378  -27.904 25.618 1.00 26.16  ? 123 ALA F CA  1 
ATOM   6484  C  C   . ALA F  1 124 ? 35.128  -27.120 24.548 1.00 24.10  ? 123 ALA F C   1 
ATOM   6485  O  O   . ALA F  1 124 ? 35.636  -26.041 24.810 1.00 22.79  ? 123 ALA F O   1 
ATOM   6486  C  CB  . ALA F  1 124 ? 32.939  -27.459 25.683 1.00 26.11  ? 123 ALA F CB  1 
ATOM   6487  N  N   . ASP F  1 125 ? 35.190  -27.689 23.347 1.00 23.71  ? 124 ASP F N   1 
ATOM   6488  C  CA  . ASP F  1 125 ? 35.636  -26.976 22.166 1.00 23.37  ? 124 ASP F CA  1 
ATOM   6489  C  C   . ASP F  1 125 ? 34.429  -26.236 21.593 1.00 23.32  ? 124 ASP F C   1 
ATOM   6490  O  O   . ASP F  1 125 ? 33.421  -26.860 21.277 1.00 23.37  ? 124 ASP F O   1 
ATOM   6491  C  CB  . ASP F  1 125 ? 36.255  -27.975 21.183 1.00 23.60  ? 124 ASP F CB  1 
ATOM   6492  C  CG  . ASP F  1 125 ? 36.632  -27.400 19.828 1.00 25.36  ? 124 ASP F CG  1 
ATOM   6493  O  OD1 . ASP F  1 125 ? 36.349  -26.211 19.578 1.00 26.13  ? 124 ASP F OD1 1 
ATOM   6494  O  OD2 . ASP F  1 125 ? 37.203  -28.153 19.020 1.00 26.93  ? 124 ASP F OD2 1 
ATOM   6495  N  N   . ASP F  1 126 ? 34.531  -24.910 21.447 1.00 23.73  ? 125 ASP F N   1 
ATOM   6496  C  CA  . ASP F  1 126 ? 33.398  -24.110 20.999 1.00 23.88  ? 125 ASP F CA  1 
ATOM   6497  C  C   . ASP F  1 126 ? 33.259  -24.149 19.475 1.00 23.13  ? 125 ASP F C   1 
ATOM   6498  O  O   . ASP F  1 126 ? 32.426  -23.445 18.910 1.00 22.27  ? 125 ASP F O   1 
ATOM   6499  C  CB  . ASP F  1 126 ? 33.403  -22.702 21.607 1.00 26.66  ? 125 ASP F CB  1 
ATOM   6500  C  CG  . ASP F  1 126 ? 34.471  -21.751 21.057 1.00 30.75  ? 125 ASP F CG  1 
ATOM   6501  O  OD1 . ASP F  1 126 ? 34.958  -21.980 19.913 1.00 29.57  ? 125 ASP F OD1 1 
ATOM   6502  O  OD2 . ASP F  1 126 ? 34.799  -20.771 21.772 1.00 32.18  ? 125 ASP F OD2 1 
ATOM   6503  N  N   . LEU F  1 127 ? 34.072  -24.982 18.817 1.00 23.07  ? 126 LEU F N   1 
ATOM   6504  C  CA  . LEU F  1 127 ? 33.983  -25.235 17.383 1.00 24.35  ? 126 LEU F CA  1 
ATOM   6505  C  C   . LEU F  1 127 ? 34.142  -23.942 16.586 1.00 25.43  ? 126 LEU F C   1 
ATOM   6506  O  O   . LEU F  1 127 ? 33.697  -23.868 15.439 1.00 25.90  ? 126 LEU F O   1 
ATOM   6507  C  CB  . LEU F  1 127 ? 32.657  -25.934 17.043 1.00 23.82  ? 126 LEU F CB  1 
ATOM   6508  C  CG  . LEU F  1 127 ? 32.278  -27.141 17.909 1.00 23.49  ? 126 LEU F CG  1 
ATOM   6509  C  CD1 . LEU F  1 127 ? 31.040  -27.834 17.353 1.00 21.76  ? 126 LEU F CD1 1 
ATOM   6510  C  CD2 . LEU F  1 127 ? 33.415  -28.155 17.974 1.00 24.58  ? 126 LEU F CD2 1 
ATOM   6511  N  N   . GLY F  1 128 ? 34.786  -22.938 17.204 1.00 26.02  ? 127 GLY F N   1 
ATOM   6512  C  CA  . GLY F  1 128 ? 35.206  -21.725 16.521 1.00 26.70  ? 127 GLY F CA  1 
ATOM   6513  C  C   . GLY F  1 128 ? 34.108  -20.665 16.460 1.00 26.95  ? 127 GLY F C   1 
ATOM   6514  O  O   . GLY F  1 128 ? 34.195  -19.729 15.675 1.00 24.42  ? 127 GLY F O   1 
ATOM   6515  N  N   . LYS F  1 129 ? 33.093  -20.812 17.317 1.00 29.02  ? 128 LYS F N   1 
ATOM   6516  C  CA  . LYS F  1 129 ? 31.917  -19.959 17.282 1.00 29.07  ? 128 LYS F CA  1 
ATOM   6517  C  C   . LYS F  1 129 ? 31.818  -19.157 18.573 1.00 29.04  ? 128 LYS F C   1 
ATOM   6518  O  O   . LYS F  1 129 ? 30.719  -18.839 19.016 1.00 30.94  ? 128 LYS F O   1 
ATOM   6519  C  CB  . LYS F  1 129 ? 30.653  -20.809 17.111 1.00 28.54  ? 128 LYS F CB  1 
ATOM   6520  C  CG  . LYS F  1 129 ? 30.677  -21.766 15.929 1.00 29.35  ? 128 LYS F CG  1 
ATOM   6521  C  CD  . LYS F  1 129 ? 29.572  -22.769 15.982 1.00 27.70  ? 128 LYS F CD  1 
ATOM   6522  C  CE  . LYS F  1 129 ? 28.253  -22.186 15.541 1.00 27.32  ? 128 LYS F CE  1 
ATOM   6523  N  NZ  . LYS F  1 129 ? 27.144  -22.794 16.307 1.00 27.90  ? 128 LYS F NZ  1 
ATOM   6524  N  N   . GLY F  1 130 ? 32.969  -18.826 19.162 1.00 29.11  ? 129 GLY F N   1 
ATOM   6525  C  CA  . GLY F  1 130 ? 33.010  -18.155 20.455 1.00 29.33  ? 129 GLY F CA  1 
ATOM   6526  C  C   . GLY F  1 130 ? 33.207  -16.645 20.319 1.00 29.65  ? 129 GLY F C   1 
ATOM   6527  O  O   . GLY F  1 130 ? 33.133  -15.931 21.318 1.00 30.30  ? 129 GLY F O   1 
ATOM   6528  N  N   . GLY F  1 131 ? 33.505  -16.194 19.089 1.00 28.57  ? 130 GLY F N   1 
ATOM   6529  C  CA  . GLY F  1 131 ? 33.576  -14.784 18.755 1.00 30.51  ? 130 GLY F CA  1 
ATOM   6530  C  C   . GLY F  1 131 ? 34.761  -14.055 19.384 1.00 33.44  ? 130 GLY F C   1 
ATOM   6531  O  O   . GLY F  1 131 ? 34.718  -12.839 19.550 1.00 36.72  ? 130 GLY F O   1 
ATOM   6532  N  N   . ASN F  1 132 ? 35.814  -14.793 19.746 1.00 33.61  ? 131 ASN F N   1 
ATOM   6533  C  CA  . ASN F  1 132 ? 37.060  -14.179 20.169 1.00 34.33  ? 131 ASN F CA  1 
ATOM   6534  C  C   . ASN F  1 132 ? 38.211  -14.798 19.393 1.00 36.18  ? 131 ASN F C   1 
ATOM   6535  O  O   . ASN F  1 132 ? 38.002  -15.735 18.616 1.00 36.44  ? 131 ASN F O   1 
ATOM   6536  C  CB  . ASN F  1 132 ? 37.254  -14.187 21.690 1.00 32.16  ? 131 ASN F CB  1 
ATOM   6537  C  CG  . ASN F  1 132 ? 37.253  -15.562 22.316 1.00 31.48  ? 131 ASN F CG  1 
ATOM   6538  O  OD1 . ASN F  1 132 ? 37.455  -16.568 21.645 1.00 31.17  ? 131 ASN F OD1 1 
ATOM   6539  N  ND2 . ASN F  1 132 ? 37.042  -15.614 23.614 1.00 31.98  ? 131 ASN F ND2 1 
ATOM   6540  N  N   . GLU F  1 133 ? 39.423  -14.268 19.604 1.00 40.96  ? 132 GLU F N   1 
ATOM   6541  C  CA  . GLU F  1 133 ? 40.538  -14.690 18.781 1.00 48.11  ? 132 GLU F CA  1 
ATOM   6542  C  C   . GLU F  1 133 ? 40.904  -16.120 19.150 1.00 47.26  ? 132 GLU F C   1 
ATOM   6543  O  O   . GLU F  1 133 ? 41.210  -16.924 18.274 1.00 41.79  ? 132 GLU F O   1 
ATOM   6544  C  CB  . GLU F  1 133 ? 41.702  -13.694 18.861 1.00 59.85  ? 132 GLU F CB  1 
ATOM   6545  C  CG  . GLU F  1 133 ? 42.859  -14.033 17.941 1.00 68.64  ? 132 GLU F CG  1 
ATOM   6546  C  CD  . GLU F  1 133 ? 43.600  -12.934 17.230 1.00 74.35  ? 132 GLU F CD  1 
ATOM   6547  O  OE1 . GLU F  1 133 ? 42.923  -11.973 16.874 1.00 81.92  ? 132 GLU F OE1 1 
ATOM   6548  O  OE2 . GLU F  1 133 ? 44.813  -13.081 17.053 1.00 73.76  ? 132 GLU F OE2 1 
ATOM   6549  N  N   . GLU F  1 134 ? 40.807  -16.406 20.452 1.00 49.15  ? 133 GLU F N   1 
ATOM   6550  C  CA  . GLU F  1 134 ? 41.072  -17.720 21.015 1.00 45.64  ? 133 GLU F CA  1 
ATOM   6551  C  C   . GLU F  1 134 ? 40.217  -18.783 20.318 1.00 41.34  ? 133 GLU F C   1 
ATOM   6552  O  O   . GLU F  1 134 ? 40.707  -19.857 19.987 1.00 39.97  ? 133 GLU F O   1 
ATOM   6553  C  CB  . GLU F  1 134 ? 40.819  -17.658 22.526 1.00 46.75  ? 133 GLU F CB  1 
ATOM   6554  C  CG  . GLU F  1 134 ? 41.514  -18.746 23.326 1.00 47.15  ? 133 GLU F CG  1 
ATOM   6555  C  CD  . GLU F  1 134 ? 42.959  -19.075 22.999 1.00 49.50  ? 133 GLU F CD  1 
ATOM   6556  O  OE1 . GLU F  1 134 ? 43.729  -18.144 22.654 1.00 51.09  ? 133 GLU F OE1 1 
ATOM   6557  O  OE2 . GLU F  1 134 ? 43.319  -20.268 23.104 1.00 50.09  ? 133 GLU F OE2 1 
ATOM   6558  N  N   . SER F  1 135 ? 38.938  -18.464 20.087 1.00 39.62  ? 134 SER F N   1 
ATOM   6559  C  CA  . SER F  1 135 ? 37.998  -19.404 19.502 1.00 38.56  ? 134 SER F CA  1 
ATOM   6560  C  C   . SER F  1 135 ? 38.515  -19.912 18.162 1.00 37.21  ? 134 SER F C   1 
ATOM   6561  O  O   . SER F  1 135 ? 38.384  -21.091 17.865 1.00 38.86  ? 134 SER F O   1 
ATOM   6562  C  CB  . SER F  1 135 ? 36.623  -18.815 19.365 1.00 38.86  ? 134 SER F CB  1 
ATOM   6563  O  OG  . SER F  1 135 ? 35.686  -19.769 18.873 1.00 36.90  ? 134 SER F OG  1 
ATOM   6564  N  N   . THR F  1 136 ? 39.108  -19.030 17.357 1.00 36.36  ? 135 THR F N   1 
ATOM   6565  C  CA  . THR F  1 136 ? 39.476  -19.422 16.008 1.00 36.58  ? 135 THR F CA  1 
ATOM   6566  C  C   . THR F  1 136 ? 40.857  -20.078 15.985 1.00 36.47  ? 135 THR F C   1 
ATOM   6567  O  O   . THR F  1 136 ? 41.340  -20.434 14.910 1.00 39.36  ? 135 THR F O   1 
ATOM   6568  C  CB  . THR F  1 136 ? 39.425  -18.247 15.028 1.00 37.93  ? 135 THR F CB  1 
ATOM   6569  O  OG1 . THR F  1 136 ? 40.437  -17.335 15.463 1.00 41.19  ? 135 THR F OG1 1 
ATOM   6570  C  CG2 . THR F  1 136 ? 38.055  -17.612 14.950 1.00 36.23  ? 135 THR F CG2 1 
ATOM   6571  N  N   . LYS F  1 137 ? 41.476  -20.236 17.163 1.00 34.38  ? 136 LYS F N   1 
ATOM   6572  C  CA  . LYS F  1 137 ? 42.754  -20.920 17.279 1.00 35.90  ? 136 LYS F CA  1 
ATOM   6573  C  C   . LYS F  1 137 ? 42.569  -22.276 17.964 1.00 35.03  ? 136 LYS F C   1 
ATOM   6574  O  O   . LYS F  1 137 ? 42.976  -23.300 17.421 1.00 38.48  ? 136 LYS F O   1 
ATOM   6575  C  CB  . LYS F  1 137 ? 43.773  -20.075 18.042 1.00 41.07  ? 136 LYS F CB  1 
ATOM   6576  C  CG  . LYS F  1 137 ? 44.454  -18.984 17.223 1.00 46.92  ? 136 LYS F CG  1 
ATOM   6577  C  CD  . LYS F  1 137 ? 45.473  -18.167 17.999 1.00 54.83  ? 136 LYS F CD  1 
ATOM   6578  C  CE  . LYS F  1 137 ? 46.747  -17.787 17.236 1.00 63.60  ? 136 LYS F CE  1 
ATOM   6579  N  NZ  . LYS F  1 137 ? 47.204  -16.400 17.506 1.00 68.31  ? 136 LYS F NZ  1 
ATOM   6580  N  N   . THR F  1 138 ? 41.952  -22.272 19.151 1.00 30.89  ? 137 THR F N   1 
ATOM   6581  C  CA  . THR F  1 138 ? 41.945  -23.444 20.010 1.00 28.62  ? 137 THR F CA  1 
ATOM   6582  C  C   . THR F  1 138 ? 40.532  -23.883 20.380 1.00 28.18  ? 137 THR F C   1 
ATOM   6583  O  O   . THR F  1 138 ? 40.367  -24.859 21.099 1.00 27.25  ? 137 THR F O   1 
ATOM   6584  C  CB  . THR F  1 138 ? 42.704  -23.169 21.311 1.00 28.08  ? 137 THR F CB  1 
ATOM   6585  O  OG1 . THR F  1 138 ? 41.931  -22.293 22.133 1.00 27.64  ? 137 THR F OG1 1 
ATOM   6586  C  CG2 . THR F  1 138 ? 44.069  -22.575 21.059 1.00 27.86  ? 137 THR F CG2 1 
ATOM   6587  N  N   . GLY F  1 139 ? 39.528  -23.132 19.918 1.00 28.60  ? 138 GLY F N   1 
ATOM   6588  C  CA  . GLY F  1 139 ? 38.145  -23.367 20.296 1.00 27.87  ? 138 GLY F CA  1 
ATOM   6589  C  C   . GLY F  1 139 ? 37.897  -23.196 21.795 1.00 29.28  ? 138 GLY F C   1 
ATOM   6590  O  O   . GLY F  1 139 ? 36.848  -23.599 22.291 1.00 26.85  ? 138 GLY F O   1 
ATOM   6591  N  N   . ASN F  1 140 ? 38.858  -22.607 22.520 1.00 30.63  ? 139 ASN F N   1 
ATOM   6592  C  CA  . ASN F  1 140 ? 38.660  -22.252 23.922 1.00 30.68  ? 139 ASN F CA  1 
ATOM   6593  C  C   . ASN F  1 140 ? 38.581  -23.516 24.772 1.00 31.03  ? 139 ASN F C   1 
ATOM   6594  O  O   . ASN F  1 140 ? 37.973  -23.504 25.839 1.00 32.72  ? 139 ASN F O   1 
ATOM   6595  C  CB  . ASN F  1 140 ? 37.426  -21.365 24.157 1.00 29.71  ? 139 ASN F CB  1 
ATOM   6596  C  CG  . ASN F  1 140 ? 37.636  -19.917 23.748 1.00 32.31  ? 139 ASN F CG  1 
ATOM   6597  O  OD1 . ASN F  1 140 ? 38.400  -19.196 24.372 1.00 34.06  ? 139 ASN F OD1 1 
ATOM   6598  N  ND2 . ASN F  1 140 ? 36.982  -19.469 22.691 1.00 33.81  ? 139 ASN F ND2 1 
ATOM   6599  N  N   . ALA F  1 141 ? 39.226  -24.593 24.308 1.00 31.07  ? 140 ALA F N   1 
ATOM   6600  C  CA  . ALA F  1 141 ? 39.100  -25.905 24.928 1.00 28.83  ? 140 ALA F CA  1 
ATOM   6601  C  C   . ALA F  1 141 ? 39.903  -25.988 26.226 1.00 28.80  ? 140 ALA F C   1 
ATOM   6602  O  O   . ALA F  1 141 ? 39.807  -26.970 26.966 1.00 28.07  ? 140 ALA F O   1 
ATOM   6603  C  CB  . ALA F  1 141 ? 39.515  -26.977 23.952 1.00 27.20  ? 140 ALA F CB  1 
ATOM   6604  N  N   . GLY F  1 142 ? 40.690  -24.950 26.514 1.00 28.62  ? 141 GLY F N   1 
ATOM   6605  C  CA  . GLY F  1 142 ? 41.431  -24.905 27.762 1.00 26.63  ? 141 GLY F CA  1 
ATOM   6606  C  C   . GLY F  1 142 ? 42.652  -25.817 27.715 1.00 25.67  ? 141 GLY F C   1 
ATOM   6607  O  O   . GLY F  1 142 ? 43.148  -26.134 26.631 1.00 25.88  ? 141 GLY F O   1 
ATOM   6608  N  N   . SER F  1 143 ? 43.097  -26.249 28.901 1.00 24.24  ? 142 SER F N   1 
ATOM   6609  C  CA  . SER F  1 143 ? 44.382  -26.909 29.060 1.00 23.70  ? 142 SER F CA  1 
ATOM   6610  C  C   . SER F  1 143 ? 44.351  -28.329 28.497 1.00 23.65  ? 142 SER F C   1 
ATOM   6611  O  O   . SER F  1 143 ? 43.290  -28.840 28.137 1.00 25.16  ? 142 SER F O   1 
ATOM   6612  C  CB  . SER F  1 143 ? 44.835  -26.889 30.494 1.00 23.16  ? 142 SER F CB  1 
ATOM   6613  O  OG  . SER F  1 143 ? 43.952  -27.643 31.299 1.00 22.64  ? 142 SER F OG  1 
ATOM   6614  N  N   . ARG F  1 144 ? 45.535  -28.945 28.445 1.00 23.11  ? 143 ARG F N   1 
ATOM   6615  C  CA  . ARG F  1 144 ? 45.761  -30.264 27.882 1.00 22.07  ? 143 ARG F CA  1 
ATOM   6616  C  C   . ARG F  1 144 ? 45.797  -31.273 29.028 1.00 23.70  ? 143 ARG F C   1 
ATOM   6617  O  O   . ARG F  1 144 ? 46.747  -31.290 29.803 1.00 24.64  ? 143 ARG F O   1 
ATOM   6618  C  CB  . ARG F  1 144 ? 47.074  -30.259 27.090 1.00 21.40  ? 143 ARG F CB  1 
ATOM   6619  C  CG  . ARG F  1 144 ? 47.107  -29.199 25.994 1.00 20.72  ? 143 ARG F CG  1 
ATOM   6620  C  CD  . ARG F  1 144 ? 48.482  -29.020 25.348 1.00 21.83  ? 143 ARG F CD  1 
ATOM   6621  N  NE  . ARG F  1 144 ? 48.434  -27.930 24.371 1.00 22.97  ? 143 ARG F NE  1 
ATOM   6622  C  CZ  . ARG F  1 144 ? 49.235  -27.802 23.312 1.00 24.15  ? 143 ARG F CZ  1 
ATOM   6623  N  NH1 . ARG F  1 144 ? 50.173  -28.697 23.058 1.00 28.81  ? 143 ARG F NH1 1 
ATOM   6624  N  NH2 . ARG F  1 144 ? 49.098  -26.788 22.490 1.00 22.14  ? 143 ARG F NH2 1 
ATOM   6625  N  N   . LEU F  1 145 ? 44.743  -32.089 29.165 1.00 23.67  ? 144 LEU F N   1 
ATOM   6626  C  CA  . LEU F  1 145 ? 44.625  -32.933 30.338 1.00 23.81  ? 144 LEU F CA  1 
ATOM   6627  C  C   . LEU F  1 145 ? 45.504  -34.169 30.170 1.00 26.44  ? 144 LEU F C   1 
ATOM   6628  O  O   . LEU F  1 145 ? 46.125  -34.649 31.122 1.00 27.77  ? 144 LEU F O   1 
ATOM   6629  C  CB  . LEU F  1 145 ? 43.160  -33.314 30.534 1.00 23.89  ? 144 LEU F CB  1 
ATOM   6630  C  CG  . LEU F  1 145 ? 42.245  -32.177 31.004 1.00 25.09  ? 144 LEU F CG  1 
ATOM   6631  C  CD1 . LEU F  1 145 ? 40.824  -32.694 31.244 1.00 25.32  ? 144 LEU F CD1 1 
ATOM   6632  C  CD2 . LEU F  1 145 ? 42.809  -31.520 32.258 1.00 23.54  ? 144 LEU F CD2 1 
ATOM   6633  N  N   . ALA F  1 146 ? 45.554  -34.684 28.936 1.00 27.80  ? 145 ALA F N   1 
ATOM   6634  C  CA  . ALA F  1 146 ? 46.320  -35.879 28.622 1.00 27.96  ? 145 ALA F CA  1 
ATOM   6635  C  C   . ALA F  1 146 ? 46.600  -35.913 27.123 1.00 28.72  ? 145 ALA F C   1 
ATOM   6636  O  O   . ALA F  1 146 ? 45.813  -35.397 26.320 1.00 29.28  ? 145 ALA F O   1 
ATOM   6637  C  CB  . ALA F  1 146 ? 45.574  -37.114 29.095 1.00 27.12  ? 145 ALA F CB  1 
ATOM   6638  N  N   . CYS F  1 147 ? 47.714  -36.559 26.770 1.00 27.86  ? 146 CYS F N   1 
ATOM   6639  C  CA  . CYS F  1 147 ? 48.096  -36.669 25.377 1.00 27.83  ? 146 CYS F CA  1 
ATOM   6640  C  C   . CYS F  1 147 ? 48.934  -37.927 25.197 1.00 27.89  ? 146 CYS F C   1 
ATOM   6641  O  O   . CYS F  1 147 ? 49.287  -38.579 26.173 1.00 30.01  ? 146 CYS F O   1 
ATOM   6642  C  CB  . CYS F  1 147 ? 48.884  -35.443 24.943 1.00 29.19  ? 146 CYS F CB  1 
ATOM   6643  S  SG  . CYS F  1 147 ? 50.393  -35.162 25.924 1.00 32.00  ? 146 CYS F SG  1 
ATOM   6644  N  N   . GLY F  1 148 ? 49.206  -38.255 23.932 1.00 25.85  ? 147 GLY F N   1 
ATOM   6645  C  CA  . GLY F  1 148 ? 50.102  -39.333 23.563 1.00 24.85  ? 147 GLY F CA  1 
ATOM   6646  C  C   . GLY F  1 148 ? 50.547  -39.188 22.110 1.00 25.13  ? 147 GLY F C   1 
ATOM   6647  O  O   . GLY F  1 148 ? 49.883  -38.523 21.308 1.00 26.28  ? 147 GLY F O   1 
ATOM   6648  N  N   . VAL F  1 149 ? 51.677  -39.815 21.777 1.00 23.56  ? 148 VAL F N   1 
ATOM   6649  C  CA  . VAL F  1 149 ? 52.081  -39.848 20.386 1.00 22.25  ? 148 VAL F CA  1 
ATOM   6650  C  C   . VAL F  1 149 ? 51.291  -40.940 19.667 1.00 20.31  ? 148 VAL F C   1 
ATOM   6651  O  O   . VAL F  1 149 ? 51.021  -42.002 20.225 1.00 17.98  ? 148 VAL F O   1 
ATOM   6652  C  CB  . VAL F  1 149 ? 53.608  -40.001 20.243 1.00 22.55  ? 148 VAL F CB  1 
ATOM   6653  C  CG1 . VAL F  1 149 ? 54.043  -39.904 18.783 1.00 21.35  ? 148 VAL F CG1 1 
ATOM   6654  C  CG2 . VAL F  1 149 ? 54.327  -38.958 21.087 1.00 21.09  ? 148 VAL F CG2 1 
ATOM   6655  N  N   . ILE F  1 150 ? 50.889  -40.632 18.435 1.00 20.71  ? 149 ILE F N   1 
ATOM   6656  C  CA  . ILE F  1 150 ? 50.060  -41.512 17.637 1.00 22.83  ? 149 ILE F CA  1 
ATOM   6657  C  C   . ILE F  1 150 ? 50.990  -42.449 16.882 1.00 22.42  ? 149 ILE F C   1 
ATOM   6658  O  O   . ILE F  1 150 ? 51.738  -42.005 16.016 1.00 22.22  ? 149 ILE F O   1 
ATOM   6659  C  CB  . ILE F  1 150 ? 49.199  -40.675 16.670 1.00 24.67  ? 149 ILE F CB  1 
ATOM   6660  C  CG1 . ILE F  1 150 ? 48.213  -39.771 17.414 1.00 23.72  ? 149 ILE F CG1 1 
ATOM   6661  C  CG2 . ILE F  1 150 ? 48.506  -41.557 15.636 1.00 25.19  ? 149 ILE F CG2 1 
ATOM   6662  C  CD1 . ILE F  1 150 ? 47.637  -38.679 16.541 1.00 24.07  ? 149 ILE F CD1 1 
ATOM   6663  N  N   . GLY F  1 151 ? 50.911  -43.744 17.208 1.00 22.31  ? 150 GLY F N   1 
ATOM   6664  C  CA  . GLY F  1 151 ? 51.878  -44.720 16.730 1.00 23.60  ? 150 GLY F CA  1 
ATOM   6665  C  C   . GLY F  1 151 ? 51.251  -45.877 15.962 1.00 24.30  ? 150 GLY F C   1 
ATOM   6666  O  O   . GLY F  1 151 ? 50.055  -46.117 16.065 1.00 24.23  ? 150 GLY F O   1 
ATOM   6667  N  N   . ILE F  1 152 ? 52.092  -46.600 15.219 1.00 26.30  ? 151 ILE F N   1 
ATOM   6668  C  CA  . ILE F  1 152 ? 51.675  -47.714 14.380 1.00 24.84  ? 151 ILE F CA  1 
ATOM   6669  C  C   . ILE F  1 152 ? 51.377  -48.902 15.286 1.00 25.07  ? 151 ILE F C   1 
ATOM   6670  O  O   . ILE F  1 152 ? 52.164  -49.194 16.186 1.00 25.47  ? 151 ILE F O   1 
ATOM   6671  C  CB  . ILE F  1 152 ? 52.786  -48.046 13.370 1.00 22.75  ? 151 ILE F CB  1 
ATOM   6672  C  CG1 . ILE F  1 152 ? 53.027  -46.888 12.403 1.00 23.00  ? 151 ILE F CG1 1 
ATOM   6673  C  CG2 . ILE F  1 152 ? 52.472  -49.337 12.642 1.00 21.70  ? 151 ILE F CG2 1 
ATOM   6674  C  CD1 . ILE F  1 152 ? 54.412  -46.935 11.771 1.00 24.20  ? 151 ILE F CD1 1 
ATOM   6675  N  N   . ALA F  1 153 ? 50.237  -49.563 15.035 1.00 27.01  ? 152 ALA F N   1 
ATOM   6676  C  CA  . ALA F  1 153 ? 49.797  -50.718 15.808 1.00 33.12  ? 152 ALA F CA  1 
ATOM   6677  C  C   . ALA F  1 153 ? 49.753  -51.950 14.911 1.00 38.16  ? 152 ALA F C   1 
ATOM   6678  O  O   . ALA F  1 153 ? 49.848  -51.824 13.691 1.00 43.35  ? 152 ALA F O   1 
ATOM   6679  C  CB  . ALA F  1 153 ? 48.454  -50.447 16.434 1.00 30.31  ? 152 ALA F CB  1 
ATOM   6680  N  N   . GLN F  1 154 ? 49.603  -53.133 15.526 1.00 46.08  ? 153 GLN F N   1 
ATOM   6681  C  CA  . GLN F  1 154 ? 49.638  -54.388 14.786 1.00 54.89  ? 153 GLN F CA  1 
ATOM   6682  C  C   . GLN F  1 154 ? 48.380  -54.567 13.915 1.00 58.91  ? 153 GLN F C   1 
ATOM   6683  O  O   . GLN F  1 154 ? 47.219  -54.435 14.361 1.00 63.76  ? 153 GLN F O   1 
ATOM   6684  C  CB  . GLN F  1 154 ? 49.784  -55.595 15.715 1.00 58.84  ? 153 GLN F CB  1 
ATOM   6685  C  CG  . GLN F  1 154 ? 49.817  -56.907 14.942 1.00 63.65  ? 153 GLN F CG  1 
ATOM   6686  C  CD  . GLN F  1 154 ? 50.526  -58.011 15.672 1.00 66.65  ? 153 GLN F CD  1 
ATOM   6687  O  OE1 . GLN F  1 154 ? 50.198  -58.340 16.807 1.00 71.26  ? 153 GLN F OE1 1 
ATOM   6688  N  NE2 . GLN F  1 154 ? 51.511  -58.592 15.010 1.00 64.07  ? 153 GLN F NE2 1 
ATOM   6689  O  OXT . GLN F  1 154 ? 48.523  -54.878 12.726 1.00 52.73  ? 153 GLN F OXT 1 
ATOM   6690  N  N   . ALA G  1 2   ? -15.767 -22.810 65.764 1.00 68.50  ? 1   ALA G N   1 
ATOM   6691  C  CA  . ALA G  1 2   ? -16.071 -23.946 64.844 1.00 67.38  ? 1   ALA G CA  1 
ATOM   6692  C  C   . ALA G  1 2   ? -14.805 -24.534 64.216 1.00 64.64  ? 1   ALA G C   1 
ATOM   6693  O  O   . ALA G  1 2   ? -13.856 -23.788 63.929 1.00 78.38  ? 1   ALA G O   1 
ATOM   6694  C  CB  . ALA G  1 2   ? -17.094 -23.551 63.798 1.00 65.05  ? 1   ALA G CB  1 
ATOM   6695  N  N   . THR G  1 3   ? -14.826 -25.852 63.938 1.00 53.07  ? 2   THR G N   1 
ATOM   6696  C  CA  . THR G  1 3   ? -13.758 -26.483 63.172 1.00 46.34  ? 2   THR G CA  1 
ATOM   6697  C  C   . THR G  1 3   ? -14.251 -26.769 61.748 1.00 38.43  ? 2   THR G C   1 
ATOM   6698  O  O   . THR G  1 3   ? -15.286 -27.393 61.554 1.00 37.90  ? 2   THR G O   1 
ATOM   6699  C  CB  . THR G  1 3   ? -13.101 -27.643 63.942 1.00 46.65  ? 2   THR G CB  1 
ATOM   6700  O  OG1 . THR G  1 3   ? -14.115 -28.579 64.256 1.00 53.26  ? 2   THR G OG1 1 
ATOM   6701  C  CG2 . THR G  1 3   ? -12.489 -27.220 65.260 1.00 47.51  ? 2   THR G CG2 1 
ATOM   6702  N  N   . LYS G  1 4   ? -13.515 -26.268 60.748 1.00 36.00  ? 3   LYS G N   1 
ATOM   6703  C  CA  . LYS G  1 4   ? -13.810 -26.505 59.342 1.00 36.79  ? 3   LYS G CA  1 
ATOM   6704  C  C   . LYS G  1 4   ? -12.683 -27.324 58.718 1.00 35.17  ? 3   LYS G C   1 
ATOM   6705  O  O   . LYS G  1 4   ? -11.498 -27.038 58.903 1.00 37.89  ? 3   LYS G O   1 
ATOM   6706  C  CB  . LYS G  1 4   ? -13.938 -25.207 58.537 1.00 40.58  ? 3   LYS G CB  1 
ATOM   6707  C  CG  . LYS G  1 4   ? -15.262 -24.461 58.609 1.00 48.70  ? 3   LYS G CG  1 
ATOM   6708  C  CD  . LYS G  1 4   ? -15.349 -23.343 57.556 1.00 51.75  ? 3   LYS G CD  1 
ATOM   6709  C  CE  . LYS G  1 4   ? -16.030 -23.780 56.266 1.00 52.16  ? 3   LYS G CE  1 
ATOM   6710  N  NZ  . LYS G  1 4   ? -15.463 -23.093 55.074 1.00 49.13  ? 3   LYS G NZ  1 
ATOM   6711  N  N   . VAL G  1 5   ? -13.076 -28.333 57.940 1.00 29.65  ? 4   VAL G N   1 
ATOM   6712  C  CA  . VAL G  1 5   ? -12.162 -29.269 57.321 1.00 25.70  ? 4   VAL G CA  1 
ATOM   6713  C  C   . VAL G  1 5   ? -12.594 -29.439 55.867 1.00 23.84  ? 4   VAL G C   1 
ATOM   6714  O  O   . VAL G  1 5   ? -13.749 -29.212 55.522 1.00 25.40  ? 4   VAL G O   1 
ATOM   6715  C  CB  . VAL G  1 5   ? -12.198 -30.595 58.095 1.00 27.39  ? 4   VAL G CB  1 
ATOM   6716  C  CG1 . VAL G  1 5   ? -11.560 -31.742 57.324 1.00 29.16  ? 4   VAL G CG1 1 
ATOM   6717  C  CG2 . VAL G  1 5   ? -11.564 -30.439 59.460 1.00 27.03  ? 4   VAL G CG2 1 
ATOM   6718  N  N   . VAL G  1 6   ? -11.654 -29.816 55.002 1.00 21.16  ? 5   VAL G N   1 
ATOM   6719  C  CA  . VAL G  1 6   ? -12.001 -29.943 53.600 1.00 19.03  ? 5   VAL G CA  1 
ATOM   6720  C  C   . VAL G  1 6   ? -11.256 -31.127 52.985 1.00 18.84  ? 5   VAL G C   1 
ATOM   6721  O  O   . VAL G  1 6   ? -10.253 -31.601 53.515 1.00 18.49  ? 5   VAL G O   1 
ATOM   6722  C  CB  . VAL G  1 6   ? -11.735 -28.634 52.836 1.00 17.69  ? 5   VAL G CB  1 
ATOM   6723  C  CG1 . VAL G  1 6   ? -10.248 -28.373 52.673 1.00 17.30  ? 5   VAL G CG1 1 
ATOM   6724  C  CG2 . VAL G  1 6   ? -12.423 -28.632 51.485 1.00 18.07  ? 5   VAL G CG2 1 
ATOM   6725  N  N   . CYS G  1 7   ? -11.751 -31.577 51.834 1.00 18.70  ? 6   CYS G N   1 
ATOM   6726  C  CA  . CYS G  1 7   ? -11.151 -32.705 51.163 1.00 20.03  ? 6   CYS G CA  1 
ATOM   6727  C  C   . CYS G  1 7   ? -11.401 -32.571 49.669 1.00 20.33  ? 6   CYS G C   1 
ATOM   6728  O  O   . CYS G  1 7   ? -12.539 -32.354 49.258 1.00 23.44  ? 6   CYS G O   1 
ATOM   6729  C  CB  . CYS G  1 7   ? -11.800 -33.978 51.678 1.00 22.20  ? 6   CYS G CB  1 
ATOM   6730  S  SG  . CYS G  1 7   ? -11.084 -35.478 50.953 1.00 27.09  ? 6   CYS G SG  1 
ATOM   6731  N  N   . VAL G  1 8   ? -10.335 -32.676 48.871 1.00 18.79  ? 7   VAL G N   1 
ATOM   6732  C  CA  . VAL G  1 8   ? -10.465 -32.643 47.425 1.00 18.25  ? 7   VAL G CA  1 
ATOM   6733  C  C   . VAL G  1 8   ? -10.339 -34.073 46.917 1.00 19.80  ? 7   VAL G C   1 
ATOM   6734  O  O   . VAL G  1 8   ? -9.313  -34.706 47.146 1.00 19.84  ? 7   VAL G O   1 
ATOM   6735  C  CB  . VAL G  1 8   ? -9.392  -31.749 46.779 1.00 17.25  ? 7   VAL G CB  1 
ATOM   6736  C  CG1 . VAL G  1 8   ? -9.429  -31.837 45.253 1.00 16.62  ? 7   VAL G CG1 1 
ATOM   6737  C  CG2 . VAL G  1 8   ? -9.486  -30.311 47.258 1.00 16.85  ? 7   VAL G CG2 1 
ATOM   6738  N  N   . LEU G  1 9   ? -11.371 -34.571 46.226 1.00 21.95  ? 8   LEU G N   1 
ATOM   6739  C  CA  . LEU G  1 9   ? -11.325 -35.936 45.728 1.00 23.71  ? 8   LEU G CA  1 
ATOM   6740  C  C   . LEU G  1 9   ? -10.803 -35.933 44.296 1.00 25.36  ? 8   LEU G C   1 
ATOM   6741  O  O   . LEU G  1 9   ? -11.331 -35.206 43.449 1.00 27.13  ? 8   LEU G O   1 
ATOM   6742  C  CB  . LEU G  1 9   ? -12.728 -36.544 45.774 1.00 22.52  ? 8   LEU G CB  1 
ATOM   6743  C  CG  . LEU G  1 9   ? -13.405 -36.561 47.141 1.00 23.14  ? 8   LEU G CG  1 
ATOM   6744  C  CD1 . LEU G  1 9   ? -14.880 -36.878 46.984 1.00 23.33  ? 8   LEU G CD1 1 
ATOM   6745  C  CD2 . LEU G  1 9   ? -12.745 -37.560 48.079 1.00 23.07  ? 8   LEU G CD2 1 
ATOM   6746  N  N   . LYS G  1 10  ? -9.754  -36.733 44.052 1.00 26.45  ? 9   LYS G N   1 
ATOM   6747  C  CA  . LYS G  1 10  ? -9.225  -36.987 42.719 1.00 27.87  ? 9   LYS G CA  1 
ATOM   6748  C  C   . LYS G  1 10  ? -8.962  -38.481 42.589 1.00 27.17  ? 9   LYS G C   1 
ATOM   6749  O  O   . LYS G  1 10  ? -8.804  -39.182 43.593 1.00 27.61  ? 9   LYS G O   1 
ATOM   6750  C  CB  . LYS G  1 10  ? -7.928  -36.231 42.448 1.00 30.17  ? 9   LYS G CB  1 
ATOM   6751  C  CG  . LYS G  1 10  ? -8.018  -34.732 42.213 1.00 36.39  ? 9   LYS G CG  1 
ATOM   6752  C  CD  . LYS G  1 10  ? -6.611  -34.079 42.066 1.00 42.39  ? 9   LYS G CD  1 
ATOM   6753  C  CE  . LYS G  1 10  ? -6.076  -33.038 43.069 1.00 45.00  ? 9   LYS G CE  1 
ATOM   6754  N  NZ  . LYS G  1 10  ? -6.445  -31.638 42.739 1.00 47.22  ? 9   LYS G NZ  1 
ATOM   6755  N  N   . GLY G  1 11  ? -8.925  -38.970 41.340 1.00 27.16  ? 10  GLY G N   1 
ATOM   6756  C  CA  . GLY G  1 11  ? -8.549  -40.347 41.065 1.00 31.39  ? 10  GLY G CA  1 
ATOM   6757  C  C   . GLY G  1 11  ? -7.952  -40.488 39.669 1.00 35.64  ? 10  GLY G C   1 
ATOM   6758  O  O   . GLY G  1 11  ? -7.713  -39.492 38.986 1.00 36.69  ? 10  GLY G O   1 
ATOM   6759  N  N   . ASP G  1 12  ? -7.826  -41.732 39.200 1.00 38.33  ? 11  ASP G N   1 
ATOM   6760  C  CA  . ASP G  1 12  ? -7.327  -41.991 37.857 1.00 39.22  ? 11  ASP G CA  1 
ATOM   6761  C  C   . ASP G  1 12  ? -8.372  -41.658 36.799 1.00 39.09  ? 11  ASP G C   1 
ATOM   6762  O  O   . ASP G  1 12  ? -8.017  -41.354 35.667 1.00 37.87  ? 11  ASP G O   1 
ATOM   6763  C  CB  . ASP G  1 12  ? -6.874  -43.438 37.717 1.00 41.67  ? 11  ASP G CB  1 
ATOM   6764  C  CG  . ASP G  1 12  ? -5.646  -43.697 38.568 1.00 43.67  ? 11  ASP G CG  1 
ATOM   6765  O  OD1 . ASP G  1 12  ? -4.806  -42.772 38.672 1.00 42.98  ? 11  ASP G OD1 1 
ATOM   6766  O  OD2 . ASP G  1 12  ? -5.556  -44.795 39.159 1.00 44.71  ? 11  ASP G OD2 1 
ATOM   6767  N  N   . GLY G  1 13  ? -9.653  -41.745 37.175 1.00 40.29  ? 12  GLY G N   1 
ATOM   6768  C  CA  . GLY G  1 13  ? -10.747 -41.569 36.243 1.00 39.56  ? 12  GLY G CA  1 
ATOM   6769  C  C   . GLY G  1 13  ? -11.253 -40.133 36.238 1.00 40.10  ? 12  GLY G C   1 
ATOM   6770  O  O   . GLY G  1 13  ? -10.547 -39.229 36.675 1.00 39.62  ? 12  GLY G O   1 
ATOM   6771  N  N   . PRO G  1 14  ? -12.487 -39.886 35.753 1.00 40.26  ? 13  PRO G N   1 
ATOM   6772  C  CA  . PRO G  1 14  ? -13.022 -38.523 35.676 1.00 37.25  ? 13  PRO G CA  1 
ATOM   6773  C  C   . PRO G  1 14  ? -13.684 -38.032 36.966 1.00 35.09  ? 13  PRO G C   1 
ATOM   6774  O  O   . PRO G  1 14  ? -14.195 -36.914 37.017 1.00 33.06  ? 13  PRO G O   1 
ATOM   6775  C  CB  . PRO G  1 14  ? -14.073 -38.666 34.562 1.00 39.27  ? 13  PRO G CB  1 
ATOM   6776  C  CG  . PRO G  1 14  ? -14.611 -40.095 34.732 1.00 39.92  ? 13  PRO G CG  1 
ATOM   6777  C  CD  . PRO G  1 14  ? -13.430 -40.905 35.242 1.00 40.75  ? 13  PRO G CD  1 
ATOM   6778  N  N   . VAL G  1 15  ? -13.689 -38.862 38.021 1.00 31.13  ? 14  VAL G N   1 
ATOM   6779  C  CA  . VAL G  1 15  ? -14.418 -38.479 39.215 1.00 29.89  ? 14  VAL G CA  1 
ATOM   6780  C  C   . VAL G  1 15  ? -13.594 -37.459 39.990 1.00 32.00  ? 14  VAL G C   1 
ATOM   6781  O  O   . VAL G  1 15  ? -12.418 -37.685 40.262 1.00 35.39  ? 14  VAL G O   1 
ATOM   6782  C  CB  . VAL G  1 15  ? -14.784 -39.694 40.077 1.00 27.69  ? 14  VAL G CB  1 
ATOM   6783  C  CG1 . VAL G  1 15  ? -15.464 -39.270 41.363 1.00 26.06  ? 14  VAL G CG1 1 
ATOM   6784  C  CG2 . VAL G  1 15  ? -15.653 -40.664 39.309 1.00 28.18  ? 14  VAL G CG2 1 
ATOM   6785  N  N   . GLN G  1 16  ? -14.221 -36.329 40.327 1.00 32.39  ? 15  GLN G N   1 
ATOM   6786  C  CA  . GLN G  1 16  ? -13.551 -35.328 41.147 1.00 32.67  ? 15  GLN G CA  1 
ATOM   6787  C  C   . GLN G  1 16  ? -14.585 -34.492 41.893 1.00 32.03  ? 15  GLN G C   1 
ATOM   6788  O  O   . GLN G  1 16  ? -15.732 -34.372 41.435 1.00 35.75  ? 15  GLN G O   1 
ATOM   6789  C  CB  . GLN G  1 16  ? -12.605 -34.473 40.314 1.00 35.54  ? 15  GLN G CB  1 
ATOM   6790  C  CG  . GLN G  1 16  ? -13.296 -33.666 39.218 1.00 43.38  ? 15  GLN G CG  1 
ATOM   6791  C  CD  . GLN G  1 16  ? -12.288 -32.956 38.356 1.00 48.49  ? 15  GLN G CD  1 
ATOM   6792  O  OE1 . GLN G  1 16  ? -11.170 -32.691 38.789 1.00 54.80  ? 15  GLN G OE1 1 
ATOM   6793  N  NE2 . GLN G  1 16  ? -12.694 -32.638 37.131 1.00 50.55  ? 15  GLN G NE2 1 
ATOM   6794  N  N   . GLY G  1 17  ? -14.166 -33.933 43.036 1.00 26.99  ? 16  GLY G N   1 
ATOM   6795  C  CA  . GLY G  1 17  ? -15.100 -33.195 43.866 1.00 25.34  ? 16  GLY G CA  1 
ATOM   6796  C  C   . GLY G  1 17  ? -14.429 -32.536 45.068 1.00 24.54  ? 16  GLY G C   1 
ATOM   6797  O  O   . GLY G  1 17  ? -13.277 -32.829 45.379 1.00 28.55  ? 16  GLY G O   1 
ATOM   6798  N  N   . ILE G  1 18  ? -15.181 -31.651 45.734 1.00 20.86  ? 17  ILE G N   1 
ATOM   6799  C  CA  . ILE G  1 18  ? -14.730 -31.009 46.956 1.00 18.80  ? 17  ILE G CA  1 
ATOM   6800  C  C   . ILE G  1 18  ? -15.769 -31.318 48.030 1.00 18.07  ? 17  ILE G C   1 
ATOM   6801  O  O   . ILE G  1 18  ? -16.962 -31.142 47.787 1.00 17.49  ? 17  ILE G O   1 
ATOM   6802  C  CB  . ILE G  1 18  ? -14.595 -29.490 46.736 1.00 18.07  ? 17  ILE G CB  1 
ATOM   6803  C  CG1 . ILE G  1 18  ? -13.513 -29.181 45.695 1.00 17.50  ? 17  ILE G CG1 1 
ATOM   6804  C  CG2 . ILE G  1 18  ? -14.364 -28.751 48.057 1.00 17.37  ? 17  ILE G CG2 1 
ATOM   6805  C  CD1 . ILE G  1 18  ? -13.203 -27.718 45.476 1.00 16.72  ? 17  ILE G CD1 1 
ATOM   6806  N  N   . ILE G  1 19  ? -15.321 -31.790 49.196 1.00 17.16  ? 18  ILE G N   1 
ATOM   6807  C  CA  . ILE G  1 19  ? -16.266 -32.051 50.267 1.00 17.42  ? 18  ILE G CA  1 
ATOM   6808  C  C   . ILE G  1 19  ? -15.826 -31.271 51.496 1.00 18.52  ? 18  ILE G C   1 
ATOM   6809  O  O   . ILE G  1 19  ? -14.669 -31.373 51.899 1.00 20.69  ? 18  ILE G O   1 
ATOM   6810  C  CB  . ILE G  1 19  ? -16.375 -33.558 50.571 1.00 16.25  ? 18  ILE G CB  1 
ATOM   6811  C  CG1 . ILE G  1 19  ? -16.839 -34.372 49.356 1.00 15.76  ? 18  ILE G CG1 1 
ATOM   6812  C  CG2 . ILE G  1 19  ? -17.256 -33.799 51.794 1.00 15.40  ? 18  ILE G CG2 1 
ATOM   6813  C  CD1 . ILE G  1 19  ? -18.239 -34.057 48.869 1.00 16.27  ? 18  ILE G CD1 1 
ATOM   6814  N  N   . ASN G  1 20  ? -16.763 -30.523 52.086 1.00 19.07  ? 19  ASN G N   1 
ATOM   6815  C  CA  . ASN G  1 20  ? -16.482 -29.762 53.292 1.00 20.87  ? 19  ASN G CA  1 
ATOM   6816  C  C   . ASN G  1 20  ? -17.049 -30.469 54.510 1.00 21.06  ? 19  ASN G C   1 
ATOM   6817  O  O   . ASN G  1 20  ? -18.078 -31.128 54.414 1.00 22.37  ? 19  ASN G O   1 
ATOM   6818  C  CB  . ASN G  1 20  ? -17.101 -28.368 53.227 1.00 22.62  ? 19  ASN G CB  1 
ATOM   6819  C  CG  . ASN G  1 20  ? -16.693 -27.654 51.964 1.00 23.22  ? 19  ASN G CG  1 
ATOM   6820  O  OD1 . ASN G  1 20  ? -17.440 -27.655 50.994 1.00 26.13  ? 19  ASN G OD1 1 
ATOM   6821  N  ND2 . ASN G  1 20  ? -15.498 -27.090 51.966 1.00 22.15  ? 19  ASN G ND2 1 
ATOM   6822  N  N   . PHE G  1 21  ? -16.371 -30.305 55.647 1.00 21.34  ? 20  PHE G N   1 
ATOM   6823  C  CA  . PHE G  1 21  ? -16.850 -30.831 56.913 1.00 24.22  ? 20  PHE G CA  1 
ATOM   6824  C  C   . PHE G  1 21  ? -16.841 -29.695 57.924 1.00 26.93  ? 20  PHE G C   1 
ATOM   6825  O  O   . PHE G  1 21  ? -15.863 -28.959 58.018 1.00 27.65  ? 20  PHE G O   1 
ATOM   6826  C  CB  . PHE G  1 21  ? -15.911 -31.911 57.453 1.00 23.30  ? 20  PHE G CB  1 
ATOM   6827  C  CG  . PHE G  1 21  ? -15.763 -33.132 56.585 1.00 22.65  ? 20  PHE G CG  1 
ATOM   6828  C  CD1 . PHE G  1 21  ? -15.085 -33.070 55.378 1.00 22.60  ? 20  PHE G CD1 1 
ATOM   6829  C  CD2 . PHE G  1 21  ? -16.262 -34.359 56.998 1.00 23.43  ? 20  PHE G CD2 1 
ATOM   6830  C  CE1 . PHE G  1 21  ? -14.926 -34.205 54.594 1.00 23.25  ? 20  PHE G CE1 1 
ATOM   6831  C  CE2 . PHE G  1 21  ? -16.105 -35.494 56.214 1.00 23.46  ? 20  PHE G CE2 1 
ATOM   6832  C  CZ  . PHE G  1 21  ? -15.435 -35.418 55.014 1.00 22.86  ? 20  PHE G CZ  1 
ATOM   6833  N  N   . GLU G  1 22  ? -17.929 -29.563 58.682 1.00 29.86  ? 21  GLU G N   1 
ATOM   6834  C  CA  . GLU G  1 22  ? -18.004 -28.513 59.681 1.00 32.90  ? 21  GLU G CA  1 
ATOM   6835  C  C   . GLU G  1 22  ? -18.623 -29.081 60.953 1.00 30.56  ? 21  GLU G C   1 
ATOM   6836  O  O   . GLU G  1 22  ? -19.561 -29.867 60.874 1.00 32.38  ? 21  GLU G O   1 
ATOM   6837  C  CB  . GLU G  1 22  ? -18.802 -27.334 59.116 1.00 39.86  ? 21  GLU G CB  1 
ATOM   6838  C  CG  . GLU G  1 22  ? -18.582 -26.063 59.924 1.00 51.24  ? 21  GLU G CG  1 
ATOM   6839  C  CD  . GLU G  1 22  ? -19.278 -24.818 59.407 1.00 57.46  ? 21  GLU G CD  1 
ATOM   6840  O  OE1 . GLU G  1 22  ? -19.116 -24.490 58.199 1.00 65.55  ? 21  GLU G OE1 1 
ATOM   6841  O  OE2 . GLU G  1 22  ? -19.917 -24.164 60.220 1.00 63.24  ? 21  GLU G OE2 1 
ATOM   6842  N  N   . GLN G  1 23  ? -18.084 -28.684 62.109 1.00 28.48  ? 22  GLN G N   1 
ATOM   6843  C  CA  . GLN G  1 23  ? -18.551 -29.183 63.393 1.00 30.16  ? 22  GLN G CA  1 
ATOM   6844  C  C   . GLN G  1 23  ? -18.623 -28.025 64.385 1.00 33.93  ? 22  GLN G C   1 
ATOM   6845  O  O   . GLN G  1 23  ? -17.592 -27.564 64.864 1.00 36.03  ? 22  GLN G O   1 
ATOM   6846  C  CB  . GLN G  1 23  ? -17.617 -30.279 63.902 1.00 29.76  ? 22  GLN G CB  1 
ATOM   6847  C  CG  . GLN G  1 23  ? -18.146 -31.016 65.118 1.00 30.23  ? 22  GLN G CG  1 
ATOM   6848  C  CD  . GLN G  1 23  ? -17.186 -32.052 65.656 1.00 32.09  ? 22  GLN G CD  1 
ATOM   6849  O  OE1 . GLN G  1 23  ? -15.965 -31.890 65.594 1.00 34.91  ? 22  GLN G OE1 1 
ATOM   6850  N  NE2 . GLN G  1 23  ? -17.740 -33.125 66.209 1.00 32.47  ? 22  GLN G NE2 1 
ATOM   6851  N  N   . LYS G  1 24  ? -19.849 -27.567 64.695 1.00 37.56  ? 23  LYS G N   1 
ATOM   6852  C  CA  . LYS G  1 24  ? -20.055 -26.378 65.514 1.00 38.72  ? 23  LYS G CA  1 
ATOM   6853  C  C   . LYS G  1 24  ? -19.683 -26.633 66.976 1.00 43.25  ? 23  LYS G C   1 
ATOM   6854  O  O   . LYS G  1 24  ? -18.910 -25.869 67.532 1.00 45.20  ? 23  LYS G O   1 
ATOM   6855  C  CB  . LYS G  1 24  ? -21.451 -25.774 65.284 1.00 37.60  ? 23  LYS G CB  1 
ATOM   6856  C  CG  . LYS G  1 24  ? -21.604 -24.963 63.996 0.40 36.29  ? 23  LYS G CG  1 
ATOM   6857  C  CD  . LYS G  1 24  ? -23.013 -24.862 63.429 0.40 34.87  ? 23  LYS G CD  1 
ATOM   6858  C  CE  . LYS G  1 24  ? -23.059 -23.918 62.253 0.40 32.43  ? 23  LYS G CE  1 
ATOM   6859  N  NZ  . LYS G  1 24  ? -24.452 -23.555 61.919 0.40 31.45  ? 23  LYS G NZ  1 
ATOM   6860  N  N   . GLU G  1 25  ? -20.171 -27.716 67.582 1.00 50.12  ? 24  GLU G N   1 
ATOM   6861  C  CA  . GLU G  1 25  ? -19.830 -28.041 68.964 1.00 55.09  ? 24  GLU G CA  1 
ATOM   6862  C  C   . GLU G  1 25  ? -18.809 -29.180 68.946 1.00 55.26  ? 24  GLU G C   1 
ATOM   6863  O  O   . GLU G  1 25  ? -18.806 -29.973 68.000 1.00 57.52  ? 24  GLU G O   1 
ATOM   6864  C  CB  . GLU G  1 25  ? -21.067 -28.483 69.757 1.00 67.54  ? 24  GLU G CB  1 
ATOM   6865  C  CG  . GLU G  1 25  ? -22.367 -27.748 69.463 1.00 77.28  ? 24  GLU G CG  1 
ATOM   6866  C  CD  . GLU G  1 25  ? -22.471 -26.333 69.998 1.00 80.82  ? 24  GLU G CD  1 
ATOM   6867  O  OE1 . GLU G  1 25  ? -21.674 -25.954 70.887 1.00 87.51  ? 24  GLU G OE1 1 
ATOM   6868  O  OE2 . GLU G  1 25  ? -23.355 -25.614 69.512 1.00 85.49  ? 24  GLU G OE2 1 
ATOM   6869  N  N   . SER G  1 26  ? -18.001 -29.299 70.004 1.00 60.09  ? 25  SER G N   1 
ATOM   6870  C  CA  . SER G  1 26  ? -16.858 -30.202 69.967 1.00 68.18  ? 25  SER G CA  1 
ATOM   6871  C  C   . SER G  1 26  ? -17.267 -31.676 69.930 1.00 68.84  ? 25  SER G C   1 
ATOM   6872  O  O   . SER G  1 26  ? -16.556 -32.481 69.323 1.00 76.62  ? 25  SER G O   1 
ATOM   6873  C  CB  . SER G  1 26  ? -15.833 -29.925 71.039 1.00 67.87  ? 25  SER G CB  1 
ATOM   6874  O  OG  . SER G  1 26  ? -16.485 -29.542 72.240 1.00 74.00  ? 25  SER G OG  1 
ATOM   6875  N  N   . ASN G  1 27  ? -18.386 -32.035 70.571 1.00 62.45  ? 26  ASN G N   1 
ATOM   6876  C  CA  . ASN G  1 27  ? -18.807 -33.424 70.452 1.00 65.91  ? 26  ASN G CA  1 
ATOM   6877  C  C   . ASN G  1 27  ? -20.106 -33.519 69.658 1.00 66.79  ? 26  ASN G C   1 
ATOM   6878  O  O   . ASN G  1 27  ? -20.782 -34.552 69.674 1.00 80.19  ? 26  ASN G O   1 
ATOM   6879  C  CB  . ASN G  1 27  ? -18.793 -34.196 71.773 1.00 67.99  ? 26  ASN G CB  1 
ATOM   6880  C  CG  . ASN G  1 27  ? -18.664 -35.690 71.534 1.00 65.27  ? 26  ASN G CG  1 
ATOM   6881  O  OD1 . ASN G  1 27  ? -19.680 -36.371 71.512 1.00 60.46  ? 26  ASN G OD1 1 
ATOM   6882  N  ND2 . ASN G  1 27  ? -17.465 -36.185 71.244 1.00 65.94  ? 26  ASN G ND2 1 
ATOM   6883  N  N   . GLY G  1 28  ? -20.419 -32.465 68.919 1.00 59.84  ? 27  GLY G N   1 
ATOM   6884  C  CA  . GLY G  1 28  ? -21.690 -32.344 68.219 1.00 44.73  ? 27  GLY G CA  1 
ATOM   6885  C  C   . GLY G  1 28  ? -21.620 -32.932 66.815 1.00 37.03  ? 27  GLY G C   1 
ATOM   6886  O  O   . GLY G  1 28  ? -20.574 -33.410 66.378 1.00 38.90  ? 27  GLY G O   1 
ATOM   6887  N  N   . PRO G  1 29  ? -22.743 -32.920 66.059 1.00 32.02  ? 28  PRO G N   1 
ATOM   6888  C  CA  . PRO G  1 29  ? -22.784 -33.520 64.722 1.00 30.00  ? 28  PRO G CA  1 
ATOM   6889  C  C   . PRO G  1 29  ? -21.874 -32.782 63.740 1.00 26.87  ? 28  PRO G C   1 
ATOM   6890  O  O   . PRO G  1 29  ? -21.544 -31.611 63.954 1.00 25.29  ? 28  PRO G O   1 
ATOM   6891  C  CB  . PRO G  1 29  ? -24.263 -33.361 64.328 1.00 29.48  ? 28  PRO G CB  1 
ATOM   6892  C  CG  . PRO G  1 29  ? -24.716 -32.149 65.115 1.00 28.46  ? 28  PRO G CG  1 
ATOM   6893  C  CD  . PRO G  1 29  ? -24.017 -32.306 66.444 1.00 29.23  ? 28  PRO G CD  1 
ATOM   6894  N  N   . VAL G  1 30  ? -21.496 -33.482 62.663 1.00 23.81  ? 29  VAL G N   1 
ATOM   6895  C  CA  . VAL G  1 30  ? -20.647 -32.932 61.615 1.00 22.13  ? 29  VAL G CA  1 
ATOM   6896  C  C   . VAL G  1 30  ? -21.477 -32.784 60.342 1.00 23.07  ? 29  VAL G C   1 
ATOM   6897  O  O   . VAL G  1 30  ? -22.083 -33.750 59.891 1.00 23.66  ? 29  VAL G O   1 
ATOM   6898  C  CB  . VAL G  1 30  ? -19.431 -33.837 61.354 1.00 20.30  ? 29  VAL G CB  1 
ATOM   6899  C  CG1 . VAL G  1 30  ? -18.534 -33.264 60.279 1.00 19.87  ? 29  VAL G CG1 1 
ATOM   6900  C  CG2 . VAL G  1 30  ? -18.633 -34.125 62.614 1.00 20.31  ? 29  VAL G CG2 1 
ATOM   6901  N  N   . LYS G  1 31  ? -21.512 -31.568 59.782 1.00 23.67  ? 30  LYS G N   1 
ATOM   6902  C  CA  . LYS G  1 31  ? -22.175 -31.371 58.510 1.00 26.08  ? 30  LYS G CA  1 
ATOM   6903  C  C   . LYS G  1 31  ? -21.173 -31.680 57.406 1.00 25.23  ? 30  LYS G C   1 
ATOM   6904  O  O   . LYS G  1 31  ? -20.066 -31.151 57.395 1.00 26.60  ? 30  LYS G O   1 
ATOM   6905  C  CB  . LYS G  1 31  ? -22.709 -29.939 58.362 1.00 29.95  ? 30  LYS G CB  1 
ATOM   6906  C  CG  . LYS G  1 31  ? -24.015 -29.582 59.038 1.00 37.01  ? 30  LYS G CG  1 
ATOM   6907  C  CD  . LYS G  1 31  ? -24.580 -28.290 58.466 1.00 42.98  ? 30  LYS G CD  1 
ATOM   6908  C  CE  . LYS G  1 31  ? -26.062 -28.239 58.705 1.00 49.77  ? 30  LYS G CE  1 
ATOM   6909  N  NZ  . LYS G  1 31  ? -26.399 -26.929 59.299 1.00 53.21  ? 30  LYS G NZ  1 
ATOM   6910  N  N   . VAL G  1 32  ? -21.556 -32.562 56.486 1.00 23.08  ? 31  VAL G N   1 
ATOM   6911  C  CA  . VAL G  1 32  ? -20.698 -32.917 55.372 1.00 22.22  ? 31  VAL G CA  1 
ATOM   6912  C  C   . VAL G  1 32  ? -21.404 -32.498 54.091 1.00 22.49  ? 31  VAL G C   1 
ATOM   6913  O  O   . VAL G  1 32  ? -22.464 -33.025 53.783 1.00 24.29  ? 31  VAL G O   1 
ATOM   6914  C  CB  . VAL G  1 32  ? -20.405 -34.429 55.376 1.00 20.56  ? 31  VAL G CB  1 
ATOM   6915  C  CG1 . VAL G  1 32  ? -19.428 -34.811 54.279 1.00 20.18  ? 31  VAL G CG1 1 
ATOM   6916  C  CG2 . VAL G  1 32  ? -19.903 -34.899 56.730 1.00 19.84  ? 31  VAL G CG2 1 
ATOM   6917  N  N   . TRP G  1 33  ? -20.829 -31.558 53.341 1.00 22.26  ? 32  TRP G N   1 
ATOM   6918  C  CA  . TRP G  1 33  ? -21.487 -31.169 52.101 1.00 23.23  ? 32  TRP G CA  1 
ATOM   6919  C  C   . TRP G  1 33  ? -20.466 -30.837 51.018 1.00 22.61  ? 32  TRP G C   1 
ATOM   6920  O  O   . TRP G  1 33  ? -19.317 -30.466 51.307 1.00 24.85  ? 32  TRP G O   1 
ATOM   6921  C  CB  . TRP G  1 33  ? -22.428 -29.982 52.317 1.00 25.80  ? 32  TRP G CB  1 
ATOM   6922  C  CG  . TRP G  1 33  ? -21.718 -28.658 52.382 1.00 28.43  ? 32  TRP G CG  1 
ATOM   6923  C  CD1 . TRP G  1 33  ? -21.567 -27.736 51.379 1.00 28.06  ? 32  TRP G CD1 1 
ATOM   6924  C  CD2 . TRP G  1 33  ? -21.034 -28.120 53.526 1.00 29.11  ? 32  TRP G CD2 1 
ATOM   6925  N  NE1 . TRP G  1 33  ? -20.852 -26.656 51.829 1.00 29.07  ? 32  TRP G NE1 1 
ATOM   6926  C  CE2 . TRP G  1 33  ? -20.517 -26.862 53.146 1.00 28.62  ? 32  TRP G CE2 1 
ATOM   6927  C  CE3 . TRP G  1 33  ? -20.817 -28.581 54.833 1.00 30.43  ? 32  TRP G CE3 1 
ATOM   6928  C  CZ2 . TRP G  1 33  ? -19.794 -26.060 54.031 1.00 28.98  ? 32  TRP G CZ2 1 
ATOM   6929  C  CZ3 . TRP G  1 33  ? -20.096 -27.787 55.707 1.00 31.59  ? 32  TRP G CZ3 1 
ATOM   6930  C  CH2 . TRP G  1 33  ? -19.599 -26.540 55.312 1.00 30.67  ? 32  TRP G CH2 1 
ATOM   6931  N  N   . GLY G  1 34  ? -20.940 -30.920 49.776 1.00 20.12  ? 33  GLY G N   1 
ATOM   6932  C  CA  . GLY G  1 34  ? -20.150 -30.517 48.638 1.00 19.49  ? 33  GLY G CA  1 
ATOM   6933  C  C   . GLY G  1 34  ? -20.674 -31.195 47.381 1.00 19.61  ? 33  GLY G C   1 
ATOM   6934  O  O   . GLY G  1 34  ? -21.809 -31.658 47.329 1.00 19.06  ? 33  GLY G O   1 
ATOM   6935  N  N   . SER G  1 35  ? -19.824 -31.277 46.369 1.00 20.27  ? 34  SER G N   1 
ATOM   6936  C  CA  . SER G  1 35  ? -20.285 -31.764 45.087 1.00 20.84  ? 34  SER G CA  1 
ATOM   6937  C  C   . SER G  1 35  ? -19.234 -32.712 44.498 1.00 22.48  ? 34  SER G C   1 
ATOM   6938  O  O   . SER G  1 35  ? -18.030 -32.469 44.637 1.00 25.86  ? 34  SER G O   1 
ATOM   6939  C  CB  . SER G  1 35  ? -20.539 -30.570 44.239 1.00 20.72  ? 34  SER G CB  1 
ATOM   6940  O  OG  . SER G  1 35  ? -20.752 -30.965 42.900 1.00 24.04  ? 34  SER G OG  1 
ATOM   6941  N  N   . ILE G  1 36  ? -19.682 -33.827 43.902 1.00 22.53  ? 35  ILE G N   1 
ATOM   6942  C  CA  . ILE G  1 36  ? -18.783 -34.695 43.162 1.00 22.81  ? 35  ILE G CA  1 
ATOM   6943  C  C   . ILE G  1 36  ? -19.343 -34.845 41.749 1.00 25.97  ? 35  ILE G C   1 
ATOM   6944  O  O   . ILE G  1 36  ? -20.550 -35.026 41.572 1.00 25.84  ? 35  ILE G O   1 
ATOM   6945  C  CB  . ILE G  1 36  ? -18.662 -36.061 43.852 1.00 21.38  ? 35  ILE G CB  1 
ATOM   6946  C  CG1 . ILE G  1 36  ? -18.377 -35.916 45.344 1.00 21.72  ? 35  ILE G CG1 1 
ATOM   6947  C  CG2 . ILE G  1 36  ? -17.619 -36.918 43.159 1.00 21.27  ? 35  ILE G CG2 1 
ATOM   6948  C  CD1 . ILE G  1 36  ? -18.449 -37.210 46.116 1.00 22.11  ? 35  ILE G CD1 1 
ATOM   6949  N  N   . LYS G  1 37  ? -18.457 -34.768 40.748 1.00 28.62  ? 36  LYS G N   1 
ATOM   6950  C  CA  . LYS G  1 37  ? -18.905 -34.902 39.371 1.00 29.63  ? 36  LYS G CA  1 
ATOM   6951  C  C   . LYS G  1 37  ? -18.173 -36.062 38.700 1.00 29.20  ? 36  LYS G C   1 
ATOM   6952  O  O   . LYS G  1 37  ? -17.171 -36.551 39.222 1.00 30.40  ? 36  LYS G O   1 
ATOM   6953  C  CB  . LYS G  1 37  ? -18.761 -33.571 38.627 1.00 32.66  ? 36  LYS G CB  1 
ATOM   6954  C  CG  . LYS G  1 37  ? -17.324 -33.098 38.412 1.00 34.91  ? 36  LYS G CG  1 
ATOM   6955  C  CD  . LYS G  1 37  ? -17.185 -32.043 37.339 1.00 40.89  ? 36  LYS G CD  1 
ATOM   6956  C  CE  . LYS G  1 37  ? -15.861 -32.100 36.594 1.00 49.33  ? 36  LYS G CE  1 
ATOM   6957  N  NZ  . LYS G  1 37  ? -15.726 -30.969 35.647 1.00 50.48  ? 36  LYS G NZ  1 
ATOM   6958  N  N   . GLY G  1 38  ? -18.706 -36.508 37.557 1.00 27.59  ? 37  GLY G N   1 
ATOM   6959  C  CA  . GLY G  1 38  ? -18.103 -37.576 36.770 1.00 25.85  ? 37  GLY G CA  1 
ATOM   6960  C  C   . GLY G  1 38  ? -18.495 -38.982 37.229 1.00 25.05  ? 37  GLY G C   1 
ATOM   6961  O  O   . GLY G  1 38  ? -17.877 -39.959 36.806 1.00 25.95  ? 37  GLY G O   1 
ATOM   6962  N  N   . LEU G  1 39  ? -19.525 -39.085 38.077 1.00 24.06  ? 38  LEU G N   1 
ATOM   6963  C  CA  . LEU G  1 39  ? -19.976 -40.375 38.587 1.00 25.42  ? 38  LEU G CA  1 
ATOM   6964  C  C   . LEU G  1 39  ? -21.019 -40.964 37.641 1.00 26.98  ? 38  LEU G C   1 
ATOM   6965  O  O   . LEU G  1 39  ? -21.689 -40.224 36.919 1.00 27.32  ? 38  LEU G O   1 
ATOM   6966  C  CB  . LEU G  1 39  ? -20.594 -40.166 39.975 1.00 24.99  ? 38  LEU G CB  1 
ATOM   6967  C  CG  . LEU G  1 39  ? -19.600 -39.836 41.084 1.00 24.86  ? 38  LEU G CG  1 
ATOM   6968  C  CD1 . LEU G  1 39  ? -20.325 -39.277 42.291 1.00 23.44  ? 38  LEU G CD1 1 
ATOM   6969  C  CD2 . LEU G  1 39  ? -18.779 -41.063 41.456 1.00 25.06  ? 38  LEU G CD2 1 
ATOM   6970  N  N   . THR G  1 40  ? -21.166 -42.293 37.669 1.00 27.57  ? 39  THR G N   1 
ATOM   6971  C  CA  . THR G  1 40  ? -22.294 -42.928 37.002 1.00 27.87  ? 39  THR G CA  1 
ATOM   6972  C  C   . THR G  1 40  ? -23.553 -42.657 37.823 1.00 30.33  ? 39  THR G C   1 
ATOM   6973  O  O   . THR G  1 40  ? -23.480 -42.533 39.047 1.00 30.58  ? 39  THR G O   1 
ATOM   6974  C  CB  . THR G  1 40  ? -22.098 -44.440 36.854 1.00 25.91  ? 39  THR G CB  1 
ATOM   6975  O  OG1 . THR G  1 40  ? -21.718 -44.905 38.144 1.00 26.88  ? 39  THR G OG1 1 
ATOM   6976  C  CG2 . THR G  1 40  ? -21.034 -44.824 35.856 1.00 25.07  ? 39  THR G CG2 1 
ATOM   6977  N  N   . GLU G  1 41  ? -24.701 -42.559 37.144 1.00 30.43  ? 40  GLU G N   1 
ATOM   6978  C  CA  . GLU G  1 41  ? -25.956 -42.277 37.818 1.00 30.56  ? 40  GLU G CA  1 
ATOM   6979  C  C   . GLU G  1 41  ? -26.191 -43.333 38.892 1.00 31.41  ? 40  GLU G C   1 
ATOM   6980  O  O   . GLU G  1 41  ? -25.879 -44.508 38.683 1.00 35.37  ? 40  GLU G O   1 
ATOM   6981  C  CB  . GLU G  1 41  ? -27.105 -42.267 36.812 1.00 32.89  ? 40  GLU G CB  1 
ATOM   6982  C  CG  . GLU G  1 41  ? -28.420 -41.867 37.451 1.00 36.65  ? 40  GLU G CG  1 
ATOM   6983  C  CD  . GLU G  1 41  ? -29.627 -41.744 36.551 1.00 38.71  ? 40  GLU G CD  1 
ATOM   6984  O  OE1 . GLU G  1 41  ? -29.524 -42.145 35.377 1.00 39.12  ? 40  GLU G OE1 1 
ATOM   6985  O  OE2 . GLU G  1 41  ? -30.663 -41.238 37.034 1.00 37.73  ? 40  GLU G OE2 1 
ATOM   6986  N  N   . GLY G  1 42  ? -26.708 -42.909 40.052 1.00 28.20  ? 41  GLY G N   1 
ATOM   6987  C  CA  . GLY G  1 42  ? -27.078 -43.861 41.084 1.00 27.01  ? 41  GLY G CA  1 
ATOM   6988  C  C   . GLY G  1 42  ? -26.238 -43.718 42.355 1.00 28.48  ? 41  GLY G C   1 
ATOM   6989  O  O   . GLY G  1 42  ? -25.571 -42.699 42.573 1.00 30.20  ? 41  GLY G O   1 
ATOM   6990  N  N   . LEU G  1 43  ? -26.303 -44.765 43.202 1.00 25.62  ? 42  LEU G N   1 
ATOM   6991  C  CA  . LEU G  1 43  ? -25.715 -44.745 44.536 1.00 24.14  ? 42  LEU G CA  1 
ATOM   6992  C  C   . LEU G  1 43  ? -24.229 -45.071 44.456 1.00 24.20  ? 42  LEU G C   1 
ATOM   6993  O  O   . LEU G  1 43  ? -23.826 -45.925 43.671 1.00 25.43  ? 42  LEU G O   1 
ATOM   6994  C  CB  . LEU G  1 43  ? -26.430 -45.776 45.411 1.00 23.23  ? 42  LEU G CB  1 
ATOM   6995  C  CG  . LEU G  1 43  ? -27.893 -45.482 45.728 1.00 22.38  ? 42  LEU G CG  1 
ATOM   6996  C  CD1 . LEU G  1 43  ? -28.579 -46.699 46.313 1.00 21.79  ? 42  LEU G CD1 1 
ATOM   6997  C  CD2 . LEU G  1 43  ? -27.987 -44.276 46.650 1.00 23.30  ? 42  LEU G CD2 1 
ATOM   6998  N  N   . HIS G  1 44  ? -23.435 -44.384 45.286 1.00 23.38  ? 43  HIS G N   1 
ATOM   6999  C  CA  . HIS G  1 44  ? -22.011 -44.642 45.436 1.00 21.30  ? 43  HIS G CA  1 
ATOM   7000  C  C   . HIS G  1 44  ? -21.642 -44.622 46.917 1.00 22.42  ? 43  HIS G C   1 
ATOM   7001  O  O   . HIS G  1 44  ? -22.040 -43.726 47.664 1.00 22.48  ? 43  HIS G O   1 
ATOM   7002  C  CB  . HIS G  1 44  ? -21.181 -43.634 44.645 1.00 19.32  ? 43  HIS G CB  1 
ATOM   7003  C  CG  . HIS G  1 44  ? -21.369 -43.722 43.171 1.00 19.03  ? 43  HIS G CG  1 
ATOM   7004  N  ND1 . HIS G  1 44  ? -20.513 -44.451 42.361 1.00 19.20  ? 43  HIS G ND1 1 
ATOM   7005  C  CD2 . HIS G  1 44  ? -22.285 -43.163 42.349 1.00 19.13  ? 43  HIS G CD2 1 
ATOM   7006  C  CE1 . HIS G  1 44  ? -20.890 -44.341 41.101 1.00 19.06  ? 43  HIS G CE1 1 
ATOM   7007  N  NE2 . HIS G  1 44  ? -21.979 -43.552 41.068 1.00 19.66  ? 43  HIS G NE2 1 
ATOM   7008  N  N   . GLY G  1 45  ? -20.892 -45.647 47.324 1.00 24.15  ? 44  GLY G N   1 
ATOM   7009  C  CA  . GLY G  1 45  ? -20.415 -45.764 48.686 1.00 23.89  ? 44  GLY G CA  1 
ATOM   7010  C  C   . GLY G  1 45  ? -19.457 -44.622 49.022 1.00 23.71  ? 44  GLY G C   1 
ATOM   7011  O  O   . GLY G  1 45  ? -18.652 -44.188 48.189 1.00 23.62  ? 44  GLY G O   1 
ATOM   7012  N  N   . PHE G  1 46  ? -19.554 -44.160 50.270 1.00 22.15  ? 45  PHE G N   1 
ATOM   7013  C  CA  . PHE G  1 46  ? -18.907 -42.933 50.680 1.00 20.98  ? 45  PHE G CA  1 
ATOM   7014  C  C   . PHE G  1 46  ? -18.354 -43.150 52.078 1.00 21.48  ? 45  PHE G C   1 
ATOM   7015  O  O   . PHE G  1 46  ? -19.134 -43.218 53.026 1.00 25.99  ? 45  PHE G O   1 
ATOM   7016  C  CB  . PHE G  1 46  ? -19.965 -41.829 50.678 1.00 19.09  ? 45  PHE G CB  1 
ATOM   7017  C  CG  . PHE G  1 46  ? -19.457 -40.413 50.771 1.00 18.07  ? 45  PHE G CG  1 
ATOM   7018  C  CD1 . PHE G  1 46  ? -18.708 -39.857 49.744 1.00 17.14  ? 45  PHE G CD1 1 
ATOM   7019  C  CD2 . PHE G  1 46  ? -19.786 -39.622 51.861 1.00 17.78  ? 45  PHE G CD2 1 
ATOM   7020  C  CE1 . PHE G  1 46  ? -18.258 -38.548 49.825 1.00 16.88  ? 45  PHE G CE1 1 
ATOM   7021  C  CE2 . PHE G  1 46  ? -19.361 -38.300 51.922 1.00 17.98  ? 45  PHE G CE2 1 
ATOM   7022  C  CZ  . PHE G  1 46  ? -18.615 -37.761 50.895 1.00 17.19  ? 45  PHE G CZ  1 
ATOM   7023  N  N   . HIS G  1 47  ? -17.026 -43.284 52.187 1.00 20.13  ? 46  HIS G N   1 
ATOM   7024  C  CA  . HIS G  1 47  ? -16.442 -43.689 53.453 1.00 21.08  ? 46  HIS G CA  1 
ATOM   7025  C  C   . HIS G  1 47  ? -15.180 -42.895 53.771 1.00 21.01  ? 46  HIS G C   1 
ATOM   7026  O  O   . HIS G  1 47  ? -14.464 -42.430 52.885 1.00 20.48  ? 46  HIS G O   1 
ATOM   7027  C  CB  . HIS G  1 47  ? -16.096 -45.181 53.442 1.00 22.90  ? 46  HIS G CB  1 
ATOM   7028  C  CG  . HIS G  1 47  ? -17.146 -46.028 52.811 1.00 25.79  ? 46  HIS G CG  1 
ATOM   7029  N  ND1 . HIS G  1 47  ? -16.968 -46.627 51.581 1.00 26.30  ? 46  HIS G ND1 1 
ATOM   7030  C  CD2 . HIS G  1 47  ? -18.394 -46.363 53.213 1.00 27.11  ? 46  HIS G CD2 1 
ATOM   7031  C  CE1 . HIS G  1 47  ? -18.061 -47.291 51.260 1.00 25.45  ? 46  HIS G CE1 1 
ATOM   7032  N  NE2 . HIS G  1 47  ? -18.955 -47.144 52.244 1.00 25.17  ? 46  HIS G NE2 1 
ATOM   7033  N  N   . VAL G  1 48  ? -14.915 -42.790 55.073 1.00 20.60  ? 47  VAL G N   1 
ATOM   7034  C  CA  . VAL G  1 48  ? -13.604 -42.394 55.550 1.00 21.25  ? 47  VAL G CA  1 
ATOM   7035  C  C   . VAL G  1 48  ? -12.780 -43.658 55.770 1.00 22.62  ? 47  VAL G C   1 
ATOM   7036  O  O   . VAL G  1 48  ? -13.133 -44.488 56.608 1.00 23.51  ? 47  VAL G O   1 
ATOM   7037  C  CB  . VAL G  1 48  ? -13.683 -41.564 56.844 1.00 21.73  ? 47  VAL G CB  1 
ATOM   7038  C  CG1 . VAL G  1 48  ? -12.310 -41.099 57.279 1.00 21.08  ? 47  VAL G CG1 1 
ATOM   7039  C  CG2 . VAL G  1 48  ? -14.635 -40.384 56.714 1.00 21.24  ? 47  VAL G CG2 1 
ATOM   7040  N  N   . HIS G  1 49  ? -11.687 -43.795 55.007 1.00 23.01  ? 48  HIS G N   1 
ATOM   7041  C  CA  . HIS G  1 49  ? -10.721 -44.862 55.213 1.00 24.32  ? 48  HIS G CA  1 
ATOM   7042  C  C   . HIS G  1 49  ? -9.659  -44.430 56.229 1.00 26.44  ? 48  HIS G C   1 
ATOM   7043  O  O   . HIS G  1 49  ? -9.570  -43.257 56.583 1.00 27.09  ? 48  HIS G O   1 
ATOM   7044  C  CB  . HIS G  1 49  ? -10.124 -45.293 53.873 1.00 25.48  ? 48  HIS G CB  1 
ATOM   7045  C  CG  . HIS G  1 49  ? -11.121 -45.939 52.973 1.00 27.09  ? 48  HIS G CG  1 
ATOM   7046  N  ND1 . HIS G  1 49  ? -10.952 -47.230 52.499 1.00 28.13  ? 48  HIS G ND1 1 
ATOM   7047  C  CD2 . HIS G  1 49  ? -12.288 -45.486 52.457 1.00 28.45  ? 48  HIS G CD2 1 
ATOM   7048  C  CE1 . HIS G  1 49  ? -11.966 -47.550 51.722 1.00 29.53  ? 48  HIS G CE1 1 
ATOM   7049  N  NE2 . HIS G  1 49  ? -12.810 -46.487 51.688 1.00 28.41  ? 48  HIS G NE2 1 
ATOM   7050  N  N   . GLU G  1 50  ? -8.830  -45.388 56.664 1.00 27.46  ? 49  GLU G N   1 
ATOM   7051  C  CA  . GLU G  1 50  ? -7.998  -45.258 57.852 1.00 26.84  ? 49  GLU G CA  1 
ATOM   7052  C  C   . GLU G  1 50  ? -6.824  -44.298 57.651 1.00 25.43  ? 49  GLU G C   1 
ATOM   7053  O  O   . GLU G  1 50  ? -6.526  -43.513 58.549 1.00 26.26  ? 49  GLU G O   1 
ATOM   7054  C  CB  . GLU G  1 50  ? -7.441  -46.620 58.260 1.00 27.94  ? 49  GLU G CB  1 
ATOM   7055  C  CG  . GLU G  1 50  ? -6.897  -46.617 59.673 1.00 30.38  ? 49  GLU G CG  1 
ATOM   7056  C  CD  . GLU G  1 50  ? -6.335  -47.944 60.156 1.00 31.29  ? 49  GLU G CD  1 
ATOM   7057  O  OE1 . GLU G  1 50  ? -6.656  -49.009 59.555 1.00 29.32  ? 49  GLU G OE1 1 
ATOM   7058  O  OE2 . GLU G  1 50  ? -5.569  -47.900 61.142 1.00 32.31  ? 49  GLU G OE2 1 
ATOM   7059  N  N   . PHE G  1 51  ? -6.154  -44.380 56.494 1.00 23.31  ? 50  PHE G N   1 
ATOM   7060  C  CA  . PHE G  1 51  ? -4.875  -43.716 56.321 1.00 22.77  ? 50  PHE G CA  1 
ATOM   7061  C  C   . PHE G  1 51  ? -4.962  -42.571 55.324 1.00 22.35  ? 50  PHE G C   1 
ATOM   7062  O  O   . PHE G  1 51  ? -5.484  -42.745 54.222 1.00 23.26  ? 50  PHE G O   1 
ATOM   7063  C  CB  . PHE G  1 51  ? -3.823  -44.707 55.818 1.00 22.39  ? 50  PHE G CB  1 
ATOM   7064  C  CG  . PHE G  1 51  ? -3.676  -45.910 56.705 1.00 20.91  ? 50  PHE G CG  1 
ATOM   7065  C  CD1 . PHE G  1 51  ? -3.376  -45.751 58.053 1.00 20.59  ? 50  PHE G CD1 1 
ATOM   7066  C  CD2 . PHE G  1 51  ? -3.854  -47.188 56.201 1.00 19.95  ? 50  PHE G CD2 1 
ATOM   7067  C  CE1 . PHE G  1 51  ? -3.249  -46.853 58.890 1.00 19.90  ? 50  PHE G CE1 1 
ATOM   7068  C  CE2 . PHE G  1 51  ? -3.717  -48.289 57.041 1.00 20.85  ? 50  PHE G CE2 1 
ATOM   7069  C  CZ  . PHE G  1 51  ? -3.425  -48.118 58.386 1.00 19.67  ? 50  PHE G CZ  1 
ATOM   7070  N  N   . GLY G  1 52  ? -4.402  -41.424 55.729 1.00 21.61  ? 51  GLY G N   1 
ATOM   7071  C  CA  . GLY G  1 52  ? -4.146  -40.309 54.838 1.00 21.75  ? 51  GLY G CA  1 
ATOM   7072  C  C   . GLY G  1 52  ? -2.902  -40.573 53.998 1.00 21.25  ? 51  GLY G C   1 
ATOM   7073  O  O   . GLY G  1 52  ? -1.955  -39.793 53.990 1.00 21.58  ? 51  GLY G O   1 
ATOM   7074  N  N   . ASP G  1 53  ? -2.922  -41.688 53.279 1.00 21.61  ? 52  ASP G N   1 
ATOM   7075  C  CA  . ASP G  1 53  ? -1.748  -42.139 52.558 1.00 23.31  ? 52  ASP G CA  1 
ATOM   7076  C  C   . ASP G  1 53  ? -2.148  -42.364 51.106 1.00 25.00  ? 52  ASP G C   1 
ATOM   7077  O  O   . ASP G  1 53  ? -2.959  -43.237 50.813 1.00 25.89  ? 52  ASP G O   1 
ATOM   7078  C  CB  . ASP G  1 53  ? -1.179  -43.395 53.210 1.00 22.73  ? 52  ASP G CB  1 
ATOM   7079  C  CG  . ASP G  1 53  ? 0.069   -43.944 52.530 1.00 22.59  ? 52  ASP G CG  1 
ATOM   7080  O  OD1 . ASP G  1 53  ? 0.270   -43.670 51.318 1.00 19.98  ? 52  ASP G OD1 1 
ATOM   7081  O  OD2 . ASP G  1 53  ? 0.820   -44.670 53.223 1.00 23.50  ? 52  ASP G OD2 1 
ATOM   7082  N  N   . ASN G  1 54  ? -1.581  -41.554 50.209 1.00 25.43  ? 53  ASN G N   1 
ATOM   7083  C  CA  . ASN G  1 54  ? -1.962  -41.616 48.812 1.00 24.78  ? 53  ASN G CA  1 
ATOM   7084  C  C   . ASN G  1 54  ? -0.763  -42.082 47.987 1.00 23.96  ? 53  ASN G C   1 
ATOM   7085  O  O   . ASN G  1 54  ? -0.738  -41.920 46.774 1.00 23.39  ? 53  ASN G O   1 
ATOM   7086  C  CB  . ASN G  1 54  ? -2.572  -40.277 48.382 1.00 25.88  ? 53  ASN G CB  1 
ATOM   7087  C  CG  . ASN G  1 54  ? -3.039  -40.244 46.939 1.00 28.85  ? 53  ASN G CG  1 
ATOM   7088  O  OD1 . ASN G  1 54  ? -3.820  -41.098 46.504 1.00 30.62  ? 53  ASN G OD1 1 
ATOM   7089  N  ND2 . ASN G  1 54  ? -2.579  -39.243 46.198 1.00 31.09  ? 53  ASN G ND2 1 
ATOM   7090  N  N   . THR G  1 55  ? 0.221   -42.701 48.649 1.00 25.18  ? 54  THR G N   1 
ATOM   7091  C  CA  . THR G  1 55  ? 1.485   -43.031 48.003 1.00 26.72  ? 54  THR G CA  1 
ATOM   7092  C  C   . THR G  1 55  ? 1.267   -43.974 46.825 1.00 28.66  ? 54  THR G C   1 
ATOM   7093  O  O   . THR G  1 55  ? 2.012   -43.921 45.854 1.00 29.69  ? 54  THR G O   1 
ATOM   7094  C  CB  . THR G  1 55  ? 2.500   -43.652 48.973 1.00 25.87  ? 54  THR G CB  1 
ATOM   7095  O  OG1 . THR G  1 55  ? 1.895   -44.816 49.538 1.00 25.06  ? 54  THR G OG1 1 
ATOM   7096  C  CG2 . THR G  1 55  ? 2.912   -42.714 50.086 1.00 25.33  ? 54  THR G CG2 1 
ATOM   7097  N  N   . ALA G  1 56  ? 0.253   -44.839 46.923 1.00 31.67  ? 55  ALA G N   1 
ATOM   7098  C  CA  . ALA G  1 56  ? -0.026  -45.808 45.879 1.00 34.77  ? 55  ALA G CA  1 
ATOM   7099  C  C   . ALA G  1 56  ? -1.453  -45.606 45.389 1.00 35.18  ? 55  ALA G C   1 
ATOM   7100  O  O   . ALA G  1 56  ? -2.183  -46.572 45.208 1.00 43.54  ? 55  ALA G O   1 
ATOM   7101  C  CB  . ALA G  1 56  ? 0.183   -47.201 46.426 1.00 35.08  ? 55  ALA G CB  1 
ATOM   7102  N  N   . GLY G  1 57  ? -1.847  -44.344 45.196 1.00 31.62  ? 56  GLY G N   1 
ATOM   7103  C  CA  . GLY G  1 57  ? -3.218  -44.017 44.839 1.00 27.84  ? 56  GLY G CA  1 
ATOM   7104  C  C   . GLY G  1 57  ? -4.169  -44.230 46.016 1.00 28.26  ? 56  GLY G C   1 
ATOM   7105  O  O   . GLY G  1 57  ? -3.743  -44.232 47.175 1.00 27.53  ? 56  GLY G O   1 
ATOM   7106  N  N   . CYS G  1 58  ? -5.447  -44.444 45.699 1.00 28.14  ? 57  CYS G N   1 
ATOM   7107  C  CA  . CYS G  1 58  ? -6.462  -44.575 46.730 1.00 26.76  ? 57  CYS G CA  1 
ATOM   7108  C  C   . CYS G  1 58  ? -6.288  -45.862 47.533 1.00 24.73  ? 57  CYS G C   1 
ATOM   7109  O  O   . CYS G  1 58  ? -6.727  -45.929 48.675 1.00 23.28  ? 57  CYS G O   1 
ATOM   7110  C  CB  . CYS G  1 58  ? -7.868  -44.504 46.143 1.00 27.71  ? 57  CYS G CB  1 
ATOM   7111  S  SG  . CYS G  1 58  ? -8.221  -42.852 45.472 1.00 32.81  ? 57  CYS G SG  1 
ATOM   7112  N  N   . THR G  1 59  ? -5.620  -46.856 46.938 1.00 24.19  ? 58  THR G N   1 
ATOM   7113  C  CA  . THR G  1 59  ? -5.438  -48.157 47.560 1.00 27.24  ? 58  THR G CA  1 
ATOM   7114  C  C   . THR G  1 59  ? -4.761  -48.012 48.920 1.00 30.52  ? 58  THR G C   1 
ATOM   7115  O  O   . THR G  1 59  ? -5.094  -48.733 49.868 1.00 34.28  ? 58  THR G O   1 
ATOM   7116  C  CB  . THR G  1 59  ? -4.502  -49.064 46.757 1.00 26.42  ? 58  THR G CB  1 
ATOM   7117  O  OG1 . THR G  1 59  ? -4.941  -49.038 45.403 1.00 25.66  ? 58  THR G OG1 1 
ATOM   7118  C  CG2 . THR G  1 59  ? -4.504  -50.485 47.278 1.00 25.43  ? 58  THR G CG2 1 
ATOM   7119  N  N   . SER G  1 60  ? -3.787  -47.097 48.998 1.00 29.50  ? 59  SER G N   1 
ATOM   7120  C  CA  . SER G  1 60  ? -2.929  -47.067 50.169 1.00 26.92  ? 59  SER G CA  1 
ATOM   7121  C  C   . SER G  1 60  ? -3.639  -46.407 51.352 1.00 24.68  ? 59  SER G C   1 
ATOM   7122  O  O   . SER G  1 60  ? -3.073  -46.305 52.440 1.00 24.47  ? 59  SER G O   1 
ATOM   7123  C  CB  . SER G  1 60  ? -1.561  -46.504 49.856 1.00 27.10  ? 59  SER G CB  1 
ATOM   7124  O  OG  . SER G  1 60  ? -1.664  -45.229 49.252 1.00 28.09  ? 59  SER G OG  1 
ATOM   7125  N  N   . ALA G  1 61  ? -4.908  -46.032 51.141 1.00 23.07  ? 60  ALA G N   1 
ATOM   7126  C  CA  . ALA G  1 61  ? -5.735  -45.419 52.169 1.00 22.04  ? 60  ALA G CA  1 
ATOM   7127  C  C   . ALA G  1 61  ? -6.151  -46.461 53.206 1.00 21.73  ? 60  ALA G C   1 
ATOM   7128  O  O   . ALA G  1 61  ? -6.568  -46.104 54.312 1.00 21.62  ? 60  ALA G O   1 
ATOM   7129  C  CB  . ALA G  1 61  ? -6.941  -44.778 51.543 1.00 21.13  ? 60  ALA G CB  1 
ATOM   7130  N  N   . GLY G  1 62  ? -6.036  -47.744 52.826 1.00 20.06  ? 61  GLY G N   1 
ATOM   7131  C  CA  . GLY G  1 62  ? -6.383  -48.844 53.708 1.00 19.54  ? 61  GLY G CA  1 
ATOM   7132  C  C   . GLY G  1 62  ? -7.892  -49.058 53.827 1.00 19.80  ? 61  GLY G C   1 
ATOM   7133  O  O   . GLY G  1 62  ? -8.650  -48.617 52.961 1.00 18.30  ? 61  GLY G O   1 
ATOM   7134  N  N   . PRO G  1 63  ? -8.368  -49.738 54.899 1.00 20.47  ? 62  PRO G N   1 
ATOM   7135  C  CA  . PRO G  1 63  ? -9.781  -50.107 55.041 1.00 21.17  ? 62  PRO G CA  1 
ATOM   7136  C  C   . PRO G  1 63  ? -10.625 -48.946 55.570 1.00 22.01  ? 62  PRO G C   1 
ATOM   7137  O  O   . PRO G  1 63  ? -10.089 -47.878 55.855 1.00 22.10  ? 62  PRO G O   1 
ATOM   7138  C  CB  . PRO G  1 63  ? -9.714  -51.211 56.103 1.00 19.74  ? 62  PRO G CB  1 
ATOM   7139  C  CG  . PRO G  1 63  ? -8.591  -50.773 56.999 1.00 20.03  ? 62  PRO G CG  1 
ATOM   7140  C  CD  . PRO G  1 63  ? -7.567  -50.167 56.056 1.00 20.74  ? 62  PRO G CD  1 
ATOM   7141  N  N   . HIS G  1 64  ? -11.944 -49.156 55.704 1.00 21.73  ? 63  HIS G N   1 
ATOM   7142  C  CA  . HIS G  1 64  ? -12.793 -48.158 56.333 1.00 21.65  ? 63  HIS G CA  1 
ATOM   7143  C  C   . HIS G  1 64  ? -12.234 -47.857 57.721 1.00 22.59  ? 63  HIS G C   1 
ATOM   7144  O  O   . HIS G  1 64  ? -11.852 -48.778 58.430 1.00 22.55  ? 63  HIS G O   1 
ATOM   7145  C  CB  . HIS G  1 64  ? -14.241 -48.658 56.451 1.00 21.11  ? 63  HIS G CB  1 
ATOM   7146  C  CG  . HIS G  1 64  ? -14.932 -48.900 55.150 1.00 20.73  ? 63  HIS G CG  1 
ATOM   7147  N  ND1 . HIS G  1 64  ? -16.200 -49.478 55.095 1.00 20.11  ? 63  HIS G ND1 1 
ATOM   7148  C  CD2 . HIS G  1 64  ? -14.551 -48.643 53.874 1.00 19.90  ? 63  HIS G CD2 1 
ATOM   7149  C  CE1 . HIS G  1 64  ? -16.581 -49.571 53.845 1.00 19.74  ? 63  HIS G CE1 1 
ATOM   7150  N  NE2 . HIS G  1 64  ? -15.579 -49.065 53.066 1.00 20.91  ? 63  HIS G NE2 1 
ATOM   7151  N  N   . PHE G  1 65  ? -12.186 -46.570 58.095 1.00 22.46  ? 64  PHE G N   1 
ATOM   7152  C  CA  . PHE G  1 65  ? -11.723 -46.157 59.413 1.00 21.15  ? 64  PHE G CA  1 
ATOM   7153  C  C   . PHE G  1 65  ? -12.542 -46.855 60.494 1.00 21.04  ? 64  PHE G C   1 
ATOM   7154  O  O   . PHE G  1 65  ? -13.739 -46.630 60.614 1.00 21.06  ? 64  PHE G O   1 
ATOM   7155  C  CB  . PHE G  1 65  ? -11.755 -44.632 59.543 1.00 20.38  ? 64  PHE G CB  1 
ATOM   7156  C  CG  . PHE G  1 65  ? -11.308 -44.096 60.881 1.00 21.47  ? 64  PHE G CG  1 
ATOM   7157  C  CD1 . PHE G  1 65  ? -10.184 -44.622 61.518 1.00 22.36  ? 64  PHE G CD1 1 
ATOM   7158  C  CD2 . PHE G  1 65  ? -11.988 -43.049 61.498 1.00 20.16  ? 64  PHE G CD2 1 
ATOM   7159  C  CE1 . PHE G  1 65  ? -9.765  -44.128 62.746 1.00 20.49  ? 64  PHE G CE1 1 
ATOM   7160  C  CE2 . PHE G  1 65  ? -11.564 -42.560 62.729 1.00 19.57  ? 64  PHE G CE2 1 
ATOM   7161  C  CZ  . PHE G  1 65  ? -10.454 -43.099 63.344 1.00 19.75  ? 64  PHE G CZ  1 
ATOM   7162  N  N   . ASN G  1 66  ? -11.878 -47.684 61.304 1.00 22.47  ? 65  ASN G N   1 
ATOM   7163  C  CA  . ASN G  1 66  ? -12.605 -48.603 62.158 1.00 26.07  ? 65  ASN G CA  1 
ATOM   7164  C  C   . ASN G  1 66  ? -11.979 -48.670 63.550 1.00 26.47  ? 65  ASN G C   1 
ATOM   7165  O  O   . ASN G  1 66  ? -11.651 -49.757 64.022 1.00 26.58  ? 65  ASN G O   1 
ATOM   7166  C  CB  . ASN G  1 66  ? -12.742 -49.979 61.487 1.00 25.85  ? 65  ASN G CB  1 
ATOM   7167  C  CG  . ASN G  1 66  ? -13.604 -50.937 62.280 1.00 26.25  ? 65  ASN G CG  1 
ATOM   7168  O  OD1 . ASN G  1 66  ? -14.405 -50.523 63.126 1.00 28.62  ? 65  ASN G OD1 1 
ATOM   7169  N  ND2 . ASN G  1 66  ? -13.447 -52.217 62.024 1.00 24.68  ? 65  ASN G ND2 1 
ATOM   7170  N  N   . PRO G  1 67  ? -11.853 -47.551 64.301 1.00 26.68  ? 66  PRO G N   1 
ATOM   7171  C  CA  . PRO G  1 67  ? -11.126 -47.579 65.569 1.00 27.60  ? 66  PRO G CA  1 
ATOM   7172  C  C   . PRO G  1 67  ? -11.738 -48.476 66.640 1.00 30.87  ? 66  PRO G C   1 
ATOM   7173  O  O   . PRO G  1 67  ? -11.055 -48.863 67.590 1.00 31.80  ? 66  PRO G O   1 
ATOM   7174  C  CB  . PRO G  1 67  ? -11.165 -46.129 66.070 1.00 27.69  ? 66  PRO G CB  1 
ATOM   7175  C  CG  . PRO G  1 67  ? -12.330 -45.488 65.334 1.00 28.21  ? 66  PRO G CG  1 
ATOM   7176  C  CD  . PRO G  1 67  ? -12.441 -46.231 64.005 1.00 28.33  ? 66  PRO G CD  1 
ATOM   7177  N  N   . LEU G  1 68  ? -13.032 -48.816 66.498 1.00 35.44  ? 67  LEU G N   1 
ATOM   7178  C  CA  . LEU G  1 68  ? -13.721 -49.565 67.537 1.00 34.71  ? 67  LEU G CA  1 
ATOM   7179  C  C   . LEU G  1 68  ? -13.869 -51.040 67.159 1.00 35.15  ? 67  LEU G C   1 
ATOM   7180  O  O   . LEU G  1 68  ? -14.535 -51.785 67.872 1.00 33.13  ? 67  LEU G O   1 
ATOM   7181  C  CB  . LEU G  1 68  ? -15.082 -48.915 67.802 1.00 33.75  ? 67  LEU G CB  1 
ATOM   7182  C  CG  . LEU G  1 68  ? -15.049 -47.546 68.490 1.00 33.09  ? 67  LEU G CG  1 
ATOM   7183  C  CD1 . LEU G  1 68  ? -16.445 -47.063 68.826 1.00 33.88  ? 67  LEU G CD1 1 
ATOM   7184  C  CD2 . LEU G  1 68  ? -14.183 -47.568 69.741 1.00 32.50  ? 67  LEU G CD2 1 
ATOM   7185  N  N   . SER G  1 69  ? -13.269 -51.450 66.035 1.00 36.53  ? 68  SER G N   1 
ATOM   7186  C  CA  . SER G  1 69  ? -13.241 -52.840 65.588 1.00 37.78  ? 68  SER G CA  1 
ATOM   7187  C  C   . SER G  1 69  ? -14.639 -53.439 65.467 1.00 35.37  ? 68  SER G C   1 
ATOM   7188  O  O   . SER G  1 69  ? -14.887 -54.492 66.030 1.00 34.49  ? 68  SER G O   1 
ATOM   7189  C  CB  . SER G  1 69  ? -12.400 -53.686 66.495 1.00 40.78  ? 68  SER G CB  1 
ATOM   7190  O  OG  . SER G  1 69  ? -11.045 -53.299 66.400 1.00 38.85  ? 68  SER G OG  1 
ATOM   7191  N  N   . ARG G  1 70  ? -15.530 -52.778 64.729 1.00 35.31  ? 69  ARG G N   1 
ATOM   7192  C  CA  . ARG G  1 70  ? -16.880 -53.279 64.504 1.00 32.31  ? 69  ARG G CA  1 
ATOM   7193  C  C   . ARG G  1 70  ? -17.010 -53.717 63.046 1.00 29.69  ? 69  ARG G C   1 
ATOM   7194  O  O   . ARG G  1 70  ? -16.094 -53.517 62.247 1.00 28.97  ? 69  ARG G O   1 
ATOM   7195  C  CB  . ARG G  1 70  ? -17.924 -52.199 64.820 1.00 35.56  ? 69  ARG G CB  1 
ATOM   7196  C  CG  . ARG G  1 70  ? -17.778 -51.557 66.185 1.00 39.46  ? 69  ARG G CG  1 
ATOM   7197  C  CD  . ARG G  1 70  ? -18.565 -52.213 67.302 1.00 44.11  ? 69  ARG G CD  1 
ATOM   7198  N  NE  . ARG G  1 70  ? -18.612 -51.286 68.434 1.00 55.27  ? 69  ARG G NE  1 
ATOM   7199  C  CZ  . ARG G  1 70  ? -19.516 -50.301 68.596 1.00 61.34  ? 69  ARG G CZ  1 
ATOM   7200  N  NH1 . ARG G  1 70  ? -20.466 -50.091 67.692 1.00 77.11  ? 69  ARG G NH1 1 
ATOM   7201  N  NH2 . ARG G  1 70  ? -19.471 -49.522 69.663 1.00 55.55  ? 69  ARG G NH2 1 
ATOM   7202  N  N   . LYS G  1 71  ? -18.162 -54.318 62.725 1.00 29.79  ? 70  LYS G N   1 
ATOM   7203  C  CA  . LYS G  1 71  ? -18.471 -54.724 61.367 1.00 30.62  ? 70  LYS G CA  1 
ATOM   7204  C  C   . LYS G  1 71  ? -19.084 -53.542 60.618 1.00 26.66  ? 70  LYS G C   1 
ATOM   7205  O  O   . LYS G  1 71  ? -19.561 -52.590 61.232 1.00 22.15  ? 70  LYS G O   1 
ATOM   7206  C  CB  . LYS G  1 71  ? -19.308 -56.019 61.359 1.00 35.40  ? 70  LYS G CB  1 
ATOM   7207  C  CG  . LYS G  1 71  ? -18.715 -57.186 62.150 1.00 43.93  ? 70  LYS G CG  1 
ATOM   7208  C  CD  . LYS G  1 71  ? -18.580 -58.590 61.476 1.00 53.61  ? 70  LYS G CD  1 
ATOM   7209  C  CE  . LYS G  1 71  ? -17.188 -59.181 61.663 1.00 57.59  ? 70  LYS G CE  1 
ATOM   7210  N  NZ  . LYS G  1 71  ? -16.722 -59.957 60.486 1.00 56.23  ? 70  LYS G NZ  1 
ATOM   7211  N  N   . HIS G  1 72  ? -19.039 -53.605 59.280 1.00 25.50  ? 71  HIS G N   1 
ATOM   7212  C  CA  . HIS G  1 72  ? -19.513 -52.525 58.433 1.00 25.87  ? 71  HIS G CA  1 
ATOM   7213  C  C   . HIS G  1 72  ? -21.030 -52.388 58.538 1.00 27.90  ? 71  HIS G C   1 
ATOM   7214  O  O   . HIS G  1 72  ? -21.743 -53.385 58.586 1.00 28.31  ? 71  HIS G O   1 
ATOM   7215  C  CB  . HIS G  1 72  ? -19.054 -52.769 56.995 1.00 25.16  ? 71  HIS G CB  1 
ATOM   7216  C  CG  . HIS G  1 72  ? -19.587 -51.774 56.022 1.00 25.50  ? 71  HIS G CG  1 
ATOM   7217  N  ND1 . HIS G  1 72  ? -18.988 -50.544 55.789 1.00 25.95  ? 71  HIS G ND1 1 
ATOM   7218  C  CD2 . HIS G  1 72  ? -20.670 -51.834 55.220 1.00 25.63  ? 71  HIS G CD2 1 
ATOM   7219  C  CE1 . HIS G  1 72  ? -19.685 -49.890 54.890 1.00 26.11  ? 71  HIS G CE1 1 
ATOM   7220  N  NE2 . HIS G  1 72  ? -20.726 -50.659 54.528 1.00 26.22  ? 71  HIS G NE2 1 
ATOM   7221  N  N   . GLY G  1 73  ? -21.518 -51.141 58.579 1.00 30.50  ? 72  GLY G N   1 
ATOM   7222  C  CA  . GLY G  1 73  ? -22.947 -50.864 58.580 1.00 30.54  ? 72  GLY G CA  1 
ATOM   7223  C  C   . GLY G  1 73  ? -23.280 -49.639 57.728 1.00 31.35  ? 72  GLY G C   1 
ATOM   7224  O  O   . GLY G  1 73  ? -22.394 -49.067 57.094 1.00 30.95  ? 72  GLY G O   1 
ATOM   7225  N  N   . GLY G  1 74  ? -24.570 -49.279 57.687 1.00 31.13  ? 73  GLY G N   1 
ATOM   7226  C  CA  . GLY G  1 74  ? -25.011 -47.978 57.211 1.00 29.78  ? 73  GLY G CA  1 
ATOM   7227  C  C   . GLY G  1 74  ? -24.836 -46.935 58.318 1.00 28.01  ? 73  GLY G C   1 
ATOM   7228  O  O   . GLY G  1 74  ? -24.697 -47.294 59.492 1.00 29.39  ? 73  GLY G O   1 
ATOM   7229  N  N   . PRO G  1 75  ? -24.804 -45.620 57.996 1.00 25.15  ? 74  PRO G N   1 
ATOM   7230  C  CA  . PRO G  1 75  ? -24.519 -44.597 58.998 1.00 26.06  ? 74  PRO G CA  1 
ATOM   7231  C  C   . PRO G  1 75  ? -25.471 -44.657 60.187 1.00 28.10  ? 74  PRO G C   1 
ATOM   7232  O  O   . PRO G  1 75  ? -25.091 -44.298 61.305 1.00 25.77  ? 74  PRO G O   1 
ATOM   7233  C  CB  . PRO G  1 75  ? -24.665 -43.263 58.252 1.00 25.11  ? 74  PRO G CB  1 
ATOM   7234  C  CG  . PRO G  1 75  ? -25.337 -43.615 56.940 1.00 24.21  ? 74  PRO G CG  1 
ATOM   7235  C  CD  . PRO G  1 75  ? -24.983 -45.055 56.653 1.00 24.66  ? 74  PRO G CD  1 
ATOM   7236  N  N   . LYS G  1 76  ? -26.707 -45.143 59.948 1.00 29.50  ? 75  LYS G N   1 
ATOM   7237  C  CA  . LYS G  1 76  ? -27.714 -45.098 61.000 1.00 29.91  ? 75  LYS G CA  1 
ATOM   7238  C  C   . LYS G  1 76  ? -27.650 -46.316 61.917 1.00 32.61  ? 75  LYS G C   1 
ATOM   7239  O  O   . LYS G  1 76  ? -28.308 -46.311 62.948 1.00 35.02  ? 75  LYS G O   1 
ATOM   7240  C  CB  . LYS G  1 76  ? -29.099 -44.752 60.466 1.00 29.67  ? 75  LYS G CB  1 
ATOM   7241  C  CG  . LYS G  1 76  ? -29.291 -43.250 60.260 1.00 30.25  ? 75  LYS G CG  1 
ATOM   7242  C  CD  . LYS G  1 76  ? -28.588 -42.362 61.266 1.00 27.27  ? 75  LYS G CD  1 
ATOM   7243  C  CE  . LYS G  1 76  ? -28.932 -40.914 60.970 1.00 30.31  ? 75  LYS G CE  1 
ATOM   7244  N  NZ  . LYS G  1 76  ? -27.869 -39.984 61.402 1.00 29.17  ? 75  LYS G NZ  1 
ATOM   7245  N  N   . ASP G  1 77  ? -26.842 -47.318 61.564 1.00 35.81  ? 76  ASP G N   1 
ATOM   7246  C  CA  . ASP G  1 77  ? -26.717 -48.563 62.328 1.00 37.81  ? 76  ASP G CA  1 
ATOM   7247  C  C   . ASP G  1 77  ? -25.866 -48.339 63.576 1.00 38.36  ? 76  ASP G C   1 
ATOM   7248  O  O   . ASP G  1 77  ? -24.985 -47.483 63.598 1.00 39.69  ? 76  ASP G O   1 
ATOM   7249  C  CB  . ASP G  1 77  ? -26.117 -49.691 61.481 1.00 39.78  ? 76  ASP G CB  1 
ATOM   7250  C  CG  . ASP G  1 77  ? -27.085 -50.160 60.394 1.00 42.77  ? 76  ASP G CG  1 
ATOM   7251  O  OD1 . ASP G  1 77  ? -28.313 -50.099 60.638 1.00 50.34  ? 76  ASP G OD1 1 
ATOM   7252  O  OD2 . ASP G  1 77  ? -26.619 -50.559 59.301 1.00 37.85  ? 76  ASP G OD2 1 
ATOM   7253  N  N   . GLU G  1 78  ? -26.148 -49.098 64.635 1.00 41.37  ? 77  GLU G N   1 
ATOM   7254  C  CA  . GLU G  1 78  ? -25.296 -49.028 65.809 1.00 47.25  ? 77  GLU G CA  1 
ATOM   7255  C  C   . GLU G  1 78  ? -24.004 -49.785 65.519 1.00 44.78  ? 77  GLU G C   1 
ATOM   7256  O  O   . GLU G  1 78  ? -22.926 -49.357 65.920 1.00 45.80  ? 77  GLU G O   1 
ATOM   7257  C  CB  . GLU G  1 78  ? -26.046 -49.522 67.050 1.00 58.55  ? 77  GLU G CB  1 
ATOM   7258  C  CG  . GLU G  1 78  ? -27.519 -49.131 67.061 1.00 73.23  ? 77  GLU G CG  1 
ATOM   7259  C  CD  . GLU G  1 78  ? -28.505 -50.033 66.321 1.00 82.23  ? 77  GLU G CD  1 
ATOM   7260  O  OE1 . GLU G  1 78  ? -28.167 -50.574 65.232 1.00 83.01  ? 77  GLU G OE1 1 
ATOM   7261  O  OE2 . GLU G  1 78  ? -29.612 -50.186 66.836 1.00 86.97  ? 77  GLU G OE2 1 
ATOM   7262  N  N   . GLU G  1 79  ? -24.124 -50.895 64.775 1.00 41.40  ? 78  GLU G N   1 
ATOM   7263  C  CA  . GLU G  1 79  ? -22.976 -51.667 64.324 1.00 38.32  ? 78  GLU G CA  1 
ATOM   7264  C  C   . GLU G  1 79  ? -22.489 -51.074 62.996 1.00 33.97  ? 78  GLU G C   1 
ATOM   7265  O  O   . GLU G  1 79  ? -22.998 -51.401 61.920 1.00 32.50  ? 78  GLU G O   1 
ATOM   7266  C  CB  . GLU G  1 79  ? -23.350 -53.157 64.309 1.00 44.26  ? 78  GLU G CB  1 
ATOM   7267  C  CG  . GLU G  1 79  ? -22.212 -54.129 64.014 1.00 49.21  ? 78  GLU G CG  1 
ATOM   7268  C  CD  . GLU G  1 79  ? -21.116 -54.316 65.063 1.00 53.38  ? 78  GLU G CD  1 
ATOM   7269  O  OE1 . GLU G  1 79  ? -21.239 -53.759 66.184 1.00 55.53  ? 78  GLU G OE1 1 
ATOM   7270  O  OE2 . GLU G  1 79  ? -20.123 -55.025 64.755 1.00 51.06  ? 78  GLU G OE2 1 
ATOM   7271  N  N   . ARG G  1 80  ? -21.492 -50.181 63.097 1.00 28.98  ? 79  ARG G N   1 
ATOM   7272  C  CA  . ARG G  1 80  ? -20.860 -49.577 61.932 1.00 26.66  ? 79  ARG G CA  1 
ATOM   7273  C  C   . ARG G  1 80  ? -19.401 -49.231 62.225 1.00 24.37  ? 79  ARG G C   1 
ATOM   7274  O  O   . ARG G  1 80  ? -18.987 -49.111 63.382 1.00 21.61  ? 79  ARG G O   1 
ATOM   7275  C  CB  . ARG G  1 80  ? -21.576 -48.285 61.528 1.00 27.22  ? 79  ARG G CB  1 
ATOM   7276  C  CG  . ARG G  1 80  ? -21.642 -47.236 62.633 1.00 25.43  ? 79  ARG G CG  1 
ATOM   7277  C  CD  . ARG G  1 80  ? -22.202 -45.939 62.076 1.00 24.62  ? 79  ARG G CD  1 
ATOM   7278  N  NE  . ARG G  1 80  ? -21.157 -45.060 61.570 1.00 25.13  ? 79  ARG G NE  1 
ATOM   7279  C  CZ  . ARG G  1 80  ? -21.315 -43.761 61.275 1.00 26.09  ? 79  ARG G CZ  1 
ATOM   7280  N  NH1 . ARG G  1 80  ? -22.490 -43.184 61.426 1.00 26.38  ? 79  ARG G NH1 1 
ATOM   7281  N  NH2 . ARG G  1 80  ? -20.299 -43.040 60.831 1.00 25.09  ? 79  ARG G NH2 1 
ATOM   7282  N  N   . HIS G  1 81  ? -18.633 -49.079 61.138 1.00 23.43  ? 80  HIS G N   1 
ATOM   7283  C  CA  . HIS G  1 81  ? -17.337 -48.428 61.177 1.00 21.68  ? 80  HIS G CA  1 
ATOM   7284  C  C   . HIS G  1 81  ? -17.565 -46.932 61.395 1.00 21.64  ? 80  HIS G C   1 
ATOM   7285  O  O   . HIS G  1 81  ? -18.541 -46.369 60.889 1.00 22.80  ? 80  HIS G O   1 
ATOM   7286  C  CB  . HIS G  1 81  ? -16.629 -48.630 59.837 1.00 20.69  ? 80  HIS G CB  1 
ATOM   7287  C  CG  . HIS G  1 81  ? -16.396 -50.058 59.491 1.00 20.49  ? 80  HIS G CG  1 
ATOM   7288  N  ND1 . HIS G  1 81  ? -16.442 -50.532 58.188 1.00 20.44  ? 80  HIS G ND1 1 
ATOM   7289  C  CD2 . HIS G  1 81  ? -16.094 -51.119 60.265 1.00 20.58  ? 80  HIS G CD2 1 
ATOM   7290  C  CE1 . HIS G  1 81  ? -16.169 -51.822 58.183 1.00 19.90  ? 80  HIS G CE1 1 
ATOM   7291  N  NE2 . HIS G  1 81  ? -15.966 -52.207 59.435 1.00 20.34  ? 80  HIS G NE2 1 
ATOM   7292  N  N   . VAL G  1 82  ? -16.652 -46.285 62.128 1.00 19.87  ? 81  VAL G N   1 
ATOM   7293  C  CA  . VAL G  1 82  ? -16.727 -44.840 62.284 1.00 18.12  ? 81  VAL G CA  1 
ATOM   7294  C  C   . VAL G  1 82  ? -16.783 -44.183 60.903 1.00 17.59  ? 81  VAL G C   1 
ATOM   7295  O  O   . VAL G  1 82  ? -17.520 -43.227 60.707 1.00 18.74  ? 81  VAL G O   1 
ATOM   7296  C  CB  . VAL G  1 82  ? -15.588 -44.277 63.152 1.00 17.23  ? 81  VAL G CB  1 
ATOM   7297  C  CG1 . VAL G  1 82  ? -15.486 -42.754 63.018 1.00 17.62  ? 81  VAL G CG1 1 
ATOM   7298  C  CG2 . VAL G  1 82  ? -15.770 -44.649 64.611 1.00 17.35  ? 81  VAL G CG2 1 
ATOM   7299  N  N   . GLY G  1 83  ? -16.045 -44.723 59.936 1.00 17.08  ? 82  GLY G N   1 
ATOM   7300  C  CA  . GLY G  1 83  ? -15.949 -44.090 58.631 1.00 17.40  ? 82  GLY G CA  1 
ATOM   7301  C  C   . GLY G  1 83  ? -17.139 -44.371 57.713 1.00 18.71  ? 82  GLY G C   1 
ATOM   7302  O  O   . GLY G  1 83  ? -17.125 -43.915 56.567 1.00 18.39  ? 82  GLY G O   1 
ATOM   7303  N  N   . ASP G  1 84  ? -18.158 -45.087 58.230 1.00 20.07  ? 83  ASP G N   1 
ATOM   7304  C  CA  . ASP G  1 84  ? -19.270 -45.565 57.419 1.00 20.88  ? 83  ASP G CA  1 
ATOM   7305  C  C   . ASP G  1 84  ? -20.307 -44.448 57.218 1.00 21.62  ? 83  ASP G C   1 
ATOM   7306  O  O   . ASP G  1 84  ? -21.178 -44.230 58.061 1.00 20.85  ? 83  ASP G O   1 
ATOM   7307  C  CB  . ASP G  1 84  ? -19.883 -46.829 58.027 1.00 20.83  ? 83  ASP G CB  1 
ATOM   7308  C  CG  . ASP G  1 84  ? -19.060 -48.090 57.810 1.00 21.87  ? 83  ASP G CG  1 
ATOM   7309  O  OD1 . ASP G  1 84  ? -18.157 -48.080 56.934 1.00 22.71  ? 83  ASP G OD1 1 
ATOM   7310  O  OD2 . ASP G  1 84  ? -19.326 -49.091 58.515 1.00 21.64  ? 83  ASP G OD2 1 
ATOM   7311  N  N   . LEU G  1 85  ? -20.235 -43.761 56.071 1.00 21.55  ? 84  LEU G N   1 
ATOM   7312  C  CA  . LEU G  1 85  ? -21.106 -42.627 55.821 1.00 22.13  ? 84  LEU G CA  1 
ATOM   7313  C  C   . LEU G  1 85  ? -22.194 -42.975 54.809 1.00 23.73  ? 84  LEU G C   1 
ATOM   7314  O  O   . LEU G  1 85  ? -22.896 -42.079 54.331 1.00 27.78  ? 84  LEU G O   1 
ATOM   7315  C  CB  . LEU G  1 85  ? -20.275 -41.429 55.342 1.00 21.68  ? 84  LEU G CB  1 
ATOM   7316  C  CG  . LEU G  1 85  ? -19.416 -40.737 56.402 1.00 21.57  ? 84  LEU G CG  1 
ATOM   7317  C  CD1 . LEU G  1 85  ? -18.777 -39.486 55.815 1.00 20.11  ? 84  LEU G CD1 1 
ATOM   7318  C  CD2 . LEU G  1 85  ? -20.247 -40.357 57.626 1.00 20.93  ? 84  LEU G CD2 1 
ATOM   7319  N  N   . GLY G  1 86  ? -22.339 -44.260 54.474 1.00 22.50  ? 85  GLY G N   1 
ATOM   7320  C  CA  . GLY G  1 86  ? -23.436 -44.681 53.611 1.00 23.06  ? 85  GLY G CA  1 
ATOM   7321  C  C   . GLY G  1 86  ? -23.185 -44.352 52.136 1.00 24.46  ? 85  GLY G C   1 
ATOM   7322  O  O   . GLY G  1 86  ? -22.065 -44.530 51.636 1.00 25.94  ? 85  GLY G O   1 
ATOM   7323  N  N   . ASN G  1 87  ? -24.241 -43.877 51.450 1.00 24.10  ? 86  ASN G N   1 
ATOM   7324  C  CA  . ASN G  1 87  ? -24.162 -43.615 50.020 1.00 24.51  ? 86  ASN G CA  1 
ATOM   7325  C  C   . ASN G  1 87  ? -24.366 -42.134 49.710 1.00 25.53  ? 86  ASN G C   1 
ATOM   7326  O  O   . ASN G  1 87  ? -24.951 -41.376 50.489 1.00 26.91  ? 86  ASN G O   1 
ATOM   7327  C  CB  . ASN G  1 87  ? -25.193 -44.410 49.227 1.00 25.60  ? 86  ASN G CB  1 
ATOM   7328  C  CG  . ASN G  1 87  ? -24.914 -45.892 49.257 1.00 26.83  ? 86  ASN G CG  1 
ATOM   7329  O  OD1 . ASN G  1 87  ? -24.003 -46.379 48.592 1.00 29.31  ? 86  ASN G OD1 1 
ATOM   7330  N  ND2 . ASN G  1 87  ? -25.676 -46.613 50.058 1.00 25.92  ? 86  ASN G ND2 1 
ATOM   7331  N  N   . VAL G  1 88  ? -23.855 -41.743 48.542 1.00 24.26  ? 87  VAL G N   1 
ATOM   7332  C  CA  . VAL G  1 88  ? -24.210 -40.480 47.927 1.00 23.64  ? 87  VAL G CA  1 
ATOM   7333  C  C   . VAL G  1 88  ? -24.870 -40.819 46.592 1.00 24.30  ? 87  VAL G C   1 
ATOM   7334  O  O   . VAL G  1 88  ? -24.671 -41.915 46.062 1.00 25.46  ? 87  VAL G O   1 
ATOM   7335  C  CB  . VAL G  1 88  ? -22.992 -39.540 47.794 1.00 22.15  ? 87  VAL G CB  1 
ATOM   7336  C  CG1 . VAL G  1 88  ? -22.353 -39.233 49.154 1.00 19.87  ? 87  VAL G CG1 1 
ATOM   7337  C  CG2 . VAL G  1 88  ? -21.957 -40.065 46.804 1.00 20.98  ? 87  VAL G CG2 1 
ATOM   7338  N  N   . THR G  1 89  ? -25.701 -39.904 46.082 1.00 24.20  ? 88  THR G N   1 
ATOM   7339  C  CA  . THR G  1 89  ? -26.481 -40.215 44.895 1.00 24.76  ? 88  THR G CA  1 
ATOM   7340  C  C   . THR G  1 89  ? -26.088 -39.282 43.759 1.00 26.23  ? 88  THR G C   1 
ATOM   7341  O  O   . THR G  1 89  ? -26.164 -38.065 43.900 1.00 27.50  ? 88  THR G O   1 
ATOM   7342  C  CB  . THR G  1 89  ? -27.982 -40.068 45.158 1.00 25.06  ? 88  THR G CB  1 
ATOM   7343  O  OG1 . THR G  1 89  ? -28.350 -40.841 46.305 1.00 25.23  ? 88  THR G OG1 1 
ATOM   7344  C  CG2 . THR G  1 89  ? -28.807 -40.471 43.955 1.00 25.26  ? 88  THR G CG2 1 
ATOM   7345  N  N   . ALA G  1 90  ? -25.705 -39.866 42.623 1.00 28.08  ? 89  ALA G N   1 
ATOM   7346  C  CA  . ALA G  1 90  ? -25.420 -39.083 41.433 1.00 28.66  ? 89  ALA G CA  1 
ATOM   7347  C  C   . ALA G  1 90  ? -26.657 -39.020 40.541 1.00 31.16  ? 89  ALA G C   1 
ATOM   7348  O  O   . ALA G  1 90  ? -27.291 -40.048 40.277 1.00 32.89  ? 89  ALA G O   1 
ATOM   7349  C  CB  . ALA G  1 90  ? -24.236 -39.675 40.704 1.00 30.49  ? 89  ALA G CB  1 
ATOM   7350  N  N   . ASP G  1 91  ? -26.961 -37.800 40.060 1.00 32.94  ? 90  ASP G N   1 
ATOM   7351  C  CA  . ASP G  1 91  ? -28.074 -37.529 39.160 1.00 33.27  ? 90  ASP G CA  1 
ATOM   7352  C  C   . ASP G  1 91  ? -27.715 -37.981 37.744 1.00 33.93  ? 90  ASP G C   1 
ATOM   7353  O  O   . ASP G  1 91  ? -26.622 -38.494 37.521 1.00 31.33  ? 90  ASP G O   1 
ATOM   7354  C  CB  . ASP G  1 91  ? -28.484 -36.053 39.218 1.00 33.75  ? 90  ASP G CB  1 
ATOM   7355  C  CG  . ASP G  1 91  ? -27.440 -35.055 38.728 1.00 34.67  ? 90  ASP G CG  1 
ATOM   7356  O  OD1 . ASP G  1 91  ? -26.530 -35.443 37.954 1.00 32.94  ? 90  ASP G OD1 1 
ATOM   7357  O  OD2 . ASP G  1 91  ? -27.551 -33.882 39.128 1.00 36.08  ? 90  ASP G OD2 1 
ATOM   7358  N  N   . LYS G  1 92  ? -28.637 -37.771 36.792 1.00 38.03  ? 91  LYS G N   1 
ATOM   7359  C  CA  . LYS G  1 92  ? -28.470 -38.269 35.427 1.00 41.88  ? 91  LYS G CA  1 
ATOM   7360  C  C   . LYS G  1 92  ? -27.233 -37.657 34.768 1.00 42.45  ? 91  LYS G C   1 
ATOM   7361  O  O   . LYS G  1 92  ? -26.763 -38.177 33.766 1.00 41.35  ? 91  LYS G O   1 
ATOM   7362  C  CB  . LYS G  1 92  ? -29.722 -38.063 34.563 1.00 43.04  ? 91  LYS G CB  1 
ATOM   7363  C  CG  . LYS G  1 92  ? -30.102 -36.621 34.234 1.00 45.11  ? 91  LYS G CG  1 
ATOM   7364  C  CD  . LYS G  1 92  ? -30.890 -36.464 32.934 0.40 43.26  ? 91  LYS G CD  1 
ATOM   7365  C  CE  . LYS G  1 92  ? -30.522 -35.230 32.138 0.40 40.46  ? 91  LYS G CE  1 
ATOM   7366  N  NZ  . LYS G  1 92  ? -31.733 -34.587 31.595 0.40 40.33  ? 91  LYS G NZ  1 
ATOM   7367  N  N   . ASP G  1 93  ? -26.721 -36.555 35.330 1.00 44.57  ? 92  ASP G N   1 
ATOM   7368  C  CA  . ASP G  1 93  ? -25.588 -35.835 34.763 1.00 45.32  ? 92  ASP G CA  1 
ATOM   7369  C  C   . ASP G  1 93  ? -24.282 -36.283 35.413 1.00 44.12  ? 92  ASP G C   1 
ATOM   7370  O  O   . ASP G  1 93  ? -23.219 -35.791 35.059 1.00 46.85  ? 92  ASP G O   1 
ATOM   7371  C  CB  . ASP G  1 93  ? -25.729 -34.327 34.960 1.00 49.63  ? 92  ASP G CB  1 
ATOM   7372  C  CG  . ASP G  1 93  ? -26.904 -33.742 34.207 1.00 54.09  ? 92  ASP G CG  1 
ATOM   7373  O  OD1 . ASP G  1 93  ? -27.087 -34.133 33.024 1.00 53.09  ? 92  ASP G OD1 1 
ATOM   7374  O  OD2 . ASP G  1 93  ? -27.620 -32.896 34.806 1.00 58.06  ? 92  ASP G OD2 1 
ATOM   7375  N  N   . GLY G  1 94  ? -24.369 -37.197 36.380 1.00 44.21  ? 93  GLY G N   1 
ATOM   7376  C  CA  . GLY G  1 94  ? -23.180 -37.715 37.036 1.00 42.14  ? 93  GLY G CA  1 
ATOM   7377  C  C   . GLY G  1 94  ? -22.692 -36.793 38.152 1.00 38.53  ? 93  GLY G C   1 
ATOM   7378  O  O   . GLY G  1 94  ? -21.520 -36.843 38.531 1.00 41.69  ? 93  GLY G O   1 
ATOM   7379  N  N   . VAL G  1 95  ? -23.607 -35.970 38.679 1.00 32.03  ? 94  VAL G N   1 
ATOM   7380  C  CA  . VAL G  1 95  ? -23.257 -35.076 39.768 1.00 28.11  ? 94  VAL G CA  1 
ATOM   7381  C  C   . VAL G  1 95  ? -23.965 -35.522 41.043 1.00 26.77  ? 94  VAL G C   1 
ATOM   7382  O  O   . VAL G  1 95  ? -25.181 -35.699 41.054 1.00 25.15  ? 94  VAL G O   1 
ATOM   7383  C  CB  . VAL G  1 95  ? -23.579 -33.608 39.431 1.00 25.23  ? 94  VAL G CB  1 
ATOM   7384  C  CG1 . VAL G  1 95  ? -23.312 -32.682 40.621 1.00 23.54  ? 94  VAL G CG1 1 
ATOM   7385  C  CG2 . VAL G  1 95  ? -22.842 -33.152 38.185 1.00 23.79  ? 94  VAL G CG2 1 
ATOM   7386  N  N   . ALA G  1 96  ? -23.193 -35.677 42.122 1.00 26.30  ? 95  ALA G N   1 
ATOM   7387  C  CA  . ALA G  1 96  ? -23.779 -35.949 43.423 1.00 26.86  ? 95  ALA G CA  1 
ATOM   7388  C  C   . ALA G  1 96  ? -23.689 -34.695 44.278 1.00 27.82  ? 95  ALA G C   1 
ATOM   7389  O  O   . ALA G  1 96  ? -22.583 -34.237 44.580 1.00 32.77  ? 95  ALA G O   1 
ATOM   7390  C  CB  . ALA G  1 96  ? -23.051 -37.096 44.078 1.00 25.05  ? 95  ALA G CB  1 
ATOM   7391  N  N   . ASP G  1 97  ? -24.842 -34.141 44.672 1.00 28.62  ? 96  ASP G N   1 
ATOM   7392  C  CA  . ASP G  1 97  ? -24.829 -33.036 45.617 1.00 32.98  ? 96  ASP G CA  1 
ATOM   7393  C  C   . ASP G  1 97  ? -24.854 -33.610 47.021 1.00 29.88  ? 96  ASP G C   1 
ATOM   7394  O  O   . ASP G  1 97  ? -25.909 -33.936 47.535 1.00 32.05  ? 96  ASP G O   1 
ATOM   7395  C  CB  . ASP G  1 97  ? -25.913 -31.984 45.358 1.00 38.85  ? 96  ASP G CB  1 
ATOM   7396  C  CG  . ASP G  1 97  ? -25.671 -31.228 44.043 1.00 48.60  ? 96  ASP G CG  1 
ATOM   7397  O  OD1 . ASP G  1 97  ? -24.542 -30.726 43.820 1.00 46.34  ? 96  ASP G OD1 1 
ATOM   7398  O  OD2 . ASP G  1 97  ? -26.592 -31.184 43.204 1.00 51.24  ? 96  ASP G OD2 1 
ATOM   7399  N  N   . VAL G  1 98  ? -23.671 -33.742 47.616 1.00 27.41  ? 97  VAL G N   1 
ATOM   7400  C  CA  . VAL G  1 98  ? -23.542 -34.394 48.903 1.00 26.38  ? 97  VAL G CA  1 
ATOM   7401  C  C   . VAL G  1 98  ? -24.034 -33.463 50.005 1.00 26.27  ? 97  VAL G C   1 
ATOM   7402  O  O   . VAL G  1 98  ? -23.705 -32.276 50.041 1.00 25.70  ? 97  VAL G O   1 
ATOM   7403  C  CB  . VAL G  1 98  ? -22.089 -34.821 49.158 1.00 24.90  ? 97  VAL G CB  1 
ATOM   7404  C  CG1 . VAL G  1 98  ? -21.949 -35.540 50.500 1.00 23.16  ? 97  VAL G CG1 1 
ATOM   7405  C  CG2 . VAL G  1 98  ? -21.572 -35.678 48.008 1.00 24.36  ? 97  VAL G CG2 1 
ATOM   7406  N  N   . SER G  1 99  ? -24.815 -34.041 50.917 1.00 25.57  ? 98  SER G N   1 
ATOM   7407  C  CA  . SER G  1 99  ? -25.251 -33.332 52.102 1.00 27.64  ? 98  SER G CA  1 
ATOM   7408  C  C   . SER G  1 99  ? -25.627 -34.359 53.166 1.00 30.57  ? 98  SER G C   1 
ATOM   7409  O  O   . SER G  1 99  ? -26.610 -35.091 53.016 1.00 35.69  ? 98  SER G O   1 
ATOM   7410  C  CB  . SER G  1 99  ? -26.401 -32.436 51.772 1.00 26.02  ? 98  SER G CB  1 
ATOM   7411  O  OG  . SER G  1 99  ? -26.905 -31.835 52.951 1.00 24.72  ? 98  SER G OG  1 
ATOM   7412  N  N   . ILE G  1 100 ? -24.810 -34.429 54.218 1.00 28.32  ? 99  ILE G N   1 
ATOM   7413  C  CA  . ILE G  1 100 ? -24.917 -35.481 55.214 1.00 28.52  ? 99  ILE G CA  1 
ATOM   7414  C  C   . ILE G  1 100 ? -24.724 -34.834 56.571 1.00 29.26  ? 99  ILE G C   1 
ATOM   7415  O  O   . ILE G  1 100 ? -23.995 -33.861 56.698 1.00 29.07  ? 99  ILE G O   1 
ATOM   7416  C  CB  . ILE G  1 100 ? -23.873 -36.595 54.980 1.00 26.37  ? 99  ILE G CB  1 
ATOM   7417  C  CG1 . ILE G  1 100 ? -24.268 -37.491 53.809 1.00 26.48  ? 99  ILE G CG1 1 
ATOM   7418  C  CG2 . ILE G  1 100 ? -23.574 -37.387 56.251 1.00 23.66  ? 99  ILE G CG2 1 
ATOM   7419  C  CD1 . ILE G  1 100 ? -23.204 -38.461 53.400 1.00 29.42  ? 99  ILE G CD1 1 
ATOM   7420  N  N   . GLU G  1 101 ? -25.363 -35.408 57.577 1.00 33.74  ? 100 GLU G N   1 
ATOM   7421  C  CA  . GLU G  1 101 ? -25.062 -35.025 58.938 1.00 35.26  ? 100 GLU G CA  1 
ATOM   7422  C  C   . GLU G  1 101 ? -24.777 -36.305 59.704 1.00 34.82  ? 100 GLU G C   1 
ATOM   7423  O  O   . GLU G  1 101 ? -25.519 -37.277 59.581 1.00 37.63  ? 100 GLU G O   1 
ATOM   7424  C  CB  . GLU G  1 101 ? -26.222 -34.209 59.489 1.00 39.72  ? 100 GLU G CB  1 
ATOM   7425  C  CG  . GLU G  1 101 ? -26.119 -33.938 60.960 1.00 50.61  ? 100 GLU G CG  1 
ATOM   7426  C  CD  . GLU G  1 101 ? -26.955 -32.729 61.390 1.00 58.18  ? 100 GLU G CD  1 
ATOM   7427  O  OE1 . GLU G  1 101 ? -27.598 -32.815 62.459 1.00 66.17  ? 100 GLU G OE1 1 
ATOM   7428  O  OE2 . GLU G  1 101 ? -27.000 -31.718 60.614 1.00 56.30  ? 100 GLU G OE2 1 
ATOM   7429  N  N   . ASP G  1 102 ? -23.654 -36.341 60.422 1.00 30.81  ? 101 ASP G N   1 
ATOM   7430  C  CA  . ASP G  1 102 ? -23.263 -37.576 61.079 1.00 29.84  ? 101 ASP G CA  1 
ATOM   7431  C  C   . ASP G  1 102 ? -22.773 -37.238 62.478 1.00 30.37  ? 101 ASP G C   1 
ATOM   7432  O  O   . ASP G  1 102 ? -22.130 -36.210 62.670 1.00 31.03  ? 101 ASP G O   1 
ATOM   7433  C  CB  . ASP G  1 102 ? -22.207 -38.349 60.299 1.00 27.97  ? 101 ASP G CB  1 
ATOM   7434  C  CG  . ASP G  1 102 ? -22.015 -39.763 60.824 1.00 29.53  ? 101 ASP G CG  1 
ATOM   7435  O  OD1 . ASP G  1 102 ? -22.912 -40.574 60.648 1.00 34.48  ? 101 ASP G OD1 1 
ATOM   7436  O  OD2 . ASP G  1 102 ? -20.983 -40.037 61.460 1.00 28.29  ? 101 ASP G OD2 1 
ATOM   7437  N  N   . SER G  1 103 ? -23.079 -38.111 63.444 1.00 32.23  ? 102 SER G N   1 
ATOM   7438  C  CA  . SER G  1 103 ? -22.718 -37.849 64.824 1.00 31.62  ? 102 SER G CA  1 
ATOM   7439  C  C   . SER G  1 103 ? -21.673 -38.833 65.329 1.00 31.12  ? 102 SER G C   1 
ATOM   7440  O  O   . SER G  1 103 ? -21.329 -38.803 66.509 1.00 30.77  ? 102 SER G O   1 
ATOM   7441  C  CB  . SER G  1 103 ? -23.931 -37.838 65.694 1.00 31.13  ? 102 SER G CB  1 
ATOM   7442  O  OG  . SER G  1 103 ? -24.471 -36.524 65.706 1.00 34.38  ? 102 SER G OG  1 
ATOM   7443  N  N   . VAL G  1 104 ? -21.147 -39.676 64.433 1.00 29.73  ? 103 VAL G N   1 
ATOM   7444  C  CA  . VAL G  1 104 ? -20.179 -40.675 64.844 1.00 27.06  ? 103 VAL G CA  1 
ATOM   7445  C  C   . VAL G  1 104 ? -18.785 -40.196 64.465 1.00 24.98  ? 103 VAL G C   1 
ATOM   7446  O  O   . VAL G  1 104 ? -17.872 -40.284 65.279 1.00 28.94  ? 103 VAL G O   1 
ATOM   7447  C  CB  . VAL G  1 104 ? -20.487 -42.075 64.283 1.00 26.80  ? 103 VAL G CB  1 
ATOM   7448  C  CG1 . VAL G  1 104 ? -19.352 -43.085 64.530 1.00 24.83  ? 103 VAL G CG1 1 
ATOM   7449  C  CG2 . VAL G  1 104 ? -21.805 -42.601 64.820 1.00 24.89  ? 103 VAL G CG2 1 
ATOM   7450  N  N   . ILE G  1 105 ? -18.625 -39.699 63.235 1.00 21.43  ? 104 ILE G N   1 
ATOM   7451  C  CA  . ILE G  1 105 ? -17.377 -39.054 62.875 1.00 20.49  ? 104 ILE G CA  1 
ATOM   7452  C  C   . ILE G  1 105 ? -17.257 -37.783 63.717 1.00 23.17  ? 104 ILE G C   1 
ATOM   7453  O  O   . ILE G  1 105 ? -18.254 -37.265 64.231 1.00 24.47  ? 104 ILE G O   1 
ATOM   7454  C  CB  . ILE G  1 105 ? -17.307 -38.730 61.369 1.00 17.87  ? 104 ILE G CB  1 
ATOM   7455  C  CG1 . ILE G  1 105 ? -18.369 -37.708 60.941 1.00 15.84  ? 104 ILE G CG1 1 
ATOM   7456  C  CG2 . ILE G  1 105 ? -17.356 -40.018 60.565 1.00 17.33  ? 104 ILE G CG2 1 
ATOM   7457  C  CD1 . ILE G  1 105 ? -18.136 -37.127 59.588 1.00 15.22  ? 104 ILE G CD1 1 
ATOM   7458  N  N   . SER G  1 106 ? -16.014 -37.311 63.881 1.00 24.94  ? 105 SER G N   1 
ATOM   7459  C  CA  . SER G  1 106 ? -15.773 -36.083 64.611 1.00 24.79  ? 105 SER G CA  1 
ATOM   7460  C  C   . SER G  1 106 ? -14.593 -35.342 63.994 1.00 26.18  ? 105 SER G C   1 
ATOM   7461  O  O   . SER G  1 106 ? -13.767 -35.939 63.298 1.00 26.61  ? 105 SER G O   1 
ATOM   7462  C  CB  . SER G  1 106 ? -15.526 -36.370 66.056 1.00 24.57  ? 105 SER G CB  1 
ATOM   7463  O  OG  . SER G  1 106 ? -15.611 -35.165 66.793 1.00 24.47  ? 105 SER G OG  1 
ATOM   7464  N  N   . LEU G  1 107 ? -14.538 -34.027 64.261 1.00 26.25  ? 106 LEU G N   1 
ATOM   7465  C  CA  . LEU G  1 107 ? -13.371 -33.246 63.881 1.00 25.93  ? 106 LEU G CA  1 
ATOM   7466  C  C   . LEU G  1 107 ? -12.519 -32.917 65.110 1.00 28.64  ? 106 LEU G C   1 
ATOM   7467  O  O   . LEU G  1 107 ? -11.611 -32.106 65.039 1.00 28.91  ? 106 LEU G O   1 
ATOM   7468  C  CB  . LEU G  1 107 ? -13.825 -31.983 63.154 1.00 23.92  ? 106 LEU G CB  1 
ATOM   7469  C  CG  . LEU G  1 107 ? -14.698 -32.211 61.922 1.00 23.71  ? 106 LEU G CG  1 
ATOM   7470  C  CD1 . LEU G  1 107 ? -14.969 -30.895 61.206 1.00 23.02  ? 106 LEU G CD1 1 
ATOM   7471  C  CD2 . LEU G  1 107 ? -14.059 -33.211 60.959 1.00 22.32  ? 106 LEU G CD2 1 
ATOM   7472  N  N   . SER G  1 108 ? -12.801 -33.567 66.245 1.00 34.34  ? 107 SER G N   1 
ATOM   7473  C  CA  . SER G  1 108 ? -11.934 -33.531 67.413 1.00 39.55  ? 107 SER G CA  1 
ATOM   7474  C  C   . SER G  1 108 ? -12.159 -34.777 68.266 1.00 46.31  ? 107 SER G C   1 
ATOM   7475  O  O   . SER G  1 108 ? -13.187 -35.439 68.159 1.00 54.06  ? 107 SER G O   1 
ATOM   7476  C  CB  . SER G  1 108 ? -12.127 -32.260 68.186 1.00 39.31  ? 107 SER G CB  1 
ATOM   7477  O  OG  . SER G  1 108 ? -13.451 -32.177 68.687 1.00 39.61  ? 107 SER G OG  1 
ATOM   7478  N  N   . GLY G  1 109 ? -11.161 -35.109 69.091 1.00 54.15  ? 108 GLY G N   1 
ATOM   7479  C  CA  . GLY G  1 109 ? -11.291 -36.196 70.051 1.00 60.01  ? 108 GLY G CA  1 
ATOM   7480  C  C   . GLY G  1 109 ? -10.982 -37.548 69.418 1.00 61.76  ? 108 GLY G C   1 
ATOM   7481  O  O   . GLY G  1 109 ? -10.294 -37.609 68.413 1.00 63.22  ? 108 GLY G O   1 
ATOM   7482  N  N   . ASP G  1 110 ? -11.584 -38.605 69.968 1.00 63.25  ? 109 ASP G N   1 
ATOM   7483  C  CA  . ASP G  1 110 ? -11.208 -39.967 69.670 1.00 60.75  ? 109 ASP G CA  1 
ATOM   7484  C  C   . ASP G  1 110 ? -11.510 -40.343 68.220 1.00 58.15  ? 109 ASP G C   1 
ATOM   7485  O  O   . ASP G  1 110 ? -10.872 -41.231 67.670 1.00 50.41  ? 109 ASP G O   1 
ATOM   7486  C  CB  . ASP G  1 110 ? -11.927 -40.939 70.618 1.00 69.94  ? 109 ASP G CB  1 
ATOM   7487  C  CG  . ASP G  1 110 ? -11.362 -42.339 70.534 1.00 84.29  ? 109 ASP G CG  1 
ATOM   7488  O  OD1 . ASP G  1 110 ? -10.132 -42.466 70.663 1.00 97.70  ? 109 ASP G OD1 1 
ATOM   7489  O  OD2 . ASP G  1 110 ? -12.154 -43.288 70.303 1.00 88.76  ? 109 ASP G OD2 1 
ATOM   7490  N  N   . HIS G  1 111 ? -12.506 -39.706 67.601 1.00 59.91  ? 110 HIS G N   1 
ATOM   7491  C  CA  . HIS G  1 111 ? -12.904 -40.181 66.291 1.00 53.99  ? 110 HIS G CA  1 
ATOM   7492  C  C   . HIS G  1 111 ? -12.537 -39.155 65.225 1.00 47.45  ? 110 HIS G C   1 
ATOM   7493  O  O   . HIS G  1 111 ? -13.225 -39.041 64.211 1.00 48.49  ? 110 HIS G O   1 
ATOM   7494  C  CB  . HIS G  1 111 ? -14.383 -40.593 66.297 1.00 58.56  ? 110 HIS G CB  1 
ATOM   7495  C  CG  . HIS G  1 111 ? -14.728 -41.646 67.305 1.00 66.93  ? 110 HIS G CG  1 
ATOM   7496  N  ND1 . HIS G  1 111 ? -16.002 -41.737 67.857 1.00 64.18  ? 110 HIS G ND1 1 
ATOM   7497  C  CD2 . HIS G  1 111 ? -13.995 -42.658 67.834 1.00 74.60  ? 110 HIS G CD2 1 
ATOM   7498  C  CE1 . HIS G  1 111 ? -16.034 -42.737 68.716 1.00 63.93  ? 110 HIS G CE1 1 
ATOM   7499  N  NE2 . HIS G  1 111 ? -14.822 -43.309 68.726 1.00 67.03  ? 110 HIS G NE2 1 
ATOM   7500  N  N   . CYS G  1 112 ? -11.430 -38.441 65.453 1.00 38.50  ? 111 CYS G N   1 
ATOM   7501  C  CA  . CYS G  1 112 ? -11.017 -37.400 64.529 1.00 34.13  ? 111 CYS G CA  1 
ATOM   7502  C  C   . CYS G  1 112 ? -10.694 -38.043 63.183 1.00 29.16  ? 111 CYS G C   1 
ATOM   7503  O  O   . CYS G  1 112 ? -10.030 -39.073 63.125 1.00 28.70  ? 111 CYS G O   1 
ATOM   7504  C  CB  . CYS G  1 112 ? -9.823  -36.665 65.108 1.00 39.12  ? 111 CYS G CB  1 
ATOM   7505  S  SG  . CYS G  1 112 ? -9.701  -34.929 64.615 1.00 58.47  ? 111 CYS G SG  1 
ATOM   7506  N  N   . ILE G  1 113 ? -11.254 -37.476 62.108 1.00 25.48  ? 112 ILE G N   1 
ATOM   7507  C  CA  . ILE G  1 113 ? -11.057 -37.989 60.759 1.00 25.40  ? 112 ILE G CA  1 
ATOM   7508  C  C   . ILE G  1 113 ? -10.028 -37.134 60.017 1.00 26.60  ? 112 ILE G C   1 
ATOM   7509  O  O   . ILE G  1 113 ? -9.733  -37.381 58.847 1.00 26.03  ? 112 ILE G O   1 
ATOM   7510  C  CB  . ILE G  1 113 ? -12.385 -38.055 59.978 1.00 25.42  ? 112 ILE G CB  1 
ATOM   7511  C  CG1 . ILE G  1 113 ? -13.122 -36.714 59.957 1.00 25.35  ? 112 ILE G CG1 1 
ATOM   7512  C  CG2 . ILE G  1 113 ? -13.263 -39.195 60.488 1.00 26.07  ? 112 ILE G CG2 1 
ATOM   7513  C  CD1 . ILE G  1 113 ? -14.069 -36.570 58.796 1.00 25.24  ? 112 ILE G CD1 1 
ATOM   7514  N  N   . ILE G  1 114 ? -9.497  -36.105 60.705 1.00 26.61  ? 113 ILE G N   1 
ATOM   7515  C  CA  . ILE G  1 114 ? -8.491  -35.241 60.114 1.00 24.32  ? 113 ILE G CA  1 
ATOM   7516  C  C   . ILE G  1 114 ? -7.258  -36.077 59.815 1.00 23.97  ? 113 ILE G C   1 
ATOM   7517  O  O   . ILE G  1 114 ? -6.826  -36.877 60.651 1.00 23.58  ? 113 ILE G O   1 
ATOM   7518  C  CB  . ILE G  1 114 ? -8.166  -34.060 61.030 1.00 23.58  ? 113 ILE G CB  1 
ATOM   7519  C  CG1 . ILE G  1 114 ? -9.444  -33.306 61.400 1.00 23.16  ? 113 ILE G CG1 1 
ATOM   7520  C  CG2 . ILE G  1 114 ? -7.120  -33.163 60.392 1.00 24.39  ? 113 ILE G CG2 1 
ATOM   7521  C  CD1 . ILE G  1 114 ? -9.223  -31.884 61.821 1.00 24.42  ? 113 ILE G CD1 1 
ATOM   7522  N  N   . GLY G  1 115 ? -6.739  -35.892 58.596 1.00 22.64  ? 114 GLY G N   1 
ATOM   7523  C  CA  . GLY G  1 115 ? -5.519  -36.549 58.169 1.00 23.33  ? 114 GLY G CA  1 
ATOM   7524  C  C   . GLY G  1 115 ? -5.768  -37.989 57.728 1.00 24.20  ? 114 GLY G C   1 
ATOM   7525  O  O   . GLY G  1 115 ? -4.813  -38.755 57.573 1.00 24.25  ? 114 GLY G O   1 
