data_5J0F
# 
_entry.id   5J0F 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5J0F         
WWPDB D_1000219763 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5J0F 
_pdbx_database_status.recvd_initial_deposition_date   2016-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_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 
'Wang, H.'       1 
'Lang, L.'       2 
'Logan, D.'      3 
'Danielsson, J.' 4 
'Oliveberg, M.'  5 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J. Am. Chem. Soc.' 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            138 
_citation.language                  ? 
_citation.page_first                15571 
_citation.page_last                 15579 
_citation.title                     'Tricking a Protein To Swap Strands.' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.6b05151 
_citation.pdbx_database_id_PubMed   27783493 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Wang, H.'       1 
primary 'Lang, L.'       2 
primary 'Logan, D.T.'    3 
primary 'Danielsson, J.' 4 
primary 'Oliveberg, M.'  5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5J0F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.720 
_cell.length_a_esd                 ? 
_cell.length_b                     71.720 
_cell.length_b_esd                 ? 
_cell.length_c                     69.510 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5J0F 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_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],OXIDOREDUCTASE,Superoxide dismutase [Cu-Zn]' 11260.579 2   1.15.1.1,1.15.1.1 ? ? ? 
2 non-polymer syn GLYCEROL                                                                   92.094    5   ?                 ? ? ? 
3 water       nat water                                                                      18.015    263 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1,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       
;AGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKAGAGAGSRLASGVIGIAQAGAGATKAVAVLKGDGPVQG
IINFEQKESNGPVKVWGSIKGLTEGLHGFHVHGA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKAGAGAGSRLASGVIGIAQAGAGATKAVAVLKGDGPVQG
IINFEQKESNGPVKVWGSIKGLTEGLHGFHVHGA
;
_entity_poly.pdbx_strand_id                 A,B 
_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   ALA n 
1 2   GLY n 
1 3   ASP n 
1 4   LEU n 
1 5   GLY n 
1 6   ASN n 
1 7   VAL n 
1 8   THR n 
1 9   ALA n 
1 10  ASP n 
1 11  LYS n 
1 12  ASP n 
1 13  GLY n 
1 14  VAL n 
1 15  ALA n 
1 16  ASP n 
1 17  VAL n 
1 18  SER n 
1 19  ILE n 
1 20  GLU n 
1 21  ASP n 
1 22  SER n 
1 23  VAL n 
1 24  ILE n 
1 25  SER n 
1 26  LEU n 
1 27  SER n 
1 28  GLY n 
1 29  ASP n 
1 30  HIS n 
1 31  SER n 
1 32  ILE n 
1 33  ILE n 
1 34  GLY n 
1 35  ARG n 
1 36  THR n 
1 37  LEU n 
1 38  VAL n 
1 39  VAL n 
1 40  HIS n 
1 41  GLU n 
1 42  LYS n 
1 43  ALA n 
1 44  GLY n 
1 45  ALA n 
1 46  GLY n 
1 47  ALA n 
1 48  GLY n 
1 49  SER n 
1 50  ARG n 
1 51  LEU n 
1 52  ALA n 
1 53  SER n 
1 54  GLY n 
1 55  VAL n 
1 56  ILE n 
1 57  GLY n 
1 58  ILE n 
1 59  ALA n 
1 60  GLN n 
1 61  ALA n 
1 62  GLY n 
1 63  ALA n 
1 64  GLY n 
1 65  ALA n 
1 66  THR n 
1 67  LYS n 
1 68  ALA n 
1 69  VAL n 
1 70  ALA n 
1 71  VAL n 
1 72  LEU n 
1 73  LYS n 
1 74  GLY n 
1 75  ASP n 
1 76  GLY n 
1 77  PRO n 
1 78  VAL n 
1 79  GLN n 
1 80  GLY n 
1 81  ILE n 
1 82  ILE n 
1 83  ASN n 
1 84  PHE n 
1 85  GLU n 
1 86  GLN n 
1 87  LYS n 
1 88  GLU n 
1 89  SER n 
1 90  ASN n 
1 91  GLY n 
1 92  PRO n 
1 93  VAL n 
1 94  LYS n 
1 95  VAL n 
1 96  TRP n 
1 97  GLY n 
1 98  SER n 
1 99  ILE n 
1 100 LYS n 
1 101 GLY n 
1 102 LEU n 
1 103 THR n 
1 104 GLU n 
1 105 GLY n 
1 106 LEU n 
1 107 HIS n 
1 108 GLY n 
1 109 PHE n 
1 110 HIS n 
1 111 VAL n 
1 112 HIS n 
1 113 GLY n 
1 114 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1  43  Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 83333 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 48 60  HUMAN ? ?    ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 83333 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 65 114 Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 83333 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SODC_HUMAN P00441 ? 1 GDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKA       83 
2 PDB 5J0F       5J0F   ? 1 ?                                                48 
3 UNP SODC_HUMAN P00441 ? 1 ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVH 2  
# 
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 5J0F A 2  ? 43  ? P00441 83 ? 124 ? 2  43  
2 2 5J0F A 48 ? 60  ? 5J0F   48 ? 60  ? 48 60  
3 3 5J0F A 65 ? 112 ? P00441 2  ? 49  ? 65 112 
4 1 5J0F B 2  ? 43  ? P00441 83 ? 124 ? 2  43  
5 2 5J0F B 48 ? 60  ? 5J0F   48 ? 60  ? 48 60  
6 3 5J0F B 65 ? 112 ? P00441 2  ? 49  ? 65 112 
# 
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 5J0F ALA A 1   ? UNP P00441 ?   ?   'expression tag' 1   1  
1 5J0F SER A 31  ? UNP P00441 CYS 112 conflict         31  2  
1 5J0F GLY A 44  ? UNP P00441 ?   ?   linker           44  3  
1 5J0F ALA A 45  ? UNP P00441 ?   ?   linker           45  4  
1 5J0F GLY A 46  ? UNP P00441 ?   ?   linker           46  5  
1 5J0F ALA A 47  ? UNP P00441 ?   ?   linker           47  6  
1 5J0F ALA A 61  ? UNP P00441 ?   ?   linker           61  7  
1 5J0F GLY A 62  ? UNP P00441 ?   ?   linker           62  8  
1 5J0F ALA A 63  ? UNP P00441 ?   ?   linker           63  9  
1 5J0F GLY A 64  ? UNP P00441 ?   ?   linker           64  10 
3 5J0F ALA A 70  ? UNP P00441 CYS 7   conflict         70  11 
3 5J0F GLY A 113 ? UNP P00441 ?   ?   'expression tag' 113 12 
3 5J0F ALA A 114 ? UNP P00441 ?   ?   'expression tag' 114 13 
4 5J0F ALA B 1   ? UNP P00441 ?   ?   'expression tag' 1   14 
4 5J0F SER B 31  ? UNP P00441 CYS 112 conflict         31  15 
4 5J0F GLY B 44  ? UNP P00441 ?   ?   linker           44  16 
4 5J0F ALA B 45  ? UNP P00441 ?   ?   linker           45  17 
4 5J0F GLY B 46  ? UNP P00441 ?   ?   linker           46  18 
4 5J0F ALA B 47  ? UNP P00441 ?   ?   linker           47  19 
4 5J0F ALA B 61  ? UNP P00441 ?   ?   linker           61  20 
4 5J0F GLY B 62  ? UNP P00441 ?   ?   linker           62  21 
4 5J0F ALA B 63  ? UNP P00441 ?   ?   linker           63  22 
4 5J0F GLY B 64  ? UNP P00441 ?   ?   linker           64  23 
6 5J0F ALA B 70  ? UNP P00441 CYS 7   conflict         70  24 
6 5J0F GLY B 113 ? UNP P00441 ?   ?   'expression tag' 113 25 
6 5J0F ALA B 114 ? UNP P00441 ?   ?   'expression tag' 114 26 
# 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
_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                   5J0F 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.29 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         46.32 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.17 M ammonium sulfate, 25.5 % w/v PEG 4K, 15 % v/v Glycerol' 
_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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         MARRESEARCH 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-11-01 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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                        'MAX II BEAMLINE I911-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I911-3 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5J0F 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.25 
_reflns.d_resolution_low                 46.36 
_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                       56396 
_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             100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.9 
_reflns.pdbx_Rmerge_I_obs                0.039 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            29.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  1.25 
_reflns_shell.d_res_low                   1.29 
_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           ? 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.563 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            0.0800 
_refine.aniso_B[1][2]                            0.0800 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.0800 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.2500 
_refine.B_iso_max                                205.760 
_refine.B_iso_mean                               20.9820 
_refine.B_iso_min                                7.730 
_refine.correlation_coeff_Fo_to_Fc               0.9800 
_refine.correlation_coeff_Fo_to_Fc_free          0.9660 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_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                                 5J0F 
_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                            1.2500 
_refine.ls_d_res_low                             46.3600 
_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                     53233 
_refine.ls_number_reflns_R_free                  2848 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9600 
_refine.ls_percent_reflns_R_free                 5.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1313 
_refine.ls_R_factor_R_free                       0.1696 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1293 
_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                          0.000 
_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                      4bcz 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0370 
_refine.pdbx_overall_ESU_R_Free                  0.0410 
_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                             1.0840 
_refine.overall_SU_ML                            0.0220 
_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.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.2500 
_refine_hist.d_res_low                        46.3600 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             263 
_refine_hist.number_atoms_total               1879 
_refine_hist.pdbx_number_residues_total       228 
_refine_hist.pdbx_B_iso_mean_ligand           40.69 
_refine_hist.pdbx_B_iso_mean_solvent          39.31 
_refine_hist.pdbx_number_atoms_protein        1586 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
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' ? 0.022  0.019  1631 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1604 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.004  1.956  2195 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.905  3.000  3690 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 7.959  5.000  226  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 45.017 25.714 56   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 11.732 15.000 252  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 22.320 15.000 4    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.147  0.200  257  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1890 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  334  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 4.548  1.710  910  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 4.544  1.708  909  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 5.463  2.577  1134 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 5.663  3.000  3235 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 53.620 5.000  69   ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 24.168 5.000  3414 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2500 
_refine_ls_shell.d_res_low                        1.2820 
_refine_ls_shell.number_reflns_all                4192 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             237 
_refine_ls_shell.number_reflns_R_work             3955 
_refine_ls_shell.percent_reflns_obs               100.0000 
_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                  0.2320 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1970 
_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                    ? 
# 
_struct.entry_id                     5J0F 
_struct.title                        
'Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P4/5' 
_struct.pdbx_descriptor              
'Superoxide dismutase [Cu-Zn],OXIDOREDUCTASE,Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1,1.15.1.1)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5J0F 
_struct_keywords.text            'SOD1, 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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ALA 
_struct_mon_prot_cis.label_seq_id           63 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ALA 
_struct_mon_prot_cis.auth_seq_id            63 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   GLY 
_struct_mon_prot_cis.pdbx_label_seq_id_2    64 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    GLY 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     64 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       7.51 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 9 ? 
# 
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 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? 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 ASP A 3   ? ALA A 9   ? ASP A 3   ALA A 9   
AA1 2 GLY A 105 ? HIS A 112 ? GLY A 105 HIS A 112 
AA1 3 THR A 36  ? HIS A 40  ? THR A 36  HIS A 40  
AA1 4 LEU A 51  ? ALA A 59  ? LEU A 51  ALA A 59  
AA1 5 THR A 66  ? LYS A 73  ? THR A 66  LYS A 73  
AA1 6 GLN A 79  ? GLN A 86  ? GLN A 79  GLN A 86  
AA1 7 VAL A 93  ? LYS A 100 ? VAL A 93  LYS A 100 
AA1 8 ALA A 15  ? ASP A 21  ? ALA A 15  ASP A 21  
AA2 1 ASP B 3   ? ALA B 9   ? ASP B 3   ALA B 9   
AA2 2 ALA B 15  ? ASP B 21  ? ALA B 15  ASP B 21  
AA2 3 VAL B 93  ? LYS B 100 ? VAL B 93  LYS B 100 
AA2 4 GLN B 79  ? GLN B 86  ? GLN B 79  GLN B 86  
AA2 5 ALA B 65  ? LYS B 73  ? ALA B 65  LYS B 73  
AA2 6 LEU B 51  ? GLY B 62  ? LEU B 51  GLY B 62  
AA2 7 THR B 36  ? HIS B 40  ? THR B 36  HIS B 40  
AA2 8 GLY B 105 ? VAL B 111 ? GLY B 105 VAL B 111 
AA2 9 ASP B 3   ? ALA B 9   ? ASP B 3   ALA B 9   
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 9   ? N ALA A 9   O GLY A 105 ? O GLY A 105 
AA1 2 3 O HIS A 112 ? O HIS A 112 N THR A 36  ? N THR A 36  
AA1 3 4 N LEU A 37  ? N LEU A 37  O GLY A 54  ? O GLY A 54  
AA1 4 5 N GLY A 57  ? N GLY A 57  O VAL A 69  ? O VAL A 69  
AA1 5 6 N ALA A 70  ? N ALA A 70  O ILE A 82  ? O ILE A 82  
AA1 6 7 N ASN A 83  ? N ASN A 83  O TRP A 96  ? O TRP A 96  
AA1 7 8 O ILE A 99  ? O ILE A 99  N ALA A 15  ? N ALA A 15  
AA2 1 2 N THR B 8   ? N THR B 8   O ASP B 16  ? O ASP B 16  
AA2 2 3 N ASP B 21  ? N ASP B 21  O VAL B 93  ? O VAL B 93  
AA2 3 4 O TRP B 96  ? O TRP B 96  N ASN B 83  ? N ASN B 83  
AA2 4 5 O ILE B 82  ? O ILE B 82  N ALA B 70  ? N ALA B 70  
AA2 5 6 O ALA B 65  ? O ALA B 65  N GLY B 62  ? N GLY B 62  
AA2 6 7 O GLY B 54  ? O GLY B 54  N LEU B 37  ? N LEU B 37  
AA2 7 8 N VAL B 38  ? N VAL B 38  O HIS B 110 ? O HIS B 110 
AA2 8 9 O GLY B 105 ? O GLY B 105 N ALA B 9   ? N ALA B 9   
# 
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 GOL 201 ? 9 'binding site for residue GOL A 201' 
AC2 Software A GOL 202 ? 7 'binding site for residue GOL A 202' 
AC3 Software A GOL 203 ? 7 'binding site for residue GOL A 203' 
AC4 Software B GOL 201 ? 7 'binding site for residue GOL B 201' 
AC5 Software B GOL 202 ? 7 'binding site for residue GOL B 202' 
# 
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 9 THR A 8   ? THR A 8   . ? 1_555 ? 
2  AC1 9 ASP A 10  ? ASP A 10  . ? 1_555 ? 
3  AC1 9 VAL A 14  ? VAL A 14  . ? 1_555 ? 
4  AC1 9 ALA A 15  ? ALA A 15  . ? 1_555 ? 
5  AC1 9 ASP A 16  ? ASP A 16  . ? 1_555 ? 
6  AC1 9 HIS A 112 ? HIS A 112 . ? 5_555 ? 
7  AC1 9 HOH H .   ? HOH A 329 . ? 1_555 ? 
8  AC1 9 PRO B 92  ? PRO B 92  . ? 2_544 ? 
9  AC1 9 HOH I .   ? HOH B 308 . ? 2_544 ? 
10 AC2 7 GLY A 97  ? GLY A 97  . ? 1_555 ? 
11 AC2 7 SER A 98  ? SER A 98  . ? 1_555 ? 
12 AC2 7 HOH H .   ? HOH A 310 . ? 1_555 ? 
13 AC2 7 HOH H .   ? HOH A 322 . ? 1_555 ? 
14 AC2 7 HOH H .   ? HOH A 359 . ? 1_555 ? 
15 AC2 7 HOH H .   ? HOH A 395 . ? 1_555 ? 
16 AC2 7 ALA B 59  ? ALA B 59  . ? 1_555 ? 
17 AC3 7 VAL A 14  ? VAL A 14  . ? 1_555 ? 
18 AC3 7 THR A 36  ? THR A 36  . ? 5_555 ? 
19 AC3 7 SER A 53  ? SER A 53  . ? 5_555 ? 
20 AC3 7 LYS A 100 ? LYS A 100 . ? 1_555 ? 
21 AC3 7 HIS A 112 ? HIS A 112 . ? 5_555 ? 
22 AC3 7 HOH H .   ? HOH A 354 . ? 5_555 ? 
23 AC3 7 HOH H .   ? HOH A 409 . ? 5_555 ? 
24 AC4 7 ILE A 58  ? ILE A 58  . ? 5_555 ? 
25 AC4 7 ASP B 16  ? ASP B 16  . ? 5_555 ? 
26 AC4 7 THR B 36  ? THR B 36  . ? 1_555 ? 
27 AC4 7 HIS B 112 ? HIS B 112 . ? 1_555 ? 
28 AC4 7 GOL G .   ? GOL B 202 . ? 5_555 ? 
29 AC4 7 HOH I .   ? HOH B 306 . ? 1_555 ? 
30 AC4 7 HOH I .   ? HOH B 339 . ? 1_555 ? 
31 AC5 7 VAL A 69  ? VAL A 69  . ? 1_555 ? 
32 AC5 7 HOH H .   ? HOH A 326 . ? 1_555 ? 
33 AC5 7 ILE B 81  ? ILE B 81  . ? 1_555 ? 
34 AC5 7 GLY B 97  ? GLY B 97  . ? 1_555 ? 
35 AC5 7 SER B 98  ? SER B 98  . ? 1_555 ? 
36 AC5 7 GOL F .   ? GOL B 201 . ? 6_554 ? 
37 AC5 7 HOH I .   ? HOH B 301 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5J0F 
_atom_sites.fract_transf_matrix[1][1]   0.013943 
_atom_sites.fract_transf_matrix[1][2]   0.008050 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016100 
_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]   0.014386 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 1   ? 35.757 5.722   -7.644  1.00 12.89  ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? 35.664 4.444   -6.886  1.00 11.36  ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? 34.203 4.035   -6.797  1.00 11.37  ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? 33.332 4.864   -7.100  1.00 13.87  ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? 36.269 4.611   -5.505  1.00 13.09  ? 1   ALA A CB  1 
ATOM   6    N N   . GLY A 1 2   ? 33.909 2.827   -6.336  1.00 10.68  ? 2   GLY A N   1 
ATOM   7    C CA  . GLY A 1 2   ? 32.604 2.464   -5.884  1.00 11.60  ? 2   GLY A CA  1 
ATOM   8    C C   . GLY A 1 2   ? 32.006 1.238   -6.497  1.00 10.61  ? 2   GLY A C   1 
ATOM   9    O O   . GLY A 1 2   ? 30.977 0.749   -6.001  1.00 11.64  ? 2   GLY A O   1 
ATOM   10   N N   . ASP A 1 3   ? 32.556 0.705   -7.601  1.00 11.48  ? 3   ASP A N   1 
ATOM   11   C CA  . ASP A 1 3   ? 31.993 -0.478  -8.168  1.00 12.21  ? 3   ASP A CA  1 
ATOM   12   C C   . ASP A 1 3   ? 32.239 -1.658  -7.212  1.00 12.69  ? 3   ASP A C   1 
ATOM   13   O O   . ASP A 1 3   ? 33.373 -1.866  -6.790  1.00 15.70  ? 3   ASP A O   1 
ATOM   14   C CB  . ASP A 1 3   ? 32.600 -0.841  -9.469  1.00 15.74  ? 3   ASP A CB  1 
ATOM   15   C CG  . ASP A 1 3   ? 31.756 -1.996  -10.052 1.00 20.88  ? 3   ASP A CG  1 
ATOM   16   O OD1 . ASP A 1 3   ? 30.630 -1.762  -10.496 1.00 30.88  ? 3   ASP A OD1 1 
ATOM   17   O OD2 . ASP A 1 3   ? 32.096 -3.118  -9.867  1.00 24.70  ? 3   ASP A OD2 1 
ATOM   18   N N   . LEU A 1 4   ? 31.172 -2.371  -6.860  1.00 11.00  ? 4   LEU A N   1 
ATOM   19   C CA  . LEU A 1 4   ? 31.243 -3.529  -5.969  1.00 11.86  ? 4   LEU A CA  1 
ATOM   20   C C   . LEU A 1 4   ? 30.718 -4.788  -6.641  1.00 12.83  ? 4   LEU A C   1 
ATOM   21   O O   . LEU A 1 4   ? 30.315 -5.701  -5.955  1.00 15.52  ? 4   LEU A O   1 
ATOM   22   C CB  . LEU A 1 4   ? 30.581 -3.266  -4.619  1.00 11.74  ? 4   LEU A CB  1 
ATOM   23   C CG  . LEU A 1 4   ? 31.244 -2.115  -3.822  1.00 13.29  ? 4   LEU A CG  1 
ATOM   24   C CD1 . LEU A 1 4   ? 30.362 -1.794  -2.603  1.00 13.74  ? 4   LEU A CD1 1 
ATOM   25   C CD2 . LEU A 1 4   ? 32.699 -2.459  -3.386  1.00 16.14  ? 4   LEU A CD2 1 
ATOM   26   N N   . GLY A 1 5   ? 30.683 -4.839  -7.943  1.00 12.77  ? 5   GLY A N   1 
ATOM   27   C CA  . GLY A 1 5   ? 30.281 -6.022  -8.658  1.00 14.06  ? 5   GLY A CA  1 
ATOM   28   C C   . GLY A 1 5   ? 28.789 -6.291  -8.595  1.00 13.40  ? 5   GLY A C   1 
ATOM   29   O O   . GLY A 1 5   ? 27.992 -5.360  -8.668  1.00 13.43  ? 5   GLY A O   1 
ATOM   30   N N   . ASN A 1 6   ? 28.426 -7.548  -8.549  1.00 13.82  ? 6   ASN A N   1 
ATOM   31   C CA  . ASN A 1 6   ? 27.093 -7.966  -8.409  1.00 13.03  ? 6   ASN A CA  1 
ATOM   32   C C   . ASN A 1 6   ? 26.913 -8.786  -7.136  1.00 14.87  ? 6   ASN A C   1 
ATOM   33   O O   . ASN A 1 6   ? 27.882 -9.465  -6.679  1.00 20.62  ? 6   ASN A O   1 
ATOM   34   C CB  . ASN A 1 6   ? 26.727 -8.921  -9.551  1.00 15.79  ? 6   ASN A CB  1 
ATOM   35   C CG  . ASN A 1 6   ? 26.667 -8.240  -10.875 1.00 18.26  ? 6   ASN A CG  1 
ATOM   36   O OD1 . ASN A 1 6   ? 26.020 -7.235  -11.040 1.00 19.52  ? 6   ASN A OD1 1 
ATOM   37   N ND2 . ASN A 1 6   ? 27.215 -8.911  -11.898 1.00 26.54  ? 6   ASN A ND2 1 
ATOM   38   N N   . VAL A 1 7   ? 25.732 -8.709  -6.529  1.00 13.25  ? 7   VAL A N   1 
ATOM   39   C CA  . VAL A 1 7   ? 25.334 -9.649  -5.487  1.00 14.05  ? 7   VAL A CA  1 
ATOM   40   C C   . VAL A 1 7   ? 24.387 -10.692 -6.088  1.00 13.56  ? 7   VAL A C   1 
ATOM   41   O O   . VAL A 1 7   ? 23.754 -10.421 -7.081  1.00 17.19  ? 7   VAL A O   1 
ATOM   42   C CB  . VAL A 1 7   ? 24.784 -8.905  -4.251  1.00 14.70  ? 7   VAL A CB  1 
ATOM   43   C CG1 . VAL A 1 7   ? 25.868 -7.953  -3.725  1.00 18.50  ? 7   VAL A CG1 1 
ATOM   44   C CG2 . VAL A 1 7   ? 23.464 -8.241  -4.585  1.00 16.86  ? 7   VAL A CG2 1 
ATOM   45   N N   . THR A 1 8   ? 24.253 -11.820 -5.444  1.00 13.99  ? 8   THR A N   1 
ATOM   46   C CA  . THR A 1 8   ? 23.422 -12.900 -5.961  1.00 13.85  ? 8   THR A CA  1 
ATOM   47   C C   . THR A 1 8   ? 22.338 -13.191 -4.941  1.00 13.32  ? 8   THR A C   1 
ATOM   48   O O   . THR A 1 8   ? 22.619 -13.472 -3.769  1.00 14.57  ? 8   THR A O   1 
ATOM   49   C CB  . THR A 1 8   ? 24.248 -14.154 -6.208  1.00 17.03  ? 8   THR A CB  1 
ATOM   50   O OG1 . THR A 1 8   ? 25.211 -13.897 -7.219  1.00 20.67  ? 8   THR A OG1 1 
ATOM   51   C CG2 . THR A 1 8   ? 23.373 -15.288 -6.680  1.00 17.84  ? 8   THR A CG2 1 
ATOM   52   N N   . ALA A 1 9   ? 21.090 -13.039 -5.373  1.00 13.45  ? 9   ALA A N   1 
ATOM   53   C CA  . ALA A 1 9   ? 19.948 -13.396 -4.549  1.00 13.06  ? 9   ALA A CA  1 
ATOM   54   C C   . ALA A 1 9   ? 19.544 -14.815 -4.864  1.00 13.91  ? 9   ALA A C   1 
ATOM   55   O O   . ALA A 1 9   ? 19.462 -15.215 -6.041  1.00 15.45  ? 9   ALA A O   1 
ATOM   56   C CB  . ALA A 1 9   ? 18.782 -12.462 -4.801  1.00 14.25  ? 9   ALA A CB  1 
ATOM   57   N N   . ASP A 1 10  ? 19.203 -15.553 -3.822  1.00 14.64  ? 10  ASP A N   1 
ATOM   58   C CA  . ASP A 1 10  ? 18.696 -16.937 -3.949  1.00 15.30  ? 10  ASP A CA  1 
ATOM   59   C C   . ASP A 1 10  ? 17.217 -16.949 -4.229  1.00 16.63  ? 10  ASP A C   1 
ATOM   60   O O   . ASP A 1 10  ? 16.585 -15.946 -4.468  1.00 17.81  ? 10  ASP A O   1 
ATOM   61   C CB  . ASP A 1 10  ? 19.095 -17.746 -2.725  1.00 16.77  ? 10  ASP A CB  1 
ATOM   62   C CG  . ASP A 1 10  ? 18.402 -17.257 -1.408  1.00 15.66  ? 10  ASP A CG  1 
ATOM   63   O OD1 . ASP A 1 10  ? 17.396 -16.549 -1.481  1.00 16.22  ? 10  ASP A OD1 1 
ATOM   64   O OD2 . ASP A 1 10  ? 18.858 -17.664 -0.332  1.00 19.16  ? 10  ASP A OD2 1 
ATOM   65   N N   . LYS A 1 11  ? 16.650 -18.164 -4.267  1.00 17.70  ? 11  LYS A N   1 
ATOM   66   C CA  . LYS A 1 11  ? 15.268 -18.308 -4.589  1.00 22.43  ? 11  LYS A CA  1 
ATOM   67   C C   . LYS A 1 11  ? 14.339 -17.719 -3.580  1.00 22.94  ? 11  LYS A C   1 
ATOM   68   O O   . LYS A 1 11  ? 13.161 -17.443 -3.881  1.00 29.42  ? 11  LYS A O   1 
ATOM   69   C CB  . LYS A 1 11  ? 14.895 -19.833 -4.770  1.00 28.31  ? 11  LYS A CB  1 
ATOM   70   C CG  . LYS A 1 11  ? 14.074 -20.043 -6.002  1.00 42.33  ? 11  LYS A CG  1 
ATOM   71   C CD  . LYS A 1 11  ? 13.966 -21.524 -6.296  1.00 52.07  ? 11  LYS A CD  1 
ATOM   72   C CE  . LYS A 1 11  ? 12.801 -21.846 -7.226  1.00 60.10  ? 11  LYS A CE  1 
ATOM   73   N NZ  . LYS A 1 11  ? 12.269 -23.236 -7.065  1.00 71.45  ? 11  LYS A NZ  1 
ATOM   74   N N   . ASP A 1 12  ? 14.858 -17.533 -2.363  1.00 19.28  ? 12  ASP A N   1 
ATOM   75   C CA  . ASP A 1 12  ? 14.130 -16.830 -1.285  1.00 20.53  ? 12  ASP A CA  1 
ATOM   76   C C   . ASP A 1 12  ? 14.252 -15.318 -1.340  1.00 20.55  ? 12  ASP A C   1 
ATOM   77   O O   . ASP A 1 12  ? 13.654 -14.622 -0.550  1.00 23.02  ? 12  ASP A O   1 
ATOM   78   C CB  . ASP A 1 12  ? 14.559 -17.313 0.084   1.00 21.48  ? 12  ASP A CB  1 
ATOM   79   C CG  . ASP A 1 12  ? 14.007 -18.595 0.471   1.00 24.10  ? 12  ASP A CG  1 
ATOM   80   O OD1 . ASP A 1 12  ? 13.125 -19.171 -0.236  1.00 23.00  ? 12  ASP A OD1 1 
ATOM   81   O OD2 . ASP A 1 12  ? 14.470 -19.073 1.497   1.00 29.28  ? 12  ASP A OD2 1 
ATOM   82   N N   . GLY A 1 13  ? 14.967 -14.805 -2.329  1.00 18.57  ? 13  GLY A N   1 
ATOM   83   C CA  . GLY A 1 13  ? 15.201 -13.378 -2.480  1.00 18.12  ? 13  GLY A CA  1 
ATOM   84   C C   . GLY A 1 13  ? 16.213 -12.746 -1.557  1.00 16.12  ? 13  GLY A C   1 
ATOM   85   O O   . GLY A 1 13  ? 16.261 -11.546 -1.459  1.00 15.86  ? 13  GLY A O   1 
ATOM   86   N N   . VAL A 1 14  ? 17.065 -13.610 -0.950  1.00 13.95  ? 14  VAL A N   1 
ATOM   87   C CA  . VAL A 1 14  ? 18.105 -13.171 -0.026  1.00 14.10  ? 14  VAL A CA  1 
ATOM   88   C C   . VAL A 1 14  ? 19.432 -13.196 -0.701  1.00 13.19  ? 14  VAL A C   1 
ATOM   89   O O   . VAL A 1 14  ? 19.817 -14.200 -1.279  1.00 13.91  ? 14  VAL A O   1 
ATOM   90   C CB  . VAL A 1 14  ? 18.114 -14.017 1.247   1.00 14.97  ? 14  VAL A CB  1 
ATOM   91   C CG1 . VAL A 1 14  ? 19.215 -13.561 2.177   1.00 16.00  ? 14  VAL A CG1 1 
ATOM   92   C CG2 . VAL A 1 14  ? 16.762 -14.028 1.933   1.00 18.98  ? 14  VAL A CG2 1 
ATOM   93   N N   . ALA A 1 15  ? 20.129 -12.061 -0.633  1.00 13.84  ? 15  ALA A N   1 
ATOM   94   C CA  . ALA A 1 15  ? 21.553 -11.963 -1.073  1.00 13.37  ? 15  ALA A CA  1 
ATOM   95   C C   . ALA A 1 15  ? 22.422 -11.736 0.140   1.00 13.60  ? 15  ALA A C   1 
ATOM   96   O O   . ALA A 1 15  ? 22.342 -10.694 0.764   1.00 17.73  ? 15  ALA A O   1 
ATOM   97   C CB  . ALA A 1 15  ? 21.739 -10.821 -2.042  1.00 14.73  ? 15  ALA A CB  1 
ATOM   98   N N   . ASP A 1 16  ? 23.277 -12.678 0.468   1.00 14.49  ? 16  ASP A N   1 
ATOM   99   C CA  . ASP A 1 16  ? 24.278 -12.532 1.460   1.00 13.20  ? 16  ASP A CA  1 
ATOM   100  C C   . ASP A 1 16  ? 25.497 -11.967 0.801   1.00 13.73  ? 16  ASP A C   1 
ATOM   101  O O   . ASP A 1 16  ? 25.921 -12.422 -0.228  1.00 17.67  ? 16  ASP A O   1 
ATOM   102  C CB  . ASP A 1 16  ? 24.542 -13.874 2.158   1.00 14.99  ? 16  ASP A CB  1 
ATOM   103  C CG  . ASP A 1 16  ? 23.375 -14.296 3.024   1.00 16.89  ? 16  ASP A CG  1 
ATOM   104  O OD1 . ASP A 1 16  ? 22.790 -13.456 3.757   1.00 22.83  ? 16  ASP A OD1 1 
ATOM   105  O OD2 . ASP A 1 16  ? 22.990 -15.428 2.982   1.00 20.45  ? 16  ASP A OD2 1 
ATOM   106  N N   . VAL A 1 17  ? 26.103 -10.975 1.427   1.00 11.91  ? 17  VAL A N   1 
ATOM   107  C CA  . VAL A 1 17  ? 27.189 -10.204 0.868   1.00 12.11  ? 17  VAL A CA  1 
ATOM   108  C C   . VAL A 1 17  ? 28.390 -10.373 1.688   1.00 11.66  ? 17  VAL A C   1 
ATOM   109  O O   . VAL A 1 17  ? 28.400 -10.145 2.896   1.00 11.63  ? 17  VAL A O   1 
ATOM   110  C CB  . VAL A 1 17  ? 26.800 -8.686  0.776   1.00 13.06  ? 17  VAL A CB  1 
ATOM   111  C CG1 . VAL A 1 17  ? 27.988 -7.898  0.227   1.00 15.15  ? 17  VAL A CG1 1 
ATOM   112  C CG2 . VAL A 1 17  ? 25.527 -8.531  -0.054  1.00 16.08  ? 17  VAL A CG2 1 
ATOM   113  N N   . SER A 1 18  ? 29.423 -10.658 0.955   1.00 15.27  ? 18  SER A N   1 
ATOM   114  C CA  . SER A 1 18  ? 30.653 -10.714 1.553   1.00 15.35  ? 18  SER A CA  1 
ATOM   115  C C   . SER A 1 18  ? 31.738 -10.330 0.475   1.00 16.26  ? 18  SER A C   1 
ATOM   116  O O   . SER A 1 18  ? 32.013 -11.117 -0.464  1.00 21.01  ? 18  SER A O   1 
ATOM   117  C CB  . SER A 1 18  ? 30.932 -12.122 1.992   1.00 20.44  ? 18  SER A CB  1 
ATOM   118  O OG  . SER A 1 18  ? 32.157 -12.199 2.650   1.00 28.40  ? 18  SER A OG  1 
ATOM   119  N N   . ILE A 1 19  ? 32.348 -9.179  0.556   1.00 13.61  ? 19  ILE A N   1 
ATOM   120  C CA  . ILE A 1 19  ? 33.205 -8.613  -0.520  1.00 14.31  ? 19  ILE A CA  1 
ATOM   121  C C   . ILE A 1 19  ? 34.450 -8.016  0.317   1.00 13.64  ? 19  ILE A C   1 
ATOM   122  O O   . ILE A 1 19  ? 34.344 -7.504  1.493   1.00 15.15  ? 19  ILE A O   1 
ATOM   123  C CB  . ILE A 1 19  ? 32.384 -7.382  -1.234  1.00 15.06  ? 19  ILE A CB  1 
ATOM   124  C CG1 . ILE A 1 19  ? 31.230 -8.008  -2.102  1.00 18.61  ? 19  ILE A CG1 1 
ATOM   125  C CG2 . ILE A 1 19  ? 33.290 -6.608  -2.200  1.00 22.92  ? 19  ILE A CG2 1 
ATOM   126  C CD1 . ILE A 1 19  ? 30.270 -7.045  -2.714  1.00 20.54  ? 19  ILE A CD1 1 
ATOM   127  N N   . GLU A 1 20  ? 35.628 -7.936  -0.286  1.00 13.89  ? 20  GLU A N   1 
ATOM   128  C CA  . GLU A 1 20  ? 36.693 -6.996  0.080   1.00 14.16  ? 20  GLU A CA  1 
ATOM   129  C C   . GLU A 1 20  ? 37.012 -6.141  -1.171  1.00 13.48  ? 20  GLU A C   1 
ATOM   130  O O   . GLU A 1 20  ? 37.095 -6.656  -2.279  1.00 16.90  ? 20  GLU A O   1 
ATOM   131  C CB  . GLU A 1 20  ? 37.952 -7.713  0.561   1.00 17.87  ? 20  GLU A CB  1 
ATOM   132  C CG  . GLU A 1 20  ? 39.119 -6.822  0.946   1.00 24.39  ? 20  GLU A CG  1 
ATOM   133  C CD  . GLU A 1 20  ? 40.389 -7.553  1.322   1.00 30.34  ? 20  GLU A CD  1 
ATOM   134  O OE1 . GLU A 1 20  ? 41.394 -7.400  0.589   1.00 39.94  ? 20  GLU A OE1 1 
ATOM   135  O OE2 . GLU A 1 20  ? 40.358 -8.286  2.303   1.00 48.50  ? 20  GLU A OE2 1 
ATOM   136  N N   . ASP A 1 21  ? 37.148 -4.857  -0.955  1.00 11.46  ? 21  ASP A N   1 
ATOM   137  C CA  . ASP A 1 21  ? 37.493 -3.943  -2.033  1.00 11.20  ? 21  ASP A CA  1 
ATOM   138  C C   . ASP A 1 21  ? 38.551 -2.981  -1.524  1.00 10.69  ? 21  ASP A C   1 
ATOM   139  O O   . ASP A 1 21  ? 38.444 -2.415  -0.439  1.00 12.37  ? 21  ASP A O   1 
ATOM   140  C CB  . ASP A 1 21  ? 36.265 -3.175  -2.552  1.00 12.41  ? 21  ASP A CB  1 
ATOM   141  C CG  . ASP A 1 21  ? 36.547 -2.459  -3.859  1.00 13.75  ? 21  ASP A CG  1 
ATOM   142  O OD1 . ASP A 1 21  ? 36.388 -3.082  -4.943  1.00 18.50  ? 21  ASP A OD1 1 
ATOM   143  O OD2 . ASP A 1 21  ? 36.901 -1.273  -3.847  1.00 12.71  ? 21  ASP A OD2 1 
ATOM   144  N N   . SER A 1 22  ? 39.532 -2.708  -2.396  1.00 12.28  ? 22  SER A N   1 
ATOM   145  C CA  . SER A 1 22  ? 40.643 -1.804  -2.033  1.00 12.43  ? 22  SER A CA  1 
ATOM   146  C C   . SER A 1 22  ? 40.714 -0.529  -2.873  1.00 10.93  ? 22  SER A C   1 
ATOM   147  O O   . SER A 1 22  ? 41.648 0.239   -2.736  1.00 12.52  ? 22  SER A O   1 
ATOM   148  C CB  . SER A 1 22  ? 41.981 -2.555  -2.082  1.00 18.78  ? 22  SER A CB  1 
ATOM   149  O OG  . SER A 1 22  ? 41.944 -3.556  -1.070  1.00 25.58  ? 22  SER A OG  1 
ATOM   150  N N   . VAL A 1 23  ? 39.701 -0.312  -3.717  1.00 10.21  ? 23  VAL A N   1 
ATOM   151  C CA  . VAL A 1 23  ? 39.563 0.907   -4.442  1.00 9.96   ? 23  VAL A CA  1 
ATOM   152  C C   . VAL A 1 23  ? 38.780 1.919   -3.644  1.00 9.96   ? 23  VAL A C   1 
ATOM   153  O O   . VAL A 1 23  ? 39.181 3.073   -3.558  1.00 12.90  ? 23  VAL A O   1 
ATOM   154  C CB  . VAL A 1 23  ? 38.961 0.679   -5.846  1.00 12.09  ? 23  VAL A CB  1 
ATOM   155  C CG1 . VAL A 1 23  ? 38.834 1.994   -6.551  1.00 14.53  ? 23  VAL A CG1 1 
ATOM   156  C CG2 . VAL A 1 23  ? 39.751 -0.310  -6.650  1.00 13.61  ? 23  VAL A CG2 1 
ATOM   157  N N   . ILE A 1 24  ? 37.678 1.502   -3.008  1.00 9.89   ? 24  ILE A N   1 
ATOM   158  C CA  . ILE A 1 24  ? 36.991 2.336   -2.053  1.00 9.75   ? 24  ILE A CA  1 
ATOM   159  C C   . ILE A 1 24  ? 37.811 2.499   -0.755  1.00 10.06  ? 24  ILE A C   1 
ATOM   160  O O   . ILE A 1 24  ? 38.703 1.685   -0.440  1.00 10.94  ? 24  ILE A O   1 
ATOM   161  C CB  . ILE A 1 24  ? 35.570 1.811   -1.672  1.00 9.37   ? 24  ILE A CB  1 
ATOM   162  C CG1 . ILE A 1 24  ? 35.657 0.399   -1.084  1.00 9.96   ? 24  ILE A CG1 1 
ATOM   163  C CG2 . ILE A 1 24  ? 34.627 1.920   -2.831  1.00 10.25  ? 24  ILE A CG2 1 
ATOM   164  C CD1 . ILE A 1 24  ? 34.369 -0.050  -0.411  1.00 10.61  ? 24  ILE A CD1 1 
ATOM   165  N N   . SER A 1 25  ? 37.508 3.562   -0.014  1.00 8.93   ? 25  SER A N   1 
ATOM   166  C CA  . SER A 1 25  ? 38.090 3.811   1.289   1.00 8.85   ? 25  SER A CA  1 
ATOM   167  C C   . SER A 1 25  ? 37.032 4.426   2.211   1.00 9.03   ? 25  SER A C   1 
ATOM   168  O O   . SER A 1 25  ? 36.133 5.118   1.709   1.00 9.54   ? 25  SER A O   1 
ATOM   169  C CB  . SER A 1 25  ? 39.263 4.769   1.175   1.00 9.76   ? 25  SER A CB  1 
ATOM   170  O OG  . SER A 1 25  ? 39.922 4.906   2.444   1.00 10.56  ? 25  SER A OG  1 
ATOM   171  N N   . LEU A 1 26  ? 37.170 4.199   3.508   1.00 10.17  ? 26  LEU A N   1 
ATOM   172  C CA  . LEU A 1 26  ? 36.373 4.916   4.518   1.00 10.37  ? 26  LEU A CA  1 
ATOM   173  C C   . LEU A 1 26  ? 37.148 6.093   5.108   1.00 11.70  ? 26  LEU A C   1 
ATOM   174  O O   . LEU A 1 26  ? 36.668 6.662   6.083   1.00 15.37  ? 26  LEU A O   1 
ATOM   175  C CB  . LEU A 1 26  ? 35.933 3.979   5.645   1.00 10.38  ? 26  LEU A CB  1 
ATOM   176  C CG  . LEU A 1 26  ? 35.188 2.725   5.212   1.00 10.82  ? 26  LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 26  ? 34.784 1.918   6.429   1.00 11.33  ? 26  LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 26  ? 33.992 3.017   4.339   1.00 12.43  ? 26  LEU A CD2 1 
ATOM   179  N N   . SER A 1 27  ? 38.316 6.420   4.532   1.00 11.94  ? 27  SER A N   1 
ATOM   180  C CA  . SER A 1 27  ? 39.236 7.358   5.087   1.00 13.19  ? 27  SER A CA  1 
ATOM   181  C C   . SER A 1 27  ? 39.923 8.078   3.966   1.00 15.03  ? 27  SER A C   1 
ATOM   182  O O   . SER A 1 27  ? 39.539 7.980   2.825   1.00 12.77  ? 27  SER A O   1 
ATOM   183  C CB  . SER A 1 27  ? 40.246 6.642   6.026   1.00 15.25  ? 27  SER A CB  1 
ATOM   184  O OG  . SER A 1 27  ? 40.844 5.508   5.433   1.00 17.85  ? 27  SER A OG  1 
ATOM   185  N N   . GLY A 1 28  ? 41.006 8.781   4.279   1.00 19.29  ? 28  GLY A N   1 
ATOM   186  C CA  . GLY A 1 28  ? 41.762 9.535   3.297   1.00 17.65  ? 28  GLY A CA  1 
ATOM   187  C C   . GLY A 1 28  ? 40.918 10.684  2.781   1.00 16.47  ? 28  GLY A C   1 
ATOM   188  O O   . GLY A 1 28  ? 40.042 11.135  3.483   1.00 19.98  ? 28  GLY A O   1 
ATOM   189  N N   . ASP A 1 29  ? 41.206 11.213  1.575   1.00 15.91  ? 29  ASP A N   1 
ATOM   190  C CA  . ASP A 1 29  ? 40.503 12.375  1.075   1.00 17.38  ? 29  ASP A CA  1 
ATOM   191  C C   . ASP A 1 29  ? 39.380 12.111  0.166   1.00 17.40  ? 29  ASP A C   1 
ATOM   192  O O   . ASP A 1 29  ? 38.812 13.037  -0.292  1.00 19.90  ? 29  ASP A O   1 
ATOM   193  C CB  . ASP A 1 29  ? 41.513 13.370  0.423   1.00 20.96  ? 29  ASP A CB  1 
ATOM   194  C CG  . ASP A 1 29  ? 42.059 12.930  -0.887  1.00 19.10  ? 29  ASP A CG  1 
ATOM   195  O OD1 . ASP A 1 29  ? 41.551 12.044  -1.556  1.00 16.41  ? 29  ASP A OD1 1 
ATOM   196  O OD2 . ASP A 1 29  ? 43.034 13.609  -1.330  1.00 22.97  ? 29  ASP A OD2 1 
ATOM   197  N N   . HIS A 1 30  ? 39.023 10.832  -0.085  1.00 15.32  ? 30  HIS A N   1 
ATOM   198  C CA  . HIS A 1 30  ? 37.985 10.400  -1.031  1.00 13.47  ? 30  HIS A CA  1 
ATOM   199  C C   . HIS A 1 30  ? 37.092 9.289   -0.363  1.00 13.17  ? 30  HIS A C   1 
ATOM   200  O O   . HIS A 1 30  ? 36.591 8.358   -0.973  1.00 15.68  ? 30  HIS A O   1 
ATOM   201  C CB  . HIS A 1 30  ? 38.748 9.880   -2.216  1.00 20.17  ? 30  HIS A CB  1 
ATOM   202  C CG  . HIS A 1 30  ? 38.062 9.871   -3.490  1.00 25.19  ? 30  HIS A CG  1 
ATOM   203  N ND1 . HIS A 1 30  ? 38.594 10.479  -4.609  1.00 37.74  ? 30  HIS A ND1 1 
ATOM   204  C CD2 . HIS A 1 30  ? 36.895 9.310   -3.845  1.00 17.88  ? 30  HIS A CD2 1 
ATOM   205  C CE1 . HIS A 1 30  ? 37.769 10.272  -5.622  1.00 47.86  ? 30  HIS A CE1 1 
ATOM   206  N NE2 . HIS A 1 30  ? 36.734 9.558   -5.189  1.00 32.80  ? 30  HIS A NE2 1 
ATOM   207  N N   . SER A 1 31  ? 36.815 9.451   0.909   1.00 11.48  ? 31  SER A N   1 
ATOM   208  C CA  . SER A 1 31  ? 36.008 8.525   1.676   1.00 11.61  ? 31  SER A CA  1 
ATOM   209  C C   . SER A 1 31  ? 34.612 8.370   1.102   1.00 11.96  ? 31  SER A C   1 
ATOM   210  O O   . SER A 1 31  ? 33.958 9.352   0.690   1.00 12.49  ? 31  SER A O   1 
ATOM   211  C CB  . SER A 1 31  ? 35.891 9.024   3.111   1.00 13.67  ? 31  SER A CB  1 
ATOM   212  O OG  . SER A 1 31  ? 35.024 8.185   3.825   1.00 14.78  ? 31  SER A OG  1 
ATOM   213  N N   . ILE A 1 32  ? 34.061 7.139   1.138   1.00 10.45  ? 32  ILE A N   1 
ATOM   214  C CA  . ILE A 1 32  ? 32.693 6.898   0.746   1.00 9.90   ? 32  ILE A CA  1 
ATOM   215  C C   . ILE A 1 32  ? 31.660 7.171   1.871   1.00 9.40   ? 32  ILE A C   1 
ATOM   216  O O   . ILE A 1 32  ? 30.477 7.033   1.634   1.00 9.51   ? 32  ILE A O   1 
ATOM   217  C CB  . ILE A 1 32  ? 32.484 5.494   0.191   1.00 9.70   ? 32  ILE A CB  1 
ATOM   218  C CG1 . ILE A 1 32  ? 32.720 4.407   1.207   1.00 10.62  ? 32  ILE A CG1 1 
ATOM   219  C CG2 . ILE A 1 32  ? 33.291 5.300   -1.060  1.00 12.27  ? 32  ILE A CG2 1 
ATOM   220  C CD1 . ILE A 1 32  ? 32.384 3.018   0.729   1.00 11.05  ? 32  ILE A CD1 1 
ATOM   221  N N   . ILE A 1 33  ? 32.117 7.558   3.049   1.00 9.47   ? 33  ILE A N   1 
ATOM   222  C CA  . ILE A 1 33  ? 31.174 7.930   4.092   1.00 10.22  ? 33  ILE A CA  1 
ATOM   223  C C   . ILE A 1 33  ? 30.317 9.078   3.575   1.00 9.54   ? 33  ILE A C   1 
ATOM   224  O O   . ILE A 1 33  ? 30.792 10.061  3.043   1.00 10.85  ? 33  ILE A O   1 
ATOM   225  C CB  . ILE A 1 33  ? 31.919 8.359   5.366   1.00 11.27  ? 33  ILE A CB  1 
ATOM   226  C CG1 . ILE A 1 33  ? 32.783 7.334   5.941   1.00 15.88  ? 33  ILE A CG1 1 
ATOM   227  C CG2 . ILE A 1 33  ? 30.960 8.951   6.390   1.00 13.06  ? 33  ILE A CG2 1 
ATOM   228  C CD1 . ILE A 1 33  ? 32.021 6.217   6.404   1.00 17.41  ? 33  ILE A CD1 1 
ATOM   229  N N   . GLY A 1 34  ? 28.998 8.931   3.721   1.00 9.04   ? 34  GLY A N   1 
ATOM   230  C CA  . GLY A 1 34  ? 28.069 9.923   3.219   1.00 9.86   ? 34  GLY A CA  1 
ATOM   231  C C   . GLY A 1 34  ? 27.610 9.719   1.777   1.00 9.08   ? 34  GLY A C   1 
ATOM   232  O O   . GLY A 1 34  ? 26.746 10.446  1.334   1.00 10.26  ? 34  GLY A O   1 
ATOM   233  N N   . ARG A 1 35  ? 28.226 8.768   1.072   1.00 8.95   ? 35  ARG A N   1 
ATOM   234  C CA  . ARG A 1 35  ? 27.742 8.394   -0.233  1.00 8.94   ? 35  ARG A CA  1 
ATOM   235  C C   . ARG A 1 35  ? 26.599 7.432   -0.124  1.00 8.82   ? 35  ARG A C   1 
ATOM   236  O O   . ARG A 1 35  ? 26.416 6.760   0.884   1.00 10.27  ? 35  ARG A O   1 
ATOM   237  C CB  . ARG A 1 35  ? 28.886 7.862   -1.118  1.00 9.63   ? 35  ARG A CB  1 
ATOM   238  C CG  . ARG A 1 35  ? 30.023 8.817   -1.304  1.00 10.51  ? 35  ARG A CG  1 
ATOM   239  C CD  . ARG A 1 35  ? 29.669 9.962   -2.220  1.00 11.79  ? 35  ARG A CD  1 
ATOM   240  N NE  . ARG A 1 35  ? 30.854 10.812  -2.437  1.00 13.51  ? 35  ARG A NE  1 
ATOM   241  C CZ  . ARG A 1 35  ? 30.820 11.998  -2.969  1.00 13.54  ? 35  ARG A CZ  1 
ATOM   242  N NH1 . ARG A 1 35  ? 29.696 12.519  -3.380  1.00 14.80  ? 35  ARG A NH1 1 
ATOM   243  N NH2 . ARG A 1 35  ? 31.939 12.670  -3.061  1.00 18.49  ? 35  ARG A NH2 1 
ATOM   244  N N   . THR A 1 36  ? 25.846 7.247   -1.211  1.00 9.33   ? 36  THR A N   1 
ATOM   245  C CA  . THR A 1 36  ? 24.705 6.350   -1.260  1.00 9.37   ? 36  THR A CA  1 
ATOM   246  C C   . THR A 1 36  ? 25.093 5.023   -1.917  1.00 9.31   ? 36  THR A C   1 
ATOM   247  O O   . THR A 1 36  ? 25.594 5.002   -3.034  1.00 11.01  ? 36  THR A O   1 
ATOM   248  C CB  . THR A 1 36  ? 23.568 7.029   -2.023  1.00 11.28  ? 36  THR A CB  1 
ATOM   249  O OG1 . THR A 1 36  ? 23.138 8.176   -1.298  1.00 13.40  ? 36  THR A OG1 1 
ATOM   250  C CG2 . THR A 1 36  ? 22.364 6.109   -2.161  1.00 11.64  ? 36  THR A CG2 1 
ATOM   251  N N   . LEU A 1 37  ? 24.865 3.945   -1.188  1.00 8.51   ? 37  LEU A N   1 
ATOM   252  C CA  . LEU A 1 37  ? 24.982 2.596   -1.687  1.00 8.53   ? 37  LEU A CA  1 
ATOM   253  C C   . LEU A 1 37  ? 23.684 2.246   -2.439  1.00 9.25   ? 37  LEU A C   1 
ATOM   254  O O   . LEU A 1 37  ? 22.581 2.465   -1.909  1.00 10.05  ? 37  LEU A O   1 
ATOM   255  C CB  . LEU A 1 37  ? 25.224 1.654   -0.510  1.00 9.24   ? 37  LEU A CB  1 
ATOM   256  C CG  . LEU A 1 37  ? 25.415 0.177   -0.878  1.00 9.94   ? 37  LEU A CG  1 
ATOM   257  C CD1 . LEU A 1 37  ? 26.696 -0.036  -1.699  1.00 10.69  ? 37  LEU A CD1 1 
ATOM   258  C CD2 . LEU A 1 37  ? 25.453 -0.662  0.401   1.00 11.34  ? 37  LEU A CD2 1 
ATOM   259  N N   . VAL A 1 38  ? 23.813 1.613   -3.607  1.00 9.26   ? 38  VAL A N   1 
ATOM   260  C CA  . VAL A 1 38  ? 22.684 1.224   -4.404  1.00 10.29  ? 38  VAL A CA  1 
ATOM   261  C C   . VAL A 1 38  ? 22.761 -0.258  -4.832  1.00 10.59  ? 38  VAL A C   1 
ATOM   262  O O   . VAL A 1 38  ? 23.860 -0.786  -5.094  1.00 11.62  ? 38  VAL A O   1 
ATOM   263  C CB  . VAL A 1 38  ? 22.550 2.142   -5.634  1.00 14.53  ? 38  VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 38  ? 22.498 3.592   -5.293  1.00 15.01  ? 38  VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 38  ? 23.535 1.963   -6.707  1.00 18.91  ? 38  VAL A CG2 1 
ATOM   266  N N   . VAL A 1 39  ? 21.588 -0.853  -4.932  1.00 11.03  ? 39  VAL A N   1 
ATOM   267  C CA  . VAL A 1 39  ? 21.443 -2.160  -5.536  1.00 12.03  ? 39  VAL A CA  1 
ATOM   268  C C   . VAL A 1 39  ? 20.357 -2.065  -6.595  1.00 11.99  ? 39  VAL A C   1 
ATOM   269  O O   . VAL A 1 39  ? 19.281 -1.507  -6.396  1.00 12.38  ? 39  VAL A O   1 
ATOM   270  C CB  . VAL A 1 39  ? 21.178 -3.285  -4.499  1.00 13.08  ? 39  VAL A CB  1 
ATOM   271  C CG1 . VAL A 1 39  ? 19.920 -3.069  -3.725  1.00 14.25  ? 39  VAL A CG1 1 
ATOM   272  C CG2 . VAL A 1 39  ? 21.200 -4.665  -5.113  1.00 14.60  ? 39  VAL A CG2 1 
ATOM   273  N N   . HIS A 1 40  ? 20.638 -2.649  -7.766  1.00 12.52  ? 40  HIS A N   1 
ATOM   274  C CA  . HIS A 1 40  ? 19.586 -2.712  -8.798  1.00 14.11  ? 40  HIS A CA  1 
ATOM   275  C C   . HIS A 1 40  ? 18.540 -3.720  -8.353  1.00 17.26  ? 40  HIS A C   1 
ATOM   276  O O   . HIS A 1 40  ? 18.891 -4.883  -8.107  1.00 17.70  ? 40  HIS A O   1 
ATOM   277  C CB  . HIS A 1 40  ? 20.168 -3.224  -10.090 1.00 17.48  ? 40  HIS A CB  1 
ATOM   278  C CG  . HIS A 1 40  ? 20.844 -2.209  -10.862 1.00 17.82  ? 40  HIS A CG  1 
ATOM   279  N ND1 . HIS A 1 40  ? 20.877 -2.273  -12.239 1.00 26.71  ? 40  HIS A ND1 1 
ATOM   280  C CD2 . HIS A 1 40  ? 21.553 -1.125  -10.519 1.00 19.52  ? 40  HIS A CD2 1 
ATOM   281  C CE1 . HIS A 1 40  ? 21.546 -1.235  -12.715 1.00 28.86  ? 40  HIS A CE1 1 
ATOM   282  N NE2 . HIS A 1 40  ? 21.996 -0.531  -11.702 1.00 22.03  ? 40  HIS A NE2 1 
ATOM   283  N N   . GLU A 1 41  ? 17.264 -3.341  -8.408  1.00 16.46  ? 41  GLU A N   1 
ATOM   284  C CA  . GLU A 1 41  ? 16.218 -4.288  -8.143  1.00 17.53  ? 41  GLU A CA  1 
ATOM   285  C C   . GLU A 1 41  ? 15.963 -5.223  -9.311  1.00 18.85  ? 41  GLU A C   1 
ATOM   286  O O   . GLU A 1 41  ? 15.490 -6.329  -9.113  1.00 19.23  ? 41  GLU A O   1 
ATOM   287  C CB  . GLU A 1 41  ? 14.977 -3.533  -7.754  1.00 19.55  ? 41  GLU A CB  1 
ATOM   288  C CG  . GLU A 1 41  ? 15.164 -2.841  -6.386  1.00 20.36  ? 41  GLU A CG  1 
ATOM   289  C CD  . GLU A 1 41  ? 13.950 -2.094  -5.918  1.00 22.61  ? 41  GLU A CD  1 
ATOM   290  O OE1 . GLU A 1 41  ? 13.832 -1.828  -4.730  1.00 23.65  ? 41  GLU A OE1 1 
ATOM   291  O OE2 . GLU A 1 41  ? 13.091 -1.766  -6.756  1.00 31.39  ? 41  GLU A OE2 1 