ATOM   7526  N  N   . ARG G  1 116 ? -7.050  -38.344 57.532 1.00 23.14  ? 115 ARG G N   1 
ATOM   7527  C  CA  . ARG G  1 116 ? -7.427  -39.628 56.965 1.00 22.01  ? 115 ARG G CA  1 
ATOM   7528  C  C   . ARG G  1 116 ? -7.948  -39.403 55.546 1.00 22.49  ? 115 ARG G C   1 
ATOM   7529  O  O   . ARG G  1 116 ? -7.820  -38.300 55.015 1.00 26.12  ? 115 ARG G O   1 
ATOM   7530  C  CB  . ARG G  1 116 ? -8.364  -40.349 57.928 1.00 21.83  ? 115 ARG G CB  1 
ATOM   7531  C  CG  . ARG G  1 116 ? -7.804  -40.421 59.332 1.00 21.76  ? 115 ARG G CG  1 
ATOM   7532  C  CD  . ARG G  1 116 ? -8.611  -41.286 60.260 1.00 22.99  ? 115 ARG G CD  1 
ATOM   7533  N  NE  . ARG G  1 116 ? -8.035  -41.364 61.603 1.00 23.84  ? 115 ARG G NE  1 
ATOM   7534  C  CZ  . ARG G  1 116 ? -7.113  -42.245 61.993 1.00 21.74  ? 115 ARG G CZ  1 
ATOM   7535  N  NH1 . ARG G  1 116 ? -6.648  -43.160 61.155 1.00 20.93  ? 115 ARG G NH1 1 
ATOM   7536  N  NH2 . ARG G  1 116 ? -6.683  -42.205 63.239 1.00 21.71  ? 115 ARG G NH2 1 
ATOM   7537  N  N   . THR G  1 117 ? -8.488  -40.449 54.906 1.00 21.27  ? 116 THR G N   1 
ATOM   7538  C  CA  . THR G  1 117 ? -8.905  -40.312 53.518 1.00 20.69  ? 116 THR G CA  1 
ATOM   7539  C  C   . THR G  1 117 ? -10.414 -40.459 53.374 1.00 21.41  ? 116 THR G C   1 
ATOM   7540  O  O   . THR G  1 117 ? -11.035 -41.312 54.000 1.00 23.67  ? 116 THR G O   1 
ATOM   7541  C  CB  . THR G  1 117 ? -8.182  -41.299 52.601 1.00 20.25  ? 116 THR G CB  1 
ATOM   7542  O  OG1 . THR G  1 117 ? -6.791  -40.978 52.675 1.00 19.66  ? 116 THR G OG1 1 
ATOM   7543  C  CG2 . THR G  1 117 ? -8.653  -41.221 51.162 1.00 20.30  ? 116 THR G CG2 1 
ATOM   7544  N  N   . LEU G  1 118 ? -10.991 -39.618 52.518 1.00 21.21  ? 117 LEU G N   1 
ATOM   7545  C  CA  . LEU G  1 118 ? -12.370 -39.793 52.115 1.00 21.05  ? 117 LEU G CA  1 
ATOM   7546  C  C   . LEU G  1 118 ? -12.354 -40.429 50.731 1.00 21.76  ? 117 LEU G C   1 
ATOM   7547  O  O   . LEU G  1 118 ? -11.581 -40.005 49.869 1.00 21.26  ? 117 LEU G O   1 
ATOM   7548  C  CB  . LEU G  1 118 ? -13.037 -38.419 52.091 1.00 21.02  ? 117 LEU G CB  1 
ATOM   7549  C  CG  . LEU G  1 118 ? -14.482 -38.389 51.621 1.00 20.34  ? 117 LEU G CG  1 
ATOM   7550  C  CD1 . LEU G  1 118 ? -15.350 -39.120 52.626 1.00 19.97  ? 117 LEU G CD1 1 
ATOM   7551  C  CD2 . LEU G  1 118 ? -14.964 -36.952 51.444 1.00 19.01  ? 117 LEU G CD2 1 
ATOM   7552  N  N   . VAL G  1 119 ? -13.185 -41.462 50.542 1.00 22.04  ? 118 VAL G N   1 
ATOM   7553  C  CA  . VAL G  1 119 ? -13.211 -42.202 49.288 1.00 21.38  ? 118 VAL G CA  1 
ATOM   7554  C  C   . VAL G  1 119 ? -14.652 -42.295 48.786 1.00 21.35  ? 118 VAL G C   1 
ATOM   7555  O  O   . VAL G  1 119 ? -15.579 -42.616 49.540 1.00 19.97  ? 118 VAL G O   1 
ATOM   7556  C  CB  . VAL G  1 119 ? -12.627 -43.622 49.432 1.00 21.47  ? 118 VAL G CB  1 
ATOM   7557  C  CG1 . VAL G  1 119 ? -12.645 -44.372 48.115 1.00 20.69  ? 118 VAL G CG1 1 
ATOM   7558  C  CG2 . VAL G  1 119 ? -11.233 -43.627 50.034 1.00 21.25  ? 118 VAL G CG2 1 
ATOM   7559  N  N   . VAL G  1 120 ? -14.816 -42.067 47.485 1.00 20.83  ? 119 VAL G N   1 
ATOM   7560  C  CA  . VAL G  1 120 ? -16.083 -42.345 46.840 1.00 21.07  ? 119 VAL G CA  1 
ATOM   7561  C  C   . VAL G  1 120 ? -15.886 -43.568 45.949 1.00 23.47  ? 119 VAL G C   1 
ATOM   7562  O  O   . VAL G  1 120 ? -14.958 -43.609 45.133 1.00 23.74  ? 119 VAL G O   1 
ATOM   7563  C  CB  . VAL G  1 120 ? -16.613 -41.119 46.075 1.00 20.62  ? 119 VAL G CB  1 
ATOM   7564  C  CG1 . VAL G  1 120 ? -15.644 -40.621 45.017 1.00 20.18  ? 119 VAL G CG1 1 
ATOM   7565  C  CG2 . VAL G  1 120 ? -17.986 -41.366 45.491 1.00 20.33  ? 119 VAL G CG2 1 
ATOM   7566  N  N   . HIS G  1 121 ? -16.781 -44.553 46.121 1.00 25.69  ? 120 HIS G N   1 
ATOM   7567  C  CA  . HIS G  1 121 ? -16.619 -45.880 45.545 1.00 24.81  ? 120 HIS G CA  1 
ATOM   7568  C  C   . HIS G  1 121 ? -17.437 -46.063 44.268 1.00 26.83  ? 120 HIS G C   1 
ATOM   7569  O  O   . HIS G  1 121 ? -18.280 -45.234 43.918 1.00 25.92  ? 120 HIS G O   1 
ATOM   7570  C  CB  . HIS G  1 121 ? -17.007 -46.940 46.574 1.00 23.85  ? 120 HIS G CB  1 
ATOM   7571  C  CG  . HIS G  1 121 ? -16.003 -47.102 47.657 1.00 23.34  ? 120 HIS G CG  1 
ATOM   7572  N  ND1 . HIS G  1 121 ? -14.975 -48.022 47.580 1.00 23.88  ? 120 HIS G ND1 1 
ATOM   7573  C  CD2 . HIS G  1 121 ? -15.876 -46.484 48.851 1.00 23.06  ? 120 HIS G CD2 1 
ATOM   7574  C  CE1 . HIS G  1 121 ? -14.257 -47.964 48.678 1.00 23.34  ? 120 HIS G CE1 1 
ATOM   7575  N  NE2 . HIS G  1 121 ? -14.792 -47.034 49.485 1.00 21.98  ? 120 HIS G NE2 1 
ATOM   7576  N  N   . GLU G  1 122 ? -17.203 -47.209 43.619 1.00 29.04  ? 121 GLU G N   1 
ATOM   7577  C  CA  . GLU G  1 122 ? -17.673 -47.499 42.278 1.00 30.87  ? 121 GLU G CA  1 
ATOM   7578  C  C   . GLU G  1 122 ? -19.177 -47.790 42.264 1.00 32.47  ? 121 GLU G C   1 
ATOM   7579  O  O   . GLU G  1 122 ? -19.869 -47.323 41.366 1.00 32.68  ? 121 GLU G O   1 
ATOM   7580  C  CB  . GLU G  1 122 ? -16.843 -48.667 41.768 1.00 32.03  ? 121 GLU G CB  1 
ATOM   7581  C  CG  . GLU G  1 122 ? -17.466 -49.444 40.634 1.00 34.56  ? 121 GLU G CG  1 
ATOM   7582  C  CD  . GLU G  1 122 ? -16.778 -50.790 40.468 1.00 39.24  ? 121 GLU G CD  1 
ATOM   7583  O  OE1 . GLU G  1 122 ? -16.639 -51.224 39.314 1.00 46.51  ? 121 GLU G OE1 1 
ATOM   7584  O  OE2 . GLU G  1 122 ? -16.351 -51.388 41.492 1.00 36.85  ? 121 GLU G OE2 1 
ATOM   7585  N  N   . LYS G  1 123 ? -19.659 -48.540 43.267 1.00 32.23  ? 122 LYS G N   1 
ATOM   7586  C  CA  . LYS G  1 123 ? -21.017 -49.069 43.326 1.00 30.76  ? 122 LYS G CA  1 
ATOM   7587  C  C   . LYS G  1 123 ? -21.686 -48.676 44.643 1.00 29.25  ? 122 LYS G C   1 
ATOM   7588  O  O   . LYS G  1 123 ? -21.074 -48.038 45.498 1.00 28.27  ? 122 LYS G O   1 
ATOM   7589  C  CB  . LYS G  1 123 ? -20.987 -50.602 43.304 1.00 32.05  ? 122 LYS G CB  1 
ATOM   7590  C  CG  . LYS G  1 123 ? -20.458 -51.239 42.027 1.00 36.99  ? 122 LYS G CG  1 
ATOM   7591  C  CD  . LYS G  1 123 ? -20.489 -52.770 42.030 1.00 38.00  ? 122 LYS G CD  1 
ATOM   7592  C  CE  . LYS G  1 123 ? -19.423 -53.409 42.890 1.00 37.53  ? 122 LYS G CE  1 
ATOM   7593  N  NZ  . LYS G  1 123 ? -19.459 -54.883 42.748 1.00 41.40  ? 122 LYS G NZ  1 
ATOM   7594  N  N   . ALA G  1 124 ? -22.948 -49.098 44.805 1.00 25.79  ? 123 ALA G N   1 
ATOM   7595  C  CA  . ALA G  1 124 ? -23.704 -48.848 46.019 1.00 24.52  ? 123 ALA G CA  1 
ATOM   7596  C  C   . ALA G  1 124 ? -23.072 -49.564 47.204 1.00 23.43  ? 123 ALA G C   1 
ATOM   7597  O  O   . ALA G  1 124 ? -22.535 -50.646 47.054 1.00 25.60  ? 123 ALA G O   1 
ATOM   7598  C  CB  . ALA G  1 124 ? -25.126 -49.306 45.828 1.00 23.98  ? 123 ALA G CB  1 
ATOM   7599  N  N   . ASP G  1 125 ? -23.146 -48.936 48.371 1.00 22.94  ? 124 ASP G N   1 
ATOM   7600  C  CA  . ASP G  1 125 ? -22.828 -49.585 49.628 1.00 22.98  ? 124 ASP G CA  1 
ATOM   7601  C  C   . ASP G  1 125 ? -24.091 -50.302 50.104 1.00 22.54  ? 124 ASP G C   1 
ATOM   7602  O  O   . ASP G  1 125 ? -25.128 -49.670 50.282 1.00 21.84  ? 124 ASP G O   1 
ATOM   7603  C  CB  . ASP G  1 125 ? -22.318 -48.536 50.621 1.00 23.96  ? 124 ASP G CB  1 
ATOM   7604  C  CG  . ASP G  1 125 ? -22.083 -49.042 52.032 1.00 24.56  ? 124 ASP G CG  1 
ATOM   7605  O  OD1 . ASP G  1 125 ? -22.391 -50.220 52.305 1.00 24.21  ? 124 ASP G OD1 1 
ATOM   7606  O  OD2 . ASP G  1 125 ? -21.593 -48.246 52.855 1.00 26.47  ? 124 ASP G OD2 1 
ATOM   7607  N  N   . ASP G  1 126 ? -24.005 -51.618 50.325 1.00 21.81  ? 125 ASP G N   1 
ATOM   7608  C  CA  . ASP G  1 126 ? -25.180 -52.401 50.691 1.00 20.18  ? 125 ASP G CA  1 
ATOM   7609  C  C   . ASP G  1 126 ? -25.475 -52.293 52.193 1.00 19.47  ? 125 ASP G C   1 
ATOM   7610  O  O   . ASP G  1 126 ? -26.365 -52.976 52.706 1.00 17.87  ? 125 ASP G O   1 
ATOM   7611  C  CB  . ASP G  1 126 ? -25.110 -53.836 50.155 1.00 19.03  ? 125 ASP G CB  1 
ATOM   7612  C  CG  . ASP G  1 126 ? -24.113 -54.750 50.856 1.00 19.78  ? 125 ASP G CG  1 
ATOM   7613  O  OD1 . ASP G  1 126 ? -23.750 -54.471 52.030 1.00 20.08  ? 125 ASP G OD1 1 
ATOM   7614  O  OD2 . ASP G  1 126 ? -23.715 -55.759 50.223 1.00 18.83  ? 125 ASP G OD2 1 
ATOM   7615  N  N   . LEU G  1 127 ? -24.729 -51.426 52.888 1.00 18.74  ? 126 LEU G N   1 
ATOM   7616  C  CA  . LEU G  1 127 ? -24.961 -51.104 54.290 1.00 19.45  ? 126 LEU G CA  1 
ATOM   7617  C  C   . LEU G  1 127 ? -24.873 -52.354 55.163 1.00 20.03  ? 126 LEU G C   1 
ATOM   7618  O  O   . LEU G  1 127 ? -25.417 -52.374 56.262 1.00 20.32  ? 126 LEU G O   1 
ATOM   7619  C  CB  . LEU G  1 127 ? -26.313 -50.391 54.459 1.00 18.41  ? 126 LEU G CB  1 
ATOM   7620  C  CG  . LEU G  1 127 ? -26.607 -49.242 53.494 1.00 17.05  ? 126 LEU G CG  1 
ATOM   7621  C  CD1 . LEU G  1 127 ? -27.952 -48.615 53.813 1.00 16.90  ? 126 LEU G CD1 1 
ATOM   7622  C  CD2 . LEU G  1 127 ? -25.478 -48.216 53.496 1.00 17.47  ? 126 LEU G CD2 1 
ATOM   7623  N  N   . GLY G  1 128 ? -24.198 -53.391 54.664 1.00 21.58  ? 127 GLY G N   1 
ATOM   7624  C  CA  . GLY G  1 128 ? -23.856 -54.568 55.448 1.00 23.74  ? 127 GLY G CA  1 
ATOM   7625  C  C   . GLY G  1 128 ? -24.953 -55.625 55.447 1.00 24.57  ? 127 GLY G C   1 
ATOM   7626  O  O   . GLY G  1 128 ? -24.946 -56.523 56.281 1.00 24.81  ? 127 GLY G O   1 
ATOM   7627  N  N   . LYS G  1 129 ? -25.880 -55.513 54.495 1.00 26.94  ? 128 LYS G N   1 
ATOM   7628  C  CA  . LYS G  1 129 ? -27.063 -56.366 54.473 1.00 26.08  ? 128 LYS G CA  1 
ATOM   7629  C  C   . LYS G  1 129 ? -27.057 -57.216 53.211 1.00 25.93  ? 128 LYS G C   1 
ATOM   7630  O  O   . LYS G  1 129 ? -28.117 -57.552 52.698 1.00 25.47  ? 128 LYS G O   1 
ATOM   7631  C  CB  . LYS G  1 129 ? -28.349 -55.524 54.534 1.00 25.82  ? 128 LYS G CB  1 
ATOM   7632  C  CG  . LYS G  1 129 ? -28.395 -54.459 55.597 1.00 26.92  ? 128 LYS G CG  1 
ATOM   7633  C  CD  . LYS G  1 129 ? -29.593 -54.261 56.497 1.00 29.47  ? 128 LYS G CD  1 
ATOM   7634  C  CE  . LYS G  1 129 ? -29.150 -53.224 57.505 1.00 32.51  ? 128 LYS G CE  1 
ATOM   7635  N  NZ  . LYS G  1 129 ? -29.587 -53.465 58.916 1.00 35.24  ? 128 LYS G NZ  1 
ATOM   7636  N  N   . GLY G  1 130 ? -25.855 -57.562 52.726 1.00 28.29  ? 129 GLY G N   1 
ATOM   7637  C  CA  . GLY G  1 130 ? -25.695 -58.284 51.471 1.00 29.15  ? 129 GLY G CA  1 
ATOM   7638  C  C   . GLY G  1 130 ? -25.565 -59.798 51.673 1.00 28.42  ? 129 GLY G C   1 
ATOM   7639  O  O   . GLY G  1 130 ? -25.619 -60.561 50.708 1.00 25.60  ? 129 GLY G O   1 
ATOM   7640  N  N   . GLY G  1 131 ? -25.369 -60.201 52.941 1.00 26.94  ? 130 GLY G N   1 
ATOM   7641  C  CA  . GLY G  1 131 ? -25.347 -61.596 53.337 1.00 28.09  ? 130 GLY G CA  1 
ATOM   7642  C  C   . GLY G  1 131 ? -24.120 -62.356 52.831 1.00 30.34  ? 130 GLY G C   1 
ATOM   7643  O  O   . GLY G  1 131 ? -24.156 -63.578 52.682 1.00 30.58  ? 130 GLY G O   1 
ATOM   7644  N  N   . ASN G  1 132 ? -23.032 -61.631 52.560 1.00 34.95  ? 131 ASN G N   1 
ATOM   7645  C  CA  . ASN G  1 132 ? -21.747 -62.265 52.301 1.00 36.15  ? 131 ASN G CA  1 
ATOM   7646  C  C   . ASN G  1 132 ? -20.686 -61.616 53.182 1.00 39.30  ? 131 ASN G C   1 
ATOM   7647  O  O   . ASN G  1 132 ? -20.964 -60.648 53.899 1.00 38.80  ? 131 ASN G O   1 
ATOM   7648  C  CB  . ASN G  1 132 ? -21.392 -62.307 50.812 1.00 35.94  ? 131 ASN G CB  1 
ATOM   7649  C  CG  . ASN G  1 132 ? -21.313 -60.954 50.142 1.00 35.19  ? 131 ASN G CG  1 
ATOM   7650  O  OD1 . ASN G  1 132 ? -21.155 -59.933 50.797 1.00 34.43  ? 131 ASN G OD1 1 
ATOM   7651  N  ND2 . ASN G  1 132 ? -21.475 -60.939 48.824 1.00 38.42  ? 131 ASN G ND2 1 
ATOM   7652  N  N   . GLU G  1 133 ? -19.467 -62.163 53.122 1.00 43.02  ? 132 GLU G N   1 
ATOM   7653  C  CA  . GLU G  1 133 ? -18.435 -61.728 54.049 1.00 40.78  ? 132 GLU G CA  1 
ATOM   7654  C  C   . GLU G  1 133 ? -18.012 -60.310 53.682 1.00 33.94  ? 132 GLU G C   1 
ATOM   7655  O  O   . GLU G  1 133 ? -17.787 -59.469 54.552 1.00 28.57  ? 132 GLU G O   1 
ATOM   7656  C  CB  . GLU G  1 133 ? -17.272 -62.718 54.066 1.00 46.96  ? 132 GLU G CB  1 
ATOM   7657  C  CG  . GLU G  1 133 ? -16.310 -62.440 55.192 1.00 52.29  ? 132 GLU G CG  1 
ATOM   7658  C  CD  . GLU G  1 133 ? -14.922 -63.032 55.053 1.00 54.38  ? 132 GLU G CD  1 
ATOM   7659  O  OE1 . GLU G  1 133 ? -14.539 -63.525 53.956 1.00 56.14  ? 132 GLU G OE1 1 
ATOM   7660  O  OE2 . GLU G  1 133 ? -14.221 -62.981 56.053 1.00 55.70  ? 132 GLU G OE2 1 
ATOM   7661  N  N   . GLU G  1 134 ? -17.965 -60.071 52.365 1.00 32.20  ? 133 GLU G N   1 
ATOM   7662  C  CA  . GLU G  1 134 ? -17.606 -58.792 51.786 1.00 36.14  ? 133 GLU G CA  1 
ATOM   7663  C  C   . GLU G  1 134 ? -18.518 -57.692 52.336 1.00 37.14  ? 133 GLU G C   1 
ATOM   7664  O  O   . GLU G  1 134 ? -18.054 -56.596 52.661 1.00 37.72  ? 133 GLU G O   1 
ATOM   7665  C  CB  . GLU G  1 134 ? -17.680 -58.929 50.264 1.00 42.24  ? 133 GLU G CB  1 
ATOM   7666  C  CG  . GLU G  1 134 ? -16.880 -57.880 49.504 1.00 48.19  ? 133 GLU G CG  1 
ATOM   7667  C  CD  . GLU G  1 134 ? -15.480 -57.527 49.985 1.00 52.77  ? 133 GLU G CD  1 
ATOM   7668  O  OE1 . GLU G  1 134 ? -14.763 -58.411 50.532 1.00 55.70  ? 133 GLU G OE1 1 
ATOM   7669  O  OE2 . GLU G  1 134 ? -15.121 -56.342 49.832 1.00 51.82  ? 133 GLU G OE2 1 
ATOM   7670  N  N   . SER G  1 135 ? -19.820 -57.990 52.439 1.00 33.81  ? 134 SER G N   1 
ATOM   7671  C  CA  . SER G  1 135 ? -20.801 -57.022 52.882 1.00 29.95  ? 134 SER G CA  1 
ATOM   7672  C  C   . SER G  1 135 ? -20.424 -56.451 54.239 1.00 28.41  ? 134 SER G C   1 
ATOM   7673  O  O   . SER G  1 135 ? -20.571 -55.255 54.465 1.00 29.80  ? 134 SER G O   1 
ATOM   7674  C  CB  . SER G  1 135 ? -22.196 -57.609 52.899 1.00 32.09  ? 134 SER G CB  1 
ATOM   7675  O  OG  . SER G  1 135 ? -23.166 -56.632 53.242 1.00 30.81  ? 134 SER G OG  1 
ATOM   7676  N  N   . THR G  1 136 ? -19.930 -57.297 55.143 1.00 27.15  ? 135 THR G N   1 
ATOM   7677  C  CA  . THR G  1 136 ? -19.697 -56.832 56.504 1.00 28.16  ? 135 THR G CA  1 
ATOM   7678  C  C   . THR G  1 136 ? -18.319 -56.179 56.638 1.00 27.85  ? 135 THR G C   1 
ATOM   7679  O  O   . THR G  1 136 ? -17.948 -55.767 57.730 1.00 25.34  ? 135 THR G O   1 
ATOM   7680  C  CB  . THR G  1 136 ? -19.858 -57.957 57.531 1.00 27.92  ? 135 THR G CB  1 
ATOM   7681  O  OG1 . THR G  1 136 ? -18.817 -58.894 57.248 1.00 30.75  ? 135 THR G OG1 1 
ATOM   7682  C  CG2 . THR G  1 136 ? -21.214 -58.617 57.481 1.00 26.30  ? 135 THR G CG2 1 
ATOM   7683  N  N   . LYS G  1 137 ? -17.580 -56.083 55.525 1.00 29.15  ? 136 LYS G N   1 
ATOM   7684  C  CA  . LYS G  1 137 ? -16.293 -55.405 55.510 1.00 30.04  ? 136 LYS G CA  1 
ATOM   7685  C  C   . LYS G  1 137 ? -16.384 -54.084 54.746 1.00 30.56  ? 136 LYS G C   1 
ATOM   7686  O  O   . LYS G  1 137 ? -16.032 -53.027 55.278 1.00 32.85  ? 136 LYS G O   1 
ATOM   7687  C  CB  . LYS G  1 137 ? -15.214 -56.299 54.891 1.00 32.91  ? 136 LYS G CB  1 
ATOM   7688  C  CG  . LYS G  1 137 ? -14.640 -57.379 55.787 1.00 40.61  ? 136 LYS G CG  1 
ATOM   7689  C  CD  . LYS G  1 137 ? -13.815 -58.371 54.955 1.00 46.24  ? 136 LYS G CD  1 
ATOM   7690  C  CE  . LYS G  1 137 ? -12.990 -59.329 55.780 1.00 51.83  ? 136 LYS G CE  1 
ATOM   7691  N  NZ  . LYS G  1 137 ? -11.866 -59.822 54.952 1.00 60.88  ? 136 LYS G NZ  1 
ATOM   7692  N  N   . THR G  1 138 ? -16.877 -54.145 53.505 1.00 28.22  ? 137 THR G N   1 
ATOM   7693  C  CA  . THR G  1 138 ? -16.783 -53.006 52.601 1.00 27.59  ? 137 THR G CA  1 
ATOM   7694  C  C   . THR G  1 138 ? -18.149 -52.590 52.067 1.00 26.55  ? 137 THR G C   1 
ATOM   7695  O  O   . THR G  1 138 ? -18.228 -51.649 51.285 1.00 27.75  ? 137 THR G O   1 
ATOM   7696  C  CB  . THR G  1 138 ? -15.893 -53.350 51.398 1.00 27.92  ? 137 THR G CB  1 
ATOM   7697  O  OG1 . THR G  1 138 ? -16.581 -54.270 50.549 1.00 27.61  ? 137 THR G OG1 1 
ATOM   7698  C  CG2 . THR G  1 138 ? -14.562 -53.919 51.820 1.00 26.55  ? 137 THR G CG2 1 
ATOM   7699  N  N   . GLY G  1 139 ? -19.202 -53.318 52.455 1.00 24.74  ? 138 GLY G N   1 
ATOM   7700  C  CA  . GLY G  1 139 ? -20.534 -53.098 51.922 1.00 24.35  ? 138 GLY G CA  1 
ATOM   7701  C  C   . GLY G  1 139 ? -20.622 -53.329 50.412 1.00 24.98  ? 138 GLY G C   1 
ATOM   7702  O  O   . GLY G  1 139 ? -21.609 -52.954 49.789 1.00 25.67  ? 138 GLY G O   1 
ATOM   7703  N  N   . ASN G  1 140 ? -19.593 -53.948 49.822 1.00 25.07  ? 139 ASN G N   1 
ATOM   7704  C  CA  . ASN G  1 140 ? -19.633 -54.371 48.426 1.00 25.78  ? 139 ASN G CA  1 
ATOM   7705  C  C   . ASN G  1 140 ? -19.610 -53.154 47.515 1.00 24.76  ? 139 ASN G C   1 
ATOM   7706  O  O   . ASN G  1 140 ? -20.102 -53.219 46.393 1.00 25.70  ? 139 ASN G O   1 
ATOM   7707  C  CB  . ASN G  1 140 ? -20.839 -55.273 48.106 1.00 27.62  ? 139 ASN G CB  1 
ATOM   7708  C  CG  . ASN G  1 140 ? -20.677 -56.697 48.601 1.00 29.02  ? 139 ASN G CG  1 
ATOM   7709  O  OD1 . ASN G  1 140 ? -19.849 -57.448 48.101 1.00 29.03  ? 139 ASN G OD1 1 
ATOM   7710  N  ND2 . ASN G  1 140 ? -21.458 -57.082 49.598 1.00 30.59  ? 139 ASN G ND2 1 
ATOM   7711  N  N   . ALA G  1 141 ? -19.016 -52.061 47.989 1.00 25.78  ? 140 ALA G N   1 
ATOM   7712  C  CA  . ALA G  1 141 ? -19.069 -50.778 47.296 1.00 27.22  ? 140 ALA G CA  1 
ATOM   7713  C  C   . ALA G  1 141 ? -18.132 -50.753 46.090 1.00 26.93  ? 140 ALA G C   1 
ATOM   7714  O  O   . ALA G  1 141 ? -18.156 -49.810 45.292 1.00 26.25  ? 140 ALA G O   1 
ATOM   7715  C  CB  . ALA G  1 141 ? -18.753 -49.659 48.256 1.00 28.62  ? 140 ALA G CB  1 
ATOM   7716  N  N   . GLY G  1 142 ? -17.311 -51.803 45.948 1.00 28.78  ? 141 GLY G N   1 
ATOM   7717  C  CA  . GLY G  1 142 ? -16.439 -51.904 44.790 1.00 27.70  ? 141 GLY G CA  1 
ATOM   7718  C  C   . GLY G  1 142 ? -15.240 -50.966 44.911 1.00 26.69  ? 141 GLY G C   1 
ATOM   7719  O  O   . GLY G  1 142 ? -14.862 -50.589 46.020 1.00 25.36  ? 141 GLY G O   1 
ATOM   7720  N  N   . SER G  1 143 ? -14.677 -50.588 43.757 1.00 25.21  ? 142 SER G N   1 
ATOM   7721  C  CA  . SER G  1 143 ? -13.384 -49.929 43.698 1.00 24.87  ? 142 SER G CA  1 
ATOM   7722  C  C   . SER G  1 143 ? -13.482 -48.483 44.174 1.00 25.37  ? 142 SER G C   1 
ATOM   7723  O  O   . SER G  1 143 ? -14.579 -47.963 44.395 1.00 27.50  ? 142 SER G O   1 
ATOM   7724  C  CB  . SER G  1 143 ? -12.781 -50.018 42.323 1.00 25.53  ? 142 SER G CB  1 
ATOM   7725  O  OG  . SER G  1 143 ? -13.580 -49.311 41.388 1.00 26.97  ? 142 SER G OG  1 
ATOM   7726  N  N   . ARG G  1 144 ? -12.309 -47.850 44.308 1.00 23.56  ? 143 ARG G N   1 
ATOM   7727  C  CA  . ARG G  1 144 ? -12.151 -46.498 44.811 1.00 21.69  ? 143 ARG G CA  1 
ATOM   7728  C  C   . ARG G  1 144 ? -12.011 -45.561 43.618 1.00 21.93  ? 143 ARG G C   1 
ATOM   7729  O  O   . ARG G  1 144 ? -10.992 -45.574 42.943 1.00 24.52  ? 143 ARG G O   1 
ATOM   7730  C  CB  . ARG G  1 144 ? -10.931 -46.439 45.738 1.00 20.26  ? 143 ARG G CB  1 
ATOM   7731  C  CG  . ARG G  1 144 ? -11.007 -47.437 46.888 1.00 19.89  ? 143 ARG G CG  1 
ATOM   7732  C  CD  . ARG G  1 144 ? -9.667  -47.645 47.610 1.00 20.29  ? 143 ARG G CD  1 
ATOM   7733  N  NE  . ARG G  1 144 ? -9.830  -48.663 48.662 1.00 19.42  ? 143 ARG G NE  1 
ATOM   7734  C  CZ  . ARG G  1 144 ? -9.157  -48.710 49.806 1.00 19.14  ? 143 ARG G CZ  1 
ATOM   7735  N  NH1 . ARG G  1 144 ? -8.257  -47.789 50.099 1.00 21.09  ? 143 ARG G NH1 1 
ATOM   7736  N  NH2 . ARG G  1 144 ? -9.394  -49.676 50.660 1.00 18.90  ? 143 ARG G NH2 1 
ATOM   7737  N  N   . LEU G  1 145 ? -13.046 -44.762 43.342 1.00 21.66  ? 144 LEU G N   1 
ATOM   7738  C  CA  . LEU G  1 145 ? -13.048 -43.973 42.126 1.00 22.21  ? 144 LEU G CA  1 
ATOM   7739  C  C   . LEU G  1 145 ? -12.199 -42.721 42.326 1.00 22.09  ? 144 LEU G C   1 
ATOM   7740  O  O   . LEU G  1 145 ? -11.500 -42.284 41.413 1.00 22.66  ? 144 LEU G O   1 
ATOM   7741  C  CB  . LEU G  1 145 ? -14.494 -43.618 41.772 1.00 24.77  ? 144 LEU G CB  1 
ATOM   7742  C  CG  . LEU G  1 145 ? -15.348 -44.782 41.259 1.00 26.73  ? 144 LEU G CG  1 
ATOM   7743  C  CD1 . LEU G  1 145 ? -16.733 -44.292 40.851 1.00 27.47  ? 144 LEU G CD1 1 
ATOM   7744  C  CD2 . LEU G  1 145 ? -14.652 -45.509 40.105 1.00 25.24  ? 144 LEU G CD2 1 
ATOM   7745  N  N   . ALA G  1 146 ? -12.275 -42.149 43.530 1.00 21.88  ? 145 ALA G N   1 
ATOM   7746  C  CA  . ALA G  1 146 ? -11.571 -40.922 43.859 1.00 22.15  ? 145 ALA G CA  1 
ATOM   7747  C  C   . ALA G  1 146 ? -11.457 -40.789 45.374 1.00 23.23  ? 145 ALA G C   1 
ATOM   7748  O  O   . ALA G  1 146 ? -12.305 -41.282 46.119 1.00 24.05  ? 145 ALA G O   1 
ATOM   7749  C  CB  . ALA G  1 146 ? -12.262 -39.718 43.247 1.00 20.82  ? 145 ALA G CB  1 
ATOM   7750  N  N   . CYS G  1 147 ? -10.387 -40.122 45.809 1.00 24.15  ? 146 CYS G N   1 
ATOM   7751  C  CA  . CYS G  1 147 ? -10.139 -39.945 47.226 1.00 24.44  ? 146 CYS G CA  1 
ATOM   7752  C  C   . CYS G  1 147 ? -9.318  -38.677 47.424 1.00 24.26  ? 146 CYS G C   1 
ATOM   7753  O  O   . CYS G  1 147 ? -8.863  -38.073 46.455 1.00 22.77  ? 146 CYS G O   1 
ATOM   7754  C  CB  . CYS G  1 147 ? -9.404  -41.147 47.795 1.00 25.10  ? 146 CYS G CB  1 
ATOM   7755  S  SG  . CYS G  1 147 ? -7.816  -41.461 46.971 1.00 28.76  ? 146 CYS G SG  1 
ATOM   7756  N  N   . GLY G  1 148 ? -9.172  -38.290 48.693 1.00 24.03  ? 147 GLY G N   1 
ATOM   7757  C  CA  . GLY G  1 148 ? -8.319  -37.189 49.099 1.00 22.45  ? 147 GLY G CA  1 
ATOM   7758  C  C   . GLY G  1 148 ? -8.027  -37.266 50.597 1.00 21.22  ? 147 GLY G C   1 
ATOM   7759  O  O   . GLY G  1 148 ? -8.763  -37.900 51.359 1.00 21.36  ? 147 GLY G O   1 
ATOM   7760  N  N   . VAL G  1 149 ? -6.941  -36.619 51.019 1.00 19.45  ? 148 VAL G N   1 
ATOM   7761  C  CA  . VAL G  1 149 ? -6.679  -36.523 52.440 1.00 18.55  ? 148 VAL G CA  1 
ATOM   7762  C  C   . VAL G  1 149 ? -7.542  -35.407 53.021 1.00 18.24  ? 148 VAL G C   1 
ATOM   7763  O  O   . VAL G  1 149 ? -7.753  -34.371 52.392 1.00 18.22  ? 148 VAL G O   1 
ATOM   7764  C  CB  . VAL G  1 149 ? -5.176  -36.351 52.731 1.00 18.32  ? 148 VAL G CB  1 
ATOM   7765  C  CG1 . VAL G  1 149 ? -4.891  -36.380 54.226 1.00 17.50  ? 148 VAL G CG1 1 
ATOM   7766  C  CG2 . VAL G  1 149 ? -4.378  -37.436 52.024 1.00 17.37  ? 148 VAL G CG2 1 
ATOM   7767  N  N   . ILE G  1 150 ? -8.068  -35.659 54.218 1.00 17.57  ? 149 ILE G N   1 
ATOM   7768  C  CA  . ILE G  1 150 ? -8.971  -34.743 54.886 1.00 17.62  ? 149 ILE G CA  1 
ATOM   7769  C  C   . ILE G  1 150 ? -8.114  -33.766 55.682 1.00 19.01  ? 149 ILE G C   1 
ATOM   7770  O  O   . ILE G  1 150 ? -7.457  -34.165 56.643 1.00 19.64  ? 149 ILE G O   1 
ATOM   7771  C  CB  . ILE G  1 150 ? -9.915  -35.541 55.808 1.00 16.35  ? 149 ILE G CB  1 
ATOM   7772  C  CG1 . ILE G  1 150 ? -10.819 -36.484 55.015 1.00 15.43  ? 149 ILE G CG1 1 
ATOM   7773  C  CG2 . ILE G  1 150 ? -10.708 -34.616 56.719 1.00 15.72  ? 149 ILE G CG2 1 
ATOM   7774  C  CD1 . ILE G  1 150 ? -11.476 -37.541 55.871 1.00 15.13  ? 149 ILE G CD1 1 
ATOM   7775  N  N   . GLY G  1 151 ? -8.149  -32.489 55.285 1.00 19.70  ? 150 GLY G N   1 
ATOM   7776  C  CA  . GLY G  1 151 ? -7.228  -31.490 55.808 1.00 20.79  ? 150 GLY G CA  1 
ATOM   7777  C  C   . GLY G  1 151 ? -7.932  -30.293 56.447 1.00 22.60  ? 150 GLY G C   1 
ATOM   7778  O  O   . GLY G  1 151 ? -9.121  -30.064 56.219 1.00 22.78  ? 150 GLY G O   1 
ATOM   7779  N  N   . ILE G  1 152 ? -7.171  -29.539 57.253 1.00 24.34  ? 151 ILE G N   1 
ATOM   7780  C  CA  . ILE G  1 152 ? -7.694  -28.399 57.987 1.00 26.71  ? 151 ILE G CA  1 
ATOM   7781  C  C   . ILE G  1 152 ? -7.888  -27.242 57.012 1.00 28.69  ? 151 ILE G C   1 
ATOM   7782  O  O   . ILE G  1 152 ? -7.007  -26.981 56.208 1.00 29.43  ? 151 ILE G O   1 
ATOM   7783  C  CB  . ILE G  1 152 ? -6.740  -28.018 59.131 1.00 25.09  ? 151 ILE G CB  1 
ATOM   7784  C  CG1 . ILE G  1 152 ? -6.645  -29.138 60.163 1.00 23.01  ? 151 ILE G CG1 1 
ATOM   7785  C  CG2 . ILE G  1 152 ? -7.172  -26.711 59.764 1.00 23.84  ? 151 ILE G CG2 1 
ATOM   7786  C  CD1 . ILE G  1 152 ? -5.424  -29.086 61.031 1.00 22.30  ? 151 ILE G CD1 1 
ATOM   7787  N  N   . ALA G  1 153 ? -9.050  -26.579 57.096 1.00 31.80  ? 152 ALA G N   1 
ATOM   7788  C  CA  . ALA G  1 153 ? -9.406  -25.470 56.227 1.00 35.59  ? 152 ALA G CA  1 
ATOM   7789  C  C   . ALA G  1 153 ? -9.554  -24.200 57.056 1.00 39.33  ? 152 ALA G C   1 
ATOM   7790  O  O   . ALA G  1 153 ? -9.615  -24.250 58.285 1.00 39.02  ? 152 ALA G O   1 
ATOM   7791  C  CB  . ALA G  1 153 ? -10.674 -25.775 55.484 1.00 34.15  ? 152 ALA G CB  1 
ATOM   7792  N  N   . GLN G  1 154 ? -9.605  -23.054 56.359 1.00 45.69  ? 153 GLN G N   1 
ATOM   7793  C  CA  . GLN G  1 154 ? -9.688  -21.759 57.015 1.00 51.99  ? 153 GLN G CA  1 
ATOM   7794  C  C   . GLN G  1 154 ? -11.065 -21.549 57.663 1.00 59.62  ? 153 GLN G C   1 
ATOM   7795  O  O   . GLN G  1 154 ? -12.151 -21.741 57.045 1.00 61.06  ? 153 GLN G O   1 
ATOM   7796  C  CB  . GLN G  1 154 ? -9.428  -20.627 56.017 1.00 50.12  ? 153 GLN G CB  1 
ATOM   7797  C  CG  . GLN G  1 154 ? -9.528  -19.250 56.664 1.00 48.80  ? 153 GLN G CG  1 
ATOM   7798  C  CD  . GLN G  1 154 ? -8.650  -18.235 55.967 1.00 50.69  ? 153 GLN G CD  1 
ATOM   7799  O  OE1 . GLN G  1 154 ? -8.724  -18.031 54.755 1.00 50.22  ? 153 GLN G OE1 1 
ATOM   7800  N  NE2 . GLN G  1 154 ? -7.787  -17.599 56.743 1.00 53.12  ? 153 GLN G NE2 1 
ATOM   7801  O  OXT . GLN G  1 154 ? -11.082 -21.151 58.845 1.00 62.21  ? 153 GLN G OXT 1 
ATOM   7802  N  N   . ALA H  1 2   ? 66.453  -31.864 7.029  1.00 55.31  ? 1   ALA H N   1 
ATOM   7803  C  CA  . ALA H  1 2   ? 65.054  -31.505 6.704  1.00 56.52  ? 1   ALA H CA  1 
ATOM   7804  C  C   . ALA H  1 2   ? 64.124  -31.978 7.824  1.00 54.43  ? 1   ALA H C   1 
ATOM   7805  O  O   . ALA H  1 2   ? 63.212  -31.235 8.165  1.00 64.23  ? 1   ALA H O   1 
ATOM   7806  C  CB  . ALA H  1 2   ? 64.639  -32.001 5.316  1.00 49.37  ? 1   ALA H CB  1 
ATOM   7807  N  N   . THR H  1 3   ? 64.251  -33.243 8.246  1.00 45.62  ? 2   THR H N   1 
ATOM   7808  C  CA  . THR H  1 3   ? 63.259  -33.861 9.117  1.00 40.81  ? 2   THR H CA  1 
ATOM   7809  C  C   . THR H  1 3   ? 63.862  -34.016 10.516 1.00 37.10  ? 2   THR H C   1 
ATOM   7810  O  O   . THR H  1 3   ? 64.903  -34.636 10.655 1.00 39.64  ? 2   THR H O   1 
ATOM   7811  C  CB  . THR H  1 3   ? 62.720  -35.158 8.482  1.00 38.67  ? 2   THR H CB  1 
ATOM   7812  O  OG1 . THR H  1 3   ? 62.344  -34.983 7.119  1.00 40.14  ? 2   THR H OG1 1 
ATOM   7813  C  CG2 . THR H  1 3   ? 61.644  -35.878 9.268  1.00 38.10  ? 2   THR H CG2 1 
ATOM   7814  N  N   . LYS H  1 4   ? 63.186  -33.467 11.535 1.00 31.34  ? 3   LYS H N   1 
ATOM   7815  C  CA  . LYS H  1 4   ? 63.555  -33.676 12.926 1.00 31.04  ? 3   LYS H CA  1 
ATOM   7816  C  C   . LYS H  1 4   ? 62.463  -34.477 13.635 1.00 31.24  ? 3   LYS H C   1 
ATOM   7817  O  O   . LYS H  1 4   ? 61.271  -34.193 13.519 1.00 31.09  ? 3   LYS H O   1 
ATOM   7818  C  CB  . LYS H  1 4   ? 63.750  -32.365 13.692 1.00 32.62  ? 3   LYS H CB  1 
ATOM   7819  C  CG  . LYS H  1 4   ? 65.118  -31.708 13.582 1.00 34.66  ? 3   LYS H CG  1 
ATOM   7820  C  CD  . LYS H  1 4   ? 65.205  -30.302 14.149 0.20 32.71  ? 3   LYS H CD  1 
ATOM   7821  C  CE  . LYS H  1 4   ? 66.050  -29.350 13.324 0.20 31.79  ? 3   LYS H CE  1 
ATOM   7822  N  NZ  . LYS H  1 4   ? 65.661  -27.931 13.491 0.20 30.61  ? 3   LYS H NZ  1 
ATOM   7823  N  N   . VAL H  1 5   ? 62.909  -35.457 14.421 1.00 29.48  ? 4   VAL H N   1 
ATOM   7824  C  CA  . VAL H  1 5   ? 62.043  -36.377 15.123 1.00 26.88  ? 4   VAL H CA  1 
ATOM   7825  C  C   . VAL H  1 5   ? 62.560  -36.497 16.551 1.00 24.88  ? 4   VAL H C   1 
ATOM   7826  O  O   . VAL H  1 5   ? 63.729  -36.255 16.816 1.00 23.90  ? 4   VAL H O   1 
ATOM   7827  C  CB  . VAL H  1 5   ? 62.035  -37.726 14.387 1.00 28.05  ? 4   VAL H CB  1 
ATOM   7828  C  CG1 . VAL H  1 5   ? 61.465  -38.849 15.230 1.00 29.97  ? 4   VAL H CG1 1 
ATOM   7829  C  CG2 . VAL H  1 5   ? 61.317  -37.618 13.054 1.00 28.51  ? 4   VAL H CG2 1 
ATOM   7830  N  N   . VAL H  1 6   ? 61.677  -36.849 17.482 1.00 24.44  ? 5   VAL H N   1 
ATOM   7831  C  CA  . VAL H  1 6   ? 62.104  -36.929 18.865 1.00 23.19  ? 5   VAL H CA  1 
ATOM   7832  C  C   . VAL H  1 6   ? 61.402  -38.095 19.555 1.00 22.44  ? 5   VAL H C   1 
ATOM   7833  O  O   . VAL H  1 6   ? 60.375  -38.592 19.097 1.00 22.54  ? 5   VAL H O   1 
ATOM   7834  C  CB  . VAL H  1 6   ? 61.875  -35.598 19.606 1.00 22.23  ? 5   VAL H CB  1 
ATOM   7835  C  CG1 . VAL H  1 6   ? 60.396  -35.339 19.848 1.00 20.98  ? 5   VAL H CG1 1 
ATOM   7836  C  CG2 . VAL H  1 6   ? 62.634  -35.555 20.924 1.00 21.92  ? 5   VAL H CG2 1 
ATOM   7837  N  N   . CYS H  1 7   ? 61.965  -38.507 20.688 1.00 21.77  ? 6   CYS H N   1 
ATOM   7838  C  CA  . CYS H  1 7   ? 61.404  -39.606 21.432 1.00 23.75  ? 6   CYS H CA  1 
ATOM   7839  C  C   . CYS H  1 7   ? 61.740  -39.407 22.903 1.00 25.02  ? 6   CYS H C   1 
ATOM   7840  O  O   . CYS H  1 7   ? 62.902  -39.179 23.241 1.00 29.16  ? 6   CYS H O   1 
ATOM   7841  C  CB  . CYS H  1 7   ? 62.031  -40.895 20.928 1.00 25.13  ? 6   CYS H CB  1 
ATOM   7842  S  SG  . CYS H  1 7   ? 61.371  -42.371 21.743 1.00 25.88  ? 6   CYS H SG  1 
ATOM   7843  N  N   . VAL H  1 8   ? 60.719  -39.491 23.762 1.00 23.39  ? 7   VAL H N   1 
ATOM   7844  C  CA  . VAL H  1 8   ? 60.936  -39.429 25.198 1.00 22.36  ? 7   VAL H CA  1 
ATOM   7845  C  C   . VAL H  1 8   ? 60.852  -40.848 25.741 1.00 22.10  ? 7   VAL H C   1 
ATOM   7846  O  O   . VAL H  1 8   ? 59.823  -41.501 25.572 1.00 22.99  ? 7   VAL H O   1 
ATOM   7847  C  CB  . VAL H  1 8   ? 59.904  -38.521 25.889 1.00 22.16  ? 7   VAL H CB  1 
ATOM   7848  C  CG1 . VAL H  1 8   ? 60.002  -38.579 27.405 1.00 20.02  ? 7   VAL H CG1 1 
ATOM   7849  C  CG2 . VAL H  1 8   ? 59.994  -37.086 25.391 1.00 22.83  ? 7   VAL H CG2 1 
ATOM   7850  N  N   . LEU H  1 9   ? 61.927  -41.318 26.388 1.00 21.43  ? 8   LEU H N   1 
ATOM   7851  C  CA  . LEU H  1 9   ? 61.916  -42.667 26.927 1.00 22.07  ? 8   LEU H CA  1 
ATOM   7852  C  C   . LEU H  1 9   ? 61.469  -42.622 28.384 1.00 22.86  ? 8   LEU H C   1 
ATOM   7853  O  O   . LEU H  1 9   ? 62.041  -41.872 29.187 1.00 23.95  ? 8   LEU H O   1 
ATOM   7854  C  CB  . LEU H  1 9   ? 63.324  -43.255 26.827 1.00 22.08  ? 8   LEU H CB  1 
ATOM   7855  C  CG  . LEU H  1 9   ? 63.925  -43.313 25.423 1.00 22.52  ? 8   LEU H CG  1 
ATOM   7856  C  CD1 . LEU H  1 9   ? 65.406  -43.615 25.495 1.00 21.59  ? 8   LEU H CD1 1 
ATOM   7857  C  CD2 . LEU H  1 9   ? 63.223  -44.367 24.568 1.00 23.07  ? 8   LEU H CD2 1 
ATOM   7858  N  N   . LYS H  1 10  ? 60.438  -43.419 28.706 1.00 23.39  ? 9   LYS H N   1 
ATOM   7859  C  CA  . LYS H  1 10  ? 59.986  -43.635 30.076 1.00 25.76  ? 9   LYS H CA  1 
ATOM   7860  C  C   . LYS H  1 10  ? 59.739  -45.124 30.272 1.00 25.94  ? 9   LYS H C   1 
ATOM   7861  O  O   . LYS H  1 10  ? 59.542  -45.861 29.309 1.00 27.02  ? 9   LYS H O   1 
ATOM   7862  C  CB  . LYS H  1 10  ? 58.688  -42.861 30.368 1.00 27.85  ? 9   LYS H CB  1 
ATOM   7863  C  CG  . LYS H  1 10  ? 58.824  -41.373 30.617 1.00 34.35  ? 9   LYS H CG  1 
ATOM   7864  C  CD  . LYS H  1 10  ? 57.530  -40.610 30.620 1.00 38.20  ? 9   LYS H CD  1 
ATOM   7865  C  CE  . LYS H  1 10  ? 57.909  -39.197 30.986 1.00 42.11  ? 9   LYS H CE  1 
ATOM   7866  N  NZ  . LYS H  1 10  ? 57.206  -38.253 30.113 1.00 42.57  ? 9   LYS H NZ  1 
ATOM   7867  N  N   . GLY H  1 11  ? 59.773  -45.555 31.535 1.00 26.91  ? 10  GLY H N   1 
ATOM   7868  C  CA  . GLY H  1 11  ? 59.472  -46.920 31.920 1.00 29.77  ? 10  GLY H CA  1 
ATOM   7869  C  C   . GLY H  1 11  ? 59.039  -46.978 33.383 1.00 32.72  ? 10  GLY H C   1 
ATOM   7870  O  O   . GLY H  1 11  ? 58.840  -45.949 34.026 1.00 34.01  ? 10  GLY H O   1 
ATOM   7871  N  N   . ASP H  1 12  ? 58.886  -48.197 33.917 1.00 34.64  ? 11  ASP H N   1 
ATOM   7872  C  CA  . ASP H  1 12  ? 58.416  -48.379 35.280 1.00 33.39  ? 11  ASP H CA  1 
ATOM   7873  C  C   . ASP H  1 12  ? 59.490  -48.034 36.301 1.00 31.91  ? 11  ASP H C   1 
ATOM   7874  O  O   . ASP H  1 12  ? 59.172  -47.675 37.423 1.00 33.27  ? 11  ASP H O   1 
ATOM   7875  C  CB  . ASP H  1 12  ? 57.904  -49.794 35.488 1.00 35.82  ? 11  ASP H CB  1 
ATOM   7876  C  CG  . ASP H  1 12  ? 56.617  -50.005 34.699 1.00 38.99  ? 11  ASP H CG  1 
ATOM   7877  O  OD1 . ASP H  1 12  ? 55.824  -49.042 34.582 1.00 37.19  ? 11  ASP H OD1 1 
ATOM   7878  O  OD2 . ASP H  1 12  ? 56.431  -51.111 34.159 1.00 42.29  ? 11  ASP H OD2 1 
ATOM   7879  N  N   . GLY H  1 13  ? 60.749  -48.170 35.912 1.00 31.78  ? 12  GLY H N   1 
ATOM   7880  C  CA  . GLY H  1 13  ? 61.870  -47.962 36.817 1.00 30.37  ? 12  GLY H CA  1 
ATOM   7881  C  C   . GLY H  1 13  ? 62.434  -46.557 36.661 1.00 30.54  ? 12  GLY H C   1 
ATOM   7882  O  O   . GLY H  1 13  ? 61.715  -45.648 36.264 1.00 31.37  ? 12  GLY H O   1 
ATOM   7883  N  N   . PRO H  1 14  ? 63.733  -46.339 36.987 1.00 28.06  ? 13  PRO H N   1 
ATOM   7884  C  CA  . PRO H  1 14  ? 64.303  -44.993 36.984 1.00 25.54  ? 13  PRO H CA  1 
ATOM   7885  C  C   . PRO H  1 14  ? 64.809  -44.512 35.625 1.00 25.09  ? 13  PRO H C   1 
ATOM   7886  O  O   . PRO H  1 14  ? 65.293  -43.391 35.509 1.00 24.58  ? 13  PRO H O   1 
ATOM   7887  C  CB  . PRO H  1 14  ? 65.464  -45.130 37.972 1.00 25.11  ? 13  PRO H CB  1 
ATOM   7888  C  CG  . PRO H  1 14  ? 65.913  -46.553 37.803 1.00 23.90  ? 13  PRO H CG  1 
ATOM   7889  C  CD  . PRO H  1 14  ? 64.699  -47.368 37.402 1.00 25.45  ? 13  PRO H CD  1 
ATOM   7890  N  N   . VAL H  1 15  ? 64.719  -45.364 34.589 1.00 24.98  ? 14  VAL H N   1 
ATOM   7891  C  CA  . VAL H  1 15  ? 65.394  -45.003 33.346 1.00 26.34  ? 14  VAL H CA  1 
ATOM   7892  C  C   . VAL H  1 15  ? 64.515  -44.013 32.594 1.00 30.21  ? 14  VAL H C   1 
ATOM   7893  O  O   . VAL H  1 15  ? 63.323  -44.255 32.394 1.00 34.84  ? 14  VAL H O   1 
ATOM   7894  C  CB  . VAL H  1 15  ? 65.727  -46.233 32.491 1.00 24.95  ? 14  VAL H CB  1 
ATOM   7895  C  CG1 . VAL H  1 15  ? 66.326  -45.832 31.158 1.00 23.69  ? 14  VAL H CG1 1 
ATOM   7896  C  CG2 . VAL H  1 15  ? 66.672  -47.153 33.258 1.00 28.29  ? 14  VAL H CG2 1 
ATOM   7897  N  N   . GLN H  1 16  ? 65.106  -42.885 32.190 1.00 30.44  ? 15  GLN H N   1 
ATOM   7898  C  CA  . GLN H  1 16  ? 64.382  -41.922 31.372 1.00 31.79  ? 15  GLN H CA  1 
ATOM   7899  C  C   . GLN H  1 16  ? 65.359  -41.095 30.546 1.00 30.44  ? 15  GLN H C   1 
ATOM   7900  O  O   . GLN H  1 16  ? 66.521  -40.955 30.923 1.00 35.04  ? 15  GLN H O   1 
ATOM   7901  C  CB  . GLN H  1 16  ? 63.472  -41.052 32.238 1.00 36.27  ? 15  GLN H CB  1 
ATOM   7902  C  CG  . GLN H  1 16  ? 64.206  -40.211 33.279 1.00 41.30  ? 15  GLN H CG  1 
ATOM   7903  C  CD  . GLN H  1 16  ? 63.220  -39.631 34.274 1.00 43.93  ? 15  GLN H CD  1 
ATOM   7904  O  OE1 . GLN H  1 16  ? 63.552  -39.252 35.395 1.00 47.06  ? 15  GLN H OE1 1 
ATOM   7905  N  NE2 . GLN H  1 16  ? 61.961  -39.562 33.875 1.00 44.58  ? 15  GLN H NE2 1 
ATOM   7906  N  N   . GLY H  1 17  ? 64.877  -40.560 29.417 1.00 26.29  ? 16  GLY H N   1 
ATOM   7907  C  CA  . GLY H  1 17  ? 65.761  -39.840 28.512 1.00 23.58  ? 16  GLY H CA  1 
ATOM   7908  C  C   . GLY H  1 17  ? 65.024  -39.232 27.325 1.00 22.44  ? 16  GLY H C   1 
ATOM   7909  O  O   . GLY H  1 17  ? 63.849  -39.527 27.095 1.00 23.29  ? 16  GLY H O   1 
ATOM   7910  N  N   . ILE H  1 18  ? 65.738  -38.384 26.579 1.00 20.04  ? 17  ILE H N   1 
ATOM   7911  C  CA  . ILE H  1 18  ? 65.220  -37.777 25.366 1.00 19.19  ? 17  ILE H CA  1 
ATOM   7912  C  C   . ILE H  1 18  ? 66.194  -38.125 24.246 1.00 18.32  ? 17  ILE H C   1 
ATOM   7913  O  O   . ILE H  1 18  ? 67.397  -37.934 24.409 1.00 17.87  ? 17  ILE H O   1 
ATOM   7914  C  CB  . ILE H  1 18  ? 65.110  -36.248 25.547 1.00 18.89  ? 17  ILE H CB  1 
ATOM   7915  C  CG1 . ILE H  1 18  ? 64.111  -35.890 26.649 1.00 18.73  ? 17  ILE H CG1 1 
ATOM   7916  C  CG2 . ILE H  1 18  ? 64.802  -35.545 24.225 1.00 17.98  ? 17  ILE H CG2 1 
ATOM   7917  C  CD1 . ILE H  1 18  ? 63.916  -34.409 26.876 1.00 18.48  ? 17  ILE H CD1 1 
ATOM   7918  N  N   . ILE H  1 19  ? 65.680  -38.624 23.120 1.00 17.99  ? 18  ILE H N   1 
ATOM   7919  C  CA  . ILE H  1 19  ? 66.561  -38.908 21.999 1.00 19.59  ? 18  ILE H CA  1 
ATOM   7920  C  C   . ILE H  1 19  ? 66.045  -38.165 20.778 1.00 20.46  ? 18  ILE H C   1 
ATOM   7921  O  O   . ILE H  1 19  ? 64.870  -38.289 20.453 1.00 21.53  ? 18  ILE H O   1 
ATOM   7922  C  CB  . ILE H  1 19  ? 66.672  -40.426 21.728 1.00 18.57  ? 18  ILE H CB  1 
ATOM   7923  C  CG1 . ILE H  1 19  ? 67.229  -41.197 22.927 1.00 18.73  ? 18  ILE H CG1 1 
ATOM   7924  C  CG2 . ILE H  1 19  ? 67.465  -40.707 20.466 1.00 16.86  ? 18  ILE H CG2 1 
ATOM   7925  C  CD1 . ILE H  1 19  ? 68.647  -40.847 23.312 1.00 19.89  ? 18  ILE H CD1 1 
ATOM   7926  N  N   . ASN H  1 20  ? 66.937  -37.440 20.102 1.00 21.64  ? 19  ASN H N   1 
ATOM   7927  C  CA  . ASN H  1 20  ? 66.582  -36.720 18.892 1.00 25.10  ? 19  ASN H CA  1 
ATOM   7928  C  C   . ASN H  1 20  ? 67.077  -37.474 17.667 1.00 26.53  ? 19  ASN H C   1 
ATOM   7929  O  O   . ASN H  1 20  ? 68.112  -38.133 17.718 1.00 29.01  ? 19  ASN H O   1 
ATOM   7930  C  CB  . ASN H  1 20  ? 67.202  -35.327 18.869 1.00 28.94  ? 19  ASN H CB  1 
ATOM   7931  C  CG  . ASN H  1 20  ? 66.877  -34.568 20.138 1.00 29.83  ? 19  ASN H CG  1 
ATOM   7932  O  OD1 . ASN H  1 20  ? 67.690  -34.536 21.056 1.00 31.13  ? 19  ASN H OD1 1 
ATOM   7933  N  ND2 . ASN H  1 20  ? 65.675  -34.014 20.227 1.00 27.42  ? 19  ASN H ND2 1 
ATOM   7934  N  N   . PHE H  1 21  ? 66.337  -37.354 16.567 1.00 28.27  ? 20  PHE H N   1 
ATOM   7935  C  CA  . PHE H  1 21  ? 66.736  -37.922 15.291 1.00 33.01  ? 20  PHE H CA  1 
ATOM   7936  C  C   . PHE H  1 21  ? 66.664  -36.827 14.238 1.00 38.83  ? 20  PHE H C   1 
ATOM   7937  O  O   . PHE H  1 21  ? 65.687  -36.094 14.185 1.00 46.14  ? 20  PHE H O   1 
ATOM   7938  C  CB  . PHE H  1 21  ? 65.771  -39.024 14.846 1.00 30.71  ? 20  PHE H CB  1 
ATOM   7939  C  CG  . PHE H  1 21  ? 65.678  -40.213 15.767 1.00 28.33  ? 20  PHE H CG  1 
ATOM   7940  C  CD1 . PHE H  1 21  ? 65.076  -40.109 17.014 1.00 28.36  ? 20  PHE H CD1 1 
ATOM   7941  C  CD2 . PHE H  1 21  ? 66.162  -41.451 15.371 1.00 27.64  ? 20  PHE H CD2 1 
ATOM   7942  C  CE1 . PHE H  1 21  ? 64.963  -41.216 17.842 1.00 27.37  ? 20  PHE H CE1 1 
ATOM   7943  C  CE2 . PHE H  1 21  ? 66.060  -42.556 16.201 1.00 27.32  ? 20  PHE H CE2 1 
ATOM   7944  C  CZ  . PHE H  1 21  ? 65.456  -42.441 17.432 1.00 27.38  ? 20  PHE H CZ  1 
ATOM   7945  N  N   . GLU H  1 22  ? 67.700  -36.720 13.407 1.00 42.13  ? 21  GLU H N   1 
ATOM   7946  C  CA  . GLU H  1 22  ? 67.718  -35.704 12.372 1.00 44.45  ? 21  GLU H CA  1 
ATOM   7947  C  C   . GLU H  1 22  ? 68.256  -36.313 11.080 1.00 43.82  ? 21  GLU H C   1 
ATOM   7948  O  O   . GLU H  1 22  ? 69.192  -37.101 11.123 1.00 46.68  ? 21  GLU H O   1 
ATOM   7949  C  CB  . GLU H  1 22  ? 68.542  -34.506 12.845 1.00 46.47  ? 21  GLU H CB  1 
ATOM   7950  C  CG  . GLU H  1 22  ? 68.313  -33.265 11.999 1.00 51.27  ? 21  GLU H CG  1 
ATOM   7951  C  CD  . GLU H  1 22  ? 69.079  -32.032 12.414 1.00 57.87  ? 21  GLU H CD  1 
ATOM   7952  O  OE1 . GLU H  1 22  ? 68.961  -31.628 13.612 1.00 61.23  ? 21  GLU H OE1 1 
ATOM   7953  O  OE2 . GLU H  1 22  ? 69.781  -31.476 11.533 1.00 63.19  ? 21  GLU H OE2 1 
ATOM   7954  N  N   . GLN H  1 23  ? 67.651  -35.944 9.945  1.00 42.58  ? 22  GLN H N   1 
ATOM   7955  C  CA  . GLN H  1 23  ? 68.038  -36.487 8.652  1.00 44.40  ? 22  GLN H CA  1 
ATOM   7956  C  C   . GLN H  1 23  ? 68.060  -35.372 7.607  1.00 46.46  ? 22  GLN H C   1 
ATOM   7957  O  O   . GLN H  1 23  ? 66.999  -34.911 7.192  1.00 47.16  ? 22  GLN H O   1 
ATOM   7958  C  CB  . GLN H  1 23  ? 67.056  -37.591 8.247  1.00 41.90  ? 22  GLN H CB  1 
ATOM   7959  C  CG  . GLN H  1 23  ? 67.500  -38.382 7.035  1.00 41.90  ? 22  GLN H CG  1 
ATOM   7960  C  CD  . GLN H  1 23  ? 66.502  -39.420 6.604  1.00 44.91  ? 22  GLN H CD  1 
ATOM   7961  O  OE1 . GLN H  1 23  ? 65.291  -39.255 6.730  1.00 47.52  ? 22  GLN H OE1 1 
ATOM   7962  N  NE2 . GLN H  1 23  ? 67.015  -40.502 6.054  1.00 44.10  ? 22  GLN H NE2 1 
ATOM   7963  N  N   . LYS H  1 24  ? 69.260  -34.949 7.185  1.00 51.42  ? 23  LYS H N   1 
ATOM   7964  C  CA  . LYS H  1 24  ? 69.419  -33.784 6.322  1.00 53.56  ? 23  LYS H CA  1 
ATOM   7965  C  C   . LYS H  1 24  ? 68.922  -34.078 4.903  1.00 55.46  ? 23  LYS H C   1 
ATOM   7966  O  O   . LYS H  1 24  ? 68.109  -33.330 4.372  1.00 59.84  ? 23  LYS H O   1 
ATOM   7967  C  CB  . LYS H  1 24  ? 70.812  -33.147 6.423  1.00 47.41  ? 23  LYS H CB  1 
ATOM   7968  C  CG  . LYS H  1 24  ? 71.049  -32.322 7.689  0.40 45.57  ? 23  LYS H CG  1 
ATOM   7969  C  CD  . LYS H  1 24  ? 72.477  -31.853 7.873  0.40 45.60  ? 23  LYS H CD  1 
ATOM   7970  C  CE  . LYS H  1 24  ? 72.790  -31.419 9.292  0.40 44.01  ? 23  LYS H CE  1 
ATOM   7971  N  NZ  . LYS H  1 24  ? 73.974  -30.537 9.341  0.40 41.21  ? 23  LYS H NZ  1 
ATOM   7972  N  N   . GLU H  1 25  ? 69.393  -35.170 4.285  1.00 55.64  ? 24  GLU H N   1 
ATOM   7973  C  CA  . GLU H  1 25  ? 68.917  -35.563 2.962  1.00 58.90  ? 24  GLU H CA  1 
ATOM   7974  C  C   . GLU H  1 25  ? 67.920  -36.706 3.109  1.00 56.68  ? 24  GLU H C   1 
ATOM   7975  O  O   . GLU H  1 25  ? 68.001  -37.459 4.070  1.00 61.98  ? 24  GLU H O   1 
ATOM   7976  C  CB  . GLU H  1 25  ? 70.070  -35.972 2.047  1.00 65.94  ? 24  GLU H CB  1 
ATOM   7977  C  CG  . GLU H  1 25  ? 71.070  -34.849 1.873  1.00 74.63  ? 24  GLU H CG  1 
ATOM   7978  C  CD  . GLU H  1 25  ? 72.349  -35.218 1.139  1.00 75.53  ? 24  GLU H CD  1 
ATOM   7979  O  OE1 . GLU H  1 25  ? 72.686  -36.429 1.052  1.00 72.56  ? 24  GLU H OE1 1 
ATOM   7980  O  OE2 . GLU H  1 25  ? 73.027  -34.285 0.667  1.00 74.90  ? 24  GLU H OE2 1 
ATOM   7981  N  N   . SER H  1 26  ? 67.026  -36.847 2.130  1.00 57.58  ? 25  SER H N   1 
ATOM   7982  C  CA  . SER H  1 26  ? 65.867  -37.707 2.284  1.00 64.14  ? 25  SER H CA  1 
ATOM   7983  C  C   . SER H  1 26  ? 66.235  -39.185 2.352  1.00 63.83  ? 25  SER H C   1 
ATOM   7984  O  O   . SER H  1 26  ? 65.546  -39.943 3.022  1.00 66.05  ? 25  SER H O   1 
ATOM   7985  C  CB  . SER H  1 26  ? 64.786  -37.433 1.254  1.00 68.94  ? 25  SER H CB  1 
ATOM   7986  O  OG  . SER H  1 26  ? 65.369  -37.122 0.000  1.00 72.08  ? 25  SER H OG  1 
ATOM   7987  N  N   . ASN H  1 27  ? 67.283  -39.612 1.661  1.00 64.05  ? 26  ASN H N   1 
ATOM   7988  C  CA  . ASN H  1 27  ? 67.669  -41.011 1.775  1.00 66.63  ? 26  ASN H CA  1 
ATOM   7989  C  C   . ASN H  1 27  ? 68.998  -41.146 2.515  1.00 62.82  ? 26  ASN H C   1 
ATOM   7990  O  O   . ASN H  1 27  ? 69.599  -42.215 2.517  1.00 66.28  ? 26  ASN H O   1 
ATOM   7991  C  CB  . ASN H  1 27  ? 67.548  -41.793 0.463  1.00 75.96  ? 26  ASN H CB  1 
ATOM   7992  C  CG  . ASN H  1 27  ? 67.894  -40.992 -0.776 1.00 81.98  ? 26  ASN H CG  1 
ATOM   7993  O  OD1 . ASN H  1 27  ? 68.751  -40.115 -0.740 1.00 82.35  ? 26  ASN H OD1 1 
ATOM   7994  N  ND2 . ASN H  1 27  ? 67.224  -41.274 -1.883 1.00 84.42  ? 26  ASN H ND2 1 
ATOM   7995  N  N   . GLY H  1 28  ? 69.440  -40.051 3.137  1.00 58.00  ? 27  GLY H N   1 
ATOM   7996  C  CA  . GLY H  1 28  ? 70.768  -39.966 3.724  1.00 50.92  ? 27  GLY H CA  1 
ATOM   7997  C  C   . GLY H  1 28  ? 70.824  -40.447 5.170  1.00 44.69  ? 27  GLY H C   1 
ATOM   7998  O  O   . GLY H  1 28  ? 69.814  -40.863 5.721  1.00 45.74  ? 27  GLY H O   1 
ATOM   7999  N  N   . PRO H  1 29  ? 71.997  -40.370 5.834  1.00 38.44  ? 28  PRO H N   1 
ATOM   8000  C  CA  . PRO H  1 29  ? 72.156  -40.892 7.193  1.00 35.22  ? 28  PRO H CA  1 
ATOM   8001  C  C   . PRO H  1 29  ? 71.328  -40.115 8.213  1.00 32.77  ? 28  PRO H C   1 
ATOM   8002  O  O   . PRO H  1 29  ? 70.963  -38.959 7.968  1.00 34.86  ? 28  PRO H O   1 
ATOM   8003  C  CB  . PRO H  1 29  ? 73.656  -40.674 7.469  1.00 35.72  ? 28  PRO H CB  1 
ATOM   8004  C  CG  . PRO H  1 29  ? 74.033  -39.511 6.565  1.00 33.74  ? 28  PRO H CG  1 
ATOM   8005  C  CD  . PRO H  1 29  ? 73.223  -39.741 5.313  1.00 35.48  ? 28  PRO H CD  1 
ATOM   8006  N  N   . VAL H  1 30  ? 71.033  -40.771 9.346  1.00 29.26  ? 29  VAL H N   1 
ATOM   8007  C  CA  . VAL H  1 30  ? 70.249  -40.186 10.425 1.00 26.11  ? 29  VAL H CA  1 
ATOM   8008  C  C   . VAL H  1 30  ? 71.153  -39.986 11.637 1.00 25.74  ? 29  VAL H C   1 
ATOM   8009  O  O   . VAL H  1 30  ? 71.787  -40.931 12.090 1.00 27.38  ? 29  VAL H O   1 
ATOM   8010  C  CB  . VAL H  1 30  ? 69.053  -41.084 10.792 1.00 24.82  ? 29  VAL H CB  1 
ATOM   8011  C  CG1 . VAL H  1 30  ? 68.220  -40.477 11.910 1.00 23.75  ? 29  VAL H CG1 1 
ATOM   8012  C  CG2 . VAL H  1 30  ? 68.182  -41.417 9.595  1.00 23.68  ? 29  VAL H CG2 1 
ATOM   8013  N  N   . LYS H  1 31  ? 71.210  -38.759 12.150 1.00 25.03  ? 30  LYS H N   1 
ATOM   8014  C  CA  . LYS H  1 31  ? 71.951  -38.503 13.375 1.00 26.16  ? 30  LYS H CA  1 
ATOM   8015  C  C   . LYS H  1 31  ? 71.025  -38.781 14.557 1.00 25.22  ? 30  LYS H C   1 
ATOM   8016  O  O   . LYS H  1 31  ? 69.919  -38.259 14.617 1.00 25.91  ? 30  LYS H O   1 
ATOM   8017  C  CB  . LYS H  1 31  ? 72.485  -37.061 13.433 1.00 26.68  ? 30  LYS H CB  1 
ATOM   8018  C  CG  . LYS H  1 31  ? 73.692  -36.710 12.593 1.00 25.78  ? 30  LYS H CG  1 
ATOM   8019  C  CD  . LYS H  1 31  ? 74.300  -35.394 12.970 0.50 25.60  ? 30  LYS H CD  1 
ATOM   8020  C  CE  . LYS H  1 31  ? 75.425  -35.137 12.013 0.50 25.30  ? 30  LYS H CE  1 
ATOM   8021  N  NZ  . LYS H  1 31  ? 75.334  -33.772 11.450 0.50 25.30  ? 30  LYS H NZ  1 
ATOM   8022  N  N   . VAL H  1 32  ? 71.464  -39.630 15.481 1.00 23.96  ? 31  VAL H N   1 
ATOM   8023  C  CA  . VAL H  1 32  ? 70.679  -39.949 16.658 1.00 22.99  ? 31  VAL H CA  1 
ATOM   8024  C  C   . VAL H  1 32  ? 71.457  -39.485 17.884 1.00 24.63  ? 31  VAL H C   1 
ATOM   8025  O  O   . VAL H  1 32  ? 72.542  -39.989 18.146 1.00 27.64  ? 31  VAL H O   1 
ATOM   8026  C  CB  . VAL H  1 32  ? 70.400  -41.462 16.728 1.00 21.08  ? 31  VAL H CB  1 
ATOM   8027  C  CG1 . VAL H  1 32  ? 69.495  -41.821 17.909 1.00 19.99  ? 31  VAL H CG1 1 
ATOM   8028  C  CG2 . VAL H  1 32  ? 69.818  -41.979 15.430 1.00 20.09  ? 31  VAL H CG2 1 
ATOM   8029  N  N   . TRP H  1 33  ? 70.921  -38.522 18.633 1.00 24.43  ? 32  TRP H N   1 
ATOM   8030  C  CA  . TRP H  1 33  ? 71.645  -38.085 19.821 1.00 24.30  ? 32  TRP H CA  1 
ATOM   8031  C  C   . TRP H  1 33  ? 70.693  -37.712 20.949 1.00 22.08  ? 32  TRP H C   1 
ATOM   8032  O  O   . TRP H  1 33  ? 69.537  -37.357 20.719 1.00 21.65  ? 32  TRP H O   1 
ATOM   8033  C  CB  . TRP H  1 33  ? 72.574  -36.906 19.503 1.00 26.30  ? 32  TRP H CB  1 
ATOM   8034  C  CG  . TRP H  1 33  ? 71.862  -35.589 19.429 1.00 27.75  ? 32  TRP H CG  1 
ATOM   8035  C  CD1 . TRP H  1 33  ? 71.781  -34.631 20.402 1.00 28.07  ? 32  TRP H CD1 1 
ATOM   8036  C  CD2 . TRP H  1 33  ? 71.111  -35.094 18.310 1.00 29.05  ? 32  TRP H CD2 1 
ATOM   8037  N  NE1 . TRP H  1 33  ? 71.038  -33.567 19.958 1.00 29.27  ? 32  TRP H NE1 1 
ATOM   8038  C  CE2 . TRP H  1 33  ? 70.616  -33.823 18.677 1.00 29.83  ? 32  TRP H CE2 1 
ATOM   8039  C  CE3 . TRP H  1 33  ? 70.810  -35.601 17.039 1.00 30.81  ? 32  TRP H CE3 1 
ATOM   8040  C  CZ2 . TRP H  1 33  ? 69.833  -33.057 17.809 1.00 30.85  ? 32  TRP H CZ2 1 
ATOM   8041  C  CZ3 . TRP H  1 33  ? 70.034  -34.840 16.183 1.00 32.27  ? 32  TRP H CZ3 1 
ATOM   8042  C  CH2 . TRP H  1 33  ? 69.560  -33.582 16.559 1.00 30.99  ? 32  TRP H CH2 1 
ATOM   8043  N  N   . GLY H  1 34  ? 71.230  -37.747 22.162 1.00 20.49  ? 33  GLY H N   1 
ATOM   8044  C  CA  . GLY H  1 34  ? 70.518  -37.287 23.333 1.00 20.95  ? 33  GLY H CA  1 
ATOM   8045  C  C   . GLY H  1 34  ? 71.121  -37.922 24.581 1.00 22.56  ? 33  GLY H C   1 
ATOM   8046  O  O   . GLY H  1 34  ? 72.258  -38.379 24.576 1.00 22.92  ? 33  GLY H O   1 
ATOM   8047  N  N   . SER H  1 35  ? 70.336  -37.984 25.643 1.00 24.02  ? 34  SER H N   1 
ATOM   8048  C  CA  . SER H  1 35  ? 70.878  -38.412 26.912 1.00 23.85  ? 34  SER H CA  1 
ATOM   8049  C  C   . SER H  1 35  ? 69.864  -39.326 27.606 1.00 24.82  ? 34  SER H C   1 
ATOM   8050  O  O   . SER H  1 35  ? 68.650  -39.083 27.545 1.00 28.20  ? 34  SER H O   1 
ATOM   8051  C  CB  . SER H  1 35  ? 71.198  -37.185 27.694 1.00 26.03  ? 34  SER H CB  1 
ATOM   8052  O  OG  . SER H  1 35  ? 71.470  -37.511 29.033 1.00 31.55  ? 34  SER H OG  1 
ATOM   8053  N  N   . ILE H  1 36  ? 70.347  -40.417 28.223 1.00 22.07  ? 35  ILE H N   1 
ATOM   8054  C  CA  . ILE H  1 36  ? 69.491  -41.268 29.033 1.00 21.17  ? 35  ILE H CA  1 
ATOM   8055  C  C   . ILE H  1 36  ? 70.119  -41.379 30.414 1.00 21.37  ? 35  ILE H C   1 
ATOM   8056  O  O   . ILE H  1 36  ? 71.336  -41.540 30.523 1.00 22.23  ? 35  ILE H O   1 
ATOM   8057  C  CB  . ILE H  1 36  ? 69.336  -42.657 28.384 1.00 20.71  ? 35  ILE H CB  1 
ATOM   8058  C  CG1 . ILE H  1 36  ? 68.980  -42.553 26.901 1.00 20.29  ? 35  ILE H CG1 1 
ATOM   8059  C  CG2 . ILE H  1 36  ? 68.344  -43.510 29.162 1.00 19.68  ? 35  ILE H CG2 1 
ATOM   8060  C  CD1 . ILE H  1 36  ? 69.015  -43.874 26.169 1.00 19.94  ? 35  ILE H CD1 1 
ATOM   8061  N  N   . LYS H  1 37  ? 69.290  -41.286 31.459 1.00 21.70  ? 36  LYS H N   1 
ATOM   8062  C  CA  . LYS H  1 37  ? 69.815  -41.356 32.813 1.00 23.42  ? 36  LYS H CA  1 
ATOM   8063  C  C   . LYS H  1 37  ? 69.143  -42.495 33.571 1.00 23.90  ? 36  LYS H C   1 
ATOM   8064  O  O   . LYS H  1 37  ? 68.118  -43.026 33.120 1.00 25.25  ? 36  LYS H O   1 
ATOM   8065  C  CB  . LYS H  1 37  ? 69.679  -39.998 33.507 1.00 25.36  ? 36  LYS H CB  1 
ATOM   8066  C  CG  . LYS H  1 37  ? 68.263  -39.533 33.781 1.00 27.94  ? 36  LYS H CG  1 
ATOM   8067  C  CD  . LYS H  1 37  ? 68.213  -38.401 34.803 1.00 32.08  ? 36  LYS H CD  1 
ATOM   8068  C  CE  . LYS H  1 37  ? 66.876  -38.268 35.506 1.00 34.29  ? 36  LYS H CE  1 
ATOM   8069  N  NZ  . LYS H  1 37  ? 66.789  -36.965 36.204 1.00 38.35  ? 36  LYS H NZ  1 
ATOM   8070  N  N   . GLY H  1 38  ? 69.752  -42.883 34.704 1.00 23.82  ? 37  GLY H N   1 
ATOM   8071  C  CA  . GLY H  1 38  ? 69.222  -43.937 35.561 1.00 23.74  ? 37  GLY H CA  1 
ATOM   8072  C  C   . GLY H  1 38  ? 69.599  -45.354 35.120 1.00 24.57  ? 37  GLY H C   1 
ATOM   8073  O  O   . GLY H  1 38  ? 69.025  -46.319 35.602 1.00 26.37  ? 37  GLY H O   1 
ATOM   8074  N  N   . LEU H  1 39  ? 70.570  -45.479 34.208 1.00 24.27  ? 38  LEU H N   1 
ATOM   8075  C  CA  . LEU H  1 39  ? 71.017  -46.778 33.715 1.00 23.67  ? 38  LEU H CA  1 
ATOM   8076  C  C   . LEU H  1 39  ? 72.124  -47.317 34.613 1.00 23.35  ? 38  LEU H C   1 
ATOM   8077  O  O   . LEU H  1 39  ? 72.819  -46.552 35.269 1.00 22.55  ? 38  LEU H O   1 
ATOM   8078  C  CB  . LEU H  1 39  ? 71.540  -46.622 32.287 1.00 23.27  ? 38  LEU H CB  1 
ATOM   8079  C  CG  . LEU H  1 39  ? 70.471  -46.339 31.234 1.00 24.06  ? 38  LEU H CG  1 
ATOM   8080  C  CD1 . LEU H  1 39  ? 71.115  -45.807 29.964 1.00 24.25  ? 38  LEU H CD1 1 
ATOM   8081  C  CD2 . LEU H  1 39  ? 69.663  -47.597 30.953 1.00 23.83  ? 38  LEU H CD2 1 
ATOM   8082  N  N   . THR H  1 40  ? 72.286  -48.642 34.631 1.00 24.46  ? 39  THR H N   1 
ATOM   8083  C  CA  . THR H  1 40  ? 73.452  -49.243 35.263 1.00 26.10  ? 39  THR H CA  1 
ATOM   8084  C  C   . THR H  1 40  ? 74.656  -49.000 34.359 1.00 30.02  ? 39  THR H C   1 
ATOM   8085  O  O   . THR H  1 40  ? 74.511  -48.930 33.139 1.00 32.45  ? 39  THR H O   1 
ATOM   8086  C  CB  . THR H  1 40  ? 73.269  -50.744 35.495 1.00 23.77  ? 39  THR H CB  1 
ATOM   8087  O  OG1 . THR H  1 40  ? 72.833  -51.272 34.242 1.00 22.54  ? 39  THR H OG1 1 
ATOM   8088  C  CG2 . THR H  1 40  ? 72.276  -51.043 36.601 1.00 24.16  ? 39  THR H CG2 1 
ATOM   8089  N  N   . GLU H  1 41  ? 75.838  -48.866 34.970 1.00 30.55  ? 40  GLU H N   1 
ATOM   8090  C  CA  . GLU H  1 41  ? 77.049  -48.594 34.217 1.00 28.94  ? 40  GLU H CA  1 
ATOM   8091  C  C   . GLU H  1 41  ? 77.241  -49.683 33.169 1.00 27.93  ? 40  GLU H C   1 
ATOM   8092  O  O   . GLU H  1 41  ? 76.959  -50.852 33.437 1.00 27.14  ? 40  GLU H O   1 
ATOM   8093  C  CB  . GLU H  1 41  ? 78.242  -48.533 35.164 1.00 29.67  ? 40  GLU H CB  1 
ATOM   8094  C  CG  . GLU H  1 41  ? 79.518  -48.128 34.464 1.00 33.39  ? 40  GLU H CG  1 
ATOM   8095  C  CD  . GLU H  1 41  ? 80.733  -47.963 35.387 1.00 35.29  ? 40  GLU H CD  1 
ATOM   8096  O  OE1 . GLU H  1 41  ? 80.637  -48.299 36.607 1.00 32.87  ? 40  GLU H OE1 1 
ATOM   8097  O  OE2 . GLU H  1 41  ? 81.788  -47.484 34.888 1.00 36.85  ? 40  GLU H OE2 1 
ATOM   8098  N  N   . GLY H  1 42  ? 77.684  -49.291 31.968 1.00 26.16  ? 41  GLY H N   1 
ATOM   8099  C  CA  . GLY H  1 42  ? 77.996  -50.275 30.942 1.00 26.50  ? 41  GLY H CA  1 
ATOM   8100  C  C   . GLY H  1 42  ? 77.083  -50.202 29.715 1.00 26.84  ? 41  GLY H C   1 
ATOM   8101  O  O   . GLY H  1 42  ? 76.393  -49.195 29.510 1.00 29.30  ? 41  GLY H O   1 
ATOM   8102  N  N   . LEU H  1 43  ? 77.110  -51.276 28.908 1.00 24.43  ? 42  LEU H N   1 
ATOM   8103  C  CA  . LEU H  1 43  ? 76.441  -51.309 27.615 1.00 24.56  ? 42  LEU H CA  1 
ATOM   8104  C  C   . LEU H  1 43  ? 74.967  -51.647 27.787 1.00 25.85  ? 42  LEU H C   1 
ATOM   8105  O  O   . LEU H  1 43  ? 74.622  -52.482 28.622 1.00 27.04  ? 42  LEU H O   1 
ATOM   8106  C  CB  . LEU H  1 43  ? 77.104  -52.367 26.726 1.00 22.41  ? 42  LEU H CB  1 
ATOM   8107  C  CG  . LEU H  1 43  ? 78.531  -52.096 26.284 1.00 20.39  ? 42  LEU H CG  1 
ATOM   8108  C  CD1 . LEU H  1 43  ? 79.024  -53.289 25.487 1.00 19.92  ? 42  LEU H CD1 1 
ATOM   8109  C  CD2 . LEU H  1 43  ? 78.573  -50.908 25.350 1.00 21.06  ? 42  LEU H CD2 1 
ATOM   8110  N  N   . HIS H  1 44  ? 74.120  -50.990 26.979 1.00 27.32  ? 43  HIS H N   1 
ATOM   8111  C  CA  . HIS H  1 44  ? 72.692  -51.275 26.921 1.00 26.50  ? 43  HIS H CA  1 
ATOM   8112  C  C   . HIS H  1 44  ? 72.233  -51.304 25.465 1.00 27.05  ? 43  HIS H C   1 
ATOM   8113  O  O   . HIS H  1 44  ? 72.580  -50.426 24.662 1.00 26.35  ? 43  HIS H O   1 
ATOM   8114  C  CB  . HIS H  1 44  ? 71.901  -50.247 27.728 1.00 25.47  ? 43  HIS H CB  1 
ATOM   8115  C  CG  . HIS H  1 44  ? 72.174  -50.292 29.194 1.00 25.31  ? 43  HIS H CG  1 
ATOM   8116  N  ND1 . HIS H  1 44  ? 71.378  -51.009 30.075 1.00 23.80  ? 43  HIS H ND1 1 
ATOM   8117  C  CD2 . HIS H  1 44  ? 73.132  -49.695 29.943 1.00 24.64  ? 43  HIS H CD2 1 
ATOM   8118  C  CE1 . HIS H  1 44  ? 71.828  -50.851 31.307 1.00 23.79  ? 43  HIS H CE1 1 
ATOM   8119  N  NE2 . HIS H  1 44  ? 72.908  -50.044 31.251 1.00 24.57  ? 43  HIS H NE2 1 
ATOM   8120  N  N   . GLY H  1 45  ? 71.468  -52.351 25.136 1.00 26.25  ? 44  GLY H N   1 
ATOM   8121  C  CA  . GLY H  1 45  ? 70.917  -52.523 23.807 1.00 26.14  ? 44  GLY H CA  1 
ATOM   8122  C  C   . GLY H  1 45  ? 69.937  -51.400 23.480 1.00 27.39  ? 44  GLY H C   1 
ATOM   8123  O  O   . GLY H  1 45  ? 69.179  -50.942 24.341 1.00 28.95  ? 44  GLY H O   1 
ATOM   8124  N  N   . PHE H  1 46  ? 69.956  -50.981 22.213 1.00 25.31  ? 45  PHE H N   1 
ATOM   8125  C  CA  . PHE H  1 46  ? 69.281  -49.770 21.800 1.00 23.17  ? 45  PHE H CA  1 
ATOM   8126  C  C   . PHE H  1 46  ? 68.660  -50.042 20.440 1.00 23.93  ? 45  PHE H C   1 
ATOM   8127  O  O   . PHE H  1 46  ? 69.392  -50.141 19.447 1.00 24.52  ? 45  PHE H O   1 
ATOM   8128  C  CB  . PHE H  1 46  ? 70.332  -48.660 21.702 1.00 23.21  ? 45  PHE H CB  1 
ATOM   8129  C  CG  . PHE H  1 46  ? 69.821  -47.250 21.578 1.00 21.99  ? 45  PHE H CG  1 
ATOM   8130  C  CD1 . PHE H  1 46  ? 69.122  -46.657 22.619 1.00 21.92  ? 45  PHE H CD1 1 
ATOM   8131  C  CD2 . PHE H  1 46  ? 70.079  -46.502 20.439 1.00 21.12  ? 45  PHE H CD2 1 
ATOM   8132  C  CE1 . PHE H  1 46  ? 68.649  -45.355 22.507 1.00 22.53  ? 45  PHE H CE1 1 
ATOM   8133  C  CE2 . PHE H  1 46  ? 69.621  -45.193 20.330 1.00 21.17  ? 45  PHE H CE2 1 
ATOM   8134  C  CZ  . PHE H  1 46  ? 68.922  -44.620 21.370 1.00 21.53  ? 45  PHE H CZ  1 
ATOM   8135  N  N   . HIS H  1 47  ? 67.329  -50.185 20.404 1.00 25.17  ? 46  HIS H N   1 
ATOM   8136  C  CA  . HIS H  1 47  ? 66.679  -50.642 19.185 1.00 25.12  ? 46  HIS H CA  1 
ATOM   8137  C  C   . HIS H  1 47  ? 65.400  -49.868 18.908 1.00 24.91  ? 46  HIS H C   1 
ATOM   8138  O  O   . HIS H  1 47  ? 64.725  -49.374 19.821 1.00 25.46  ? 46  HIS H O   1 
ATOM   8139  C  CB  . HIS H  1 47  ? 66.345  -52.132 19.273 1.00 26.43  ? 46  HIS H CB  1 
ATOM   8140  C  CG  . HIS H  1 47  ? 67.429  -52.951 19.877 1.00 29.70  ? 46  HIS H CG  1 
ATOM   8141  N  ND1 . HIS H  1 47  ? 67.319  -53.507 21.136 1.00 29.41  ? 46  HIS H ND1 1 
ATOM   8142  C  CD2 . HIS H  1 47  ? 68.653  -53.294 19.409 1.00 33.20  ? 46  HIS H CD2 1 
ATOM   8143  C  CE1 . HIS H  1 47  ? 68.434  -54.155 21.418 1.00 30.76  ? 46  HIS H CE1 1 
ATOM   8144  N  NE2 . HIS H  1 47  ? 69.272  -54.038 20.377 1.00 31.23  ? 46  HIS H NE2 1 
ATOM   8145  N  N   . VAL H  1 48  ? 65.072  -49.812 17.616 1.00 24.45  ? 47  VAL H N   1 
ATOM   8146  C  CA  . VAL H  1 48  ? 63.734  -49.429 17.197 1.00 24.88  ? 47  VAL H CA  1 
ATOM   8147  C  C   . VAL H  1 48  ? 62.903  -50.703 17.064 1.00 25.58  ? 47  VAL H C   1 
ATOM   8148  O  O   . VAL H  1 48  ? 63.210  -51.551 16.231 1.00 25.93  ? 47  VAL H O   1 
ATOM   8149  C  CB  . VAL H  1 48  ? 63.743  -48.640 15.875 1.00 23.05  ? 47  VAL H CB  1 
ATOM   8150  C  CG1 . VAL H  1 48  ? 62.340  -48.187 15.515 1.00 22.26  ? 47  VAL H CG1 1 
ATOM   8151  C  CG2 . VAL H  1 48  ? 64.673  -47.443 15.942 1.00 22.48  ? 47  VAL H CG2 1 
ATOM   8152  N  N   . HIS H  1 49  ? 61.855  -50.819 17.888 1.00 25.42  ? 48  HIS H N   1 
ATOM   8153  C  CA  . HIS H  1 49  ? 60.885  -51.895 17.770 1.00 25.00  ? 48  HIS H CA  1 
ATOM   8154  C  C   . HIS H  1 49  ? 59.769  -51.504 16.798 1.00 26.49  ? 48  HIS H C   1 
ATOM   8155  O  O   . HIS H  1 49  ? 59.651  -50.343 16.414 1.00 28.55  ? 48  HIS H O   1 
ATOM   8156  C  CB  . HIS H  1 49  ? 60.367  -52.284 19.157 1.00 24.30  ? 48  HIS H CB  1 
ATOM   8157  C  CG  . HIS H  1 49  ? 61.412  -52.891 20.024 1.00 24.65  ? 48  HIS H CG  1 
ATOM   8158  N  ND1 . HIS H  1 49  ? 61.290  -54.168 20.543 1.00 25.23  ? 48  HIS H ND1 1 
ATOM   8159  C  CD2 . HIS H  1 49  ? 62.600  -52.419 20.464 1.00 24.03  ? 48  HIS H CD2 1 
ATOM   8160  C  CE1 . HIS H  1 49  ? 62.352  -54.453 21.277 1.00 24.69  ? 48  HIS H CE1 1 
ATOM   8161  N  NE2 . HIS H  1 49  ? 63.173  -53.395 21.243 1.00 24.33  ? 48  HIS H NE2 1 
ATOM   8162  N  N   . GLU H  1 50  ? 58.930  -52.483 16.439 1.00 27.69  ? 49  GLU H N   1 
ATOM   8163  C  CA  . GLU H  1 50  ? 58.033  -52.393 15.291 1.00 27.74  ? 49  GLU H CA  1 
ATOM   8164  C  C   . GLU H  1 50  ? 56.860  -51.440 15.527 1.00 26.64  ? 49  GLU H C   1 
ATOM   8165  O  O   . GLU H  1 50  ? 56.504  -50.690 14.626 1.00 26.81  ? 49  GLU H O   1 
ATOM   8166  C  CB  . GLU H  1 50  ? 57.473  -53.773 14.949 1.00 27.00  ? 49  GLU H CB  1 
ATOM   8167  C  CG  . GLU H  1 50  ? 56.841  -53.816 13.576 1.00 26.55  ? 49  GLU H CG  1 
ATOM   8168  C  CD  . GLU H  1 50  ? 56.266  -55.144 13.154 1.00 28.54  ? 49  GLU H CD  1 
ATOM   8169  O  OE1 . GLU H  1 50  ? 56.640  -56.203 13.766 1.00 29.08  ? 49  GLU H OE1 1 
ATOM   8170  O  OE2 . GLU H  1 50  ? 55.446  -55.106 12.214 1.00 28.19  ? 49  GLU H OE2 1 
ATOM   8171  N  N   . PHE H  1 51  ? 56.255  -51.493 16.719 1.00 26.12  ? 50  PHE H N   1 
ATOM   8172  C  CA  . PHE H  1 51  ? 54.976  -50.839 16.941 1.00 26.55  ? 50  PHE H CA  1 
ATOM   8173  C  C   . PHE H  1 51  ? 55.108  -49.661 17.899 1.00 27.27  ? 50  PHE H C   1 
ATOM   8174  O  O   . PHE H  1 51  ? 55.695  -49.797 18.975 1.00 26.34  ? 50  PHE H O   1 
ATOM   8175  C  CB  . PHE H  1 51  ? 53.965  -51.823 17.528 1.00 25.68  ? 50  PHE H CB  1 
ATOM   8176  C  CG  . PHE H  1 51  ? 53.788  -53.057 16.691 1.00 25.32  ? 50  PHE H CG  1 
ATOM   8177  C  CD1 . PHE H  1 51  ? 53.412  -52.947 15.360 1.00 26.71  ? 50  PHE H CD1 1 
ATOM   8178  C  CD2 . PHE H  1 51  ? 54.012  -54.319 17.216 1.00 23.69  ? 50  PHE H CD2 1 
ATOM   8179  C  CE1 . PHE H  1 51  ? 53.238  -54.080 14.571 1.00 25.41  ? 50  PHE H CE1 1 
ATOM   8180  C  CE2 . PHE H  1 51  ? 53.849  -55.448 16.427 1.00 23.41  ? 50  PHE H CE2 1 
ATOM   8181  C  CZ  . PHE H  1 51  ? 53.473  -55.325 15.104 1.00 23.71  ? 50  PHE H CZ  1 
ATOM   8182  N  N   . GLY H  1 52  ? 54.514  -48.530 17.491 1.00 25.58  ? 51  GLY H N   1 
ATOM   8183  C  CA  . GLY H  1 52  ? 54.298  -47.392 18.365 1.00 26.34  ? 51  GLY H CA  1 
ATOM   8184  C  C   . GLY H  1 52  ? 53.107  -47.638 19.284 1.00 26.07  ? 51  GLY H C   1 
ATOM   8185  O  O   . GLY H  1 52  ? 52.151  -46.864 19.318 1.00 27.02  ? 51  GLY H O   1 
ATOM   8186  N  N   . ASP H  1 53  ? 53.177  -48.737 20.031 1.00 24.15  ? 52  ASP H N   1 
ATOM   8187  C  CA  . ASP H  1 53  ? 52.051  -49.175 20.825 1.00 24.13  ? 52  ASP H CA  1 
ATOM   8188  C  C   . ASP H  1 53  ? 52.523  -49.356 22.259 1.00 24.84  ? 52  ASP H C   1 
ATOM   8189  O  O   . ASP H  1 53  ? 53.353  -50.214 22.532 1.00 25.73  ? 52  ASP H O   1 
ATOM   8190  C  CB  . ASP H  1 53  ? 51.462  -50.455 20.234 1.00 23.51  ? 52  ASP H CB  1 
ATOM   8191  C  CG  . ASP H  1 53  ? 50.247  -50.986 20.986 1.00 23.75  ? 52  ASP H CG  1 
ATOM   8192  O  OD1 . ASP H  1 53  ? 50.110  -50.685 22.201 1.00 22.05  ? 52  ASP H OD1 1 
ATOM   8193  O  OD2 . ASP H  1 53  ? 49.376  -51.617 20.324 1.00 22.98  ? 52  ASP H OD2 1 
ATOM   8194  N  N   . ASN H  1 54  ? 51.991  -48.531 23.162 1.00 25.47  ? 53  ASN H N   1 
ATOM   8195  C  CA  . ASN H  1 54  ? 52.442  -48.551 24.541 1.00 25.92  ? 53  ASN H CA  1 
ATOM   8196  C  C   . ASN H  1 54  ? 51.293  -49.012 25.435 1.00 25.61  ? 53  ASN H C   1 
ATOM   8197  O  O   . ASN H  1 54  ? 51.328  -48.824 26.643 1.00 26.48  ? 53  ASN H O   1 
ATOM   8198  C  CB  . ASN H  1 54  ? 53.058  -47.196 24.913 1.00 25.98  ? 53  ASN H CB  1 
ATOM   8199  C  CG  . ASN H  1 54  ? 53.604  -47.131 26.328 1.00 29.05  ? 53  ASN H CG  1 
ATOM   8200  O  OD1 . ASN H  1 54  ? 54.421  -47.960 26.728 1.00 33.49  ? 53  ASN H OD1 1 
ATOM   8201  N  ND2 . ASN H  1 54  ? 53.181  -46.150 27.110 1.00 29.11  ? 53  ASN H ND2 1 
ATOM   8202  N  N   . THR H  1 55  ? 50.283  -49.661 24.838 1.00 25.57  ? 54  THR H N   1 
ATOM   8203  C  CA  . THR H  1 55  ? 49.059  -49.992 25.556 1.00 26.39  ? 54  THR H CA  1 
ATOM   8204  C  C   . THR H  1 55  ? 49.348  -50.900 26.745 1.00 27.23  ? 54  THR H C   1 
ATOM   8205  O  O   . THR H  1 55  ? 48.655  -50.823 27.751 1.00 29.41  ? 54  THR H O   1 
ATOM   8206  C  CB  . THR H  1 55  ? 48.002  -50.647 24.657 1.00 24.66  ? 54  THR H CB  1 
ATOM   8207  O  OG1 . THR H  1 55  ? 48.589  -51.811 24.088 1.00 24.55  ? 54  THR H OG1 1 
ATOM   8208  C  CG2 . THR H  1 55  ? 47.516  -49.749 23.546 1.00 24.35  ? 54  THR H CG2 1 
ATOM   8209  N  N   . ALA H  1 56  ? 50.364  -51.758 26.616 1.00 29.38  ? 55  ALA H N   1 
ATOM   8210  C  CA  . ALA H  1 56  ? 50.709  -52.696 27.670 1.00 32.09  ? 55  ALA H CA  1 
ATOM   8211  C  C   . ALA H  1 56  ? 52.160  -52.465 28.081 1.00 34.01  ? 55  ALA H C   1 
ATOM   8212  O  O   . ALA H  1 56  ? 52.915  -53.415 28.252 1.00 39.03  ? 55  ALA H O   1 
ATOM   8213  C  CB  . ALA H  1 56  ? 50.489  -54.103 27.173 1.00 31.86  ? 55  ALA H CB  1 
ATOM   8214  N  N   . GLY H  1 57  ? 52.547  -51.194 28.218 1.00 32.73  ? 56  GLY H N   1 
ATOM   8215  C  CA  . GLY H  1 57  ? 53.928  -50.840 28.500 1.00 32.13  ? 56  GLY H CA  1 
ATOM   8216  C  C   . GLY H  1 57  ? 54.823  -51.074 27.287 1.00 32.29  ? 56  GLY H C   1 
ATOM   8217  O  O   . GLY H  1 57  ? 54.334  -51.111 26.149 1.00 30.26  ? 56  GLY H O   1 
ATOM   8218  N  N   . CYS H  1 58  ? 56.126  -51.260 27.547 1.00 31.05  ? 57  CYS H N   1 
ATOM   8219  C  CA  . CYS H  1 58  ? 57.079  -51.400 26.461 1.00 30.91  ? 57  CYS H CA  1 
ATOM   8220  C  C   . CYS H  1 58  ? 56.879  -52.710 25.703 1.00 32.55  ? 57  CYS H C   1 
ATOM   8221  O  O   . CYS H  1 58  ? 57.253  -52.791 24.533 1.00 31.31  ? 57  CYS H O   1 
ATOM   8222  C  CB  . CYS H  1 58  ? 58.510  -51.286 26.960 1.00 29.27  ? 57  CYS H CB  1 
ATOM   8223  S  SG  . CYS H  1 58  ? 58.901  -49.621 27.541 1.00 33.99  ? 57  CYS H SG  1 
ATOM   8224  N  N   . THR H  1 59  ? 56.267  -53.704 26.363 1.00 31.95  ? 58  THR H N   1 
ATOM   8225  C  CA  . THR H  1 59  ? 56.063  -55.019 25.774 1.00 32.21  ? 58  THR H CA  1 
ATOM   8226  C  C   . THR H  1 59  ? 55.311  -54.915 24.451 1.00 32.60  ? 58  THR H C   1 
ATOM   8227  O  O   . THR H  1 59  ? 55.606  -55.656 23.509 1.00 32.42  ? 58  THR H O   1 
ATOM   8228  C  CB  . THR H  1 59  ? 55.178  -55.918 26.645 1.00 32.05  ? 58  THR H CB  1 
ATOM   8229  O  OG1 . THR H  1 59  ? 55.695  -55.863 27.971 1.00 34.20  ? 58  THR H OG1 1 
ATOM   8230  C  CG2 . THR H  1 59  ? 55.133  -57.348 26.158 1.00 29.57  ? 58  THR H CG2 1 
ATOM   8231  N  N   . SER H  1 60  ? 54.325  -54.014 24.397 1.00 29.25  ? 59  SER H N   1 
ATOM   8232  C  CA  . SER H  1 60  ? 53.406  -54.026 23.274 1.00 27.32  ? 59  SER H CA  1 
ATOM   8233  C  C   . SER H  1 60  ? 54.040  -53.392 22.037 1.00 25.01  ? 59  SER H C   1 
ATOM   8234  O  O   . SER H  1 60  ? 53.416  -53.324 20.980 1.00 22.45  ? 59  SER H O   1 
ATOM   8235  C  CB  . SER H  1 60  ? 52.045  -53.467 23.639 1.00 27.87  ? 59  SER H CB  1 
ATOM   8236  O  OG  . SER H  1 60  ? 52.166  -52.177 24.204 1.00 25.72  ? 59  SER H OG  1 
ATOM   8237  N  N   . ALA H  1 61  ? 55.315  -52.996 22.172 1.00 25.51  ? 60  ALA H N   1 
ATOM   8238  C  CA  . ALA H  1 61  ? 56.078  -52.405 21.084 1.00 25.40  ? 60  ALA H CA  1 
ATOM   8239  C  C   . ALA H  1 61  ? 56.454  -53.476 20.059 1.00 25.68  ? 60  ALA H C   1 
ATOM   8240  O  O   . ALA H  1 61  ? 56.807  -53.153 18.923 1.00 25.82  ? 60  ALA H O   1 
ATOM   8241  C  CB  . ALA H  1 61  ? 57.306  -51.732 21.630 1.00 24.38  ? 60  ALA H CB  1 
ATOM   8242  N  N   . GLY H  1 62  ? 56.376  -54.745 20.483 1.00 23.80  ? 61  GLY H N   1 
ATOM   8243  C  CA  . GLY H  1 62  ? 56.683  -55.870 19.620 1.00 22.27  ? 61  GLY H CA  1 
ATOM   8244  C  C   . GLY H  1 62  ? 58.186  -56.080 19.443 1.00 21.84  ? 61  GLY H C   1 
ATOM   8245  O  O   . GLY H  1 62  ? 58.987  -55.603 20.252 1.00 20.27  ? 61  GLY H O   1 
ATOM   8246  N  N   . PRO H  1 63  ? 58.608  -56.789 18.365 1.00 22.34  ? 62  PRO H N   1 
ATOM   8247  C  CA  . PRO H  1 63  ? 60.020  -57.145 18.163 1.00 23.31  ? 62  PRO H CA  1 
ATOM   8248  C  C   . PRO H  1 63  ? 60.815  -55.990 17.554 1.00 24.24  ? 62  PRO H C   1 
ATOM   8249  O  O   . PRO H  1 63  ? 60.251  -54.934 17.262 1.00 27.16  ? 62  PRO H O   1 
ATOM   8250  C  CB  . PRO H  1 63  ? 59.899  -58.281 17.135 1.00 22.04  ? 62  PRO H CB  1 
ATOM   8251  C  CG  . PRO H  1 63  ? 58.718  -57.870 16.277 1.00 21.47  ? 62  PRO H CG  1 
ATOM   8252  C  CD  . PRO H  1 63  ? 57.746  -57.243 17.255 1.00 22.23  ? 62  PRO H CD  1 
ATOM   8253  N  N   . HIS H  1 64  ? 62.121  -56.189 17.355 1.00 23.60  ? 63  HIS H N   1 
ATOM   8254  C  CA  . HIS H  1 64  ? 62.925  -55.204 16.648 1.00 23.57  ? 63  HIS H CA  1 
ATOM   8255  C  C   . HIS H  1 64  ? 62.286  -54.962 15.282 1.00 25.10  ? 63  HIS H C   1 
ATOM   8256  O  O   . HIS H  1 64  ? 61.880  -55.914 14.622 1.00 23.60  ? 63  HIS H O   1 
ATOM   8257  C  CB  . HIS H  1 64  ? 64.374  -55.689 16.468 1.00 22.76  ? 63  HIS H CB  1 
ATOM   8258  C  CG  . HIS H  1 64  ? 65.131  -55.885 17.738 1.00 22.74  ? 63  HIS H CG  1 
ATOM   8259  N  ND1 . HIS H  1 64  ? 66.388  -56.475 17.750 1.00 23.65  ? 63  HIS H ND1 1 
ATOM   8260  C  CD2 . HIS H  1 64  ? 64.813  -55.612 19.026 1.00 22.36  ? 63  HIS H CD2 1 
ATOM   8261  C  CE1 . HIS H  1 64  ? 66.834  -56.528 18.984 1.00 23.36  ? 63  HIS H CE1 1 
ATOM   8262  N  NE2 . HIS H  1 64  ? 65.877  -56.006 19.794 1.00 23.16  ? 63  HIS H NE2 1 
ATOM   8263  N  N   . PHE H  1 65  ? 62.208  -53.691 14.868 1.00 27.44  ? 64  PHE H N   1 
ATOM   8264  C  CA  . PHE H  1 65  ? 61.672  -53.329 13.563 1.00 27.95  ? 64  PHE H CA  1 
ATOM   8265  C  C   . PHE H  1 65  ? 62.425  -54.065 12.456 1.00 27.90  ? 64  PHE H C   1 
ATOM   8266  O  O   . PHE H  1 65  ? 63.612  -53.843 12.266 1.00 28.53  ? 64  PHE H O   1 
ATOM   8267  C  CB  . PHE H  1 65  ? 61.686  -51.806 13.380 1.00 25.58  ? 64  PHE H CB  1 
ATOM   8268  C  CG  . PHE H  1 65  ? 61.148  -51.326 12.055 1.00 25.17  ? 64  PHE H CG  1 
ATOM   8269  C  CD1 . PHE H  1 65  ? 59.991  -51.880 11.504 1.00 25.73  ? 64  PHE H CD1 1 
ATOM   8270  C  CD2 . PHE H  1 65  ? 61.778  -50.300 11.367 1.00 25.09  ? 64  PHE H CD2 1 
ATOM   8271  C  CE1 . PHE H  1 65  ? 59.497  -51.431 10.289 1.00 25.75  ? 64  PHE H CE1 1 
ATOM   8272  C  CE2 . PHE H  1 65  ? 61.280  -49.845 10.151 1.00 26.34  ? 64  PHE H CE2 1 
ATOM   8273  C  CZ  . PHE H  1 65  ? 60.144  -50.408 9.615  1.00 26.97  ? 64  PHE H CZ  1 
ATOM   8274  N  N   . ASN H  1 66  ? 61.719  -54.923 11.714 1.00 27.82  ? 65  ASN H N   1 
ATOM   8275  C  CA  . ASN H  1 66  ? 62.401  -55.864 10.846 1.00 29.26  ? 65  ASN H CA  1 
ATOM   8276  C  C   . ASN H  1 66  ? 61.705  -55.978 9.489  1.00 29.61  ? 65  ASN H C   1 
ATOM   8277  O  O   . ASN H  1 66  ? 61.367  -57.077 9.061  1.00 30.96  ? 65  ASN H O   1 
ATOM   8278  C  CB  . ASN H  1 66  ? 62.592  -57.216 11.550 1.00 28.83  ? 65  ASN H CB  1 
ATOM   8279  C  CG  . ASN H  1 66  ? 63.418  -58.188 10.740 1.00 30.08  ? 65  ASN H CG  1 
ATOM   8280  O  OD1 . ASN H  1 66  ? 64.168  -57.793 9.845  1.00 29.76  ? 65  ASN H OD1 1 
ATOM   8281  N  ND2 . ASN H  1 66  ? 63.282  -59.465 11.035 1.00 31.18  ? 65  ASN H ND2 1 
ATOM   8282  N  N   . PRO H  1 67  ? 61.531  -54.882 8.716  1.00 30.50  ? 66  PRO H N   1 
ATOM   8283  C  CA  . PRO H  1 67  ? 60.749  -54.950 7.480  1.00 31.53  ? 66  PRO H CA  1 
ATOM   8284  C  C   . PRO H  1 67  ? 61.323  -55.867 6.401  1.00 33.06  ? 66  PRO H C   1 
ATOM   8285  O  O   . PRO H  1 67  ? 60.609  -56.270 5.493  1.00 34.42  ? 66  PRO H O   1 
ATOM   8286  C  CB  . PRO H  1 67  ? 60.741  -53.509 6.948  1.00 29.81  ? 66  PRO H CB  1 
ATOM   8287  C  CG  . PRO H  1 67  ? 61.921  -52.853 7.614  1.00 30.95  ? 66  PRO H CG  1 
ATOM   8288  C  CD  . PRO H  1 67  ? 62.113  -53.552 8.945  1.00 32.00  ? 66  PRO H CD  1 
ATOM   8289  N  N   . LEU H  1 68  ? 62.616  -56.196 6.494  1.00 35.28  ? 67  LEU H N   1 
ATOM   8290  C  CA  . LEU H  1 68  ? 63.267  -56.964 5.443  1.00 34.78  ? 67  LEU H CA  1 
ATOM   8291  C  C   . LEU H  1 68  ? 63.447  -58.427 5.854  1.00 35.68  ? 67  LEU H C   1 
ATOM   8292  O  O   . LEU H  1 68  ? 64.091  -59.186 5.126  1.00 34.28  ? 67  LEU H O   1 
ATOM   8293  C  CB  . LEU H  1 68  ? 64.616  -56.324 5.095  1.00 35.50  ? 67  LEU H CB  1 
ATOM   8294  C  CG  . LEU H  1 68  ? 64.572  -54.954 4.431  1.00 36.56  ? 67  LEU H CG  1 
ATOM   8295  C  CD1 . LEU H  1 68  ? 65.984  -54.492 4.092  1.00 37.88  ? 67  LEU H CD1 1 
ATOM   8296  C  CD2 . LEU H  1 68  ? 63.665  -54.987 3.209  1.00 36.29  ? 67  LEU H CD2 1 
ATOM   8297  N  N   . SER H  1 69  ? 62.897  -58.814 7.016  1.00 36.58  ? 68  SER H N   1 
ATOM   8298  C  CA  . SER H  1 69  ? 62.909  -60.188 7.500  1.00 39.95  ? 68  SER H CA  1 
ATOM   8299  C  C   . SER H  1 69  ? 64.323  -60.764 7.570  1.00 42.92  ? 68  SER H C   1 
ATOM   8300  O  O   . SER H  1 69  ? 64.561  -61.838 7.018  1.00 44.60  ? 68  SER H O   1 
ATOM   8301  C  CB  . SER H  1 69  ? 62.050  -61.075 6.643  1.00 35.36  ? 68  SER H CB  1 
ATOM   8302  O  OG  . SER H  1 69  ? 60.696  -60.714 6.766  1.00 33.81  ? 68  SER H OG  1 
ATOM   8303  N  N   . ARG H  1 70  ? 65.242  -60.065 8.247  1.00 39.98  ? 69  ARG H N   1 
ATOM   8304  C  CA  . ARG H  1 70  ? 66.601  -60.555 8.426  1.00 39.61  ? 69  ARG H CA  1 
ATOM   8305  C  C   . ARG H  1 70  ? 66.803  -60.955 9.885  1.00 37.62  ? 69  ARG H C   1 
ATOM   8306  O  O   . ARG H  1 70  ? 65.926  -60.741 10.720 1.00 37.08  ? 69  ARG H O   1 
ATOM   8307  C  CB  . ARG H  1 70  ? 67.631  -59.497 8.018  1.00 40.44  ? 69  ARG H CB  1 
ATOM   8308  C  CG  . ARG H  1 70  ? 67.415  -58.903 6.635  1.00 42.10  ? 69  ARG H CG  1 
ATOM   8309  C  CD  . ARG H  1 70  ? 68.135  -59.612 5.501  1.00 48.92  ? 69  ARG H CD  1 
ATOM   8310  N  NE  . ARG H  1 70  ? 68.116  -58.729 4.334  1.00 61.58  ? 69  ARG H NE  1 
ATOM   8311  C  CZ  . ARG H  1 70  ? 69.000  -57.757 4.066  1.00 64.55  ? 69  ARG H CZ  1 
ATOM   8312  N  NH1 . ARG H  1 70  ? 70.015  -57.530 4.888  1.00 71.95  ? 69  ARG H NH1 1 
ATOM   8313  N  NH2 . ARG H  1 70  ? 68.856  -57.006 2.984  1.00 58.55  ? 69  ARG H NH2 1 
ATOM   8314  N  N   . LYS H  1 71  ? 67.966  -61.554 10.176 1.00 36.40  ? 70  LYS H N   1 
ATOM   8315  C  CA  . LYS H  1 71  ? 68.335  -61.937 11.531 1.00 33.13  ? 70  LYS H CA  1 
ATOM   8316  C  C   . LYS H  1 71  ? 68.987  -60.731 12.214 1.00 31.09  ? 70  LYS H C   1 
ATOM   8317  O  O   . LYS H  1 71  ? 69.433  -59.799 11.548 1.00 29.00  ? 70  LYS H O   1 
ATOM   8318  C  CB  . LYS H  1 71  ? 69.161  -63.231 11.529 1.00 35.97  ? 70  LYS H CB  1 
ATOM   8319  C  CG  . LYS H  1 71  ? 68.510  -64.403 10.807 1.00 40.80  ? 70  LYS H CG  1 
ATOM   8320  C  CD  . LYS H  1 71  ? 69.362  -65.628 10.736 1.00 47.25  ? 70  LYS H CD  1 
ATOM   8321  C  CE  . LYS H  1 71  ? 68.520  -66.879 10.544 1.00 51.52  ? 70  LYS H CE  1 
ATOM   8322  N  NZ  . LYS H  1 71  ? 69.173  -68.129 11.026 1.00 50.88  ? 70  LYS H NZ  1 
ATOM   8323  N  N   . HIS H  1 72  ? 69.013  -60.747 13.550 1.00 30.79  ? 71  HIS H N   1 
ATOM   8324  C  CA  . HIS H  1 72  ? 69.530  -59.634 14.336 1.00 29.87  ? 71  HIS H CA  1 
ATOM   8325  C  C   . HIS H  1 72  ? 71.041  -59.502 14.148 1.00 28.69  ? 71  HIS H C   1 
ATOM   8326  O  O   . HIS H  1 72  ? 71.754  -60.501 14.098 1.00 29.81  ? 71  HIS H O   1 
ATOM   8327  C  CB  . HIS H  1 72  ? 69.151  -59.829 15.810 1.00 29.04  ? 71  HIS H CB  1 
ATOM   8328  C  CG  . HIS H  1 72  ? 69.734  -58.806 16.717 1.00 28.09  ? 71  HIS H CG  1 
ATOM   8329  N  ND1 . HIS H  1 72  ? 69.143  -57.567 16.942 1.00 28.34  ? 71  HIS H ND1 1 
ATOM   8330  C  CD2 . HIS H  1 72  ? 70.855  -58.831 17.463 1.00 28.66  ? 71  HIS H CD2 1 
ATOM   8331  C  CE1 . HIS H  1 72  ? 69.879  -56.876 17.783 1.00 29.10  ? 71  HIS H CE1 1 
ATOM   8332  N  NE2 . HIS H  1 72  ? 70.940  -57.626 18.113 1.00 28.86  ? 71  HIS H NE2 1 
ATOM   8333  N  N   . GLY H  1 73  ? 71.521  -58.262 14.042 1.00 27.98  ? 72  GLY H N   1 
ATOM   8334  C  CA  . GLY H  1 73  ? 72.947  -57.987 13.956 1.00 28.51  ? 72  GLY H CA  1 
ATOM   8335  C  C   . GLY H  1 73  ? 73.326  -56.733 14.743 1.00 29.15  ? 72  GLY H C   1 
ATOM   8336  O  O   . GLY H  1 73  ? 72.471  -56.133 15.402 1.00 30.68  ? 72  GLY H O   1 
ATOM   8337  N  N   . GLY H  1 74  ? 74.619  -56.376 14.686 1.00 28.01  ? 73  GLY H N   1 
ATOM   8338  C  CA  . GLY H  1 74  ? 75.084  -55.056 15.087 1.00 25.10  ? 73  GLY H CA  1 
ATOM   8339  C  C   . GLY H  1 74  ? 74.837  -54.051 13.964 1.00 23.41  ? 73  GLY H C   1 
ATOM   8340  O  O   . GLY H  1 74  ? 74.634  -54.447 12.817 1.00 22.29  ? 73  GLY H O   1 
ATOM   8341  N  N   . PRO H  1 75  ? 74.803  -52.726 14.249 1.00 23.79  ? 74  PRO H N   1 
ATOM   8342  C  CA  . PRO H  1 75  ? 74.461  -51.731 13.230 1.00 24.57  ? 74  PRO H CA  1 
ATOM   8343  C  C   . PRO H  1 75  ? 75.349  -51.822 11.994 1.00 25.25  ? 74  PRO H C   1 
ATOM   8344  O  O   . PRO H  1 75  ? 74.905  -51.502 10.896 1.00 24.97  ? 74  PRO H O   1 
ATOM   8345  C  CB  . PRO H  1 75  ? 74.636  -50.374 13.926 1.00 23.84  ? 74  PRO H CB  1 
ATOM   8346  C  CG  . PRO H  1 75  ? 75.381  -50.684 15.209 1.00 22.49  ? 74  PRO H CG  1 
ATOM   8347  C  CD  . PRO H  1 75  ? 75.044  -52.114 15.565 1.00 22.50  ? 74  PRO H CD  1 
ATOM   8348  N  N   . LYS H  1 76  ? 76.589  -52.296 12.173 1.00 27.95  ? 75  LYS H N   1 
ATOM   8349  C  CA  . LYS H  1 76  ? 77.543  -52.284 11.067 1.00 29.43  ? 75  LYS H CA  1 
ATOM   8350  C  C   . LYS H  1 76  ? 77.439  -53.534 10.200 1.00 30.74  ? 75  LYS H C   1 
ATOM   8351  O  O   . LYS H  1 76  ? 78.033  -53.548 9.127  1.00 32.21  ? 75  LYS H O   1 
ATOM   8352  C  CB  . LYS H  1 76  ? 78.962  -51.952 11.526 1.00 33.37  ? 75  LYS H CB  1 
ATOM   8353  C  CG  . LYS H  1 76  ? 79.195  -50.458 11.719 1.00 35.85  ? 75  LYS H CG  1 
ATOM   8354  C  CD  . LYS H  1 76  ? 78.429  -49.548 10.757 1.00 34.17  ? 75  LYS H CD  1 
ATOM   8355  C  CE  . LYS H  1 76  ? 78.942  -48.123 10.869 1.00 36.97  ? 75  LYS H CE  1 
ATOM   8356  N  NZ  . LYS H  1 76  ? 77.876  -47.095 10.791 1.00 41.32  ? 75  LYS H NZ  1 
ATOM   8357  N  N   . ASP H  1 77  ? 76.657  -54.528 10.625 1.00 34.08  ? 76  ASP H N   1 
ATOM   8358  C  CA  . ASP H  1 77  ? 76.494  -55.791 9.903  1.00 35.56  ? 76  ASP H CA  1 
ATOM   8359  C  C   . ASP H  1 77  ? 75.585  -55.608 8.689  1.00 35.26  ? 76  ASP H C   1 
ATOM   8360  O  O   . ASP H  1 77  ? 74.690  -54.758 8.709  1.00 40.32  ? 76  ASP H O   1 
ATOM   8361  C  CB  . ASP H  1 77  ? 75.944  -56.896 10.817 1.00 37.87  ? 76  ASP H CB  1 
ATOM   8362  C  CG  . ASP H  1 77  ? 76.958  -57.346 11.847 1.00 43.11  ? 76  ASP H CG  1 
ATOM   8363  O  OD1 . ASP H  1 77  ? 78.169  -57.306 11.514 1.00 49.52  ? 76  ASP H OD1 1 
ATOM   8364  O  OD2 . ASP H  1 77  ? 76.540  -57.720 12.972 1.00 42.78  ? 76  ASP H OD2 1 
ATOM   8365  N  N   . GLU H  1 78  ? 75.811  -56.405 7.642  1.00 32.63  ? 77  GLU H N   1 
ATOM   8366  C  CA  . GLU H  1 78  ? 74.878  -56.370 6.529  1.00 35.16  ? 77  GLU H CA  1 
ATOM   8367  C  C   . GLU H  1 78  ? 73.609  -57.120 6.927  1.00 38.02  ? 77  GLU H C   1 
ATOM   8368  O  O   . GLU H  1 78  ? 72.502  -56.705 6.581  1.00 42.94  ? 77  GLU H O   1 
ATOM   8369  C  CB  . GLU H  1 78  ? 75.509  -56.872 5.230  1.00 33.53  ? 77  GLU H CB  1 
ATOM   8370  C  CG  . GLU H  1 78  ? 74.464  -56.658 4.029  0.00 85.81  ? 77  GLU H CG  1 
ATOM   8371  C  CD  . GLU H  1 78  ? 74.950  -57.038 2.630  0.00 99.10  ? 77  GLU H CD  1 
ATOM   8372  O  OE1 . GLU H  1 78  ? 76.122  -57.463 2.483  0.00 104.18 ? 77  GLU H OE1 1 
ATOM   8373  O  OE2 . GLU H  1 78  ? 74.159  -56.893 1.677  0.00 108.96 ? 77  GLU H OE2 1 
ATOM   8374  N  N   . GLU H  1 79  ? 73.780  -58.207 7.692  1.00 40.58  ? 78  GLU H N   1 
ATOM   8375  C  CA  . GLU H  1 79  ? 72.666  -58.968 8.237  1.00 40.43  ? 78  GLU H CA  1 
ATOM   8376  C  C   . GLU H  1 79  ? 72.249  -58.339 9.573  1.00 42.13  ? 78  GLU H C   1 
ATOM   8377  O  O   . GLU H  1 79  ? 72.821  -58.631 10.632 1.00 42.88  ? 78  GLU H O   1 
ATOM   8378  C  CB  . GLU H  1 79  ? 73.043  -60.453 8.279  1.00 44.82  ? 78  GLU H CB  1 
ATOM   8379  C  CG  . GLU H  1 79  ? 71.925  -61.416 8.663  1.00 51.06  ? 78  GLU H CG  1 
ATOM   8380  C  CD  . GLU H  1 79  ? 70.784  -61.647 7.681  1.00 57.07  ? 78  GLU H CD  1 
ATOM   8381  O  OE1 . GLU H  1 79  ? 70.852  -61.132 6.537  1.00 61.52  ? 78  GLU H OE1 1 
ATOM   8382  O  OE2 . GLU H  1 79  ? 69.807  -62.344 8.065  1.00 54.50  ? 78  GLU H OE2 1 
ATOM   8383  N  N   . ARG H  1 80  ? 71.247  -57.447 9.504  1.00 37.59  ? 79  ARG H N   1 
ATOM   8384  C  CA  . ARG H  1 80  ? 70.678  -56.807 10.679 1.00 32.39  ? 79  ARG H CA  1 
ATOM   8385  C  C   . ARG H  1 80  ? 69.204  -56.477 10.453 1.00 32.56  ? 79  ARG H C   1 
ATOM   8386  O  O   . ARG H  1 80  ? 68.731  -56.390 9.316  1.00 31.77  ? 79  ARG H O   1 
ATOM   8387  C  CB  . ARG H  1 80  ? 71.408  -55.503 11.001 1.00 29.06  ? 79  ARG H CB  1 
ATOM   8388  C  CG  . ARG H  1 80  ? 71.406  -54.491 9.865  1.00 27.12  ? 79  ARG H CG  1 
ATOM   8389  C  CD  . ARG H  1 80  ? 71.983  -53.172 10.335 1.00 26.86  ? 79  ARG H CD  1 
ATOM   8390  N  NE  . ARG H  1 80  ? 70.958  -52.282 10.870 1.00 25.87  ? 79  ARG H NE  1 
ATOM   8391  C  CZ  . ARG H  1 80  ? 71.124  -50.974 11.114 1.00 26.91  ? 79  ARG H CZ  1 
ATOM   8392  N  NH1 . ARG H  1 80  ? 72.286  -50.385 10.882 1.00 27.73  ? 79  ARG H NH1 1 
ATOM   8393  N  NH2 . ARG H  1 80  ? 70.122  -50.256 11.589 1.00 25.67  ? 79  ARG H NH2 1 
ATOM   8394  N  N   . HIS H  1 81  ? 68.491  -56.294 11.573 1.00 32.31  ? 80  HIS H N   1 
ATOM   8395  C  CA  . HIS H  1 81  ? 67.192  -55.648 11.582 1.00 28.93  ? 80  HIS H CA  1 
ATOM   8396  C  C   . HIS H  1 81  ? 67.395  -54.160 11.304 1.00 28.64  ? 80  HIS H C   1 
ATOM   8397  O  O   . HIS H  1 81  ? 68.392  -53.578 11.737 1.00 28.35  ? 80  HIS H O   1 
ATOM   8398  C  CB  . HIS H  1 81  ? 66.557  -55.806 12.961 1.00 26.85  ? 80  HIS H CB  1 
ATOM   8399  C  CG  . HIS H  1 81  ? 66.346  -57.221 13.365 1.00 24.26  ? 80  HIS H CG  1 
ATOM   8400  N  ND1 . HIS H  1 81  ? 66.466  -57.646 14.684 1.00 23.19  ? 80  HIS H ND1 1 
ATOM   8401  C  CD2 . HIS H  1 81  ? 66.007  -58.304 12.640 1.00 23.54  ? 80  HIS H CD2 1 
ATOM   8402  C  CE1 . HIS H  1 81  ? 66.202  -58.930 14.747 1.00 22.40  ? 80  HIS H CE1 1 
ATOM   8403  N  NE2 . HIS H  1 81  ? 65.929  -59.364 13.506 1.00 22.96  ? 80  HIS H NE2 1 
ATOM   8404  N  N   . VAL H  1 82  ? 66.441  -53.545 10.599 1.00 25.98  ? 81  VAL H N   1 
ATOM   8405  C  CA  . VAL H  1 82  ? 66.491  -52.107 10.392 1.00 25.51  ? 81  VAL H CA  1 
ATOM   8406  C  C   . VAL H  1 82  ? 66.617  -51.404 11.745 1.00 24.67  ? 81  VAL H C   1 
ATOM   8407  O  O   . VAL H  1 82  ? 67.357  -50.437 11.866 1.00 27.52  ? 81  VAL H O   1 
ATOM   8408  C  CB  . VAL H  1 82  ? 65.298  -51.585 9.569  1.00 25.44  ? 81  VAL H CB  1 
ATOM   8409  C  CG1 . VAL H  1 82  ? 65.174  -50.072 9.661  1.00 26.44  ? 81  VAL H CG1 1 
ATOM   8410  C  CG2 . VAL H  1 82  ? 65.400  -52.010 8.114  1.00 25.54  ? 81  VAL H CG2 1 
ATOM   8411  N  N   . GLY H  1 83  ? 65.939  -51.915 12.769 1.00 22.99  ? 82  GLY H N   1 
ATOM   8412  C  CA  . GLY H  1 83  ? 65.911  -51.239 14.054 1.00 24.14  ? 82  GLY H CA  1 
ATOM   8413  C  C   . GLY H  1 83  ? 67.151  -51.486 14.915 1.00 25.81  ? 82  GLY H C   1 
ATOM   8414  O  O   . GLY H  1 83  ? 67.190  -51.015 16.053 1.00 26.02  ? 82  GLY H O   1 
ATOM   8415  N  N   . ASP H  1 84  ? 68.143  -52.211 14.368 1.00 26.98  ? 83  ASP H N   1 
ATOM   8416  C  CA  . ASP H  1 84  ? 69.304  -52.658 15.130 1.00 26.75  ? 83  ASP H CA  1 
ATOM   8417  C  C   . ASP H  1 84  ? 70.345  -51.536 15.243 1.00 26.68  ? 83  ASP H C   1 
ATOM   8418  O  O   . ASP H  1 84  ? 71.171  -51.344 14.345 1.00 26.56  ? 83  ASP H O   1 
ATOM   8419  C  CB  . ASP H  1 84  ? 69.896  -53.939 14.533 1.00 25.88  ? 83  ASP H CB  1 
ATOM   8420  C  CG  . ASP H  1 84  ? 69.095  -55.193 14.833 1.00 27.88  ? 83  ASP H CG  1 
ATOM   8421  O  OD1 . ASP H  1 84  ? 68.252  -55.154 15.757 1.00 28.39  ? 83  ASP H OD1 1 
ATOM   8422  O  OD2 . ASP H  1 84  ? 69.329  -56.211 14.152 1.00 28.43  ? 83  ASP H OD2 1 
ATOM   8423  N  N   . LEU H  1 85  ? 70.324  -50.810 16.368 1.00 25.08  ? 84  LEU H N   1 
ATOM   8424  C  CA  . LEU H  1 85  ? 71.192  -49.655 16.523 1.00 25.41  ? 84  LEU H CA  1 
ATOM   8425  C  C   . LEU H  1 85  ? 72.350  -49.953 17.476 1.00 26.35  ? 84  LEU H C   1 
ATOM   8426  O  O   . LEU H  1 85  ? 73.070  -49.038 17.873 1.00 27.41  ? 84  LEU H O   1 
ATOM   8427  C  CB  . LEU H  1 85  ? 70.373  -48.453 17.007 1.00 25.10  ? 84  LEU H CB  1 
ATOM   8428  C  CG  . LEU H  1 85  ? 69.432  -47.820 15.983 1.00 26.03  ? 84  LEU H CG  1 
ATOM   8429  C  CD1 . LEU H  1 85  ? 68.735  -46.607 16.577 1.00 25.27  ? 84  LEU H CD1 1 
ATOM   8430  C  CD2 . LEU H  1 85  ? 70.167  -47.470 14.697 1.00 26.10  ? 84  LEU H CD2 1 
ATOM   8431  N  N   . GLY H  1 86  ? 72.524  -51.223 17.857 1.00 25.41  ? 85  GLY H N   1 
ATOM   8432  C  CA  . GLY H  1 86  ? 73.663  -51.604 18.676 1.00 24.24  ? 85  GLY H CA  1 
ATOM   8433  C  C   . GLY H  1 86  ? 73.477  -51.215 20.148 1.00 24.68  ? 85  GLY H C   1 
ATOM   8434  O  O   . GLY H  1 86  ? 72.390  -51.386 20.714 1.00 24.34  ? 85  GLY H O   1 
ATOM   8435  N  N   . ASN H  1 87  ? 74.565  -50.706 20.760 1.00 23.03  ? 86  ASN H N   1 
ATOM   8436  C  CA  . ASN H  1 87  ? 74.560  -50.398 22.182 1.00 23.39  ? 86  ASN H CA  1 
ATOM   8437  C  C   . ASN H  1 87  ? 74.772  -48.907 22.429 1.00 23.87  ? 86  ASN H C   1 
ATOM   8438  O  O   . ASN H  1 87  ? 75.298  -48.178 21.584 1.00 24.89  ? 86  ASN H O   1 
ATOM   8439  C  CB  . ASN H  1 87  ? 75.641  -51.162 22.943 1.00 23.32  ? 86  ASN H CB  1 
ATOM   8440  C  CG  . ASN H  1 87  ? 75.369  -52.646 22.978 1.00 23.81  ? 86  ASN H CG  1 
ATOM   8441  O  OD1 . ASN H  1 87  ? 74.500  -53.111 23.711 1.00 22.99  ? 86  ASN H OD1 1 
ATOM   8442  N  ND2 . ASN H  1 87  ? 76.087  -53.392 22.154 1.00 24.87  ? 86  ASN H ND2 1 
ATOM   8443  N  N   . VAL H  1 88  ? 74.341  -48.476 23.614 1.00 22.50  ? 87  VAL H N   1 
ATOM   8444  C  CA  . VAL H  1 88  ? 74.726  -47.186 24.151 1.00 22.88  ? 87  VAL H CA  1 
ATOM   8445  C  C   . VAL H  1 88  ? 75.467  -47.472 25.458 1.00 25.86  ? 87  VAL H C   1 
ATOM   8446  O  O   . VAL H  1 88  ? 75.292  -48.552 26.047 1.00 24.16  ? 87  VAL H O   1 
ATOM   8447  C  CB  . VAL H  1 88  ? 73.514  -46.239 24.322 1.00 20.64  ? 87  VAL H CB  1 
ATOM   8448  C  CG1 . VAL H  1 88  ? 72.780  -46.001 23.003 1.00 19.46  ? 87  VAL H CG1 1 
ATOM   8449  C  CG2 . VAL H  1 88  ? 72.536  -46.730 25.380 1.00 19.97  ? 87  VAL H CG2 1 
ATOM   8450  N  N   . THR H  1 89  ? 76.308  -46.521 25.898 1.00 25.67  ? 88  THR H N   1 
ATOM   8451  C  CA  . THR H  1 89  ? 77.138  -46.782 27.061 1.00 26.22  ? 88  THR H CA  1 
ATOM   8452  C  C   . THR H  1 89  ? 76.787  -45.817 28.182 1.00 26.26  ? 88  THR H C   1 
ATOM   8453  O  O   . THR H  1 89  ? 76.840  -44.608 27.991 1.00 28.00  ? 88  THR H O   1 
ATOM   8454  C  CB  . THR H  1 89  ? 78.627  -46.634 26.728 1.00 27.10  ? 88  THR H CB  1 
ATOM   8455  O  OG1 . THR H  1 89  ? 78.958  -47.474 25.624 1.00 29.22  ? 88  THR H OG1 1 
ATOM   8456  C  CG2 . THR H  1 89  ? 79.523  -46.969 27.896 1.00 25.49  ? 88  THR H CG2 1 
ATOM   8457  N  N   . ALA H  1 90  ? 76.471  -46.362 29.357 1.00 26.89  ? 89  ALA H N   1 
ATOM   8458  C  CA  . ALA H  1 90  ? 76.251  -45.537 30.533 1.00 26.44  ? 89  ALA H CA  1 
ATOM   8459  C  C   . ALA H  1 90  ? 77.541  -45.425 31.352 1.00 28.03  ? 89  ALA H C   1 
ATOM   8460  O  O   . ALA H  1 90  ? 78.196  -46.432 31.622 1.00 27.24  ? 89  ALA H O   1 
ATOM   8461  C  CB  . ALA H  1 90  ? 75.121  -46.116 31.346 1.00 25.08  ? 89  ALA H CB  1 
ATOM   8462  N  N   . ASP H  1 91  ? 77.860  -44.191 31.767 1.00 31.50  ? 90  ASP H N   1 
ATOM   8463  C  CA  . ASP H  1 91  ? 79.014  -43.873 32.596 1.00 35.34  ? 90  ASP H CA  1 
ATOM   8464  C  C   . ASP H  1 91  ? 78.738  -44.268 34.052 1.00 35.50  ? 90  ASP H C   1 
ATOM   8465  O  O   . ASP H  1 91  ? 77.662  -44.784 34.353 1.00 32.25  ? 90  ASP H O   1 
ATOM   8466  C  CB  . ASP H  1 91  ? 79.410  -42.398 32.459 1.00 38.29  ? 90  ASP H CB  1 
ATOM   8467  C  CG  . ASP H  1 91  ? 78.377  -41.388 32.958 1.00 42.96  ? 90  ASP H CG  1 
ATOM   8468  O  OD1 . ASP H  1 91  ? 77.513  -41.754 33.793 1.00 41.39  ? 90  ASP H OD1 1 
ATOM   8469  O  OD2 . ASP H  1 91  ? 78.445  -40.226 32.511 1.00 43.55  ? 90  ASP H OD2 1 
ATOM   8470  N  N   . LYS H  1 92  ? 79.714  -44.010 34.948 1.00 36.11  ? 91  LYS H N   1 
ATOM   8471  C  CA  . LYS H  1 92  ? 79.606  -44.431 36.338 1.00 35.45  ? 91  LYS H CA  1 
ATOM   8472  C  C   . LYS H  1 92  ? 78.408  -43.794 37.032 1.00 34.23  ? 91  LYS H C   1 
ATOM   8473  O  O   . LYS H  1 92  ? 77.997  -44.271 38.084 1.00 34.78  ? 91  LYS H O   1 
ATOM   8474  C  CB  . LYS H  1 92  ? 80.890  -44.154 37.138 1.00 36.36  ? 91  LYS H CB  1 
ATOM   8475  C  CG  . LYS H  1 92  ? 82.041  -45.099 36.888 1.00 38.07  ? 91  LYS H CG  1 
ATOM   8476  C  CD  . LYS H  1 92  ? 82.928  -45.342 38.156 1.00 36.42  ? 91  LYS H CD  1 
ATOM   8477  C  CE  . LYS H  1 92  ? 83.411  -46.775 38.285 1.00 38.21  ? 91  LYS H CE  1 
ATOM   8478  N  NZ  . LYS H  1 92  ? 84.215  -47.187 37.107 1.00 38.27  ? 91  LYS H NZ  1 
ATOM   8479  N  N   . ASP H  1 93  ? 77.855  -42.726 36.442 1.00 34.96  ? 92  ASP H N   1 
ATOM   8480  C  CA  . ASP H  1 93  ? 76.741  -41.999 37.037 1.00 37.03  ? 92  ASP H CA  1 
ATOM   8481  C  C   . ASP H  1 93  ? 75.407  -42.500 36.489 1.00 33.20  ? 92  ASP H C   1 
ATOM   8482  O  O   . ASP H  1 93  ? 74.357  -42.025 36.893 1.00 32.37  ? 92  ASP H O   1 
ATOM   8483  C  CB  . ASP H  1 93  ? 76.834  -40.501 36.762 1.00 41.75  ? 92  ASP H CB  1 
ATOM   8484  C  CG  . ASP H  1 93  ? 78.034  -39.854 37.418 1.00 46.92  ? 92  ASP H CG  1 
ATOM   8485  O  OD1 . ASP H  1 93  ? 78.319  -40.189 38.597 1.00 50.87  ? 92  ASP H OD1 1 
ATOM   8486  O  OD2 . ASP H  1 93  ? 78.657  -39.004 36.745 1.00 50.77  ? 92  ASP H OD2 1 
ATOM   8487  N  N   . GLY H  1 94  ? 75.459  -43.458 35.561 1.00 30.68  ? 93  GLY H N   1 
ATOM   8488  C  CA  . GLY H  1 94  ? 74.245  -44.015 34.997 1.00 27.79  ? 93  GLY H CA  1 
ATOM   8489  C  C   . GLY H  1 94  ? 73.690  -43.154 33.870 1.00 25.94  ? 93  GLY H C   1 
ATOM   8490  O  O   . GLY H  1 94  ? 72.503  -43.234 33.559 1.00 27.80  ? 93  GLY H O   1 
ATOM   8491  N  N   . VAL H  1 95  ? 74.561  -42.344 33.260 1.00 23.86  ? 94  VAL H N   1 
ATOM   8492  C  CA  . VAL H  1 95  ? 74.138  -41.493 32.162 1.00 23.37  ? 94  VAL H CA  1 
ATOM   8493  C  C   . VAL H  1 95  ? 74.780  -41.979 30.867 1.00 22.70  ? 94  VAL H C   1 
ATOM   8494  O  O   . VAL H  1 95  ? 75.995  -42.144 30.795 1.00 23.48  ? 94  VAL H O   1 
ATOM   8495  C  CB  . VAL H  1 95  ? 74.459  -40.009 32.434 1.00 22.13  ? 94  VAL H CB  1 
ATOM   8496  C  CG1 . VAL H  1 95  ? 74.124  -39.129 31.241 1.00 20.67  ? 94  VAL H CG1 1 
ATOM   8497  C  CG2 . VAL H  1 95  ? 73.764  -39.517 33.693 1.00 19.37  ? 94  VAL H CG2 1 
ATOM   8498  N  N   . ALA H  1 96  ? 73.950  -42.178 29.841 1.00 22.58  ? 95  ALA H N   1 
ATOM   8499  C  CA  . ALA H  1 96  ? 74.460  -42.499 28.523 1.00 24.32  ? 95  ALA H CA  1 
ATOM   8500  C  C   . ALA H  1 96  ? 74.318  -41.288 27.620 1.00 25.64  ? 95  ALA H C   1 
ATOM   8501  O  O   . ALA H  1 96  ? 73.200  -40.846 27.370 1.00 28.95  ? 95  ALA H O   1 
ATOM   8502  C  CB  . ALA H  1 96  ? 73.710  -43.674 27.956 1.00 25.41  ? 95  ALA H CB  1 
ATOM   8503  N  N   . ASP H  1 97  ? 75.447  -40.751 27.139 1.00 27.94  ? 96  ASP H N   1 
ATOM   8504  C  CA  . ASP H  1 97  ? 75.376  -39.674 26.161 1.00 31.32  ? 96  ASP H CA  1 
ATOM   8505  C  C   . ASP H  1 97  ? 75.333  -40.297 24.777 1.00 27.77  ? 96  ASP H C   1 
ATOM   8506  O  O   . ASP H  1 97  ? 76.361  -40.631 24.213 1.00 28.34  ? 96  ASP H O   1 
ATOM   8507  C  CB  . ASP H  1 97  ? 76.474  -38.618 26.317 1.00 39.60  ? 96  ASP H CB  1 
ATOM   8508  C  CG  . ASP H  1 97  ? 76.347  -37.836 27.618 1.00 52.58  ? 96  ASP H CG  1 
ATOM   8509  O  OD1 . ASP H  1 97  ? 75.223  -37.322 27.920 1.00 56.39  ? 96  ASP H OD1 1 
ATOM   8510  O  OD2 . ASP H  1 97  ? 77.360  -37.775 28.345 1.00 60.54  ? 96  ASP H OD2 1 
ATOM   8511  N  N   . VAL H  1 98  ? 74.121  -40.462 24.254 1.00 25.31  ? 97  VAL H N   1 
ATOM   8512  C  CA  . VAL H  1 98  ? 73.929  -41.161 23.000 1.00 24.35  ? 97  VAL H CA  1 
ATOM   8513  C  C   . VAL H  1 98  ? 74.342  -40.266 21.839 1.00 25.04  ? 97  VAL H C   1 
ATOM   8514  O  O   . VAL H  1 98  ? 73.999  -39.086 21.783 1.00 26.29  ? 97  VAL H O   1 
ATOM   8515  C  CB  . VAL H  1 98  ? 72.471  -41.610 22.846 1.00 22.95  ? 97  VAL H CB  1 
ATOM   8516  C  CG1 . VAL H  1 98  ? 72.258  -42.378 21.547 1.00 22.41  ? 97  VAL H CG1 1 
ATOM   8517  C  CG2 . VAL H  1 98  ? 72.022  -42.419 24.055 1.00 22.91  ? 97  VAL H CG2 1 
ATOM   8518  N  N   . SER H  1 99  ? 75.075  -40.862 20.901 1.00 26.68  ? 98  SER H N   1 
ATOM   8519  C  CA  . SER H  1 99  ? 75.437  -40.185 19.671 1.00 27.95  ? 98  SER H CA  1 
ATOM   8520  C  C   . SER H  1 99  ? 75.770  -41.232 18.613 1.00 28.19  ? 98  SER H C   1 
ATOM   8521  O  O   . SER H  1 99  ? 76.773  -41.943 18.730 1.00 30.90  ? 98  SER H O   1 
ATOM   8522  C  CB  . SER H  1 99  ? 76.603  -39.276 19.918 1.00 28.68  ? 98  SER H CB  1 
ATOM   8523  O  OG  . SER H  1 99  ? 77.007  -38.682 18.698 1.00 31.64  ? 98  SER H OG  1 
ATOM   8524  N  N   . ILE H  1 100 ? 74.896  -41.352 17.616 1.00 26.44  ? 99  ILE H N   1 
ATOM   8525  C  CA  . ILE H  1 100 ? 74.960  -42.444 16.657 1.00 27.80  ? 99  ILE H CA  1 
ATOM   8526  C  C   . ILE H  1 100 ? 74.670  -41.852 15.289 1.00 27.58  ? 99  ILE H C   1 
ATOM   8527  O  O   . ILE H  1 100 ? 73.904  -40.902 15.172 1.00 25.51  ? 99  ILE H O   1 
ATOM   8528  C  CB  . ILE H  1 100 ? 73.949  -43.561 16.997 1.00 29.28  ? 99  ILE H CB  1 
ATOM   8529  C  CG1 . ILE H  1 100 ? 74.407  -44.393 18.191 1.00 31.47  ? 99  ILE H CG1 1 
ATOM   8530  C  CG2 . ILE H  1 100 ? 73.618  -44.421 15.784 1.00 29.94  ? 99  ILE H CG2 1 
ATOM   8531  C  CD1 . ILE H  1 100 ? 73.396  -45.387 18.674 1.00 33.72  ? 99  ILE H CD1 1 
ATOM   8532  N  N   . GLU H  1 101 ? 75.258  -42.447 14.262 1.00 31.09  ? 100 GLU H N   1 
ATOM   8533  C  CA  . GLU H  1 101 ? 74.848  -42.126 12.913 1.00 35.66  ? 100 GLU H CA  1 
ATOM   8534  C  C   . GLU H  1 101 ? 74.533  -43.443 12.218 1.00 35.54  ? 100 GLU H C   1 
ATOM   8535  O  O   . GLU H  1 101 ? 75.299  -44.398 12.323 1.00 38.70  ? 100 GLU H O   1 
ATOM   8536  C  CB  . GLU H  1 101 ? 75.942  -41.307 12.242 1.00 40.13  ? 100 GLU H CB  1 
ATOM   8537  C  CG  . GLU H  1 101 ? 75.730  -41.118 10.754 1.00 46.38  ? 100 GLU H CG  1 
ATOM   8538  C  CD  . GLU H  1 101 ? 76.504  -39.924 10.204 1.00 52.82  ? 100 GLU H CD  1 
ATOM   8539  O  OE1 . GLU H  1 101 ? 77.067  -40.048 9.103  1.00 54.05  ? 100 GLU H OE1 1 
ATOM   8540  O  OE2 . GLU H  1 101 ? 76.559  -38.880 10.896 1.00 58.96  ? 100 GLU H OE2 1 
ATOM   8541  N  N   . ASP H  1 102 ? 73.366  -43.522 11.584 1.00 34.15  ? 101 ASP H N   1 
ATOM   8542  C  CA  . ASP H  1 102 ? 72.961  -44.781 10.991 1.00 35.55  ? 101 ASP H CA  1 
ATOM   8543  C  C   . ASP H  1 102 ? 72.384  -44.495 9.612  1.00 38.39  ? 101 ASP H C   1 
ATOM   8544  O  O   . ASP H  1 102 ? 71.710  -43.481 9.416  1.00 37.42  ? 101 ASP H O   1 
ATOM   8545  C  CB  . ASP H  1 102 ? 71.953  -45.525 11.858 1.00 34.59  ? 101 ASP H CB  1 
ATOM   8546  C  CG  . ASP H  1 102 ? 71.754  -46.960 11.395 1.00 35.44  ? 101 ASP H CG  1 
ATOM   8547  O  OD1 . ASP H  1 102 ? 72.698  -47.753 11.571 1.00 38.37  ? 101 ASP H OD1 1 
ATOM   8548  O  OD2 . ASP H  1 102 ? 70.681  -47.267 10.825 1.00 33.35  ? 101 ASP H OD2 1 
ATOM   8549  N  N   . SER H  1 103 ? 72.655  -45.403 8.664  1.00 39.20  ? 102 SER H N   1 
ATOM   8550  C  CA  . SER H  1 103 ? 72.221  -45.191 7.298  1.00 37.85  ? 102 SER H CA  1 
ATOM   8551  C  C   . SER H  1 103 ? 71.144  -46.184 6.881  1.00 36.36  ? 102 SER H C   1 
ATOM   8552  O  O   . SER H  1 103 ? 70.739  -46.197 5.724  1.00 38.90  ? 102 SER H O   1 
ATOM   8553  C  CB  . SER H  1 103 ? 73.384  -45.206 6.368  1.00 38.58  ? 102 SER H CB  1 
ATOM   8554  O  OG  . SER H  1 103 ? 73.906  -43.887 6.276  1.00 43.90  ? 102 SER H OG  1 
ATOM   8555  N  N   . VAL H  1 104 ? 70.675  -46.995 7.833  1.00 32.43  ? 103 VAL H N   1 
ATOM   8556  C  CA  . VAL H  1 104 ? 69.701  -48.020 7.513  1.00 30.39  ? 103 VAL H CA  1 
ATOM   8557  C  C   . VAL H  1 104 ? 68.324  -47.540 7.949  1.00 28.53  ? 103 VAL H C   1 
ATOM   8558  O  O   . VAL H  1 104 ? 67.370  -47.669 7.191  1.00 31.21  ? 103 VAL H O   1 
ATOM   8559  C  CB  . VAL H  1 104 ? 70.074  -49.392 8.112  1.00 30.64  ? 103 VAL H CB  1 
ATOM   8560  C  CG1 . VAL H  1 104 ? 68.960  -50.421 7.953  1.00 29.37  ? 103 VAL H CG1 1 
ATOM   8561  C  CG2 . VAL H  1 104 ? 71.367  -49.919 7.518  1.00 27.54  ? 103 VAL H CG2 1 
ATOM   8562  N  N   . ILE H  1 105 ? 68.227  -46.998 9.165  1.00 27.29  ? 104 ILE H N   1 
ATOM   8563  C  CA  . ILE H  1 105 ? 66.993  -46.345 9.570  1.00 26.17  ? 104 ILE H CA  1 
ATOM   8564  C  C   . ILE H  1 105 ? 66.800  -45.115 8.690  1.00 26.18  ? 104 ILE H C   1 
ATOM   8565  O  O   . ILE H  1 105 ? 67.755  -44.611 8.099  1.00 26.49  ? 104 ILE H O   1 
ATOM   8566  C  CB  . ILE H  1 105 ? 66.998  -45.978 11.066 1.00 25.16  ? 104 ILE H CB  1 
ATOM   8567  C  CG1 . ILE H  1 105 ? 68.078  -44.942 11.396 1.00 25.31  ? 104 ILE H CG1 1 
ATOM   8568  C  CG2 . ILE H  1 105 ? 67.104  -47.232 11.914 1.00 24.22  ? 104 ILE H CG2 1 