ATOM   292  N N   . LYS A 1 42  ? 16.248 -4.819  -10.541 1.00 18.32  ? 42  LYS A N   1 
ATOM   293  C CA  . LYS A 1 42  ? 16.094 -5.738  -11.689 1.00 19.96  ? 42  LYS A CA  1 
ATOM   294  C C   . LYS A 1 42  ? 17.323 -6.666  -11.662 1.00 19.02  ? 42  LYS A C   1 
ATOM   295  O O   . LYS A 1 42  ? 18.463 -6.208  -11.518 1.00 21.84  ? 42  LYS A O   1 
ATOM   296  C CB  . LYS A 1 42  ? 16.099 -4.907  -12.959 1.00 21.93  ? 42  LYS A CB  1 
ATOM   297  C CG  . LYS A 1 42  ? 15.934 -5.702  -14.231 1.00 24.58  ? 42  LYS A CG  1 
ATOM   298  C CD  . LYS A 1 42  ? 15.961 -4.815  -15.474 1.00 31.33  ? 42  LYS A CD  1 
ATOM   299  C CE  . LYS A 1 42  ? 16.015 -5.692  -16.720 1.00 48.71  ? 42  LYS A CE  1 
ATOM   300  N NZ  . LYS A 1 42  ? 15.571 -5.028  -17.981 1.00 66.97  ? 42  LYS A NZ  1 
ATOM   301  N N   . ALA A 1 43  ? 17.047 -7.948  -11.886 1.00 19.68  ? 43  ALA A N   1 
ATOM   302  C CA  . ALA A 1 43  ? 18.108 -8.944  -11.979 1.00 20.45  ? 43  ALA A CA  1 
ATOM   303  C C   . ALA A 1 43  ? 18.763 -8.842  -13.362 1.00 21.71  ? 43  ALA A C   1 
ATOM   304  O O   . ALA A 1 43  ? 18.085 -8.538  -14.341 1.00 24.76  ? 43  ALA A O   1 
ATOM   305  C CB  . ALA A 1 43  ? 17.531 -10.339 -11.770 1.00 23.47  ? 43  ALA A CB  1 
ATOM   306  N N   . GLY A 1 44  ? 20.081 -9.057  -13.428 1.00 21.32  ? 44  GLY A N   1 
ATOM   307  C CA  . GLY A 1 44  ? 20.814 -9.065  -14.671 1.00 25.87  ? 44  GLY A CA  1 
ATOM   308  C C   . GLY A 1 44  ? 21.138 -7.679  -15.194 1.00 26.46  ? 44  GLY A C   1 
ATOM   309  O O   . GLY A 1 44  ? 20.990 -6.668  -14.484 1.00 31.02  ? 44  GLY A O   1 
ATOM   310  N N   . ALA A 1 45  ? 21.583 -7.637  -16.444 1.00 29.78  ? 45  ALA A N   1 
ATOM   311  C CA  . ALA A 1 45  ? 22.289 -6.476  -17.004 1.00 33.04  ? 45  ALA A CA  1 
ATOM   312  C C   . ALA A 1 45  ? 21.379 -5.436  -17.648 1.00 35.34  ? 45  ALA A C   1 
ATOM   313  O O   . ALA A 1 45  ? 21.870 -4.386  -18.106 1.00 38.49  ? 45  ALA A O   1 
ATOM   314  C CB  . ALA A 1 45  ? 23.323 -6.946  -18.012 1.00 42.00  ? 45  ALA A CB  1 
ATOM   315  N N   . GLY A 1 46  ? 20.067 -5.710  -17.672 1.00 38.48  ? 46  GLY A N   1 
ATOM   316  C CA  . GLY A 1 46  ? 19.109 -4.893  -18.465 1.00 29.93  ? 46  GLY A CA  1 
ATOM   317  C C   . GLY A 1 46  ? 18.943 -3.482  -17.911 1.00 34.86  ? 46  GLY A C   1 
ATOM   318  O O   . GLY A 1 46  ? 19.144 -3.222  -16.701 1.00 33.26  ? 46  GLY A O   1 
ATOM   319  N N   . ALA A 1 47  ? 18.598 -2.535  -18.785 1.00 34.83  ? 47  ALA A N   1 
ATOM   320  C CA  . ALA A 1 47  ? 18.366 -1.119  -18.412 1.00 33.60  ? 47  ALA A CA  1 
ATOM   321  C C   . ALA A 1 47  ? 17.021 -0.981  -17.695 1.00 33.76  ? 47  ALA A C   1 
ATOM   322  O O   . ALA A 1 47  ? 16.172 -1.910  -17.781 1.00 38.19  ? 47  ALA A O   1 
ATOM   323  C CB  . ALA A 1 47  ? 18.361 -0.260  -19.678 1.00 33.86  ? 47  ALA A CB  1 
ATOM   324  N N   . GLY A 1 48  ? 16.837 0.148   -16.984 1.00 38.94  ? 48  GLY A N   1 
ATOM   325  C CA  . GLY A 1 48  ? 15.526 0.500   -16.396 1.00 43.87  ? 48  GLY A CA  1 
ATOM   326  C C   . GLY A 1 48  ? 15.218 -0.085  -15.029 1.00 32.45  ? 48  GLY A C   1 
ATOM   327  O O   . GLY A 1 48  ? 14.066 -0.114  -14.572 1.00 37.85  ? 48  GLY A O   1 
ATOM   328  N N   . SER A 1 49  ? 16.249 -0.538  -14.335 1.00 29.03  ? 49  SER A N   1 
ATOM   329  C CA  . SER A 1 49  ? 16.049 -1.014  -13.012 1.00 25.58  ? 49  SER A CA  1 
ATOM   330  C C   . SER A 1 49  ? 15.598 0.050   -12.026 1.00 21.42  ? 49  SER A C   1 
ATOM   331  O O   . SER A 1 49  ? 16.106 1.171   -11.913 1.00 27.58  ? 49  SER A O   1 
ATOM   332  C CB  . SER A 1 49  ? 17.365 -1.690  -12.499 1.00 23.62  ? 49  SER A CB  1 
ATOM   333  O OG  . SER A 1 49  ? 17.201 -2.230  -11.268 1.00 21.86  ? 49  SER A OG  1 
ATOM   334  N N   . ARG A 1 50  ? 14.716 -0.322  -11.112 1.00 25.74  ? 50  ARG A N   1 
ATOM   335  C CA  . ARG A 1 50  ? 14.527 0.539   -9.978  1.00 22.38  ? 50  ARG A CA  1 
ATOM   336  C C   . ARG A 1 50  ? 15.739 0.311   -9.045  1.00 18.83  ? 50  ARG A C   1 
ATOM   337  O O   . ARG A 1 50  ? 16.430 -0.725  -9.176  1.00 18.67  ? 50  ARG A O   1 
ATOM   338  C CB  . ARG A 1 50  ? 13.160 0.210   -9.376  1.00 27.78  ? 50  ARG A CB  1 
ATOM   339  C CG  . ARG A 1 50  ? 11.995 0.537   -10.330 1.00 32.67  ? 50  ARG A CG  1 
ATOM   340  C CD  . ARG A 1 50  ? 10.690 0.617   -9.555  1.00 49.53  ? 50  ARG A CD  1 
ATOM   341  N NE  . ARG A 1 50  ? 9.648  1.283   -10.339 1.00 56.92  ? 50  ARG A NE  1 
ATOM   342  C CZ  . ARG A 1 50  ? 8.757  2.175   -9.883  1.00 73.93  ? 50  ARG A CZ  1 
ATOM   343  N NH1 . ARG A 1 50  ? 8.759  2.594   -8.614  1.00 83.81  ? 50  ARG A NH1 1 
ATOM   344  N NH2 . ARG A 1 50  ? 7.850  2.664   -10.722 1.00 83.25  ? 50  ARG A NH2 1 
ATOM   345  N N   . LEU A 1 51  ? 15.963 1.188   -8.088  1.00 18.36  ? 51  LEU A N   1 
ATOM   346  C CA  . LEU A 1 51  ? 17.114 1.067   -7.146  1.00 15.61  ? 51  LEU A CA  1 
ATOM   347  C C   . LEU A 1 51  ? 16.612 0.931   -5.749  1.00 16.01  ? 51  LEU A C   1 
ATOM   348  O O   . LEU A 1 51  ? 15.677 1.675   -5.352  1.00 20.16  ? 51  LEU A O   1 
ATOM   349  C CB  . LEU A 1 51  ? 17.989 2.310   -7.207  1.00 16.31  ? 51  LEU A CB  1 
ATOM   350  C CG  . LEU A 1 51  ? 18.557 2.645   -8.585  1.00 19.50  ? 51  LEU A CG  1 
ATOM   351  C CD1 . LEU A 1 51  ? 19.376 3.920   -8.469  1.00 23.80  ? 51  LEU A CD1 1 
ATOM   352  C CD2 . LEU A 1 51  ? 19.322 1.458   -9.153  1.00 19.25  ? 51  LEU A CD2 1 
ATOM   353  N N   . ALA A 1 52  ? 17.249 0.110   -4.931  1.00 13.03  ? 52  ALA A N   1 
ATOM   354  C CA  . ALA A 1 52  ? 17.145 0.221   -3.447  1.00 13.05  ? 52  ALA A CA  1 
ATOM   355  C C   . ALA A 1 52  ? 18.449 0.880   -3.048  1.00 11.88  ? 52  ALA A C   1 
ATOM   356  O O   . ALA A 1 52  ? 19.500 0.666   -3.621  1.00 13.91  ? 52  ALA A O   1 
ATOM   357  C CB  . ALA A 1 52  ? 16.986 -1.151  -2.831  1.00 15.58  ? 52  ALA A CB  1 
ATOM   358  N N   . SER A 1 53  ? 18.379 1.717   -2.005  1.00 11.11  ? 53  SER A N   1 
ATOM   359  C CA  . SER A 1 53  ? 19.509 2.562   -1.665  1.00 11.13  ? 53  SER A CA  1 
ATOM   360  C C   . SER A 1 53  ? 19.540 2.905   -0.204  1.00 10.07  ? 53  SER A C   1 
ATOM   361  O O   . SER A 1 53  ? 18.517 2.839   0.490   1.00 11.36  ? 53  SER A O   1 
ATOM   362  C CB  . SER A 1 53  ? 19.503 3.772   -2.528  1.00 14.12  ? 53  SER A CB  1 
ATOM   363  O OG  . SER A 1 53  ? 18.450 4.634   -2.258  1.00 19.19  ? 53  SER A OG  1 
ATOM   364  N N   . GLY A 1 54  ? 20.688 3.341   0.252   1.00 10.48  ? 54  GLY A N   1 
ATOM   365  C CA  . GLY A 1 54  ? 20.832 3.870   1.580   1.00 10.46  ? 54  GLY A CA  1 
ATOM   366  C C   . GLY A 1 54  ? 22.154 4.623   1.680   1.00 9.26   ? 54  GLY A C   1 
ATOM   367  O O   . GLY A 1 54  ? 23.131 4.257   1.070   1.00 9.77   ? 54  GLY A O   1 
ATOM   368  N N   . VAL A 1 55  ? 22.159 5.625   2.547   1.00 9.13   ? 55  VAL A N   1 
ATOM   369  C CA  . VAL A 1 55  ? 23.364 6.428   2.773   1.00 8.92   ? 55  VAL A CA  1 
ATOM   370  C C   . VAL A 1 55  ? 24.320 5.696   3.705   1.00 8.55   ? 55  VAL A C   1 
ATOM   371  O O   . VAL A 1 55  ? 23.911 5.116   4.710   1.00 10.25  ? 55  VAL A O   1 
ATOM   372  C CB  . VAL A 1 55  ? 23.014 7.811   3.345   1.00 10.85  ? 55  VAL A CB  1 
ATOM   373  C CG1 . VAL A 1 55  ? 24.257 8.661   3.567   1.00 11.66  ? 55  VAL A CG1 1 
ATOM   374  C CG2 . VAL A 1 55  ? 22.043 8.549   2.408   1.00 13.53  ? 55  VAL A CG2 1 
ATOM   375  N N   . ILE A 1 56  ? 25.594 5.715   3.381   1.00 8.47   ? 56  ILE A N   1 
ATOM   376  C CA  . ILE A 1 56  ? 26.617 5.073   4.186   1.00 8.34   ? 56  ILE A CA  1 
ATOM   377  C C   . ILE A 1 56  ? 26.941 5.972   5.399   1.00 8.98   ? 56  ILE A C   1 
ATOM   378  O O   . ILE A 1 56  ? 27.476 7.078   5.243   1.00 10.80  ? 56  ILE A O   1 
ATOM   379  C CB  . ILE A 1 56  ? 27.881 4.802   3.347   1.00 8.34   ? 56  ILE A CB  1 
ATOM   380  C CG1 . ILE A 1 56  ? 27.543 3.879   2.196   1.00 9.38   ? 56  ILE A CG1 1 
ATOM   381  C CG2 . ILE A 1 56  ? 28.983 4.238   4.209   1.00 9.67   ? 56  ILE A CG2 1 
ATOM   382  C CD1 . ILE A 1 56  ? 28.615 3.757   1.155   1.00 10.26  ? 56  ILE A CD1 1 
ATOM   383  N N   . GLY A 1 57  ? 26.545 5.530   6.581   1.00 8.46   ? 57  GLY A N   1 
ATOM   384  C CA  . GLY A 1 57  ? 26.686 6.300   7.788   1.00 8.90   ? 57  GLY A CA  1 
ATOM   385  C C   . GLY A 1 57  ? 27.801 5.778   8.662   1.00 10.03  ? 57  GLY A C   1 
ATOM   386  O O   . GLY A 1 57  ? 28.080 4.575   8.740   1.00 13.13  ? 57  GLY A O   1 
ATOM   387  N N   . ILE A 1 58  ? 28.446 6.664   9.382   1.00 9.90   ? 58  ILE A N   1 
ATOM   388  C CA  . ILE A 1 58  ? 29.501 6.307   10.304  1.00 10.42  ? 58  ILE A CA  1 
ATOM   389  C C   . ILE A 1 58  ? 28.947 5.555   11.454  1.00 10.75  ? 58  ILE A C   1 
ATOM   390  O O   . ILE A 1 58  ? 27.922 5.944   12.085  1.00 13.31  ? 58  ILE A O   1 
ATOM   391  C CB  . ILE A 1 58  ? 30.200 7.505   10.910  1.00 15.09  ? 58  ILE A CB  1 
ATOM   392  C CG1 . ILE A 1 58  ? 30.813 8.412   9.923   1.00 17.99  ? 58  ILE A CG1 1 
ATOM   393  C CG2 . ILE A 1 58  ? 31.254 7.100   11.880  1.00 20.57  ? 58  ILE A CG2 1 
ATOM   394  C CD1 . ILE A 1 58  ? 31.133 9.838   10.374  1.00 18.88  ? 58  ILE A CD1 1 
ATOM   395  N N   . ALA A 1 59  ? 29.638 4.511   11.848  1.00 12.23  ? 59  ALA A N   1 
ATOM   396  C CA  . ALA A 1 59  ? 29.373 3.815   13.104  1.00 15.10  ? 59  ALA A CA  1 
ATOM   397  C C   . ALA A 1 59  ? 30.598 3.986   14.050  1.00 16.39  ? 59  ALA A C   1 
ATOM   398  O O   . ALA A 1 59  ? 31.693 4.017   13.576  1.00 20.00  ? 59  ALA A O   1 
ATOM   399  C CB  . ALA A 1 59  ? 29.153 2.343   12.797  1.00 17.42  ? 59  ALA A CB  1 
ATOM   400  N N   . GLN A 1 60  ? 30.373 4.193   15.335  1.00 20.06  ? 60  GLN A N   1 
ATOM   401  C CA  . GLN A 1 60  ? 31.559 4.200   16.305  1.00 22.56  ? 60  GLN A CA  1 
ATOM   402  C C   . GLN A 1 60  ? 32.542 2.970   16.150  1.00 28.99  ? 60  GLN A C   1 
ATOM   403  O O   . GLN A 1 60  ? 32.165 1.833   16.082  1.00 28.63  ? 60  GLN A O   1 
ATOM   404  C CB  . GLN A 1 60  ? 31.058 4.253   17.754  1.00 21.22  ? 60  GLN A CB  1 
ATOM   405  C CG  . GLN A 1 60  ? 31.953 4.788   18.830  1.00 27.51  ? 60  GLN A CG  1 
ATOM   406  C CD  . GLN A 1 60  ? 31.235 4.996   20.161  1.00 33.63  ? 60  GLN A CD  1 
ATOM   407  O OE1 . GLN A 1 60  ? 30.672 6.090   20.440  1.00 38.29  ? 60  GLN A OE1 1 
ATOM   408  N NE2 . GLN A 1 60  ? 31.230 3.950   20.988  1.00 33.20  ? 60  GLN A NE2 1 
ATOM   409  N N   . ALA A 1 61  ? 33.832 3.285   16.039  1.00 29.73  ? 61  ALA A N   1 
ATOM   410  C CA  . ALA A 1 61  ? 34.871 2.211   15.958  1.00 28.09  ? 61  ALA A CA  1 
ATOM   411  C C   . ALA A 1 61  ? 36.104 2.531   16.839  1.00 41.43  ? 61  ALA A C   1 
ATOM   412  O O   . ALA A 1 61  ? 35.932 3.006   17.969  1.00 51.60  ? 61  ALA A O   1 
ATOM   413  C CB  . ALA A 1 61  ? 35.278 1.891   14.539  1.00 30.78  ? 61  ALA A CB  1 
ATOM   414  N N   . GLY A 1 62  ? 37.329 2.246   16.329  1.00 60.75  ? 62  GLY A N   1 
ATOM   415  C CA  . GLY A 1 62  ? 38.630 2.565   17.000  1.00 64.64  ? 62  GLY A CA  1 
ATOM   416  C C   . GLY A 1 62  ? 39.474 3.689   16.357  1.00 73.03  ? 62  GLY A C   1 
ATOM   417  O O   . GLY A 1 62  ? 38.947 4.806   16.114  1.00 80.76  ? 62  GLY A O   1 
ATOM   418  N N   . ALA A 1 63  ? 40.745 3.358   16.035  1.00 65.88  ? 63  ALA A N   1 
ATOM   419  C CA  . ALA A 1 63  ? 41.917 4.299   15.902  1.00 48.98  ? 63  ALA A CA  1 
ATOM   420  C C   . ALA A 1 63  ? 42.753 4.032   14.622  1.00 44.12  ? 63  ALA A C   1 
ATOM   421  O O   . ALA A 1 63  ? 43.578 3.088   14.562  1.00 55.26  ? 63  ALA A O   1 
ATOM   422  C CB  . ALA A 1 63  ? 42.831 4.166   17.109  1.00 55.30  ? 63  ALA A CB  1 
ATOM   423  N N   . GLY A 1 64  ? 42.556 4.878   13.615  1.00 34.01  ? 64  GLY A N   1 
ATOM   424  C CA  . GLY A 1 64  ? 42.869 4.523   12.229  1.00 35.88  ? 64  GLY A CA  1 
ATOM   425  C C   . GLY A 1 64  ? 41.835 3.584   11.655  1.00 28.74  ? 64  GLY A C   1 
ATOM   426  O O   . GLY A 1 64  ? 41.814 3.425   10.408  1.00 36.24  ? 64  GLY A O   1 
ATOM   427  N N   . ALA A 1 65  ? 40.948 2.968   12.519  1.00 28.40  ? 65  ALA A N   1 
ATOM   428  C CA  . ALA A 1 65  ? 39.880 2.112   12.031  1.00 24.29  ? 65  ALA A CA  1 
ATOM   429  C C   . ALA A 1 65  ? 38.618 2.879   11.885  1.00 20.82  ? 65  ALA A C   1 
ATOM   430  O O   . ALA A 1 65  ? 38.353 3.873   12.579  1.00 22.07  ? 65  ALA A O   1 
ATOM   431  C CB  . ALA A 1 65  ? 39.634 0.920   12.927  1.00 23.97  ? 65  ALA A CB  1 
ATOM   432  N N   . THR A 1 66  ? 37.781 2.328   11.020  1.00 20.06  ? 66  THR A N   1 
ATOM   433  C CA  . THR A 1 66  ? 36.513 2.985   10.718  1.00 16.60  ? 66  THR A CA  1 
ATOM   434  C C   . THR A 1 66  ? 35.532 1.880   10.404  1.00 12.06  ? 66  THR A C   1 
ATOM   435  O O   . THR A 1 66  ? 35.846 0.907   9.728   1.00 12.67  ? 66  THR A O   1 
ATOM   436  C CB  . THR A 1 66  ? 36.664 4.002   9.488   1.00 18.20  ? 66  THR A CB  1 
ATOM   437  O OG1 . THR A 1 66  ? 37.765 4.889   9.683   1.00 25.03  ? 66  THR A OG1 1 
ATOM   438  C CG2 . THR A 1 66  ? 35.349 4.774   9.281   1.00 22.77  ? 66  THR A CG2 1 
ATOM   439  N N   . LYS A 1 67  ? 34.309 2.109   10.830  1.00 13.15  ? 67  LYS A N   1 
ATOM   440  C CA  . LYS A 1 67  ? 33.194 1.248   10.515  1.00 13.24  ? 67  LYS A CA  1 
ATOM   441  C C   . LYS A 1 67  ? 32.064 2.114   10.031  1.00 11.51  ? 67  LYS A C   1 
ATOM   442  O O   . LYS A 1 67  ? 31.886 3.208   10.543  1.00 14.49  ? 67  LYS A O   1 
ATOM   443  C CB  . LYS A 1 67  ? 32.792 0.403   11.695  1.00 14.45  ? 67  LYS A CB  1 
ATOM   444  C CG  . LYS A 1 67  ? 33.945 -0.492  12.148  1.00 15.12  ? 67  LYS A CG  1 
ATOM   445  C CD  . LYS A 1 67  ? 33.549 -1.286  13.371  1.00 16.76  ? 67  LYS A CD  1 
ATOM   446  C CE  . LYS A 1 67  ? 34.718 -2.010  14.004  1.00 24.12  ? 67  LYS A CE  1 
ATOM   447  N NZ  . LYS A 1 67  ? 35.330 -2.874  13.005  1.00 30.66  ? 67  LYS A NZ  1 
ATOM   448  N N   . ALA A 1 68  ? 31.259 1.586   9.108   1.00 10.33  ? 68  ALA A N   1 
ATOM   449  C CA  . ALA A 1 68  ? 30.129 2.311   8.575   1.00 9.94   ? 68  ALA A CA  1 
ATOM   450  C C   . ALA A 1 68  ? 29.022 1.312   8.228   1.00 9.35   ? 68  ALA A C   1 
ATOM   451  O O   . ALA A 1 68  ? 29.264 0.128   8.116   1.00 10.28  ? 68  ALA A O   1 
ATOM   452  C CB  . ALA A 1 68  ? 30.537 3.087   7.341   1.00 12.51  ? 68  ALA A CB  1 
ATOM   453  N N   . VAL A 1 69  ? 27.813 1.815   8.077   1.00 9.46   ? 69  VAL A N   1 
ATOM   454  C CA  . VAL A 1 69  ? 26.655 0.994   7.829   1.00 9.37   ? 69  VAL A CA  1 
ATOM   455  C C   . VAL A 1 69  ? 25.716 1.730   6.869   1.00 8.62   ? 69  VAL A C   1 
ATOM   456  O O   . VAL A 1 69  ? 25.474 2.920   7.037   1.00 9.58   ? 69  VAL A O   1 
ATOM   457  C CB  . VAL A 1 69  ? 25.880 0.669   9.137   1.00 12.00  ? 69  VAL A CB  1 
ATOM   458  C CG1 . VAL A 1 69  ? 24.674 -0.195  8.874   1.00 13.55  ? 69  VAL A CG1 1 
ATOM   459  C CG2 . VAL A 1 69  ? 26.735 0.092   10.201  1.00 15.27  ? 69  VAL A CG2 1 
ATOM   460  N N   . ALA A 1 70  ? 25.189 1.013   5.883   1.00 8.95   ? 70  ALA A N   1 
ATOM   461  C CA  . ALA A 1 70  ? 24.116 1.519   5.019   1.00 8.79   ? 70  ALA A CA  1 
ATOM   462  C C   . ALA A 1 70  ? 22.900 0.654   5.248   1.00 9.08   ? 70  ALA A C   1 
ATOM   463  O O   . ALA A 1 70  ? 22.962 -0.584  5.115   1.00 9.94   ? 70  ALA A O   1 
ATOM   464  C CB  . ALA A 1 70  ? 24.513 1.462   3.558   1.00 9.95   ? 70  ALA A CB  1 
ATOM   465  N N   . VAL A 1 71  ? 21.762 1.300   5.498   1.00 10.06  ? 71  VAL A N   1 
ATOM   466  C CA  . VAL A 1 71  ? 20.469 0.648   5.588   1.00 10.73  ? 71  VAL A CA  1 
ATOM   467  C C   . VAL A 1 71  ? 19.797 0.831   4.247   1.00 10.32  ? 71  VAL A C   1 
ATOM   468  O O   . VAL A 1 71  ? 19.490 1.944   3.828   1.00 12.13  ? 71  VAL A O   1 
ATOM   469  C CB  . VAL A 1 71  ? 19.623 1.221   6.718   1.00 12.39  ? 71  VAL A CB  1 
ATOM   470  C CG1 . VAL A 1 71  ? 18.281 0.528   6.772   1.00 15.42  ? 71  VAL A CG1 1 
ATOM   471  C CG2 . VAL A 1 71  ? 20.323 1.077   8.065   1.00 14.82  ? 71  VAL A CG2 1 
ATOM   472  N N   . LEU A 1 72  ? 19.625 -0.263  3.506   1.00 12.64  ? 72  LEU A N   1 
ATOM   473  C CA  . LEU A 1 72  ? 19.054 -0.188  2.163   1.00 13.01  ? 72  LEU A CA  1 
ATOM   474  C C   . LEU A 1 72  ? 17.555 -0.305  2.230   1.00 13.59  ? 72  LEU A C   1 
ATOM   475  O O   . LEU A 1 72  ? 17.013 -1.161  2.915   1.00 15.26  ? 72  LEU A O   1 
ATOM   476  C CB  . LEU A 1 72  ? 19.626 -1.303  1.267   1.00 14.08  ? 72  LEU A CB  1 
ATOM   477  C CG  . LEU A 1 72  ? 21.115 -1.307  0.974   1.00 14.11  ? 72  LEU A CG  1 
ATOM   478  C CD1 . LEU A 1 72  ? 21.536 -2.592  0.250   1.00 16.71  ? 72  LEU A CD1 1 
ATOM   479  C CD2 . LEU A 1 72  ? 21.480 -0.105  0.128   1.00 19.60  ? 72  LEU A CD2 1 
ATOM   480  N N   . LYS A 1 73  ? 16.878 0.550   1.488   1.00 13.67  ? 73  LYS A N   1 
ATOM   481  C CA  . LYS A 1 73  ? 15.429 0.516   1.372   1.00 16.05  ? 73  LYS A CA  1 
ATOM   482  C C   . LYS A 1 73  ? 15.068 0.722   -0.065  1.00 15.95  ? 73  LYS A C   1 
ATOM   483  O O   . LYS A 1 73  ? 15.622 1.589   -0.752  1.00 15.64  ? 73  LYS A O   1 
ATOM   484  C CB  . LYS A 1 73  ? 14.777 1.604   2.224   1.00 19.12  ? 73  LYS A CB  1 
ATOM   485  C CG  . LYS A 1 73  ? 13.278 1.634   2.085   1.00 28.91  ? 73  LYS A CG  1 
ATOM   486  C CD  . LYS A 1 73  ? 12.561 0.435   2.714   1.00 35.25  ? 73  LYS A CD  1 
ATOM   487  C CE  . LYS A 1 73  ? 11.033 0.568   2.702   1.00 38.30  ? 73  LYS A CE  1 
ATOM   488  N NZ  . LYS A 1 73  ? 10.471 -0.483  3.588   1.00 49.12  ? 73  LYS A NZ  1 
ATOM   489  N N   . GLY A 1 74  ? 14.191 -0.182  -0.537  1.00 19.43  ? 74  GLY A N   1 
ATOM   490  C CA  . GLY A 1 74  ? 13.630 -0.110  -1.861  1.00 21.31  ? 74  GLY A CA  1 
ATOM   491  C C   . GLY A 1 74  ? 12.154 -0.390  -1.817  1.00 23.55  ? 74  GLY A C   1 
ATOM   492  O O   . GLY A 1 74  ? 11.474 -0.203  -0.774  1.00 35.82  ? 74  GLY A O   1 
ATOM   493  N N   . ASP A 1 75  ? 11.650 -0.769  -2.986  1.00 24.52  ? 75  ASP A N   1 
ATOM   494  C CA  . ASP A 1 75  ? 10.221 -1.027  -3.247  1.00 25.26  ? 75  ASP A CA  1 
ATOM   495  C C   . ASP A 1 75  ? 9.797  -2.380  -2.655  1.00 32.68  ? 75  ASP A C   1 
ATOM   496  O O   . ASP A 1 75  ? 10.580 -3.365  -2.612  1.00 30.09  ? 75  ASP A O   1 
ATOM   497  C CB  . ASP A 1 75  ? 10.010 -1.066  -4.736  1.00 31.66  ? 75  ASP A CB  1 
ATOM   498  C CG  . ASP A 1 75  ? 10.472 0.216   -5.419  1.00 31.38  ? 75  ASP A CG  1 
ATOM   499  O OD1 . ASP A 1 75  ? 9.832  1.282   -5.215  1.00 39.20  ? 75  ASP A OD1 1 
ATOM   500  O OD2 . ASP A 1 75  ? 11.460 0.163   -6.185  1.00 38.45  ? 75  ASP A OD2 1 
ATOM   501  N N   . GLY A 1 76  ? 8.544  -2.384  -2.213  1.00 39.56  ? 76  GLY A N   1 
ATOM   502  C CA  . GLY A 1 76  ? 7.911  -3.562  -1.620  1.00 39.31  ? 76  GLY A CA  1 
ATOM   503  C C   . GLY A 1 76  ? 8.824  -4.152  -0.553  1.00 31.50  ? 76  GLY A C   1 
ATOM   504  O O   . GLY A 1 76  ? 9.229  -3.453  0.392   1.00 39.68  ? 76  GLY A O   1 
ATOM   505  N N   . PRO A 1 77  ? 9.239  -5.406  -0.740  1.00 32.71  ? 77  PRO A N   1 
ATOM   506  C CA  . PRO A 1 77  ? 9.969  -6.018  0.355   1.00 27.39  ? 77  PRO A CA  1 
ATOM   507  C C   . PRO A 1 77  ? 11.510 -5.755  0.308   1.00 28.36  ? 77  PRO A C   1 
ATOM   508  O O   . PRO A 1 77  ? 12.150 -6.327  1.134   1.00 27.97  ? 77  PRO A O   1 
ATOM   509  C CB  . PRO A 1 77  ? 9.684  -7.519  0.158   1.00 33.87  ? 77  PRO A CB  1 
ATOM   510  C CG  . PRO A 1 77  ? 9.446  -7.673  -1.328  1.00 46.34  ? 77  PRO A CG  1 
ATOM   511  C CD  . PRO A 1 77  ? 9.184  -6.296  -1.911  1.00 37.16  ? 77  PRO A CD  1 
ATOM   512  N N   . VAL A 1 78  ? 12.072 -4.939  -0.588  1.00 28.43  ? 78  VAL A N   1 
ATOM   513  C CA  . VAL A 1 78  ? 13.549 -4.853  -0.633  1.00 20.04  ? 78  VAL A CA  1 
ATOM   514  C C   . VAL A 1 78  ? 14.106 -4.037  0.528   1.00 19.19  ? 78  VAL A C   1 
ATOM   515  O O   . VAL A 1 78  ? 13.819 -2.845  0.686   1.00 22.59  ? 78  VAL A O   1 
ATOM   516  C CB  . VAL A 1 78  ? 14.100 -4.361  -2.002  1.00 24.66  ? 78  VAL A CB  1 
ATOM   517  C CG1 . VAL A 1 78  ? 15.620 -4.282  -1.980  1.00 22.10  ? 78  VAL A CG1 1 
ATOM   518  C CG2 . VAL A 1 78  ? 13.601 -5.235  -3.145  1.00 24.54  ? 78  VAL A CG2 1 
ATOM   519  N N   . GLN A 1 79  ? 14.982 -4.674  1.287   1.00 16.62  ? 79  GLN A N   1 
ATOM   520  C CA  . GLN A 1 79  ? 15.589 -4.023  2.409   1.00 17.09  ? 79  GLN A CA  1 
ATOM   521  C C   . GLN A 1 79  ? 16.842 -4.790  2.814   1.00 13.75  ? 79  GLN A C   1 
ATOM   522  O O   . GLN A 1 79  ? 16.919 -6.010  2.644   1.00 15.41  ? 79  GLN A O   1 
ATOM   523  C CB  . GLN A 1 79  ? 14.644 -3.892  3.571   1.00 22.59  ? 79  GLN A CB  1 
ATOM   524  C CG  . GLN A 1 79  ? 14.113 -5.170  4.147   1.00 27.79  ? 79  GLN A CG  1 
ATOM   525  C CD  . GLN A 1 79  ? 13.110 -4.864  5.228   1.00 38.05  ? 79  GLN A CD  1 
ATOM   526  O OE1 . GLN A 1 79  ? 13.462 -4.430  6.320   1.00 66.80  ? 79  GLN A OE1 1 
ATOM   527  N NE2 . GLN A 1 79  ? 11.852 -5.047  4.917   1.00 47.26  ? 79  GLN A NE2 1 
ATOM   528  N N   . GLY A 1 80  ? 17.812 -4.104  3.370   1.00 12.51  ? 80  GLY A N   1 
ATOM   529  C CA  . GLY A 1 80  ? 18.965 -4.763  3.895   1.00 14.59  ? 80  GLY A CA  1 
ATOM   530  C C   . GLY A 1 80  ? 19.851 -3.903  4.719   1.00 10.85  ? 80  GLY A C   1 
ATOM   531  O O   . GLY A 1 80  ? 19.563 -2.724  4.891   1.00 12.79  ? 80  GLY A O   1 
ATOM   532  N N   . ILE A 1 81  ? 20.896 -4.488  5.248   1.00 10.80  ? 81  ILE A N   1 
ATOM   533  C CA  . ILE A 1 81  ? 21.903 -3.799  6.063   1.00 10.93  ? 81  ILE A CA  1 
ATOM   534  C C   . ILE A 1 81  ? 23.251 -4.259  5.557   1.00 10.35  ? 81  ILE A C   1 
ATOM   535  O O   . ILE A 1 81  ? 23.531 -5.438  5.507   1.00 12.10  ? 81  ILE A O   1 
ATOM   536  C CB  . ILE A 1 81  ? 21.738 -4.159  7.560   1.00 13.66  ? 81  ILE A CB  1 
ATOM   537  C CG1 . ILE A 1 81  ? 20.374 -3.903  8.077   1.00 18.09  ? 81  ILE A CG1 1 
ATOM   538  C CG2 . ILE A 1 81  ? 22.897 -3.479  8.318   1.00 15.99  ? 81  ILE A CG2 1 
ATOM   539  C CD1 . ILE A 1 81  ? 20.218 -2.571  8.466   1.00 22.57  ? 81  ILE A CD1 1 
ATOM   540  N N   . ILE A 1 82  ? 24.079 -3.300  5.173   1.00 8.76   ? 82  ILE A N   1 
ATOM   541  C CA  . ILE A 1 82  ? 25.417 -3.544  4.683   1.00 8.81   ? 82  ILE A CA  1 
ATOM   542  C C   . ILE A 1 82  ? 26.408 -2.802  5.548   1.00 8.31   ? 82  ILE A C   1 
ATOM   543  O O   . ILE A 1 82  ? 26.329 -1.556  5.697   1.00 9.10   ? 82  ILE A O   1 
ATOM   544  C CB  . ILE A 1 82  ? 25.582 -3.144  3.213   1.00 9.17   ? 82  ILE A CB  1 
ATOM   545  C CG1 . ILE A 1 82  ? 24.598 -3.897  2.312   1.00 11.35  ? 82  ILE A CG1 1 
ATOM   546  C CG2 . ILE A 1 82  ? 26.998 -3.340  2.760   1.00 9.98   ? 82  ILE A CG2 1 
ATOM   547  C CD1 . ILE A 1 82  ? 24.843 -5.399  2.226   1.00 13.39  ? 82  ILE A CD1 1 
ATOM   548  N N   . ASN A 1 83  ? 27.383 -3.517  6.088   1.00 8.34   ? 83  ASN A N   1 
ATOM   549  C CA  . ASN A 1 83  ? 28.448 -3.030  6.917   1.00 8.52   ? 83  ASN A CA  1 
ATOM   550  C C   . ASN A 1 83  ? 29.747 -2.852  6.092   1.00 8.76   ? 83  ASN A C   1 
ATOM   551  O O   . ASN A 1 83  ? 30.012 -3.651  5.191   1.00 9.44   ? 83  ASN A O   1 
ATOM   552  C CB  . ASN A 1 83  ? 28.707 -3.986  8.055   1.00 8.68   ? 83  ASN A CB  1 
ATOM   553  C CG  . ASN A 1 83  ? 27.467 -4.169  8.885   1.00 9.33   ? 83  ASN A CG  1 
ATOM   554  O OD1 . ASN A 1 83  ? 26.959 -3.210  9.443   1.00 11.59  ? 83  ASN A OD1 1 
ATOM   555  N ND2 . ASN A 1 83  ? 26.966 -5.378  8.941   1.00 12.13  ? 83  ASN A ND2 1 
ATOM   556  N N   . PHE A 1 84  ? 30.518 -1.835  6.482   1.00 9.19   ? 84  PHE A N   1 
ATOM   557  C CA  . PHE A 1 84  ? 31.822 -1.560  5.896   1.00 9.48   ? 84  PHE A CA  1 
ATOM   558  C C   . PHE A 1 84  ? 32.831 -1.418  7.026   1.00 9.65   ? 84  PHE A C   1 
ATOM   559  O O   . PHE A 1 84  ? 32.551 -0.734  8.012   1.00 11.41  ? 84  PHE A O   1 
ATOM   560  C CB  . PHE A 1 84  ? 31.807 -0.227  5.146   1.00 10.39  ? 84  PHE A CB  1 
ATOM   561  C CG  . PHE A 1 84  ? 30.839 -0.163  3.981   1.00 9.71   ? 84  PHE A CG  1 
ATOM   562  C CD1 . PHE A 1 84  ? 29.490 0.062   4.190   1.00 9.73   ? 84  PHE A CD1 1 
ATOM   563  C CD2 . PHE A 1 84  ? 31.308 -0.250  2.693   1.00 10.89  ? 84  PHE A CD2 1 
ATOM   564  C CE1 . PHE A 1 84  ? 28.606 0.129   3.118   1.00 10.82  ? 84  PHE A CE1 1 
ATOM   565  C CE2 . PHE A 1 84  ? 30.444 -0.177  1.621   1.00 11.52  ? 84  PHE A CE2 1 
ATOM   566  C CZ  . PHE A 1 84  ? 29.110 -0.012  1.817   1.00 11.48  ? 84  PHE A CZ  1 
ATOM   567  N N   . GLU A 1 85  ? 33.995 -2.031  6.869   1.00 9.77   ? 85  GLU A N   1 
ATOM   568  C CA  . GLU A 1 85  ? 35.026 -1.909  7.896   1.00 9.98   ? 85  GLU A CA  1 
ATOM   569  C C   . GLU A 1 85  ? 36.382 -1.731  7.253   1.00 10.35  ? 85  GLU A C   1 
ATOM   570  O O   . GLU A 1 85  ? 36.710 -2.427  6.312   1.00 11.39  ? 85  GLU A O   1 
ATOM   571  C CB  . GLU A 1 85  ? 35.037 -3.131  8.791   1.00 11.88  ? 85  GLU A CB  1 
ATOM   572  C CG  . GLU A 1 85  ? 33.807 -3.561  9.490   1.00 19.63  ? 85  GLU A CG  1 
ATOM   573  C CD  . GLU A 1 85  ? 34.318 -4.540  10.612  1.00 26.90  ? 85  GLU A CD  1 
ATOM   574  O OE1 . GLU A 1 85  ? 35.155 -5.440  10.381  1.00 29.53  ? 85  GLU A OE1 1 
ATOM   575  O OE2 . GLU A 1 85  ? 34.318 -4.265  11.708  1.00 27.20  ? 85  GLU A OE2 1 
ATOM   576  N N   . GLN A 1 86  ? 37.215 -0.872  7.835   1.00 10.28  ? 86  GLN A N   1 
ATOM   577  C CA  . GLN A 1 86  ? 38.535 -0.597  7.333   1.00 10.38  ? 86  GLN A CA  1 
ATOM   578  C C   . GLN A 1 86  ? 39.480 -0.465  8.524   1.00 12.55  ? 86  GLN A C   1 
ATOM   579  O O   . GLN A 1 86  ? 39.261 0.353   9.395   1.00 17.56  ? 86  GLN A O   1 
ATOM   580  C CB  . GLN A 1 86  ? 38.528 0.676   6.535   1.00 11.15  ? 86  GLN A CB  1 
ATOM   581  C CG  . GLN A 1 86  ? 39.817 0.948   5.791   1.00 11.02  ? 86  GLN A CG  1 
ATOM   582  C CD  . GLN A 1 86  ? 39.808 2.259   5.070   1.00 11.21  ? 86  GLN A CD  1 
ATOM   583  O OE1 . GLN A 1 86  ? 39.311 3.262   5.598   1.00 13.61  ? 86  GLN A OE1 1 
ATOM   584  N NE2 . GLN A 1 86  ? 40.307 2.290   3.872   1.00 11.92  ? 86  GLN A NE2 1 
ATOM   585  N N   . LYS A 1 87  ? 40.454 -1.323  8.607   1.00 14.44  ? 87  LYS A N   1 
ATOM   586  C CA  . LYS A 1 87  ? 41.313 -1.424  9.752   1.00 16.22  ? 87  LYS A CA  1 
ATOM   587  C C   . LYS A 1 87  ? 42.340 -0.350  9.786   1.00 17.44  ? 87  LYS A C   1 
ATOM   588  O O   . LYS A 1 87  ? 42.799 0.018   10.846  1.00 21.77  ? 87  LYS A O   1 
ATOM   589  C CB  . LYS A 1 87  ? 42.004 -2.780  9.759   1.00 20.05  ? 87  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 87  ? 42.974 -3.077  10.892  1.00 35.22  ? 87  LYS A CG  1 
ATOM   591  C CD  . LYS A 1 87  ? 43.768 -4.386  10.718  1.00 47.11  ? 87  LYS A CD  1 
ATOM   592  C CE  . LYS A 1 87  ? 44.781 -4.637  11.850  1.00 52.78  ? 87  LYS A CE  1 
ATOM   593  N NZ  . LYS A 1 87  ? 45.701 -3.480  12.070  1.00 61.34  ? 87  LYS A NZ  1 
ATOM   594  N N   . GLU A 1 88  ? 42.803 0.116   8.634   1.00 18.13  ? 88  GLU A N   1 
ATOM   595  C CA  . GLU A 1 88  ? 43.812 1.171   8.599   1.00 21.56  ? 88  GLU A CA  1 
ATOM   596  C C   . GLU A 1 88  ? 43.519 2.130   7.478   1.00 17.60  ? 88  GLU A C   1 
ATOM   597  O O   . GLU A 1 88  ? 42.802 1.846   6.538   1.00 15.59  ? 88  GLU A O   1 
ATOM   598  C CB  . GLU A 1 88  ? 45.218 0.711   8.455   1.00 29.81  ? 88  GLU A CB  1 
ATOM   599  C CG  . GLU A 1 88  ? 45.364 -0.269  7.382   1.00 26.80  ? 88  GLU A CG  1 
ATOM   600  C CD  . GLU A 1 88  ? 46.092 -1.438  7.989   1.00 37.68  ? 88  GLU A CD  1 
ATOM   601  O OE1 . GLU A 1 88  ? 45.434 -2.321  8.588   1.00 55.05  ? 88  GLU A OE1 1 
ATOM   602  O OE2 . GLU A 1 88  ? 47.334 -1.420  7.944   1.00 49.18  ? 88  GLU A OE2 1 
ATOM   603  N N   . SER A 1 89  ? 44.079 3.307   7.629   1.00 17.49  ? 89  SER A N   1 
ATOM   604  C CA  . SER A 1 89  ? 43.832 4.419   6.737   1.00 17.53  ? 89  SER A CA  1 
ATOM   605  C C   . SER A 1 89  ? 44.175 3.978   5.339   1.00 14.21  ? 89  SER A C   1 
ATOM   606  O O   . SER A 1 89  ? 45.259 3.485   5.083   1.00 17.04  ? 89  SER A O   1 
ATOM   607  C CB  . SER A 1 89  ? 44.693 5.637   7.118   1.00 22.90  ? 89  SER A CB  1 
ATOM   608  O OG  . SER A 1 89  ? 44.572 6.668   6.208   1.00 31.26  ? 89  SER A OG  1 
ATOM   609  N N   . ASN A 1 90  ? 43.240 4.173   4.448   1.00 14.71  ? 90  ASN A N   1 
ATOM   610  C CA  . ASN A 1 90  ? 43.403 3.803   3.033   1.00 14.64  ? 90  ASN A CA  1 
ATOM   611  C C   . ASN A 1 90  ? 43.805 2.344   2.784   1.00 13.98  ? 90  ASN A C   1 
ATOM   612  O O   . ASN A 1 90  ? 44.358 2.003   1.720   1.00 16.10  ? 90  ASN A O   1 
ATOM   613  C CB  . ASN A 1 90  ? 44.270 4.806   2.302   1.00 15.76  ? 90  ASN A CB  1 
ATOM   614  C CG  . ASN A 1 90  ? 43.478 6.070   1.915   1.00 16.34  ? 90  ASN A CG  1 
ATOM   615  O OD1 . ASN A 1 90  ? 42.275 6.240   2.166   1.00 16.21  ? 90  ASN A OD1 1 
ATOM   616  N ND2 . ASN A 1 90  ? 44.203 6.953   1.287   1.00 17.33  ? 90  ASN A ND2 1 
ATOM   617  N N   . GLY A 1 91  ? 43.468 1.475   3.727   1.00 13.85  ? 91  GLY A N   1 
ATOM   618  C CA  . GLY A 1 91  ? 43.649 0.027   3.605   1.00 15.02  ? 91  GLY A CA  1 
ATOM   619  C C   . GLY A 1 91  ? 42.428 -0.635  2.943   1.00 12.15  ? 91  GLY A C   1 
ATOM   620  O O   . GLY A 1 91  ? 41.467 0.022   2.587   1.00 12.16  ? 91  GLY A O   1 
ATOM   621  N N   . PRO A 1 92  ? 42.435 -1.972  2.753   1.00 12.39  ? 92  PRO A N   1 
ATOM   622  C CA  . PRO A 1 92  ? 41.264 -2.650  2.203   1.00 13.35  ? 92  PRO A CA  1 
ATOM   623  C C   . PRO A 1 92  ? 40.013 -2.479  3.046   1.00 11.87  ? 92  PRO A C   1 
ATOM   624  O O   . PRO A 1 92  ? 40.092 -2.340  4.280   1.00 12.73  ? 92  PRO A O   1 
ATOM   625  C CB  . PRO A 1 92  ? 41.654 -4.123  2.184   1.00 18.89  ? 92  PRO A CB  1 
ATOM   626  C CG  . PRO A 1 92  ? 42.923 -4.199  2.935   1.00 23.01  ? 92  PRO A CG  1 
ATOM   627  C CD  . PRO A 1 92  ? 43.522 -2.869  3.122   1.00 16.31  ? 92  PRO A CD  1 
ATOM   628  N N   . VAL A 1 93  ? 38.835 -2.450  2.394   1.00 11.12  ? 93  VAL A N   1 
ATOM   629  C CA  . VAL A 1 93  ? 37.576 -2.337  3.070   1.00 10.27  ? 93  VAL A CA  1 
ATOM   630  C C   . VAL A 1 93  ? 36.794 -3.656  2.925   1.00 10.91  ? 93  VAL A C   1 
ATOM   631  O O   . VAL A 1 93  ? 36.625 -4.150  1.832   1.00 12.73  ? 93  VAL A O   1 
ATOM   632  C CB  . VAL A 1 93  ? 36.741 -1.200  2.470   1.00 10.17  ? 93  VAL A CB  1 
ATOM   633  C CG1 . VAL A 1 93  ? 35.410 -1.043  3.194   1.00 11.82  ? 93  VAL A CG1 1 
ATOM   634  C CG2 . VAL A 1 93  ? 37.506 0.120   2.517   1.00 10.99  ? 93  VAL A CG2 1 
ATOM   635  N N   . LYS A 1 94  ? 36.351 -4.179  4.042   1.00 10.65  ? 94  LYS A N   1 
ATOM   636  C CA  . LYS A 1 94  ? 35.469 -5.323  4.057   1.00 10.73  ? 94  LYS A CA  1 
ATOM   637  C C   . LYS A 1 94  ? 34.028 -4.867  4.021   1.00 10.53  ? 94  LYS A C   1 
ATOM   638  O O   . LYS A 1 94  ? 33.658 -3.933  4.752   1.00 11.85  ? 94  LYS A O   1 
ATOM   639  C CB  . LYS A 1 94  ? 35.691 -6.168  5.326   1.00 14.26  ? 94  LYS A CB  1 
ATOM   640  C CG  . LYS A 1 94  ? 37.109 -6.600  5.600   1.00 22.70  ? 94  LYS A CG  1 
ATOM   641  C CD  . LYS A 1 94  ? 37.595 -7.646  4.650   1.00 34.76  ? 94  LYS A CD  1 
ATOM   642  C CE  . LYS A 1 94  ? 38.940 -8.232  5.089   1.00 45.39  ? 94  LYS A CE  1 
ATOM   643  N NZ  . LYS A 1 94  ? 38.882 -8.919  6.413   1.00 53.83  ? 94  LYS A NZ  1 
ATOM   644  N N   . VAL A 1 95  ? 33.211 -5.494  3.166   1.00 10.26  ? 95  VAL A N   1 
ATOM   645  C CA  . VAL A 1 95  ? 31.816 -5.123  2.947   1.00 9.66   ? 95  VAL A CA  1 
ATOM   646  C C   . VAL A 1 95  ? 31.003 -6.378  3.192   1.00 9.95   ? 95  VAL A C   1 
ATOM   647  O O   . VAL A 1 95  ? 31.213 -7.403  2.517   1.00 11.55  ? 95  VAL A O   1 
ATOM   648  C CB  . VAL A 1 95  ? 31.596 -4.578  1.557   1.00 10.89  ? 95  VAL A CB  1 
ATOM   649  C CG1 . VAL A 1 95  ? 30.147 -4.125  1.360   1.00 12.06  ? 95  VAL A CG1 1 
ATOM   650  C CG2 . VAL A 1 95  ? 32.576 -3.457  1.217   1.00 11.91  ? 95  VAL A CG2 1 
ATOM   651  N N   . TRP A 1 96  ? 30.056 -6.353  4.109   1.00 9.42   ? 96  TRP A N   1 
ATOM   652  C CA  . TRP A 1 96  ? 29.297 -7.575  4.414   1.00 10.04  ? 96  TRP A CA  1 
ATOM   653  C C   . TRP A 1 96  ? 27.927 -7.238  4.954   1.00 9.10   ? 96  TRP A C   1 
ATOM   654  O O   . TRP A 1 96  ? 27.708 -6.198  5.581   1.00 10.51  ? 96  TRP A O   1 
ATOM   655  C CB  . TRP A 1 96  ? 30.084 -8.498  5.395   1.00 11.01  ? 96  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 96  ? 30.273 -7.884  6.824   1.00 12.37  ? 96  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 96  ? 31.278 -6.979  7.240   1.00 13.80  ? 96  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 96  ? 29.479 -8.129  7.951   1.00 16.19  ? 96  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 96  ? 31.162 -6.764  8.543   1.00 16.94  ? 96  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 96  ? 30.063 -7.364  9.009   1.00 11.80  ? 96  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 96  ? 28.387 -8.815  8.136   1.00 14.13  ? 96  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 96  ? 29.481 -7.396  10.358  1.00 14.51  ? 96  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 96  ? 27.806 -8.823  9.439   1.00 14.22  ? 96  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 96  ? 28.364 -8.166  10.509  1.00 20.21  ? 96  TRP A CH2 1 
ATOM   665  N N   . GLY A 1 97  ? 26.989 -8.142  4.745   1.00 9.95   ? 97  GLY A N   1 
ATOM   666  C CA  . GLY A 1 97  ? 25.629 -8.004  5.285   1.00 10.83  ? 97  GLY A CA  1 
ATOM   667  C C   . GLY A 1 97  ? 24.691 -8.808  4.448   1.00 10.71  ? 97  GLY A C   1 
ATOM   668  O O   . GLY A 1 97  ? 25.075 -9.838  3.880   1.00 12.28  ? 97  GLY A O   1 
ATOM   669  N N   . SER A 1 98  ? 23.454 -8.378  4.378   1.00 11.03  ? 98  SER A N   1 
ATOM   670  C CA  . SER A 1 98  ? 22.469 -9.123  3.662   1.00 12.19  ? 98  SER A CA  1 
ATOM   671  C C   . SER A 1 98  ? 21.377 -8.195  3.174   1.00 12.63  ? 98  SER A C   1 
ATOM   672  O O   . SER A 1 98  ? 21.084 -7.175  3.783   1.00 13.49  ? 98  SER A O   1 
ATOM   673  C CB  . SER A 1 98  ? 21.942 -10.218 4.492   1.00 15.91  ? 98  SER A CB  1 
ATOM   674  O OG  . SER A 1 98  ? 21.276 -9.769  5.538   1.00 23.93  ? 98  SER A OG  1 
ATOM   675  N N   . ILE A 1 99  ? 20.762 -8.575  2.053   1.00 13.13  ? 99  ILE A N   1 
ATOM   676  C CA  . ILE A 1 99  ? 19.692 -7.868  1.441   1.00 11.76  ? 99  ILE A CA  1 
ATOM   677  C C   . ILE A 1 99  ? 18.588 -8.893  1.169   1.00 13.70  ? 99  ILE A C   1 
ATOM   678  O O   . ILE A 1 99  ? 18.854 -9.955  0.630   1.00 16.19  ? 99  ILE A O   1 
ATOM   679  C CB  . ILE A 1 99  ? 20.114 -7.213  0.106   1.00 13.30  ? 99  ILE A CB  1 
ATOM   680  C CG1 . ILE A 1 99  ? 21.430 -6.476  0.262   1.00 14.85  ? 99  ILE A CG1 1 
ATOM   681  C CG2 . ILE A 1 99  ? 18.979 -6.337  -0.452  1.00 14.56  ? 99  ILE A CG2 1 
ATOM   682  C CD1 . ILE A 1 99  ? 22.004 -6.035  -1.036  1.00 16.19  ? 99  ILE A CD1 1 
ATOM   683  N N   . LYS A 1 100 ? 17.357 -8.561  1.507   1.00 14.52  ? 100 LYS A N   1 
ATOM   684  C CA  . LYS A 1 100 ? 16.201 -9.419  1.267   1.00 15.84  ? 100 LYS A CA  1 
ATOM   685  C C   . LYS A 1 100 ? 15.181 -8.700  0.330   1.00 14.67  ? 100 LYS A C   1 
ATOM   686  O O   . LYS A 1 100 ? 15.268 -7.506  0.040   1.00 15.25  ? 100 LYS A O   1 
ATOM   687  C CB  . LYS A 1 100 ? 15.535 -9.947  2.554   1.00 23.39  ? 100 LYS A CB  1 
ATOM   688  C CG  . LYS A 1 100 ? 16.344 -9.648  3.836   1.00 32.60  ? 100 LYS A CG  1 
ATOM   689  C CD  . LYS A 1 100 ? 17.626 -10.496 3.971   1.00 30.65  ? 100 LYS A CD  1 
ATOM   690  C CE  . LYS A 1 100 ? 18.248 -10.419 5.345   1.00 36.81  ? 100 LYS A CE  1 
ATOM   691  N NZ  . LYS A 1 100 ? 18.907 -11.716 5.689   1.00 36.61  ? 100 LYS A NZ  1 
ATOM   692  N N   . GLY A 1 101 ? 14.212 -9.508  -0.163  1.00 15.63  ? 101 GLY A N   1 
ATOM   693  C CA  . GLY A 1 101 ? 13.189 -8.976  -1.051  1.00 18.39  ? 101 GLY A CA  1 
ATOM   694  C C   . GLY A 1 101 ? 13.516 -8.947  -2.524  1.00 17.50  ? 101 GLY A C   1 
ATOM   695  O O   . GLY A 1 101 ? 12.746 -8.317  -3.276  1.00 20.88  ? 101 GLY A O   1 
ATOM   696  N N   . LEU A 1 102 ? 14.699 -9.399  -2.891  1.00 16.94  ? 102 LEU A N   1 
ATOM   697  C CA  . LEU A 1 102 ? 15.211 -9.292  -4.279  1.00 14.71  ? 102 LEU A CA  1 
ATOM   698  C C   . LEU A 1 102 ? 14.671 -10.426 -5.138  1.00 17.40  ? 102 LEU A C   1 
ATOM   699  O O   . LEU A 1 102 ? 14.361 -11.515 -4.652  1.00 20.13  ? 102 LEU A O   1 
ATOM   700  C CB  . LEU A 1 102 ? 16.716 -9.364  -4.260  1.00 14.82  ? 102 LEU A CB  1 
ATOM   701  C CG  . LEU A 1 102 ? 17.424 -8.167  -3.684  1.00 14.69  ? 102 LEU A CG  1 
ATOM   702  C CD1 . LEU A 1 102 ? 18.875 -8.576  -3.427  1.00 15.24  ? 102 LEU A CD1 1 
ATOM   703  C CD2 . LEU A 1 102 ? 17.391 -6.963  -4.610  1.00 16.60  ? 102 LEU A CD2 1 
ATOM   704  N N   . THR A 1 103 ? 14.519 -10.169 -6.445  1.00 17.42  ? 103 THR A N   1 
ATOM   705  C CA  . THR A 1 103 ? 14.324 -11.259 -7.371  1.00 17.29  ? 103 THR A CA  1 
ATOM   706  C C   . THR A 1 103 ? 15.543 -12.190 -7.450  1.00 17.01  ? 103 THR A C   1 
ATOM   707  O O   . THR A 1 103 ? 16.683 -11.786 -7.272  1.00 17.24  ? 103 THR A O   1 
ATOM   708  C CB  . THR A 1 103 ? 13.950 -10.737 -8.771  1.00 20.34  ? 103 THR A CB  1 
ATOM   709  O OG1 . THR A 1 103 ? 14.974 -9.833  -9.160  1.00 19.44  ? 103 THR A OG1 1 
ATOM   710  C CG2 . THR A 1 103 ? 12.612 -9.942  -8.711  1.00 21.33  ? 103 THR A CG2 1 
ATOM   711  N N   . GLU A 1 104 ? 15.293 -13.454 -7.722  1.00 17.96  ? 104 GLU A N   1 
ATOM   712  C CA  . GLU A 1 104 ? 16.400 -14.393 -7.787  1.00 15.76  ? 104 GLU A CA  1 
ATOM   713  C C   . GLU A 1 104 ? 17.403 -13.983 -8.904  1.00 16.51  ? 104 GLU A C   1 
ATOM   714  O O   . GLU A 1 104 ? 16.967 -13.611 -10.002 1.00 20.13  ? 104 GLU A O   1 
ATOM   715  C CB  . GLU A 1 104 ? 15.869 -15.786 -8.161  1.00 19.09  ? 104 GLU A CB  1 
ATOM   716  C CG  . GLU A 1 104 ? 16.937 -16.911 -8.172  1.00 21.35  ? 104 GLU A CG  1 
ATOM   717  C CD  . GLU A 1 104 ? 16.407 -18.285 -8.447  1.00 30.04  ? 104 GLU A CD  1 
ATOM   718  O OE1 . GLU A 1 104 ? 15.187 -18.384 -8.622  1.00 34.53  ? 104 GLU A OE1 1 
ATOM   719  O OE2 . GLU A 1 104 ? 17.198 -19.262 -8.435  1.00 33.08  ? 104 GLU A OE2 1 
ATOM   720  N N   . GLY A 1 105 ? 18.682 -14.111 -8.637  1.00 16.33  ? 105 GLY A N   1 
ATOM   721  C CA  . GLY A 1 105 ? 19.714 -13.847 -9.619  1.00 16.14  ? 105 GLY A CA  1 
ATOM   722  C C   . GLY A 1 105 ? 20.654 -12.716 -9.251  1.00 14.31  ? 105 GLY A C   1 
ATOM   723  O O   . GLY A 1 105 ? 20.795 -12.362 -8.104  1.00 14.77  ? 105 GLY A O   1 
ATOM   724  N N   . LEU A 1 106 ? 21.345 -12.199 -10.252 1.00 15.69  ? 106 LEU A N   1 
ATOM   725  C CA  . LEU A 1 106 ? 22.436 -11.213 -10.087 1.00 15.58  ? 106 LEU A CA  1 
ATOM   726  C C   . LEU A 1 106 ? 21.864 -9.822  -10.036 1.00 13.66  ? 106 LEU A C   1 
ATOM   727  O O   . LEU A 1 106 ? 21.067 -9.449  -10.880 1.00 17.78  ? 106 LEU A O   1 
ATOM   728  C CB  . LEU A 1 106 ? 23.398 -11.291 -11.248 1.00 18.81  ? 106 LEU A CB  1 
ATOM   729  C CG  . LEU A 1 106 ? 24.190 -12.546 -11.361 1.00 21.01  ? 106 LEU A CG  1 
ATOM   730  C CD1 . LEU A 1 106 ? 24.884 -12.572 -12.720 1.00 31.74  ? 106 LEU A CD1 1 
ATOM   731  C CD2 . LEU A 1 106 ? 25.254 -12.695 -10.299 1.00 23.84  ? 106 LEU A CD2 1 
ATOM   732  N N   . HIS A 1 107 ? 22.378 -9.001  -9.104  1.00 13.55  ? 107 HIS A N   1 
ATOM   733  C CA  . HIS A 1 107 ? 21.974 -7.627  -8.957  1.00 13.06  ? 107 HIS A CA  1 
ATOM   734  C C   . HIS A 1 107 ? 23.201 -6.733  -8.859  1.00 12.13  ? 107 HIS A C   1 
ATOM   735  O O   . HIS A 1 107 ? 24.034 -6.913  -7.969  1.00 12.17  ? 107 HIS A O   1 
ATOM   736  C CB  . HIS A 1 107 ? 21.078 -7.436  -7.731  1.00 13.29  ? 107 HIS A CB  1 
ATOM   737  C CG  . HIS A 1 107 ? 19.750 -8.109  -7.863  1.00 13.83  ? 107 HIS A CG  1 
ATOM   738  N ND1 . HIS A 1 107 ? 19.445 -9.446  -7.617  1.00 17.16  ? 107 HIS A ND1 1 
ATOM   739  C CD2 . HIS A 1 107 ? 18.617 -7.548  -8.333  1.00 13.49  ? 107 HIS A CD2 1 
ATOM   740  C CE1 . HIS A 1 107 ? 18.173 -9.625  -7.894  1.00 12.82  ? 107 HIS A CE1 1 
ATOM   741  N NE2 . HIS A 1 107 ? 17.658 -8.499  -8.309  1.00 18.47  ? 107 HIS A NE2 1 
ATOM   742  N N   . GLY A 1 108 ? 23.244 -5.699  -9.716  1.00 12.53  ? 108 GLY A N   1 
ATOM   743  C CA  . GLY A 1 108 ? 24.335 -4.752  -9.637  1.00 11.64  ? 108 GLY A CA  1 
ATOM   744  C C   . GLY A 1 108 ? 24.368 -4.044  -8.285  1.00 11.26  ? 108 GLY A C   1 
ATOM   745  O O   . GLY A 1 108 ? 23.352 -3.657  -7.752  1.00 12.63  ? 108 GLY A O   1 
ATOM   746  N N   . PHE A 1 109 ? 25.578 -3.830  -7.772  1.00 10.47  ? 109 PHE A N   1 
ATOM   747  C CA  . PHE A 1 109 ? 25.797 -3.357  -6.421  1.00 10.08  ? 109 PHE A CA  1 
ATOM   748  C C   . PHE A 1 109 ? 26.981 -2.371  -6.441  1.00 10.58  ? 109 PHE A C   1 
ATOM   749  O O   . PHE A 1 109 ? 28.103 -2.753  -6.818  1.00 12.43  ? 109 PHE A O   1 
ATOM   750  C CB  . PHE A 1 109 ? 26.116 -4.565  -5.555  1.00 11.39  ? 109 PHE A CB  1 
ATOM   751  C CG  . PHE A 1 109 ? 26.265 -4.309  -4.083  1.00 10.51  ? 109 PHE A CG  1 
ATOM   752  C CD1 . PHE A 1 109 ? 25.245 -3.820  -3.339  1.00 13.87  ? 109 PHE A CD1 1 
ATOM   753  C CD2 . PHE A 1 109 ? 27.380 -4.693  -3.435  1.00 12.13  ? 109 PHE A CD2 1 
ATOM   754  C CE1 . PHE A 1 109 ? 25.343 -3.706  -1.951  1.00 14.40  ? 109 PHE A CE1 1 
ATOM   755  C CE2 . PHE A 1 109 ? 27.488 -4.585  -2.061  1.00 13.27  ? 109 PHE A CE2 1 
ATOM   756  C CZ  . PHE A 1 109 ? 26.481 -4.081  -1.337  1.00 12.73  ? 109 PHE A CZ  1 
ATOM   757  N N   . HIS A 1 110 ? 26.778 -1.144  -6.027  1.00 10.41  ? 110 HIS A N   1 
ATOM   758  C CA  . HIS A 1 110 ? 27.844 -0.159  -6.117  1.00 11.21  ? 110 HIS A CA  1 
ATOM   759  C C   . HIS A 1 110 ? 27.490 1.095   -5.324  1.00 9.30   ? 110 HIS A C   1 
ATOM   760  O O   . HIS A 1 110 ? 26.341 1.365   -4.992  1.00 10.09  ? 110 HIS A O   1 
ATOM   761  C CB  . HIS A 1 110 ? 28.229 0.179   -7.537  1.00 12.68  ? 110 HIS A CB  1 
ATOM   762  C CG  . HIS A 1 110 ? 27.097 0.293   -8.391  1.00 15.63  ? 110 HIS A CG  1 
ATOM   763  N ND1 . HIS A 1 110 ? 26.260 1.351   -8.438  1.00 21.22  ? 110 HIS A ND1 1 
ATOM   764  C CD2 . HIS A 1 110 ? 26.650 -0.614  -9.273  1.00 16.32  ? 110 HIS A CD2 1 
ATOM   765  C CE1 . HIS A 1 110 ? 25.352 1.105   -9.384  1.00 19.35  ? 110 HIS A CE1 1 
ATOM   766  N NE2 . HIS A 1 110 ? 25.572 -0.080  -9.899  1.00 24.05  ? 110 HIS A NE2 1 
ATOM   767  N N   . VAL A 1 111 ? 28.542 1.838   -5.007  1.00 9.49   ? 111 VAL A N   1 
ATOM   768  C CA  . VAL A 1 111 ? 28.415 3.151   -4.375  1.00 9.19   ? 111 VAL A CA  1 
ATOM   769  C C   . VAL A 1 111 ? 28.194 4.187   -5.469  1.00 10.73  ? 111 VAL A C   1 
ATOM   770  O O   . VAL A 1 111 ? 28.972 4.194   -6.452  1.00 15.40  ? 111 VAL A O   1 
ATOM   771  C CB  . VAL A 1 111 ? 29.671 3.475   -3.538  1.00 9.61   ? 111 VAL A CB  1 
ATOM   772  C CG1 . VAL A 1 111 ? 29.484 4.793   -2.816  1.00 11.07  ? 111 VAL A CG1 1 
ATOM   773  C CG2 . VAL A 1 111 ? 29.946 2.355   -2.551  1.00 11.89  ? 111 VAL A CG2 1 
ATOM   774  N N   . HIS A 1 112 ? 27.192 5.015   -5.356  1.00 10.34  ? 112 HIS A N   1 
ATOM   775  C CA  . HIS A 1 112 ? 26.917 6.056   -6.332  1.00 10.08  ? 112 HIS A CA  1 
ATOM   776  C C   . HIS A 1 112 ? 27.739 7.279   -6.024  1.00 10.59  ? 112 HIS A C   1 
ATOM   777  O O   . HIS A 1 112 ? 27.867 7.730   -4.874  1.00 12.15  ? 112 HIS A O   1 
ATOM   778  C CB  . HIS A 1 112 ? 25.470 6.450   -6.258  1.00 12.33  ? 112 HIS A CB  1 