ATOM   8569  C  CD1 . ILE H  1 105 ? 67.941  -44.322 12.757 1.00 24.25  ? 104 ILE H CD1 1 
ATOM   8570  N  N   . SER H  1 106 ? 65.553  -44.656 8.592  1.00 28.32  ? 105 SER H N   1 
ATOM   8571  C  CA  . SER H  1 106 ? 65.239  -43.452 7.843  1.00 30.08  ? 105 SER H CA  1 
ATOM   8572  C  C   . SER H  1 106 ? 64.102  -42.688 8.512  1.00 29.98  ? 105 SER H C   1 
ATOM   8573  O  O   . SER H  1 106 ? 63.337  -43.267 9.264  1.00 27.13  ? 105 SER H O   1 
ATOM   8574  C  CB  . SER H  1 106 ? 64.913  -43.778 6.420  1.00 30.16  ? 105 SER H CB  1 
ATOM   8575  O  OG  . SER H  1 106 ? 64.948  -42.592 5.658  1.00 30.85  ? 105 SER H OG  1 
ATOM   8576  N  N   . LEU H  1 107 ? 63.989  -41.396 8.210  1.00 31.02  ? 106 LEU H N   1 
ATOM   8577  C  CA  . LEU H  1 107 ? 62.840  -40.612 8.632  1.00 33.43  ? 106 LEU H CA  1 
ATOM   8578  C  C   . LEU H  1 107 ? 61.913  -40.342 7.440  1.00 38.16  ? 106 LEU H C   1 
ATOM   8579  O  O   . LEU H  1 107 ? 60.995  -39.531 7.570  1.00 38.70  ? 106 LEU H O   1 
ATOM   8580  C  CB  . LEU H  1 107 ? 63.309  -39.314 9.300  1.00 29.33  ? 106 LEU H CB  1 
ATOM   8581  C  CG  . LEU H  1 107 ? 64.277  -39.482 10.466 1.00 28.03  ? 106 LEU H CG  1 
ATOM   8582  C  CD1 . LEU H  1 107 ? 64.598  -38.140 11.118 1.00 28.74  ? 106 LEU H CD1 1 
ATOM   8583  C  CD2 . LEU H  1 107 ? 63.724  -40.447 11.498 1.00 27.91  ? 106 LEU H CD2 1 
ATOM   8584  N  N   . SER H  1 108 ? 62.155  -41.004 6.302  1.00 43.42  ? 107 SER H N   1 
ATOM   8585  C  CA  . SER H  1 108 ? 61.209  -41.018 5.193  1.00 52.35  ? 107 SER H CA  1 
ATOM   8586  C  C   . SER H  1 108 ? 61.505  -42.192 4.269  1.00 56.95  ? 107 SER H C   1 
ATOM   8587  O  O   . SER H  1 108 ? 62.686  -42.398 4.035  1.00 64.90  ? 107 SER H O   1 
ATOM   8588  C  CB  . SER H  1 108 ? 61.222  -39.748 4.398  1.00 54.16  ? 107 SER H CB  1 
ATOM   8589  O  OG  . SER H  1 108 ? 62.511  -39.516 3.832  1.00 55.85  ? 107 SER H OG  1 
ATOM   8590  N  N   . GLY H  1 109 ? 60.500  -42.741 3.597  1.00 60.52  ? 108 GLY H N   1 
ATOM   8591  C  CA  . GLY H  1 109 ? 60.715  -43.882 2.725  1.00 60.18  ? 108 GLY H CA  1 
ATOM   8592  C  C   . GLY H  1 109 ? 60.229  -45.186 3.346  1.00 66.62  ? 108 GLY H C   1 
ATOM   8593  O  O   . GLY H  1 109 ? 59.566  -45.186 4.384  1.00 76.19  ? 108 GLY H O   1 
ATOM   8594  N  N   . ASP H  1 110 ? 60.748  -46.292 2.813  1.00 69.15  ? 109 ASP H N   1 
ATOM   8595  C  CA  . ASP H  1 110 ? 60.380  -47.631 3.238  1.00 72.89  ? 109 ASP H CA  1 
ATOM   8596  C  C   . ASP H  1 110 ? 60.799  -47.911 4.680  1.00 69.56  ? 109 ASP H C   1 
ATOM   8597  O  O   . ASP H  1 110 ? 60.217  -48.763 5.332  1.00 61.91  ? 109 ASP H O   1 
ATOM   8598  C  CB  . ASP H  1 110 ? 60.968  -48.684 2.300  1.00 84.23  ? 109 ASP H CB  1 
ATOM   8599  C  CG  . ASP H  1 110 ? 60.521  -48.540 0.864  1.00 95.77  ? 109 ASP H CG  1 
ATOM   8600  O  OD1 . ASP H  1 110 ? 59.313  -48.353 0.639  1.00 101.32 ? 109 ASP H OD1 1 
ATOM   8601  O  OD2 . ASP H  1 110 ? 61.393  -48.611 -0.008 1.00 97.01  ? 109 ASP H OD2 1 
ATOM   8602  N  N   . HIS H  1 111 ? 61.831  -47.235 5.179  1.00 70.20  ? 110 HIS H N   1 
ATOM   8603  C  CA  . HIS H  1 111 ? 62.333  -47.621 6.482  1.00 66.72  ? 110 HIS H CA  1 
ATOM   8604  C  C   . HIS H  1 111 ? 62.016  -46.549 7.517  1.00 61.44  ? 110 HIS H C   1 
ATOM   8605  O  O   . HIS H  1 111 ? 62.753  -46.392 8.476  1.00 68.68  ? 110 HIS H O   1 
ATOM   8606  C  CB  . HIS H  1 111 ? 63.813  -48.024 6.399  1.00 73.96  ? 110 HIS H CB  1 
ATOM   8607  C  CG  . HIS H  1 111 ? 64.106  -49.113 5.414  1.00 81.97  ? 110 HIS H CG  1 
ATOM   8608  N  ND1 . HIS H  1 111 ? 65.350  -49.234 4.814  1.00 80.56  ? 110 HIS H ND1 1 
ATOM   8609  C  CD2 . HIS H  1 111 ? 63.362  -50.138 4.945  1.00 81.01  ? 110 HIS H CD2 1 
ATOM   8610  C  CE1 . HIS H  1 111 ? 65.355  -50.280 4.009  1.00 78.23  ? 110 HIS H CE1 1 
ATOM   8611  N  NE2 . HIS H  1 111 ? 64.137  -50.841 4.063  1.00 79.93  ? 110 HIS H NE2 1 
ATOM   8612  N  N   . CYS H  1 112 ? 60.900  -45.840 7.317  1.00 53.75  ? 111 CYS H N   1 
ATOM   8613  C  CA  . CYS H  1 112 ? 60.519  -44.767 8.215  1.00 46.47  ? 111 CYS H CA  1 
ATOM   8614  C  C   . CYS H  1 112 ? 60.276  -45.352 9.609  1.00 42.29  ? 111 CYS H C   1 
ATOM   8615  O  O   . CYS H  1 112 ? 59.632  -46.377 9.743  1.00 39.93  ? 111 CYS H O   1 
ATOM   8616  C  CB  . CYS H  1 112 ? 59.287  -44.071 7.666  1.00 46.92  ? 111 CYS H CB  1 
ATOM   8617  S  SG  . CYS H  1 112 ? 59.123  -42.329 8.127  1.00 65.98  ? 111 CYS H SG  1 
ATOM   8618  N  N   . ILE H  1 113 ? 60.895  -44.743 10.625 1.00 39.24  ? 112 ILE H N   1 
ATOM   8619  C  CA  . ILE H  1 113 ? 60.793  -45.199 12.002 1.00 35.39  ? 112 ILE H CA  1 
ATOM   8620  C  C   . ILE H  1 113 ? 59.822  -44.303 12.770 1.00 34.61  ? 112 ILE H C   1 
ATOM   8621  O  O   . ILE H  1 113 ? 59.601  -44.519 13.968 1.00 34.63  ? 112 ILE H O   1 
ATOM   8622  C  CB  . ILE H  1 113 ? 62.163  -45.261 12.711 1.00 34.52  ? 112 ILE H CB  1 
ATOM   8623  C  CG1 . ILE H  1 113 ? 62.914  -43.932 12.642 1.00 34.85  ? 112 ILE H CG1 1 
ATOM   8624  C  CG2 . ILE H  1 113 ? 63.011  -46.402 12.182 1.00 35.91  ? 112 ILE H CG2 1 
ATOM   8625  C  CD1 . ILE H  1 113 ? 63.929  -43.743 13.740 1.00 36.85  ? 112 ILE H CD1 1 
ATOM   8626  N  N   . ILE H  1 114 ? 59.245  -43.304 12.085 1.00 30.37  ? 113 ILE H N   1 
ATOM   8627  C  CA  . ILE H  1 114 ? 58.269  -42.428 12.712 1.00 27.30  ? 113 ILE H CA  1 
ATOM   8628  C  C   . ILE H  1 114 ? 57.064  -43.268 13.106 1.00 28.40  ? 113 ILE H C   1 
ATOM   8629  O  O   . ILE H  1 114 ? 56.592  -44.097 12.321 1.00 28.28  ? 113 ILE H O   1 
ATOM   8630  C  CB  . ILE H  1 114 ? 57.861  -41.279 11.782 1.00 25.24  ? 113 ILE H CB  1 
ATOM   8631  C  CG1 . ILE H  1 114 ? 59.091  -40.531 11.269 1.00 24.83  ? 113 ILE H CG1 1 
ATOM   8632  C  CG2 . ILE H  1 114 ? 56.852  -40.366 12.472 1.00 24.24  ? 113 ILE H CG2 1 
ATOM   8633  C  CD1 . ILE H  1 114 ? 58.811  -39.099 10.877 1.00 23.64  ? 113 ILE H CD1 1 
ATOM   8634  N  N   . GLY H  1 115 ? 56.615  -43.060 14.350 1.00 28.98  ? 114 GLY H N   1 
ATOM   8635  C  CA  . GLY H  1 115 ? 55.434  -43.724 14.868 1.00 28.19  ? 114 GLY H CA  1 
ATOM   8636  C  C   . GLY H  1 115 ? 55.724  -45.150 15.325 1.00 27.18  ? 114 GLY H C   1 
ATOM   8637  O  O   . GLY H  1 115 ? 54.793  -45.917 15.555 1.00 28.12  ? 114 GLY H O   1 
ATOM   8638  N  N   . ARG H  1 116 ? 57.015  -45.485 15.455 1.00 25.68  ? 115 ARG H N   1 
ATOM   8639  C  CA  . ARG H  1 116 ? 57.448  -46.747 16.036 1.00 24.61  ? 115 ARG H CA  1 
ATOM   8640  C  C   . ARG H  1 116 ? 58.042  -46.477 17.418 1.00 25.24  ? 115 ARG H C   1 
ATOM   8641  O  O   . ARG H  1 116 ? 57.929  -45.359 17.926 1.00 29.13  ? 115 ARG H O   1 
ATOM   8642  C  CB  . ARG H  1 116 ? 58.344  -47.484 15.043 1.00 23.96  ? 115 ARG H CB  1 
ATOM   8643  C  CG  . ARG H  1 116 ? 57.699  -47.601 13.669 1.00 23.49  ? 115 ARG H CG  1 
ATOM   8644  C  CD  . ARG H  1 116 ? 58.461  -48.517 12.740 1.00 23.86  ? 115 ARG H CD  1 
ATOM   8645  N  NE  . ARG H  1 116 ? 57.814  -48.638 11.433 1.00 25.10  ? 115 ARG H NE  1 
ATOM   8646  C  CZ  . ARG H  1 116 ? 56.880  -49.532 11.112 1.00 24.77  ? 115 ARG H CZ  1 
ATOM   8647  N  NH1 . ARG H  1 116 ? 56.462  -50.420 12.006 1.00 25.23  ? 115 ARG H NH1 1 
ATOM   8648  N  NH2 . ARG H  1 116 ? 56.382  -49.535 9.888  1.00 23.44  ? 115 ARG H NH2 1 
ATOM   8649  N  N   . THR H  1 117 ? 58.632  -47.496 18.056 1.00 22.97  ? 116 THR H N   1 
ATOM   8650  C  CA  . THR H  1 117 ? 59.122  -47.309 19.415 1.00 21.38  ? 116 THR H CA  1 
ATOM   8651  C  C   . THR H  1 117 ? 60.638  -47.441 19.483 1.00 20.61  ? 116 THR H C   1 
ATOM   8652  O  O   . THR H  1 117 ? 61.240  -48.300 18.844 1.00 21.10  ? 116 THR H O   1 
ATOM   8653  C  CB  . THR H  1 117 ? 58.463  -48.281 20.400 1.00 21.84  ? 116 THR H CB  1 
ATOM   8654  O  OG1 . THR H  1 117 ? 57.065  -47.971 20.391 1.00 22.11  ? 116 THR H OG1 1 
ATOM   8655  C  CG2 . THR H  1 117 ? 59.010  -48.162 21.811 1.00 21.05  ? 116 THR H CG2 1 
ATOM   8656  N  N   . LEU H  1 118 ? 61.249  -46.577 20.283 1.00 20.26  ? 117 LEU H N   1 
ATOM   8657  C  CA  . LEU H  1 118 ? 62.649  -46.731 20.624 1.00 20.35  ? 117 LEU H CA  1 
ATOM   8658  C  C   . LEU H  1 118 ? 62.712  -47.328 22.024 1.00 20.61  ? 117 LEU H C   1 
ATOM   8659  O  O   . LEU H  1 118 ? 61.981  -46.884 22.913 1.00 20.83  ? 117 LEU H O   1 
ATOM   8660  C  CB  . LEU H  1 118 ? 63.293  -45.341 20.578 1.00 19.58  ? 117 LEU H CB  1 
ATOM   8661  C  CG  . LEU H  1 118 ? 64.763  -45.298 20.955 1.00 19.29  ? 117 LEU H CG  1 
ATOM   8662  C  CD1 . LEU H  1 118 ? 65.575  -46.053 19.915 1.00 19.14  ? 117 LEU H CD1 1 
ATOM   8663  C  CD2 . LEU H  1 118 ? 65.229  -43.853 21.070 1.00 20.19  ? 117 LEU H CD2 1 
ATOM   8664  N  N   . VAL H  1 119 ? 63.562  -48.348 22.196 1.00 20.40  ? 118 VAL H N   1 
ATOM   8665  C  CA  . VAL H  1 119 ? 63.666  -49.043 23.475 1.00 19.81  ? 118 VAL H CA  1 
ATOM   8666  C  C   . VAL H  1 119 ? 65.129  -49.112 23.903 1.00 19.23  ? 118 VAL H C   1 
ATOM   8667  O  O   . VAL H  1 119 ? 66.011  -49.454 23.107 1.00 18.76  ? 118 VAL H O   1 
ATOM   8668  C  CB  . VAL H  1 119 ? 63.084  -50.467 23.417 1.00 20.06  ? 118 VAL H CB  1 
ATOM   8669  C  CG1 . VAL H  1 119 ? 63.177  -51.164 24.764 1.00 20.91  ? 118 VAL H CG1 1 
ATOM   8670  C  CG2 . VAL H  1 119 ? 61.661  -50.508 22.896 1.00 20.32  ? 118 VAL H CG2 1 
ATOM   8671  N  N   . VAL H  1 120 ? 65.363  -48.830 25.184 1.00 18.89  ? 119 VAL H N   1 
ATOM   8672  C  CA  . VAL H  1 120 ? 66.669  -49.070 25.765 1.00 20.02  ? 119 VAL H CA  1 
ATOM   8673  C  C   . VAL H  1 120 ? 66.541  -50.261 26.714 1.00 22.66  ? 119 VAL H C   1 
ATOM   8674  O  O   . VAL H  1 120 ? 65.661  -50.279 27.578 1.00 20.98  ? 119 VAL H O   1 
ATOM   8675  C  CB  . VAL H  1 120 ? 67.240  -47.813 26.446 1.00 18.56  ? 119 VAL H CB  1 
ATOM   8676  C  CG1 . VAL H  1 120 ? 66.317  -47.276 27.538 1.00 17.76  ? 119 VAL H CG1 1 
ATOM   8677  C  CG2 . VAL H  1 120 ? 68.646  -48.037 26.973 1.00 16.93  ? 119 VAL H CG2 1 
ATOM   8678  N  N   . HIS H  1 121 ? 67.438  -51.245 26.527 1.00 25.05  ? 120 HIS H N   1 
ATOM   8679  C  CA  . HIS H  1 121 ? 67.323  -52.552 27.156 1.00 27.00  ? 120 HIS H CA  1 
ATOM   8680  C  C   . HIS H  1 121 ? 68.211  -52.691 28.392 1.00 28.17  ? 120 HIS H C   1 
ATOM   8681  O  O   . HIS H  1 121 ? 69.063  -51.848 28.667 1.00 28.95  ? 120 HIS H O   1 
ATOM   8682  C  CB  . HIS H  1 121 ? 67.650  -53.647 26.145 1.00 26.63  ? 120 HIS H CB  1 
ATOM   8683  C  CG  . HIS H  1 121 ? 66.584  -53.848 25.126 1.00 26.85  ? 120 HIS H CG  1 
ATOM   8684  N  ND1 . HIS H  1 121 ? 65.565  -54.764 25.300 1.00 26.70  ? 120 HIS H ND1 1 
ATOM   8685  C  CD2 . HIS H  1 121 ? 66.386  -53.274 23.919 1.00 26.08  ? 120 HIS H CD2 1 
ATOM   8686  C  CE1 . HIS H  1 121 ? 64.786  -54.749 24.239 1.00 27.36  ? 120 HIS H CE1 1 
ATOM   8687  N  NE2 . HIS H  1 121 ? 65.274  -53.845 23.366 1.00 26.48  ? 120 HIS H NE2 1 
ATOM   8688  N  N   . GLU H  1 122 ? 68.022  -53.815 29.091 1.00 28.56  ? 121 GLU H N   1 
ATOM   8689  C  CA  . GLU H  1 122 ? 68.566  -54.061 30.413 1.00 29.62  ? 121 GLU H CA  1 
ATOM   8690  C  C   . GLU H  1 122 ? 70.069  -54.345 30.355 1.00 29.16  ? 121 GLU H C   1 
ATOM   8691  O  O   . GLU H  1 122 ? 70.807  -53.849 31.197 1.00 30.11  ? 121 GLU H O   1 
ATOM   8692  C  CB  . GLU H  1 122 ? 67.775  -55.215 31.014 1.00 32.20  ? 121 GLU H CB  1 
ATOM   8693  C  CG  . GLU H  1 122 ? 68.468  -55.957 32.128 1.00 36.88  ? 121 GLU H CG  1 
ATOM   8694  C  CD  . GLU H  1 122 ? 67.805  -57.295 32.389 1.00 40.17  ? 121 GLU H CD  1 
ATOM   8695  O  OE1 . GLU H  1 122 ? 67.796  -57.701 33.568 1.00 41.43  ? 121 GLU H OE1 1 
ATOM   8696  O  OE2 . GLU H  1 122 ? 67.319  -57.927 31.413 1.00 39.49  ? 121 GLU H OE2 1 
ATOM   8697  N  N   . LYS H  1 123 ? 70.502  -55.122 29.353 1.00 29.45  ? 122 LYS H N   1 
ATOM   8698  C  CA  . LYS H  1 123 ? 71.858  -55.643 29.228 1.00 30.75  ? 122 LYS H CA  1 
ATOM   8699  C  C   . LYS H  1 123 ? 72.448  -55.283 27.866 1.00 28.57  ? 122 LYS H C   1 
ATOM   8700  O  O   . LYS H  1 123 ? 71.784  -54.681 27.029 1.00 28.23  ? 122 LYS H O   1 
ATOM   8701  C  CB  . LYS H  1 123 ? 71.843  -57.175 29.304 1.00 35.28  ? 122 LYS H CB  1 
ATOM   8702  C  CG  . LYS H  1 123 ? 71.387  -57.778 30.627 1.00 41.22  ? 122 LYS H CG  1 
ATOM   8703  C  CD  . LYS H  1 123 ? 71.442  -59.301 30.682 1.00 44.60  ? 122 LYS H CD  1 
ATOM   8704  C  CE  . LYS H  1 123 ? 70.325  -59.971 29.907 1.00 49.01  ? 122 LYS H CE  1 
ATOM   8705  N  NZ  . LYS H  1 123 ? 70.357  -61.446 30.073 1.00 54.12  ? 122 LYS H NZ  1 
ATOM   8706  N  N   . ALA H  1 124 ? 73.695  -55.696 27.643 1.00 28.82  ? 123 ALA H N   1 
ATOM   8707  C  CA  . ALA H  1 124 ? 74.380  -55.482 26.377 1.00 30.75  ? 123 ALA H CA  1 
ATOM   8708  C  C   . ALA H  1 124 ? 73.683  -56.255 25.262 1.00 30.44  ? 123 ALA H C   1 
ATOM   8709  O  O   . ALA H  1 124 ? 73.164  -57.340 25.481 1.00 33.27  ? 123 ALA H O   1 
ATOM   8710  C  CB  . ALA H  1 124 ? 75.818  -55.924 26.491 1.00 30.81  ? 123 ALA H CB  1 
ATOM   8711  N  N   . ASP H  1 125 ? 73.679  -55.667 24.068 1.00 30.05  ? 124 ASP H N   1 
ATOM   8712  C  CA  . ASP H  1 125 ? 73.295  -56.366 22.857 1.00 29.51  ? 124 ASP H CA  1 
ATOM   8713  C  C   . ASP H  1 125 ? 74.533  -57.098 22.336 1.00 27.42  ? 124 ASP H C   1 
ATOM   8714  O  O   . ASP H  1 125 ? 75.550  -56.467 22.080 1.00 26.41  ? 124 ASP H O   1 
ATOM   8715  C  CB  . ASP H  1 125 ? 72.722  -55.352 21.860 1.00 32.39  ? 124 ASP H CB  1 
ATOM   8716  C  CG  . ASP H  1 125 ? 72.414  -55.910 20.478 1.00 34.42  ? 124 ASP H CG  1 
ATOM   8717  O  OD1 . ASP H  1 125 ? 72.713  -57.104 20.228 1.00 35.94  ? 124 ASP H OD1 1 
ATOM   8718  O  OD2 . ASP H  1 125 ? 71.876  -55.143 19.653 1.00 32.43  ? 124 ASP H OD2 1 
ATOM   8719  N  N   . ASP H  1 126 ? 74.439  -58.420 22.166 1.00 24.90  ? 125 ASP H N   1 
ATOM   8720  C  CA  . ASP H  1 126 ? 75.596  -59.212 21.768 1.00 23.52  ? 125 ASP H CA  1 
ATOM   8721  C  C   . ASP H  1 126 ? 75.808  -59.157 20.251 1.00 22.92  ? 125 ASP H C   1 
ATOM   8722  O  O   . ASP H  1 126 ? 76.680  -59.854 19.722 1.00 22.12  ? 125 ASP H O   1 
ATOM   8723  C  CB  . ASP H  1 126 ? 75.567  -60.627 22.358 1.00 21.36  ? 125 ASP H CB  1 
ATOM   8724  C  CG  . ASP H  1 126 ? 74.536  -61.568 21.753 1.00 22.10  ? 125 ASP H CG  1 
ATOM   8725  O  OD1 . ASP H  1 126 ? 74.112  -61.336 20.586 1.00 21.72  ? 125 ASP H OD1 1 
ATOM   8726  O  OD2 . ASP H  1 126 ? 74.174  -62.558 22.451 1.00 21.69  ? 125 ASP H OD2 1 
ATOM   8727  N  N   . LEU H  1 127 ? 75.017  -58.322 19.561 1.00 21.22  ? 126 LEU H N   1 
ATOM   8728  C  CA  . LEU H  1 127 ? 75.185  -58.052 18.139 1.00 22.55  ? 126 LEU H CA  1 
ATOM   8729  C  C   . LEU H  1 127 ? 75.075  -59.342 17.318 1.00 24.11  ? 126 LEU H C   1 
ATOM   8730  O  O   . LEU H  1 127 ? 75.567  -59.406 16.190 1.00 24.67  ? 126 LEU H O   1 
ATOM   8731  C  CB  . LEU H  1 127 ? 76.518  -57.340 17.875 1.00 22.67  ? 126 LEU H CB  1 
ATOM   8732  C  CG  . LEU H  1 127 ? 76.833  -56.147 18.788 1.00 22.50  ? 126 LEU H CG  1 
ATOM   8733  C  CD1 . LEU H  1 127 ? 78.189  -55.532 18.534 1.00 21.26  ? 126 LEU H CD1 1 
ATOM   8734  C  CD2 . LEU H  1 127 ? 75.714  -55.130 18.796 1.00 22.08  ? 126 LEU H CD2 1 
ATOM   8735  N  N   . GLY H  1 128 ? 74.420  -60.360 17.892 1.00 25.65  ? 127 GLY H N   1 
ATOM   8736  C  CA  . GLY H  1 128 ? 74.044  -61.568 17.171 1.00 26.48  ? 127 GLY H CA  1 
ATOM   8737  C  C   . GLY H  1 128 ? 75.144  -62.623 17.170 1.00 28.76  ? 127 GLY H C   1 
ATOM   8738  O  O   . GLY H  1 128 ? 75.097  -63.560 16.382 1.00 27.87  ? 127 GLY H O   1 
ATOM   8739  N  N   . LYS H  1 129 ? 76.118  -62.472 18.073 1.00 32.81  ? 128 LYS H N   1 
ATOM   8740  C  CA  . LYS H  1 129 ? 77.301  -63.321 18.079 1.00 32.89  ? 128 LYS H CA  1 
ATOM   8741  C  C   . LYS H  1 129 ? 77.355  -64.127 19.374 1.00 32.32  ? 128 LYS H C   1 
ATOM   8742  O  O   . LYS H  1 129 ? 78.441  -64.432 19.871 1.00 32.73  ? 128 LYS H O   1 
ATOM   8743  C  CB  . LYS H  1 129 ? 78.563  -62.457 17.959 1.00 33.59  ? 128 LYS H CB  1 
ATOM   8744  C  CG  . LYS H  1 129 ? 78.582  -61.488 16.794 1.00 36.86  ? 128 LYS H CG  1 
ATOM   8745  C  CD  . LYS H  1 129 ? 80.016  -61.125 16.401 1.00 42.16  ? 128 LYS H CD  1 
ATOM   8746  C  CE  . LYS H  1 129 ? 80.156  -60.776 14.936 1.00 44.57  ? 128 LYS H CE  1 
ATOM   8747  N  NZ  . LYS H  1 129 ? 79.151  -59.756 14.534 1.00 49.73  ? 128 LYS H NZ  1 
ATOM   8748  N  N   . GLY H  1 130 ? 76.179  -64.460 19.923 1.00 31.11  ? 129 GLY H N   1 
ATOM   8749  C  CA  . GLY H  1 130 ? 76.087  -65.123 21.218 1.00 27.47  ? 129 GLY H CA  1 
ATOM   8750  C  C   . GLY H  1 130 ? 75.922  -66.632 21.103 1.00 26.62  ? 129 GLY H C   1 
ATOM   8751  O  O   . GLY H  1 130 ? 75.958  -67.334 22.107 1.00 24.66  ? 129 GLY H O   1 
ATOM   8752  N  N   . GLY H  1 131 ? 75.701  -67.104 19.872 1.00 28.75  ? 130 GLY H N   1 
ATOM   8753  C  CA  . GLY H  1 131 ? 75.680  -68.520 19.539 1.00 30.88  ? 130 GLY H CA  1 
ATOM   8754  C  C   . GLY H  1 131 ? 74.463  -69.254 20.096 1.00 33.72  ? 130 GLY H C   1 
ATOM   8755  O  O   . GLY H  1 131 ? 74.511  -70.468 20.299 1.00 34.52  ? 130 GLY H O   1 
ATOM   8756  N  N   . ASN H  1 132 ? 73.380  -68.523 20.370 1.00 35.41  ? 131 ASN H N   1 
ATOM   8757  C  CA  . ASN H  1 132 ? 72.112  -69.148 20.710 1.00 33.68  ? 131 ASN H CA  1 
ATOM   8758  C  C   . ASN H  1 132 ? 71.017  -68.530 19.853 1.00 33.93  ? 131 ASN H C   1 
ATOM   8759  O  O   . ASN H  1 132 ? 71.257  -67.589 19.097 1.00 31.71  ? 131 ASN H O   1 
ATOM   8760  C  CB  . ASN H  1 132 ? 71.813  -69.143 22.215 1.00 33.60  ? 131 ASN H CB  1 
ATOM   8761  C  CG  . ASN H  1 132 ? 71.766  -67.773 22.842 1.00 35.98  ? 131 ASN H CG  1 
ATOM   8762  O  OD1 . ASN H  1 132 ? 71.584  -66.772 22.157 1.00 43.79  ? 131 ASN H OD1 1 
ATOM   8763  N  ND2 . ASN H  1 132 ? 71.970  -67.716 24.150 1.00 38.67  ? 131 ASN H ND2 1 
ATOM   8764  N  N   . GLU H  1 133 ? 69.804  -69.079 19.978 1.00 38.39  ? 132 GLU H N   1 
ATOM   8765  C  CA  . GLU H  1 133 ? 68.733  -68.665 19.084 1.00 40.55  ? 132 GLU H CA  1 
ATOM   8766  C  C   . GLU H  1 133 ? 68.316  -67.247 19.435 1.00 39.30  ? 132 GLU H C   1 
ATOM   8767  O  O   . GLU H  1 133 ? 68.042  -66.436 18.554 1.00 38.07  ? 132 GLU H O   1 
ATOM   8768  C  CB  . GLU H  1 133 ? 67.641  -69.705 18.977 1.00 42.70  ? 132 GLU H CB  1 
ATOM   8769  C  CG  . GLU H  1 133 ? 66.485  -69.689 19.967 1.00 50.23  ? 132 GLU H CG  1 
ATOM   8770  C  CD  . GLU H  1 133 ? 65.205  -70.271 19.386 1.00 53.93  ? 132 GLU H CD  1 
ATOM   8771  O  OE1 . GLU H  1 133 ? 64.926  -70.038 18.174 1.00 51.27  ? 132 GLU H OE1 1 
ATOM   8772  O  OE2 . GLU H  1 133 ? 64.457  -70.955 20.151 1.00 60.60  ? 132 GLU H OE2 1 
ATOM   8773  N  N   . GLU H  1 134 ? 68.321  -66.977 20.740 1.00 36.66  ? 133 GLU H N   1 
ATOM   8774  C  CA  . GLU H  1 134 ? 67.997  -65.671 21.300 1.00 36.72  ? 133 GLU H CA  1 
ATOM   8775  C  C   . GLU H  1 134 ? 68.877  -64.586 20.671 1.00 34.23  ? 133 GLU H C   1 
ATOM   8776  O  O   . GLU H  1 134 ? 68.391  -63.505 20.330 1.00 33.76  ? 133 GLU H O   1 
ATOM   8777  C  CB  . GLU H  1 134 ? 68.145  -65.750 22.821 1.00 42.12  ? 133 GLU H CB  1 
ATOM   8778  C  CG  . GLU H  1 134 ? 67.384  -64.683 23.584 1.00 47.24  ? 133 GLU H CG  1 
ATOM   8779  C  CD  . GLU H  1 134 ? 65.959  -64.353 23.163 1.00 50.64  ? 133 GLU H CD  1 
ATOM   8780  O  OE1 . GLU H  1 134 ? 65.223  -65.256 22.693 1.00 51.82  ? 133 GLU H OE1 1 
ATOM   8781  O  OE2 . GLU H  1 134 ? 65.595  -63.163 23.285 1.00 49.97  ? 133 GLU H OE2 1 
ATOM   8782  N  N   . SER H  1 135 ? 70.171  -64.888 20.513 1.00 31.80  ? 134 SER H N   1 
ATOM   8783  C  CA  . SER H  1 135 ? 71.130  -63.930 19.988 1.00 29.37  ? 134 SER H CA  1 
ATOM   8784  C  C   . SER H  1 135 ? 70.680  -63.406 18.629 1.00 29.17  ? 134 SER H C   1 
ATOM   8785  O  O   . SER H  1 135 ? 70.809  -62.218 18.356 1.00 27.16  ? 134 SER H O   1 
ATOM   8786  C  CB  . SER H  1 135 ? 72.524  -64.512 19.925 1.00 27.37  ? 134 SER H CB  1 
ATOM   8787  O  OG  . SER H  1 135 ? 73.467  -63.543 19.499 1.00 26.66  ? 134 SER H OG  1 
ATOM   8788  N  N   . THR H  1 136 ? 70.143  -64.283 17.783 1.00 32.08  ? 135 THR H N   1 
ATOM   8789  C  CA  . THR H  1 136 ? 69.840  -63.867 16.419 1.00 33.40  ? 135 THR H CA  1 
ATOM   8790  C  C   . THR H  1 136 ? 68.460  -63.220 16.330 1.00 31.77  ? 135 THR H C   1 
ATOM   8791  O  O   . THR H  1 136 ? 68.032  -62.851 15.238 1.00 30.03  ? 135 THR H O   1 
ATOM   8792  C  CB  . THR H  1 136 ? 69.948  -65.030 15.422 1.00 33.92  ? 135 THR H CB  1 
ATOM   8793  O  OG1 . THR H  1 136 ? 68.933  -65.958 15.791 1.00 34.89  ? 135 THR H OG1 1 
ATOM   8794  C  CG2 . THR H  1 136 ? 71.287  -65.725 15.439 1.00 33.85  ? 135 THR H CG2 1 
ATOM   8795  N  N   . LYS H  1 137 ? 67.776  -63.090 17.475 1.00 31.80  ? 136 LYS H N   1 
ATOM   8796  C  CA  . LYS H  1 137 ? 66.485  -62.418 17.532 1.00 30.29  ? 136 LYS H CA  1 
ATOM   8797  C  C   . LYS H  1 137 ? 66.610  -61.068 18.244 1.00 26.24  ? 136 LYS H C   1 
ATOM   8798  O  O   . LYS H  1 137 ? 66.225  -60.032 17.697 1.00 23.55  ? 136 LYS H O   1 
ATOM   8799  C  CB  . LYS H  1 137 ? 65.440  -63.294 18.225 1.00 34.60  ? 136 LYS H CB  1 
ATOM   8800  C  CG  . LYS H  1 137 ? 64.832  -64.391 17.365 1.00 39.61  ? 136 LYS H CG  1 
ATOM   8801  C  CD  . LYS H  1 137 ? 63.931  -65.335 18.109 1.00 45.40  ? 136 LYS H CD  1 
ATOM   8802  C  CE  . LYS H  1 137 ? 63.440  -66.426 17.182 1.00 51.97  ? 136 LYS H CE  1 
ATOM   8803  N  NZ  . LYS H  1 137 ? 62.608  -67.404 17.916 1.00 60.30  ? 136 LYS H NZ  1 
ATOM   8804  N  N   . THR H  1 138 ? 67.165  -61.088 19.463 1.00 22.99  ? 137 THR H N   1 
ATOM   8805  C  CA  . THR H  1 138 ? 67.115  -59.918 20.329 1.00 22.55  ? 137 THR H CA  1 
ATOM   8806  C  C   . THR H  1 138 ? 68.505  -59.477 20.777 1.00 22.00  ? 137 THR H C   1 
ATOM   8807  O  O   . THR H  1 138 ? 68.621  -58.511 21.526 1.00 22.22  ? 137 THR H O   1 
ATOM   8808  C  CB  . THR H  1 138 ? 66.293  -60.229 21.587 1.00 22.70  ? 137 THR H CB  1 
ATOM   8809  O  OG1 . THR H  1 138 ? 67.030  -61.111 22.440 1.00 22.67  ? 137 THR H OG1 1 
ATOM   8810  C  CG2 . THR H  1 138 ? 64.942  -60.820 21.251 1.00 21.03  ? 137 THR H CG2 1 
ATOM   8811  N  N   . GLY H  1 139 ? 69.539  -60.214 20.360 1.00 21.45  ? 138 GLY H N   1 
ATOM   8812  C  CA  . GLY H  1 139 ? 70.896  -59.970 20.814 1.00 21.88  ? 138 GLY H CA  1 
ATOM   8813  C  C   . GLY H  1 139 ? 71.066  -60.151 22.323 1.00 22.93  ? 138 GLY H C   1 
ATOM   8814  O  O   . GLY H  1 139 ? 72.085  -59.750 22.877 1.00 22.91  ? 138 GLY H O   1 
ATOM   8815  N  N   . ASN H  1 140 ? 70.073  -60.753 22.990 1.00 24.30  ? 139 ASN H N   1 
ATOM   8816  C  CA  . ASN H  1 140 ? 70.192  -61.125 24.395 1.00 26.45  ? 139 ASN H CA  1 
ATOM   8817  C  C   . ASN H  1 140 ? 70.227  -59.874 25.265 1.00 28.06  ? 139 ASN H C   1 
ATOM   8818  O  O   . ASN H  1 140 ? 70.789  -59.900 26.359 1.00 30.37  ? 139 ASN H O   1 
ATOM   8819  C  CB  . ASN H  1 140 ? 71.409  -62.014 24.680 1.00 26.68  ? 139 ASN H CB  1 
ATOM   8820  C  CG  . ASN H  1 140 ? 71.222  -63.454 24.248 1.00 28.62  ? 139 ASN H CG  1 
ATOM   8821  O  OD1 . ASN H  1 140 ? 70.419  -64.183 24.819 1.00 31.14  ? 139 ASN H OD1 1 
ATOM   8822  N  ND2 . ASN H  1 140 ? 71.962  -63.876 23.235 1.00 28.49  ? 139 ASN H ND2 1 
ATOM   8823  N  N   . ALA H  1 141 ? 69.597  -58.795 24.786 1.00 27.52  ? 140 ALA H N   1 
ATOM   8824  C  CA  . ALA H  1 141 ? 69.694  -57.494 25.434 1.00 27.02  ? 140 ALA H CA  1 
ATOM   8825  C  C   . ALA H  1 141 ? 68.834  -57.434 26.699 1.00 27.12  ? 140 ALA H C   1 
ATOM   8826  O  O   . ALA H  1 141 ? 68.895  -56.462 27.456 1.00 25.87  ? 140 ALA H O   1 
ATOM   8827  C  CB  . ALA H  1 141 ? 69.315  -56.412 24.457 1.00 27.11  ? 140 ALA H CB  1 
ATOM   8828  N  N   . GLY H  1 142 ? 68.029  -58.483 26.927 1.00 26.58  ? 141 GLY H N   1 
ATOM   8829  C  CA  . GLY H  1 142 ? 67.230  -58.543 28.138 1.00 26.35  ? 141 GLY H CA  1 
ATOM   8830  C  C   . GLY H  1 142 ? 66.019  -57.618 28.051 1.00 26.11  ? 141 GLY H C   1 
ATOM   8831  O  O   . GLY H  1 142 ? 65.579  -57.278 26.952 1.00 27.84  ? 141 GLY H O   1 
ATOM   8832  N  N   . SER H  1 143 ? 65.514  -57.212 29.221 1.00 24.71  ? 142 SER H N   1 
ATOM   8833  C  CA  . SER H  1 143 ? 64.221  -56.553 29.328 1.00 24.94  ? 142 SER H CA  1 
ATOM   8834  C  C   . SER H  1 143 ? 64.279  -55.122 28.797 1.00 25.72  ? 142 SER H C   1 
ATOM   8835  O  O   . SER H  1 143 ? 65.358  -54.602 28.495 1.00 25.32  ? 142 SER H O   1 
ATOM   8836  C  CB  . SER H  1 143 ? 63.701  -56.594 30.741 1.00 25.09  ? 142 SER H CB  1 
ATOM   8837  O  OG  . SER H  1 143 ? 64.547  -55.854 31.602 1.00 25.31  ? 142 SER H OG  1 
ATOM   8838  N  N   . ARG H  1 144 ? 63.091  -54.507 28.709 1.00 26.32  ? 143 ARG H N   1 
ATOM   8839  C  CA  . ARG H  1 144 ? 62.895  -53.171 28.164 1.00 25.59  ? 143 ARG H CA  1 
ATOM   8840  C  C   . ARG H  1 144 ? 62.822  -52.185 29.327 1.00 25.48  ? 143 ARG H C   1 
ATOM   8841  O  O   . ARG H  1 144 ? 61.852  -52.180 30.070 1.00 28.32  ? 143 ARG H O   1 
ATOM   8842  C  CB  . ARG H  1 144 ? 61.619  -53.157 27.316 1.00 24.12  ? 143 ARG H CB  1 
ATOM   8843  C  CG  . ARG H  1 144 ? 61.634  -54.196 26.199 1.00 23.89  ? 143 ARG H CG  1 
ATOM   8844  C  CD  . ARG H  1 144 ? 60.294  -54.402 25.495 1.00 23.60  ? 143 ARG H CD  1 
ATOM   8845  N  NE  . ARG H  1 144 ? 60.411  -55.452 24.488 1.00 24.31  ? 143 ARG H NE  1 
ATOM   8846  C  CZ  . ARG H  1 144 ? 59.669  -55.559 23.384 1.00 25.15  ? 143 ARG H CZ  1 
ATOM   8847  N  NH1 . ARG H  1 144 ? 58.740  -54.667 23.096 1.00 26.39  ? 143 ARG H NH1 1 
ATOM   8848  N  NH2 . ARG H  1 144 ? 59.860  -56.557 22.551 1.00 24.97  ? 143 ARG H NH2 1 
ATOM   8849  N  N   . LEU H  1 145 ? 63.866  -51.376 29.513 1.00 25.05  ? 144 LEU H N   1 
ATOM   8850  C  CA  . LEU H  1 145 ? 63.941  -50.542 30.700 1.00 25.43  ? 144 LEU H CA  1 
ATOM   8851  C  C   . LEU H  1 145 ? 63.071  -49.302 30.514 1.00 25.24  ? 144 LEU H C   1 
ATOM   8852  O  O   . LEU H  1 145 ? 62.429  -48.839 31.458 1.00 23.89  ? 144 LEU H O   1 
ATOM   8853  C  CB  . LEU H  1 145 ? 65.406  -50.171 30.948 1.00 25.47  ? 144 LEU H CB  1 
ATOM   8854  C  CG  . LEU H  1 145 ? 66.287  -51.310 31.463 1.00 26.21  ? 144 LEU H CG  1 
ATOM   8855  C  CD1 . LEU H  1 145 ? 67.688  -50.814 31.783 1.00 25.19  ? 144 LEU H CD1 1 
ATOM   8856  C  CD2 . LEU H  1 145 ? 65.670  -51.995 32.676 1.00 24.60  ? 144 LEU H CD2 1 
ATOM   8857  N  N   . ALA H  1 146 ? 63.067  -48.773 29.285 1.00 24.54  ? 145 ALA H N   1 
ATOM   8858  C  CA  . ALA H  1 146 ? 62.308  -47.579 28.955 1.00 24.29  ? 145 ALA H CA  1 
ATOM   8859  C  C   . ALA H  1 146 ? 62.110  -47.512 27.442 1.00 24.79  ? 145 ALA H C   1 
ATOM   8860  O  O   . ALA H  1 146 ? 62.926  -48.018 26.664 1.00 26.27  ? 145 ALA H O   1 
ATOM   8861  C  CB  . ALA H  1 146 ? 63.020  -46.351 29.472 1.00 24.85  ? 145 ALA H CB  1 
ATOM   8862  N  N   . CYS H  1 147 ? 61.011  -46.868 27.043 1.00 23.93  ? 146 CYS H N   1 
ATOM   8863  C  CA  . CYS H  1 147 ? 60.693  -46.739 25.634 1.00 24.00  ? 146 CYS H CA  1 
ATOM   8864  C  C   . CYS H  1 147 ? 59.849  -45.488 25.436 1.00 22.19  ? 146 CYS H C   1 
ATOM   8865  O  O   . CYS H  1 147 ? 59.443  -44.857 26.406 1.00 20.80  ? 146 CYS H O   1 
ATOM   8866  C  CB  . CYS H  1 147 ? 59.942  -47.970 25.138 1.00 26.34  ? 146 CYS H CB  1 
ATOM   8867  S  SG  . CYS H  1 147 ? 58.401  -48.288 26.044 1.00 29.67  ? 146 CYS H SG  1 
ATOM   8868  N  N   . GLY H  1 148 ? 59.628  -45.146 24.165 1.00 21.00  ? 147 GLY H N   1 
ATOM   8869  C  CA  . GLY H  1 148 ? 58.740  -44.068 23.772 1.00 21.41  ? 147 GLY H CA  1 
ATOM   8870  C  C   . GLY H  1 148 ? 58.367  -44.196 22.296 1.00 22.32  ? 147 GLY H C   1 
ATOM   8871  O  O   . GLY H  1 148 ? 59.073  -44.842 21.514 1.00 22.92  ? 147 GLY H O   1 
ATOM   8872  N  N   . VAL H  1 149 ? 57.253  -43.572 21.914 1.00 22.17  ? 148 VAL H N   1 
ATOM   8873  C  CA  . VAL H  1 149 ? 56.910  -43.520 20.505 1.00 20.95  ? 148 VAL H CA  1 
ATOM   8874  C  C   . VAL H  1 149 ? 57.729  -42.411 19.848 1.00 20.99  ? 148 VAL H C   1 
ATOM   8875  O  O   . VAL H  1 149 ? 57.963  -41.355 20.435 1.00 20.42  ? 148 VAL H O   1 
ATOM   8876  C  CB  . VAL H  1 149 ? 55.394  -43.364 20.294 1.00 20.26  ? 148 VAL H CB  1 
ATOM   8877  C  CG1 . VAL H  1 149 ? 55.024  -43.443 18.826 1.00 20.28  ? 148 VAL H CG1 1 
ATOM   8878  C  CG2 . VAL H  1 149 ? 54.643  -44.426 21.076 1.00 20.24  ? 148 VAL H CG2 1 
ATOM   8879  N  N   . ILE H  1 150 ? 58.188  -42.693 18.631 1.00 21.38  ? 149 ILE H N   1 
ATOM   8880  C  CA  . ILE H  1 150 ? 59.048  -41.789 17.889 1.00 22.88  ? 149 ILE H CA  1 
ATOM   8881  C  C   . ILE H  1 150 ? 58.144  -40.839 17.113 1.00 23.40  ? 149 ILE H C   1 
ATOM   8882  O  O   . ILE H  1 150 ? 57.434  -41.272 16.207 1.00 24.02  ? 149 ILE H O   1 
ATOM   8883  C  CB  . ILE H  1 150 ? 59.946  -42.608 16.940 1.00 23.07  ? 149 ILE H CB  1 
ATOM   8884  C  CG1 . ILE H  1 150 ? 60.903  -43.523 17.707 1.00 22.66  ? 149 ILE H CG1 1 
ATOM   8885  C  CG2 . ILE H  1 150 ? 60.681  -41.706 15.961 1.00 22.83  ? 149 ILE H CG2 1 
ATOM   8886  C  CD1 . ILE H  1 150 ? 61.520  -44.598 16.847 1.00 21.94  ? 149 ILE H CD1 1 
ATOM   8887  N  N   . GLY H  1 151 ? 58.191  -39.552 17.471 1.00 22.80  ? 150 GLY H N   1 
ATOM   8888  C  CA  . GLY H  1 151 ? 57.234  -38.574 16.971 1.00 23.13  ? 150 GLY H CA  1 
ATOM   8889  C  C   . GLY H  1 151 ? 57.883  -37.385 16.270 1.00 23.71  ? 150 GLY H C   1 
ATOM   8890  O  O   . GLY H  1 151 ? 59.077  -37.143 16.424 1.00 24.62  ? 150 GLY H O   1 
ATOM   8891  N  N   . ILE H  1 152 ? 57.067  -36.645 15.508 1.00 24.85  ? 151 ILE H N   1 
ATOM   8892  C  CA  . ILE H  1 152 ? 57.529  -35.517 14.715 1.00 26.67  ? 151 ILE H CA  1 
ATOM   8893  C  C   . ILE H  1 152 ? 57.786  -34.343 15.651 1.00 30.05  ? 151 ILE H C   1 
ATOM   8894  O  O   . ILE H  1 152 ? 56.962  -34.064 16.511 1.00 31.35  ? 151 ILE H O   1 
ATOM   8895  C  CB  . ILE H  1 152 ? 56.488  -35.170 13.637 1.00 24.58  ? 151 ILE H CB  1 
ATOM   8896  C  CG1 . ILE H  1 152 ? 56.357  -36.305 12.624 1.00 24.17  ? 151 ILE H CG1 1 
ATOM   8897  C  CG2 . ILE H  1 152 ? 56.831  -33.869 12.956 1.00 23.00  ? 151 ILE H CG2 1 
ATOM   8898  C  CD1 . ILE H  1 152 ? 55.073  -36.299 11.843 1.00 25.50  ? 151 ILE H CD1 1 
ATOM   8899  N  N   . ALA H  1 153 ? 58.940  -33.681 15.468 1.00 33.80  ? 152 ALA H N   1 
ATOM   8900  C  CA  . ALA H  1 153 ? 59.341  -32.533 16.271 1.00 35.82  ? 152 ALA H CA  1 
ATOM   8901  C  C   . ALA H  1 153 ? 59.429  -31.294 15.383 1.00 41.42  ? 152 ALA H C   1 
ATOM   8902  O  O   . ALA H  1 153 ? 59.397  -31.404 14.154 1.00 38.96  ? 152 ALA H O   1 
ATOM   8903  C  CB  . ALA H  1 153 ? 60.656  -32.822 16.939 1.00 31.89  ? 152 ALA H CB  1 
ATOM   8904  N  N   . GLN H  1 154 ? 59.558  -30.119 16.016 1.00 52.06  ? 153 GLN H N   1 
ATOM   8905  C  CA  . GLN H  1 154 ? 59.591  -28.859 15.283 1.00 59.40  ? 153 GLN H CA  1 
ATOM   8906  C  C   . GLN H  1 154 ? 60.898  -28.690 14.488 1.00 58.50  ? 153 GLN H C   1 
ATOM   8907  O  O   . GLN H  1 154 ? 62.013  -28.824 15.013 1.00 55.39  ? 153 GLN H O   1 
ATOM   8908  C  CB  . GLN H  1 154 ? 59.383  -27.650 16.195 1.00 60.44  ? 153 GLN H CB  1 
ATOM   8909  C  CG  . GLN H  1 154 ? 59.381  -26.351 15.400 1.00 61.61  ? 153 GLN H CG  1 
ATOM   8910  C  CD  . GLN H  1 154 ? 58.689  -25.228 16.115 1.00 67.45  ? 153 GLN H CD  1 
ATOM   8911  O  OE1 . GLN H  1 154 ? 59.021  -24.887 17.247 1.00 74.24  ? 153 GLN H OE1 1 
ATOM   8912  N  NE2 . GLN H  1 154 ? 57.719  -24.639 15.439 1.00 72.38  ? 153 GLN H NE2 1 
ATOM   8913  O  OXT . GLN H  1 154 ? 60.840  -28.379 13.293 1.00 54.77  ? 153 GLN H OXT 1 
ATOM   8914  N  N   . ALA I  1 2   ? 38.381  20.180  67.469 1.00 71.66  ? 1   ALA I N   1 
ATOM   8915  C  CA  . ALA I  1 2   ? 38.043  18.798  67.870 1.00 70.46  ? 1   ALA I CA  1 
ATOM   8916  C  C   . ALA I  1 2   ? 37.136  18.158  66.824 1.00 65.19  ? 1   ALA I C   1 
ATOM   8917  O  O   . ALA I  1 2   ? 37.368  16.991  66.510 1.00 70.86  ? 1   ALA I O   1 
ATOM   8918  C  CB  . ALA I  1 2   ? 37.488  18.717  69.289 1.00 68.92  ? 1   ALA I CB  1 
ATOM   8919  N  N   . THR I  1 3   ? 36.062  18.857  66.414 1.00 55.59  ? 2   THR I N   1 
ATOM   8920  C  CA  . THR I  1 3   ? 35.052  18.245  65.556 1.00 50.57  ? 2   THR I CA  1 
ATOM   8921  C  C   . THR I  1 3   ? 35.173  18.829  64.145 1.00 44.04  ? 2   THR I C   1 
ATOM   8922  O  O   . THR I  1 3   ? 35.142  20.042  63.960 1.00 42.60  ? 2   THR I O   1 
ATOM   8923  C  CB  . THR I  1 3   ? 33.648  18.237  66.193 1.00 50.67  ? 2   THR I CB  1 
ATOM   8924  O  OG1 . THR I  1 3   ? 33.391  19.573  66.593 1.00 65.76  ? 2   THR I OG1 1 
ATOM   8925  C  CG2 . THR I  1 3   ? 33.582  17.432  67.469 1.00 51.93  ? 2   THR I CG2 1 
ATOM   8926  N  N   . LYS I  1 4   ? 35.344  17.951  63.142 1.00 37.79  ? 3   LYS I N   1 
ATOM   8927  C  CA  . LYS I  1 4   ? 35.309  18.328  61.738 1.00 33.54  ? 3   LYS I CA  1 
ATOM   8928  C  C   . LYS I  1 4   ? 34.081  17.709  61.072 1.00 31.70  ? 3   LYS I C   1 
ATOM   8929  O  O   . LYS I  1 4   ? 33.781  16.524  61.227 1.00 35.28  ? 3   LYS I O   1 
ATOM   8930  C  CB  . LYS I  1 4   ? 36.558  17.854  60.982 1.00 34.28  ? 3   LYS I CB  1 
ATOM   8931  C  CG  . LYS I  1 4   ? 37.514  18.908  60.430 1.00 38.53  ? 3   LYS I CG  1 
ATOM   8932  C  CD  . LYS I  1 4   ? 38.785  18.241  59.887 1.00 42.25  ? 3   LYS I CD  1 
ATOM   8933  C  CE  . LYS I  1 4   ? 39.466  18.982  58.754 1.00 46.70  ? 3   LYS I CE  1 
ATOM   8934  N  NZ  . LYS I  1 4   ? 38.703  18.985  57.482 1.00 47.03  ? 3   LYS I NZ  1 
ATOM   8935  N  N   . VAL I  1 5   ? 33.420  18.536  60.265 1.00 27.25  ? 4   VAL I N   1 
ATOM   8936  C  CA  . VAL I  1 5   ? 32.179  18.178  59.603 1.00 24.71  ? 4   VAL I CA  1 
ATOM   8937  C  C   . VAL I  1 5   ? 32.282  18.640  58.155 1.00 22.42  ? 4   VAL I C   1 
ATOM   8938  O  O   . VAL I  1 5   ? 33.047  19.541  57.841 1.00 21.43  ? 4   VAL I O   1 
ATOM   8939  C  CB  . VAL I  1 5   ? 31.004  18.833  60.350 1.00 26.02  ? 4   VAL I CB  1 
ATOM   8940  C  CG1 . VAL I  1 5   ? 29.730  18.832  59.546 1.00 28.79  ? 4   VAL I CG1 1 
ATOM   8941  C  CG2 . VAL I  1 5   ? 30.789  18.210  61.709 1.00 26.24  ? 4   VAL I CG2 1 
ATOM   8942  N  N   . VAL I  1 6   ? 31.530  18.009  57.262 1.00 22.20  ? 5   VAL I N   1 
ATOM   8943  C  CA  . VAL I  1 6   ? 31.621  18.388  55.864 1.00 23.77  ? 5   VAL I CA  1 
ATOM   8944  C  C   . VAL I  1 6   ? 30.243  18.298  55.209 1.00 25.28  ? 5   VAL I C   1 
ATOM   8945  O  O   . VAL I  1 6   ? 29.328  17.656  55.721 1.00 28.22  ? 5   VAL I O   1 
ATOM   8946  C  CB  . VAL I  1 6   ? 32.662  17.527  55.118 1.00 23.55  ? 5   VAL I CB  1 
ATOM   8947  C  CG1 . VAL I  1 6   ? 32.187  16.091  54.938 1.00 23.54  ? 5   VAL I CG1 1 
ATOM   8948  C  CG2 . VAL I  1 6   ? 33.030  18.134  53.770 1.00 21.83  ? 5   VAL I CG2 1 
ATOM   8949  N  N   . CYS I  1 7   ? 30.113  18.933  54.046 1.00 24.23  ? 6   CYS I N   1 
ATOM   8950  C  CA  . CYS I  1 7   ? 28.848  18.949  53.350 1.00 23.57  ? 6   CYS I CA  1 
ATOM   8951  C  C   . CYS I  1 7   ? 29.121  19.106  51.865 1.00 22.66  ? 6   CYS I C   1 
ATOM   8952  O  O   . CYS I  1 7   ? 29.862  20.004  51.467 1.00 21.46  ? 6   CYS I O   1 
ATOM   8953  C  CB  . CYS I  1 7   ? 28.032  20.135  53.844 1.00 26.12  ? 6   CYS I CB  1 
ATOM   8954  S  SG  . CYS I  1 7   ? 26.399  20.241  53.089 1.00 29.70  ? 6   CYS I SG  1 
ATOM   8955  N  N   . VAL I  1 8   ? 28.536  18.212  51.063 1.00 22.27  ? 7   VAL I N   1 
ATOM   8956  C  CA  . VAL I  1 8   ? 28.667  18.302  49.617 1.00 22.91  ? 7   VAL I CA  1 
ATOM   8957  C  C   . VAL I  1 8   ? 27.364  18.868  49.076 1.00 24.38  ? 7   VAL I C   1 
ATOM   8958  O  O   . VAL I  1 8   ? 26.316  18.274  49.283 1.00 26.53  ? 7   VAL I O   1 
ATOM   8959  C  CB  . VAL I  1 8   ? 28.967  16.929  48.987 1.00 22.23  ? 7   VAL I CB  1 
ATOM   8960  C  CG1 . VAL I  1 8   ? 28.949  16.987  47.466 1.00 20.95  ? 7   VAL I CG1 1 
ATOM   8961  C  CG2 . VAL I  1 8   ? 30.275  16.342  49.498 1.00 21.88  ? 7   VAL I CG2 1 
ATOM   8962  N  N   . LEU I  1 9   ? 27.433  20.008  48.380 1.00 25.51  ? 8   LEU I N   1 
ATOM   8963  C  CA  . LEU I  1 9   ? 26.229  20.621  47.853 1.00 26.00  ? 8   LEU I CA  1 
ATOM   8964  C  C   . LEU I  1 9   ? 26.012  20.148  46.419 1.00 28.04  ? 8   LEU I C   1 
ATOM   8965  O  O   . LEU I  1 9   ? 26.911  20.283  45.594 1.00 29.81  ? 8   LEU I O   1 
ATOM   8966  C  CB  . LEU I  1 9   ? 26.370  22.142  47.904 1.00 25.94  ? 8   LEU I CB  1 
ATOM   8967  C  CG  . LEU I  1 9   ? 26.658  22.752  49.269 1.00 25.52  ? 8   LEU I CG  1 
ATOM   8968  C  CD1 . LEU I  1 9   ? 27.097  24.196  49.122 1.00 27.19  ? 8   LEU I CD1 1 
ATOM   8969  C  CD2 . LEU I  1 9   ? 25.447  22.678  50.163 1.00 27.25  ? 8   LEU I CD2 1 
ATOM   8970  N  N   . LYS I  1 10  ? 24.817  19.600  46.149 1.00 29.01  ? 9   LYS I N   1 
ATOM   8971  C  CA  . LYS I  1 10  ? 24.360  19.256  44.811 1.00 29.43  ? 9   LYS I CA  1 
ATOM   8972  C  C   . LYS I  1 10  ? 22.922  19.735  44.646 1.00 25.69  ? 9   LYS I C   1 
ATOM   8973  O  O   . LYS I  1 10  ? 22.216  19.946  45.631 1.00 22.34  ? 9   LYS I O   1 
ATOM   8974  C  CB  . LYS I  1 10  ? 24.444  17.742  44.559 1.00 34.86  ? 9   LYS I CB  1 
ATOM   8975  C  CG  . LYS I  1 10  ? 25.824  17.250  44.146 1.00 43.50  ? 9   LYS I CG  1 
ATOM   8976  C  CD  . LYS I  1 10  ? 25.942  15.777  43.858 1.00 47.17  ? 9   LYS I CD  1 
ATOM   8977  C  CE  . LYS I  1 10  ? 27.410  15.451  43.895 1.00 49.77  ? 9   LYS I CE  1 
ATOM   8978  N  NZ  . LYS I  1 10  ? 27.694  14.359  44.855 1.00 52.13  ? 9   LYS I NZ  1 
ATOM   8979  N  N   . GLY I  1 11  ? 22.511  19.916  43.388 1.00 22.64  ? 10  GLY I N   1 
ATOM   8980  C  CA  . GLY I  1 11  ? 21.143  20.269  43.064 1.00 22.92  ? 10  GLY I CA  1 
ATOM   8981  C  C   . GLY I  1 11  ? 20.809  19.874  41.629 1.00 24.95  ? 10  GLY I C   1 
ATOM   8982  O  O   . GLY I  1 11  ? 21.577  19.178  40.975 1.00 25.73  ? 10  GLY I O   1 
ATOM   8983  N  N   . ASP I  1 12  ? 19.651  20.332  41.129 1.00 26.10  ? 11  ASP I N   1 
ATOM   8984  C  CA  . ASP I  1 12  ? 19.213  19.986  39.790 1.00 26.78  ? 11  ASP I CA  1 
ATOM   8985  C  C   . ASP I  1 12  ? 20.006  20.721  38.720 1.00 29.51  ? 11  ASP I C   1 
ATOM   8986  O  O   . ASP I  1 12  ? 20.103  20.249  37.604 1.00 30.69  ? 11  ASP I O   1 
ATOM   8987  C  CB  . ASP I  1 12  ? 17.725  20.246  39.644 1.00 26.92  ? 11  ASP I CB  1 
ATOM   8988  C  CG  . ASP I  1 12  ? 16.937  19.230  40.460 1.00 30.28  ? 11  ASP I CG  1 
ATOM   8989  O  OD1 . ASP I  1 12  ? 17.388  18.073  40.590 1.00 29.15  ? 11  ASP I OD1 1 
ATOM   8990  O  OD2 . ASP I  1 12  ? 15.895  19.605  41.002 1.00 37.38  ? 11  ASP I OD2 1 
ATOM   8991  N  N   . GLY I  1 13  ? 20.536  21.891  39.063 1.00 34.57  ? 12  GLY I N   1 
ATOM   8992  C  CA  . GLY I  1 13  ? 21.233  22.744  38.115 1.00 31.04  ? 12  GLY I CA  1 
ATOM   8993  C  C   . GLY I  1 13  ? 22.736  22.512  38.174 1.00 30.72  ? 12  GLY I C   1 
ATOM   8994  O  O   . GLY I  1 13  ? 23.182  21.453  38.608 1.00 32.56  ? 12  GLY I O   1 
ATOM   8995  N  N   . PRO I  1 14  ? 23.561  23.488  37.734 1.00 28.31  ? 13  PRO I N   1 
ATOM   8996  C  CA  . PRO I  1 14  ? 25.014  23.307  37.705 1.00 26.49  ? 13  PRO I CA  1 
ATOM   8997  C  C   . PRO I  1 14  ? 25.721  23.622  39.025 1.00 24.30  ? 13  PRO I C   1 
ATOM   8998  O  O   . PRO I  1 14  ? 26.949  23.530  39.113 1.00 24.79  ? 13  PRO I O   1 
ATOM   8999  C  CB  . PRO I  1 14  ? 25.440  24.288  36.605 1.00 25.98  ? 13  PRO I CB  1 
ATOM   9000  C  CG  . PRO I  1 14  ? 24.442  25.424  36.737 1.00 26.52  ? 13  PRO I CG  1 
ATOM   9001  C  CD  . PRO I  1 14  ? 23.143  24.797  37.213 1.00 26.82  ? 13  PRO I CD  1 
ATOM   9002  N  N   . VAL I  1 15  ? 24.964  24.023  40.055 1.00 22.28  ? 14  VAL I N   1 
ATOM   9003  C  CA  . VAL I  1 15  ? 25.628  24.485  41.267 1.00 23.12  ? 14  VAL I CA  1 
ATOM   9004  C  C   . VAL I  1 15  ? 26.109  23.280  42.063 1.00 23.23  ? 14  VAL I C   1 
ATOM   9005  O  O   . VAL I  1 15  ? 25.339  22.363  42.327 1.00 24.55  ? 14  VAL I O   1 
ATOM   9006  C  CB  . VAL I  1 15  ? 24.731  25.408  42.109 1.00 22.24  ? 14  VAL I CB  1 
ATOM   9007  C  CG1 . VAL I  1 15  ? 25.410  25.808  43.409 1.00 21.43  ? 14  VAL I CG1 1 
ATOM   9008  C  CG2 . VAL I  1 15  ? 24.365  26.645  41.310 1.00 23.42  ? 14  VAL I CG2 1 
ATOM   9009  N  N   . GLN I  1 16  ? 27.392  23.289  42.430 1.00 24.28  ? 15  GLN I N   1 
ATOM   9010  C  CA  . GLN I  1 16  ? 27.924  22.248  43.293 1.00 25.76  ? 15  GLN I CA  1 
ATOM   9011  C  C   . GLN I  1 16  ? 29.132  22.760  44.061 1.00 23.75  ? 15  GLN I C   1 
ATOM   9012  O  O   . GLN I  1 16  ? 29.793  23.692  43.628 1.00 24.67  ? 15  GLN I O   1 
ATOM   9013  C  CB  . GLN I  1 16  ? 28.244  20.990  42.479 1.00 31.34  ? 15  GLN I CB  1 
ATOM   9014  C  CG  . GLN I  1 16  ? 29.303  21.189  41.403 1.00 37.23  ? 15  GLN I CG  1 
ATOM   9015  C  CD  . GLN I  1 16  ? 29.189  20.135  40.319 1.00 38.45  ? 15  GLN I CD  1 
ATOM   9016  O  OE1 . GLN I  1 16  ? 28.207  19.405  40.229 1.00 38.23  ? 15  GLN I OE1 1 
ATOM   9017  N  NE2 . GLN I  1 16  ? 30.209  20.044  39.492 1.00 40.14  ? 15  GLN I NE2 1 
ATOM   9018  N  N   . GLY I  1 17  ? 29.395  22.153  45.220 1.00 21.66  ? 16  GLY I N   1 
ATOM   9019  C  CA  . GLY I  1 17  ? 30.498  22.600  46.059 1.00 20.48  ? 16  GLY I CA  1 
ATOM   9020  C  C   . GLY I  1 17  ? 30.699  21.727  47.287 1.00 20.29  ? 16  GLY I C   1 
ATOM   9021  O  O   . GLY I  1 17  ? 29.898  20.838  47.571 1.00 22.75  ? 16  GLY I O   1 
ATOM   9022  N  N   . ILE I  1 18  ? 31.796  21.983  47.995 1.00 18.72  ? 17  ILE I N   1 
ATOM   9023  C  CA  . ILE I  1 18  ? 32.132  21.275  49.219 1.00 18.47  ? 17  ILE I CA  1 
ATOM   9024  C  C   . ILE I  1 18  ? 32.338  22.330  50.292 1.00 18.65  ? 17  ILE I C   1 
ATOM   9025  O  O   . ILE I  1 18  ? 33.078  23.284  50.069 1.00 18.95  ? 17  ILE I O   1 
ATOM   9026  C  CB  . ILE I  1 18  ? 33.420  20.443  49.013 1.00 17.52  ? 17  ILE I CB  1 
ATOM   9027  C  CG1 . ILE I  1 18  ? 33.249  19.381  47.928 1.00 17.50  ? 17  ILE I CG1 1 
ATOM   9028  C  CG2 . ILE I  1 18  ? 33.906  19.848  50.316 1.00 16.82  ? 17  ILE I CG2 1 
ATOM   9029  C  CD1 . ILE I  1 18  ? 34.527  18.675  47.580 1.00 18.08  ? 17  ILE I CD1 1 
ATOM   9030  N  N   . ILE I  1 19  ? 31.694  22.165  51.450 1.00 18.18  ? 18  ILE I N   1 
ATOM   9031  C  CA  . ILE I  1 19  ? 31.896  23.120  52.528 1.00 18.89  ? 18  ILE I CA  1 
ATOM   9032  C  C   . ILE I  1 19  ? 32.331  22.361  53.768 1.00 19.46  ? 18  ILE I C   1 
ATOM   9033  O  O   . ILE I  1 19  ? 31.678  21.403  54.148 1.00 21.06  ? 18  ILE I O   1 
ATOM   9034  C  CB  . ILE I  1 19  ? 30.624  23.951  52.796 1.00 18.74  ? 18  ILE I CB  1 
ATOM   9035  C  CG1 . ILE I  1 19  ? 30.178  24.762  51.574 1.00 19.53  ? 18  ILE I CG1 1 
ATOM   9036  C  CG2 . ILE I  1 19  ? 30.782  24.824  54.029 1.00 18.66  ? 18  ILE I CG2 1 
ATOM   9037  C  CD1 . ILE I  1 19  ? 31.141  25.829  51.132 1.00 18.04  ? 18  ILE I CD1 1 
ATOM   9038  N  N   . ASN I  1 20  ? 33.409  22.819  54.406 1.00 19.03  ? 19  ASN I N   1 
ATOM   9039  C  CA  . ASN I  1 20  ? 33.905  22.208  55.629 1.00 20.04  ? 19  ASN I CA  1 
ATOM   9040  C  C   . ASN I  1 20  ? 33.504  23.039  56.836 1.00 20.65  ? 19  ASN I C   1 
ATOM   9041  O  O   . ASN I  1 20  ? 33.406  24.259  56.736 1.00 22.71  ? 19  ASN I O   1 
ATOM   9042  C  CB  . ASN I  1 20  ? 35.426  22.092  55.611 1.00 20.02  ? 19  ASN I CB  1 
ATOM   9043  C  CG  . ASN I  1 20  ? 35.908  21.401  54.359 1.00 19.91  ? 19  ASN I CG  1 
ATOM   9044  O  OD1 . ASN I  1 20  ? 36.295  22.061  53.405 1.00 18.98  ? 19  ASN I OD1 1 
ATOM   9045  N  ND2 . ASN I  1 20  ? 35.846  20.082  54.340 1.00 19.88  ? 19  ASN I ND2 1 
ATOM   9046  N  N   . PHE I  1 21  ? 33.297  22.366  57.970 1.00 20.56  ? 20  PHE I N   1 
ATOM   9047  C  CA  . PHE I  1 21  ? 33.017  23.033  59.229 1.00 23.07  ? 20  PHE I CA  1 
ATOM   9048  C  C   . PHE I  1 21  ? 33.977  22.499  60.277 1.00 25.56  ? 20  PHE I C   1 
ATOM   9049  O  O   . PHE I  1 21  ? 34.162  21.293  60.379 1.00 27.53  ? 20  PHE I O   1 
ATOM   9050  C  CB  . PHE I  1 21  ? 31.603  22.720  59.729 1.00 21.78  ? 20  PHE I CB  1 
ATOM   9051  C  CG  . PHE I  1 21  ? 30.484  23.152  58.820 1.00 22.91  ? 20  PHE I CG  1 
ATOM   9052  C  CD1 . PHE I  1 21  ? 30.261  22.528  57.598 1.00 22.32  ? 20  PHE I CD1 1 
ATOM   9053  C  CD2 . PHE I  1 21  ? 29.641  24.193  59.195 1.00 23.69  ? 20  PHE I CD2 1 
ATOM   9054  C  CE1 . PHE I  1 21  ? 29.221  22.943  56.771 1.00 21.92  ? 20  PHE I CE1 1 
ATOM   9055  C  CE2 . PHE I  1 21  ? 28.587  24.584  58.377 1.00 22.72  ? 20  PHE I CE2 1 
ATOM   9056  C  CZ  . PHE I  1 21  ? 28.378  23.957  57.166 1.00 22.20  ? 20  PHE I CZ  1 
ATOM   9057  N  N   . GLU I  1 22  ? 34.578  23.397  61.058 1.00 29.42  ? 21  GLU I N   1 
ATOM   9058  C  CA  . GLU I  1 22  ? 35.506  22.963  62.089 1.00 33.14  ? 21  GLU I CA  1 
ATOM   9059  C  C   . GLU I  1 22  ? 35.266  23.777  63.354 1.00 32.12  ? 21  GLU I C   1 
ATOM   9060  O  O   . GLU I  1 22  ? 35.023  24.981  63.262 1.00 33.09  ? 21  GLU I O   1 
ATOM   9061  C  CB  . GLU I  1 22  ? 36.939  23.106  61.568 1.00 40.77  ? 21  GLU I CB  1 
ATOM   9062  C  CG  . GLU I  1 22  ? 37.932  22.303  62.399 1.00 50.24  ? 21  GLU I CG  1 
ATOM   9063  C  CD  . GLU I  1 22  ? 39.383  22.424  61.923 1.00 59.08  ? 21  GLU I CD  1 
ATOM   9064  O  OE1 . GLU I  1 22  ? 39.648  22.085  60.742 1.00 60.23  ? 21  GLU I OE1 1 
ATOM   9065  O  OE2 . GLU I  1 22  ? 40.255  22.889  62.715 1.00 69.04  ? 21  GLU I OE2 1 
ATOM   9066  N  N   . GLN I  1 23  ? 35.329  23.111  64.515 1.00 32.00  ? 22  GLN I N   1 
ATOM   9067  C  CA  . GLN I  1 23  ? 35.075  23.772  65.790 1.00 33.40  ? 22  GLN I CA  1 
ATOM   9068  C  C   . GLN I  1 23  ? 36.090  23.277  66.822 1.00 35.38  ? 22  GLN I C   1 
ATOM   9069  O  O   . GLN I  1 23  ? 35.979  22.138  67.304 1.00 35.74  ? 22  GLN I O   1 
ATOM   9070  C  CB  . GLN I  1 23  ? 33.652  23.475  66.260 1.00 30.98  ? 22  GLN I CB  1 
ATOM   9071  C  CG  . GLN I  1 23  ? 33.224  24.297  67.461 1.00 32.36  ? 22  GLN I CG  1 
ATOM   9072  C  CD  . GLN I  1 23  ? 31.846  23.943  67.969 1.00 35.19  ? 22  GLN I CD  1 
ATOM   9073  O  OE1 . GLN I  1 23  ? 31.407  22.794  67.905 1.00 37.43  ? 22  GLN I OE1 1 
ATOM   9074  N  NE2 . GLN I  1 23  ? 31.151  24.937  68.496 1.00 35.84  ? 22  GLN I NE2 1 
ATOM   9075  N  N   . LYS I  1 24  ? 37.077  24.127  67.159 1.00 38.12  ? 23  LYS I N   1 
ATOM   9076  C  CA  . LYS I  1 24  ? 38.194  23.728  68.002 1.00 38.99  ? 23  LYS I CA  1 
ATOM   9077  C  C   . LYS I  1 24  ? 37.745  23.518  69.450 1.00 40.20  ? 23  LYS I C   1 
ATOM   9078  O  O   . LYS I  1 24  ? 38.010  22.471  70.027 1.00 42.79  ? 23  LYS I O   1 
ATOM   9079  C  CB  . LYS I  1 24  ? 39.425  24.628  67.819 1.00 37.97  ? 23  LYS I CB  1 
ATOM   9080  C  CG  . LYS I  1 24  ? 40.230  24.390  66.548 0.40 37.22  ? 23  LYS I CG  1 
ATOM   9081  C  CD  . LYS I  1 24  ? 41.423  25.301  66.394 0.40 37.65  ? 23  LYS I CD  1 
ATOM   9082  C  CE  . LYS I  1 24  ? 42.173  25.067  65.098 0.40 37.29  ? 23  LYS I CE  1 
ATOM   9083  N  NZ  . LYS I  1 24  ? 43.106  26.180  64.821 0.40 35.48  ? 23  LYS I NZ  1 
ATOM   9084  N  N   . GLU I  1 25  ? 37.059  24.503  70.047 1.00 46.65  ? 24  GLU I N   1 
ATOM   9085  C  CA  . GLU I  1 25  ? 36.523  24.359  71.394 1.00 47.43  ? 24  GLU I CA  1 
ATOM   9086  C  C   . GLU I  1 25  ? 35.040  24.053  71.327 1.00 49.32  ? 24  GLU I C   1 
ATOM   9087  O  O   . GLU I  1 25  ? 34.386  24.449  70.377 1.00 51.32  ? 24  GLU I O   1 
ATOM   9088  C  CB  . GLU I  1 25  ? 36.794  25.600  72.248 0.40 44.35  ? 24  GLU I CB  1 
ATOM   9089  C  CG  . GLU I  1 25  ? 38.278  25.933  72.321 0.40 42.08  ? 24  GLU I CG  1 
ATOM   9090  C  CD  . GLU I  1 25  ? 39.155  24.921  73.054 0.40 41.24  ? 24  GLU I CD  1 
ATOM   9091  O  OE1 . GLU I  1 25  ? 38.635  24.300  74.001 0.40 40.55  ? 24  GLU I OE1 1 
ATOM   9092  O  OE2 . GLU I  1 25  ? 40.335  24.724  72.665 0.40 37.54  ? 24  GLU I OE2 1 
ATOM   9093  N  N   . SER I  1 26  ? 34.526  23.365  72.348 1.00 58.59  ? 25  SER I N   1 
ATOM   9094  C  CA  . SER I  1 26  ? 33.199  22.763  72.258 1.00 68.13  ? 25  SER I CA  1 
ATOM   9095  C  C   . SER I  1 26  ? 32.093  23.813  72.228 1.00 67.76  ? 25  SER I C   1 
ATOM   9096  O  O   . SER I  1 26  ? 31.062  23.564  71.605 1.00 71.15  ? 25  SER I O   1 
ATOM   9097  C  CB  . SER I  1 26  ? 32.953  21.704  73.309 1.00 67.74  ? 25  SER I CB  1 
ATOM   9098  O  OG  . SER I  1 26  ? 33.572  22.068  74.528 1.00 80.56  ? 25  SER I OG  1 
ATOM   9099  N  N   . ASN I  1 27  ? 32.279  24.961  72.888 1.00 66.06  ? 26  ASN I N   1 
ATOM   9100  C  CA  . ASN I  1 27  ? 31.242  25.973  72.771 1.00 68.62  ? 26  ASN I CA  1 
ATOM   9101  C  C   . ASN I  1 27  ? 31.698  27.162  71.924 1.00 62.73  ? 26  ASN I C   1 
ATOM   9102  O  O   . ASN I  1 27  ? 31.028  28.179  71.883 1.00 60.26  ? 26  ASN I O   1 
ATOM   9103  C  CB  . ASN I  1 27  ? 30.584  26.314  74.104 1.00 79.81  ? 26  ASN I CB  1 
ATOM   9104  C  CG  . ASN I  1 27  ? 29.162  26.814  73.942 1.00 90.90  ? 26  ASN I CG  1 
ATOM   9105  O  OD1 . ASN I  1 27  ? 28.475  26.592  72.935 1.00 91.53  ? 26  ASN I OD1 1 
ATOM   9106  N  ND2 . ASN I  1 27  ? 28.668  27.437  74.996 1.00 94.25  ? 26  ASN I ND2 1 
ATOM   9107  N  N   . GLY I  1 28  ? 32.841  26.993  71.257 1.00 61.23  ? 27  GLY I N   1 
ATOM   9108  C  CA  . GLY I  1 28  ? 33.521  28.090  70.595 1.00 50.83  ? 27  GLY I CA  1 
ATOM   9109  C  C   . GLY I  1 28  ? 33.074  28.284  69.148 1.00 44.36  ? 27  GLY I C   1 
ATOM   9110  O  O   . GLY I  1 28  ? 32.197  27.579  68.661 1.00 42.87  ? 27  GLY I O   1 
ATOM   9111  N  N   . PRO I  1 29  ? 33.691  29.234  68.413 1.00 39.92  ? 28  PRO I N   1 
ATOM   9112  C  CA  . PRO I  1 29  ? 33.256  29.563  67.054 1.00 37.62  ? 28  PRO I CA  1 
ATOM   9113  C  C   . PRO I  1 29  ? 33.501  28.416  66.076 1.00 34.18  ? 28  PRO I C   1 
ATOM   9114  O  O   . PRO I  1 29  ? 34.349  27.558  66.328 1.00 33.10  ? 28  PRO I O   1 
ATOM   9115  C  CB  . PRO I  1 29  ? 34.139  30.772  66.694 1.00 37.19  ? 28  PRO I CB  1 
ATOM   9116  C  CG  . PRO I  1 29  ? 35.373  30.590  67.548 1.00 36.05  ? 28  PRO I CG  1 
ATOM   9117  C  CD  . PRO I  1 29  ? 34.851  30.030  68.852 1.00 37.34  ? 28  PRO I CD  1 
ATOM   9118  N  N   . VAL I  1 30  ? 32.743  28.421  64.969 1.00 30.73  ? 29  VAL I N   1 
ATOM   9119  C  CA  . VAL I  1 30  ? 32.842  27.409  63.929 1.00 28.54  ? 29  VAL I CA  1 
ATOM   9120  C  C   . VAL I  1 30  ? 33.401  28.060  62.668 1.00 26.20  ? 29  VAL I C   1 
ATOM   9121  O  O   . VAL I  1 30  ? 32.846  29.047  62.188 1.00 24.78  ? 29  VAL I O   1 
ATOM   9122  C  CB  . VAL I  1 30  ? 31.469  26.772  63.639 1.00 27.30  ? 29  VAL I CB  1 
ATOM   9123  C  CG1 . VAL I  1 30  ? 31.563  25.703  62.551 1.00 28.67  ? 29  VAL I CG1 1 
ATOM   9124  C  CG2 . VAL I  1 30  ? 30.808  26.218  64.886 1.00 27.74  ? 29  VAL I CG2 1 
ATOM   9125  N  N   . LYS I  1 31  ? 34.490  27.502  62.136 1.00 26.27  ? 30  LYS I N   1 
ATOM   9126  C  CA  . LYS I  1 31  ? 35.019  27.988  60.872 1.00 28.89  ? 30  LYS I CA  1 
ATOM   9127  C  C   . LYS I  1 31  ? 34.288  27.254  59.748 1.00 28.22  ? 30  LYS I C   1 
ATOM   9128  O  O   . LYS I  1 31  ? 34.224  26.026  59.745 1.00 28.93  ? 30  LYS I O   1 
ATOM   9129  C  CB  . LYS I  1 31  ? 36.530  27.783  60.771 1.00 33.43  ? 30  LYS I CB  1 
ATOM   9130  C  CG  . LYS I  1 31  ? 37.392  28.833  61.482 1.00 43.24  ? 30  LYS I CG  1 
ATOM   9131  C  CD  . LYS I  1 31  ? 38.888  28.754  61.127 1.00 55.07  ? 30  LYS I CD  1 
ATOM   9132  C  CE  . LYS I  1 31  ? 39.928  28.222  62.135 1.00 63.98  ? 30  LYS I CE  1 
ATOM   9133  N  NZ  . LYS I  1 31  ? 40.215  26.762  61.962 1.00 67.04  ? 30  LYS I NZ  1 
ATOM   9134  N  N   . VAL I  1 32  ? 33.725  28.012  58.808 1.00 25.21  ? 31  VAL I N   1 
ATOM   9135  C  CA  . VAL I  1 32  ? 33.041  27.414  57.674 1.00 24.57  ? 31  VAL I CA  1 
ATOM   9136  C  C   . VAL I  1 32  ? 33.780  27.834  56.409 1.00 25.46  ? 31  VAL I C   1 
ATOM   9137  O  O   . VAL I  1 32  ? 33.829  29.022  56.092 1.00 30.27  ? 31  VAL I O   1 
ATOM   9138  C  CB  . VAL I  1 32  ? 31.573  27.876  57.628 1.00 24.02  ? 31  VAL I CB  1 
ATOM   9139  C  CG1 . VAL I  1 32  ? 30.805  27.198  56.519 1.00 23.39  ? 31  VAL I CG1 1 
ATOM   9140  C  CG2 . VAL I  1 32  ? 30.879  27.665  58.957 1.00 24.08  ? 31  VAL I CG2 1 
ATOM   9141  N  N   . TRP I  1 33  ? 34.365  26.879  55.684 1.00 24.02  ? 32  TRP I N   1 
ATOM   9142  C  CA  . TRP I  1 33  ? 35.072  27.266  54.468 1.00 22.71  ? 32  TRP I CA  1 
ATOM   9143  C  C   . TRP I  1 33  ? 34.933  26.211  53.381 1.00 21.37  ? 32  TRP I C   1 
ATOM   9144  O  O   . TRP I  1 33  ? 34.704  25.036  53.667 1.00 23.44  ? 32  TRP I O   1 
ATOM   9145  C  CB  . TRP I  1 33  ? 36.552  27.540  54.748 1.00 24.20  ? 32  TRP I CB  1 
ATOM   9146  C  CG  . TRP I  1 33  ? 37.383  26.296  54.845 1.00 25.52  ? 32  TRP I CG  1 
ATOM   9147  C  CD1 . TRP I  1 33  ? 38.169  25.731  53.874 1.00 25.49  ? 32  TRP I CD1 1 
ATOM   9148  C  CD2 . TRP I  1 33  ? 37.491  25.440  55.994 1.00 26.45  ? 32  TRP I CD2 1 
ATOM   9149  N  NE1 . TRP I  1 33  ? 38.768  24.589  54.345 1.00 25.12  ? 32  TRP I NE1 1 
ATOM   9150  C  CE2 . TRP I  1 33  ? 38.371  24.386  55.643 1.00 26.38  ? 32  TRP I CE2 1 
ATOM   9151  C  CE3 . TRP I  1 33  ? 36.928  25.462  57.277 1.00 25.92  ? 32  TRP I CE3 1 
ATOM   9152  C  CZ2 . TRP I  1 33  ? 38.696  23.368  56.540 1.00 26.60  ? 32  TRP I CZ2 1 
ATOM   9153  C  CZ3 . TRP I  1 33  ? 37.254  24.452  58.163 1.00 26.96  ? 32  TRP I CZ3 1 
ATOM   9154  C  CH2 . TRP I  1 33  ? 38.128  23.422  57.800 1.00 27.61  ? 32  TRP I CH2 1 
ATOM   9155  N  N   . GLY I  1 34  ? 35.131  26.650  52.141 1.00 18.76  ? 33  GLY I N   1 
ATOM   9156  C  CA  . GLY I  1 34  ? 35.160  25.761  51.002 1.00 18.29  ? 33  GLY I CA  1 
ATOM   9157  C  C   . GLY I  1 34  ? 34.855  26.536  49.726 1.00 19.00  ? 33  GLY I C   1 
ATOM   9158  O  O   . GLY I  1 34  ? 34.994  27.750  49.677 1.00 19.72  ? 33  GLY I O   1 
ATOM   9159  N  N   . SER I  1 35  ? 34.385  25.843  48.704 1.00 19.51  ? 34  SER I N   1 
ATOM   9160  C  CA  . SER I  1 35  ? 34.223  26.472  47.413 1.00 19.44  ? 34  SER I CA  1 
ATOM   9161  C  C   . SER I  1 35  ? 32.911  25.998  46.778 1.00 21.27  ? 34  SER I C   1 
ATOM   9162  O  O   . SER I  1 35  ? 32.546  24.824  46.900 1.00 23.26  ? 34  SER I O   1 
ATOM   9163  C  CB  . SER I  1 35  ? 35.432  26.127  46.603 1.00 17.92  ? 34  SER I CB  1 
ATOM   9164  O  OG  . SER I  1 35  ? 35.236  26.465  45.258 1.00 19.00  ? 34  SER I OG  1 
ATOM   9165  N  N   . ILE I  1 36  ? 32.165  26.912  46.137 1.00 19.99  ? 35  ILE I N   1 
ATOM   9166  C  CA  . ILE I  1 36  ? 30.984  26.537  45.372 1.00 19.82  ? 35  ILE I CA  1 
ATOM   9167  C  C   . ILE I  1 36  ? 31.140  27.076  43.959 1.00 21.37  ? 35  ILE I C   1 
ATOM   9168  O  O   . ILE I  1 36  ? 31.583  28.211  43.788 1.00 22.64  ? 35  ILE I O   1 
ATOM   9169  C  CB  . ILE I  1 36  ? 29.708  27.085  46.033 1.00 18.93  ? 35  ILE I CB  1 
ATOM   9170  C  CG1 . ILE I  1 36  ? 29.678  26.790  47.539 1.00 19.75  ? 35  ILE I CG1 1 
ATOM   9171  C  CG2 . ILE I  1 36  ? 28.464  26.585  45.311 1.00 18.36  ? 35  ILE I CG2 1 
ATOM   9172  C  CD1 . ILE I  1 36  ? 28.565  27.471  48.277 1.00 20.08  ? 35  ILE I CD1 1 
ATOM   9173  N  N   . LYS I  1 37  ? 30.795  26.268  42.958 1.00 24.12  ? 36  LYS I N   1 
ATOM   9174  C  CA  . LYS I  1 37  ? 30.954  26.691  41.576 1.00 26.83  ? 36  LYS I CA  1 
ATOM   9175  C  C   . LYS I  1 37  ? 29.609  26.602  40.859 1.00 26.85  ? 36  LYS I C   1 
ATOM   9176  O  O   . LYS I  1 37  ? 28.667  25.968  41.361 1.00 27.11  ? 36  LYS I O   1 
ATOM   9177  C  CB  . LYS I  1 37  ? 32.068  25.910  40.875 1.00 28.87  ? 36  LYS I CB  1 
ATOM   9178  C  CG  . LYS I  1 37  ? 31.792  24.422  40.686 1.00 32.79  ? 36  LYS I CG  1 
ATOM   9179  C  CD  . LYS I  1 37  ? 32.845  23.699  39.892 1.00 38.30  ? 36  LYS I CD  1 
ATOM   9180  C  CE  . LYS I  1 37  ? 32.335  22.469  39.171 1.00 35.29  ? 36  LYS I CE  1 
ATOM   9181  N  NZ  . LYS I  1 37  ? 33.423  21.736  38.498 1.00 35.79  ? 36  LYS I NZ  1 
ATOM   9182  N  N   . GLY I  1 38  ? 29.525  27.265  39.690 1.00 25.15  ? 37  GLY I N   1 
ATOM   9183  C  CA  . GLY I  1 38  ? 28.328  27.249  38.863 1.00 23.65  ? 37  GLY I CA  1 
ATOM   9184  C  C   . GLY I  1 38  ? 27.270  28.272  39.280 1.00 24.26  ? 37  GLY I C   1 
ATOM   9185  O  O   . GLY I  1 38  ? 26.132  28.192  38.833 1.00 24.80  ? 37  GLY I O   1 
ATOM   9186  N  N   . LEU I  1 39  ? 27.642  29.228  40.141 1.00 26.17  ? 38  LEU I N   1 
ATOM   9187  C  CA  . LEU I  1 39  ? 26.720  30.247  40.618 1.00 24.95  ? 38  LEU I CA  1 
ATOM   9188  C  C   . LEU I  1 39  ? 26.740  31.437  39.664 1.00 24.50  ? 38  LEU I C   1 
ATOM   9189  O  O   . LEU I  1 39  ? 27.733  31.665  38.974 1.00 25.30  ? 38  LEU I O   1 
ATOM   9190  C  CB  . LEU I  1 39  ? 27.158  30.700  42.015 1.00 23.41  ? 38  LEU I CB  1 
ATOM   9191  C  CG  . LEU I  1 39  ? 26.950  29.684  43.125 1.00 22.87  ? 38  LEU I CG  1 
ATOM   9192  C  CD1 . LEU I  1 39  ? 27.768  30.077  44.342 1.00 21.32  ? 38  LEU I CD1 1 
ATOM   9193  C  CD2 . LEU I  1 39  ? 25.477  29.579  43.476 1.00 22.28  ? 38  LEU I CD2 1 
ATOM   9194  N  N   . THR I  1 40  ? 25.639  32.203  39.657 1.00 23.60  ? 39  THR I N   1 
ATOM   9195  C  CA  . THR I  1 40  ? 25.637  33.484  38.974 1.00 23.09  ? 39  THR I CA  1 
ATOM   9196  C  C   . THR I  1 40  ? 26.450  34.469  39.806 1.00 23.19  ? 39  THR I C   1 
ATOM   9197  O  O   . THR I  1 40  ? 26.495  34.362  41.030 1.00 22.59  ? 39  THR I O   1 
ATOM   9198  C  CB  . THR I  1 40  ? 24.216  34.015  38.776 1.00 22.80  ? 39  THR I CB  1 
ATOM   9199  O  OG1 . THR I  1 40  ? 23.592  33.931  40.060 1.00 24.64  ? 39  THR I OG1 1 
ATOM   9200  C  CG2 . THR I  1 40  ? 23.447  33.265  37.710 1.00 21.28  ? 39  THR I CG2 1 
ATOM   9201  N  N   . GLU I  1 41  ? 27.093  35.426  39.130 1.00 24.25  ? 40  GLU I N   1 
ATOM   9202  C  CA  . GLU I  1 41  ? 27.924  36.397  39.817 1.00 25.75  ? 40  GLU I CA  1 
ATOM   9203  C  C   . GLU I  1 41  ? 27.087  37.121  40.870 1.00 23.61  ? 40  GLU I C   1 
ATOM   9204  O  O   . GLU I  1 41  ? 25.923  37.413  40.624 1.00 22.25  ? 40  GLU I O   1 
ATOM   9205  C  CB  . GLU I  1 41  ? 28.518  37.376  38.809 1.00 28.60  ? 40  GLU I CB  1 
ATOM   9206  C  CG  . GLU I  1 41  ? 29.494  38.339  39.458 1.00 31.05  ? 40  GLU I CG  1 
ATOM   9207  C  CD  . GLU I  1 41  ? 30.202  39.309  38.527 1.00 31.22  ? 40  GLU I CD  1 
ATOM   9208  O  OE1 . GLU I  1 41  ? 29.846  39.366  37.331 1.00 30.52  ? 40  GLU I OE1 1 
ATOM   9209  O  OE2 . GLU I  1 41  ? 31.120  40.001  39.008 1.00 34.25  ? 40  GLU I OE2 1 
ATOM   9210  N  N   . GLY I  1 42  ? 27.677  37.375  42.041 1.00 22.79  ? 41  GLY I N   1 
ATOM   9211  C  CA  . GLY I  1 42  ? 26.981  38.161  43.049 1.00 22.93  ? 41  GLY I CA  1 
ATOM   9212  C  C   . GLY I  1 42  ? 26.698  37.403  44.339 1.00 21.62  ? 41  GLY I C   1 
ATOM   9213  O  O   . GLY I  1 42  ? 27.266  36.331  44.574 1.00 23.02  ? 41  GLY I O   1 
ATOM   9214  N  N   . LEU I  1 43  ? 25.810  37.975  45.170 1.00 19.88  ? 42  LEU I N   1 
ATOM   9215  C  CA  . LEU I  1 43  ? 25.506  37.454  46.498 1.00 19.58  ? 42  LEU I CA  1 
ATOM   9216  C  C   . LEU I  1 43  ? 24.504  36.308  46.404 1.00 19.01  ? 42  LEU I C   1 
ATOM   9217  O  O   . LEU I  1 43  ? 23.582  36.363  45.593 1.00 17.65  ? 42  LEU I O   1 
ATOM   9218  C  CB  . LEU I  1 43  ? 24.923  38.571  47.369 1.00 19.05  ? 42  LEU I CB  1 
ATOM   9219  C  CG  . LEU I  1 43  ? 25.875  39.709  47.713 1.00 18.47  ? 42  LEU I CG  1 
ATOM   9220  C  CD1 . LEU I  1 43  ? 25.123  40.864  48.335 1.00 17.61  ? 42  LEU I CD1 1 
ATOM   9221  C  CD2 . LEU I  1 43  ? 26.957  39.219  48.658 1.00 19.36  ? 42  LEU I CD2 1 
ATOM   9222  N  N   . HIS I  1 44  ? 24.707  35.287  47.250 1.00 18.92  ? 43  HIS I N   1 
ATOM   9223  C  CA  . HIS I  1 44  ? 23.797  34.162  47.384 1.00 18.11  ? 43  HIS I CA  1 
ATOM   9224  C  C   . HIS I  1 44  ? 23.598  33.835  48.862 1.00 19.05  ? 43  HIS I C   1 
ATOM   9225  O  O   . HIS I  1 44  ? 24.556  33.761  49.639 1.00 19.24  ? 43  HIS I O   1 
ATOM   9226  C  CB  . HIS I  1 44  ? 24.308  32.950  46.611 1.00 16.82  ? 43  HIS I CB  1 
ATOM   9227  C  CG  . HIS I  1 44  ? 24.356  33.147  45.136 1.00 17.47  ? 43  HIS I CG  1 
ATOM   9228  N  ND1 . HIS I  1 44  ? 23.328  32.745  44.299 1.00 18.48  ? 43  HIS I ND1 1 
ATOM   9229  C  CD2 . HIS I  1 44  ? 25.295  33.675  44.326 1.00 17.17  ? 43  HIS I CD2 1 
ATOM   9230  C  CE1 . HIS I  1 44  ? 23.634  33.008  43.042 1.00 17.83  ? 43  HIS I CE1 1 
ATOM   9231  N  NE2 . HIS I  1 44  ? 24.840  33.576  43.028 1.00 17.62  ? 43  HIS I NE2 1 
ATOM   9232  N  N   . GLY I  1 45  ? 22.327  33.670  49.238 1.00 19.42  ? 44  GLY I N   1 
ATOM   9233  C  CA  . GLY I  1 45  ? 21.966  33.317  50.598 1.00 19.88  ? 44  GLY I CA  1 
ATOM   9234  C  C   . GLY I  1 45  ? 22.503  31.936  50.966 1.00 20.32  ? 44  GLY I C   1 
ATOM   9235  O  O   . GLY I  1 45  ? 22.508  31.021  50.144 1.00 20.75  ? 44  GLY I O   1 
ATOM   9236  N  N   . PHE I  1 46  ? 22.925  31.806  52.226 1.00 19.79  ? 45  PHE I N   1 
ATOM   9237  C  CA  . PHE I  1 46  ? 23.683  30.655  52.670 1.00 19.83  ? 45  PHE I CA  1 
ATOM   9238  C  C   . PHE I  1 46  ? 23.195  30.287  54.064 1.00 20.06  ? 45  PHE I C   1 
ATOM   9239  O  O   . PHE I  1 46  ? 23.481  31.012  55.024 1.00 20.86  ? 45  PHE I O   1 
ATOM   9240  C  CB  . PHE I  1 46  ? 25.153  31.066  52.706 1.00 19.58  ? 45  PHE I CB  1 
ATOM   9241  C  CG  . PHE I  1 46  ? 26.165  29.961  52.857 1.00 20.16  ? 45  PHE I CG  1 
ATOM   9242  C  CD1 . PHE I  1 46  ? 26.332  29.009  51.854 1.00 20.31  ? 45  PHE I CD1 1 
ATOM   9243  C  CD2 . PHE I  1 46  ? 26.989  29.908  53.976 1.00 19.64  ? 45  PHE I CD2 1 
ATOM   9244  C  CE1 . PHE I  1 46  ? 27.298  28.021  51.977 1.00 19.69  ? 45  PHE I CE1 1 
ATOM   9245  C  CE2 . PHE I  1 46  ? 27.933  28.904  54.097 1.00 19.11  ? 45  PHE I CE2 1 
ATOM   9246  C  CZ  . PHE I  1 46  ? 28.085  27.960  53.103 1.00 19.34  ? 45  PHE I CZ  1 
ATOM   9247  N  N   . HIS I  1 47  ? 22.439  29.185  54.165 1.00 20.01  ? 46  HIS I N   1 
ATOM   9248  C  CA  . HIS I  1 47  ? 21.761  28.884  55.418 1.00 20.57  ? 46  HIS I CA  1 
ATOM   9249  C  C   . HIS I  1 47  ? 21.819  27.403  55.754 1.00 21.48  ? 46  HIS I C   1 
ATOM   9250  O  O   . HIS I  1 47  ? 21.899  26.547  54.868 1.00 21.03  ? 46  HIS I O   1 
ATOM   9251  C  CB  . HIS I  1 47  ? 20.289  29.295  55.361 1.00 19.80  ? 46  HIS I CB  1 
ATOM   9252  C  CG  . HIS I  1 47  ? 20.072  30.612  54.706 1.00 20.61  ? 46  HIS I CG  1 
ATOM   9253  N  ND1 . HIS I  1 47  ? 19.488  30.722  53.450 1.00 20.86  ? 46  HIS I ND1 1 
ATOM   9254  C  CD2 . HIS I  1 47  ? 20.369  31.864  55.115 1.00 20.58  ? 46  HIS I CD2 1 
ATOM   9255  C  CE1 . HIS I  1 47  ? 19.432  31.998  53.117 1.00 19.98  ? 46  HIS I CE1 1 
ATOM   9256  N  NE2 . HIS I  1 47  ? 19.970  32.715  54.119 1.00 20.58  ? 46  HIS I NE2 1 
ATOM   9257  N  N   . VAL I  1 48  ? 21.752  27.137  57.064 1.00 22.76  ? 47  VAL I N   1 
ATOM   9258  C  CA  . VAL I  1 48  ? 21.454  25.802  57.540 1.00 23.95  ? 47  VAL I CA  1 
ATOM   9259  C  C   . VAL I  1 48  ? 19.943  25.686  57.718 1.00 24.69  ? 47  VAL I C   1 
ATOM   9260  O  O   . VAL I  1 48  ? 19.373  26.390  58.548 1.00 24.58  ? 47  VAL I O   1 
ATOM   9261  C  CB  . VAL I  1 48  ? 22.193  25.479  58.853 1.00 23.30  ? 47  VAL I CB  1 
ATOM   9262  C  CG1 . VAL I  1 48  ? 21.918  24.050  59.299 1.00 23.52  ? 47  VAL I CG1 1 
ATOM   9263  C  CG2 . VAL I  1 48  ? 23.690  25.716  58.727 1.00 23.31  ? 47  VAL I CG2 1 
ATOM   9264  N  N   . HIS I  1 49  ? 19.320  24.791  56.942 1.00 25.32  ? 48  HIS I N   1 
ATOM   9265  C  CA  . HIS I  1 49  ? 17.919  24.448  57.112 1.00 27.14  ? 48  HIS I CA  1 
ATOM   9266  C  C   . HIS I  1 49  ? 17.758  23.314  58.127 1.00 29.62  ? 48  HIS I C   1 
ATOM   9267  O  O   . HIS I  1 49  ? 18.731  22.674  58.505 1.00 31.44  ? 48  HIS I O   1 
ATOM   9268  C  CB  . HIS I  1 49  ? 17.285  24.135  55.758 1.00 27.87  ? 48  HIS I CB  1 
ATOM   9269  C  CG  . HIS I  1 49  ? 17.220  25.315  54.851 1.00 28.43  ? 48  HIS I CG  1 
ATOM   9270  N  ND1 . HIS I  1 49  ? 16.023  25.792  54.348 1.00 27.44  ? 48  HIS I ND1 1 
ATOM   9271  C  CD2 . HIS I  1 49  ? 18.196  26.106  54.345 1.00 29.40  ? 48  HIS I CD2 1 
ATOM   9272  C  CE1 . HIS I  1 49  ? 16.262  26.826  53.560 1.00 26.37  ? 48  HIS I CE1 1 
ATOM   9273  N  NE2 . HIS I  1 49  ? 17.587  27.039  53.541 1.00 27.36  ? 48  HIS I NE2 1 
ATOM   9274  N  N   . GLU I  1 50  ? 16.507  23.053  58.534 1.00 29.74  ? 49  GLU I N   1 
ATOM   9275  C  CA  . GLU I  1 50  ? 16.189  22.265  59.719 1.00 29.37  ? 49  GLU I CA  1 
ATOM   9276  C  C   . GLU I  1 50  ? 16.461  20.775  59.527 1.00 27.88  ? 49  GLU I C   1 
ATOM   9277  O  O   . GLU I  1 50  ? 16.978  20.133  60.436 1.00 26.55  ? 49  GLU I O   1 
ATOM   9278  C  CB  . GLU I  1 50  ? 14.722  22.442  60.100 1.00 31.48  ? 49  GLU I CB  1 
ATOM   9279  C  CG  . GLU I  1 50  ? 14.426  21.969  61.505 1.00 33.50  ? 49  GLU I CG  1 
ATOM   9280  C  CD  . GLU I  1 50  ? 12.981  22.123  61.951 1.00 35.30  ? 49  GLU I CD  1 
ATOM   9281  O  OE1 . GLU I  1 50  ? 12.220  22.919  61.321 1.00 34.17  ? 49  GLU I OE1 1 
ATOM   9282  O  OE2 . GLU I  1 50  ? 12.616  21.437  62.930 1.00 36.38  ? 49  GLU I OE2 1 
ATOM   9283  N  N   . PHE I  1 51  ? 16.091  20.230  58.362 1.00 24.88  ? 50  PHE I N   1 
ATOM   9284  C  CA  . PHE I  1 51  ? 16.056  18.789  58.184 1.00 24.48  ? 50  PHE I CA  1 
ATOM   9285  C  C   . PHE I  1 51  ? 17.127  18.317  57.210 1.00 25.01  ? 50  PHE I C   1 
ATOM   9286  O  O   . PHE I  1 51  ? 17.257  18.865  56.116 1.00 27.17  ? 50  PHE I O   1 
ATOM   9287  C  CB  . PHE I  1 51  ? 14.693  18.348  57.650 1.00 23.58  ? 50  PHE I CB  1 
ATOM   9288  C  CG  . PHE I  1 51  ? 13.551  18.802  58.514 1.00 23.06  ? 50  PHE I CG  1 
ATOM   9289  C  CD1 . PHE I  1 51  ? 13.514  18.468  59.866 1.00 22.25  ? 50  PHE I CD1 1 
ATOM   9290  C  CD2 . PHE I  1 51  ? 12.530  19.582  57.987 1.00 23.19  ? 50  PHE I CD2 1 
ATOM   9291  C  CE1 . PHE I  1 51  ? 12.476  18.894  60.677 1.00 21.33  ? 50  PHE I CE1 1 
ATOM   9292  C  CE2 . PHE I  1 51  ? 11.485  20.007  58.795 1.00 22.50  ? 50  PHE I CE2 1 
ATOM   9293  C  CZ  . PHE I  1 51  ? 11.468  19.666  60.137 1.00 22.64  ? 50  PHE I CZ  1 
ATOM   9294  N  N   . GLY I  1 52  ? 17.847  17.268  57.626 1.00 24.92  ? 51  GLY I N   1 
ATOM   9295  C  CA  . GLY I  1 52  ? 18.722  16.505  56.755 1.00 25.47  ? 51  GLY I CA  1 
ATOM   9296  C  C   . GLY I  1 52  ? 17.911  15.557  55.876 1.00 26.28  ? 51  GLY I C   1 
ATOM   9297  O  O   . GLY I  1 52  ? 18.136  14.349  55.880 1.00 29.04  ? 51  GLY I O   1 
ATOM   9298  N  N   . ASP I  1 53  ? 16.959  16.124  55.137 1.00 25.08  ? 52  ASP I N   1 
ATOM   9299  C  CA  . ASP I  1 53  ? 16.018  15.318  54.388 1.00 24.94  ? 52  ASP I CA  1 
ATOM   9300  C  C   . ASP I  1 53  ? 16.037  15.780  52.939 1.00 24.96  ? 52  ASP I C   1 
ATOM   9301  O  O   . ASP I  1 53  ? 15.668  16.905  52.640 1.00 28.36  ? 52  ASP I O   1 
ATOM   9302  C  CB  . ASP I  1 53  ? 14.630  15.420  55.020 1.00 24.77  ? 52  ASP I CB  1 
ATOM   9303  C  CG  . ASP I  1 53  ? 13.556  14.603  54.328 1.00 24.42  ? 52  ASP I CG  1 
ATOM   9304  O  OD1 . ASP I  1 53  ? 13.723  14.294  53.119 1.00 24.24  ? 52  ASP I OD1 1 
ATOM   9305  O  OD2 . ASP I  1 53  ? 12.540  14.330  55.000 1.00 22.06  ? 52  ASP I OD2 1 
ATOM   9306  N  N   . ASN I  1 54  ? 16.480  14.910  52.042 1.00 24.93  ? 53  ASN I N   1 
ATOM   9307  C  CA  . ASN I  1 54  ? 16.626  15.268  50.644 1.00 25.05  ? 53  ASN I CA  1 
ATOM   9308  C  C   . ASN I  1 54  ? 15.645  14.440  49.807 1.00 25.23  ? 53  ASN I C   1 
ATOM   9309  O  O   . ASN I  1 54  ? 15.788  14.337  48.593 1.00 24.75  ? 53  ASN I O   1 
ATOM   9310  C  CB  . ASN I  1 54  ? 18.096  15.171  50.228 1.00 27.32  ? 53  ASN I CB  1 
ATOM   9311  C  CG  . ASN I  1 54  ? 18.366  15.537  48.782 1.00 32.16  ? 53  ASN I CG  1 
ATOM   9312  O  OD1 . ASN I  1 54  ? 18.007  16.626  48.345 1.00 33.38  ? 53  ASN I OD1 1 
ATOM   9313  N  ND2 . ASN I  1 54  ? 19.010  14.647  48.033 1.00 34.48  ? 53  ASN I ND2 1 
ATOM   9314  N  N   . THR I  1 55  ? 14.619  13.878  50.459 1.00 25.71  ? 54  THR I N   1 
ATOM   9315  C  CA  . THR I  1 55  ? 13.727  12.931  49.804 1.00 25.09  ? 54  THR I CA  1 
ATOM   9316  C  C   . THR I  1 55  ? 13.021  13.569  48.611 1.00 23.94  ? 54  THR I C   1 
ATOM   9317  O  O   . THR I  1 55  ? 12.728  12.885  47.640 1.00 22.98  ? 54  THR I O   1 
ATOM   9318  C  CB  . THR I  1 55  ? 12.684  12.344  50.762 1.00 24.19  ? 54  THR I CB  1 
ATOM   9319  O  OG1 . THR I  1 55  ? 11.952  13.430  51.312 1.00 22.75  ? 54  THR I OG1 1 
ATOM   9320  C  CG2 . THR I  1 55  ? 13.286  11.529  51.882 1.00 24.57  ? 54  THR I CG2 1 
ATOM   9321  N  N   . ALA I  1 56  ? 12.746  14.871  48.699 1.00 24.59  ? 55  ALA I N   1 
ATOM   9322  C  CA  . ALA I  1 56  ? 12.051  15.579  47.640 1.00 26.16  ? 55  ALA I CA  1 
ATOM   9323  C  C   . ALA I  1 56  ? 12.924  16.733  47.156 1.00 28.15  ? 55  ALA I C   1 
ATOM   9324  O  O   . ALA I  1 56  ? 12.439  17.850  46.975 1.00 34.66  ? 55  ALA I O   1 
ATOM   9325  C  CB  . ALA I  1 56  ? 10.730  16.075  48.172 1.00 25.35  ? 55  ALA I CB  1 
ATOM   9326  N  N   . GLY I  1 57  ? 14.221  16.468  46.987 1.00 27.52  ? 56  GLY I N   1 
ATOM   9327  C  CA  . GLY I  1 57  ? 15.171  17.511  46.641 1.00 28.28  ? 56  GLY I CA  1 
ATOM   9328  C  C   . GLY I  1 57  ? 15.433  18.437  47.826 1.00 29.18  ? 56  GLY I C   1 
ATOM   9329  O  O   . GLY I  1 57  ? 15.207  18.065  48.981 1.00 30.46  ? 56  GLY I O   1 
ATOM   9330  N  N   . CYS I  1 58  ? 15.893  19.661  47.529 1.00 27.27  ? 57  CYS I N   1 
ATOM   9331  C  CA  . CYS I  1 58  ? 16.273  20.580  48.587 1.00 25.60  ? 57  CYS I CA  1 
ATOM   9332  C  C   . CYS I  1 58  ? 15.054  21.059  49.368 1.00 24.89  ? 57  CYS I C   1 
ATOM   9333  O  O   . CYS I  1 58  ? 15.198  21.465  50.520 1.00 23.87  ? 57  CYS I O   1 
ATOM   9334  C  CB  . CYS I  1 58  ? 17.056  21.757  48.034 1.00 23.87  ? 57  CYS I CB  1 
ATOM   9335  S  SG  . CYS I  1 58  ? 18.684  21.267  47.411 1.00 25.23  ? 57  CYS I SG  1 
ATOM   9336  N  N   . THR I  1 59  ? 13.865  20.979  48.746 1.00 25.04  ? 58  THR I N   1 
ATOM   9337  C  CA  . THR I  1 59  ? 12.633  21.459  49.356 1.00 26.96  ? 58  THR I CA  1 
ATOM   9338  C  C   . THR I  1 59  ? 12.404  20.793  50.708 1.00 27.21  ? 58  THR I C   1 
ATOM   9339  O  O   . THR I  1 59  ? 11.924  21.429  51.643 1.00 26.45  ? 58  THR I O   1 
ATOM   9340  C  CB  . THR I  1 59  ? 11.396  21.094  48.529 1.00 26.74  ? 58  THR I CB  1 
ATOM   9341  O  OG1 . THR I  1 59  ? 11.667  21.476  47.184 1.00 28.05  ? 58  THR I OG1 1 
ATOM   9342  C  CG2 . THR I  1 59  ? 10.140  21.769  49.039 1.00 24.97  ? 58  THR I CG2 1 
ATOM   9343  N  N   . SER I  1 60  ? 12.722  19.497  50.790 1.00 27.10  ? 59  SER I N   1 
ATOM   9344  C  CA  . SER I  1 60  ? 12.309  18.729  51.951 1.00 27.47  ? 59  SER I CA  1 
ATOM   9345  C  C   . SER I  1 60  ? 13.211  19.020  53.152 1.00 25.85  ? 59  SER I C   1 
ATOM   9346  O  O   . SER I  1 60  ? 13.006  18.475  54.233 1.00 25.34  ? 59  SER I O   1 
ATOM   9347  C  CB  . SER I  1 60  ? 12.139  17.261  51.630 1.00 28.99  ? 59  SER I CB  1 
ATOM   9348  O  OG  . SER I  1 60  ? 13.310  16.739  51.038 1.00 30.89  ? 59  SER I OG  1 
ATOM   9349  N  N   . ALA I  1 61  ? 14.162  19.945  52.964 1.00 25.48  ? 60  ALA I N   1 
ATOM   9350  C  CA  . ALA I  1 61  ? 15.078  20.367  54.013 1.00 24.25  ? 60  ALA I CA  1 
ATOM   9351  C  C   . ALA I  1 61  ? 14.346  21.238  55.032 1.00 24.40  ? 60  ALA I C   1 
ATOM   9352  O  O   . ALA I  1 61  ? 14.828  21.432  56.151 1.00 25.59  ? 60  ALA I O   1 
ATOM   9353  C  CB  . ALA I  1 61  ? 16.245  21.100  53.410 1.00 23.90  ? 60  ALA I CB  1 
ATOM   9354  N  N   . GLY I  1 62  ? 13.184  21.763  54.625 1.00 22.56  ? 61  GLY I N   1 
ATOM   9355  C  CA  . GLY I  1 62  ? 12.357  22.591  55.484 1.00 22.22  ? 61  GLY I CA  1 
ATOM   9356  C  C   . GLY I  1 62  ? 12.890  24.020  55.592 1.00 23.53  ? 61  GLY I C   1 
ATOM   9357  O  O   . GLY I  1 62  ? 13.675  24.467  54.749 1.00 23.47  ? 61  GLY I O   1 
ATOM   9358  N  N   . PRO I  1 63  ? 12.496  24.770  56.654 1.00 23.79  ? 62  PRO I N   1 
ATOM   9359  C  CA  . PRO I  1 63  ? 12.871  26.179  56.806 1.00 23.34  ? 62  PRO I CA  1 
ATOM   9360  C  C   . PRO I  1 63  ? 14.283  26.333  57.377 1.00 24.42  ? 62  PRO I C   1 
ATOM   9361  O  O   . PRO I  1 63  ? 14.947  25.343  57.678 1.00 22.69  ? 62  PRO I O   1 
ATOM   9362  C  CB  . PRO I  1 63  ? 11.850  26.647  57.856 1.00 23.38  ? 62  PRO I CB  1 
ATOM   9363  C  CG  . PRO I  1 63  ? 11.664  25.450  58.750 1.00 22.76  ? 62  PRO I CG  1 
ATOM   9364  C  CD  . PRO I  1 63  ? 11.704  24.274  57.800 1.00 23.50  ? 62  PRO I CD  1 
ATOM   9365  N  N   . HIS I  1 64  ? 14.739  27.586  57.520 1.00 24.70  ? 63  HIS I N   1 
ATOM   9366  C  CA  . HIS I  1 64  ? 16.004  27.831  58.186 1.00 22.85  ? 63  HIS I CA  1 
ATOM   9367  C  C   . HIS I  1 64  ? 15.962  27.201  59.574 1.00 22.43  ? 63  HIS I C   1 
ATOM   9368  O  O   . HIS I  1 64  ? 14.960  27.318  60.256 1.00 22.85  ? 63  HIS I O   1 
ATOM   9369  C  CB  . HIS I  1 64  ? 16.307  29.322  58.281 1.00 20.95  ? 63  HIS I CB  1 
ATOM   9370  C  CG  . HIS I  1 64  ? 16.448  30.039  56.985 1.00 19.91  ? 63  HIS I CG  1 
ATOM   9371  N  ND1 . HIS I  1 64  ? 16.570  31.398  56.914 1.00 20.36  ? 63  HIS I ND1 1 
ATOM   9372  C  CD2 . HIS I  1 64  ? 16.507  29.605  55.720 1.00 19.82  ? 63  HIS I CD2 1 
ATOM   9373  C  CE1 . HIS I  1 64  ? 16.681  31.768  55.656 1.00 20.21  ? 63  HIS I CE1 1 
ATOM   9374  N  NE2 . HIS I  1 64  ? 16.660  30.685  54.905 1.00 19.85  ? 63  HIS I NE2 1 
ATOM   9375  N  N   . PHE I  1 65  ? 17.053  26.547  59.977 1.00 21.86  ? 64  PHE I N   1 
ATOM   9376  C  CA  . PHE I  1 65  ? 17.170  25.953  61.300 1.00 22.48  ? 64  PHE I CA  1 
ATOM   9377  C  C   . PHE I  1 65  ? 16.925  27.006  62.375 1.00 21.97  ? 64  PHE I C   1 
ATOM   9378  O  O   . PHE I  1 65  ? 17.695  27.946  62.509 1.00 21.86  ? 64  PHE I O   1 
ATOM   9379  C  CB  . PHE I  1 65  ? 18.517  25.240  61.465 1.00 22.28  ? 64  PHE I CB  1 
ATOM   9380  C  CG  . PHE I  1 65  ? 18.718  24.578  62.808 1.00 21.98  ? 64  PHE I CG  1 
ATOM   9381  C  CD1 . PHE I  1 65  ? 17.693  23.852  63.411 1.00 22.59  ? 64  PHE I CD1 1 
ATOM   9382  C  CD2 . PHE I  1 65  ? 19.934  24.669  63.472 1.00 21.31  ? 64  PHE I CD2 1 
ATOM   9383  C  CE1 . PHE I  1 65  ? 17.879  23.250  64.649 1.00 22.01  ? 64  PHE I CE1 1 
ATOM   9384  C  CE2 . PHE I  1 65  ? 20.119  24.060  64.703 1.00 20.78  ? 64  PHE I CE2 1 
ATOM   9385  C  CZ  . PHE I  1 65  ? 19.095  23.350  65.289 1.00 21.45  ? 64  PHE I CZ  1 
ATOM   9386  N  N   . ASN I  1 66  ? 15.854  26.820  63.158 1.00 22.24  ? 65  ASN I N   1 
ATOM   9387  C  CA  . ASN I  1 66  ? 15.382  27.904  63.997 1.00 24.81  ? 65  ASN I CA  1 
ATOM   9388  C  C   . ASN I  1 66  ? 14.973  27.388  65.378 1.00 27.33  ? 65  ASN I C   1 
ATOM   9389  O  O   . ASN I  1 66  ? 13.850  27.627  65.827 1.00 27.48  ? 65  ASN I O   1 
ATOM   9390  C  CB  . ASN I  1 66  ? 14.259  28.676  63.294 1.00 23.11  ? 65  ASN I CB  1 
ATOM   9391  C  CG  . ASN I  1 66  ? 13.808  29.894  64.062 1.00 21.78  ? 65  ASN I CG  1 
ATOM   9392  O  OD1 . ASN I  1 66  ? 14.528  30.405  64.912 1.00 21.71  ? 65  ASN I OD1 1 
ATOM   9393  N  ND2 . ASN I  1 66  ? 12.610  30.361  63.774 1.00 22.24  ? 65  ASN I ND2 1 
ATOM   9394  N  N   . PRO I  1 67  ? 15.872  26.740  66.157 1.00 28.55  ? 66  PRO I N   1 
ATOM   9395  C  CA  . PRO I  1 67  ? 15.462  26.136  67.428 1.00 28.66  ? 66  PRO I CA  1 
ATOM   9396  C  C   . PRO I  1 67  ? 14.972  27.130  68.483 1.00 31.61  ? 66  PRO I C   1 
ATOM   9397  O  O   . PRO I  1 67  ? 14.296  26.735  69.428 1.00 31.30  ? 66  PRO I O   1 
ATOM   9398  C  CB  . PRO I  1 67  ? 16.734  25.456  67.948 1.00 28.00  ? 66  PRO I CB  1 
ATOM   9399  C  CG  . PRO I  1 67  ? 17.873  26.164  67.227 1.00 28.94  ? 66  PRO I CG  1 
ATOM   9400  C  CD  . PRO I  1 67  ? 17.316  26.614  65.893 1.00 28.58  ? 66  PRO I CD  1 
ATOM   9401  N  N   . LEU I  1 68  ? 15.298  28.421  68.321 1.00 34.13  ? 67  LEU I N   1 
ATOM   9402  C  CA  . LEU I  1 68  ? 14.958  29.407  69.333 1.00 33.82  ? 67  LEU I CA  1 
ATOM   9403  C  C   . LEU I  1 68  ? 13.741  30.235  68.928 1.00 34.22  ? 67  LEU I C   1 
ATOM   9404  O  O   . LEU I  1 68  ? 13.392  31.182  69.623 1.00 37.96  ? 67  LEU I O   1 
ATOM   9405  C  CB  . LEU I  1 68  ? 16.172  30.305  69.596 1.00 36.47  ? 67  LEU I CB  1 
ATOM   9406  C  CG  . LEU I  1 68  ? 17.365  29.651  70.298 1.00 38.28  ? 67  LEU I CG  1 
ATOM   9407  C  CD1 . LEU I  1 68  ? 18.417  30.711  70.634 1.00 40.57  ? 67  LEU I CD1 1 
ATOM   9408  C  CD2 . LEU I  1 68  ? 16.914  28.924  71.561 1.00 38.26  ? 67  LEU I CD2 1 
ATOM   9409  N  N   . SER I  1 69  ? 13.110  29.887  67.801 1.00 34.55  ? 68  SER I N   1 
ATOM   9410  C  CA  . SER I  1 69  ? 11.886  30.521  67.322 1.00 36.22  ? 68  SER I CA  1 
ATOM   9411  C  C   . SER I  1 69  ? 12.035  32.034  67.185 1.00 35.57  ? 68  SER I C   1 
ATOM   9412  O  O   . SER I  1 69  ? 11.214  32.761  67.722 1.00 34.23  ? 68  SER I O   1 
ATOM   9413  C  CB  . SER I  1 69  ? 10.729  30.195  68.213 1.00 35.01  ? 68  SER I CB  1 
ATOM   9414  O  OG  . SER I  1 69  ? 10.425  28.818  68.135 1.00 32.07  ? 68  SER I OG  1 
ATOM   9415  N  N   . ARG I  1 70  ? 13.062  32.492  66.461 1.00 36.89  ? 69  ARG I N   1 
ATOM   9416  C  CA  . ARG I  1 70  ? 13.259  33.912  66.212 1.00 37.45  ? 69  ARG I CA  1 
ATOM   9417  C  C   . ARG I  1 70  ? 12.957  34.216  64.745 1.00 37.58  ? 69  ARG I C   1 
ATOM   9418  O  O   . ARG I  1 70  ? 12.721  33.300  63.954 1.00 35.78  ? 69  ARG I O   1 
ATOM   9419  C  CB  . ARG I  1 70  ? 14.688  34.337  66.562 1.00 38.91  ? 69  ARG I CB  1 
ATOM   9420  C  CG  . ARG I  1 70  ? 15.149  33.929  67.954 1.00 44.77  ? 69  ARG I CG  1 
ATOM   9421  C  CD  . ARG I  1 70  ? 14.883  34.949  69.053 1.00 49.85  ? 69  ARG I CD  1 
ATOM   9422  N  NE  . ARG I  1 70  ? 15.680  34.582  70.217 1.00 59.89  ? 69  ARG I NE  1 
ATOM   9423  C  CZ  . ARG I  1 70  ? 16.963  34.940  70.428 1.00 69.45  ? 69  ARG I CZ  1 
ATOM   9424  N  NH1 . ARG I  1 70  ? 17.627  35.679  69.535 1.00 83.53  ? 69  ARG I NH1 1 
ATOM   9425  N  NH2 . ARG I  1 70  ? 17.577  34.547  71.540 1.00 65.15  ? 69  ARG I NH2 1 
ATOM   9426  N  N   . LYS I  1 71  ? 12.969  35.510  64.399 1.00 35.75  ? 70  LYS I N   1 
ATOM   9427  C  CA  . LYS I  1 71  ? 12.785  35.948  63.023 1.00 32.92  ? 70  LYS I CA  1 
ATOM   9428  C  C   . LYS I  1 71  ? 14.137  35.918  62.308 1.00 30.27  ? 70  LYS I C   1 
ATOM   9429  O  O   . LYS I  1 71  ? 15.188  35.906  62.957 1.00 30.64  ? 70  LYS I O   1 
ATOM   9430  C  CB  . LYS I  1 71  ? 12.052  37.296  62.968 1.00 33.35  ? 70  LYS I CB  1 
ATOM   9431  C  CG  . LYS I  1 71  ? 10.729  37.352  63.722 1.00 36.95  ? 70  LYS I CG  1 
ATOM   9432  C  CD  . LYS I  1 71  ? 9.574   36.956  62.834 1.00 40.31  ? 70  LYS I CD  1 
ATOM   9433  C  CE  . LYS I  1 71  ? 8.243   37.575  63.176 1.00 39.45  ? 70  LYS I CE  1 
ATOM   9434  N  NZ  . LYS I  1 71  ? 7.297   37.258  62.086 1.00 38.19  ? 70  LYS I NZ  1 
ATOM   9435  N  N   . HIS I  1 72  ? 14.100  35.883  60.968 1.00 26.73  ? 71  HIS I N   1 
ATOM   9436  C  CA  . HIS I  1 72  ? 15.303  35.780  60.159 1.00 24.28  ? 71  HIS I CA  1 
ATOM   9437  C  C   . HIS I  1 72  ? 16.139  37.051  60.272 1.00 25.07  ? 71  HIS I C   1 
ATOM   9438  O  O   . HIS I  1 72  ? 15.599  38.144  60.295 1.00 25.97  ? 71  HIS I O   1 
ATOM   9439  C  CB  . HIS I  1 72  ? 14.918  35.456  58.711 1.00 24.28  ? 71  HIS I CB  1 
ATOM   9440  C  CG  . HIS I  1 72  ? 16.076  35.450  57.778 1.00 25.84  ? 71  HIS I CG  1 
ATOM   9441  N  ND1 . HIS I  1 72  ? 16.897  34.346  57.584 1.00 24.96  ? 71  HIS I ND1 1 
ATOM   9442  C  CD2 . HIS I  1 72  ? 16.559  36.409  56.974 1.00 26.94  ? 71  HIS I CD2 1 
ATOM   9443  C  CE1 . HIS I  1 72  ? 17.833  34.659  56.708 1.00 24.34  ? 71  HIS I CE1 1 
ATOM   9444  N  NE2 . HIS I  1 72  ? 17.648  35.910  56.318 1.00 26.11  ? 71  HIS I NE2 1 
ATOM   9445  N  N   . GLY I  1 73  ? 17.463  36.896  60.355 1.00 26.19  ? 72  GLY I N   1 
ATOM   9446  C  CA  . GLY I  1 73  ? 18.387  38.016  60.373 1.00 27.58  ? 72  GLY I CA  1 
ATOM   9447  C  C   . GLY I  1 73  ? 19.649  37.716  59.563 1.00 29.67  ? 72  GLY I C   1 
ATOM   9448  O  O   . GLY I  1 73  ? 19.752  36.672  58.945 1.00 31.33  ? 72  GLY I O   1 
ATOM   9449  N  N   . GLY I  1 74  ? 20.578  38.679  59.521 1.00 29.48  ? 73  GLY I N   1 
ATOM   9450  C  CA  . GLY I  1 74  ? 21.944  38.460  59.084 1.00 27.62  ? 73  GLY I CA  1 
ATOM   9451  C  C   . GLY I  1 74  ? 22.747  37.832  60.220 1.00 28.79  ? 73  GLY I C   1 
ATOM   9452  O  O   . GLY I  1 74  ? 22.331  37.904  61.382 1.00 30.45  ? 73  GLY I O   1 
ATOM   9453  N  N   . PRO I  1 75  ? 23.904  37.181  59.942 1.00 27.74  ? 74  PRO I N   1 
ATOM   9454  C  CA  . PRO I  1 75  ? 24.648  36.479  60.989 1.00 27.13  ? 74  PRO I CA  1 
ATOM   9455  C  C   . PRO I  1 75  ? 25.006  37.376  62.169 1.00 26.64  ? 74  PRO I C   1 
ATOM   9456  O  O   . PRO I  1 75  ? 25.108  36.909  63.296 1.00 25.55  ? 74  PRO I O   1 
ATOM   9457  C  CB  . PRO I  1 75  ? 25.911  35.960  60.287 1.00 26.28  ? 74  PRO I CB  1 
ATOM   9458  C  CG  . PRO I  1 75  ? 25.956  36.686  58.963 1.00 24.50  ? 74  PRO I CG  1 
ATOM   9459  C  CD  . PRO I  1 75  ? 24.533  37.061  58.620 1.00 26.15  ? 74  PRO I CD  1 
ATOM   9460  N  N   . LYS I  1 76  ? 25.146  38.681  61.904 1.00 29.20  ? 75  LYS I N   1 
ATOM   9461  C  CA  . LYS I  1 76  ? 25.629  39.621  62.900 1.00 30.38  ? 75  LYS I CA  1 
ATOM   9462  C  C   . LYS I  1 76  ? 24.497  40.130  63.797 1.00 31.03  ? 75  LYS I C   1 
ATOM   9463  O  O   . LYS I  1 76  ? 24.772  40.758  64.801 1.00 32.06  ? 75  LYS I O   1 
ATOM   9464  C  CB  . LYS I  1 76  ? 26.423  40.737  62.220 1.00 27.85  ? 75  LYS I CB  1 
ATOM   9465  C  CG  . LYS I  1 76  ? 27.320  41.556  63.139 0.40 28.38  ? 75  LYS I CG  1 
ATOM   9466  C  CD  . LYS I  1 76  ? 27.766  42.885  62.553 0.40 27.89  ? 75  LYS I CD  1 
ATOM   9467  C  CE  . LYS I  1 76  ? 28.272  43.863  63.599 0.40 25.91  ? 75  LYS I CE  1 
ATOM   9468  N  NZ  . LYS I  1 76  ? 29.469  44.612  63.146 0.40 23.73  ? 75  LYS I NZ  1 
ATOM   9469  N  N   . ASP I  1 77  ? 23.238  39.858  63.442 1.00 32.69  ? 76  ASP I N   1 
ATOM   9470  C  CA  . ASP I  1 77  ? 22.065  40.345  64.163 1.00 33.30  ? 76  ASP I CA  1 
ATOM   9471  C  C   . ASP I  1 77  ? 21.843  39.524  65.425 1.00 35.89  ? 76  ASP I C   1 
ATOM   9472  O  O   . ASP I  1 77  ? 22.189  38.344  65.478 1.00 38.99  ? 76  ASP I O   1 
ATOM   9473  C  CB  . ASP I  1 77  ? 20.810  40.318  63.283 1.00 34.81  ? 76  ASP I CB  1 
ATOM   9474  C  CG  . ASP I  1 77  ? 20.868  41.369  62.178 1.00 38.81  ? 76  ASP I CG  1 
ATOM   9475  O  OD1 . ASP I  1 77  ? 21.454  42.426  62.428 1.00 46.48  ? 76  ASP I OD1 1 
ATOM   9476  O  OD2 . ASP I  1 77  ? 20.361  41.129  61.075 1.00 38.10  ? 76  ASP I OD2 1 
ATOM   9477  N  N   . GLU I  1 78  ? 21.273  40.157  66.461 1.00 37.63  ? 77  GLU I N   1 
ATOM   9478  C  CA  . GLU I  1 78  ? 20.904  39.393  67.641 1.00 37.06  ? 77  GLU I CA  1 
ATOM   9479  C  C   . GLU I  1 78  ? 19.643  38.584  67.325 1.00 38.47  ? 77  GLU I C   1 
ATOM   9480  O  O   . GLU I  1 78  ? 19.508  37.441  67.751 1.00 41.65  ? 77  GLU I O   1 
ATOM   9481  C  CB  . GLU I  1 78  ? 20.796  40.308  68.853 0.20 35.36  ? 77  GLU I CB  1 
ATOM   9482  C  CG  . GLU I  1 78  ? 20.703  39.563  70.167 0.20 34.27  ? 77  GLU I CG  1 
ATOM   9483  C  CD  . GLU I  1 78  ? 19.617  40.038  71.119 0.20 33.62  ? 77  GLU I CD  1 
ATOM   9484  O  OE1 . GLU I  1 78  ? 18.477  40.344  70.689 0.20 32.41  ? 77  GLU I OE1 1 
ATOM   9485  O  OE2 . GLU I  1 78  ? 19.902  40.093  72.341 0.20 33.78  ? 77  GLU I OE2 1 
ATOM   9486  N  N   . GLU I  1 79  ? 18.735  39.197  66.548 1.00 35.32  ? 78  GLU I N   1 
ATOM   9487  C  CA  . GLU I  1 79  ? 17.522  38.532  66.092 1.00 32.17  ? 78  GLU I CA  1 
ATOM   9488  C  C   . GLU I  1 79  ? 17.845  37.798  64.783 1.00 31.30  ? 78  GLU I C   1 
ATOM   9489  O  O   . GLU I  1 79  ? 17.829  38.383  63.691 1.00 30.73  ? 78  GLU I O   1 
ATOM   9490  C  CB  . GLU I  1 79  ? 16.383  39.556  66.026 1.00 32.97  ? 78  GLU I CB  1 
ATOM   9491  C  CG  . GLU I  1 79  ? 14.998  39.007  65.702 1.00 36.79  ? 78  GLU I CG  1 
ATOM   9492  C  CD  . GLU I  1 79  ? 14.281  38.148  66.741 1.00 39.76  ? 78  GLU I CD  1 
ATOM   9493  O  OE1 . GLU I  1 79  ? 14.786  38.015  67.876 1.00 41.01  ? 78  GLU I OE1 1 
ATOM   9494  O  OE2 . GLU I  1 79  ? 13.201  37.596  66.407 1.00 37.21  ? 78  GLU I OE2 1 
ATOM   9495  N  N   . ARG I  1 80  ? 18.162  36.496  64.917 1.00 26.94  ? 79  ARG I N   1 
ATOM   9496  C  CA  . ARG I  1 80  ? 18.435  35.639  63.767 1.00 24.44  ? 79  ARG I CA  1 
ATOM   9497  C  C   . ARG I  1 80  ? 18.041  34.196  64.061 1.00 23.53  ? 79  ARG I C   1 
ATOM   9498  O  O   . ARG I  1 80  ? 17.925  33.790  65.217 1.00 25.07  ? 79  ARG I O   1 
ATOM   9499  C  CB  . ARG I  1 80  ? 19.923  35.662  63.401 1.00 23.91  ? 79  ARG I CB  1 
ATOM   9500  C  CG  . ARG I  1 80  ? 20.847  35.251  64.535 1.00 24.26  ? 79  ARG I CG  1 
ATOM   9501  C  CD  . ARG I  1 80  ? 22.278  35.129  64.028 1.00 25.10  ? 79  ARG I CD  1 
ATOM   9502  N  NE  . ARG I  1 80  ? 22.569  33.781  63.543 1.00 27.66  ? 79  ARG I NE  1 
ATOM   9503  C  CZ  . ARG I  1 80  ? 23.787  33.305  63.289 1.00 28.79  ? 79  ARG I CZ  1 
ATOM   9504  N  NH1 . ARG I  1 80  ? 24.863  34.058  63.463 1.00 28.80  ? 79  ARG I NH1 1 
ATOM   9505  N  NH2 . ARG I  1 80  ? 23.926  32.063  62.864 1.00 30.99  ? 79  ARG I NH2 1 
ATOM   9506  N  N   . HIS I  1 81  ? 17.848  33.432  62.983 1.00 22.13  ? 80  HIS I N   1 
ATOM   9507  C  CA  . HIS I  1 81  ? 17.807  31.982  63.038 1.00 21.10  ? 80  HIS I CA  1 
ATOM   9508  C  C   . HIS I  1 81  ? 19.223  31.479  63.308 1.00 22.09  ? 80  HIS I C   1 
ATOM   9509  O  O   . HIS I  1 81  ? 20.196  32.068  62.823 1.00 23.36  ? 80  HIS I O   1 
ATOM   9510  C  CB  . HIS I  1 81  ? 17.336  31.432  61.687 1.00 19.19  ? 80  HIS I CB  1 
ATOM   9511  C  CG  . HIS I  1 81  ? 15.980  31.889  61.297 1.00 18.93  ? 80  HIS I CG  1 
ATOM   9512  N  ND1 . HIS I  1 81  ? 15.622  32.127  59.988 1.00 19.45  ? 80  HIS I ND1 1 
ATOM   9513  C  CD2 . HIS I  1 81  ? 14.881  32.138  62.040 1.00 18.68  ? 80  HIS I CD2 1 
ATOM   9514  C  CE1 . HIS I  1 81  ? 14.356  32.492  59.927 1.00 19.41  ? 80  HIS I CE1 1 
ATOM   9515  N  NE2 . HIS I  1 81  ? 13.883  32.521  61.179 1.00 19.31  ? 80  HIS I NE2 1 
ATOM   9516  N  N   . VAL I  1 82  ? 19.329  30.374  64.054 1.00 21.63  ? 81  VAL I N   1 
ATOM   9517  C  CA  . VAL I  1 82  ? 20.625  29.745  64.249 1.00 19.71  ? 81  VAL I CA  1 
ATOM   9518  C  C   . VAL I  1 82  ? 21.276  29.487  62.892 1.00 18.90  ? 81  VAL I C   1 
ATOM   9519  O  O   . VAL I  1 82  ? 22.470  29.688  62.744 1.00 18.86  ? 81  VAL I O   1 
ATOM   9520  C  CB  . VAL I  1 82  ? 20.539  28.471  65.116 1.00 19.86  ? 81  VAL I CB  1 
ATOM   9521  C  CG1 . VAL I  1 82  ? 21.785  27.618  65.012 1.00 20.33  ? 81  VAL I CG1 1 
ATOM   9522  C  CG2 . VAL I  1 82  ? 20.263  28.807  66.566 1.00 21.27  ? 81  VAL I CG2 1 
ATOM   9523  N  N   . GLY I  1 83  ? 20.483  29.081  61.896 1.00 18.49  ? 82  GLY I N   1 
ATOM   9524  C  CA  . GLY I  1 83  ? 21.035  28.683  60.614 1.00 18.40  ? 82  GLY I CA  1 
ATOM   9525  C  C   . GLY I  1 83  ? 21.395  29.850  59.697 1.00 18.05  ? 82  GLY I C   1 
ATOM   9526  O  O   . GLY I  1 83  ? 21.771  29.626  58.537 1.00 17.61  ? 82  GLY I O   1 
ATOM   9527  N  N   . ASP I  1 84  ? 21.228  31.088  60.198 1.00 18.25  ? 83  ASP I N   1 
ATOM   9528  C  CA  . ASP I  1 84  ? 21.364  32.292  59.386 1.00 19.39  ? 83  ASP I CA  1 
ATOM   9529  C  C   . ASP I  1 84  ? 22.834  32.676  59.198 1.00 20.54  ? 83  ASP I C   1 
ATOM   9530  O  O   . ASP I  1 84  ? 23.421  33.344  60.054 1.00 20.42  ? 83  ASP I O   1 
ATOM   9531  C  CB  . ASP I  1 84  ? 20.518  33.428  59.953 1.00 20.00  ? 83  ASP I CB  1 
ATOM   9532  C  CG  . ASP I  1 84  ? 19.023  33.290  59.692 1.00 21.43  ? 83  ASP I CG  1 
ATOM   9533  O  OD1 . ASP I  1 84  ? 18.648  32.495  58.811 1.00 21.77  ? 83  ASP I OD1 1 
ATOM   9534  O  OD2 . ASP I  1 84  ? 18.242  33.999  60.358 1.00 22.64  ? 83  ASP I OD2 1 
ATOM   9535  N  N   . LEU I  1 85  ? 23.429  32.270  58.069 1.00 21.89  ? 84  LEU I N   1 
ATOM   9536  C  CA  . LEU I  1 85  ? 24.855  32.486  57.860 1.00 22.94  ? 84  LEU I CA  1 
ATOM   9537  C  C   . LEU I  1 85  ? 25.099  33.597  56.836 1.00 24.83  ? 84  LEU I C   1 
ATOM   9538  O  O   . LEU I  1 85  ? 26.237  33.782  56.389 1.00 27.01  ? 84  LEU I O   1 
ATOM   9539  C  CB  . LEU I  1 85  ? 25.514  31.178  57.408 1.00 22.35  ? 84  LEU I CB  1 
ATOM   9540  C  CG  . LEU I  1 85  ? 25.658  30.087  58.467 1.00 22.69  ? 84  LEU I CG  1 
ATOM   9541  C  CD1 . LEU I  1 85  ? 26.449  28.913  57.913 1.00 21.86  ? 84  LEU I CD1 1 
ATOM   9542  C  CD2 . LEU I  1 85  ? 26.328  30.605  59.729 1.00 21.84  ? 84  LEU I CD2 1 
ATOM   9543  N  N   . GLY I  1 86  ? 24.044  34.332  56.458 1.00 23.87  ? 85  GLY I N   1 
ATOM   9544  C  CA  . GLY I  1 86  ? 24.221  35.486  55.586 1.00 25.31  ? 85  GLY I CA  1 
ATOM   9545  C  C   . GLY I  1 86  ? 24.440  35.090  54.121 1.00 26.47  ? 85  GLY I C   1 
ATOM   9546  O  O   . GLY I  1 86  ? 23.758  34.196  53.609 1.00 28.96  ? 85  GLY I O   1 
ATOM   9547  N  N   . ASN I  1 87  ? 25.377  35.780  53.449 1.00 24.22  ? 86  ASN I N   1 
ATOM   9548  C  CA  . ASN I  1 87  ? 25.599  35.579  52.024 1.00 23.32  ? 86  ASN I CA  1 
ATOM   9549  C  C   . ASN I  1 87  ? 27.005  35.052  51.748 1.00 23.26  ? 86  ASN I C   1 
ATOM   9550  O  O   . ASN I  1 87  ? 27.926  35.196  52.559 1.00 23.39  ? 86  ASN I O   1 
ATOM   9551  C  CB  . ASN I  1 87  ? 25.413  36.863  51.218 1.00 23.69  ? 86  ASN I CB  1 
ATOM   9552  C  CG  . ASN I  1 87  ? 23.977  37.325  51.212 1.00 24.33  ? 86  ASN I CG  1 
ATOM   9553  O  OD1 . ASN I  1 87  ? 23.138  36.753  50.525 1.00 27.34  ? 86  ASN I OD1 1 
ATOM   9554  N  ND2 . ASN I  1 87  ? 23.678  38.336  52.007 1.00 25.97  ? 86  ASN I ND2 1 
ATOM   9555  N  N   . VAL I  1 88  ? 27.139  34.422  50.581 1.00 20.88  ? 87  VAL I N   1 
ATOM   9556  C  CA  . VAL I  1 88  ? 28.435  34.131  50.002 1.00 20.08  ? 87  VAL I CA  1 
ATOM   9557  C  C   . VAL I  1 88  ? 28.485  34.862  48.663 1.00 19.82  ? 87  VAL I C   1 
ATOM   9558  O  O   . VAL I  1 88  ? 27.442  35.198  48.102 1.00 18.56  ? 87  VAL I O   1 
ATOM   9559  C  CB  . VAL I  1 88  ? 28.688  32.610  49.884 1.00 20.07  ? 87  VAL I CB  1 
ATOM   9560  C  CG1 . VAL I  1 88  ? 28.592  31.908  51.236 1.00 19.50  ? 87  VAL I CG1 1 
ATOM   9561  C  CG2 . VAL I  1 88  ? 27.753  31.939  48.888 1.00 20.83  ? 87  VAL I CG2 1 
ATOM   9562  N  N   . THR I  1 89  ? 29.693  35.138  48.162 1.00 20.51  ? 88  THR I N   1 
ATOM   9563  C  CA  . THR I  1 89  ? 29.818  35.947  46.961 1.00 22.56  ? 88  THR I CA  1 
ATOM   9564  C  C   . THR I  1 89  ? 30.466  35.130  45.853 1.00 24.48  ? 88  THR I C   1 
ATOM   9565  O  O   . THR I  1 89  ? 31.565  34.612  46.030 1.00 24.27  ? 88  THR I O   1 
ATOM   9566  C  CB  . THR I  1 89  ? 30.668  37.198  47.215 1.00 23.07  ? 88  THR I CB  1 
ATOM   9567  O  OG1 . THR I  1 89  ? 30.165  37.910  48.350 1.00 23.78  ? 88  THR I OG1 1 
ATOM   9568  C  CG2 . THR I  1 89  ? 30.759  38.089  45.995 1.00 21.53  ? 88  THR I CG2 1 
ATOM   9569  N  N   . ALA I  1 90  ? 29.791  35.058  44.703 1.00 27.13  ? 89  ALA I N   1 
ATOM   9570  C  CA  . ALA I  1 90  ? 30.371  34.406  43.538 1.00 29.23  ? 89  ALA I CA  1 
ATOM   9571  C  C   . ALA I  1 90  ? 31.036  35.446  42.638 1.00 32.44  ? 89  ALA I C   1 
ATOM   9572  O  O   . ALA I  1 90  ? 30.450  36.498  42.342 1.00 32.54  ? 89  ALA I O   1 
ATOM   9573  C  CB  . ALA I  1 90  ? 29.306  33.652  42.791 1.00 29.70  ? 89  ALA I CB  1 
ATOM   9574  N  N   . ASP I  1 91  ? 32.266  35.128  42.199 1.00 33.27  ? 90  ASP I N   1 
ATOM   9575  C  CA  . ASP I  1 91  ? 33.064  35.968  41.323 1.00 34.44  ? 90  ASP I CA  1 
ATOM   9576  C  C   . ASP I  1 91  ? 32.541  35.847  39.889 1.00 36.41  ? 90  ASP I C   1 
ATOM   9577  O  O   . ASP I  1 91  ? 31.573  35.130  39.638 1.00 32.24  ? 90  ASP I O   1 
ATOM   9578  C  CB  . ASP I  1 91  ? 34.553  35.631  41.437 1.00 37.27  ? 90  ASP I CB  1 
ATOM   9579  C  CG  . ASP I  1 91  ? 34.954  34.229  40.983 1.00 41.40  ? 90  ASP I CG  1 
ATOM   9580  O  OD1 . ASP I  1 91  ? 34.207  33.604  40.196 1.00 40.44  ? 90  ASP I OD1 1 
ATOM   9581  O  OD2 . ASP I  1 91  ? 36.029  33.765  41.426 1.00 42.77  ? 90  ASP I OD2 1 
ATOM   9582  N  N   . LYS I  1 92  ? 33.203  36.546  38.947 1.00 40.54  ? 91  LYS I N   1 
ATOM   9583  C  CA  . LYS I  1 92  ? 32.748  36.611  37.564 1.00 40.36  ? 91  LYS I CA  1 
ATOM   9584  C  C   . LYS I  1 92  ? 32.726  35.223  36.927 1.00 40.32  ? 91  LYS I C   1 
ATOM   9585  O  O   . LYS I  1 92  ? 32.092  35.042  35.898 1.00 37.90  ? 91  LYS I O   1 
ATOM   9586  C  CB  . LYS I  1 92  ? 33.583  37.590  36.728 1.00 41.48  ? 91  LYS I CB  1 
ATOM   9587  C  CG  . LYS I  1 92  ? 33.330  39.060  37.015 0.60 42.94  ? 91  LYS I CG  1 
ATOM   9588  C  CD  . LYS I  1 92  ? 33.584  40.031  35.834 0.60 40.64  ? 91  LYS I CD  1 
ATOM   9589  C  CE  . LYS I  1 92  ? 32.501  41.082  35.637 0.60 35.89  ? 91  LYS I CE  1 
ATOM   9590  N  NZ  . LYS I  1 92  ? 33.022  42.469  35.642 0.60 35.13  ? 91  LYS I NZ  1 
ATOM   9591  N  N   . ASP I  1 93  ? 33.428  34.256  37.532 1.00 44.83  ? 92  ASP I N   1 
ATOM   9592  C  CA  . ASP I  1 93  ? 33.547  32.910  36.989 1.00 46.87  ? 92  ASP I CA  1 
ATOM   9593  C  C   . ASP I  1 93  ? 32.501  31.984  37.609 1.00 42.69  ? 92  ASP I C   1 
ATOM   9594  O  O   . ASP I  1 93  ? 32.433  30.811  37.269 1.00 41.21  ? 92  ASP I O   1 
ATOM   9595  C  CB  . ASP I  1 93  ? 34.929  32.315  37.253 1.00 52.66  ? 92  ASP I CB  1 
ATOM   9596  C  CG  . ASP I  1 93  ? 36.042  33.063  36.545 1.00 61.29  ? 92  ASP I CG  1 
ATOM   9597  O  OD1 . ASP I  1 93  ? 35.853  33.426  35.360 1.00 63.52  ? 92  ASP I OD1 1 
ATOM   9598  O  OD2 . ASP I  1 93  ? 37.098  33.272  37.184 1.00 68.28  ? 92  ASP I OD2 1 
ATOM   9599  N  N   . GLY I  1 94  ? 31.699  32.510  38.536 1.00 40.56  ? 93  GLY I N   1 
ATOM   9600  C  CA  . GLY I  1 94  ? 30.651  31.722  39.162 1.00 31.22  ? 93  GLY I CA  1 
ATOM   9601  C  C   . GLY I  1 94  ? 31.182  30.886  40.322 1.00 28.22  ? 93  GLY I C   1 
ATOM   9602  O  O   . GLY I  1 94  ? 30.558  29.897  40.695 1.00 27.98  ? 93  GLY I O   1 
ATOM   9603  N  N   . VAL I  1 95  ? 32.329  31.294  40.881 1.00 23.17  ? 94  VAL I N   1 
ATOM   9604  C  CA  . VAL I  1 95  ? 32.905  30.574  42.002 1.00 20.31  ? 94  VAL I CA  1 
ATOM   9605  C  C   . VAL I  1 95  ? 32.819  31.424  43.268 1.00 20.34  ? 94  VAL I C   1 
ATOM   9606  O  O   . VAL I  1 95  ? 33.243  32.574  43.274 1.00 21.57  ? 94  VAL I O   1 
ATOM   9607  C  CB  . VAL I  1 95  ? 34.355  30.151  41.712 1.00 18.62  ? 94  VAL I CB  1 
ATOM   9608  C  CG1 . VAL I  1 95  ? 34.999  29.475  42.914 1.00 17.50  ? 94  VAL I CG1 1 
ATOM   9609  C  CG2 . VAL I  1 95  ? 34.441  29.261  40.492 1.00 18.68  ? 94  VAL I CG2 1 
ATOM   9610  N  N   . ALA I  1 96  ? 32.285  30.839  44.336 1.00 19.79  ? 95  ALA I N   1 
ATOM   9611  C  CA  . ALA I  1 96  ? 32.293  31.499  45.631 1.00 20.27  ? 95  ALA I CA  1 