ATOM   779  C CG  . HIS A 1 112 ? 25.125 7.611   -7.126  1.00 13.07  ? 112 HIS A CG  1 
ATOM   780  N ND1 . HIS A 1 112 ? 24.977 7.497   -8.480  1.00 16.30  ? 112 HIS A ND1 1 
ATOM   781  C CD2 . HIS A 1 112 ? 25.015 8.929   -6.845  1.00 15.26  ? 112 HIS A CD2 1 
ATOM   782  C CE1 . HIS A 1 112 ? 24.779 8.686   -9.019  1.00 15.99  ? 112 HIS A CE1 1 
ATOM   783  N NE2 . HIS A 1 112 ? 24.854 9.579   -8.040  1.00 15.83  ? 112 HIS A NE2 1 
ATOM   784  N N   . GLY A 1 113 ? 28.267 7.911   -7.068  1.00 12.03  ? 113 GLY A N   1 
ATOM   785  C CA  . GLY A 1 113 ? 28.831 9.254   -6.917  1.00 14.63  ? 113 GLY A CA  1 
ATOM   786  C C   . GLY A 1 113 ? 30.177 9.357   -6.252  1.00 13.48  ? 113 GLY A C   1 
ATOM   787  O O   . GLY A 1 113 ? 30.577 10.458  -5.815  1.00 17.49  ? 113 GLY A O   1 
ATOM   788  N N   . ALA A 1 114 ? 30.901 8.263   -6.175  1.00 13.97  ? 114 ALA A N   1 
ATOM   789  C CA  . ALA A 1 114 ? 32.203 8.156   -5.550  1.00 15.37  ? 114 ALA A CA  1 
ATOM   790  C C   . ALA A 1 114 ? 33.291 8.011   -6.574  1.00 14.04  ? 114 ALA A C   1 
ATOM   791  O O   . ALA A 1 114 ? 34.463 7.724   -6.144  1.00 16.62  ? 114 ALA A O   1 
ATOM   792  C CB  . ALA A 1 114 ? 32.155 6.913   -4.643  1.00 19.18  ? 114 ALA A CB  1 
ATOM   793  O OXT . ALA A 1 114 ? 33.054 8.150   -7.773  1.00 14.89  ? 114 ALA A OXT 1 
ATOM   794  N N   . ALA B 1 1   ? 31.111 -16.713 30.779  1.00 36.45  ? 1   ALA B N   1 
ATOM   795  C CA  . ALA B 1 1   ? 30.999 -15.294 31.123  1.00 25.64  ? 1   ALA B CA  1 
ATOM   796  C C   . ALA B 1 1   ? 30.293 -14.493 30.030  1.00 20.61  ? 1   ALA B C   1 
ATOM   797  O O   . ALA B 1 1   ? 30.748 -14.482 28.889  1.00 27.59  ? 1   ALA B O   1 
ATOM   798  C CB  . ALA B 1 1   ? 32.349 -14.671 31.361  1.00 30.84  ? 1   ALA B CB  1 
ATOM   799  N N   . GLY B 1 2   ? 29.251 -13.791 30.451  1.00 13.65  ? 2   GLY B N   1 
ATOM   800  C CA  . GLY B 1 2   ? 28.492 -13.028 29.508  1.00 12.81  ? 2   GLY B CA  1 
ATOM   801  C C   . GLY B 1 2   ? 28.304 -11.550 29.788  1.00 10.27  ? 2   GLY B C   1 
ATOM   802  O O   . GLY B 1 2   ? 27.696 -10.877 28.973  1.00 11.71  ? 2   GLY B O   1 
ATOM   803  N N   . ASP B 1 3   ? 28.824 -11.007 30.882  1.00 9.87   ? 3   ASP B N   1 
ATOM   804  C CA  . ASP B 1 3   ? 28.690 -9.603  31.138  1.00 10.29  ? 3   ASP B CA  1 
ATOM   805  C C   . ASP B 1 3   ? 29.461 -8.815  30.091  1.00 10.18  ? 3   ASP B C   1 
ATOM   806  O O   . ASP B 1 3   ? 30.643 -9.047  29.885  1.00 12.42  ? 3   ASP B O   1 
ATOM   807  C CB  . ASP B 1 3   ? 29.143 -9.187  32.536  1.00 11.76  ? 3   ASP B CB  1 
ATOM   808  C CG  . ASP B 1 3   ? 28.262 -9.610  33.672  1.00 14.80  ? 3   ASP B CG  1 
ATOM   809  O OD1 . ASP B 1 3   ? 27.144 -10.057 33.430  1.00 17.62  ? 3   ASP B OD1 1 
ATOM   810  O OD2 . ASP B 1 3   ? 28.719 -9.399  34.835  1.00 14.98  ? 3   ASP B OD2 1 
ATOM   811  N N   . LEU B 1 4   ? 28.833 -7.851  29.489  1.00 10.03  ? 4   LEU B N   1 
ATOM   812  C CA  . LEU B 1 4   ? 29.443 -6.901  28.530  1.00 11.80  ? 4   LEU B CA  1 
ATOM   813  C C   . LEU B 1 4   ? 29.424 -5.446  29.093  1.00 12.55  ? 4   LEU B C   1 
ATOM   814  O O   . LEU B 1 4   ? 29.438 -4.454  28.343  1.00 17.97  ? 4   LEU B O   1 
ATOM   815  C CB  . LEU B 1 4   ? 28.728 -6.952  27.174  1.00 10.65  ? 4   LEU B CB  1 
ATOM   816  C CG  . LEU B 1 4   ? 28.766 -8.257  26.428  1.00 11.88  ? 4   LEU B CG  1 
ATOM   817  C CD1 . LEU B 1 4   ? 27.947 -8.129  25.173  1.00 13.86  ? 4   LEU B CD1 1 
ATOM   818  C CD2 . LEU B 1 4   ? 30.154 -8.680  26.134  1.00 18.16  ? 4   LEU B CD2 1 
ATOM   819  N N   . GLY B 1 5   ? 29.370 -5.298  30.356  1.00 11.34  ? 5   GLY B N   1 
ATOM   820  C CA  . GLY B 1 5   ? 29.359 -3.991  30.969  1.00 12.02  ? 5   GLY B CA  1 
ATOM   821  C C   . GLY B 1 5   ? 28.016 -3.330  30.803  1.00 11.75  ? 5   GLY B C   1 
ATOM   822  O O   . GLY B 1 5   ? 26.965 -3.980  30.695  1.00 14.07  ? 5   GLY B O   1 
ATOM   823  N N   . ASN B 1 6   ? 28.030 -2.023  30.825  1.00 10.70  ? 6   ASN B N   1 
ATOM   824  C CA  . ASN B 1 6   ? 26.883 -1.190  30.637  1.00 9.90   ? 6   ASN B CA  1 
ATOM   825  C C   . ASN B 1 6   ? 27.010 -0.431  29.295  1.00 9.92   ? 6   ASN B C   1 
ATOM   826  O O   . ASN B 1 6   ? 28.125 -0.031  28.928  1.00 12.55  ? 6   ASN B O   1 
ATOM   827  C CB  . ASN B 1 6   ? 26.740 -0.168  31.743  1.00 11.52  ? 6   ASN B CB  1 
ATOM   828  C CG  . ASN B 1 6   ? 26.562 -0.779  33.072  1.00 12.18  ? 6   ASN B CG  1 
ATOM   829  O OD1 . ASN B 1 6   ? 25.477 -1.246  33.385  1.00 16.56  ? 6   ASN B OD1 1 
ATOM   830  N ND2 . ASN B 1 6   ? 27.674 -0.838  33.843  1.00 12.49  ? 6   ASN B ND2 1 
ATOM   831  N N   . VAL B 1 7   ? 25.884 -0.264  28.623  1.00 9.42   ? 7   VAL B N   1 
ATOM   832  C CA  . VAL B 1 7   ? 25.837 0.685   27.532  1.00 9.78   ? 7   VAL B CA  1 
ATOM   833  C C   . VAL B 1 7   ? 25.335 1.999   28.089  1.00 10.47  ? 7   VAL B C   1 
ATOM   834  O O   . VAL B 1 7   ? 24.624 2.027   29.075  1.00 12.86  ? 7   VAL B O   1 
ATOM   835  C CB  . VAL B 1 7   ? 25.014 0.185   26.327  1.00 10.64  ? 7   VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 7   ? 25.534 -1.132  25.846  1.00 11.70  ? 7   VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 7   ? 23.538 0.142   26.649  1.00 11.73  ? 7   VAL B CG2 1 
ATOM   838  N N   . THR B 1 8   ? 25.757 3.075   27.501  1.00 10.11  ? 8   THR B N   1 
ATOM   839  C CA  . THR B 1 8   ? 25.398 4.396   27.936  1.00 11.37  ? 8   THR B CA  1 
ATOM   840  C C   . THR B 1 8   ? 24.503 5.053   26.902  1.00 10.92  ? 8   THR B C   1 
ATOM   841  O O   . THR B 1 8   ? 24.935 5.317   25.778  1.00 12.22  ? 8   THR B O   1 
ATOM   842  C CB  . THR B 1 8   ? 26.623 5.292   28.156  1.00 14.88  ? 8   THR B CB  1 
ATOM   843  O OG1 . THR B 1 8   ? 27.450 4.740   29.162  1.00 18.10  ? 8   THR B OG1 1 
ATOM   844  C CG2 . THR B 1 8   ? 26.219 6.688   28.583  1.00 19.20  ? 8   THR B CG2 1 
ATOM   845  N N   . ALA B 1 9   ? 23.255 5.325   27.273  1.00 11.01  ? 9   ALA B N   1 
ATOM   846  C CA  . ALA B 1 9   ? 22.325 6.033   26.419  1.00 11.87  ? 9   ALA B CA  1 
ATOM   847  C C   . ALA B 1 9   ? 22.364 7.510   26.747  1.00 11.54  ? 9   ALA B C   1 
ATOM   848  O O   . ALA B 1 9   ? 22.307 7.910   27.907  1.00 12.91  ? 9   ALA B O   1 
ATOM   849  C CB  . ALA B 1 9   ? 20.904 5.492   26.595  1.00 13.32  ? 9   ALA B CB  1 
ATOM   850  N N   . ASP B 1 10  ? 22.455 8.322   25.687  1.00 12.50  ? 10  ASP B N   1 
ATOM   851  C CA  . ASP B 1 10  ? 22.450 9.752   25.788  1.00 13.67  ? 10  ASP B CA  1 
ATOM   852  C C   . ASP B 1 10  ? 21.037 10.314  25.979  1.00 14.27  ? 10  ASP B C   1 
ATOM   853  O O   . ASP B 1 10  ? 20.078 9.570   26.109  1.00 14.63  ? 10  ASP B O   1 
ATOM   854  C CB  . ASP B 1 10  ? 23.225 10.362  24.602  1.00 14.12  ? 10  ASP B CB  1 
ATOM   855  C CG  . ASP B 1 10  ? 22.527 10.178  23.266  1.00 14.13  ? 10  ASP B CG  1 
ATOM   856  O OD1 . ASP B 1 10  ? 21.317 9.873   23.222  1.00 14.19  ? 10  ASP B OD1 1 
ATOM   857  O OD2 . ASP B 1 10  ? 23.248 10.293  22.257  1.00 17.04  ? 10  ASP B OD2 1 
ATOM   858  N N   . LYS B 1 11  ? 20.937 11.636  25.968  1.00 15.50  ? 11  LYS B N   1 
ATOM   859  C CA  . LYS B 1 11  ? 19.670 12.301  26.177  1.00 18.72  ? 11  LYS B CA  1 
ATOM   860  C C   . LYS B 1 11  ? 18.688 12.126  25.015  1.00 18.46  ? 11  LYS B C   1 
ATOM   861  O O   . LYS B 1 11  ? 17.489 12.479  25.145  1.00 20.59  ? 11  LYS B O   1 
ATOM   862  C CB  . LYS B 1 11  ? 19.842 13.773  26.553  1.00 22.22  ? 11  LYS B CB  1 
ATOM   863  C CG  . LYS B 1 11  ? 20.466 14.623  25.490  1.00 20.58  ? 11  LYS B CG  1 
ATOM   864  C CD  . LYS B 1 11  ? 20.729 16.035  26.042  1.00 26.40  ? 11  LYS B CD  1 
ATOM   865  C CE  . LYS B 1 11  ? 21.531 16.923  25.114  1.00 38.83  ? 11  LYS B CE  1 
ATOM   866  N NZ  . LYS B 1 11  ? 20.997 16.800  23.756  1.00 37.59  ? 11  LYS B NZ  1 
ATOM   867  N N   . ASP B 1 12  ? 19.123 11.572  23.904  1.00 15.09  ? 12  ASP B N   1 
ATOM   868  C CA  . ASP B 1 12  ? 18.231 11.208  22.806  1.00 14.25  ? 12  ASP B CA  1 
ATOM   869  C C   . ASP B 1 12  ? 17.858 9.730   22.808  1.00 13.65  ? 12  ASP B C   1 
ATOM   870  O O   . ASP B 1 12  ? 17.160 9.274   21.930  1.00 15.95  ? 12  ASP B O   1 
ATOM   871  C CB  . ASP B 1 12  ? 18.901 11.548  21.484  1.00 14.67  ? 12  ASP B CB  1 
ATOM   872  C CG  . ASP B 1 12  ? 19.249 13.045  21.353  1.00 18.51  ? 12  ASP B CG  1 
ATOM   873  O OD1 . ASP B 1 12  ? 18.418 13.917  21.703  1.00 19.91  ? 12  ASP B OD1 1 
ATOM   874  O OD2 . ASP B 1 12  ? 20.336 13.357  20.868  1.00 21.59  ? 12  ASP B OD2 1 
ATOM   875  N N   . GLY B 1 13  ? 18.344 8.995   23.816  1.00 13.06  ? 13  GLY B N   1 
ATOM   876  C CA  . GLY B 1 13  ? 18.027 7.601   23.948  1.00 13.25  ? 13  GLY B CA  1 
ATOM   877  C C   . GLY B 1 13  ? 18.888 6.655   23.148  1.00 10.95  ? 13  GLY B C   1 
ATOM   878  O O   . GLY B 1 13  ? 18.559 5.479   23.028  1.00 12.35  ? 13  GLY B O   1 
ATOM   879  N N   . VAL B 1 14  ? 20.007 7.153   22.625  1.00 11.05  ? 14  VAL B N   1 
ATOM   880  C CA  . VAL B 1 14  ? 20.919 6.398   21.774  1.00 10.63  ? 14  VAL B CA  1 
ATOM   881  C C   . VAL B 1 14  ? 22.174 5.998   22.508  1.00 10.18  ? 14  VAL B C   1 
ATOM   882  O O   . VAL B 1 14  ? 22.824 6.827   23.151  1.00 10.99  ? 14  VAL B O   1 
ATOM   883  C CB  . VAL B 1 14  ? 21.304 7.249   20.535  1.00 12.51  ? 14  VAL B CB  1 
ATOM   884  C CG1 . VAL B 1 14  ? 22.182 6.436   19.600  1.00 13.09  ? 14  VAL B CG1 1 
ATOM   885  C CG2 . VAL B 1 14  ? 20.031 7.716   19.803  1.00 13.77  ? 14  VAL B CG2 1 
ATOM   886  N N   . ALA B 1 15  ? 22.497 4.708   22.417  1.00 10.51  ? 15  ALA B N   1 
ATOM   887  C CA  . ALA B 1 15  ? 23.754 4.145   22.919  1.00 10.62  ? 15  ALA B CA  1 
ATOM   888  C C   . ALA B 1 15  ? 24.575 3.575   21.813  1.00 10.48  ? 15  ALA B C   1 
ATOM   889  O O   . ALA B 1 15  ? 24.111 2.803   21.029  1.00 15.05  ? 15  ALA B O   1 
ATOM   890  C CB  . ALA B 1 15  ? 23.464 3.048   23.947  1.00 11.97  ? 15  ALA B CB  1 
ATOM   891  N N   . ASP B 1 16  ? 25.805 3.997   21.724  1.00 11.49  ? 16  ASP B N   1 
ATOM   892  C CA  . ASP B 1 16  ? 26.781 3.437   20.799  1.00 11.09  ? 16  ASP B CA  1 
ATOM   893  C C   . ASP B 1 16  ? 27.609 2.419   21.537  1.00 9.98   ? 16  ASP B C   1 
ATOM   894  O O   . ASP B 1 16  ? 28.044 2.625   22.658  1.00 12.72  ? 16  ASP B O   1 
ATOM   895  C CB  . ASP B 1 16  ? 27.687 4.485   20.184  1.00 14.78  ? 16  ASP B CB  1 
ATOM   896  C CG  . ASP B 1 16  ? 26.928 5.287   19.174  1.00 18.00  ? 16  ASP B CG  1 
ATOM   897  O OD1 . ASP B 1 16  ? 26.475 4.811   18.101  1.00 25.36  ? 16  ASP B OD1 1 
ATOM   898  O OD2 . ASP B 1 16  ? 26.706 6.366   19.480  1.00 22.47  ? 16  ASP B OD2 1 
ATOM   899  N N   . VAL B 1 17  ? 27.913 1.325   20.848  1.00 9.52   ? 17  VAL B N   1 
ATOM   900  C CA  . VAL B 1 17  ? 28.707 0.252   21.400  1.00 9.30   ? 17  VAL B CA  1 
ATOM   901  C C   . VAL B 1 17  ? 29.946 0.039   20.549  1.00 9.09   ? 17  VAL B C   1 
ATOM   902  O O   . VAL B 1 17  ? 29.851 -0.106  19.353  1.00 9.27   ? 17  VAL B O   1 
ATOM   903  C CB  . VAL B 1 17  ? 27.875 -1.044  21.439  1.00 10.72  ? 17  VAL B CB  1 
ATOM   904  C CG1 . VAL B 1 17  ? 28.714 -2.227  21.951  1.00 12.39  ? 17  VAL B CG1 1 
ATOM   905  C CG2 . VAL B 1 17  ? 26.624 -0.827  22.261  1.00 11.70  ? 17  VAL B CG2 1 
ATOM   906  N N   . SER B 1 18  ? 31.104 -0.006  21.199  1.00 9.99   ? 18  SER B N   1 
ATOM   907  C CA  . SER B 1 18  ? 32.369 -0.312  20.515  1.00 10.60  ? 18  SER B CA  1 
ATOM   908  C C   . SER B 1 18  ? 33.319 -0.949  21.511  1.00 10.84  ? 18  SER B C   1 
ATOM   909  O O   . SER B 1 18  ? 33.984 -0.225  22.244  1.00 15.74  ? 18  SER B O   1 
ATOM   910  C CB  . SER B 1 18  ? 33.041 0.934   19.923  1.00 14.15  ? 18  SER B CB  1 
ATOM   911  O OG  . SER B 1 18  ? 34.210 0.598   19.256  1.00 18.85  ? 18  SER B OG  1 
ATOM   912  N N   . ILE B 1 19  ? 33.330 -2.252  21.614  1.00 10.18  ? 19  ILE B N   1 
ATOM   913  C CA  . ILE B 1 19  ? 34.052 -3.013  22.643  1.00 11.07  ? 19  ILE B CA  1 
ATOM   914  C C   . ILE B 1 19  ? 34.894 -4.066  21.954  1.00 10.52  ? 19  ILE B C   1 
ATOM   915  O O   . ILE B 1 19  ? 34.539 -4.575  20.895  1.00 11.73  ? 19  ILE B O   1 
ATOM   916  C CB  . ILE B 1 19  ? 33.004 -3.798  23.562  1.00 15.46  ? 19  ILE B CB  1 
ATOM   917  C CG1 . ILE B 1 19  ? 32.027 -2.816  24.245  1.00 18.34  ? 19  ILE B CG1 1 
ATOM   918  C CG2 . ILE B 1 19  ? 33.666 -4.694  24.555  1.00 19.53  ? 19  ILE B CG2 1 
ATOM   919  C CD1 . ILE B 1 19  ? 30.860 -3.595  24.868  1.00 19.06  ? 19  ILE B CD1 1 
ATOM   920  N N   . GLU B 1 20  ? 35.998 -4.401  22.587  1.00 11.99  ? 20  GLU B N   1 
ATOM   921  C CA  . GLU B 1 20  ? 36.738 -5.600  22.217  1.00 12.53  ? 20  GLU B CA  1 
ATOM   922  C C   . GLU B 1 20  ? 36.756 -6.497  23.471  1.00 11.37  ? 20  GLU B C   1 
ATOM   923  O O   . GLU B 1 20  ? 37.200 -6.046  24.547  1.00 12.71  ? 20  GLU B O   1 
ATOM   924  C CB  . GLU B 1 20  ? 38.170 -5.306  21.708  1.00 15.83  ? 20  GLU B CB  1 
ATOM   925  C CG  . GLU B 1 20  ? 38.794 -6.549  21.180  1.00 21.19  ? 20  GLU B CG  1 
ATOM   926  C CD  . GLU B 1 20  ? 40.284 -6.421  20.977  1.00 29.34  ? 20  GLU B CD  1 
ATOM   927  O OE1 . GLU B 1 20  ? 41.026 -6.397  21.985  1.00 33.08  ? 20  GLU B OE1 1 
ATOM   928  O OE2 . GLU B 1 20  ? 40.700 -6.372  19.830  1.00 46.34  ? 20  GLU B OE2 1 
ATOM   929  N N   . ASP B 1 21  ? 36.335 -7.737  23.307  1.00 12.15  ? 21  ASP B N   1 
ATOM   930  C CA  . ASP B 1 21  ? 36.204 -8.643  24.405  1.00 11.37  ? 21  ASP B CA  1 
ATOM   931  C C   . ASP B 1 21  ? 37.014 -9.884  24.160  1.00 12.20  ? 21  ASP B C   1 
ATOM   932  O O   . ASP B 1 21  ? 36.766 -10.627 23.218  1.00 13.19  ? 21  ASP B O   1 
ATOM   933  C CB  . ASP B 1 21  ? 34.717 -8.967  24.607  1.00 13.58  ? 21  ASP B CB  1 
ATOM   934  C CG  . ASP B 1 21  ? 34.438 -9.773  25.807  1.00 14.26  ? 21  ASP B CG  1 
ATOM   935  O OD1 . ASP B 1 21  ? 35.170 -10.740 26.087  1.00 16.23  ? 21  ASP B OD1 1 
ATOM   936  O OD2 . ASP B 1 21  ? 33.411 -9.520  26.446  1.00 17.04  ? 21  ASP B OD2 1 
ATOM   937  N N   . SER B 1 22  ? 38.028 -10.113 24.985  1.00 11.77  ? 22  SER B N   1 
ATOM   938  C CA  . SER B 1 22  ? 38.894 -11.240 24.836  1.00 12.83  ? 22  SER B CA  1 
ATOM   939  C C   . SER B 1 22  ? 38.490 -12.479 25.561  1.00 14.53  ? 22  SER B C   1 
ATOM   940  O O   . SER B 1 22  ? 39.130 -13.534 25.425  1.00 19.48  ? 22  SER B O   1 
ATOM   941  C CB  . SER B 1 22  ? 40.297 -10.873 25.345  1.00 15.43  ? 22  SER B CB  1 
ATOM   942  O OG  . SER B 1 22  ? 40.849 -9.803  24.593  1.00 19.11  ? 22  SER B OG  1 
ATOM   943  N N   . VAL B 1 23  ? 37.369 -12.444 26.262  1.00 13.55  ? 23  VAL B N   1 
ATOM   944  C CA  . VAL B 1 23  ? 36.896 -13.511 27.056  1.00 15.62  ? 23  VAL B CA  1 
ATOM   945  C C   . VAL B 1 23  ? 35.850 -14.349 26.298  1.00 17.26  ? 23  VAL B C   1 
ATOM   946  O O   . VAL B 1 23  ? 35.926 -15.561 26.302  1.00 22.27  ? 23  VAL B O   1 
ATOM   947  C CB  . VAL B 1 23  ? 36.316 -12.940 28.391  1.00 20.04  ? 23  VAL B CB  1 
ATOM   948  C CG1 . VAL B 1 23  ? 35.709 -14.039 29.231  1.00 25.47  ? 23  VAL B CG1 1 
ATOM   949  C CG2 . VAL B 1 23  ? 37.390 -12.202 29.173  1.00 23.16  ? 23  VAL B CG2 1 
ATOM   950  N N   . ILE B 1 24  ? 34.925 -13.744 25.632  1.00 13.80  ? 24  ILE B N   1 
ATOM   951  C CA  . ILE B 1 24  ? 33.915 -14.451 24.823  1.00 12.98  ? 24  ILE B CA  1 
ATOM   952  C C   . ILE B 1 24  ? 34.509 -14.930 23.543  1.00 11.75  ? 24  ILE B C   1 
ATOM   953  O O   . ILE B 1 24  ? 35.578 -14.495 23.140  1.00 12.82  ? 24  ILE B O   1 
ATOM   954  C CB  . ILE B 1 24  ? 32.686 -13.534 24.530  1.00 13.52  ? 24  ILE B CB  1 
ATOM   955  C CG1 . ILE B 1 24  ? 33.066 -12.322 23.619  1.00 12.19  ? 24  ILE B CG1 1 
ATOM   956  C CG2 . ILE B 1 24  ? 32.082 -13.050 25.821  1.00 15.87  ? 24  ILE B CG2 1 
ATOM   957  C CD1 . ILE B 1 24  ? 31.956 -11.358 23.322  1.00 13.92  ? 24  ILE B CD1 1 
ATOM   958  N N   . SER B 1 25  ? 33.828 -15.828 22.857  1.00 11.96  ? 25  SER B N   1 
ATOM   959  C CA  . SER B 1 25  ? 34.309 -16.367 21.582  1.00 12.15  ? 25  SER B CA  1 
ATOM   960  C C   . SER B 1 25  ? 33.106 -16.636 20.654  1.00 11.65  ? 25  SER B C   1 
ATOM   961  O O   . SER B 1 25  ? 32.004 -16.889 21.147  1.00 12.19  ? 25  SER B O   1 
ATOM   962  C CB  . SER B 1 25  ? 35.054 -17.671 21.800  1.00 13.00  ? 25  SER B CB  1 
ATOM   963  O OG  . SER B 1 25  ? 35.582 -18.103 20.586  1.00 15.00  ? 25  SER B OG  1 
ATOM   964  N N   . LEU B 1 26  ? 33.358 -16.592 19.339  1.00 11.55  ? 26  LEU B N   1 
ATOM   965  C CA  . LEU B 1 26  ? 32.371 -17.004 18.324  1.00 12.36  ? 26  LEU B CA  1 
ATOM   966  C C   . LEU B 1 26  ? 32.690 -18.400 17.805  1.00 14.64  ? 26  LEU B C   1 
ATOM   967  O O   . LEU B 1 26  ? 32.072 -18.818 16.841  1.00 17.62  ? 26  LEU B O   1 
ATOM   968  C CB  . LEU B 1 26  ? 32.329 -16.027 17.161  1.00 12.37  ? 26  LEU B CB  1 
ATOM   969  C CG  . LEU B 1 26  ? 32.048 -14.573 17.539  1.00 12.38  ? 26  LEU B CG  1 
ATOM   970  C CD1 . LEU B 1 26  ? 31.987 -13.716 16.294  1.00 12.37  ? 26  LEU B CD1 1 
ATOM   971  C CD2 . LEU B 1 26  ? 30.825 -14.401 18.432  1.00 15.14  ? 26  LEU B CD2 1 
ATOM   972  N N   . SER B 1 27  ? 33.576 -19.145 18.456  1.00 15.53  ? 27  SER B N   1 
ATOM   973  C CA  . SER B 1 27  ? 34.026 -20.454 17.935  1.00 20.65  ? 27  SER B CA  1 
ATOM   974  C C   . SER B 1 27  ? 34.204 -21.375 19.129  1.00 21.62  ? 27  SER B C   1 
ATOM   975  O O   . SER B 1 27  ? 34.223 -20.926 20.298  1.00 20.71  ? 27  SER B O   1 
ATOM   976  C CB  . SER B 1 27  ? 35.323 -20.286 17.137  1.00 26.69  ? 27  SER B CB  1 
ATOM   977  O OG  . SER B 1 27  ? 36.312 -19.694 17.911  1.00 42.74  ? 27  SER B OG  1 
ATOM   978  N N   . GLY B 1 28  ? 34.280 -22.669 18.835  1.00 27.66  ? 28  GLY B N   1 
ATOM   979  C CA  . GLY B 1 28  ? 34.537 -23.697 19.827  1.00 27.97  ? 28  GLY B CA  1 
ATOM   980  C C   . GLY B 1 28  ? 33.357 -24.037 20.714  1.00 26.65  ? 28  GLY B C   1 
ATOM   981  O O   . GLY B 1 28  ? 32.228 -23.574 20.533  1.00 25.28  ? 28  GLY B O   1 
ATOM   982  N N   . ASP B 1 29  ? 33.671 -24.840 21.716  1.00 30.23  ? 29  ASP B N   1 
ATOM   983  C CA  . ASP B 1 29  ? 32.695 -25.415 22.606  1.00 37.12  ? 29  ASP B CA  1 
ATOM   984  C C   . ASP B 1 29  ? 31.906 -24.402 23.395  1.00 29.88  ? 29  ASP B C   1 
ATOM   985  O O   . ASP B 1 29  ? 30.805 -24.709 23.836  1.00 36.22  ? 29  ASP B O   1 
ATOM   986  C CB  . ASP B 1 29  ? 33.371 -26.417 23.565  1.00 41.33  ? 29  ASP B CB  1 
ATOM   987  C CG  . ASP B 1 29  ? 33.928 -27.623 22.834  1.00 45.89  ? 29  ASP B CG  1 
ATOM   988  O OD1 . ASP B 1 29  ? 33.468 -27.896 21.695  1.00 58.49  ? 29  ASP B OD1 1 
ATOM   989  O OD2 . ASP B 1 29  ? 34.818 -28.283 23.410  1.00 63.55  ? 29  ASP B OD2 1 
ATOM   990  N N   . HIS B 1 30  ? 32.433 -23.199 23.543  1.00 24.70  ? 30  HIS B N   1 
ATOM   991  C CA  . HIS B 1 30  ? 31.751 -22.180 24.303  1.00 23.99  ? 30  HIS B CA  1 
ATOM   992  C C   . HIS B 1 30  ? 31.396 -20.954 23.466  1.00 19.84  ? 30  HIS B C   1 
ATOM   993  O O   . HIS B 1 30  ? 31.108 -19.879 23.989  1.00 18.63  ? 30  HIS B O   1 
ATOM   994  C CB  . HIS B 1 30  ? 32.584 -21.772 25.485  1.00 29.37  ? 30  HIS B CB  1 
ATOM   995  C CG  . HIS B 1 30  ? 32.920 -22.925 26.364  1.00 40.91  ? 30  HIS B CG  1 
ATOM   996  N ND1 . HIS B 1 30  ? 31.975 -23.535 27.159  1.00 53.16  ? 30  HIS B ND1 1 
ATOM   997  C CD2 . HIS B 1 30  ? 34.048 -23.658 26.483  1.00 49.30  ? 30  HIS B CD2 1 
ATOM   998  C CE1 . HIS B 1 30  ? 32.525 -24.557 27.782  1.00 54.26  ? 30  HIS B CE1 1 
ATOM   999  N NE2 . HIS B 1 30  ? 33.788 -24.643 27.401  1.00 61.96  ? 30  HIS B NE2 1 
ATOM   1000 N N   . SER B 1 31  ? 31.248 -21.145 22.171  1.00 16.99  ? 31  SER B N   1 
ATOM   1001 C CA  . SER B 1 31  ? 30.810 -20.114 21.275  1.00 14.66  ? 31  SER B CA  1 
ATOM   1002 C C   . SER B 1 31  ? 29.515 -19.459 21.801  1.00 13.92  ? 31  SER B C   1 
ATOM   1003 O O   . SER B 1 31  ? 28.590 -20.154 22.217  1.00 16.48  ? 31  SER B O   1 
ATOM   1004 C CB  . SER B 1 31  ? 30.566 -20.731 19.898  1.00 15.68  ? 31  SER B CB  1 
ATOM   1005 O OG  . SER B 1 31  ? 30.041 -19.713 19.065  1.00 15.48  ? 31  SER B OG  1 
ATOM   1006 N N   . ILE B 1 32  ? 29.391 -18.135 21.597  1.00 12.44  ? 32  ILE B N   1 
ATOM   1007 C CA  . ILE B 1 32  ? 28.173 -17.421 21.895  1.00 11.89  ? 32  ILE B CA  1 
ATOM   1008 C C   . ILE B 1 32  ? 27.171 -17.352 20.744  1.00 10.78  ? 32  ILE B C   1 
ATOM   1009 O O   . ILE B 1 32  ? 26.085 -16.768 20.873  1.00 10.88  ? 32  ILE B O   1 
ATOM   1010 C CB  . ILE B 1 32  ? 28.386 -16.064 22.470  1.00 12.24  ? 32  ILE B CB  1 
ATOM   1011 C CG1 . ILE B 1 32  ? 29.009 -15.108 21.455  1.00 12.70  ? 32  ILE B CG1 1 
ATOM   1012 C CG2 . ILE B 1 32  ? 29.257 -16.177 23.745  1.00 15.67  ? 32  ILE B CG2 1 
ATOM   1013 C CD1 . ILE B 1 32  ? 29.153 -13.680 21.969  1.00 14.48  ? 32  ILE B CD1 1 
ATOM   1014 N N   . ILE B 1 33  ? 27.523 -17.930 19.605  1.00 10.53  ? 33  ILE B N   1 
ATOM   1015 C CA  . ILE B 1 33  ? 26.562 -18.039 18.535  1.00 10.60  ? 33  ILE B CA  1 
ATOM   1016 C C   . ILE B 1 33  ? 25.304 -18.751 18.999  1.00 9.01   ? 33  ILE B C   1 
ATOM   1017 O O   . ILE B 1 33  ? 25.379 -19.798 19.595  1.00 10.88  ? 33  ILE B O   1 
ATOM   1018 C CB  . ILE B 1 33  ? 27.190 -18.750 17.321  1.00 11.50  ? 33  ILE B CB  1 
ATOM   1019 C CG1 . ILE B 1 33  ? 28.383 -18.016 16.761  1.00 14.15  ? 33  ILE B CG1 1 
ATOM   1020 C CG2 . ILE B 1 33  ? 26.146 -19.057 16.263  1.00 12.67  ? 33  ILE B CG2 1 
ATOM   1021 C CD1 . ILE B 1 33  ? 28.054 -16.712 16.154  1.00 14.27  ? 33  ILE B CD1 1 
ATOM   1022 N N   . GLY B 1 34  ? 24.139 -18.161 18.709  1.00 9.28   ? 34  GLY B N   1 
ATOM   1023 C CA  . GLY B 1 34  ? 22.886 -18.740 19.142  1.00 10.30  ? 34  GLY B CA  1 
ATOM   1024 C C   . GLY B 1 34  ? 22.453 -18.387 20.546  1.00 9.32   ? 34  GLY B C   1 
ATOM   1025 O O   . GLY B 1 34  ? 21.369 -18.777 20.957  1.00 10.76  ? 34  GLY B O   1 
ATOM   1026 N N   . ARG B 1 35  ? 23.273 -17.671 21.294  1.00 9.57   ? 35  ARG B N   1 
ATOM   1027 C CA  . ARG B 1 35  ? 22.889 -17.134 22.589  1.00 9.36   ? 35  ARG B CA  1 
ATOM   1028 C C   . ARG B 1 35  ? 22.092 -15.855 22.416  1.00 8.54   ? 35  ARG B C   1 
ATOM   1029 O O   . ARG B 1 35  ? 22.186 -15.176 21.393  1.00 9.69   ? 35  ARG B O   1 
ATOM   1030 C CB  . ARG B 1 35  ? 24.087 -16.902 23.500  1.00 9.29   ? 35  ARG B CB  1 
ATOM   1031 C CG  . ARG B 1 35  ? 24.863 -18.159 23.816  1.00 11.69  ? 35  ARG B CG  1 
ATOM   1032 C CD  . ARG B 1 35  ? 24.204 -19.121 24.689  1.00 14.91  ? 35  ARG B CD  1 
ATOM   1033 N NE  . ARG B 1 35  ? 25.107 -20.219 25.074  1.00 21.35  ? 35  ARG B NE  1 
ATOM   1034 C CZ  . ARG B 1 35  ? 24.727 -21.296 25.685  1.00 22.07  ? 35  ARG B CZ  1 
ATOM   1035 N NH1 . ARG B 1 35  ? 23.460 -21.456 26.026  1.00 21.12  ? 35  ARG B NH1 1 
ATOM   1036 N NH2 . ARG B 1 35  ? 25.622 -22.196 25.987  1.00 25.45  ? 35  ARG B NH2 1 
ATOM   1037 N N   . THR B 1 36  ? 21.274 -15.547 23.412  1.00 9.08   ? 36  THR B N   1 
ATOM   1038 C CA  . THR B 1 36  ? 20.475 -14.330 23.402  1.00 9.13   ? 36  THR B CA  1 
ATOM   1039 C C   . THR B 1 36  ? 21.215 -13.172 24.089  1.00 8.78   ? 36  THR B C   1 
ATOM   1040 O O   . THR B 1 36  ? 21.621 -13.290 25.244  1.00 9.65   ? 36  THR B O   1 
ATOM   1041 C CB  . THR B 1 36  ? 19.143 -14.588 24.067  1.00 10.31  ? 36  THR B CB  1 
ATOM   1042 O OG1 . THR B 1 36  ? 18.447 -15.619 23.345  1.00 12.86  ? 36  THR B OG1 1 
ATOM   1043 C CG2 . THR B 1 36  ? 18.269 -13.364 24.117  1.00 12.10  ? 36  THR B CG2 1 
ATOM   1044 N N   . LEU B 1 37  ? 21.391 -12.098 23.344  1.00 8.35   ? 37  LEU B N   1 
ATOM   1045 C CA  . LEU B 1 37  ? 21.932 -10.856 23.835  1.00 8.37   ? 37  LEU B CA  1 
ATOM   1046 C C   . LEU B 1 37  ? 20.801 -10.056 24.469  1.00 8.02   ? 37  LEU B C   1 
ATOM   1047 O O   . LEU B 1 37  ? 19.738 -9.932  23.866  1.00 9.51   ? 37  LEU B O   1 
ATOM   1048 C CB  . LEU B 1 37  ? 22.544 -10.114 22.684  1.00 8.80   ? 37  LEU B CB  1 
ATOM   1049 C CG  . LEU B 1 37  ? 23.229 -8.776  23.011  1.00 9.35   ? 37  LEU B CG  1 
ATOM   1050 C CD1 . LEU B 1 37  ? 24.464 -8.978  23.883  1.00 11.48  ? 37  LEU B CD1 1 
ATOM   1051 C CD2 . LEU B 1 37  ? 23.608 -8.031  21.726  1.00 10.15  ? 37  LEU B CD2 1 
ATOM   1052 N N   . VAL B 1 38  ? 21.019 -9.528  25.673  1.00 8.18   ? 38  VAL B N   1 
ATOM   1053 C CA  . VAL B 1 38  ? 20.013 -8.775  26.387  1.00 9.04   ? 38  VAL B CA  1 
ATOM   1054 C C   . VAL B 1 38  ? 20.546 -7.431  26.821  1.00 9.01   ? 38  VAL B C   1 
ATOM   1055 O O   . VAL B 1 38  ? 21.735 -7.263  27.142  1.00 9.56   ? 38  VAL B O   1 
ATOM   1056 C CB  . VAL B 1 38  ? 19.422 -9.565  27.575  1.00 10.33  ? 38  VAL B CB  1 
ATOM   1057 C CG1 . VAL B 1 38  ? 18.883 -10.899 27.160  1.00 11.00  ? 38  VAL B CG1 1 
ATOM   1058 C CG2 . VAL B 1 38  ? 20.362 -9.675  28.719  1.00 12.34  ? 38  VAL B CG2 1 
ATOM   1059 N N   . VAL B 1 39  ? 19.654 -6.443  26.882  1.00 9.80   ? 39  VAL B N   1 
ATOM   1060 C CA  . VAL B 1 39  ? 19.922 -5.130  27.459  1.00 9.37   ? 39  VAL B CA  1 
ATOM   1061 C C   . VAL B 1 39  ? 18.807 -4.789  28.403  1.00 9.51   ? 39  VAL B C   1 
ATOM   1062 O O   . VAL B 1 39  ? 17.611 -4.894  28.073  1.00 10.34  ? 39  VAL B O   1 
ATOM   1063 C CB  . VAL B 1 39  ? 20.132 -4.033  26.405  1.00 11.14  ? 39  VAL B CB  1 
ATOM   1064 C CG1 . VAL B 1 39  ? 19.037 -3.817  25.479  1.00 14.62  ? 39  VAL B CG1 1 
ATOM   1065 C CG2 . VAL B 1 39  ? 20.593 -2.719  27.033  1.00 13.99  ? 39  VAL B CG2 1 
ATOM   1066 N N   . HIS B 1 40  ? 19.132 -4.337  29.589  1.00 9.27   ? 40  HIS B N   1 
ATOM   1067 C CA  . HIS B 1 40  ? 18.135 -3.894  30.555  1.00 10.45  ? 40  HIS B CA  1 
ATOM   1068 C C   . HIS B 1 40  ? 17.478 -2.625  30.079  1.00 11.69  ? 40  HIS B C   1 
ATOM   1069 O O   . HIS B 1 40  ? 18.185 -1.646  29.770  1.00 13.31  ? 40  HIS B O   1 
ATOM   1070 C CB  . HIS B 1 40  ? 18.807 -3.586  31.897  1.00 11.77  ? 40  HIS B CB  1 
ATOM   1071 C CG  . HIS B 1 40  ? 19.133 -4.803  32.649  1.00 12.73  ? 40  HIS B CG  1 
ATOM   1072 N ND1 . HIS B 1 40  ? 19.936 -5.858  32.316  1.00 17.28  ? 40  HIS B ND1 1 
ATOM   1073 C CD2 . HIS B 1 40  ? 18.538 -5.174  33.784  1.00 19.31  ? 40  HIS B CD2 1 
ATOM   1074 C CE1 . HIS B 1 40  ? 19.971 -6.729  33.323  1.00 14.06  ? 40  HIS B CE1 1 
ATOM   1075 N NE2 . HIS B 1 40  ? 19.095 -6.355  34.203  1.00 25.48  ? 40  HIS B NE2 1 
ATOM   1076 N N   . GLU B 1 41  ? 16.149 -2.579  30.078  1.00 11.96  ? 41  GLU B N   1 
ATOM   1077 C CA  . GLU B 1 41  ? 15.451 -1.379  29.715  1.00 12.56  ? 41  GLU B CA  1 
ATOM   1078 C C   . GLU B 1 41  ? 15.399 -0.331  30.840  1.00 13.72  ? 41  GLU B C   1 
ATOM   1079 O O   . GLU B 1 41  ? 15.313 0.841   30.585  1.00 15.92  ? 41  GLU B O   1 
ATOM   1080 C CB  . GLU B 1 41  ? 14.044 -1.730  29.183  1.00 14.20  ? 41  GLU B CB  1 
ATOM   1081 C CG  . GLU B 1 41  ? 14.134 -2.464  27.865  1.00 15.04  ? 41  GLU B CG  1 
ATOM   1082 C CD  . GLU B 1 41  ? 12.835 -2.860  27.272  1.00 17.72  ? 41  GLU B CD  1 
ATOM   1083 O OE1 . GLU B 1 41  ? 11.878 -3.046  28.059  1.00 28.36  ? 41  GLU B OE1 1 
ATOM   1084 O OE2 . GLU B 1 41  ? 12.702 -2.999  26.086  1.00 19.15  ? 41  GLU B OE2 1 
ATOM   1085 N N   . LYS B 1 42  ? 15.506 -0.780  32.102  1.00 15.11  ? 42  LYS B N   1 
ATOM   1086 C CA  . LYS B 1 42  ? 15.632 0.173   33.234  1.00 17.00  ? 42  LYS B CA  1 
ATOM   1087 C C   . LYS B 1 42  ? 17.067 0.666   33.327  1.00 15.89  ? 42  LYS B C   1 
ATOM   1088 O O   . LYS B 1 42  ? 18.005 -0.159  33.298  1.00 18.29  ? 42  LYS B O   1 
ATOM   1089 C CB  . LYS B 1 42  ? 15.264 -0.522  34.544  1.00 21.65  ? 42  LYS B CB  1 
ATOM   1090 C CG  . LYS B 1 42  ? 15.314 0.416   35.783  1.00 27.22  ? 42  LYS B CG  1 
ATOM   1091 C CD  . LYS B 1 42  ? 14.296 0.031   36.835  1.00 41.40  ? 42  LYS B CD  1 
ATOM   1092 C CE  . LYS B 1 42  ? 14.210 1.109   37.919  1.00 56.96  ? 42  LYS B CE  1 
ATOM   1093 N NZ  . LYS B 1 42  ? 13.733 2.428   37.383  1.00 59.80  ? 42  LYS B NZ  1 
ATOM   1094 N N   . ALA B 1 43  ? 17.289 1.965   33.477  1.00 15.66  ? 43  ALA B N   1 
ATOM   1095 C CA  . ALA B 1 43  ? 18.615 2.559   33.646  1.00 16.80  ? 43  ALA B CA  1 
ATOM   1096 C C   . ALA B 1 43  ? 19.077 2.371   35.083  1.00 20.39  ? 43  ALA B C   1 
ATOM   1097 O O   . ALA B 1 43  ? 18.276 2.322   36.021  1.00 23.88  ? 43  ALA B O   1 
ATOM   1098 C CB  . ALA B 1 43  ? 18.574 4.024   33.309  1.00 19.98  ? 43  ALA B CB  1 
ATOM   1099 N N   . GLY B 1 44  ? 20.399 2.263   35.217  1.00 22.80  ? 44  GLY B N   1 
ATOM   1100 C CA  . GLY B 1 44  ? 20.986 1.877   36.537  1.00 33.90  ? 44  GLY B CA  1 
ATOM   1101 C C   . GLY B 1 44  ? 20.872 0.367   36.802  1.00 49.03  ? 44  GLY B C   1 
ATOM   1102 O O   . GLY B 1 44  ? 21.545 -0.384  36.100  1.00 50.17  ? 44  GLY B O   1 
ATOM   1103 N N   . ALA B 1 45  ? 20.047 -0.080  37.776  1.00 69.89  ? 45  ALA B N   1 
ATOM   1104 C CA  . ALA B 1 45  ? 20.084 -1.495  38.322  1.00 63.77  ? 45  ALA B CA  1 
ATOM   1105 C C   . ALA B 1 45  ? 18.745 -2.258  38.635  1.00 73.99  ? 45  ALA B C   1 
ATOM   1106 O O   . ALA B 1 45  ? 17.752 -1.661  39.065  1.00 84.24  ? 45  ALA B O   1 
ATOM   1107 C CB  . ALA B 1 45  ? 20.965 -1.535  39.570  1.00 66.17  ? 45  ALA B CB  1 
ATOM   1108 N N   . GLY B 1 46  ? 18.758 -3.588  38.445  1.00 69.51  ? 46  GLY B N   1 
ATOM   1109 C CA  . GLY B 1 46  ? 17.652 -4.482  38.888  1.00 59.73  ? 46  GLY B CA  1 
ATOM   1110 C C   . GLY B 1 46  ? 17.331 -5.683  38.007  1.00 65.61  ? 46  GLY B C   1 
ATOM   1111 O O   . GLY B 1 46  ? 17.589 -5.647  36.816  1.00 78.60  ? 46  GLY B O   1 
ATOM   1112 N N   . ALA B 1 47  ? 16.736 -6.748  38.584  1.00 49.61  ? 47  ALA B N   1 
ATOM   1113 C CA  . ALA B 1 47  ? 16.344 -7.998  37.830  1.00 51.67  ? 47  ALA B CA  1 
ATOM   1114 C C   . ALA B 1 47  ? 14.839 -8.258  37.719  1.00 60.29  ? 47  ALA B C   1 
ATOM   1115 O O   . ALA B 1 47  ? 14.436 -9.123  36.947  1.00 51.38  ? 47  ALA B O   1 
ATOM   1116 C CB  . ALA B 1 47  ? 16.998 -9.236  38.423  1.00 41.40  ? 47  ALA B CB  1 
ATOM   1117 N N   . GLY B 1 48  ? 14.001 -7.539  38.463  1.00 68.27  ? 48  GLY B N   1 
ATOM   1118 C CA  . GLY B 1 48  ? 12.546 -7.612  38.248  1.00 58.37  ? 48  GLY B CA  1 
ATOM   1119 C C   . GLY B 1 48  ? 12.156 -7.064  36.885  1.00 53.47  ? 48  GLY B C   1 
ATOM   1120 O O   . GLY B 1 48  ? 11.240 -6.188  36.778  1.00 46.39  ? 48  GLY B O   1 
ATOM   1121 N N   . SER B 1 49  ? 12.769 -7.686  35.865  1.00 47.99  ? 49  SER B N   1 
ATOM   1122 C CA  . SER B 1 49  ? 13.553 -6.935  34.914  1.00 37.62  ? 49  SER B CA  1 
ATOM   1123 C C   . SER B 1 49  ? 13.029 -6.957  33.434  1.00 18.41  ? 49  SER B C   1 
ATOM   1124 O O   . SER B 1 49  ? 12.997 -7.967  32.805  1.00 19.30  ? 49  SER B O   1 
ATOM   1125 C CB  . SER B 1 49  ? 15.047 -7.371  34.852  1.00 60.55  ? 49  SER B CB  1 
ATOM   1126 O OG  . SER B 1 49  ? 15.937 -6.524  35.595  1.00 63.87  ? 49  SER B OG  1 
ATOM   1127 N N   . ARG B 1 50  ? 12.750 -5.818  32.893  1.00 19.46  ? 50  ARG B N   1 
ATOM   1128 C CA  . ARG B 1 50  ? 12.352 -5.647  31.526  1.00 17.58  ? 50  ARG B CA  1 
ATOM   1129 C C   . ARG B 1 50  ? 13.619 -5.607  30.631  1.00 13.94  ? 50  ARG B C   1 
ATOM   1130 O O   . ARG B 1 50  ? 14.489 -4.823  30.843  1.00 16.23  ? 50  ARG B O   1 
ATOM   1131 C CB  . ARG B 1 50  ? 11.567 -4.367  31.335  1.00 26.66  ? 50  ARG B CB  1 
ATOM   1132 C CG  . ARG B 1 50  ? 10.240 -4.315  32.056  1.00 28.90  ? 50  ARG B CG  1 
ATOM   1133 C CD  . ARG B 1 50  ? 9.239  -3.510  31.222  1.00 43.93  ? 50  ARG B CD  1 
ATOM   1134 N NE  . ARG B 1 50  ? 8.378  -4.446  30.489  1.00 50.77  ? 50  ARG B NE  1 
ATOM   1135 C CZ  . ARG B 1 50  ? 7.188  -4.884  30.910  1.00 52.07  ? 50  ARG B CZ  1 
ATOM   1136 N NH1 . ARG B 1 50  ? 6.647  -4.448  32.054  1.00 59.50  ? 50  ARG B NH1 1 
ATOM   1137 N NH2 . ARG B 1 50  ? 6.512  -5.758  30.162  1.00 60.26  ? 50  ARG B NH2 1 
ATOM   1138 N N   . LEU B 1 51  ? 13.646 -6.483  29.621  1.00 13.90  ? 51  LEU B N   1 
ATOM   1139 C CA  . LEU B 1 51  ? 14.771 -6.643  28.709  1.00 12.86  ? 51  LEU B CA  1 
ATOM   1140 C C   . LEU B 1 51  ? 14.352 -6.393  27.289  1.00 12.89  ? 51  LEU B C   1 
ATOM   1141 O O   . LEU B 1 51  ? 13.322 -6.877  26.831  1.00 17.53  ? 51  LEU B O   1 
ATOM   1142 C CB  . LEU B 1 51  ? 15.326 -8.064  28.768  1.00 12.74  ? 51  LEU B CB  1 
ATOM   1143 C CG  . LEU B 1 51  ? 15.806 -8.525  30.128  1.00 12.21  ? 51  LEU B CG  1 
ATOM   1144 C CD1 . LEU B 1 51  ? 16.252 -10.012 30.042  1.00 13.99  ? 51  LEU B CD1 1 
ATOM   1145 C CD2 . LEU B 1 51  ? 16.907 -7.695  30.714  1.00 16.12  ? 51  LEU B CD2 1 
ATOM   1146 N N   . ALA B 1 52  ? 15.284 -5.816  26.508  1.00 10.65  ? 52  ALA B N   1 
ATOM   1147 C CA  . ALA B 1 52  ? 15.263 -5.940  25.059  1.00 11.01  ? 52  ALA B CA  1 
ATOM   1148 C C   . ALA B 1 52  ? 16.274 -7.031  24.702  1.00 10.23  ? 52  ALA B C   1 
ATOM   1149 O O   . ALA B 1 52  ? 17.258 -7.188  25.378  1.00 12.16  ? 52  ALA B O   1 
ATOM   1150 C CB  . ALA B 1 52  ? 15.625 -4.635  24.383  1.00 11.67  ? 52  ALA B CB  1 
ATOM   1151 N N   . SER B 1 53  ? 16.008 -7.794  23.643  1.00 10.35  ? 53  SER B N   1 
ATOM   1152 C CA  . SER B 1 53  ? 16.825 -8.992  23.385  1.00 10.74  ? 53  SER B CA  1 
ATOM   1153 C C   . SER B 1 53  ? 16.810 -9.323  21.906  1.00 9.35   ? 53  SER B C   1 
ATOM   1154 O O   . SER B 1 53  ? 15.922 -8.915  21.142  1.00 10.41  ? 53  SER B O   1 
ATOM   1155 C CB  . SER B 1 53  ? 16.313 -10.155 24.170  1.00 12.98  ? 53  SER B CB  1 
ATOM   1156 O OG  . SER B 1 53  ? 15.068 -10.603 23.787  1.00 16.21  ? 53  SER B OG  1 
ATOM   1157 N N   . GLY B 1 54  ? 17.787 -10.132 21.532  1.00 9.55   ? 54  GLY B N   1 
ATOM   1158 C CA  . GLY B 1 54  ? 17.858 -10.739 20.235  1.00 10.22  ? 54  GLY B CA  1 
ATOM   1159 C C   . GLY B 1 54  ? 18.894 -11.841 20.201  1.00 9.21   ? 54  GLY B C   1 
ATOM   1160 O O   . GLY B 1 54  ? 19.854 -11.798 20.956  1.00 10.07  ? 54  GLY B O   1 
ATOM   1161 N N   . VAL B 1 55  ? 18.669 -12.830 19.341  1.00 9.28   ? 55  VAL B N   1 
ATOM   1162 C CA  . VAL B 1 55  ? 19.566 -13.961 19.269  1.00 9.36   ? 55  VAL B CA  1 
ATOM   1163 C C   . VAL B 1 55  ? 20.752 -13.614 18.379  1.00 9.32   ? 55  VAL B C   1 
ATOM   1164 O O   . VAL B 1 55  ? 20.595 -12.972 17.308  1.00 10.53  ? 55  VAL B O   1 
ATOM   1165 C CB  . VAL B 1 55  ? 18.811 -15.182 18.710  1.00 10.57  ? 55  VAL B CB  1 
ATOM   1166 C CG1 . VAL B 1 55  ? 19.708 -16.387 18.589  1.00 11.78  ? 55  VAL B CG1 1 
ATOM   1167 C CG2 . VAL B 1 55  ? 17.588 -15.536 19.573  1.00 13.12  ? 55  VAL B CG2 1 
ATOM   1168 N N   . ILE B 1 56  ? 21.941 -14.038 18.805  1.00 8.64   ? 56  ILE B N   1 
ATOM   1169 C CA  . ILE B 1 56  ? 23.172 -13.818 18.013  1.00 8.74   ? 56  ILE B CA  1 
ATOM   1170 C C   . ILE B 1 56  ? 23.205 -14.814 16.844  1.00 9.09   ? 56  ILE B C   1 
ATOM   1171 O O   . ILE B 1 56  ? 23.354 -16.005 17.062  1.00 10.97  ? 56  ILE B O   1 
ATOM   1172 C CB  . ILE B 1 56  ? 24.404 -13.943 18.917  1.00 9.12   ? 56  ILE B CB  1 
ATOM   1173 C CG1 . ILE B 1 56  ? 24.345 -12.904 20.043  1.00 9.78   ? 56  ILE B CG1 1 
ATOM   1174 C CG2 . ILE B 1 56  ? 25.669 -13.821 18.093  1.00 11.01  ? 56  ILE B CG2 1 
ATOM   1175 C CD1 . ILE B 1 56  ? 25.396 -13.108 21.112  1.00 10.75  ? 56  ILE B CD1 1 
ATOM   1176 N N   . GLY B 1 57  ? 23.024 -14.274 15.633  1.00 8.83   ? 57  GLY B N   1 
ATOM   1177 C CA  . GLY B 1 57  ? 22.959 -15.104 14.457  1.00 9.05   ? 57  GLY B CA  1 
ATOM   1178 C C   . GLY B 1 57  ? 24.193 -14.973 13.596  1.00 9.98   ? 57  GLY B C   1 
ATOM   1179 O O   . GLY B 1 57  ? 24.836 -13.937 13.543  1.00 12.94  ? 57  GLY B O   1 
ATOM   1180 N N   . ILE B 1 58  ? 24.519 -16.029 12.909  1.00 9.73   ? 58  ILE B N   1 
ATOM   1181 C CA  . ILE B 1 58  ? 25.702 -16.055 12.021  1.00 10.52  ? 58  ILE B CA  1 
ATOM   1182 C C   . ILE B 1 58  ? 25.440 -15.205 10.797  1.00 12.63  ? 58  ILE B C   1 
ATOM   1183 O O   . ILE B 1 58  ? 24.396 -15.347 10.117  1.00 14.50  ? 58  ILE B O   1 
ATOM   1184 C CB  . ILE B 1 58  ? 26.022 -17.457 11.530  1.00 12.60  ? 58  ILE B CB  1 
ATOM   1185 C CG1 . ILE B 1 58  ? 26.245 -18.387 12.675  1.00 12.74  ? 58  ILE B CG1 1 
ATOM   1186 C CG2 . ILE B 1 58  ? 27.183 -17.450 10.581  1.00 15.92  ? 58  ILE B CG2 1 
ATOM   1187 C CD1 . ILE B 1 58  ? 26.173 -19.897 12.347  1.00 14.22  ? 58  ILE B CD1 1 
ATOM   1188 N N   . ALA B 1 59  ? 26.421 -14.394 10.454  1.00 13.13  ? 59  ALA B N   1 
ATOM   1189 C CA  . ALA B 1 59  ? 26.424 -13.696 9.189   1.00 15.36  ? 59  ALA B CA  1 
ATOM   1190 C C   . ALA B 1 59  ? 27.390 -14.343 8.212   1.00 18.13  ? 59  ALA B C   1 
ATOM   1191 O O   . ALA B 1 59  ? 27.070 -14.597 7.016   1.00 22.73  ? 59  ALA B O   1 
ATOM   1192 C CB  . ALA B 1 59  ? 26.693 -12.244 9.354   1.00 16.21  ? 59  ALA B CB  1 
ATOM   1193 N N   . GLN B 1 60  ? 28.562 -14.661 8.705   1.00 17.87  ? 60  GLN B N   1 
ATOM   1194 C CA  . GLN B 1 60  ? 29.563 -15.320 7.895   1.00 22.27  ? 60  GLN B CA  1 
ATOM   1195 C C   . GLN B 1 60  ? 30.327 -16.248 8.840   1.00 21.28  ? 60  GLN B C   1 
ATOM   1196 O O   . GLN B 1 60  ? 30.608 -15.929 10.006  1.00 16.94  ? 60  GLN B O   1 
ATOM   1197 C CB  . GLN B 1 60  ? 30.581 -14.348 7.368   1.00 33.88  ? 60  GLN B CB  1 
ATOM   1198 C CG  . GLN B 1 60  ? 30.161 -13.168 6.537   1.00 33.14  ? 60  GLN B CG  1 
ATOM   1199 C CD  . GLN B 1 60  ? 31.475 -12.479 6.153   1.00 39.91  ? 60  GLN B CD  1 
ATOM   1200 O OE1 . GLN B 1 60  ? 32.553 -12.904 6.624   1.00 58.68  ? 60  GLN B OE1 1 
ATOM   1201 N NE2 . GLN B 1 60  ? 31.418 -11.448 5.322   1.00 62.11  ? 60  GLN B NE2 1 
ATOM   1202 N N   . ALA B 1 61  ? 30.728 -17.397 8.356   1.00 28.03  ? 61  ALA B N   1 
ATOM   1203 C CA  . ALA B 1 61  ? 31.562 -18.215 9.188   1.00 29.78  ? 61  ALA B CA  1 
ATOM   1204 C C   . ALA B 1 61  ? 32.353 -19.188 8.280   1.00 43.78  ? 61  ALA B C   1 
ATOM   1205 O O   . ALA B 1 61  ? 31.811 -19.741 7.304   1.00 51.36  ? 61  ALA B O   1 
ATOM   1206 C CB  . ALA B 1 61  ? 30.708 -18.900 10.269  1.00 26.64  ? 61  ALA B CB  1 
ATOM   1207 N N   . GLY B 1 62  ? 33.658 -19.299 8.567   1.00 59.15  ? 62  GLY B N   1 
ATOM   1208 C CA  . GLY B 1 62  ? 34.590 -20.190 7.846   1.00 63.29  ? 62  GLY B CA  1 
ATOM   1209 C C   . GLY B 1 62  ? 36.035 -19.722 7.990   1.00 84.70  ? 62  GLY B C   1 
ATOM   1210 O O   . GLY B 1 62  ? 36.303 -18.585 8.400   1.00 78.80  ? 62  GLY B O   1 
ATOM   1211 N N   . ALA B 1 63  ? 36.982 -20.592 7.645   1.00 86.38  ? 63  ALA B N   1 
ATOM   1212 C CA  . ALA B 1 63  ? 38.397 -20.222 7.717   1.00 99.30  ? 63  ALA B CA  1 
ATOM   1213 C C   . ALA B 1 63  ? 38.666 -18.972 6.847   1.00 96.90  ? 63  ALA B C   1 
ATOM   1214 O O   . ALA B 1 63  ? 38.473 -19.023 5.631   1.00 118.17 ? 63  ALA B O   1 
ATOM   1215 C CB  . ALA B 1 63  ? 39.281 -21.384 7.293   1.00 92.65  ? 63  ALA B CB  1 
ATOM   1216 N N   . GLY B 1 64  ? 39.094 -17.855 7.447   1.00 85.65  ? 64  GLY B N   1 
ATOM   1217 C CA  . GLY B 1 64  ? 39.477 -17.779 8.857   1.00 75.46  ? 64  GLY B CA  1 
ATOM   1218 C C   . GLY B 1 64  ? 38.888 -16.623 9.667   1.00 75.65  ? 64  GLY B C   1 
ATOM   1219 O O   . GLY B 1 64  ? 39.667 -15.881 10.299  1.00 71.43  ? 64  GLY B O   1 
ATOM   1220 N N   . ALA B 1 65  ? 37.541 -16.481 9.690   1.00 55.23  ? 65  ALA B N   1 
ATOM   1221 C CA  . ALA B 1 65  ? 36.851 -15.500 10.532  1.00 36.76  ? 65  ALA B CA  1 
ATOM   1222 C C   . ALA B 1 65  ? 35.383 -15.880 10.753  1.00 29.14  ? 65  ALA B C   1 
ATOM   1223 O O   . ALA B 1 65  ? 34.801 -16.733 10.080  1.00 37.27  ? 65  ALA B O   1 
ATOM   1224 C CB  . ALA B 1 65  ? 36.916 -14.104 9.922   1.00 36.61  ? 65  ALA B CB  1 
ATOM   1225 N N   . THR B 1 66  ? 34.763 -15.196 11.695  1.00 21.30  ? 66  THR B N   1 
ATOM   1226 C CA  . THR B 1 66  ? 33.358 -15.331 11.989  1.00 16.84  ? 66  THR B CA  1 
ATOM   1227 C C   . THR B 1 66  ? 32.776 -13.953 12.213  1.00 12.87  ? 66  THR B C   1 
ATOM   1228 O O   . THR B 1 66  ? 33.396 -13.128 12.901  1.00 13.94  ? 66  THR B O   1 
ATOM   1229 C CB  . THR B 1 66  ? 33.078 -16.236 13.223  1.00 22.32  ? 66  THR B CB  1 
ATOM   1230 O OG1 . THR B 1 66  ? 33.750 -17.488 13.151  1.00 31.62  ? 66  THR B OG1 1 
ATOM   1231 C CG2 . THR B 1 66  ? 31.582 -16.440 13.439  1.00 24.45  ? 66  THR B CG2 1 
ATOM   1232 N N   . LYS B 1 67  ? 31.581 -13.733 11.682  1.00 12.48  ? 67  LYS B N   1 
ATOM   1233 C CA  . LYS B 1 67  ? 30.824 -12.522 11.914  1.00 12.81  ? 67  LYS B CA  1 
ATOM   1234 C C   . LYS B 1 67  ? 29.437 -12.913 12.319  1.00 12.63  ? 67  LYS B C   1 
ATOM   1235 O O   . LYS B 1 67  ? 28.852 -13.870 11.776  1.00 15.39  ? 67  LYS B O   1 
ATOM   1236 C CB  . LYS B 1 67  ? 30.799 -11.631 10.727  1.00 13.73  ? 67  LYS B CB  1 
ATOM   1237 C CG  . LYS B 1 67  ? 32.138 -11.171 10.315  1.00 17.33  ? 67  LYS B CG  1 
ATOM   1238 C CD  . LYS B 1 67  ? 32.126 -10.280 9.104   1.00 19.98  ? 67  LYS B CD  1 
ATOM   1239 C CE  . LYS B 1 67  ? 33.474 -9.947  8.494   1.00 28.42  ? 67  LYS B CE  1 
ATOM   1240 N NZ  . LYS B 1 67  ? 34.434 -9.489  9.513   1.00 32.20  ? 67  LYS B NZ  1 
ATOM   1241 N N   . ALA B 1 68  ? 28.838 -12.170 13.226  1.00 10.87  ? 68  ALA B N   1 
ATOM   1242 C CA  . ALA B 1 68  ? 27.495 -12.450 13.720  1.00 11.10  ? 68  ALA B CA  1 
ATOM   1243 C C   . ALA B 1 68  ? 26.793 -11.167 14.024  1.00 9.43   ? 68  ALA B C   1 
ATOM   1244 O O   . ALA B 1 68  ? 27.408 -10.099 14.157  1.00 10.39  ? 68  ALA B O   1 
ATOM   1245 C CB  . ALA B 1 68  ? 27.596 -13.352 14.969  1.00 12.04  ? 68  ALA B CB  1 
ATOM   1246 N N   . VAL B 1 69  ? 25.486 -11.225 14.177  1.00 9.45   ? 69  VAL B N   1 
ATOM   1247 C CA  . VAL B 1 69  ? 24.656 -10.066 14.371  1.00 9.14   ? 69  VAL B CA  1 
ATOM   1248 C C   . VAL B 1 69  ? 23.477 -10.423 15.277  1.00 8.39   ? 69  VAL B C   1 
ATOM   1249 O O   . VAL B 1 69  ? 22.851 -11.470 15.079  1.00 9.39   ? 69  VAL B O   1 
ATOM   1250 C CB  . VAL B 1 69  ? 24.096 -9.509  13.054  1.00 11.72  ? 69  VAL B CB  1 
ATOM   1251 C CG1 . VAL B 1 69  ? 23.312 -8.239  13.238  1.00 12.84  ? 69  VAL B CG1 1 
ATOM   1252 C CG2 . VAL B 1 69  ? 25.084 -9.369  11.985  1.00 15.13  ? 69  VAL B CG2 1 
ATOM   1253 N N   . ALA B 1 70  ? 23.175 -9.569  16.245  1.00 8.35   ? 70  ALA B N   1 
ATOM   1254 C CA  . ALA B 1 70  ? 21.961 -9.643  17.026  1.00 8.49   ? 70  ALA B CA  1 
ATOM   1255 C C   . ALA B 1 70  ? 21.127 -8.438  16.756  1.00 8.27   ? 70  ALA B C   1 
ATOM   1256 O O   . ALA B 1 70  ? 21.575 -7.301  16.861  1.00 9.60   ? 70  ALA B O   1 
ATOM   1257 C CB  . ALA B 1 70  ? 22.277 -9.695  18.519  1.00 9.59   ? 70  ALA B CB  1 
ATOM   1258 N N   . VAL B 1 71  ? 19.857 -8.673  16.402  1.00 9.67   ? 71  VAL B N   1 
ATOM   1259 C CA  . VAL B 1 71  ? 18.856 -7.640  16.224  1.00 10.49  ? 71  VAL B CA  1 
ATOM   1260 C C   . VAL B 1 71  ? 18.074 -7.566  17.509  1.00 10.53  ? 71  VAL B C   1 
ATOM   1261 O O   . VAL B 1 71  ? 17.393 -8.499  17.886  1.00 12.31  ? 71  VAL B O   1 
ATOM   1262 C CB  . VAL B 1 71  ? 17.949 -7.949  15.037  1.00 12.71  ? 71  VAL B CB  1 
ATOM   1263 C CG1 . VAL B 1 71  ? 16.864 -6.899  14.889  1.00 16.21  ? 71  VAL B CG1 1 
ATOM   1264 C CG2 . VAL B 1 71  ? 18.718 -8.062  13.766  1.00 14.96  ? 71  VAL B CG2 1 
ATOM   1265 N N   . LEU B 1 72  ? 18.238 -6.471  18.240  1.00 11.28  ? 72  LEU B N   1 
ATOM   1266 C CA  . LEU B 1 72  ? 17.620 -6.294  19.549  1.00 11.75  ? 72  LEU B CA  1 