ATOM   9612  C  C   . ALA I  1 96  ? 33.319  30.835  46.541 1.00 20.40  ? 95  ALA I C   1 
ATOM   9613  O  O   . ALA I  1 96  ? 33.180  29.653  46.849 1.00 20.74  ? 95  ALA I O   1 
ATOM   9614  C  CB  . ALA I  1 96  ? 30.916  31.421  46.244 1.00 19.86  ? 95  ALA I CB  1 
ATOM   9615  N  N   . ASP I  1 97  ? 34.342  31.578  46.955 1.00 23.22  ? 96  ASP I N   1 
ATOM   9616  C  CA  . ASP I  1 97  ? 35.283  31.040  47.931 1.00 29.42  ? 96  ASP I CA  1 
ATOM   9617  C  C   . ASP I  1 97  ? 34.773  31.353  49.328 1.00 28.21  ? 96  ASP I C   1 
ATOM   9618  O  O   . ASP I  1 97  ? 34.992  32.436  49.842 1.00 33.70  ? 96  ASP I O   1 
ATOM   9619  C  CB  . ASP I  1 97  ? 36.737  31.491  47.713 1.00 36.79  ? 96  ASP I CB  1 
ATOM   9620  C  CG  . ASP I  1 97  ? 37.324  30.951  46.422 1.00 46.34  ? 96  ASP I CG  1 
ATOM   9621  O  OD1 . ASP I  1 97  ? 37.223  29.712  46.166 1.00 49.91  ? 96  ASP I OD1 1 
ATOM   9622  O  OD2 . ASP I  1 97  ? 37.854  31.777  45.666 1.00 53.59  ? 96  ASP I OD2 1 
ATOM   9623  N  N   . VAL I  1 98  ? 34.073  30.395  49.913 1.00 24.87  ? 97  VAL I N   1 
ATOM   9624  C  CA  . VAL I  1 98  ? 33.422  30.613  51.195 1.00 23.40  ? 97  VAL I CA  1 
ATOM   9625  C  C   . VAL I  1 98  ? 34.445  30.594  52.323 1.00 23.39  ? 97  VAL I C   1 
ATOM   9626  O  O   . VAL I  1 98  ? 35.291  29.718  52.381 1.00 23.95  ? 97  VAL I O   1 
ATOM   9627  C  CB  . VAL I  1 98  ? 32.319  29.572  51.429 1.00 22.27  ? 97  VAL I CB  1 
ATOM   9628  C  CG1 . VAL I  1 98  ? 31.586  29.877  52.724 1.00 21.48  ? 97  VAL I CG1 1 
ATOM   9629  C  CG2 . VAL I  1 98  ? 31.356  29.501  50.238 1.00 21.43  ? 97  VAL I CG2 1 
ATOM   9630  N  N   . SER I  1 99  ? 34.334  31.553  53.232 1.00 23.39  ? 98  SER I N   1 
ATOM   9631  C  CA  . SER I  1 99  ? 35.105  31.541  54.461 1.00 23.65  ? 98  SER I CA  1 
ATOM   9632  C  C   . SER I  1 99  ? 34.408  32.403  55.504 1.00 23.38  ? 98  SER I C   1 
ATOM   9633  O  O   . SER I  1 99  ? 34.345  33.616  55.361 1.00 25.67  ? 98  SER I O   1 
ATOM   9634  C  CB  . SER I  1 99  ? 36.511  32.009  54.224 1.00 25.78  ? 98  SER I CB  1 
ATOM   9635  O  OG  . SER I  1 99  ? 37.217  32.004  55.452 1.00 26.13  ? 98  SER I OG  1 
ATOM   9636  N  N   . ILE I  1 100 ? 33.843  31.759  56.525 1.00 22.09  ? 99  ILE I N   1 
ATOM   9637  C  CA  . ILE I  1 100 ? 32.960  32.423  57.472 1.00 21.35  ? 99  ILE I CA  1 
ATOM   9638  C  C   . ILE I  1 100 ? 33.315  31.905  58.852 1.00 23.07  ? 99  ILE I C   1 
ATOM   9639  O  O   . ILE I  1 100 ? 33.741  30.766  59.001 1.00 25.65  ? 99  ILE I O   1 
ATOM   9640  C  CB  . ILE I  1 100 ? 31.482  32.134  57.153 1.00 20.29  ? 99  ILE I CB  1 
ATOM   9641  C  CG1 . ILE I  1 100 ? 30.997  32.908  55.931 1.00 19.55  ? 99  ILE I CG1 1 
ATOM   9642  C  CG2 . ILE I  1 100 ? 30.585  32.359  58.370 1.00 19.07  ? 99  ILE I CG2 1 
ATOM   9643  C  CD1 . ILE I  1 100 ? 29.626  32.425  55.454 1.00 20.27  ? 99  ILE I CD1 1 
ATOM   9644  N  N   . GLU I  1 101 ? 33.118  32.752  59.858 1.00 24.32  ? 100 GLU I N   1 
ATOM   9645  C  CA  . GLU I  1 101 ? 33.236  32.279  61.218 1.00 26.00  ? 100 GLU I CA  1 
ATOM   9646  C  C   . GLU I  1 101 ? 31.953  32.654  61.941 1.00 25.81  ? 100 GLU I C   1 
ATOM   9647  O  O   . GLU I  1 101 ? 31.485  33.773  61.820 1.00 26.13  ? 100 GLU I O   1 
ATOM   9648  C  CB  . GLU I  1 101 ? 34.510  32.858  61.819 1.00 28.13  ? 100 GLU I CB  1 
ATOM   9649  C  CG  . GLU I  1 101 ? 34.622  32.652  63.311 1.00 36.34  ? 100 GLU I CG  1 
ATOM   9650  C  CD  . GLU I  1 101 ? 36.033  32.878  63.831 1.00 42.07  ? 100 GLU I CD  1 
ATOM   9651  O  OE1 . GLU I  1 101 ? 36.167  33.496  64.908 1.00 44.06  ? 100 GLU I OE1 1 
ATOM   9652  O  OE2 . GLU I  1 101 ? 36.999  32.448  63.147 1.00 44.07  ? 100 GLU I OE2 1 
ATOM   9653  N  N   . ASP I  1 102 ? 31.358  31.693  62.640 1.00 27.99  ? 101 ASP I N   1 
ATOM   9654  C  CA  . ASP I  1 102 ? 30.086  31.961  63.285 1.00 29.11  ? 101 ASP I CA  1 
ATOM   9655  C  C   . ASP I  1 102 ? 30.112  31.377  64.686 1.00 29.23  ? 101 ASP I C   1 
ATOM   9656  O  O   . ASP I  1 102 ? 30.689  30.312  64.898 1.00 30.61  ? 101 ASP I O   1 
ATOM   9657  C  CB  . ASP I  1 102 ? 28.930  31.382  62.477 1.00 30.96  ? 101 ASP I CB  1 
ATOM   9658  C  CG  . ASP I  1 102 ? 27.592  31.916  62.951 1.00 34.48  ? 101 ASP I CG  1 
ATOM   9659  O  OD1 . ASP I  1 102 ? 27.348  33.119  62.724 1.00 35.21  ? 101 ASP I OD1 1 
ATOM   9660  O  OD2 . ASP I  1 102 ? 26.825  31.135  63.575 1.00 35.81  ? 101 ASP I OD2 1 
ATOM   9661  N  N   . SER I  1 103 ? 29.466  32.067  65.627 1.00 31.93  ? 102 SER I N   1 
ATOM   9662  C  CA  . SER I  1 103 ? 29.485  31.621  67.012 1.00 34.48  ? 102 SER I CA  1 
ATOM   9663  C  C   . SER I  1 103 ? 28.112  31.164  67.485 1.00 33.27  ? 102 SER I C   1 
ATOM   9664  O  O   . SER I  1 103 ? 27.938  30.855  68.660 1.00 33.44  ? 102 SER I O   1 
ATOM   9665  C  CB  . SER I  1 103 ? 30.051  32.676  67.904 1.00 37.75  ? 102 SER I CB  1 
ATOM   9666  O  OG  . SER I  1 103 ? 31.457  32.533  67.950 1.00 44.72  ? 102 SER I OG  1 
ATOM   9667  N  N   . VAL I  1 104 ? 27.149  31.111  66.559 1.00 31.71  ? 103 VAL I N   1 
ATOM   9668  C  CA  . VAL I  1 104 ? 25.789  30.762  66.931 1.00 28.97  ? 103 VAL I CA  1 
ATOM   9669  C  C   . VAL I  1 104 ? 25.535  29.306  66.556 1.00 26.72  ? 103 VAL I C   1 
ATOM   9670  O  O   . VAL I  1 104 ? 24.987  28.557  67.365 1.00 26.03  ? 103 VAL I O   1 
ATOM   9671  C  CB  . VAL I  1 104 ? 24.751  31.724  66.325 1.00 27.34  ? 103 VAL I CB  1 
ATOM   9672  C  CG1 . VAL I  1 104 ? 23.319  31.245  66.544 1.00 26.28  ? 103 VAL I CG1 1 
ATOM   9673  C  CG2 . VAL I  1 104 ? 24.930  33.133  66.858 1.00 26.17  ? 103 VAL I CG2 1 
ATOM   9674  N  N   . ILE I  1 105 ? 25.938  28.918  65.341 1.00 24.19  ? 104 ILE I N   1 
ATOM   9675  C  CA  . ILE I  1 105 ? 25.917  27.508  64.994 1.00 23.74  ? 104 ILE I CA  1 
ATOM   9676  C  C   . ILE I  1 105 ? 26.924  26.786  65.877 1.00 25.52  ? 104 ILE I C   1 
ATOM   9677  O  O   . ILE I  1 105 ? 27.837  27.406  66.411 1.00 27.68  ? 104 ILE I O   1 
ATOM   9678  C  CB  . ILE I  1 105 ? 26.195  27.272  63.499 1.00 21.24  ? 104 ILE I CB  1 
ATOM   9679  C  CG1 . ILE I  1 105 ? 27.601  27.716  63.106 1.00 19.41  ? 104 ILE I CG1 1 
ATOM   9680  C  CG2 . ILE I  1 105 ? 25.128  27.920  62.651 1.00 20.19  ? 104 ILE I CG2 1 
ATOM   9681  C  CD1 . ILE I  1 105 ? 28.030  27.242  61.747 1.00 19.27  ? 104 ILE I CD1 1 
ATOM   9682  N  N   . SER I  1 106 ? 26.733  25.473  66.040 1.00 26.99  ? 105 SER I N   1 
ATOM   9683  C  CA  . SER I  1 106 ? 27.670  24.663  66.799 1.00 26.52  ? 105 SER I CA  1 
ATOM   9684  C  C   . SER I  1 106 ? 27.785  23.274  66.181 1.00 28.29  ? 105 SER I C   1 
ATOM   9685  O  O   . SER I  1 106 ? 26.895  22.843  65.459 1.00 28.27  ? 105 SER I O   1 
ATOM   9686  C  CB  . SER I  1 106 ? 27.258  24.587  68.233 1.00 25.63  ? 105 SER I CB  1 
ATOM   9687  O  OG  . SER I  1 106 ? 28.326  24.074  69.003 1.00 26.89  ? 105 SER I OG  1 
ATOM   9688  N  N   . LEU I  1 107 ? 28.883  22.581  66.487 1.00 29.02  ? 106 LEU I N   1 
ATOM   9689  C  CA  . LEU I  1 107 ? 29.020  21.181  66.117 1.00 29.46  ? 106 LEU I CA  1 
ATOM   9690  C  C   . LEU I  1 107 ? 28.857  20.280  67.345 1.00 34.25  ? 106 LEU I C   1 
ATOM   9691  O  O   . LEU I  1 107 ? 29.159  19.092  67.283 1.00 36.56  ? 106 LEU I O   1 
ATOM   9692  C  CB  . LEU I  1 107 ? 30.364  20.966  65.422 1.00 25.31  ? 106 LEU I CB  1 
ATOM   9693  C  CG  . LEU I  1 107 ? 30.637  21.836  64.205 1.00 23.40  ? 106 LEU I CG  1 
ATOM   9694  C  CD1 . LEU I  1 107 ? 31.922  21.431  63.504 1.00 23.72  ? 106 LEU I CD1 1 
ATOM   9695  C  CD2 . LEU I  1 107 ? 29.508  21.739  63.213 1.00 24.94  ? 106 LEU I CD2 1 
ATOM   9696  N  N   . SER I  1 108 ? 28.378  20.845  68.464 1.00 39.48  ? 107 SER I N   1 
ATOM   9697  C  CA  . SER I  1 108 ? 27.952  20.071  69.621 1.00 42.47  ? 107 SER I CA  1 
ATOM   9698  C  C   . SER I  1 108 ? 26.953  20.881  70.451 1.00 49.51  ? 107 SER I C   1 
ATOM   9699  O  O   . SER I  1 108 ? 26.867  22.096  70.330 1.00 48.59  ? 107 SER I O   1 
ATOM   9700  C  CB  . SER I  1 108 ? 29.128  19.612  70.433 1.00 41.16  ? 107 SER I CB  1 
ATOM   9701  O  OG  . SER I  1 108 ? 29.835  20.723  70.952 1.00 42.47  ? 107 SER I OG  1 
ATOM   9702  N  N   . GLY I  1 109 ? 26.162  20.188  71.279 1.00 59.99  ? 108 GLY I N   1 
ATOM   9703  C  CA  . GLY I  1 109 ? 25.236  20.839  72.194 1.00 67.93  ? 108 GLY I CA  1 
ATOM   9704  C  C   . GLY I  1 109 ? 23.915  21.165  71.510 1.00 81.46  ? 108 GLY I C   1 
ATOM   9705  O  O   . GLY I  1 109 ? 23.574  20.568  70.495 1.00 83.08  ? 108 GLY I O   1 
ATOM   9706  N  N   . ASP I  1 110 ? 23.226  22.188  72.027 1.00 89.43  ? 109 ASP I N   1 
ATOM   9707  C  CA  . ASP I  1 110 ? 21.858  22.485  71.638 1.00 82.71  ? 109 ASP I CA  1 
ATOM   9708  C  C   . ASP I  1 110 ? 21.756  22.940  70.187 1.00 75.18  ? 109 ASP I C   1 
ATOM   9709  O  O   . ASP I  1 110 ? 20.708  22.817  69.579 1.00 62.69  ? 109 ASP I O   1 
ATOM   9710  C  CB  . ASP I  1 110 ? 21.240  23.522  72.579 1.00 90.49  ? 109 ASP I CB  1 
ATOM   9711  C  CG  . ASP I  1 110 ? 21.174  23.039  74.020 1.00 96.26  ? 109 ASP I CG  1 
ATOM   9712  O  OD1 . ASP I  1 110 ? 20.766  21.878  74.243 1.00 97.34  ? 109 ASP I OD1 1 
ATOM   9713  O  OD2 . ASP I  1 110 ? 21.581  23.805  74.899 1.00 96.40  ? 109 ASP I OD2 1 
ATOM   9714  N  N   . HIS I  1 111 ? 22.819  23.505  69.632 1.00 77.93  ? 110 HIS I N   1 
ATOM   9715  C  CA  . HIS I  1 111 ? 22.673  24.092  68.311 1.00 72.84  ? 110 HIS I CA  1 
ATOM   9716  C  C   . HIS I  1 111 ? 23.431  23.264  67.279 1.00 65.33  ? 110 HIS I C   1 
ATOM   9717  O  O   . HIS I  1 111 ? 23.890  23.809  66.287 1.00 67.80  ? 110 HIS I O   1 
ATOM   9718  C  CB  . HIS I  1 111 ? 23.035  25.588  68.336 1.00 79.83  ? 110 HIS I CB  1 
ATOM   9719  C  CG  . HIS I  1 111 ? 22.258  26.396  69.326 1.00 82.80  ? 110 HIS I CG  1 
ATOM   9720  N  ND1 . HIS I  1 111 ? 22.787  27.554  69.888 1.00 74.69  ? 110 HIS I ND1 1 
ATOM   9721  C  CD2 . HIS I  1 111 ? 21.014  26.251  69.848 1.00 85.65  ? 110 HIS I CD2 1 
ATOM   9722  C  CE1 . HIS I  1 111 ? 21.907  28.095  70.709 1.00 74.46  ? 110 HIS I CE1 1 
ATOM   9723  N  NE2 . HIS I  1 111 ? 20.797  27.336  70.679 1.00 82.60  ? 110 HIS I NE2 1 
ATOM   9724  N  N   . CYS I  1 112 ? 23.536  21.951  67.522 1.00 53.05  ? 111 CYS I N   1 
ATOM   9725  C  CA  . CYS I  1 112 ? 24.285  21.084  66.633 1.00 46.64  ? 111 CYS I CA  1 
ATOM   9726  C  C   . CYS I  1 112 ? 23.615  21.092  65.261 1.00 41.47  ? 111 CYS I C   1 
ATOM   9727  O  O   . CYS I  1 112 ? 22.399  20.999  65.166 1.00 39.21  ? 111 CYS I O   1 
ATOM   9728  C  CB  . CYS I  1 112 ? 24.341  19.684  67.223 1.00 53.55  ? 111 CYS I CB  1 
ATOM   9729  S  SG  . CYS I  1 112 ? 25.792  18.704  66.756 1.00 67.75  ? 111 CYS I SG  1 
ATOM   9730  N  N   . ILE I  1 113 ? 24.418  21.308  64.211 1.00 35.76  ? 112 ILE I N   1 
ATOM   9731  C  CA  . ILE I  1 113 ? 23.915  21.386  62.847 1.00 32.30  ? 112 ILE I CA  1 
ATOM   9732  C  C   . ILE I  1 113 ? 24.202  20.076  62.111 1.00 32.23  ? 112 ILE I C   1 
ATOM   9733  O  O   . ILE I  1 113 ? 23.880  19.942  60.927 1.00 31.82  ? 112 ILE I O   1 
ATOM   9734  C  CB  . ILE I  1 113 ? 24.499  22.592  62.078 1.00 29.77  ? 112 ILE I CB  1 
ATOM   9735  C  CG1 . ILE I  1 113 ? 26.027  22.608  62.099 1.00 27.27  ? 112 ILE I CG1 1 
ATOM   9736  C  CG2 . ILE I  1 113 ? 23.924  23.905  62.579 1.00 28.57  ? 112 ILE I CG2 1 
ATOM   9737  C  CD1 . ILE I  1 113 ? 26.645  23.376  60.970 1.00 26.04  ? 112 ILE I CD1 1 
ATOM   9738  N  N   . ILE I  1 114 ? 24.822  19.116  62.813 1.00 29.76  ? 113 ILE I N   1 
ATOM   9739  C  CA  . ILE I  1 114 ? 25.115  17.821  62.222 1.00 28.91  ? 113 ILE I CA  1 
ATOM   9740  C  C   . ILE I  1 114 ? 23.795  17.145  61.879 1.00 29.57  ? 113 ILE I C   1 
ATOM   9741  O  O   . ILE I  1 114 ? 22.859  17.150  62.689 1.00 28.25  ? 113 ILE I O   1 
ATOM   9742  C  CB  . ILE I  1 114 ? 25.958  16.955  63.166 1.00 27.63  ? 113 ILE I CB  1 
ATOM   9743  C  CG1 . ILE I  1 114 ? 27.221  17.707  63.588 1.00 27.59  ? 113 ILE I CG1 1 
ATOM   9744  C  CG2 . ILE I  1 114 ? 26.267  15.615  62.526 1.00 26.60  ? 113 ILE I CG2 1 
ATOM   9745  C  CD1 . ILE I  1 114 ? 28.350  16.842  64.042 1.00 28.66  ? 113 ILE I CD1 1 
ATOM   9746  N  N   . GLY I  1 115 ? 23.741  16.609  60.654 1.00 28.42  ? 114 GLY I N   1 
ATOM   9747  C  CA  . GLY I  1 115 ? 22.583  15.868  60.189 1.00 27.78  ? 114 GLY I CA  1 
ATOM   9748  C  C   . GLY I  1 115 ? 21.455  16.785  59.724 1.00 28.25  ? 114 GLY I C   1 
ATOM   9749  O  O   . GLY I  1 115 ? 20.330  16.325  59.536 1.00 30.63  ? 114 GLY I O   1 
ATOM   9750  N  N   . ARG I  1 116 ? 21.775  18.077  59.541 1.00 26.59  ? 115 ARG I N   1 
ATOM   9751  C  CA  . ARG I  1 116 ? 20.851  19.038  58.953 1.00 23.35  ? 115 ARG I CA  1 
ATOM   9752  C  C   . ARG I  1 116 ? 21.335  19.386  57.547 1.00 23.85  ? 115 ARG I C   1 
ATOM   9753  O  O   . ARG I  1 116 ? 22.251  18.740  57.037 1.00 29.09  ? 115 ARG I O   1 
ATOM   9754  C  CB  . ARG I  1 116 ? 20.652  20.209  59.914 1.00 21.48  ? 115 ARG I CB  1 
ATOM   9755  C  CG  . ARG I  1 116 ? 20.276  19.740  61.311 1.00 21.35  ? 115 ARG I CG  1 
ATOM   9756  C  CD  . ARG I  1 116 ? 19.875  20.851  62.236 1.00 20.95  ? 115 ARG I CD  1 
ATOM   9757  N  NE  . ARG I  1 116 ? 19.491  20.387  63.565 1.00 20.16  ? 115 ARG I NE  1 
ATOM   9758  C  CZ  . ARG I  1 116 ? 18.262  20.012  63.921 1.00 19.21  ? 115 ARG I CZ  1 
ATOM   9759  N  NH1 . ARG I  1 116 ? 17.264  20.042  63.048 1.00 18.35  ? 115 ARG I NH1 1 
ATOM   9760  N  NH2 . ARG I  1 116 ? 18.032  19.626  65.162 1.00 18.85  ? 115 ARG I NH2 1 
ATOM   9761  N  N   . THR I  1 117 ? 20.708  20.372  56.896 1.00 20.86  ? 116 THR I N   1 
ATOM   9762  C  CA  . THR I  1 117 ? 21.068  20.670  55.518 1.00 19.53  ? 116 THR I CA  1 
ATOM   9763  C  C   . THR I  1 117 ? 21.677  22.062  55.390 1.00 20.37  ? 116 THR I C   1 
ATOM   9764  O  O   . THR I  1 117 ? 21.220  23.018  56.005 1.00 20.97  ? 116 THR I O   1 
ATOM   9765  C  CB  . THR I  1 117 ? 19.871  20.526  54.571 1.00 18.30  ? 116 THR I CB  1 
ATOM   9766  O  OG1 . THR I  1 117 ? 19.480  19.157  54.625 1.00 17.25  ? 116 THR I OG1 1 
ATOM   9767  C  CG2 . THR I  1 117 ? 20.203  20.887  53.142 1.00 17.65  ? 116 THR I CG2 1 
ATOM   9768  N  N   . LEU I  1 118 ? 22.710  22.161  54.557 1.00 19.70  ? 117 LEU I N   1 
ATOM   9769  C  CA  . LEU I  1 118 ? 23.225  23.454  54.155 1.00 17.96  ? 117 LEU I CA  1 
ATOM   9770  C  C   . LEU I  1 118 ? 22.691  23.730  52.754 1.00 18.58  ? 117 LEU I C   1 
ATOM   9771  O  O   . LEU I  1 118 ? 22.711  22.845  51.896 1.00 18.71  ? 117 LEU I O   1 
ATOM   9772  C  CB  . LEU I  1 118 ? 24.750  23.374  54.167 1.00 17.58  ? 117 LEU I CB  1 
ATOM   9773  C  CG  . LEU I  1 118 ? 25.475  24.628  53.696 1.00 17.58  ? 117 LEU I CG  1 
ATOM   9774  C  CD1 . LEU I  1 118 ? 25.234  25.766  54.673 1.00 17.29  ? 117 LEU I CD1 1 
ATOM   9775  C  CD2 . LEU I  1 118 ? 26.958  24.360  53.545 1.00 15.94  ? 117 LEU I CD2 1 
ATOM   9776  N  N   . VAL I  1 119 ? 22.187  24.951  52.540 1.00 18.88  ? 118 VAL I N   1 
ATOM   9777  C  CA  . VAL I  1 119 ? 21.592  25.322  51.262 1.00 18.78  ? 118 VAL I CA  1 
ATOM   9778  C  C   . VAL I  1 119 ? 22.216  26.624  50.765 1.00 19.45  ? 118 VAL I C   1 
ATOM   9779  O  O   . VAL I  1 119 ? 22.357  27.593  51.518 1.00 19.11  ? 118 VAL I O   1 
ATOM   9780  C  CB  . VAL I  1 119 ? 20.062  25.492  51.357 1.00 18.43  ? 118 VAL I CB  1 
ATOM   9781  C  CG1 . VAL I  1 119 ? 19.451  25.851  50.009 1.00 18.15  ? 118 VAL I CG1 1 
ATOM   9782  C  CG2 . VAL I  1 119 ? 19.364  24.287  51.951 1.00 18.43  ? 118 VAL I CG2 1 
ATOM   9783  N  N   . VAL I  1 120 ? 22.540  26.643  49.470 1.00 18.49  ? 119 VAL I N   1 
ATOM   9784  C  CA  . VAL I  1 120 ? 22.930  27.877  48.825 1.00 18.53  ? 119 VAL I CA  1 
ATOM   9785  C  C   . VAL I  1 120 ? 21.794  28.286  47.894 1.00 21.53  ? 119 VAL I C   1 
ATOM   9786  O  O   . VAL I  1 120 ? 21.335  27.486  47.070 1.00 22.92  ? 119 VAL I O   1 
ATOM   9787  C  CB  . VAL I  1 120 ? 24.284  27.749  48.106 1.00 17.02  ? 119 VAL I CB  1 
ATOM   9788  C  CG1 . VAL I  1 120 ? 24.289  26.651  47.050 1.00 16.96  ? 119 VAL I CG1 1 
ATOM   9789  C  CG2 . VAL I  1 120 ? 24.741  29.070  47.514 1.00 16.06  ? 119 VAL I CG2 1 
ATOM   9790  N  N   . HIS I  1 121 ? 21.354  29.550  48.043 1.00 23.75  ? 120 HIS I N   1 
ATOM   9791  C  CA  . HIS I  1 121 ? 20.129  30.037  47.426 1.00 23.64  ? 120 HIS I CA  1 
ATOM   9792  C  C   . HIS I  1 121 ? 20.394  30.834  46.148 1.00 24.28  ? 120 HIS I C   1 
ATOM   9793  O  O   . HIS I  1 121 ? 21.529  31.172  45.826 1.00 23.16  ? 120 HIS I O   1 
ATOM   9794  C  CB  . HIS I  1 121 ? 19.355  30.878  48.429 1.00 22.60  ? 120 HIS I CB  1 
ATOM   9795  C  CG  . HIS I  1 121 ? 18.696  30.083  49.497 1.00 21.88  ? 120 HIS I CG  1 
ATOM   9796  N  ND1 . HIS I  1 121 ? 17.395  29.626  49.377 1.00 21.34  ? 120 HIS I ND1 1 
ATOM   9797  C  CD2 . HIS I  1 121 ? 19.140  29.698  50.710 1.00 21.61  ? 120 HIS I CD2 1 
ATOM   9798  C  CE1 . HIS I  1 121 ? 17.059  28.988  50.483 1.00 21.65  ? 120 HIS I CE1 1 
ATOM   9799  N  NE2 . HIS I  1 121 ? 18.112  29.019  51.323 1.00 21.79  ? 120 HIS I NE2 1 
ATOM   9800  N  N   . GLU I  1 122 ? 19.296  31.178  45.466 1.00 24.56  ? 121 GLU I N   1 
ATOM   9801  C  CA  . GLU I  1 122 ? 19.300  31.719  44.119 1.00 24.71  ? 121 GLU I CA  1 
ATOM   9802  C  C   . GLU I  1 122 ? 19.765  33.172  44.105 1.00 26.00  ? 121 GLU I C   1 
ATOM   9803  O  O   . GLU I  1 122 ? 20.531  33.546  43.225 1.00 27.04  ? 121 GLU I O   1 
ATOM   9804  C  CB  . GLU I  1 122 ? 17.892  31.549  43.563 1.00 25.17  ? 121 GLU I CB  1 
ATOM   9805  C  CG  . GLU I  1 122 ? 17.543  32.461  42.416 1.00 26.17  ? 121 GLU I CG  1 
ATOM   9806  C  CD  . GLU I  1 122 ? 16.043  32.504  42.200 1.00 28.54  ? 121 GLU I CD  1 
ATOM   9807  O  OE1 . GLU I  1 122 ? 15.639  32.669  41.034 1.00 30.74  ? 121 GLU I OE1 1 
ATOM   9808  O  OE2 . GLU I  1 122 ? 15.284  32.412  43.198 1.00 27.79  ? 121 GLU I OE2 1 
ATOM   9809  N  N   . LYS I  1 123 ? 19.314  33.966  45.089 1.00 28.00  ? 122 LYS I N   1 
ATOM   9810  C  CA  . LYS I  1 123 ? 19.499  35.410  45.149 1.00 27.75  ? 122 LYS I CA  1 
ATOM   9811  C  C   . LYS I  1 123 ? 20.124  35.813  46.486 1.00 28.70  ? 122 LYS I C   1 
ATOM   9812  O  O   . LYS I  1 123 ? 20.376  34.979  47.348 1.00 31.33  ? 122 LYS I O   1 
ATOM   9813  C  CB  . LYS I  1 123 ? 18.138  36.109  45.088 1.00 29.54  ? 122 LYS I CB  1 
ATOM   9814  C  CG  . LYS I  1 123 ? 17.369  35.951  43.778 1.00 32.67  ? 122 LYS I CG  1 
ATOM   9815  C  CD  . LYS I  1 123 ? 16.032  36.670  43.691 1.00 32.45  ? 122 LYS I CD  1 
ATOM   9816  C  CE  . LYS I  1 123 ? 14.948  36.086  44.575 1.00 33.62  ? 122 LYS I CE  1 
ATOM   9817  N  NZ  . LYS I  1 123 ? 13.674  36.827  44.398 1.00 33.15  ? 122 LYS I NZ  1 
ATOM   9818  N  N   . ALA I  1 124 ? 20.354  37.120  46.657 1.00 26.70  ? 123 ALA I N   1 
ATOM   9819  C  CA  . ALA I  1 124 ? 20.907  37.668  47.884 1.00 23.65  ? 123 ALA I CA  1 
ATOM   9820  C  C   . ALA I  1 124 ? 19.936  37.466  49.037 1.00 23.78  ? 123 ALA I C   1 
ATOM   9821  O  O   . ALA I  1 124 ? 18.727  37.515  48.850 1.00 27.08  ? 123 ALA I O   1 
ATOM   9822  C  CB  . ALA I  1 124 ? 21.192  39.133  47.701 1.00 23.96  ? 123 ALA I CB  1 
ATOM   9823  N  N   . ASP I  1 125 ? 20.484  37.225  50.228 1.00 21.78  ? 124 ASP I N   1 
ATOM   9824  C  CA  . ASP I  1 125 ? 19.724  37.258  51.461 1.00 19.55  ? 124 ASP I CA  1 
ATOM   9825  C  C   . ASP I  1 125 ? 19.665  38.711  51.931 1.00 18.87  ? 124 ASP I C   1 
ATOM   9826  O  O   . ASP I  1 125 ? 20.707  39.323  52.132 1.00 18.89  ? 124 ASP I O   1 
ATOM   9827  C  CB  . ASP I  1 125 ? 20.376  36.315  52.473 1.00 19.28  ? 124 ASP I CB  1 
ATOM   9828  C  CG  . ASP I  1 125 ? 19.784  36.357  53.879 1.00 19.89  ? 124 ASP I CG  1 
ATOM   9829  O  OD1 . ASP I  1 125 ? 18.878  37.180  54.124 1.00 21.26  ? 124 ASP I OD1 1 
ATOM   9830  O  OD2 . ASP I  1 125 ? 20.233  35.563  54.725 1.00 18.06  ? 124 ASP I OD2 1 
ATOM   9831  N  N   . ASP I  1 126 ? 18.448  39.252  52.116 1.00 17.55  ? 125 ASP I N   1 
ATOM   9832  C  CA  . ASP I  1 126 ? 18.296  40.655  52.472 1.00 16.47  ? 125 ASP I CA  1 
ATOM   9833  C  C   . ASP I  1 126 ? 18.476  40.871  53.976 1.00 16.54  ? 125 ASP I C   1 
ATOM   9834  O  O   . ASP I  1 126 ? 18.255  41.981  54.498 1.00 16.67  ? 125 ASP I O   1 
ATOM   9835  C  CB  . ASP I  1 126 ? 17.012  41.265  51.904 1.00 16.12  ? 125 ASP I CB  1 
ATOM   9836  C  CG  . ASP I  1 126 ? 15.705  40.812  52.569 1.00 16.16  ? 125 ASP I CG  1 
ATOM   9837  O  OD1 . ASP I  1 126 ? 15.747  40.354  53.738 1.00 15.32  ? 125 ASP I OD1 1 
ATOM   9838  O  OD2 . ASP I  1 126 ? 14.649  40.935  51.910 1.00 15.88  ? 125 ASP I OD2 1 
ATOM   9839  N  N   . LEU I  1 127 ? 18.889  39.811  54.683 1.00 16.47  ? 126 LEU I N   1 
ATOM   9840  C  CA  . LEU I  1 127 ? 19.245  39.873  56.097 1.00 17.56  ? 126 LEU I CA  1 
ATOM   9841  C  C   . LEU I  1 127 ? 18.058  40.353  56.931 1.00 18.90  ? 126 LEU I C   1 
ATOM   9842  O  O   . LEU I  1 127 ? 18.255  40.845  58.035 1.00 19.69  ? 126 LEU I O   1 
ATOM   9843  C  CB  . LEU I  1 127 ? 20.483  40.753  56.304 1.00 16.71  ? 126 LEU I CB  1 
ATOM   9844  C  CG  . LEU I  1 127 ? 21.664  40.470  55.363 1.00 16.35  ? 126 LEU I CG  1 
ATOM   9845  C  CD1 . LEU I  1 127 ? 22.818  41.424  55.602 1.00 15.22  ? 126 LEU I CD1 1 
ATOM   9846  C  CD2 . LEU I  1 127 ? 22.068  38.981  55.379 1.00 16.64  ? 126 LEU I CD2 1 
ATOM   9847  N  N   . GLY I  1 128 ? 16.837  40.216  56.397 1.00 18.90  ? 127 GLY I N   1 
ATOM   9848  C  CA  . GLY I  1 128 ? 15.612  40.440  57.142 1.00 18.79  ? 127 GLY I CA  1 
ATOM   9849  C  C   . GLY I  1 128 ? 15.161  41.886  57.155 1.00 21.12  ? 127 GLY I C   1 
ATOM   9850  O  O   . GLY I  1 128 ? 14.328  42.267  57.968 1.00 22.80  ? 127 GLY I O   1 
ATOM   9851  N  N   . LYS I  1 129 ? 15.715  42.682  56.229 1.00 22.45  ? 128 LYS I N   1 
ATOM   9852  C  CA  . LYS I  1 129 ? 15.508  44.122  56.228 1.00 21.92  ? 128 LYS I CA  1 
ATOM   9853  C  C   . LYS I  1 129 ? 14.764  44.528  54.959 1.00 22.58  ? 128 LYS I C   1 
ATOM   9854  O  O   . LYS I  1 129 ? 14.961  45.642  54.475 1.00 25.38  ? 128 LYS I O   1 
ATOM   9855  C  CB  . LYS I  1 129 ? 16.855  44.842  56.302 1.00 23.50  ? 128 LYS I CB  1 
ATOM   9856  C  CG  . LYS I  1 129 ? 17.715  44.435  57.468 1.00 23.91  ? 128 LYS I CG  1 
ATOM   9857  C  CD  . LYS I  1 129 ? 19.050  44.984  57.627 1.00 26.93  ? 128 LYS I CD  1 
ATOM   9858  C  CE  . LYS I  1 129 ? 19.585  44.501  58.960 1.00 27.66  ? 128 LYS I CE  1 
ATOM   9859  N  NZ  . LYS I  1 129 ? 18.640  44.661  60.106 1.00 27.95  ? 128 LYS I NZ  1 
ATOM   9860  N  N   . GLY I  1 130 ? 13.930  43.623  54.425 1.00 22.58  ? 129 GLY I N   1 
ATOM   9861  C  CA  . GLY I  1 130 ? 13.268  43.836  53.149 1.00 24.94  ? 129 GLY I CA  1 
ATOM   9862  C  C   . GLY I  1 130 ? 11.843  44.375  53.301 1.00 25.68  ? 129 GLY I C   1 
ATOM   9863  O  O   . GLY I  1 130 ? 11.205  44.723  52.307 1.00 24.92  ? 129 GLY I O   1 
ATOM   9864  N  N   . GLY I  1 131 ? 11.352  44.389  54.546 1.00 27.55  ? 130 GLY I N   1 
ATOM   9865  C  CA  . GLY I  1 131 ? 10.094  45.019  54.905 1.00 29.45  ? 130 GLY I CA  1 
ATOM   9866  C  C   . GLY I  1 131 ? 8.868   44.283  54.376 1.00 29.86  ? 130 GLY I C   1 
ATOM   9867  O  O   . GLY I  1 131 ? 7.808   44.877  54.207 1.00 32.40  ? 130 GLY I O   1 
ATOM   9868  N  N   . ASN I  1 132 ? 9.014   42.985  54.101 1.00 30.67  ? 131 ASN I N   1 
ATOM   9869  C  CA  . ASN I  1 132 ? 7.870   42.143  53.792 1.00 29.62  ? 131 ASN I CA  1 
ATOM   9870  C  C   . ASN I  1 132 ? 7.933   40.897  54.663 1.00 32.15  ? 131 ASN I C   1 
ATOM   9871  O  O   . ASN I  1 132 ? 8.894   40.694  55.401 1.00 31.68  ? 131 ASN I O   1 
ATOM   9872  C  CB  . ASN I  1 132 ? 7.713   41.861  52.295 1.00 27.91  ? 131 ASN I CB  1 
ATOM   9873  C  CG  . ASN I  1 132 ? 8.894   41.174  51.653 1.00 26.95  ? 131 ASN I CG  1 
ATOM   9874  O  OD1 . ASN I  1 132 ? 9.712   40.563  52.329 1.00 25.76  ? 131 ASN I OD1 1 
ATOM   9875  N  ND2 . ASN I  1 132 ? 9.015   41.323  50.337 1.00 28.30  ? 131 ASN I ND2 1 
ATOM   9876  N  N   . GLU I  1 133 ? 6.893   40.069  54.571 1.00 36.75  ? 132 GLU I N   1 
ATOM   9877  C  CA  . GLU I  1 133 ? 6.777   38.948  55.488 1.00 36.83  ? 132 GLU I CA  1 
ATOM   9878  C  C   . GLU I  1 133 ? 7.845   37.923  55.133 1.00 32.86  ? 132 GLU I C   1 
ATOM   9879  O  O   . GLU I  1 133 ? 8.462   37.331  56.023 1.00 31.17  ? 132 GLU I O   1 
ATOM   9880  C  CB  . GLU I  1 133 ? 5.361   38.380  55.481 1.00 44.53  ? 132 GLU I CB  1 
ATOM   9881  C  CG  . GLU I  1 133 ? 5.156   37.440  56.643 1.00 49.85  ? 132 GLU I CG  1 
ATOM   9882  C  CD  . GLU I  1 133 ? 3.921   36.568  56.599 1.00 51.63  ? 132 GLU I CD  1 
ATOM   9883  O  OE1 . GLU I  1 133 ? 2.942   36.907  55.887 1.00 51.88  ? 132 GLU I OE1 1 
ATOM   9884  O  OE2 . GLU I  1 133 ? 3.947   35.555  57.293 1.00 50.81  ? 132 GLU I OE2 1 
ATOM   9885  N  N   . GLU I  1 134 ? 8.075   37.779  53.825 1.00 30.55  ? 133 GLU I N   1 
ATOM   9886  C  CA  . GLU I  1 134 ? 9.075   36.884  53.271 1.00 31.68  ? 133 GLU I CA  1 
ATOM   9887  C  C   . GLU I  1 134 ? 10.453  37.184  53.869 1.00 30.85  ? 133 GLU I C   1 
ATOM   9888  O  O   . GLU I  1 134 ? 11.190  36.266  54.236 1.00 30.31  ? 133 GLU I O   1 
ATOM   9889  C  CB  . GLU I  1 134 ? 9.055   37.017  51.748 1.00 33.78  ? 133 GLU I CB  1 
ATOM   9890  C  CG  . GLU I  1 134 ? 9.652   35.828  51.004 1.00 35.86  ? 133 GLU I CG  1 
ATOM   9891  C  CD  . GLU I  1 134 ? 9.284   34.419  51.473 1.00 38.44  ? 133 GLU I CD  1 
ATOM   9892  O  OE1 . GLU I  1 134 ? 8.128   34.203  51.927 1.00 39.61  ? 133 GLU I OE1 1 
ATOM   9893  O  OE2 . GLU I  1 134 ? 10.161  33.538  51.390 1.00 39.17  ? 133 GLU I OE2 1 
ATOM   9894  N  N   . SER I  1 135 ? 10.780  38.478  53.986 1.00 29.52  ? 134 SER I N   1 
ATOM   9895  C  CA  . SER I  1 135 ? 12.083  38.903  54.464 1.00 27.88  ? 134 SER I CA  1 
ATOM   9896  C  C   . SER I  1 135 ? 12.362  38.304  55.839 1.00 30.16  ? 134 SER I C   1 
ATOM   9897  O  O   . SER I  1 135 ? 13.483  37.886  56.105 1.00 32.86  ? 134 SER I O   1 
ATOM   9898  C  CB  . SER I  1 135 ? 12.207  40.400  54.489 1.00 27.13  ? 134 SER I CB  1 
ATOM   9899  O  OG  . SER I  1 135 ? 13.515  40.805  54.879 1.00 27.21  ? 134 SER I OG  1 
ATOM   9900  N  N   . THR I  1 136 ? 11.351  38.258  56.712 1.00 33.22  ? 135 THR I N   1 
ATOM   9901  C  CA  . THR I  1 136 ? 11.606  37.857  58.083 1.00 34.43  ? 135 THR I CA  1 
ATOM   9902  C  C   . THR I  1 136 ? 11.561  36.342  58.233 1.00 31.59  ? 135 THR I C   1 
ATOM   9903  O  O   . THR I  1 136 ? 11.730  35.841  59.348 1.00 33.19  ? 135 THR I O   1 
ATOM   9904  C  CB  . THR I  1 136 ? 10.634  38.520  59.064 1.00 38.30  ? 135 THR I CB  1 
ATOM   9905  O  OG1 . THR I  1 136 ? 9.339   38.006  58.746 1.00 35.00  ? 135 THR I OG1 1 
ATOM   9906  C  CG2 . THR I  1 136 ? 10.699  40.031  59.023 1.00 39.52  ? 135 THR I CG2 1 
ATOM   9907  N  N   . LYS I  1 137 ? 11.343  35.628  57.114 1.00 28.73  ? 136 LYS I N   1 
ATOM   9908  C  CA  . LYS I  1 137 ? 11.358  34.174  57.115 1.00 25.65  ? 136 LYS I CA  1 
ATOM   9909  C  C   . LYS I  1 137 ? 12.599  33.658  56.390 1.00 23.72  ? 136 LYS I C   1 
ATOM   9910  O  O   . LYS I  1 137 ? 13.351  32.868  56.952 1.00 22.88  ? 136 LYS I O   1 
ATOM   9911  C  CB  . LYS I  1 137 ? 10.086  33.617  56.476 1.00 27.22  ? 136 LYS I CB  1 
ATOM   9912  C  CG  . LYS I  1 137 ? 8.855   33.601  57.379 1.00 31.15  ? 136 LYS I CG  1 
ATOM   9913  C  CD  . LYS I  1 137 ? 7.545   33.349  56.667 1.00 36.39  ? 136 LYS I CD  1 
ATOM   9914  C  CE  . LYS I  1 137 ? 6.499   32.687  57.546 1.00 41.14  ? 136 LYS I CE  1 
ATOM   9915  N  NZ  . LYS I  1 137 ? 5.564   31.846  56.752 1.00 44.67  ? 136 LYS I NZ  1 
ATOM   9916  N  N   . THR I  1 138 ? 12.799  34.109  55.146 1.00 22.83  ? 137 THR I N   1 
ATOM   9917  C  CA  . THR I  1 138 ? 13.787  33.511  54.268 1.00 22.55  ? 137 THR I CA  1 
ATOM   9918  C  C   . THR I  1 138 ? 14.816  34.523  53.763 1.00 22.54  ? 137 THR I C   1 
ATOM   9919  O  O   . THR I  1 138 ? 15.708  34.163  53.007 1.00 22.24  ? 137 THR I O   1 
ATOM   9920  C  CB  . THR I  1 138 ? 13.126  32.868  53.052 1.00 22.18  ? 137 THR I CB  1 
ATOM   9921  O  OG1 . THR I  1 138 ? 12.659  33.899  52.177 1.00 21.76  ? 137 THR I OG1 1 
ATOM   9922  C  CG2 . THR I  1 138 ? 11.988  31.960  53.450 1.00 23.53  ? 137 THR I CG2 1 
ATOM   9923  N  N   . GLY I  1 139 ? 14.653  35.786  54.148 1.00 21.08  ? 138 GLY I N   1 
ATOM   9924  C  CA  . GLY I  1 139 ? 15.481  36.868  53.639 1.00 19.42  ? 138 GLY I CA  1 
ATOM   9925  C  C   . GLY I  1 139 ? 15.345  37.063  52.129 1.00 19.75  ? 138 GLY I C   1 
ATOM   9926  O  O   . GLY I  1 139 ? 16.163  37.761  51.532 1.00 20.11  ? 138 GLY I O   1 
ATOM   9927  N  N   . ASN I  1 140 ? 14.329  36.439  51.507 1.00 19.06  ? 139 ASN I N   1 
ATOM   9928  C  CA  . ASN I  1 140 ? 14.022  36.677  50.105 1.00 20.55  ? 139 ASN I CA  1 
ATOM   9929  C  C   . ASN I  1 140 ? 15.126  36.112  49.220 1.00 19.97  ? 139 ASN I C   1 
ATOM   9930  O  O   . ASN I  1 140 ? 15.331  36.582  48.102 1.00 20.53  ? 139 ASN I O   1 
ATOM   9931  C  CB  . ASN I  1 140 ? 13.800  38.166  49.774 1.00 21.92  ? 139 ASN I CB  1 
ATOM   9932  C  CG  . ASN I  1 140 ? 12.451  38.690  50.209 1.00 24.31  ? 139 ASN I CG  1 
ATOM   9933  O  OD1 . ASN I  1 140 ? 11.421  38.301  49.669 1.00 26.69  ? 139 ASN I OD1 1 
ATOM   9934  N  ND2 . ASN I  1 140 ? 12.432  39.553  51.201 1.00 24.79  ? 139 ASN I ND2 1 
ATOM   9935  N  N   . ALA I  1 141 ? 15.805  35.072  49.716 1.00 20.48  ? 140 ALA I N   1 
ATOM   9936  C  CA  . ALA I  1 141 ? 16.974  34.520  49.051 1.00 20.83  ? 140 ALA I CA  1 
ATOM   9937  C  C   . ALA I  1 141 ? 16.575  33.681  47.841 1.00 21.38  ? 140 ALA I C   1 
ATOM   9938  O  O   . ALA I  1 141 ? 17.430  33.254  47.074 1.00 21.54  ? 140 ALA I O   1 
ATOM   9939  C  CB  . ALA I  1 141 ? 17.783  33.728  50.043 1.00 21.43  ? 140 ALA I CB  1 
ATOM   9940  N  N   . GLY I  1 142 ? 15.274  33.466  47.651 1.00 21.97  ? 141 GLY I N   1 
ATOM   9941  C  CA  . GLY I  1 142 ? 14.800  32.755  46.477 1.00 22.17  ? 141 GLY I CA  1 
ATOM   9942  C  C   . GLY I  1 142 ? 15.019  31.253  46.621 1.00 21.93  ? 141 GLY I C   1 
ATOM   9943  O  O   . GLY I  1 142 ? 15.136  30.745  47.742 1.00 20.42  ? 141 GLY I O   1 
ATOM   9944  N  N   . SER I  1 143 ? 15.110  30.573  45.470 1.00 22.02  ? 142 SER I N   1 
ATOM   9945  C  CA  . SER I  1 143 ? 15.072  29.121  45.420 1.00 22.93  ? 142 SER I CA  1 
ATOM   9946  C  C   . SER I  1 143 ? 16.374  28.520  45.940 1.00 23.64  ? 142 SER I C   1 
ATOM   9947  O  O   . SER I  1 143 ? 17.354  29.236  46.190 1.00 22.67  ? 142 SER I O   1 
ATOM   9948  C  CB  . SER I  1 143 ? 14.760  28.626  44.031 1.00 24.27  ? 142 SER I CB  1 
ATOM   9949  O  OG  . SER I  1 143 ? 15.791  28.985  43.127 1.00 25.00  ? 142 SER I OG  1 
ATOM   9950  N  N   . ARG I  1 144 ? 16.345  27.179  46.088 1.00 22.93  ? 143 ARG I N   1 
ATOM   9951  C  CA  . ARG I  1 144 ? 17.448  26.407  46.644 1.00 21.38  ? 143 ARG I CA  1 
ATOM   9952  C  C   . ARG I  1 144 ? 18.254  25.817  45.491 1.00 20.62  ? 143 ARG I C   1 
ATOM   9953  O  O   . ARG I  1 144 ? 17.781  24.919  44.816 1.00 21.16  ? 143 ARG I O   1 
ATOM   9954  C  CB  . ARG I  1 144 ? 16.868  25.331  47.564 1.00 19.80  ? 143 ARG I CB  1 
ATOM   9955  C  CG  . ARG I  1 144 ? 15.994  25.882  48.674 1.00 19.07  ? 143 ARG I CG  1 
ATOM   9956  C  CD  . ARG I  1 144 ? 15.161  24.864  49.426 1.00 18.43  ? 143 ARG I CD  1 
ATOM   9957  N  NE  . ARG I  1 144 ? 14.330  25.503  50.447 1.00 18.92  ? 143 ARG I NE  1 
ATOM   9958  C  CZ  . ARG I  1 144 ? 13.939  24.947  51.592 1.00 18.84  ? 143 ARG I CZ  1 
ATOM   9959  N  NH1 . ARG I  1 144 ? 14.302  23.716  51.912 1.00 19.57  ? 143 ARG I NH1 1 
ATOM   9960  N  NH2 . ARG I  1 144 ? 13.179  25.624  52.426 1.00 19.05  ? 143 ARG I NH2 1 
ATOM   9961  N  N   . LEU I  1 145 ? 19.451  26.348  45.238 1.00 20.49  ? 144 LEU I N   1 
ATOM   9962  C  CA  . LEU I  1 145 ? 20.181  25.970  44.040 1.00 19.62  ? 144 LEU I CA  1 
ATOM   9963  C  C   . LEU I  1 145 ? 20.869  24.626  44.259 1.00 19.47  ? 144 LEU I C   1 
ATOM   9964  O  O   . LEU I  1 145 ? 20.944  23.801  43.351 1.00 20.11  ? 144 LEU I O   1 
ATOM   9965  C  CB  . LEU I  1 145 ? 21.192  27.069  43.710 1.00 18.85  ? 144 LEU I CB  1 
ATOM   9966  C  CG  . LEU I  1 145 ? 20.598  28.364  43.170 1.00 19.97  ? 144 LEU I CG  1 
ATOM   9967  C  CD1 . LEU I  1 145 ? 21.688  29.345  42.771 1.00 20.67  ? 144 LEU I CD1 1 
ATOM   9968  C  CD2 . LEU I  1 145 ? 19.689  28.102  41.993 1.00 20.36  ? 144 LEU I CD2 1 
ATOM   9969  N  N   . ALA I  1 146 ? 21.384  24.430  45.478 1.00 19.19  ? 145 ALA I N   1 
ATOM   9970  C  CA  . ALA I  1 146 ? 22.077  23.215  45.849 1.00 18.40  ? 145 ALA I CA  1 
ATOM   9971  C  C   . ALA I  1 146 ? 22.079  23.074  47.368 1.00 18.61  ? 145 ALA I C   1 
ATOM   9972  O  O   . ALA I  1 146 ? 22.052  24.061  48.107 1.00 18.40  ? 145 ALA I O   1 
ATOM   9973  C  CB  . ALA I  1 146 ? 23.461  23.234  45.284 1.00 18.04  ? 145 ALA I CB  1 
ATOM   9974  N  N   . CYS I  1 147 ? 22.120  21.819  47.818 1.00 18.79  ? 146 CYS I N   1 
ATOM   9975  C  CA  . CYS I  1 147 ? 22.124  21.540  49.240 1.00 19.62  ? 146 CYS I CA  1 
ATOM   9976  C  C   . CYS I  1 147 ? 22.829  20.207  49.467 1.00 19.10  ? 146 CYS I C   1 
ATOM   9977  O  O   . CYS I  1 147 ? 23.156  19.507  48.515 1.00 18.34  ? 146 CYS I O   1 
ATOM   9978  C  CB  . CYS I  1 147 ? 20.702  21.483  49.775 1.00 20.73  ? 146 CYS I CB  1 
ATOM   9979  S  SG  . CYS I  1 147 ? 19.657  20.252  48.938 1.00 23.00  ? 146 CYS I SG  1 
ATOM   9980  N  N   . GLY I  1 148 ? 23.077  19.910  50.742 1.00 17.77  ? 147 GLY I N   1 
ATOM   9981  C  CA  . GLY I  1 148 ? 23.633  18.648  51.171 1.00 17.31  ? 147 GLY I CA  1 
ATOM   9982  C  C   . GLY I  1 148 ? 23.380  18.429  52.657 1.00 17.94  ? 147 GLY I C   1 
ATOM   9983  O  O   . GLY I  1 148 ? 23.164  19.380  53.414 1.00 17.70  ? 147 GLY I O   1 
ATOM   9984  N  N   . VAL I  1 149 ? 23.413  17.158  53.071 1.00 17.67  ? 148 VAL I N   1 
ATOM   9985  C  CA  . VAL I  1 149 ? 23.328  16.879  54.491 1.00 17.27  ? 148 VAL I CA  1 
ATOM   9986  C  C   . VAL I  1 149 ? 24.705  17.092  55.110 1.00 16.94  ? 148 VAL I C   1 
ATOM   9987  O  O   . VAL I  1 149 ? 25.726  16.778  54.506 1.00 15.92  ? 148 VAL I O   1 
ATOM   9988  C  CB  . VAL I  1 149 ? 22.736  15.486  54.760 1.00 17.23  ? 148 VAL I CB  1 
ATOM   9989  C  CG1 . VAL I  1 149 ? 22.532  15.248  56.247 1.00 17.36  ? 148 VAL I CG1 1 
ATOM   9990  C  CG2 . VAL I  1 149 ? 21.424  15.321  54.014 1.00 17.10  ? 148 VAL I CG2 1 
ATOM   9991  N  N   . ILE I  1 150 ? 24.704  17.668  56.312 1.00 17.59  ? 149 ILE I N   1 
ATOM   9992  C  CA  . ILE I  1 150 ? 25.924  18.022  57.012 1.00 18.56  ? 149 ILE I CA  1 
ATOM   9993  C  C   . ILE I  1 150 ? 26.351  16.799  57.813 1.00 19.41  ? 149 ILE I C   1 
ATOM   9994  O  O   . ILE I  1 150 ? 25.661  16.407  58.757 1.00 20.02  ? 149 ILE I O   1 
ATOM   9995  C  CB  . ILE I  1 150 ? 25.656  19.231  57.929 1.00 18.19  ? 149 ILE I CB  1 
ATOM   9996  C  CG1 . ILE I  1 150 ? 25.287  20.482  57.127 1.00 18.22  ? 149 ILE I CG1 1 
ATOM   9997  C  CG2 . ILE I  1 150 ? 26.822  19.480  58.869 1.00 17.12  ? 149 ILE I CG2 1 
ATOM   9998  C  CD1 . ILE I  1 150 ? 24.651  21.565  57.981 1.00 18.72  ? 149 ILE I CD1 1 
ATOM   9999  N  N   . GLY I  1 151 ? 27.498  16.223  57.439 1.00 20.60  ? 150 GLY I N   1 
ATOM   10000 C  CA  . GLY I  1 151 ? 27.918  14.927  57.950 1.00 22.51  ? 150 GLY I CA  1 
ATOM   10001 C  C   . GLY I  1 151 ? 29.294  14.960  58.611 1.00 23.78  ? 150 GLY I C   1 
ATOM   10002 O  O   . GLY I  1 151 ? 30.068  15.897  58.421 1.00 23.02  ? 150 GLY I O   1 
ATOM   10003 N  N   . ILE I  1 152 ? 29.577  13.918  59.411 1.00 24.76  ? 151 ILE I N   1 
ATOM   10004 C  CA  . ILE I  1 152 ? 30.811  13.820  60.172 1.00 25.29  ? 151 ILE I CA  1 
ATOM   10005 C  C   . ILE I  1 152 ? 31.947  13.464  59.221 1.00 26.07  ? 151 ILE I C   1 
ATOM   10006 O  O   . ILE I  1 152 ? 31.783  12.584  58.383 1.00 25.10  ? 151 ILE I O   1 
ATOM   10007 C  CB  . ILE I  1 152 ? 30.632  12.783  61.289 1.00 24.44  ? 151 ILE I CB  1 
ATOM   10008 C  CG1 . ILE I  1 152 ? 29.635  13.312  62.332 1.00 22.99  ? 151 ILE I CG1 1 
ATOM   10009 C  CG2 . ILE I  1 152 ? 31.970  12.415  61.919 1.00 24.19  ? 151 ILE I CG2 1 
ATOM   10010 C  CD1 . ILE I  1 152 ? 29.032  12.256  63.214 1.00 23.38  ? 151 ILE I CD1 1 
ATOM   10011 N  N   . ALA I  1 153 ? 33.061  14.189  59.350 1.00 28.61  ? 152 ALA I N   1 
ATOM   10012 C  CA  . ALA I  1 153 ? 34.253  13.968  58.501 1.00 33.56  ? 152 ALA I CA  1 
ATOM   10013 C  C   . ALA I  1 153 ? 35.411  13.485  59.378 1.00 38.87  ? 152 ALA I C   1 
ATOM   10014 O  O   . ALA I  1 153 ? 35.289  13.545  60.617 1.00 40.53  ? 152 ALA I O   1 
ATOM   10015 C  CB  . ALA I  1 153 ? 34.606  15.240  57.769 1.00 30.10  ? 152 ALA I CB  1 
ATOM   10016 N  N   . GLN I  1 154 ? 36.489  13.025  58.740 1.00 47.58  ? 153 GLN I N   1 
ATOM   10017 C  CA  . GLN I  1 154 ? 37.693  12.519  59.452 1.00 59.67  ? 153 GLN I CA  1 
ATOM   10018 C  C   . GLN I  1 154 ? 38.395  13.688  60.153 1.00 68.49  ? 153 GLN I C   1 
ATOM   10019 O  O   . GLN I  1 154 ? 38.668  14.694  59.498 1.00 72.78  ? 153 GLN I O   1 
ATOM   10020 C  CB  . GLN I  1 154 ? 38.637  11.819  58.472 1.00 59.72  ? 153 GLN I CB  1 
ATOM   10021 C  CG  . GLN I  1 154 ? 39.850  11.187  59.140 1.00 60.05  ? 153 GLN I CG  1 
ATOM   10022 C  CD  . GLN I  1 154 ? 40.346  9.974   58.392 1.00 62.02  ? 153 GLN I CD  1 
ATOM   10023 O  OE1 . GLN I  1 154 ? 40.784  10.063  57.247 1.00 60.93  ? 153 GLN I OE1 1 
ATOM   10024 N  NE2 . GLN I  1 154 ? 40.280  8.822   59.040 1.00 61.33  ? 153 GLN I NE2 1 
ATOM   10025 O  OXT . GLN I  1 154 ? 38.655  13.559  61.358 1.00 68.60  ? 153 GLN I OXT 1 
ATOM   10026 N  N   . ALA J  1 2   ? 47.407  -50.825 69.159 1.00 49.39  ? 1   ALA J N   1 
ATOM   10027 C  CA  . ALA J  1 2   ? 48.517  -50.537 68.211 1.00 47.49  ? 1   ALA J CA  1 
ATOM   10028 C  C   . ALA J  1 2   ? 48.392  -49.166 67.535 1.00 47.71  ? 1   ALA J C   1 
ATOM   10029 O  O   . ALA J  1 2   ? 47.297  -48.675 67.305 1.00 58.83  ? 1   ALA J O   1 
ATOM   10030 C  CB  . ALA J  1 2   ? 48.670  -51.648 67.212 1.00 42.70  ? 1   ALA J CB  1 
ATOM   10031 N  N   . THR J  1 3   ? 49.534  -48.542 67.239 1.00 38.85  ? 2   THR J N   1 
ATOM   10032 C  CA  . THR J  1 3   ? 49.568  -47.264 66.534 1.00 35.11  ? 2   THR J CA  1 
ATOM   10033 C  C   . THR J  1 3   ? 50.030  -47.490 65.094 1.00 34.82  ? 2   THR J C   1 
ATOM   10034 O  O   . THR J  1 3   ? 51.104  -48.046 64.919 1.00 35.92  ? 2   THR J O   1 
ATOM   10035 C  CB  . THR J  1 3   ? 50.439  -46.268 67.315 1.00 31.73  ? 2   THR J CB  1 
ATOM   10036 O  OG1 . THR J  1 3   ? 50.155  -46.234 68.709 1.00 30.34  ? 2   THR J OG1 1 
ATOM   10037 C  CG2 . THR J  1 3   ? 50.515  -44.870 66.734 1.00 29.55  ? 2   THR J CG2 1 
ATOM   10038 N  N   . LYS J  1 4   ? 49.227  -47.078 64.102 1.00 33.96  ? 3   LYS J N   1 
ATOM   10039 C  CA  . LYS J  1 4   ? 49.615  -47.180 62.698 1.00 33.84  ? 3   LYS J CA  1 
ATOM   10040 C  C   . LYS J  1 4   ? 49.777  -45.792 62.087 1.00 31.21  ? 3   LYS J C   1 
ATOM   10041 O  O   . LYS J  1 4   ? 48.929  -44.915 62.256 1.00 34.09  ? 3   LYS J O   1 
ATOM   10042 C  CB  . LYS J  1 4   ? 48.601  -47.955 61.846 1.00 39.24  ? 3   LYS J CB  1 
ATOM   10043 C  CG  . LYS J  1 4   ? 48.718  -49.474 61.852 1.00 50.76  ? 3   LYS J CG  1 
ATOM   10044 C  CD  . LYS J  1 4   ? 47.623  -50.177 61.070 1.00 62.51  ? 3   LYS J CD  1 
ATOM   10045 C  CE  . LYS J  1 4   ? 47.151  -51.472 61.713 1.00 71.36  ? 3   LYS J CE  1 
ATOM   10046 N  NZ  . LYS J  1 4   ? 45.795  -51.856 61.245 1.00 74.01  ? 3   LYS J NZ  1 
ATOM   10047 N  N   . VAL J  1 5   ? 50.857  -45.628 61.320 1.00 26.32  ? 4   VAL J N   1 
ATOM   10048 C  CA  . VAL J  1 5   ? 51.204  -44.374 60.679 1.00 21.57  ? 4   VAL J CA  1 
ATOM   10049 C  C   . VAL J  1 5   ? 51.590  -44.678 59.236 1.00 19.73  ? 4   VAL J C   1 
ATOM   10050 O  O   . VAL J  1 5   ? 51.973  -45.802 58.907 1.00 20.02  ? 4   VAL J O   1 
ATOM   10051 C  CB  . VAL J  1 5   ? 52.359  -43.731 61.461 1.00 20.89  ? 4   VAL J CB  1 
ATOM   10052 C  CG1 . VAL J  1 5   ? 53.041  -42.608 60.687 1.00 22.83  ? 4   VAL J CG1 1 
ATOM   10053 C  CG2 . VAL J  1 5   ? 51.890  -43.232 62.818 1.00 19.85  ? 4   VAL J CG2 1 
ATOM   10054 N  N   . VAL J  1 6   ? 51.470  -43.689 58.353 1.00 18.73  ? 5   VAL J N   1 
ATOM   10055 C  CA  . VAL J  1 6   ? 51.787  -43.950 56.959 1.00 20.08  ? 5   VAL J CA  1 
ATOM   10056 C  C   . VAL J  1 6   ? 52.461  -42.726 56.338 1.00 20.59  ? 5   VAL J C   1 
ATOM   10057 O  O   . VAL J  1 6   ? 52.370  -41.609 56.853 1.00 20.29  ? 5   VAL J O   1 
ATOM   10058 C  CB  . VAL J  1 6   ? 50.532  -44.379 56.168 1.00 19.18  ? 5   VAL J CB  1 
ATOM   10059 C  CG1 . VAL J  1 6   ? 49.576  -43.210 55.969 1.00 18.81  ? 5   VAL J CG1 1 
ATOM   10060 C  CG2 . VAL J  1 6   ? 50.895  -44.994 54.827 1.00 17.76  ? 5   VAL J CG2 1 
ATOM   10061 N  N   . CYS J  1 7   ? 53.113  -42.951 55.199 1.00 20.34  ? 6   CYS J N   1 
ATOM   10062 C  CA  . CYS J  1 7   ? 53.777  -41.872 54.507 1.00 20.44  ? 6   CYS J CA  1 
ATOM   10063 C  C   . CYS J  1 7   ? 53.804  -42.200 53.021 1.00 20.16  ? 6   CYS J C   1 
ATOM   10064 O  O   . CYS J  1 7   ? 54.206  -43.297 52.635 1.00 21.30  ? 6   CYS J O   1 
ATOM   10065 C  CB  . CYS J  1 7   ? 55.197  -41.781 55.028 1.00 23.09  ? 6   CYS J CB  1 
ATOM   10066 S  SG  . CYS J  1 7   ? 56.126  -40.413 54.289 1.00 27.85  ? 6   CYS J SG  1 
ATOM   10067 N  N   . VAL J  1 8   ? 53.362  -41.249 52.193 1.00 19.68  ? 7   VAL J N   1 
ATOM   10068 C  CA  . VAL J  1 8   ? 53.433  -41.404 50.752 1.00 19.66  ? 7   VAL J CA  1 
ATOM   10069 C  C   . VAL J  1 8   ? 54.615  -40.584 50.248 1.00 21.05  ? 7   VAL J C   1 
ATOM   10070 O  O   . VAL J  1 8   ? 54.653  -39.377 50.464 1.00 23.83  ? 7   VAL J O   1 
ATOM   10071 C  CB  . VAL J  1 8   ? 52.127  -40.949 50.079 1.00 19.05  ? 7   VAL J CB  1 
ATOM   10072 C  CG1 . VAL J  1 8   ? 52.238  -40.944 48.559 1.00 19.23  ? 7   VAL J CG1 1 
ATOM   10073 C  CG2 . VAL J  1 8   ? 50.943  -41.800 50.519 1.00 18.91  ? 7   VAL J CG2 1 
ATOM   10074 N  N   . LEU J  1 9   ? 55.571  -41.236 49.583 1.00 20.92  ? 8   LEU J N   1 
ATOM   10075 C  CA  . LEU J  1 9   ? 56.734  -40.520 49.081 1.00 21.75  ? 8   LEU J CA  1 
ATOM   10076 C  C   . LEU J  1 9   ? 56.485  -40.095 47.640 1.00 23.11  ? 8   LEU J C   1 
ATOM   10077 O  O   . LEU J  1 9   ? 56.182  -40.946 46.818 1.00 22.32  ? 8   LEU J O   1 
ATOM   10078 C  CB  . LEU J  1 9   ? 57.967  -41.426 49.166 1.00 21.55  ? 8   LEU J CB  1 
ATOM   10079 C  CG  . LEU J  1 9   ? 58.298  -41.979 50.549 1.00 21.05  ? 8   LEU J CG  1 
ATOM   10080 C  CD1 . LEU J  1 9   ? 59.324  -43.084 50.432 1.00 21.89  ? 8   LEU J CD1 1 
ATOM   10081 C  CD2 . LEU J  1 9   ? 58.817  -40.898 51.466 1.00 19.81  ? 8   LEU J CD2 1 
ATOM   10082 N  N   . LYS J  1 10  ? 56.635  -38.790 47.363 1.00 26.82  ? 9   LYS J N   1 
ATOM   10083 C  CA  . LYS J  1 10  ? 56.644  -38.238 46.016 1.00 28.32  ? 9   LYS J CA  1 
ATOM   10084 C  C   . LYS J  1 10  ? 57.806  -37.262 45.880 1.00 28.26  ? 9   LYS J C   1 
ATOM   10085 O  O   . LYS J  1 10  ? 58.303  -36.764 46.885 1.00 29.76  ? 9   LYS J O   1 
ATOM   10086 C  CB  . LYS J  1 10  ? 55.314  -37.580 45.632 1.00 32.95  ? 9   LYS J CB  1 
ATOM   10087 C  CG  . LYS J  1 10  ? 54.321  -38.584 45.047 1.00 42.53  ? 9   LYS J CG  1 
ATOM   10088 C  CD  . LYS J  1 10  ? 52.973  -38.122 44.580 1.00 49.12  ? 9   LYS J CD  1 
ATOM   10089 C  CE  . LYS J  1 10  ? 52.066  -39.323 44.703 1.00 49.38  ? 9   LYS J CE  1 
ATOM   10090 N  NZ  . LYS J  1 10  ? 50.851  -38.983 45.476 1.00 51.82  ? 9   LYS J NZ  1 
ATOM   10091 N  N   . GLY J  1 11  ? 58.211  -37.015 44.631 1.00 27.81  ? 10  GLY J N   1 
ATOM   10092 C  CA  . GLY J  1 11  ? 59.237  -36.024 44.350 1.00 27.89  ? 10  GLY J CA  1 
ATOM   10093 C  C   . GLY J  1 11  ? 59.183  -35.564 42.904 1.00 28.11  ? 10  GLY J C   1 
ATOM   10094 O  O   . GLY J  1 11  ? 58.213  -35.829 42.209 1.00 27.37  ? 10  GLY J O   1 
ATOM   10095 N  N   . ASP J  1 12  ? 60.242  -34.887 42.458 1.00 30.01  ? 11  ASP J N   1 
ATOM   10096 C  CA  . ASP J  1 12  ? 60.256  -34.297 41.126 1.00 33.01  ? 11  ASP J CA  1 
ATOM   10097 C  C   . ASP J  1 12  ? 60.464  -35.359 40.056 1.00 32.64  ? 11  ASP J C   1 
ATOM   10098 O  O   . ASP J  1 12  ? 60.049  -35.175 38.921 1.00 32.30  ? 11  ASP J O   1 
ATOM   10099 C  CB  . ASP J  1 12  ? 61.329  -33.219 41.015 1.00 36.52  ? 11  ASP J CB  1 
ATOM   10100 C  CG  . ASP J  1 12  ? 60.990  -32.032 41.892 1.00 37.64  ? 11  ASP J CG  1 
ATOM   10101 O  OD1 . ASP J  1 12  ? 59.792  -31.710 41.970 1.00 36.74  ? 11  ASP J OD1 1 
ATOM   10102 O  OD2 . ASP J  1 12  ? 61.916  -31.472 42.536 1.00 41.89  ? 11  ASP J OD2 1 
ATOM   10103 N  N   . GLY J  1 13  ? 61.139  -36.451 40.420 1.00 34.08  ? 12  GLY J N   1 
ATOM   10104 C  CA  . GLY J  1 13  ? 61.508  -37.483 39.465 1.00 31.62  ? 12  GLY J CA  1 
ATOM   10105 C  C   . GLY J  1 13  ? 60.496  -38.615 39.474 1.00 31.34  ? 12  GLY J C   1 
ATOM   10106 O  O   . GLY J  1 13  ? 59.358  -38.425 39.889 1.00 35.44  ? 12  GLY J O   1 
ATOM   10107 N  N   . PRO J  1 14  ? 60.887  -39.834 39.038 1.00 31.05  ? 13  PRO J N   1 
ATOM   10108 C  CA  . PRO J  1 14  ? 59.964  -40.972 39.012 1.00 28.38  ? 13  PRO J CA  1 
ATOM   10109 C  C   . PRO J  1 14  ? 59.844  -41.732 40.335 1.00 26.23  ? 13  PRO J C   1 
ATOM   10110 O  O   . PRO J  1 14  ? 59.100  -42.705 40.412 1.00 24.56  ? 13  PRO J O   1 
ATOM   10111 C  CB  . PRO J  1 14  ? 60.593  -41.857 37.926 1.00 27.86  ? 13  PRO J CB  1 
ATOM   10112 C  CG  . PRO J  1 14  ? 62.072  -41.609 38.066 1.00 27.32  ? 13  PRO J CG  1 
ATOM   10113 C  CD  . PRO J  1 14  ? 62.229  -40.181 38.542 1.00 29.01  ? 13  PRO J CD  1 
ATOM   10114 N  N   . VAL J  1 15  ? 60.556  -41.292 41.373 1.00 24.88  ? 14  VAL J N   1 
ATOM   10115 C  CA  . VAL J  1 15  ? 60.555  -42.061 42.607 1.00 24.43  ? 14  VAL J CA  1 
ATOM   10116 C  C   . VAL J  1 15  ? 59.251  -41.827 43.362 1.00 25.68  ? 14  VAL J C   1 
ATOM   10117 O  O   . VAL J  1 15  ? 58.861  -40.691 43.596 1.00 27.54  ? 14  VAL J O   1 
ATOM   10118 C  CB  . VAL J  1 15  ? 61.777  -41.755 43.486 1.00 23.33  ? 14  VAL J CB  1 
ATOM   10119 C  CG1 . VAL J  1 15  ? 61.721  -42.522 44.797 1.00 22.23  ? 14  VAL J CG1 1 
ATOM   10120 C  CG2 . VAL J  1 15  ? 63.070  -42.025 42.750 1.00 22.99  ? 14  VAL J CG2 1 
ATOM   10121 N  N   . GLN J  1 16  ? 58.573  -42.920 43.718 1.00 26.52  ? 15  GLN J N   1 
ATOM   10122 C  CA  . GLN J  1 16  ? 57.364  -42.826 44.519 1.00 29.56  ? 15  GLN J CA  1 
ATOM   10123 C  C   . GLN J  1 16  ? 57.136  -44.121 45.289 1.00 29.74  ? 15  GLN J C   1 
ATOM   10124 O  O   . GLN J  1 16  ? 57.598  -45.172 44.860 1.00 32.46  ? 15  GLN J O   1 
ATOM   10125 C  CB  . GLN J  1 16  ? 56.154  -42.423 43.684 1.00 34.86  ? 15  GLN J CB  1 
ATOM   10126 C  CG  . GLN J  1 16  ? 55.805  -43.423 42.603 1.00 42.86  ? 15  GLN J CG  1 
ATOM   10127 C  CD  . GLN J  1 16  ? 54.593  -43.027 41.812 1.00 49.82  ? 15  GLN J CD  1 
ATOM   10128 O  OE1 . GLN J  1 16  ? 54.081  -41.910 41.941 1.00 54.70  ? 15  GLN J OE1 1 
ATOM   10129 N  NE2 . GLN J  1 16  ? 54.130  -43.963 40.998 1.00 47.54  ? 15  GLN J NE2 1 
ATOM   10130 N  N   . GLY J  1 17  ? 56.447  -44.022 46.434 1.00 26.60  ? 16  GLY J N   1 
ATOM   10131 C  CA  . GLY J  1 17  ? 56.230  -45.183 47.272 1.00 24.19  ? 16  GLY J CA  1 
ATOM   10132 C  C   . GLY J  1 17  ? 55.318  -44.911 48.460 1.00 22.52  ? 16  GLY J C   1 
ATOM   10133 O  O   . GLY J  1 17  ? 55.017  -43.768 48.759 1.00 23.52  ? 16  GLY J O   1 
ATOM   10134 N  N   . ILE J  1 18  ? 54.922  -45.989 49.147 1.00 20.12  ? 17  ILE J N   1 
ATOM   10135 C  CA  . ILE J  1 18  ? 54.125  -45.900 50.360 1.00 18.67  ? 17  ILE J CA  1 
ATOM   10136 C  C   . ILE J  1 18  ? 54.886  -46.637 51.451 1.00 18.06  ? 17  ILE J C   1 
ATOM   10137 O  O   . ILE J  1 18  ? 55.327  -47.758 51.227 1.00 19.00  ? 17  ILE J O   1 
ATOM   10138 C  CB  . ILE J  1 18  ? 52.745  -46.546 50.121 1.00 18.14  ? 17  ILE J CB  1 
ATOM   10139 C  CG1 . ILE J  1 18  ? 51.950  -45.780 49.059 1.00 19.00  ? 17  ILE J CG1 1 
ATOM   10140 C  CG2 . ILE J  1 18  ? 51.957  -46.695 51.417 1.00 16.92  ? 17  ILE J CG2 1 
ATOM   10141 C  CD1 . ILE J  1 18  ? 50.619  -46.419 48.711 1.00 18.55  ? 17  ILE J CD1 1 
ATOM   10142 N  N   . ILE J  1 19  ? 55.053  -46.006 52.613 1.00 17.57  ? 18  ILE J N   1 
ATOM   10143 C  CA  . ILE J  1 19  ? 55.748  -46.678 53.701 1.00 17.60  ? 18  ILE J CA  1 
ATOM   10144 C  C   . ILE J  1 19  ? 54.843  -46.655 54.918 1.00 18.22  ? 18  ILE J C   1 
ATOM   10145 O  O   . ILE J  1 19  ? 54.361  -45.587 55.302 1.00 19.88  ? 18  ILE J O   1 
ATOM   10146 C  CB  . ILE J  1 19  ? 57.109  -46.011 54.004 1.00 17.69  ? 18  ILE J CB  1 
ATOM   10147 C  CG1 . ILE J  1 19  ? 58.052  -46.018 52.795 1.00 17.94  ? 18  ILE J CG1 1 
ATOM   10148 C  CG2 . ILE J  1 19  ? 57.745  -46.601 55.258 1.00 16.65  ? 18  ILE J CG2 1 
ATOM   10149 C  CD1 . ILE J  1 19  ? 58.480  -47.414 52.357 1.00 17.65  ? 18  ILE J CD1 1 
ATOM   10150 N  N   . ASN J  1 20  ? 54.661  -47.824 55.535 1.00 18.54  ? 19  ASN J N   1 
ATOM   10151 C  CA  . ASN J  1 20  ? 53.842  -47.940 56.731 1.00 20.06  ? 19  ASN J CA  1 
ATOM   10152 C  C   . ASN J  1 20  ? 54.730  -48.045 57.958 1.00 20.54  ? 19  ASN J C   1 
ATOM   10153 O  O   . ASN J  1 20  ? 55.827  -48.594 57.888 1.00 21.73  ? 19  ASN J O   1 
ATOM   10154 C  CB  . ASN J  1 20  ? 52.958  -49.180 56.678 1.00 20.89  ? 19  ASN J CB  1 
ATOM   10155 C  CG  . ASN J  1 20  ? 52.151  -49.221 55.397 1.00 22.97  ? 19  ASN J CG  1 
ATOM   10156 O  OD1 . ASN J  1 20  ? 52.550  -49.892 54.447 1.00 22.12  ? 19  ASN J OD1 1 
ATOM   10157 N  ND2 . ASN J  1 20  ? 51.067  -48.439 55.332 1.00 25.22  ? 19  ASN J ND2 1 
ATOM   10158 N  N   . PHE J  1 21  ? 54.228  -47.522 59.079 1.00 21.41  ? 20  PHE J N   1 
ATOM   10159 C  CA  . PHE J  1 21  ? 54.904  -47.655 60.361 1.00 22.76  ? 20  PHE J CA  1 
ATOM   10160 C  C   . PHE J  1 21  ? 53.909  -48.216 61.358 1.00 24.74  ? 20  PHE J C   1 
ATOM   10161 O  O   . PHE J  1 21  ? 52.783  -47.737 61.425 1.00 24.75  ? 20  PHE J O   1 
ATOM   10162 C  CB  . PHE J  1 21  ? 55.357  -46.297 60.889 1.00 20.24  ? 20  PHE J CB  1 
ATOM   10163 C  CG  . PHE J  1 21  ? 56.342  -45.551 60.029 1.00 18.73  ? 20  PHE J CG  1 
ATOM   10164 C  CD1 . PHE J  1 21  ? 55.966  -45.020 58.803 1.00 17.50  ? 20  PHE J CD1 1 
ATOM   10165 C  CD2 . PHE J  1 21  ? 57.649  -45.361 60.458 1.00 17.61  ? 20  PHE J CD2 1 
ATOM   10166 C  CE1 . PHE J  1 21  ? 56.874  -44.328 58.020 1.00 17.87  ? 20  PHE J CE1 1 
ATOM   10167 C  CE2 . PHE J  1 21  ? 58.553  -44.657 59.675 1.00 17.45  ? 20  PHE J CE2 1 
ATOM   10168 C  CZ  . PHE J  1 21  ? 58.164  -44.137 58.456 1.00 17.83  ? 20  PHE J CZ  1 
ATOM   10169 N  N   . GLU J  1 22  ? 54.337  -49.217 62.126 1.00 30.22  ? 21  GLU J N   1 
ATOM   10170 C  CA  . GLU J  1 22  ? 53.461  -49.815 63.112 1.00 33.38  ? 21  GLU J CA  1 
ATOM   10171 C  C   . GLU J  1 22  ? 54.248  -50.059 64.391 1.00 30.17  ? 21  GLU J C   1 
ATOM   10172 O  O   . GLU J  1 22  ? 55.396  -50.484 64.335 1.00 29.59  ? 21  GLU J O   1 
ATOM   10173 C  CB  . GLU J  1 22  ? 52.836  -51.088 62.561 1.00 41.08  ? 21  GLU J CB  1 
ATOM   10174 C  CG  . GLU J  1 22  ? 51.647  -51.579 63.355 1.00 54.57  ? 21  GLU J CG  1 
ATOM   10175 C  CD  . GLU J  1 22  ? 50.954  -52.821 62.839 1.00 62.81  ? 21  GLU J CD  1 
ATOM   10176 O  OE1 . GLU J  1 22  ? 50.576  -52.846 61.643 1.00 67.21  ? 21  GLU J OE1 1 
ATOM   10177 O  OE2 . GLU J  1 22  ? 50.836  -53.782 63.643 1.00 72.52  ? 21  GLU J OE2 1 
ATOM   10178 N  N   . GLN J  1 23  ? 53.620  -49.786 65.540 1.00 28.91  ? 22  GLN J N   1 
ATOM   10179 C  CA  . GLN J  1 23  ? 54.271  -49.942 66.831 1.00 29.76  ? 22  GLN J CA  1 
ATOM   10180 C  C   . GLN J  1 23  ? 53.332  -50.642 67.810 1.00 30.22  ? 22  GLN J C   1 
ATOM   10181 O  O   . GLN J  1 23  ? 52.387  -50.032 68.273 1.00 31.09  ? 22  GLN J O   1 
ATOM   10182 C  CB  . GLN J  1 23  ? 54.710  -48.576 67.345 1.00 27.63  ? 22  GLN J CB  1 
ATOM   10183 C  CG  . GLN J  1 23  ? 55.591  -48.648 68.590 1.00 27.22  ? 22  GLN J CG  1 
ATOM   10184 C  CD  . GLN J  1 23  ? 55.966  -47.286 69.122 1.00 30.72  ? 22  GLN J CD  1 
ATOM   10185 O  OE1 . GLN J  1 23  ? 55.221  -46.324 68.998 1.00 32.39  ? 22  GLN J OE1 1 
ATOM   10186 N  NE2 . GLN J  1 23  ? 57.153  -47.175 69.700 1.00 30.34  ? 22  GLN J NE2 1 
ATOM   10187 N  N   . LYS J  1 24  ? 53.593  -51.932 68.075 1.00 30.36  ? 23  LYS J N   1 
ATOM   10188 C  CA  . LYS J  1 24  ? 52.711  -52.752 68.897 1.00 32.88  ? 23  LYS J CA  1 
ATOM   10189 C  C   . LYS J  1 24  ? 52.761  -52.315 70.365 1.00 35.58  ? 23  LYS J C   1 
ATOM   10190 O  O   . LYS J  1 24  ? 51.718  -52.075 70.956 1.00 34.96  ? 23  LYS J O   1 
ATOM   10191 C  CB  . LYS J  1 24  ? 52.921  -54.254 68.649 1.00 32.63  ? 23  LYS J CB  1 
ATOM   10192 C  CG  . LYS J  1 24  ? 52.286  -54.803 67.376 1.00 33.55  ? 23  LYS J CG  1 
ATOM   10193 C  CD  . LYS J  1 24  ? 52.855  -56.163 66.950 0.40 33.22  ? 23  LYS J CD  1 
ATOM   10194 C  CE  . LYS J  1 24  ? 52.463  -56.577 65.546 0.40 32.36  ? 23  LYS J CE  1 
ATOM   10195 N  NZ  . LYS J  1 24  ? 53.563  -57.259 64.812 0.40 30.64  ? 23  LYS J NZ  1 
ATOM   10196 N  N   . GLU J  1 25  ? 53.961  -52.198 70.949 1.00 41.35  ? 24  GLU J N   1 
ATOM   10197 C  CA  . GLU J  1 25  ? 54.099  -51.797 72.340 1.00 47.37  ? 24  GLU J CA  1 
ATOM   10198 C  C   . GLU J  1 25  ? 54.515  -50.329 72.406 1.00 47.20  ? 24  GLU J C   1 
ATOM   10199 O  O   . GLU J  1 25  ? 55.149  -49.844 71.460 1.00 45.77  ? 24  GLU J O   1 
ATOM   10200 C  CB  . GLU J  1 25  ? 55.138  -52.655 73.059 1.00 51.32  ? 24  GLU J CB  1 
ATOM   10201 C  CG  . GLU J  1 25  ? 54.923  -54.153 72.896 1.00 59.25  ? 24  GLU J CG  1 
ATOM   10202 C  CD  . GLU J  1 25  ? 56.165  -55.017 73.067 1.00 62.98  ? 24  GLU J CD  1 
ATOM   10203 O  OE1 . GLU J  1 25  ? 57.274  -54.522 72.765 1.00 62.34  ? 24  GLU J OE1 1 
ATOM   10204 O  OE2 . GLU J  1 25  ? 56.024  -56.185 73.508 1.00 61.65  ? 24  GLU J OE2 1 
ATOM   10205 N  N   . SER J  1 26  ? 54.159  -49.645 73.503 1.00 50.34  ? 25  SER J N   1 
ATOM   10206 C  CA  . SER J  1 26  ? 54.173  -48.185 73.484 1.00 57.20  ? 25  SER J CA  1 
ATOM   10207 C  C   . SER J  1 26  ? 55.580  -47.592 73.390 1.00 53.10  ? 25  SER J C   1 
ATOM   10208 O  O   . SER J  1 26  ? 55.786  -46.547 72.780 1.00 60.51  ? 25  SER J O   1 
ATOM   10209 C  CB  . SER J  1 26  ? 53.363  -47.564 74.604 1.00 56.30  ? 25  SER J CB  1 
ATOM   10210 O  OG  . SER J  1 26  ? 53.502  -48.341 75.783 1.00 48.96  ? 25  SER J OG  1 
ATOM   10211 N  N   . ASN J  1 27  ? 56.552  -48.248 74.024 1.00 43.16  ? 26  ASN J N   1 
ATOM   10212 C  CA  . ASN J  1 27  ? 57.911  -47.749 73.918 1.00 43.58  ? 26  ASN J CA  1 
ATOM   10213 C  C   . ASN J  1 27  ? 58.763  -48.736 73.123 1.00 45.44  ? 26  ASN J C   1 
ATOM   10214 O  O   . ASN J  1 27  ? 59.985  -48.649 73.105 1.00 53.60  ? 26  ASN J O   1 
ATOM   10215 C  CB  . ASN J  1 27  ? 58.475  -47.368 75.290 0.20 40.00  ? 26  ASN J CB  1 
ATOM   10216 C  CG  . ASN J  1 27  ? 59.693  -46.475 75.231 0.20 37.00  ? 26  ASN J CG  1 
ATOM   10217 O  OD1 . ASN J  1 27  ? 59.870  -45.707 74.289 0.20 35.44  ? 26  ASN J OD1 1 
ATOM   10218 N  ND2 . ASN J  1 27  ? 60.552  -46.592 76.226 0.20 35.63  ? 26  ASN J ND2 1 
ATOM   10219 N  N   . GLY J  1 28  ? 58.106  -49.674 72.446 1.00 41.20  ? 27  GLY J N   1 
ATOM   10220 C  CA  . GLY J  1 28  ? 58.756  -50.813 71.827 1.00 33.94  ? 27  GLY J CA  1 
ATOM   10221 C  C   . GLY J  1 28  ? 59.090  -50.524 70.368 1.00 31.27  ? 27  GLY J C   1 
ATOM   10222 O  O   . GLY J  1 28  ? 58.932  -49.403 69.871 1.00 30.97  ? 27  GLY J O   1 
ATOM   10223 N  N   . PRO J  1 29  ? 59.581  -51.548 69.629 1.00 28.82  ? 28  PRO J N   1 
ATOM   10224 C  CA  . PRO J  1 29  ? 60.112  -51.338 68.285 1.00 26.74  ? 28  PRO J CA  1 
ATOM   10225 C  C   . PRO J  1 29  ? 59.025  -50.943 67.294 1.00 25.28  ? 28  PRO J C   1 
ATOM   10226 O  O   . PRO J  1 29  ? 57.864  -51.242 67.510 1.00 28.69  ? 28  PRO J O   1 
ATOM   10227 C  CB  . PRO J  1 29  ? 60.721  -52.700 67.936 1.00 27.64  ? 28  PRO J CB  1 
ATOM   10228 C  CG  . PRO J  1 29  ? 59.935  -53.669 68.755 1.00 28.37  ? 28  PRO J CG  1 
ATOM   10229 C  CD  . PRO J  1 29  ? 59.700  -52.943 70.061 1.00 28.43  ? 28  PRO J CD  1 
ATOM   10230 N  N   . VAL J  1 30  ? 59.438  -50.285 66.206 1.00 23.15  ? 29  VAL J N   1 
ATOM   10231 C  CA  . VAL J  1 30  ? 58.553  -49.836 65.144 1.00 21.52  ? 29  VAL J CA  1 
ATOM   10232 C  C   . VAL J  1 30  ? 58.879  -50.636 63.887 1.00 20.00  ? 29  VAL J C   1 
ATOM   10233 O  O   . VAL J  1 30  ? 60.026  -50.665 63.455 1.00 21.44  ? 29  VAL J O   1 
ATOM   10234 C  CB  . VAL J  1 30  ? 58.720  -48.325 64.879 1.00 21.33  ? 29  VAL J CB  1 
ATOM   10235 C  CG1 . VAL J  1 30  ? 57.795  -47.851 63.775 1.00 20.50  ? 29  VAL J CG1 1 
ATOM   10236 C  CG2 . VAL J  1 30  ? 58.553  -47.478 66.137 1.00 20.76  ? 29  VAL J CG2 1 
ATOM   10237 N  N   . LYS J  1 31  ? 57.872  -51.284 63.301 1.00 18.22  ? 30  LYS J N   1 
ATOM   10238 C  CA  . LYS J  1 31  ? 58.063  -51.961 62.031 1.00 18.74  ? 30  LYS J CA  1 
ATOM   10239 C  C   . LYS J  1 31  ? 57.845  -50.928 60.930 1.00 18.27  ? 30  LYS J C   1 
ATOM   10240 O  O   . LYS J  1 31  ? 56.824  -50.245 60.896 1.00 19.63  ? 30  LYS J O   1 
ATOM   10241 C  CB  . LYS J  1 31  ? 57.116  -53.146 61.849 1.00 19.48  ? 30  LYS J CB  1 
ATOM   10242 C  CG  . LYS J  1 31  ? 57.513  -54.455 62.536 1.00 19.99  ? 30  LYS J CG  1 
ATOM   10243 C  CD  . LYS J  1 31  ? 56.710  -55.679 62.074 0.20 18.84  ? 30  LYS J CD  1 
ATOM   10244 C  CE  . LYS J  1 31  ? 55.619  -56.315 62.953 0.20 18.35  ? 30  LYS J CE  1 
ATOM   10245 N  NZ  . LYS J  1 31  ? 56.076  -57.399 63.859 0.20 18.03  ? 30  LYS J NZ  1 
ATOM   10246 N  N   . VAL J  1 32  ? 58.823  -50.817 60.026 1.00 16.58  ? 31  VAL J N   1 
ATOM   10247 C  CA  . VAL J  1 32  ? 58.697  -49.915 58.896 1.00 16.41  ? 31  VAL J CA  1 
ATOM   10248 C  C   . VAL J  1 32  ? 58.711  -50.752 57.625 1.00 16.06  ? 31  VAL J C   1 
ATOM   10249 O  O   . VAL J  1 32  ? 59.709  -51.400 57.344 1.00 16.13  ? 31  VAL J O   1 
ATOM   10250 C  CB  . VAL J  1 32  ? 59.847  -48.892 58.900 1.00 16.42  ? 31  VAL J CB  1 
ATOM   10251 C  CG1 . VAL J  1 32  ? 59.695  -47.875 57.790 1.00 15.84  ? 31  VAL J CG1 1 
ATOM   10252 C  CG2 . VAL J  1 32  ? 59.985  -48.213 60.262 1.00 16.80  ? 31  VAL J CG2 1 
ATOM   10253 N  N   . TRP J  1 33  ? 57.612  -50.757 56.867 1.00 16.22  ? 32  TRP J N   1 
ATOM   10254 C  CA  . TRP J  1 33  ? 57.610  -51.548 55.651 1.00 16.90  ? 32  TRP J CA  1 
ATOM   10255 C  C   . TRP J  1 33  ? 56.810  -50.870 54.550 1.00 17.42  ? 32  TRP J C   1 
ATOM   10256 O  O   . TRP J  1 33  ? 55.908  -50.074 54.815 1.00 18.97  ? 32  TRP J O   1 
ATOM   10257 C  CB  . TRP J  1 33  ? 57.073  -52.960 55.905 1.00 18.10  ? 32  TRP J CB  1 
ATOM   10258 C  CG  . TRP J  1 33  ? 55.577  -53.035 55.945 1.00 19.95  ? 32  TRP J CG  1 
ATOM   10259 C  CD1 . TRP J  1 33  ? 54.715  -53.406 54.939 1.00 20.70  ? 32  TRP J CD1 1 
ATOM   10260 C  CD2 . TRP J  1 33  ? 54.748  -52.693 57.067 1.00 20.04  ? 32  TRP J CD2 1 
ATOM   10261 N  NE1 . TRP J  1 33  ? 53.413  -53.331 55.357 1.00 20.01  ? 32  TRP J NE1 1 
ATOM   10262 C  CE2 . TRP J  1 33  ? 53.405  -52.896 56.663 1.00 20.83  ? 32  TRP J CE2 1 
ATOM   10263 C  CE3 . TRP J  1 33  ? 55.016  -52.233 58.358 1.00 20.28  ? 32  TRP J CE3 1 
ATOM   10264 C  CZ2 . TRP J  1 33  ? 52.333  -52.664 57.530 1.00 21.82  ? 32  TRP J CZ2 1 
ATOM   10265 C  CZ3 . TRP J  1 33  ? 53.952  -52.013 59.206 1.00 22.45  ? 32  TRP J CZ3 1 
ATOM   10266 C  CH2 . TRP J  1 33  ? 52.628  -52.223 58.798 1.00 21.78  ? 32  TRP J CH2 1 
ATOM   10267 N  N   . GLY J  1 34  ? 57.117  -51.254 53.315 1.00 16.93  ? 33  GLY J N   1 
ATOM   10268 C  CA  . GLY J  1 34  ? 56.359  -50.821 52.160 1.00 18.04  ? 33  GLY J CA  1 
ATOM   10269 C  C   . GLY J  1 34  ? 57.209  -50.965 50.911 1.00 19.28  ? 33  GLY J C   1 
ATOM   10270 O  O   . GLY J  1 34  ? 58.175  -51.727 50.884 1.00 21.39  ? 33  GLY J O   1 
ATOM   10271 N  N   . SER J  1 35  ? 56.867  -50.201 49.883 1.00 20.07  ? 34  SER J N   1 
ATOM   10272 C  CA  . SER J  1 35  ? 57.534  -50.378 48.614 1.00 21.16  ? 34  SER J CA  1 
ATOM   10273 C  C   . SER J  1 35  ? 57.835  -49.008 48.005 1.00 22.61  ? 34  SER J C   1 
ATOM   10274 O  O   . SER J  1 35  ? 57.022  -48.089 48.110 1.00 24.16  ? 34  SER J O   1 
ATOM   10275 C  CB  . SER J  1 35  ? 56.647  -51.225 47.765 1.00 22.00  ? 34  SER J CB  1 
ATOM   10276 O  OG  . SER J  1 35  ? 57.083  -51.219 46.425 1.00 24.66  ? 34  SER J OG  1 
ATOM   10277 N  N   . ILE J  1 36  ? 59.028  -48.850 47.411 1.00 21.88  ? 35  ILE J N   1 
ATOM   10278 C  CA  . ILE J  1 36  ? 59.349  -47.653 46.650 1.00 21.32  ? 35  ILE J CA  1 
ATOM   10279 C  C   . ILE J  1 36  ? 59.761  -48.085 45.249 1.00 22.79  ? 35  ILE J C   1 
ATOM   10280 O  O   . ILE J  1 36  ? 60.504  -49.046 45.093 1.00 22.40  ? 35  ILE J O   1 
ATOM   10281 C  CB  . ILE J  1 36  ? 60.467  -46.862 47.342 1.00 21.09  ? 35  ILE J CB  1 
ATOM   10282 C  CG1 . ILE J  1 36  ? 60.167  -46.643 48.827 1.00 21.71  ? 35  ILE J CG1 1 
ATOM   10283 C  CG2 . ILE J  1 36  ? 60.711  -45.543 46.633 1.00 21.77  ? 35  ILE J CG2 1 
ATOM   10284 C  CD1 . ILE J  1 36  ? 61.328  -46.064 49.612 1.00 21.53  ? 35  ILE J CD1 1 
ATOM   10285 N  N   . LYS J  1 37  ? 59.279  -47.371 44.229 1.00 23.63  ? 36  LYS J N   1 
ATOM   10286 C  CA  . LYS J  1 37  ? 59.631  -47.704 42.857 1.00 24.50  ? 36  LYS J CA  1 
ATOM   10287 C  C   . LYS J  1 37  ? 60.299  -46.507 42.182 1.00 23.46  ? 36  LYS J C   1 
ATOM   10288 O  O   . LYS J  1 37  ? 60.237  -45.400 42.690 1.00 23.09  ? 36  LYS J O   1 
ATOM   10289 C  CB  . LYS J  1 37  ? 58.409  -48.231 42.107 1.00 27.57  ? 36  LYS J CB  1 
ATOM   10290 C  CG  . LYS J  1 37  ? 57.297  -47.217 41.870 1.00 32.91  ? 36  LYS J CG  1 
ATOM   10291 C  CD  . LYS J  1 37  ? 56.079  -47.798 41.194 1.00 39.84  ? 36  LYS J CD  1 
ATOM   10292 C  CE  . LYS J  1 37  ? 54.778  -47.102 41.566 1.00 43.55  ? 36  LYS J CE  1 
ATOM   10293 N  NZ  . LYS J  1 37  ? 53.606  -47.699 40.904 1.00 45.94  ? 36  LYS J NZ  1 
ATOM   10294 N  N   . GLY J  1 38  ? 60.960  -46.762 41.050 1.00 22.86  ? 37  GLY J N   1 
ATOM   10295 C  CA  . GLY J  1 38  ? 61.623  -45.754 40.240 1.00 23.81  ? 37  GLY J CA  1 
ATOM   10296 C  C   . GLY J  1 38  ? 63.027  -45.371 40.731 1.00 26.29  ? 37  GLY J C   1 
ATOM   10297 O  O   . GLY J  1 38  ? 63.578  -44.360 40.299 1.00 28.99  ? 37  GLY J O   1 
ATOM   10298 N  N   . LEU J  1 39  ? 63.612  -46.183 41.621 1.00 25.80  ? 38  LEU J N   1 
ATOM   10299 C  CA  . LEU J  1 39  ? 64.946  -45.932 42.146 1.00 24.77  ? 38  LEU J CA  1 
ATOM   10300 C  C   . LEU J  1 39  ? 65.990  -46.567 41.238 1.00 27.35  ? 38  LEU J C   1 
ATOM   10301 O  O   . LEU J  1 39  ? 65.694  -47.533 40.537 1.00 29.71  ? 38  LEU J O   1 
ATOM   10302 C  CB  . LEU J  1 39  ? 65.049  -46.535 43.545 1.00 23.63  ? 38  LEU J CB  1 
ATOM   10303 C  CG  . LEU J  1 39  ? 64.264  -45.809 44.629 1.00 23.04  ? 38  LEU J CG  1 
ATOM   10304 C  CD1 . LEU J  1 39  ? 64.130  -46.672 45.867 1.00 23.01  ? 38  LEU J CD1 1 
ATOM   10305 C  CD2 . LEU J  1 39  ? 64.924  -44.487 44.982 1.00 22.94  ? 38  LEU J CD2 1 
ATOM   10306 N  N   . THR J  1 40  ? 67.214  -46.021 41.260 1.00 27.94  ? 39  THR J N   1 
ATOM   10307 C  CA  . THR J  1 40  ? 68.335  -46.684 40.608 1.00 27.98  ? 39  THR J CA  1 
ATOM   10308 C  C   . THR J  1 40  ? 68.732  -47.890 41.453 1.00 28.82  ? 39  THR J C   1 
ATOM   10309 O  O   . THR J  1 40  ? 68.568  -47.875 42.673 1.00 29.97  ? 39  THR J O   1 
ATOM   10310 C  CB  . THR J  1 40  ? 69.539  -45.751 40.456 1.00 26.51  ? 39  THR J CB  1 
ATOM   10311 O  OG1 . THR J  1 40  ? 69.741  -45.171 41.740 1.00 27.32  ? 39  THR J OG1 1 
ATOM   10312 C  CG2 . THR J  1 40  ? 69.346  -44.669 39.421 1.00 25.60  ? 39  THR J CG2 1 
ATOM   10313 N  N   . GLU J  1 41  ? 69.234  -48.938 40.794 1.00 29.12  ? 40  GLU J N   1 
ATOM   10314 C  CA  . GLU J  1 41  ? 69.588  -50.161 41.490 1.00 31.17  ? 40  GLU J CA  1 
ATOM   10315 C  C   . GLU J  1 41  ? 70.604  -49.841 42.582 1.00 29.64  ? 40  GLU J C   1 
ATOM   10316 O  O   . GLU J  1 41  ? 71.475  -48.999 42.389 1.00 27.96  ? 40  GLU J O   1 
ATOM   10317 C  CB  . GLU J  1 41  ? 70.149  -51.169 40.497 1.00 36.11  ? 40  GLU J CB  1 
ATOM   10318 C  CG  . GLU J  1 41  ? 70.430  -52.513 41.140 1.00 44.75  ? 40  GLU J CG  1 
ATOM   10319 C  CD  . GLU J  1 41  ? 70.923  -53.601 40.189 1.00 49.69  ? 40  GLU J CD  1 
ATOM   10320 O  OE1 . GLU J  1 41  ? 71.194  -53.302 38.986 1.00 45.59  ? 40  GLU J OE1 1 
ATOM   10321 O  OE2 . GLU J  1 41  ? 71.019  -54.757 40.654 1.00 56.70  ? 40  GLU J OE2 1 
ATOM   10322 N  N   . GLY J  1 42  ? 70.460  -50.485 43.745 1.00 30.91  ? 41  GLY J N   1 
ATOM   10323 C  CA  . GLY J  1 42  ? 71.447  -50.331 44.805 1.00 30.46  ? 41  GLY J CA  1 
ATOM   10324 C  C   . GLY J  1 42  ? 70.885  -49.663 46.062 1.00 30.74  ? 41  GLY J C   1 
ATOM   10325 O  O   . GLY J  1 42  ? 69.666  -49.570 46.243 1.00 33.30  ? 41  GLY J O   1 
ATOM   10326 N  N   . LEU J  1 43  ? 71.804  -49.200 46.925 1.00 26.67  ? 42  LEU J N   1 
ATOM   10327 C  CA  . LEU J  1 43  ? 71.475  -48.665 48.237 1.00 24.79  ? 42  LEU J CA  1 
ATOM   10328 C  C   . LEU J  1 43  ? 71.035  -47.210 48.118 1.00 23.54  ? 42  LEU J C   1 
ATOM   10329 O  O   . LEU J  1 43  ? 71.601  -46.456 47.327 1.00 23.21  ? 42  LEU J O   1 
ATOM   10330 C  CB  . LEU J  1 43  ? 72.707  -48.762 49.136 1.00 24.84  ? 42  LEU J CB  1 
ATOM   10331 C  CG  . LEU J  1 43  ? 73.143  -50.175 49.523 1.00 24.12  ? 42  LEU J CG  1 
ATOM   10332 C  CD1 . LEU J  1 43  ? 74.481  -50.140 50.238 1.00 23.05  ? 42  LEU J CD1 1 
ATOM   10333 C  CD2 . LEU J  1 43  ? 72.111  -50.852 50.407 1.00 23.84  ? 42  LEU J CD2 1 
ATOM   10334 N  N   . HIS J  1 44  ? 70.029  -46.836 48.921 1.00 21.83  ? 43  HIS J N   1 
ATOM   10335 C  CA  . HIS J  1 44  ? 69.558  -45.464 49.037 1.00 19.27  ? 43  HIS J CA  1 
ATOM   10336 C  C   . HIS J  1 44  ? 69.323  -45.122 50.505 1.00 19.24  ? 43  HIS J C   1 
ATOM   10337 O  O   . HIS J  1 44  ? 68.718  -45.897 51.257 1.00 19.37  ? 43  HIS J O   1 
ATOM   10338 C  CB  . HIS J  1 44  ? 68.292  -45.252 48.220 1.00 18.96  ? 43  HIS J CB  1 
ATOM   10339 C  CG  . HIS J  1 44  ? 68.488  -45.396 46.751 1.00 19.91  ? 43  HIS J CG  1 
ATOM   10340 N  ND1 . HIS J  1 44  ? 68.721  -44.300 45.927 1.00 20.15  ? 43  HIS J ND1 1 
ATOM   10341 C  CD2 . HIS J  1 44  ? 68.466  -46.485 45.947 1.00 19.66  ? 43  HIS J CD2 1 
ATOM   10342 C  CE1 . HIS J  1 44  ? 68.825  -44.702 44.679 1.00 19.69  ? 43  HIS J CE1 1 
ATOM   10343 N  NE2 . HIS J  1 44  ? 68.674  -46.042 44.667 1.00 20.08  ? 43  HIS J NE2 1 
ATOM   10344 N  N   . GLY J  1 45  ? 69.840  -43.960 50.904 1.00 19.18  ? 44  GLY J N   1 
ATOM   10345 C  CA  . GLY J  1 45  ? 69.684  -43.465 52.260 1.00 19.14  ? 44  GLY J CA  1 
ATOM   10346 C  C   . GLY J  1 45  ? 68.221  -43.194 52.583 1.00 19.59  ? 44  GLY J C   1 
ATOM   10347 O  O   . GLY J  1 45  ? 67.469  -42.719 51.738 1.00 21.08  ? 44  GLY J O   1 
ATOM   10348 N  N   . PHE J  1 46  ? 67.845  -43.482 53.825 1.00 18.55  ? 45  PHE J N   1 
ATOM   10349 C  CA  . PHE J  1 46  ? 66.453  -43.527 54.220 1.00 18.93  ? 45  PHE J CA  1 
ATOM   10350 C  C   . PHE J  1 46  ? 66.349  -42.922 55.611 1.00 20.23  ? 45  PHE J C   1 
ATOM   10351 O  O   . PHE J  1 46  ? 66.776  -43.550 56.580 1.00 21.97  ? 45  PHE J O   1 
ATOM   10352 C  CB  . PHE J  1 46  ? 66.017  -44.990 54.238 1.00 18.22  ? 45  PHE J CB  1 
ATOM   10353 C  CG  . PHE J  1 46  ? 64.535  -45.255 54.319 1.00 17.31  ? 45  PHE J CG  1 
ATOM   10354 C  CD1 . PHE J  1 46  ? 63.679  -44.884 53.283 1.00 16.71  ? 45  PHE J CD1 1 
ATOM   10355 C  CD2 . PHE J  1 46  ? 64.008  -45.929 55.409 1.00 16.24  ? 45  PHE J CD2 1 
ATOM   10356 C  CE1 . PHE J  1 46  ? 62.327  -45.186 53.339 1.00 16.41  ? 45  PHE J CE1 1 
ATOM   10357 C  CE2 . PHE J  1 46  ? 62.654  -46.222 55.467 1.00 16.37  ? 45  PHE J CE2 1 
ATOM   10358 C  CZ  . PHE J  1 46  ? 61.819  -45.857 54.436 1.00 16.69  ? 45  PHE J CZ  1 
ATOM   10359 N  N   . HIS J  1 47  ? 65.806  -41.697 55.693 1.00 19.77  ? 46  HIS J N   1 
ATOM   10360 C  CA  . HIS J  1 47  ? 65.857  -40.971 56.950 1.00 21.39  ? 46  HIS J CA  1 
ATOM   10361 C  C   . HIS J  1 47  ? 64.544  -40.267 57.248 1.00 21.61  ? 46  HIS J C   1 
ATOM   10362 O  O   . HIS J  1 47  ? 63.802  -39.890 56.339 1.00 21.14  ? 46  HIS J O   1 
ATOM   10363 C  CB  . HIS J  1 47  ? 66.987  -39.940 56.944 1.00 22.32  ? 46  HIS J CB  1 
ATOM   10364 C  CG  . HIS J  1 47  ? 68.248  -40.440 56.336 1.00 23.90  ? 46  HIS J CG  1 
ATOM   10365 N  ND1 . HIS J  1 47  ? 68.700  -40.000 55.107 1.00 24.43  ? 46  HIS J ND1 1 
ATOM   10366 C  CD2 . HIS J  1 47  ? 69.141  -41.354 56.774 1.00 25.15  ? 46  HIS J CD2 1 
ATOM   10367 C  CE1 . HIS J  1 47  ? 69.821  -40.624 54.808 1.00 25.32  ? 46  HIS J CE1 1 
ATOM   10368 N  NE2 . HIS J  1 47  ? 70.110  -41.468 55.815 1.00 24.78  ? 46  HIS J NE2 1 
ATOM   10369 N  N   . VAL J  1 48  ? 64.316  -40.074 58.553 1.00 21.40  ? 47  VAL J N   1 
ATOM   10370 C  CA  . VAL J  1 48  ? 63.310  -39.130 59.000 1.00 21.84  ? 47  VAL J CA  1 
ATOM   10371 C  C   . VAL J  1 48  ? 63.999  -37.789 59.215 1.00 22.78  ? 47  VAL J C   1 
ATOM   10372 O  O   . VAL J  1 48  ? 64.867  -37.671 60.079 1.00 24.49  ? 47  VAL J O   1 
ATOM   10373 C  CB  . VAL J  1 48  ? 62.607  -39.598 60.286 1.00 21.90  ? 47  VAL J CB  1 
ATOM   10374 C  CG1 . VAL J  1 48  ? 61.511  -38.629 60.694 1.00 21.06  ? 47  VAL J CG1 1 
ATOM   10375 C  CG2 . VAL J  1 48  ? 62.074  -41.020 60.172 1.00 22.21  ? 47  VAL J CG2 1 
ATOM   10376 N  N   . HIS J  1 49  ? 63.593  -36.782 58.429 1.00 23.83  ? 48  HIS J N   1 
ATOM   10377 C  CA  . HIS J  1 49  ? 64.042  -35.412 58.625 1.00 23.61  ? 48  HIS J CA  1 
ATOM   10378 C  C   . HIS J  1 49  ? 63.123  -34.686 59.611 1.00 24.99  ? 48  HIS J C   1 
ATOM   10379 O  O   . HIS J  1 49  ? 62.044  -35.184 59.951 1.00 25.26  ? 48  HIS J O   1 
ATOM   10380 C  CB  . HIS J  1 49  ? 64.150  -34.703 57.280 1.00 23.82  ? 48  HIS J CB  1 
ATOM   10381 C  CG  . HIS J  1 49  ? 65.215  -35.265 56.400 1.00 25.54  ? 48  HIS J CG  1 
ATOM   10382 N  ND1 . HIS J  1 49  ? 66.274  -34.505 55.946 1.00 25.27  ? 48  HIS J ND1 1 
ATOM   10383 C  CD2 . HIS J  1 49  ? 65.397  -36.500 55.893 1.00 26.16  ? 48  HIS J CD2 1 
ATOM   10384 C  CE1 . HIS J  1 49  ? 67.057  -35.249 55.194 1.00 26.65  ? 48  HIS J CE1 1 
ATOM   10385 N  NE2 . HIS J  1 49  ? 66.542  -36.469 55.135 1.00 27.32  ? 48  HIS J NE2 1 
ATOM   10386 N  N   . GLU J  1 50  ? 63.545  -33.487 60.035 1.00 25.87  ? 49  GLU J N   1 
ATOM   10387 C  CA  . GLU J  1 50  ? 63.000  -32.809 61.202 1.00 25.54  ? 49  GLU J CA  1 
ATOM   10388 C  C   . GLU J  1 50  ? 61.593  -32.261 60.966 1.00 24.90  ? 49  GLU J C   1 
ATOM   10389 O  O   . GLU J  1 50  ? 60.737  -32.379 61.850 1.00 25.37  ? 49  GLU J O   1 
ATOM   10390 C  CB  . GLU J  1 50  ? 63.903  -31.650 61.616 1.00 26.66  ? 49  GLU J CB  1 
ATOM   10391 C  CG  . GLU J  1 50  ? 63.608  -31.169 63.017 1.00 29.25  ? 49  GLU J CG  1 
ATOM   10392 C  CD  . GLU J  1 50  ? 64.484  -30.022 63.506 1.00 31.91  ? 49  GLU J CD  1 
ATOM   10393 O  OE1 . GLU J  1 50  ? 65.588  -29.789 62.923 1.00 29.36  ? 49  GLU J OE1 1 
ATOM   10394 O  OE2 . GLU J  1 50  ? 64.043  -29.352 64.474 1.00 32.16  ? 49  GLU J OE2 1 
ATOM   10395 N  N   . PHE J  1 51  ? 61.362  -31.658 59.791 1.00 23.72  ? 50  PHE J N   1 
ATOM   10396 C  CA  . PHE J  1 51  ? 60.156  -30.877 59.577 1.00 24.57  ? 50  PHE J CA  1 
ATOM   10397 C  C   . PHE J  1 51  ? 59.231  -31.544 58.571 1.00 23.74  ? 50  PHE J C   1 
ATOM   10398 O  O   . PHE J  1 51  ? 59.673  -31.933 57.488 1.00 24.93  ? 50  PHE J O   1 
ATOM   10399 C  CB  . PHE J  1 51  ? 60.509  -29.480 59.054 1.00 25.89  ? 50  PHE J CB  1 
ATOM   10400 C  CG  . PHE J  1 51  ? 61.461  -28.747 59.961 1.00 26.76  ? 50  PHE J CG  1 
ATOM   10401 C  CD1 . PHE J  1 51  ? 61.150  -28.546 61.305 1.00 25.57  ? 50  PHE J CD1 1 
ATOM   10402 C  CD2 . PHE J  1 51  ? 62.680  -28.282 59.470 1.00 27.48  ? 50  PHE J CD2 1 
ATOM   10403 C  CE1 . PHE J  1 51  ? 62.041  -27.895 62.147 1.00 24.90  ? 50  PHE J CE1 1 
ATOM   10404 C  CE2 . PHE J  1 51  ? 63.568  -27.636 60.325 1.00 27.77  ? 50  PHE J CE2 1 
ATOM   10405 C  CZ  . PHE J  1 51  ? 63.245  -27.438 61.657 1.00 25.85  ? 50  PHE J CZ  1 
ATOM   10406 N  N   . GLY J  1 52  ? 57.944  -31.612 58.942 1.00 22.11  ? 51  GLY J N   1 
ATOM   10407 C  CA  . GLY J  1 52  ? 56.866  -31.948 58.030 1.00 20.72  ? 51  GLY J CA  1 
ATOM   10408 C  C   . GLY J  1 52  ? 56.521  -30.756 57.136 1.00 20.40  ? 51  GLY J C   1 
ATOM   10409 O  O   . GLY J  1 52  ? 55.379  -30.306 57.103 1.00 20.39  ? 51  GLY J O   1 
ATOM   10410 N  N   . ASP J  1 53  ? 57.528  -30.247 56.430 1.00 20.02  ? 52  ASP J N   1 
ATOM   10411 C  CA  . ASP J  1 53  ? 57.360  -29.034 55.662 1.00 21.10  ? 52  ASP J CA  1 
ATOM   10412 C  C   . ASP J  1 53  ? 57.792  -29.304 54.230 1.00 21.82  ? 52  ASP J C   1 
ATOM   10413 O  O   . ASP J  1 53  ? 58.959  -29.569 53.976 1.00 25.58  ? 52  ASP J O   1 
ATOM   10414 C  CB  . ASP J  1 53  ? 58.155  -27.900 56.310 1.00 21.49  ? 52  ASP J CB  1 
ATOM   10415 C  CG  . ASP J  1 53  ? 58.020  -26.560 55.601 1.00 22.79  ? 52  ASP J CG  1 
ATOM   10416 O  OD1 . ASP J  1 53  ? 57.711  -26.553 54.381 1.00 23.63  ? 52  ASP J OD1 1 
ATOM   10417 O  OD2 . ASP J  1 53  ? 58.272  -25.541 56.272 1.00 22.57  ? 52  ASP J OD2 1 
ATOM   10418 N  N   A ASN J  1 54  ? 56.843  -29.238 53.300 0.50 21.53  ? 53  ASN J N   1 
ATOM   10419 N  N   B ASN J  1 54  ? 56.844  -29.249 53.295 0.50 20.78  ? 53  ASN J N   1 
ATOM   10420 C  CA  A ASN J  1 54  ? 57.123  -29.563 51.913 0.50 21.14  ? 53  ASN J CA  1 
ATOM   10421 C  CA  B ASN J  1 54  ? 57.158  -29.565 51.908 0.50 19.97  ? 53  ASN J CA  1 
ATOM   10422 C  C   A ASN J  1 54  ? 56.950  -28.307 51.058 0.50 21.41  ? 53  ASN J C   1 
ATOM   10423 C  C   B ASN J  1 54  ? 56.957  -28.312 51.052 0.50 20.67  ? 53  ASN J C   1 
ATOM   10424 O  O   A ASN J  1 54  ? 56.827  -28.384 49.838 0.50 20.71  ? 53  ASN J O   1 
ATOM   10425 O  O   B ASN J  1 54  ? 56.832  -28.396 49.832 0.50 20.07  ? 53  ASN J O   1 
ATOM   10426 C  CB  A ASN J  1 54  ? 56.293  -30.773 51.471 0.50 21.43  ? 53  ASN J CB  1 
ATOM   10427 C  CB  B ASN J  1 54  ? 56.554  -30.898 51.433 0.50 19.13  ? 53  ASN J CB  1 
ATOM   10428 C  CG  A ASN J  1 54  ? 56.504  -31.200 50.032 0.50 21.56  ? 53  ASN J CG  1 
ATOM   10429 C  CG  B ASN J  1 54  ? 57.168  -32.114 52.125 0.50 18.45  ? 53  ASN J CG  1 
ATOM   10430 O  OD1 A ASN J  1 54  ? 57.629  -31.451 49.615 0.50 22.13  ? 53  ASN J OD1 1 
ATOM   10431 O  OD1 B ASN J  1 54  ? 58.253  -32.028 52.698 0.50 18.15  ? 53  ASN J OD1 1 
ATOM   10432 N  ND2 A ASN J  1 54  ? 55.430  -31.306 49.263 0.50 21.31  ? 53  ASN J ND2 1 
ATOM   10433 N  ND2 B ASN J  1 54  ? 56.492  -33.255 52.104 0.50 17.17  ? 53  ASN J ND2 1 
ATOM   10434 N  N   . THR J  1 55  ? 56.978  -27.137 51.700 1.00 21.73  ? 54  THR J N   1 
ATOM   10435 C  CA  . THR J  1 55  ? 56.650  -25.885 51.024 1.00 22.62  ? 54  THR J CA  1 
ATOM   10436 C  C   . THR J  1 55  ? 57.604  -25.623 49.861 1.00 24.73  ? 54  THR J C   1 
ATOM   10437 O  O   . THR J  1 55  ? 57.205  -25.026 48.868 1.00 26.72  ? 54  THR J O   1 
ATOM   10438 C  CB  . THR J  1 55  ? 56.645  -24.683 51.971 1.00 20.78  ? 54  THR J CB  1 
ATOM   10439 O  OG1 . THR J  1 55  ? 57.941  -24.609 52.562 1.00 19.47  ? 54  THR J OG1 1 
ATOM   10440 C  CG2 . THR J  1 55  ? 55.591  -24.793 53.052 1.00 21.38  ? 54  THR J CG2 1 
ATOM   10441 N  N   . ALA J  1 56  ? 58.858  -26.061 50.000 1.00 25.41  ? 55  ALA J N   1 
ATOM   10442 C  CA  . ALA J  1 56  ? 59.861  -25.839 48.976 1.00 27.51  ? 55  ALA J CA  1 
ATOM   10443 C  C   . ALA J  1 56  ? 60.413  -27.184 48.523 1.00 30.57  ? 55  ALA J C   1 
ATOM   10444 O  O   . ALA J  1 56  ? 61.620  -27.348 48.384 1.00 36.52  ? 55  ALA J O   1 
ATOM   10445 C  CB  . ALA J  1 56  ? 60.949  -24.954 49.536 1.00 26.95  ? 55  ALA J CB  1 
ATOM   10446 N  N   . GLY J  1 57  ? 59.522  -28.157 48.324 1.00 31.21  ? 56  GLY J N   1 
ATOM   10447 C  CA  . GLY J  1 57  ? 59.929  -29.516 47.998 1.00 30.03  ? 56  GLY J CA  1 
ATOM   10448 C  C   . GLY J  1 57  ? 60.540  -30.210 49.215 1.00 31.22  ? 56  GLY J C   1 
ATOM   10449 O  O   . GLY J  1 57  ? 60.301  -29.819 50.360 1.00 34.25  ? 56  GLY J O   1 
ATOM   10450 N  N   . CYS J  1 58  ? 61.363  -31.232 48.953 1.00 28.23  ? 57  CYS J N   1 
ATOM   10451 C  CA  . CYS J  1 58  ? 61.915  -32.022 50.038 1.00 25.83  ? 57  CYS J CA  1 
ATOM   10452 C  C   . CYS J  1 58  ? 62.932  -31.223 50.847 1.00 25.41  ? 57  CYS J C   1 
ATOM   10453 O  O   . CYS J  1 58  ? 63.166  -31.542 52.008 1.00 23.37  ? 57  CYS J O   1 
ATOM   10454 C  CB  . CYS J  1 58  ? 62.533  -33.296 49.500 1.00 26.45  ? 57  CYS J CB  1 
ATOM   10455 S  SG  . CYS J  1 58  ? 61.325  -34.450 48.795 1.00 27.51  ? 57  CYS J SG  1 
ATOM   10456 N  N   . THR J  1 59  ? 63.502  -30.169 50.240 1.00 26.70  ? 58  THR J N   1 
ATOM   10457 C  CA  . THR J  1 59  ? 64.529  -29.356 50.877 1.00 27.21  ? 58  THR J CA  1 
ATOM   10458 C  C   . THR J  1 59  ? 64.035  -28.806 52.211 1.00 27.88  ? 58  THR J C   1 
ATOM   10459 O  O   . THR J  1 59  ? 64.801  -28.723 53.176 1.00 28.27  ? 58  THR J O   1 
ATOM   10460 C  CB  . THR J  1 59  ? 64.873  -28.111 50.057 1.00 27.16  ? 58  THR J CB  1 
ATOM   10461 O  OG1 . THR J  1 59  ? 65.106  -28.545 48.717 1.00 29.26  ? 58  THR J OG1 1 
ATOM   10462 C  CG2 . THR J  1 59  ? 66.076  -27.367 50.596 1.00 25.91  ? 58  THR J CG2 1 
ATOM   10463 N  N   . SER J  1 60  ? 62.754  -28.407 52.245 1.00 27.20  ? 59  SER J N   1 
ATOM   10464 C  CA  . SER J  1 60  ? 62.284  -27.646 53.387 1.00 27.14  ? 59  SER J CA  1 
ATOM   10465 C  C   . SER J  1 60  ? 62.026  -28.558 54.589 1.00 26.23  ? 59  SER J C   1 
ATOM   10466 O  O   . SER J  1 60  ? 61.635  -28.093 55.658 1.00 28.49  ? 59  SER J O   1 
ATOM   10467 C  CB  . SER J  1 60  ? 61.123  -26.749 53.012 1.00 28.91  ? 59  SER J CB  1 
ATOM   10468 O  OG  . SER J  1 60  ? 60.087  -27.485 52.394 1.00 32.19  ? 59  SER J OG  1 
ATOM   10469 N  N   . ALA J  1 61  ? 62.327  -29.854 54.418 1.00 25.03  ? 60  ALA J N   1 
ATOM   10470 C  CA  . ALA J  1 61  ? 62.169  -30.851 55.467 1.00 23.73  ? 60  ALA J CA  1 
ATOM   10471 C  C   . ALA J  1 61  ? 63.250  -30.681 56.526 1.00 24.71  ? 60  ALA J C   1 
ATOM   10472 O  O   . ALA J  1 61  ? 63.119  -31.197 57.641 1.00 25.02  ? 60  ALA J O   1 
ATOM   10473 C  CB  . ALA J  1 61  ? 62.206  -32.229 54.866 1.00 22.69  ? 60  ALA J CB  1 
ATOM   10474 N  N   . GLY J  1 62  ? 64.324  -29.961 56.155 1.00 25.73  ? 61  GLY J N   1 
ATOM   10475 C  CA  . GLY J  1 62  ? 65.433  -29.705 57.058 1.00 23.51  ? 61  GLY J CA  1 
ATOM   10476 C  C   . GLY J  1 62  ? 66.354  -30.920 57.213 1.00 22.35  ? 61  GLY J C   1 
ATOM   10477 O  O   . GLY J  1 62  ? 66.360  -31.812 56.362 1.00 20.35  ? 61  GLY J O   1 
ATOM   10478 N  N   . PRO J  1 63  ? 67.156  -30.983 58.304 1.00 22.07  ? 62  PRO J N   1 
ATOM   10479 C  CA  . PRO J  1 63  ? 68.168  -32.033 58.477 1.00 22.81  ? 62  PRO J CA  1 
ATOM   10480 C  C   . PRO J  1 63  ? 67.552  -33.327 59.020 1.00 24.25  ? 62  PRO J C   1 
ATOM   10481 O  O   . PRO J  1 63  ? 66.350  -33.377 59.285 1.00 26.97  ? 62  PRO J O   1 
ATOM   10482 C  CB  . PRO J  1 63  ? 69.076  -31.411 59.551 1.00 20.97  ? 62  PRO J CB  1 
ATOM   10483 C  CG  . PRO J  1 63  ? 68.122  -30.631 60.423 1.00 20.49  ? 62  PRO J CG  1 
ATOM   10484 C  CD  . PRO J  1 63  ? 67.107  -30.058 59.452 1.00 21.86  ? 62  PRO J CD  1 
ATOM   10485 N  N   . HIS J  1 64  ? 68.375  -34.366 59.197 1.00 21.94  ? 63  HIS J N   1 
ATOM   10486 C  CA  . HIS J  1 64  ? 67.903  -35.583 59.835 1.00 20.66  ? 63  HIS J CA  1 
ATOM   10487 C  C   . HIS J  1 64  ? 67.340  -35.214 61.205 1.00 20.45  ? 63  HIS J C   1 
ATOM   10488 O  O   . HIS J  1 64  ? 67.953  -34.426 61.922 1.00 21.80  ? 63  HIS J O   1 
ATOM   10489 C  CB  . HIS J  1 64  ? 69.048  -36.603 59.984 1.00 20.12  ? 63  HIS J CB  1 
ATOM   10490 C  CG  . HIS J  1 64  ? 69.620  -37.094 58.695 1.00 20.04  ? 63  HIS J CG  1 
ATOM   10491 N  ND1 . HIS J  1 64  ? 70.756  -37.887 58.659 1.00 19.74  ? 63  HIS J ND1 1 
ATOM   10492 C  CD2 . HIS J  1 64  ? 69.239  -36.906 57.409 1.00 19.79  ? 63  HIS J CD2 1 
ATOM   10493 C  CE1 . HIS J  1 64  ? 71.037  -38.192 57.403 1.00 19.62  ? 63  HIS J CE1 1 
ATOM   10494 N  NE2 . HIS J  1 64  ? 70.128  -37.588 56.616 1.00 19.65  ? 63  HIS J NE2 1 
ATOM   10495 N  N   . PHE J  1 65  ? 66.188  -35.795 61.564 1.00 19.90  ? 64  PHE J N   1 
ATOM   10496 C  CA  . PHE J  1 65  ? 65.584  -35.579 62.871 1.00 19.65  ? 64  PHE J CA  1 
ATOM   10497 C  C   . PHE J  1 65  ? 66.576  -35.943 63.981 1.00 19.53  ? 64  PHE J C   1 
ATOM   10498 O  O   . PHE J  1 65  ? 66.972  -37.099 64.112 1.00 20.14  ? 64  PHE J O   1 
ATOM   10499 C  CB  . PHE J  1 65  ? 64.270  -36.355 62.980 1.00 19.18  ? 64  PHE J CB  1 
ATOM   10500 C  CG  . PHE J  1 65  ? 63.554  -36.219 64.300 1.00 20.10  ? 64  PHE J CG  1 
ATOM   10501 C  CD1 . PHE J  1 65  ? 63.444  -34.984 64.919 1.00 20.49  ? 64  PHE J CD1 1 
ATOM   10502 C  CD2 . PHE J  1 65  ? 62.971  -37.321 64.919 1.00 20.14  ? 64  PHE J CD2 1 
ATOM   10503 C  CE1 . PHE J  1 65  ? 62.781  -34.847 66.133 1.00 20.17  ? 64  PHE J CE1 1 
ATOM   10504 C  CE2 . PHE J  1 65  ? 62.296  -37.187 66.129 1.00 19.96  ? 64  PHE J CE2 1 
ATOM   10505 C  CZ  . PHE J  1 65  ? 62.205  -35.945 66.734 1.00 19.90  ? 64  PHE J CZ  1 
ATOM   10506 N  N   . ASN J  1 66  ? 66.967  -34.959 64.793 1.00 20.24  ? 65  ASN J N   1 
ATOM   10507 C  CA  . ASN J  1 66  ? 68.108  -35.150 65.674 1.00 21.83  ? 65  ASN J CA  1 
ATOM   10508 C  C   . ASN J  1 66  ? 67.843  -34.583 67.075 1.00 23.61  ? 65  ASN J C   1 
ATOM   10509 O  O   . ASN J  1 66  ? 68.623  -33.783 67.580 1.00 22.55  ? 65  ASN J O   1 
ATOM   10510 C  CB  . ASN J  1 66  ? 69.388  -34.608 65.032 1.00 22.53  ? 65  ASN J CB  1 
ATOM   10511 C  CG  . ASN J  1 66  ? 70.632  -34.894 65.864 1.00 23.93  ? 65  ASN J CG  1 
ATOM   10512 O  OD1 . ASN J  1 66  ? 70.648  -35.792 66.699 1.00 23.56  ? 65  ASN J OD1 1 
ATOM   10513 N  ND2 . ASN J  1 66  ? 71.684  -34.129 65.646 1.00 23.63  ? 65  ASN J ND2 1 
ATOM   10514 N  N   . PRO J  1 67  ? 66.781  -35.005 67.796 1.00 25.47  ? 66  PRO J N   1 
ATOM   10515 C  CA  . PRO J  1 67  ? 66.443  -34.387 69.078 1.00 25.56  ? 66  PRO J CA  1 
ATOM   10516 C  C   . PRO J  1 67  ? 67.498  -34.545 70.177 1.00 26.44  ? 66  PRO J C   1 
ATOM   10517 O  O   . PRO J  1 67  ? 67.479  -33.788 71.142 1.00 26.11  ? 66  PRO J O   1 
ATOM   10518 C  CB  . PRO J  1 67  ? 65.153  -35.091 69.517 1.00 26.35  ? 66  PRO J CB  1 
ATOM   10519 C  CG  . PRO J  1 67  ? 65.165  -36.392 68.775 1.00 27.05  ? 66  PRO J CG  1 
ATOM   10520 C  CD  . PRO J  1 67  ? 65.894  -36.129 67.470 1.00 25.64  ? 66  PRO J CD  1 
ATOM   10521 N  N   . LEU J  1 68  ? 68.414  -35.510 70.022 1.00 27.24  ? 67  LEU J N   1 
ATOM   10522 C  CA  . LEU J  1 68  ? 69.394  -35.769 71.066 1.00 25.26  ? 67  LEU J CA  1 
ATOM   10523 C  C   . LEU J  1 68  ? 70.759  -35.156 70.745 1.00 24.72  ? 67  LEU J C   1 
ATOM   10524 O  O   . LEU J  1 68  ? 71.710  -35.384 71.481 1.00 24.02  ? 67  LEU J O   1 
ATOM   10525 C  CB  . LEU J  1 68  ? 69.507  -37.274 71.307 1.00 24.41  ? 67  LEU J CB  1 
ATOM   10526 C  CG  . LEU J  1 68  ? 68.320  -37.938 71.987 1.00 24.89  ? 67  LEU J CG  1 
ATOM   10527 C  CD1 . LEU J  1 68  ? 68.639  -39.395 72.356 1.00 24.68  ? 67  LEU J CD1 1 
ATOM   10528 C  CD2 . LEU J  1 68  ? 67.870  -37.189 73.232 1.00 24.52  ? 67  LEU J CD2 1 
ATOM   10529 N  N   . SER J  1 69  ? 70.845  -34.402 69.639 1.00 25.23  ? 68  SER J N   1 
ATOM   10530 C  CA  . SER J  1 69  ? 72.048  -33.690 69.233 1.00 25.35  ? 68  SER J CA  1 
ATOM   10531 C  C   . SER J  1 69  ? 73.252  -34.617 69.121 1.00 26.65  ? 68  SER J C   1 
ATOM   10532 O  O   . SER J  1 69  ? 74.289  -34.323 69.715 1.00 26.18  ? 68  SER J O   1 
ATOM   10533 C  CB  . SER J  1 69  ? 72.367  -32.571 70.185 1.00 23.75  ? 68  SER J CB  1 
ATOM   10534 O  OG  . SER J  1 69  ? 71.373  -31.569 70.125 1.00 25.69  ? 68  SER J OG  1 
ATOM   10535 N  N   . ARG J  1 70  ? 73.120  -35.719 68.362 1.00 28.34  ? 69  ARG J N   1 
ATOM   10536 C  CA  . ARG J  1 70  ? 74.233  -36.629 68.142 1.00 29.62  ? 69  ARG J CA  1 
ATOM   10537 C  C   . ARG J  1 70  ? 74.714  -36.505 66.699 1.00 29.23  ? 69  ARG J C   1 
ATOM   10538 O  O   . ARG J  1 70  ? 74.100  -35.803 65.898 1.00 27.41  ? 69  ARG J O   1 
ATOM   10539 C  CB  . ARG J  1 70  ? 73.838  -38.072 68.463 1.00 29.35  ? 69  ARG J CB  1 
ATOM   10540 C  CG  . ARG J  1 70  ? 73.192  -38.280 69.822 1.00 29.82  ? 69  ARG J CG  1 
ATOM   10541 C  CD  . ARG J  1 70  ? 74.142  -38.612 70.947 1.00 36.81  ? 69  ARG J CD  1 
ATOM   10542 N  NE  . ARG J  1 70  ? 73.385  -39.109 72.092 1.00 41.36  ? 69  ARG J NE  1 
ATOM   10543 C  CZ  . ARG J  1 70  ? 72.993  -40.376 72.289 1.00 41.39  ? 69  ARG J CZ  1 
ATOM   10544 N  NH1 . ARG J  1 70  ? 73.282  -41.310 71.404 1.00 40.80  ? 69  ARG J NH1 1 
ATOM   10545 N  NH2 . ARG J  1 70  ? 72.329  -40.718 73.384 1.00 42.47  ? 69  ARG J NH2 1 
ATOM   10546 N  N   . LYS J  1 71  ? 75.822  -37.194 66.385 1.00 28.58  ? 70  LYS J N   1 
ATOM   10547 C  CA  . LYS J  1 71  ? 76.352  -37.242 65.027 1.00 28.77  ? 70  LYS J CA  1 
ATOM   10548 C  C   . LYS J  1 71  ? 75.645  -38.363 64.260 1.00 26.38  ? 70  LYS J C   1 
ATOM   10549 O  O   . LYS J  1 71  ? 75.051  -39.246 64.863 1.00 24.85  ? 70  LYS J O   1 
ATOM   10550 C  CB  . LYS J  1 71  ? 77.885  -37.318 65.041 1.00 31.54  ? 70  LYS J CB  1 
ATOM   10551 C  CG  . LYS J  1 71  ? 78.578  -36.220 65.837 1.00 33.83  ? 70  LYS J CG  1 
ATOM   10552 C  CD  . LYS J  1 71  ? 80.066  -36.142 65.537 1.00 35.77  ? 70  LYS J CD  1 
ATOM   10553 C  CE  . LYS J  1 71  ? 80.890  -35.621 66.699 0.40 33.76  ? 70  LYS J CE  1 
ATOM   10554 N  NZ  . LYS J  1 71  ? 82.265  -36.181 66.730 0.40 31.57  ? 70  LYS J NZ  1 
ATOM   10555 N  N   . HIS J  1 72  ? 75.688  -38.299 62.926 1.00 25.70  ? 71  HIS J N   1 
ATOM   10556 C  CA  . HIS J  1 72  ? 74.993  -39.248 62.068 1.00 24.15  ? 71  HIS J CA  1 
ATOM   10557 C  C   . HIS J  1 72  ? 75.624  -40.635 62.183 1.00 24.66  ? 71  HIS J C   1 
ATOM   10558 O  O   . HIS J  1 72  ? 76.841  -40.763 62.244 1.00 25.18  ? 71  HIS J O   1 
ATOM   10559 C  CB  . HIS J  1 72  ? 74.989  -38.740 60.627 1.00 23.09  ? 71  HIS J CB  1 
ATOM   10560 C  CG  . HIS J  1 72  ? 74.404  -39.697 59.650 1.00 23.55  ? 71  HIS J CG  1 
ATOM   10561 N  ND1 . HIS J  1 72  ? 73.041  -39.782 59.399 1.00 23.55  ? 71  HIS J ND1 1 
ATOM   10562 C  CD2 . HIS J  1 72  ? 74.991  -40.616 58.858 1.00 25.69  ? 71  HIS J CD2 1 
ATOM   10563 C  CE1 . HIS J  1 72  ? 72.824  -40.718 58.498 1.00 24.82  ? 71  HIS J CE1 1 
ATOM   10564 N  NE2 . HIS J  1 72  ? 74.003  -41.247 58.155 1.00 26.85  ? 71  HIS J NE2 1 
ATOM   10565 N  N   . GLY J  1 73  ? 74.781  -41.674 62.218 1.00 25.52  ? 72  GLY J N   1 
ATOM   10566 C  CA  . GLY J  1 73  ? 75.241  -43.055 62.233 1.00 25.12  ? 72  GLY J CA  1 
ATOM   10567 C  C   . GLY J  1 73  ? 74.336  -43.948 61.381 1.00 26.06  ? 72  GLY J C   1 
ATOM   10568 O  O   . GLY J  1 73  ? 73.415  -43.463 60.728 1.00 27.05  ? 72  GLY J O   1 
ATOM   10569 N  N   . GLY J  1 74  ? 74.637  -45.251 61.351 1.00 24.33  ? 73  GLY J N   1 
ATOM   10570 C  CA  . GLY J  1 74  ? 73.721  -46.271 60.877 1.00 22.58  ? 73  GLY J CA  1 
ATOM   10571 C  C   . GLY J  1 74  ? 72.715  -46.607 61.978 1.00 22.79  ? 73  GLY J C   1 
ATOM   10572 O  O   . GLY J  1 74  ? 72.954  -46.312 63.148 1.00 20.12  ? 73  GLY J O   1 
ATOM   10573 N  N   . PRO J  1 75  ? 71.560  -47.226 61.648 1.00 24.27  ? 74  PRO J N   1 
ATOM   10574 C  CA  . PRO J  1 75  ? 70.527  -47.488 62.645 1.00 25.96  ? 74  PRO J CA  1 
ATOM   10575 C  C   . PRO J  1 75  ? 71.035  -48.287 63.841 1.00 27.52  ? 74  PRO J C   1 
ATOM   10576 O  O   . PRO J  1 75  ? 70.534  -48.135 64.948 1.00 24.13  ? 74  PRO J O   1 
ATOM   10577 C  CB  . PRO J  1 75  ? 69.448  -48.264 61.877 1.00 25.77  ? 74  PRO J CB  1 
ATOM   10578 C  CG  . PRO J  1 75  ? 70.094  -48.704 60.589 1.00 24.98  ? 74  PRO J CG  1 
ATOM   10579 C  CD  . PRO J  1 75  ? 71.176  -47.688 60.305 1.00 25.23  ? 74  PRO J CD  1 
ATOM   10580 N  N   . LYS J  1 76  ? 72.062  -49.111 63.614 1.00 32.60  ? 75  LYS J N   1 
ATOM   10581 C  CA  . LYS J  1 76  ? 72.541  -50.028 64.637 1.00 33.09  ? 75  LYS J CA  1 
ATOM   10582 C  C   . LYS J  1 76  ? 73.551  -49.368 65.571 1.00 30.59  ? 75  LYS J C   1 
ATOM   10583 O  O   . LYS J  1 76  ? 73.876  -49.946 66.591 1.00 28.39  ? 75  LYS J O   1 
ATOM   10584 C  CB  . LYS J  1 76  ? 73.024  -51.336 64.003 1.00 36.76  ? 75  LYS J CB  1 
ATOM   10585 C  CG  . LYS J  1 76  ? 71.884  -52.308 63.712 1.00 41.14  ? 75  LYS J CG  1 
ATOM   10586 C  CD  . LYS J  1 76  ? 71.971  -53.217 62.473 1.00 41.17  ? 75  LYS J CD  1 
ATOM   10587 C  CE  . LYS J  1 76  ? 70.873  -54.256 62.583 1.00 41.46  ? 75  LYS J CE  1 
ATOM   10588 N  NZ  . LYS J  1 76  ? 70.194  -54.580 61.299 1.00 40.68  ? 75  LYS J NZ  1 
ATOM   10589 N  N   . ASP J  1 77  ? 74.018  -48.164 65.234 1.00 32.31  ? 76  ASP J N   1 
ATOM   10590 C  CA  . ASP J  1 77  ? 75.033  -47.443 66.000 1.00 34.61  ? 76  ASP J CA  1 
ATOM   10591 C  C   . ASP J  1 77  ? 74.408  -46.822 67.241 1.00 37.52  ? 76  ASP J C   1 
ATOM   10592 O  O   . ASP J  1 77  ? 73.232  -46.472 67.244 1.00 40.18  ? 76  ASP J O   1 
ATOM   10593 C  CB  . ASP J  1 77  ? 75.729  -46.369 65.153 1.00 31.82  ? 76  ASP J CB  1 
ATOM   10594 C  CG  . ASP J  1 77  ? 76.621  -46.980 64.081 1.00 31.27  ? 76  ASP J CG  1 
ATOM   10595 O  OD1 . ASP J  1 77  ? 77.176  -48.032 64.342 1.00 32.56  ? 76  ASP J OD1 1 
ATOM   10596 O  OD2 . ASP J  1 77  ? 76.741  -46.412 62.988 1.00 31.54  ? 76  ASP J OD2 1 
ATOM   10597 N  N   . GLU J  1 78  ? 75.205  -46.688 68.308 1.00 40.07  ? 77  GLU J N   1 
ATOM   10598 C  CA  . GLU J  1 78  ? 74.709  -45.973 69.467 1.00 42.66  ? 77  GLU J CA  1 
ATOM   10599 C  C   . GLU J  1 78  ? 74.728  -44.477 69.155 1.00 39.45  ? 77  GLU J C   1 
ATOM   10600 O  O   . GLU J  1 78  ? 73.830  -43.745 69.556 1.00 37.22  ? 77  GLU J O   1 
ATOM   10601 C  CB  . GLU J  1 78  ? 75.469  -46.382 70.728 1.00 52.81  ? 77  GLU J CB  1 
ATOM   10602 C  CG  . GLU J  1 78  ? 74.736  -45.963 71.994 1.00 68.65  ? 77  GLU J CG  1 
ATOM   10603 C  CD  . GLU J  1 78  ? 75.555  -45.199 73.030 1.00 88.57  ? 77  GLU J CD  1 
ATOM   10604 O  OE1 . GLU J  1 78  ? 76.658  -45.691 73.372 1.00 102.93 ? 77  GLU J OE1 1 
ATOM   10605 O  OE2 . GLU J  1 78  ? 75.106  -44.096 73.488 1.00 98.63  ? 77  GLU J OE2 1 
ATOM   10606 N  N   . GLU J  1 79  ? 75.766  -44.038 68.435 1.00 35.71  ? 78  GLU J N   1 
ATOM   10607 C  CA  . GLU J  1 79  ? 75.886  -42.659 67.984 1.00 30.72  ? 78  GLU J CA  1 
ATOM   10608 C  C   . GLU J  1 79  ? 75.148  -42.519 66.646 1.00 28.23  ? 78  GLU J C   1 
ATOM   10609 O  O   . GLU J  1 79  ? 75.697  -42.809 65.576 1.00 26.10  ? 78  GLU J O   1 
ATOM   10610 C  CB  . GLU J  1 79  ? 77.366  -42.255 67.985 1.00 31.18  ? 78  GLU J CB  1 
ATOM   10611 C  CG  . GLU J  1 79  ? 77.653  -40.783 67.701 1.00 33.35  ? 78  GLU J CG  1 
ATOM   10612 C  CD  . GLU J  1 79  ? 77.275  -39.743 68.750 1.00 33.84  ? 78  GLU J CD  1 
ATOM   10613 O  OE1 . GLU J  1 79  ? 76.847  -40.130 69.868 1.00 32.35  ? 78  GLU J OE1 1 
ATOM   10614 O  OE2 . GLU J  1 79  ? 77.388  -38.527 68.433 1.00 34.83  ? 78  GLU J OE2 1 
ATOM   10615 N  N   . ARG J  1 80  ? 73.879  -42.085 66.731 1.00 25.19  ? 79  ARG J N   1 
ATOM   10616 C  CA  . ARG J  1 80  ? 73.055  -41.841 65.552 1.00 23.12  ? 79  ARG J CA  1 
ATOM   10617 C  C   . ARG J  1 80  ? 72.029  -40.745 65.823 1.00 22.76  ? 79  ARG J C   1 
ATOM   10618 O  O   . ARG J  1 80  ? 71.700  -40.446 66.971 1.00 21.20  ? 79  ARG J O   1 
ATOM   10619 C  CB  . ARG J  1 80  ? 72.289  -43.102 65.146 1.00 22.93  ? 79  ARG J CB  1 
ATOM   10620 C  CG  . ARG J  1 80  ? 71.400  -43.669 66.245 1.00 23.05  ? 79  ARG J CG  1 
ATOM   10621 C  CD  . ARG J  1 80  ? 70.549  -44.793 65.712 1.00 22.70  ? 79  ARG J CD  1 
ATOM   10622 N  NE  . ARG J  1 80  ? 69.278  -44.311 65.182 1.00 21.71  ? 79  ARG J NE  1 
ATOM   10623 C  CZ  . ARG J  1 80  ? 68.238  -45.076 64.891 1.00 20.93  ? 79  ARG J CZ  1 
ATOM   10624 N  NH1 . ARG J  1 80  ? 68.304  -46.383 65.059 1.00 20.05  ? 79  ARG J NH1 1 
ATOM   10625 N  NH2 . ARG J  1 80  ? 67.126  -44.539 64.430 1.00 20.40  ? 79  ARG J NH2 1 
ATOM   10626 N  N   . HIS J  1 81  ? 71.531  -40.156 64.732 1.00 22.99  ? 80  HIS J N   1 
ATOM   10627 C  CA  . HIS J  1 81  ? 70.321  -39.351 64.745 1.00 21.95  ? 80  HIS J CA  1 
ATOM   10628 C  C   . HIS J  1 81  ? 69.130  -40.270 64.957 1.00 22.88  ? 80  HIS J C   1 
ATOM   10629 O  O   . HIS J  1 81  ? 69.130  -41.395 64.462 1.00 24.86  ? 80  HIS J O   1 
ATOM   10630 C  CB  . HIS J  1 81  ? 70.165  -38.637 63.401 1.00 21.91  ? 80  HIS J CB  1 
ATOM   10631 C  CG  . HIS J  1 81  ? 71.301  -37.736 63.066 1.00 21.05  ? 80  HIS J CG  1 
ATOM   10632 N  ND1 . HIS J  1 81  ? 71.748  -37.553 61.767 1.00 20.61  ? 80  HIS J ND1 1 
ATOM   10633 C  CD2 . HIS J  1 81  ? 72.065  -36.956 63.859 1.00 20.32  ? 80  HIS J CD2 1 
ATOM   10634 C  CE1 . HIS J  1 81  ? 72.737  -36.684 61.772 1.00 21.56  ? 80  HIS J CE1 1 
ATOM   10635 N  NE2 . HIS J  1 81  ? 72.959  -36.313 63.052 1.00 21.71  ? 80  HIS J NE2 1 
ATOM   10636 N  N   . VAL J  1 82  ? 68.113  -39.787 65.671 1.00 22.32  ? 81  VAL J N   1 
ATOM   10637 C  CA  . VAL J  1 82  ? 66.889  -40.559 65.816 1.00 22.23  ? 81  VAL J CA  1 
ATOM   10638 C  C   . VAL J  1 82  ? 66.361  -40.943 64.434 1.00 21.69  ? 81  VAL J C   1 
ATOM   10639 O  O   . VAL J  1 82  ? 65.896  -42.058 64.245 1.00 24.65  ? 81  VAL J O   1 
ATOM   10640 C  CB  . VAL J  1 82  ? 65.826  -39.829 66.659 1.00 23.99  ? 81  VAL J CB  1 
ATOM   10641 C  CG1 . VAL J  1 82  ? 64.453  -40.459 66.516 1.00 23.85  ? 81  VAL J CG1 1 
ATOM   10642 C  CG2 . VAL J  1 82  ? 66.233  -39.779 68.126 1.00 24.66  ? 81  VAL J CG2 1 
ATOM   10643 N  N   . GLY J  1 83  ? 66.479  -40.047 63.456 1.00 19.12  ? 82  GLY J N   1 
ATOM   10644 C  CA  . GLY J  1 83  ? 65.893  -40.291 62.149 1.00 18.56  ? 82  GLY J CA  1 
ATOM   10645 C  C   . GLY J  1 83  ? 66.743  -41.185 61.250 1.00 19.11  ? 82  GLY J C   1 
ATOM   10646 O  O   . GLY J  1 83  ? 66.379  -41.391 60.085 1.00 19.84  ? 82  GLY J O   1 
ATOM   10647 N  N   . ASP J  1 84  ? 67.858  -41.718 61.788 1.00 18.04  ? 83  ASP J N   1 
ATOM   10648 C  CA  . ASP J  1 84  ? 68.830  -42.467 61.002 1.00 18.01  ? 83  ASP J CA  1 
ATOM   10649 C  C   . ASP J  1 84  ? 68.366  -43.914 60.807 1.00 18.49  ? 83  ASP J C   1 
ATOM   10650 O  O   . ASP J  1 84  ? 68.582  -44.766 61.666 1.00 19.59  ? 83  ASP J O   1 
ATOM   10651 C  CB  . ASP J  1 84  ? 70.223  -42.375 61.623 1.00 18.42  ? 83  ASP J CB  1 
ATOM   10652 C  CG  . ASP J  1 84  ? 70.921  -41.038 61.403 1.00 19.28  ? 83  ASP J CG  1 
ATOM   10653 O  OD1 . ASP J  1 84  ? 70.485  -40.275 60.515 1.00 19.64  ? 83  ASP J OD1 1 
ATOM   10654 O  OD2 . ASP J  1 84  ? 71.913  -40.773 62.116 1.00 18.70  ? 83  ASP J OD2 1 