ATOM   1267 C C   . LEU B 1 72  ? 16.255 -5.667  19.371  1.00 12.30  ? 72  LEU B C   1 
ATOM   1268 O O   . LEU B 1 72  ? 16.102 -4.660  18.691  1.00 14.04  ? 72  LEU B O   1 
ATOM   1269 C CB  . LEU B 1 72  ? 18.462 -5.379  20.474  1.00 12.71  ? 72  LEU B CB  1 
ATOM   1270 C CG  . LEU B 1 72  ? 19.833 -5.934  20.854  1.00 12.77  ? 72  LEU B CG  1 
ATOM   1271 C CD1 . LEU B 1 72  ? 20.587 -4.843  21.595  1.00 15.78  ? 72  LEU B CD1 1 
ATOM   1272 C CD2 . LEU B 1 72  ? 19.704 -7.076  21.752  1.00 17.17  ? 72  LEU B CD2 1 
ATOM   1273 N N   . LYS B 1 73  ? 15.279 -6.228  20.066  1.00 12.43  ? 73  LYS B N   1 
ATOM   1274 C CA  . LYS B 1 73  ? 13.940 -5.695  20.067  1.00 14.88  ? 73  LYS B CA  1 
ATOM   1275 C C   . LYS B 1 73  ? 13.409 -5.758  21.468  1.00 14.13  ? 73  LYS B C   1 
ATOM   1276 O O   . LYS B 1 73  ? 13.568 -6.742  22.196  1.00 13.25  ? 73  LYS B O   1 
ATOM   1277 C CB  . LYS B 1 73  ? 13.026 -6.565  19.183  1.00 21.56  ? 73  LYS B CB  1 
ATOM   1278 C CG  . LYS B 1 73  ? 11.617 -6.128  19.091  1.00 25.17  ? 73  LYS B CG  1 
ATOM   1279 C CD  . LYS B 1 73  ? 11.409 -4.818  18.355  1.00 28.95  ? 73  LYS B CD  1 
ATOM   1280 C CE  . LYS B 1 73  ? 9.917  -4.451  18.220  1.00 37.92  ? 73  LYS B CE  1 
ATOM   1281 N NZ  . LYS B 1 73  ? 9.772  -3.216  17.422  1.00 45.79  ? 73  LYS B NZ  1 
ATOM   1282 N N   . GLY B 1 74  ? 12.815 -4.655  21.848  1.00 15.96  ? 74  GLY B N   1 
ATOM   1283 C CA  . GLY B 1 74  ? 12.210 -4.517  23.111  1.00 16.51  ? 74  GLY B CA  1 
ATOM   1284 C C   . GLY B 1 74  ? 10.877 -3.868  23.065  1.00 20.40  ? 74  GLY B C   1 
ATOM   1285 O O   . GLY B 1 74  ? 10.181 -3.866  22.047  1.00 25.66  ? 74  GLY B O   1 
ATOM   1286 N N   . ASP B 1 75  ? 10.512 -3.364  24.245  1.00 22.53  ? 75  ASP B N   1 
ATOM   1287 C CA  . ASP B 1 75  ? 9.265  -2.647  24.437  1.00 25.89  ? 75  ASP B CA  1 
ATOM   1288 C C   . ASP B 1 75  ? 9.353  -1.270  23.926  1.00 29.24  ? 75  ASP B C   1 
ATOM   1289 O O   . ASP B 1 75  ? 10.416 -0.639  23.925  1.00 26.31  ? 75  ASP B O   1 
ATOM   1290 C CB  . ASP B 1 75  ? 8.883  -2.628  25.911  1.00 26.66  ? 75  ASP B CB  1 
ATOM   1291 C CG  . ASP B 1 75  ? 8.833  -3.999  26.478  1.00 38.26  ? 75  ASP B CG  1 
ATOM   1292 O OD1 . ASP B 1 75  ? 7.849  -4.705  26.196  1.00 57.54  ? 75  ASP B OD1 1 
ATOM   1293 O OD2 . ASP B 1 75  ? 9.824  -4.369  27.154  1.00 33.34  ? 75  ASP B OD2 1 
ATOM   1294 N N   . GLY B 1 76  ? 8.219  -0.775  23.470  1.00 28.19  ? 76  GLY B N   1 
ATOM   1295 C CA  . GLY B 1 76  ? 8.089  0.553   22.926  1.00 33.50  ? 76  GLY B CA  1 
ATOM   1296 C C   . GLY B 1 76  ? 9.157  0.725   21.889  1.00 28.50  ? 76  GLY B C   1 
ATOM   1297 O O   . GLY B 1 76  ? 9.302  -0.095  20.998  1.00 28.25  ? 76  GLY B O   1 
ATOM   1298 N N   . PRO B 1 77  ? 9.966  1.752   22.078  1.00 30.63  ? 77  PRO B N   1 
ATOM   1299 C CA  . PRO B 1 77  ? 10.853 2.136   21.023  1.00 26.72  ? 77  PRO B CA  1 
ATOM   1300 C C   . PRO B 1 77  ? 12.234 1.487   21.072  1.00 19.31  ? 77  PRO B C   1 
ATOM   1301 O O   . PRO B 1 77  ? 13.033 1.784   20.187  1.00 19.35  ? 77  PRO B O   1 
ATOM   1302 C CB  . PRO B 1 77  ? 11.004 3.615   21.255  1.00 29.80  ? 77  PRO B CB  1 
ATOM   1303 C CG  . PRO B 1 77  ? 10.979 3.719   22.747  1.00 28.03  ? 77  PRO B CG  1 
ATOM   1304 C CD  . PRO B 1 77  ? 9.964  2.723   23.192  1.00 33.72  ? 77  PRO B CD  1 
ATOM   1305 N N   . VAL B 1 78  ? 12.488 0.543   22.000  1.00 18.74  ? 78  VAL B N   1 
ATOM   1306 C CA  . VAL B 1 78  ? 13.856 0.022   22.079  1.00 15.86  ? 78  VAL B CA  1 
ATOM   1307 C C   . VAL B 1 78  ? 14.169 -0.918  20.914  1.00 15.58  ? 78  VAL B C   1 
ATOM   1308 O O   . VAL B 1 78  ? 13.441 -1.907  20.660  1.00 16.87  ? 78  VAL B O   1 
ATOM   1309 C CB  . VAL B 1 78  ? 14.097 -0.695  23.367  1.00 19.12  ? 78  VAL B CB  1 
ATOM   1310 C CG1 . VAL B 1 78  ? 15.504 -1.226  23.406  1.00 19.44  ? 78  VAL B CG1 1 
ATOM   1311 C CG2 . VAL B 1 78  ? 13.855 0.280   24.505  1.00 19.39  ? 78  VAL B CG2 1 
ATOM   1312 N N   . GLN B 1 79  ? 15.248 -0.642  20.192  1.00 13.53  ? 79  GLN B N   1 
ATOM   1313 C CA  . GLN B 1 79  ? 15.666 -1.470  19.083  1.00 14.93  ? 79  GLN B CA  1 
ATOM   1314 C C   . GLN B 1 79  ? 17.124 -1.200  18.809  1.00 13.19  ? 79  GLN B C   1 
ATOM   1315 O O   . GLN B 1 79  ? 17.591 -0.072  19.008  1.00 13.99  ? 79  GLN B O   1 
ATOM   1316 C CB  . GLN B 1 79  ? 14.869 -1.292  17.832  1.00 20.65  ? 79  GLN B CB  1 
ATOM   1317 C CG  . GLN B 1 79  ? 14.893 0.109   17.349  1.00 21.16  ? 79  GLN B CG  1 
ATOM   1318 C CD  . GLN B 1 79  ? 13.913 0.341   16.204  1.00 39.03  ? 79  GLN B CD  1 
ATOM   1319 O OE1 . GLN B 1 79  ? 12.701 0.586   16.387  1.00 43.74  ? 79  GLN B OE1 1 
ATOM   1320 N NE2 . GLN B 1 79  ? 14.442 0.294   15.005  1.00 45.99  ? 79  GLN B NE2 1 
ATOM   1321 N N   . GLY B 1 80  ? 17.846 -2.173  18.327  1.00 12.36  ? 80  GLY B N   1 
ATOM   1322 C CA  . GLY B 1 80  ? 19.214 -1.986  17.946  1.00 13.19  ? 80  GLY B CA  1 
ATOM   1323 C C   . GLY B 1 80  ? 19.766 -3.113  17.147  1.00 10.54  ? 80  GLY B C   1 
ATOM   1324 O O   . GLY B 1 80  ? 19.100 -4.117  16.925  1.00 11.63  ? 80  GLY B O   1 
ATOM   1325 N N   . ILE B 1 81  ? 20.990 -2.925  16.677  1.00 10.13  ? 81  ILE B N   1 
ATOM   1326 C CA  . ILE B 1 81  ? 21.734 -3.912  15.918  1.00 9.74   ? 81  ILE B CA  1 
ATOM   1327 C C   . ILE B 1 81  ? 23.115 -3.965  16.523  1.00 9.12   ? 81  ILE B C   1 
ATOM   1328 O O   . ILE B 1 81  ? 23.782 -2.912  16.581  1.00 11.13  ? 81  ILE B O   1 
ATOM   1329 C CB  . ILE B 1 81  ? 21.785 -3.600  14.401  1.00 13.03  ? 81  ILE B CB  1 
ATOM   1330 C CG1 . ILE B 1 81  ? 20.441 -3.416  13.868  1.00 15.92  ? 81  ILE B CG1 1 
ATOM   1331 C CG2 . ILE B 1 81  ? 22.586 -4.662  13.659  1.00 16.48  ? 81  ILE B CG2 1 
ATOM   1332 C CD1 . ILE B 1 81  ? 19.800 -4.641  13.488  1.00 21.05  ? 81  ILE B CD1 1 
ATOM   1333 N N   . ILE B 1 82  ? 23.569 -5.145  16.904  1.00 8.32   ? 82  ILE B N   1 
ATOM   1334 C CA  . ILE B 1 82  ? 24.900 -5.330  17.446  1.00 7.89   ? 82  ILE B CA  1 
ATOM   1335 C C   . ILE B 1 82  ? 25.606 -6.407  16.656  1.00 8.05   ? 82  ILE B C   1 
ATOM   1336 O O   . ILE B 1 82  ? 25.121 -7.539  16.513  1.00 9.44   ? 82  ILE B O   1 
ATOM   1337 C CB  . ILE B 1 82  ? 24.840 -5.720  18.951  1.00 8.35   ? 82  ILE B CB  1 
ATOM   1338 C CG1 . ILE B 1 82  ? 24.115 -4.661  19.777  1.00 9.96   ? 82  ILE B CG1 1 
ATOM   1339 C CG2 . ILE B 1 82  ? 26.215 -5.995  19.480  1.00 8.76   ? 82  ILE B CG2 1 
ATOM   1340 C CD1 . ILE B 1 82  ? 24.856 -3.347  19.864  1.00 13.47  ? 82  ILE B CD1 1 
ATOM   1341 N N   . ASN B 1 83  ? 26.785 -6.063  16.161  1.00 7.73   ? 83  ASN B N   1 
ATOM   1342 C CA  . ASN B 1 83  ? 27.652 -6.900  15.384  1.00 8.40   ? 83  ASN B CA  1 
ATOM   1343 C C   . ASN B 1 83  ? 28.775 -7.472  16.257  1.00 8.18   ? 83  ASN B C   1 
ATOM   1344 O O   . ASN B 1 83  ? 29.265 -6.826  17.169  1.00 9.27   ? 83  ASN B O   1 
ATOM   1345 C CB  . ASN B 1 83  ? 28.263 -6.117  14.244  1.00 8.54   ? 83  ASN B CB  1 
ATOM   1346 C CG  . ASN B 1 83  ? 27.208 -5.519  13.378  1.00 9.68   ? 83  ASN B CG  1 
ATOM   1347 O OD1 . ASN B 1 83  ? 27.071 -4.223  13.302  1.00 13.73  ? 83  ASN B OD1 1 
ATOM   1348 N ND2 . ASN B 1 83  ? 26.443 -6.311  12.782  1.00 9.15   ? 83  ASN B ND2 1 
ATOM   1349 N N   . PHE B 1 84  ? 29.178 -8.693  15.913  1.00 8.78   ? 84  PHE B N   1 
ATOM   1350 C CA  . PHE B 1 84  ? 30.259 -9.391  16.589  1.00 9.47   ? 84  PHE B CA  1 
ATOM   1351 C C   . PHE B 1 84  ? 31.219 -9.924  15.515  1.00 9.73   ? 84  PHE B C   1 
ATOM   1352 O O   . PHE B 1 84  ? 30.776 -10.489 14.501  1.00 12.45  ? 84  PHE B O   1 
ATOM   1353 C CB  . PHE B 1 84  ? 29.762 -10.620 17.359  1.00 10.85  ? 84  PHE B CB  1 
ATOM   1354 C CG  . PHE B 1 84  ? 28.768 -10.312 18.448  1.00 9.99   ? 84  PHE B CG  1 
ATOM   1355 C CD1 . PHE B 1 84  ? 27.448 -10.013 18.175  1.00 10.41  ? 84  PHE B CD1 1 
ATOM   1356 C CD2 . PHE B 1 84  ? 29.184 -10.329 19.768  1.00 11.08  ? 84  PHE B CD2 1 
ATOM   1357 C CE1 . PHE B 1 84  ? 26.570 -9.708  19.208  1.00 12.24  ? 84  PHE B CE1 1 
ATOM   1358 C CE2 . PHE B 1 84  ? 28.315 -10.028 20.768  1.00 12.12  ? 84  PHE B CE2 1 
ATOM   1359 C CZ  . PHE B 1 84  ? 27.005 -9.724  20.514  1.00 11.99  ? 84  PHE B CZ  1 
ATOM   1360 N N   . GLU B 1 85  ? 32.517 -9.811  15.726  1.00 9.12   ? 85  GLU B N   1 
ATOM   1361 C CA  . GLU B 1 85  ? 33.485 -10.314 14.746  1.00 10.08  ? 85  GLU B CA  1 
ATOM   1362 C C   . GLU B 1 85  ? 34.673 -10.915 15.466  1.00 9.77   ? 85  GLU B C   1 
ATOM   1363 O O   . GLU B 1 85  ? 35.151 -10.400 16.452  1.00 11.28  ? 85  GLU B O   1 
ATOM   1364 C CB  . GLU B 1 85  ? 33.957 -9.252  13.827  1.00 11.95  ? 85  GLU B CB  1 
ATOM   1365 C CG  . GLU B 1 85  ? 32.981 -8.414  13.083  1.00 18.92  ? 85  GLU B CG  1 
ATOM   1366 C CD  . GLU B 1 85  ? 33.772 -7.724  11.897  1.00 25.29  ? 85  GLU B CD  1 
ATOM   1367 O OE1 . GLU B 1 85  ? 33.371 -7.851  10.822  1.00 35.52  ? 85  GLU B OE1 1 
ATOM   1368 O OE2 . GLU B 1 85  ? 34.930 -7.219  12.036  1.00 24.19  ? 85  GLU B OE2 1 
ATOM   1369 N N   . GLN B 1 86  ? 35.182 -11.994 14.911  1.00 11.12  ? 86  GLN B N   1 
ATOM   1370 C CA  . GLN B 1 86  ? 36.353 -12.717 15.460  1.00 11.41  ? 86  GLN B CA  1 
ATOM   1371 C C   . GLN B 1 86  ? 37.179 -13.208 14.270  1.00 12.53  ? 86  GLN B C   1 
ATOM   1372 O O   . GLN B 1 86  ? 36.652 -13.724 13.328  1.00 16.42  ? 86  GLN B O   1 
ATOM   1373 C CB  . GLN B 1 86  ? 35.907 -13.901 16.346  1.00 11.45  ? 86  GLN B CB  1 
ATOM   1374 C CG  . GLN B 1 86  ? 37.034 -14.542 17.131  1.00 13.12  ? 86  GLN B CG  1 
ATOM   1375 C CD  . GLN B 1 86  ? 36.541 -15.733 17.920  1.00 13.92  ? 86  GLN B CD  1 
ATOM   1376 O OE1 . GLN B 1 86  ? 35.687 -16.511 17.430  1.00 17.04  ? 86  GLN B OE1 1 
ATOM   1377 N NE2 . GLN B 1 86  ? 37.019 -15.895 19.112  1.00 14.26  ? 86  GLN B NE2 1 
ATOM   1378 N N   . LYS B 1 87  ? 38.477 -13.072 14.339  1.00 15.10  ? 87  LYS B N   1 
ATOM   1379 C CA  . LYS B 1 87  ? 39.383 -13.521 13.271  1.00 19.27  ? 87  LYS B CA  1 
ATOM   1380 C C   . LYS B 1 87  ? 39.959 -14.879 13.382  1.00 27.33  ? 87  LYS B C   1 
ATOM   1381 O O   . LYS B 1 87  ? 40.234 -15.492 12.319  1.00 36.60  ? 87  LYS B O   1 
ATOM   1382 C CB  . LYS B 1 87  ? 40.506 -12.491 13.116  1.00 23.19  ? 87  LYS B CB  1 
ATOM   1383 C CG  . LYS B 1 87  ? 41.449 -12.785 11.936  1.00 33.14  ? 87  LYS B CG  1 
ATOM   1384 C CD  . LYS B 1 87  ? 42.428 -11.651 11.729  1.00 39.96  ? 87  LYS B CD  1 
ATOM   1385 C CE  . LYS B 1 87  ? 43.554 -12.078 10.820  1.00 50.25  ? 87  LYS B CE  1 
ATOM   1386 N NZ  . LYS B 1 87  ? 43.036 -12.327 9.446   1.00 62.63  ? 87  LYS B NZ  1 
ATOM   1387 N N   . GLU B 1 88  ? 40.424 -15.259 14.550  1.00 30.00  ? 88  GLU B N   1 
ATOM   1388 C CA  . GLU B 1 88  ? 40.990 -16.556 14.855  1.00 31.52  ? 88  GLU B CA  1 
ATOM   1389 C C   . GLU B 1 88  ? 40.220 -17.185 15.986  1.00 23.21  ? 88  GLU B C   1 
ATOM   1390 O O   . GLU B 1 88  ? 39.567 -16.502 16.776  1.00 22.71  ? 88  GLU B O   1 
ATOM   1391 C CB  . GLU B 1 88  ? 42.495 -16.468 15.193  1.00 36.92  ? 88  GLU B CB  1 
ATOM   1392 C CG  . GLU B 1 88  ? 42.878 -15.700 16.452  1.00 53.31  ? 88  GLU B CG  1 
ATOM   1393 C CD  . GLU B 1 88  ? 42.910 -14.180 16.267  1.00 60.98  ? 88  GLU B CD  1 
ATOM   1394 O OE1 . GLU B 1 88  ? 43.345 -13.644 15.150  1.00 68.47  ? 88  GLU B OE1 1 
ATOM   1395 O OE2 . GLU B 1 88  ? 42.521 -13.497 17.264  1.00 98.84  ? 88  GLU B OE2 1 
ATOM   1396 N N   . SER B 1 89  ? 40.268 -18.504 16.018  1.00 23.63  ? 89  SER B N   1 
ATOM   1397 C CA  . SER B 1 89  ? 39.430 -19.287 16.886  1.00 26.11  ? 89  SER B CA  1 
ATOM   1398 C C   . SER B 1 89  ? 39.482 -18.858 18.329  1.00 33.22  ? 89  SER B C   1 
ATOM   1399 O O   . SER B 1 89  ? 38.455 -18.817 18.990  1.00 35.54  ? 89  SER B O   1 
ATOM   1400 C CB  . SER B 1 89  ? 39.748 -20.788 16.775  1.00 39.17  ? 89  SER B CB  1 
ATOM   1401 O OG  . SER B 1 89  ? 40.981 -21.073 17.399  1.00 57.20  ? 89  SER B OG  1 
ATOM   1402 N N   . ASN B 1 90  ? 40.654 -18.555 18.849  1.00 35.70  ? 90  ASN B N   1 
ATOM   1403 C CA  . ASN B 1 90  ? 40.686 -18.192 20.271  1.00 40.58  ? 90  ASN B CA  1 
ATOM   1404 C C   . ASN B 1 90  ? 40.802 -16.699 20.491  1.00 32.13  ? 90  ASN B C   1 
ATOM   1405 O O   . ASN B 1 90  ? 41.133 -16.269 21.586  1.00 28.00  ? 90  ASN B O   1 
ATOM   1406 C CB  . ASN B 1 90  ? 41.832 -18.953 20.977  1.00 41.17  ? 90  ASN B CB  1 
ATOM   1407 C CG  . ASN B 1 90  ? 43.225 -18.656 20.366  1.00 62.24  ? 90  ASN B CG  1 
ATOM   1408 O OD1 . ASN B 1 90  ? 43.354 -17.857 19.421  1.00 79.48  ? 90  ASN B OD1 1 
ATOM   1409 N ND2 . ASN B 1 90  ? 44.279 -19.327 20.895  1.00 52.67  ? 90  ASN B ND2 1 
ATOM   1410 N N   . GLY B 1 91  ? 40.539 -15.915 19.452  1.00 22.89  ? 91  GLY B N   1 
ATOM   1411 C CA  . GLY B 1 91  ? 40.947 -14.532 19.443  1.00 18.42  ? 91  GLY B CA  1 
ATOM   1412 C C   . GLY B 1 91  ? 39.906 -13.594 20.000  1.00 15.32  ? 91  GLY B C   1 
ATOM   1413 O O   . GLY B 1 91  ? 38.798 -13.985 20.244  1.00 16.15  ? 91  GLY B O   1 
ATOM   1414 N N   . PRO B 1 92  ? 40.266 -12.311 20.198  1.00 15.62  ? 92  PRO B N   1 
ATOM   1415 C CA  . PRO B 1 92  ? 39.292 -11.368 20.683  1.00 14.89  ? 92  PRO B CA  1 
ATOM   1416 C C   . PRO B 1 92  ? 38.108 -11.140 19.750  1.00 12.39  ? 92  PRO B C   1 
ATOM   1417 O O   . PRO B 1 92  ? 38.228 -11.256 18.550  1.00 13.51  ? 92  PRO B O   1 
ATOM   1418 C CB  . PRO B 1 92  ? 40.117 -10.107 20.870  1.00 18.19  ? 92  PRO B CB  1 
ATOM   1419 C CG  . PRO B 1 92  ? 41.509 -10.585 20.953  1.00 23.20  ? 92  PRO B CG  1 
ATOM   1420 C CD  . PRO B 1 92  ? 41.615 -11.739 20.063  1.00 16.67  ? 92  PRO B CD  1 
ATOM   1421 N N   . VAL B 1 93  ? 37.008 -10.771 20.373  1.00 11.64  ? 93  VAL B N   1 
ATOM   1422 C CA  . VAL B 1 93  ? 35.792 -10.515 19.639  1.00 10.49  ? 93  VAL B CA  1 
ATOM   1423 C C   . VAL B 1 93  ? 35.469 -9.029  19.686  1.00 9.80   ? 93  VAL B C   1 
ATOM   1424 O O   . VAL B 1 93  ? 35.361 -8.437  20.771  1.00 12.66  ? 93  VAL B O   1 
ATOM   1425 C CB  . VAL B 1 93  ? 34.606 -11.336 20.229  1.00 10.56  ? 93  VAL B CB  1 
ATOM   1426 C CG1 . VAL B 1 93  ? 33.321 -11.033 19.509  1.00 11.19  ? 93  VAL B CG1 1 
ATOM   1427 C CG2 . VAL B 1 93  ? 34.912 -12.809 20.210  1.00 11.91  ? 93  VAL B CG2 1 
ATOM   1428 N N   . LYS B 1 94  ? 35.293 -8.397  18.540  1.00 10.20  ? 94  LYS B N   1 
ATOM   1429 C CA  . LYS B 1 94  ? 34.859 -7.029  18.448  1.00 10.52  ? 94  LYS B CA  1 
ATOM   1430 C C   . LYS B 1 94  ? 33.332 -7.025  18.483  1.00 10.17  ? 94  LYS B C   1 
ATOM   1431 O O   . LYS B 1 94  ? 32.704 -7.784  17.775  1.00 11.98  ? 94  LYS B O   1 
ATOM   1432 C CB  . LYS B 1 94  ? 35.360 -6.427  17.131  1.00 15.77  ? 94  LYS B CB  1 
ATOM   1433 C CG  . LYS B 1 94  ? 36.846 -6.446  16.876  1.00 24.89  ? 94  LYS B CG  1 
ATOM   1434 C CD  . LYS B 1 94  ? 37.171 -5.624  15.658  1.00 37.99  ? 94  LYS B CD  1 
ATOM   1435 C CE  . LYS B 1 94  ? 38.453 -6.066  14.944  1.00 47.14  ? 94  LYS B CE  1 
ATOM   1436 N NZ  . LYS B 1 94  ? 38.501 -5.510  13.564  1.00 57.10  ? 94  LYS B NZ  1 
ATOM   1437 N N   . VAL B 1 95  ? 32.768 -6.129  19.257  1.00 9.59   ? 95  VAL B N   1 
ATOM   1438 C CA  . VAL B 1 95  ? 31.346 -5.955  19.455  1.00 9.39   ? 95  VAL B CA  1 
ATOM   1439 C C   . VAL B 1 95  ? 31.026 -4.494  19.169  1.00 9.26   ? 95  VAL B C   1 
ATOM   1440 O O   . VAL B 1 95  ? 31.558 -3.594  19.825  1.00 10.74  ? 95  VAL B O   1 
ATOM   1441 C CB  . VAL B 1 95  ? 30.920 -6.341  20.884  1.00 10.97  ? 95  VAL B CB  1 
ATOM   1442 C CG1 . VAL B 1 95  ? 29.414 -6.266  21.004  1.00 12.69  ? 95  VAL B CG1 1 
ATOM   1443 C CG2 . VAL B 1 95  ? 31.463 -7.718  21.288  1.00 12.05  ? 95  VAL B CG2 1 
ATOM   1444 N N   . TRP B 1 96  ? 30.154 -4.233  18.198  1.00 8.50   ? 96  TRP B N   1 
ATOM   1445 C CA  . TRP B 1 96  ? 29.877 -2.862  17.852  1.00 8.74   ? 96  TRP B CA  1 
ATOM   1446 C C   . TRP B 1 96  ? 28.465 -2.686  17.269  1.00 8.46   ? 96  TRP B C   1 
ATOM   1447 O O   . TRP B 1 96  ? 27.957 -3.599  16.639  1.00 9.25   ? 96  TRP B O   1 
ATOM   1448 C CB  . TRP B 1 96  ? 30.943 -2.289  16.903  1.00 10.20  ? 96  TRP B CB  1 
ATOM   1449 C CG  . TRP B 1 96  ? 30.968 -2.960  15.528  1.00 12.84  ? 96  TRP B CG  1 
ATOM   1450 C CD1 . TRP B 1 96  ? 31.630 -4.174  15.157  1.00 11.89  ? 96  TRP B CD1 1 
ATOM   1451 C CD2 . TRP B 1 96  ? 30.325 -2.484  14.411  1.00 14.73  ? 96  TRP B CD2 1 
ATOM   1452 N NE1 . TRP B 1 96  ? 31.467 -4.371  13.869  1.00 13.76  ? 96  TRP B NE1 1 
ATOM   1453 C CE2 . TRP B 1 96  ? 30.660 -3.436  13.338  1.00 10.14  ? 96  TRP B CE2 1 
ATOM   1454 C CE3 . TRP B 1 96  ? 29.576 -1.433  14.172  1.00 12.12  ? 96  TRP B CE3 1 
ATOM   1455 C CZ2 . TRP B 1 96  ? 30.172 -3.263  11.998  1.00 14.29  ? 96  TRP B CZ2 1 
ATOM   1456 C CZ3 . TRP B 1 96  ? 29.042 -1.261  12.860  1.00 13.88  ? 96  TRP B CZ3 1 
ATOM   1457 C CH2 . TRP B 1 96  ? 29.413 -2.174  11.819  1.00 13.90  ? 96  TRP B CH2 1 
ATOM   1458 N N   . GLY B 1 97  ? 27.898 -1.504  17.461  1.00 8.87   ? 97  GLY B N   1 
ATOM   1459 C CA  . GLY B 1 97  ? 26.615 -1.157  16.911  1.00 9.20   ? 97  GLY B CA  1 
ATOM   1460 C C   . GLY B 1 97  ? 25.989 -0.091  17.716  1.00 9.26   ? 97  GLY B C   1 
ATOM   1461 O O   . GLY B 1 97  ? 26.638 0.723   18.339  1.00 9.84   ? 97  GLY B O   1 
ATOM   1462 N N   . SER B 1 98  ? 24.676 -0.117  17.698  1.00 10.10  ? 98  SER B N   1 
ATOM   1463 C CA  . SER B 1 98  ? 23.964 0.887   18.393  1.00 11.04  ? 98  SER B CA  1 
ATOM   1464 C C   . SER B 1 98  ? 22.607 0.410   18.798  1.00 11.13  ? 98  SER B C   1 
ATOM   1465 O O   . SER B 1 98  ? 22.048 -0.527  18.203  1.00 11.99  ? 98  SER B O   1 
ATOM   1466 C CB  . SER B 1 98  ? 23.867 2.136   17.606  1.00 13.98  ? 98  SER B CB  1 
ATOM   1467 O OG  . SER B 1 98  ? 23.142 1.967   16.470  1.00 18.56  ? 98  SER B OG  1 
ATOM   1468 N N   . ILE B 1 99  ? 22.061 1.104   19.794  1.00 12.25  ? 99  ILE B N   1 
ATOM   1469 C CA  . ILE B 1 99  ? 20.734 0.831   20.380  1.00 12.40  ? 99  ILE B CA  1 
ATOM   1470 C C   . ILE B 1 99  ? 20.052 2.166   20.585  1.00 14.48  ? 99  ILE B C   1 
ATOM   1471 O O   . ILE B 1 99  ? 20.660 3.093   21.068  1.00 15.94  ? 99  ILE B O   1 
ATOM   1472 C CB  . ILE B 1 99  ? 20.816 0.071   21.698  1.00 12.42  ? 99  ILE B CB  1 
ATOM   1473 C CG1 . ILE B 1 99  ? 21.792 -1.080  21.628  1.00 13.23  ? 99  ILE B CG1 1 
ATOM   1474 C CG2 . ILE B 1 99  ? 19.439 -0.390  22.174  1.00 13.25  ? 99  ILE B CG2 1 
ATOM   1475 C CD1 . ILE B 1 99  ? 22.126 -1.696  22.937  1.00 15.12  ? 99  ILE B CD1 1 
ATOM   1476 N N   . LYS B 1 100 ? 18.785 2.253   20.192  1.00 13.22  ? 100 LYS B N   1 
ATOM   1477 C CA  . LYS B 1 100 ? 17.990 3.478   20.419  1.00 13.64  ? 100 LYS B CA  1 
ATOM   1478 C C   . LYS B 1 100 ? 16.746 3.123   21.171  1.00 12.43  ? 100 LYS B C   1 
ATOM   1479 O O   . LYS B 1 100 ? 16.409 1.953   21.389  1.00 12.84  ? 100 LYS B O   1 
ATOM   1480 C CB  . LYS B 1 100 ? 17.682 4.259   19.146  1.00 19.16  ? 100 LYS B CB  1 
ATOM   1481 C CG  . LYS B 1 100 ? 16.748 3.578   18.253  1.00 21.43  ? 100 LYS B CG  1 
ATOM   1482 C CD  . LYS B 1 100 ? 16.210 4.473   17.148  1.00 28.01  ? 100 LYS B CD  1 
ATOM   1483 C CE  . LYS B 1 100 ? 15.578 3.609   16.058  1.00 31.94  ? 100 LYS B CE  1 
ATOM   1484 N NZ  . LYS B 1 100 ? 15.730 4.108   14.677  1.00 50.80  ? 100 LYS B NZ  1 
ATOM   1485 N N   . GLY B 1 101 ? 16.037 4.165   21.585  1.00 12.46  ? 101 GLY B N   1 
ATOM   1486 C CA  . GLY B 1 101 ? 14.839 4.054   22.355  1.00 12.23  ? 101 GLY B CA  1 
ATOM   1487 C C   . GLY B 1 101 ? 15.008 3.862   23.842  1.00 12.30  ? 101 GLY B C   1 
ATOM   1488 O O   . GLY B 1 101 ? 14.009 3.630   24.534  1.00 15.33  ? 101 GLY B O   1 
ATOM   1489 N N   . LEU B 1 102 ? 16.252 3.934   24.324  1.00 13.21  ? 102 LEU B N   1 
ATOM   1490 C CA  . LEU B 1 102 ? 16.565 3.690   25.691  1.00 13.85  ? 102 LEU B CA  1 
ATOM   1491 C C   . LEU B 1 102 ? 16.349 4.958   26.579  1.00 13.31  ? 102 LEU B C   1 
ATOM   1492 O O   . LEU B 1 102 ? 16.549 6.062   26.101  1.00 16.44  ? 102 LEU B O   1 
ATOM   1493 C CB  . LEU B 1 102 ? 18.015 3.239   25.842  1.00 12.29  ? 102 LEU B CB  1 
ATOM   1494 C CG  . LEU B 1 102 ? 18.351 1.882   25.273  1.00 12.69  ? 102 LEU B CG  1 
ATOM   1495 C CD1 . LEU B 1 102 ? 19.848 1.742   25.150  1.00 13.93  ? 102 LEU B CD1 1 
ATOM   1496 C CD2 . LEU B 1 102 ? 17.825 0.753   26.166  1.00 15.44  ? 102 LEU B CD2 1 
ATOM   1497 N N   . THR B 1 103 ? 15.994 4.760   27.838  1.00 13.47  ? 103 THR B N   1 
ATOM   1498 C CA  . THR B 1 103 ? 16.057 5.869   28.765  1.00 13.83  ? 103 THR B CA  1 
ATOM   1499 C C   . THR B 1 103 ? 17.513 6.362   28.955  1.00 14.39  ? 103 THR B C   1 
ATOM   1500 O O   . THR B 1 103 ? 18.473 5.581   28.860  1.00 13.96  ? 103 THR B O   1 
ATOM   1501 C CB  . THR B 1 103 ? 15.415 5.480   30.097  1.00 16.06  ? 103 THR B CB  1 
ATOM   1502 O OG1 . THR B 1 103 ? 16.077 4.340   30.596  1.00 15.87  ? 103 THR B OG1 1 
ATOM   1503 C CG2 . THR B 1 103 ? 13.947 5.225   29.936  1.00 17.41  ? 103 THR B CG2 1 
ATOM   1504 N N   . GLU B 1 104 ? 17.708 7.621   29.274  1.00 15.99  ? 104 GLU B N   1 
ATOM   1505 C CA  . GLU B 1 104 ? 19.033 8.195   29.442  1.00 15.90  ? 104 GLU B CA  1 
ATOM   1506 C C   . GLU B 1 104 ? 19.737 7.510   30.610  1.00 14.29  ? 104 GLU B C   1 
ATOM   1507 O O   . GLU B 1 104 ? 19.117 7.291   31.672  1.00 18.47  ? 104 GLU B O   1 
ATOM   1508 C CB  . GLU B 1 104 ? 18.920 9.672   29.729  1.00 16.50  ? 104 GLU B CB  1 
ATOM   1509 C CG  . GLU B 1 104 ? 20.248 10.385  29.801  1.00 18.31  ? 104 GLU B CG  1 
ATOM   1510 C CD  . GLU B 1 104 ? 20.118 11.898  29.988  1.00 22.67  ? 104 GLU B CD  1 