ATOM   10655 N  N   . LEU J  1 85  ? 67.743  -44.199 59.654 1.00 17.98  ? 84  LEU J N   1 
ATOM   10656 C  CA  . LEU J  1 85  ? 67.175  -45.517 59.416 1.00 17.83  ? 84  LEU J CA  1 
ATOM   10657 C  C   . LEU J  1 85  ? 68.021  -46.305 58.415 1.00 20.22  ? 84  LEU J C   1 
ATOM   10658 O  O   . LEU J  1 85  ? 67.596  -47.361 57.944 1.00 21.22  ? 84  LEU J O   1 
ATOM   10659 C  CB  . LEU J  1 85  ? 65.737  -45.374 58.914 1.00 16.21  ? 84  LEU J CB  1 
ATOM   10660 C  CG  . LEU J  1 85  ? 64.700  -44.928 59.941 1.00 15.63  ? 84  LEU J CG  1 
ATOM   10661 C  CD1 . LEU J  1 85  ? 63.310  -44.957 59.324 1.00 14.63  ? 84  LEU J CD1 1 
ATOM   10662 C  CD2 . LEU J  1 85  ? 64.741  -45.808 61.191 1.00 15.34  ? 84  LEU J CD2 1 
ATOM   10663 N  N   . GLY J  1 86  ? 69.220  -45.801 58.090 1.00 20.79  ? 85  GLY J N   1 
ATOM   10664 C  CA  . GLY J  1 86  ? 70.135  -46.549 57.244 1.00 20.61  ? 85  GLY J CA  1 
ATOM   10665 C  C   . GLY J  1 86  ? 69.753  -46.519 55.767 1.00 21.20  ? 85  GLY J C   1 
ATOM   10666 O  O   . GLY J  1 86  ? 69.379  -45.469 55.250 1.00 23.73  ? 85  GLY J O   1 
ATOM   10667 N  N   . ASN J  1 87  ? 69.863  -47.674 55.094 1.00 19.85  ? 86  ASN J N   1 
ATOM   10668 C  CA  . ASN J  1 87  ? 69.625  -47.755 53.662 1.00 19.05  ? 86  ASN J CA  1 
ATOM   10669 C  C   . ASN J  1 87  ? 68.449  -48.673 53.346 1.00 19.36  ? 86  ASN J C   1 
ATOM   10670 O  O   . ASN J  1 87  ? 68.059  -49.534 54.142 1.00 18.27  ? 86  ASN J O   1 
ATOM   10671 C  CB  . ASN J  1 87  ? 70.842  -48.275 52.897 1.00 19.44  ? 86  ASN J CB  1 
ATOM   10672 C  CG  . ASN J  1 87  ? 71.986  -47.300 52.928 1.00 20.49  ? 86  ASN J CG  1 
ATOM   10673 O  OD1 . ASN J  1 87  ? 71.979  -46.283 52.249 1.00 21.94  ? 86  ASN J OD1 1 
ATOM   10674 N  ND2 . ASN J  1 87  ? 72.969  -47.593 53.741 1.00 21.47  ? 86  ASN J ND2 1 
ATOM   10675 N  N   . VAL J  1 88  ? 67.888  -48.448 52.154 1.00 18.71  ? 87  VAL J N   1 
ATOM   10676 C  CA  . VAL J  1 88  ? 66.973  -49.392 51.543 1.00 17.68  ? 87  VAL J CA  1 
ATOM   10677 C  C   . VAL J  1 88  ? 67.616  -49.822 50.227 1.00 17.58  ? 87  VAL J C   1 
ATOM   10678 O  O   . VAL J  1 88  ? 68.475  -49.112 49.698 1.00 16.10  ? 87  VAL J O   1 
ATOM   10679 C  CB  . VAL J  1 88  ? 65.563  -48.787 51.366 1.00 16.96  ? 87  VAL J CB  1 
ATOM   10680 C  CG1 . VAL J  1 88  ? 64.966  -48.335 52.692 1.00 15.95  ? 87  VAL J CG1 1 
ATOM   10681 C  CG2 . VAL J  1 88  ? 65.516  -47.651 50.354 1.00 15.98  ? 87  VAL J CG2 1 
ATOM   10682 N  N   . THR J  1 89  ? 67.226  -50.998 49.722 1.00 17.97  ? 88  THR J N   1 
ATOM   10683 C  CA  . THR J  1 89  ? 67.900  -51.544 48.558 1.00 19.29  ? 88  THR J CA  1 
ATOM   10684 C  C   . THR J  1 89  ? 66.921  -51.673 47.401 1.00 20.02  ? 88  THR J C   1 
ATOM   10685 O  O   . THR J  1 89  ? 65.903  -52.340 47.534 1.00 19.57  ? 88  THR J O   1 
ATOM   10686 C  CB  . THR J  1 89  ? 68.502  -52.921 48.849 1.00 19.24  ? 88  THR J CB  1 
ATOM   10687 O  OG1 . THR J  1 89  ? 69.308  -52.861 50.026 1.00 19.47  ? 88  THR J OG1 1 
ATOM   10688 C  CG2 . THR J  1 89  ? 69.291  -53.449 47.664 1.00 19.83  ? 88  THR J CG2 1 
ATOM   10689 N  N   . ALA J  1 90  ? 67.258  -51.062 46.263 1.00 21.45  ? 89  ALA J N   1 
ATOM   10690 C  CA  . ALA J  1 90  ? 66.453  -51.219 45.063 1.00 23.02  ? 89  ALA J CA  1 
ATOM   10691 C  C   . ALA J  1 90  ? 67.028  -52.333 44.187 1.00 23.54  ? 89  ALA J C   1 
ATOM   10692 O  O   . ALA J  1 90  ? 68.240  -52.385 43.945 1.00 24.95  ? 89  ALA J O   1 
ATOM   10693 C  CB  . ALA J  1 90  ? 66.406  -49.909 44.322 1.00 23.19  ? 89  ALA J CB  1 
ATOM   10694 N  N   . ASP J  1 91  ? 66.133  -53.202 43.701 1.00 24.08  ? 90  ASP J N   1 
ATOM   10695 C  CA  . ASP J  1 91  ? 66.466  -54.312 42.818 1.00 26.63  ? 90  ASP J CA  1 
ATOM   10696 C  C   . ASP J  1 91  ? 66.692  -53.790 41.398 1.00 28.84  ? 90  ASP J C   1 
ATOM   10697 O  O   . ASP J  1 91  ? 66.598  -52.590 41.158 1.00 28.01  ? 90  ASP J O   1 
ATOM   10698 C  CB  . ASP J  1 91  ? 65.400  -55.411 42.876 1.00 26.80  ? 90  ASP J CB  1 
ATOM   10699 C  CG  . ASP J  1 91  ? 64.016  -55.017 42.374 1.00 27.49  ? 90  ASP J CG  1 
ATOM   10700 O  OD1 . ASP J  1 91  ? 63.901  -54.053 41.590 1.00 25.27  ? 90  ASP J OD1 1 
ATOM   10701 O  OD2 . ASP J  1 91  ? 63.049  -55.695 42.771 1.00 29.54  ? 90  ASP J OD2 1 
ATOM   10702 N  N   . LYS J  1 92  ? 66.981  -54.705 40.458 1.00 31.06  ? 91  LYS J N   1 
ATOM   10703 C  CA  . LYS J  1 92  ? 67.326  -54.337 39.089 1.00 30.28  ? 91  LYS J CA  1 
ATOM   10704 C  C   . LYS J  1 92  ? 66.178  -53.592 38.414 1.00 30.02  ? 91  LYS J C   1 
ATOM   10705 O  O   . LYS J  1 92  ? 66.394  -52.944 37.400 1.00 31.87  ? 91  LYS J O   1 
ATOM   10706 C  CB  . LYS J  1 92  ? 67.761  -55.552 38.252 1.00 29.82  ? 91  LYS J CB  1 
ATOM   10707 C  CG  . LYS J  1 92  ? 66.708  -56.603 37.952 1.00 31.25  ? 91  LYS J CG  1 
ATOM   10708 C  CD  . LYS J  1 92  ? 67.243  -57.708 37.104 1.00 33.63  ? 91  LYS J CD  1 
ATOM   10709 C  CE  . LYS J  1 92  ? 66.138  -58.662 36.731 1.00 37.20  ? 91  LYS J CE  1 
ATOM   10710 N  NZ  . LYS J  1 92  ? 66.729  -59.975 36.405 1.00 42.67  ? 91  LYS J NZ  1 
ATOM   10711 N  N   . ASP J  1 93  ? 64.967  -53.689 38.971 1.00 30.39  ? 92  ASP J N   1 
ATOM   10712 C  CA  . ASP J  1 93  ? 63.779  -53.075 38.391 1.00 31.14  ? 92  ASP J CA  1 
ATOM   10713 C  C   . ASP J  1 93  ? 63.510  -51.712 39.018 1.00 30.50  ? 92  ASP J C   1 
ATOM   10714 O  O   . ASP J  1 93  ? 62.553  -51.036 38.649 1.00 28.88  ? 92  ASP J O   1 
ATOM   10715 C  CB  . ASP J  1 93  ? 62.537  -53.943 38.591 1.00 32.93  ? 92  ASP J CB  1 
ATOM   10716 C  CG  . ASP J  1 93  ? 62.617  -55.256 37.849 1.00 37.54  ? 92  ASP J CG  1 
ATOM   10717 O  OD1 . ASP J  1 93  ? 63.048  -55.236 36.677 1.00 35.01  ? 92  ASP J OD1 1 
ATOM   10718 O  OD2 . ASP J  1 93  ? 62.237  -56.288 38.453 1.00 47.86  ? 92  ASP J OD2 1 
ATOM   10719 N  N   . GLY J  1 94  ? 64.341  -51.325 39.984 1.00 30.29  ? 93  GLY J N   1 
ATOM   10720 C  CA  . GLY J  1 94  ? 64.193  -50.031 40.623 1.00 29.72  ? 93  GLY J CA  1 
ATOM   10721 C  C   . GLY J  1 94  ? 63.155  -50.061 41.736 1.00 28.76  ? 93  GLY J C   1 
ATOM   10722 O  O   . GLY J  1 94  ? 62.634  -49.017 42.112 1.00 30.85  ? 93  GLY J O   1 
ATOM   10723 N  N   . VAL J  1 95  ? 62.876  -51.256 42.266 1.00 24.97  ? 94  VAL J N   1 
ATOM   10724 C  CA  . VAL J  1 95  ? 61.917  -51.388 43.348 1.00 22.90  ? 94  VAL J CA  1 
ATOM   10725 C  C   . VAL J  1 95  ? 62.643  -51.765 44.639 1.00 22.44  ? 94  VAL J C   1 
ATOM   10726 O  O   . VAL J  1 95  ? 63.409  -52.718 44.670 1.00 22.78  ? 94  VAL J O   1 
ATOM   10727 C  CB  . VAL J  1 95  ? 60.814  -52.400 43.004 1.00 21.19  ? 94  VAL J CB  1 
ATOM   10728 C  CG1 . VAL J  1 95  ? 59.862  -52.618 44.177 1.00 20.74  ? 94  VAL J CG1 1 
ATOM   10729 C  CG2 . VAL J  1 95  ? 60.057  -51.986 41.759 1.00 20.06  ? 94  VAL J CG2 1 
ATOM   10730 N  N   . ALA J  1 96  ? 62.379  -51.004 45.700 1.00 21.46  ? 95  ALA J N   1 
ATOM   10731 C  CA  . ALA J  1 96  ? 62.896  -51.342 47.009 1.00 22.37  ? 95  ALA J CA  1 
ATOM   10732 C  C   . ALA J  1 96  ? 61.764  -51.877 47.871 1.00 22.98  ? 95  ALA J C   1 
ATOM   10733 O  O   . ALA J  1 96  ? 60.808  -51.161 48.143 1.00 24.37  ? 95  ALA J O   1 
ATOM   10734 C  CB  . ALA J  1 96  ? 63.512  -50.117 47.645 1.00 23.08  ? 95  ALA J CB  1 
ATOM   10735 N  N   A ASP J  1 97  ? 61.860  -53.148 48.284 0.50 22.34  ? 96  ASP J N   1 
ATOM   10736 N  N   B ASP J  1 97  ? 61.883  -53.135 48.301 0.50 22.37  ? 96  ASP J N   1 
ATOM   10737 C  CA  A ASP J  1 97  ? 60.878  -53.687 49.213 0.50 21.40  ? 96  ASP J CA  1 
ATOM   10738 C  CA  B ASP J  1 97  ? 60.921  -53.713 49.217 0.50 21.47  ? 96  ASP J CA  1 
ATOM   10739 C  C   A ASP J  1 97  ? 61.370  -53.413 50.626 0.50 20.36  ? 96  ASP J C   1 
ATOM   10740 C  C   B ASP J  1 97  ? 61.393  -53.409 50.629 0.50 20.39  ? 96  ASP J C   1 
ATOM   10741 O  O   A ASP J  1 97  ? 62.163  -54.170 51.163 0.50 20.90  ? 96  ASP J O   1 
ATOM   10742 O  O   B ASP J  1 97  ? 62.205  -54.147 51.173 0.50 20.94  ? 96  ASP J O   1 
ATOM   10743 C  CB  A ASP J  1 97  ? 60.554  -55.161 48.940 0.50 21.04  ? 96  ASP J CB  1 
ATOM   10744 C  CB  B ASP J  1 97  ? 60.866  -55.224 48.986 0.50 21.05  ? 96  ASP J CB  1 
ATOM   10745 C  CG  A ASP J  1 97  ? 59.799  -55.350 47.625 0.50 20.62  ? 96  ASP J CG  1 
ATOM   10746 C  CG  B ASP J  1 97  ? 60.194  -56.028 50.086 0.50 21.04  ? 96  ASP J CG  1 
ATOM   10747 O  OD1 A ASP J  1 97  ? 58.779  -54.628 47.388 0.50 20.45  ? 96  ASP J OD1 1 
ATOM   10748 O  OD1 B ASP J  1 97  ? 59.539  -55.424 50.965 0.50 20.96  ? 96  ASP J OD1 1 
ATOM   10749 O  OD2 A ASP J  1 97  ? 60.248  -56.179 46.822 0.50 19.85  ? 96  ASP J OD2 1 
ATOM   10750 O  OD2 B ASP J  1 97  ? 60.320  -57.256 50.045 0.50 20.94  ? 96  ASP J OD2 1 
ATOM   10751 N  N   . VAL J  1 98  ? 60.902  -52.310 51.198 1.00 19.16  ? 97  VAL J N   1 
ATOM   10752 C  CA  . VAL J  1 98  ? 61.408  -51.844 52.473 1.00 18.85  ? 97  VAL J CA  1 
ATOM   10753 C  C   . VAL J  1 98  ? 60.845  -52.699 53.600 1.00 18.34  ? 97  VAL J C   1 
ATOM   10754 O  O   . VAL J  1 98  ? 59.655  -52.989 53.636 1.00 19.30  ? 97  VAL J O   1 
ATOM   10755 C  CB  . VAL J  1 98  ? 61.072  -50.362 52.691 1.00 18.02  ? 97  VAL J CB  1 
ATOM   10756 C  CG1 . VAL J  1 98  ? 61.620  -49.850 54.016 1.00 16.81  ? 97  VAL J CG1 1 
ATOM   10757 C  CG2 . VAL J  1 98  ? 61.534  -49.514 51.527 1.00 17.61  ? 97  VAL J CG2 1 
ATOM   10758 N  N   . SER J  1 99  ? 61.715  -53.071 54.529 1.00 18.32  ? 98  SER J N   1 
ATOM   10759 C  CA  . SER J  1 99  ? 61.297  -53.735 55.747 1.00 19.18  ? 98  SER J CA  1 
ATOM   10760 C  C   . SER J  1 99  ? 62.378  -53.556 56.801 1.00 18.68  ? 98  SER J C   1 
ATOM   10761 O  O   . SER J  1 99  ? 63.466  -54.101 56.673 1.00 19.98  ? 98  SER J O   1 
ATOM   10762 C  CB  . SER J  1 99  ? 60.999  -55.185 55.507 1.00 21.94  ? 98  SER J CB  1 
ATOM   10763 O  OG  . SER J  1 99  ? 60.645  -55.803 56.722 1.00 23.72  ? 98  SER J OG  1 
ATOM   10764 N  N   . ILE J  1 100 ? 62.071  -52.756 57.823 1.00 17.85  ? 99  ILE J N   1 
ATOM   10765 C  CA  . ILE J  1 100 ? 63.043  -52.370 58.828 1.00 18.37  ? 99  ILE J CA  1 
ATOM   10766 C  C   . ILE J  1 100 ? 62.374  -52.448 60.183 1.00 19.88  ? 99  ILE J C   1 
ATOM   10767 O  O   . ILE J  1 100 ? 61.173  -52.240 60.291 1.00 22.63  ? 99  ILE J O   1 
ATOM   10768 C  CB  . ILE J  1 100 ? 63.543  -50.935 58.557 1.00 17.52  ? 99  ILE J CB  1 
ATOM   10769 C  CG1 . ILE J  1 100 ? 64.516  -50.882 57.382 1.00 17.49  ? 99  ILE J CG1 1 
ATOM   10770 C  CG2 . ILE J  1 100 ? 64.168  -50.315 59.807 1.00 16.71  ? 99  ILE J CG2 1 
ATOM   10771 C  CD1 . ILE J  1 100 ? 64.724  -49.499 56.872 1.00 18.28  ? 99  ILE J CD1 1 
ATOM   10772 N  N   . GLU J  1 101 ? 63.171  -52.731 61.207 1.00 21.26  ? 100 GLU J N   1 
ATOM   10773 C  CA  . GLU J  1 101 ? 62.656  -52.627 62.556 1.00 24.36  ? 100 GLU J CA  1 
ATOM   10774 C  C   . GLU J  1 101 ? 63.600  -51.723 63.337 1.00 25.19  ? 100 GLU J C   1 
ATOM   10775 O  O   . GLU J  1 101 ? 64.807  -51.876 63.256 1.00 27.06  ? 100 GLU J O   1 
ATOM   10776 C  CB  . GLU J  1 101 ? 62.490  -54.028 63.124 1.00 26.86  ? 100 GLU J CB  1 
ATOM   10777 C  CG  . GLU J  1 101 ? 62.198  -54.043 64.600 1.00 32.98  ? 100 GLU J CG  1 
ATOM   10778 C  CD  . GLU J  1 101 ? 61.825  -55.400 65.143 1.00 38.76  ? 100 GLU J CD  1 
ATOM   10779 O  OE1 . GLU J  1 101 ? 62.296  -55.749 66.243 1.00 41.21  ? 100 GLU J OE1 1 
ATOM   10780 O  OE2 . GLU J  1 101 ? 61.079  -56.123 64.446 1.00 43.78  ? 100 GLU J OE2 1 
ATOM   10781 N  N   . ASP J  1 102 ? 63.041  -50.742 64.035 1.00 26.12  ? 101 ASP J N   1 
ATOM   10782 C  CA  . ASP J  1 102 ? 63.881  -49.771 64.704 1.00 24.79  ? 101 ASP J CA  1 
ATOM   10783 C  C   . ASP J  1 102 ? 63.313  -49.504 66.087 1.00 25.22  ? 101 ASP J C   1 
ATOM   10784 O  O   . ASP J  1 102 ? 62.107  -49.455 66.256 1.00 24.64  ? 101 ASP J O   1 
ATOM   10785 C  CB  . ASP J  1 102 ? 63.980  -48.472 63.898 1.00 25.10  ? 101 ASP J CB  1 
ATOM   10786 C  CG  . ASP J  1 102 ? 65.099  -47.595 64.413 1.00 27.89  ? 101 ASP J CG  1 
ATOM   10787 O  OD1 . ASP J  1 102 ? 66.253  -48.001 64.224 1.00 30.08  ? 101 ASP J OD1 1 
ATOM   10788 O  OD2 . ASP J  1 102 ? 64.815  -46.548 65.048 1.00 28.27  ? 101 ASP J OD2 1 
ATOM   10789 N  N   . SER J  1 103 ? 64.200  -49.306 67.060 1.00 25.81  ? 102 SER J N   1 
ATOM   10790 C  CA  . SER J  1 103 ? 63.764  -49.119 68.436 1.00 25.51  ? 102 SER J CA  1 
ATOM   10791 C  C   . SER J  1 103 ? 64.065  -47.711 68.930 1.00 26.39  ? 102 SER J C   1 
ATOM   10792 O  O   . SER J  1 103 ? 63.852  -47.417 70.104 1.00 29.15  ? 102 SER J O   1 
ATOM   10793 C  CB  . SER J  1 103 ? 64.371  -50.149 69.327 1.00 26.43  ? 102 SER J CB  1 
ATOM   10794 O  OG  . SER J  1 103 ? 63.552  -51.299 69.319 1.00 29.22  ? 102 SER J OG  1 
ATOM   10795 N  N   . VAL J  1 104 ? 64.546  -46.844 68.029 1.00 24.46  ? 103 VAL J N   1 
ATOM   10796 C  CA  . VAL J  1 104 ? 64.933  -45.507 68.434 1.00 21.84  ? 103 VAL J CA  1 
ATOM   10797 C  C   . VAL J  1 104 ? 63.832  -44.537 68.028 1.00 21.12  ? 103 VAL J C   1 
ATOM   10798 O  O   . VAL J  1 104 ? 63.454  -43.687 68.825 1.00 22.13  ? 103 VAL J O   1 
ATOM   10799 C  CB  . VAL J  1 104 ? 66.312  -45.112 67.875 1.00 21.48  ? 103 VAL J CB  1 
ATOM   10800 C  CG1 . VAL J  1 104 ? 66.642  -43.644 68.113 1.00 20.55  ? 103 VAL J CG1 1 
ATOM   10801 C  CG2 . VAL J  1 104 ? 67.409  -45.990 68.440 1.00 20.25  ? 103 VAL J CG2 1 
ATOM   10802 N  N   . ILE J  1 105 ? 63.331  -44.661 66.795 1.00 20.00  ? 104 ILE J N   1 
ATOM   10803 C  CA  . ILE J  1 105 ? 62.149  -43.904 66.419 1.00 19.67  ? 104 ILE J CA  1 
ATOM   10804 C  C   . ILE J  1 105 ? 60.980  -44.416 67.255 1.00 20.05  ? 104 ILE J C   1 
ATOM   10805 O  O   . ILE J  1 105 ? 61.024  -45.526 67.779 1.00 20.37  ? 104 ILE J O   1 
ATOM   10806 C  CB  . ILE J  1 105 ? 61.853  -44.006 64.908 1.00 18.39  ? 104 ILE J CB  1 
ATOM   10807 C  CG1 . ILE J  1 105 ? 61.511  -45.436 64.485 1.00 16.72  ? 104 ILE J CG1 1 
ATOM   10808 C  CG2 . ILE J  1 105 ? 63.002  -43.428 64.101 1.00 18.41  ? 104 ILE J CG2 1 
ATOM   10809 C  CD1 . ILE J  1 105 ? 60.909  -45.537 63.119 1.00 16.04  ? 104 ILE J CD1 1 
ATOM   10810 N  N   . SER J  1 106 ? 59.948  -43.582 67.392 1.00 20.58  ? 105 SER J N   1 
ATOM   10811 C  CA  . SER J  1 106 ? 58.745  -43.986 68.098 1.00 21.84  ? 105 SER J CA  1 
ATOM   10812 C  C   . SER J  1 106 ? 57.518  -43.360 67.446 1.00 21.78  ? 105 SER J C   1 
ATOM   10813 O  O   . SER J  1 106 ? 57.626  -42.350 66.737 1.00 22.08  ? 105 SER J O   1 
ATOM   10814 C  CB  . SER J  1 106 ? 58.817  -43.606 69.541 1.00 21.45  ? 105 SER J CB  1 
ATOM   10815 O  OG  . SER J  1 106 ? 57.813  -44.327 70.247 1.00 22.23  ? 105 SER J OG  1 
ATOM   10816 N  N   . LEU J  1 107 ? 56.362  -44.004 67.682 1.00 23.22  ? 106 LEU J N   1 
ATOM   10817 C  CA  . LEU J  1 107 ? 55.103  -43.420 67.261 1.00 25.69  ? 106 LEU J CA  1 
ATOM   10818 C  C   . LEU J  1 107 ? 54.335  -42.854 68.454 1.00 28.97  ? 106 LEU J C   1 
ATOM   10819 O  O   . LEU J  1 107 ? 53.180  -42.473 68.310 1.00 31.79  ? 106 LEU J O   1 
ATOM   10820 C  CB  . LEU J  1 107 ? 54.281  -44.460 66.503 1.00 23.66  ? 106 LEU J CB  1 
ATOM   10821 C  CG  . LEU J  1 107 ? 54.970  -45.111 65.310 1.00 23.30  ? 106 LEU J CG  1 
ATOM   10822 C  CD1 . LEU J  1 107 ? 53.941  -45.980 64.616 1.00 24.49  ? 106 LEU J CD1 1 
ATOM   10823 C  CD2 . LEU J  1 107 ? 55.517  -44.047 64.357 1.00 21.52  ? 106 LEU J CD2 1 
ATOM   10824 N  N   . SER J  1 108 ? 54.993  -42.762 69.617 1.00 35.17  ? 107 SER J N   1 
ATOM   10825 C  CA  . SER J  1 108 ? 54.461  -42.029 70.758 1.00 37.69  ? 107 SER J CA  1 
ATOM   10826 C  C   . SER J  1 108 ? 55.599  -41.675 71.709 1.00 39.92  ? 107 SER J C   1 
ATOM   10827 O  O   . SER J  1 108 ? 56.671  -42.287 71.667 1.00 48.30  ? 107 SER J O   1 
ATOM   10828 C  CB  . SER J  1 108 ? 53.383  -42.829 71.477 1.00 39.15  ? 107 SER J CB  1 
ATOM   10829 O  OG  . SER J  1 108 ? 53.922  -44.055 72.001 1.00 42.89  ? 107 SER J OG  1 
ATOM   10830 N  N   . GLY J  1 109 ? 55.396  -40.644 72.533 1.00 37.77  ? 108 GLY J N   1 
ATOM   10831 C  CA  . GLY J  1 109 ? 56.403  -40.221 73.497 1.00 39.58  ? 108 GLY J CA  1 
ATOM   10832 C  C   . GLY J  1 109 ? 57.478  -39.343 72.852 1.00 43.88  ? 108 GLY J C   1 
ATOM   10833 O  O   . GLY J  1 109 ? 57.197  -38.704 71.841 1.00 47.65  ? 108 GLY J O   1 
ATOM   10834 N  N   . ASP J  1 110 ? 58.694  -39.394 73.419 1.00 42.98  ? 109 ASP J N   1 
ATOM   10835 C  CA  . ASP J  1 110 ? 59.684  -38.366 73.201 1.00 47.05  ? 109 ASP J CA  1 
ATOM   10836 C  C   . ASP J  1 110 ? 60.165  -38.318 71.752 1.00 50.21  ? 109 ASP J C   1 
ATOM   10837 O  O   . ASP J  1 110 ? 60.572  -37.253 71.269 1.00 61.98  ? 109 ASP J O   1 
ATOM   10838 C  CB  . ASP J  1 110 ? 60.866  -38.528 74.159 1.00 47.32  ? 109 ASP J CB  1 
ATOM   10839 C  CG  . ASP J  1 110 ? 60.462  -38.457 75.623 1.00 44.63  ? 109 ASP J CG  1 
ATOM   10840 O  OD1 . ASP J  1 110 ? 59.740  -37.513 75.973 1.00 38.18  ? 109 ASP J OD1 1 
ATOM   10841 O  OD2 . ASP J  1 110 ? 60.843  -39.366 76.388 1.00 49.50  ? 109 ASP J OD2 1 
ATOM   10842 N  N   . HIS J  1 111 ? 60.172  -39.468 71.070 1.00 42.16  ? 110 HIS J N   1 
ATOM   10843 C  CA  . HIS J  1 111 ? 60.811  -39.452 69.766 1.00 41.96  ? 110 HIS J CA  1 
ATOM   10844 C  C   . HIS J  1 111 ? 59.768  -39.639 68.666 1.00 39.77  ? 110 HIS J C   1 
ATOM   10845 O  O   . HIS J  1 111 ? 60.029  -40.309 67.655 1.00 39.81  ? 110 HIS J O   1 
ATOM   10846 C  CB  . HIS J  1 111 ? 61.971  -40.459 69.734 1.00 48.25  ? 110 HIS J CB  1 
ATOM   10847 C  CG  . HIS J  1 111 ? 63.041  -40.204 70.749 1.00 49.90  ? 110 HIS J CG  1 
ATOM   10848 N  ND1 . HIS J  1 111 ? 63.847  -41.212 71.245 1.00 47.46  ? 110 HIS J ND1 1 
ATOM   10849 C  CD2 . HIS J  1 111 ? 63.465  -39.063 71.346 1.00 46.95  ? 110 HIS J CD2 1 
ATOM   10850 C  CE1 . HIS J  1 111 ? 64.722  -40.711 72.096 1.00 49.23  ? 110 HIS J CE1 1 
ATOM   10851 N  NE2 . HIS J  1 111 ? 64.491  -39.387 72.187 1.00 49.84  ? 110 HIS J NE2 1 
ATOM   10852 N  N   . CYS J  1 112 ? 58.583  -39.056 68.885 1.00 34.97  ? 111 CYS J N   1 
ATOM   10853 C  CA  . CYS J  1 112 ? 57.503  -39.224 67.926 1.00 32.02  ? 111 CYS J CA  1 
ATOM   10854 C  C   . CYS J  1 112 ? 57.914  -38.628 66.577 1.00 30.25  ? 111 CYS J C   1 
ATOM   10855 O  O   . CYS J  1 112 ? 58.480  -37.534 66.524 1.00 29.73  ? 111 CYS J O   1 
ATOM   10856 C  CB  . CYS J  1 112 ? 56.233  -38.613 68.478 1.00 34.41  ? 111 CYS J CB  1 
ATOM   10857 S  SG  . CYS J  1 112 ? 54.713  -39.429 67.905 1.00 30.14  ? 111 CYS J SG  1 
ATOM   10858 N  N   . ILE J  1 113 ? 57.719  -39.405 65.502 1.00 27.30  ? 112 ILE J N   1 
ATOM   10859 C  CA  . ILE J  1 113 ? 58.087  -38.990 64.158 1.00 25.61  ? 112 ILE J CA  1 
ATOM   10860 C  C   . ILE J  1 113 ? 56.850  -38.519 63.387 1.00 26.76  ? 112 ILE J C   1 
ATOM   10861 O  O   . ILE J  1 113 ? 56.952  -38.170 62.203 1.00 29.88  ? 112 ILE J O   1 
ATOM   10862 C  CB  . ILE J  1 113 ? 58.828  -40.110 63.399 1.00 23.05  ? 112 ILE J CB  1 
ATOM   10863 C  CG1 . ILE J  1 113 ? 58.032  -41.418 63.380 1.00 24.84  ? 112 ILE J CG1 1 
ATOM   10864 C  CG2 . ILE J  1 113 ? 60.236  -40.298 63.928 1.00 21.61  ? 112 ILE J CG2 1 
ATOM   10865 C  CD1 . ILE J  1 113 ? 58.407  -42.320 62.218 1.00 23.56  ? 112 ILE J CD1 1 
ATOM   10866 N  N   . ILE J  1 114 ? 55.684  -38.548 64.049 1.00 24.97  ? 113 ILE J N   1 
ATOM   10867 C  CA  . ILE J  1 114 ? 54.448  -38.109 63.417 1.00 24.04  ? 113 ILE J CA  1 
ATOM   10868 C  C   . ILE J  1 114 ? 54.579  -36.630 63.076 1.00 22.43  ? 113 ILE J C   1 
ATOM   10869 O  O   . ILE J  1 114 ? 55.046  -35.841 63.896 1.00 21.31  ? 113 ILE J O   1 
ATOM   10870 C  CB  . ILE J  1 114 ? 53.234  -38.368 64.324 1.00 25.18  ? 113 ILE J CB  1 
ATOM   10871 C  CG1 . ILE J  1 114 ? 53.173  -39.851 64.686 1.00 26.41  ? 113 ILE J CG1 1 
ATOM   10872 C  CG2 . ILE J  1 114 ? 51.952  -37.927 63.628 1.00 25.21  ? 113 ILE J CG2 1 
ATOM   10873 C  CD1 . ILE J  1 114 ? 51.810  -40.370 65.079 1.00 25.74  ? 113 ILE J CD1 1 
ATOM   10874 N  N   . GLY J  1 115 ? 54.192  -36.297 61.846 1.00 20.61  ? 114 GLY J N   1 
ATOM   10875 C  CA  . GLY J  1 115 ? 54.183  -34.924 61.374 1.00 19.76  ? 114 GLY J CA  1 
ATOM   10876 C  C   . GLY J  1 115 ? 55.566  -34.447 60.947 1.00 19.32  ? 114 GLY J C   1 
ATOM   10877 O  O   . GLY J  1 115 ? 55.765  -33.243 60.771 1.00 19.48  ? 114 GLY J O   1 
ATOM   10878 N  N   . ARG J  1 116 ? 56.505  -35.398 60.796 1.00 19.15  ? 115 ARG J N   1 
ATOM   10879 C  CA  . ARG J  1 116 ? 57.824  -35.107 60.250 1.00 18.89  ? 115 ARG J CA  1 
ATOM   10880 C  C   . ARG J  1 116 ? 57.921  -35.681 58.833 1.00 18.64  ? 115 ARG J C   1 
ATOM   10881 O  O   . ARG J  1 116 ? 56.911  -36.113 58.284 1.00 19.26  ? 115 ARG J O   1 
ATOM   10882 C  CB  . ARG J  1 116 ? 58.890  -35.556 61.249 1.00 18.48  ? 115 ARG J CB  1 
ATOM   10883 C  CG  . ARG J  1 116 ? 58.645  -34.997 62.639 1.00 18.31  ? 115 ARG J CG  1 
ATOM   10884 C  CD  . ARG J  1 116 ? 59.778  -35.269 63.605 1.00 19.03  ? 115 ARG J CD  1 
ATOM   10885 N  NE  . ARG J  1 116 ? 59.545  -34.709 64.927 1.00 20.15  ? 115 ARG J NE  1 
ATOM   10886 C  CZ  . ARG J  1 116 ? 59.864  -33.457 65.299 1.00 19.39  ? 115 ARG J CZ  1 
ATOM   10887 N  NH1 . ARG J  1 116 ? 60.443  -32.621 64.450 1.00 17.46  ? 115 ARG J NH1 1 
ATOM   10888 N  NH2 . ARG J  1 116 ? 59.622  -33.054 66.538 1.00 18.92  ? 115 ARG J NH2 1 
ATOM   10889 N  N   . THR J  1 117 ? 59.109  -35.661 58.223 1.00 18.73  ? 116 THR J N   1 
ATOM   10890 C  CA  . THR J  1 117 ? 59.222  -36.106 56.840 1.00 19.29  ? 116 THR J CA  1 
ATOM   10891 C  C   . THR J  1 117 ? 60.092  -37.351 56.729 1.00 20.05  ? 116 THR J C   1 
ATOM   10892 O  O   . THR J  1 117 ? 61.132  -37.463 57.383 1.00 22.85  ? 116 THR J O   1 
ATOM   10893 C  CB  . THR J  1 117 ? 59.769  -35.015 55.916 1.00 19.51  ? 116 THR J CB  1 
ATOM   10894 O  OG1 . THR J  1 117 ? 58.815  -33.963 55.948 1.00 23.06  ? 116 THR J OG1 1 
ATOM   10895 C  CG2 . THR J  1 117 ? 59.929  -35.473 54.484 1.00 19.74  ? 116 THR J CG2 1 
ATOM   10896 N  N   . LEU J  1 118 ? 59.651  -38.277 55.878 1.00 18.97  ? 117 LEU J N   1 
ATOM   10897 C  CA  . LEU J  1 118 ? 60.495  -39.394 55.502 1.00 18.16  ? 117 LEU J CA  1 
ATOM   10898 C  C   . LEU J  1 118 ? 61.064  -39.083 54.123 1.00 17.34  ? 117 LEU J C   1 
ATOM   10899 O  O   . LEU J  1 118 ? 60.330  -38.638 53.243 1.00 16.49  ? 117 LEU J O   1 
ATOM   10900 C  CB  . LEU J  1 118 ? 59.627  -40.656 55.496 1.00 16.70  ? 117 LEU J CB  1 
ATOM   10901 C  CG  . LEU J  1 118 ? 60.324  -41.931 55.051 1.00 14.82  ? 117 LEU J CG  1 
ATOM   10902 C  CD1 . LEU J  1 118 ? 61.376  -42.308 56.071 1.00 14.39  ? 117 LEU J CD1 1 
ATOM   10903 C  CD2 . LEU J  1 118 ? 59.310  -43.060 54.874 1.00 13.79  ? 117 LEU J CD2 1 
ATOM   10904 N  N   . VAL J  1 119 ? 62.372  -39.302 53.957 1.00 16.69  ? 118 VAL J N   1 
ATOM   10905 C  CA  . VAL J  1 119 ? 63.050  -38.979 52.707 1.00 16.61  ? 118 VAL J CA  1 
ATOM   10906 C  C   . VAL J  1 119 ? 63.848  -40.187 52.235 1.00 16.41  ? 118 VAL J C   1 
ATOM   10907 O  O   . VAL J  1 119 ? 64.571  -40.809 53.009 1.00 15.79  ? 118 VAL J O   1 
ATOM   10908 C  CB  . VAL J  1 119 ? 63.994  -37.762 52.846 1.00 16.60  ? 118 VAL J CB  1 
ATOM   10909 C  CG1 . VAL J  1 119 ? 64.670  -37.425 51.528 1.00 15.95  ? 118 VAL J CG1 1 
ATOM   10910 C  CG2 . VAL J  1 119 ? 63.310  -36.542 53.427 1.00 16.95  ? 118 VAL J CG2 1 
ATOM   10911 N  N   . VAL J  1 120 ? 63.746  -40.466 50.936 1.00 16.68  ? 119 VAL J N   1 
ATOM   10912 C  CA  . VAL J  1 120 ? 64.625  -41.436 50.316 1.00 17.94  ? 119 VAL J CA  1 
ATOM   10913 C  C   . VAL J  1 120 ? 65.603  -40.673 49.426 1.00 20.23  ? 119 VAL J C   1 
ATOM   10914 O  O   . VAL J  1 120 ? 65.189  -39.866 48.589 1.00 20.47  ? 119 VAL J O   1 
ATOM   10915 C  CB  . VAL J  1 120 ? 63.834  -42.520 49.565 1.00 17.45  ? 119 VAL J CB  1 
ATOM   10916 C  CG1 . VAL J  1 120 ? 62.939  -41.952 48.475 1.00 17.88  ? 119 VAL J CG1 1 
ATOM   10917 C  CG2 . VAL J  1 120 ? 64.742  -43.596 49.010 1.00 16.97  ? 119 VAL J CG2 1 
ATOM   10918 N  N   . HIS J  1 121 ? 66.901  -40.955 49.621 1.00 22.31  ? 120 HIS J N   1 
ATOM   10919 C  CA  . HIS J  1 121 ? 67.984  -40.170 49.047 1.00 22.87  ? 120 HIS J CA  1 
ATOM   10920 C  C   . HIS J  1 121 ? 68.563  -40.805 47.783 1.00 24.54  ? 120 HIS J C   1 
ATOM   10921 O  O   . HIS J  1 121 ? 68.267  -41.949 47.443 1.00 25.23  ? 120 HIS J O   1 
ATOM   10922 C  CB  . HIS J  1 121 ? 69.080  -39.961 50.087 1.00 22.69  ? 120 HIS J CB  1 
ATOM   10923 C  CG  . HIS J  1 121 ? 68.711  -38.995 51.154 1.00 23.86  ? 120 HIS J CG  1 
ATOM   10924 N  ND1 . HIS J  1 121 ? 69.015  -37.652 51.060 1.00 23.53  ? 120 HIS J ND1 1 
ATOM   10925 C  CD2 . HIS J  1 121 ? 68.087  -39.170 52.343 1.00 24.51  ? 120 HIS J CD2 1 
ATOM   10926 C  CE1 . HIS J  1 121 ? 68.587  -37.038 52.150 1.00 25.03  ? 120 HIS J CE1 1 
ATOM   10927 N  NE2 . HIS J  1 121 ? 68.019  -37.949 52.957 1.00 25.02  ? 120 HIS J NE2 1 
ATOM   10928 N  N   . GLU J  1 122 ? 69.452  -40.049 47.137 1.00 26.69  ? 121 GLU J N   1 
ATOM   10929 C  CA  . GLU J  1 122 ? 69.958  -40.325 45.805 1.00 28.65  ? 121 GLU J CA  1 
ATOM   10930 C  C   . GLU J  1 122 ? 70.952  -41.483 45.813 1.00 27.48  ? 121 GLU J C   1 
ATOM   10931 O  O   . GLU J  1 122 ? 70.901  -42.324 44.923 1.00 25.46  ? 121 GLU J O   1 
ATOM   10932 C  CB  . GLU J  1 122 ? 70.565  -39.030 45.281 1.00 31.57  ? 121 GLU J CB  1 
ATOM   10933 C  CG  . GLU J  1 122 ? 71.560  -39.200 44.161 1.00 35.85  ? 121 GLU J CG  1 
ATOM   10934 C  CD  . GLU J  1 122 ? 72.381  -37.936 43.977 1.00 38.25  ? 121 GLU J CD  1 
ATOM   10935 O  OE1 . GLU J  1 122 ? 72.645  -37.585 42.801 1.00 42.78  ? 121 GLU J OE1 1 
ATOM   10936 O  OE2 . GLU J  1 122 ? 72.688  -37.261 45.002 1.00 36.22  ? 121 GLU J OE2 1 
ATOM   10937 N  N   . LYS J  1 123 ? 71.828  -41.522 46.828 1.00 29.91  ? 122 LYS J N   1 
ATOM   10938 C  CA  . LYS J  1 123 ? 72.958  -42.445 46.921 1.00 29.54  ? 122 LYS J CA  1 
ATOM   10939 C  C   . LYS J  1 123 ? 72.912  -43.205 48.247 1.00 26.18  ? 122 LYS J C   1 
ATOM   10940 O  O   . LYS J  1 123 ? 72.044  -42.972 49.086 1.00 26.55  ? 122 LYS J O   1 
ATOM   10941 C  CB  . LYS J  1 123 ? 74.278  -41.662 46.910 1.00 34.40  ? 122 LYS J CB  1 
ATOM   10942 C  CG  . LYS J  1 123 ? 74.579  -40.890 45.622 1.00 40.88  ? 122 LYS J CG  1 
ATOM   10943 C  CD  . LYS J  1 123 ? 75.883  -40.125 45.568 1.00 43.05  ? 122 LYS J CD  1 
ATOM   10944 C  CE  . LYS J  1 123 ? 75.936  -38.921 46.485 1.00 45.06  ? 122 LYS J CE  1 
ATOM   10945 N  NZ  . LYS J  1 123 ? 77.197  -38.159 46.370 1.00 46.55  ? 122 LYS J NZ  1 
ATOM   10946 N  N   . ALA J  1 124 ? 73.893  -44.087 48.448 1.00 24.66  ? 123 ALA J N   1 
ATOM   10947 C  CA  . ALA J  1 124 ? 74.025  -44.852 49.680 1.00 22.68  ? 123 ALA J CA  1 
ATOM   10948 C  C   . ALA J  1 124 ? 74.322  -43.921 50.844 1.00 21.38  ? 123 ALA J C   1 
ATOM   10949 O  O   . ALA J  1 124 ? 75.018  -42.920 50.687 1.00 19.54  ? 123 ALA J O   1 
ATOM   10950 C  CB  . ALA J  1 124 ? 75.122  -45.870 49.533 1.00 22.48  ? 123 ALA J CB  1 
ATOM   10951 N  N   . ASP J  1 125 ? 73.785  -44.276 52.014 1.00 21.44  ? 124 ASP J N   1 
ATOM   10952 C  CA  . ASP J  1 125 ? 74.168  -43.653 53.265 1.00 20.21  ? 124 ASP J CA  1 
ATOM   10953 C  C   . ASP J  1 125 ? 75.401  -44.395 53.769 1.00 19.67  ? 124 ASP J C   1 
ATOM   10954 O  O   . ASP J  1 125 ? 75.354  -45.605 53.963 1.00 21.57  ? 124 ASP J O   1 
ATOM   10955 C  CB  . ASP J  1 125 ? 72.994  -43.711 54.239 1.00 20.12  ? 124 ASP J CB  1 
ATOM   10956 C  CG  . ASP J  1 125 ? 73.298  -43.234 55.653 1.00 21.19  ? 124 ASP J CG  1 
ATOM   10957 O  OD1 . ASP J  1 125 ? 74.469  -42.930 55.947 1.00 21.28  ? 124 ASP J OD1 1 
ATOM   10958 O  OD2 . ASP J  1 125 ? 72.356  -43.199 56.469 1.00 20.81  ? 124 ASP J OD2 1 
ATOM   10959 N  N   . ASP J  1 126 ? 76.506  -43.677 53.997 1.00 19.01  ? 125 ASP J N   1 
ATOM   10960 C  CA  . ASP J  1 126 ? 77.752  -44.322 54.384 1.00 20.06  ? 125 ASP J CA  1 
ATOM   10961 C  C   . ASP J  1 126 ? 77.767  -44.632 55.884 1.00 20.95  ? 125 ASP J C   1 
ATOM   10962 O  O   . ASP J  1 126 ? 78.770  -45.079 56.405 1.00 22.61  ? 125 ASP J O   1 
ATOM   10963 C  CB  . ASP J  1 126 ? 78.983  -43.567 53.863 1.00 21.01  ? 125 ASP J CB  1 
ATOM   10964 C  CG  . ASP J  1 126 ? 79.283  -42.246 54.567 1.00 23.11  ? 125 ASP J CG  1 
ATOM   10965 O  OD1 . ASP J  1 126 ? 78.838  -42.057 55.737 1.00 20.05  ? 125 ASP J OD1 1 
ATOM   10966 O  OD2 . ASP J  1 126 ? 79.985  -41.411 53.940 1.00 26.35  ? 125 ASP J OD2 1 
ATOM   10967 N  N   . LEU J  1 127 ? 76.646  -44.397 56.566 1.00 20.83  ? 126 LEU J N   1 
ATOM   10968 C  CA  . LEU J  1 127 ? 76.453  -44.749 57.967 1.00 21.17  ? 126 LEU J CA  1 
ATOM   10969 C  C   . LEU J  1 127 ? 77.493  -44.068 58.848 1.00 22.84  ? 126 LEU J C   1 
ATOM   10970 O  O   . LEU J  1 127 ? 77.763  -44.536 59.948 1.00 22.70  ? 126 LEU J O   1 
ATOM   10971 C  CB  . LEU J  1 127 ? 76.477  -46.273 58.144 1.00 19.58  ? 126 LEU J CB  1 
ATOM   10972 C  CG  . LEU J  1 127 ? 75.614  -47.093 57.183 1.00 18.67  ? 126 LEU J CG  1 
ATOM   10973 C  CD1 . LEU J  1 127 ? 75.602  -48.566 57.570 1.00 17.87  ? 126 LEU J CD1 1 
ATOM   10974 C  CD2 . LEU J  1 127 ? 74.195  -46.592 57.171 1.00 18.08  ? 126 LEU J CD2 1 
ATOM   10975 N  N   . GLY J  1 128 ? 78.067  -42.962 58.356 1.00 26.36  ? 127 GLY J N   1 
ATOM   10976 C  CA  . GLY J  1 128 ? 78.927  -42.093 59.148 1.00 28.16  ? 127 GLY J CA  1 
ATOM   10977 C  C   . GLY J  1 128 ? 80.384  -42.561 59.166 1.00 29.04  ? 127 GLY J C   1 
ATOM   10978 O  O   . GLY J  1 128 ? 81.163  -42.131 60.015 1.00 29.33  ? 127 GLY J O   1 
ATOM   10979 N  N   . LYS J  1 129 ? 80.744  -43.424 58.210 1.00 28.46  ? 128 LYS J N   1 
ATOM   10980 C  CA  . LYS J  1 129 ? 82.049  -44.054 58.184 1.00 29.05  ? 128 LYS J CA  1 
ATOM   10981 C  C   . LYS J  1 129 ? 82.827  -43.605 56.953 1.00 29.91  ? 128 LYS J C   1 
ATOM   10982 O  O   . LYS J  1 129 ? 83.679  -44.351 56.483 1.00 27.21  ? 128 LYS J O   1 
ATOM   10983 C  CB  . LYS J  1 129 ? 81.901  -45.577 58.183 1.00 26.57  ? 128 LYS J CB  1 
ATOM   10984 C  CG  . LYS J  1 129 ? 81.045  -46.139 59.300 1.00 27.51  ? 128 LYS J CG  1 
ATOM   10985 C  CD  . LYS J  1 129 ? 81.339  -47.576 59.660 1.00 32.29  ? 128 LYS J CD  1 
ATOM   10986 C  CE  . LYS J  1 129 ? 81.258  -47.855 61.152 1.00 35.08  ? 128 LYS J CE  1 
ATOM   10987 N  NZ  . LYS J  1 129 ? 80.104  -47.168 61.799 1.00 32.72  ? 128 LYS J NZ  1 
ATOM   10988 N  N   . GLY J  1 130 ? 82.556  -42.378 56.482 1.00 34.26  ? 129 GLY J N   1 
ATOM   10989 C  CA  . GLY J  1 130 ? 83.134  -41.884 55.247 1.00 39.72  ? 129 GLY J CA  1 
ATOM   10990 C  C   . GLY J  1 130 ? 84.369  -41.013 55.489 1.00 42.76  ? 129 GLY J C   1 
ATOM   10991 O  O   . GLY J  1 130 ? 85.079  -40.677 54.530 1.00 50.26  ? 129 GLY J O   1 
ATOM   10992 N  N   . GLY J  1 131 ? 84.602  -40.652 56.765 1.00 35.93  ? 130 GLY J N   1 
ATOM   10993 C  CA  . GLY J  1 131 ? 85.806  -39.948 57.166 1.00 38.31  ? 130 GLY J CA  1 
ATOM   10994 C  C   . GLY J  1 131 ? 85.877  -38.502 56.657 1.00 40.18  ? 130 GLY J C   1 
ATOM   10995 O  O   . GLY J  1 131 ? 86.956  -37.936 56.576 1.00 39.85  ? 130 GLY J O   1 
ATOM   10996 N  N   . ASN J  1 132 ? 84.724  -37.905 56.329 1.00 39.68  ? 131 ASN J N   1 
ATOM   10997 C  CA  . ASN J  1 132 ? 84.654  -36.479 56.088 1.00 36.80  ? 131 ASN J CA  1 
ATOM   10998 C  C   . ASN J  1 132 ? 83.551  -35.867 56.946 1.00 38.92  ? 131 ASN J C   1 
ATOM   10999 O  O   . ASN J  1 132 ? 82.832  -36.576 57.646 1.00 41.37  ? 131 ASN J O   1 
ATOM   11000 C  CB  . ASN J  1 132 ? 84.557  -36.154 54.600 1.00 36.30  ? 131 ASN J CB  1 
ATOM   11001 C  CG  . ASN J  1 132 ? 83.339  -36.723 53.904 1.00 36.83  ? 131 ASN J CG  1 
ATOM   11002 O  OD1 . ASN J  1 132 ? 82.360  -37.105 54.534 1.00 36.74  ? 131 ASN J OD1 1 
ATOM   11003 N  ND2 . ASN J  1 132 ? 83.373  -36.732 52.594 1.00 38.72  ? 131 ASN J ND2 1 
ATOM   11004 N  N   . GLU J  1 133 ? 83.434  -34.538 56.888 1.00 41.43  ? 132 GLU J N   1 
ATOM   11005 C  CA  . GLU J  1 133 ? 82.529  -33.844 57.784 1.00 41.68  ? 132 GLU J CA  1 
ATOM   11006 C  C   . GLU J  1 133 ? 81.097  -34.171 57.377 1.00 39.68  ? 132 GLU J C   1 
ATOM   11007 O  O   . GLU J  1 133 ? 80.238  -34.379 58.231 1.00 37.59  ? 132 GLU J O   1 
ATOM   11008 C  CB  . GLU J  1 133 ? 82.842  -32.353 57.792 1.00 47.77  ? 132 GLU J CB  1 
ATOM   11009 C  CG  . GLU J  1 133 ? 82.051  -31.583 58.836 1.00 54.49  ? 132 GLU J CG  1 
ATOM   11010 C  CD  . GLU J  1 133 ? 82.047  -30.077 58.613 1.00 59.17  ? 132 GLU J CD  1 
ATOM   11011 O  OE1 . GLU J  1 133 ? 83.124  -29.541 58.298 1.00 63.53  ? 132 GLU J OE1 1 
ATOM   11012 O  OE2 . GLU J  1 133 ? 80.975  -29.417 58.766 1.00 65.25  ? 132 GLU J OE2 1 
ATOM   11013 N  N   . GLU J  1 134 ? 80.894  -34.255 56.068 1.00 39.26  ? 133 GLU J N   1 
ATOM   11014 C  CA  . GLU J  1 134 ? 79.617  -34.571 55.457 1.00 39.69  ? 133 GLU J CA  1 
ATOM   11015 C  C   . GLU J  1 134 ? 79.089  -35.905 56.002 1.00 39.15  ? 133 GLU J C   1 
ATOM   11016 O  O   . GLU J  1 134 ? 77.900  -36.038 56.310 1.00 36.75  ? 133 GLU J O   1 
ATOM   11017 C  CB  . GLU J  1 134 ? 79.764  -34.598 53.928 1.00 43.20  ? 133 GLU J CB  1 
ATOM   11018 C  CG  . GLU J  1 134 ? 78.782  -33.781 53.052 1.00 50.86  ? 133 GLU J CG  1 
ATOM   11019 C  CD  . GLU J  1 134 ? 77.483  -33.298 53.672 1.00 61.77  ? 133 GLU J CD  1 
ATOM   11020 O  OE1 . GLU J  1 134 ? 76.803  -34.134 54.233 1.00 73.42  ? 133 GLU J OE1 1 
ATOM   11021 O  OE2 . GLU J  1 134 ? 77.152  -32.077 53.565 1.00 70.17  ? 133 GLU J OE2 1 
ATOM   11022 N  N   . SER J  1 135 ? 79.986  -36.895 56.130 1.00 35.83  ? 134 SER J N   1 
ATOM   11023 C  CA  . SER J  1 135 ? 79.615  -38.226 56.574 1.00 34.23  ? 134 SER J CA  1 
ATOM   11024 C  C   . SER J  1 135 ? 78.906  -38.166 57.921 1.00 34.85  ? 134 SER J C   1 
ATOM   11025 O  O   . SER J  1 135 ? 77.936  -38.876 58.135 1.00 38.93  ? 134 SER J O   1 
ATOM   11026 C  CB  . SER J  1 135 ? 80.804  -39.156 56.615 1.00 32.70  ? 134 SER J CB  1 
ATOM   11027 O  OG  . SER J  1 135 ? 80.421  -40.484 56.969 1.00 32.10  ? 134 SER J OG  1 
ATOM   11028 N  N   . THR J  1 136 ? 79.381  -37.311 58.826 1.00 35.13  ? 135 THR J N   1 
ATOM   11029 C  CA  . THR J  1 136 ? 78.844  -37.318 60.179 1.00 34.67  ? 135 THR J CA  1 
ATOM   11030 C  C   . THR J  1 136 ? 77.600  -36.438 60.286 1.00 34.78  ? 135 THR J C   1 
ATOM   11031 O  O   . THR J  1 136 ? 77.044  -36.296 61.378 1.00 31.96  ? 135 THR J O   1 
ATOM   11032 C  CB  . THR J  1 136 ? 79.886  -36.903 61.221 1.00 34.30  ? 135 THR J CB  1 
ATOM   11033 O  OG1 . THR J  1 136 ? 80.194  -35.540 60.928 1.00 31.54  ? 135 THR J OG1 1 
ATOM   11034 C  CG2 . THR J  1 136 ? 81.126  -37.774 61.197 1.00 34.27  ? 135 THR J CG2 1 
ATOM   11035 N  N   . LYS J  1 137 ? 77.172  -35.854 59.158 1.00 36.30  ? 136 LYS J N   1 
ATOM   11036 C  CA  . LYS J  1 137 ? 75.953  -35.057 59.116 1.00 36.21  ? 136 LYS J CA  1 
ATOM   11037 C  C   . LYS J  1 137 ? 74.858  -35.793 58.346 1.00 34.26  ? 136 LYS J C   1 
ATOM   11038 O  O   . LYS J  1 137 ? 73.755  -35.995 58.865 1.00 33.97  ? 136 LYS J O   1 
ATOM   11039 C  CB  . LYS J  1 137 ? 76.212  -33.684 58.489 1.00 40.44  ? 136 LYS J CB  1 
ATOM   11040 C  CG  . LYS J  1 137 ? 76.853  -32.654 59.408 1.00 47.47  ? 136 LYS J CG  1 
ATOM   11041 C  CD  . LYS J  1 137 ? 77.178  -31.349 58.705 1.00 55.23  ? 136 LYS J CD  1 
ATOM   11042 C  CE  . LYS J  1 137 ? 77.312  -30.177 59.661 1.00 53.83  ? 136 LYS J CE  1 
ATOM   11043 N  NZ  . LYS J  1 137 ? 76.929  -28.892 59.026 1.00 51.72  ? 136 LYS J NZ  1 
ATOM   11044 N  N   . THR J  1 138 ? 75.174  -36.202 57.107 1.00 32.23  ? 137 THR J N   1 
ATOM   11045 C  CA  . THR J  1 138 ? 74.147  -36.688 56.193 1.00 29.72  ? 137 THR J CA  1 
ATOM   11046 C  C   . THR J  1 138 ? 74.462  -38.087 55.668 1.00 28.18  ? 137 THR J C   1 
ATOM   11047 O  O   . THR J  1 138 ? 73.694  -38.626 54.871 1.00 26.25  ? 137 THR J O   1 
ATOM   11048 C  CB  . THR J  1 138 ? 74.033  -35.756 54.985 1.00 29.63  ? 137 THR J CB  1 
ATOM   11049 O  OG1 . THR J  1 138 ? 75.190  -35.908 54.153 1.00 31.07  ? 137 THR J OG1 1 
ATOM   11050 C  CG2 . THR J  1 138 ? 73.845  -34.316 55.399 1.00 31.77  ? 137 THR J CG2 1 
ATOM   11051 N  N   . GLY J  1 139 ? 75.611  -38.645 56.080 1.00 25.49  ? 138 GLY J N   1 
ATOM   11052 C  CA  . GLY J  1 139 ? 76.078  -39.915 55.562 1.00 23.61  ? 138 GLY J CA  1 
ATOM   11053 C  C   . GLY J  1 139 ? 76.351  -39.890 54.053 1.00 22.81  ? 138 GLY J C   1 
ATOM   11054 O  O   . GLY J  1 139 ? 76.515  -40.942 53.441 1.00 21.09  ? 138 GLY J O   1 
ATOM   11055 N  N   . ASN J  1 140 ? 76.396  -38.693 53.456 1.00 21.78  ? 139 ASN J N   1 
ATOM   11056 C  CA  . ASN J  1 140 ? 76.809  -38.543 52.066 1.00 23.13  ? 139 ASN J CA  1 
ATOM   11057 C  C   . ASN J  1 140 ? 75.750  -39.131 51.134 1.00 23.30  ? 139 ASN J C   1 
ATOM   11058 O  O   . ASN J  1 140 ? 76.071  -39.536 50.016 1.00 22.18  ? 139 ASN J O   1 
ATOM   11059 C  CB  . ASN J  1 140 ? 78.191  -39.155 51.772 1.00 23.23  ? 139 ASN J CB  1 
ATOM   11060 C  CG  . ASN J  1 140 ? 79.350  -38.315 52.283 1.00 23.33  ? 139 ASN J CG  1 
ATOM   11061 O  OD1 . ASN J  1 140 ? 79.604  -37.229 51.777 1.00 23.32  ? 139 ASN J OD1 1 
ATOM   11062 N  ND2 . ASN J  1 140 ? 80.055  -38.788 53.300 1.00 22.51  ? 139 ASN J ND2 1 
ATOM   11063 N  N   . ALA J  1 141 ? 74.492  -39.145 51.590 1.00 23.80  ? 140 ALA J N   1 
ATOM   11064 C  CA  . ALA J  1 141 ? 73.422  -39.844 50.886 1.00 24.64  ? 140 ALA J CA  1 
ATOM   11065 C  C   . ALA J  1 141 ? 72.960  -39.070 49.642 1.00 25.72  ? 140 ALA J C   1 
ATOM   11066 O  O   . ALA J  1 141 ? 72.161  -39.566 48.841 1.00 24.55  ? 140 ALA J O   1 
ATOM   11067 C  CB  . ALA J  1 141 ? 72.282  -40.120 51.829 1.00 23.29  ? 140 ALA J CB  1 
ATOM   11068 N  N   . GLY J  1 142 ? 73.461  -37.846 49.487 1.00 27.29  ? 141 GLY J N   1 
ATOM   11069 C  CA  . GLY J  1 142 ? 73.127  -37.068 48.305 1.00 25.89  ? 141 GLY J CA  1 
ATOM   11070 C  C   . GLY J  1 142 ? 71.733  -36.466 48.405 1.00 24.80  ? 141 GLY J C   1 
ATOM   11071 O  O   . GLY J  1 142 ? 71.204  -36.307 49.507 1.00 24.53  ? 141 GLY J O   1 
ATOM   11072 N  N   . SER J  1 143 ? 71.147  -36.170 47.240 1.00 25.21  ? 142 SER J N   1 
ATOM   11073 C  CA  . SER J  1 143 ? 69.931  -35.372 47.159 1.00 24.39  ? 142 SER J CA  1 
ATOM   11074 C  C   . SER J  1 143 ? 68.714  -36.179 47.622 1.00 24.03  ? 142 SER J C   1 
ATOM   11075 O  O   . SER J  1 143 ? 68.804  -37.382 47.865 1.00 23.52  ? 142 SER J O   1 
ATOM   11076 C  CB  . SER J  1 143 ? 69.731  -34.826 45.768 1.00 24.54  ? 142 SER J CB  1 
ATOM   11077 O  OG  . SER J  1 143 ? 69.512  -35.881 44.839 1.00 26.76  ? 142 SER J OG  1 
ATOM   11078 N  N   . ARG J  1 144 ? 67.580  -35.481 47.726 1.00 22.32  ? 143 ARG J N   1 
ATOM   11079 C  CA  . ARG J  1 144 ? 66.322  -36.007 48.220 1.00 21.95  ? 143 ARG J CA  1 
ATOM   11080 C  C   . ARG J  1 144 ? 65.447  -36.368 47.023 1.00 22.95  ? 143 ARG J C   1 
ATOM   11081 O  O   . ARG J  1 144 ? 64.964  -35.492 46.326 1.00 25.12  ? 143 ARG J O   1 
ATOM   11082 C  CB  . ARG J  1 144 ? 65.675  -34.952 49.122 1.00 21.00  ? 143 ARG J CB  1 
ATOM   11083 C  CG  . ARG J  1 144 ? 66.556  -34.512 50.279 1.00 20.24  ? 143 ARG J CG  1 
ATOM   11084 C  CD  . ARG J  1 144 ? 66.108  -33.305 51.046 1.00 19.91  ? 143 ARG J CD  1 
ATOM   11085 N  NE  . ARG J  1 144 ? 67.057  -32.930 52.087 1.00 20.70  ? 143 ARG J NE  1 
ATOM   11086 C  CZ  . ARG J  1 144 ? 66.750  -32.286 53.216 1.00 20.90  ? 143 ARG J CZ  1 
ATOM   11087 N  NH1 . ARG J  1 144 ? 65.505  -31.938 53.489 1.00 20.42  ? 143 ARG J NH1 1 
ATOM   11088 N  NH2 . ARG J  1 144 ? 67.693  -31.993 54.090 1.00 23.19  ? 143 ARG J NH2 1 
ATOM   11089 N  N   . LEU J  1 145 ? 65.270  -37.664 46.762 1.00 23.33  ? 144 LEU J N   1 
ATOM   11090 C  CA  . LEU J  1 145 ? 64.606  -38.080 45.539 1.00 21.64  ? 144 LEU J CA  1 
ATOM   11091 C  C   . LEU J  1 145 ? 63.095  -37.966 45.711 1.00 22.35  ? 144 LEU J C   1 
ATOM   11092 O  O   . LEU J  1 145 ? 62.383  -37.592 44.781 1.00 23.70  ? 144 LEU J O   1 
ATOM   11093 C  CB  . LEU J  1 145 ? 65.022  -39.515 45.211 1.00 23.23  ? 144 LEU J CB  1 
ATOM   11094 C  CG  . LEU J  1 145 ? 66.459  -39.679 44.721 1.00 25.40  ? 144 LEU J CG  1 
ATOM   11095 C  CD1 . LEU J  1 145 ? 66.730  -41.126 44.334 1.00 25.72  ? 144 LEU J CD1 1 
ATOM   11096 C  CD2 . LEU J  1 145 ? 66.757  -38.733 43.558 1.00 24.88  ? 144 LEU J CD2 1 
ATOM   11097 N  N   . ALA J  1 146 ? 62.618  -38.302 46.911 1.00 21.55  ? 145 ALA J N   1 
ATOM   11098 C  CA  . ALA J  1 146 ? 61.194  -38.304 47.213 1.00 21.68  ? 145 ALA J CA  1 
ATOM   11099 C  C   . ALA J  1 146 ? 60.997  -38.258 48.723 1.00 23.08  ? 145 ALA J C   1 
ATOM   11100 O  O   . ALA J  1 146 ? 61.856  -38.698 49.499 1.00 25.00  ? 145 ALA J O   1 
ATOM   11101 C  CB  . ALA J  1 146 ? 60.503  -39.501 46.611 1.00 21.30  ? 145 ALA J CB  1 
ATOM   11102 N  N   . CYS J  1 147 ? 59.886  -37.636 49.133 1.00 22.99  ? 146 CYS J N   1 
ATOM   11103 C  CA  . CYS J  1 147 ? 59.601  -37.480 50.548 1.00 23.32  ? 146 CYS J CA  1 
ATOM   11104 C  C   . CYS J  1 147 ? 58.094  -37.383 50.731 1.00 23.10  ? 146 CYS J C   1 
ATOM   11105 O  O   . CYS J  1 147 ? 57.359  -37.301 49.748 1.00 23.08  ? 146 CYS J O   1 
ATOM   11106 C  CB  . CYS J  1 147 ? 60.290  -36.251 51.126 1.00 24.11  ? 146 CYS J CB  1 
ATOM   11107 S  SG  . CYS J  1 147 ? 59.845  -34.732 50.266 1.00 26.57  ? 146 CYS J SG  1 
ATOM   11108 N  N   . GLY J  1 148 ? 57.669  -37.417 51.998 1.00 23.18  ? 147 GLY J N   1 
ATOM   11109 C  CA  . GLY J  1 148 ? 56.283  -37.215 52.378 1.00 22.61  ? 147 GLY J CA  1 
ATOM   11110 C  C   . GLY J  1 148 ? 56.183  -36.894 53.873 1.00 23.61  ? 147 GLY J C   1 
ATOM   11111 O  O   . GLY J  1 148 ? 57.088  -37.200 54.658 1.00 23.74  ? 147 GLY J O   1 
ATOM   11112 N  N   . VAL J  1 149 ? 55.071  -36.264 54.265 1.00 21.81  ? 148 VAL J N   1 
ATOM   11113 C  CA  . VAL J  1 149 ? 54.838  -36.052 55.678 1.00 19.73  ? 148 VAL J CA  1 
ATOM   11114 C  C   . VAL J  1 149 ? 54.280  -37.339 56.283 1.00 19.43  ? 148 VAL J C   1 
ATOM   11115 O  O   . VAL J  1 149 ? 53.501  -38.057 55.652 1.00 18.60  ? 148 VAL J O   1 
ATOM   11116 C  CB  . VAL J  1 149 ? 53.949  -34.821 55.925 1.00 19.27  ? 148 VAL J CB  1 
ATOM   11117 C  CG1 . VAL J  1 149 ? 53.800  -34.531 57.416 1.00 19.39  ? 148 VAL J CG1 1 
ATOM   11118 C  CG2 . VAL J  1 149 ? 54.522  -33.611 55.205 1.00 17.65  ? 148 VAL J CG2 1 
ATOM   11119 N  N   . ILE J  1 150 ? 54.736  -37.640 57.498 1.00 19.29  ? 149 ILE J N   1 
ATOM   11120 C  CA  . ILE J  1 150 ? 54.376  -38.861 58.193 1.00 19.83  ? 149 ILE J CA  1 
ATOM   11121 C  C   . ILE J  1 150 ? 53.083  -38.600 58.950 1.00 20.37  ? 149 ILE J C   1 
ATOM   11122 O  O   . ILE J  1 150 ? 53.080  -37.814 59.896 1.00 22.79  ? 149 ILE J O   1 
ATOM   11123 C  CB  . ILE J  1 150 ? 55.520  -39.271 59.142 1.00 18.66  ? 149 ILE J CB  1 
ATOM   11124 C  CG1 . ILE J  1 150 ? 56.799  -39.614 58.372 1.00 18.21  ? 149 ILE J CG1 1 
ATOM   11125 C  CG2 . ILE J  1 150 ? 55.087  -40.404 60.068 1.00 18.33  ? 149 ILE J CG2 1 
ATOM   11126 C  CD1 . ILE J  1 150 ? 58.024  -39.646 59.243 1.00 18.78  ? 149 ILE J CD1 1 
ATOM   11127 N  N   . GLY J  1 151 ? 52.013  -39.298 58.547 1.00 18.97  ? 150 GLY J N   1 
ATOM   11128 C  CA  . GLY J  1 151 ? 50.674  -39.004 59.036 1.00 20.02  ? 150 GLY J CA  1 
ATOM   11129 C  C   . GLY J  1 151 ? 49.996  -40.202 59.700 1.00 22.00  ? 150 GLY J C   1 
ATOM   11130 O  O   . GLY J  1 151 ? 50.418  -41.347 59.511 1.00 25.11  ? 150 GLY J O   1 
ATOM   11131 N  N   . ILE J  1 152 ? 48.928  -39.923 60.460 1.00 20.77  ? 151 ILE J N   1 
ATOM   11132 C  CA  . ILE J  1 152 ? 48.198  -40.939 61.205 1.00 22.32  ? 151 ILE J CA  1 
ATOM   11133 C  C   . ILE J  1 152 ? 47.354  -41.735 60.209 1.00 24.25  ? 151 ILE J C   1 
ATOM   11134 O  O   . ILE J  1 152 ? 46.694  -41.140 59.354 1.00 27.01  ? 151 ILE J O   1 
ATOM   11135 C  CB  . ILE J  1 152 ? 47.318  -40.258 62.268 1.00 21.21  ? 151 ILE J CB  1 
ATOM   11136 C  CG1 . ILE J  1 152 ? 48.171  -39.521 63.310 1.00 21.85  ? 151 ILE J CG1 1 
ATOM   11137 C  CG2 . ILE J  1 152 ? 46.357  -41.268 62.887 1.00 20.16  ? 151 ILE J CG2 1 
ATOM   11138 C  CD1 . ILE J  1 152 ? 47.362  -38.462 64.048 1.00 21.04  ? 151 ILE J CD1 1 
ATOM   11139 N  N   . ALA J  1 153 ? 47.471  -43.067 60.225 1.00 26.23  ? 152 ALA J N   1 
ATOM   11140 C  CA  . ALA J  1 153 ? 46.752  -43.898 59.226 1.00 26.44  ? 152 ALA J CA  1 
ATOM   11141 C  C   . ALA J  1 153 ? 45.571  -44.628 59.870 1.00 27.41  ? 152 ALA J C   1 
ATOM   11142 O  O   . ALA J  1 153 ? 45.463  -44.592 61.112 1.00 31.38  ? 152 ALA J O   1 
ATOM   11143 C  CB  . ALA J  1 153 ? 47.713  -44.866 58.580 1.00 25.15  ? 152 ALA J CB  1 
ATOM   11144 N  N   . GLN J  1 154 ? 44.719  -45.266 59.055 1.00 47.83  ? 153 GLN J N   1 
ATOM   11145 C  CA  . GLN J  1 154 ? 43.555  -45.999 59.653 1.00 56.19  ? 153 GLN J CA  1 
ATOM   11146 C  C   . GLN J  1 154 ? 43.963  -47.444 59.949 1.00 60.54  ? 153 GLN J C   1 
ATOM   11147 O  O   . GLN J  1 154 ? 44.393  -48.128 59.017 1.00 62.65  ? 153 GLN J O   1 
ATOM   11148 C  CB  . GLN J  1 154 ? 42.432  -45.988 58.631 1.00 55.03  ? 153 GLN J CB  1 
ATOM   11149 C  CG  . GLN J  1 154 ? 42.618  -44.839 57.647 1.00 59.95  ? 153 GLN J CG  1 
ATOM   11150 C  CD  . GLN J  1 154 ? 42.476  -45.231 56.197 1.00 58.71  ? 153 GLN J CD  1 
ATOM   11151 O  OE1 . GLN J  1 154 ? 41.497  -44.901 55.522 1.00 55.78  ? 153 GLN J OE1 1 
ATOM   11152 N  NE2 . GLN J  1 154 ? 43.481  -45.937 55.710 1.00 56.95  ? 153 GLN J NE2 1 
ATOM   11153 O  OXT . GLN J  1 154 ? 43.882  -47.930 61.079 1.00 60.60  ? 153 GLN J OXT 1 
ATOM   11154 N  N   . ALA K  1 2   ? 1.257   -57.763 5.581  1.00 43.12  ? 1   ALA K N   1 
ATOM   11155 C  CA  . ALA K  1 2   ? 2.394   -57.000 5.010  1.00 44.14  ? 1   ALA K CA  1 
ATOM   11156 C  C   . ALA K  1 2   ? 2.410   -55.539 5.452  1.00 44.35  ? 1   ALA K C   1 
ATOM   11157 O  O   . ALA K  1 2   ? 3.464   -54.976 5.726  1.00 47.95  ? 1   ALA K O   1 
ATOM   11158 C  CB  . ALA K  1 2   ? 2.452   -57.119 3.519  1.00 51.33  ? 1   ALA K CB  1 
ATOM   11159 N  N   . THR K  1 3   ? 1.235   -54.945 5.645  1.00 42.85  ? 2   THR K N   1 
ATOM   11160 C  CA  . THR K  1 3   ? 1.079   -53.704 6.402  1.00 42.79  ? 2   THR K CA  1 
ATOM   11161 C  C   . THR K  1 3   ? 0.528   -54.028 7.791  1.00 40.49  ? 2   THR K C   1 
ATOM   11162 O  O   . THR K  1 3   ? -0.532  -54.601 7.902  1.00 42.62  ? 2   THR K O   1 
ATOM   11163 C  CB  . THR K  1 3   ? 0.213   -52.723 5.607  1.00 43.22  ? 2   THR K CB  1 
ATOM   11164 O  OG1 . THR K  1 3   ? 0.596   -52.598 4.243  1.00 56.64  ? 2   THR K OG1 1 
ATOM   11165 C  CG2 . THR K  1 3   ? 0.051   -51.352 6.228  1.00 42.75  ? 2   THR K CG2 1 
ATOM   11166 N  N   . LYS K  1 4   ? 1.256   -53.636 8.848  1.00 39.52  ? 3   LYS K N   1 
ATOM   11167 C  CA  . LYS K  1 4   ? 0.815   -53.797 10.224 1.00 36.52  ? 3   LYS K CA  1 
ATOM   11168 C  C   . LYS K  1 4   ? 0.590   -52.420 10.841 1.00 34.56  ? 3   LYS K C   1 
ATOM   11169 O  O   . LYS K  1 4   ? 1.424   -51.519 10.726 1.00 36.98  ? 3   LYS K O   1 
ATOM   11170 C  CB  . LYS K  1 4   ? 1.824   -54.564 11.086 1.00 34.66  ? 3   LYS K CB  1 
ATOM   11171 C  CG  . LYS K  1 4   ? 1.741   -56.086 11.030 0.40 34.23  ? 3   LYS K CG  1 
ATOM   11172 C  CD  . LYS K  1 4   ? 2.781   -56.793 11.872 0.40 33.81  ? 3   LYS K CD  1 
ATOM   11173 C  CE  . LYS K  1 4   ? 3.301   -58.068 11.242 0.40 33.46  ? 3   LYS K CE  1 
ATOM   11174 N  NZ  . LYS K  1 4   ? 4.422   -58.615 12.037 0.40 33.12  ? 3   LYS K NZ  1 
ATOM   11175 N  N   . VAL K  1 5   ? -0.524  -52.304 11.556 1.00 32.06  ? 4   VAL K N   1 
ATOM   11176 C  CA  . VAL K  1 5   ? -0.927  -51.073 12.205 1.00 29.64  ? 4   VAL K CA  1 
ATOM   11177 C  C   . VAL K  1 5   ? -1.369  -51.429 13.621 1.00 28.56  ? 4   VAL K C   1 
ATOM   11178 O  O   . VAL K  1 5   ? -1.758  -52.563 13.904 1.00 28.09  ? 4   VAL K O   1 
ATOM   11179 C  CB  . VAL K  1 5   ? -2.051  -50.419 11.393 1.00 29.60  ? 4   VAL K CB  1 
ATOM   11180 C  CG1 . VAL K  1 5   ? -2.749  -49.327 12.160 1.00 33.12  ? 4   VAL K CG1 1 
ATOM   11181 C  CG2 . VAL K  1 5   ? -1.532  -49.879 10.074 1.00 27.37  ? 4   VAL K CG2 1 
ATOM   11182 N  N   . VAL K  1 6   ? -1.276  -50.463 14.530 1.00 28.07  ? 5   VAL K N   1 
ATOM   11183 C  CA  . VAL K  1 6   ? -1.640  -50.762 15.902 1.00 28.47  ? 5   VAL K CA  1 
ATOM   11184 C  C   . VAL K  1 6   ? -2.336  -49.556 16.524 1.00 27.92  ? 5   VAL K C   1 
ATOM   11185 O  O   . VAL K  1 6   ? -2.234  -48.432 16.045 1.00 26.97  ? 5   VAL K O   1 
ATOM   11186 C  CB  . VAL K  1 6   ? -0.417  -51.215 16.724 1.00 28.33  ? 5   VAL K CB  1 
ATOM   11187 C  CG1 . VAL K  1 6   ? 0.533   -50.056 16.989 1.00 26.93  ? 5   VAL K CG1 1 
ATOM   11188 C  CG2 . VAL K  1 6   ? -0.842  -51.878 18.023 1.00 28.46  ? 5   VAL K CG2 1 
ATOM   11189 N  N   . CYS K  1 7   ? -3.040  -49.820 17.619 1.00 28.20  ? 6   CYS K N   1 
ATOM   11190 C  CA  . CYS K  1 7   ? -3.762  -48.772 18.299 1.00 29.74  ? 6   CYS K CA  1 
ATOM   11191 C  C   . CYS K  1 7   ? -3.832  -49.124 19.775 1.00 28.99  ? 6   CYS K C   1 
ATOM   11192 O  O   . CYS K  1 7   ? -4.229  -50.230 20.117 1.00 30.93  ? 6   CYS K O   1 
ATOM   11193 C  CB  . CYS K  1 7   ? -5.160  -48.695 17.711 1.00 31.64  ? 6   CYS K CB  1 
ATOM   11194 S  SG  . CYS K  1 7   ? -6.157  -47.374 18.428 1.00 35.95  ? 6   CYS K SG  1 
ATOM   11195 N  N   . VAL K  1 8   ? -3.441  -48.176 20.628 1.00 27.36  ? 7   VAL K N   1 
ATOM   11196 C  CA  . VAL K  1 8   ? -3.581  -48.343 22.061 1.00 26.87  ? 7   VAL K CA  1 
ATOM   11197 C  C   . VAL K  1 8   ? -4.797  -47.543 22.504 1.00 28.68  ? 7   VAL K C   1 
ATOM   11198 O  O   . VAL K  1 8   ? -4.832  -46.335 22.312 1.00 34.69  ? 7   VAL K O   1 
ATOM   11199 C  CB  . VAL K  1 8   ? -2.318  -47.888 22.814 1.00 25.72  ? 7   VAL K CB  1 
ATOM   11200 C  CG1 . VAL K  1 8   ? -2.513  -47.891 24.323 1.00 24.35  ? 7   VAL K CG1 1 
ATOM   11201 C  CG2 . VAL K  1 8   ? -1.108  -48.723 22.432 1.00 23.47  ? 7   VAL K CG2 1 
ATOM   11202 N  N   . LEU K  1 9   ? -5.780  -48.215 23.114 1.00 29.84  ? 8   LEU K N   1 
ATOM   11203 C  CA  . LEU K  1 9   ? -6.971  -47.525 23.575 1.00 32.31  ? 8   LEU K CA  1 
ATOM   11204 C  C   . LEU K  1 9   ? -6.786  -47.106 25.030 1.00 34.00  ? 8   LEU K C   1 
ATOM   11205 O  O   . LEU K  1 9   ? -6.461  -47.940 25.862 1.00 34.26  ? 8   LEU K O   1 
ATOM   11206 C  CB  . LEU K  1 9   ? -8.176  -48.452 23.434 1.00 31.86  ? 8   LEU K CB  1 
ATOM   11207 C  CG  . LEU K  1 9   ? -8.448  -48.997 22.032 1.00 31.80  ? 8   LEU K CG  1 
ATOM   11208 C  CD1 . LEU K  1 9   ? -9.453  -50.139 22.104 1.00 32.71  ? 8   LEU K CD1 1 
ATOM   11209 C  CD2 . LEU K  1 9   ? -8.963  -47.913 21.106 1.00 30.45  ? 8   LEU K CD2 1 
ATOM   11210 N  N   . LYS K  1 10  ? -6.977  -45.807 25.306 1.00 35.85  ? 9   LYS K N   1 
ATOM   11211 C  CA  . LYS K  1 10  ? -7.015  -45.251 26.651 1.00 41.03  ? 9   LYS K CA  1 
ATOM   11212 C  C   . LYS K  1 10  ? -8.201  -44.298 26.746 1.00 40.92  ? 9   LYS K C   1 
ATOM   11213 O  O   . LYS K  1 10  ? -8.684  -43.802 25.731 1.00 42.25  ? 9   LYS K O   1 
ATOM   11214 C  CB  . LYS K  1 10  ? -5.734  -44.509 27.011 1.00 44.15  ? 9   LYS K CB  1 
ATOM   11215 C  CG  . LYS K  1 10  ? -4.534  -45.377 27.375 1.00 55.04  ? 9   LYS K CG  1 
ATOM   11216 C  CD  . LYS K  1 10  ? -3.264  -44.578 27.752 1.00 69.48  ? 9   LYS K CD  1 
ATOM   11217 C  CE  . LYS K  1 10  ? -1.986  -44.636 26.892 1.00 72.53  ? 9   LYS K CE  1 
ATOM   11218 N  NZ  . LYS K  1 10  ? -1.048  -45.735 27.243 1.00 70.27  ? 9   LYS K NZ  1 
ATOM   11219 N  N   . GLY K  1 11  ? -8.676  -44.036 27.969 1.00 40.60  ? 10  GLY K N   1 
ATOM   11220 C  CA  . GLY K  1 11  ? -9.718  -43.039 28.188 1.00 39.56  ? 10  GLY K CA  1 
ATOM   11221 C  C   . GLY K  1 11  ? -9.647  -42.433 29.582 1.00 41.22  ? 10  GLY K C   1 
ATOM   11222 O  O   . GLY K  1 11  ? -8.692  -42.688 30.310 1.00 42.13  ? 10  GLY K O   1 
ATOM   11223 N  N   . ASP K  1 12  ? -10.734 -41.787 30.003 1.00 44.32  ? 11  ASP K N   1 
ATOM   11224 C  CA  . ASP K  1 12  ? -10.825 -41.257 31.355 1.00 48.55  ? 11  ASP K CA  1 
ATOM   11225 C  C   . ASP K  1 12  ? -11.042 -42.369 32.377 1.00 46.62  ? 11  ASP K C   1 
ATOM   11226 O  O   . ASP K  1 12  ? -10.665 -42.217 33.535 1.00 50.66  ? 11  ASP K O   1 
ATOM   11227 C  CB  . ASP K  1 12  ? -11.945 -40.229 31.464 1.00 54.62  ? 11  ASP K CB  1 
ATOM   11228 C  CG  . ASP K  1 12  ? -11.627 -38.998 30.657 1.00 62.83  ? 11  ASP K CG  1 
ATOM   11229 O  OD1 . ASP K  1 12  ? -10.435 -38.628 30.616 1.00 71.50  ? 11  ASP K OD1 1 
ATOM   11230 O  OD2 . ASP K  1 12  ? -12.563 -38.439 30.059 1.00 74.23  ? 11  ASP K OD2 1 
ATOM   11231 N  N   . GLY K  1 13  ? -11.672 -43.461 31.941 1.00 45.57  ? 12  GLY K N   1 
ATOM   11232 C  CA  . GLY K  1 13  ? -12.072 -44.520 32.846 1.00 45.99  ? 12  GLY K CA  1 
ATOM   11233 C  C   . GLY K  1 13  ? -11.034 -45.634 32.888 1.00 42.74  ? 12  GLY K C   1 
ATOM   11234 O  O   . GLY K  1 13  ? -9.895  -45.427 32.469 1.00 39.22  ? 12  GLY K O   1 
ATOM   11235 N  N   . PRO K  1 14  ? -11.409 -46.839 33.366 1.00 41.41  ? 13  PRO K N   1 
ATOM   11236 C  CA  . PRO K  1 14  ? -10.469 -47.956 33.444 1.00 40.01  ? 13  PRO K CA  1 
ATOM   11237 C  C   . PRO K  1 14  ? -10.337 -48.763 32.149 1.00 39.11  ? 13  PRO K C   1 
ATOM   11238 O  O   . PRO K  1 14  ? -9.615  -49.764 32.104 1.00 40.17  ? 13  PRO K O   1 
ATOM   11239 C  CB  . PRO K  1 14  ? -11.139 -48.809 34.540 1.00 39.09  ? 13  PRO K CB  1 
ATOM   11240 C  CG  . PRO K  1 14  ? -12.664 -48.627 34.306 1.00 41.85  ? 13  PRO K CG  1 
ATOM   11241 C  CD  . PRO K  1 14  ? -12.762 -47.184 33.852 1.00 38.04  ? 13  PRO K CD  1 
ATOM   11242 N  N   . VAL K  1 15  ? -11.033 -48.357 31.080 1.00 38.62  ? 14  VAL K N   1 
ATOM   11243 C  CA  . VAL K  1 15  ? -10.994 -49.149 29.865 1.00 42.44  ? 14  VAL K CA  1 
ATOM   11244 C  C   . VAL K  1 15  ? -9.669  -48.900 29.152 1.00 45.37  ? 14  VAL K C   1 
ATOM   11245 O  O   . VAL K  1 15  ? -9.287  -47.753 28.927 1.00 49.84  ? 14  VAL K O   1 
ATOM   11246 C  CB  . VAL K  1 15  ? -12.193 -48.862 28.949 1.00 42.24  ? 14  VAL K CB  1 
ATOM   11247 C  CG1 . VAL K  1 15  ? -12.078 -49.624 27.632 1.00 40.53  ? 14  VAL K CG1 1 
ATOM   11248 C  CG2 . VAL K  1 15  ? -13.502 -49.167 29.654 1.00 43.67  ? 14  VAL K CG2 1 
ATOM   11249 N  N   . GLN K  1 16  ? -8.967  -49.988 28.819 1.00 43.62  ? 15  GLN K N   1 
ATOM   11250 C  CA  . GLN K  1 16  ? -7.738  -49.873 28.058 1.00 41.82  ? 15  GLN K CA  1 
ATOM   11251 C  C   . GLN K  1 16  ? -7.473  -51.160 27.290 1.00 37.88  ? 15  GLN K C   1 
ATOM   11252 O  O   . GLN K  1 16  ? -7.939  -52.221 27.679 1.00 37.37  ? 15  GLN K O   1 
ATOM   11253 C  CB  . GLN K  1 16  ? -6.571  -49.472 28.954 1.00 45.46  ? 15  GLN K CB  1 
ATOM   11254 C  CG  . GLN K  1 16  ? -6.232  -50.482 30.034 1.00 49.43  ? 15  GLN K CG  1 
ATOM   11255 C  CD  . GLN K  1 16  ? -5.014  -50.022 30.810 1.00 52.36  ? 15  GLN K CD  1 
ATOM   11256 O  OE1 . GLN K  1 16  ? -4.747  -48.830 30.917 1.00 51.38  ? 15  GLN K OE1 1 
ATOM   11257 N  NE2 . GLN K  1 16  ? -4.275  -50.966 31.387 1.00 57.13  ? 15  GLN K NE2 1 
ATOM   11258 N  N   . GLY K  1 17  ? -6.728  -51.047 26.185 1.00 32.71  ? 16  GLY K N   1 
ATOM   11259 C  CA  . GLY K  1 17  ? -6.536  -52.182 25.300 1.00 30.90  ? 16  GLY K CA  1 
ATOM   11260 C  C   . GLY K  1 17  ? -5.566  -51.901 24.167 1.00 29.10  ? 16  GLY K C   1 
ATOM   11261 O  O   . GLY K  1 17  ? -5.223  -50.756 23.927 1.00 29.48  ? 16  GLY K O   1 
ATOM   11262 N  N   . ILE K  1 18  ? -5.146  -52.966 23.482 1.00 25.81  ? 17  ILE K N   1 
ATOM   11263 C  CA  . ILE K  1 18  ? -4.287  -52.870 22.318 1.00 24.50  ? 17  ILE K CA  1 
ATOM   11264 C  C   . ILE K  1 18  ? -4.997  -53.578 21.177 1.00 24.44  ? 17  ILE K C   1 
ATOM   11265 O  O   . ILE K  1 18  ? -5.440  -54.705 21.353 1.00 26.49  ? 17  ILE K O   1 
ATOM   11266 C  CB  . ILE K  1 18  ? -2.924  -53.527 22.609 1.00 23.47  ? 17  ILE K CB  1 
ATOM   11267 C  CG1 . ILE K  1 18  ? -2.192  -52.844 23.769 1.00 23.45  ? 17  ILE K CG1 1 
ATOM   11268 C  CG2 . ILE K  1 18  ? -2.076  -53.637 21.342 1.00 21.78  ? 17  ILE K CG2 1 
ATOM   11269 C  CD1 . ILE K  1 18  ? -0.901  -53.533 24.138 1.00 23.96  ? 17  ILE K CD1 1 
ATOM   11270 N  N   . ILE K  1 19  ? -5.118  -52.922 20.022 1.00 23.51  ? 18  ILE K N   1 
ATOM   11271 C  CA  . ILE K  1 19  ? -5.752  -53.573 18.891 1.00 24.98  ? 18  ILE K CA  1 
ATOM   11272 C  C   . ILE K  1 19  ? -4.790  -53.524 17.714 1.00 26.24  ? 18  ILE K C   1 
ATOM   11273 O  O   . ILE K  1 19  ? -4.291  -52.453 17.377 1.00 28.27  ? 18  ILE K O   1 
ATOM   11274 C  CB  . ILE K  1 19  ? -7.102  -52.921 18.535 1.00 25.84  ? 18  ILE K CB  1 
ATOM   11275 C  CG1 . ILE K  1 19  ? -8.104  -52.979 19.693 1.00 25.59  ? 18  ILE K CG1 1 
ATOM   11276 C  CG2 . ILE K  1 19  ? -7.675  -53.508 17.247 1.00 24.97  ? 18  ILE K CG2 1 
ATOM   11277 C  CD1 . ILE K  1 19  ? -8.537  -54.376 20.096 1.00 24.58  ? 18  ILE K CD1 1 
ATOM   11278 N  N   . ASN K  1 20  ? -4.571  -54.687 17.090 1.00 25.19  ? 19  ASN K N   1 
ATOM   11279 C  CA  . ASN K  1 20  ? -3.704  -54.776 15.929 1.00 25.89  ? 19  ASN K CA  1 
ATOM   11280 C  C   . ASN K  1 20  ? -4.535  -54.861 14.660 1.00 26.02  ? 19  ASN K C   1 
ATOM   11281 O  O   . ASN K  1 20  ? -5.616  -55.431 14.669 1.00 25.39  ? 19  ASN K O   1 
ATOM   11282 C  CB  . ASN K  1 20  ? -2.804  -56.004 15.997 1.00 24.28  ? 19  ASN K CB  1 
ATOM   11283 C  CG  . ASN K  1 20  ? -2.056  -56.055 17.306 1.00 25.07  ? 19  ASN K CG  1 
ATOM   11284 O  OD1 . ASN K  1 20  ? -2.482  -56.740 18.228 1.00 26.64  ? 19  ASN K OD1 1 
ATOM   11285 N  ND2 . ASN K  1 20  ? -0.979  -55.290 17.413 1.00 24.82  ? 19  ASN K ND2 1 
ATOM   11286 N  N   . PHE K  1 21  ? -3.989  -54.293 13.581 1.00 28.02  ? 20  PHE K N   1 
ATOM   11287 C  CA  . PHE K  1 21  ? -4.598  -54.402 12.265 1.00 28.80  ? 20  PHE K CA  1 
ATOM   11288 C  C   . PHE K  1 21  ? -3.541  -54.917 11.305 1.00 30.72  ? 20  PHE K C   1 
ATOM   11289 O  O   . PHE K  1 21  ? -2.419  -54.425 11.304 1.00 32.03  ? 20  PHE K O   1 
ATOM   11290 C  CB  . PHE K  1 21  ? -5.038  -53.034 11.754 1.00 26.09  ? 20  PHE K CB  1 
ATOM   11291 C  CG  . PHE K  1 21  ? -6.087  -52.339 12.583 1.00 25.49  ? 20  PHE K CG  1 
ATOM   11292 C  CD1 . PHE K  1 21  ? -5.775  -51.831 13.836 1.00 24.35  ? 20  PHE K CD1 1 
ATOM   11293 C  CD2 . PHE K  1 21  ? -7.375  -52.153 12.093 1.00 23.65  ? 20  PHE K CD2 1 
ATOM   11294 C  CE1 . PHE K  1 21  ? -6.729  -51.161 14.585 1.00 24.48  ? 20  PHE K CE1 1 
ATOM   11295 C  CE2 . PHE K  1 21  ? -8.331  -51.494 12.848 1.00 23.32  ? 20  PHE K CE2 1 
ATOM   11296 C  CZ  . PHE K  1 21  ? -8.009  -50.991 14.091 1.00 23.68  ? 20  PHE K CZ  1 
ATOM   11297 N  N   . GLU K  1 22  ? -3.908  -55.908 10.497 1.00 34.91  ? 21  GLU K N   1 
ATOM   11298 C  CA  . GLU K  1 22  ? -2.965  -56.457 9.540  1.00 36.51  ? 21  GLU K CA  1 
ATOM   11299 C  C   . GLU K  1 22  ? -3.675  -56.673 8.211  1.00 35.34  ? 21  GLU K C   1 
ATOM   11300 O  O   . GLU K  1 22  ? -4.817  -57.105 8.196  1.00 35.84  ? 21  GLU K O   1 
ATOM   11301 C  CB  . GLU K  1 22  ? -2.360  -57.742 10.099 1.00 39.78  ? 21  GLU K CB  1 
ATOM   11302 C  CG  . GLU K  1 22  ? -1.109  -58.175 9.369  1.00 48.27  ? 21  GLU K CG  1 
ATOM   11303 C  CD  . GLU K  1 22  ? -0.428  -59.427 9.892  1.00 55.15  ? 21  GLU K CD  1 
ATOM   11304 O  OE1 . GLU K  1 22  ? -0.107  -59.470 11.094 1.00 55.90  ? 21  GLU K OE1 1 
ATOM   11305 O  OE2 . GLU K  1 22  ? -0.266  -60.386 9.085  1.00 62.72  ? 21  GLU K OE2 1 
ATOM   11306 N  N   . GLN K  1 23  ? -2.983  -56.358 7.114  1.00 34.79  ? 22  GLN K N   1 
ATOM   11307 C  CA  . GLN K  1 23  ? -3.548  -56.471 5.776  1.00 36.93  ? 22  GLN K CA  1 
ATOM   11308 C  C   . GLN K  1 23  ? -2.501  -57.091 4.848  1.00 39.43  ? 22  GLN K C   1 
ATOM   11309 O  O   . GLN K  1 23  ? -1.539  -56.432 4.474  1.00 38.50  ? 22  GLN K O   1 
ATOM   11310 C  CB  . GLN K  1 23  ? -3.977  -55.087 5.292  1.00 33.95  ? 22  GLN K CB  1 
ATOM   11311 C  CG  . GLN K  1 23  ? -4.788  -55.122 4.026  1.00 35.37  ? 22  GLN K CG  1 
ATOM   11312 C  CD  . GLN K  1 23  ? -5.171  -53.741 3.514  1.00 40.43  ? 22  GLN K CD  1 
ATOM   11313 O  OE1 . GLN K  1 23  ? -4.451  -52.754 3.685  1.00 41.29  ? 22  GLN K OE1 1 
ATOM   11314 N  NE2 . GLN K  1 23  ? -6.323  -53.661 2.860  1.00 42.39  ? 22  GLN K NE2 1 
ATOM   11315 N  N   . LYS K  1 24  ? -2.704  -58.364 4.476  1.00 45.46  ? 23  LYS K N   1 
ATOM   11316 C  CA  . LYS K  1 24  ? -1.705  -59.127 3.727  1.00 47.01  ? 23  LYS K CA  1 
ATOM   11317 C  C   . LYS K  1 24  ? -1.623  -58.640 2.275  1.00 54.38  ? 23  LYS K C   1 
ATOM   11318 O  O   . LYS K  1 24  ? -0.533  -58.341 1.807  1.00 55.51  ? 23  LYS K O   1 
ATOM   11319 C  CB  . LYS K  1 24  ? -1.906  -60.644 3.886  1.00 45.51  ? 23  LYS K CB  1 
ATOM   11320 C  CG  . LYS K  1 24  ? -1.424  -61.226 5.211  0.40 43.78  ? 23  LYS K CG  1 
ATOM   11321 C  CD  . LYS K  1 24  ? -1.927  -62.633 5.494  0.40 42.88  ? 23  LYS K CD  1 
ATOM   11322 C  CE  . LYS K  1 24  ? -1.490  -63.142 6.853  0.40 41.84  ? 23  LYS K CE  1 
ATOM   11323 N  NZ  . LYS K  1 24  ? -2.495  -64.037 7.485  0.40 40.06  ? 23  LYS K NZ  1 
ATOM   11324 N  N   . GLU K  1 25  ? -2.755  -58.495 1.577  1.00 63.51  ? 24  GLU K N   1 
ATOM   11325 C  CA  . GLU K  1 25  ? -2.758  -57.948 0.226  1.00 62.63  ? 24  GLU K CA  1 
ATOM   11326 C  C   . GLU K  1 25  ? -3.220  -56.496 0.294  1.00 66.36  ? 24  GLU K C   1 
ATOM   11327 O  O   . GLU K  1 25  ? -3.981  -56.131 1.184  1.00 72.31  ? 24  GLU K O   1 
ATOM   11328 C  CB  . GLU K  1 25  ? -3.694  -58.745 -0.690 0.40 60.38  ? 24  GLU K CB  1 
ATOM   11329 C  CG  . GLU K  1 25  ? -3.624  -60.256 -0.555 0.40 56.90  ? 24  GLU K CG  1 
ATOM   11330 C  CD  . GLU K  1 25  ? -2.379  -60.919 -1.106 0.40 56.04  ? 24  GLU K CD  1 
ATOM   11331 O  OE1 . GLU K  1 25  ? -1.681  -60.298 -1.929 0.40 54.47  ? 24  GLU K OE1 1 
ATOM   11332 O  OE2 . GLU K  1 25  ? -2.135  -62.073 -0.735 0.40 57.08  ? 24  GLU K OE2 1 
ATOM   11333 N  N   . SER K  1 26  ? -2.806  -55.687 -0.681 1.00 71.29  ? 25  SER K N   1 
ATOM   11334 C  CA  . SER K  1 26  ? -3.010  -54.249 -0.611 1.00 72.74  ? 25  SER K CA  1 
ATOM   11335 C  C   . SER K  1 26  ? -4.485  -53.857 -0.709 1.00 69.44  ? 25  SER K C   1 
ATOM   11336 O  O   . SER K  1 26  ? -4.886  -52.855 -0.116 1.00 73.55  ? 25  SER K O   1 
ATOM   11337 C  CB  . SER K  1 26  ? -2.149  -53.482 -1.577 1.00 82.47  ? 25  SER K CB  1 
ATOM   11338 O  OG  . SER K  1 26  ? -2.029  -54.190 -2.800 1.00 97.14  ? 25  SER K OG  1 
ATOM   11339 N  N   . ASN K  1 27  ? -5.293  -54.625 -1.443 1.00 66.98  ? 26  ASN K N   1 
ATOM   11340 C  CA  . ASN K  1 27  ? -6.701  -54.284 -1.501 1.00 67.77  ? 26  ASN K CA  1 
ATOM   11341 C  C   . ASN K  1 27  ? -7.538  -55.315 -0.721 1.00 57.55  ? 26  ASN K C   1 
ATOM   11342 O  O   . ASN K  1 27  ? -8.758  -55.326 -0.831 1.00 59.11  ? 26  ASN K O   1 
ATOM   11343 C  CB  . ASN K  1 27  ? -7.161  -54.083 -2.943 1.00 82.43  ? 26  ASN K CB  1 
ATOM   11344 C  CG  . ASN K  1 27  ? -6.331  -53.160 -3.792 1.00 93.93  ? 26  ASN K CG  1 
ATOM   11345 O  OD1 . ASN K  1 27  ? -5.809  -52.184 -3.282 1.00 105.18 ? 26  ASN K OD1 1 
ATOM   11346 N  ND2 . ASN K  1 27  ? -6.227  -53.462 -5.078 1.00 95.29  ? 26  ASN K ND2 1 
ATOM   11347 N  N   . GLY K  1 28  ? -6.861  -56.188 0.036  1.00 50.34  ? 27  GLY K N   1 
ATOM   11348 C  CA  . GLY K  1 28  ? -7.486  -57.351 0.625  1.00 40.67  ? 27  GLY K CA  1 
ATOM   11349 C  C   . GLY K  1 28  ? -8.069  -57.076 2.008  1.00 35.42  ? 27  GLY K C   1 
ATOM   11350 O  O   . GLY K  1 28  ? -7.991  -55.959 2.516  1.00 33.56  ? 27  GLY K O   1 
ATOM   11351 N  N   . PRO K  1 29  ? -8.653  -58.104 2.669  1.00 32.73  ? 28  PRO K N   1 
ATOM   11352 C  CA  . PRO K  1 29  ? -9.285  -57.925 3.978  1.00 31.24  ? 28  PRO K CA  1 
ATOM   11353 C  C   . PRO K  1 29  ? -8.272  -57.560 5.061  1.00 29.36  ? 28  PRO K C   1 
ATOM   11354 O  O   . PRO K  1 29  ? -7.078  -57.826 4.910  1.00 28.93  ? 28  PRO K O   1 
ATOM   11355 C  CB  . PRO K  1 29  ? -9.888  -59.312 4.262  1.00 31.13  ? 28  PRO K CB  1 
ATOM   11356 C  CG  . PRO K  1 29  ? -9.014  -60.258 3.467  1.00 33.16  ? 28  PRO K CG  1 
ATOM   11357 C  CD  . PRO K  1 29  ? -8.692  -59.499 2.199  1.00 31.92  ? 28  PRO K CD  1 
ATOM   11358 N  N   . VAL K  1 30  ? -8.769  -56.940 6.138  1.00 28.12  ? 29  VAL K N   1 
ATOM   11359 C  CA  . VAL K  1 30  ? -7.952  -56.510 7.262  1.00 26.33  ? 29  VAL K CA  1 
ATOM   11360 C  C   . VAL K  1 30  ? -8.316  -57.349 8.483  1.00 25.35  ? 29  VAL K C   1 
ATOM   11361 O  O   . VAL K  1 30  ? -9.476  -57.424 8.862  1.00 25.49  ? 29  VAL K O   1 
ATOM   11362 C  CB  . VAL K  1 30  ? -8.165  -55.009 7.553  1.00 26.98  ? 29  VAL K CB  1 
ATOM   11363 C  CG1 . VAL K  1 30  ? -7.309  -54.550 8.722  1.00 26.93  ? 29  VAL K CG1 1 
ATOM   11364 C  CG2 . VAL K  1 30  ? -7.952  -54.123 6.314  1.00 26.51  ? 29  VAL K CG2 1 
ATOM   11365 N  N   . LYS K  1 31  ? -7.327  -57.984 9.097  1.00 25.67  ? 30  LYS K N   1 
ATOM   11366 C  CA  . LYS K  1 31  ? -7.563  -58.715 10.335 1.00 28.27  ? 30  LYS K CA  1 
ATOM   11367 C  C   . LYS K  1 31  ? -7.428  -57.732 11.490 1.00 27.86  ? 30  LYS K C   1 
ATOM   11368 O  O   . LYS K  1 31  ? -6.425  -57.025 11.585 1.00 28.47  ? 30  LYS K O   1 
ATOM   11369 C  CB  . LYS K  1 31  ? -6.588  -59.894 10.506 1.00 32.55  ? 30  LYS K CB  1 
ATOM   11370 C  CG  . LYS K  1 31  ? -6.875  -61.147 9.688  1.00 36.30  ? 30  LYS K CG  1 
ATOM   11371 C  CD  . LYS K  1 31  ? -6.173  -62.382 10.138 1.00 40.75  ? 30  LYS K CD  1 
ATOM   11372 C  CE  . LYS K  1 31  ? -7.046  -63.566 9.797  1.00 44.73  ? 30  LYS K CE  1 
ATOM   11373 N  NZ  . LYS K  1 31  ? -6.245  -64.606 9.114  1.00 48.17  ? 30  LYS K NZ  1 
ATOM   11374 N  N   . VAL K  1 32  ? -8.446  -57.673 12.348 1.00 27.33  ? 31  VAL K N   1 
ATOM   11375 C  CA  . VAL K  1 32  ? -8.403  -56.789 13.502 1.00 26.71  ? 31  VAL K CA  1 
ATOM   11376 C  C   . VAL K  1 32  ? -8.464  -57.652 14.757 1.00 26.85  ? 31  VAL K C   1 
ATOM   11377 O  O   . VAL K  1 32  ? -9.460  -58.329 14.995 1.00 27.14  ? 31  VAL K O   1 
ATOM   11378 C  CB  . VAL K  1 32  ? -9.575  -55.791 13.464 1.00 24.27  ? 31  VAL K CB  1 
ATOM   11379 C  CG1 . VAL K  1 32  ? -9.491  -54.789 14.607 1.00 21.99  ? 31  VAL K CG1 1 
ATOM   11380 C  CG2 . VAL K  1 32  ? -9.646  -55.071 12.120 1.00 22.86  ? 31  VAL K CG2 1 
ATOM   11381 N  N   . TRP K  1 33  ? -7.407  -57.646 15.568 1.00 26.78  ? 32  TRP K N   1 
ATOM   11382 C  CA  . TRP K  1 33  ? -7.455  -58.453 16.779 1.00 26.74  ? 32  TRP K CA  1 
ATOM   11383 C  C   . TRP K  1 33  ? -6.719  -57.776 17.927 1.00 26.00  ? 32  TRP K C   1 
ATOM   11384 O  O   . TRP K  1 33  ? -5.823  -56.959 17.715 1.00 25.48  ? 32  TRP K O   1 
ATOM   11385 C  CB  . TRP K  1 33  ? -6.881  -59.853 16.534 1.00 29.42  ? 32  TRP K CB  1 
ATOM   11386 C  CG  . TRP K  1 33  ? -5.385  -59.897 16.553 1.00 31.65  ? 32  TRP K CG  1 
ATOM   11387 C  CD1 . TRP K  1 33  ? -4.567  -60.269 17.587 1.00 33.27  ? 32  TRP K CD1 1 
ATOM   11388 C  CD2 . TRP K  1 33  ? -4.517  -59.533 15.470 1.00 34.05  ? 32  TRP K CD2 1 
ATOM   11389 N  NE1 . TRP K  1 33  ? -3.249  -60.167 17.222 1.00 33.85  ? 32  TRP K NE1 1 
ATOM   11390 C  CE2 . TRP K  1 33  ? -3.189  -59.722 15.924 1.00 35.96  ? 32  TRP K CE2 1 
ATOM   11391 C  CE3 . TRP K  1 33  ? -4.732  -59.061 14.169 1.00 35.53  ? 32  TRP K CE3 1 
ATOM   11392 C  CZ2 . TRP K  1 33  ? -2.084  -59.458 15.109 1.00 38.07  ? 32  TRP K CZ2 1 
ATOM   11393 C  CZ3 . TRP K  1 33  ? -3.637  -58.798 13.369 1.00 38.72  ? 32  TRP K CZ3 1 
ATOM   11394 C  CH2 . TRP K  1 33  ? -2.333  -59.000 13.835 1.00 37.53  ? 32  TRP K CH2 1 
ATOM   11395 N  N   . GLY K  1 34  ? -7.078  -58.186 19.140 1.00 24.43  ? 33  GLY K N   1 
ATOM   11396 C  CA  . GLY K  1 34  ? -6.387  -57.762 20.335 1.00 25.45  ? 33  GLY K CA  1 
ATOM   11397 C  C   . GLY K  1 34  ? -7.285  -57.930 21.546 1.00 25.91  ? 33  GLY K C   1 
ATOM   11398 O  O   . GLY K  1 34  ? -8.229  -58.701 21.522 1.00 26.77  ? 33  GLY K O   1 
ATOM   11399 N  N   . SER K  1 35  ? -6.997  -57.182 22.598 1.00 27.95  ? 34  SER K N   1 
ATOM   11400 C  CA  . SER K  1 35  ? -7.689  -57.394 23.846 1.00 30.13  ? 34  SER K CA  1 
ATOM   11401 C  C   . SER K  1 35  ? -8.025  -56.040 24.476 1.00 33.76  ? 34  SER K C   1 
ATOM   11402 O  O   . SER K  1 35  ? -7.228  -55.111 24.414 1.00 38.18  ? 34  SER K O   1 
ATOM   11403 C  CB  . SER K  1 35  ? -6.816  -58.252 24.702 1.00 29.08  ? 34  SER K CB  1 
ATOM   11404 O  OG  . SER K  1 35  ? -7.296  -58.280 26.028 1.00 31.86  ? 34  SER K OG  1 
ATOM   11405 N  N   . ILE K  1 36  ? -9.232  -55.906 25.043 1.00 32.94  ? 35  ILE K N   1 
ATOM   11406 C  CA  . ILE K  1 36  ? -9.601  -54.719 25.800 1.00 32.37  ? 35  ILE K CA  1 
ATOM   11407 C  C   . ILE K  1 36  ? -10.049 -55.160 27.185 1.00 35.22  ? 35  ILE K C   1 
ATOM   11408 O  O   . ILE K  1 36  ? -10.779 -56.141 27.299 1.00 36.05  ? 35  ILE K O   1 
ATOM   11409 C  CB  . ILE K  1 36  ? -10.705 -53.928 25.079 1.00 30.93  ? 35  ILE K CB  1 
ATOM   11410 C  CG1 . ILE K  1 36  ? -10.381 -53.720 23.597 1.00 32.78  ? 35  ILE K CG1 1 
ATOM   11411 C  CG2 . ILE K  1 36  ? -10.978 -52.616 25.790 1.00 30.95  ? 35  ILE K CG2 1 
ATOM   11412 C  CD1 . ILE K  1 36  ? -11.529 -53.126 22.794 1.00 30.92  ? 35  ILE K CD1 1 
ATOM   11413 N  N   . LYS K  1 37  ? -9.617  -54.446 28.226 1.00 37.47  ? 36  LYS K N   1 
ATOM   11414 C  CA  . LYS K  1 37  ? -10.008 -54.808 29.579 1.00 36.07  ? 36  LYS K CA  1 
ATOM   11415 C  C   . LYS K  1 37  ? -10.702 -53.624 30.248 1.00 35.62  ? 36  LYS K C   1 
ATOM   11416 O  O   . LYS K  1 37  ? -10.623 -52.494 29.762 1.00 36.17  ? 36  LYS K O   1 
ATOM   11417 C  CB  . LYS K  1 37  ? -8.792  -55.319 30.368 1.00 36.23  ? 36  LYS K CB  1 
ATOM   11418 C  CG  . LYS K  1 37  ? -7.709  -54.301 30.661 1.00 34.89  ? 36  LYS K CG  1 
ATOM   11419 C  CD  . LYS K  1 37  ? -6.818  -54.762 31.821 1.00 36.86  ? 36  LYS K CD  1 
ATOM   11420 C  CE  . LYS K  1 37  ? -5.688  -53.812 32.138 1.00 35.20  ? 36  LYS K CE  1 
ATOM   11421 N  NZ  . LYS K  1 37  ? -4.470  -54.492 32.663 1.00 34.92  ? 36  LYS K NZ  1 
ATOM   11422 N  N   . GLY K  1 38  ? -11.401 -53.905 31.355 1.00 36.73  ? 37  GLY K N   1 
ATOM   11423 C  CA  . GLY K  1 38  ? -12.079 -52.884 32.146 1.00 37.00  ? 37  GLY K CA  1 
ATOM   11424 C  C   . GLY K  1 38  ? -13.477 -52.528 31.630 1.00 37.12  ? 37  GLY K C   1 
ATOM   11425 O  O   . GLY K  1 38  ? -14.045 -51.526 32.071 1.00 35.64  ? 37  GLY K O   1 
ATOM   11426 N  N   . LEU K  1 39  ? -14.024 -53.342 30.714 1.00 39.68  ? 38  LEU K N   1 
ATOM   11427 C  CA  . LEU K  1 39  ? -15.338 -53.086 30.144 1.00 41.29  ? 38  LEU K CA  1 
ATOM   11428 C  C   . LEU K  1 39  ? -16.408 -53.742 31.011 1.00 43.68  ? 38  LEU K C   1 
ATOM   11429 O  O   . LEU K  1 39  ? -16.130 -54.719 31.710 1.00 46.09  ? 38  LEU K O   1 
ATOM   11430 C  CB  . LEU K  1 39  ? -15.390 -53.681 28.733 1.00 37.97  ? 38  LEU K CB  1 
ATOM   11431 C  CG  . LEU K  1 39  ? -14.577 -52.946 27.683 1.00 34.42  ? 38  LEU K CG  1 
ATOM   11432 C  CD1 . LEU K  1 39  ? -14.408 -53.804 26.446 1.00 33.00  ? 38  LEU K CD1 1 
ATOM   11433 C  CD2 . LEU K  1 39  ? -15.232 -51.637 27.309 1.00 32.62  ? 38  LEU K CD2 1 
ATOM   11434 N  N   . THR K  1 40  ? -17.636 -53.209 30.928 1.00 40.67  ? 39  THR K N   1 
ATOM   11435 C  CA  . THR K  1 40  ? -18.773 -53.892 31.522 1.00 41.05  ? 39  THR K CA  1 
ATOM   11436 C  C   . THR K  1 40  ? -19.121 -55.096 30.655 1.00 43.36  ? 39  THR K C   1 
ATOM   11437 O  O   . THR K  1 40  ? -18.911 -55.073 29.445 1.00 45.36  ? 39  THR K O   1 
ATOM   11438 C  CB  . THR K  1 40  ? -19.987 -52.968 31.637 1.00 40.72  ? 39  THR K CB  1 
ATOM   11439 O  OG1 . THR K  1 40  ? -20.149 -52.386 30.346 1.00 42.80  ? 39  THR K OG1 1 
ATOM   11440 C  CG2 . THR K  1 40  ? -19.830 -51.900 32.700 1.00 37.93  ? 39  THR K CG2 1 
ATOM   11441 N  N   . GLU K  1 41  ? -19.637 -56.157 31.281 1.00 46.01  ? 40  GLU K N   1 
ATOM   11442 C  CA  . GLU K  1 41  ? -19.947 -57.379 30.557 1.00 47.85  ? 40  GLU K CA  1 
ATOM   11443 C  C   . GLU K  1 41  ? -20.927 -57.052 29.432 1.00 46.76  ? 40  GLU K C   1 
ATOM   11444 O  O   . GLU K  1 41  ? -21.813 -56.220 29.604 1.00 45.53  ? 40  GLU K O   1 
ATOM   11445 C  CB  . GLU K  1 41  ? -20.536 -58.402 31.520 1.00 56.02  ? 40  GLU K CB  1 
ATOM   11446 C  CG  . GLU K  1 41  ? -20.789 -59.740 30.853 1.00 68.22  ? 40  GLU K CG  1 
ATOM   11447 C  CD  . GLU K  1 41  ? -21.306 -60.844 31.766 1.00 72.01  ? 40  GLU K CD  1 
ATOM   11448 O  OE1 . GLU K  1 41  ? -21.613 -60.560 32.965 1.00 69.40  ? 40  GLU K OE1 1 
ATOM   11449 O  OE2 . GLU K  1 41  ? -21.388 -61.993 31.272 1.00 79.60  ? 40  GLU K OE2 1 
ATOM   11450 N  N   . GLY K  1 42  ? -20.742 -57.683 28.269 1.00 45.24  ? 41  GLY K N   1 
ATOM   11451 C  CA  . GLY K  1 42  ? -21.697 -57.525 27.181 1.00 43.58  ? 41  GLY K CA  1 
ATOM   11452 C  C   . GLY K  1 42  ? -21.100 -56.862 25.941 1.00 42.54  ? 41  GLY K C   1 
ATOM   11453 O  O   . GLY K  1 42  ? -19.875 -56.756 25.806 1.00 42.99  ? 41  GLY K O   1 
ATOM   11454 N  N   . LEU K  1 43  ? -21.984 -56.417 25.034 1.00 39.20  ? 42  LEU K N   1 
ATOM   11455 C  CA  . LEU K  1 43  ? -21.606 -55.862 23.744 1.00 37.69  ? 42  LEU K CA  1 
ATOM   11456 C  C   . LEU K  1 43  ? -21.187 -54.401 23.895 1.00 38.58  ? 42  LEU K C   1 
ATOM   11457 O  O   . LEU K  1 43  ? -21.790 -53.662 24.675 1.00 42.35  ? 42  LEU K O   1 
ATOM   11458 C  CB  . LEU K  1 43  ? -22.787 -55.959 22.784 1.00 37.43  ? 42  LEU K CB  1 
ATOM   11459 C  CG  . LEU K  1 43  ? -23.212 -57.357 22.369 1.00 38.38  ? 42  LEU K CG  1 
ATOM   11460 C  CD1 . LEU K  1 43  ? -24.514 -57.281 21.580 1.00 38.04  ? 42  LEU K CD1 1 
ATOM   11461 C  CD2 . LEU K  1 43  ? -22.149 -58.013 21.507 1.00 38.21  ? 42  LEU K CD2 1 
ATOM   11462 N  N   . HIS K  1 44  ? -20.153 -54.012 23.132 1.00 34.28  ? 43  HIS K N   1 
ATOM   11463 C  CA  . HIS K  1 44  ? -19.694 -52.638 23.048 1.00 30.71  ? 43  HIS K CA  1 
ATOM   11464 C  C   . HIS K  1 44  ? -19.417 -52.272 21.593 1.00 32.00  ? 43  HIS K C   1 
ATOM   11465 O  O   . HIS K  1 44  ? -18.781 -53.028 20.851 1.00 30.95  ? 43  HIS K O   1 
ATOM   11466 C  CB  . HIS K  1 44  ? -18.460 -52.429 23.915 1.00 28.15  ? 43  HIS K CB  1 
ATOM   11467 C  CG  . HIS K  1 44  ? -18.706 -52.582 25.375 1.00 29.35  ? 43  HIS K CG  1 
ATOM   11468 N  ND1 . HIS K  1 44  ? -18.986 -51.503 26.201 1.00 29.46  ? 43  HIS K ND1 1 
ATOM   11469 C  CD2 . HIS K  1 44  ? -18.705 -53.671 26.172 1.00 31.20  ? 43  HIS K CD2 1 
ATOM   11470 C  CE1 . HIS K  1 44  ? -19.138 -51.919 27.437 1.00 30.59  ? 43  HIS K CE1 1 
ATOM   11471 N  NE2 . HIS K  1 44  ? -18.970 -53.239 27.452 1.00 32.01  ? 43  HIS K NE2 1 
ATOM   11472 N  N   . GLY K  1 45  ? -19.936 -51.105 21.196 1.00 31.36  ? 44  GLY K N   1 
ATOM   11473 C  CA  . GLY K  1 45  ? -19.737 -50.584 19.855 1.00 27.75  ? 44  GLY K CA  1 
ATOM   11474 C  C   . GLY K  1 45  ? -18.266 -50.291 19.594 1.00 25.42  ? 44  GLY K C   1 
ATOM   11475 O  O   . GLY K  1 45  ? -17.553 -49.825 20.474 1.00 24.10  ? 44  GLY K O   1 
ATOM   11476 N  N   . PHE K  1 46  ? -17.843 -50.551 18.360 1.00 24.44  ? 45  PHE K N   1 
ATOM   11477 C  CA  . PHE K  1 46  ? -16.438 -50.574 18.011 1.00 25.07  ? 45  PHE K CA  1 
ATOM   11478 C  C   . PHE K  1 46  ? -16.285 -49.936 16.638 1.00 25.74  ? 45  PHE K C   1 
ATOM   11479 O  O   . PHE K  1 46  ? -16.665 -50.543 15.647 1.00 24.39  ? 45  PHE K O   1 
ATOM   11480 C  CB  . PHE K  1 46  ? -15.996 -52.038 17.984 1.00 23.49  ? 45  PHE K CB  1 
ATOM   11481 C  CG  . PHE K  1 46  ? -14.518 -52.299 17.952 1.00 23.44  ? 45  PHE K CG  1 
ATOM   11482 C  CD1 . PHE K  1 46  ? -13.701 -51.939 19.022 1.00 23.55  ? 45  PHE K CD1 1 
ATOM   11483 C  CD2 . PHE K  1 46  ? -13.953 -52.961 16.872 1.00 22.96  ? 45  PHE K CD2 1 
ATOM   11484 C  CE1 . PHE K  1 46  ? -12.345 -52.231 19.009 1.00 23.94  ? 45  PHE K CE1 1 
ATOM   11485 C  CE2 . PHE K  1 46  ? -12.590 -53.228 16.849 1.00 22.82  ? 45  PHE K CE2 1 
ATOM   11486 C  CZ  . PHE K  1 46  ? -11.797 -52.864 17.911 1.00 22.88  ? 45  PHE K CZ  1 
ATOM   11487 N  N   . HIS K  1 47  ? -15.753 -48.707 16.592 1.00 24.46  ? 46  HIS K N   1 
ATOM   11488 C  CA  . HIS K  1 47  ? -15.763 -47.946 15.351 1.00 24.92  ? 46  HIS K CA  1 
ATOM   11489 C  C   . HIS K  1 47  ? -14.450 -47.218 15.112 1.00 24.71  ? 46  HIS K C   1 
ATOM   11490 O  O   . HIS K  1 47  ? -13.751 -46.854 16.052 1.00 25.43  ? 46  HIS K O   1 
ATOM   11491 C  CB  . HIS K  1 47  ? -16.912 -46.930 15.333 1.00 28.36  ? 46  HIS K CB  1 
ATOM   11492 C  CG  . HIS K  1 47  ? -18.187 -47.459 15.890 1.00 32.06  ? 46  HIS K CG  1 
ATOM   11493 N  ND1 . HIS K  1 47  ? -18.688 -47.058 17.109 1.00 33.15  ? 46  HIS K ND1 1 
ATOM   11494 C  CD2 . HIS K  1 47  ? -19.055 -48.374 15.411 1.00 34.26  ? 46  HIS K CD2 1 
ATOM   11495 C  CE1 . HIS K  1 47  ? -19.809 -47.701 17.356 1.00 33.60  ? 46  HIS K CE1 1 
ATOM   11496 N  NE2 . HIS K  1 47  ? -20.055 -48.519 16.331 1.00 33.69  ? 46  HIS K NE2 1 
ATOM   11497 N  N   . VAL K  1 48  ? -14.162 -46.985 13.838 1.00 24.49  ? 47  VAL K N   1 
ATOM   11498 C  CA  . VAL K  1 48  ? -13.154 -46.019 13.440 1.00 24.56  ? 47  VAL K CA  1 
ATOM   11499 C  C   . VAL K  1 48  ? -13.845 -44.673 13.239 1.00 25.58  ? 47  VAL K C   1 
ATOM   11500 O  O   . VAL K  1 48  ? -14.691 -44.546 12.353 1.00 27.25  ? 47  VAL K O   1 
ATOM   11501 C  CB  . VAL K  1 48  ? -12.398 -46.432 12.162 1.00 22.48  ? 47  VAL K CB  1 
ATOM   11502 C  CG1 . VAL K  1 48  ? -11.295 -45.437 11.846 1.00 21.36  ? 47  VAL K CG1 1 
ATOM   11503 C  CG2 . VAL K  1 48  ? -11.891 -47.855 12.207 1.00 21.65  ? 47  VAL K CG2 1 
ATOM   11504 N  N   . HIS K  1 49  ? -13.479 -43.683 14.066 1.00 25.05  ? 48  HIS K N   1 
ATOM   11505 C  CA  . HIS K  1 49  ? -13.931 -42.314 13.884 1.00 25.48  ? 48  HIS K CA  1 
ATOM   11506 C  C   . HIS K  1 49  ? -12.980 -41.552 12.957 1.00 25.89  ? 48  HIS K C   1 
ATOM   11507 O  O   . HIS K  1 49  ? -11.884 -42.030 12.655 1.00 25.88  ? 48  HIS K O   1 
ATOM   11508 C  CB  . HIS K  1 49  ? -14.099 -41.638 15.246 1.00 26.68  ? 48  HIS K CB  1 
ATOM   11509 C  CG  . HIS K  1 49  ? -15.207 -42.233 16.055 1.00 29.19  ? 48  HIS K CG  1 
ATOM   11510 N  ND1 . HIS K  1 49  ? -16.292 -41.488 16.483 1.00 26.89  ? 48  HIS K ND1 1 
ATOM   11511 C  CD2 . HIS K  1 49  ? -15.408 -43.493 16.512 1.00 28.74  ? 48  HIS K CD2 1 
ATOM   11512 C  CE1 . HIS K  1 49  ? -17.106 -42.252 17.176 1.00 28.14  ? 48  HIS K CE1 1 
ATOM   11513 N  NE2 . HIS K  1 49  ? -16.578 -43.492 17.221 1.00 28.19  ? 48  HIS K NE2 1 
ATOM   11514 N  N   . GLU K  1 50  ? -13.392 -40.342 12.548 1.00 26.05  ? 49  GLU K N   1 
ATOM   11515 C  CA  . GLU K  1 50  ? -12.794 -39.632 11.424 1.00 26.46  ? 49  GLU K CA  1 
ATOM   11516 C  C   . GLU K  1 50  ? -11.395 -39.083 11.733 1.00 25.70  ? 49  GLU K C   1 
ATOM   11517 O  O   . GLU K  1 50  ? -10.510 -39.161 10.890 1.00 25.06  ? 49  GLU K O   1 
ATOM   11518 C  CB  . GLU K  1 50  ? -13.683 -38.468 11.000 1.00 28.16  ? 49  GLU K CB  1 
ATOM   11519 C  CG  . GLU K  1 50  ? -13.326 -37.934 9.633  1.00 31.62  ? 49  GLU K CG  1 
ATOM   11520 C  CD  . GLU K  1 50  ? -14.163 -36.786 9.118  1.00 36.83  ? 49  GLU K CD  1 
ATOM   11521 O  OE1 . GLU K  1 50  ? -15.297 -36.569 9.659  1.00 41.56  ? 49  GLU K OE1 1 
ATOM   11522 O  OE2 . GLU K  1 50  ? -13.671 -36.106 8.193  1.00 37.31  ? 49  GLU K OE2 1 
ATOM   11523 N  N   . PHE K  1 51  ? -11.207 -38.509 12.925 1.00 24.74  ? 50  PHE K N   1 
ATOM   11524 C  CA  . PHE K  1 51  ? -10.017 -37.719 13.211 1.00 25.16  ? 50  PHE K CA  1 
ATOM   11525 C  C   . PHE K  1 51  ? -9.125  -38.389 14.241 1.00 26.94  ? 50  PHE K C   1 
ATOM   11526 O  O   . PHE K  1 51  ? -9.607  -38.818 15.289 1.00 28.73  ? 50  PHE K O   1 
ATOM   11527 C  CB  . PHE K  1 51  ? -10.399 -36.337 13.743 1.00 24.41  ? 50  PHE K CB  1 
ATOM   11528 C  CG  . PHE K  1 51  ? -11.323 -35.591 12.821 1.00 25.01  ? 50  PHE K CG  1 
ATOM   11529 C  CD1 . PHE K  1 51  ? -10.953 -35.353 11.503 1.00 25.61  ? 50  PHE K CD1 1 
ATOM   11530 C  CD2 . PHE K  1 51  ? -12.561 -35.149 13.258 1.00 25.69  ? 50  PHE K CD2 1 
ATOM   11531 C  CE1 . PHE K  1 51  ? -11.799 -34.673 10.634 1.00 25.55  ? 50  PHE K CE1 1 
ATOM   11532 C  CE2 . PHE K  1 51  ? -13.411 -34.477 12.390 1.00 26.29  ? 50  PHE K CE2 1 
ATOM   11533 C  CZ  . PHE K  1 51  ? -13.027 -34.235 11.082 1.00 25.72  ? 50  PHE K CZ  1 
ATOM   11534 N  N   . GLY K  1 52  ? -7.821  -38.436 13.927 1.00 26.23  ? 51  GLY K N   1 
ATOM   11535 C  CA  . GLY K  1 52  ? -6.782  -38.801 14.881 1.00 27.01  ? 51  GLY K CA  1 
ATOM   11536 C  C   . GLY K  1 52  ? -6.481  -37.640 15.830 1.00 28.65  ? 51  GLY K C   1 
ATOM   11537 O  O   . GLY K  1 52  ? -5.344  -37.195 15.944 1.00 27.60  ? 51  GLY K O   1 
ATOM   11538 N  N   . ASP K  1 53  ? -7.530  -37.141 16.490 1.00 28.72  ? 52  ASP K N   1 
ATOM   11539 C  CA  . ASP K  1 53  ? -7.407  -35.938 17.284 1.00 27.25  ? 52  ASP K CA  1 
ATOM   11540 C  C   . ASP K  1 53  ? -7.897  -36.229 18.691 1.00 26.32  ? 52  ASP K C   1 
ATOM   11541 O  O   . ASP K  1 53  ? -9.066  -36.515 18.881 1.00 26.12  ? 52  ASP K O   1 
ATOM   11542 C  CB  . ASP K  1 53  ? -8.168  -34.795 16.611 1.00 27.98  ? 52  ASP K CB  1 
ATOM   11543 C  CG  . ASP K  1 53  ? -8.074  -33.463 17.354 1.00 28.81  ? 52  ASP K CG  1 
ATOM   11544 O  OD1 . ASP K  1 53  ? -7.834  -33.476 18.590 1.00 28.16  ? 52  ASP K OD1 1 
ATOM   11545 O  OD2 . ASP K  1 53  ? -8.155  -32.405 16.676 1.00 27.88  ? 52  ASP K OD2 1 
ATOM   11546 N  N   . ASN K  1 54  ? -6.990  -36.165 19.663 1.00 27.13  ? 53  ASN K N   1 
ATOM   11547 C  CA  . ASN K  1 54  ? -7.333  -36.519 21.028 1.00 28.90  ? 53  ASN K CA  1 
ATOM   11548 C  C   . ASN K  1 54  ? -7.219  -35.280 21.915 1.00 27.47  ? 53  ASN K C   1 
ATOM   11549 O  O   . ASN K  1 54  ? -7.157  -35.382 23.140 1.00 24.17  ? 53  ASN K O   1 
ATOM   11550 C  CB  . ASN K  1 54  ? -6.508  -37.729 21.482 1.00 34.47  ? 53  ASN K CB  1 
ATOM   11551 C  CG  . ASN K  1 54  ? -6.797  -38.201 22.892 1.00 40.19  ? 53  ASN K CG  1 
ATOM   11552 O  OD1 . ASN K  1 54  ? -7.940  -38.471 23.250 1.00 39.96  ? 53  ASN K OD1 1 
ATOM   11553 N  ND2 . ASN K  1 54  ? -5.761  -38.319 23.705 1.00 45.57  ? 53  ASN K ND2 1 
ATOM   11554 N  N   . THR K  1 55  ? -7.233  -34.096 21.292 1.00 28.52  ? 54  THR K N   1 
ATOM   11555 C  CA  . THR K  1 55  ? -6.949  -32.857 22.011 1.00 29.44  ? 54  THR K CA  1 
ATOM   11556 C  C   . THR K  1 55  ? -7.961  -32.627 23.129 1.00 28.35  ? 54  THR K C   1 
ATOM   11557 O  O   . THR K  1 55  ? -7.623  -32.047 24.151 1.00 26.19  ? 54  THR K O   1 
ATOM   11558 C  CB  . THR K  1 55  ? -6.910  -31.636 21.086 1.00 29.39  ? 54  THR K CB  1 
ATOM   11559 O  OG1 . THR K  1 55  ? -8.173  -31.565 20.427 1.00 30.43  ? 54  THR K OG1 1 
ATOM   11560 C  CG2 . THR K  1 55  ? -5.804  -31.709 20.057 1.00 29.52  ? 54  THR K CG2 1 
ATOM   11561 N  N   . ALA K  1 56  ? -9.200  -33.073 22.918 1.00 30.85  ? 55  ALA K N   1 
ATOM   11562 C  CA  . ALA K  1 56  ? -10.260 -32.882 23.891 1.00 31.38  ? 55  ALA K CA  1 
ATOM   11563 C  C   . ALA K  1 56  ? -10.823 -34.245 24.278 1.00 32.79  ? 55  ALA K C   1 
ATOM   11564 O  O   . ALA K  1 56  ? -12.036 -34.424 24.347 1.00 34.35  ? 55  ALA K O   1 
ATOM   11565 C  CB  . ALA K  1 56  ? -11.324 -31.994 23.291 1.00 31.89  ? 55  ALA K CB  1 
ATOM   11566 N  N   . GLY K  1 57  ? -9.931  -35.213 24.506 1.00 32.80  ? 56  GLY K N   1 
ATOM   11567 C  CA  . GLY K  1 57  ? -10.338 -36.580 24.785 1.00 32.14  ? 56  GLY K CA  1 
ATOM   11568 C  C   . GLY K  1 57  ? -10.874 -37.258 23.532 1.00 33.51  ? 56  GLY K C   1 
ATOM   11569 O  O   . GLY K  1 57  ? -10.583 -36.841 22.411 1.00 36.13  ? 56  GLY K O   1 
ATOM   11570 N  N   . CYS K  1 58  ? -11.689 -38.299 23.732 1.00 33.73  ? 57  CYS K N   1 
ATOM   11571 C  CA  . CYS K  1 58  ? -12.178 -39.077 22.605 1.00 32.55  ? 57  CYS K CA  1 
ATOM   11572 C  C   . CYS K  1 58  ? -13.170 -38.275 21.769 1.00 31.90  ? 57  CYS K C   1 
ATOM   11573 O  O   . CYS K  1 58  ? -13.351 -38.573 20.598 1.00 30.64  ? 57  CYS K O   1 
ATOM   11574 C  CB  . CYS K  1 58  ? -12.794 -40.377 23.078 1.00 33.40  ? 57  CYS K CB  1 
ATOM   11575 S  SG  . CYS K  1 58  ? -11.566 -41.507 23.782 1.00 38.62  ? 57  CYS K SG  1 
ATOM   11576 N  N   . THR K  1 59  ? -13.783 -37.244 22.368 1.00 31.29  ? 58  THR K N   1 
ATOM   11577 C  CA  . THR K  1 59  ? -14.784 -36.424 21.703 1.00 30.96  ? 58  THR K CA  1 
ATOM   11578 C  C   . THR K  1 59  ? -14.232 -35.841 20.409 1.00 31.19  ? 58  THR K C   1 
ATOM   11579 O  O   . THR K  1 59  ? -14.951 -35.744 19.413 1.00 33.35  ? 58  THR K O   1 
ATOM   11580 C  CB  . THR K  1 59  ? -15.196 -35.212 22.533 1.00 31.68  ? 58  THR K CB  1 
ATOM   11581 O  OG1 . THR K  1 59  ? -15.494 -35.690 23.843 1.00 35.65  ? 58  THR K OG1 1 
ATOM   11582 C  CG2 . THR K  1 59  ? -16.374 -34.464 21.952 1.00 31.86  ? 58  THR K CG2 1 
ATOM   11583 N  N   . SER K  1 60  ? -12.963 -35.429 20.438 1.00 29.69  ? 59  SER K N   1 
ATOM   11584 C  CA  . SER K  1 60  ? -12.438 -34.641 19.337 1.00 28.83  ? 59  SER K CA  1 
ATOM   11585 C  C   . SER K  1 60  ? -12.111 -35.532 18.136 1.00 26.51  ? 59  SER K C   1 
ATOM   11586 O  O   . SER K  1 60  ? -11.672 -35.042 17.099 1.00 25.11  ? 59  SER K O   1 
ATOM   11587 C  CB  . SER K  1 60  ? -11.304 -33.733 19.780 1.00 29.48  ? 59  SER K CB  1 
ATOM   11588 O  OG  . SER K  1 60  ? -10.294 -34.468 20.436 1.00 28.45  ? 59  SER K OG  1 
ATOM   11589 N  N   . ALA K  1 61  ? -12.410 -36.830 18.269 1.00 24.40  ? 60  ALA K N   1 
ATOM   11590 C  CA  . ALA K  1 61  ? -12.199 -37.809 17.214 1.00 24.43  ? 60  ALA K CA  1 
ATOM   11591 C  C   . ALA K  1 61  ? -13.239 -37.626 16.113 1.00 24.54  ? 60  ALA K C   1 
ATOM   11592 O  O   . ALA K  1 61  ? -13.057 -38.116 15.003 1.00 24.01  ? 60  ALA K O   1 
ATOM   11593 C  CB  . ALA K  1 61  ? -12.256 -39.204 17.786 1.00 22.50  ? 60  ALA K CB  1 
ATOM   11594 N  N   . GLY K  1 62  ? -14.330 -36.925 16.444 1.00 23.89  ? 61  GLY K N   1 
ATOM   11595 C  CA  . GLY K  1 62  ? -15.401 -36.662 15.495 1.00 22.86  ? 61  GLY K CA  1 
ATOM   11596 C  C   . GLY K  1 62  ? -16.308 -37.875 15.279 1.00 23.22  ? 61  GLY K C   1 
ATOM   11597 O  O   . GLY K  1 62  ? -16.350 -38.780 16.115 1.00 21.58  ? 61  GLY K O   1 
ATOM   11598 N  N   . PRO K  1 63  ? -17.072 -37.918 14.160 1.00 23.35  ? 62  PRO K N   1 
ATOM   11599 C  CA  . PRO K  1 63  ? -18.079 -38.964 13.929 1.00 23.77  ? 62  PRO K CA  1 
ATOM   11600 C  C   . PRO K  1 63  ? -17.448 -40.253 13.396 1.00 23.43  ? 62  PRO K C   1 
ATOM   11601 O  O   . PRO K  1 63  ? -16.233 -40.292 13.169 1.00 23.92  ? 62  PRO K O   1 
ATOM   11602 C  CB  . PRO K  1 63  ? -18.948 -38.326 12.841 1.00 22.52  ? 62  PRO K CB  1 
ATOM   11603 C  CG  . PRO K  1 63  ? -17.949 -37.536 12.009 1.00 22.91  ? 62  PRO K CG  1 
ATOM   11604 C  CD  . PRO K  1 63  ? -16.996 -36.965 13.040 1.00 22.96  ? 62  PRO K CD  1 
ATOM   11605 N  N   . HIS K  1 64  ? -18.272 -41.296 13.184 1.00 22.39  ? 63  HIS K N   1 
ATOM   11606 C  CA  . HIS K  1 64  ? -17.769 -42.506 12.547 1.00 22.82  ? 63  HIS K CA  1 
ATOM   11607 C  C   . HIS K  1 64  ? -17.167 -42.111 11.203 1.00 23.71  ? 63  HIS K C   1 
ATOM   11608 O  O   . HIS K  1 64  ? -17.765 -41.312 10.481 1.00 26.18  ? 63  HIS K O   1 
ATOM   11609 C  CB  . HIS K  1 64  ? -18.908 -43.533 12.318 1.00 22.80  ? 63  HIS K CB  1 
ATOM   11610 C  CG  . HIS K  1 64  ? -19.528 -44.058 13.569 1.00 23.85  ? 63  HIS K CG  1 
ATOM   11611 N  ND1 . HIS K  1 64  ? -20.640 -44.895 13.545 1.00 23.28  ? 63  HIS K ND1 1 
ATOM   11612 C  CD2 . HIS K  1 64  ? -19.193 -43.901 14.872 1.00 24.68  ? 63  HIS K CD2 1 
ATOM   11613 C  CE1 . HIS K  1 64  ? -20.973 -45.226 14.779 1.00 22.77  ? 63  HIS K CE1 1 
ATOM   11614 N  NE2 . HIS K  1 64  ? -20.102 -44.624 15.614 1.00 24.93  ? 63  HIS K NE2 1 
ATOM   11615 N  N   . PHE K  1 65  ? -15.984 -42.661 10.875 1.00 24.10  ? 64  PHE K N   1 
ATOM   11616 C  CA  . PHE K  1 65  ? -15.333 -42.372 9.606  1.00 25.17  ? 64  PHE K CA  1 
ATOM   11617 C  C   . PHE K  1 65  ? -16.277 -42.744 8.452  1.00 27.57  ? 64  PHE K C   1 
ATOM   11618 O  O   . PHE K  1 65  ? -16.653 -43.917 8.277  1.00 34.39  ? 64  PHE K O   1 
ATOM   11619 C  CB  . PHE K  1 65  ? -14.006 -43.128 9.518  1.00 23.30  ? 64  PHE K CB  1 
ATOM   11620 C  CG  . PHE K  1 65  ? -13.239 -42.919 8.239  1.00 24.01  ? 64  PHE K CG  1 
ATOM   11621 C  CD1 . PHE K  1 65  ? -13.121 -41.658 7.665  1.00 22.11  ? 64  PHE K CD1 1 
ATOM   11622 C  CD2 . PHE K  1 65  ? -12.617 -44.002 7.611  1.00 25.51  ? 64  PHE K CD2 1 
ATOM   11623 C  CE1 . PHE K  1 65  ? -12.415 -41.484 6.483  1.00 22.01  ? 64  PHE K CE1 1 
ATOM   11624 C  CE2 . PHE K  1 65  ? -11.905 -43.821 6.433  1.00 24.90  ? 64  PHE K CE2 1 
ATOM   11625 C  CZ  . PHE K  1 65  ? -11.809 -42.564 5.870  1.00 22.95  ? 64  PHE K CZ  1 
ATOM   11626 N  N   . ASN K  1 66  ? -16.662 -41.741 7.650  1.00 25.86  ? 65  ASN K N   1 
ATOM   11627 C  CA  . ASN K  1 66  ? -17.772 -41.951 6.728  1.00 27.67  ? 65  ASN K CA  1 
ATOM   11628 C  C   . ASN K  1 66  ? -17.470 -41.337 5.357  1.00 29.03  ? 65  ASN K C   1 
ATOM   11629 O  O   . ASN K  1 66  ? -18.251 -40.532 4.848  1.00 29.38  ? 65  ASN K O   1 
ATOM   11630 C  CB  . ASN K  1 66  ? -19.093 -41.461 7.335  1.00 26.11  ? 65  ASN K CB  1 
ATOM   11631 C  CG  . ASN K  1 66  ? -20.297 -41.740 6.451  1.00 26.47  ? 65  ASN K CG  1 
ATOM   11632 O  OD1 . ASN K  1 66  ? -20.265 -42.610 5.590  1.00 26.14  ? 65  ASN K OD1 1 
ATOM   11633 N  ND2 . ASN K  1 66  ? -21.371 -41.003 6.651  1.00 28.02  ? 65  ASN K ND2 1 
ATOM   11634 N  N   . PRO K  1 67  ? -16.374 -41.719 4.661  1.00 28.43  ? 66  PRO K N   1 
ATOM   11635 C  CA  . PRO K  1 67  ? -15.997 -41.036 3.424  1.00 28.38  ? 66  PRO K CA  1 
ATOM   11636 C  C   . PRO K  1 67  ? -17.003 -41.168 2.282  1.00 30.11  ? 66  PRO K C   1 
ATOM   11637 O  O   . PRO K  1 67  ? -16.964 -40.383 1.342  1.00 30.45  ? 66  PRO K O   1 
ATOM   11638 C  CB  . PRO K  1 67  ? -14.670 -41.679 3.023  1.00 27.09  ? 66  PRO K CB  1 
ATOM   11639 C  CG  . PRO K  1 67  ? -14.679 -43.021 3.711  1.00 28.46  ? 66  PRO K CG  1 
ATOM   11640 C  CD  . PRO K  1 67  ? -15.464 -42.818 4.992  1.00 27.46  ? 66  PRO K CD  1 
ATOM   11641 N  N   . LEU K  1 68  ? -17.900 -42.161 2.365  1.00 31.15  ? 67  LEU K N   1 
ATOM   11642 C  CA  . LEU K  1 68  ? -18.831 -42.419 1.272  1.00 30.73  ? 67  LEU K CA  1 
ATOM   11643 C  C   . LEU K  1 68  ? -20.221 -41.851 1.564  1.00 31.35  ? 67  LEU K C   1 
ATOM   11644 O  O   . LEU K  1 68  ? -21.139 -42.079 0.787  1.00 35.19  ? 67  LEU K O   1 
ATOM   11645 C  CB  . LEU K  1 68  ? -18.889 -43.917 0.973  1.00 29.62  ? 67  LEU K CB  1 
ATOM   11646 C  CG  . LEU K  1 68  ? -17.612 -44.507 0.354  1.00 31.74  ? 67  LEU K CG  1 
ATOM   11647 C  CD1 . LEU K  1 68  ? -17.715 -45.979 0.043  1.00 33.84  ? 67  LEU K CD1 1 
ATOM   11648 C  CD2 . LEU K  1 68  ? -17.164 -43.729 -0.867 1.00 31.08  ? 67  LEU K CD2 1 
ATOM   11649 N  N   . SER K  1 69  ? -20.371 -41.134 2.688  1.00 29.56  ? 68  SER K N   1 
ATOM   11650 C  CA  . SER K  1 69  ? -21.605 -40.459 3.068  1.00 27.70  ? 68  SER K CA  1 
ATOM   11651 C  C   . SER K  1 69  ? -22.794 -41.412 3.105  1.00 28.66  ? 68  SER K C   1 
ATOM   11652 O  O   . SER K  1 69  ? -23.808 -41.125 2.478  1.00 29.43  ? 68  SER K O   1 
ATOM   11653 C  CB  . SER K  1 69  ? -21.908 -39.319 2.136  1.00 24.75  ? 68  SER K CB  1 
ATOM   11654 O  OG  . SER K  1 69  ? -20.942 -38.301 2.266  1.00 26.21  ? 68  SER K OG  1 
ATOM   11655 N  N   . ARG K  1 70  ? -22.676 -42.527 3.835  1.00 30.59  ? 69  ARG K N   1 
ATOM   11656 C  CA  . ARG K  1 70  ? -23.773 -43.471 3.982  1.00 34.12  ? 69  ARG K CA  1 
ATOM   11657 C  C   . ARG K  1 70  ? -24.316 -43.397 5.410  1.00 35.59  ? 69  ARG K C   1 
ATOM   11658 O  O   . ARG K  1 70  ? -23.749 -42.704 6.257  1.00 36.63  ? 69  ARG K O   1 
ATOM   11659 C  CB  . ARG K  1 70  ? -23.319 -44.897 3.661  1.00 35.06  ? 69  ARG K CB  1 
ATOM   11660 C  CG  . ARG K  1 70  ? -22.608 -45.048 2.327  1.00 38.35  ? 69  ARG K CG  1 
ATOM   11661 C  CD  . ARG K  1 70  ? -23.498 -45.401 1.143  1.00 44.63  ? 69  ARG K CD  1 
ATOM   11662 N  NE  . ARG K  1 70  ? -22.597 -45.866 0.071  1.00 57.15  ? 69  ARG K NE  1 
ATOM   11663 C  CZ  . ARG K  1 70  ? -22.125 -47.113 -0.084 1.00 64.75  ? 69  ARG K CZ  1 
ATOM   11664 N  NH1 . ARG K  1 70  ? -22.511 -48.063 0.746  1.00 72.04  ? 69  ARG K NH1 1 
ATOM   11665 N  NH2 . ARG K  1 70  ? -21.263 -47.402 -1.043 1.00 58.88  ? 69  ARG K NH2 1 
ATOM   11666 N  N   . LYS K  1 71  ? -25.415 -44.123 5.660  1.00 34.61  ? 70  LYS K N   1 
ATOM   11667 C  CA  . LYS K  1 71  ? -25.998 -44.220 6.987  1.00 36.31  ? 70  LYS K CA  1 
ATOM   11668 C  C   . LYS K  1 71  ? -25.300 -45.341 7.756  1.00 32.64  ? 70  LYS K C   1 
ATOM   11669 O  O   . LYS K  1 71  ? -24.659 -46.202 7.158  1.00 32.27  ? 70  LYS K O   1 
ATOM   11670 C  CB  . LYS K  1 71  ? -27.531 -44.340 6.908  1.00 40.48  ? 70  LYS K CB  1 
ATOM   11671 C  CG  . LYS K  1 71  ? -28.226 -43.242 6.109  1.00 50.72  ? 70  LYS K CG  1 
ATOM   11672 C  CD  . LYS K  1 71  ? -29.588 -42.784 6.631  1.00 59.95  ? 70  LYS K CD  1 
ATOM   11673 C  CE  . LYS K  1 71  ? -29.772 -41.283 6.475  1.00 61.29  ? 70  LYS K CE  1 
ATOM   11674 N  NZ  . LYS K  1 71  ? -31.169 -40.895 6.741  1.00 57.77  ? 70  LYS K NZ  1 
ATOM   11675 N  N   . HIS K  1 72  ? -25.405 -45.303 9.091  1.00 28.11  ? 71  HIS K N   1 
ATOM   11676 C  CA  . HIS K  1 72  ? -24.728 -46.259 9.950  1.00 27.74  ? 71  HIS K CA  1 
ATOM   11677 C  C   . HIS K  1 72  ? -25.324 -47.656 9.779  1.00 27.45  ? 71  HIS K C   1 
ATOM   11678 O  O   . HIS K  1 72  ? -26.536 -47.804 9.665  1.00 27.31  ? 71  HIS K O   1 
ATOM   11679 C  CB  . HIS K  1 72  ? -24.794 -45.779 11.398 1.00 28.15  ? 71  HIS K CB  1 
ATOM   11680 C  CG  . HIS K  1 72  ? -24.229 -46.747 12.378 1.00 29.11  ? 71  HIS K CG  1 
ATOM   11681 N  ND1 . HIS K  1 72  ? -22.874 -46.811 12.680 1.00 31.61  ? 71  HIS K ND1 1 
ATOM   11682 C  CD2 . HIS K  1 72  ? -24.840 -47.690 13.126 1.00 30.51  ? 71  HIS K CD2 1 
ATOM   11683 C  CE1 . HIS K  1 72  ? -22.678 -47.760 13.567 1.00 34.48  ? 71  HIS K CE1 1 
ATOM   11684 N  NE2 . HIS K  1 72  ? -23.875 -48.318 13.854 1.00 32.58  ? 71  HIS K NE2 1 
ATOM   11685 N  N   . GLY K  1 73  ? -24.460 -48.678 9.757  1.00 27.29  ? 72  GLY K N   1 
ATOM   11686 C  CA  . GLY K  1 73  ? -24.894 -50.064 9.700  1.00 26.46  ? 72  GLY K CA  1 
ATOM   11687 C  C   . GLY K  1 73  ? -24.017 -50.964 10.569 1.00 27.74  ? 72  GLY K C   1 
ATOM   11688 O  O   . GLY K  1 73  ? -23.127 -50.476 11.266 1.00 28.57  ? 72  GLY K O   1 
ATOM   11689 N  N   . GLY K  1 74  ? -24.308 -52.269 10.551 1.00 27.86  ? 73  GLY K N   1 
ATOM   11690 C  CA  . GLY K  1 74  ? -23.385 -53.286 11.031 1.00 28.75  ? 73  GLY K CA  1 
ATOM   11691 C  C   . GLY K  1 74  ? -22.326 -53.581 9.965  1.00 28.58  ? 73  GLY K C   1 
ATOM   11692 O  O   . GLY K  1 74  ? -22.525 -53.268 8.799  1.00 26.24  ? 73  GLY K O   1 
ATOM   11693 N  N   . PRO K  1 75  ? -21.171 -54.181 10.325 1.00 32.12  ? 74  PRO K N   1 
ATOM   11694 C  CA  . PRO K  1 75  ? -20.086 -54.402 9.366  1.00 31.93  ? 74  PRO K CA  1 
ATOM   11695 C  C   . PRO K  1 75  ? -20.529 -55.184 8.137  1.00 32.51  ? 74  PRO K C   1 
ATOM   11696 O  O   . PRO K  1 75  ? -19.985 -54.997 7.056  1.00 29.36  ? 74  PRO K O   1 
ATOM   11697 C  CB  . PRO K  1 75  ? -19.016 -55.179 10.148 1.00 31.62  ? 74  PRO K CB  1 
ATOM   11698 C  CG  . PRO K  1 75  ? -19.714 -55.653 11.411 1.00 32.79  ? 74  PRO K CG  1 
ATOM   11699 C  CD  . PRO K  1 75  ? -20.833 -54.667 11.675 1.00 33.77  ? 74  PRO K CD  1 
ATOM   11700 N  N   . LYS K  1 76  ? -21.549 -56.033 8.303  1.00 36.93  ? 75  LYS K N   1 
ATOM   11701 C  CA  . LYS K  1 76  ? -21.954 -56.941 7.239  1.00 36.56  ? 75  LYS K CA  1 
ATOM   11702 C  C   . LYS K  1 76  ? -22.944 -56.283 6.282  1.00 36.25  ? 75  LYS K C   1 
ATOM   11703 O  O   . LYS K  1 76  ? -23.201 -56.843 5.226  1.00 33.28  ? 75  LYS K O   1 
ATOM   11704 C  CB  . LYS K  1 76  ? -22.426 -58.281 7.805  1.00 35.85  ? 75  LYS K CB  1 
ATOM   11705 C  CG  . LYS K  1 76  ? -21.281 -59.221 8.181  0.60 37.18  ? 75  LYS K CG  1 
ATOM   11706 C  CD  . LYS K  1 76  ? -21.516 -60.191 9.356  0.60 37.16  ? 75  LYS K CD  1 
ATOM   11707 C  CE  . LYS K  1 76  ? -20.234 -60.511 10.110 0.60 34.33  ? 75  LYS K CE  1 
ATOM   11708 N  NZ  . LYS K  1 76  ? -20.063 -61.953 10.409 0.60 30.81  ? 75  LYS K NZ  1 
ATOM   11709 N  N   . ASP K  1 77  ? -23.456 -55.094 6.627  1.00 39.88  ? 76  ASP K N   1 
ATOM   11710 C  CA  . ASP K  1 77  ? -24.454 -54.383 5.829  1.00 41.81  ? 76  ASP K CA  1 
ATOM   11711 C  C   . ASP K  1 77  ? -23.792 -53.721 4.626  1.00 47.00  ? 76  ASP K C   1 
ATOM   11712 O  O   . ASP K  1 77  ? -22.621 -53.337 4.691  1.00 52.21  ? 76  ASP K O   1 
ATOM   11713 C  CB  . ASP K  1 77  ? -25.203 -53.344 6.673  1.00 40.57  ? 76  ASP K CB  1 
ATOM   11714 C  CG  . ASP K  1 77  ? -26.126 -53.984 7.694  1.00 40.22  ? 76  ASP K CG  1 
ATOM   11715 O  OD1 . ASP K  1 77  ? -26.643 -55.056 7.398  1.00 41.81  ? 76  ASP K OD1 1 
ATOM   11716 O  OD2 . ASP K  1 77  ? -26.310 -53.409 8.781  1.00 43.36  ? 76  ASP K OD2 1 
ATOM   11717 N  N   . GLU K  1 78  ? -24.539 -53.579 3.526  1.00 49.88  ? 77  GLU K N   1 
ATOM   11718 C  CA  . GLU K  1 78  ? -24.006 -52.808 2.416  1.00 51.13  ? 77  GLU K CA  1 
ATOM   11719 C  C   . GLU K  1 78  ? -24.083 -51.322 2.766  1.00 48.03  ? 77  GLU K C   1 
ATOM   11720 O  O   . GLU K  1 78  ? -23.171 -50.554 2.450  1.00 51.10  ? 77  GLU K O   1 
ATOM   11721 C  CB  . GLU K  1 78  ? -24.644 -53.158 1.074  1.00 59.37  ? 77  GLU K CB  1 
ATOM   11722 C  CG  . GLU K  1 78  ? -23.721 -52.775 -0.084 1.00 75.35  ? 77  GLU K CG  1 
ATOM   11723 C  CD  . GLU K  1 78  ? -24.307 -51.938 -1.217 1.00 89.59  ? 77  GLU K CD  1 
ATOM   11724 O  OE1 . GLU K  1 78  ? -25.367 -52.339 -1.714 1.00 101.81 ? 77  GLU K OE1 1 
ATOM   11725 O  OE2 . GLU K  1 78  ? -23.726 -50.857 -1.572 1.00 88.99  ? 77  GLU K OE2 1 
ATOM   11726 N  N   . GLU K  1 79  ? -25.161 -50.934 3.458  1.00 39.99  ? 78  GLU K N   1 
ATOM   11727 C  CA  . GLU K  1 79  ? -25.325 -49.581 3.962  1.00 37.89  ? 78  GLU K CA  1 
ATOM   11728 C  C   . GLU K  1 79  ? -24.632 -49.450 5.322  1.00 38.13  ? 78  GLU K C   1 
ATOM   11729 O  O   . GLU K  1 79  ? -25.214 -49.774 6.351  1.00 40.30  ? 78  GLU K O   1 
ATOM   11730 C  CB  . GLU K  1 79  ? -26.806 -49.184 3.902  1.00 36.87  ? 78  GLU K CB  1 
ATOM   11731 C  CG  . GLU K  1 79  ? -27.122 -47.726 4.200  1.00 39.07  ? 78  GLU K CG  1 
ATOM   11732 C  CD  . GLU K  1 79  ? -26.694 -46.659 3.190  1.00 43.79  ? 78  GLU K CD  1 
ATOM   11733 O  OE1 . GLU K  1 79  ? -26.192 -47.019 2.092  1.00 47.06  ? 78  GLU K OE1 1 
ATOM   11734 O  OE2 . GLU K  1 79  ? -26.853 -45.453 3.515  1.00 43.20  ? 78  GLU K OE2 1 
ATOM   11735 N  N   . ARG K  1 80  ? -23.369 -48.993 5.295  1.00 33.22  ? 79  ARG K N   1 
ATOM   11736 C  CA  . ARG K  1 80  ? -22.591 -48.753 6.498  1.00 29.69  ? 79  ARG K CA  1 
ATOM   11737 C  C   . ARG K  1 80  ? -21.575 -47.632 6.287  1.00 28.68  ? 79  ARG K C   1 
ATOM   11738 O  O   . ARG K  1 80  ? -21.212 -47.306 5.161  1.00 26.51  ? 79  ARG K O   1 
ATOM   11739 C  CB  . ARG K  1 80  ? -21.820 -50.008 6.906  1.00 29.95  ? 79  ARG K CB  1 
ATOM   11740 C  CG  . ARG K  1 80  ? -20.878 -50.539 5.837  1.00 29.27  ? 79  ARG K CG  1 
ATOM   11741 C  CD  . ARG K  1 80  ? -20.018 -51.651 6.362  1.00 28.38  ? 79  ARG K CD  1 
ATOM   11742 N  NE  . ARG K  1 80  ? -18.776 -51.154 6.948  1.00 28.23  ? 79  ARG K NE  1 
ATOM   11743 C  CZ  . ARG K  1 80  ? -17.727 -51.910 7.267  1.00 27.85  ? 79  ARG K CZ  1 
ATOM   11744 N  NH1 . ARG K  1 80  ? -17.768 -53.214 7.068  1.00 27.70  ? 79  ARG K NH1 1 
ATOM   11745 N  NH2 . ARG K  1 80  ? -16.641 -51.364 7.788  1.00 25.98  ? 79  ARG K NH2 1 
ATOM   11746 N  N   . HIS K  1 81  ? -21.132 -47.054 7.407  1.00 28.31  ? 80  HIS K N   1 
ATOM   11747 C  CA  . HIS K  1 81  ? -19.939 -46.224 7.461  1.00 27.38  ? 80  HIS K CA  1 
ATOM   11748 C  C   . HIS K  1 81  ? -18.720 -47.115 7.272  1.00 25.72  ? 80  HIS K C   1 
ATOM   11749 O  O   . HIS K  1 81  ? -18.718 -48.256 7.738  1.00 25.02  ? 80  HIS K O   1 
ATOM   11750 C  CB  . HIS K  1 81  ? -19.850 -45.536 8.824  1.00 27.15  ? 80  HIS K CB  1 
ATOM   11751 C  CG  . HIS K  1 81  ? -21.023 -44.669 9.135  1.00 26.61  ? 80  HIS K CG  1 
ATOM   11752 N  ND1 . HIS K  1 81  ? -21.525 -44.519 10.417 1.00 25.61  ? 80  HIS K ND1 1 
ATOM   11753 C  CD2 . HIS K  1 81  ? -21.769 -43.883 8.336  1.00 26.63  ? 80  HIS K CD2 1 
ATOM   11754 C  CE1 . HIS K  1 81  ? -22.524 -43.666 10.387 1.00 26.51  ? 80  HIS K CE1 1 
ATOM   11755 N  NE2 . HIS K  1 81  ? -22.704 -43.272 9.124  1.00 28.07  ? 80  HIS K NE2 1 
ATOM   11756 N  N   . VAL K  1 82  ? -17.685 -46.590 6.607  1.00 24.32  ? 81  VAL K N   1 
ATOM   11757 C  CA  . VAL K  1 82  ? -16.433 -47.324 6.494  1.00 22.72  ? 81  VAL K CA  1 
ATOM   11758 C  C   . VAL K  1 82  ? -15.960 -47.743 7.887  1.00 21.56  ? 81  VAL K C   1 
ATOM   11759 O  O   . VAL K  1 82  ? -15.478 -48.853 8.067  1.00 21.76  ? 81  VAL K O   1 
ATOM   11760 C  CB  . VAL K  1 82  ? -15.342 -46.546 5.718  1.00 20.78  ? 81  VAL K CB  1 
ATOM   11761 C  CG1 . VAL K  1 82  ? -13.961 -47.160 5.909  1.00 20.01  ? 81  VAL K CG1 1 
ATOM   11762 C  CG2 . VAL K  1 82  ? -15.674 -46.469 4.241  1.00 19.97  ? 81  VAL K CG2 1 
ATOM   11763 N  N   . GLY K  1 83  ? -16.136 -46.870 8.877  1.00 20.86  ? 82  GLY K N   1 
ATOM   11764 C  CA  . GLY K  1 83  ? -15.607 -47.138 10.201 1.00 21.20  ? 82  GLY K CA  1 
ATOM   11765 C  C   . GLY K  1 83  ? -16.477 -48.069 11.044 1.00 21.76  ? 82  GLY K C   1 
ATOM   11766 O  O   . GLY K  1 83  ? -16.138 -48.311 12.197 1.00 21.63  ? 82  GLY K O   1 
ATOM   11767 N  N   . ASP K  1 84  ? -17.553 -48.607 10.456 1.00 21.98  ? 83  ASP K N   1 
ATOM   11768 C  CA  . ASP K  1 84  ? -18.544 -49.387 11.187 1.00 23.56  ? 83  ASP K CA  1 
ATOM   11769 C  C   . ASP K  1 84  ? -18.070 -50.837 11.361 1.00 24.43  ? 83  ASP K C   1 
ATOM   11770 O  O   . ASP K  1 84  ? -18.239 -51.673 10.476 1.00 23.29  ? 83  ASP K O   1 
ATOM   11771 C  CB  . ASP K  1 84  ? -19.918 -49.311 10.515 1.00 24.70  ? 83  ASP K CB  1 
ATOM   11772 C  CG  . ASP K  1 84  ? -20.649 -47.993 10.737 1.00 24.72  ? 83  ASP K CG  1 
ATOM   11773 O  OD1 . ASP K  1 84  ? -20.261 -47.231 11.658 1.00 25.90  ? 83  ASP K OD1 1 
ATOM   11774 O  OD2 . ASP K  1 84  ? -21.613 -47.731 9.993  1.00 24.29  ? 83  ASP K OD2 1 
ATOM   11775 N  N   . LEU K  1 85  ? -17.487 -51.141 12.528 1.00 24.69  ? 84  LEU K N   1 
ATOM   11776 C  CA  . LEU K  1 85  ? -16.919 -52.459 12.761 1.00 26.36  ? 84  LEU K CA  1 
ATOM   11777 C  C   . LEU K  1 85  ? -17.794 -53.270 13.725 1.00 29.40  ? 84  LEU K C   1 
ATOM   11778 O  O   . LEU K  1 85  ? -17.373 -54.333 14.202 1.00 29.10  ? 84  LEU K O   1 
ATOM   11779 C  CB  . LEU K  1 85  ? -15.502 -52.305 13.318 1.00 23.74  ? 84  LEU K CB  1 
ATOM   11780 C  CG  . LEU K  1 85  ? -14.433 -51.825 12.341 1.00 21.11  ? 84  LEU K CG  1 
ATOM   11781 C  CD1 . LEU K  1 85  ? -13.085 -51.783 13.045 1.00 20.13  ? 84  LEU K CD1 1 
ATOM   11782 C  CD2 . LEU K  1 85  ? -14.405 -52.667 11.052 1.00 19.74  ? 84  LEU K CD2 1 
ATOM   11783 N  N   . GLY K  1 86  ? -19.013 -52.786 14.006 1.00 30.13  ? 85  GLY K N   1 
ATOM   11784 C  CA  . GLY K  1 86  ? -19.956 -53.560 14.795 1.00 30.28  ? 85  GLY K CA  1 
ATOM   11785 C  C   . GLY K  1 86  ? -19.647 -53.565 16.291 1.00 31.44  ? 85  GLY K C   1 
ATOM   11786 O  O   . GLY K  1 86  ? -19.304 -52.521 16.843 1.00 32.46  ? 85  GLY K O   1 
ATOM   11787 N  N   . ASN K  1 87  ? -19.772 -54.735 16.935 1.00 30.61  ? 86  ASN K N   1 
ATOM   11788 C  CA  . ASN K  1 87  ? -19.584 -54.844 18.375 1.00 29.75  ? 86  ASN K CA  1 
ATOM   11789 C  C   . ASN K  1 87  ? -18.419 -55.758 18.728 1.00 28.98  ? 86  ASN K C   1 
ATOM   11790 O  O   . ASN K  1 87  ? -17.995 -56.599 17.935 1.00 27.69  ? 86  ASN K O   1 
ATOM   11791 C  CB  . ASN K  1 87  ? -20.824 -55.390 19.088 1.00 31.20  ? 86  ASN K CB  1 
ATOM   11792 C  CG  . ASN K  1 87  ? -21.976 -54.427 19.031 1.00 31.79  ? 86  ASN K CG  1 
ATOM   11793 O  OD1 . ASN K  1 87  ? -21.997 -53.424 19.734 1.00 34.84  ? 86  ASN K OD1 1 
ATOM   11794 N  ND2 . ASN K  1 87  ? -22.926 -54.719 18.174 1.00 31.43  ? 86  ASN K ND2 1 
ATOM   11795 N  N   . VAL K  1 88  ? -17.903 -55.558 19.944 1.00 28.47  ? 87  VAL K N   1 
ATOM   11796 C  CA  . VAL K  1 88  ? -17.007 -56.507 20.576 1.00 29.74  ? 87  VAL K CA  1 
ATOM   11797 C  C   . VAL K  1 88  ? -17.692 -56.972 21.860 1.00 33.12  ? 87  VAL K C   1 
ATOM   11798 O  O   . VAL K  1 88  ? -18.573 -56.272 22.369 1.00 34.00  ? 87  VAL K O   1 
ATOM   11799 C  CB  . VAL K  1 88  ? -15.613 -55.885 20.815 1.00 25.87  ? 87  VAL K CB  1 
ATOM   11800 C  CG1 . VAL K  1 88  ? -14.974 -55.400 19.523 1.00 23.90  ? 87  VAL K CG1 1 
ATOM   11801 C  CG2 . VAL K  1 88  ? -15.611 -54.776 21.848 1.00 23.48  ? 87  VAL K CG2 1 
ATOM   11802 N  N   . THR K  1 89  ? -17.306 -58.142 22.380 1.00 34.42  ? 88  THR K N   1 
ATOM   11803 C  CA  . THR K  1 89  ? -18.010 -58.696 23.527 1.00 37.19  ? 88  THR K CA  1 
ATOM   11804 C  C   . THR K  1 89  ? -17.074 -58.815 24.718 1.00 35.87  ? 88  THR K C   1 
ATOM   11805 O  O   . THR K  1 89  ? -16.046 -59.459 24.619 1.00 36.26  ? 88  THR K O   1 
ATOM   11806 C  CB  . THR K  1 89  ? -18.588 -60.085 23.214 1.00 38.13  ? 88  THR K CB  1 
ATOM   11807 O  OG1 . THR K  1 89  ? -19.355 -60.037 22.005 1.00 41.93  ? 88  THR K OG1 1 
ATOM   11808 C  CG2 . THR K  1 89  ? -19.396 -60.640 24.370 1.00 35.95  ? 88  THR K CG2 1 
ATOM   11809 N  N   . ALA K  1 90  ? -17.455 -58.219 25.845 1.00 38.64  ? 89  ALA K N   1 
ATOM   11810 C  CA  . ALA K  1 90  ? -16.695 -58.376 27.080 1.00 41.27  ? 89  ALA K CA  1 
ATOM   11811 C  C   . ALA K  1 90  ? -17.289 -59.506 27.921 1.00 45.73  ? 89  ALA K C   1 
ATOM   11812 O  O   . ALA K  1 90  ? -18.508 -59.569 28.124 1.00 50.21  ? 89  ALA K O   1 
ATOM   11813 C  CB  . ALA K  1 90  ? -16.682 -57.075 27.841 1.00 38.26  ? 89  ALA K CB  1 
ATOM   11814 N  N   . ASP K  1 91  ? -16.402 -60.383 28.422 1.00 48.45  ? 90  ASP K N   1 
ATOM   11815 C  CA  . ASP K  1 91  ? -16.755 -61.513 29.270 1.00 48.27  ? 90  ASP K CA  1 
ATOM   11816 C  C   . ASP K  1 91  ? -17.044 -61.020 30.689 1.00 45.90  ? 90  ASP K C   1 
ATOM   11817 O  O   . ASP K  1 91  ? -16.971 -59.821 30.950 1.00 40.79  ? 90  ASP K O   1 
ATOM   11818 C  CB  . ASP K  1 91  ? -15.670 -62.596 29.231 1.00 52.44  ? 90  ASP K CB  1 
ATOM   11819 C  CG  . ASP K  1 91  ? -14.310 -62.193 29.801 1.00 54.29  ? 90  ASP K CG  1 
ATOM   11820 O  OD1 . ASP K  1 91  ? -14.239 -61.232 30.610 1.00 51.83  ? 90  ASP K OD1 1 
ATOM   11821 O  OD2 . ASP K  1 91  ? -13.317 -62.852 29.431 1.00 51.23  ? 90  ASP K OD2 1 
ATOM   11822 N  N   . LYS K  1 92  ? -17.358 -61.954 31.600 1.00 42.66  ? 91  LYS K N   1 
ATOM   11823 C  CA  . LYS K  1 92  ? -17.754 -61.618 32.961 1.00 42.22  ? 91  LYS K CA  1 
ATOM   11824 C  C   . LYS K  1 92  ? -16.655 -60.853 33.692 1.00 45.20  ? 91  LYS K C   1 
ATOM   11825 O  O   . LYS K  1 92  ? -16.930 -60.219 34.701 1.00 48.25  ? 91  LYS K O   1 
ATOM   11826 C  CB  . LYS K  1 92  ? -18.210 -62.846 33.762 0.20 39.68  ? 91  LYS K CB  1 
ATOM   11827 C  CG  . LYS K  1 92  ? -17.140 -63.880 34.093 0.20 36.94  ? 91  LYS K CG  1 
ATOM   11828 C  CD  . LYS K  1 92  ? -17.668 -65.249 34.428 0.20 35.06  ? 91  LYS K CD  1 
ATOM   11829 C  CE  . LYS K  1 92  ? -16.657 -66.321 34.096 0.20 33.82  ? 91  LYS K CE  1 
ATOM   11830 N  NZ  . LYS K  1 92  ? -16.685 -67.418 35.088 0.20 33.63  ? 91  LYS K NZ  1 
ATOM   11831 N  N   . ASP K  1 93  ? -15.417 -60.925 33.183 1.00 49.32  ? 92  ASP K N   1 
ATOM   11832 C  CA  . ASP K  1 93  ? -14.269 -60.296 33.823 1.00 51.15  ? 92  ASP K CA  1 
ATOM   11833 C  C   . ASP K  1 93  ? -13.997 -58.921 33.227 1.00 50.57  ? 92  ASP K C   1 
ATOM   11834 O  O   . ASP K  1 93  ? -13.062 -58.242 33.643 1.00 48.61  ? 92  ASP K O   1 
ATOM   11835 C  CB  . ASP K  1 93  ? -13.008 -61.148 33.664 1.00 56.05  ? 92  ASP K CB  1 
ATOM   11836 C  CG  . ASP K  1 93  ? -13.096 -62.469 34.398 1.00 54.26  ? 92  ASP K CG  1 
ATOM   11837 O  OD1 . ASP K  1 93  ? -13.576 -62.467 35.544 1.00 52.59  ? 92  ASP K OD1 1 
ATOM   11838 O  OD2 . ASP K  1 93  ? -12.658 -63.481 33.838 1.00 56.92  ? 92  ASP K OD2 1 
ATOM   11839 N  N   . GLY K  1 94  ? -14.792 -58.530 32.228 1.00 51.41  ? 93  GLY K N   1 
ATOM   11840 C  CA  . GLY K  1 94  ? -14.635 -57.223 31.612 1.00 47.97  ? 93  GLY K CA  1 
ATOM   11841 C  C   . GLY K  1 94  ? -13.544 -57.222 30.546 1.00 46.86  ? 93  GLY K C   1 
ATOM   11842 O  O   . GLY K  1 94  ? -13.012 -56.162 30.215 1.00 45.13  ? 93  GLY K O   1 
ATOM   11843 N  N   . VAL K  1 95  ? -13.236 -58.412 30.006 1.00 37.80  ? 94  VAL K N   1 
ATOM   11844 C  CA  . VAL K  1 95  ? -12.235 -58.515 28.962 1.00 36.66  ? 94  VAL K CA  1 
ATOM   11845 C  C   . VAL K  1 95  ? -12.896 -58.884 27.638 1.00 37.56  ? 94  VAL K C   1 
ATOM   11846 O  O   . VAL K  1 95  ? -13.647 -59.847 27.566 1.00 41.15  ? 94  VAL K O   1 
ATOM   11847 C  CB  . VAL K  1 95  ? -11.127 -59.516 29.339 1.00 34.35  ? 94  VAL K CB  1 
ATOM   11848 C  CG1 . VAL K  1 95  ? -10.127 -59.719 28.194 1.00 33.05  ? 94  VAL K CG1 1 
ATOM   11849 C  CG2 . VAL K  1 95  ? -10.417 -59.093 30.617 1.00 31.53  ? 94  VAL K CG2 1 
ATOM   11850 N  N   . ALA K  1 96  ? -12.600 -58.109 26.596 1.00 36.96  ? 95  ALA K N   1 
ATOM   11851 C  CA  . ALA K  1 96  ? -13.070 -58.431 25.261 1.00 37.25  ? 95  ALA K CA  1 
ATOM   11852 C  C   . ALA K  1 96  ? -11.919 -58.951 24.417 1.00 36.37  ? 95  ALA K C   1 
ATOM   11853 O  O   . ALA K  1 96  ? -10.966 -58.211 24.184 1.00 44.76  ? 95  ALA K O   1 
ATOM   11854 C  CB  . ALA K  1 96  ? -13.682 -57.205 24.624 1.00 35.82  ? 95  ALA K CB  1 
ATOM   11855 N  N   A ASP K  1 97  ? -11.990 -60.209 23.980 0.50 34.21  ? 96  ASP K N   1 
ATOM   11856 N  N   B ASP K  1 97  ? -12.041 -60.232 24.028 0.50 33.06  ? 96  ASP K N   1 
ATOM   11857 C  CA  A ASP K  1 97  ? -10.970 -60.715 23.066 0.50 32.34  ? 96  ASP K CA  1 
ATOM   11858 C  CA  B ASP K  1 97  ? -11.273 -60.847 22.957 0.50 30.44  ? 96  ASP K CA  1 
ATOM   11859 C  C   A ASP K  1 97  ? -11.412 -60.429 21.636 0.50 30.75  ? 96  ASP K C   1 
ATOM   11860 C  C   B ASP K  1 97  ? -11.763 -60.202 21.671 0.50 29.17  ? 96  ASP K C   1 
ATOM   11861 O  O   A ASP K  1 97  ? -12.175 -61.178 21.060 0.50 32.97  ? 96  ASP K O   1 
ATOM   11862 O  O   B ASP K  1 97  ? -12.889 -60.453 21.244 0.50 29.73  ? 96  ASP K O   1 
ATOM   11863 C  CB  A ASP K  1 97  ? -10.613 -62.188 23.310 0.50 31.85  ? 96  ASP K CB  1 
ATOM   11864 C  CB  B ASP K  1 97  ? -11.463 -62.376 22.918 0.50 29.18  ? 96  ASP K CB  1 
ATOM   11865 C  CG  A ASP K  1 97  ? -9.927  -62.409 24.653 0.50 30.29  ? 96  ASP K CG  1 
ATOM   11866 C  CG  B ASP K  1 97  ? -10.504 -63.180 22.033 0.50 27.78  ? 96  ASP K CG  1 
ATOM   11867 O  OD1 A ASP K  1 97  ? -8.943  -61.677 24.979 0.50 28.84  ? 96  ASP K OD1 1 
ATOM   11868 O  OD1 B ASP K  1 97  ? -10.054 -62.662 20.983 0.50 26.74  ? 96  ASP K OD1 1 
ATOM   11869 O  OD2 A ASP K  1 97  ? -10.400 -63.283 25.388 0.50 29.33  ? 96  ASP K OD2 1 
ATOM   11870 O  OD2 B ASP K  1 97  ? -10.223 -64.339 22.394 0.50 25.96  ? 96  ASP K OD2 1 
ATOM   11871 N  N   . VAL K  1 98  ? -10.948 -59.319 21.092 1.00 28.15  ? 97  VAL K N   1 
ATOM   11872 C  CA  . VAL K  1 98  ? -11.386 -58.847 19.792 1.00 26.00  ? 97  VAL K CA  1 
ATOM   11873 C  C   . VAL K  1 98  ? -10.766 -59.684 18.683 1.00 25.63  ? 97  VAL K C   1 
ATOM   11874 O  O   . VAL K  1 98  ? -9.569  -59.951 18.700 1.00 26.79  ? 97  VAL K O   1 
ATOM   11875 C  CB  . VAL K  1 98  ? -11.068 -57.361 19.608 1.00 26.07  ? 97  VAL K CB  1 
ATOM   11876 C  CG1 . VAL K  1 98  ? -11.571 -56.856 18.261 1.00 26.38  ? 97  VAL K CG1 1 
ATOM   11877 C  CG2 . VAL K  1 98  ? -11.576 -56.531 20.774 1.00 26.60  ? 97  VAL K CG2 1 
ATOM   11878 N  N   . SER K  1 99  ? -11.590 -60.064 17.710 1.00 26.06  ? 98  SER K N   1 
ATOM   11879 C  CA  . SER K  1 99  ? -11.093 -60.724 16.515 1.00 27.99  ? 98  SER K CA  1 
ATOM   11880 C  C   . SER K  1 99  ? -12.093 -60.564 15.377 1.00 28.37  ? 98  SER K C   1 
ATOM   11881 O  O   . SER K  1 99  ? -13.185 -61.123 15.436 1.00 31.70  ? 98  SER K O   1 
ATOM   11882 C  CB  . SER K  1 99  ? -10.829 -62.183 16.804 1.00 28.47  ? 98  SER K CB  1 
ATOM   11883 O  OG  . SER K  1 99  ? -10.386 -62.820 15.628 1.00 33.48  ? 98  SER K OG  1 
ATOM   11884 N  N   . ILE K  1 100 ? -11.739 -59.770 14.371 1.00 26.51  ? 99  ILE K N   1 
ATOM   11885 C  CA  . ILE K  1 100 ? -12.679 -59.346 13.338 1.00 26.45  ? 99  ILE K CA  1 
ATOM   11886 C  C   . ILE K  1 100 ? -11.945 -59.385 12.010 1.00 28.20  ? 99  ILE K C   1 
ATOM   11887 O  O   . ILE K  1 100 ? -10.735 -59.163 11.958 1.00 32.51  ? 99  ILE K O   1 
ATOM   11888 C  CB  . ILE K  1 100 ? -13.211 -57.921 13.620 1.00 24.14  ? 99  ILE K CB  1 
ATOM   11889 C  CG1 . ILE K  1 100 ? -14.230 -57.904 14.753 1.00 22.64  ? 99  ILE K CG1 1 
ATOM   11890 C  CG2 . ILE K  1 100 ? -13.747 -57.247 12.373 1.00 23.15  ? 99  ILE K CG2 1 
ATOM   11891 C  CD1 . ILE K  1 100 ? -14.519 -56.522 15.276 1.00 23.25  ? 99  ILE K CD1 1 
ATOM   11892 N  N   . GLU K  1 101 ? -12.681 -59.615 10.929 1.00 28.17  ? 100 GLU K N   1 
ATOM   11893 C  CA  . GLU K  1 101 ? -12.104 -59.442 9.615  1.00 30.97  ? 100 GLU K CA  1 
ATOM   11894 C  C   . GLU K  1 101 ? -13.026 -58.523 8.829  1.00 32.82  ? 100 GLU K C   1 
ATOM   11895 O  O   . GLU K  1 101 ? -14.233 -58.694 8.851  1.00 37.11  ? 100 GLU K O   1 
ATOM   11896 C  CB  . GLU K  1 101 ? -11.901 -60.820 8.989  1.00 31.84  ? 100 GLU K CB  1 
ATOM   11897 C  CG  . GLU K  1 101 ? -11.539 -60.782 7.516  1.00 38.93  ? 100 GLU K CG  1 
ATOM   11898 C  CD  . GLU K  1 101 ? -10.765 -62.027 7.073  1.00 45.56  ? 100 GLU K CD  1 
ATOM   11899 O  OE1 . GLU K  1 101 ? -10.004 -62.604 7.904  1.00 48.71  ? 100 GLU K OE1 1 
ATOM   11900 O  OE2 . GLU K  1 101 ? -10.880 -62.382 5.873  1.00 48.21  ? 100 GLU K OE2 1 
ATOM   11901 N  N   . ASP K  1 102 ? -12.461 -57.511 8.178  1.00 33.13  ? 101 ASP K N   1 
ATOM   11902 C  CA  . ASP K  1 102 ? -13.286 -56.541 7.487  1.00 31.70  ? 101 ASP K CA  1 
ATOM   11903 C  C   . ASP K  1 102 ? -12.676 -56.243 6.128  1.00 30.46  ? 101 ASP K C   1 
ATOM   11904 O  O   . ASP K  1 102 ? -11.460 -56.185 6.008  1.00 27.20  ? 101 ASP K O   1 
ATOM   11905 C  CB  . ASP K  1 102 ? -13.439 -55.259 8.315  1.00 31.71  ? 101 ASP K CB  1 
ATOM   11906 C  CG  . ASP K  1 102 ? -14.556 -54.392 7.774  1.00 32.51  ? 101 ASP K CG  1 
ATOM   11907 O  OD1 . ASP K  1 102 ? -15.718 -54.828 7.913  1.00 32.42  ? 101 ASP K OD1 1 
ATOM   11908 O  OD2 . ASP K  1 102 ? -14.263 -53.327 7.184  1.00 32.67  ? 101 ASP K OD2 1 
ATOM   11909 N  N   . SER K  1 103 ? -13.532 -56.031 5.128  1.00 33.79  ? 102 SER K N   1 
ATOM   11910 C  CA  . SER K  1 103 ? -13.046 -55.787 3.779  1.00 38.31  ? 102 SER K CA  1 
ATOM   11911 C  C   . SER K  1 103 ? -13.338 -54.364 3.312  1.00 38.89  ? 102 SER K C   1 
ATOM   11912 O  O   . SER K  1 103 ? -13.092 -54.027 2.156  1.00 42.29  ? 102 SER K O   1 
ATOM   11913 C  CB  . SER K  1 103 ? -13.572 -56.803 2.822  1.00 39.54  ? 102 SER K CB  1 
ATOM   11914 O  OG  . SER K  1 103 ? -12.675 -57.909 2.804  1.00 47.43  ? 102 SER K OG  1 
ATOM   11915 N  N   . VAL K  1 104 ? -13.863 -53.535 4.217  1.00 34.53  ? 103 VAL K N   1 
ATOM   11916 C  CA  . VAL K  1 104 ? -14.268 -52.192 3.837  1.00 31.01  ? 103 VAL K CA  1 
ATOM   11917 C  C   . VAL K  1 104 ? -13.196 -51.210 4.298  1.00 30.47  ? 103 VAL K C   1 
ATOM   11918 O  O   . VAL K  1 104 ? -12.810 -50.327 3.545  1.00 30.38  ? 103 VAL K O   1 
ATOM   11919 C  CB  . VAL K  1 104 ? -15.674 -51.833 4.364  1.00 29.48  ? 103 VAL K CB  1 
ATOM   11920 C  CG1 . VAL K  1 104 ? -16.015 -50.359 4.157  1.00 28.82  ? 103 VAL K CG1 1 
ATOM   11921 C  CG2 . VAL K  1 104 ? -16.732 -52.727 3.745  1.00 27.59  ? 103 VAL K CG2 1 
ATOM   11922 N  N   . ILE K  1 105 ? -12.735 -51.363 5.544  1.00 29.64  ? 104 ILE K N   1 
ATOM   11923 C  CA  . ILE K  1 105 ? -11.588 -50.589 5.988  1.00 27.26  ? 104 ILE K CA  1 
ATOM   11924 C  C   . ILE K  1 105 ? -10.374 -51.058 5.180  1.00 28.38  ? 104 ILE K C   1 
ATOM   11925 O  O   . ILE K  1 105 ? -10.377 -52.150 4.622  1.00 26.97  ? 104 ILE K O   1 
ATOM   11926 C  CB  . ILE K  1 105 ? -11.353 -50.729 7.502  1.00 24.71  ? 104 ILE K CB  1 
ATOM   11927 C  CG1 . ILE K  1 105 ? -11.005 -52.170 7.890  1.00 23.63  ? 104 ILE K CG1 1 
ATOM   11928 C  CG2 . ILE K  1 105 ? -12.549 -50.191 8.276  1.00 24.40  ? 104 ILE K CG2 1 
ATOM   11929 C  CD1 . ILE K  1 105 ? -10.520 -52.344 9.292  1.00 24.96  ? 104 ILE K CD1 1 
ATOM   11930 N  N   . SER K  1 106 ? -9.353  -50.206 5.098  1.00 31.07  ? 105 SER K N   1 
ATOM   11931 C  CA  . SER K  1 106 ? -8.105  -50.570 4.453  1.00 32.12  ? 105 SER K CA  1 
ATOM   11932 C  C   . SER K  1 106 ? -6.933  -49.902 5.168  1.00 32.01  ? 105 SER K C   1 
ATOM   11933 O  O   . SER K  1 106 ? -7.105  -48.912 5.893  1.00 30.66  ? 105 SER K O   1 
ATOM   11934 C  CB  . SER K  1 106 ? -8.114  -50.162 3.005  1.00 32.28  ? 105 SER K CB  1 
ATOM   11935 O  OG  . SER K  1 106 ? -7.041  -50.806 2.329  1.00 36.86  ? 105 SER K OG  1 
ATOM   11936 N  N   . LEU K  1 107 ? -5.741  -50.496 4.975  1.00 33.24  ? 106 LEU K N   1 
ATOM   11937 C  CA  . LEU K  1 107 ? -4.530  -49.872 5.484  1.00 34.95  ? 106 LEU K CA  1 
ATOM   11938 C  C   . LEU K  1 107 ? -3.733  -49.242 4.339  1.00 38.49  ? 106 LEU K C   1 
ATOM   11939 O  O   . LEU K  1 107 ? -2.613  -48.806 4.544  1.00 42.42  ? 106 LEU K O   1 
ATOM   11940 C  CB  . LEU K  1 107 ? -3.705  -50.903 6.253  1.00 31.01  ? 106 LEU K CB  1 
ATOM   11941 C  CG  . LEU K  1 107 ? -4.431  -51.643 7.377  1.00 28.66  ? 106 LEU K CG  1 
ATOM   11942 C  CD1 . LEU K  1 107 ? -3.454  -52.581 8.109  1.00 30.16  ? 106 LEU K CD1 1 
ATOM   11943 C  CD2 . LEU K  1 107 ? -5.076  -50.661 8.332  1.00 25.68  ? 106 LEU K CD2 1 
ATOM   11944 N  N   . SER K  1 108 ? -4.330  -49.158 3.138  1.00 40.60  ? 107 SER K N   1 
ATOM   11945 C  CA  . SER K  1 108 ? -3.740  -48.431 2.021  1.00 45.83  ? 107 SER K CA  1 
ATOM   11946 C  C   . SER K  1 108 ? -4.819  -48.069 1.008  1.00 48.93  ? 107 SER K C   1 
ATOM   11947 O  O   . SER K  1 108 ? -5.917  -48.614 1.036  1.00 58.63  ? 107 SER K O   1 
ATOM   11948 C  CB  . SER K  1 108 ? -2.611  -49.183 1.375  1.00 50.16  ? 107 SER K CB  1 
ATOM   11949 O  OG  . SER K  1 108 ? -3.087  -50.388 0.813  1.00 54.33  ? 107 SER K OG  1 
ATOM   11950 N  N   . GLY K  1 109 ? -4.547  -47.050 0.173  1.00 50.06  ? 108 GLY K N   1 
ATOM   11951 C  CA  . GLY K  1 109 ? -5.559  -46.500 -0.708 1.00 50.87  ? 108 GLY K CA  1 
ATOM   11952 C  C   . GLY K  1 109 ? -6.354  -45.417 0.030  1.00 49.82  ? 108 GLY K C   1 
ATOM   11953 O  O   . GLY K  1 109 ? -5.983  -44.986 1.133  1.00 45.32  ? 108 GLY K O   1 
ATOM   11954 N  N   . ASP K  1 110 ? -7.362  -44.882 -0.656 1.00 50.10  ? 109 ASP K N   1 
ATOM   11955 C  CA  . ASP K  1 110 ? -7.813  -43.506 -0.449 1.00 53.16  ? 109 ASP K CA  1 
ATOM   11956 C  C   . ASP K  1 110 ? -8.454  -43.340 0.932  1.00 53.12  ? 109 ASP K C   1 
ATOM   11957 O  O   . ASP K  1 110 ? -8.419  -42.261 1.530  1.00 63.22  ? 109 ASP K O   1 
ATOM   11958 C  CB  . ASP K  1 110 ? -8.771  -43.023 -1.532 1.00 55.17  ? 109 ASP K CB  1 
ATOM   11959 C  CG  . ASP K  1 110 ? -8.282  -43.225 -2.949 1.00 60.99  ? 109 ASP K CG  1 
ATOM   11960 O  OD1 . ASP K  1 110 ? -7.162  -42.812 -3.215 1.00 74.19  ? 109 ASP K OD1 1 
ATOM   11961 O  OD2 . ASP K  1 110 ? -9.018  -43.812 -3.756 1.00 62.31  ? 109 ASP K OD2 1 
ATOM   11962 N  N   . HIS K  1 111 ? -9.074  -44.401 1.435  1.00 44.54  ? 110 HIS K N   1 
ATOM   11963 C  CA  . HIS K  1 111 ? -9.871  -44.220 2.634  1.00 49.64  ? 110 HIS K CA  1 
ATOM   11964 C  C   . HIS K  1 111 ? -9.224  -45.008 3.771  1.00 48.39  ? 110 HIS K C   1 
ATOM   11965 O  O   . HIS K  1 111 ? -9.941  -45.604 4.606  1.00 49.04  ? 110 HIS K O   1 
ATOM   11966 C  CB  . HIS K  1 111 ? -11.368 -44.531 2.390  1.00 56.48  ? 110 HIS K CB  1 
ATOM   11967 C  CG  . HIS K  1 111 ? -11.977 -43.780 1.245  1.00 57.57  ? 110 HIS K CG  1 
ATOM   11968 N  ND1 . HIS K  1 111 ? -12.890 -44.320 0.310  1.00 55.43  ? 110 HIS K ND1 1 
ATOM   11969 C  CD2 . HIS K  1 111 ? -11.759 -42.501 0.862  1.00 51.88  ? 110 HIS K CD2 1 
ATOM   11970 C  CE1 . HIS K  1 111 ? -13.136 -43.396 -0.598 1.00 53.65  ? 110 HIS K CE1 1 
ATOM   11971 N  NE2 . HIS K  1 111 ? -12.448 -42.269 -0.293 1.00 49.56  ? 110 HIS K NE2 1 
ATOM   11972 N  N   . CYS K  1 112 ? -7.888  -44.992 3.809  1.00 41.20  ? 111 CYS K N   1 
ATOM   11973 C  CA  . CYS K  1 112 ? -7.213  -45.740 4.854  1.00 37.12  ? 111 CYS K CA  1 
ATOM   11974 C  C   . CYS K  1 112 ? -7.538  -45.180 6.229  1.00 33.20  ? 111 CYS K C   1 
ATOM   11975 O  O   . CYS K  1 112 ? -7.638  -43.978 6.385  1.00 30.14  ? 111 CYS K O   1 
ATOM   11976 C  CB  . CYS K  1 112 ? -5.780  -46.171 4.612  1.00 41.56  ? 111 CYS K CB  1 
ATOM   11977 S  SG  . CYS K  1 112 ? -4.351  -45.046 4.853  1.00 40.28  ? 111 CYS K SG  1 
ATOM   11978 N  N   . ILE K  1 113 ? -7.345  -46.008 7.243  1.00 32.69  ? 112 ILE K N   1 
ATOM   11979 C  CA  . ILE K  1 113 ? -7.714  -45.660 8.617  1.00 30.67  ? 112 ILE K CA  1 
ATOM   11980 C  C   . ILE K  1 113 ? -6.482  -45.234 9.418  1.00 30.44  ? 112 ILE K C   1 
ATOM   11981 O  O   . ILE K  1 113 ? -6.634  -44.883 10.570 1.00 30.84  ? 112 ILE K O   1 
ATOM   11982 C  CB  . ILE K  1 113 ? -8.471  -46.805 9.315  1.00 29.06  ? 112 ILE K CB  1 
ATOM   11983 C  CG1 . ILE K  1 113 ? -7.686  -48.116 9.275  1.00 28.21  ? 112 ILE K CG1 1 
ATOM   11984 C  CG2 . ILE K  1 113 ? -9.898  -46.936 8.789  1.00 27.84  ? 112 ILE K CG2 1 
ATOM   11985 C  CD1 . ILE K  1 113 ? -8.122  -49.101 10.351 1.00 30.07  ? 112 ILE K CD1 1 
ATOM   11986 N  N   . ILE K  1 114 ? -5.315  -45.225 8.781  1.00 28.20  ? 113 ILE K N   1 
ATOM   11987 C  CA  . ILE K  1 114 ? -4.100  -44.785 9.444  1.00 28.24  ? 113 ILE K CA  1 
ATOM   11988 C  C   . ILE K  1 114 ? -4.249  -43.317 9.819  1.00 29.00  ? 113 ILE K C   1 
ATOM   11989 O  O   . ILE K  1 114 ? -4.694  -42.512 8.993  1.00 30.06  ? 113 ILE K O   1 
ATOM   11990 C  CB  . ILE K  1 114 ? -2.849  -44.973 8.563  1.00 26.95  ? 113 ILE K CB  1 
ATOM   11991 C  CG1 . ILE K  1 114 ? -2.807  -46.340 7.877  1.00 28.04  ? 113 ILE K CG1 1 
ATOM   11992 C  CG2 . ILE K  1 114 ? -1.597  -44.586 9.345  1.00 25.07  ? 113 ILE K CG2 1 
ATOM   11993 C  CD1 . ILE K  1 114 ? -1.401  -46.989 7.864  1.00 29.28  ? 113 ILE K CD1 1 
ATOM   11994 N  N   . GLY K  1 115 ? -3.914  -43.012 11.081 1.00 28.37  ? 114 GLY K N   1 
ATOM   11995 C  CA  . GLY K  1 115 ? -3.940  -41.650 11.573 1.00 27.37  ? 114 GLY K CA  1 
ATOM   11996 C  C   . GLY K  1 115 ? -5.348  -41.182 11.939 1.00 27.75  ? 114 GLY K C   1 
ATOM   11997 O  O   . GLY K  1 115 ? -5.566  -39.992 12.140 1.00 30.41  ? 114 GLY K O   1 
ATOM   11998 N  N   . ARG K  1 116 ? -6.286  -42.133 12.029 1.00 25.17  ? 115 ARG K N   1 
ATOM   11999 C  CA  . ARG K  1 116 ? -7.631  -41.880 12.520 1.00 21.47  ? 115 ARG K CA  1 
ATOM   12000 C  C   . ARG K  1 116 ? -7.778  -42.512 13.907 1.00 20.83  ? 115 ARG K C   1 
ATOM   12001 O  O   . ARG K  1 116 ? -6.785  -42.958 14.482 1.00 20.65  ? 115 ARG K O   1 
ATOM   12002 C  CB  . ARG K  1 116 ? -8.654  -42.315 11.470 1.00 21.30  ? 115 ARG K CB  1 
ATOM   12003 C  CG  . ARG K  1 116 ? -8.351  -41.725 10.099 1.00 20.54  ? 115 ARG K CG  1 
ATOM   12004 C  CD  . ARG K  1 116 ? -9.498  -41.973 9.108  1.00 21.30  ? 115 ARG K CD  1 
ATOM   12005 N  NE  . ARG K  1 116 ? -9.218  -41.381 7.802  1.00 21.84  ? 115 ARG K NE  1 
ATOM   12006 C  CZ  . ARG K  1 116 ? -9.509  -40.134 7.438  1.00 22.98  ? 115 ARG K CZ  1 
ATOM   12007 N  NH1 . ARG K  1 116 ? -10.113 -39.314 8.283  1.00 23.46  ? 115 ARG K NH1 1 
ATOM   12008 N  NH2 . ARG K  1 116 ? -9.196  -39.717 6.219  1.00 21.14  ? 115 ARG K NH2 1 
ATOM   12009 N  N   . THR K  1 117 ? -8.995  -42.518 14.464 1.00 21.42  ? 116 THR K N   1 
ATOM   12010 C  CA  . THR K  1 117 ? -9.167  -43.016 15.822 1.00 21.95  ? 116 THR K CA  1 
ATOM   12011 C  C   . THR K  1 117 ? -10.033 -44.269 15.857 1.00 22.11  ? 116 THR K C   1 
ATOM   12012 O  O   . THR K  1 117 ? -11.042 -44.371 15.168 1.00 23.00  ? 116 THR K O   1 
ATOM   12013 C  CB  . THR K  1 117 ? -9.756  -41.946 16.750 1.00 21.79  ? 116 THR K CB  1 
ATOM   12014 O  OG1 . THR K  1 117 ? -8.805  -40.889 16.799 1.00 22.71  ? 116 THR K OG1 1 
ATOM   12015 C  CG2 . THR K  1 117 ? -9.990  -42.446 18.153 1.00 21.02  ? 116 THR K CG2 1 
ATOM   12016 N  N   . LEU K  1 118 ? -9.635  -45.215 16.702 1.00 21.44  ? 117 LEU K N   1 
ATOM   12017 C  CA  . LEU K  1 118 ? -10.485 -46.347 17.016 1.00 20.88  ? 117 LEU K CA  1 
ATOM   12018 C  C   . LEU K  1 118 ? -11.109 -46.068 18.379 1.00 21.51  ? 117 LEU K C   1 
ATOM   12019 O  O   . LEU K  1 118 ? -10.415 -45.636 19.299 1.00 20.82  ? 117 LEU K O   1 
ATOM   12020 C  CB  . LEU K  1 118 ? -9.598  -47.593 17.046 1.00 20.14  ? 117 LEU K CB  1 
ATOM   12021 C  CG  . LEU K  1 118 ? -10.312 -48.883 17.429 1.00 20.88  ? 117 LEU K CG  1 
ATOM   12022 C  CD1 . LEU K  1 118 ? -11.338 -49.272 16.388 1.00 20.30  ? 117 LEU K CD1 1 
ATOM   12023 C  CD2 . LEU K  1 118 ? -9.320  -50.006 17.644 1.00 21.28  ? 117 LEU K CD2 1 
ATOM   12024 N  N   . VAL K  1 119 ? -12.421 -46.295 18.493 1.00 20.97  ? 118 VAL K N   1 
ATOM   12025 C  CA  . VAL K  1 119 ? -13.151 -46.007 19.722 1.00 21.41  ? 118 VAL K CA  1 
ATOM   12026 C  C   . VAL K  1 119 ? -13.955 -47.229 20.145 1.00 22.20  ? 118 VAL K C   1 
ATOM   12027 O  O   . VAL K  1 119 ? -14.635 -47.847 19.336 1.00 22.53  ? 118 VAL K O   1 
ATOM   12028 C  CB  . VAL K  1 119 ? -14.099 -44.798 19.571 1.00 21.14  ? 118 VAL K CB  1 
ATOM   12029 C  CG1 . VAL K  1 119 ? -14.827 -44.493 20.867 1.00 21.43  ? 118 VAL K CG1 1 
ATOM   12030 C  CG2 . VAL K  1 119 ? -13.404 -43.557 19.043 1.00 20.34  ? 118 VAL K CG2 1 
ATOM   12031 N  N   . VAL K  1 120 ? -13.897 -47.533 21.442 1.00 23.80  ? 119 VAL K N   1 
ATOM   12032 C  CA  . VAL K  1 120 ? -14.786 -48.525 22.015 1.00 25.49  ? 119 VAL K CA  1 
ATOM   12033 C  C   . VAL K  1 120 ? -15.805 -47.787 22.883 1.00 28.31  ? 119 VAL K C   1 
ATOM   12034 O  O   . VAL K  1 120 ? -15.437 -46.985 23.747 1.00 27.10  ? 119 VAL K O   1 
ATOM   12035 C  CB  . VAL K  1 120 ? -14.007 -49.609 22.778 1.00 24.56  ? 119 VAL K CB  1 
ATOM   12036 C  CG1 . VAL K  1 120 ? -13.169 -49.047 23.919 1.00 25.17  ? 119 VAL K CG1 1 
ATOM   12037 C  CG2 . VAL K  1 120 ? -14.915 -50.702 23.291 1.00 24.15  ? 119 VAL K CG2 1 
ATOM   12038 N  N   . HIS K  1 121 ? -17.087 -48.085 22.636 1.00 31.39  ? 120 HIS K N   1 
ATOM   12039 C  CA  . HIS K  1 121 ? -18.202 -47.322 23.180 1.00 33.85  ? 120 HIS K CA  1 
ATOM   12040 C  C   . HIS K  1 121 ? -18.827 -47.982 24.408 1.00 36.78  ? 120 HIS K C   1 
ATOM   12041 O  O   . HIS K  1 121 ? -18.529 -49.128 24.736 1.00 39.48  ? 120 HIS K O   1 
ATOM   12042 C  CB  . HIS K  1 121 ? -19.263 -47.107 22.102 1.00 33.06  ? 120 HIS K CB  1 
ATOM   12043 C  CG  . HIS K  1 121 ? -18.860 -46.119 21.068 1.00 31.40  ? 120 HIS K CG  1 
ATOM   12044 N  ND1 . HIS K  1 121 ? -19.179 -44.787 21.174 1.00 31.22  ? 120 HIS K ND1 1 
ATOM   12045 C  CD2 . HIS K  1 121 ? -18.193 -46.265 19.903 1.00 31.77  ? 120 HIS K CD2 1 
ATOM   12046 C  CE1 . HIS K  1 121 ? -18.720 -44.150 20.114 1.00 34.32  ? 120 HIS K CE1 1 
ATOM   12047 N  NE2 . HIS K  1 121 ? -18.113 -45.034 19.313 1.00 32.95  ? 120 HIS K NE2 1 
ATOM   12048 N  N   . GLU K  1 122 ? -19.751 -47.247 25.034 1.00 37.08  ? 121 GLU K N   1 
ATOM   12049 C  CA  . GLU K  1 122 ? -20.299 -47.553 26.342 1.00 37.71  ? 121 GLU K CA  1 
ATOM   12050 C  C   . GLU K  1 122 ? -21.276 -48.722 26.276 1.00 38.23  ? 121 GLU K C   1 
ATOM   12051 O  O   . GLU K  1 122 ? -21.242 -49.579 27.153 1.00 39.20  ? 121 GLU K O   1 
ATOM   12052 C  CB  . GLU K  1 122 ? -20.948 -46.279 26.862 1.00 38.43  ? 121 GLU K CB  1 
ATOM   12053 C  CG  . GLU K  1 122 ? -21.996 -46.476 27.933 1.00 39.61  ? 121 GLU K CG  1 
ATOM   12054 C  CD  . GLU K  1 122 ? -22.842 -45.223 28.094 1.00 41.14  ? 121 GLU K CD  1 
ATOM   12055 O  OE1 . GLU K  1 122 ? -23.178 -44.873 29.238 1.00 44.63  ? 121 GLU K OE1 1 
ATOM   12056 O  OE2 . GLU K  1 122 ? -23.101 -44.543 27.081 1.00 41.95  ? 121 GLU K OE2 1 
ATOM   12057 N  N   . LYS K  1 123 ? -22.115 -48.756 25.227 1.00 40.89  ? 122 LYS K N   1 
ATOM   12058 C  CA  . LYS K  1 123 ? -23.219 -49.697 25.079 1.00 40.15  ? 122 LYS K CA  1 
ATOM   12059 C  C   . LYS K  1 123 ? -23.114 -50.433 23.743 1.00 39.49  ? 122 LYS K C   1 
ATOM   12060 O  O   . LYS K  1 123 ? -22.216 -50.174 22.939 1.00 40.48  ? 122 LYS K O   1 
ATOM   12061 C  CB  . LYS K  1 123 ? -24.549 -48.935 25.053 1.00 40.66  ? 122 LYS K CB  1 
ATOM   12062 C  CG  . LYS K  1 123 ? -24.924 -48.188 26.329 1.00 41.81  ? 122 LYS K CG  1 
ATOM   12063 C  CD  . LYS K  1 123 ? -26.286 -47.495 26.272 1.00 40.59  ? 122 LYS K CD  1 
ATOM   12064 C  CE  . LYS K  1 123 ? -26.257 -46.221 25.454 1.00 38.49  ? 122 LYS K CE  1 
ATOM   12065 N  NZ  . LYS K  1 123 ? -27.480 -45.406 25.547 1.00 37.33  ? 122 LYS K NZ  1 
ATOM   12066 N  N   . ALA K  1 124 ? -24.077 -51.332 23.498 1.00 36.75  ? 123 ALA K N   1 
ATOM   12067 C  CA  . ALA K  1 124 ? -24.155 -52.073 22.251 1.00 32.32  ? 123 ALA K CA  1 
ATOM   12068 C  C   . ALA K  1 124 ? -24.423 -51.127 21.088 1.00 30.61  ? 123 ALA K C   1 
ATOM   12069 O  O   . ALA K  1 124 ? -25.134 -50.140 21.236 1.00 30.44  ? 123 ALA K O   1 
ATOM   12070 C  CB  . ALA K  1 124 ? -25.240 -53.110 22.348 1.00 32.13  ? 123 ALA K CB  1 
ATOM   12071 N  N   . ASP K  1 125 ? -23.841 -51.447 19.935 1.00 28.01  ? 124 ASP K N   1 
ATOM   12072 C  CA  . ASP K  1 125 ? -24.191 -50.807 18.684 1.00 26.27  ? 124 ASP K CA  1 
ATOM   12073 C  C   . ASP K  1 125 ? -25.394 -51.555 18.116 1.00 26.53  ? 124 ASP K C   1 
ATOM   12074 O  O   . ASP K  1 125 ? -25.321 -52.761 17.897 1.00 30.36  ? 124 ASP K O   1 
ATOM   12075 C  CB  . ASP K  1 125 ? -22.975 -50.826 17.755 1.00 25.28  ? 124 ASP K CB  1 
ATOM   12076 C  CG  . ASP K  1 125 ? -23.232 -50.326 16.347 1.00 25.86  ? 124 ASP K CG  1 
ATOM   12077 O  OD1 . ASP K  1 125 ? -24.395 -50.035 16.015 1.00 24.11  ? 124 ASP K OD1 1 
ATOM   12078 O  OD2 . ASP K  1 125 ? -22.260 -50.266 15.573 1.00 28.53  ? 124 ASP K OD2 1 
ATOM   12079 N  N   . ASP K  1 126 ? -26.499 -50.849 17.859 1.00 24.88  ? 125 ASP K N   1 
ATOM   12080 C  CA  . ASP K  1 126 ? -27.723 -51.500 17.404 1.00 24.13  ? 125 ASP K CA  1 
ATOM   12081 C  C   . ASP K  1 126 ? -27.672 -51.775 15.898 1.00 24.38  ? 125 ASP K C   1 
ATOM   12082 O  O   . ASP K  1 126 ? -28.651 -52.230 15.332 1.00 26.00  ? 125 ASP K O   1 
ATOM   12083 C  CB  . ASP K  1 126 ? -28.987 -50.781 17.893 1.00 23.35  ? 125 ASP K CB  1 
ATOM   12084 C  CG  . ASP K  1 126 ? -29.276 -49.446 17.219 1.00 24.35  ? 125 ASP K CG  1 
ATOM   12085 O  OD1 . ASP K  1 126 ? -28.793 -49.230 16.069 1.00 24.74  ? 125 ASP K OD1 1 
ATOM   12086 O  OD2 . ASP K  1 126 ? -30.014 -48.624 17.848 1.00 22.63  ? 125 ASP K OD2 1 
ATOM   12087 N  N   . LEU K  1 127 ? -26.524 -51.504 15.266 1.00 21.81  ? 126 LEU K N   1 
ATOM   12088 C  CA  . LEU K  1 127 ? -26.275 -51.830 13.869 1.00 21.68  ? 126 LEU K CA  1 
ATOM   12089 C  C   . LEU K  1 127 ? -27.295 -51.150 12.959 1.00 23.93  ? 126 LEU K C   1 
ATOM   12090 O  O   . LEU K  1 127 ? -27.514 -51.600 11.835 1.00 24.75  ? 126 LEU K O   1 
ATOM   12091 C  CB  . LEU K  1 127 ? -26.266 -53.350 13.655 1.00 20.34  ? 126 LEU K CB  1 
ATOM   12092 C  CG  . LEU K  1 127 ? -25.430 -54.173 14.640 1.00 20.29  ? 126 LEU K CG  1 
ATOM   12093 C  CD1 . LEU K  1 127 ? -25.391 -55.642 14.273 1.00 19.39  ? 126 LEU K CD1 1 
ATOM   12094 C  CD2 . LEU K  1 127 ? -24.021 -53.658 14.713 1.00 19.89  ? 126 LEU K CD2 1 
ATOM   12095 N  N   . GLY K  1 128 ? -27.911 -50.069 13.456 1.00 26.21  ? 127 GLY K N   1 
ATOM   12096 C  CA  . GLY K  1 128 ? -28.752 -49.196 12.650 1.00 30.98  ? 127 GLY K CA  1 
ATOM   12097 C  C   . GLY K  1 128 ? -30.200 -49.680 12.573 1.00 33.67  ? 127 GLY K C   1 
ATOM   12098 O  O   . GLY K  1 128 ? -30.953 -49.245 11.706 1.00 36.59  ? 127 GLY K O   1 
ATOM   12099 N  N   . LYS K  1 129 ? -30.584 -50.564 13.496 1.00 34.17  ? 128 LYS K N   1 
ATOM   12100 C  CA  . LYS K  1 129 ? -31.885 -51.205 13.465 1.00 35.53  ? 128 LYS K CA  1 
ATOM   12101 C  C   . LYS K  1 129 ? -32.706 -50.794 14.683 1.00 35.81  ? 128 LYS K C   1 
ATOM   12102 O  O   . LYS K  1 129 ? -33.547 -51.566 15.136 1.00 32.91  ? 128 LYS K O   1 
ATOM   12103 C  CB  . LYS K  1 129 ? -31.721 -52.729 13.442 1.00 34.19  ? 128 LYS K CB  1 
ATOM   12104 C  CG  . LYS K  1 129 ? -30.809 -53.258 12.337 1.00 35.78  ? 128 LYS K CG  1 
ATOM   12105 C  CD  . LYS K  1 129 ? -31.148 -54.653 11.858 1.00 39.75  ? 128 LYS K CD  1 
ATOM   12106 C  CE  . LYS K  1 129 ? -31.145 -54.818 10.350 1.00 43.96  ? 128 LYS K CE  1 
ATOM   12107 N  NZ  . LYS K  1 129 ? -32.280 -55.697 9.974  1.00 48.59  ? 128 LYS K NZ  1 
ATOM   12108 N  N   . GLY K  1 130 ? -32.475 -49.571 15.181 1.00 36.21  ? 129 GLY K N   1 
ATOM   12109 C  CA  . GLY K  1 130 ? -33.099 -49.111 16.408 1.00 42.25  ? 129 GLY K CA  1 
ATOM   12110 C  C   . GLY K  1 130 ? -34.339 -48.255 16.148 1.00 47.60  ? 129 GLY K C   1 
ATOM   12111 O  O   . GLY K  1 130 ? -35.094 -47.956 17.083 1.00 50.03  ? 129 GLY K O   1 
ATOM   12112 N  N   . GLY K  1 131 ? -34.531 -47.869 14.874 1.00 45.40  ? 130 GLY K N   1 
ATOM   12113 C  CA  . GLY K  1 131 ? -35.728 -47.164 14.438 1.00 48.45  ? 130 GLY K CA  1 
ATOM   12114 C  C   . GLY K  1 131 ? -35.842 -45.736 14.984 1.00 46.95  ? 130 GLY K C   1 
ATOM   12115 O  O   . GLY K  1 131 ? -36.930 -45.187 15.041 1.00 44.45  ? 130 GLY K O   1 
ATOM   12116 N  N   . ASN K  1 132 ? -34.707 -45.134 15.356 1.00 48.19  ? 131 ASN K N   1 
ATOM   12117 C  CA  . ASN K  1 132 ? -34.663 -43.710 15.634 1.00 43.04  ? 131 ASN K CA  1 
ATOM   12118 C  C   . ASN K  1 132 ? -33.539 -43.071 14.824 1.00 42.31  ? 131 ASN K C   1 
ATOM   12119 O  O   . ASN K  1 132 ? -32.788 -43.766 14.134 1.00 42.19  ? 131 ASN K O   1 
ATOM   12120 C  CB  . ASN K  1 132 ? -34.623 -43.411 17.130 1.00 41.56  ? 131 ASN K CB  1 
ATOM   12121 C  CG  . ASN K  1 132 ? -33.418 -43.966 17.854 1.00 43.09  ? 131 ASN K CG  1 
ATOM   12122 O  OD1 . ASN K  1 132 ? -32.414 -44.338 17.248 1.00 45.18  ? 131 ASN K OD1 1 
ATOM   12123 N  ND2 . ASN K  1 132 ? -33.424 -43.826 19.154 1.00 46.45  ? 131 ASN K ND2 1 
ATOM   12124 N  N   . GLU K  1 133 ? -33.442 -41.741 14.914 1.00 43.87  ? 132 GLU K N   1 
ATOM   12125 C  CA  . GLU K  1 133 ? -32.520 -41.029 14.052 1.00 46.24  ? 132 GLU K CA  1 
ATOM   12126 C  C   . GLU K  1 133 ? -31.093 -41.349 14.487 1.00 47.47  ? 132 GLU K C   1 
ATOM   12127 O  O   . GLU K  1 133 ? -30.203 -41.537 13.662 1.00 41.66  ? 132 GLU K O   1 
ATOM   12128 C  CB  . GLU K  1 133 ? -32.833 -39.535 14.043 1.00 51.61  ? 132 GLU K CB  1 
ATOM   12129 C  CG  . GLU K  1 133 ? -32.081 -38.813 12.956 1.00 61.59  ? 132 GLU K CG  1 
ATOM   12130 C  CD  . GLU K  1 133 ? -31.831 -37.331 13.155 1.00 64.61  ? 132 GLU K CD  1 
ATOM   12131 O  OE1 . GLU K  1 133 ? -32.288 -36.731 14.160 1.00 68.35  ? 132 GLU K OE1 1 
ATOM   12132 O  OE2 . GLU K  1 133 ? -31.162 -36.797 12.296 1.00 68.62  ? 132 GLU K OE2 1 
ATOM   12133 N  N   . GLU K  1 134 ? -30.924 -41.445 15.807 1.00 49.24  ? 133 GLU K N   1 
ATOM   12134 C  CA  . GLU K  1 134 ? -29.665 -41.768 16.453 1.00 45.34  ? 133 GLU K CA  1 
ATOM   12135 C  C   . GLU K  1 134 ? -29.109 -43.082 15.905 1.00 42.13  ? 133 GLU K C   1 
ATOM   12136 O  O   . GLU K  1 134 ? -27.913 -43.198 15.643 1.00 41.27  ? 133 GLU K O   1 
ATOM   12137 C  CB  . GLU K  1 134 ? -29.892 -41.792 17.964 1.00 48.99  ? 133 GLU K CB  1 
ATOM   12138 C  CG  . GLU K  1 134 ? -28.638 -41.600 18.789 1.00 56.28  ? 133 GLU K CG  1 
ATOM   12139 C  CD  . GLU K  1 134 ? -27.633 -40.526 18.368 1.00 61.57  ? 133 GLU K CD  1 
ATOM   12140 O  OE1 . GLU K  1 134 ? -28.040 -39.472 17.840 1.00 66.81  ? 133 GLU K OE1 1 
ATOM   12141 O  OE2 . GLU K  1 134 ? -26.428 -40.759 18.554 1.00 63.75  ? 133 GLU K OE2 1 
ATOM   12142 N  N   . SER K  1 135 ? -29.987 -44.075 15.733 1.00 40.12  ? 134 SER K N   1 
ATOM   12143 C  CA  . SER K  1 135 ? -29.585 -45.395 15.278 1.00 39.34  ? 134 SER K CA  1 
ATOM   12144 C  C   . SER K  1 135 ? -28.829 -45.304 13.954 1.00 38.46  ? 134 SER K C   1 
ATOM   12145 O  O   . SER K  1 135 ? -27.839 -45.998 13.764 1.00 37.03  ? 134 SER K O   1 
ATOM   12146 C  CB  . SER K  1 135 ? -30.759 -46.336 15.180 1.00 37.88  ? 134 SER K CB  1 
ATOM   12147 O  OG  . SER K  1 135 ? -30.345 -47.651 14.813 1.00 34.09  ? 134 SER K OG  1 
ATOM   12148 N  N   . THR K  1 136 ? -29.284 -44.438 13.049 1.00 37.85  ? 135 THR K N   1 
ATOM   12149 C  CA  . THR K  1 136 ? -28.692 -44.418 11.719 1.00 39.40  ? 135 THR K CA  1 
ATOM   12150 C  C   . THR K  1 136 ? -27.456 -43.514 11.676 1.00 36.14  ? 135 THR K C   1 
ATOM   12151 O  O   . THR K  1 136 ? -26.856 -43.348 10.612 1.00 32.75  ? 135 THR K O   1 
ATOM   12152 C  CB  . THR K  1 136 ? -29.699 -43.993 10.643 1.00 41.42  ? 135 THR K CB  1 
ATOM   12153 O  OG1 . THR K  1 136 ? -30.037 -42.639 10.945 1.00 37.62  ? 135 THR K OG1 1 
ATOM   12154 C  CG2 . THR K  1 136 ? -30.942 -44.858 10.613 1.00 41.88  ? 135 THR K CG2 1 
ATOM   12155 N  N   . LYS K  1 137 ? -27.080 -42.947 12.827 1.00 32.96  ? 136 LYS K N   1 
ATOM   12156 C  CA  . LYS K  1 137 ? -25.873 -42.140 12.930 1.00 32.58  ? 136 LYS K CA  1 
ATOM   12157 C  C   . LYS K  1 137 ? -24.797 -42.870 13.730 1.00 29.70  ? 136 LYS K C   1 
ATOM   12158 O  O   . LYS K  1 137 ? -23.672 -43.045 13.252 1.00 27.05  ? 136 LYS K O   1 
ATOM   12159 C  CB  . LYS K  1 137 ? -26.177 -40.782 13.577 1.00 38.14  ? 136 LYS K CB  1 
ATOM   12160 C  CG  . LYS K  1 137 ? -26.807 -39.732 12.679 1.00 40.90  ? 136 LYS K CG  1 
ATOM   12161 C  CD  . LYS K  1 137 ? -26.943 -38.417 13.480 1.00 45.94  ? 136 LYS K CD  1 
ATOM   12162 C  CE  . LYS K  1 137 ? -28.023 -37.448 13.034 1.00 51.86  ? 136 LYS K CE  1 
ATOM   12163 N  NZ  . LYS K  1 137 ? -28.766 -36.878 14.192 1.00 55.82  ? 136 LYS K NZ  1 
ATOM   12164 N  N   . THR K  1 138 ? -25.155 -43.310 14.945 1.00 29.50  ? 137 THR K N   1 
ATOM   12165 C  CA  . THR K  1 138 ? -24.157 -43.799 15.890 1.00 27.87  ? 137 THR K CA  1 
ATOM   12166 C  C   . THR K  1 138 ? -24.472 -45.209 16.373 1.00 25.57  ? 137 THR K C   1 
ATOM   12167 O  O   . THR K  1 138 ? -23.727 -45.754 17.183 1.00 23.57  ? 137 THR K O   1 
ATOM   12168 C  CB  . THR K  1 138 ? -24.106 -42.887 17.121 1.00 28.22  ? 137 THR K CB  1 
ATOM   12169 O  OG1 . THR K  1 138 ? -25.292 -43.069 17.902 1.00 27.83  ? 137 THR K OG1 1 
ATOM   12170 C  CG2 . THR K  1 138 ? -23.924 -41.435 16.741 1.00 29.61  ? 137 THR K CG2 1 
ATOM   12171 N  N   . GLY K  1 139 ? -25.598 -45.772 15.907 1.00 24.05  ? 138 GLY K N   1 
ATOM   12172 C  CA  . GLY K  1 139 ? -26.070 -47.057 16.385 1.00 25.03  ? 138 GLY K CA  1 
ATOM   12173 C  C   . GLY K  1 139 ? -26.399 -47.066 17.880 1.00 24.99  ? 138 GLY K C   1 
ATOM   12174 O  O   . GLY K  1 139 ? -26.573 -48.128 18.464 1.00 24.42  ? 138 GLY K O   1 
ATOM   12175 N  N   . ASN K  1 140 ? -26.475 -45.890 18.499 1.00 26.48  ? 139 ASN K N   1 
ATOM   12176 C  CA  . ASN K  1 140 ? -26.938 -45.768 19.879 1.00 26.53  ? 139 ASN K CA  1 
ATOM   12177 C  C   . ASN K  1 140 ? -25.906 -46.359 20.833 1.00 25.90  ? 139 ASN K C   1 
ATOM   12178 O  O   . ASN K  1 140 ? -26.261 -46.789 21.925 1.00 26.73  ? 139 ASN K O   1 
ATOM   12179 C  CB  . ASN K  1 140 ? -28.325 -46.391 20.112 1.00 26.31  ? 139 ASN K CB  1 
ATOM   12180 C  CG  . ASN K  1 140 ? -29.462 -45.535 19.572 1.00 26.98  ? 139 ASN K CG  1 
ATOM   12181 O  OD1 . ASN K  1 140 ? -29.727 -44.448 20.084 1.00 25.40  ? 139 ASN K OD1 1 
ATOM   12182 N  ND2 . ASN K  1 140 ? -30.139 -46.014 18.529 1.00 27.48  ? 139 ASN K ND2 1 
ATOM   12183 N  N   . ALA K  1 141 ? -24.636 -46.349 20.421 1.00 26.15  ? 140 ALA K N   1 
ATOM   12184 C  CA  . ALA K  1 141 ? -23.577 -47.041 21.150 1.00 25.20  ? 140 ALA K CA  1 
ATOM   12185 C  C   . ALA K  1 141 ? -23.171 -46.273 22.415 1.00 25.15  ? 140 ALA K C   1 
ATOM   12186 O  O   . ALA K  1 141 ? -22.400 -46.772 23.239 1.00 24.82  ? 140 ALA K O   1 
ATOM   12187 C  CB  . ALA K  1 141 ? -22.394 -47.280 20.244 1.00 23.61  ? 140 ALA K CB  1 
ATOM   12188 N  N   . GLY K  1 142 ? -23.693 -45.055 22.564 1.00 24.99  ? 141 GLY K N   1 
ATOM   12189 C  CA  . GLY K  1 142 ? -23.414 -44.285 23.765 1.00 25.47  ? 141 GLY K CA  1 
ATOM   12190 C  C   . GLY K  1 142 ? -22.016 -43.675 23.736 1.00 24.40  ? 141 GLY K C   1 
ATOM   12191 O  O   . GLY K  1 142 ? -21.446 -43.496 22.665 1.00 22.81  ? 141 GLY K O   1 
ATOM   12192 N  N   . SER K  1 143 ? -21.477 -43.395 24.927 1.00 24.75  ? 142 SER K N   1 
ATOM   12193 C  CA  . SER K  1 143 ? -20.279 -42.588 25.075 1.00 26.55  ? 142 SER K CA  1 
ATOM   12194 C  C   . SER K  1 143 ? -19.035 -43.363 24.642 1.00 28.95  ? 142 SER K C   1 
ATOM   12195 O  O   . SER K  1 143 ? -19.101 -44.565 24.376 1.00 29.41  ? 142 SER K O   1 
ATOM   12196 C  CB  . SER K  1 143 ? -20.142 -42.068 26.484 1.00 26.69  ? 142 SER K CB  1 
ATOM   12197 O  OG  . SER K  1 143 ? -19.944 -43.139 27.394 1.00 25.72  ? 142 SER K OG  1 
ATOM   12198 N  N   . ARG K  1 144 ? -17.908 -42.640 24.592 1.00 29.46  ? 143 ARG K N   1 
ATOM   12199 C  CA  . ARG K  1 144 ? -16.625 -43.150 24.137 1.00 28.52  ? 143 ARG K CA  1 
ATOM   12200 C  C   . ARG K  1 144 ? -15.793 -43.516 25.363 1.00 29.76  ? 143 ARG K C   1 
ATOM   12201 O  O   . ARG K  1 144 ? -15.335 -42.640 26.084 1.00 28.46  ? 143 ARG K O   1 
ATOM   12202 C  CB  . ARG K  1 144 ? -15.947 -42.085 23.272 1.00 25.47  ? 143 ARG K CB  1 
ATOM   12203 C  CG  . ARG K  1 144 ? -16.790 -41.634 22.092 1.00 24.31  ? 143 ARG K CG  1 
ATOM   12204 C  CD  . ARG K  1 144 ? -16.289 -40.424 21.358 1.00 23.99  ? 143 ARG K CD  1 
ATOM   12205 N  NE  . ARG K  1 144 ? -17.217 -40.000 20.314 1.00 23.02  ? 143 ARG K NE  1 
ATOM   12206 C  CZ  . ARG K  1 144 ? -16.876 -39.314 19.224 1.00 23.87  ? 143 ARG K CZ  1 
ATOM   12207 N  NH1 . ARG K  1 144 ? -15.619 -38.961 19.011 1.00 25.10  ? 143 ARG K NH1 1 
ATOM   12208 N  NH2 . ARG K  1 144 ? -17.785 -39.002 18.317 1.00 23.10  ? 143 ARG K NH2 1 
ATOM   12209 N  N   . LEU K  1 145 ? -15.614 -44.818 25.606 1.00 29.90  ? 144 LEU K N   1 
ATOM   12210 C  CA  . LEU K  1 145 ? -14.987 -45.242 26.844 1.00 29.58  ? 144 LEU K CA  1 
ATOM   12211 C  C   . LEU K  1 145 ? -13.472 -45.105 26.731 1.00 30.98  ? 144 LEU K C   1 
ATOM   12212 O  O   . LEU K  1 145 ? -12.797 -44.744 27.693 1.00 29.66  ? 144 LEU K O   1 
ATOM   12213 C  CB  . LEU K  1 145 ? -15.398 -46.691 27.126 1.00 29.80  ? 144 LEU K CB  1 
ATOM   12214 C  CG  . LEU K  1 145 ? -16.850 -46.885 27.560 1.00 30.59  ? 144 LEU K CG  1 
ATOM   12215 C  CD1 . LEU K  1 145 ? -17.119 -48.326 27.918 1.00 28.72  ? 144 LEU K CD1 1 
ATOM   12216 C  CD2 . LEU K  1 145 ? -17.203 -45.975 28.728 1.00 32.62  ? 144 LEU K CD2 1 
ATOM   12217 N  N   . ALA K  1 146 ? -12.948 -45.413 25.540 1.00 32.17  ? 145 ALA K N   1 
ATOM   12218 C  CA  . ALA K  1 146 ? -11.520 -45.390 25.284 1.00 30.17  ? 145 ALA K CA  1 
ATOM   12219 C  C   . ALA K  1 146 ? -11.269 -45.325 23.786 1.00 32.48  ? 145 ALA K C   1 
ATOM   12220 O  O   . ALA K  1 146 ? -12.082 -45.778 22.977 1.00 33.97  ? 145 ALA K O   1 
ATOM   12221 C  CB  . ALA K  1 146 ? -10.837 -46.575 25.890 1.00 29.40  ? 145 ALA K CB  1 
ATOM   12222 N  N   . CYS K  1 147 ? -10.157 -44.685 23.419 1.00 31.72  ? 146 CYS K N   1 
ATOM   12223 C  CA  . CYS K  1 147 ? -9.813  -44.511 22.025 1.00 30.19  ? 146 CYS K CA  1 
ATOM   12224 C  C   . CYS K  1 147 ? -8.303  -44.394 21.912 1.00 31.69  ? 146 CYS K C   1 
ATOM   12225 O  O   . CYS K  1 147 ? -7.599  -44.307 22.916 1.00 36.28  ? 146 CYS K O   1 
ATOM   12226 C  CB  . CYS K  1 147 ? -10.483 -43.273 21.460 1.00 30.92  ? 146 CYS K CB  1 
ATOM   12227 S  SG  . CYS K  1 147 ? -10.073 -41.756 22.351 1.00 36.93  ? 146 CYS K SG  1 
ATOM   12228 N  N   . GLY K  1 148 ? -7.823  -44.421 20.674 1.00 28.16  ? 147 GLY K N   1 
ATOM   12229 C  CA  . GLY K  1 148 ? -6.425  -44.200 20.357 1.00 24.64  ? 147 GLY K CA  1 
ATOM   12230 C  C   . GLY K  1 148 ? -6.266  -43.852 18.887 1.00 24.56  ? 147 GLY K C   1 
ATOM   12231 O  O   . GLY K  1 148 ? -7.125  -44.158 18.058 1.00 24.77  ? 147 GLY K O   1 
ATOM   12232 N  N   . VAL K  1 149 ? -5.143  -43.208 18.573 1.00 24.55  ? 148 VAL K N   1 
ATOM   12233 C  CA  . VAL K  1 149 ? -4.836  -42.954 17.178 1.00 24.02  ? 148 VAL K CA  1 
ATOM   12234 C  C   . VAL K  1 149 ? -4.251  -44.229 16.580 1.00 23.58  ? 148 VAL K C   1 
ATOM   12235 O  O   . VAL K  1 149 ? -3.495  -44.948 17.232 1.00 23.49  ? 148 VAL K O   1 
ATOM   12236 C  CB  . VAL K  1 149 ? -3.934  -41.722 17.009 1.00 23.73  ? 148 VAL K CB  1 
ATOM   12237 C  CG1 . VAL K  1 149 ? -3.735  -41.384 15.541 1.00 23.54  ? 148 VAL K CG1 1 
ATOM   12238 C  CG2 . VAL K  1 149 ? -4.521  -40.534 17.750 1.00 23.12  ? 148 VAL K CG2 1 
ATOM   12239 N  N   . ILE K  1 150 ? -4.646  -44.502 15.334 1.00 23.28  ? 149 ILE K N   1 
ATOM   12240 C  CA  . ILE K  1 150 ? -4.246  -45.710 14.641 1.00 24.18  ? 149 ILE K CA  1 
ATOM   12241 C  C   . ILE K  1 150 ? -2.925  -45.414 13.945 1.00 23.76  ? 149 ILE K C   1 
ATOM   12242 O  O   . ILE K  1 150 ? -2.884  -44.600 13.020 1.00 25.55  ? 149 ILE K O   1 
ATOM   12243 C  CB  . ILE K  1 150 ? -5.340  -46.094 13.630 1.00 26.09  ? 149 ILE K CB  1 
ATOM   12244 C  CG1 . ILE K  1 150 ? -6.661  -46.457 14.320 1.00 27.88  ? 149 ILE K CG1 1 
ATOM   12245 C  CG2 . ILE K  1 150 ? -4.867  -47.198 12.693 1.00 26.51  ? 149 ILE K CG2 1 
ATOM   12246 C  CD1 . ILE K  1 150 ? -7.847  -46.471 13.375 1.00 24.84  ? 149 ILE K CD1 1 
ATOM   12247 N  N   . GLY K  1 151 ? -1.861  -46.089 14.391 1.00 24.11  ? 150 GLY K N   1 
ATOM   12248 C  CA  . GLY K  1 151 ? -0.500  -45.755 13.998 1.00 26.48  ? 150 GLY K CA  1 
ATOM   12249 C  C   . GLY K  1 151 ? 0.246   -46.933 13.358 1.00 27.46  ? 150 GLY K C   1 
ATOM   12250 O  O   . GLY K  1 151 ? -0.164  -48.094 13.480 1.00 30.07  ? 150 GLY K O   1 
ATOM   12251 N  N   . ILE K  1 152 ? 1.351   -46.606 12.675 1.00 25.04  ? 151 ILE K N   1 
ATOM   12252 C  CA  . ILE K  1 152 ? 2.118   -47.576 11.904 1.00 25.33  ? 151 ILE K CA  1 
ATOM   12253 C  C   . ILE K  1 152 ? 2.946   -48.396 12.883 1.00 26.14  ? 151 ILE K C   1 
ATOM   12254 O  O   . ILE K  1 152 ? 3.563   -47.824 13.778 1.00 28.37  ? 151 ILE K O   1 
ATOM   12255 C  CB  . ILE K  1 152 ? 3.021   -46.846 10.893 1.00 23.93  ? 151 ILE K CB  1 
ATOM   12256 C  CG1 . ILE K  1 152 ? 2.220   -46.009 9.893  1.00 23.37  ? 151 ILE K CG1 1 
ATOM   12257 C  CG2 . ILE K  1 152 ? 3.959   -47.838 10.234 1.00 23.20  ? 151 ILE K CG2 1 
ATOM   12258 C  CD1 . ILE K  1 152 ? 3.041   -44.929 9.244  1.00 23.45  ? 151 ILE K CD1 1 
ATOM   12259 N  N   . ALA K  1 153 ? 2.942   -49.724 12.714 1.00 27.94  ? 152 ALA K N   1 
ATOM   12260 C  CA  . ALA K  1 153 ? 3.673   -50.650 13.573 1.00 32.03  ? 152 ALA K CA  1 
ATOM   12261 C  C   . ALA K  1 153 ? 4.745   -51.373 12.755 1.00 33.59  ? 152 ALA K C   1 
ATOM   12262 O  O   . ALA K  1 153 ? 4.735   -51.300 11.519 1.00 30.98  ? 152 ALA K O   1 
ATOM   12263 C  CB  . ALA K  1 153 ? 2.737   -51.623 14.231 1.00 27.53  ? 152 ALA K CB  1 
ATOM   12264 N  N   . GLN K  1 154 ? 5.670   -52.045 13.461 1.00 35.54  ? 153 GLN K N   1 
ATOM   12265 C  CA  . GLN K  1 154 ? 6.827   -52.638 12.807 1.00 42.20  ? 153 GLN K CA  1 
ATOM   12266 C  C   . GLN K  1 154 ? 6.437   -53.873 11.976 1.00 46.38  ? 153 GLN K C   1 
ATOM   12267 O  O   . GLN K  1 154 ? 5.757   -54.808 12.445 1.00 50.70  ? 153 GLN K O   1 
ATOM   12268 C  CB  . GLN K  1 154 ? 7.923   -53.011 13.805 1.00 41.91  ? 153 GLN K CB  1 
ATOM   12269 C  CG  . GLN K  1 154 ? 9.124   -53.653 13.125 1.00 43.30  ? 153 GLN K CG  1 
ATOM   12270 C  CD  . GLN K  1 154 ? 10.409  -53.482 13.874 1.00 43.87  ? 153 GLN K CD  1 
ATOM   12271 O  OE1 . GLN K  1 154 ? 10.504  -53.823 15.047 1.00 47.84  ? 153 GLN K OE1 1 
ATOM   12272 N  NE2 . GLN K  1 154 ? 11.398  -52.943 13.183 1.00 44.38  ? 153 GLN K NE2 1 
ATOM   12273 O  OXT . GLN K  1 154 ? 6.843   -53.948 10.802 1.00 48.59  ? 153 GLN K OXT 1 
ATOM   12274 N  N   . ALA L  1 2   ? 11.231  12.698  6.443  1.00 68.51  ? 1   ALA L N   1 
ATOM   12275 C  CA  . ALA L  1 2   ? 11.518  11.294  6.130  1.00 64.49  ? 1   ALA L CA  1 
ATOM   12276 C  C   . ALA L  1 2   ? 12.439  10.698  7.194  1.00 64.62  ? 1   ALA L C   1 
ATOM   12277 O  O   . ALA L  1 2   ? 12.186  9.560   7.585  1.00 72.11  ? 1   ALA L O   1 
ATOM   12278 C  CB  . ALA L  1 2   ? 12.025  11.110  4.701  1.00 55.10  ? 1   ALA L CB  1 
ATOM   12279 N  N   . THR L  1 3   ? 13.551  11.385  7.518  1.00 59.44  ? 2   THR L N   1 
ATOM   12280 C  CA  . THR L  1 3   ? 14.585  10.788  8.354  1.00 54.52  ? 2   THR L CA  1 
ATOM   12281 C  C   . THR L  1 3   ? 14.542  11.438  9.742  1.00 49.59  ? 2   THR L C   1 
ATOM   12282 O  O   . THR L  1 3   ? 14.611  12.653  9.869  1.00 52.86  ? 2   THR L O   1 
ATOM   12283 C  CB  . THR L  1 3   ? 15.953  10.723  7.641  1.00 52.67  ? 2   THR L CB  1 
ATOM   12284 O  OG1 . THR L  1 3   ? 16.262  12.042  7.212  1.00 62.43  ? 2   THR L OG1 1 
ATOM   12285 C  CG2 . THR L  1 3   ? 15.929  9.840   6.412  1.00 52.05  ? 2   THR L CG2 1 
ATOM   12286 N  N   . LYS L  1 4   ? 14.428  10.602  10.787 1.00 45.37  ? 3   LYS L N   1 
ATOM   12287 C  CA  . LYS L  1 4   ? 14.540  11.038  12.171 1.00 45.44  ? 3   LYS L CA  1 
ATOM   12288 C  C   . LYS L  1 4   ? 15.810  10.462  12.797 1.00 44.57  ? 3   LYS L C   1 
ATOM   12289 O  O   . LYS L  1 4   ? 16.116  9.278   12.666 1.00 53.65  ? 3   LYS L O   1 
ATOM   12290 C  CB  . LYS L  1 4   ? 13.345  10.584  13.010 1.00 47.48  ? 3   LYS L CB  1 
ATOM   12291 C  CG  . LYS L  1 4   ? 12.115  11.476  12.977 1.00 55.41  ? 3   LYS L CG  1 
ATOM   12292 C  CD  . LYS L  1 4   ? 10.906  10.915  13.725 1.00 61.76  ? 3   LYS L CD  1 
ATOM   12293 C  CE  . LYS L  1 4   ? 9.589   11.210  13.020 1.00 65.50  ? 3   LYS L CE  1 
ATOM   12294 N  NZ  . LYS L  1 4   ? 8.514   10.225  13.270 1.00 61.88  ? 3   LYS L NZ  1 
ATOM   12295 N  N   . VAL L  1 5   ? 16.508  11.322  13.534 1.00 39.38  ? 4   VAL L N   1 
ATOM   12296 C  CA  . VAL L  1 5   ? 17.770  10.992  14.167 1.00 34.87  ? 4   VAL L CA  1 
ATOM   12297 C  C   . VAL L  1 5   ? 17.713  11.509  15.602 1.00 34.26  ? 4   VAL L C   1 
ATOM   12298 O  O   . VAL L  1 5   ? 16.966  12.429  15.906 1.00 34.62  ? 4   VAL L O   1 
ATOM   12299 C  CB  . VAL L  1 5   ? 18.920  11.620  13.361 1.00 31.20  ? 4   VAL L CB  1 
ATOM   12300 C  CG1 . VAL L  1 5   ? 20.222  11.646  14.123 1.00 30.86  ? 4   VAL L CG1 1 
ATOM   12301 C  CG2 . VAL L  1 5   ? 19.087  10.931  12.027 1.00 32.30  ? 4   VAL L CG2 1 
ATOM   12302 N  N   . VAL L  1 6   ? 18.495  10.899  16.490 1.00 32.00  ? 5   VAL L N   1 
ATOM   12303 C  CA  . VAL L  1 6   ? 18.454  11.329  17.875 1.00 29.32  ? 5   VAL L CA  1 
ATOM   12304 C  C   . VAL L  1 6   ? 19.851  11.268  18.483 1.00 28.03  ? 5   VAL L C   1 
ATOM   12305 O  O   . VAL L  1 6   ? 20.745  10.599  17.971 1.00 29.47  ? 5   VAL L O   1 
ATOM   12306 C  CB  . VAL L  1 6   ? 17.439  10.502  18.683 1.00 28.43  ? 5   VAL L CB  1 
ATOM   12307 C  CG1 . VAL L  1 6   ? 17.921  9.075   18.902 1.00 28.59  ? 5   VAL L CG1 1 
ATOM   12308 C  CG2 . VAL L  1 6   ? 17.117  11.170  20.015 1.00 29.07  ? 5   VAL L CG2 1 
ATOM   12309 N  N   . CYS L  1 7   ? 20.019  11.962  19.606 1.00 26.96  ? 6   CYS L N   1 
ATOM   12310 C  CA  . CYS L  1 7   ? 21.305  12.009  20.261 1.00 26.55  ? 6   CYS L CA  1 
ATOM   12311 C  C   . CYS L  1 7   ? 21.080  12.225  21.747 1.00 24.67  ? 6   CYS L C   1 
ATOM   12312 O  O   . CYS L  1 7   ? 20.355  13.141  22.128 1.00 25.44  ? 6   CYS L O   1 
ATOM   12313 C  CB  . CYS L  1 7   ? 22.110  13.166  19.687 1.00 29.30  ? 6   CYS L CB  1 
ATOM   12314 S  SG  . CYS L  1 7   ? 23.770  13.292  20.398 1.00 35.69  ? 6   CYS L SG  1 
ATOM   12315 N  N   . VAL L  1 8   ? 21.693  11.370  22.570 1.00 22.12  ? 7   VAL L N   1 
ATOM   12316 C  CA  . VAL L  1 8   ? 21.613  11.530  24.014 1.00 21.83  ? 7   VAL L CA  1 
ATOM   12317 C  C   . VAL L  1 8   ? 22.931  12.118  24.486 1.00 22.30  ? 7   VAL L C   1 
ATOM   12318 O  O   . VAL L  1 8   ? 23.975  11.519  24.269 1.00 23.43  ? 7   VAL L O   1 
ATOM   12319 C  CB  . VAL L  1 8   ? 21.334  10.184  24.715 1.00 21.82  ? 7   VAL L CB  1 
ATOM   12320 C  CG1 . VAL L  1 8   ? 21.402  10.312  26.230 1.00 20.64  ? 7   VAL L CG1 1 
ATOM   12321 C  CG2 . VAL L  1 8   ? 20.017  9.561   24.269 1.00 21.22  ? 7   VAL L CG2 1 
ATOM   12322 N  N   . LEU L  1 9   ? 22.884  13.285  25.132 1.00 23.50  ? 8   LEU L N   1 
ATOM   12323 C  CA  . LEU L  1 9   ? 24.108  13.920  25.597 1.00 24.85  ? 8   LEU L CA  1 
ATOM   12324 C  C   . LEU L  1 9   ? 24.370  13.516  27.039 1.00 26.88  ? 8   LEU L C   1 
ATOM   12325 O  O   . LEU L  1 9   ? 23.496  13.687  27.881 1.00 29.43  ? 8   LEU L O   1 
ATOM   12326 C  CB  . LEU L  1 9   ? 23.974  15.441  25.476 1.00 23.92  ? 8   LEU L CB  1 
ATOM   12327 C  CG  . LEU L  1 9   ? 23.631  15.985  24.096 1.00 23.79  ? 8   LEU L CG  1 
ATOM   12328 C  CD1 . LEU L  1 9   ? 23.209  17.430  24.191 1.00 25.93  ? 8   LEU L CD1 1 
ATOM   12329 C  CD2 . LEU L  1 9   ? 24.813  15.864  23.175 1.00 26.21  ? 8   LEU L CD2 1 
ATOM   12330 N  N   . LYS L  1 10  ? 25.569  12.979  27.304 1.00 26.81  ? 9   LYS L N   1 
ATOM   12331 C  CA  . LYS L  1 10  ? 26.053  12.707  28.657 1.00 25.08  ? 9   LYS L CA  1 
ATOM   12332 C  C   . LYS L  1 10  ? 27.501  13.187  28.749 1.00 25.28  ? 9   LYS L C   1 
ATOM   12333 O  O   . LYS L  1 10  ? 28.178  13.356  27.735 1.00 23.09  ? 9   LYS L O   1 
ATOM   12334 C  CB  . LYS L  1 10  ? 25.992  11.216  28.995 1.00 22.32  ? 9   LYS L CB  1 
ATOM   12335 C  CG  . LYS L  1 10  ? 24.617  10.679  29.373 0.20 22.32  ? 9   LYS L CG  1 
ATOM   12336 C  CD  . LYS L  1 10  ? 24.571  9.191   29.748 0.20 22.06  ? 9   LYS L CD  1 
ATOM   12337 C  CE  . LYS L  1 10  ? 23.806  8.170   28.891 0.20 21.44  ? 9   LYS L CE  1 
ATOM   12338 N  NZ  . LYS L  1 10  ? 22.371  8.001   29.237 0.20 21.07  ? 9   LYS L NZ  1 
ATOM   12339 N  N   . GLY L  1 11  ? 27.953  13.434  29.978 1.00 26.86  ? 10  GLY L N   1 
ATOM   12340 C  CA  . GLY L  1 11  ? 29.325  13.810  30.245 1.00 28.76  ? 10  GLY L CA  1 
ATOM   12341 C  C   . GLY L  1 11  ? 29.657  13.620  31.717 1.00 30.85  ? 10  GLY L C   1 
ATOM   12342 O  O   . GLY L  1 11  ? 28.920  12.949  32.431 1.00 30.46  ? 10  GLY L O   1 
ATOM   12343 N  N   . ASP L  1 12  ? 30.814  14.150  32.141 1.00 34.10  ? 11  ASP L N   1 
ATOM   12344 C  CA  . ASP L  1 12  ? 31.333  13.852  33.466 1.00 40.00  ? 11  ASP L CA  1 
ATOM   12345 C  C   . ASP L  1 12  ? 30.566  14.598  34.549 1.00 42.35  ? 11  ASP L C   1 
ATOM   12346 O  O   . ASP L  1 12  ? 30.519  14.146  35.687 1.00 43.22  ? 11  ASP L O   1 
ATOM   12347 C  CB  . ASP L  1 12  ? 32.816  14.179  33.547 1.00 45.88  ? 11  ASP L CB  1 
ATOM   12348 C  CG  . ASP L  1 12  ? 33.622  13.234  32.681 1.00 49.83  ? 11  ASP L CG  1 
ATOM   12349 O  OD1 . ASP L  1 12  ? 33.231  12.041  32.595 1.00 45.40  ? 11  ASP L OD1 1 
ATOM   12350 O  OD2 . ASP L  1 12  ? 34.608  13.706  32.081 1.00 58.73  ? 11  ASP L OD2 1 
ATOM   12351 N  N   . GLY L  1 13  ? 29.994  15.751  34.190 1.00 43.03  ? 12  GLY L N   1 
ATOM   12352 C  CA  . GLY L  1 13  ? 29.329  16.613  35.154 1.00 36.30  ? 12  GLY L CA  1 
ATOM   12353 C  C   . GLY L  1 13  ? 27.832  16.353  35.174 1.00 33.34  ? 12  GLY L C   1 
ATOM   12354 O  O   . GLY L  1 13  ? 27.388  15.280  34.785 1.00 33.28  ? 12  GLY L O   1 
ATOM   12355 N  N   . PRO L  1 14  ? 27.008  17.339  35.599 1.00 32.75  ? 13  PRO L N   1 
ATOM   12356 C  CA  . PRO L  1 14  ? 25.556  17.166  35.631 1.00 31.24  ? 13  PRO L CA  1 
ATOM   12357 C  C   . PRO L  1 14  ? 24.841  17.427  34.302 1.00 30.40  ? 13  PRO L C   1 
ATOM   12358 O  O   . PRO L  1 14  ? 23.631  17.292  34.222 1.00 30.97  ? 13  PRO L O   1 
ATOM   12359 C  CB  . PRO L  1 14  ? 25.130  18.188  36.686 1.00 30.44  ? 13  PRO L CB  1 
ATOM   12360 C  CG  . PRO L  1 14  ? 26.129  19.298  36.531 1.00 28.71  ? 13  PRO L CG  1 
ATOM   12361 C  CD  . PRO L  1 14  ? 27.425  18.669  36.064 1.00 29.79  ? 13  PRO L CD  1 
ATOM   12362 N  N   . VAL L  1 15  ? 25.584  17.774  33.254 1.00 31.36  ? 14  VAL L N   1 
ATOM   12363 C  CA  . VAL L  1 15  ? 24.935  18.141  32.009 1.00 32.75  ? 14  VAL L CA  1 
ATOM   12364 C  C   . VAL L  1 15  ? 24.445  16.890  31.291 1.00 34.13  ? 14  VAL L C   1 
ATOM   12365 O  O   . VAL L  1 15  ? 25.221  15.955  31.074 1.00 38.36  ? 14  VAL L O   1 
ATOM   12366 C  CB  . VAL L  1 15  ? 25.838  18.998  31.103 1.00 33.00  ? 14  VAL L CB  1 
ATOM   12367 C  CG1 . VAL L  1 15  ? 25.125  19.335  29.792 1.00 31.35  ? 14  VAL L CG1 1 
ATOM   12368 C  CG2 . VAL L  1 15  ? 26.230  20.276  31.824 1.00 32.57  ? 14  VAL L CG2 1 
ATOM   12369 N  N   . GLN L  1 16  ? 23.156  16.885  30.928 1.00 33.43  ? 15  GLN L N   1 
ATOM   12370 C  CA  . GLN L  1 16  ? 22.619  15.799  30.118 1.00 35.67  ? 15  GLN L CA  1 
ATOM   12371 C  C   . GLN L  1 16  ? 21.380  16.272  29.363 1.00 34.08  ? 15  GLN L C   1 
ATOM   12372 O  O   . GLN L  1 16  ? 20.734  17.226  29.788 1.00 40.51  ? 15  GLN L O   1 
ATOM   12373 C  CB  . GLN L  1 16  ? 22.318  14.576  30.996 1.00 40.33  ? 15  GLN L CB  1 
ATOM   12374 C  CG  . GLN L  1 16  ? 21.281  14.806  32.080 1.00 39.58  ? 15  GLN L CG  1 
ATOM   12375 C  CD  . GLN L  1 16  ? 21.261  13.674  33.061 1.00 39.73  ? 15  GLN L CD  1 
ATOM   12376 O  OE1 . GLN L  1 16  ? 20.706  13.778  34.146 1.00 45.72  ? 15  GLN L OE1 1 
ATOM   12377 N  NE2 . GLN L  1 16  ? 21.936  12.593  32.697 1.00 38.39  ? 15  GLN L NE2 1 
ATOM   12378 N  N   . GLY L  1 17  ? 21.049  15.598  28.257 1.00 29.34  ? 16  GLY L N   1 
ATOM   12379 C  CA  . GLY L  1 17  ? 19.913  15.989  27.450 1.00 28.02  ? 16  GLY L CA  1 
ATOM   12380 C  C   . GLY L  1 17  ? 19.664  15.050  26.270 1.00 27.52  ? 16  GLY L C   1 
ATOM   12381 O  O   . GLY L  1 17  ? 20.456  14.159  25.989 1.00 28.66  ? 16  GLY L O   1 
ATOM   12382 N  N   . ILE L  1 18  ? 18.540  15.267  25.585 1.00 24.60  ? 17  ILE L N   1 
ATOM   12383 C  CA  . ILE L  1 18  ? 18.170  14.513  24.402 1.00 22.86  ? 17  ILE L CA  1 
ATOM   12384 C  C   . ILE L  1 18  ? 17.928  15.524  23.289 1.00 23.99  ? 17  ILE L C   1 
ATOM   12385 O  O   . ILE L  1 18  ? 17.204  16.490  23.499 1.00 24.90  ? 17  ILE L O   1 
ATOM   12386 C  CB  . ILE L  1 18  ? 16.898  13.685  24.678 1.00 21.88  ? 17  ILE L CB  1 
ATOM   12387 C  CG1 . ILE L  1 18  ? 17.128  12.649  25.782 1.00 21.49  ? 17  ILE L CG1 1 
ATOM   12388 C  CG2 . ILE L  1 18  ? 16.356  13.053  23.408 1.00 20.50  ? 17  ILE L CG2 1 
ATOM   12389 C  CD1 . ILE L  1 18  ? 15.874  11.911  26.185 1.00 21.94  ? 17  ILE L CD1 1 
ATOM   12390 N  N   . ILE L  1 19  ? 18.528  15.309  22.115 1.00 22.91  ? 18  ILE L N   1 
ATOM   12391 C  CA  . ILE L  1 19  ? 18.289  16.219  21.006 1.00 21.04  ? 18  ILE L CA  1 
ATOM   12392 C  C   . ILE L  1 19  ? 17.808  15.403  19.816 1.00 20.88  ? 18  ILE L C   1 
ATOM   12393 O  O   . ILE L  1 19  ? 18.447  14.424  19.449 1.00 21.21  ? 18  ILE L O   1 
ATOM   12394 C  CB  . ILE L  1 19  ? 19.557  17.028  20.657 1.00 19.54  ? 18  ILE L CB  1 
ATOM   12395 C  CG1 . ILE L  1 19  ? 20.054  17.887  21.824 1.00 18.70  ? 18  ILE L CG1 1 
ATOM   12396 C  CG2 . ILE L  1 19  ? 19.350  17.854  19.403 1.00 19.25  ? 18  ILE L CG2 1 
ATOM   12397 C  CD1 . ILE L  1 19  ? 19.121  18.977  22.269 1.00 18.78  ? 18  ILE L CD1 1 
ATOM   12398 N  N   . ASN L  1 20  ? 16.710  15.839  19.201 1.00 21.58  ? 19  ASN L N   1 
ATOM   12399 C  CA  . ASN L  1 20  ? 16.171  15.187  18.018 1.00 22.94  ? 19  ASN L CA  1 
ATOM   12400 C  C   . ASN L  1 20  ? 16.531  15.967  16.768 1.00 22.16  ? 19  ASN L C   1 
ATOM   12401 O  O   . ASN L  1 20  ? 16.619  17.183  16.814 1.00 24.33  ? 19  ASN L O   1 
ATOM   12402 C  CB  . ASN L  1 20  ? 14.648  15.069  18.088 1.00 23.37  ? 19  ASN L CB  1 
ATOM   12403 C  CG  . ASN L  1 20  ? 14.215  14.424  19.376 1.00 24.60  ? 19  ASN L CG  1 
ATOM   12404 O  OD1 . ASN L  1 20  ? 13.858  15.120  20.320 1.00 25.24  ? 19  ASN L OD1 1 
ATOM   12405 N  ND2 . ASN L  1 20  ? 14.287  13.105  19.422 1.00 24.64  ? 19  ASN L ND2 1 
ATOM   12406 N  N   . PHE L  1 21  ? 16.702  15.250  15.659 1.00 23.45  ? 20  PHE L N   1 
ATOM   12407 C  CA  . PHE L  1 21  ? 16.932  15.860  14.361 1.00 26.30  ? 20  PHE L CA  1 
ATOM   12408 C  C   . PHE L  1 21  ? 15.934  15.275  13.377 1.00 28.70  ? 20  PHE L C   1 
ATOM   12409 O  O   . PHE L  1 21  ? 15.746  14.068  13.339 1.00 27.69  ? 20  PHE L O   1 
ATOM   12410 C  CB  . PHE L  1 21  ? 18.325  15.526  13.831 1.00 26.72  ? 20  PHE L CB  1 
ATOM   12411 C  CG  . PHE L  1 21  ? 19.475  16.010  14.678 1.00 29.20  ? 20  PHE L CG  1 
ATOM   12412 C  CD1 . PHE L  1 21  ? 19.745  15.434  15.916 1.00 28.75  ? 20  PHE L CD1 1 
ATOM   12413 C  CD2 . PHE L  1 21  ? 20.307  17.027  14.229 1.00 28.92  ? 20  PHE L CD2 1 
ATOM   12414 C  CE1 . PHE L  1 21  ? 20.812  15.881  16.684 1.00 28.74  ? 20  PHE L CE1 1 
ATOM   12415 C  CE2 . PHE L  1 21  ? 21.383  17.456  14.991 1.00 27.88  ? 20  PHE L CE2 1 
ATOM   12416 C  CZ  . PHE L  1 21  ? 21.636  16.883  16.217 1.00 28.23  ? 20  PHE L CZ  1 
ATOM   12417 N  N   . GLU L  1 22  ? 15.298  16.133  12.580 1.00 35.59  ? 21  GLU L N   1 
ATOM   12418 C  CA  . GLU L  1 22  ? 14.336  15.660  11.601 1.00 41.54  ? 21  GLU L CA  1 
ATOM   12419 C  C   . GLU L  1 22  ? 14.537  16.412  10.291 1.00 41.69  ? 21  GLU L C   1 
ATOM   12420 O  O   . GLU L  1 22  ? 14.781  17.614  10.321 1.00 43.48  ? 21  GLU L O   1 
ATOM   12421 C  CB  . GLU L  1 22  ? 12.923  15.825  12.164 1.00 50.80  ? 21  GLU L CB  1 
ATOM   12422 C  CG  . GLU L  1 22  ? 11.887  15.023  11.386 1.00 55.99  ? 21  GLU L CG  1 
ATOM   12423 C  CD  . GLU L  1 22  ? 10.468  15.119  11.905 1.00 61.36  ? 21  GLU L CD  1 
ATOM   12424 O  OE1 . GLU L  1 22  ? 10.248  14.842  13.118 1.00 66.05  ? 21  GLU L OE1 1 
ATOM   12425 O  OE2 . GLU L  1 22  ? 9.588   15.455  11.092 1.00 69.42  ? 21  GLU L OE2 1 
ATOM   12426 N  N   . GLN L  1 23  ? 14.430  15.695  9.164  1.00 42.37  ? 22  GLN L N   1 
ATOM   12427 C  CA  . GLN L  1 23  ? 14.651  16.286  7.851  1.00 45.27  ? 22  GLN L CA  1 
ATOM   12428 C  C   . GLN L  1 23  ? 13.597  15.772  6.870  1.00 48.68  ? 22  GLN L C   1 
ATOM   12429 O  O   . GLN L  1 23  ? 13.675  14.607  6.454  1.00 49.25  ? 22  GLN L O   1 
ATOM   12430 C  CB  . GLN L  1 23  ? 16.059  15.956  7.354  1.00 39.76  ? 22  GLN L CB  1 
ATOM   12431 C  CG  . GLN L  1 23  ? 16.462  16.715  6.105  1.00 40.06  ? 22  GLN L CG  1 
ATOM   12432 C  CD  . GLN L  1 23  ? 17.823  16.331  5.580  1.00 43.55  ? 22  GLN L CD  1 
ATOM   12433 O  OE1 . GLN L  1 23  ? 18.258  15.179  5.682  1.00 47.08  ? 22  GLN L OE1 1 
ATOM   12434 N  NE2 . GLN L  1 23  ? 18.500  17.301  4.986  1.00 42.27  ? 22  GLN L NE2 1 
ATOM   12435 N  N   . LYS L  1 24  ? 12.624  16.625  6.506  1.00 55.30  ? 23  LYS L N   1 
ATOM   12436 C  CA  . LYS L  1 24  ? 11.479  16.205  5.707  1.00 61.05  ? 23  LYS L CA  1 
ATOM   12437 C  C   . LYS L  1 24  ? 11.887  15.903  4.264  1.00 64.50  ? 23  LYS L C   1 
ATOM   12438 O  O   . LYS L  1 24  ? 11.592  14.825  3.757  1.00 68.74  ? 23  LYS L O   1 
ATOM   12439 C  CB  . LYS L  1 24  ? 10.267  17.137  5.858  1.00 61.24  ? 23  LYS L CB  1 
ATOM   12440 C  CG  . LYS L  1 24  ? 9.494   16.996  7.170  0.80 62.75  ? 23  LYS L CG  1 
ATOM   12441 C  CD  . LYS L  1 24  ? 8.615   18.187  7.538  0.80 67.01  ? 23  LYS L CD  1 
ATOM   12442 C  CE  . LYS L  1 24  ? 8.384   18.350  9.034  0.80 68.22  ? 23  LYS L CE  1 
ATOM   12443 N  NZ  . LYS L  1 24  ? 7.039   18.886  9.347  0.80 62.46  ? 23  LYS L NZ  1 
ATOM   12444 N  N   . GLU L  1 25  ? 12.589  16.831  3.603  1.00 69.39  ? 24  GLU L N   1 
ATOM   12445 C  CA  . GLU L  1 25  ? 13.054  16.606  2.236  1.00 70.87  ? 24  GLU L CA  1 
ATOM   12446 C  C   . GLU L  1 25  ? 14.546  16.289  2.280  1.00 68.62  ? 24  GLU L C   1 
ATOM   12447 O  O   . GLU L  1 25  ? 15.234  16.713  3.208  1.00 71.45  ? 24  GLU L O   1 
ATOM   12448 C  CB  . GLU L  1 25  ? 12.806  17.826  1.342  1.00 68.88  ? 24  GLU L CB  1 
ATOM   12449 C  CG  . GLU L  1 25  ? 11.404  18.397  1.432  0.50 63.10  ? 24  GLU L CG  1 
ATOM   12450 C  CD  . GLU L  1 25  ? 11.271  19.884  1.141  0.10 61.67  ? 24  GLU L CD  1 
ATOM   12451 O  OE1 . GLU L  1 25  ? 12.282  20.613  1.243  0.10 60.07  ? 24  GLU L OE1 1 
ATOM   12452 O  OE2 . GLU L  1 25  ? 10.151  20.314  0.819  0.10 60.84  ? 24  GLU L OE2 1 
ATOM   12453 N  N   . SER L  1 26  ? 15.040  15.568  1.270  1.00 70.88  ? 25  SER L N   1 
ATOM   12454 C  CA  . SER L  1 26  ? 16.365  14.970  1.349  1.00 76.91  ? 25  SER L CA  1 
ATOM   12455 C  C   . SER L  1 26  ? 17.479  16.012  1.331  1.00 77.20  ? 25  SER L C   1 
ATOM   12456 O  O   . SER L  1 26  ? 18.516  15.776  1.944  1.00 73.78  ? 25  SER L O   1 
ATOM   12457 C  CB  . SER L  1 26  ? 16.587  13.879  0.325  1.00 75.37  ? 25  SER L CB  1 
ATOM   12458 O  OG  . SER L  1 26  ? 15.950  14.215  -0.895 1.00 82.26  ? 25  SER L OG  1 
ATOM   12459 N  N   . ASN L  1 27  ? 17.298  17.137  0.639  1.00 79.28  ? 26  ASN L N   1 
ATOM   12460 C  CA  . ASN L  1 27  ? 18.348  18.148  0.712  1.00 78.56  ? 26  ASN L CA  1 
ATOM   12461 C  C   . ASN L  1 27  ? 17.874  19.376  1.489  1.00 70.13  ? 26  ASN L C   1 
ATOM   12462 O  O   . ASN L  1 27  ? 18.510  20.422  1.441  1.00 67.73  ? 26  ASN L O   1 
ATOM   12463 C  CB  . ASN L  1 27  ? 19.028  18.425  -0.635 1.00 88.26  ? 26  ASN L CB  1 
ATOM   12464 C  CG  . ASN L  1 27  ? 18.107  18.989  -1.694 1.00 99.71  ? 26  ASN L CG  1 
ATOM   12465 O  OD1 . ASN L  1 27  ? 16.920  18.682  -1.727 1.00 110.40 ? 26  ASN L OD1 1 
ATOM   12466 N  ND2 . ASN L  1 27  ? 18.643  19.847  -2.546 1.00 100.69 ? 26  ASN L ND2 1 
ATOM   12467 N  N   . GLY L  1 28  ? 16.743  19.230  2.178  1.00 61.21  ? 27  GLY L N   1 
ATOM   12468 C  CA  . GLY L  1 28  ? 16.063  20.349  2.811  1.00 52.85  ? 27  GLY L CA  1 
ATOM   12469 C  C   . GLY L  1 28  ? 16.553  20.617  4.232  1.00 51.86  ? 27  GLY L C   1 
ATOM   12470 O  O   . GLY L  1 28  ? 17.447  19.933  4.724  1.00 53.25  ? 27  GLY L O   1 
ATOM   12471 N  N   . PRO L  1 29  ? 15.968  21.609  4.937  1.00 48.36  ? 28  PRO L N   1 
ATOM   12472 C  CA  . PRO L  1 29  ? 16.449  21.999  6.267  1.00 43.74  ? 28  PRO L CA  1 
ATOM   12473 C  C   . PRO L  1 29  ? 16.230  20.897  7.304  1.00 40.05  ? 28  PRO L C   1 
ATOM   12474 O  O   . PRO L  1 29  ? 15.372  20.031  7.119  1.00 36.97  ? 28  PRO L O   1 
ATOM   12475 C  CB  . PRO L  1 29  ? 15.579  23.226  6.602  1.00 42.36  ? 28  PRO L CB  1 
ATOM   12476 C  CG  . PRO L  1 29  ? 14.319  23.011  5.800  1.00 40.51  ? 28  PRO L CG  1 
ATOM   12477 C  CD  . PRO L  1 29  ? 14.793  22.383  4.503  1.00 44.50  ? 28  PRO L CD  1 
ATOM   12478 N  N   . VAL L  1 30  ? 17.018  20.953  8.385  1.00 35.28  ? 29  VAL L N   1 
ATOM   12479 C  CA  . VAL L  1 30  ? 16.946  19.992  9.475  1.00 30.71  ? 29  VAL L CA  1 
ATOM   12480 C  C   . VAL L  1 30  ? 16.427  20.705  10.721 1.00 26.80  ? 29  VAL L C   1 
ATOM   12481 O  O   . VAL L  1 30  ? 16.990  21.713  11.134 1.00 24.69  ? 29  VAL L O   1 
ATOM   12482 C  CB  . VAL L  1 30  ? 18.328  19.363  9.753  1.00 31.55  ? 29  VAL L CB  1 
ATOM   12483 C  CG1 . VAL L  1 30  ? 18.262  18.353  10.883 1.00 30.61  ? 29  VAL L CG1 1 
ATOM   12484 C  CG2 . VAL L  1 30  ? 18.959  18.750  8.511  1.00 29.60  ? 29  VAL L CG2 1 
ATOM   12485 N  N   . LYS L  1 31  ? 15.355  20.178  11.312 1.00 25.67  ? 30  LYS L N   1 
ATOM   12486 C  CA  . LYS L  1 31  ? 14.870  20.718  12.573 1.00 26.66  ? 30  LYS L CA  1 
ATOM   12487 C  C   . LYS L  1 31  ? 15.628  20.041  13.706 1.00 27.03  ? 30  LYS L C   1 
ATOM   12488 O  O   . LYS L  1 31  ? 15.689  18.821  13.761 1.00 29.00  ? 30  LYS L O   1 
ATOM   12489 C  CB  . LYS L  1 31  ? 13.350  20.524  12.723 1.00 26.03  ? 30  LYS L CB  1 
ATOM   12490 C  CG  . LYS L  1 31  ? 12.461  21.534  11.995 0.40 26.04  ? 30  LYS L CG  1 
ATOM   12491 C  CD  . LYS L  1 31  ? 11.115  21.025  11.530 0.40 26.48  ? 30  LYS L CD  1 
ATOM   12492 C  CE  . LYS L  1 31  ? 10.823  21.541  10.143 0.40 26.65  ? 30  LYS L CE  1 
ATOM   12493 N  NZ  . LYS L  1 31  ? 9.469   22.122  10.123 0.40 27.05  ? 30  LYS L NZ  1 
ATOM   12494 N  N   . VAL L  1 32  ? 16.219  20.837  14.591 1.00 27.28  ? 31  VAL L N   1 
ATOM   12495 C  CA  . VAL L  1 32  ? 16.943  20.295  15.731 1.00 26.39  ? 31  VAL L CA  1 
ATOM   12496 C  C   . VAL L  1 32  ? 16.247  20.770  16.999 1.00 28.15  ? 31  VAL L C   1 
ATOM   12497 O  O   . VAL L  1 32  ? 16.205  21.967  17.269 1.00 31.37  ? 31  VAL L O   1 
ATOM   12498 C  CB  . VAL L  1 32  ? 18.411  20.760  15.705 1.00 25.75  ? 31  VAL L CB  1 
ATOM   12499 C  CG1 . VAL L  1 32  ? 19.218  20.134  16.827 1.00 24.39  ? 31  VAL L CG1 1 
ATOM   12500 C  CG2 . VAL L  1 32  ? 19.060  20.498  14.352 1.00 25.52  ? 31  VAL L CG2 1 
ATOM   12501 N  N   . TRP L  1 33  ? 15.690  19.849  17.784 1.00 28.37  ? 32  TRP L N   1 
ATOM   12502 C  CA  . TRP L  1 33  ? 15.034  20.287  19.012 1.00 27.84  ? 32  TRP L CA  1 
ATOM   12503 C  C   . TRP L  1 33  ? 15.221  19.276  20.137 1.00 26.87  ? 32  TRP L C   1 
ATOM   12504 O  O   . TRP L  1 33  ? 15.438  18.086  19.891 1.00 28.83  ? 32  TRP L O   1 
ATOM   12505 C  CB  . TRP L  1 33  ? 13.542  20.547  18.779 1.00 28.36  ? 32  TRP L CB  1 
ATOM   12506 C  CG  . TRP L  1 33  ? 12.712  19.295  18.764 1.00 28.21  ? 32  TRP L CG  1 
ATOM   12507 C  CD1 . TRP L  1 33  ? 11.969  18.769  19.788 1.00 27.85  ? 32  TRP L CD1 1 
ATOM   12508 C  CD2 . TRP L  1 33  ? 12.562  18.398  17.654 1.00 28.46  ? 32  TRP L CD2 1 
ATOM   12509 N  NE1 . TRP L  1 33  ? 11.352  17.611  19.381 1.00 28.39  ? 32  TRP L NE1 1 
ATOM   12510 C  CE2 . TRP L  1 33  ? 11.698  17.360  18.077 1.00 29.93  ? 32  TRP L CE2 1 
ATOM   12511 C  CE3 . TRP L  1 33  ? 13.076  18.369  16.349 1.00 27.90  ? 32  TRP L CE3 1 
ATOM   12512 C  CZ2 . TRP L  1 33  ? 11.339  16.305  17.232 1.00 31.16  ? 32  TRP L CZ2 1 
ATOM   12513 C  CZ3 . TRP L  1 33  ? 12.719  17.325  15.513 1.00 29.24  ? 32  TRP L CZ3 1 
ATOM   12514 C  CH2 . TRP L  1 33  ? 11.858  16.312  15.948 1.00 30.30  ? 32  TRP L CH2 1 
ATOM   12515 N  N   . GLY L  1 34  ? 15.072  19.770  21.362 1.00 24.86  ? 33  GLY L N   1 
ATOM   12516 C  CA  . GLY L  1 34  ? 15.107  18.934  22.538 1.00 26.31  ? 33  GLY L CA  1 
ATOM   12517 C  C   . GLY L  1 34  ? 15.454  19.763  23.769 1.00 26.69  ? 33  GLY L C   1 
ATOM   12518 O  O   . GLY L  1 34  ? 15.300  20.976  23.776 1.00 27.09  ? 33  GLY L O   1 
ATOM   12519 N  N   . SER L  1 35  ? 15.960  19.114  24.802 1.00 27.67  ? 34  SER L N   1 
ATOM   12520 C  CA  . SER L  1 35  ? 16.171  19.799  26.056 1.00 27.95  ? 34  SER L CA  1 
ATOM   12521 C  C   . SER L  1 35  ? 17.509  19.361  26.660 1.00 27.78  ? 34  SER L C   1 
ATOM   12522 O  O   . SER L  1 35  ? 17.875  18.189  26.567 1.00 28.51  ? 34  SER L O   1 
ATOM   12523 C  CB  . SER L  1 35  ? 14.996  19.489  26.933 1.00 28.54  ? 34  SER L CB  1 
ATOM   12524 O  OG  . SER L  1 35  ? 15.247  19.890  28.261 1.00 32.77  ? 34  SER L OG  1 
ATOM   12525 N  N   . ILE L  1 36  ? 18.271  20.307  27.227 1.00 25.54  ? 35  ILE L N   1 
ATOM   12526 C  CA  . ILE L  1 36  ? 19.479  19.972  27.966 1.00 24.20  ? 35  ILE L CA  1 
ATOM   12527 C  C   . ILE L  1 36  ? 19.359  20.582  29.357 1.00 26.56  ? 35  ILE L C   1 
ATOM   12528 O  O   . ILE L  1 36  ? 18.923  21.723  29.499 1.00 28.00  ? 35  ILE L O   1 
ATOM   12529 C  CB  . ILE L  1 36  ? 20.728  20.502  27.238 1.00 21.81  ? 35  ILE L CB  1 
ATOM   12530 C  CG1 . ILE L  1 36  ? 20.716  20.115  25.754 1.00 21.42  ? 35  ILE L CG1 1 
ATOM   12531 C  CG2 . ILE L  1 36  ? 22.000  20.044  27.941 1.00 20.81  ? 35  ILE L CG2 1 
ATOM   12532 C  CD1 . ILE L  1 36  ? 21.793  20.756  24.938 1.00 22.14  ? 35  ILE L CD1 1 
ATOM   12533 N  N   . LYS L  1 37  ? 19.743  19.819  30.386 1.00 28.07  ? 36  LYS L N   1 
ATOM   12534 C  CA  . LYS L  1 37  ? 19.649  20.313  31.750 1.00 30.08  ? 36  LYS L CA  1 
ATOM   12535 C  C   . LYS L  1 37  ? 21.027  20.277  32.410 1.00 30.48  ? 36  LYS L C   1 
ATOM   12536 O  O   . LYS L  1 37  ? 21.937  19.641  31.902 1.00 30.21  ? 36  LYS L O   1 
ATOM   12537 C  CB  . LYS L  1 37  ? 18.573  19.550  32.530 1.00 32.10  ? 36  LYS L CB  1 
ATOM   12538 C  CG  . LYS L  1 37  ? 18.869  18.085  32.788 1.00 37.63  ? 36  LYS L CG  1 
ATOM   12539 C  CD  . LYS L  1 37  ? 18.197  17.488  34.025 1.00 44.47  ? 36  LYS L CD  1 
ATOM   12540 C  CE  . LYS L  1 37  ? 17.970  15.989  33.912 1.00 49.87  ? 36  LYS L CE  1 
ATOM   12541 N  NZ  . LYS L  1 37  ? 16.837  15.524  34.762 1.00 50.38  ? 36  LYS L NZ  1 
ATOM   12542 N  N   . GLY L  1 38  ? 21.158  20.987  33.537 1.00 29.83  ? 37  GLY L N   1 
ATOM   12543 C  CA  . GLY L  1 38  ? 22.372  21.029  34.336 1.00 28.31  ? 37  GLY L CA  1 
ATOM   12544 C  C   . GLY L  1 38  ? 23.417  22.032  33.849 1.00 27.33  ? 37  GLY L C   1 
ATOM   12545 O  O   . GLY L  1 38  ? 24.569  21.988  34.271 1.00 26.61  ? 37  GLY L O   1 
ATOM   12546 N  N   . LEU L  1 39  ? 23.025  22.939  32.956 1.00 27.09  ? 38  LEU L N   1 
ATOM   12547 C  CA  . LEU L  1 39  ? 23.924  23.939  32.393 1.00 24.98  ? 38  LEU L CA  1 
ATOM   12548 C  C   . LEU L  1 39  ? 23.941  25.178  33.279 1.00 26.03  ? 38  LEU L C   1 
ATOM   12549 O  O   . LEU L  1 39  ? 22.972  25.438  33.986 1.00 27.59  ? 38  LEU L O   1 
ATOM   12550 C  CB  . LEU L  1 39  ? 23.429  24.311  30.993 1.00 21.69  ? 38  LEU L CB  1 
ATOM   12551 C  CG  . LEU L  1 39  ? 23.582  23.242  29.928 1.00 20.08  ? 38  LEU L CG  1 
ATOM   12552 C  CD1 . LEU L  1 39  ? 22.711  23.577  28.731 1.00 19.44  ? 38  LEU L CD1 1 
ATOM   12553 C  CD2 . LEU L  1 39  ? 25.037  23.090  29.530 1.00 18.78  ? 38  LEU L CD2 1 
ATOM   12554 N  N   . THR L  1 40  ? 25.032  25.944  33.219 1.00 28.58  ? 39  THR L N   1 
ATOM   12555 C  CA  . THR L  1 40  ? 25.062  27.265  33.827 1.00 30.10  ? 39  THR L CA  1 
ATOM   12556 C  C   . THR L  1 40  ? 24.211  28.203  32.980 1.00 31.46  ? 39  THR L C   1 
ATOM   12557 O  O   . THR L  1 40  ? 24.109  28.030  31.766 1.00 30.64  ? 39  THR L O   1 
ATOM   12558 C  CB  . THR L  1 40  ? 26.487  27.826  33.924 1.00 28.10  ? 39  THR L CB  1 
ATOM   12559 O  OG1 . THR L  1 40  ? 27.054  27.662  32.628 1.00 25.56  ? 39  THR L OG1 1 
ATOM   12560 C  CG2 . THR L  1 40  ? 27.332  27.131  34.967 1.00 28.01  ? 39  THR L CG2 1 
ATOM   12561 N  N   . GLU L  1 41  ? 23.590  29.190  33.636 1.00 33.92  ? 40  GLU L N   1 
ATOM   12562 C  CA  . GLU L  1 41  ? 22.720  30.118  32.937 1.00 34.29  ? 40  GLU L CA  1 
ATOM   12563 C  C   . GLU L  1 41  ? 23.502  30.794  31.816 1.00 31.93  ? 40  GLU L C   1 
ATOM   12564 O  O   . GLU L  1 41  ? 24.680  31.101  31.989 1.00 31.50  ? 40  GLU L O   1 
ATOM   12565 C  CB  . GLU L  1 41  ? 22.171  31.136  33.924 1.00 38.23  ? 40  GLU L CB  1 
ATOM   12566 C  CG  . GLU L  1 41  ? 21.160  32.069  33.281 1.00 46.88  ? 40  GLU L CG  1 
ATOM   12567 C  CD  . GLU L  1 41  ? 20.514  33.072  34.240 1.00 47.84  ? 40  GLU L CD  1 
ATOM   12568 O  OE1 . GLU L  1 41  ? 20.948  33.171  35.420 1.00 45.79  ? 40  GLU L OE1 1 
ATOM   12569 O  OE2 . GLU L  1 41  ? 19.563  33.749  33.805 1.00 50.39  ? 40  GLU L OE2 1 
ATOM   12570 N  N   . GLY L  1 42  ? 22.854  30.987  30.662 1.00 29.54  ? 41  GLY L N   1 
ATOM   12571 C  CA  . GLY L  1 42  ? 23.488  31.723  29.577 1.00 30.45  ? 41  GLY L CA  1 
ATOM   12572 C  C   . GLY L  1 42  ? 23.756  30.876  28.331 1.00 29.77  ? 41  GLY L C   1 
ATOM   12573 O  O   . GLY L  1 42  ? 23.190  29.795  28.177 1.00 30.61  ? 41  GLY L O   1 
ATOM   12574 N  N   . LEU L  1 43  ? 24.624  31.398  27.450 1.00 28.99  ? 42  LEU L N   1 
ATOM   12575 C  CA  . LEU L  1 43  ? 24.887  30.816  26.141 1.00 28.75  ? 42  LEU L CA  1 
ATOM   12576 C  C   . LEU L  1 43  ? 25.891  29.676  26.262 1.00 28.40  ? 42  LEU L C   1 
ATOM   12577 O  O   . LEU L  1 43  ? 26.835  29.771  27.037 1.00 27.82  ? 42  LEU L O   1 
ATOM   12578 C  CB  . LEU L  1 43  ? 25.443  31.892  25.203 1.00 28.01  ? 42  LEU L CB  1 
ATOM   12579 C  CG  . LEU L  1 43  ? 24.475  33.005  24.821 1.00 27.56  ? 42  LEU L CG  1 
ATOM   12580 C  CD1 . LEU L  1 43  ? 25.217  34.136  24.133 1.00 26.92  ? 42  LEU L CD1 1 
ATOM   12581 C  CD2 . LEU L  1 43  ? 23.346  32.471  23.952 1.00 26.35  ? 42  LEU L CD2 1 
ATOM   12582 N  N   . HIS L  1 44  ? 25.662  28.615  25.472 1.00 26.35  ? 43  HIS L N   1 
ATOM   12583 C  CA  . HIS L  1 44  ? 26.570  27.486  25.363 1.00 25.35  ? 43  HIS L CA  1 
ATOM   12584 C  C   . HIS L  1 44  ? 26.725  27.089  23.899 1.00 26.69  ? 43  HIS L C   1 
ATOM   12585 O  O   . HIS L  1 44  ? 25.741  26.976  23.165 1.00 28.93  ? 43  HIS L O   1 
ATOM   12586 C  CB  . HIS L  1 44  ? 26.088  26.307  26.204 1.00 24.52  ? 43  HIS L CB  1 
ATOM   12587 C  CG  . HIS L  1 44  ? 26.086  26.578  27.672 1.00 25.16  ? 43  HIS L CG  1 
ATOM   12588 N  ND1 . HIS L  1 44  ? 27.140  26.209  28.490 1.00 26.02  ? 43  HIS L ND1 1 
ATOM   12589 C  CD2 . HIS L  1 44  ? 25.170  27.147  28.481 1.00 24.69  ? 43  HIS L CD2 1 
ATOM   12590 C  CE1 . HIS L  1 44  ? 26.875  26.534  29.731 1.00 24.43  ? 43  HIS L CE1 1 
ATOM   12591 N  NE2 . HIS L  1 44  ? 25.680  27.115  29.754 1.00 25.25  ? 43  HIS L NE2 1 
ATOM   12592 N  N   . GLY L  1 45  ? 27.982  26.903  23.490 1.00 26.17  ? 44  GLY L N   1 
ATOM   12593 C  CA  . GLY L  1 45  ? 28.297  26.475  22.142 1.00 26.25  ? 44  GLY L CA  1 
ATOM   12594 C  C   . GLY L  1 45  ? 27.744  25.080  21.861 1.00 27.04  ? 44  GLY L C   1 
ATOM   12595 O  O   . GLY L  1 45  ? 27.759  24.205  22.727 1.00 28.68  ? 44  GLY L O   1 
ATOM   12596 N  N   . PHE L  1 46  ? 27.281  24.886  20.626 1.00 26.49  ? 45  PHE L N   1 
ATOM   12597 C  CA  . PHE L  1 46  ? 26.506  23.716  20.264 1.00 26.88  ? 45  PHE L CA  1 
ATOM   12598 C  C   . PHE L  1 46  ? 26.948  23.284  18.871 1.00 28.13  ? 45  PHE L C   1 
ATOM   12599 O  O   . PHE L  1 46  ? 26.631  23.963  17.891 1.00 29.17  ? 45  PHE L O   1 
ATOM   12600 C  CB  . PHE L  1 46  ? 25.035  24.128  20.260 1.00 25.53  ? 45  PHE L CB  1 
ATOM   12601 C  CG  . PHE L  1 46  ? 24.015  23.020  20.184 1.00 24.13  ? 45  PHE L CG  1 
ATOM   12602 C  CD1 . PHE L  1 46  ? 23.878  22.106  21.221 1.00 23.80  ? 45  PHE L CD1 1 
ATOM   12603 C  CD2 . PHE L  1 46  ? 23.152  22.935  19.097 1.00 22.78  ? 45  PHE L CD2 1 
ATOM   12604 C  CE1 . PHE L  1 46  ? 22.909  21.116  21.163 1.00 23.09  ? 45  PHE L CE1 1 
ATOM   12605 C  CE2 . PHE L  1 46  ? 22.194  21.935  19.046 1.00 21.71  ? 45  PHE L CE2 1 
ATOM   12606 C  CZ  . PHE L  1 46  ? 22.089  21.009  20.063 1.00 22.24  ? 45  PHE L CZ  1 
ATOM   12607 N  N   . HIS L  1 47  ? 27.698  22.178  18.793 1.00 27.64  ? 46  HIS L N   1 
ATOM   12608 C  CA  . HIS L  1 47  ? 28.334  21.815  17.534 1.00 26.98  ? 46  HIS L CA  1 
ATOM   12609 C  C   . HIS L  1 47  ? 28.266  20.321  17.264 1.00 25.97  ? 46  HIS L C   1 
ATOM   12610 O  O   . HIS L  1 47  ? 28.210  19.507  18.189 1.00 24.79  ? 46  HIS L O   1 
ATOM   12611 C  CB  . HIS L  1 47  ? 29.808  22.227  17.534 1.00 27.35  ? 46  HIS L CB  1 
ATOM   12612 C  CG  . HIS L  1 47  ? 30.047  23.577  18.112 1.00 27.35  ? 46  HIS L CG  1 
ATOM   12613 N  ND1 . HIS L  1 47  ? 30.670  23.745  19.332 1.00 28.62  ? 46  HIS L ND1 1 
ATOM   12614 C  CD2 . HIS L  1 47  ? 29.738  24.810  17.648 1.00 27.57  ? 46  HIS L CD2 1 
ATOM   12615 C  CE1 . HIS L  1 47  ? 30.739  25.038  19.603 1.00 29.73  ? 46  HIS L CE1 1 
ATOM   12616 N  NE2 . HIS L  1 47  ? 30.166  25.710  18.585 1.00 28.12  ? 46  HIS L NE2 1 
ATOM   12617 N  N   . VAL L  1 48  ? 28.298  19.995  15.972 1.00 27.15  ? 47  VAL L N   1 
ATOM   12618 C  CA  . VAL L  1 48  ? 28.576  18.638  15.544 1.00 30.26  ? 47  VAL L CA  1 
ATOM   12619 C  C   . VAL L  1 48  ? 30.079  18.508  15.321 1.00 31.25  ? 47  VAL L C   1 
ATOM   12620 O  O   . VAL L  1 48  ? 30.626  19.172  14.444 1.00 31.25  ? 47  VAL L O   1 
ATOM   12621 C  CB  . VAL L  1 48  ? 27.799  18.257  14.269 1.00 29.39  ? 47  VAL L CB  1 
ATOM   12622 C  CG1 . VAL L  1 48  ? 28.049  16.806  13.892 1.00 28.43  ? 47  VAL L CG1 1 
ATOM   12623 C  CG2 . VAL L  1 48  ? 26.309  18.521  14.409 1.00 30.02  ? 47  VAL L CG2 1 
ATOM   12624 N  N   . HIS L  1 49  ? 30.726  17.647  16.118 1.00 31.64  ? 48  HIS L N   1 
ATOM   12625 C  CA  . HIS L  1 49  ? 32.124  17.298  15.920 1.00 32.71  ? 48  HIS L CA  1 
ATOM   12626 C  C   . HIS L  1 49  ? 32.253  16.118  14.956 1.00 33.95  ? 48  HIS L C   1 
ATOM   12627 O  O   . HIS L  1 49  ? 31.264  15.461  14.640 1.00 35.03  ? 48  HIS L O   1 
ATOM   12628 C  CB  . HIS L  1 49  ? 32.800  17.047  17.265 1.00 31.27  ? 48  HIS L CB  1 
ATOM   12629 C  CG  . HIS L  1 49  ? 32.890  18.268  18.114 1.00 31.80  ? 48  HIS L CG  1 
ATOM   12630 N  ND1 . HIS L  1 49  ? 34.097  18.771  18.553 1.00 32.35  ? 48  HIS L ND1 1 
ATOM   12631 C  CD2 . HIS L  1 49  ? 31.934  19.086  18.611 1.00 33.17  ? 48  HIS L CD2 1 
ATOM   12632 C  CE1 . HIS L  1 49  ? 33.878  19.843  19.293 1.00 29.93  ? 48  HIS L CE1 1 
ATOM   12633 N  NE2 . HIS L  1 49  ? 32.567  20.057  19.351 1.00 30.36  ? 48  HIS L NE2 1 
ATOM   12634 N  N   . GLU L  1 50  ? 33.493  15.838  14.522 1.00 34.76  ? 49  GLU L N   1 
ATOM   12635 C  CA  . GLU L  1 50  ? 33.773  14.997  13.365 1.00 33.67  ? 49  GLU L CA  1 
ATOM   12636 C  C   . GLU L  1 50  ? 33.499  13.519  13.632 1.00 33.08  ? 49  GLU L C   1 
ATOM   12637 O  O   . GLU L  1 50  ? 32.945  12.837  12.772 1.00 31.64  ? 49  GLU L O   1 
ATOM   12638 C  CB  . GLU L  1 50  ? 35.228  15.147  12.933 1.00 32.82  ? 49  GLU L CB  1 
ATOM   12639 C  CG  . GLU L  1 50  ? 35.485  14.596  11.547 1.00 34.77  ? 49  GLU L CG  1 
ATOM   12640 C  CD  . GLU L  1 50  ? 36.924  14.729  11.066 1.00 38.45  ? 49  GLU L CD  1 
ATOM   12641 O  OE1 . GLU L  1 50  ? 37.706  15.552  11.645 1.00 38.81  ? 49  GLU L OE1 1 
ATOM   12642 O  OE2 . GLU L  1 50  ? 37.269  14.002  10.107 1.00 37.39  ? 49  GLU L OE2 1 
ATOM   12643 N  N   . PHE L  1 51  ? 33.903  13.024  14.810 1.00 33.59  ? 50  PHE L N   1 
ATOM   12644 C  CA  . PHE L  1 51  ? 33.936  11.593  15.052 1.00 32.77  ? 50  PHE L CA  1 
ATOM   12645 C  C   . PHE L  1 51  ? 32.892  11.178  16.079 1.00 31.45  ? 50  PHE L C   1 
ATOM   12646 O  O   . PHE L  1 51  ? 32.803  11.779  17.151 1.00 29.78  ? 50  PHE L O   1 
ATOM   12647 C  CB  . PHE L  1 51  ? 35.314  11.174  15.564 1.00 33.24  ? 50  PHE L CB  1 
ATOM   12648 C  CG  . PHE L  1 51  ? 36.432  11.576  14.646 1.00 32.66  ? 50  PHE L CG  1 
ATOM   12649 C  CD1 . PHE L  1 51  ? 36.426  11.175  13.314 1.00 31.79  ? 50  PHE L CD1 1 
ATOM   12650 C  CD2 . PHE L  1 51  ? 37.475  12.371  15.105 1.00 32.98  ? 50  PHE L CD2 1 
ATOM   12651 C  CE1 . PHE L  1 51  ? 37.449  11.552  12.454 1.00 31.62  ? 50  PHE L CE1 1 
ATOM   12652 C  CE2 . PHE L  1 51  ? 38.510  12.728  14.252 1.00 32.96  ? 50  PHE L CE2 1 
ATOM   12653 C  CZ  . PHE L  1 51  ? 38.483  12.337  12.927 1.00 32.43  ? 50  PHE L CZ  1 
ATOM   12654 N  N   . GLY L  1 52  ? 32.153  10.113  15.735 1.00 29.66  ? 51  GLY L N   1 
ATOM   12655 C  CA  . GLY L  1 52  ? 31.308  9.392   16.671 1.00 28.93  ? 51  GLY L CA  1 
ATOM   12656 C  C   . GLY L  1 52  ? 32.149  8.486   17.568 1.00 27.73  ? 51  GLY L C   1 
ATOM   12657 O  O   . GLY L  1 52  ? 31.925  7.280   17.632 1.00 30.55  ? 51  GLY L O   1 
ATOM   12658 N  N   . ASP L  1 53  ? 33.125  9.084   18.250 1.00 24.96  ? 52  ASP L N   1 
ATOM   12659 C  CA  . ASP L  1 53  ? 34.092  8.314   18.998 1.00 27.56  ? 52  ASP L CA  1 
ATOM   12660 C  C   . ASP L  1 53  ? 34.119  8.835   20.424 1.00 28.94  ? 52  ASP L C   1 
ATOM   12661 O  O   . ASP L  1 53  ? 34.504  9.971   20.656 1.00 33.09  ? 52  ASP L O   1 
ATOM   12662 C  CB  . ASP L  1 53  ? 35.459  8.375   18.321 1.00 29.66  ? 52  ASP L CB  1 
ATOM   12663 C  CG  . ASP L  1 53  ? 36.548  7.573   19.016 1.00 31.06  ? 52  ASP L CG  1 
ATOM   12664 O  OD1 . ASP L  1 53  ? 36.421  7.327   20.243 1.00 29.83  ? 52  ASP L OD1 1 
ATOM   12665 O  OD2 . ASP L  1 53  ? 37.519  7.192   18.316 1.00 30.23  ? 52  ASP L OD2 1 
ATOM   12666 N  N   . ASN L  1 54  ? 33.698  7.999   21.371 1.00 30.14  ? 53  ASN L N   1 
ATOM   12667 C  CA  . ASN L  1 54  ? 33.596  8.429   22.753 1.00 31.17  ? 53  ASN L CA  1 
ATOM   12668 C  C   . ASN L  1 54  ? 34.596  7.640   23.599 1.00 30.50  ? 53  ASN L C   1 
ATOM   12669 O  O   . ASN L  1 54  ? 34.488  7.599   24.823 1.00 28.84  ? 53  ASN L O   1 
ATOM   12670 C  CB  . ASN L  1 54  ? 32.136  8.358   23.216 1.00 34.92  ? 53  ASN L CB  1 
ATOM   12671 C  CG  . ASN L  1 54  ? 31.909  8.793   24.648 1.00 41.07  ? 53  ASN L CG  1 
ATOM   12672 O  OD1 . ASN L  1 54  ? 32.287  9.899   25.029 1.00 45.82  ? 53  ASN L OD1 1 
ATOM   12673 N  ND2 . ASN L  1 54  ? 31.278  7.939   25.446 1.00 43.50  ? 53  ASN L ND2 1 
ATOM   12674 N  N   . THR L  1 55  ? 35.601  7.040   22.944 1.00 29.37  ? 54  THR L N   1 
ATOM   12675 C  CA  . THR L  1 55  ? 36.509  6.120   23.618 1.00 27.48  ? 54  THR L CA  1 
ATOM   12676 C  C   . THR L  1 55  ? 37.252  6.815   24.754 1.00 27.43  ? 54  THR L C   1 
ATOM   12677 O  O   . THR L  1 55  ? 37.570  6.180   25.749 1.00 29.36  ? 54  THR L O   1 
ATOM   12678 C  CB  . THR L  1 55  ? 37.515  5.476   22.661 1.00 25.74  ? 54  THR L CB  1 
ATOM   12679 O  OG1 . THR L  1 55  ? 38.235  6.531   22.032 1.00 26.42  ? 54  THR L OG1 1 
ATOM   12680 C  CG2 . THR L  1 55  ? 36.873  4.618   21.596 1.00 25.87  ? 54  THR L CG2 1 
ATOM   12681 N  N   . ALA L  1 56  ? 37.528  8.111   24.595 1.00 28.12  ? 55  ALA L N   1 
ATOM   12682 C  CA  . ALA L  1 56  ? 38.259  8.868   25.595 1.00 28.04  ? 55  ALA L CA  1 
ATOM   12683 C  C   . ALA L  1 56  ? 37.405  10.050  26.043 1.00 30.64  ? 55  ALA L C   1 
ATOM   12684 O  O   . ALA L  1 56  ? 37.899  11.171  26.157 1.00 34.46  ? 55  ALA L O   1 
ATOM   12685 C  CB  . ALA L  1 56  ? 39.568  9.329   25.006 1.00 25.60  ? 55  ALA L CB  1 
ATOM   12686 N  N   . GLY L  1 57  ? 36.111  9.797   26.269 1.00 29.85  ? 56  GLY L N   1 
ATOM   12687 C  CA  . GLY L  1 57  ? 35.173  10.858  26.596 1.00 28.85  ? 56  GLY L CA  1 
ATOM   12688 C  C   . GLY L  1 57  ? 34.878  11.726  25.376 1.00 30.54  ? 56  GLY L C   1 
ATOM   12689 O  O   . GLY L  1 57  ? 35.068  11.301  24.234 1.00 29.74  ? 56  GLY L O   1 
ATOM   12690 N  N   . CYS L  1 58  ? 34.434  12.964  25.630 1.00 31.86  ? 57  CYS L N   1 
ATOM   12691 C  CA  . CYS L  1 58  ? 34.027  13.840  24.545 1.00 31.56  ? 57  CYS L CA  1 
ATOM   12692 C  C   . CYS L  1 58  ? 35.224  14.281  23.711 1.00 32.41  ? 57  CYS L C   1 
ATOM   12693 O  O   . CYS L  1 58  ? 35.049  14.631  22.547 1.00 33.66  ? 57  CYS L O   1 
ATOM   12694 C  CB  . CYS L  1 58  ? 33.263  15.038  25.073 1.00 31.40  ? 57  CYS L CB  1 
ATOM   12695 S  SG  . CYS L  1 58  ? 31.657  14.586  25.780 1.00 39.01  ? 57  CYS L SG  1 
ATOM   12696 N  N   . THR L  1 59  ? 36.430  14.229  24.297 1.00 32.04  ? 58  THR L N   1 
ATOM   12697 C  CA  . THR L  1 59  ? 37.649  14.663  23.629 1.00 32.93  ? 58  THR L CA  1 
ATOM   12698 C  C   . THR L  1 59  ? 37.834  13.933  22.306 1.00 32.69  ? 58  THR L C   1 
ATOM   12699 O  O   . THR L  1 59  ? 38.286  14.527  21.328 1.00 30.86  ? 58  THR L O   1 
ATOM   12700 C  CB  . THR L  1 59  ? 38.907  14.328  24.433 1.00 33.88  ? 58  THR L CB  1 
ATOM   12701 O  OG1 . THR L  1 59  ? 38.686  14.781  25.765 1.00 37.42  ? 58  THR L OG1 1 
ATOM   12702 C  CG2 . THR L  1 59  ? 40.159  14.954  23.859 1.00 32.38  ? 58  THR L CG2 1 
ATOM   12703 N  N   . SER L  1 60  ? 37.506  12.637  22.292 1.00 33.76  ? 59  SER L N   1 
ATOM   12704 C  CA  . SER L  1 60  ? 37.887  11.813  21.158 1.00 33.26  ? 59  SER L CA  1 
ATOM   12705 C  C   . SER L  1 60  ? 36.953  12.053  19.974 1.00 33.18  ? 59  SER L C   1 
ATOM   12706 O  O   . SER L  1 60  ? 37.126  11.455  18.912 1.00 34.85  ? 59  SER L O   1 
ATOM   12707 C  CB  . SER L  1 60  ? 38.058  10.358  21.539 1.00 32.41  ? 59  SER L CB  1 
ATOM   12708 O  OG  . SER L  1 60  ? 36.903  9.868   22.187 1.00 33.15  ? 59  SER L OG  1 
ATOM   12709 N  N   . ALA L  1 61  ? 36.008  12.992  20.148 1.00 31.72  ? 60  ALA L N   1 
ATOM   12710 C  CA  . ALA L  1 61  ? 35.059  13.366  19.109 1.00 31.58  ? 60  ALA L CA  1 
ATOM   12711 C  C   . ALA L  1 61  ? 35.762  14.183  18.028 1.00 33.18  ? 60  ALA L C   1 
ATOM   12712 O  O   . ALA L  1 61  ? 35.245  14.323  16.919 1.00 37.57  ? 60  ALA L O   1 
ATOM   12713 C  CB  . ALA L  1 61  ? 33.914  14.129  19.713 1.00 29.88  ? 60  ALA L CB  1 
ATOM   12714 N  N   . GLY L  1 62  ? 36.937  14.724  18.372 1.00 30.79  ? 61  GLY L N   1 
ATOM   12715 C  CA  . GLY L  1 62  ? 37.730  15.513  17.446 1.00 30.64  ? 61  GLY L CA  1 
ATOM   12716 C  C   . GLY L  1 62  ? 37.192  16.938  17.293 1.00 31.75  ? 61  GLY L C   1 
ATOM   12717 O  O   . GLY L  1 62  ? 36.435  17.422  18.141 1.00 30.57  ? 61  GLY L O   1 
ATOM   12718 N  N   . PRO L  1 63  ? 37.552  17.644  16.192 1.00 31.57  ? 62  PRO L N   1 
ATOM   12719 C  CA  . PRO L  1 63  ? 37.175  19.048  15.990 1.00 29.34  ? 62  PRO L CA  1 
ATOM   12720 C  C   . PRO L  1 63  ? 35.746  19.180  15.458 1.00 29.74  ? 62  PRO L C   1 
ATOM   12721 O  O   . PRO L  1 63  ? 35.076  18.173  15.219 1.00 30.41  ? 62  PRO L O   1 
ATOM   12722 C  CB  . PRO L  1 63  ? 38.167  19.481  14.900 1.00 26.90  ? 62  PRO L CB  1 
ATOM   12723 C  CG  . PRO L  1 63  ? 38.333  18.248  14.051 1.00 28.54  ? 62  PRO L CG  1 
ATOM   12724 C  CD  . PRO L  1 63  ? 38.319  17.110  15.053 1.00 30.91  ? 62  PRO L CD  1 
ATOM   12725 N  N   . HIS L  1 64  ? 35.286  20.425  15.266 1.00 29.41  ? 63  HIS L N   1 
ATOM   12726 C  CA  . HIS L  1 64  ? 33.998  20.637  14.632 1.00 27.65  ? 63  HIS L CA  1 
ATOM   12727 C  C   . HIS L  1 64  ? 34.003  19.944  13.273 1.00 27.35  ? 63  HIS L C   1 
ATOM   12728 O  O   . HIS L  1 64  ? 34.987  20.037  12.553 1.00 26.35  ? 63  HIS L O   1 
ATOM   12729 C  CB  . HIS L  1 64  ? 33.682  22.121  14.471 1.00 26.36  ? 63  HIS L CB  1 
ATOM   12730 C  CG  . HIS L  1 64  ? 33.579  22.895  15.739 1.00 28.00  ? 63  HIS L CG  1 
ATOM   12731 N  ND1 . HIS L  1 64  ? 33.478  24.267  15.753 1.00 28.65  ? 63  HIS L ND1 1 
ATOM   12732 C  CD2 . HIS L  1 64  ? 33.576  22.520  17.026 1.00 27.97  ? 63  HIS L CD2 1 
ATOM   12733 C  CE1 . HIS L  1 64  ? 33.406  24.692  16.994 1.00 28.05  ? 63  HIS L CE1 1 
ATOM   12734 N  NE2 . HIS L  1 64  ? 33.453  23.638  17.792 1.00 28.79  ? 63  HIS L NE2 1 
ATOM   12735 N  N   . PHE L  1 65  ? 32.902  19.264  12.936 1.00 27.36  ? 64  PHE L N   1 
ATOM   12736 C  CA  . PHE L  1 65  ? 32.750  18.613  11.646 1.00 29.70  ? 64  PHE L CA  1 
ATOM   12737 C  C   . PHE L  1 65  ? 32.954  19.623  10.518 1.00 30.81  ? 64  PHE L C   1 
ATOM   12738 O  O   . PHE L  1 65  ? 32.177  20.561  10.370 1.00 30.72  ? 64  PHE L O   1 
ATOM   12739 C  CB  . PHE L  1 65  ? 31.397  17.899  11.559 1.00 29.99  ? 64  PHE L CB  1 
ATOM   12740 C  CG  . PHE L  1 65  ? 31.136  17.188  10.251 1.00 29.44  ? 64  PHE L CG  1 
ATOM   12741 C  CD1 . PHE L  1 65  ? 32.132  16.434  9.642  1.00 29.18  ? 64  PHE L CD1 1 
ATOM   12742 C  CD2 . PHE L  1 65  ? 29.892  17.254  9.637  1.00 28.83  ? 64  PHE L CD2 1 
ATOM   12743 C  CE1 . PHE L  1 65  ? 31.896  15.772  8.445  1.00 29.80  ? 64  PHE L CE1 1 
ATOM   12744 C  CE2 . PHE L  1 65  ? 29.658  16.588  8.442  1.00 29.72  ? 64  PHE L CE2 1 
ATOM   12745 C  CZ  . PHE L  1 65  ? 30.657  15.848  7.849  1.00 30.91  ? 64  PHE L CZ  1 
ATOM   12746 N  N   . ASN L  1 66  ? 33.995  19.407  9.705  1.00 31.96  ? 65  ASN L N   1 
ATOM   12747 C  CA  . ASN L  1 66  ? 34.431  20.454  8.801  1.00 36.43  ? 65  ASN L CA  1 
ATOM   12748 C  C   . ASN L  1 66  ? 34.777  19.889  7.423  1.00 39.54  ? 65  ASN L C   1 
ATOM   12749 O  O   . ASN L  1 66  ? 35.879  20.107  6.921  1.00 44.28  ? 65  ASN L O   1 
ATOM   12750 C  CB  . ASN L  1 66  ? 35.579  21.255  9.428  1.00 36.00  ? 65  ASN L CB  1 
ATOM   12751 C  CG  . ASN L  1 66  ? 35.997  22.440  8.588  1.00 35.94  ? 65  ASN L CG  1 
ATOM   12752 O  OD1 . ASN L  1 66  ? 35.247  22.916  7.741  1.00 34.35  ? 65  ASN L OD1 1 
ATOM   12753 N  ND2 . ASN L  1 66  ? 37.204  22.917  8.812  1.00 38.87  ? 65  ASN L ND2 1 
ATOM   12754 N  N   . PRO L  1 67  ? 33.849  19.212  6.710  1.00 42.14  ? 66  PRO L N   1 
ATOM   12755 C  CA  . PRO L  1 67  ? 34.199  18.557  5.447  1.00 41.48  ? 66  PRO L CA  1 
ATOM   12756 C  C   . PRO L  1 67  ? 34.659  19.498  4.335  1.00 42.83  ? 66  PRO L C   1 
ATOM   12757 O  O   . PRO L  1 67  ? 35.286  19.058  3.383  1.00 45.33  ? 66  PRO L O   1 
ATOM   12758 C  CB  . PRO L  1 67  ? 32.912  17.846  5.014  1.00 39.05  ? 66  PRO L CB  1 
ATOM   12759 C  CG  . PRO L  1 67  ? 31.821  18.569  5.743  1.00 41.51  ? 66  PRO L CG  1 
ATOM   12760 C  CD  . PRO L  1 67  ? 32.425  19.078  7.035  1.00 43.95  ? 66  PRO L CD  1 
ATOM   12761 N  N   . LEU L  1 68  ? 34.346  20.791  4.452  1.00 43.21  ? 67  LEU L N   1 
ATOM   12762 C  CA  . LEU L  1 68  ? 34.648  21.736  3.384  1.00 38.70  ? 67  LEU L CA  1 
ATOM   12763 C  C   . LEU L  1 68  ? 35.885  22.575  3.709  1.00 40.40  ? 67  LEU L C   1 
ATOM   12764 O  O   . LEU L  1 68  ? 36.203  23.495  2.964  1.00 41.63  ? 67  LEU L O   1 
ATOM   12765 C  CB  . LEU L  1 68  ? 33.430  22.630  3.130  1.00 38.41  ? 67  LEU L CB  1 
ATOM   12766 C  CG  . LEU L  1 68  ? 32.203  21.944  2.524  1.00 39.27  ? 67  LEU L CG  1 
ATOM   12767 C  CD1 . LEU L  1 68  ? 31.079  22.944  2.291  1.00 35.80  ? 67  LEU L CD1 1 
ATOM   12768 C  CD2 . LEU L  1 68  ? 32.583  21.162  1.270  1.00 36.90  ? 67  LEU L CD2 1 
ATOM   12769 N  N   . SER L  1 69  ? 36.564  22.267  4.825  1.00 42.10  ? 68  SER L N   1 
ATOM   12770 C  CA  . SER L  1 69  ? 37.801  22.924  5.231  1.00 42.71  ? 68  SER L CA  1 
ATOM   12771 C  C   . SER L  1 69  ? 37.657  24.441  5.311  1.00 39.68  ? 68  SER L C   1 
ATOM   12772 O  O   . SER L  1 69  ? 38.456  25.151  4.711  1.00 40.13  ? 68  SER L O   1 
ATOM   12773 C  CB  . SER L  1 69  ? 38.932  22.583  4.290  1.00 42.86  ? 68  SER L CB  1 
ATOM   12774 O  OG  . SER L  1 69  ? 39.255  21.213  4.371  1.00 46.96  ? 68  SER L OG  1 
ATOM   12775 N  N   . ARG L  1 70  ? 36.659  24.931  6.051  1.00 37.93  ? 69  ARG L N   1 
ATOM   12776 C  CA  . ARG L  1 70  ? 36.470  26.362  6.246  1.00 40.81  ? 69  ARG L CA  1 
ATOM   12777 C  C   . ARG L  1 70  ? 36.821  26.723  7.688  1.00 41.67  ? 69  ARG L C   1 
ATOM   12778 O  O   . ARG L  1 70  ? 37.089  25.842  8.507  1.00 43.05  ? 69  ARG L O   1 
ATOM   12779 C  CB  . ARG L  1 70  ? 35.030  26.777  5.930  1.00 41.97  ? 69  ARG L CB  1 
ATOM   12780 C  CG  . ARG L  1 70  ? 34.522  26.315  4.574  1.00 46.43  ? 69  ARG L CG  1 
ATOM   12781 C  CD  . ARG L  1 70  ? 34.749  27.290  3.422  1.00 52.15  ? 69  ARG L CD  1 
ATOM   12782 N  NE  . ARG L  1 70  ? 33.889  26.838  2.321  1.00 58.74  ? 69  ARG L NE  1 
ATOM   12783 C  CZ  . ARG L  1 70  ? 32.604  27.161  2.138  1.00 63.05  ? 69  ARG L CZ  1 
ATOM   12784 N  NH1 . ARG L  1 70  ? 31.998  27.981  2.978  1.00 67.87  ? 69  ARG L NH1 1 
ATOM   12785 N  NH2 . ARG L  1 70  ? 31.930  26.651  1.127  1.00 67.20  ? 69  ARG L NH2 1 
ATOM   12786 N  N   . LYS L  1 71  ? 36.825  28.031  7.982  1.00 39.82  ? 70  LYS L N   1 
ATOM   12787 C  CA  . LYS L  1 71  ? 37.068  28.523  9.330  1.00 41.08  ? 70  LYS L CA  1 
ATOM   12788 C  C   . LYS L  1 71  ? 35.734  28.533  10.085 1.00 38.76  ? 70  LYS L C   1 
ATOM   12789 O  O   . LYS L  1 71  ? 34.657  28.493  9.471  1.00 35.31  ? 70  LYS L O   1 
ATOM   12790 C  CB  . LYS L  1 71  ? 37.818  29.859  9.310  1.00 43.79  ? 70  LYS L CB  1 
ATOM   12791 C  CG  . LYS L  1 71  ? 39.112  29.853  8.501  1.00 47.84  ? 70  LYS L CG  1 
ATOM   12792 C  CD  . LYS L  1 71  ? 39.791  31.197  8.476  1.00 53.02  ? 70  LYS L CD  1 
ATOM   12793 C  CE  . LYS L  1 71  ? 40.458  31.562  7.154  1.00 54.98  ? 70  LYS L CE  1 
ATOM   12794 N  NZ  . LYS L  1 71  ? 40.489  33.030  6.945  1.00 51.90  ? 70  LYS L NZ  1 
ATOM   12795 N  N   . HIS L  1 72  ? 35.815  28.560  11.424 1.00 35.65  ? 71  HIS L N   1 
ATOM   12796 C  CA  . HIS L  1 72  ? 34.639  28.497  12.273 1.00 34.70  ? 71  HIS L CA  1 
ATOM   12797 C  C   . HIS L  1 72  ? 33.800  29.764  12.129 1.00 37.16  ? 71  HIS L C   1 
ATOM   12798 O  O   . HIS L  1 72  ? 34.340  30.854  12.040 1.00 39.34  ? 71  HIS L O   1 
ATOM   12799 C  CB  . HIS L  1 72  ? 35.073  28.239  13.723 1.00 34.97  ? 71  HIS L CB  1 
ATOM   12800 C  CG  . HIS L  1 72  ? 33.948  28.281  14.694 1.00 33.59  ? 71  HIS L CG  1 
ATOM   12801 N  ND1 . HIS L  1 72  ? 33.134  27.188  14.965 1.00 31.39  ? 71  HIS L ND1 1 
ATOM   12802 C  CD2 . HIS L  1 72  ? 33.495  29.279  15.466 1.00 33.47  ? 71  HIS L CD2 1 
ATOM   12803 C  CE1 . HIS L  1 72  ? 32.230  27.538  15.856 1.00 31.30  ? 71  HIS L CE1 1 
ATOM   12804 N  NE2 . HIS L  1 72  ? 32.428  28.810  16.179 1.00 32.64  ? 71  HIS L NE2 1 
ATOM   12805 N  N   . GLY L  1 73  ? 32.474  29.605  12.097 1.00 39.47  ? 72  GLY L N   1 
ATOM   12806 C  CA  . GLY L  1 73  ? 31.552  30.725  12.059 1.00 37.92  ? 72  GLY L CA  1 
ATOM   12807 C  C   . GLY L  1 73  ? 30.315  30.476  12.918 1.00 37.08  ? 72  GLY L C   1 
ATOM   12808 O  O   . GLY L  1 73  ? 30.233  29.461  13.597 1.00 42.15  ? 72  GLY L O   1 
ATOM   12809 N  N   . GLY L  1 74  ? 29.398  31.449  12.928 1.00 33.43  ? 73  GLY L N   1 
ATOM   12810 C  CA  . GLY L  1 74  ? 28.044  31.254  13.414 1.00 33.60  ? 73  GLY L CA  1 
ATOM   12811 C  C   . GLY L  1 74  ? 27.204  30.558  12.348 1.00 35.65  ? 73  GLY L C   1 
ATOM   12812 O  O   . GLY L  1 74  ? 27.575  30.565  11.174 1.00 32.28  ? 73  GLY L O   1 
ATOM   12813 N  N   . PRO L  1 75  ? 26.067  29.912  12.706 1.00 39.20  ? 74  PRO L N   1 
ATOM   12814 C  CA  . PRO L  1 75  ? 25.284  29.149  11.730 1.00 38.49  ? 74  PRO L CA  1 
ATOM   12815 C  C   . PRO L  1 75  ? 24.874  29.981  10.521 1.00 37.64  ? 74  PRO L C   1 
ATOM   12816 O  O   . PRO L  1 75  ? 24.726  29.447  9.428  1.00 35.52  ? 74  PRO L O   1 
ATOM   12817 C  CB  . PRO L  1 75  ? 24.047  28.665  12.505 1.00 37.07  ? 74  PRO L CB  1 
ATOM   12818 C  CG  . PRO L  1 75  ? 24.046  29.482  13.795 1.00 35.91  ? 74  PRO L CG  1 
ATOM   12819 C  CD  . PRO L  1 75  ? 25.491  29.853  14.060 1.00 39.05  ? 74  PRO L CD  1 
ATOM   12820 N  N   . LYS L  1 76  ? 24.735  31.299  10.720 1.00 40.32  ? 75  LYS L N   1 
ATOM   12821 C  CA  . LYS L  1 76  ? 24.204  32.164  9.680  1.00 41.95  ? 75  LYS L CA  1 
ATOM   12822 C  C   . LYS L  1 76  ? 25.289  32.643  8.724  1.00 41.90  ? 75  LYS L C   1 
ATOM   12823 O  O   . LYS L  1 76  ? 24.960  33.190  7.681  1.00 41.36  ? 75  LYS L O   1 
ATOM   12824 C  CB  . LYS L  1 76  ? 23.341  33.288  10.259 1.00 43.98  ? 75  LYS L CB  1 
ATOM   12825 C  CG  . LYS L  1 76  ? 21.939  32.837  10.688 1.00 51.12  ? 75  LYS L CG  1 
ATOM   12826 C  CD  . LYS L  1 76  ? 20.674  33.642  10.344 1.00 60.52  ? 75  LYS L CD  1 
ATOM   12827 C  CE  . LYS L  1 76  ? 19.525  32.709  9.996  1.00 62.27  ? 75  LYS L CE  1 
ATOM   12828 N  NZ  . LYS L  1 76  ? 18.222  33.249  10.443 1.00 63.16  ? 75  LYS L NZ  1 
ATOM   12829 N  N   . ASP L  1 77  ? 26.562  32.404  9.051  1.00 44.90  ? 76  ASP L N   1 
ATOM   12830 C  CA  . ASP L  1 77  ? 27.704  32.847  8.253  1.00 46.28  ? 76  ASP L CA  1 
ATOM   12831 C  C   . ASP L  1 77  ? 27.875  31.957  7.025  1.00 46.24  ? 76  ASP L C   1 
ATOM   12832 O  O   . ASP L  1 77  ? 27.543  30.775  7.058  1.00 44.75  ? 76  ASP L O   1 
ATOM   12833 C  CB  . ASP L  1 77  ? 28.991  32.876  9.087  1.00 46.15  ? 76  ASP L CB  1 
ATOM   12834 C  CG  . ASP L  1 77  ? 28.986  33.978  10.125 1.00 49.87  ? 76  ASP L CG  1 
ATOM   12835 O  OD1 . ASP L  1 77  ? 28.386  35.017  9.836  1.00 60.16  ? 76  ASP L OD1 1 
ATOM   12836 O  OD2 . ASP L  1 77  ? 29.573  33.789  11.214 1.00 48.36  ? 76  ASP L OD2 1 
ATOM   12837 N  N   . GLU L  1 78  ? 28.409  32.526  5.944  1.00 52.66  ? 77  GLU L N   1 
ATOM   12838 C  CA  . GLU L  1 78  ? 28.756  31.695  4.808  1.00 60.61  ? 77  GLU L CA  1 
ATOM   12839 C  C   . GLU L  1 78  ? 30.035  30.923  5.141  1.00 62.71  ? 77  GLU L C   1 
ATOM   12840 O  O   . GLU L  1 78  ? 30.177  29.758  4.777  1.00 58.91  ? 77  GLU L O   1 
ATOM   12841 C  CB  . GLU L  1 78  ? 28.822  32.502  3.511  1.00 65.92  ? 77  GLU L CB  1 
ATOM   12842 C  CG  . GLU L  1 78  ? 28.728  31.594  2.290  1.00 77.68  ? 77  GLU L CG  1 
ATOM   12843 C  CD  . GLU L  1 78  ? 29.789  31.754  1.208  1.00 82.76  ? 77  GLU L CD  1 
ATOM   12844 O  OE1 . GLU L  1 78  ? 29.992  32.906  0.784  1.00 85.84  ? 77  GLU L OE1 1 
ATOM   12845 O  OE2 . GLU L  1 78  ? 30.432  30.729  0.814  1.00 76.08  ? 77  GLU L OE2 1 
ATOM   12846 N  N   . GLU L  1 79  ? 30.960  31.589  5.840  1.00 59.96  ? 78  GLU L N   1 
ATOM   12847 C  CA  . GLU L  1 79  ? 32.193  30.970  6.310  1.00 52.40  ? 78  GLU L CA  1 
ATOM   12848 C  C   . GLU L  1 79  ? 31.927  30.295  7.663  1.00 45.37  ? 78  GLU L C   1 
ATOM   12849 O  O   . GLU L  1 79  ? 31.979  30.931  8.717  1.00 45.37  ? 78  GLU L O   1 
ATOM   12850 C  CB  . GLU L  1 79  ? 33.323  32.012  6.286  1.00 55.52  ? 78  GLU L CB  1 
ATOM   12851 C  CG  . GLU L  1 79  ? 34.729  31.491  6.598  1.00 56.21  ? 78  GLU L CG  1 
ATOM   12852 C  CD  . GLU L  1 79  ? 35.418  30.582  5.589  1.00 63.58  ? 78  GLU L CD  1 
ATOM   12853 O  OE1 . GLU L  1 79  ? 34.877  30.399  4.474  1.00 69.46  ? 78  GLU L OE1 1 
ATOM   12854 O  OE2 . GLU L  1 79  ? 36.500  30.048  5.923  1.00 65.15  ? 78  GLU L OE2 1 
ATOM   12855 N  N   . ARG L  1 80  ? 31.619  28.992  7.606  1.00 37.25  ? 79  ARG L N   1 
ATOM   12856 C  CA  . ARG L  1 80  ? 31.381  28.186  8.794  1.00 33.74  ? 79  ARG L CA  1 
ATOM   12857 C  C   . ARG L  1 80  ? 31.764  26.732  8.547  1.00 35.05  ? 79  ARG L C   1 
ATOM   12858 O  O   . ARG L  1 80  ? 31.842  26.275  7.406  1.00 36.01  ? 79  ARG L O   1 
ATOM   12859 C  CB  . ARG L  1 80  ? 29.905  28.222  9.205  1.00 31.08  ? 79  ARG L CB  1 
ATOM   12860 C  CG  . ARG L  1 80  ? 28.943  27.753  8.131  1.00 29.66  ? 79  ARG L CG  1 
ATOM   12861 C  CD  . ARG L  1 80  ? 27.535  27.645  8.679  1.00 29.01  ? 79  ARG L CD  1 
ATOM   12862 N  NE  . ARG L  1 80  ? 27.263  26.324  9.239  1.00 30.23  ? 79  ARG L NE  1 
ATOM   12863 C  CZ  . ARG L  1 80  ? 26.056  25.856  9.558  1.00 29.56  ? 79  ARG L CZ  1 
ATOM   12864 N  NH1 . ARG L  1 80  ? 24.978  26.604  9.388  1.00 31.29  ? 79  ARG L NH1 1 
ATOM   12865 N  NH2 . ARG L  1 80  ? 25.926  24.637  10.047 1.00 28.64  ? 79  ARG L NH2 1 
ATOM   12866 N  N   . HIS L  1 81  ? 31.998  26.015  9.653  1.00 34.07  ? 80  HIS L N   1 
ATOM   12867 C  CA  . HIS L  1 81  ? 32.037  24.566  9.663  1.00 29.52  ? 80  HIS L CA  1 
ATOM   12868 C  C   . HIS L  1 81  ? 30.616  24.049  9.467  1.00 31.07  ? 80  HIS L C   1 
ATOM   12869 O  O   . HIS L  1 81  ? 29.664  24.656  9.956  1.00 32.21  ? 80  HIS L O   1 
ATOM   12870 C  CB  . HIS L  1 81  ? 32.558  24.083  11.017 1.00 27.40  ? 80  HIS L CB  1 
ATOM   12871 C  CG  . HIS L  1 81  ? 33.925  24.559  11.340 1.00 27.47  ? 80  HIS L CG  1 
ATOM   12872 N  ND1 . HIS L  1 81  ? 34.322  24.859  12.626 1.00 28.31  ? 80  HIS L ND1 1 
ATOM   12873 C  CD2 . HIS L  1 81  ? 34.998  24.771  10.551 1.00 28.14  ? 80  HIS L CD2 1 
ATOM   12874 C  CE1 . HIS L  1 81  ? 35.590  25.223  12.623 1.00 28.44  ? 80  HIS L CE1 1 
ATOM   12875 N  NE2 . HIS L  1 81  ? 36.027  25.192  11.358 1.00 28.90  ? 80  HIS L NE2 1 
ATOM   12876 N  N   . VAL L  1 82  ? 30.486  22.912  8.776  1.00 32.21  ? 81  VAL L N   1 
ATOM   12877 C  CA  . VAL L  1 82  ? 29.185  22.271  8.653  1.00 30.28  ? 81  VAL L CA  1 
ATOM   12878 C  C   . VAL L  1 82  ? 28.583  22.066  10.043 1.00 28.52  ? 81  VAL L C   1 
ATOM   12879 O  O   . VAL L  1 82  ? 27.394  22.270  10.230 1.00 30.32  ? 81  VAL L O   1 
ATOM   12880 C  CB  . VAL L  1 82  ? 29.237  20.967  7.835  1.00 28.90  ? 81  VAL L CB  1 
ATOM   12881 C  CG1 . VAL L  1 82  ? 27.986  20.129  8.016  1.00 26.94  ? 81  VAL L CG1 1 
ATOM   12882 C  CG2 . VAL L  1 82  ? 29.474  21.253  6.359  1.00 27.71  ? 81  VAL L CG2 1 
ATOM   12883 N  N   . GLY L  1 83  ? 29.412  21.712  11.024 1.00 27.53  ? 82  GLY L N   1 
ATOM   12884 C  CA  . GLY L  1 83  ? 28.907  21.378  12.343 1.00 29.56  ? 82  GLY L CA  1 
ATOM   12885 C  C   . GLY L  1 83  ? 28.585  22.591  13.218 1.00 30.23  ? 82  GLY L C   1 
ATOM   12886 O  O   . GLY L  1 83  ? 28.239  22.419  14.392 1.00 33.64  ? 82  GLY L O   1 
ATOM   12887 N  N   . ASP L  1 84  ? 28.725  23.800  12.658 1.00 28.33  ? 83  ASP L N   1 
ATOM   12888 C  CA  . ASP L  1 84  ? 28.620  25.041  13.418 1.00 28.60  ? 83  ASP L CA  1 
ATOM   12889 C  C   . ASP L  1 84  ? 27.159  25.437  13.633 1.00 29.02  ? 83  ASP L C   1 
ATOM   12890 O  O   . ASP L  1 84  ? 26.552  26.069  12.768 1.00 28.44  ? 83  ASP L O   1 
ATOM   12891 C  CB  . ASP L  1 84  ? 29.443  26.163  12.773 1.00 27.11  ? 83  ASP L CB  1 
ATOM   12892 C  CG  . ASP L  1 84  ? 30.938  26.041  12.980 1.00 27.04  ? 83  ASP L CG  1 
ATOM   12893 O  OD1 . ASP L  1 84  ? 31.346  25.288  13.878 1.00 29.44  ? 83  ASP L OD1 1 
ATOM   12894 O  OD2 . ASP L  1 84  ? 31.691  26.713  12.259 1.00 26.49  ? 83  ASP L OD2 1 
ATOM   12895 N  N   . LEU L  1 85  ? 26.603  25.082  14.800 1.00 29.04  ? 84  LEU L N   1 
ATOM   12896 C  CA  . LEU L  1 85  ? 25.184  25.310  15.040 1.00 28.35  ? 84  LEU L CA  1 
ATOM   12897 C  C   . LEU L  1 85  ? 24.967  26.470  16.011 1.00 30.42  ? 84  LEU L C   1 
ATOM   12898 O  O   . LEU L  1 85  ? 23.847  26.674  16.478 1.00 34.55  ? 84  LEU L O   1 
ATOM   12899 C  CB  . LEU L  1 85  ? 24.537  24.023  15.566 1.00 25.48  ? 84  LEU L CB  1 
ATOM   12900 C  CG  . LEU L  1 85  ? 24.361  22.883  14.566 1.00 23.79  ? 84  LEU L CG  1 
ATOM   12901 C  CD1 . LEU L  1 85  ? 23.590  21.740  15.202 1.00 21.13  ? 84  LEU L CD1 1 
ATOM   12902 C  CD2 . LEU L  1 85  ? 23.647  23.351  13.312 1.00 23.48  ? 84  LEU L CD2 1 
ATOM   12903 N  N   . GLY L  1 86  ? 26.030  27.219  16.326 1.00 30.18  ? 85  GLY L N   1 
ATOM   12904 C  CA  . GLY L  1 86  ? 25.882  28.413  17.155 1.00 28.79  ? 85  GLY L CA  1 
ATOM   12905 C  C   . GLY L  1 86  ? 25.699  28.079  18.639 1.00 26.18  ? 85  GLY L C   1 
ATOM   12906 O  O   . GLY L  1 86  ? 26.399  27.214  19.165 1.00 25.67  ? 85  GLY L O   1 
ATOM   12907 N  N   . ASN L  1 87  ? 24.787  28.802  19.304 1.00 24.51  ? 86  ASN L N   1 
ATOM   12908 C  CA  . ASN L  1 87  ? 24.608  28.682  20.744 1.00 23.80  ? 86  ASN L CA  1 
ATOM   12909 C  C   . ASN L  1 87  ? 23.215  28.166  21.095 1.00 23.01  ? 86  ASN L C   1 
ATOM   12910 O  O   . ASN L  1 87  ? 22.265  28.278  20.322 1.00 21.57  ? 86  ASN L O   1 
ATOM   12911 C  CB  . ASN L  1 87  ? 24.828  30.000  21.480 1.00 24.61  ? 86  ASN L CB  1 
ATOM   12912 C  CG  . ASN L  1 87  ? 26.267  30.461  21.405 1.00 26.64  ? 86  ASN L CG  1 
ATOM   12913 O  OD1 . ASN L  1 87  ? 27.131  29.925  22.090 1.00 31.40  ? 86  ASN L OD1 1 
ATOM   12914 N  ND2 . ASN L  1 87  ? 26.543  31.427  20.548 1.00 28.15  ? 86  ASN L ND2 1 
ATOM   12915 N  N   . VAL L  1 88  ? 23.122  27.589  22.290 1.00 21.82  ? 87  VAL L N   1 
ATOM   12916 C  CA  . VAL L  1 88  ? 21.849  27.313  22.929 1.00 21.70  ? 87  VAL L CA  1 
ATOM   12917 C  C   . VAL L  1 88  ? 21.834  28.108  24.234 1.00 22.46  ? 87  VAL L C   1 
ATOM   12918 O  O   . VAL L  1 88  ? 22.898  28.483  24.735 1.00 22.40  ? 87  VAL L O   1 
ATOM   12919 C  CB  . VAL L  1 88  ? 21.620  25.798  23.129 1.00 20.68  ? 87  VAL L CB  1 
ATOM   12920 C  CG1 . VAL L  1 88  ? 21.653  25.038  21.811 1.00 19.06  ? 87  VAL L CG1 1 
ATOM   12921 C  CG2 . VAL L  1 88  ? 22.589  25.184  24.127 1.00 19.61  ? 87  VAL L CG2 1 
ATOM   12922 N  N   . THR L  1 89  ? 20.637  28.402  24.756 1.00 22.66  ? 88  THR L N   1 
ATOM   12923 C  CA  . THR L  1 89  ? 20.551  29.282  25.911 1.00 23.42  ? 88  THR L CA  1 
ATOM   12924 C  C   . THR L  1 89  ? 19.948  28.535  27.092 1.00 23.31  ? 88  THR L C   1 
ATOM   12925 O  O   . THR L  1 89  ? 18.846  28.014  26.984 1.00 24.40  ? 88  THR L O   1 
ATOM   12926 C  CB  . THR L  1 89  ? 19.695  30.523  25.623 1.00 22.16  ? 88  THR L CB  1 
ATOM   12927 O  OG1 . THR L  1 89  ? 20.157  31.163  24.431 1.00 23.54  ? 88  THR L OG1 1 
ATOM   12928 C  CG2 . THR L  1 89  ? 19.650  31.478  26.797 1.00 21.14  ? 88  THR L CG2 1 
ATOM   12929 N  N   . ALA L  1 90  ? 20.661  28.518  28.216 1.00 23.75  ? 89  ALA L N   1 
ATOM   12930 C  CA  . ALA L  1 90  ? 20.126  27.934  29.433 1.00 26.85  ? 89  ALA L CA  1 
ATOM   12931 C  C   . ALA L  1 90  ? 19.489  29.013  30.309 1.00 28.37  ? 89  ALA L C   1 
ATOM   12932 O  O   . ALA L  1 90  ? 20.083  30.075  30.529 1.00 28.03  ? 89  ALA L O   1 
ATOM   12933 C  CB  . ALA L  1 90  ? 21.230  27.216  30.166 1.00 29.22  ? 89  ALA L CB  1 
ATOM   12934 N  N   . ASP L  1 91  ? 18.285  28.710  30.820 1.00 30.17  ? 90  ASP L N   1 
ATOM   12935 C  CA  . ASP L  1 91  ? 17.532  29.577  31.717 1.00 33.38  ? 90  ASP L CA  1 
ATOM   12936 C  C   . ASP L  1 91  ? 18.124  29.529  33.124 1.00 34.83  ? 90  ASP L C   1 
ATOM   12937 O  O   . ASP L  1 91  ? 19.106  28.827  33.347 1.00 32.50  ? 90  ASP L O   1 
ATOM   12938 C  CB  . ASP L  1 91  ? 16.040  29.232  31.698 1.00 36.62  ? 90  ASP L CB  1 
ATOM   12939 C  CG  . ASP L  1 91  ? 15.673  27.851  32.228 1.00 40.50  ? 90  ASP L CG  1 
ATOM   12940 O  OD1 . ASP L  1 91  ? 16.454  27.267  32.999 1.00 39.66  ? 90  ASP L OD1 1 
ATOM   12941 O  OD2 . ASP L  1 91  ? 14.585  27.360  31.869 1.00 43.16  ? 90  ASP L OD2 1 
ATOM   12942 N  N   . LYS L  1 92  ? 17.515  30.263  34.070 1.00 39.01  ? 91  LYS L N   1 
ATOM   12943 C  CA  . LYS L  1 92  ? 18.047  30.390  35.427 1.00 40.04  ? 91  LYS L CA  1 
ATOM   12944 C  C   . LYS L  1 92  ? 18.123  29.028  36.116 1.00 38.43  ? 91  LYS L C   1 
ATOM   12945 O  O   . LYS L  1 92  ? 18.846  28.890  37.102 1.00 39.02  ? 91  LYS L O   1 
ATOM   12946 C  CB  . LYS L  1 92  ? 17.277  31.393  36.296 1.00 40.97  ? 91  LYS L CB  1 
ATOM   12947 C  CG  . LYS L  1 92  ? 15.837  31.022  36.653 1.00 46.90  ? 91  LYS L CG  1 
ATOM   12948 C  CD  . LYS L  1 92  ? 15.053  32.115  37.294 1.00 53.28  ? 91  LYS L CD  1 
ATOM   12949 C  CE  . LYS L  1 92  ? 13.580  32.027  36.939 1.00 64.76  ? 91  LYS L CE  1 
ATOM   12950 N  NZ  . LYS L  1 92  ? 12.751  32.565  38.033 1.00 71.13  ? 91  LYS L NZ  1 
ATOM   12951 N  N   . ASP L  1 93  ? 17.372  28.036  35.598 1.00 39.90  ? 92  ASP L N   1 
ATOM   12952 C  CA  . ASP L  1 93  ? 17.313  26.717  36.200 1.00 39.14  ? 92  ASP L CA  1 
ATOM   12953 C  C   . ASP L  1 93  ? 18.310  25.764  35.549 1.00 37.16  ? 92  ASP L C   1 
ATOM   12954 O  O   . ASP L  1 93  ? 18.388  24.601  35.927 1.00 35.77  ? 92  ASP L O   1 
ATOM   12955 C  CB  . ASP L  1 93  ? 15.907  26.135  36.063 1.00 41.64  ? 92  ASP L CB  1 
ATOM   12956 C  CG  . ASP L  1 93  ? 14.905  26.863  36.951 1.00 42.94  ? 92  ASP L CG  1 
ATOM   12957 O  OD1 . ASP L  1 93  ? 15.250  27.214  38.105 1.00 37.31  ? 92  ASP L OD1 1 
ATOM   12958 O  OD2 . ASP L  1 93  ? 13.778  27.080  36.482 1.00 47.56  ? 92  ASP L OD2 1 
ATOM   12959 N  N   . GLY L  1 94  ? 19.041  26.256  34.554 1.00 36.70  ? 93  GLY L N   1 
ATOM   12960 C  CA  . GLY L  1 94  ? 20.059  25.456  33.904 1.00 33.36  ? 93  GLY L CA  1 
ATOM   12961 C  C   . GLY L  1 94  ? 19.476  24.564  32.815 1.00 31.99  ? 93  GLY L C   1 
ATOM   12962 O  O   . GLY L  1 94  ? 20.088  23.569  32.451 1.00 31.58  ? 93  GLY L O   1 
ATOM   12963 N  N   . VAL L  1 95  ? 18.306  24.940  32.295 1.00 28.59  ? 94  VAL L N   1 
ATOM   12964 C  CA  . VAL L  1 95  ? 17.678  24.175  31.233 1.00 26.76  ? 94  VAL L CA  1 
ATOM   12965 C  C   . VAL L  1 95  ? 17.701  24.968  29.931 1.00 26.26  ? 94  VAL L C   1 
ATOM   12966 O  O   . VAL L  1 95  ? 17.268  26.116  29.897 1.00 26.59  ? 94  VAL L O   1 
ATOM   12967 C  CB  . VAL L  1 95  ? 16.244  23.752  31.604 1.00 25.25  ? 94  VAL L CB  1 
ATOM   12968 C  CG1 . VAL L  1 95  ? 15.544  23.031  30.448 1.00 23.17  ? 94  VAL L CG1 1 
ATOM   12969 C  CG2 . VAL L  1 95  ? 16.224  22.914  32.873 1.00 24.12  ? 94  VAL L CG2 1 
ATOM   12970 N  N   . ALA L  1 96  ? 18.197  24.330  28.866 1.00 25.94  ? 95  ALA L N   1 
ATOM   12971 C  CA  . ALA L  1 96  ? 18.131  24.929  27.549 1.00 27.70  ? 95  ALA L CA  1 
ATOM   12972 C  C   . ALA L  1 96  ? 17.069  24.210  26.721 1.00 29.71  ? 95  ALA L C   1 
ATOM   12973 O  O   . ALA L  1 96  ? 17.207  23.012  26.454 1.00 33.38  ? 95  ALA L O   1 
ATOM   12974 C  CB  . ALA L  1 96  ? 19.484  24.821  26.885 1.00 26.57  ? 95  ALA L CB  1 
ATOM   12975 N  N   . ASP L  1 97  ? 16.028  24.933  26.307 1.00 29.61  ? 96  ASP L N   1 
ATOM   12976 C  CA  . ASP L  1 97  ? 15.061  24.342  25.385 1.00 31.21  ? 96  ASP L CA  1 
ATOM   12977 C  C   . ASP L  1 97  ? 15.527  24.591  23.961 1.00 29.28  ? 96  ASP L C   1 
ATOM   12978 O  O   . ASP L  1 97  ? 15.295  25.651  23.409 1.00 33.40  ? 96  ASP L O   1 
ATOM   12979 C  CB  . ASP L  1 97  ? 13.612  24.793  25.622 1.00 35.76  ? 96  ASP L CB  1 
ATOM   12980 C  CG  . ASP L  1 97  ? 13.071  24.325  26.961 1.00 44.42  ? 96  ASP L CG  1 
ATOM   12981 O  OD1 . ASP L  1 97  ? 13.194  23.084  27.283 1.00 46.52  ? 96  ASP L OD1 1 
ATOM   12982 O  OD2 . ASP L  1 97  ? 12.563  25.206  27.690 1.00 50.22  ? 96  ASP L OD2 1 
ATOM   12983 N  N   . VAL L  1 98  ? 16.216  23.609  23.398 1.00 27.10  ? 97  VAL L N   1 
ATOM   12984 C  CA  . VAL L  1 98  ? 16.824  23.764  22.087 1.00 26.96  ? 97  VAL L CA  1 
ATOM   12985 C  C   . VAL L  1 98  ? 15.761  23.700  20.994 1.00 27.96  ? 97  VAL L C   1 
ATOM   12986 O  O   . VAL L  1 98  ? 14.904  22.830  20.998 1.00 31.02  ? 97  VAL L O   1 
ATOM   12987 C  CB  . VAL L  1 98  ? 17.913  22.706  21.863 1.00 24.88  ? 97  VAL L CB  1 
ATOM   12988 C  CG1 . VAL L  1 98  ? 18.597  22.935  20.523 1.00 25.20  ? 97  VAL L CG1 1 
ATOM   12989 C  CG2 . VAL L  1 98  ? 18.916  22.696  23.012 1.00 23.68  ? 97  VAL L CG2 1 
ATOM   12990 N  N   . SER L  1 99  ? 15.851  24.617  20.043 1.00 29.06  ? 98  SER L N   1 
ATOM   12991 C  CA  . SER L  1 99  ? 15.035  24.573  18.844 1.00 28.39  ? 98  SER L CA  1 
ATOM   12992 C  C   . SER L  1 99  ? 15.724  25.381  17.745 1.00 28.43  ? 98  SER L C   1 
ATOM   12993 O  O   . SER L  1 99  ? 15.828  26.600  17.843 1.00 29.03  ? 98  SER L O   1 
ATOM   12994 C  CB  . SER L  1 99  ? 13.661  25.086  19.126 1.00 27.78  ? 98  SER L CB  1 
ATOM   12995 O  OG  . SER L  1 99  ? 12.906  25.091  17.934 1.00 29.84  ? 98  SER L OG  1 
ATOM   12996 N  N   . ILE L  1 100 ? 16.229  24.682  16.729 1.00 26.91  ? 99  ILE L N   1 
ATOM   12997 C  CA  . ILE L  1 100 ? 17.081  25.282  15.716 1.00 27.16  ? 99  ILE L CA  1 
ATOM   12998 C  C   . ILE L  1 100 ? 16.653  24.717  14.371 1.00 27.34  ? 99  ILE L C   1 
ATOM   12999 O  O   . ILE L  1 100 ? 16.194  23.584  14.283 1.00 26.65  ? 99  ILE L O   1 
ATOM   13000 C  CB  . ILE L  1 100 ? 18.567  24.969  15.992 1.00 26.18  ? 99  ILE L CB  1 
ATOM   13001 C  CG1 . ILE L  1 100 ? 19.114  25.835  17.127 1.00 24.30  ? 99  ILE L CG1 1 
ATOM   13002 C  CG2 . ILE L  1 100 ? 19.427  25.064  14.732 1.00 25.06  ? 99  ILE L CG2 1 
ATOM   13003 C  CD1 . ILE L  1 100 ? 20.487  25.406  17.596 1.00 25.14  ? 99  ILE L CD1 1 
ATOM   13004 N  N   . GLU L  1 101 ? 16.840  25.508  13.322 1.00 28.02  ? 100 GLU L N   1 
ATOM   13005 C  CA  . GLU L  1 101 ? 16.674  24.983  11.986 1.00 30.34  ? 100 GLU L CA  1 
ATOM   13006 C  C   . GLU L  1 101 ? 17.943  25.311  11.212 1.00 30.95  ? 100 GLU L C   1 
ATOM   13007 O  O   . GLU L  1 101 ? 18.438  26.430  11.282 1.00 31.83  ? 100 GLU L O   1 
ATOM   13008 C  CB  . GLU L  1 101 ? 15.400  25.563  11.388 1.00 35.30  ? 100 GLU L CB  1 
ATOM   13009 C  CG  . GLU L  1 101 ? 15.248  25.300  9.904  1.00 47.73  ? 100 GLU L CG  1 
ATOM   13010 C  CD  . GLU L  1 101 ? 13.816  25.490  9.423  1.00 56.79  ? 100 GLU L CD  1 
ATOM   13011 O  OE1 . GLU L  1 101 ? 13.644  26.061  8.320  1.00 59.68  ? 100 GLU L OE1 1 
ATOM   13012 O  OE2 . GLU L  1 101 ? 12.872  25.057  10.150 1.00 61.49  ? 100 GLU L OE2 1 
ATOM   13013 N  N   . ASP L  1 102 ? 18.505  24.312  10.533 1.00 32.33  ? 101 ASP L N   1 
ATOM   13014 C  CA  . ASP L  1 102 ? 19.755  24.538  9.838  1.00 32.53  ? 101 ASP L CA  1 
ATOM   13015 C  C   . ASP L  1 102 ? 19.675  23.901  8.461  1.00 34.73  ? 101 ASP L C   1 
ATOM   13016 O  O   . ASP L  1 102 ? 19.086  22.834  8.311  1.00 34.90  ? 101 ASP L O   1 
ATOM   13017 C  CB  . ASP L  1 102 ? 20.939  23.992  10.627 1.00 31.42  ? 101 ASP L CB  1 
ATOM   13018 C  CG  . ASP L  1 102 ? 22.257  24.504  10.084 1.00 34.19  ? 101 ASP L CG  1 
ATOM   13019 O  OD1 . ASP L  1 102 ? 22.513  25.712  10.251 1.00 37.14  ? 101 ASP L OD1 1 
ATOM   13020 O  OD2 . ASP L  1 102 ? 22.997  23.702  9.467  1.00 34.97  ? 101 ASP L OD2 1 
ATOM   13021 N  N   . SER L  1 103 ? 20.289  24.553  7.468  1.00 36.93  ? 102 SER L N   1 
ATOM   13022 C  CA  . SER L  1 103 ? 20.221  24.053  6.104  1.00 35.85  ? 102 SER L CA  1 
ATOM   13023 C  C   . SER L  1 103 ? 21.578  23.569  5.607  1.00 34.96  ? 102 SER L C   1 
ATOM   13024 O  O   . SER L  1 103 ? 21.711  23.212  4.441  1.00 34.64  ? 102 SER L O   1 
ATOM   13025 C  CB  . SER L  1 103 ? 19.632  25.072  5.194  1.00 36.24  ? 102 SER L CB  1 
ATOM   13026 O  OG  . SER L  1 103 ? 18.223  24.923  5.198  1.00 41.65  ? 102 SER L OG  1 
ATOM   13027 N  N   . VAL L  1 104 ? 22.572  23.550  6.499  1.00 31.79  ? 103 VAL L N   1 
ATOM   13028 C  CA  . VAL L  1 104 ? 23.917  23.180  6.097  1.00 30.33  ? 103 VAL L CA  1 
ATOM   13029 C  C   . VAL L  1 104 ? 24.181  21.743  6.523  1.00 28.93  ? 103 VAL L C   1 
ATOM   13030 O  O   . VAL L  1 104 ? 24.703  20.958  5.732  1.00 31.82  ? 103 VAL L O   1 
ATOM   13031 C  CB  . VAL L  1 104 ? 24.981  24.161  6.625  1.00 29.13  ? 103 VAL L CB  1 
ATOM   13032 C  CG1 . VAL L  1 104 ? 26.405  23.665  6.380  1.00 27.10  ? 103 VAL L CG1 1 
ATOM   13033 C  CG2 . VAL L  1 104 ? 24.785  25.550  6.040  1.00 27.60  ? 103 VAL L CG2 1 
ATOM   13034 N  N   . ILE L  1 105 ? 23.820  21.407  7.764  1.00 28.49  ? 104 ILE L N   1 
ATOM   13035 C  CA  . ILE L  1 105 ? 23.851  20.013  8.174  1.00 28.02  ? 104 ILE L CA  1 
ATOM   13036 C  C   . ILE L  1 105 ? 22.813  19.259  7.355  1.00 29.12  ? 104 ILE L C   1 
ATOM   13037 O  O   . ILE L  1 105 ? 21.882  19.857  6.824  1.00 29.05  ? 104 ILE L O   1 
ATOM   13038 C  CB  . ILE L  1 105 ? 23.621  19.845  9.688  1.00 24.72  ? 104 ILE L CB  1 
ATOM   13039 C  CG1 . ILE L  1 105 ? 22.226  20.304  10.105 1.00 23.15  ? 104 ILE L CG1 1 
ATOM   13040 C  CG2 . ILE L  1 105 ? 24.719  20.533  10.470 1.00 22.76  ? 104 ILE L CG2 1 
ATOM   13041 C  CD1 . ILE L  1 105 ? 21.833  19.900  11.498 1.00 23.23  ? 104 ILE L CD1 1 
ATOM   13042 N  N   . SER L  1 106 ? 23.001  17.938  7.247  1.00 30.23  ? 105 SER L N   1 
ATOM   13043 C  CA  . SER L  1 106 ? 22.036  17.095  6.568  1.00 30.30  ? 105 SER L CA  1 
ATOM   13044 C  C   . SER L  1 106 ? 21.938  15.740  7.253  1.00 31.54  ? 105 SER L C   1 
ATOM   13045 O  O   . SER L  1 106 ? 22.852  15.343  7.964  1.00 33.85  ? 105 SER L O   1 
ATOM   13046 C  CB  . SER L  1 106 ? 22.399  16.950  5.122  1.00 29.50  ? 105 SER L CB  1 
ATOM   13047 O  OG  . SER L  1 106 ? 21.300  16.404  4.415  1.00 32.03  ? 105 SER L OG  1 
ATOM   13048 N  N   . LEU L  1 107 ? 20.834  15.032  7.015  1.00 32.28  ? 106 LEU L N   1 
ATOM   13049 C  CA  . LEU L  1 107 ? 20.710  13.653  7.458  1.00 34.93  ? 106 LEU L CA  1 
ATOM   13050 C  C   . LEU L  1 107 ? 20.839  12.696  6.268  1.00 40.31  ? 106 LEU L C   1 
ATOM   13051 O  O   . LEU L  1 107 ? 20.549  11.508  6.400  1.00 50.81  ? 106 LEU L O   1 
ATOM   13052 C  CB  . LEU L  1 107 ? 19.384  13.464  8.202  1.00 30.46  ? 106 LEU L CB  1 
ATOM   13053 C  CG  . LEU L  1 107 ? 19.147  14.399  9.383  1.00 28.51  ? 106 LEU L CG  1 
ATOM   13054 C  CD1 . LEU L  1 107 ? 17.867  14.052  10.132 1.00 28.20  ? 106 LEU L CD1 1 
ATOM   13055 C  CD2 . LEU L  1 107 ? 20.308  14.381  10.345 1.00 29.05  ? 106 LEU L CD2 1 
ATOM   13056 N  N   . SER L  1 108 ? 21.271  13.208  5.107  1.00 42.18  ? 107 SER L N   1 
ATOM   13057 C  CA  . SER L  1 108 ? 21.646  12.379  3.969  1.00 45.59  ? 107 SER L CA  1 
ATOM   13058 C  C   . SER L  1 108 ? 22.606  13.143  3.055  1.00 47.33  ? 107 SER L C   1 
ATOM   13059 O  O   . SER L  1 108 ? 22.688  14.361  3.109  1.00 49.22  ? 107 SER L O   1 
ATOM   13060 C  CB  . SER L  1 108 ? 20.440  11.872  3.232  1.00 44.81  ? 107 SER L CB  1 
ATOM   13061 O  OG  . SER L  1 108 ? 19.710  12.953  2.692  1.00 48.74  ? 107 SER L OG  1 
ATOM   13062 N  N   . GLY L  1 109 ? 23.368  12.407  2.237  1.00 52.21  ? 108 GLY L N   1 
ATOM   13063 C  CA  . GLY L  1 109 ? 24.273  13.006  1.269  1.00 58.13  ? 108 GLY L CA  1 
ATOM   13064 C  C   . GLY L  1 109 ? 25.613  13.374  1.896  1.00 65.48  ? 108 GLY L C   1 
ATOM   13065 O  O   . GLY L  1 109 ? 25.984  12.831  2.925  1.00 62.67  ? 108 GLY L O   1 
ATOM   13066 N  N   . ASP L  1 110 ? 26.281  14.367  1.314  1.00 75.31  ? 109 ASP L N   1 
ATOM   13067 C  CA  . ASP L  1 110 ? 27.666  14.679  1.627  1.00 77.65  ? 109 ASP L CA  1 
ATOM   13068 C  C   . ASP L  1 110 ? 27.818  15.206  3.052  1.00 77.95  ? 109 ASP L C   1 
ATOM   13069 O  O   . ASP L  1 110 ? 28.891  15.101  3.630  1.00 69.06  ? 109 ASP L O   1 
ATOM   13070 C  CB  . ASP L  1 110 ? 28.244  15.688  0.630  1.00 86.61  ? 109 ASP L CB  1 
ATOM   13071 C  CG  . ASP L  1 110 ? 28.184  15.224  -0.810 1.00 89.58  ? 109 ASP L CG  1 
ATOM   13072 O  OD1 . ASP L  1 110 ? 28.572  14.068  -1.064 1.00 88.15  ? 109 ASP L OD1 1 
ATOM   13073 O  OD2 . ASP L  1 110 ? 27.709  16.012  -1.645 1.00 90.66  ? 109 ASP L OD2 1 
ATOM   13074 N  N   . HIS L  1 111 ? 26.771  15.806  3.619  1.00 82.28  ? 110 HIS L N   1 
ATOM   13075 C  CA  . HIS L  1 111 ? 26.973  16.443  4.906  1.00 81.70  ? 110 HIS L CA  1 
ATOM   13076 C  C   . HIS L  1 111 ? 26.253  15.669  6.005  1.00 74.28  ? 110 HIS L C   1 
ATOM   13077 O  O   . HIS L  1 111 ? 25.830  16.259  6.988  1.00 80.83  ? 110 HIS L O   1 
ATOM   13078 C  CB  . HIS L  1 111 ? 26.627  17.942  4.839  1.00 90.19  ? 110 HIS L CB  1 
ATOM   13079 C  CG  . HIS L  1 111 ? 27.385  18.703  3.799  1.00 94.14  ? 110 HIS L CG  1 
ATOM   13080 N  ND1 . HIS L  1 111 ? 26.864  19.852  3.221  1.00 84.84  ? 110 HIS L ND1 1 
ATOM   13081 C  CD2 . HIS L  1 111 ? 28.604  18.516  3.237  1.00 95.46  ? 110 HIS L CD2 1 
ATOM   13082 C  CE1 . HIS L  1 111 ? 27.727  20.342  2.350  1.00 87.60  ? 110 HIS L CE1 1 
ATOM   13083 N  NE2 . HIS L  1 111 ? 28.809  19.536  2.344  1.00 93.63  ? 110 HIS L NE2 1 
ATOM   13084 N  N   . CYS L  1 112 ? 26.137  14.350  5.827  1.00 62.64  ? 111 CYS L N   1 
ATOM   13085 C  CA  . CYS L  1 112 ? 25.421  13.525  6.782  1.00 55.41  ? 111 CYS L CA  1 
ATOM   13086 C  C   . CYS L  1 112 ? 26.141  13.597  8.128  1.00 50.08  ? 111 CYS L C   1 
ATOM   13087 O  O   . CYS L  1 112 ? 27.364  13.509  8.189  1.00 46.09  ? 111 CYS L O   1 
ATOM   13088 C  CB  . CYS L  1 112 ? 25.356  12.099  6.259  1.00 59.49  ? 111 CYS L CB  1 
ATOM   13089 S  SG  . CYS L  1 112 ? 23.919  11.147  6.811  1.00 80.39  ? 111 CYS L SG  1 
ATOM   13090 N  N   . ILE L  1 113 ? 25.371  13.863  9.193  1.00 43.34  ? 112 ILE L N   1 
ATOM   13091 C  CA  . ILE L  1 113 ? 25.917  13.998  10.535 1.00 39.65  ? 112 ILE L CA  1 
ATOM   13092 C  C   . ILE L  1 113 ? 25.657  12.723  11.334 1.00 39.46  ? 112 ILE L C   1 
ATOM   13093 O  O   . ILE L  1 113 ? 26.020  12.643  12.511 1.00 43.44  ? 112 ILE L O   1 
ATOM   13094 C  CB  . ILE L  1 113 ? 25.363  15.238  11.269 1.00 38.57  ? 112 ILE L CB  1 
ATOM   13095 C  CG1 . ILE L  1 113 ? 23.834  15.257  11.299 1.00 37.08  ? 112 ILE L CG1 1 
ATOM   13096 C  CG2 . ILE L  1 113 ? 25.927  16.527  10.691 1.00 39.05  ? 112 ILE L CG2 1 
ATOM   13097 C  CD1 . ILE L  1 113 ? 23.255  16.084  12.420 1.00 36.49  ? 112 ILE L CD1 1 
ATOM   13098 N  N   . ILE L  1 114 ? 25.011  11.733  10.698 1.00 34.19  ? 113 ILE L N   1 
ATOM   13099 C  CA  . ILE L  1 114 ? 24.737  10.467  11.355 1.00 31.39  ? 113 ILE L CA  1 
ATOM   13100 C  C   . ILE L  1 114 ? 26.068  9.804   11.682 1.00 32.73  ? 113 ILE L C   1 
ATOM   13101 O  O   . ILE L  1 114 ? 26.977  9.771   10.850 1.00 32.42  ? 113 ILE L O   1 
ATOM   13102 C  CB  . ILE L  1 114 ? 23.862  9.563   10.482 1.00 30.69  ? 113 ILE L CB  1 
ATOM   13103 C  CG1 . ILE L  1 114 ? 22.588  10.297  10.062 1.00 30.73  ? 113 ILE L CG1 1 
ATOM   13104 C  CG2 . ILE L  1 114 ? 23.577  8.247   11.192 1.00 30.25  ? 113 ILE L CG2 1 
ATOM   13105 C  CD1 . ILE L  1 114 ? 21.435  9.399   9.710  1.00 30.93  ? 113 ILE L CD1 1 
ATOM   13106 N  N   . GLY L  1 115 ? 26.166  9.318   12.923 1.00 31.44  ? 114 GLY L N   1 
ATOM   13107 C  CA  . GLY L  1 115 ? 27.338  8.599   13.388 1.00 28.91  ? 114 GLY L CA  1 
ATOM   13108 C  C   . GLY L  1 115 ? 28.476  9.538   13.781 1.00 27.72  ? 114 GLY L C   1 
ATOM   13109 O  O   . GLY L  1 115 ? 29.608  9.084   13.955 1.00 26.67  ? 114 GLY L O   1 
ATOM   13110 N  N   . ARG L  1 116 ? 28.159  10.835  13.917 1.00 27.29  ? 115 ARG L N   1 
ATOM   13111 C  CA  . ARG L  1 116 ? 29.103  11.820  14.430 1.00 26.88  ? 115 ARG L CA  1 
ATOM   13112 C  C   . ARG L  1 116 ? 28.672  12.235  15.835 1.00 27.70  ? 115 ARG L C   1 
ATOM   13113 O  O   . ARG L  1 116 ? 27.776  11.614  16.402 1.00 29.69  ? 115 ARG L O   1 
ATOM   13114 C  CB  . ARG L  1 116 ? 29.279  12.946  13.411 1.00 24.66  ? 115 ARG L CB  1 
ATOM   13115 C  CG  . ARG L  1 116 ? 29.607  12.419  12.026 1.00 23.45  ? 115 ARG L CG  1 
ATOM   13116 C  CD  . ARG L  1 116 ? 29.979  13.506  11.051 1.00 23.04  ? 115 ARG L CD  1 
ATOM   13117 N  NE  . ARG L  1 116 ? 30.316  12.981  9.734  1.00 24.29  ? 115 ARG L NE  1 
ATOM   13118 C  CZ  . ARG L  1 116 ? 31.529  12.579  9.351  1.00 23.50  ? 115 ARG L CZ  1 
ATOM   13119 N  NH1 . ARG L  1 116 ? 32.559  12.647  10.181 1.00 21.77  ? 115 ARG L NH1 1 
ATOM   13120 N  NH2 . ARG L  1 116 ? 31.707  12.123  8.127  1.00 24.73  ? 115 ARG L NH2 1 
ATOM   13121 N  N   . THR L  1 117 ? 29.326  13.245  16.417 1.00 26.38  ? 116 THR L N   1 
ATOM   13122 C  CA  . THR L  1 117 ? 29.019  13.608  17.792 1.00 26.20  ? 116 THR L CA  1 
ATOM   13123 C  C   . THR L  1 117 ? 28.414  15.004  17.877 1.00 26.01  ? 116 THR L C   1 
ATOM   13124 O  O   . THR L  1 117 ? 28.859  15.931  17.204 1.00 27.71  ? 116 THR L O   1 
ATOM   13125 C  CB  . THR L  1 117 ? 30.247  13.513  18.702 1.00 26.80  ? 116 THR L CB  1 
ATOM   13126 O  OG1 . THR L  1 117 ? 30.631  12.143  18.694 1.00 30.17  ? 116 THR L OG1 1 
ATOM   13127 C  CG2 . THR L  1 117 ? 29.967  13.933  20.126 1.00 23.81  ? 116 THR L CG2 1 
ATOM   13128 N  N   . LEU L  1 118 ? 27.406  15.134  18.740 1.00 23.78  ? 117 LEU L N   1 
ATOM   13129 C  CA  . LEU L  1 118 ? 26.911  16.446  19.098 1.00 22.95  ? 117 LEU L CA  1 
ATOM   13130 C  C   . LEU L  1 118 ? 27.491  16.793  20.461 1.00 23.26  ? 117 LEU L C   1 
ATOM   13131 O  O   . LEU L  1 118 ? 27.498  15.948  21.359 1.00 23.42  ? 117 LEU L O   1 
ATOM   13132 C  CB  . LEU L  1 118 ? 25.386  16.372  19.137 1.00 22.81  ? 117 LEU L CB  1 
ATOM   13133 C  CG  . LEU L  1 118 ? 24.676  17.647  19.567 1.00 23.09  ? 117 LEU L CG  1 
ATOM   13134 C  CD1 . LEU L  1 118 ? 24.886  18.723  18.519 1.00 24.47  ? 117 LEU L CD1 1 
ATOM   13135 C  CD2 . LEU L  1 118 ? 23.201  17.389  19.764 1.00 22.84  ? 117 LEU L CD2 1 
ATOM   13136 N  N   . VAL L  1 119 ? 28.001  18.025  20.596 1.00 22.55  ? 118 VAL L N   1 
ATOM   13137 C  CA  . VAL L  1 119 ? 28.639  18.455  21.833 1.00 22.88  ? 118 VAL L CA  1 
ATOM   13138 C  C   . VAL L  1 119 ? 28.031  19.776  22.293 1.00 23.16  ? 118 VAL L C   1 
ATOM   13139 O  O   . VAL L  1 119 ? 27.867  20.708  21.503 1.00 23.34  ? 118 VAL L O   1 
ATOM   13140 C  CB  . VAL L  1 119 ? 30.163  18.618  21.679 1.00 22.48  ? 118 VAL L CB  1 
ATOM   13141 C  CG1 . VAL L  1 119 ? 30.818  19.040  22.985 1.00 22.82  ? 118 VAL L CG1 1 
ATOM   13142 C  CG2 . VAL L  1 119 ? 30.840  17.380  21.121 1.00 22.15  ? 118 VAL L CG2 1 
ATOM   13143 N  N   . VAL L  1 120 ? 27.750  19.854  23.596 1.00 22.19  ? 119 VAL L N   1 
ATOM   13144 C  CA  . VAL L  1 120 ? 27.388  21.119  24.201 1.00 22.26  ? 119 VAL L CA  1 
ATOM   13145 C  C   . VAL L  1 120 ? 28.557  21.572  25.068 1.00 22.89  ? 119 VAL L C   1 
ATOM   13146 O  O   . VAL L  1 120 ? 29.041  20.812  25.910 1.00 21.97  ? 119 VAL L O   1 
ATOM   13147 C  CB  . VAL L  1 120 ? 26.056  21.024  24.970 1.00 21.13  ? 119 VAL L CB  1 
ATOM   13148 C  CG1 . VAL L  1 120 ? 26.088  19.983  26.072 1.00 20.44  ? 119 VAL L CG1 1 
ATOM   13149 C  CG2 . VAL L  1 120 ? 25.620  22.375  25.512 1.00 20.83  ? 119 VAL L CG2 1 
ATOM   13150 N  N   . HIS L  1 121 ? 28.988  22.825  24.845 1.00 24.40  ? 120 HIS L N   1 
ATOM   13151 C  CA  . HIS L  1 121 ? 30.230  23.345  25.398 1.00 27.38  ? 120 HIS L CA  1 
ATOM   13152 C  C   . HIS L  1 121 ? 30.009  24.201  26.646 1.00 29.56  ? 120 HIS L C   1 
ATOM   13153 O  O   . HIS L  1 121 ? 28.884  24.554  26.989 1.00 29.85  ? 120 HIS L O   1 
ATOM   13154 C  CB  . HIS L  1 121 ? 30.972  24.141  24.335 1.00 27.88  ? 120 HIS L CB  1 
ATOM   13155 C  CG  . HIS L  1 121 ? 31.595  23.295  23.282 1.00 29.26  ? 120 HIS L CG  1 
ATOM   13156 N  ND1 . HIS L  1 121 ? 32.898  22.846  23.381 1.00 29.20  ? 120 HIS L ND1 1 
ATOM   13157 C  CD2 . HIS L  1 121 ? 31.108  22.849  22.104 1.00 30.49  ? 120 HIS L CD2 1 
ATOM   13158 C  CE1 . HIS L  1 121 ? 33.191  22.151  22.299 1.00 33.79  ? 120 HIS L CE1 1 
ATOM   13159 N  NE2 . HIS L  1 121 ? 32.104  22.140  21.495 1.00 34.47  ? 120 HIS L NE2 1 
ATOM   13160 N  N   . GLU L  1 122 ? 31.129  24.576  27.273 1.00 29.86  ? 121 GLU L N   1 
ATOM   13161 C  CA  . GLU L  1 122 ? 31.170  25.181  28.592 1.00 31.14  ? 121 GLU L CA  1 
ATOM   13162 C  C   . GLU L  1 122 ? 30.703  26.634  28.556 1.00 30.41  ? 121 GLU L C   1 
ATOM   13163 O  O   . GLU L  1 122 ? 29.967  27.050  29.443 1.00 27.63  ? 121 GLU L O   1 
ATOM   13164 C  CB  . GLU L  1 122 ? 32.590  25.031  29.113 1.00 33.03  ? 121 GLU L CB  1 
ATOM   13165 C  CG  . GLU L  1 122 ? 32.979  25.995  30.204 1.00 35.70  ? 121 GLU L CG  1 
ATOM   13166 C  CD  . GLU L  1 122 ? 34.488  26.031  30.379 1.00 41.49  ? 121 GLU L CD  1 
ATOM   13167 O  OE1 . GLU L  1 122 ? 34.941  26.118  31.542 1.00 44.25  ? 121 GLU L OE1 1 
ATOM   13168 O  OE2 . GLU L  1 122 ? 35.216  25.900  29.356 1.00 40.56  ? 121 GLU L OE2 1 
ATOM   13169 N  N   . LYS L  1 123 ? 31.116  27.379  27.524 1.00 32.45  ? 122 LYS L N   1 
ATOM   13170 C  CA  . LYS L  1 123 ? 30.930  28.819  27.403 1.00 32.87  ? 122 LYS L CA  1 
ATOM   13171 C  C   . LYS L  1 123 ? 30.266  29.166  26.074 1.00 31.35  ? 122 LYS L C   1 
ATOM   13172 O  O   . LYS L  1 123 ? 29.989  28.291  25.260 1.00 29.51  ? 122 LYS L O   1 
ATOM   13173 C  CB  . LYS L  1 123 ? 32.294  29.523  27.396 1.00 37.77  ? 122 LYS L CB  1 
ATOM   13174 C  CG  . LYS L  1 123 ? 33.117  29.413  28.673 1.00 42.75  ? 122 LYS L CG  1 
ATOM   13175 C  CD  . LYS L  1 123 ? 34.432  30.197  28.609 1.00 48.77  ? 122 LYS L CD  1 
ATOM   13176 C  CE  . LYS L  1 123 ? 35.510  29.503  27.802 1.00 47.28  ? 122 LYS L CE  1 
ATOM   13177 N  NZ  . LYS L  1 123 ? 36.799  30.227  27.904 1.00 49.40  ? 122 LYS L NZ  1 
ATOM   13178 N  N   . ALA L  1 124 ? 30.031  30.470  25.859 1.00 29.06  ? 123 ALA L N   1 
ATOM   13179 C  CA  . ALA L  1 124 ? 29.444  30.963  24.622 1.00 27.11  ? 123 ALA L CA  1 
ATOM   13180 C  C   . ALA L  1 124 ? 30.379  30.700  23.448 1.00 26.83  ? 123 ALA L C   1 
ATOM   13181 O  O   . ALA L  1 124 ? 31.594  30.750  23.596 1.00 27.16  ? 123 ALA L O   1 
ATOM   13182 C  CB  . ALA L  1 124 ? 29.162  32.434  24.744 1.00 24.93  ? 123 ALA L CB  1 
ATOM   13183 N  N   . ASP L  1 125 ? 29.790  30.410  22.289 1.00 25.79  ? 124 ASP L N   1 
ATOM   13184 C  CA  . ASP L  1 125 ? 30.513  30.373  21.034 1.00 24.97  ? 124 ASP L CA  1 
ATOM   13185 C  C   . ASP L  1 125 ? 30.554  31.804  20.492 1.00 24.59  ? 124 ASP L C   1 
ATOM   13186 O  O   . ASP L  1 125 ? 29.506  32.407  20.288 1.00 23.23  ? 124 ASP L O   1 
ATOM   13187 C  CB  . ASP L  1 125 ? 29.832  29.379  20.089 1.00 25.66  ? 124 ASP L CB  1 
ATOM   13188 C  CG  . ASP L  1 125 ? 30.374  29.357  18.667 1.00 27.05  ? 124 ASP L CG  1 
ATOM   13189 O  OD1 . ASP L  1 125 ? 31.275  30.168  18.357 1.00 29.05  ? 124 ASP L OD1 1 
ATOM   13190 O  OD2 . ASP L  1 125 ? 29.889  28.521  17.874 1.00 23.95  ? 124 ASP L OD2 1 
ATOM   13191 N  N   . ASP L  1 126 ? 31.768  32.331  20.246 1.00 23.91  ? 125 ASP L N   1 
ATOM   13192 C  CA  . ASP L  1 126 ? 31.913  33.714  19.819 1.00 22.55  ? 125 ASP L CA  1 
ATOM   13193 C  C   . ASP L  1 126 ? 31.680  33.864  18.315 1.00 21.73  ? 125 ASP L C   1 
ATOM   13194 O  O   . ASP L  1 126 ? 31.884  34.946  17.745 1.00 20.37  ? 125 ASP L O   1 
ATOM   13195 C  CB  . ASP L  1 126 ? 33.217  34.343  20.323 1.00 22.10  ? 125 ASP L CB  1 
ATOM   13196 C  CG  . ASP L  1 126 ? 34.497  33.857  19.646 1.00 21.48  ? 125 ASP L CG  1 
ATOM   13197 O  OD1 . ASP L  1 126 ? 34.418  33.350  18.497 1.00 18.91  ? 125 ASP L OD1 1 
ATOM   13198 O  OD2 . ASP L  1 126 ? 35.578  34.007  20.278 1.00 22.16  ? 125 ASP L OD2 1 
ATOM   13199 N  N   . LEU L  1 127 ? 31.248  32.777  17.670 1.00 23.29  ? 126 LEU L N   1 
ATOM   13200 C  CA  . LEU L  1 127 ? 30.854  32.770  16.266 1.00 26.89  ? 126 LEU L CA  1 
ATOM   13201 C  C   . LEU L  1 127 ? 32.011  33.218  15.373 1.00 29.38  ? 126 LEU L C   1 
ATOM   13202 O  O   . LEU L  1 127 ? 31.778  33.667  14.253 1.00 33.03  ? 126 LEU L O   1 
ATOM   13203 C  CB  . LEU L  1 127 ? 29.606  33.638  16.060 1.00 25.66  ? 126 LEU L CB  1 
ATOM   13204 C  CG  . LEU L  1 127 ? 28.447  33.397  17.033 1.00 25.30  ? 126 LEU L CG  1 
ATOM   13205 C  CD1 . LEU L  1 127 ? 27.244  34.251  16.661 1.00 24.51  ? 126 LEU L CD1 1 
ATOM   13206 C  CD2 . LEU L  1 127 ? 28.055  31.909  17.099 1.00 27.56  ? 126 LEU L CD2 1 
ATOM   13207 N  N   . GLY L  1 128 ? 33.246  33.110  15.879 1.00 30.67  ? 127 GLY L N   1 
ATOM   13208 C  CA  . GLY L  1 128 ? 34.451  33.300  15.090 1.00 30.11  ? 127 GLY L CA  1 
ATOM   13209 C  C   . GLY L  1 128 ? 34.897  34.749  15.009 1.00 31.31  ? 127 GLY L C   1 
ATOM   13210 O  O   . GLY L  1 128 ? 35.709  35.090  14.154 1.00 31.58  ? 127 GLY L O   1 
ATOM   13211 N  N   . LYS L  1 129 ? 34.375  35.577  15.923 1.00 32.27  ? 128 LYS L N   1 
ATOM   13212 C  CA  . LYS L  1 129 ? 34.611  37.013  15.862 1.00 32.83  ? 128 LYS L CA  1 
ATOM   13213 C  C   . LYS L  1 129 ? 35.387  37.463  17.094 1.00 32.60  ? 128 LYS L C   1 
ATOM   13214 O  O   . LYS L  1 129 ? 35.203  38.589  17.554 1.00 38.42  ? 128 LYS L O   1 
ATOM   13215 C  CB  . LYS L  1 129 ? 33.309  37.812  15.726 1.00 35.70  ? 128 LYS L CB  1 
ATOM   13216 C  CG  . LYS L  1 129 ? 32.323  37.281  14.721 1.00 37.49  ? 128 LYS L CG  1 
ATOM   13217 C  CD  . LYS L  1 129 ? 31.479  38.189  13.894 1.00 44.66  ? 128 LYS L CD  1 
ATOM   13218 C  CE  . LYS L  1 129 ? 30.795  37.320  12.864 1.00 44.40  ? 128 LYS L CE  1 
ATOM   13219 N  NZ  . LYS L  1 129 ? 29.335  37.597  12.701 1.00 49.11  ? 128 LYS L NZ  1 
ATOM   13220 N  N   . GLY L  1 130 ? 36.230  36.577  17.628 1.00 30.22  ? 129 GLY L N   1 
ATOM   13221 C  CA  . GLY L  1 130 ? 36.929  36.830  18.884 1.00 31.01  ? 129 GLY L CA  1 
ATOM   13222 C  C   . GLY L  1 130 ? 38.348  37.352  18.684 1.00 30.33  ? 129 GLY L C   1 
ATOM   13223 O  O   . GLY L  1 130 ? 38.997  37.738  19.656 1.00 26.84  ? 129 GLY L O   1 
ATOM   13224 N  N   . GLY L  1 131 ? 38.815  37.319  17.426 1.00 30.87  ? 130 GLY L N   1 
ATOM   13225 C  CA  . GLY L  1 131 ? 40.071  37.920  17.022 1.00 34.07  ? 130 GLY L CA  1 
ATOM   13226 C  C   . GLY L  1 131 ? 41.306  37.211  17.579 1.00 36.66  ? 130 GLY L C   1 
ATOM   13227 O  O   . GLY L  1 131 ? 42.371  37.813  17.735 1.00 38.77  ? 130 GLY L O   1 
ATOM   13228 N  N   . ASN L  1 132 ? 41.161  35.922  17.887 1.00 39.07  ? 131 ASN L N   1 
ATOM   13229 C  CA  . ASN L  1 132 ? 42.317  35.081  18.178 1.00 38.00  ? 131 ASN L CA  1 
ATOM   13230 C  C   . ASN L  1 132 ? 42.217  33.809  17.344 1.00 39.52  ? 131 ASN L C   1 
ATOM   13231 O  O   . ASN L  1 132 ? 41.229  33.588  16.645 1.00 37.60  ? 131 ASN L O   1 
ATOM   13232 C  CB  . ASN L  1 132 ? 42.535  34.832  19.677 1.00 33.96  ? 131 ASN L CB  1 
ATOM   13233 C  CG  . ASN L  1 132 ? 41.366  34.186  20.378 1.00 32.55  ? 131 ASN L CG  1 
ATOM   13234 O  OD1 . ASN L  1 132 ? 40.510  33.570  19.738 1.00 32.96  ? 131 ASN L OD1 1 
ATOM   13235 N  ND2 . ASN L  1 132 ? 41.313  34.349  21.695 1.00 32.18  ? 131 ASN L ND2 1 
ATOM   13236 N  N   . GLU L  1 133 ? 43.254  32.973  17.426 1.00 44.78  ? 132 GLU L N   1 
ATOM   13237 C  CA  . GLU L  1 133 ? 43.325  31.822  16.543 1.00 42.97  ? 132 GLU L CA  1 
ATOM   13238 C  C   . GLU L  1 133 ? 42.267  30.817  16.971 1.00 39.81  ? 132 GLU L C   1 
ATOM   13239 O  O   . GLU L  1 133 ? 41.618  30.198  16.126 1.00 34.91  ? 132 GLU L O   1 
ATOM   13240 C  CB  . GLU L  1 133 ? 44.739  31.250  16.521 1.00 49.20  ? 132 GLU L CB  1 
ATOM   13241 C  CG  . GLU L  1 133 ? 44.921  30.223  15.440 1.00 53.28  ? 132 GLU L CG  1 
ATOM   13242 C  CD  . GLU L  1 133 ? 46.029  29.203  15.653 1.00 58.00  ? 132 GLU L CD  1 
ATOM   13243 O  OE1 . GLU L  1 133 ? 46.660  29.150  16.749 1.00 60.76  ? 132 GLU L OE1 1 
ATOM   13244 O  OE2 . GLU L  1 133 ? 46.248  28.459  14.713 1.00 58.02  ? 132 GLU L OE2 1 
ATOM   13245 N  N   . GLU L  1 134 ? 42.082  30.718  18.293 1.00 40.95  ? 133 GLU L N   1 
ATOM   13246 C  CA  . GLU L  1 134 ? 41.092  29.853  18.914 1.00 42.37  ? 133 GLU L CA  1 
ATOM   13247 C  C   . GLU L  1 134 ? 39.697  30.145  18.348 1.00 42.36  ? 133 GLU L C   1 
ATOM   13248 O  O   . GLU L  1 134 ? 38.949  29.217  18.039 1.00 42.82  ? 133 GLU L O   1 
ATOM   13249 C  CB  . GLU L  1 134 ? 41.161  30.051  20.432 1.00 42.83  ? 133 GLU L CB  1 
ATOM   13250 C  CG  . GLU L  1 134 ? 40.584  28.910  21.248 1.00 45.63  ? 133 GLU L CG  1 
ATOM   13251 C  CD  . GLU L  1 134 ? 40.919  27.483  20.841 1.00 48.01  ? 133 GLU L CD  1 
ATOM   13252 O  OE1 . GLU L  1 134 ? 42.048  27.234  20.373 1.00 53.17  ? 133 GLU L OE1 1 
ATOM   13253 O  OE2 . GLU L  1 134 ? 40.038  26.613  20.995 1.00 45.91  ? 133 GLU L OE2 1 
ATOM   13254 N  N   . SER L  1 135 ? 39.375  31.436  18.189 1.00 40.17  ? 134 SER L N   1 
ATOM   13255 C  CA  . SER L  1 135 ? 38.060  31.849  17.733 1.00 40.47  ? 134 SER L CA  1 
ATOM   13256 C  C   . SER L  1 135 ? 37.734  31.198  16.390 1.00 40.97  ? 134 SER L C   1 
ATOM   13257 O  O   . SER L  1 135 ? 36.601  30.775  16.177 1.00 43.37  ? 134 SER L O   1 
ATOM   13258 C  CB  . SER L  1 135 ? 37.940  33.344  17.652 1.00 43.37  ? 134 SER L CB  1 
ATOM   13259 O  OG  . SER L  1 135 ? 36.614  33.739  17.277 1.00 43.28  ? 134 SER L OG  1 
ATOM   13260 N  N   . THR L  1 136 ? 38.718  31.109  15.491 1.00 41.52  ? 135 THR L N   1 
ATOM   13261 C  CA  . THR L  1 136 ? 38.413  30.652  14.145 1.00 42.52  ? 135 THR L CA  1 
ATOM   13262 C  C   . THR L  1 136 ? 38.443  29.130  14.056 1.00 40.04  ? 135 THR L C   1 
ATOM   13263 O  O   . THR L  1 136 ? 38.236  28.584  12.973 1.00 38.43  ? 135 THR L O   1 
ATOM   13264 C  CB  . THR L  1 136 ? 39.355  31.262  13.100 1.00 43.02  ? 135 THR L CB  1 
ATOM   13265 O  OG1 . THR L  1 136 ? 40.657  30.756  13.399 1.00 41.86  ? 135 THR L OG1 1 
ATOM   13266 C  CG2 . THR L  1 136 ? 39.336  32.775  13.096 1.00 42.73  ? 135 THR L CG2 1 
ATOM   13267 N  N   . LYS L  1 137 ? 38.695  28.464  15.196 1.00 40.75  ? 136 LYS L N   1 
ATOM   13268 C  CA  . LYS L  1 137 ? 38.677  27.009  15.254 1.00 39.29  ? 136 LYS L CA  1 
ATOM   13269 C  C   . LYS L  1 137 ? 37.459  26.528  16.042 1.00 35.88  ? 136 LYS L C   1 
ATOM   13270 O  O   . LYS L  1 137 ? 36.693  25.715  15.539 1.00 30.94  ? 136 LYS L O   1 
ATOM   13271 C  CB  . LYS L  1 137 ? 39.970  26.472  15.877 1.00 43.52  ? 136 LYS L CB  1 
ATOM   13272 C  CG  . LYS L  1 137 ? 41.170  26.416  14.941 1.00 48.89  ? 136 LYS L CG  1 
ATOM   13273 C  CD  . LYS L  1 137 ? 42.417  25.843  15.560 1.00 54.42  ? 136 LYS L CD  1 
ATOM   13274 C  CE  . LYS L  1 137 ? 43.522  25.742  14.527 1.00 57.21  ? 136 LYS L CE  1 
ATOM   13275 N  NZ  . LYS L  1 137 ? 44.565  24.740  14.872 1.00 56.22  ? 136 LYS L NZ  1 
ATOM   13276 N  N   . THR L  1 138 ? 37.298  27.035  17.271 1.00 33.14  ? 137 THR L N   1 
ATOM   13277 C  CA  . THR L  1 138 ? 36.339  26.484  18.205 1.00 30.30  ? 137 THR L CA  1 
ATOM   13278 C  C   . THR L  1 138 ? 35.334  27.522  18.699 1.00 30.44  ? 137 THR L C   1 
ATOM   13279 O  O   . THR L  1 138 ? 34.462  27.203  19.498 1.00 28.06  ? 137 THR L O   1 
ATOM   13280 C  CB  . THR L  1 138 ? 37.037  25.887  19.425 1.00 29.26  ? 137 THR L CB  1 
ATOM   13281 O  OG1 . THR L  1 138 ? 37.531  26.950  20.244 1.00 26.75  ? 137 THR L OG1 1 
ATOM   13282 C  CG2 . THR L  1 138 ? 38.159  24.956  19.034 1.00 29.09  ? 137 THR L CG2 1 
ATOM   13283 N  N   . GLY L  1 139 ? 35.491  28.765  18.257 1.00 31.27  ? 138 GLY L N   1 
ATOM   13284 C  CA  . GLY L  1 139 ? 34.682  29.872  18.745 1.00 32.34  ? 138 GLY L CA  1 
ATOM   13285 C  C   . GLY L  1 139 ? 34.868  30.134  20.240 1.00 33.38  ? 138 GLY L C   1 
ATOM   13286 O  O   . GLY L  1 139 ? 34.071  30.861  20.833 1.00 36.45  ? 138 GLY L O   1 
ATOM   13287 N  N   . ASN L  1 140 ? 35.900  29.535  20.853 1.00 31.71  ? 139 ASN L N   1 
ATOM   13288 C  CA  . ASN L  1 140 ? 36.250  29.831  22.235 1.00 33.02  ? 139 ASN L CA  1 
ATOM   13289 C  C   . ASN L  1 140 ? 35.175  29.318  23.182 1.00 34.03  ? 139 ASN L C   1 
ATOM   13290 O  O   . ASN L  1 140 ? 35.006  29.844  24.283 1.00 34.79  ? 139 ASN L O   1 
ATOM   13291 C  CB  . ASN L  1 140 ? 36.491  31.330  22.494 1.00 31.33  ? 139 ASN L CB  1 
ATOM   13292 C  CG  . ASN L  1 140 ? 37.828  31.821  22.003 1.00 32.27  ? 139 ASN L CG  1 
ATOM   13293 O  OD1 . ASN L  1 140 ? 38.869  31.433  22.548 1.00 32.28  ? 139 ASN L OD1 1 
ATOM   13294 N  ND2 . ASN L  1 140 ? 37.812  32.649  20.976 1.00 34.67  ? 139 ASN L ND2 1 
ATOM   13295 N  N   . ALA L  1 141 ? 34.479  28.256  22.750 1.00 34.40  ? 140 ALA L N   1 
ATOM   13296 C  CA  . ALA L  1 141 ? 33.332  27.739  23.479 1.00 32.32  ? 140 ALA L CA  1 
ATOM   13297 C  C   . ALA L  1 141 ? 33.773  26.962  24.714 1.00 29.38  ? 140 ALA L C   1 
ATOM   13298 O  O   . ALA L  1 141 ? 32.943  26.575  25.521 1.00 28.03  ? 140 ALA L O   1 
ATOM   13299 C  CB  . ALA L  1 141 ? 32.492  26.906  22.546 1.00 34.13  ? 140 ALA L CB  1 
ATOM   13300 N  N   . GLY L  1 142 ? 35.084  26.749  24.864 1.00 27.54  ? 141 GLY L N   1 
ATOM   13301 C  CA  . GLY L  1 142 ? 35.603  26.089  26.047 1.00 26.64  ? 141 GLY L CA  1 
ATOM   13302 C  C   . GLY L  1 142 ? 35.364  24.587  25.986 1.00 25.59  ? 141 GLY L C   1 
ATOM   13303 O  O   . GLY L  1 142 ? 35.210  24.030  24.897 1.00 25.64  ? 141 GLY L O   1 
ATOM   13304 N  N   . SER L  1 143 ? 35.307  23.960  27.167 1.00 25.87  ? 142 SER L N   1 
ATOM   13305 C  CA  . SER L  1 143 ? 35.341  22.511  27.283 1.00 26.87  ? 142 SER L CA  1 
ATOM   13306 C  C   . SER L  1 143 ? 34.025  21.890  26.829 1.00 26.69  ? 142 SER L C   1 
ATOM   13307 O  O   . SER L  1 143 ? 33.044  22.597  26.579 1.00 26.99  ? 142 SER L O   1 
ATOM   13308 C  CB  . SER L  1 143 ? 35.697  22.078  28.687 1.00 28.87  ? 142 SER L CB  1 
ATOM   13309 O  OG  . SER L  1 143 ? 34.695  22.479  29.602 1.00 29.61  ? 142 SER L OG  1 
ATOM   13310 N  N   . ARG L  1 144 ? 34.039  20.550  26.745 1.00 26.39  ? 143 ARG L N   1 
ATOM   13311 C  CA  . ARG L  1 144 ? 32.922  19.751  26.263 1.00 25.66  ? 143 ARG L CA  1 
ATOM   13312 C  C   . ARG L  1 144 ? 32.170  19.216  27.476 1.00 26.38  ? 143 ARG L C   1 
ATOM   13313 O  O   . ARG L  1 144 ? 32.670  18.348  28.184 1.00 25.89  ? 143 ARG L O   1 
ATOM   13314 C  CB  . ARG L  1 144 ? 33.457  18.628  25.373 1.00 23.53  ? 143 ARG L CB  1 
ATOM   13315 C  CG  . ARG L  1 144 ? 34.295  19.128  24.207 1.00 22.29  ? 143 ARG L CG  1 
ATOM   13316 C  CD  . ARG L  1 144 ? 35.039  18.077  23.428 1.00 21.58  ? 143 ARG L CD  1 
ATOM   13317 N  NE  . ARG L  1 144 ? 35.869  18.677  22.390 1.00 21.35  ? 143 ARG L NE  1 
ATOM   13318 C  CZ  . ARG L  1 144 ? 36.271  18.060  21.276 1.00 21.68  ? 143 ARG L CZ  1 
ATOM   13319 N  NH1 . ARG L  1 144 ? 35.911  16.808  21.023 1.00 23.28  ? 143 ARG L NH1 1 
ATOM   13320 N  NH2 . ARG L  1 144 ? 37.005  18.705  20.387 1.00 21.43  ? 143 ARG L NH2 1 
ATOM   13321 N  N   . LEU L  1 145 ? 30.976  19.762  27.741 1.00 26.66  ? 144 LEU L N   1 
ATOM   13322 C  CA  . LEU L  1 145 ? 30.286  19.439  28.976 1.00 25.11  ? 144 LEU L CA  1 
ATOM   13323 C  C   . LEU L  1 145 ? 29.590  18.092  28.838 1.00 25.04  ? 144 LEU L C   1 
ATOM   13324 O  O   . LEU L  1 145 ? 29.538  17.317  29.790 1.00 25.55  ? 144 LEU L O   1 
ATOM   13325 C  CB  . LEU L  1 145 ? 29.297  20.561  29.281 1.00 25.05  ? 144 LEU L CB  1 
ATOM   13326 C  CG  . LEU L  1 145 ? 29.918  21.875  29.752 1.00 25.27  ? 144 LEU L CG  1 
ATOM   13327 C  CD1 . LEU L  1 145 ? 28.842  22.888  30.140 1.00 24.61  ? 144 LEU L CD1 1 
ATOM   13328 C  CD2 . LEU L  1 145 ? 30.852  21.630  30.928 1.00 22.82  ? 144 LEU L CD2 1 
ATOM   13329 N  N   . ALA L  1 146 ? 29.049  17.835  27.642 1.00 26.02  ? 145 ALA L N   1 
ATOM   13330 C  CA  . ALA L  1 146 ? 28.335  16.606  27.352 1.00 27.10  ? 145 ALA L CA  1 
ATOM   13331 C  C   . ALA L  1 146 ? 28.272  16.390  25.847 1.00 27.51  ? 145 ALA L C   1 
ATOM   13332 O  O   . ALA L  1 146 ? 28.293  17.340  25.063 1.00 27.55  ? 145 ALA L O   1 
ATOM   13333 C  CB  . ALA L  1 146 ? 26.956  16.652  27.969 1.00 27.45  ? 145 ALA L CB  1 
ATOM   13334 N  N   . CYS L  1 147 ? 28.210  15.117  25.459 1.00 27.68  ? 146 CYS L N   1 
ATOM   13335 C  CA  . CYS L  1 147 ? 28.163  14.767  24.053 1.00 28.85  ? 146 CYS L CA  1 
ATOM   13336 C  C   . CYS L  1 147 ? 27.458  13.425  23.906 1.00 26.34  ? 146 CYS L C   1 
ATOM   13337 O  O   . CYS L  1 147 ? 27.160  12.767  24.901 1.00 24.11  ? 146 CYS L O   1 
ATOM   13338 C  CB  . CYS L  1 147 ? 29.569  14.684  23.474 1.00 31.96  ? 146 CYS L CB  1 
ATOM   13339 S  SG  . CYS L  1 147 ? 30.637  13.498  24.343 1.00 33.42  ? 146 CYS L SG  1 
ATOM   13340 N  N   . GLY L  1 148 ? 27.174  13.069  22.654 1.00 24.29  ? 147 GLY L N   1 
ATOM   13341 C  CA  . GLY L  1 148 ? 26.612  11.784  22.301 1.00 25.93  ? 147 GLY L CA  1 
ATOM   13342 C  C   . GLY L  1 148 ? 26.805  11.499  20.816 1.00 27.22  ? 147 GLY L C   1 
ATOM   13343 O  O   . GLY L  1 148 ? 26.997  12.413  20.016 1.00 28.17  ? 147 GLY L O   1 
ATOM   13344 N  N   . VAL L  1 149 ? 26.749  10.215  20.457 1.00 24.49  ? 148 VAL L N   1 
ATOM   13345 C  CA  . VAL L  1 149 ? 26.787  9.871   19.052 1.00 23.56  ? 148 VAL L CA  1 
ATOM   13346 C  C   . VAL L  1 149 ? 25.390  10.061  18.469 1.00 23.31  ? 148 VAL L C   1 
ATOM   13347 O  O   . VAL L  1 149 ? 24.388  9.775   19.118 1.00 23.42  ? 148 VAL L O   1 
ATOM   13348 C  CB  . VAL L  1 149 ? 27.362  8.462   18.825 1.00 23.88  ? 148 VAL L CB  1 
ATOM   13349 C  CG1 . VAL L  1 149 ? 27.513  8.149   17.346 1.00 22.36  ? 148 VAL L CG1 1 
ATOM   13350 C  CG2 . VAL L  1 149 ? 28.693  8.316   19.543 1.00 23.66  ? 148 VAL L CG2 1 
ATOM   13351 N  N   . ILE L  1 150 ? 25.350  10.587  17.246 1.00 22.77  ? 149 ILE L N   1 
ATOM   13352 C  CA  . ILE L  1 150 ? 24.108  10.908  16.570 1.00 22.96  ? 149 ILE L CA  1 
ATOM   13353 C  C   . ILE L  1 150 ? 23.655  9.654   15.833 1.00 23.47  ? 149 ILE L C   1 
ATOM   13354 O  O   . ILE L  1 150 ? 24.317  9.222   14.892 1.00 24.07  ? 149 ILE L O   1 
ATOM   13355 C  CB  . ILE L  1 150 ? 24.344  12.077  15.595 1.00 22.85  ? 149 ILE L CB  1 
ATOM   13356 C  CG1 . ILE L  1 150 ? 24.737  13.363  16.327 1.00 23.02  ? 149 ILE L CG1 1 
ATOM   13357 C  CG2 . ILE L  1 150 ? 23.152  12.287  14.679 1.00 21.72  ? 149 ILE L CG2 1 
ATOM   13358 C  CD1 . ILE L  1 150 ? 25.349  14.408  15.414 1.00 21.37  ? 149 ILE L CD1 1 
ATOM   13359 N  N   . GLY L  1 151 ? 22.521  9.095   16.260 1.00 23.53  ? 150 GLY L N   1 
ATOM   13360 C  CA  . GLY L  1 151 ? 22.075  7.793   15.784 1.00 26.03  ? 150 GLY L CA  1 
ATOM   13361 C  C   . GLY L  1 151 ? 20.682  7.809   15.160 1.00 27.58  ? 150 GLY L C   1 
ATOM   13362 O  O   . GLY L  1 151 ? 19.917  8.747   15.357 1.00 27.68  ? 150 GLY L O   1 
ATOM   13363 N  N   . ILE L  1 152 ? 20.367  6.744   14.417 1.00 28.36  ? 151 ILE L N   1 
ATOM   13364 C  CA  . ILE L  1 152 ? 19.111  6.606   13.700 1.00 28.45  ? 151 ILE L CA  1 
ATOM   13365 C  C   . ILE L  1 152 ? 18.015  6.285   14.708 1.00 30.76  ? 151 ILE L C   1 
ATOM   13366 O  O   . ILE L  1 152 ? 18.208  5.439   15.575 1.00 33.94  ? 151 ILE L O   1 
ATOM   13367 C  CB  . ILE L  1 152 ? 19.240  5.508   12.636 1.00 27.37  ? 151 ILE L CB  1 
ATOM   13368 C  CG1 . ILE L  1 152 ? 20.243  5.914   11.553 1.00 28.61  ? 151 ILE L CG1 1 
ATOM   13369 C  CG2 . ILE L  1 152 ? 17.893  5.145   12.052 1.00 25.60  ? 151 ILE L CG2 1 
ATOM   13370 C  CD1 . ILE L  1 152 ? 20.809  4.742   10.776 1.00 30.88  ? 151 ILE L CD1 1 
ATOM   13371 N  N   . ALA L  1 153 ? 16.878  6.983   14.582 1.00 33.67  ? 152 ALA L N   1 
ATOM   13372 C  CA  . ALA L  1 153 ? 15.725  6.808   15.458 1.00 36.37  ? 152 ALA L CA  1 
ATOM   13373 C  C   . ALA L  1 153 ? 14.542  6.299   14.640 1.00 42.93  ? 152 ALA L C   1 
ATOM   13374 O  O   . ALA L  1 153 ? 14.591  6.308   13.407 1.00 44.31  ? 152 ALA L O   1 
ATOM   13375 C  CB  . ALA L  1 153 ? 15.396  8.106   16.145 1.00 32.99  ? 152 ALA L CB  1 
ATOM   13376 N  N   . GLN L  1 154 ? 13.482  5.865   15.338 1.00 53.01  ? 153 GLN L N   1 
ATOM   13377 C  CA  . GLN L  1 154 ? 12.342  5.248   14.677 1.00 64.32  ? 153 GLN L CA  1 
ATOM   13378 C  C   . GLN L  1 154 ? 11.512  6.272   13.888 1.00 71.43  ? 153 GLN L C   1 
ATOM   13379 O  O   . GLN L  1 154 ? 11.113  7.345   14.393 1.00 73.06  ? 153 GLN L O   1 
ATOM   13380 C  CB  . GLN L  1 154 ? 11.430  4.529   15.676 1.00 68.91  ? 153 GLN L CB  1 
ATOM   13381 C  CG  . GLN L  1 154 ? 10.248  3.856   14.989 1.00 73.22  ? 153 GLN L CG  1 
ATOM   13382 C  CD  . GLN L  1 154 ? 9.797   2.604   15.711 1.00 79.35  ? 153 GLN L CD  1 
ATOM   13383 O  OE1 . GLN L  1 154 ? 9.477   2.637   16.896 1.00 84.61  ? 153 GLN L OE1 1 
ATOM   13384 N  NE2 . GLN L  1 154 ? 9.808   1.481   15.005 1.00 82.11  ? 153 GLN L NE2 1 
ATOM   13385 O  OXT . GLN L  1 154 ? 11.216  6.002   12.709 1.00 69.02  ? 153 GLN L OXT 1 
HETATM 13386 C  C1  . LQW M  2 .   ? 49.144  -35.972 72.224 1.00 48.96  ? 201 LQW A C1  1 
HETATM 13387 C  C2  . LQW M  2 .   ? 48.145  -35.640 71.316 1.00 45.30  ? 201 LQW A C2  1 
HETATM 13388 C  C3  . LQW M  2 .   ? 48.349  -34.652 70.361 1.00 49.28  ? 201 LQW A C3  1 
HETATM 13389 C  C5  . LQW M  2 .   ? 50.624  -34.311 71.288 1.00 56.38  ? 201 LQW A C5  1 
HETATM 13390 C  C6  . LQW M  2 .   ? 51.945  -33.594 71.273 1.00 63.19  ? 201 LQW A C6  1 
HETATM 13391 C  C7  . LQW M  2 .   ? 54.442  -33.987 70.986 1.00 90.69  ? 201 LQW A C7  1 
HETATM 13392 C  C8  . LQW M  2 .   ? 54.525  -32.747 70.128 1.00 104.58 ? 201 LQW A C8  1 
HETATM 13393 C  C9  . LQW M  2 .   ? 54.374  -31.471 70.692 1.00 113.70 ? 201 LQW A C9  1 
HETATM 13394 C  C13 . LQW M  2 .   ? 54.743  -32.895 68.762 1.00 107.68 ? 201 LQW A C13 1 
HETATM 13395 CL CL  . LQW M  2 .   ? 54.757  -29.061 67.501 1.00 118.95 ? 201 LQW A CL  1 
HETATM 13396 C  C11 . LQW M  2 .   ? 54.667  -30.507 68.528 1.00 114.64 ? 201 LQW A C11 1 
HETATM 13397 C  C10 . LQW M  2 .   ? 54.443  -30.337 69.889 1.00 117.89 ? 201 LQW A C10 1 
HETATM 13398 C  C12 . LQW M  2 .   ? 54.807  -31.764 67.947 1.00 111.95 ? 201 LQW A C12 1 
HETATM 13399 N  N   . LQW M  2 .   ? 53.046  -34.381 71.125 1.00 74.70  ? 201 LQW A N   1 
HETATM 13400 O  O   . LQW M  2 .   ? 51.892  -32.361 71.390 1.00 60.33  ? 201 LQW A O   1 
HETATM 13401 C  C   . LQW M  2 .   ? 50.383  -35.338 72.209 1.00 51.92  ? 201 LQW A C   1 
HETATM 13402 C  C4  . LQW M  2 .   ? 49.551  -33.934 70.307 1.00 54.31  ? 201 LQW A C4  1 
HETATM 13403 SE SE  . LQW M  2 .   ? 49.784  -32.775 69.239 1.00 48.39  ? 201 LQW A SE  1 
HETATM 13404 ZN ZN  . ZN  N  3 .   ? 32.276  -31.611 59.258 1.00 21.67  ? 202 ZN  A ZN  1 
HETATM 13405 S  S   . SO4 O  4 .   ? 36.674  -37.232 46.319 1.00 95.13  ? 203 SO4 A S   1 
HETATM 13406 O  O1  . SO4 O  4 .   ? 37.522  -36.179 45.827 1.00 100.78 ? 203 SO4 A O1  1 
HETATM 13407 O  O2  . SO4 O  4 .   ? 35.905  -37.762 45.223 1.00 99.15  ? 203 SO4 A O2  1 
HETATM 13408 O  O3  . SO4 O  4 .   ? 37.493  -38.268 46.903 1.00 89.68  ? 203 SO4 A O3  1 
HETATM 13409 O  O4  . SO4 O  4 .   ? 35.772  -36.711 47.317 1.00 102.93 ? 203 SO4 A O4  1 
HETATM 13410 S  S   . SO4 P  4 .   ? 34.091  -35.562 52.110 1.00 101.91 ? 204 SO4 A S   1 
HETATM 13411 O  O1  . SO4 P  4 .   ? 33.966  -36.419 50.951 1.00 90.18  ? 204 SO4 A O1  1 
HETATM 13412 O  O2  . SO4 P  4 .   ? 33.187  -34.449 51.978 1.00 102.92 ? 204 SO4 A O2  1 
HETATM 13413 O  O3  . SO4 P  4 .   ? 33.794  -36.300 53.317 1.00 97.55  ? 204 SO4 A O3  1 
HETATM 13414 O  O4  . SO4 P  4 .   ? 35.434  -35.071 52.193 1.00 109.21 ? 204 SO4 A O4  1 
HETATM 13415 C  C1  . LQW Q  2 .   ? -0.555  -42.663 6.018  1.00 40.05  ? 201 LQW B C1  1 
HETATM 13416 C  C2  . LQW Q  2 .   ? 0.694   -42.050 6.185  1.00 41.66  ? 201 LQW B C2  1 
HETATM 13417 C  C3  . LQW Q  2 .   ? 0.965   -40.774 5.679  1.00 42.00  ? 201 LQW B C3  1 
HETATM 13418 C  C5  . LQW Q  2 .   ? -1.348  -40.731 4.793  1.00 42.41  ? 201 LQW B C5  1 
HETATM 13419 C  C6  . LQW Q  2 .   ? -2.435  -40.045 4.019  1.00 42.44  ? 201 LQW B C6  1 
HETATM 13420 C  C7  . LQW Q  2 .   ? -4.686  -39.233 3.800  1.00 39.80  ? 201 LQW B C7  1 
HETATM 13421 C  C8  . LQW Q  2 .   ? -4.870  -37.940 4.540  1.00 38.01  ? 201 LQW B C8  1 
HETATM 13422 C  C9  . LQW Q  2 .   ? -3.764  -37.202 4.905  1.00 36.46  ? 201 LQW B C9  1 
HETATM 13423 C  C13 . LQW Q  2 .   ? -6.157  -37.522 4.831  1.00 37.53  ? 201 LQW B C13 1 
HETATM 13424 CL CL  . LQW Q  2 .   ? -5.509  -34.104 6.796  1.00 46.80  ? 201 LQW B CL  1 
HETATM 13425 C  C11 . LQW Q  2 .   ? -5.249  -35.621 5.889  1.00 39.40  ? 201 LQW B C11 1 
HETATM 13426 C  C10 . LQW Q  2 .   ? -3.963  -36.033 5.585  1.00 38.33  ? 201 LQW B C10 1 
HETATM 13427 C  C12 . LQW Q  2 .   ? -6.349  -36.354 5.520  1.00 37.30  ? 201 LQW B C12 1 
HETATM 13428 N  N   . LQW Q  2 .   ? -3.687  -40.023 4.490  1.00 41.80  ? 201 LQW B N   1 
HETATM 13429 O  O   . LQW Q  2 .   ? -2.109  -39.534 2.943  1.00 43.21  ? 201 LQW B O   1 
HETATM 13430 C  C   . LQW Q  2 .   ? -1.569  -42.014 5.323  1.00 40.31  ? 201 LQW B C   1 
HETATM 13431 C  C4  . LQW Q  2 .   ? -0.009  -40.040 4.962  1.00 44.42  ? 201 LQW B C4  1 
HETATM 13432 SE SE  . LQW Q  2 .   ? 0.273   -38.554 4.370  1.00 38.86  ? 201 LQW B SE  1 
HETATM 13433 ZN ZN  . ZN  R  3 .   ? 17.836  -38.582 14.827 1.00 24.23  ? 202 ZN  B ZN  1 
HETATM 13434 S  S   . SO4 S  4 .   ? 15.994  -43.164 22.215 1.00 97.79  ? 203 SO4 B S   1 
HETATM 13435 O  O1  . SO4 S  4 .   ? 14.653  -42.887 22.639 1.00 102.12 ? 203 SO4 B O1  1 
HETATM 13436 O  O2  . SO4 S  4 .   ? 16.042  -43.217 20.762 1.00 94.06  ? 203 SO4 B O2  1 
HETATM 13437 O  O3  . SO4 S  4 .   ? 16.397  -44.429 22.782 1.00 88.29  ? 203 SO4 B O3  1 
HETATM 13438 O  O4  . SO4 S  4 .   ? 16.864  -42.112 22.689 1.00 96.48  ? 203 SO4 B O4  1 
HETATM 13439 S  S   . SO4 T  4 .   ? 12.959  -45.070 27.113 1.00 94.65  ? 204 SO4 B S   1 
HETATM 13440 O  O1  . SO4 T  4 .   ? 12.397  -45.719 25.950 1.00 96.57  ? 204 SO4 B O1  1 
HETATM 13441 O  O2  . SO4 T  4 .   ? 14.306  -44.638 26.831 1.00 102.99 ? 204 SO4 B O2  1 
HETATM 13442 O  O3  . SO4 T  4 .   ? 12.988  -46.000 28.203 1.00 100.86 ? 204 SO4 B O3  1 
HETATM 13443 O  O4  . SO4 T  4 .   ? 12.155  -43.932 27.482 1.00 95.42  ? 204 SO4 B O4  1 
HETATM 13444 C  C1  . LQW U  2 .   ? 23.952  15.186  65.922 1.00 72.94  ? 201 LQW C C1  1 
HETATM 13445 C  C2  . LQW U  2 .   ? 24.784  14.053  65.931 1.00 67.37  ? 201 LQW C C2  1 
HETATM 13446 C  C3  . LQW U  2 .   ? 24.453  12.929  66.694 1.00 73.42  ? 201 LQW C C3  1 
HETATM 13447 C  C5  . LQW U  2 .   ? 22.395  14.130  67.476 1.00 88.51  ? 201 LQW C C5  1 
HETATM 13448 C  C6  . LQW U  2 .   ? 21.107  14.287  68.274 1.00 94.53  ? 201 LQW C C6  1 
HETATM 13449 C  C7  . LQW U  2 .   ? 19.103  15.602  67.500 1.00 86.08  ? 201 LQW C C7  1 
HETATM 13450 C  C8  . LQW U  2 .   ? 17.744  15.220  66.907 1.00 91.35  ? 201 LQW C C8  1 
HETATM 13451 C  C9  . LQW U  2 .   ? 16.727  16.174  66.708 1.00 100.58 ? 201 LQW C C9  1 
HETATM 13452 C  C13 . LQW U  2 .   ? 17.471  13.890  66.547 1.00 86.66  ? 201 LQW C C13 1 
HETATM 13453 CL CL  . LQW U  2 .   ? 13.654  13.940  65.091 1.00 87.76  ? 201 LQW C CL  1 
HETATM 13454 C  C11 . LQW U  2 .   ? 15.233  14.462  65.801 1.00 92.05  ? 201 LQW C C11 1 
HETATM 13455 C  C10 . LQW U  2 .   ? 15.479  15.804  66.160 1.00 100.21 ? 201 LQW C C10 1 
HETATM 13456 C  C12 . LQW U  2 .   ? 16.241  13.513  66.000 1.00 83.77  ? 201 LQW C C12 1 
HETATM 13457 N  N   . LQW U  2 .   ? 19.924  14.403  67.650 1.00 95.19  ? 201 LQW C N   1 
HETATM 13458 O  O   . LQW U  2 .   ? 21.169  14.309  69.495 1.00 100.30 ? 201 LQW C O   1 
HETATM 13459 C  C   . LQW U  2 .   ? 22.775  15.238  66.678 1.00 78.70  ? 201 LQW C C   1 
HETATM 13460 C  C4  . LQW U  2 .   ? 23.289  12.880  67.501 1.00 80.94  ? 201 LQW C C4  1 
HETATM 13461 SE SE  . LQW U  2 .   ? 23.028  11.522  68.336 1.00 67.15  ? 201 LQW C SE  1 
HETATM 13462 ZN ZN  . ZN  V  3 .   ? 31.135  -4.489  58.952 1.00 21.25  ? 202 ZN  C ZN  1 
HETATM 13463 S  S   . SO4 W  4 .   ? 34.089  -1.336  50.932 1.00 105.74 ? 203 SO4 C S   1 
HETATM 13464 O  O1  . SO4 W  4 .   ? 33.714  -2.617  50.391 1.00 111.80 ? 203 SO4 C O1  1 
HETATM 13465 O  O2  . SO4 W  4 .   ? 33.619  -0.302  50.051 1.00 106.06 ? 203 SO4 C O2  1 
HETATM 13466 O  O3  . SO4 W  4 .   ? 35.521  -1.250  51.021 1.00 106.66 ? 203 SO4 C O3  1 
HETATM 13467 O  O4  . SO4 W  4 .   ? 33.510  -1.181  52.249 1.00 93.03  ? 203 SO4 C O4  1 
HETATM 13468 C  C1  . LQW X  2 .   ? 25.938  7.875   7.407  1.00 85.95  ? 201 LQW D C1  1 
HETATM 13469 C  C2  . LQW X  2 .   ? 25.071  6.774   7.483  1.00 85.03  ? 201 LQW D C2  1 
HETATM 13470 C  C3  . LQW X  2 .   ? 25.410  5.588   6.819  1.00 99.21  ? 201 LQW D C3  1 
HETATM 13471 C  C5  . LQW X  2 .   ? 27.524  6.676   5.973  1.00 106.73 ? 201 LQW D C5  1 
HETATM 13472 C  C6  . LQW X  2 .   ? 28.835  6.701   5.200  1.00 106.72 ? 201 LQW D C6  1 
HETATM 13473 C  C7  . LQW X  2 .   ? 30.575  8.380   6.046  1.00 104.73 ? 201 LQW D C7  1 
HETATM 13474 C  C8  . LQW X  2 .   ? 31.977  8.157   6.626  1.00 110.83 ? 201 LQW D C8  1 
HETATM 13475 C  C9  . LQW X  2 .   ? 32.325  6.886   7.109  1.00 112.74 ? 201 LQW D C9  1 
HETATM 13476 C  C13 . LQW X  2 .   ? 32.959  9.162   6.685  1.00 114.07 ? 201 LQW D C13 1 
HETATM 13477 CL CL  . LQW X  2 .   ? 36.159  7.119   8.440  1.00 109.51 ? 201 LQW D CL  1 
HETATM 13478 C  C11 . LQW X  2 .   ? 34.559  7.585   7.715  1.00 123.55 ? 201 LQW D C11 1 
HETATM 13479 C  C10 . LQW X  2 .   ? 33.580  6.600   7.655  1.00 114.75 ? 201 LQW D C10 1 
HETATM 13480 C  C12 . LQW X  2 .   ? 34.235  8.878   7.231  1.00 122.14 ? 201 LQW D C12 1 
HETATM 13481 N  N   . LQW X  2 .   ? 29.973  7.057   5.827  1.00 110.01 ? 201 LQW D N   1 
HETATM 13482 O  O   . LQW X  2 .   ? 28.851  6.363   4.024  1.00 100.28 ? 201 LQW D O   1 
HETATM 13483 C  C   . LQW X  2 .   ? 27.137  7.840   6.671  1.00 93.49  ? 201 LQW D C   1 
HETATM 13484 C  C4  . LQW X  2 .   ? 26.597  5.463   6.050  1.00 108.17 ? 201 LQW D C4  1 
HETATM 13485 SE SE  . LQW X  2 .   ? 26.868  4.055   5.334  1.00 95.04  ? 201 LQW D SE  1 
HETATM 13486 ZN ZN  . ZN  Y  3 .   ? 18.807  -11.724 15.288 1.00 27.31  ? 202 ZN  D ZN  1 
HETATM 13487 S  S   . SO4 Z  4 .   ? 26.529  -24.695 12.588 1.00 70.08  ? 203 SO4 D S   1 
HETATM 13488 O  O1  . SO4 Z  4 .   ? 27.361  -23.958 11.667 1.00 67.55  ? 203 SO4 D O1  1 
HETATM 13489 O  O2  . SO4 Z  4 .   ? 25.341  -25.189 11.922 1.00 63.37  ? 203 SO4 D O2  1 
HETATM 13490 O  O3  . SO4 Z  4 .   ? 27.277  -25.798 13.115 1.00 75.47  ? 203 SO4 D O3  1 
HETATM 13491 O  O4  . SO4 Z  4 .   ? 26.147  -23.834 13.672 1.00 73.98  ? 203 SO4 D O4  1 
HETATM 13492 S  S   . SO4 AA 4 .   ? 16.153  -8.546  23.246 1.00 103.52 ? 204 SO4 D S   1 
HETATM 13493 O  O1  . SO4 AA 4 .   ? 16.767  -8.256  21.974 1.00 105.37 ? 204 SO4 D O1  1 
HETATM 13494 O  O2  . SO4 AA 4 .   ? 14.721  -8.397  23.150 1.00 89.85  ? 204 SO4 D O2  1 
HETATM 13495 O  O3  . SO4 AA 4 .   ? 16.497  -9.899  23.620 1.00 112.47 ? 204 SO4 D O3  1 
HETATM 13496 O  O4  . SO4 AA 4 .   ? 16.637  -7.630  24.245 1.00 110.03 ? 204 SO4 D O4  1 
HETATM 13497 C  C1  . LQW BA 2 .   ? -5.111  -31.399 69.515 1.00 62.31  ? 201 LQW E C1  1 
HETATM 13498 C  C2  . LQW BA 2 .   ? -4.024  -30.865 68.849 1.00 63.74  ? 201 LQW E C2  1 
HETATM 13499 C  C3  . LQW BA 2 .   ? -3.176  -31.683 68.066 1.00 68.96  ? 201 LQW E C3  1 
HETATM 13500 C  C5  . LQW BA 2 .   ? -4.508  -33.632 68.612 1.00 72.12  ? 201 LQW E C5  1 
HETATM 13501 C  C6  . LQW BA 2 .   ? -4.917  -35.084 68.561 1.00 78.23  ? 201 LQW E C6  1 
HETATM 13502 C  C7  . LQW BA 2 .   ? -7.054  -36.293 68.672 1.00 77.44  ? 201 LQW E C7  1 
HETATM 13503 C  C8  . LQW BA 2 .   ? -7.193  -37.457 69.609 1.00 81.83  ? 201 LQW E C8  1 
HETATM 13504 C  C9  . LQW BA 2 .   ? -6.994  -38.764 69.148 1.00 77.74  ? 201 LQW E C9  1 
HETATM 13505 C  C13 . LQW BA 2 .   ? -7.531  -37.163 70.933 1.00 82.11  ? 201 LQW E C13 1 
HETATM 13506 CL CL  . LQW BA 2 .   ? -7.678  -40.810 72.595 1.00 102.87 ? 201 LQW E CL  1 
HETATM 13507 C  C11 . LQW BA 2 .   ? -7.481  -39.506 71.385 1.00 92.80  ? 201 LQW E C11 1 
HETATM 13508 C  C10 . LQW BA 2 .   ? -7.140  -39.805 70.055 1.00 86.90  ? 201 LQW E C10 1 
HETATM 13509 C  C12 . LQW BA 2 .   ? -7.677  -38.199 71.832 1.00 86.82  ? 201 LQW E C12 1 
HETATM 13510 N  N   . LQW BA 2 .   ? -6.046  -35.406 69.208 1.00 77.78  ? 201 LQW E N   1 
HETATM 13511 O  O   . LQW BA 2 .   ? -4.253  -35.907 67.919 1.00 81.78  ? 201 LQW E O   1 
HETATM 13512 C  C   . LQW BA 2 .   ? -5.333  -32.768 69.376 1.00 68.76  ? 201 LQW E C   1 
HETATM 13513 C  C4  . LQW BA 2 .   ? -3.307  -33.076 67.872 1.00 68.94  ? 201 LQW E C4  1 
HETATM 13514 SE SE  . LQW BA 2 .   ? -2.253  -33.900 66.923 1.00 59.07  ? 201 LQW E SE  1 
HETATM 13515 ZN ZN  . ZN  CA 3 .   ? 8.089   -19.336 57.884 1.00 22.19  ? 202 ZN  E ZN  1 
HETATM 13516 S  S   . SO4 DA 4 .   ? 23.957  -18.231 61.444 1.00 85.02  ? 203 SO4 E S   1 
HETATM 13517 O  O1  . SO4 DA 4 .   ? 23.031  -17.190 61.858 1.00 67.99  ? 203 SO4 E O1  1 
HETATM 13518 O  O2  . SO4 DA 4 .   ? 23.967  -18.308 60.003 1.00 81.32  ? 203 SO4 E O2  1 
HETATM 13519 O  O3  . SO4 DA 4 .   ? 23.508  -19.499 61.972 1.00 81.02  ? 203 SO4 E O3  1 
HETATM 13520 O  O4  . SO4 DA 4 .   ? 25.307  -17.953 61.929 1.00 67.22  ? 203 SO4 E O4  1 
HETATM 13521 C  C1  . LQW EA 2 .   ? 55.491  -40.810 8.676  1.00 84.33  ? 201 LQW F C1  1 
HETATM 13522 C  C2  . LQW EA 2 .   ? 54.738  -39.676 8.358  1.00 77.42  ? 201 LQW F C2  1 
HETATM 13523 C  C3  . LQW EA 2 .   ? 53.559  -39.846 7.632  1.00 89.07  ? 201 LQW F C3  1 
HETATM 13524 C  C5  . LQW EA 2 .   ? 53.921  -42.345 7.583  1.00 95.54  ? 201 LQW F C5  1 
HETATM 13525 C  C6  . LQW EA 2 .   ? 53.511  -43.759 7.177  1.00 96.38  ? 201 LQW F C6  1 
HETATM 13526 C  C7  . LQW EA 2 .   ? 54.276  -46.062 6.527  1.00 96.34  ? 201 LQW F C7  1 
HETATM 13527 C  C8  . LQW EA 2 .   ? 53.233  -46.854 7.286  1.00 94.44  ? 201 LQW F C8  1 
HETATM 13528 C  C9  . LQW EA 2 .   ? 53.660  -47.705 8.295  1.00 86.33  ? 201 LQW F C9  1 
HETATM 13529 C  C13 . LQW EA 2 .   ? 51.854  -46.722 7.005  1.00 99.56  ? 201 LQW F C13 1 
HETATM 13530 CL CL  . LQW EA 2 .   ? 50.127  -49.237 9.728  1.00 97.03  ? 201 LQW F CL  1 
HETATM 13531 C  C11 . LQW EA 2 .   ? 51.329  -48.295 8.761  1.00 94.85  ? 201 LQW F C11 1 
HETATM 13532 C  C10 . LQW EA 2 .   ? 52.704  -48.423 9.027  1.00 90.00  ? 201 LQW F C10 1 
HETATM 13533 C  C12 . LQW EA 2 .   ? 50.900  -47.433 7.742  1.00 96.29  ? 201 LQW F C12 1 
HETATM 13534 N  N   . LQW EA 2 .   ? 54.441  -44.750 7.177  1.00 93.63  ? 201 LQW F N   1 
HETATM 13535 O  O   . LQW EA 2 .   ? 52.333  -43.937 6.833  1.00 94.92  ? 201 LQW F O   1 
HETATM 13536 C  C   . LQW EA 2 .   ? 55.099  -42.118 8.320  1.00 86.11  ? 201 LQW F C   1 
HETATM 13537 C  C4  . LQW EA 2 .   ? 53.101  -41.119 7.218  1.00 94.12  ? 201 LQW F C4  1 
HETATM 13538 SE SE  . LQW EA 2 .   ? 51.727  -41.191 6.422  1.00 78.38  ? 201 LQW F SE  1 
HETATM 13539 ZN ZN  . ZN  FA 3 .   ? 41.807  -26.492 15.662 1.00 25.67  ? 202 ZN  F ZN  1 
HETATM 13540 S  S   . SO4 GA 4 .   ? 48.127  -27.035 29.078 1.00 110.72 ? 203 SO4 F S   1 
HETATM 13541 O  O1  . SO4 GA 4 .   ? 49.370  -27.254 28.376 1.00 97.52  ? 203 SO4 F O1  1 
HETATM 13542 O  O2  . SO4 GA 4 .   ? 47.129  -26.579 28.146 1.00 114.87 ? 203 SO4 F O2  1 
HETATM 13543 O  O3  . SO4 GA 4 .   ? 48.299  -26.050 30.115 1.00 113.47 ? 203 SO4 F O3  1 
HETATM 13544 O  O4  . SO4 GA 4 .   ? 47.698  -28.263 29.685 1.00 123.15 ? 203 SO4 F O4  1 
HETATM 13545 S  S   . SO4 HA 4 .   ? 46.037  -25.175 24.045 1.00 112.71 ? 204 SO4 F S   1 
HETATM 13546 O  O1  . SO4 HA 4 .   ? 46.658  -24.021 23.442 1.00 113.41 ? 204 SO4 F O1  1 
HETATM 13547 O  O2  . SO4 HA 4 .   ? 44.865  -25.555 23.290 1.00 115.52 ? 204 SO4 F O2  1 
HETATM 13548 O  O3  . SO4 HA 4 .   ? 45.676  -24.872 25.408 1.00 103.89 ? 204 SO4 F O3  1 
HETATM 13549 O  O4  . SO4 HA 4 .   ? 46.963  -26.265 24.039 1.00 116.57 ? 204 SO4 F O4  1 
HETATM 13550 C  C1  . LQW IA 2 .   ? -4.721  -36.238 64.565 1.00 85.70  ? 201 LQW G C1  1 
HETATM 13551 C  C2  . LQW IA 2 .   ? -5.867  -36.917 64.941 1.00 86.94  ? 201 LQW G C2  1 
HETATM 13552 C  C3  . LQW IA 2 .   ? -6.982  -36.172 65.357 1.00 99.72  ? 201 LQW G C3  1 
HETATM 13553 C  C5  . LQW IA 2 .   ? -5.791  -34.029 64.992 1.00 93.22  ? 201 LQW G C5  1 
HETATM 13554 C  C6  . LQW IA 2 .   ? -5.605  -32.515 64.980 1.00 86.65  ? 201 LQW G C6  1 
HETATM 13555 C  C7  . LQW IA 2 .   ? -5.746  -30.309 66.098 1.00 78.01  ? 201 LQW G C7  1 
HETATM 13556 C  C8  . LQW IA 2 .   ? -6.524  -29.258 65.322 1.00 76.32  ? 201 LQW G C8  1 
HETATM 13557 C  C9  . LQW IA 2 .   ? -6.363  -27.866 65.454 1.00 76.03  ? 201 LQW G C9  1 
HETATM 13558 C  C13 . LQW IA 2 .   ? -7.485  -29.727 64.441 1.00 79.29  ? 201 LQW G C13 1 
HETATM 13559 CL CL  . LQW IA 2 .   ? -9.240  -26.529 62.720 1.00 78.05  ? 201 LQW G CL  1 
HETATM 13560 C  C11 . LQW IA 2 .   ? -8.132  -27.500 63.784 1.00 79.64  ? 201 LQW G C11 1 
HETATM 13561 C  C10 . LQW IA 2 .   ? -7.167  -26.988 64.685 1.00 78.06  ? 201 LQW G C10 1 
HETATM 13562 C  C12 . LQW IA 2 .   ? -8.273  -28.873 63.683 1.00 78.48  ? 201 LQW G C12 1 
HETATM 13563 N  N   . LQW IA 2 .   ? -6.246  -31.675 65.825 1.00 79.78  ? 201 LQW G N   1 
HETATM 13564 O  O   . LQW IA 2 .   ? -4.787  -32.081 64.174 1.00 85.67  ? 201 LQW G O   1 
HETATM 13565 C  C   . LQW IA 2 .   ? -4.697  -34.832 64.582 1.00 88.75  ? 201 LQW G C   1 
HETATM 13566 C  C4  . LQW IA 2 .   ? -7.050  -34.755 65.411 1.00 99.52  ? 201 LQW G C4  1 
HETATM 13567 SE SE  . LQW IA 2 .   ? -8.410  -34.049 65.901 1.00 86.23  ? 201 LQW G SE  1 
HETATM 13568 ZN ZN  . ZN  JA 3 .   ? -17.376 -49.744 56.723 1.00 22.53  ? 202 ZN  G ZN  1 
HETATM 13569 S  S   . SO4 KA 4 .   ? -9.348  -49.666 44.468 1.00 93.11  ? 203 SO4 G S   1 
HETATM 13570 O  O1  . SO4 KA 4 .   ? -9.257  -50.566 43.352 1.00 92.44  ? 203 SO4 G O1  1 
HETATM 13571 O  O2  . SO4 KA 4 .   ? -9.270  -48.315 43.974 1.00 106.95 ? 203 SO4 G O2  1 
HETATM 13572 O  O3  . SO4 KA 4 .   ? -8.270  -49.907 45.405 1.00 88.50  ? 203 SO4 G O3  1 
HETATM 13573 O  O4  . SO4 KA 4 .   ? -10.604 -49.870 45.138 1.00 101.90 ? 203 SO4 G O4  1 
HETATM 13574 C  C1  . LQW LA 2 .   ? 54.965  -43.459 3.730  1.00 71.92  ? 201 LQW H C1  1 
HETATM 13575 C  C2  . LQW LA 2 .   ? 56.004  -44.207 4.259  1.00 68.16  ? 201 LQW H C2  1 
HETATM 13576 C  C3  . LQW LA 2 .   ? 56.927  -43.580 5.118  1.00 78.35  ? 201 LQW H C3  1 
HETATM 13577 C  C5  . LQW LA 2 .   ? 55.745  -41.394 4.885  1.00 91.94  ? 201 LQW H C5  1 
HETATM 13578 C  C6  . LQW LA 2 .   ? 55.454  -39.898 5.086  1.00 99.82  ? 201 LQW H C6  1 
HETATM 13579 C  C7  . LQW LA 2 .   ? 54.807  -39.476 2.822  1.00 102.48 ? 201 LQW H C7  1 
HETATM 13580 C  C8  . LQW LA 2 .   ? 54.141  -38.429 1.988  1.00 107.32 ? 201 LQW H C8  1 
HETATM 13581 C  C9  . LQW LA 2 .   ? 54.499  -37.087 2.137  1.00 109.07 ? 201 LQW H C9  1 
HETATM 13582 C  C13 . LQW LA 2 .   ? 53.180  -38.835 1.058  1.00 107.92 ? 201 LQW H C13 1 
HETATM 13583 CL CL  . LQW LA 2 .   ? 52.066  -35.299 -0.628 1.00 136.49 ? 201 LQW H CL  1 
HETATM 13584 C  C11 . LQW LA 2 .   ? 52.895  -36.525 0.405  1.00 122.36 ? 201 LQW H C11 1 
HETATM 13585 C  C10 . LQW LA 2 .   ? 53.867  -36.128 1.340  1.00 111.97 ? 201 LQW H C10 1 
HETATM 13586 C  C12 . LQW LA 2 .   ? 52.549  -37.878 0.265  1.00 114.95 ? 201 LQW H C12 1 
HETATM 13587 N  N   . LQW LA 2 .   ? 54.604  -39.284 4.245  1.00 91.93  ? 201 LQW H N   1 
HETATM 13588 O  O   . LQW LA 2 .   ? 55.992  -39.264 5.991  1.00 106.39 ? 201 LQW H O   1 
HETATM 13589 C  C   . LQW LA 2 .   ? 54.842  -42.093 4.046  1.00 82.15  ? 201 LQW H C   1 
HETATM 13590 C  C4  . LQW LA 2 .   ? 56.907  -42.208 5.481  1.00 86.11  ? 201 LQW H C4  1 
HETATM 13591 SE SE  . LQW LA 2 .   ? 58.067  -41.699 6.501  1.00 81.43  ? 201 LQW H SE  1 
HETATM 13592 ZN ZN  . ZN  MA 3 .   ? 67.523  -56.787 16.115 1.00 24.82  ? 202 ZN  H ZN  1 
HETATM 13593 S  S   . SO4 NA 4 .   ? 63.271  -58.157 23.734 1.00 115.43 ? 203 SO4 H S   1 
HETATM 13594 O  O1  . SO4 NA 4 .   ? 62.570  -59.338 24.201 1.00 102.09 ? 203 SO4 H O1  1 
HETATM 13595 O  O2  . SO4 NA 4 .   ? 63.281  -58.126 22.296 1.00 116.95 ? 203 SO4 H O2  1 
HETATM 13596 O  O3  . SO4 NA 4 .   ? 64.633  -58.171 24.214 1.00 112.28 ? 203 SO4 H O3  1 
HETATM 13597 O  O4  . SO4 NA 4 .   ? 62.600  -56.981 24.217 1.00 113.28 ? 203 SO4 H O4  1 
HETATM 13598 C  C1  . LQW OA 2 .   ? 23.090  15.519  71.052 1.00 71.41  ? 201 LQW I C1  1 
HETATM 13599 C  C2  . LQW OA 2 .   ? 22.977  16.777  70.466 1.00 67.31  ? 201 LQW I C2  1 
HETATM 13600 C  C3  . LQW OA 2 .   ? 23.917  17.198  69.511 1.00 72.41  ? 201 LQW I C3  1 
HETATM 13601 C  C5  . LQW OA 2 .   ? 25.125  15.025  69.732 1.00 87.37  ? 201 LQW I C5  1 
HETATM 13602 C  C6  . LQW OA 2 .   ? 26.188  13.952  69.476 1.00 89.51  ? 201 LQW I C6  1 
HETATM 13603 C  C7  . LQW OA 2 .   ? 27.819  12.904  67.983 1.00 94.70  ? 201 LQW I C7  1 
HETATM 13604 C  C8  . LQW OA 2 .   ? 29.117  13.258  67.277 1.00 97.78  ? 201 LQW I C8  1 
HETATM 13605 C  C9  . LQW OA 2 .   ? 29.449  14.601  67.070 1.00 99.88  ? 201 LQW I C9  1 
HETATM 13606 C  C13 . LQW OA 2 .   ? 30.009  12.269  66.817 1.00 90.04  ? 201 LQW I C13 1 
HETATM 13607 CL CL  . LQW OA 2 .   ? 33.096  14.435  65.082 1.00 79.26  ? 201 LQW I CL  1 
HETATM 13608 C  C11 . LQW OA 2 .   ? 31.553  13.957  65.940 1.00 84.97  ? 201 LQW I C11 1 
HETATM 13609 C  C10 . LQW OA 2 .   ? 30.647  14.934  66.409 1.00 93.03  ? 201 LQW I C10 1 
HETATM 13610 C  C12 . LQW OA 2 .   ? 31.212  12.612  66.160 1.00 83.57  ? 201 LQW I C12 1 
HETATM 13611 N  N   . LQW OA 2 .   ? 27.141  14.082  68.528 1.00 90.25  ? 201 LQW I N   1 
HETATM 13612 O  O   . LQW OA 2 .   ? 26.100  12.936  70.191 1.00 77.55  ? 201 LQW I O   1 
HETATM 13613 C  C   . LQW OA 2 .   ? 24.137  14.657  70.687 1.00 78.28  ? 201 LQW I C   1 
HETATM 13614 C  C4  . LQW OA 2 .   ? 25.019  16.418  69.079 1.00 82.55  ? 201 LQW I C4  1 
HETATM 13615 SE SE  . LQW OA 2 .   ? 26.000  17.078  67.961 1.00 82.12  ? 201 LQW I SE  1 
HETATM 13616 ZN ZN  . ZN  PA 3 .   ? 16.900  32.585  58.543 1.00 21.08  ? 202 ZN  I ZN  1 
HETATM 13617 C  C1  . LQW QA 2 .   ? 52.297  -34.982 67.108 1.00 33.29  ? 201 LQW J C1  1 
HETATM 13618 C  C2  . LQW QA 2 .   ? 53.596  -35.521 67.104 1.00 33.05  ? 201 LQW J C2  1 
HETATM 13619 C  C3  . LQW QA 2 .   ? 53.829  -36.792 67.608 1.00 33.50  ? 201 LQW J C3  1 
HETATM 13620 C  C5  . LQW QA 2 .   ? 51.391  -36.940 68.135 1.00 34.68  ? 201 LQW J C5  1 
HETATM 13621 C  C6  . LQW QA 2 .   ? 50.247  -37.715 68.705 1.00 38.83  ? 201 LQW J C6  1 
HETATM 13622 C  C7  . LQW QA 2 .   ? 47.995  -38.528 68.686 1.00 38.16  ? 201 LQW J C7  1 
HETATM 13623 C  C8  . LQW QA 2 .   ? 47.895  -39.764 67.835 1.00 37.91  ? 201 LQW J C8  1 
HETATM 13624 C  C9  . LQW QA 2 .   ? 46.627  -40.225 67.459 1.00 38.52  ? 201 LQW J C9  1 
HETATM 13625 C  C13 . LQW QA 2 .   ? 49.050  -40.432 67.437 1.00 37.96  ? 201 LQW J C13 1 
HETATM 13626 CL CL  . LQW QA 2 .   ? 47.479  -43.474 65.239 1.00 38.86  ? 201 LQW J CL  1 
HETATM 13627 C  C11 . LQW QA 2 .   ? 47.641  -42.015 66.255 1.00 36.99  ? 201 LQW J C11 1 
HETATM 13628 C  C10 . LQW QA 2 .   ? 46.491  -41.357 66.663 1.00 37.35  ? 201 LQW J C10 1 
HETATM 13629 C  C12 . LQW QA 2 .   ? 48.913  -41.557 66.638 1.00 38.38  ? 201 LQW J C12 1 
HETATM 13630 N  N   . LQW QA 2 .   ? 49.020  -37.626 68.182 1.00 39.00  ? 201 LQW J N   1 
HETATM 13631 O  O   . LQW QA 2 .   ? 50.493  -38.438 69.674 1.00 44.94  ? 201 LQW J O   1 
HETATM 13632 C  C   . LQW QA 2 .   ? 51.190  -35.671 67.615 1.00 33.44  ? 201 LQW J C   1 
HETATM 13633 C  C4  . LQW QA 2 .   ? 52.765  -37.546 68.126 1.00 33.67  ? 201 LQW J C4  1 
HETATM 13634 SE SE  . LQW QA 2 .   ? 53.007  -38.990 68.714 1.00 27.86  ? 201 LQW J SE  1 
HETATM 13635 ZN ZN  . ZN  RA 3 .   ? 71.480  -38.746 60.348 1.00 20.46  ? 202 ZN  J ZN  1 
HETATM 13636 S  S   . SO4 SA 4 .   ? 67.682  -31.899 47.801 1.00 79.24  ? 203 SO4 J S   1 
HETATM 13637 O  O1  . SO4 SA 4 .   ? 68.048  -30.856 46.883 1.00 87.04  ? 203 SO4 J O1  1 
HETATM 13638 O  O2  . SO4 SA 4 .   ? 67.383  -33.081 47.043 1.00 85.76  ? 203 SO4 J O2  1 
HETATM 13639 O  O3  . SO4 SA 4 .   ? 68.777  -32.159 48.707 1.00 78.81  ? 203 SO4 J O3  1 
HETATM 13640 O  O4  . SO4 SA 4 .   ? 66.516  -31.497 48.555 1.00 89.56  ? 203 SO4 J O4  1 
HETATM 13641 S  S   . SO4 TA 4 .   ? 75.014  -35.120 50.888 1.00 119.56 ? 204 SO4 J S   1 
HETATM 13642 O  O1  . SO4 TA 4 .   ? 75.501  -35.965 49.829 1.00 127.01 ? 204 SO4 J O1  1 
HETATM 13643 O  O2  . SO4 TA 4 .   ? 75.114  -33.735 50.495 1.00 110.90 ? 204 SO4 J O2  1 
HETATM 13644 O  O3  . SO4 TA 4 .   ? 73.640  -35.454 51.186 1.00 135.80 ? 204 SO4 J O3  1 
HETATM 13645 O  O4  . SO4 TA 4 .   ? 75.813  -35.335 52.054 1.00 126.26 ? 204 SO4 J O4  1 
HETATM 13646 C  C1  . LQW UA 2 .   ? -3.218  -41.804 0.773  1.00 57.76  ? 201 LQW K C1  1 
HETATM 13647 C  C2  . LQW UA 2 .   ? -4.252  -42.219 1.609  1.00 54.09  ? 201 LQW K C2  1 
HETATM 13648 C  C3  . LQW UA 2 .   ? -4.038  -43.226 2.544  1.00 54.20  ? 201 LQW K C3  1 
HETATM 13649 C  C5  . LQW UA 2 .   ? -1.746  -43.446 1.772  1.00 58.20  ? 201 LQW K C5  1 
HETATM 13650 C  C6  . LQW UA 2 .   ? -0.385  -44.024 1.802  1.00 64.39  ? 201 LQW K C6  1 
HETATM 13651 C  C7  . LQW UA 2 .   ? 1.022   -45.947 1.597  1.00 99.76  ? 201 LQW K C7  1 
HETATM 13652 C  C8  . LQW UA 2 .   ? 1.451   -46.374 2.988  1.00 94.24  ? 201 LQW K C8  1 
HETATM 13653 C  C9  . LQW UA 2 .   ? 1.670   -45.450 4.019  1.00 82.03  ? 201 LQW K C9  1 
HETATM 13654 C  C13 . LQW UA 2 .   ? 1.633   -47.748 3.194  1.00 102.89 ? 201 LQW K C13 1 
HETATM 13655 CL CL  . LQW UA 2 .   ? 2.747   -47.977 7.027  1.00 92.67  ? 201 LQW K CL  1 
HETATM 13656 C  C11 . LQW UA 2 .   ? 2.241   -47.308 5.449  1.00 87.05  ? 201 LQW K C11 1 
HETATM 13657 C  C10 . LQW UA 2 .   ? 2.068   -45.930 5.259  1.00 81.93  ? 201 LQW K C10 1 
HETATM 13658 C  C12 . LQW UA 2 .   ? 2.026   -48.225 4.431  1.00 90.06  ? 201 LQW K C12 1 
HETATM 13659 N  N   . LQW UA 2 .   ? -0.291  -45.335 1.612  1.00 67.48  ? 201 LQW K N   1 
HETATM 13660 O  O   . LQW UA 2 .   ? 0.562   -43.253 2.009  1.00 62.83  ? 201 LQW K O   1 
HETATM 13661 C  C   . LQW UA 2 .   ? -1.967  -42.409 0.861  1.00 59.69  ? 201 LQW K C   1 
HETATM 13662 C  C4  . LQW UA 2 .   ? -2.834  -43.915 2.687  1.00 53.26  ? 201 LQW K C4  1 
HETATM 13663 SE SE  . LQW UA 2 .   ? -2.704  -45.087 3.780  1.00 39.60  ? 201 LQW K SE  1 
HETATM 13664 ZN ZN  . ZN  VA 3 .   ? -21.395 -45.776 11.864 1.00 24.40  ? 202 ZN  K ZN  1 
HETATM 13665 S  S   . SO4 WA 4 .   ? -18.542 -39.192 24.397 1.00 101.75 ? 203 SO4 K S   1 
HETATM 13666 O  O1  . SO4 WA 4 .   ? -18.055 -37.908 23.951 1.00 100.31 ? 203 SO4 K O1  1 
HETATM 13667 O  O2  . SO4 WA 4 .   ? -19.067 -39.923 23.270 1.00 114.42 ? 203 SO4 K O2  1 
HETATM 13668 O  O3  . SO4 WA 4 .   ? -17.459 -39.926 25.006 1.00 98.88  ? 203 SO4 K O3  1 
HETATM 13669 O  O4  . SO4 WA 4 .   ? -19.599 -39.012 25.356 1.00 109.78 ? 203 SO4 K O4  1 
HETATM 13670 S  S   . SO4 XA 4 .   ? -25.446 -42.280 21.353 1.00 107.42 ? 204 SO4 K S   1 
HETATM 13671 O  O1  . SO4 XA 4 .   ? -24.334 -43.038 20.835 1.00 118.62 ? 204 SO4 K O1  1 
HETATM 13672 O  O2  . SO4 XA 4 .   ? -25.447 -40.962 20.774 1.00 101.53 ? 204 SO4 K O2  1 
HETATM 13673 O  O3  . SO4 XA 4 .   ? -25.336 -42.162 22.783 1.00 113.76 ? 204 SO4 K O3  1 
HETATM 13674 O  O4  . SO4 XA 4 .   ? -26.670 -42.958 21.025 1.00 117.16 ? 204 SO4 K O4  1 
HETATM 13675 S  S   . SO4 YA 4 .   ? -20.529 -41.064 18.971 1.00 116.52 ? 205 SO4 K S   1 
HETATM 13676 O  O1  . SO4 YA 4 .   ? -20.567 -40.627 17.593 1.00 112.66 ? 205 SO4 K O1  1 
HETATM 13677 O  O2  . SO4 YA 4 .   ? -21.335 -42.253 19.110 1.00 109.94 ? 205 SO4 K O2  1 
HETATM 13678 O  O3  . SO4 YA 4 .   ? -19.174 -41.360 19.333 1.00 119.22 ? 205 SO4 K O3  1 
HETATM 13679 O  O4  . SO4 YA 4 .   ? -21.023 -40.026 19.852 1.00 103.44 ? 205 SO4 K O4  1 
HETATM 13680 C  C1  . LQW ZA 2 .   ? 26.685  8.340   2.262  1.00 81.79  ? 201 LQW L C1  1 
HETATM 13681 C  C2  . LQW ZA 2 .   ? 26.689  9.591   2.854  1.00 80.87  ? 201 LQW L C2  1 
HETATM 13682 C  C3  . LQW ZA 2 .   ? 25.760  9.875   3.870  1.00 91.79  ? 201 LQW L C3  1 
HETATM 13683 C  C5  . LQW ZA 2 .   ? 24.796  7.593   3.700  1.00 96.94  ? 201 LQW L C5  1 
HETATM 13684 C  C6  . LQW ZA 2 .   ? 23.883  6.395   4.021  1.00 100.61 ? 201 LQW L C6  1 
HETATM 13685 C  C7  . LQW ZA 2 .   ? 22.035  5.440   5.452  1.00 106.72 ? 201 LQW L C7  1 
HETATM 13686 C  C8  . LQW ZA 2 .   ? 20.791  5.821   6.267  1.00 106.53 ? 201 LQW L C8  1 
HETATM 13687 C  C9  . LQW ZA 2 .   ? 19.930  4.803   6.718  1.00 100.04 ? 201 LQW L C9  1 
HETATM 13688 C  C13 . LQW ZA 2 .   ? 20.470  7.152   6.586  1.00 106.81 ? 201 LQW L C13 1 
HETATM 13689 CL CL  . LQW ZA 2 .   ? 16.983  6.822   8.771  1.00 80.64  ? 201 LQW L CL  1 
HETATM 13690 C  C11 . LQW ZA 2 .   ? 18.463  6.427   7.793  1.00 93.02  ? 201 LQW L C11 1 
HETATM 13691 C  C10 . LQW ZA 2 .   ? 18.780  5.098   7.467  1.00 93.36  ? 201 LQW L C10 1 
HETATM 13692 C  C12 . LQW ZA 2 .   ? 19.317  7.449   7.338  1.00 98.03  ? 201 LQW L C12 1 
HETATM 13693 N  N   . LQW ZA 2 .   ? 22.857  6.534   4.912  1.00 106.48 ? 201 LQW L N   1 
HETATM 13694 O  O   . LQW ZA 2 .   ? 24.128  5.307   3.453  1.00 80.26  ? 201 LQW L O   1 
HETATM 13695 C  C   . LQW ZA 2 .   ? 25.762  7.371   2.686  1.00 88.40  ? 201 LQW L C   1 
HETATM 13696 C  C4  . LQW ZA 2 .   ? 24.778  8.980   4.371  1.00 96.60  ? 201 LQW L C4  1 
HETATM 13697 SE SE  . LQW ZA 2 .   ? 23.807  9.532   5.571  1.00 97.45  ? 201 LQW L SE  1 
HETATM 13698 ZN ZN  . ZN  AB 3 .   ? 33.122  25.358  14.187 1.00 29.03  ? 202 ZN  L ZN  1 
HETATM 13699 S  S   . SO4 BB 4 .   ? 37.387  19.078  26.676 1.00 92.59  ? 203 SO4 L S   1 
HETATM 13700 O  O1  . SO4 BB 4 .   ? 37.444  20.101  25.664 1.00 94.63  ? 203 SO4 L O1  1 
HETATM 13701 O  O2  . SO4 BB 4 .   ? 37.413  17.785  26.037 1.00 101.72 ? 203 SO4 L O2  1 
HETATM 13702 O  O3  . SO4 BB 4 .   ? 38.522  19.214  27.553 1.00 90.32  ? 203 SO4 L O3  1 
HETATM 13703 O  O4  . SO4 BB 4 .   ? 36.170  19.209  27.444 1.00 93.91  ? 203 SO4 L O4  1 
HETATM 13704 O  O   . HOH CB 5 .   ? 32.097  -26.492 58.542 1.00 18.23  ? 301 HOH A O   1 
HETATM 13705 O  O   . HOH CB 5 .   ? 60.053  -25.011 58.645 1.00 11.70  ? 302 HOH A O   1 
HETATM 13706 O  O   . HOH CB 5 .   ? 33.089  -32.141 53.063 1.00 17.01  ? 303 HOH A O   1 
HETATM 13707 O  O   . HOH CB 5 .   ? 51.846  -30.713 53.621 1.00 15.85  ? 304 HOH A O   1 
HETATM 13708 O  O   . HOH CB 5 .   ? 38.098  -25.100 41.712 1.00 18.26  ? 305 HOH A O   1 
HETATM 13709 O  O   . HOH CB 5 .   ? 32.224  -23.594 67.709 1.00 21.38  ? 306 HOH A O   1 
HETATM 13710 O  O   . HOH CB 5 .   ? 19.690  -29.261 57.444 1.00 12.13  ? 307 HOH A O   1 
HETATM 13711 O  O   . HOH CB 5 .   ? 32.494  -38.638 50.544 1.00 23.94  ? 308 HOH A O   1 
HETATM 13712 O  O   . HOH CB 5 .   ? 19.548  -37.706 53.028 1.00 30.95  ? 309 HOH A O   1 
HETATM 13713 O  O   . HOH CB 5 .   ? 34.602  -33.597 66.657 1.00 16.64  ? 310 HOH A O   1 
HETATM 13714 O  O   . HOH CB 5 .   ? 39.443  -17.543 51.767 1.00 26.17  ? 311 HOH A O   1 
HETATM 13715 O  O   . HOH CB 5 .   ? 29.834  -20.926 61.064 1.00 22.63  ? 312 HOH A O   1 
HETATM 13716 O  O   . HOH CB 5 .   ? 25.178  -23.592 68.053 1.00 25.69  ? 313 HOH A O   1 
HETATM 13717 O  O   . HOH CB 5 .   ? 35.548  -40.425 54.463 1.00 17.18  ? 314 HOH A O   1 
HETATM 13718 O  O   . HOH CB 5 .   ? 36.232  -20.858 67.714 1.00 21.39  ? 315 HOH A O   1 
HETATM 13719 O  O   . HOH CB 5 .   ? 29.109  -33.818 49.502 1.00 16.45  ? 316 HOH A O   1 
HETATM 13720 O  O   . HOH CB 5 .   ? 46.727  -36.314 52.529 1.00 21.94  ? 317 HOH A O   1 
HETATM 13721 O  O   . HOH CB 5 .   ? 39.501  -30.648 70.691 1.00 14.44  ? 318 HOH A O   1 
HETATM 13722 O  O   . HOH CB 5 .   ? 37.520  -16.878 61.433 1.00 14.05  ? 319 HOH A O   1 
HETATM 13723 O  O   . HOH CB 5 .   ? 37.702  -10.719 42.497 1.00 23.81  ? 320 HOH A O   1 
HETATM 13724 O  O   . HOH CB 5 .   ? 49.006  -13.912 59.788 1.00 19.67  ? 321 HOH A O   1 
HETATM 13725 O  O   . HOH CB 5 .   ? 53.437  -12.893 55.892 1.00 22.93  ? 322 HOH A O   1 
HETATM 13726 O  O   . HOH CB 5 .   ? 30.784  -39.991 58.461 1.00 17.03  ? 323 HOH A O   1 
HETATM 13727 O  O   . HOH DB 5 .   ? 17.617  -33.504 16.177 1.00 16.82  ? 301 HOH B O   1 
HETATM 13728 O  O   . HOH DB 5 .   ? 0.349   -47.259 18.929 1.00 16.73  ? 302 HOH B O   1 
HETATM 13729 O  O   . HOH DB 5 .   ? -10.434 -31.955 14.421 1.00 28.32  ? 303 HOH B O   1 
HETATM 13730 O  O   . HOH DB 5 .   ? 16.762  -39.646 20.889 1.00 9.14   ? 304 HOH B O   1 
HETATM 13731 O  O   . HOH DB 5 .   ? 13.979  -28.043 6.845  1.00 20.37  ? 305 HOH B O   1 
HETATM 13732 O  O   . HOH DB 5 .   ? 10.388  -24.946 23.052 1.00 12.93  ? 306 HOH B O   1 
HETATM 13733 O  O   . HOH DB 5 .   ? 16.045  -40.069 7.020  1.00 24.24  ? 307 HOH B O   1 
HETATM 13734 O  O   . HOH DB 5 .   ? -1.119  -41.420 21.331 1.00 10.30  ? 308 HOH B O   1 
HETATM 13735 O  O   . HOH DB 5 .   ? 24.893  -29.408 7.243  1.00 12.14  ? 309 HOH B O   1 
HETATM 13736 O  O   . HOH DB 5 .   ? 19.648  -27.250 29.097 1.00 21.95  ? 310 HOH B O   1 
HETATM 13737 O  O   . HOH DB 5 .   ? 20.555  -41.364 24.730 1.00 18.26  ? 311 HOH B O   1 
HETATM 13738 O  O   . HOH DB 5 .   ? 3.550   -43.731 21.049 1.00 21.39  ? 312 HOH B O   1 
HETATM 13739 O  O   . HOH DB 5 .   ? 20.324  -27.700 14.137 1.00 9.68   ? 313 HOH B O   1 
HETATM 13740 O  O   . HOH DB 5 .   ? -6.057  -22.119 9.168  1.00 33.42  ? 314 HOH B O   1 
HETATM 13741 O  O   . HOH DB 5 .   ? 0.197   -20.818 14.512 1.00 17.37  ? 315 HOH B O   1 
HETATM 13742 O  O   . HOH EB 5 .   ? 11.729  15.522  57.474 1.00 19.14  ? 301 HOH C O   1 
HETATM 13743 O  O   . HOH EB 5 .   ? 40.892  -11.146 52.187 1.00 24.43  ? 302 HOH C O   1 
HETATM 13744 O  O   . HOH EB 5 .   ? 20.327  11.446  52.881 1.00 13.03  ? 303 HOH C O   1 
HETATM 13745 O  O   . HOH EB 5 .   ? 26.658  -6.897  57.991 1.00 21.38  ? 304 HOH C O   1 
HETATM 13746 O  O   . HOH EB 5 .   ? 20.110  -6.115  67.270 1.00 16.18  ? 305 HOH C O   1 
HETATM 13747 O  O   . HOH EB 5 .   ? 29.405  14.810  52.755 1.00 14.36  ? 306 HOH C O   1 
HETATM 13748 O  O   . HOH EB 5 .   ? 34.557  -1.532  55.802 1.00 20.94  ? 307 HOH C O   1 
HETATM 13749 O  O   . HOH EB 5 .   ? 23.206  -8.799  67.599 1.00 21.26  ? 308 HOH C O   1 
HETATM 13750 O  O   . HOH EB 5 .   ? 28.762  -14.023 68.026 1.00 18.43  ? 309 HOH C O   1 
HETATM 13751 O  O   . HOH EB 5 .   ? 15.423  -5.704  36.873 1.00 15.48  ? 310 HOH C O   1 
HETATM 13752 O  O   . HOH EB 5 .   ? 22.552  -11.809 60.724 1.00 15.18  ? 311 HOH C O   1 
HETATM 13753 O  O   . HOH EB 5 .   ? 24.567  -19.079 56.687 1.00 19.40  ? 312 HOH C O   1 
HETATM 13754 O  O   . HOH EB 5 .   ? 33.434  1.493   45.812 1.00 6.18   ? 313 HOH C O   1 
HETATM 13755 O  O   . HOH EB 5 .   ? 34.838  -6.445  49.041 1.00 21.52  ? 314 HOH C O   1 
HETATM 13756 O  O   . HOH EB 5 .   ? 15.206  -7.990  61.850 1.00 19.49  ? 315 HOH C O   1 
HETATM 13757 O  O   . HOH EB 5 .   ? 14.046  7.124   44.659 1.00 21.60  ? 316 HOH C O   1 
HETATM 13758 O  O   . HOH EB 5 .   ? 24.169  -15.398 53.278 1.00 6.24   ? 317 HOH C O   1 
HETATM 13759 O  O   . HOH EB 5 .   ? 2.279   13.193  58.431 1.00 18.92  ? 318 HOH C O   1 
HETATM 13760 O  O   . HOH FB 5 .   ? 29.825  4.138   20.804 1.00 14.87  ? 301 HOH D O   1 
HETATM 13761 O  O   . HOH FB 5 .   ? 14.636  -23.398 17.109 1.00 21.84  ? 302 HOH D O   1 
HETATM 13762 O  O   . HOH FB 5 .   ? 37.369  -13.551 25.733 1.00 22.24  ? 303 HOH D O   1 
HETATM 13763 O  O   . HOH FB 5 .   ? 34.671  -13.424 22.679 1.00 40.70  ? 304 HOH D O   1 
HETATM 13764 O  O   . HOH FB 5 .   ? 39.194  8.672   15.920 1.00 17.34  ? 305 HOH D O   1 
HETATM 13765 O  O   . HOH FB 5 .   ? 23.408  -14.355 16.092 1.00 30.37  ? 306 HOH D O   1 
HETATM 13766 O  O   . HOH FB 5 .   ? 20.742  7.638   20.968 1.00 27.29  ? 307 HOH D O   1 
HETATM 13767 O  O   . HOH FB 5 .   ? 31.344  -15.197 35.944 1.00 17.17  ? 308 HOH D O   1 
HETATM 13768 O  O   . HOH FB 5 .   ? 20.494  -19.114 25.612 1.00 10.76  ? 309 HOH D O   1 
HETATM 13769 O  O   . HOH FB 5 .   ? 14.879  -9.360  16.575 1.00 12.30  ? 310 HOH D O   1 
HETATM 13770 O  O   . HOH FB 5 .   ? 15.617  -8.148  19.117 1.00 21.33  ? 311 HOH D O   1 
HETATM 13771 O  O   . HOH FB 5 .   ? 39.566  -1.399  21.674 1.00 11.68  ? 312 HOH D O   1 
HETATM 13772 O  O   . HOH FB 5 .   ? 16.876  -5.105  28.162 1.00 6.86   ? 313 HOH D O   1 
HETATM 13773 O  O   . HOH FB 5 .   ? 43.405  -1.677  19.102 1.00 22.01  ? 314 HOH D O   1 
HETATM 13774 O  O   . HOH FB 5 .   ? 21.870  -24.520 22.585 1.00 11.08  ? 315 HOH D O   1 
HETATM 13775 O  O   . HOH GB 5 .   ? 13.091  -24.462 40.971 1.00 22.87  ? 301 HOH E O   1 
HETATM 13776 O  O   . HOH GB 5 .   ? -7.487  -30.033 50.728 1.00 32.81  ? 302 HOH E O   1 
HETATM 13777 O  O   . HOH GB 5 .   ? 17.323  -38.029 62.362 1.00 18.07  ? 303 HOH E O   1 
HETATM 13778 O  O   . HOH GB 5 .   ? 18.231  -23.145 60.684 1.00 21.12  ? 304 HOH E O   1 
HETATM 13779 O  O   . HOH GB 5 .   ? 16.635  -28.005 56.482 1.00 12.78  ? 305 HOH E O   1 
HETATM 13780 O  O   . HOH GB 5 .   ? 12.493  -22.146 57.544 1.00 15.77  ? 306 HOH E O   1 
HETATM 13781 O  O   . HOH GB 5 .   ? 4.392   -20.575 65.081 1.00 17.28  ? 307 HOH E O   1 
HETATM 13782 O  O   . HOH GB 5 .   ? 17.668  -32.200 51.116 1.00 29.15  ? 308 HOH E O   1 
HETATM 13783 O  O   . HOH GB 5 .   ? -2.510  -35.619 70.285 1.00 18.59  ? 309 HOH E O   1 
HETATM 13784 O  O   . HOH GB 5 .   ? 17.752  -18.015 68.366 1.00 14.30  ? 310 HOH E O   1 
HETATM 13785 O  O   . HOH GB 5 .   ? 2.823   -20.294 44.350 1.00 24.40  ? 311 HOH E O   1 
HETATM 13786 O  O   . HOH GB 5 .   ? 17.536  -18.477 45.611 1.00 19.15  ? 312 HOH E O   1 
HETATM 13787 O  O   . HOH GB 5 .   ? 3.936   -39.119 69.213 1.00 22.66  ? 313 HOH E O   1 
HETATM 13788 O  O   . HOH GB 5 .   ? 18.897  -31.638 63.950 1.00 14.10  ? 314 HOH E O   1 
HETATM 13789 O  O   . HOH GB 5 .   ? 19.225  -36.185 60.169 1.00 14.09  ? 315 HOH E O   1 
HETATM 13790 O  O   . HOH GB 5 .   ? 4.633   -18.461 50.261 1.00 15.77  ? 316 HOH E O   1 
HETATM 13791 O  O   . HOH GB 5 .   ? -2.084  -41.085 64.562 1.00 7.76   ? 317 HOH E O   1 
HETATM 13792 O  O   . HOH GB 5 .   ? -1.759  -29.564 42.811 1.00 20.41  ? 318 HOH E O   1 
HETATM 13793 O  O   . HOH HB 5 .   ? 33.745  -35.095 18.328 1.00 8.02   ? 301 HOH F O   1 
HETATM 13794 O  O   . HOH HB 5 .   ? 38.287  -33.756 33.144 1.00 22.78  ? 302 HOH F O   1 
HETATM 13795 O  O   . HOH HB 5 .   ? 32.677  -34.366 36.818 1.00 15.63  ? 303 HOH F O   1 
HETATM 13796 O  O   . HOH HB 5 .   ? 37.563  -29.269 16.435 1.00 13.28  ? 304 HOH F O   1 
HETATM 13797 O  O   . HOH HB 5 .   ? 58.165  -37.164 22.039 1.00 24.99  ? 305 HOH F O   1 
HETATM 13798 O  O   . HOH HB 5 .   ? 34.756  -31.253 7.153  1.00 15.44  ? 306 HOH F O   1 
HETATM 13799 O  O   . HOH HB 5 .   ? 26.051  -40.349 32.442 1.00 18.38  ? 307 HOH F O   1 
HETATM 13800 O  O   . HOH HB 5 .   ? 51.224  -24.789 21.500 1.00 18.94  ? 308 HOH F O   1 
HETATM 13801 O  O   . HOH HB 5 .   ? 53.104  -34.826 23.784 1.00 14.29  ? 309 HOH F O   1 
HETATM 13802 O  O   . HOH HB 5 .   ? 31.000  -25.247 6.683  1.00 13.33  ? 310 HOH F O   1 
HETATM 13803 O  O   . HOH HB 5 .   ? 31.033  -30.692 14.027 1.00 19.21  ? 311 HOH F O   1 
HETATM 13804 O  O   . HOH HB 5 .   ? 35.773  -19.731 29.172 1.00 13.61  ? 312 HOH F O   1 
HETATM 13805 O  O   . HOH HB 5 .   ? 41.961  -53.080 19.094 1.00 16.72  ? 313 HOH F O   1 
HETATM 13806 O  O   . HOH HB 5 .   ? 33.530  -24.656 28.785 1.00 8.94   ? 314 HOH F O   1 
HETATM 13807 O  O   . HOH HB 5 .   ? 31.983  -34.744 9.132  1.00 20.33  ? 315 HOH F O   1 
HETATM 13808 O  O   . HOH HB 5 .   ? 34.471  -51.178 16.863 1.00 15.86  ? 316 HOH F O   1 
HETATM 13809 O  O   . HOH HB 5 .   ? 35.774  -49.993 14.247 1.00 21.31  ? 317 HOH F O   1 
HETATM 13810 O  O   . HOH HB 5 .   ? 24.333  -44.982 32.371 1.00 26.06  ? 318 HOH F O   1 
HETATM 13811 O  O   . HOH IB 5 .   ? -8.874  -22.779 54.027 1.00 23.40  ? 301 HOH G O   1 
HETATM 13812 O  O   . HOH IB 5 .   ? -21.968 -47.176 55.473 1.00 22.82  ? 302 HOH G O   1 
HETATM 13813 O  O   . HOH IB 5 .   ? -8.079  -32.896 50.065 1.00 9.81   ? 303 HOH G O   1 
HETATM 13814 O  O   . HOH IB 5 .   ? -16.339 -49.618 50.453 1.00 21.61  ? 304 HOH G O   1 
HETATM 13815 O  O   . HOH IB 5 .   ? -5.253  -42.506 49.134 1.00 18.43  ? 305 HOH G O   1 
HETATM 13816 O  O   . HOH IB 5 .   ? -21.190 -39.594 34.066 1.00 18.31  ? 306 HOH G O   1 
HETATM 13817 O  O   . HOH IB 5 .   ? -27.964 -46.900 41.828 1.00 11.50  ? 307 HOH G O   1 
HETATM 13818 O  O   . HOH IB 5 .   ? -12.688 -51.101 53.427 1.00 22.38  ? 308 HOH G O   1 
HETATM 13819 O  O   . HOH IB 5 .   ? -25.550 -37.036 50.178 1.00 23.36  ? 309 HOH G O   1 
HETATM 13820 O  O   . HOH IB 5 .   ? -17.071 -23.108 52.200 1.00 14.02  ? 310 HOH G O   1 
HETATM 13821 O  O   . HOH IB 5 .   ? -7.398  -51.981 52.635 1.00 11.77  ? 311 HOH G O   1 
HETATM 13822 O  O   . HOH IB 5 .   ? -5.070  -39.828 49.817 1.00 16.70  ? 312 HOH G O   1 
HETATM 13823 O  O   . HOH IB 5 .   ? -22.678 -57.986 45.826 1.00 16.92  ? 313 HOH G O   1 
HETATM 13824 O  O   . HOH IB 5 .   ? -8.581  -33.087 70.847 1.00 12.77  ? 314 HOH G O   1 
HETATM 13825 O  O   . HOH IB 5 .   ? -19.723 -62.115 59.775 1.00 13.40  ? 315 HOH G O   1 
HETATM 13826 O  O   . HOH IB 5 .   ? -30.403 -42.063 41.439 1.00 26.56  ? 316 HOH G O   1 
HETATM 13827 O  O   . HOH IB 5 .   ? -13.136 -50.795 49.832 1.00 13.65  ? 317 HOH G O   1 
HETATM 13828 O  O   . HOH IB 5 .   ? -23.475 -25.518 55.312 1.00 15.93  ? 318 HOH G O   1 
HETATM 13829 O  O   . HOH JB 5 .   ? 75.186  -66.241 17.694 1.00 28.47  ? 301 HOH H O   1 
HETATM 13830 O  O   . HOH JB 5 .   ? 57.873  -40.073 22.651 1.00 14.03  ? 302 HOH H O   1 
HETATM 13831 O  O   . HOH JB 5 .   ? 63.152  -58.256 18.562 1.00 24.86  ? 303 HOH H O   1 
HETATM 13832 O  O   . HOH JB 5 .   ? 60.044  -50.341 32.948 1.00 11.73  ? 304 HOH H O   1 
HETATM 13833 O  O   . HOH JB 5 .   ? 80.814  -46.606 31.073 1.00 24.86  ? 305 HOH H O   1 
HETATM 13834 O  O   . HOH JB 5 .   ? 72.049  -54.114 17.155 1.00 31.21  ? 306 HOH H O   1 
HETATM 13835 O  O   . HOH JB 5 .   ? 69.988  -49.788 33.659 1.00 13.51  ? 307 HOH H O   1 
HETATM 13836 O  O   . HOH JB 5 .   ? 76.175  -48.490 37.680 1.00 17.68  ? 308 HOH H O   1 
HETATM 13837 O  O   . HOH JB 5 .   ? 69.977  -52.663 33.544 1.00 11.14  ? 309 HOH H O   1 
HETATM 13838 O  O   . HOH JB 5 .   ? 66.659  -56.763 22.380 1.00 16.00  ? 310 HOH H O   1 
HETATM 13839 O  O   . HOH JB 5 .   ? 63.050  -47.774 34.019 1.00 11.09  ? 311 HOH H O   1 
HETATM 13840 O  O   . HOH JB 5 .   ? 56.269  -41.773 23.887 1.00 16.53  ? 312 HOH H O   1 
HETATM 13841 O  O   . HOH JB 5 .   ? 78.069  -53.760 14.131 1.00 21.03  ? 313 HOH H O   1 
HETATM 13842 O  O   . HOH JB 5 .   ? 55.599  -49.442 24.201 1.00 21.60  ? 314 HOH H O   1 
HETATM 13843 O  O   . HOH JB 5 .   ? 75.611  -56.509 29.781 1.00 21.78  ? 315 HOH H O   1 
HETATM 13844 O  O   . HOH JB 5 .   ? 57.961  -59.014 20.261 1.00 10.69  ? 316 HOH H O   1 
HETATM 13845 O  O   . HOH JB 5 .   ? 81.419  -39.358 32.435 1.00 25.87  ? 317 HOH H O   1 
HETATM 13846 O  O   . HOH JB 5 .   ? 60.617  -56.374 29.068 1.00 9.26   ? 318 HOH H O   1 
HETATM 13847 O  O   . HOH JB 5 .   ? 78.766  -53.462 30.398 1.00 18.60  ? 319 HOH H O   1 
HETATM 13848 O  O   . HOH JB 5 .   ? 66.893  -61.262 26.021 1.00 14.18  ? 320 HOH H O   1 
HETATM 13849 O  O   . HOH JB 5 .   ? 64.232  -36.542 5.071  1.00 20.28  ? 321 HOH H O   1 
HETATM 13850 O  O   . HOH JB 5 .   ? 55.507  -47.160 23.101 1.00 20.00  ? 322 HOH H O   1 
HETATM 13851 O  O   . HOH JB 5 .   ? 55.582  -46.800 29.997 1.00 10.61  ? 323 HOH H O   1 
HETATM 13852 O  O   . HOH JB 5 .   ? 78.582  -56.399 28.773 1.00 20.80  ? 324 HOH H O   1 
HETATM 13853 O  O   . HOH KB 5 .   ? 26.918  16.316  52.367 1.00 7.95   ? 301 HOH I O   1 
HETATM 13854 O  O   . HOH KB 5 .   ? 16.286  40.086  62.613 1.00 12.14  ? 302 HOH I O   1 
HETATM 13855 O  O   . HOH KB 5 .   ? 26.948  35.598  36.579 1.00 31.62  ? 303 HOH I O   1 
HETATM 13856 O  O   . HOH KB 5 .   ? 21.386  35.417  57.300 1.00 16.44  ? 304 HOH I O   1 
HETATM 13857 O  O   . HOH KB 5 .   ? 18.071  13.277  53.390 1.00 16.91  ? 305 HOH I O   1 
HETATM 13858 O  O   . HOH KB 5 .   ? 36.623  11.948  56.228 1.00 19.84  ? 306 HOH I O   1 
HETATM 13859 O  O   . HOH KB 5 .   ? 28.675  34.646  65.144 1.00 22.18  ? 307 HOH I O   1 
HETATM 13860 O  O   . HOH KB 5 .   ? 31.819  33.884  49.572 1.00 24.37  ? 308 HOH I O   1 
HETATM 13861 O  O   . HOH KB 5 .   ? 40.749  22.934  53.083 1.00 17.94  ? 309 HOH I O   1 
HETATM 13862 O  O   . HOH KB 5 .   ? 34.723  38.910  39.876 1.00 37.85  ? 310 HOH I O   1 
HETATM 13863 O  O   . HOH KB 5 .   ? 25.157  40.327  59.436 1.00 8.80   ? 311 HOH I O   1 
HETATM 13864 O  O   . HOH KB 5 .   ? 23.456  30.143  39.844 1.00 9.12   ? 312 HOH I O   1 
HETATM 13865 O  O   . HOH KB 5 .   ? 10.375  25.106  54.477 1.00 12.35  ? 313 HOH I O   1 
HETATM 13866 O  O   . HOH KB 5 .   ? 6.106   39.892  60.688 1.00 14.63  ? 314 HOH I O   1 
HETATM 13867 O  O   . HOH KB 5 .   ? 13.390  25.763  46.128 1.00 10.01  ? 315 HOH I O   1 
HETATM 13868 O  O   . HOH KB 5 .   ? 20.393  44.590  64.855 1.00 15.78  ? 316 HOH I O   1 
HETATM 13869 O  O   . HOH KB 5 .   ? 28.365  41.435  40.768 1.00 22.67  ? 317 HOH I O   1 
HETATM 13870 O  O   . HOH KB 5 .   ? 9.288   31.905  64.222 1.00 15.75  ? 318 HOH I O   1 
HETATM 13871 O  O   . HOH KB 5 .   ? 40.201  26.347  58.261 1.00 22.67  ? 319 HOH I O   1 
HETATM 13872 O  O   . HOH KB 5 .   ? 33.616  21.648  44.659 1.00 25.69  ? 320 HOH I O   1 
HETATM 13873 O  O   . HOH KB 5 .   ? 29.250  38.820  63.563 1.00 22.12  ? 321 HOH I O   1 
HETATM 13874 O  O   . HOH LB 5 .   ? 60.511  -48.884 39.800 1.00 15.45  ? 301 HOH J O   1 
HETATM 13875 O  O   . HOH LB 5 .   ? 63.842  -43.733 71.685 1.00 23.20  ? 302 HOH J O   1 
HETATM 13876 O  O   . HOH LB 5 .   ? 70.964  -37.516 54.184 1.00 34.73  ? 303 HOH J O   1 
HETATM 13877 O  O   . HOH LB 5 .   ? 66.689  -50.029 67.180 1.00 5.07   ? 304 HOH J O   1 
HETATM 13878 O  O   . HOH LB 5 .   ? 61.108  -56.701 52.723 1.00 19.49  ? 305 HOH J O   1 
HETATM 13879 O  O   . HOH LB 5 .   ? 54.531  -29.867 54.538 1.00 23.03  ? 306 HOH J O   1 
HETATM 13880 O  O   . HOH LB 5 .   ? 71.198  -44.120 58.831 1.00 38.48  ? 307 HOH J O   1 
HETATM 13881 O  O   . HOH LB 5 .   ? 71.124  -48.113 67.940 1.00 11.05  ? 308 HOH J O   1 
HETATM 13882 O  O   . HOH LB 5 .   ? 73.532  -49.916 61.200 1.00 2.57   ? 309 HOH J O   1 
HETATM 13883 O  O   . HOH LB 5 .   ? 79.064  -47.836 55.355 1.00 19.69  ? 310 HOH J O   1 
HETATM 13884 O  O   . HOH LB 5 .   ? 68.431  -29.374 55.343 1.00 9.99   ? 311 HOH J O   1 
HETATM 13885 O  O   . HOH LB 5 .   ? 68.416  -30.047 50.813 1.00 30.84  ? 312 HOH J O   1 
HETATM 13886 O  O   . HOH LB 5 .   ? 78.156  -45.649 67.326 1.00 25.50  ? 313 HOH J O   1 
HETATM 13887 O  O   . HOH LB 5 .   ? 76.003  -44.888 46.270 1.00 11.52  ? 314 HOH J O   1 
HETATM 13888 O  O   . HOH LB 5 .   ? 52.006  -50.576 51.430 1.00 19.67  ? 315 HOH J O   1 
HETATM 13889 O  O   . HOH LB 5 .   ? 67.463  -57.779 41.560 1.00 8.93   ? 316 HOH J O   1 
HETATM 13890 O  O   . HOH LB 5 .   ? 69.592  -61.589 36.938 1.00 17.38  ? 317 HOH J O   1 
HETATM 13891 O  O   . HOH LB 5 .   ? 70.154  -33.741 56.448 1.00 16.32  ? 318 HOH J O   1 
HETATM 13892 O  O   . HOH LB 5 .   ? 70.256  -33.924 53.175 1.00 7.32   ? 319 HOH J O   1 
HETATM 13893 O  O   . HOH LB 5 .   ? 56.830  -45.422 39.352 1.00 26.06  ? 320 HOH J O   1 
HETATM 13894 O  O   . HOH LB 5 .   ? 64.177  -49.950 35.331 1.00 13.43  ? 321 HOH J O   1 
HETATM 13895 O  O   . HOH LB 5 .   ? 68.654  -51.790 65.457 1.00 11.22  ? 322 HOH J O   1 
HETATM 13896 O  O   . HOH LB 5 .   ? 47.886  -50.994 56.097 1.00 10.98  ? 323 HOH J O   1 
HETATM 13897 O  O   . HOH LB 5 .   ? 65.982  -35.306 41.641 1.00 12.14  ? 324 HOH J O   1 
HETATM 13898 O  O   . HOH MB 5 .   ? -10.824 -47.727 4.390  1.00 25.03  ? 301 HOH K O   1 
HETATM 13899 O  O   . HOH MB 5 .   ? -8.339  -45.632 29.630 1.00 28.24  ? 302 HOH K O   1 
HETATM 13900 O  O   . HOH MB 5 .   ? -9.194  -38.830 20.171 1.00 23.46  ? 303 HOH K O   1 
HETATM 13901 O  O   . HOH MB 5 .   ? -20.829 -51.008 13.121 1.00 40.66  ? 304 HOH K O   1 
HETATM 13902 O  O   . HOH MB 5 .   ? -21.156 -44.846 18.225 1.00 18.28  ? 305 HOH K O   1 
HETATM 13903 O  O   . HOH MB 5 .   ? -24.847 -42.438 26.680 1.00 17.05  ? 306 HOH K O   1 
HETATM 13904 O  O   . HOH MB 5 .   ? -18.004 -36.215 17.485 1.00 11.94  ? 307 HOH K O   1 
HETATM 13905 O  O   . HOH MB 5 .   ? -3.285  -43.615 20.788 1.00 19.76  ? 308 HOH K O   1 
HETATM 13906 O  O   . HOH MB 5 .   ? -22.939 -56.914 10.774 1.00 5.17   ? 309 HOH K O   1 
HETATM 13907 O  O   . HOH MB 5 .   ? -35.865 -40.117 15.682 1.00 39.09  ? 310 HOH K O   1 
HETATM 13908 O  O   . HOH MB 5 .   ? -13.167 -47.223 1.699  1.00 21.99  ? 311 HOH K O   1 
HETATM 13909 O  O   . HOH MB 5 .   ? -6.485  -64.768 12.456 1.00 20.65  ? 312 HOH K O   1 
HETATM 13910 O  O   . HOH MB 5 .   ? 4.080   -51.837 7.818  1.00 17.69  ? 313 HOH K O   1 
HETATM 13911 O  O   . HOH MB 5 .   ? -7.307  -40.573 19.958 1.00 14.84  ? 314 HOH K O   1 
HETATM 13912 O  O   . HOH MB 5 .   ? -11.528 -31.663 27.510 1.00 19.93  ? 315 HOH K O   1 
HETATM 13913 O  O   . HOH NB 5 .   ? 22.094  28.308  17.950 1.00 10.12  ? 301 HOH L O   1 
HETATM 13914 O  O   . HOH NB 5 .   ? 28.195  30.707  28.918 1.00 24.07  ? 302 HOH L O   1 
HETATM 13915 O  O   . HOH NB 5 .   ? 25.895  8.553   22.326 1.00 20.04  ? 303 HOH L O   1 
HETATM 13916 O  O   . HOH NB 5 .   ? 23.186  9.279   21.438 1.00 11.56  ? 304 HOH L O   1 
HETATM 13917 O  O   . HOH NB 5 .   ? 31.295  37.161  19.278 1.00 16.65  ? 305 HOH L O   1 
HETATM 13918 O  O   . HOH NB 5 .   ? 28.607  27.796  15.532 1.00 28.97  ? 306 HOH L O   1 
HETATM 13919 O  O   . HOH NB 5 .   ? 33.978  24.446  20.382 1.00 13.40  ? 307 HOH L O   1 
HETATM 13920 O  O   . HOH NB 5 .   ? 31.987  6.065   20.176 1.00 9.72   ? 308 HOH L O   1 
HETATM 13921 O  O   . HOH NB 5 .   ? 15.376  31.990  33.419 1.00 12.65  ? 309 HOH L O   1 
HETATM 13922 O  O   . HOH NB 5 .   ? 13.317  4.898   18.025 1.00 15.07  ? 310 HOH L O   1 
HETATM 13923 O  O   . HOH NB 5 .   ? 25.240  34.192  27.970 1.00 18.51  ? 311 HOH L O   1 
HETATM 13924 O  O   . HOH NB 5 .   ? 27.130  23.958  32.750 1.00 17.31  ? 312 HOH L O   1 
HETATM 13925 O  O   . HOH NB 5 .   ? 37.798  27.001  23.206 1.00 15.11  ? 313 HOH L O   1 
HETATM 13926 O  O   . HOH NB 5 .   ? 24.941  33.109  13.354 1.00 19.27  ? 314 HOH L O   1 
HETATM 13927 O  O   . HOH NB 5 .   ? 36.211  21.833  20.214 1.00 14.03  ? 315 HOH L O   1 
HETATM 13928 O  O   . HOH NB 5 .   ? 30.725  32.763  28.505 1.00 23.30  ? 316 HOH L O   1 
HETATM 13929 O  O   . HOH NB 5 .   ? 20.746  28.202  7.217  1.00 13.69  ? 317 HOH L O   1 
HETATM 13930 O  O   . HOH NB 5 .   ? 42.503  21.688  2.319  1.00 14.39  ? 318 HOH L O   1 
HETATM 13931 O  O   . HOH NB 5 .   ? 13.310  15.182  24.241 1.00 17.02  ? 319 HOH L O   1 
HETATM 13932 O  O   . HOH NB 5 .   ? 31.081  10.495  29.264 1.00 14.14  ? 320 HOH L O   1 
HETATM 13933 O  O   . HOH NB 5 .   ? 20.784  34.766  28.823 1.00 12.61  ? 321 HOH L O   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   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   VAL 5   4   4   VAL VAL A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 CYS 112 111 111 CYS CYS A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   VAL 5   4   4   VAL VAL B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 CYS 112 111 111 CYS CYS B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
C 1 1   MET 1   0   ?   ?   ?   C . n 
C 1 2   ALA 2   1   1   ALA ALA C . n 
C 1 3   THR 3   2   2   THR THR C . n 
C 1 4   LYS 4   3   3   LYS LYS C . n 
C 1 5   VAL 5   4   4   VAL VAL C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   CYS 7   6   6   CYS CYS C . n 
C 1 8   VAL 8   7   7   VAL VAL C . n 
C 1 9   LEU 9   8   8   LEU LEU C . n 
C 1 10  LYS 10  9   9   LYS LYS C . n 
C 1 11  GLY 11  10  10  GLY GLY C . n 
C 1 12  ASP 12  11  11  ASP ASP C . n 
C 1 13  GLY 13  12  12  GLY GLY C . n 
C 1 14  PRO 14  13  13  PRO PRO C . n 
C 1 15  VAL 15  14  14  VAL VAL C . n 
C 1 16  GLN 16  15  15  GLN GLN C . n 
C 1 17  GLY 17  16  16  GLY GLY C . n 
C 1 18  ILE 18  17  17  ILE ILE C . n 
C 1 19  ILE 19  18  18  ILE ILE C . n 
C 1 20  ASN 20  19  19  ASN ASN C . n 
C 1 21  PHE 21  20  20  PHE PHE C . n 
C 1 22  GLU 22  21  21  GLU GLU C . n 
C 1 23  GLN 23  22  22  GLN GLN C . n 
C 1 24  LYS 24  23  23  LYS LYS C . n 
C 1 25  GLU 25  24  24  GLU GLU C . n 
C 1 26  SER 26  25  25  SER SER C . n 
C 1 27  ASN 27  26  26  ASN ASN C . n 
C 1 28  GLY 28  27  27  GLY GLY C . n 
C 1 29  PRO 29  28  28  PRO PRO C . n 
C 1 30  VAL 30  29  29  VAL VAL C . n 
C 1 31  LYS 31  30  30  LYS LYS C . n 
C 1 32  VAL 32  31  31  VAL VAL C . n 
C 1 33  TRP 33  32  32  TRP TRP C . n 
C 1 34  GLY 34  33  33  GLY GLY C . n 
C 1 35  SER 35  34  34  SER SER C . n 
C 1 36  ILE 36  35  35  ILE ILE C . n 
C 1 37  LYS 37  36  36  LYS LYS C . n 
C 1 38  GLY 38  37  37  GLY GLY C . n 
C 1 39  LEU 39  38  38  LEU LEU C . n 
C 1 40  THR 40  39  39  THR THR C . n 
C 1 41  GLU 41  40  40  GLU GLU C . n 
C 1 42  GLY 42  41  41  GLY GLY C . n 
C 1 43  LEU 43  42  42  LEU LEU C . n 
C 1 44  HIS 44  43  43  HIS HIS C . n 
C 1 45  GLY 45  44  44  GLY GLY C . n 
C 1 46  PHE 46  45  45  PHE PHE C . n 
C 1 47  HIS 47  46  46  HIS HIS C . n 
C 1 48  VAL 48  47  47  VAL VAL C . n 
C 1 49  HIS 49  48  48  HIS HIS C . n 
C 1 50  GLU 50  49  49  GLU GLU C . n 
C 1 51  PHE 51  50  50  PHE PHE C . n 
C 1 52  GLY 52  51  51  GLY GLY C . n 
C 1 53  ASP 53  52  52  ASP ASP C . n 
C 1 54  ASN 54  53  53  ASN ASN C . n 
C 1 55  THR 55  54  54  THR THR C . n 
C 1 56  ALA 56  55  55  ALA ALA C . n 
C 1 57  GLY 57  56  56  GLY GLY C . n 
C 1 58  CYS 58  57  57  CYS CYS C . n 
C 1 59  THR 59  58  58  THR THR C . n 
C 1 60  SER 60  59  59  SER SER C . n 
C 1 61  ALA 61  60  60  ALA ALA C . n 
C 1 62  GLY 62  61  61  GLY GLY C . n 
C 1 63  PRO 63  62  62  PRO PRO C . n 
C 1 64  HIS 64  63  63  HIS HIS C . n 
C 1 65  PHE 65  64  64  PHE PHE C . n 
C 1 66  ASN 66  65  65  ASN ASN C . n 
C 1 67  PRO 67  66  66  PRO PRO C . n 
C 1 68  LEU 68  67  67  LEU LEU C . n 
C 1 69  SER 69  68  68  SER SER C . n 
C 1 70  ARG 70  69  69  ARG ARG C . n 
C 1 71  LYS 71  70  70  LYS LYS C . n 
C 1 72  HIS 72  71  71  HIS HIS C . n 
C 1 73  GLY 73  72  72  GLY GLY C . n 
C 1 74  GLY 74  73  73  GLY GLY C . n 
C 1 75  PRO 75  74  74  PRO PRO C . n 
C 1 76  LYS 76  75  75  LYS LYS C . n 
C 1 77  ASP 77  76  76  ASP ASP C . n 
C 1 78  GLU 78  77  77  GLU GLU C . n 
C 1 79  GLU 79  78  78  GLU GLU C . n 
C 1 80  ARG 80  79  79  ARG ARG C . n 
C 1 81  HIS 81  80  80  HIS HIS C . n 
C 1 82  VAL 82  81  81  VAL VAL C . n 
C 1 83  GLY 83  82  82  GLY GLY C . n 
C 1 84  ASP 84  83  83  ASP ASP C . n 
C 1 85  LEU 85  84  84  LEU LEU C . n 
C 1 86  GLY 86  85  85  GLY GLY C . n 
C 1 87  ASN 87  86  86  ASN ASN C . n 
C 1 88  VAL 88  87  87  VAL VAL C . n 
C 1 89  THR 89  88  88  THR THR C . n 
C 1 90  ALA 90  89  89  ALA ALA C . n 
C 1 91  ASP 91  90  90  ASP ASP C . n 
C 1 92  LYS 92  91  91  LYS LYS C . n 
C 1 93  ASP 93  92  92  ASP ASP C . n 
C 1 94  GLY 94  93  93  GLY GLY C . n 
C 1 95  VAL 95  94  94  VAL VAL C . n 
C 1 96  ALA 96  95  95  ALA ALA C . n 
C 1 97  ASP 97  96  96  ASP ASP C . n 
C 1 98  VAL 98  97  97  VAL VAL C . n 
C 1 99  SER 99  98  98  SER SER C . n 
C 1 100 ILE 100 99  99  ILE ILE C . n 
C 1 101 GLU 101 100 100 GLU GLU C . n 
C 1 102 ASP 102 101 101 ASP ASP C . n 
C 1 103 SER 103 102 102 SER SER C . n 
C 1 104 VAL 104 103 103 VAL VAL C . n 
C 1 105 ILE 105 104 104 ILE ILE C . n 
C 1 106 SER 106 105 105 SER SER C . n 
C 1 107 LEU 107 106 106 LEU LEU C . n 
C 1 108 SER 108 107 107 SER SER C . n 
C 1 109 GLY 109 108 108 GLY GLY C . n 
C 1 110 ASP 110 109 109 ASP ASP C . n 
C 1 111 HIS 111 110 110 HIS HIS C . n 
C 1 112 CYS 112 111 111 CYS CYS C . n 
C 1 113 ILE 113 112 112 ILE ILE C . n 
C 1 114 ILE 114 113 113 ILE ILE C . n 
C 1 115 GLY 115 114 114 GLY GLY C . n 
C 1 116 ARG 116 115 115 ARG ARG C . n 
C 1 117 THR 117 116 116 THR THR C . n 
C 1 118 LEU 118 117 117 LEU LEU C . n 
C 1 119 VAL 119 118 118 VAL VAL C . n 
C 1 120 VAL 120 119 119 VAL VAL C . n 
C 1 121 HIS 121 120 120 HIS HIS C . n 
C 1 122 GLU 122 121 121 GLU GLU C . n 
C 1 123 LYS 123 122 122 LYS LYS C . n 
C 1 124 ALA 124 123 123 ALA ALA C . n 
C 1 125 ASP 125 124 124 ASP ASP C . n 
C 1 126 ASP 126 125 125 ASP ASP C . n 
C 1 127 LEU 127 126 126 LEU LEU C . n 
C 1 128 GLY 128 127 127 GLY GLY C . n 
C 1 129 LYS 129 128 128 LYS LYS C . n 
C 1 130 GLY 130 129 129 GLY GLY C . n 
C 1 131 GLY 131 130 130 GLY GLY C . n 
C 1 132 ASN 132 131 131 ASN ASN C . n 
C 1 133 GLU 133 132 132 GLU GLU C . n 
C 1 134 GLU 134 133 133 GLU GLU C . n 
C 1 135 SER 135 134 134 SER SER C . n 
C 1 136 THR 136 135 135 THR THR C . n 
C 1 137 LYS 137 136 136 LYS LYS C . n 
C 1 138 THR 138 137 137 THR THR C . n 
C 1 139 GLY 139 138 138 GLY GLY C . n 
C 1 140 ASN 140 139 139 ASN ASN C . n 
C 1 141 ALA 141 140 140 ALA ALA C . n 
C 1 142 GLY 142 141 141 GLY GLY C . n 
C 1 143 SER 143 142 142 SER SER C . n 
C 1 144 ARG 144 143 143 ARG ARG C . n 
C 1 145 LEU 145 144 144 LEU LEU C . n 
C 1 146 ALA 146 145 145 ALA ALA C . n 
C 1 147 CYS 147 146 146 CYS CYS C . n 
C 1 148 GLY 148 147 147 GLY GLY C . n 
C 1 149 VAL 149 148 148 VAL VAL C . n 
C 1 150 ILE 150 149 149 ILE ILE C . n 
C 1 151 GLY 151 150 150 GLY GLY C . n 
C 1 152 ILE 152 151 151 ILE ILE C . n 
C 1 153 ALA 153 152 152 ALA ALA C . n 
C 1 154 GLN 154 153 153 GLN GLN C . n 
D 1 1   MET 1   0   ?   ?   ?   D . n 
D 1 2   ALA 2   1   1   ALA ALA D . n 
D 1 3   THR 3   2   2   THR THR D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   VAL 5   4   4   VAL VAL D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   CYS 7   6   6   CYS CYS D . n 
D 1 8   VAL 8   7   7   VAL VAL D . n 
D 1 9   LEU 9   8   8   LEU LEU D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  GLY 11  10  10  GLY GLY D . n 
D 1 12  ASP 12  11  11  ASP ASP D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  PRO 14  13  13  PRO PRO D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  GLN 16  15  15  GLN GLN D . n 
D 1 17  GLY 17  16  16  GLY GLY D . n 
D 1 18  ILE 18  17  17  ILE ILE D . n 
D 1 19  ILE 19  18  18  ILE ILE D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  PHE 21  20  20  PHE PHE D . n 
D 1 22  GLU 22  21  21  GLU GLU D . n 
D 1 23  GLN 23  22  22  GLN GLN D . n 
D 1 24  LYS 24  23  23  LYS LYS D . n 
D 1 25  GLU 25  24  24  GLU GLU D . n 
D 1 26  SER 26  25  25  SER SER D . n 
D 1 27  ASN 27  26  26  ASN ASN D . n 
D 1 28  GLY 28  27  27  GLY GLY D . n 
D 1 29  PRO 29  28  28  PRO PRO D . n 
D 1 30  VAL 30  29  29  VAL VAL D . n 
D 1 31  LYS 31  30  30  LYS LYS D . n 
D 1 32  VAL 32  31  31  VAL VAL D . n 
D 1 33  TRP 33  32  32  TRP TRP D . n 
D 1 34  GLY 34  33  33  GLY GLY D . n 
D 1 35  SER 35  34  34  SER SER D . n 
D 1 36  ILE 36  35  35  ILE ILE D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  LEU 39  38  38  LEU LEU D . n 
D 1 40  THR 40  39  39  THR THR D . n 
D 1 41  GLU 41  40  40  GLU GLU D . n 
D 1 42  GLY 42  41  41  GLY GLY D . n 
D 1 43  LEU 43  42  42  LEU LEU D . n 
D 1 44  HIS 44  43  43  HIS HIS D . n 
D 1 45  GLY 45  44  44  GLY GLY D . n 
D 1 46  PHE 46  45  45  PHE PHE D . n 
D 1 47  HIS 47  46  46  HIS HIS D . n 
D 1 48  VAL 48  47  47  VAL VAL D . n 
D 1 49  HIS 49  48  48  HIS HIS D . n 
D 1 50  GLU 50  49  49  GLU GLU D . n 
D 1 51  PHE 51  50  50  PHE PHE D . n 
D 1 52  GLY 52  51  51  GLY GLY D . n 
D 1 53  ASP 53  52  52  ASP ASP D . n 
D 1 54  ASN 54  53  53  ASN ASN D . n 
D 1 55  THR 55  54  54  THR THR D . n 
D 1 56  ALA 56  55  55  ALA ALA D . n 
D 1 57  GLY 57  56  56  GLY GLY D . n 
D 1 58  CYS 58  57  57  CYS CYS D . n 
D 1 59  THR 59  58  58  THR THR D . n 
D 1 60  SER 60  59  59  SER SER D . n 
D 1 61  ALA 61  60  60  ALA ALA D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  HIS 64  63  63  HIS HIS D . n 
D 1 65  PHE 65  64  64  PHE PHE D . n 
D 1 66  ASN 66  65  65  ASN ASN D . n 
D 1 67  PRO 67  66  66  PRO PRO D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  SER 69  68  68  SER SER D . n 
D 1 70  ARG 70  69  69  ARG ARG D . n 
D 1 71  LYS 71  70  70  LYS LYS D . n 
D 1 72  HIS 72  71  71  HIS HIS D . n 
D 1 73  GLY 73  72  72  GLY GLY D . n 
D 1 74  GLY 74  73  73  GLY GLY D . n 
D 1 75  PRO 75  74  74  PRO PRO D . n 
D 1 76  LYS 76  75  75  LYS LYS D . n 
D 1 77  ASP 77  76  76  ASP ASP D . n 
D 1 78  GLU 78  77  77  GLU GLU D . n 
D 1 79  GLU 79  78  78  GLU GLU D . n 
D 1 80  ARG 80  79  79  ARG ARG D . n 
D 1 81  HIS 81  80  80  HIS HIS D . n 
D 1 82  VAL 82  81  81  VAL VAL D . n 
D 1 83  GLY 83  82  82  GLY GLY D . n 
D 1 84  ASP 84  83  83  ASP ASP D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  GLY 86  85  85  GLY GLY D . n 
D 1 87  ASN 87  86  86  ASN ASN D . n 
D 1 88  VAL 88  87  87  VAL VAL D . n 
D 1 89  THR 89  88  88  THR THR D . n 
D 1 90  ALA 90  89  89  ALA ALA D . n 
D 1 91  ASP 91  90  90  ASP ASP D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  ASP 93  92  92  ASP ASP D . n 
D 1 94  GLY 94  93  93  GLY GLY D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  ALA 96  95  95  ALA ALA D . n 
D 1 97  ASP 97  96  96  ASP ASP D . n 
D 1 98  VAL 98  97  97  VAL VAL D . n 
D 1 99  SER 99  98  98  SER SER D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 GLU 101 100 100 GLU GLU D . n 
D 1 102 ASP 102 101 101 ASP ASP D . n 
D 1 103 SER 103 102 102 SER SER D . n 
D 1 104 VAL 104 103 103 VAL VAL D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 SER 106 105 105 SER SER D . n 
D 1 107 LEU 107 106 106 LEU LEU D . n 
D 1 108 SER 108 107 107 SER SER D . n 
D 1 109 GLY 109 108 108 GLY GLY D . n 
D 1 110 ASP 110 109 109 ASP ASP D . n 
D 1 111 HIS 111 110 110 HIS HIS D . n 
D 1 112 CYS 112 111 111 CYS CYS D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 ILE 114 113 113 ILE ILE D . n 
D 1 115 GLY 115 114 114 GLY GLY D . n 
D 1 116 ARG 116 115 115 ARG ARG D . n 
D 1 117 THR 117 116 116 THR THR D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 VAL 119 118 118 VAL VAL D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 HIS 121 120 120 HIS HIS D . n 
D 1 122 GLU 122 121 121 GLU GLU D . n 
D 1 123 LYS 123 122 122 LYS LYS D . n 
D 1 124 ALA 124 123 123 ALA ALA D . n 
D 1 125 ASP 125 124 124 ASP ASP D . n 
D 1 126 ASP 126 125 125 ASP ASP D . n 
D 1 127 LEU 127 126 126 LEU LEU D . n 
D 1 128 GLY 128 127 127 GLY GLY D . n 
D 1 129 LYS 129 128 128 LYS LYS D . n 
D 1 130 GLY 130 129 129 GLY GLY D . n 
D 1 131 GLY 131 130 130 GLY GLY D . n 
D 1 132 ASN 132 131 131 ASN ASN D . n 
D 1 133 GLU 133 132 132 GLU GLU D . n 
D 1 134 GLU 134 133 133 GLU GLU D . n 
D 1 135 SER 135 134 134 SER SER D . n 
D 1 136 THR 136 135 135 THR THR D . n 
D 1 137 LYS 137 136 136 LYS LYS D . n 
D 1 138 THR 138 137 137 THR THR D . n 
D 1 139 GLY 139 138 138 GLY GLY D . n 
D 1 140 ASN 140 139 139 ASN ASN D . n 
D 1 141 ALA 141 140 140 ALA ALA D . n 
D 1 142 GLY 142 141 141 GLY GLY D . n 
D 1 143 SER 143 142 142 SER SER D . n 
D 1 144 ARG 144 143 143 ARG ARG D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 ALA 146 145 145 ALA ALA D . n 
D 1 147 CYS 147 146 146 CYS CYS D . n 
D 1 148 GLY 148 147 147 GLY GLY D . n 
D 1 149 VAL 149 148 148 VAL VAL D . n 
D 1 150 ILE 150 149 149 ILE ILE D . n 
D 1 151 GLY 151 150 150 GLY GLY D . n 
D 1 152 ILE 152 151 151 ILE ILE D . n 
D 1 153 ALA 153 152 152 ALA ALA D . n 
D 1 154 GLN 154 153 153 GLN GLN D . n 
E 1 1   MET 1   0   ?   ?   ?   E . n 
E 1 2   ALA 2   1   1   ALA ALA E . n 
E 1 3   THR 3   2   2   THR THR E . n 
E 1 4   LYS 4   3   3   LYS LYS E . n 
E 1 5   VAL 5   4   4   VAL VAL E . n 
E 1 6   VAL 6   5   5   VAL VAL E . n 
E 1 7   CYS 7   6   6   CYS CYS E . n 
E 1 8   VAL 8   7   7   VAL VAL E . n 
E 1 9   LEU 9   8   8   LEU LEU E . n 
E 1 10  LYS 10  9   9   LYS LYS E . n 
E 1 11  GLY 11  10  10  GLY GLY E . n 
E 1 12  ASP 12  11  11  ASP ASP E . n 
E 1 13  GLY 13  12  12  GLY GLY E . n 
E 1 14  PRO 14  13  13  PRO PRO E . n 
E 1 15  VAL 15  14  14  VAL VAL E . n 
E 1 16  GLN 16  15  15  GLN GLN E . n 
E 1 17  GLY 17  16  16  GLY GLY E . n 
E 1 18  ILE 18  17  17  ILE ILE E . n 
E 1 19  ILE 19  18  18  ILE ILE E . n 
E 1 20  ASN 20  19  19  ASN ASN E . n 
E 1 21  PHE 21  20  20  PHE PHE E . n 
E 1 22  GLU 22  21  21  GLU GLU E . n 
E 1 23  GLN 23  22  22  GLN GLN E . n 
E 1 24  LYS 24  23  23  LYS LYS E . n 
E 1 25  GLU 25  24  24  GLU GLU E . n 
E 1 26  SER 26  25  25  SER SER E . n 
E 1 27  ASN 27  26  26  ASN ASN E . n 
E 1 28  GLY 28  27  27  GLY GLY E . n 
E 1 29  PRO 29  28  28  PRO PRO E . n 
E 1 30  VAL 30  29  29  VAL VAL E . n 
E 1 31  LYS 31  30  30  LYS LYS E . n 
E 1 32  VAL 32  31  31  VAL VAL E . n 
E 1 33  TRP 33  32  32  TRP TRP E . n 
E 1 34  GLY 34  33  33  GLY GLY E . n 
E 1 35  SER 35  34  34  SER SER E . n 
E 1 36  ILE 36  35  35  ILE ILE E . n 
E 1 37  LYS 37  36  36  LYS LYS E . n 
E 1 38  GLY 38  37  37  GLY GLY E . n 
E 1 39  LEU 39  38  38  LEU LEU E . n 
E 1 40  THR 40  39  39  THR THR E . n 
E 1 41  GLU 41  40  40  GLU GLU E . n 
E 1 42  GLY 42  41  41  GLY GLY E . n 
E 1 43  LEU 43  42  42  LEU LEU E . n 
E 1 44  HIS 44  43  43  HIS HIS E . n 
E 1 45  GLY 45  44  44  GLY GLY E . n 
E 1 46  PHE 46  45  45  PHE PHE E . n 
E 1 47  HIS 47  46  46  HIS HIS E . n 
E 1 48  VAL 48  47  47  VAL VAL E . n 
E 1 49  HIS 49  48  48  HIS HIS E . n 
E 1 50  GLU 50  49  49  GLU GLU E . n 
E 1 51  PHE 51  50  50  PHE PHE E . n 
E 1 52  GLY 52  51  51  GLY GLY E . n 
E 1 53  ASP 53  52  52  ASP ASP E . n 
E 1 54  ASN 54  53  53  ASN ASN E . n 
E 1 55  THR 55  54  54  THR THR E . n 
E 1 56  ALA 56  55  55  ALA ALA E . n 
E 1 57  GLY 57  56  56  GLY GLY E . n 
E 1 58  CYS 58  57  57  CYS CYS E . n 
E 1 59  THR 59  58  58  THR THR E . n 
E 1 60  SER 60  59  59  SER SER E . n 
E 1 61  ALA 61  60  60  ALA ALA E . n 
E 1 62  GLY 62  61  61  GLY GLY E . n 
E 1 63  PRO 63  62  62  PRO PRO E . n 
E 1 64  HIS 64  63  63  HIS HIS E . n 
E 1 65  PHE 65  64  64  PHE PHE E . n 
E 1 66  ASN 66  65  65  ASN ASN E . n 
E 1 67  PRO 67  66  66  PRO PRO E . n 
E 1 68  LEU 68  67  67  LEU LEU E . n 
E 1 69  SER 69  68  68  SER SER E . n 
E 1 70  ARG 70  69  69  ARG ARG E . n 
E 1 71  LYS 71  70  70  LYS LYS E . n 
E 1 72  HIS 72  71  71  HIS HIS E . n 
E 1 73  GLY 73  72  72  GLY GLY E . n 
E 1 74  GLY 74  73  73  GLY GLY E . n 
E 1 75  PRO 75  74  74  PRO PRO E . n 
E 1 76  LYS 76  75  75  LYS LYS E . n 
E 1 77  ASP 77  76  76  ASP ASP E . n 
E 1 78  GLU 78  77  77  GLU GLU E . n 
E 1 79  GLU 79  78  78  GLU GLU E . n 
E 1 80  ARG 80  79  79  ARG ARG E . n 
E 1 81  HIS 81  80  80  HIS HIS E . n 
E 1 82  VAL 82  81  81  VAL VAL E . n 
E 1 83  GLY 83  82  82  GLY GLY E . n 
E 1 84  ASP 84  83  83  ASP ASP E . n 
E 1 85  LEU 85  84  84  LEU LEU E . n 
E 1 86  GLY 86  85  85  GLY GLY E . n 
E 1 87  ASN 87  86  86  ASN ASN E . n 
E 1 88  VAL 88  87  87  VAL VAL E . n 
E 1 89  THR 89  88  88  THR THR E . n 
E 1 90  ALA 90  89  89  ALA ALA E . n 
E 1 91  ASP 91  90  90  ASP ASP E . n 
E 1 92  LYS 92  91  91  LYS LYS E . n 
E 1 93  ASP 93  92  92  ASP ASP E . n 
E 1 94  GLY 94  93  93  GLY GLY E . n 
E 1 95  VAL 95  94  94  VAL VAL E . n 
E 1 96  ALA 96  95  95  ALA ALA E . n 
E 1 97  ASP 97  96  96  ASP ASP E . n 
E 1 98  VAL 98  97  97  VAL VAL E . n 
E 1 99  SER 99  98  98  SER SER E . n 
E 1 100 ILE 100 99  99  ILE ILE E . n 
E 1 101 GLU 101 100 100 GLU GLU E . n 
E 1 102 ASP 102 101 101 ASP ASP E . n 
E 1 103 SER 103 102 102 SER SER E . n 
E 1 104 VAL 104 103 103 VAL VAL E . n 
E 1 105 ILE 105 104 104 ILE ILE E . n 
E 1 106 SER 106 105 105 SER SER E . n 
E 1 107 LEU 107 106 106 LEU LEU E . n 
E 1 108 SER 108 107 107 SER SER E . n 
E 1 109 GLY 109 108 108 GLY GLY E . n 
E 1 110 ASP 110 109 109 ASP ASP E . n 
E 1 111 HIS 111 110 110 HIS HIS E . n 
E 1 112 CYS 112 111 111 CYS CYS E . n 
E 1 113 ILE 113 112 112 ILE ILE E . n 
E 1 114 ILE 114 113 113 ILE ILE E . n 
E 1 115 GLY 115 114 114 GLY GLY E . n 
E 1 116 ARG 116 115 115 ARG ARG E . n 
E 1 117 THR 117 116 116 THR THR E . n 
E 1 118 LEU 118 117 117 LEU LEU E . n 
E 1 119 VAL 119 118 118 VAL VAL E . n 
E 1 120 VAL 120 119 119 VAL VAL E . n 
E 1 121 HIS 121 120 120 HIS HIS E . n 
E 1 122 GLU 122 121 121 GLU GLU E . n 
E 1 123 LYS 123 122 122 LYS LYS E . n 
E 1 124 ALA 124 123 123 ALA ALA E . n 
E 1 125 ASP 125 124 124 ASP ASP E . n 
E 1 126 ASP 126 125 125 ASP ASP E . n 
E 1 127 LEU 127 126 126 LEU LEU E . n 
E 1 128 GLY 128 127 127 GLY GLY E . n 
E 1 129 LYS 129 128 128 LYS LYS E . n 
E 1 130 GLY 130 129 129 GLY GLY E . n 
E 1 131 GLY 131 130 130 GLY GLY E . n 
E 1 132 ASN 132 131 131 ASN ASN E . n 
E 1 133 GLU 133 132 132 GLU GLU E . n 
E 1 134 GLU 134 133 133 GLU GLU E . n 
E 1 135 SER 135 134 134 SER SER E . n 
E 1 136 THR 136 135 135 THR THR E . n 
E 1 137 LYS 137 136 136 LYS LYS E . n 
E 1 138 THR 138 137 137 THR THR E . n 
E 1 139 GLY 139 138 138 GLY GLY E . n 
E 1 140 ASN 140 139 139 ASN ASN E . n 
E 1 141 ALA 141 140 140 ALA ALA E . n 
E 1 142 GLY 142 141 141 GLY GLY E . n 
E 1 143 SER 143 142 142 SER SER E . n 
E 1 144 ARG 144 143 143 ARG ARG E . n 
E 1 145 LEU 145 144 144 LEU LEU E . n 
E 1 146 ALA 146 145 145 ALA ALA E . n 
E 1 147 CYS 147 146 146 CYS CYS E . n 
E 1 148 GLY 148 147 147 GLY GLY E . n 
E 1 149 VAL 149 148 148 VAL VAL E . n 
E 1 150 ILE 150 149 149 ILE ILE E . n 
E 1 151 GLY 151 150 150 GLY GLY E . n 
E 1 152 ILE 152 151 151 ILE ILE E . n 
E 1 153 ALA 153 152 152 ALA ALA E . n 
E 1 154 GLN 154 153 153 GLN GLN E . n 
F 1 1   MET 1   0   ?   ?   ?   F . n 
F 1 2   ALA 2   1   1   ALA ALA F . n 
F 1 3   THR 3   2   2   THR THR F . n 
F 1 4   LYS 4   3   3   LYS LYS F . n 
F 1 5   VAL 5   4   4   VAL VAL F . n 
F 1 6   VAL 6   5   5   VAL VAL F . n 
F 1 7   CYS 7   6   6   CYS CYS F . n 
F 1 8   VAL 8   7   7   VAL VAL F . n 
F 1 9   LEU 9   8   8   LEU LEU F . n 
F 1 10  LYS 10  9   9   LYS LYS F . n 
F 1 11  GLY 11  10  10  GLY GLY F . n 
F 1 12  ASP 12  11  11  ASP ASP F . n 
F 1 13  GLY 13  12  12  GLY GLY F . n 
F 1 14  PRO 14  13  13  PRO PRO F . n 
F 1 15  VAL 15  14  14  VAL VAL F . n 
F 1 16  GLN 16  15  15  GLN GLN F . n 
F 1 17  GLY 17  16  16  GLY GLY F . n 
F 1 18  ILE 18  17  17  ILE ILE F . n 
F 1 19  ILE 19  18  18  ILE ILE F . n 
F 1 20  ASN 20  19  19  ASN ASN F . n 
F 1 21  PHE 21  20  20  PHE PHE F . n 
F 1 22  GLU 22  21  21  GLU GLU F . n 
F 1 23  GLN 23  22  22  GLN GLN F . n 
F 1 24  LYS 24  23  23  LYS LYS F . n 
F 1 25  GLU 25  24  24  GLU GLU F . n 
F 1 26  SER 26  25  25  SER SER F . n 
F 1 27  ASN 27  26  26  ASN ASN F . n 
F 1 28  GLY 28  27  27  GLY GLY F . n 
F 1 29  PRO 29  28  28  PRO PRO F . n 
F 1 30  VAL 30  29  29  VAL VAL F . n 
F 1 31  LYS 31  30  30  LYS LYS F . n 
F 1 32  VAL 32  31  31  VAL VAL F . n 
F 1 33  TRP 33  32  32  TRP TRP F . n 
F 1 34  GLY 34  33  33  GLY GLY F . n 
F 1 35  SER 35  34  34  SER SER F . n 
F 1 36  ILE 36  35  35  ILE ILE F . n 
F 1 37  LYS 37  36  36  LYS LYS F . n 
F 1 38  GLY 38  37  37  GLY GLY F . n 
F 1 39  LEU 39  38  38  LEU LEU F . n 
F 1 40  THR 40  39  39  THR THR F . n 
F 1 41  GLU 41  40  40  GLU GLU F . n 
F 1 42  GLY 42  41  41  GLY GLY F . n 
F 1 43  LEU 43  42  42  LEU LEU F . n 
F 1 44  HIS 44  43  43  HIS HIS F . n 
F 1 45  GLY 45  44  44  GLY GLY F . n 
F 1 46  PHE 46  45  45  PHE PHE F . n 
F 1 47  HIS 47  46  46  HIS HIS F . n 
F 1 48  VAL 48  47  47  VAL VAL F . n 
F 1 49  HIS 49  48  48  HIS HIS F . n 
F 1 50  GLU 50  49  49  GLU GLU F . n 
F 1 51  PHE 51  50  50  PHE PHE F . n 
F 1 52  GLY 52  51  51  GLY GLY F . n 
F 1 53  ASP 53  52  52  ASP ASP F . n 
F 1 54  ASN 54  53  53  ASN ASN F . n 
F 1 55  THR 55  54  54  THR THR F . n 
F 1 56  ALA 56  55  55  ALA ALA F . n 
F 1 57  GLY 57  56  56  GLY GLY F . n 
F 1 58  CYS 58  57  57  CYS CYS F . n 
F 1 59  THR 59  58  58  THR THR F . n 
F 1 60  SER 60  59  59  SER SER F . n 
F 1 61  ALA 61  60  60  ALA ALA F . n 
F 1 62  GLY 62  61  61  GLY GLY F . n 
F 1 63  PRO 63  62  62  PRO PRO F . n 
F 1 64  HIS 64  63  63  HIS HIS F . n 
F 1 65  PHE 65  64  64  PHE PHE F . n 
F 1 66  ASN 66  65  65  ASN ASN F . n 
F 1 67  PRO 67  66  66  PRO PRO F . n 
F 1 68  LEU 68  67  67  LEU LEU F . n 
F 1 69  SER 69  68  68  SER SER F . n 
F 1 70  ARG 70  69  69  ARG ARG F . n 
F 1 71  LYS 71  70  70  LYS LYS F . n 
F 1 72  HIS 72  71  71  HIS HIS F . n 
F 1 73  GLY 73  72  72  GLY GLY F . n 
F 1 74  GLY 74  73  73  GLY GLY F . n 
F 1 75  PRO 75  74  74  PRO PRO F . n 
F 1 76  LYS 76  75  75  LYS LYS F . n 
F 1 77  ASP 77  76  76  ASP ASP F . n 
F 1 78  GLU 78  77  77  GLU GLU F . n 
F 1 79  GLU 79  78  78  GLU GLU F . n 
F 1 80  ARG 80  79  79  ARG ARG F . n 
F 1 81  HIS 81  80  80  HIS HIS F . n 
F 1 82  VAL 82  81  81  VAL VAL F . n 
F 1 83  GLY 83  82  82  GLY GLY F . n 
F 1 84  ASP 84  83  83  ASP ASP F . n 
F 1 85  LEU 85  84  84  LEU LEU F . n 
F 1 86  GLY 86  85  85  GLY GLY F . n 
F 1 87  ASN 87  86  86  ASN ASN F . n 
F 1 88  VAL 88  87  87  VAL VAL F . n 
F 1 89  THR 89  88  88  THR THR F . n 
F 1 90  ALA 90  89  89  ALA ALA F . n 
F 1 91  ASP 91  90  90  ASP ASP F . n 
F 1 92  LYS 92  91  91  LYS LYS F . n 
F 1 93  ASP 93  92  92  ASP ASP F . n 
F 1 94  GLY 94  93  93  GLY GLY F . n 
F 1 95  VAL 95  94  94  VAL VAL F . n 
F 1 96  ALA 96  95  95  ALA ALA F . n 
F 1 97  ASP 97  96  96  ASP ASP F . n 
F 1 98  VAL 98  97  97  VAL VAL F . n 
F 1 99  SER 99  98  98  SER SER F . n 
F 1 100 ILE 100 99  99  ILE ILE F . n 
F 1 101 GLU 101 100 100 GLU GLU F . n 
F 1 102 ASP 102 101 101 ASP ASP F . n 
F 1 103 SER 103 102 102 SER SER F . n 
F 1 104 VAL 104 103 103 VAL VAL F . n 
F 1 105 ILE 105 104 104 ILE ILE F . n 
F 1 106 SER 106 105 105 SER SER F . n 
F 1 107 LEU 107 106 106 LEU LEU F . n 
F 1 108 SER 108 107 107 SER SER F . n 
F 1 109 GLY 109 108 108 GLY GLY F . n 
F 1 110 ASP 110 109 109 ASP ASP F . n 
F 1 111 HIS 111 110 110 HIS HIS F . n 
F 1 112 CYS 112 111 111 CYS CYS F . n 
F 1 113 ILE 113 112 112 ILE ILE F . n 
F 1 114 ILE 114 113 113 ILE ILE F . n 
F 1 115 GLY 115 114 114 GLY GLY F . n 
F 1 116 ARG 116 115 115 ARG ARG F . n 
F 1 117 THR 117 116 116 THR THR F . n 
F 1 118 LEU 118 117 117 LEU LEU F . n 
F 1 119 VAL 119 118 118 VAL VAL F . n 
F 1 120 VAL 120 119 119 VAL VAL F . n 
F 1 121 HIS 121 120 120 HIS HIS F . n 
F 1 122 GLU 122 121 121 GLU GLU F . n 
F 1 123 LYS 123 122 122 LYS LYS F . n 
F 1 124 ALA 124 123 123 ALA ALA F . n 
F 1 125 ASP 125 124 124 ASP ASP F . n 
F 1 126 ASP 126 125 125 ASP ASP F . n 
F 1 127 LEU 127 126 126 LEU LEU F . n 
F 1 128 GLY 128 127 127 GLY GLY F . n 
F 1 129 LYS 129 128 128 LYS LYS F . n 
F 1 130 GLY 130 129 129 GLY GLY F . n 
F 1 131 GLY 131 130 130 GLY GLY F . n 
F 1 132 ASN 132 131 131 ASN ASN F . n 
F 1 133 GLU 133 132 132 GLU GLU F . n 
F 1 134 GLU 134 133 133 GLU GLU F . n 
F 1 135 SER 135 134 134 SER SER F . n 
F 1 136 THR 136 135 135 THR THR F . n 
F 1 137 LYS 137 136 136 LYS LYS F . n 
F 1 138 THR 138 137 137 THR THR F . n 
F 1 139 GLY 139 138 138 GLY GLY F . n 
F 1 140 ASN 140 139 139 ASN ASN F . n 
F 1 141 ALA 141 140 140 ALA ALA F . n 
F 1 142 GLY 142 141 141 GLY GLY F . n 
F 1 143 SER 143 142 142 SER SER F . n 
F 1 144 ARG 144 143 143 ARG ARG F . n 
F 1 145 LEU 145 144 144 LEU LEU F . n 
F 1 146 ALA 146 145 145 ALA ALA F . n 
F 1 147 CYS 147 146 146 CYS CYS F . n 
F 1 148 GLY 148 147 147 GLY GLY F . n 
F 1 149 VAL 149 148 148 VAL VAL F . n 
F 1 150 ILE 150 149 149 ILE ILE F . n 
F 1 151 GLY 151 150 150 GLY GLY F . n 
F 1 152 ILE 152 151 151 ILE ILE F . n 
F 1 153 ALA 153 152 152 ALA ALA F . n 
F 1 154 GLN 154 153 153 GLN GLN F . n 
G 1 1   MET 1   0   ?   ?   ?   G . n 
G 1 2   ALA 2   1   1   ALA ALA G . n 
G 1 3   THR 3   2   2   THR THR G . n 
G 1 4   LYS 4   3   3   LYS LYS G . n 
G 1 5   VAL 5   4   4   VAL VAL G . n 
G 1 6   VAL 6   5   5   VAL VAL G . n 
G 1 7   CYS 7   6   6   CYS CYS G . n 
G 1 8   VAL 8   7   7   VAL VAL G . n 
G 1 9   LEU 9   8   8   LEU LEU G . n 
G 1 10  LYS 10  9   9   LYS LYS G . n 
G 1 11  GLY 11  10  10  GLY GLY G . n 
G 1 12  ASP 12  11  11  ASP ASP G . n 
G 1 13  GLY 13  12  12  GLY GLY G . n 
G 1 14  PRO 14  13  13  PRO PRO G . n 
G 1 15  VAL 15  14  14  VAL VAL G . n 
G 1 16  GLN 16  15  15  GLN GLN G . n 
G 1 17  GLY 17  16  16  GLY GLY G . n 
G 1 18  ILE 18  17  17  ILE ILE G . n 
G 1 19  ILE 19  18  18  ILE ILE G . n 
G 1 20  ASN 20  19  19  ASN ASN G . n 
G 1 21  PHE 21  20  20  PHE PHE G . n 
G 1 22  GLU 22  21  21  GLU GLU G . n 
G 1 23  GLN 23  22  22  GLN GLN G . n 
G 1 24  LYS 24  23  23  LYS LYS G . n 
G 1 25  GLU 25  24  24  GLU GLU G . n 
G 1 26  SER 26  25  25  SER SER G . n 
G 1 27  ASN 27  26  26  ASN ASN G . n 
G 1 28  GLY 28  27  27  GLY GLY G . n 
G 1 29  PRO 29  28  28  PRO PRO G . n 
G 1 30  VAL 30  29  29  VAL VAL G . n 
G 1 31  LYS 31  30  30  LYS LYS G . n 
G 1 32  VAL 32  31  31  VAL VAL G . n 
G 1 33  TRP 33  32  32  TRP TRP G . n 
G 1 34  GLY 34  33  33  GLY GLY G . n 
G 1 35  SER 35  34  34  SER SER G . n 
G 1 36  ILE 36  35  35  ILE ILE G . n 
G 1 37  LYS 37  36  36  LYS LYS G . n 
G 1 38  GLY 38  37  37  GLY GLY G . n 
G 1 39  LEU 39  38  38  LEU LEU G . n 
G 1 40  THR 40  39  39  THR THR G . n 
G 1 41  GLU 41  40  40  GLU GLU G . n 
G 1 42  GLY 42  41  41  GLY GLY G . n 
G 1 43  LEU 43  42  42  LEU LEU G . n 
G 1 44  HIS 44  43  43  HIS HIS G . n 
G 1 45  GLY 45  44  44  GLY GLY G . n 
G 1 46  PHE 46  45  45  PHE PHE G . n 
G 1 47  HIS 47  46  46  HIS HIS G . n 
G 1 48  VAL 48  47  47  VAL VAL G . n 
G 1 49  HIS 49  48  48  HIS HIS G . n 
G 1 50  GLU 50  49  49  GLU GLU G . n 
G 1 51  PHE 51  50  50  PHE PHE G . n 
G 1 52  GLY 52  51  51  GLY GLY G . n 
G 1 53  ASP 53  52  52  ASP ASP G . n 
G 1 54  ASN 54  53  53  ASN ASN G . n 
G 1 55  THR 55  54  54  THR THR G . n 
G 1 56  ALA 56  55  55  ALA ALA G . n 
G 1 57  GLY 57  56  56  GLY GLY G . n 
G 1 58  CYS 58  57  57  CYS CYS G . n 
G 1 59  THR 59  58  58  THR THR G . n 
G 1 60  SER 60  59  59  SER SER G . n 
G 1 61  ALA 61  60  60  ALA ALA G . n 
G 1 62  GLY 62  61  61  GLY GLY G . n 
G 1 63  PRO 63  62  62  PRO PRO G . n 
G 1 64  HIS 64  63  63  HIS HIS G . n 
G 1 65  PHE 65  64  64  PHE PHE G . n 
G 1 66  ASN 66  65  65  ASN ASN G . n 
G 1 67  PRO 67  66  66  PRO PRO G . n 
G 1 68  LEU 68  67  67  LEU LEU G . n 
G 1 69  SER 69  68  68  SER SER G . n 
G 1 70  ARG 70  69  69  ARG ARG G . n 
G 1 71  LYS 71  70  70  LYS LYS G . n 
G 1 72  HIS 72  71  71  HIS HIS G . n 
G 1 73  GLY 73  72  72  GLY GLY G . n 
G 1 74  GLY 74  73  73  GLY GLY G . n 
G 1 75  PRO 75  74  74  PRO PRO G . n 
G 1 76  LYS 76  75  75  LYS LYS G . n 
G 1 77  ASP 77  76  76  ASP ASP G . n 
G 1 78  GLU 78  77  77  GLU GLU G . n 
G 1 79  GLU 79  78  78  GLU GLU G . n 
G 1 80  ARG 80  79  79  ARG ARG G . n 
G 1 81  HIS 81  80  80  HIS HIS G . n 
G 1 82  VAL 82  81  81  VAL VAL G . n 
G 1 83  GLY 83  82  82  GLY GLY G . n 
G 1 84  ASP 84  83  83  ASP ASP G . n 
G 1 85  LEU 85  84  84  LEU LEU G . n 
G 1 86  GLY 86  85  85  GLY GLY G . n 
G 1 87  ASN 87  86  86  ASN ASN G . n 
G 1 88  VAL 88  87  87  VAL VAL G . n 
G 1 89  THR 89  88  88  THR THR G . n 
G 1 90  ALA 90  89  89  ALA ALA G . n 
G 1 91  ASP 91  90  90  ASP ASP G . n 
G 1 92  LYS 92  91  91  LYS LYS G . n 
G 1 93  ASP 93  92  92  ASP ASP G . n 
G 1 94  GLY 94  93  93  GLY GLY G . n 
G 1 95  VAL 95  94  94  VAL VAL G . n 
G 1 96  ALA 96  95  95  ALA ALA G . n 
G 1 97  ASP 97  96  96  ASP ASP G . n 
G 1 98  VAL 98  97  97  VAL VAL G . n 
G 1 99  SER 99  98  98  SER SER G . n 
G 1 100 ILE 100 99  99  ILE ILE G . n 
G 1 101 GLU 101 100 100 GLU GLU G . n 
G 1 102 ASP 102 101 101 ASP ASP G . n 
G 1 103 SER 103 102 102 SER SER G . n 
G 1 104 VAL 104 103 103 VAL VAL G . n 
G 1 105 ILE 105 104 104 ILE ILE G . n 
G 1 106 SER 106 105 105 SER SER G . n 
G 1 107 LEU 107 106 106 LEU LEU G . n 
G 1 108 SER 108 107 107 SER SER G . n 
G 1 109 GLY 109 108 108 GLY GLY G . n 
G 1 110 ASP 110 109 109 ASP ASP G . n 
G 1 111 HIS 111 110 110 HIS HIS G . n 
G 1 112 CYS 112 111 111 CYS CYS G . n 
G 1 113 ILE 113 112 112 ILE ILE G . n 
G 1 114 ILE 114 113 113 ILE ILE G . n 
G 1 115 GLY 115 114 114 GLY GLY G . n 
G 1 116 ARG 116 115 115 ARG ARG G . n 
G 1 117 THR 117 116 116 THR THR G . n 
G 1 118 LEU 118 117 117 LEU LEU G . n 
G 1 119 VAL 119 118 118 VAL VAL G . n 
G 1 120 VAL 120 119 119 VAL VAL G . n 
G 1 121 HIS 121 120 120 HIS HIS G . n 
G 1 122 GLU 122 121 121 GLU GLU G . n 
G 1 123 LYS 123 122 122 LYS LYS G . n 
G 1 124 ALA 124 123 123 ALA ALA G . n 
G 1 125 ASP 125 124 124 ASP ASP G . n 
G 1 126 ASP 126 125 125 ASP ASP G . n 
G 1 127 LEU 127 126 126 LEU LEU G . n 
G 1 128 GLY 128 127 127 GLY GLY G . n 
G 1 129 LYS 129 128 128 LYS LYS G . n 
G 1 130 GLY 130 129 129 GLY GLY G . n 
G 1 131 GLY 131 130 130 GLY GLY G . n 
G 1 132 ASN 132 131 131 ASN ASN G . n 
G 1 133 GLU 133 132 132 GLU GLU G . n 
G 1 134 GLU 134 133 133 GLU GLU G . n 
G 1 135 SER 135 134 134 SER SER G . n 
G 1 136 THR 136 135 135 THR THR G . n 
G 1 137 LYS 137 136 136 LYS LYS G . n 
G 1 138 THR 138 137 137 THR THR G . n 
G 1 139 GLY 139 138 138 GLY GLY G . n 
G 1 140 ASN 140 139 139 ASN ASN G . n 
G 1 141 ALA 141 140 140 ALA ALA G . n 
G 1 142 GLY 142 141 141 GLY GLY G . n 
G 1 143 SER 143 142 142 SER SER G . n 
G 1 144 ARG 144 143 143 ARG ARG G . n 
G 1 145 LEU 145 144 144 LEU LEU G . n 
G 1 146 ALA 146 145 145 ALA ALA G . n 
G 1 147 CYS 147 146 146 CYS CYS G . n 
G 1 148 GLY 148 147 147 GLY GLY G . n 
G 1 149 VAL 149 148 148 VAL VAL G . n 
G 1 150 ILE 150 149 149 ILE ILE G . n 
G 1 151 GLY 151 150 150 GLY GLY G . n 
G 1 152 ILE 152 151 151 ILE ILE G . n 
G 1 153 ALA 153 152 152 ALA ALA G . n 
G 1 154 GLN 154 153 153 GLN GLN G . n 
H 1 1   MET 1   0   ?   ?   ?   H . n 
H 1 2   ALA 2   1   1   ALA ALA H . n 
H 1 3   THR 3   2   2   THR THR H . n 
H 1 4   LYS 4   3   3   LYS LYS H . n 
H 1 5   VAL 5   4   4   VAL VAL H . n 
H 1 6   VAL 6   5   5   VAL VAL H . n 
H 1 7   CYS 7   6   6   CYS CYS H . n 
H 1 8   VAL 8   7   7   VAL VAL H . n 
H 1 9   LEU 9   8   8   LEU LEU H . n 
H 1 10  LYS 10  9   9   LYS LYS H . n 
H 1 11  GLY 11  10  10  GLY GLY H . n 
H 1 12  ASP 12  11  11  ASP ASP H . n 
H 1 13  GLY 13  12  12  GLY GLY H . n 
H 1 14  PRO 14  13  13  PRO PRO H . n 
H 1 15  VAL 15  14  14  VAL VAL H . n 
H 1 16  GLN 16  15  15  GLN GLN H . n 
H 1 17  GLY 17  16  16  GLY GLY H . n 
H 1 18  ILE 18  17  17  ILE ILE H . n 
H 1 19  ILE 19  18  18  ILE ILE H . n 
H 1 20  ASN 20  19  19  ASN ASN H . n 
H 1 21  PHE 21  20  20  PHE PHE H . n 
H 1 22  GLU 22  21  21  GLU GLU H . n 
H 1 23  GLN 23  22  22  GLN GLN H . n 
H 1 24  LYS 24  23  23  LYS LYS H . n 
H 1 25  GLU 25  24  24  GLU GLU H . n 
H 1 26  SER 26  25  25  SER SER H . n 
H 1 27  ASN 27  26  26  ASN ASN H . n 
H 1 28  GLY 28  27  27  GLY GLY H . n 
H 1 29  PRO 29  28  28  PRO PRO H . n 
H 1 30  VAL 30  29  29  VAL VAL H . n 
H 1 31  LYS 31  30  30  LYS LYS H . n 
H 1 32  VAL 32  31  31  VAL VAL H . n 
H 1 33  TRP 33  32  32  TRP TRP H . n 
H 1 34  GLY 34  33  33  GLY GLY H . n 
H 1 35  SER 35  34  34  SER SER H . n 
H 1 36  ILE 36  35  35  ILE ILE H . n 
H 1 37  LYS 37  36  36  LYS LYS H . n 
H 1 38  GLY 38  37  37  GLY GLY H . n 
H 1 39  LEU 39  38  38  LEU LEU H . n 
H 1 40  THR 40  39  39  THR THR H . n 
H 1 41  GLU 41  40  40  GLU GLU H . n 
H 1 42  GLY 42  41  41  GLY GLY H . n 
H 1 43  LEU 43  42  42  LEU LEU H . n 
H 1 44  HIS 44  43  43  HIS HIS H . n 
H 1 45  GLY 45  44  44  GLY GLY H . n 
H 1 46  PHE 46  45  45  PHE PHE H . n 
H 1 47  HIS 47  46  46  HIS HIS H . n 
H 1 48  VAL 48  47  47  VAL VAL H . n 
H 1 49  HIS 49  48  48  HIS HIS H . n 
H 1 50  GLU 50  49  49  GLU GLU H . n 
H 1 51  PHE 51  50  50  PHE PHE H . n 
H 1 52  GLY 52  51  51  GLY GLY H . n 
H 1 53  ASP 53  52  52  ASP ASP H . n 
H 1 54  ASN 54  53  53  ASN ASN H . n 
H 1 55  THR 55  54  54  THR THR H . n 
H 1 56  ALA 56  55  55  ALA ALA H . n 
H 1 57  GLY 57  56  56  GLY GLY H . n 
H 1 58  CYS 58  57  57  CYS CYS H . n 
H 1 59  THR 59  58  58  THR THR H . n 
H 1 60  SER 60  59  59  SER SER H . n 
H 1 61  ALA 61  60  60  ALA ALA H . n 
H 1 62  GLY 62  61  61  GLY GLY H . n 
H 1 63  PRO 63  62  62  PRO PRO H . n 
H 1 64  HIS 64  63  63  HIS HIS H . n 
H 1 65  PHE 65  64  64  PHE PHE H . n 
H 1 66  ASN 66  65  65  ASN ASN H . n 
H 1 67  PRO 67  66  66  PRO PRO H . n 
H 1 68  LEU 68  67  67  LEU LEU H . n 
H 1 69  SER 69  68  68  SER SER H . n 
H 1 70  ARG 70  69  69  ARG ARG H . n 
H 1 71  LYS 71  70  70  LYS LYS H . n 
H 1 72  HIS 72  71  71  HIS HIS H . n 
H 1 73  GLY 73  72  72  GLY GLY H . n 
H 1 74  GLY 74  73  73  GLY GLY H . n 
H 1 75  PRO 75  74  74  PRO PRO H . n 
H 1 76  LYS 76  75  75  LYS LYS H . n 
H 1 77  ASP 77  76  76  ASP ASP H . n 
H 1 78  GLU 78  77  77  GLU GLU H . n 
H 1 79  GLU 79  78  78  GLU GLU H . n 
H 1 80  ARG 80  79  79  ARG ARG H . n 
H 1 81  HIS 81  80  80  HIS HIS H . n 
H 1 82  VAL 82  81  81  VAL VAL H . n 
H 1 83  GLY 83  82  82  GLY GLY H . n 
H 1 84  ASP 84  83  83  ASP ASP H . n 
H 1 85  LEU 85  84  84  LEU LEU H . n 
H 1 86  GLY 86  85  85  GLY GLY H . n 
H 1 87  ASN 87  86  86  ASN ASN H . n 
H 1 88  VAL 88  87  87  VAL VAL H . n 
H 1 89  THR 89  88  88  THR THR H . n 
H 1 90  ALA 90  89  89  ALA ALA H . n 
H 1 91  ASP 91  90  90  ASP ASP H . n 
H 1 92  LYS 92  91  91  LYS LYS H . n 
H 1 93  ASP 93  92  92  ASP ASP H . n 
H 1 94  GLY 94  93  93  GLY GLY H . n 
H 1 95  VAL 95  94  94  VAL VAL H . n 
H 1 96  ALA 96  95  95  ALA ALA H . n 
H 1 97  ASP 97  96  96  ASP ASP H . n 
H 1 98  VAL 98  97  97  VAL VAL H . n 
H 1 99  SER 99  98  98  SER SER H . n 
H 1 100 ILE 100 99  99  ILE ILE H . n 
H 1 101 GLU 101 100 100 GLU GLU H . n 
H 1 102 ASP 102 101 101 ASP ASP H . n 
H 1 103 SER 103 102 102 SER SER H . n 
H 1 104 VAL 104 103 103 VAL VAL H . n 
H 1 105 ILE 105 104 104 ILE ILE H . n 
H 1 106 SER 106 105 105 SER SER H . n 
H 1 107 LEU 107 106 106 LEU LEU H . n 
H 1 108 SER 108 107 107 SER SER H . n 
H 1 109 GLY 109 108 108 GLY GLY H . n 
H 1 110 ASP 110 109 109 ASP ASP H . n 
H 1 111 HIS 111 110 110 HIS HIS H . n 
H 1 112 CYS 112 111 111 CYS CYS H . n 
H 1 113 ILE 113 112 112 ILE ILE H . n 
H 1 114 ILE 114 113 113 ILE ILE H . n 
H 1 115 GLY 115 114 114 GLY GLY H . n 
H 1 116 ARG 116 115 115 ARG ARG H . n 
H 1 117 THR 117 116 116 THR THR H . n 
H 1 118 LEU 118 117 117 LEU LEU H . n 
H 1 119 VAL 119 118 118 VAL VAL H . n 
H 1 120 VAL 120 119 119 VAL VAL H . n 
H 1 121 HIS 121 120 120 HIS HIS H . n 
H 1 122 GLU 122 121 121 GLU GLU H . n 
H 1 123 LYS 123 122 122 LYS LYS H . n 
H 1 124 ALA 124 123 123 ALA ALA H . n 
H 1 125 ASP 125 124 124 ASP ASP H . n 
H 1 126 ASP 126 125 125 ASP ASP H . n 
H 1 127 LEU 127 126 126 LEU LEU H . n 
H 1 128 GLY 128 127 127 GLY GLY H . n 
H 1 129 LYS 129 128 128 LYS LYS H . n 
H 1 130 GLY 130 129 129 GLY GLY H . n 
H 1 131 GLY 131 130 130 GLY GLY H . n 
H 1 132 ASN 132 131 131 ASN ASN H . n 
H 1 133 GLU 133 132 132 GLU GLU H . n 
H 1 134 GLU 134 133 133 GLU GLU H . n 
H 1 135 SER 135 134 134 SER SER H . n 
H 1 136 THR 136 135 135 THR THR H . n 
H 1 137 LYS 137 136 136 LYS LYS H . n 
H 1 138 THR 138 137 137 THR THR H . n 
H 1 139 GLY 139 138 138 GLY GLY H . n 
H 1 140 ASN 140 139 139 ASN ASN H . n 
H 1 141 ALA 141 140 140 ALA ALA H . n 
H 1 142 GLY 142 141 141 GLY GLY H . n 
H 1 143 SER 143 142 142 SER SER H . n 
H 1 144 ARG 144 143 143 ARG ARG H . n 
H 1 145 LEU 145 144 144 LEU LEU H . n 
H 1 146 ALA 146 145 145 ALA ALA H . n 
H 1 147 CYS 147 146 146 CYS CYS H . n 
H 1 148 GLY 148 147 147 GLY GLY H . n 
H 1 149 VAL 149 148 148 VAL VAL H . n 
H 1 150 ILE 150 149 149 ILE ILE H . n 
H 1 151 GLY 151 150 150 GLY GLY H . n 
H 1 152 ILE 152 151 151 ILE ILE H . n 
H 1 153 ALA 153 152 152 ALA ALA H . n 
H 1 154 GLN 154 153 153 GLN GLN H . n 
I 1 1   MET 1   0   ?   ?   ?   I . n 
I 1 2   ALA 2   1   1   ALA ALA I . n 
I 1 3   THR 3   2   2   THR THR I . n 
I 1 4   LYS 4   3   3   LYS LYS I . n 
I 1 5   VAL 5   4   4   VAL VAL I . n 
I 1 6   VAL 6   5   5   VAL VAL I . n 
I 1 7   CYS 7   6   6   CYS CYS I . n 
I 1 8   VAL 8   7   7   VAL VAL I . n 
I 1 9   LEU 9   8   8   LEU LEU I . n 
I 1 10  LYS 10  9   9   LYS LYS I . n 
I 1 11  GLY 11  10  10  GLY GLY I . n 
I 1 12  ASP 12  11  11  ASP ASP I . n 
I 1 13  GLY 13  12  12  GLY GLY I . n 
I 1 14  PRO 14  13  13  PRO PRO I . n 
I 1 15  VAL 15  14  14  VAL VAL I . n 
I 1 16  GLN 16  15  15  GLN GLN I . n 
I 1 17  GLY 17  16  16  GLY GLY I . n 
I 1 18  ILE 18  17  17  ILE ILE I . n 
I 1 19  ILE 19  18  18  ILE ILE I . n 
I 1 20  ASN 20  19  19  ASN ASN I . n 
I 1 21  PHE 21  20  20  PHE PHE I . n 
I 1 22  GLU 22  21  21  GLU GLU I . n 
I 1 23  GLN 23  22  22  GLN GLN I . n 
I 1 24  LYS 24  23  23  LYS LYS I . n 
I 1 25  GLU 25  24  24  GLU GLU I . n 
I 1 26  SER 26  25  25  SER SER I . n 
I 1 27  ASN 27  26  26  ASN ASN I . n 
I 1 28  GLY 28  27  27  GLY GLY I . n 
I 1 29  PRO 29  28  28  PRO PRO I . n 
I 1 30  VAL 30  29  29  VAL VAL I . n 
I 1 31  LYS 31  30  30  LYS LYS I . n 
I 1 32  VAL 32  31  31  VAL VAL I . n 
I 1 33  TRP 33  32  32  TRP TRP I . n 
I 1 34  GLY 34  33  33  GLY GLY I . n 
I 1 35  SER 35  34  34  SER SER I . n 
I 1 36  ILE 36  35  35  ILE ILE I . n 
I 1 37  LYS 37  36  36  LYS LYS I . n 
I 1 38  GLY 38  37  37  GLY GLY I . n 
I 1 39  LEU 39  38  38  LEU LEU I . n 
I 1 40  THR 40  39  39  THR THR I . n 
I 1 41  GLU 41  40  40  GLU GLU I . n 
I 1 42  GLY 42  41  41  GLY GLY I . n 
I 1 43  LEU 43  42  42  LEU LEU I . n 
I 1 44  HIS 44  43  43  HIS HIS I . n 
I 1 45  GLY 45  44  44  GLY GLY I . n 
I 1 46  PHE 46  45  45  PHE PHE I . n 
I 1 47  HIS 47  46  46  HIS HIS I . n 
I 1 48  VAL 48  47  47  VAL VAL I . n 
I 1 49  HIS 49  48  48  HIS HIS I . n 
I 1 50  GLU 50  49  49  GLU GLU I . n 
I 1 51  PHE 51  50  50  PHE PHE I . n 
I 1 52  GLY 52  51  51  GLY GLY I . n 
I 1 53  ASP 53  52  52  ASP ASP I . n 
I 1 54  ASN 54  53  53  ASN ASN I . n 
I 1 55  THR 55  54  54  THR THR I . n 
I 1 56  ALA 56  55  55  ALA ALA I . n 
I 1 57  GLY 57  56  56  GLY GLY I . n 
I 1 58  CYS 58  57  57  CYS CYS I . n 
I 1 59  THR 59  58  58  THR THR I . n 
I 1 60  SER 60  59  59  SER SER I . n 
I 1 61  ALA 61  60  60  ALA ALA I . n 
I 1 62  GLY 62  61  61  GLY GLY I . n 
I 1 63  PRO 63  62  62  PRO PRO I . n 
I 1 64  HIS 64  63  63  HIS HIS I . n 
I 1 65  PHE 65  64  64  PHE PHE I . n 
I 1 66  ASN 66  65  65  ASN ASN I . n 
I 1 67  PRO 67  66  66  PRO PRO I . n 
I 1 68  LEU 68  67  67  LEU LEU I . n 
I 1 69  SER 69  68  68  SER SER I . n 
I 1 70  ARG 70  69  69  ARG ARG I . n 
I 1 71  LYS 71  70  70  LYS LYS I . n 
I 1 72  HIS 72  71  71  HIS HIS I . n 
I 1 73  GLY 73  72  72  GLY GLY I . n 
I 1 74  GLY 74  73  73  GLY GLY I . n 
I 1 75  PRO 75  74  74  PRO PRO I . n 
I 1 76  LYS 76  75  75  LYS LYS I . n 
I 1 77  ASP 77  76  76  ASP ASP I . n 
I 1 78  GLU 78  77  77  GLU GLU I . n 
I 1 79  GLU 79  78  78  GLU GLU I . n 
I 1 80  ARG 80  79  79  ARG ARG I . n 
I 1 81  HIS 81  80  80  HIS HIS I . n 
I 1 82  VAL 82  81  81  VAL VAL I . n 
I 1 83  GLY 83  82  82  GLY GLY I . n 
I 1 84  ASP 84  83  83  ASP ASP I . n 
I 1 85  LEU 85  84  84  LEU LEU I . n 
I 1 86  GLY 86  85  85  GLY GLY I . n 
I 1 87  ASN 87  86  86  ASN ASN I . n 
I 1 88  VAL 88  87  87  VAL VAL I . n 
I 1 89  THR 89  88  88  THR THR I . n 
I 1 90  ALA 90  89  89  ALA ALA I . n 
I 1 91  ASP 91  90  90  ASP ASP I . n 
I 1 92  LYS 92  91  91  LYS LYS I . n 
I 1 93  ASP 93  92  92  ASP ASP I . n 
I 1 94  GLY 94  93  93  GLY GLY I . n 
I 1 95  VAL 95  94  94  VAL VAL I . n 
I 1 96  ALA 96  95  95  ALA ALA I . n 
I 1 97  ASP 97  96  96  ASP ASP I . n 
I 1 98  VAL 98  97  97  VAL VAL I . n 
I 1 99  SER 99  98  98  SER SER I . n 
I 1 100 ILE 100 99  99  ILE ILE I . n 
I 1 101 GLU 101 100 100 GLU GLU I . n 
I 1 102 ASP 102 101 101 ASP ASP I . n 
I 1 103 SER 103 102 102 SER SER I . n 
I 1 104 VAL 104 103 103 VAL VAL I . n 
I 1 105 ILE 105 104 104 ILE ILE I . n 
I 1 106 SER 106 105 105 SER SER I . n 
I 1 107 LEU 107 106 106 LEU LEU I . n 
I 1 108 SER 108 107 107 SER SER I . n 
I 1 109 GLY 109 108 108 GLY GLY I . n 
I 1 110 ASP 110 109 109 ASP ASP I . n 
I 1 111 HIS 111 110 110 HIS HIS I . n 
I 1 112 CYS 112 111 111 CYS CYS I . n 
I 1 113 ILE 113 112 112 ILE ILE I . n 
I 1 114 ILE 114 113 113 ILE ILE I . n 
I 1 115 GLY 115 114 114 GLY GLY I . n 
I 1 116 ARG 116 115 115 ARG ARG I . n 
I 1 117 THR 117 116 116 THR THR I . n 
I 1 118 LEU 118 117 117 LEU LEU I . n 
I 1 119 VAL 119 118 118 VAL VAL I . n 
I 1 120 VAL 120 119 119 VAL VAL I . n 
I 1 121 HIS 121 120 120 HIS HIS I . n 
I 1 122 GLU 122 121 121 GLU GLU I . n 
I 1 123 LYS 123 122 122 LYS LYS I . n 
I 1 124 ALA 124 123 123 ALA ALA I . n 
I 1 125 ASP 125 124 124 ASP ASP I . n 
I 1 126 ASP 126 125 125 ASP ASP I . n 
I 1 127 LEU 127 126 126 LEU LEU I . n 
I 1 128 GLY 128 127 127 GLY GLY I . n 
I 1 129 LYS 129 128 128 LYS LYS I . n 
I 1 130 GLY 130 129 129 GLY GLY I . n 
I 1 131 GLY 131 130 130 GLY GLY I . n 
I 1 132 ASN 132 131 131 ASN ASN I . n 
I 1 133 GLU 133 132 132 GLU GLU I . n 
I 1 134 GLU 134 133 133 GLU GLU I . n 
I 1 135 SER 135 134 134 SER SER I . n 
I 1 136 THR 136 135 135 THR THR I . n 
I 1 137 LYS 137 136 136 LYS LYS I . n 
I 1 138 THR 138 137 137 THR THR I . n 
I 1 139 GLY 139 138 138 GLY GLY I . n 
I 1 140 ASN 140 139 139 ASN ASN I . n 
I 1 141 ALA 141 140 140 ALA ALA I . n 
I 1 142 GLY 142 141 141 GLY GLY I . n 
I 1 143 SER 143 142 142 SER SER I . n 
I 1 144 ARG 144 143 143 ARG ARG I . n 
I 1 145 LEU 145 144 144 LEU LEU I . n 
I 1 146 ALA 146 145 145 ALA ALA I . n 
I 1 147 CYS 147 146 146 CYS CYS I . n 
I 1 148 GLY 148 147 147 GLY GLY I . n 
I 1 149 VAL 149 148 148 VAL VAL I . n 
I 1 150 ILE 150 149 149 ILE ILE I . n 
I 1 151 GLY 151 150 150 GLY GLY I . n 
I 1 152 ILE 152 151 151 ILE ILE I . n 
I 1 153 ALA 153 152 152 ALA ALA I . n 
I 1 154 GLN 154 153 153 GLN GLN I . n 
J 1 1   MET 1   0   ?   ?   ?   J . n 
J 1 2   ALA 2   1   1   ALA ALA J . n 
J 1 3   THR 3   2   2   THR THR J . n 
J 1 4   LYS 4   3   3   LYS LYS J . n 
J 1 5   VAL 5   4   4   VAL VAL J . n 
J 1 6   VAL 6   5   5   VAL VAL J . n 
J 1 7   CYS 7   6   6   CYS CYS J . n 
J 1 8   VAL 8   7   7   VAL VAL J . n 
J 1 9   LEU 9   8   8   LEU LEU J . n 
J 1 10  LYS 10  9   9   LYS LYS J . n 
J 1 11  GLY 11  10  10  GLY GLY J . n 
J 1 12  ASP 12  11  11  ASP ASP J . n 
J 1 13  GLY 13  12  12  GLY GLY J . n 
J 1 14  PRO 14  13  13  PRO PRO J . n 
J 1 15  VAL 15  14  14  VAL VAL J . n 
J 1 16  GLN 16  15  15  GLN GLN J . n 
J 1 17  GLY 17  16  16  GLY GLY J . n 
J 1 18  ILE 18  17  17  ILE ILE J . n 
J 1 19  ILE 19  18  18  ILE ILE J . n 
J 1 20  ASN 20  19  19  ASN ASN J . n 
J 1 21  PHE 21  20  20  PHE PHE J . n 
J 1 22  GLU 22  21  21  GLU GLU J . n 
J 1 23  GLN 23  22  22  GLN GLN J . n 
J 1 24  LYS 24  23  23  LYS LYS J . n 
J 1 25  GLU 25  24  24  GLU GLU J . n 
J 1 26  SER 26  25  25  SER SER J . n 
J 1 27  ASN 27  26  26  ASN ASN J . n 
J 1 28  GLY 28  27  27  GLY GLY J . n 
J 1 29  PRO 29  28  28  PRO PRO J . n 
J 1 30  VAL 30  29  29  VAL VAL J . n 
J 1 31  LYS 31  30  30  LYS LYS J . n 
J 1 32  VAL 32  31  31  VAL VAL J . n 
J 1 33  TRP 33  32  32  TRP TRP J . n 
J 1 34  GLY 34  33  33  GLY GLY J . n 
J 1 35  SER 35  34  34  SER SER J . n 
J 1 36  ILE 36  35  35  ILE ILE J . n 
J 1 37  LYS 37  36  36  LYS LYS J . n 
J 1 38  GLY 38  37  37  GLY GLY J . n 
J 1 39  LEU 39  38  38  LEU LEU J . n 
J 1 40  THR 40  39  39  THR THR J . n 
J 1 41  GLU 41  40  40  GLU GLU J . n 
J 1 42  GLY 42  41  41  GLY GLY J . n 
J 1 43  LEU 43  42  42  LEU LEU J . n 
J 1 44  HIS 44  43  43  HIS HIS J . n 
J 1 45  GLY 45  44  44  GLY GLY J . n 
J 1 46  PHE 46  45  45  PHE PHE J . n 
J 1 47  HIS 47  46  46  HIS HIS J . n 
J 1 48  VAL 48  47  47  VAL VAL J . n 
J 1 49  HIS 49  48  48  HIS HIS J . n 
J 1 50  GLU 50  49  49  GLU GLU J . n 
J 1 51  PHE 51  50  50  PHE PHE J . n 
J 1 52  GLY 52  51  51  GLY GLY J . n 
J 1 53  ASP 53  52  52  ASP ASP J . n 
J 1 54  ASN 54  53  53  ASN ASN J . n 
J 1 55  THR 55  54  54  THR THR J . n 
J 1 56  ALA 56  55  55  ALA ALA J . n 
J 1 57  GLY 57  56  56  GLY GLY J . n 
J 1 58  CYS 58  57  57  CYS CYS J . n 
J 1 59  THR 59  58  58  THR THR J . n 
J 1 60  SER 60  59  59  SER SER J . n 
J 1 61  ALA 61  60  60  ALA ALA J . n 
J 1 62  GLY 62  61  61  GLY GLY J . n 
J 1 63  PRO 63  62  62  PRO PRO J . n 
J 1 64  HIS 64  63  63  HIS HIS J . n 
J 1 65  PHE 65  64  64  PHE PHE J . n 
J 1 66  ASN 66  65  65  ASN ASN J . n 
J 1 67  PRO 67  66  66  PRO PRO J . n 
J 1 68  LEU 68  67  67  LEU LEU J . n 
J 1 69  SER 69  68  68  SER SER J . n 
J 1 70  ARG 70  69  69  ARG ARG J . n 
J 1 71  LYS 71  70  70  LYS LYS J . n 
J 1 72  HIS 72  71  71  HIS HIS J . n 
J 1 73  GLY 73  72  72  GLY GLY J . n 
J 1 74  GLY 74  73  73  GLY GLY J . n 
J 1 75  PRO 75  74  74  PRO PRO J . n 
J 1 76  LYS 76  75  75  LYS LYS J . n 
J 1 77  ASP 77  76  76  ASP ASP J . n 
J 1 78  GLU 78  77  77  GLU GLU J . n 
J 1 79  GLU 79  78  78  GLU GLU J . n 
J 1 80  ARG 80  79  79  ARG ARG J . n 
J 1 81  HIS 81  80  80  HIS HIS J . n 
J 1 82  VAL 82  81  81  VAL VAL J . n 
J 1 83  GLY 83  82  82  GLY GLY J . n 
J 1 84  ASP 84  83  83  ASP ASP J . n 
J 1 85  LEU 85  84  84  LEU LEU J . n 
J 1 86  GLY 86  85  85  GLY GLY J . n 
J 1 87  ASN 87  86  86  ASN ASN J . n 
J 1 88  VAL 88  87  87  VAL VAL J . n 
J 1 89  THR 89  88  88  THR THR J . n 
J 1 90  ALA 90  89  89  ALA ALA J . n 
J 1 91  ASP 91  90  90  ASP ASP J . n 
J 1 92  LYS 92  91  91  LYS LYS J . n 
J 1 93  ASP 93  92  92  ASP ASP J . n 
J 1 94  GLY 94  93  93  GLY GLY J . n 
J 1 95  VAL 95  94  94  VAL VAL J . n 
J 1 96  ALA 96  95  95  ALA ALA J . n 
J 1 97  ASP 97  96  96  ASP ASP J . n 
J 1 98  VAL 98  97  97  VAL VAL J . n 
J 1 99  SER 99  98  98  SER SER J . n 
J 1 100 ILE 100 99  99  ILE ILE J . n 
J 1 101 GLU 101 100 100 GLU GLU J . n 
J 1 102 ASP 102 101 101 ASP ASP J . n 
J 1 103 SER 103 102 102 SER SER J . n 
J 1 104 VAL 104 103 103 VAL VAL J . n 
J 1 105 ILE 105 104 104 ILE ILE J . n 
J 1 106 SER 106 105 105 SER SER J . n 
J 1 107 LEU 107 106 106 LEU LEU J . n 
J 1 108 SER 108 107 107 SER SER J . n 
J 1 109 GLY 109 108 108 GLY GLY J . n 
J 1 110 ASP 110 109 109 ASP ASP J . n 
J 1 111 HIS 111 110 110 HIS HIS J . n 
J 1 112 CYS 112 111 111 CYS CYS J . n 
J 1 113 ILE 113 112 112 ILE ILE J . n 
J 1 114 ILE 114 113 113 ILE ILE J . n 
J 1 115 GLY 115 114 114 GLY GLY J . n 
J 1 116 ARG 116 115 115 ARG ARG J . n 
J 1 117 THR 117 116 116 THR THR J . n 
J 1 118 LEU 118 117 117 LEU LEU J . n 
J 1 119 VAL 119 118 118 VAL VAL J . n 
J 1 120 VAL 120 119 119 VAL VAL J . n 
J 1 121 HIS 121 120 120 HIS HIS J . n 
J 1 122 GLU 122 121 121 GLU GLU J . n 
J 1 123 LYS 123 122 122 LYS LYS J . n 
J 1 124 ALA 124 123 123 ALA ALA J . n 
J 1 125 ASP 125 124 124 ASP ASP J . n 
J 1 126 ASP 126 125 125 ASP ASP J . n 
J 1 127 LEU 127 126 126 LEU LEU J . n 
J 1 128 GLY 128 127 127 GLY GLY J . n 
J 1 129 LYS 129 128 128 LYS LYS J . n 
J 1 130 GLY 130 129 129 GLY GLY J . n 
J 1 131 GLY 131 130 130 GLY GLY J . n 
J 1 132 ASN 132 131 131 ASN ASN J . n 
J 1 133 GLU 133 132 132 GLU GLU J . n 
J 1 134 GLU 134 133 133 GLU GLU J . n 
J 1 135 SER 135 134 134 SER SER J . n 
J 1 136 THR 136 135 135 THR THR J . n 
J 1 137 LYS 137 136 136 LYS LYS J . n 
J 1 138 THR 138 137 137 THR THR J . n 
J 1 139 GLY 139 138 138 GLY GLY J . n 
J 1 140 ASN 140 139 139 ASN ASN J . n 
J 1 141 ALA 141 140 140 ALA ALA J . n 
J 1 142 GLY 142 141 141 GLY GLY J . n 
J 1 143 SER 143 142 142 SER SER J . n 
J 1 144 ARG 144 143 143 ARG ARG J . n 
J 1 145 LEU 145 144 144 LEU LEU J . n 
J 1 146 ALA 146 145 145 ALA ALA J . n 
J 1 147 CYS 147 146 146 CYS CYS J . n 
J 1 148 GLY 148 147 147 GLY GLY J . n 
J 1 149 VAL 149 148 148 VAL VAL J . n 
J 1 150 ILE 150 149 149 ILE ILE J . n 
J 1 151 GLY 151 150 150 GLY GLY J . n 
J 1 152 ILE 152 151 151 ILE ILE J . n 
J 1 153 ALA 153 152 152 ALA ALA J . n 
J 1 154 GLN 154 153 153 GLN GLN J . n 
K 1 1   MET 1   0   ?   ?   ?   K . n 
K 1 2   ALA 2   1   1   ALA ALA K . n 
K 1 3   THR 3   2   2   THR THR K . n 
K 1 4   LYS 4   3   3   LYS LYS K . n 
K 1 5   VAL 5   4   4   VAL VAL K . n 
K 1 6   VAL 6   5   5   VAL VAL K . n 
K 1 7   CYS 7   6   6   CYS CYS K . n 
K 1 8   VAL 8   7   7   VAL VAL K . n 
K 1 9   LEU 9   8   8   LEU LEU K . n 
K 1 10  LYS 10  9   9   LYS LYS K . n 
K 1 11  GLY 11  10  10  GLY GLY K . n 
K 1 12  ASP 12  11  11  ASP ASP K . n 
K 1 13  GLY 13  12  12  GLY GLY K . n 
K 1 14  PRO 14  13  13  PRO PRO K . n 
K 1 15  VAL 15  14  14  VAL VAL K . n 
K 1 16  GLN 16  15  15  GLN GLN K . n 
K 1 17  GLY 17  16  16  GLY GLY K . n 
K 1 18  ILE 18  17  17  ILE ILE K . n 
K 1 19  ILE 19  18  18  ILE ILE K . n 
K 1 20  ASN 20  19  19  ASN ASN K . n 
K 1 21  PHE 21  20  20  PHE PHE K . n 
K 1 22  GLU 22  21  21  GLU GLU K . n 
K 1 23  GLN 23  22  22  GLN GLN K . n 
K 1 24  LYS 24  23  23  LYS LYS K . n 
K 1 25  GLU 25  24  24  GLU GLU K . n 
K 1 26  SER 26  25  25  SER SER K . n 
K 1 27  ASN 27  26  26  ASN ASN K . n 
K 1 28  GLY 28  27  27  GLY GLY K . n 
K 1 29  PRO 29  28  28  PRO PRO K . n 
K 1 30  VAL 30  29  29  VAL VAL K . n 
K 1 31  LYS 31  30  30  LYS LYS K . n 
K 1 32  VAL 32  31  31  VAL VAL K . n 
K 1 33  TRP 33  32  32  TRP TRP K . n 
K 1 34  GLY 34  33  33  GLY GLY K . n 
K 1 35  SER 35  34  34  SER SER K . n 
K 1 36  ILE 36  35  35  ILE ILE K . n 
K 1 37  LYS 37  36  36  LYS LYS K . n 
K 1 38  GLY 38  37  37  GLY GLY K . n 
K 1 39  LEU 39  38  38  LEU LEU K . n 
K 1 40  THR 40  39  39  THR THR K . n 
K 1 41  GLU 41  40  40  GLU GLU K . n 
K 1 42  GLY 42  41  41  GLY GLY K . n 
K 1 43  LEU 43  42  42  LEU LEU K . n 
K 1 44  HIS 44  43  43  HIS HIS K . n 
K 1 45  GLY 45  44  44  GLY GLY K . n 
K 1 46  PHE 46  45  45  PHE PHE K . n 
K 1 47  HIS 47  46  46  HIS HIS K . n 
K 1 48  VAL 48  47  47  VAL VAL K . n 
K 1 49  HIS 49  48  48  HIS HIS K . n 
K 1 50  GLU 50  49  49  GLU GLU K . n 
K 1 51  PHE 51  50  50  PHE PHE K . n 
K 1 52  GLY 52  51  51  GLY GLY K . n 
K 1 53  ASP 53  52  52  ASP ASP K . n 
K 1 54  ASN 54  53  53  ASN ASN K . n 
K 1 55  THR 55  54  54  THR THR K . n 
K 1 56  ALA 56  55  55  ALA ALA K . n 
K 1 57  GLY 57  56  56  GLY GLY K . n 
K 1 58  CYS 58  57  57  CYS CYS K . n 
K 1 59  THR 59  58  58  THR THR K . n 
K 1 60  SER 60  59  59  SER SER K . n 
K 1 61  ALA 61  60  60  ALA ALA K . n 
K 1 62  GLY 62  61  61  GLY GLY K . n 
K 1 63  PRO 63  62  62  PRO PRO K . n 
K 1 64  HIS 64  63  63  HIS HIS K . n 
K 1 65  PHE 65  64  64  PHE PHE K . n 
K 1 66  ASN 66  65  65  ASN ASN K . n 
K 1 67  PRO 67  66  66  PRO PRO K . n 
K 1 68  LEU 68  67  67  LEU LEU K . n 
K 1 69  SER 69  68  68  SER SER K . n 
K 1 70  ARG 70  69  69  ARG ARG K . n 
K 1 71  LYS 71  70  70  LYS LYS K . n 
K 1 72  HIS 72  71  71  HIS HIS K . n 
K 1 73  GLY 73  72  72  GLY GLY K . n 
K 1 74  GLY 74  73  73  GLY GLY K . n 
K 1 75  PRO 75  74  74  PRO PRO K . n 
K 1 76  LYS 76  75  75  LYS LYS K . n 
K 1 77  ASP 77  76  76  ASP ASP K . n 
K 1 78  GLU 78  77  77  GLU GLU K . n 
K 1 79  GLU 79  78  78  GLU GLU K . n 
K 1 80  ARG 80  79  79  ARG ARG K . n 
K 1 81  HIS 81  80  80  HIS HIS K . n 
K 1 82  VAL 82  81  81  VAL VAL K . n 
K 1 83  GLY 83  82  82  GLY GLY K . n 
K 1 84  ASP 84  83  83  ASP ASP K . n 
K 1 85  LEU 85  84  84  LEU LEU K . n 
K 1 86  GLY 86  85  85  GLY GLY K . n 
K 1 87  ASN 87  86  86  ASN ASN K . n 
K 1 88  VAL 88  87  87  VAL VAL K . n 
K 1 89  THR 89  88  88  THR THR K . n 
K 1 90  ALA 90  89  89  ALA ALA K . n 
K 1 91  ASP 91  90  90  ASP ASP K . n 
K 1 92  LYS 92  91  91  LYS LYS K . n 
K 1 93  ASP 93  92  92  ASP ASP K . n 
K 1 94  GLY 94  93  93  GLY GLY K . n 
K 1 95  VAL 95  94  94  VAL VAL K . n 
K 1 96  ALA 96  95  95  ALA ALA K . n 
K 1 97  ASP 97  96  96  ASP ASP K . n 
K 1 98  VAL 98  97  97  VAL VAL K . n 
K 1 99  SER 99  98  98  SER SER K . n 
K 1 100 ILE 100 99  99  ILE ILE K . n 
K 1 101 GLU 101 100 100 GLU GLU K . n 
K 1 102 ASP 102 101 101 ASP ASP K . n 
K 1 103 SER 103 102 102 SER SER K . n 
K 1 104 VAL 104 103 103 VAL VAL K . n 
K 1 105 ILE 105 104 104 ILE ILE K . n 
K 1 106 SER 106 105 105 SER SER K . n 
K 1 107 LEU 107 106 106 LEU LEU K . n 
K 1 108 SER 108 107 107 SER SER K . n 
K 1 109 GLY 109 108 108 GLY GLY K . n 
K 1 110 ASP 110 109 109 ASP ASP K . n 
K 1 111 HIS 111 110 110 HIS HIS K . n 
K 1 112 CYS 112 111 111 CYS CYS K . n 
K 1 113 ILE 113 112 112 ILE ILE K . n 
K 1 114 ILE 114 113 113 ILE ILE K . n 
K 1 115 GLY 115 114 114 GLY GLY K . n 
K 1 116 ARG 116 115 115 ARG ARG K . n 
K 1 117 THR 117 116 116 THR THR K . n 
K 1 118 LEU 118 117 117 LEU LEU K . n 
K 1 119 VAL 119 118 118 VAL VAL K . n 
K 1 120 VAL 120 119 119 VAL VAL K . n 
K 1 121 HIS 121 120 120 HIS HIS K . n 
K 1 122 GLU 122 121 121 GLU GLU K . n 
K 1 123 LYS 123 122 122 LYS LYS K . n 
K 1 124 ALA 124 123 123 ALA ALA K . n 
K 1 125 ASP 125 124 124 ASP ASP K . n 
K 1 126 ASP 126 125 125 ASP ASP K . n 
K 1 127 LEU 127 126 126 LEU LEU K . n 
K 1 128 GLY 128 127 127 GLY GLY K . n 
K 1 129 LYS 129 128 128 LYS LYS K . n 
K 1 130 GLY 130 129 129 GLY GLY K . n 
K 1 131 GLY 131 130 130 GLY GLY K . n 
K 1 132 ASN 132 131 131 ASN ASN K . n 
K 1 133 GLU 133 132 132 GLU GLU K . n 
K 1 134 GLU 134 133 133 GLU GLU K . n 
K 1 135 SER 135 134 134 SER SER K . n 
K 1 136 THR 136 135 135 THR THR K . n 
K 1 137 LYS 137 136 136 LYS LYS K . n 
K 1 138 THR 138 137 137 THR THR K . n 
K 1 139 GLY 139 138 138 GLY GLY K . n 
K 1 140 ASN 140 139 139 ASN ASN K . n 
K 1 141 ALA 141 140 140 ALA ALA K . n 
K 1 142 GLY 142 141 141 GLY GLY K . n 
K 1 143 SER 143 142 142 SER SER K . n 
K 1 144 ARG 144 143 143 ARG ARG K . n 
K 1 145 LEU 145 144 144 LEU LEU K . n 
K 1 146 ALA 146 145 145 ALA ALA K . n 
K 1 147 CYS 147 146 146 CYS CYS K . n 
K 1 148 GLY 148 147 147 GLY GLY K . n 
K 1 149 VAL 149 148 148 VAL VAL K . n 
K 1 150 ILE 150 149 149 ILE ILE K . n 
K 1 151 GLY 151 150 150 GLY GLY K . n 
K 1 152 ILE 152 151 151 ILE ILE K . n 
K 1 153 ALA 153 152 152 ALA ALA K . n 
K 1 154 GLN 154 153 153 GLN GLN K . n 
L 1 1   MET 1   0   ?   ?   ?   L . n 
L 1 2   ALA 2   1   1   ALA ALA L . n 
L 1 3   THR 3   2   2   THR THR L . n 
L 1 4   LYS 4   3   3   LYS LYS L . n 
L 1 5   VAL 5   4   4   VAL VAL L . n 
L 1 6   VAL 6   5   5   VAL VAL L . n 
L 1 7   CYS 7   6   6   CYS CYS L . n 
L 1 8   VAL 8   7   7   VAL VAL L . n 
L 1 9   LEU 9   8   8   LEU LEU L . n 
L 1 10  LYS 10  9   9   LYS LYS L . n 
L 1 11  GLY 11  10  10  GLY GLY L . n 
L 1 12  ASP 12  11  11  ASP ASP L . n 
L 1 13  GLY 13  12  12  GLY GLY L . n 
L 1 14  PRO 14  13  13  PRO PRO L . n 
L 1 15  VAL 15  14  14  VAL VAL L . n 
L 1 16  GLN 16  15  15  GLN GLN L . n 
L 1 17  GLY 17  16  16  GLY GLY L . n 
L 1 18  ILE 18  17  17  ILE ILE L . n 
L 1 19  ILE 19  18  18  ILE ILE L . n 
L 1 20  ASN 20  19  19  ASN ASN L . n 
L 1 21  PHE 21  20  20  PHE PHE L . n 
L 1 22  GLU 22  21  21  GLU GLU L . n 
L 1 23  GLN 23  22  22  GLN GLN L . n 
L 1 24  LYS 24  23  23  LYS LYS L . n 
L 1 25  GLU 25  24  24  GLU GLU L . n 
L 1 26  SER 26  25  25  SER SER L . n 
L 1 27  ASN 27  26  26  ASN ASN L . n 
L 1 28  GLY 28  27  27  GLY GLY L . n 
L 1 29  PRO 29  28  28  PRO PRO L . n 
L 1 30  VAL 30  29  29  VAL VAL L . n 
L 1 31  LYS 31  30  30  LYS LYS L . n 
L 1 32  VAL 32  31  31  VAL VAL L . n 
L 1 33  TRP 33  32  32  TRP TRP L . n 
L 1 34  GLY 34  33  33  GLY GLY L . n 
L 1 35  SER 35  34  34  SER SER L . n 
L 1 36  ILE 36  35  35  ILE ILE L . n 
L 1 37  LYS 37  36  36  LYS LYS L . n 
L 1 38  GLY 38  37  37  GLY GLY L . n 
L 1 39  LEU 39  38  38  LEU LEU L . n 
L 1 40  THR 40  39  39  THR THR L . n 
L 1 41  GLU 41  40  40  GLU GLU L . n 
L 1 42  GLY 42  41  41  GLY GLY L . n 
L 1 43  LEU 43  42  42  LEU LEU L . n 
L 1 44  HIS 44  43  43  HIS HIS L . n 
L 1 45  GLY 45  44  44  GLY GLY L . n 
L 1 46  PHE 46  45  45  PHE PHE L . n 
L 1 47  HIS 47  46  46  HIS HIS L . n 
L 1 48  VAL 48  47  47  VAL VAL L . n 
L 1 49  HIS 49  48  48  HIS HIS L . n 
L 1 50  GLU 50  49  49  GLU GLU L . n 
L 1 51  PHE 51  50  50  PHE PHE L . n 
L 1 52  GLY 52  51  51  GLY GLY L . n 
L 1 53  ASP 53  52  52  ASP ASP L . n 
L 1 54  ASN 54  53  53  ASN ASN L . n 
L 1 55  THR 55  54  54  THR THR L . n 
L 1 56  ALA 56  55  55  ALA ALA L . n 
L 1 57  GLY 57  56  56  GLY GLY L . n 
L 1 58  CYS 58  57  57  CYS CYS L . n 
L 1 59  THR 59  58  58  THR THR L . n 
L 1 60  SER 60  59  59  SER SER L . n 
L 1 61  ALA 61  60  60  ALA ALA L . n 
L 1 62  GLY 62  61  61  GLY GLY L . n 
L 1 63  PRO 63  62  62  PRO PRO L . n 
L 1 64  HIS 64  63  63  HIS HIS L . n 
L 1 65  PHE 65  64  64  PHE PHE L . n 
L 1 66  ASN 66  65  65  ASN ASN L . n 
L 1 67  PRO 67  66  66  PRO PRO L . n 
L 1 68  LEU 68  67  67  LEU LEU L . n 
L 1 69  SER 69  68  68  SER SER L . n 
L 1 70  ARG 70  69  69  ARG ARG L . n 
L 1 71  LYS 71  70  70  LYS LYS L . n 
L 1 72  HIS 72  71  71  HIS HIS L . n 
L 1 73  GLY 73  72  72  GLY GLY L . n 
L 1 74  GLY 74  73  73  GLY GLY L . n 
L 1 75  PRO 75  74  74  PRO PRO L . n 
L 1 76  LYS 76  75  75  LYS LYS L . n 
L 1 77  ASP 77  76  76  ASP ASP L . n 
L 1 78  GLU 78  77  77  GLU GLU L . n 
L 1 79  GLU 79  78  78  GLU GLU L . n 
L 1 80  ARG 80  79  79  ARG ARG L . n 
L 1 81  HIS 81  80  80  HIS HIS L . n 
L 1 82  VAL 82  81  81  VAL VAL L . n 
L 1 83  GLY 83  82  82  GLY GLY L . n 
L 1 84  ASP 84  83  83  ASP ASP L . n 
L 1 85  LEU 85  84  84  LEU LEU L . n 
L 1 86  GLY 86  85  85  GLY GLY L . n 
L 1 87  ASN 87  86  86  ASN ASN L . n 
L 1 88  VAL 88  87  87  VAL VAL L . n 
L 1 89  THR 89  88  88  THR THR L . n 
L 1 90  ALA 90  89  89  ALA ALA L . n 
L 1 91  ASP 91  90  90  ASP ASP L . n 
L 1 92  LYS 92  91  91  LYS LYS L . n 
L 1 93  ASP 93  92  92  ASP ASP L . n 
L 1 94  GLY 94  93  93  GLY GLY L . n 
L 1 95  VAL 95  94  94  VAL VAL L . n 
L 1 96  ALA 96  95  95  ALA ALA L . n 
L 1 97  ASP 97  96  96  ASP ASP L . n 
L 1 98  VAL 98  97  97  VAL VAL L . n 
L 1 99  SER 99  98  98  SER SER L . n 
L 1 100 ILE 100 99  99  ILE ILE L . n 
L 1 101 GLU 101 100 100 GLU GLU L . n 
L 1 102 ASP 102 101 101 ASP ASP L . n 
L 1 103 SER 103 102 102 SER SER L . n 
L 1 104 VAL 104 103 103 VAL VAL L . n 
L 1 105 ILE 105 104 104 ILE ILE L . n 
L 1 106 SER 106 105 105 SER SER L . n 
L 1 107 LEU 107 106 106 LEU LEU L . n 
L 1 108 SER 108 107 107 SER SER L . n 
L 1 109 GLY 109 108 108 GLY GLY L . n 
L 1 110 ASP 110 109 109 ASP ASP L . n 
L 1 111 HIS 111 110 110 HIS HIS L . n 
L 1 112 CYS 112 111 111 CYS CYS L . n 
L 1 113 ILE 113 112 112 ILE ILE L . n 
L 1 114 ILE 114 113 113 ILE ILE L . n 
L 1 115 GLY 115 114 114 GLY GLY L . n 
L 1 116 ARG 116 115 115 ARG ARG L . n 
L 1 117 THR 117 116 116 THR THR L . n 
L 1 118 LEU 118 117 117 LEU LEU L . n 
L 1 119 VAL 119 118 118 VAL VAL L . n 
L 1 120 VAL 120 119 119 VAL VAL L . n 
L 1 121 HIS 121 120 120 HIS HIS L . n 
L 1 122 GLU 122 121 121 GLU GLU L . n 
L 1 123 LYS 123 122 122 LYS LYS L . n 
L 1 124 ALA 124 123 123 ALA ALA L . n 
L 1 125 ASP 125 124 124 ASP ASP L . n 
L 1 126 ASP 126 125 125 ASP ASP L . n 
L 1 127 LEU 127 126 126 LEU LEU L . n 
L 1 128 GLY 128 127 127 GLY GLY L . n 
L 1 129 LYS 129 128 128 LYS LYS L . n 
L 1 130 GLY 130 129 129 GLY GLY L . n 
L 1 131 GLY 131 130 130 GLY GLY L . n 
L 1 132 ASN 132 131 131 ASN ASN L . n 
L 1 133 GLU 133 132 132 GLU GLU L . n 
L 1 134 GLU 134 133 133 GLU GLU L . n 
L 1 135 SER 135 134 134 SER SER L . n 
L 1 136 THR 136 135 135 THR THR L . n 
L 1 137 LYS 137 136 136 LYS LYS L . n 
L 1 138 THR 138 137 137 THR THR L . n 
L 1 139 GLY 139 138 138 GLY GLY L . n 
L 1 140 ASN 140 139 139 ASN ASN L . n 
L 1 141 ALA 141 140 140 ALA ALA L . n 
L 1 142 GLY 142 141 141 GLY GLY L . n 
L 1 143 SER 143 142 142 SER SER L . n 
L 1 144 ARG 144 143 143 ARG ARG L . n 
L 1 145 LEU 145 144 144 LEU LEU L . n 
L 1 146 ALA 146 145 145 ALA ALA L . n 
L 1 147 CYS 147 146 146 CYS CYS L . n 
L 1 148 GLY 148 147 147 GLY GLY L . n 
L 1 149 VAL 149 148 148 VAL VAL L . n 
L 1 150 ILE 150 149 149 ILE ILE L . n 
L 1 151 GLY 151 150 150 GLY GLY L . n 
L 1 152 ILE 152 151 151 ILE ILE L . n 
L 1 153 ALA 153 152 152 ALA ALA L . n 
L 1 154 GLN 154 153 153 GLN GLN L . 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 
M  2 LQW 1  201 201 LQW CP4 A . 
N  3 ZN  1  202 202 ZN  ZN  A . 
O  4 SO4 1  203 5   SO4 SO4 A . 
P  4 SO4 1  204 6   SO4 SO4 A . 
Q  2 LQW 1  201 201 LQW CP4 B . 
R  3 ZN  1  202 202 ZN  ZN  B . 
S  4 SO4 1  203 7   SO4 SO4 B . 
T  4 SO4 1  204 8   SO4 SO4 B . 
U  2 LQW 1  201 201 LQW CP4 C . 
V  3 ZN  1  202 202 ZN  ZN  C . 
W  4 SO4 1  203 2   SO4 SO4 C . 
X  2 LQW 1  201 201 LQW CP4 D . 
Y  3 ZN  1  202 202 ZN  ZN  D . 
Z  4 SO4 1  203 1   SO4 SO4 D . 
AA 4 SO4 1  204 4   SO4 SO4 D . 
BA 2 LQW 1  201 201 LQW CP4 E . 
CA 3 ZN  1  202 202 ZN  ZN  E . 
DA 4 SO4 1  203 3   SO4 SO4 E . 
EA 2 LQW 1  201 201 LQW CP4 F . 
FA 3 ZN  1  202 202 ZN  ZN  F . 
GA 4 SO4 1  203 9   SO4 SO4 F . 
HA 4 SO4 1  204 10  SO4 SO4 F . 
IA 2 LQW 1  201 201 LQW CP4 G . 
JA 3 ZN  1  202 202 ZN  ZN  G . 
KA 4 SO4 1  203 14  SO4 SO4 G . 
LA 2 LQW 1  201 201 LQW CP4 H . 
MA 3 ZN  1  202 202 ZN  ZN  H . 
NA 4 SO4 1  203 15  SO4 SO4 H . 
OA 2 LQW 1  201 201 LQW CP4 I . 
PA 3 ZN  1  202 202 ZN  ZN  I . 
QA 2 LQW 1  201 201 LQW CP4 J . 
RA 3 ZN  1  202 202 ZN  ZN  J . 
SA 4 SO4 1  203 16  SO4 SO4 J . 
TA 4 SO4 1  204 17  SO4 SO4 J . 
UA 2 LQW 1  201 201 LQW CP4 K . 
VA 3 ZN  1  202 202 ZN  ZN  K . 
WA 4 SO4 1  203 11  SO4 SO4 K . 
XA 4 SO4 1  204 12  SO4 SO4 K . 
YA 4 SO4 1  205 13  SO4 SO4 K . 
ZA 2 LQW 1  201 201 LQW CP4 L . 
AB 3 ZN  1  202 202 ZN  ZN  L . 
BB 4 SO4 1  203 18  SO4 SO4 L . 
CB 5 HOH 1  301 47  HOH HOH A . 
CB 5 HOH 2  302 36  HOH HOH A . 
CB 5 HOH 3  303 37  HOH HOH A . 
CB 5 HOH 4  304 60  HOH HOH A . 
CB 5 HOH 5  305 40  HOH HOH A . 
CB 5 HOH 6  306 50  HOH HOH A . 
CB 5 HOH 7  307 56  HOH HOH A . 
CB 5 HOH 8  308 38  HOH HOH A . 
CB 5 HOH 9  309 58  HOH HOH A . 
CB 5 HOH 10 310 52  HOH HOH A . 
CB 5 HOH 11 311 12  HOH HOH A . 
CB 5 HOH 12 312 48  HOH HOH A . 
CB 5 HOH 13 313 49  HOH HOH A . 
CB 5 HOH 14 314 55  HOH HOH A . 
CB 5 HOH 15 315 51  HOH HOH A . 
CB 5 HOH 16 316 39  HOH HOH A . 
CB 5 HOH 17 317 161 HOH HOH A . 
CB 5 HOH 18 318 43  HOH HOH A . 
CB 5 HOH 19 319 54  HOH HOH A . 
CB 5 HOH 20 320 22  HOH HOH A . 
CB 5 HOH 21 321 41  HOH HOH A . 
CB 5 HOH 22 322 42  HOH HOH A . 
CB 5 HOH 23 323 59  HOH HOH A . 
DB 5 HOH 1  301 64  HOH HOH B . 
DB 5 HOH 2  302 201 HOH HOH B . 
DB 5 HOH 3  303 222 HOH HOH B . 
DB 5 HOH 4  304 65  HOH HOH B . 
DB 5 HOH 5  305 221 HOH HOH B . 
DB 5 HOH 6  306 33  HOH HOH B . 
DB 5 HOH 7  307 67  HOH HOH B . 
DB 5 HOH 8  308 66  HOH HOH B . 
DB 5 HOH 9  309 68  HOH HOH B . 
DB 5 HOH 10 310 63  HOH HOH B . 
DB 5 HOH 11 311 69  HOH HOH B . 
DB 5 HOH 12 312 219 HOH HOH B . 
DB 5 HOH 13 313 31  HOH HOH B . 
DB 5 HOH 14 314 62  HOH HOH B . 
DB 5 HOH 15 315 61  HOH HOH B . 
EB 5 HOH 1  301 16  HOH HOH C . 
EB 5 HOH 2  302 53  HOH HOH C . 
EB 5 HOH 3  303 14  HOH HOH C . 
EB 5 HOH 4  304 4   HOH HOH C . 
EB 5 HOH 5  305 8   HOH HOH C . 
EB 5 HOH 6  306 163 HOH HOH C . 
EB 5 HOH 7  307 1   HOH HOH C . 
EB 5 HOH 8  308 6   HOH HOH C . 
EB 5 HOH 9  309 9   HOH HOH C . 
EB 5 HOH 10 310 10  HOH HOH C . 
EB 5 HOH 11 311 5   HOH HOH C . 
EB 5 HOH 12 312 7   HOH HOH C . 
EB 5 HOH 13 313 3   HOH HOH C . 
EB 5 HOH 14 314 13  HOH HOH C . 
EB 5 HOH 15 315 83  HOH HOH C . 
EB 5 HOH 16 316 178 HOH HOH C . 
EB 5 HOH 17 317 11  HOH HOH C . 
EB 5 HOH 18 318 177 HOH HOH C . 
FB 5 HOH 1  301 17  HOH HOH D . 
FB 5 HOH 2  302 223 HOH HOH D . 
FB 5 HOH 3  303 228 HOH HOH D . 
FB 5 HOH 4  304 30  HOH HOH D . 
FB 5 HOH 5  305 35  HOH HOH D . 
FB 5 HOH 6  306 23  HOH HOH D . 
FB 5 HOH 7  307 184 HOH HOH D . 
FB 5 HOH 8  308 21  HOH HOH D . 
FB 5 HOH 9  309 34  HOH HOH D . 
FB 5 HOH 10 310 25  HOH HOH D . 
FB 5 HOH 11 311 24  HOH HOH D . 
FB 5 HOH 12 312 229 HOH HOH D . 
FB 5 HOH 13 313 26  HOH HOH D . 
FB 5 HOH 14 314 19  HOH HOH D . 
FB 5 HOH 15 315 32  HOH HOH D . 
GB 5 HOH 1  301 72  HOH HOH E . 
GB 5 HOH 2  302 215 HOH HOH E . 
GB 5 HOH 3  303 46  HOH HOH E . 
GB 5 HOH 4  304 75  HOH HOH E . 
GB 5 HOH 5  305 74  HOH HOH E . 
GB 5 HOH 6  306 76  HOH HOH E . 
GB 5 HOH 7  307 79  HOH HOH E . 
GB 5 HOH 8  308 57  HOH HOH E . 
GB 5 HOH 9  309 224 HOH HOH E . 
GB 5 HOH 10 310 82  HOH HOH E . 
GB 5 HOH 11 311 78  HOH HOH E . 
GB 5 HOH 12 312 73  HOH HOH E . 
GB 5 HOH 13 313 70  HOH HOH E . 
GB 5 HOH 14 314 44  HOH HOH E . 
GB 5 HOH 15 315 45  HOH HOH E . 
GB 5 HOH 16 316 77  HOH HOH E . 
GB 5 HOH 17 317 226 HOH HOH E . 
GB 5 HOH 18 318 71  HOH HOH E . 
HB 5 HOH 1  301 95  HOH HOH F . 
HB 5 HOH 2  302 88  HOH HOH F . 
HB 5 HOH 3  303 89  HOH HOH F . 
HB 5 HOH 4  304 94  HOH HOH F . 
HB 5 HOH 5  305 217 HOH HOH F . 
HB 5 HOH 6  306 99  HOH HOH F . 
HB 5 HOH 7  307 90  HOH HOH F . 
HB 5 HOH 8  308 92  HOH HOH F . 
HB 5 HOH 9  309 87  HOH HOH F . 
HB 5 HOH 10 310 97  HOH HOH F . 
HB 5 HOH 11 311 96  HOH HOH F . 
HB 5 HOH 12 312 20  HOH HOH F . 
HB 5 HOH 13 313 84  HOH HOH F . 
HB 5 HOH 14 314 93  HOH HOH F . 
HB 5 HOH 15 315 98  HOH HOH F . 
HB 5 HOH 16 316 85  HOH HOH F . 
HB 5 HOH 17 317 86  HOH HOH F . 
HB 5 HOH 18 318 91  HOH HOH F . 
IB 5 HOH 1  301 81  HOH HOH G . 
IB 5 HOH 2  302 105 HOH HOH G . 
IB 5 HOH 3  303 80  HOH HOH G . 
IB 5 HOH 4  304 107 HOH HOH G . 
IB 5 HOH 5  305 110 HOH HOH G . 
IB 5 HOH 6  306 212 HOH HOH G . 
IB 5 HOH 7  307 103 HOH HOH G . 
IB 5 HOH 8  308 108 HOH HOH G . 
IB 5 HOH 9  309 112 HOH HOH G . 
IB 5 HOH 10 310 101 HOH HOH G . 
IB 5 HOH 11 311 109 HOH HOH G . 
IB 5 HOH 12 312 111 HOH HOH G . 
IB 5 HOH 13 313 113 HOH HOH G . 
IB 5 HOH 14 314 225 HOH HOH G . 
IB 5 HOH 15 315 183 HOH HOH G . 
IB 5 HOH 16 316 131 HOH HOH G . 
IB 5 HOH 17 317 106 HOH HOH G . 
IB 5 HOH 18 318 100 HOH HOH G . 
JB 5 HOH 1  301 137 HOH HOH H . 
JB 5 HOH 2  302 115 HOH HOH H . 
JB 5 HOH 3  303 123 HOH HOH H . 
JB 5 HOH 4  304 142 HOH HOH H . 
JB 5 HOH 5  305 126 HOH HOH H . 
JB 5 HOH 6  306 132 HOH HOH H . 
JB 5 HOH 7  307 125 HOH HOH H . 
JB 5 HOH 8  308 130 HOH HOH H . 
JB 5 HOH 9  309 136 HOH HOH H . 
JB 5 HOH 10 310 124 HOH HOH H . 
JB 5 HOH 11 311 117 HOH HOH H . 
JB 5 HOH 12 312 116 HOH HOH H . 
JB 5 HOH 13 313 135 HOH HOH H . 
JB 5 HOH 14 314 133 HOH HOH H . 
JB 5 HOH 15 315 129 HOH HOH H . 
JB 5 HOH 16 316 122 HOH HOH H . 
JB 5 HOH 17 317 104 HOH HOH H . 
JB 5 HOH 18 318 120 HOH HOH H . 
JB 5 HOH 19 319 127 HOH HOH H . 
JB 5 HOH 20 320 138 HOH HOH H . 
JB 5 HOH 21 321 114 HOH HOH H . 
JB 5 HOH 22 322 134 HOH HOH H . 
JB 5 HOH 23 323 121 HOH HOH H . 
JB 5 HOH 24 324 128 HOH HOH H . 
KB 5 HOH 1  301 162 HOH HOH I . 
KB 5 HOH 2  302 181 HOH HOH I . 
KB 5 HOH 3  303 173 HOH HOH I . 
KB 5 HOH 4  304 168 HOH HOH I . 
KB 5 HOH 5  305 15  HOH HOH I . 
KB 5 HOH 6  306 2   HOH HOH I . 
KB 5 HOH 7  307 165 HOH HOH I . 
KB 5 HOH 8  308 182 HOH HOH I . 
KB 5 HOH 9  309 171 HOH HOH I . 
KB 5 HOH 10 310 174 HOH HOH I . 
KB 5 HOH 11 311 167 HOH HOH I . 
KB 5 HOH 12 312 170 HOH HOH I . 
KB 5 HOH 13 313 176 HOH HOH I . 
KB 5 HOH 14 314 180 HOH HOH I . 
KB 5 HOH 15 315 169 HOH HOH I . 
KB 5 HOH 16 316 155 HOH HOH I . 
KB 5 HOH 17 317 175 HOH HOH I . 
KB 5 HOH 18 318 179 HOH HOH I . 
KB 5 HOH 19 319 172 HOH HOH I . 
KB 5 HOH 20 320 227 HOH HOH I . 
KB 5 HOH 21 321 166 HOH HOH I . 
LB 5 HOH 1  301 119 HOH HOH J . 
LB 5 HOH 2  302 159 HOH HOH J . 
LB 5 HOH 3  303 143 HOH HOH J . 
LB 5 HOH 4  304 151 HOH HOH J . 
LB 5 HOH 5  305 218 HOH HOH J . 
LB 5 HOH 6  306 216 HOH HOH J . 
LB 5 HOH 7  307 149 HOH HOH J . 
LB 5 HOH 8  308 152 HOH HOH J . 
LB 5 HOH 9  309 154 HOH HOH J . 
LB 5 HOH 10 310 160 HOH HOH J . 
LB 5 HOH 11 311 147 HOH HOH J . 
LB 5 HOH 12 312 146 HOH HOH J . 
LB 5 HOH 13 313 153 HOH HOH J . 
LB 5 HOH 14 314 144 HOH HOH J . 
LB 5 HOH 15 315 140 HOH HOH J . 
LB 5 HOH 16 316 156 HOH HOH J . 
LB 5 HOH 17 317 157 HOH HOH J . 
LB 5 HOH 18 318 148 HOH HOH J . 
LB 5 HOH 19 319 145 HOH HOH J . 
LB 5 HOH 20 320 118 HOH HOH J . 
LB 5 HOH 21 321 158 HOH HOH J . 
LB 5 HOH 22 322 150 HOH HOH J . 
LB 5 HOH 23 323 141 HOH HOH J . 
LB 5 HOH 24 324 139 HOH HOH J . 
MB 5 HOH 1  301 210 HOH HOH K . 
MB 5 HOH 2  302 203 HOH HOH K . 
MB 5 HOH 3  303 220 HOH HOH K . 
MB 5 HOH 4  304 209 HOH HOH K . 
MB 5 HOH 5  305 102 HOH HOH K . 
MB 5 HOH 6  306 211 HOH HOH K . 
MB 5 HOH 7  307 206 HOH HOH K . 
MB 5 HOH 8  308 202 HOH HOH K . 
MB 5 HOH 9  309 208 HOH HOH K . 
MB 5 HOH 10 310 213 HOH HOH K . 
MB 5 HOH 11 311 230 HOH HOH K . 
MB 5 HOH 12 312 204 HOH HOH K . 
MB 5 HOH 13 313 214 HOH HOH K . 
MB 5 HOH 14 314 205 HOH HOH K . 
MB 5 HOH 15 315 207 HOH HOH K . 
NB 5 HOH 1  301 192 HOH HOH L . 
NB 5 HOH 2  302 187 HOH HOH L . 
NB 5 HOH 3  303 29  HOH HOH L . 
NB 5 HOH 4  304 28  HOH HOH L . 
NB 5 HOH 5  305 199 HOH HOH L . 
NB 5 HOH 6  306 193 HOH HOH L . 
NB 5 HOH 7  307 194 HOH HOH L . 
NB 5 HOH 8  308 18  HOH HOH L . 
NB 5 HOH 9  309 189 HOH HOH L . 
NB 5 HOH 10 310 27  HOH HOH L . 
NB 5 HOH 11 311 191 HOH HOH L . 
NB 5 HOH 12 312 164 HOH HOH L . 
NB 5 HOH 13 313 200 HOH HOH L . 
NB 5 HOH 14 314 197 HOH HOH L . 
NB 5 HOH 15 315 195 HOH HOH L . 
NB 5 HOH 16 316 188 HOH HOH L . 
NB 5 HOH 17 317 196 HOH HOH L . 
NB 5 HOH 18 318 198 HOH HOH L . 
NB 5 HOH 19 319 186 HOH HOH L . 
NB 5 HOH 20 320 185 HOH HOH L . 
NB 5 HOH 21 321 190 HOH HOH L . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
3 author_defined_assembly ? dimeric 2 
4 author_defined_assembly ? dimeric 2 
5 author_defined_assembly ? dimeric 2 
6 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,J,M,N,O,P,QA,RA,SA,TA,CB,LB    
2 1 B,K,Q,R,S,T,UA,VA,WA,XA,YA,DB,MB 
3 1 C,I,U,V,W,OA,PA,EB,KB            
4 1 D,L,X,Y,Z,AA,ZA,AB,BB,FB,NB      
5 1 E,G,BA,CA,DA,IA,JA,KA,GB,IB      
6 1 F,H,EA,FA,GA,HA,LA,MA,NA,HB,JB   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 64 ? A HIS 63 ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 72 ? A HIS 71 ? 1_555 99.3  ? 
2  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 110.9 ? 
3  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 123.3 ? 
4  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 104.9 ? 
5  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 96.2  ? 
6  ND1 ? A HIS 81 ? A HIS 80 ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 119.0 ? 
7  ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? R  ZN . ? B ZN 202 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 98.3  ? 
8  ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? R  ZN . ? B ZN 202 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 111.5 ? 
9  ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? R  ZN . ? B ZN 202 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 125.3 ? 
10 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? R  ZN . ? B ZN 202 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 103.1 ? 
11 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? R  ZN . ? B ZN 202 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 95.0  ? 
12 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? R  ZN . ? B ZN 202 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 119.7 ? 
13 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? V  ZN . ? C ZN 202 ? 1_555 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 99.5  ? 
14 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? V  ZN . ? C ZN 202 ? 1_555 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 113.2 ? 
15 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 ZN ? V  ZN . ? C ZN 202 ? 1_555 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 122.6 ? 
16 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? V  ZN . ? C ZN 202 ? 1_555 OD1 ? C ASP 84 ? C ASP 83 ? 1_555 105.9 ? 
17 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 ZN ? V  ZN . ? C ZN 202 ? 1_555 OD1 ? C ASP 84 ? C ASP 83 ? 1_555 94.1  ? 
18 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 ZN ? V  ZN . ? C ZN 202 ? 1_555 OD1 ? C ASP 84 ? C ASP 83 ? 1_555 118.3 ? 
19 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? Y  ZN . ? D ZN 202 ? 1_555 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 99.6  ? 
20 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? Y  ZN . ? D ZN 202 ? 1_555 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 110.6 ? 
21 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? Y  ZN . ? D ZN 202 ? 1_555 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 124.9 ? 
22 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? Y  ZN . ? D ZN 202 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 104.0 ? 
23 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? Y  ZN . ? D ZN 202 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 96.2  ? 
24 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 ZN ? Y  ZN . ? D ZN 202 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 118.3 ? 
25 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? CA ZN . ? E ZN 202 ? 1_555 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 99.6  ? 
26 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? CA ZN . ? E ZN 202 ? 1_555 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 112.1 ? 
27 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? CA ZN . ? E ZN 202 ? 1_555 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 121.5 ? 
28 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? CA ZN . ? E ZN 202 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 106.5 ? 
29 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? CA ZN . ? E ZN 202 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 95.3  ? 
30 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 ZN ? CA ZN . ? E ZN 202 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 118.9 ? 
31 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? FA ZN . ? F ZN 202 ? 1_555 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 97.8  ? 
32 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? FA ZN . ? F ZN 202 ? 1_555 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 113.6 ? 
33 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? FA ZN . ? F ZN 202 ? 1_555 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 124.6 ? 
34 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? FA ZN . ? F ZN 202 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 103.2 ? 
35 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? FA ZN . ? F ZN 202 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 93.3  ? 
36 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 ZN ? FA ZN . ? F ZN 202 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 119.9 ? 
37 ND1 ? G HIS 64 ? G HIS 63 ? 1_555 ZN ? JA ZN . ? G ZN 202 ? 1_555 ND1 ? G HIS 72 ? G HIS 71 ? 1_555 98.2  ? 
38 ND1 ? G HIS 64 ? G HIS 63 ? 1_555 ZN ? JA ZN . ? G ZN 202 ? 1_555 ND1 ? G HIS 81 ? G HIS 80 ? 1_555 112.8 ? 
39 ND1 ? G HIS 72 ? G HIS 71 ? 1_555 ZN ? JA ZN . ? G ZN 202 ? 1_555 ND1 ? G HIS 81 ? G HIS 80 ? 1_555 125.5 ? 
40 ND1 ? G HIS 64 ? G HIS 63 ? 1_555 ZN ? JA ZN . ? G ZN 202 ? 1_555 OD1 ? G ASP 84 ? G ASP 83 ? 1_555 102.6 ? 
41 ND1 ? G HIS 72 ? G HIS 71 ? 1_555 ZN ? JA ZN . ? G ZN 202 ? 1_555 OD1 ? G ASP 84 ? G ASP 83 ? 1_555 94.1  ? 
42 ND1 ? G HIS 81 ? G HIS 80 ? 1_555 ZN ? JA ZN . ? G ZN 202 ? 1_555 OD1 ? G ASP 84 ? G ASP 83 ? 1_555 119.4 ? 
43 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? MA ZN . ? H ZN 202 ? 1_555 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 100.5 ? 
44 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? MA ZN . ? H ZN 202 ? 1_555 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 110.7 ? 
45 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 ZN ? MA ZN . ? H ZN 202 ? 1_555 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 124.7 ? 
46 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? MA ZN . ? H ZN 202 ? 1_555 OD1 ? H ASP 84 ? H ASP 83 ? 1_555 104.2 ? 
47 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 ZN ? MA ZN . ? H ZN 202 ? 1_555 OD1 ? H ASP 84 ? H ASP 83 ? 1_555 96.2  ? 
48 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 ZN ? MA ZN . ? H ZN 202 ? 1_555 OD1 ? H ASP 84 ? H ASP 83 ? 1_555 117.5 ? 
49 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 97.4  ? 
50 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 110.1 ? 
51 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 123.4 ? 
52 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 104.5 ? 
53 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 96.8  ? 
54 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 120.9 ? 
55 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD2 ? I ASP 84 ? I ASP 83 ? 1_555 159.0 ? 
56 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD2 ? I ASP 84 ? I ASP 83 ? 1_555 82.0  ? 
57 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD2 ? I ASP 84 ? I ASP 83 ? 1_555 87.2  ? 
58 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 ZN ? PA ZN . ? I ZN 202 ? 1_555 OD2 ? I ASP 84 ? I ASP 83 ? 1_555 55.0  ? 
59 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? RA ZN . ? J ZN 202 ? 1_555 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 95.6  ? 
60 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? RA ZN . ? J ZN 202 ? 1_555 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 114.3 ? 
61 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? RA ZN . ? J ZN 202 ? 1_555 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 123.4 ? 
62 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? RA ZN . ? J ZN 202 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 103.6 ? 
63 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? RA ZN . ? J ZN 202 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 91.9  ? 
64 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 ZN ? RA ZN . ? J ZN 202 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 122.7 ? 
65 ND1 ? K HIS 64 ? K HIS 63 ? 1_555 ZN ? VA ZN . ? K ZN 202 ? 1_555 ND1 ? K HIS 72 ? K HIS 71 ? 1_555 99.3  ? 
66 ND1 ? K HIS 64 ? K HIS 63 ? 1_555 ZN ? VA ZN . ? K ZN 202 ? 1_555 ND1 ? K HIS 81 ? K HIS 80 ? 1_555 111.3 ? 
67 ND1 ? K HIS 72 ? K HIS 71 ? 1_555 ZN ? VA ZN . ? K ZN 202 ? 1_555 ND1 ? K HIS 81 ? K HIS 80 ? 1_555 127.0 ? 
68 ND1 ? K HIS 64 ? K HIS 63 ? 1_555 ZN ? VA ZN . ? K ZN 202 ? 1_555 OD1 ? K ASP 84 ? K ASP 83 ? 1_555 101.7 ? 
69 ND1 ? K HIS 72 ? K HIS 71 ? 1_555 ZN ? VA ZN . ? K ZN 202 ? 1_555 OD1 ? K ASP 84 ? K ASP 83 ? 1_555 95.3  ? 
70 ND1 ? K HIS 81 ? K HIS 80 ? 1_555 ZN ? VA ZN . ? K ZN 202 ? 1_555 OD1 ? K ASP 84 ? K ASP 83 ? 1_555 118.1 ? 
71 ND1 ? L HIS 64 ? L HIS 63 ? 1_555 ZN ? AB ZN . ? L ZN 202 ? 1_555 ND1 ? L HIS 72 ? L HIS 71 ? 1_555 101.6 ? 
72 ND1 ? L HIS 64 ? L HIS 63 ? 1_555 ZN ? AB ZN . ? L ZN 202 ? 1_555 ND1 ? L HIS 81 ? L HIS 80 ? 1_555 111.9 ? 
73 ND1 ? L HIS 72 ? L HIS 71 ? 1_555 ZN ? AB ZN . ? L ZN 202 ? 1_555 ND1 ? L HIS 81 ? L HIS 80 ? 1_555 121.5 ? 
74 ND1 ? L HIS 64 ? L HIS 63 ? 1_555 ZN ? AB ZN . ? L ZN 202 ? 1_555 OD1 ? L ASP 84 ? L ASP 83 ? 1_555 107.3 ? 
75 ND1 ? L HIS 72 ? L HIS 71 ? 1_555 ZN ? AB ZN . ? L ZN 202 ? 1_555 OD1 ? L ASP 84 ? L ASP 83 ? 1_555 96.2  ? 
76 ND1 ? L HIS 81 ? L HIS 80 ? 1_555 ZN ? AB ZN . ? L ZN 202 ? 1_555 OD1 ? L ASP 84 ? L ASP 83 ? 1_555 116.1 ? 
# 
_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       2020-03-18 
# 
_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_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0238 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.4    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? DIALS       ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_pdbx_entry_details.entry_id                 6SPI 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SG A CYS 111 ? ? SE A LQW 201 ? ? 1.93 
2 1 SG J CYS 111 ? ? SE J LQW 201 ? ? 1.94 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             K 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             K 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             K 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                122.75 
_pdbx_validate_rmsd_angle.angle_target_value         114.20 
_pdbx_validate_rmsd_angle.angle_deviation            8.55 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       318 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.01 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0 ? A MET 1 
2  1 Y 1 B MET 0 ? B MET 1 
3  1 Y 1 C MET 0 ? C MET 1 
4  1 Y 1 D MET 0 ? D MET 1 
5  1 Y 1 E MET 0 ? E MET 1 
6  1 Y 1 F MET 0 ? F MET 1 
7  1 Y 1 G MET 0 ? G MET 1 
8  1 Y 1 H MET 0 ? H MET 1 
9  1 Y 1 I MET 0 ? I MET 1 
10 1 Y 1 J MET 0 ? J MET 1 
11 1 Y 1 K MET 0 ? K MET 1 
12 1 Y 1 L MET 0 ? L MET 1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        LQW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LQW 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '~{N}-[(4-chlorophenyl)methyl]-2-selanyl-benzamide' LQW 
3 'ZINC ION'                                          ZN  
4 'SULFATE ION'                                       SO4 
5 water                                               HOH 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 3 'gel filtration' ? 
3 2 'gel filtration' ? 
4 4 'gel filtration' ? 
5 5 'gel filtration' ? 
6 6 'gel filtration' ? 
# 