ATOM   1511 O OE1 . GLU B 1 104 ? 18.997 12.438  29.927  1.00 29.02  ? 104 GLU B OE1 1 
ATOM   1512 O OE2 . GLU B 1 104 ? 21.173 12.525  30.174  1.00 29.33  ? 104 GLU B OE2 1 
ATOM   1513 N N   . GLY B 1 105 ? 20.985 7.135   30.428  1.00 14.16  ? 105 GLY B N   1 
ATOM   1514 C CA  . GLY B 1 105 ? 21.765 6.536   31.500  1.00 14.08  ? 105 GLY B CA  1 
ATOM   1515 C C   . GLY B 1 105 ? 22.338 5.186   31.139  1.00 11.79  ? 105 GLY B C   1 
ATOM   1516 O O   . GLY B 1 105 ? 22.429 4.826   29.972  1.00 12.36  ? 105 GLY B O   1 
ATOM   1517 N N   . LEU B 1 106 ? 22.788 4.480   32.183  1.00 12.01  ? 106 LEU B N   1 
ATOM   1518 C CA  . LEU B 1 106 ? 23.486 3.222   32.026  1.00 11.76  ? 106 LEU B CA  1 
ATOM   1519 C C   . LEU B 1 106 ? 22.488 2.067   31.937  1.00 11.34  ? 106 LEU B C   1 
ATOM   1520 O O   . LEU B 1 106 ? 21.515 2.009   32.715  1.00 13.87  ? 106 LEU B O   1 
ATOM   1521 C CB  . LEU B 1 106 ? 24.397 2.972   33.207  1.00 13.89  ? 106 LEU B CB  1 
ATOM   1522 C CG  . LEU B 1 106 ? 25.565 3.940   33.345  1.00 18.80  ? 106 LEU B CG  1 
ATOM   1523 C CD1 . LEU B 1 106 ? 26.445 3.511   34.497  1.00 22.51  ? 106 LEU B CD1 1 
ATOM   1524 C CD2 . LEU B 1 106 ? 26.346 4.170   32.062  1.00 21.49  ? 106 LEU B CD2 1 
ATOM   1525 N N   . HIS B 1 107 ? 22.724 1.126   31.034  1.00 10.01  ? 107 HIS B N   1 
ATOM   1526 C CA  . HIS B 1 107 ? 21.896 -0.045  30.883  1.00 10.13  ? 107 HIS B CA  1 
ATOM   1527 C C   . HIS B 1 107 ? 22.792 -1.307  30.846  1.00 9.43   ? 107 HIS B C   1 
ATOM   1528 O O   . HIS B 1 107 ? 23.653 -1.431  29.988  1.00 9.37   ? 107 HIS B O   1 
ATOM   1529 C CB  . HIS B 1 107 ? 21.057 0.016   29.601  1.00 9.93   ? 107 HIS B CB  1 
ATOM   1530 C CG  . HIS B 1 107 ? 20.079 1.146   29.620  1.00 10.84  ? 107 HIS B CG  1 
ATOM   1531 N ND1 . HIS B 1 107 ? 18.765 0.960   29.992  1.00 11.46  ? 107 HIS B ND1 1 
ATOM   1532 C CD2 . HIS B 1 107 ? 20.201 2.483   29.375  1.00 11.25  ? 107 HIS B CD2 1 
ATOM   1533 C CE1 . HIS B 1 107 ? 18.128 2.118   29.936  1.00 12.01  ? 107 HIS B CE1 1 
ATOM   1534 N NE2 . HIS B 1 107 ? 18.986 3.057   29.621  1.00 12.30  ? 107 HIS B NE2 1 
ATOM   1535 N N   . GLY B 1 108 ? 22.485 -2.255  31.698  1.00 9.52   ? 108 GLY B N   1 
ATOM   1536 C CA  . GLY B 1 108 ? 23.251 -3.503  31.718  1.00 10.68  ? 108 GLY B CA  1 
ATOM   1537 C C   . GLY B 1 108 ? 23.090 -4.268  30.409  1.00 9.23   ? 108 GLY B C   1 
ATOM   1538 O O   . GLY B 1 108 ? 22.007 -4.323  29.812  1.00 10.77  ? 108 GLY B O   1 
ATOM   1539 N N   . PHE B 1 109 ? 24.182 -4.898  29.979  1.00 9.51   ? 109 PHE B N   1 
ATOM   1540 C CA  . PHE B 1 109 ? 24.319 -5.515  28.657  1.00 9.15   ? 109 PHE B CA  1 
ATOM   1541 C C   . PHE B 1 109 ? 24.967 -6.865  28.855  1.00 9.66   ? 109 PHE B C   1 
ATOM   1542 O O   . PHE B 1 109 ? 26.024 -6.953  29.499  1.00 11.83  ? 109 PHE B O   1 
ATOM   1543 C CB  . PHE B 1 109 ? 25.157 -4.528  27.821  1.00 9.60   ? 109 PHE B CB  1 
ATOM   1544 C CG  . PHE B 1 109 ? 25.281 -4.795  26.352  1.00 9.16   ? 109 PHE B CG  1 
ATOM   1545 C CD1 . PHE B 1 109 ? 24.182 -5.208  25.581  1.00 12.52  ? 109 PHE B CD1 1 
ATOM   1546 C CD2 . PHE B 1 109 ? 26.434 -4.551  25.709  1.00 9.32   ? 109 PHE B CD2 1 
ATOM   1547 C CE1 . PHE B 1 109 ? 24.265 -5.294  24.220  1.00 13.79  ? 109 PHE B CE1 1 
ATOM   1548 C CE2 . PHE B 1 109 ? 26.561 -4.642  24.375  1.00 11.39  ? 109 PHE B CE2 1 
ATOM   1549 C CZ  . PHE B 1 109 ? 25.483 -4.968  23.596  1.00 12.34  ? 109 PHE B CZ  1 
ATOM   1550 N N   . HIS B 1 110 ? 24.368 -7.940  28.396  1.00 8.28   ? 110 HIS B N   1 
ATOM   1551 C CA  . HIS B 1 110 ? 24.805 -9.287  28.765  1.00 8.43   ? 110 HIS B CA  1 
ATOM   1552 C C   . HIS B 1 110 ? 24.450 -10.309 27.712  1.00 8.40   ? 110 HIS B C   1 
ATOM   1553 O O   . HIS B 1 110 ? 23.395 -10.232 27.083  1.00 9.58   ? 110 HIS B O   1 
ATOM   1554 C CB  . HIS B 1 110 ? 24.112 -9.676  30.084  1.00 9.63   ? 110 HIS B CB  1 
ATOM   1555 C CG  . HIS B 1 110 ? 24.503 -10.981 30.706  1.00 11.88  ? 110 HIS B CG  1 
ATOM   1556 N ND1 . HIS B 1 110 ? 25.540 -11.148 31.574  1.00 14.18  ? 110 HIS B ND1 1 
ATOM   1557 C CD2 . HIS B 1 110 ? 23.946 -12.200 30.571  1.00 13.51  ? 110 HIS B CD2 1 
ATOM   1558 C CE1 . HIS B 1 110 ? 25.657 -12.406 31.929  1.00 14.26  ? 110 HIS B CE1 1 
ATOM   1559 N NE2 . HIS B 1 110 ? 24.672 -13.059 31.360  1.00 14.27  ? 110 HIS B NE2 1 
ATOM   1560 N N   . VAL B 1 111 ? 25.339 -11.274 27.525  1.00 8.47   ? 111 VAL B N   1 
ATOM   1561 C CA  . VAL B 1 111 ? 25.051 -12.448 26.684  1.00 8.49   ? 111 VAL B CA  1 
ATOM   1562 C C   . VAL B 1 111 ? 24.554 -13.562 27.596  1.00 8.66   ? 111 VAL B C   1 
ATOM   1563 O O   . VAL B 1 111 ? 25.295 -14.138 28.385  1.00 10.55  ? 111 VAL B O   1 
ATOM   1564 C CB  . VAL B 1 111 ? 26.255 -12.919 25.889  1.00 9.93   ? 111 VAL B CB  1 
ATOM   1565 C CG1 . VAL B 1 111 ? 25.898 -14.086 25.008  1.00 10.88  ? 111 VAL B CG1 1 
ATOM   1566 C CG2 . VAL B 1 111 ? 26.926 -11.805 25.093  1.00 12.58  ? 111 VAL B CG2 1 
ATOM   1567 N N   . HIS B 1 112 ? 23.256 -13.864 27.520  1.00 9.20   ? 112 HIS B N   1 
ATOM   1568 C CA  . HIS B 1 112 ? 22.665 -14.833 28.393  1.00 10.18  ? 112 HIS B CA  1 
ATOM   1569 C C   . HIS B 1 112 ? 23.223 -16.231 28.138  1.00 10.95  ? 112 HIS B C   1 
ATOM   1570 O O   . HIS B 1 112 ? 23.217 -16.718 27.035  1.00 12.59  ? 112 HIS B O   1 
ATOM   1571 C CB  . HIS B 1 112 ? 21.156 -14.879 28.240  1.00 11.06  ? 112 HIS B CB  1 
ATOM   1572 C CG  . HIS B 1 112 ? 20.552 -15.878 29.156  1.00 13.11  ? 112 HIS B CG  1 
ATOM   1573 N ND1 . HIS B 1 112 ? 20.476 -15.674 30.513  1.00 14.40  ? 112 HIS B ND1 1 
ATOM   1574 C CD2 . HIS B 1 112 ? 20.072 -17.117 28.925  1.00 13.99  ? 112 HIS B CD2 1 
ATOM   1575 C CE1 . HIS B 1 112 ? 20.023 -16.774 31.091  1.00 13.59  ? 112 HIS B CE1 1 
ATOM   1576 N NE2 . HIS B 1 112 ? 19.764 -17.658 30.144  1.00 15.23  ? 112 HIS B NE2 1 
ATOM   1577 N N   . GLY B 1 113 ? 23.654 -16.865 29.202  1.00 13.36  ? 113 GLY B N   1 
ATOM   1578 C CA  . GLY B 1 113 ? 24.081 -18.196 29.131  1.00 17.33  ? 113 GLY B CA  1 
ATOM   1579 C C   . GLY B 1 113 ? 25.466 -18.418 28.594  1.00 18.01  ? 113 GLY B C   1 
ATOM   1580 O O   . GLY B 1 113 ? 25.873 -19.566 28.351  1.00 26.30  ? 113 GLY B O   1 
ATOM   1581 N N   . ALA B 1 114 ? 26.207 -17.364 28.336  1.00 15.85  ? 114 ALA B N   1 
ATOM   1582 C CA  . ALA B 1 114 ? 27.546 -17.484 27.811  1.00 18.59  ? 114 ALA B CA  1 
ATOM   1583 C C   . ALA B 1 114 ? 28.507 -17.980 28.857  1.00 30.14  ? 114 ALA B C   1 
ATOM   1584 O O   . ALA B 1 114 ? 28.415 -17.506 30.023  1.00 28.98  ? 114 ALA B O   1 
ATOM   1585 C CB  . ALA B 1 114 ? 28.082 -16.187 27.410  1.00 16.70  ? 114 ALA B CB  1 
ATOM   1586 O OXT . ALA B 1 114 ? 29.525 -18.579 28.431  1.00 38.42  ? 114 ALA B OXT 1 
HETATM 1587 C C1  . GOL C 2 .   ? 22.212 -16.357 -0.357  1.00 21.20  ? 201 GOL A C1  1 
HETATM 1588 O O1  . GOL C 2 .   ? 21.638 -15.411 0.386   1.00 29.02  ? 201 GOL A O1  1 
HETATM 1589 C C2  . GOL C 2 .   ? 22.683 -15.968 -1.698  1.00 20.00  ? 201 GOL A C2  1 
HETATM 1590 O O2  . GOL C 2 .   ? 23.569 -14.811 -1.642  1.00 19.81  ? 201 GOL A O2  1 
HETATM 1591 C C3  . GOL C 2 .   ? 23.389 -17.201 -2.304  1.00 21.90  ? 201 GOL A C3  1 
HETATM 1592 O O3  . GOL C 2 .   ? 23.546 -16.949 -3.715  1.00 26.57  ? 201 GOL A O3  1 
HETATM 1593 C C1  . GOL D 2 .   ? 23.974 -10.007 7.700   1.00 30.64  ? 202 GOL A C1  1 
HETATM 1594 O O1  . GOL D 2 .   ? 23.730 -11.351 8.191   1.00 36.82  ? 202 GOL A O1  1 
HETATM 1595 C C2  . GOL D 2 .   ? 22.919 -8.864  7.971   1.00 40.49  ? 202 GOL A C2  1 
HETATM 1596 O O2  . GOL D 2 .   ? 21.783 -9.376  8.697   1.00 59.78  ? 202 GOL A O2  1 
HETATM 1597 C C3  . GOL D 2 .   ? 23.532 -7.574  8.558   1.00 32.17  ? 202 GOL A C3  1 
HETATM 1598 O O3  . GOL D 2 .   ? 22.728 -7.244  9.719   1.00 25.47  ? 202 GOL A O3  1 
HETATM 1599 C C1  . GOL E 2 .   ? 14.738 -13.591 6.266   1.00 49.62  ? 203 GOL A C1  1 
HETATM 1600 O O1  . GOL E 2 .   ? 14.051 -12.349 6.449   1.00 51.74  ? 203 GOL A O1  1 
HETATM 1601 C C2  . GOL E 2 .   ? 16.054 -13.354 5.553   1.00 53.08  ? 203 GOL A C2  1 
HETATM 1602 O O2  . GOL E 2 .   ? 16.817 -12.515 6.421   1.00 55.78  ? 203 GOL A O2  1 
HETATM 1603 C C3  . GOL E 2 .   ? 16.824 -14.644 5.218   1.00 45.56  ? 203 GOL A C3  1 
HETATM 1604 O O3  . GOL E 2 .   ? 17.703 -15.060 6.271   1.00 53.35  ? 203 GOL A O3  1 
HETATM 1605 C C1  . GOL F 2 .   ? 15.911 -18.242 24.826  1.00 63.63  ? 201 GOL B C1  1 
HETATM 1606 O O1  . GOL F 2 .   ? 15.953 -19.593 24.291  1.00 60.12  ? 201 GOL B O1  1 
HETATM 1607 C C2  . GOL F 2 .   ? 17.070 -17.993 25.795  1.00 56.16  ? 201 GOL B C2  1 
HETATM 1608 O O2  . GOL F 2 .   ? 17.138 -16.659 26.345  1.00 58.97  ? 201 GOL B O2  1 
HETATM 1609 C C3  . GOL F 2 .   ? 16.814 -18.936 26.937  1.00 51.15  ? 201 GOL B C3  1 
HETATM 1610 O O3  . GOL F 2 .   ? 18.039 -19.198 27.554  1.00 31.08  ? 201 GOL B O3  1 
HETATM 1611 C C1  . GOL G 2 .   ? 23.746 -0.999  12.283  1.00 20.11  ? 202 GOL B C1  1 
HETATM 1612 O O1  . GOL G 2 .   ? 22.576 -0.766  11.475  1.00 51.42  ? 202 GOL B O1  1 
HETATM 1613 C C2  . GOL G 2 .   ? 23.892 -0.082  13.488  1.00 39.32  ? 202 GOL B C2  1 
HETATM 1614 O O2  . GOL G 2 .   ? 24.289 -1.183  14.258  1.00 41.46  ? 202 GOL B O2  1 
HETATM 1615 C C3  . GOL G 2 .   ? 24.833 1.156   13.424  1.00 40.96  ? 202 GOL B C3  1 
HETATM 1616 O O3  . GOL G 2 .   ? 25.767 1.362   14.507  1.00 33.28  ? 202 GOL B O3  1 
HETATM 1617 O O   . HOH H 3 .   ? 35.456 -6.743  8.824   1.00 36.35  ? 301 HOH A O   1 
HETATM 1618 O O   . HOH H 3 .   ? 30.890 3.552   23.098  1.00 33.85  ? 302 HOH A O   1 
HETATM 1619 O O   . HOH H 3 .   ? 32.505 -5.142  10.348  1.00 26.58  ? 303 HOH A O   1 
HETATM 1620 O O   . HOH H 3 .   ? 11.188 -2.661  1.894   1.00 36.80  ? 304 HOH A O   1 
HETATM 1621 O O   . HOH H 3 .   ? 12.958 1.980   -5.030  1.00 51.10  ? 305 HOH A O   1 
HETATM 1622 O O   . HOH H 3 .   ? 34.099 4.429   12.613  1.00 23.86  ? 306 HOH A O   1 
HETATM 1623 O O   . HOH H 3 .   ? 39.054 5.631   -2.974  1.00 12.96  ? 307 HOH A O   1 
HETATM 1624 O O   . HOH H 3 .   ? 25.173 5.127   -9.607  1.00 36.96  ? 308 HOH A O   1 
HETATM 1625 O O   . HOH H 3 .   ? 41.085 -5.901  -1.921  1.00 39.18  ? 309 HOH A O   1 
HETATM 1626 O O   . HOH H 3 .   ? 24.644 -5.748  10.784  1.00 12.61  ? 310 HOH A O   1 
HETATM 1627 O O   . HOH H 3 .   ? 30.690 5.812   -7.668  1.00 22.72  ? 311 HOH A O   1 
HETATM 1628 O O   . HOH H 3 .   ? 27.410 -12.416 -7.031  1.00 28.21  ? 312 HOH A O   1 
HETATM 1629 O O   . HOH H 3 .   ? 14.608 -13.432 -11.221 1.00 33.36  ? 313 HOH A O   1 
HETATM 1630 O O   . HOH H 3 .   ? 20.663 -19.629 -0.336  1.00 20.78  ? 314 HOH A O   1 
HETATM 1631 O O   . HOH H 3 .   ? 29.685 1.251   16.886  1.00 22.76  ? 315 HOH A O   1 
HETATM 1632 O O   . HOH H 3 .   ? 33.120 11.366  2.830   1.00 23.41  ? 316 HOH A O   1 
HETATM 1633 O O   . HOH H 3 .   ? 39.809 3.723   8.402   1.00 25.48  ? 317 HOH A O   1 
HETATM 1634 O O   . HOH H 3 .   ? 37.584 11.790  2.619   1.00 29.51  ? 318 HOH A O   1 
HETATM 1635 O O   . HOH H 3 .   ? 26.099 9.095   -3.371  1.00 12.33  ? 319 HOH A O   1 
HETATM 1636 O O   . HOH H 3 .   ? 21.771 4.157   6.039   1.00 12.64  ? 320 HOH A O   1 
HETATM 1637 O O   . HOH H 3 .   ? 17.868 4.098   3.861   1.00 23.57  ? 321 HOH A O   1 
HETATM 1638 O O   . HOH H 3 .   ? 20.091 -7.426  10.267  1.00 38.64  ? 322 HOH A O   1 
HETATM 1639 O O   . HOH H 3 .   ? 36.752 -2.439  -7.541  1.00 32.01  ? 323 HOH A O   1 
HETATM 1640 O O   . HOH H 3 .   ? 29.720 0.768   -10.767 1.00 32.96  ? 324 HOH A O   1 
HETATM 1641 O O   . HOH H 3 .   ? 34.897 7.701   -3.474  1.00 23.99  ? 325 HOH A O   1 
HETATM 1642 O O   . HOH H 3 .   ? 25.088 -3.100  11.398  1.00 12.48  ? 326 HOH A O   1 
HETATM 1643 O O   . HOH H 3 .   ? 15.650 -9.238  -15.302 1.00 54.35  ? 327 HOH A O   1 
HETATM 1644 O O   . HOH H 3 .   ? 18.231 -7.903  -16.978 1.00 30.66  ? 328 HOH A O   1 
HETATM 1645 O O   . HOH H 3 .   ? 22.247 -18.716 -5.318  1.00 27.64  ? 329 HOH A O   1 
HETATM 1646 O O   . HOH H 3 .   ? 42.573 -1.040  13.342  1.00 42.13  ? 330 HOH A O   1 
HETATM 1647 O O   . HOH H 3 .   ? 47.468 3.115   6.631   1.00 37.42  ? 331 HOH A O   1 
HETATM 1648 O O   . HOH H 3 .   ? 36.045 -5.784  -4.989  1.00 36.39  ? 332 HOH A O   1 
HETATM 1649 O O   . HOH H 3 .   ? 14.516 -7.292  -6.754  1.00 20.77  ? 333 HOH A O   1 
HETATM 1650 O O   . HOH H 3 .   ? 14.350 -8.856  -11.639 1.00 25.00  ? 334 HOH A O   1 
HETATM 1651 O O   . HOH H 3 .   ? 36.577 5.741   -1.782  1.00 11.79  ? 335 HOH A O   1 
HETATM 1652 O O   . HOH H 3 .   ? 28.187 -2.896  -9.968  1.00 21.25  ? 336 HOH A O   1 
HETATM 1653 O O   . HOH H 3 .   ? 13.243 -12.124 0.517   1.00 26.07  ? 337 HOH A O   1 
HETATM 1654 O O   . HOH H 3 .   ? 41.289 1.827   0.488   1.00 15.17  ? 338 HOH A O   1 
HETATM 1655 O O   . HOH H 3 .   ? 24.676 10.344  -0.566  1.00 14.03  ? 339 HOH A O   1 
HETATM 1656 O O   . HOH H 3 .   ? 40.381 8.353   0.222   1.00 13.34  ? 340 HOH A O   1 
HETATM 1657 O O   . HOH H 3 .   ? 12.022 -7.133  -5.667  1.00 29.91  ? 341 HOH A O   1 
HETATM 1658 O O   . HOH H 3 .   ? 37.473 7.715   8.510   1.00 31.97  ? 342 HOH A O   1 
HETATM 1659 O O   . HOH H 3 .   ? 20.439 8.696   -0.936  1.00 21.47  ? 343 HOH A O   1 
HETATM 1660 O O   . HOH H 3 .   ? 24.356 -17.783 2.447   1.00 30.01  ? 344 HOH A O   1 
HETATM 1661 O O   . HOH H 3 .   ? 19.129 6.353   -0.188  1.00 23.31  ? 345 HOH A O   1 
HETATM 1662 O O   . HOH H 3 .   ? 40.070 -4.065  -4.757  1.00 28.72  ? 346 HOH A O   1 
HETATM 1663 O O   . HOH H 3 .   ? 19.169 -1.020  -15.010 1.00 34.47  ? 347 HOH A O   1 
HETATM 1664 O O   . HOH H 3 .   ? 15.225 3.805   -11.734 1.00 96.57  ? 348 HOH A O   1 
HETATM 1665 O O   . HOH H 3 .   ? 23.216 3.904   8.343   1.00 21.97  ? 349 HOH A O   1 
HETATM 1666 O O   . HOH H 3 .   ? 27.719 7.911   14.051  1.00 21.21  ? 350 HOH A O   1 
HETATM 1667 O O   . HOH H 3 .   ? 28.190 -13.980 0.222   1.00 107.15 ? 351 HOH A O   1 
HETATM 1668 O O   . HOH H 3 .   ? 35.398 9.729   6.118   1.00 31.00  ? 352 HOH A O   1 
HETATM 1669 O O   . HOH H 3 .   ? 21.211 -5.835  -11.828 1.00 17.50  ? 353 HOH A O   1 
HETATM 1670 O O   . HOH H 3 .   ? 16.179 4.051   -3.773  1.00 33.88  ? 354 HOH A O   1 
HETATM 1671 O O   . HOH H 3 .   ? 20.653 -17.430 -7.274  1.00 28.21  ? 355 HOH A O   1 
HETATM 1672 O O   . HOH H 3 .   ? 33.545 9.757   -2.053  1.00 19.12  ? 356 HOH A O   1 
HETATM 1673 O O   . HOH H 3 .   ? 29.345 12.755  -6.859  1.00 31.00  ? 357 HOH A O   1 
HETATM 1674 O O   . HOH H 3 .   ? 44.749 1.601   12.105  1.00 41.14  ? 358 HOH A O   1 
HETATM 1675 O O   . HOH H 3 .   ? 25.070 -12.550 6.031   1.00 28.22  ? 359 HOH A O   1 
HETATM 1676 O O   . HOH H 3 .   ? 19.727 -4.086  -14.059 1.00 30.32  ? 360 HOH A O   1 
HETATM 1677 O O   . HOH H 3 .   ? 30.957 -8.441  -5.853  1.00 37.08  ? 361 HOH A O   1 
HETATM 1678 O O   . HOH H 3 .   ? 26.043 -12.037 -3.028  1.00 23.16  ? 362 HOH A O   1 
HETATM 1679 O O   . HOH H 3 .   ? 12.747 -16.969 -8.855  1.00 45.95  ? 363 HOH A O   1 
HETATM 1680 O O   . HOH H 3 .   ? 44.055 -3.818  6.620   1.00 33.52  ? 364 HOH A O   1 
HETATM 1681 O O   . HOH H 3 .   ? 29.350 15.013  -4.701  1.00 35.17  ? 365 HOH A O   1 
HETATM 1682 O O   . HOH H 3 .   ? 10.936 -15.274 -1.128  1.00 37.73  ? 366 HOH A O   1 
HETATM 1683 O O   . HOH H 3 .   ? 37.267 -1.354  11.556  1.00 34.67  ? 367 HOH A O   1 
HETATM 1684 O O   . HOH H 3 .   ? 14.042 3.297   -7.928  1.00 33.64  ? 368 HOH A O   1 
HETATM 1685 O O   . HOH H 3 .   ? 28.264 6.690   -9.664  1.00 19.84  ? 369 HOH A O   1 
HETATM 1686 O O   . HOH H 3 .   ? 18.732 -3.319  -21.553 1.00 50.17  ? 370 HOH A O   1 
HETATM 1687 O O   . HOH H 3 .   ? 42.213 -1.740  6.149   1.00 18.91  ? 371 HOH A O   1 
HETATM 1688 O O   . HOH H 3 .   ? 19.820 6.042   4.208   1.00 24.08  ? 372 HOH A O   1 
HETATM 1689 O O   . HOH H 3 .   ? 15.287 -0.722  5.208   1.00 32.39  ? 373 HOH A O   1 
HETATM 1690 O O   . HOH H 3 .   ? 47.006 6.458   0.692   1.00 39.55  ? 374 HOH A O   1 
HETATM 1691 O O   . HOH H 3 .   ? 43.009 9.067   6.718   1.00 38.74  ? 375 HOH A O   1 
HETATM 1692 O O   . HOH H 3 .   ? 45.747 3.568   10.000  1.00 40.35  ? 376 HOH A O   1 
HETATM 1693 O O   . HOH H 3 .   ? 35.252 0.157   -5.858  1.00 13.85  ? 377 HOH A O   1 
HETATM 1694 O O   . HOH H 3 .   ? 12.521 -14.389 -7.816  1.00 30.92  ? 378 HOH A O   1 
HETATM 1695 O O   . HOH H 3 .   ? 20.726 -13.124 -12.962 1.00 28.44  ? 379 HOH A O   1 
HETATM 1696 O O   . HOH H 3 .   ? 26.861 11.785  -3.249  1.00 15.73  ? 380 HOH A O   1 
HETATM 1697 O O   . HOH H 3 .   ? 30.047 2.681   -8.728  1.00 23.88  ? 381 HOH A O   1 
HETATM 1698 O O   . HOH H 3 .   ? 23.710 -7.368  -12.850 1.00 41.13  ? 382 HOH A O   1 
HETATM 1699 O O   . HOH H 3 .   ? 39.768 -3.904  6.758   1.00 23.72  ? 383 HOH A O   1 
HETATM 1700 O O   . HOH H 3 .   ? 28.971 -11.279 -1.893  1.00 35.94  ? 384 HOH A O   1 
HETATM 1701 O O   . HOH H 3 .   ? 35.813 -9.838  -2.534  1.00 26.12  ? 385 HOH A O   1 
HETATM 1702 O O   . HOH H 3 .   ? 10.894 -4.436  -5.347  1.00 51.76  ? 386 HOH A O   1 
HETATM 1703 O O   . HOH H 3 .   ? 15.647 4.521   -0.252  1.00 40.49  ? 387 HOH A O   1 
HETATM 1704 O O   . HOH H 3 .   ? 30.650 -9.533  -8.733  1.00 33.25  ? 388 HOH A O   1 
HETATM 1705 O O   . HOH H 3 .   ? 34.682 12.381  -1.906  1.00 31.75  ? 389 HOH A O   1 
HETATM 1706 O O   . HOH H 3 .   ? 38.399 10.610  5.929   1.00 36.29  ? 390 HOH A O   1 
HETATM 1707 O O   . HOH H 3 .   ? 27.434 -11.505 5.404   1.00 27.49  ? 391 HOH A O   1 
HETATM 1708 O O   . HOH H 3 .   ? 16.985 -2.749  6.476   1.00 29.22  ? 392 HOH A O   1 
HETATM 1709 O O   . HOH H 3 .   ? 13.208 -2.921  -11.504 1.00 38.77  ? 393 HOH A O   1 
HETATM 1710 O O   . HOH H 3 .   ? 19.736 -7.349  6.553   1.00 38.16  ? 394 HOH A O   1 
HETATM 1711 O O   . HOH H 3 .   ? 19.933 -9.977  11.039  1.00 38.39  ? 395 HOH A O   1 
HETATM 1712 O O   . HOH H 3 .   ? 28.060 -11.764 -11.104 1.00 179.14 ? 396 HOH A O   1 
HETATM 1713 O O   . HOH H 3 .   ? 34.566 -4.271  -8.420  1.00 37.47  ? 397 HOH A O   1 
HETATM 1714 O O   . HOH H 3 .   ? 18.196 -20.844 -4.303  1.00 182.52 ? 398 HOH A O   1 
HETATM 1715 O O   . HOH H 3 .   ? 38.341 -9.189  -3.586  1.00 46.62  ? 399 HOH A O   1 
HETATM 1716 O O   . HOH H 3 .   ? 41.904 6.291   9.177   1.00 47.39  ? 400 HOH A O   1 
HETATM 1717 O O   . HOH H 3 .   ? 29.927 -10.407 -4.505  1.00 35.32  ? 401 HOH A O   1 
HETATM 1718 O O   . HOH H 3 .   ? 26.482 -15.886 -1.131  1.00 138.06 ? 402 HOH A O   1 
HETATM 1719 O O   . HOH H 3 .   ? 33.833 -9.182  4.137   1.00 26.33  ? 403 HOH A O   1 
HETATM 1720 O O   . HOH H 3 .   ? 17.061 5.522   1.410   1.00 32.59  ? 404 HOH A O   1 
HETATM 1721 O O   . HOH H 3 .   ? 44.661 -7.190  0.993   1.00 54.65  ? 405 HOH A O   1 
HETATM 1722 O O   . HOH H 3 .   ? 42.606 4.109   -0.352  1.00 16.30  ? 406 HOH A O   1 
HETATM 1723 O O   . HOH H 3 .   ? 23.167 -4.286  -13.615 1.00 40.68  ? 407 HOH A O   1 
HETATM 1724 O O   . HOH H 3 .   ? 35.825 0.901   -8.366  1.00 30.67  ? 408 HOH A O   1 
HETATM 1725 O O   . HOH H 3 .   ? 23.194 9.726   -4.289  1.00 39.98  ? 409 HOH A O   1 
HETATM 1726 O O   . HOH H 3 .   ? 22.684 11.207  -5.976  1.00 38.17  ? 410 HOH A O   1 
HETATM 1727 O O   . HOH H 3 .   ? 39.984 14.538  3.753   1.00 69.41  ? 411 HOH A O   1 
HETATM 1728 O O   . HOH H 3 .   ? 24.768 -2.538  -12.272 1.00 33.36  ? 412 HOH A O   1 
HETATM 1729 O O   . HOH H 3 .   ? 34.864 2.352   -9.719  1.00 12.55  ? 413 HOH A O   1 
HETATM 1730 O O   . HOH H 3 .   ? 38.229 -4.952  8.690   1.00 41.82  ? 414 HOH A O   1 
HETATM 1731 O O   . HOH H 3 .   ? 47.342 0.652   4.419   1.00 69.24  ? 415 HOH A O   1 
HETATM 1732 O O   . HOH H 3 .   ? 24.775 -8.937  -14.516 1.00 51.77  ? 416 HOH A O   1 
HETATM 1733 O O   . HOH H 3 .   ? 27.728 4.187   -10.323 1.00 41.25  ? 417 HOH A O   1 
HETATM 1734 O O   . HOH H 3 .   ? 26.279 12.294  -5.848  1.00 30.00  ? 418 HOH A O   1 
HETATM 1735 O O   . HOH H 3 .   ? 36.656 -11.991 6.476   1.00 56.77  ? 419 HOH A O   1 
HETATM 1736 O O   . HOH H 3 .   ? 13.860 -6.937  9.242   1.00 205.76 ? 420 HOH A O   1 
HETATM 1737 O O   . HOH H 3 .   ? 38.924 -4.223  -7.819  1.00 161.83 ? 421 HOH A O   1 
HETATM 1738 O O   . HOH H 3 .   ? 17.139 -6.173  6.799   1.00 58.59  ? 422 HOH A O   1 
HETATM 1739 O O   . HOH H 3 .   ? 13.952 -11.380 -12.833 1.00 47.28  ? 423 HOH A O   1 
HETATM 1740 O O   . HOH H 3 .   ? 17.129 3.396   7.042   1.00 177.35 ? 424 HOH A O   1 
HETATM 1741 O O   . HOH H 3 .   ? 41.808 -7.537  9.191   1.00 51.28  ? 425 HOH A O   1 
HETATM 1742 O O   . HOH H 3 .   ? 25.821 -17.825 0.400   1.00 37.12  ? 426 HOH A O   1 
HETATM 1743 O O   . HOH H 3 .   ? 20.530 -20.813 -2.766  1.00 35.22  ? 427 HOH A O   1 
HETATM 1744 O O   . HOH H 3 .   ? 41.869 -5.797  6.537   1.00 33.59  ? 428 HOH A O   1 
HETATM 1745 O O   . HOH H 3 .   ? 29.044 -12.857 -9.128  1.00 55.47  ? 429 HOH A O   1 
HETATM 1746 O O   . HOH H 3 .   ? 33.716 12.247  5.452   1.00 35.69  ? 430 HOH A O   1 
HETATM 1747 O O   . HOH H 3 .   ? 22.845 -19.555 1.117   1.00 30.96  ? 431 HOH A O   1 
HETATM 1748 O O   . HOH H 3 .   ? 36.055 -2.113  -11.503 1.00 57.17  ? 432 HOH A O   1 
HETATM 1749 O O   . HOH H 3 .   ? 31.499 2.316   -12.375 1.00 39.58  ? 433 HOH A O   1 
HETATM 1750 O O   . HOH H 3 .   ? 34.268 0.769   -12.495 1.00 34.05  ? 434 HOH A O   1 
HETATM 1751 O O   . HOH H 3 .   ? 14.712 1.676   6.235   1.00 34.87  ? 435 HOH A O   1 
HETATM 1752 O O   . HOH H 3 .   ? 19.451 10.436  1.189   1.00 31.91  ? 436 HOH A O   1 
HETATM 1753 O O   . HOH H 3 .   ? 16.764 -2.136  9.412   1.00 53.28  ? 437 HOH A O   1 
HETATM 1754 O O   . HOH H 3 .   ? 17.664 -6.256  10.583  1.00 39.45  ? 438 HOH A O   1 
HETATM 1755 O O   . HOH H 3 .   ? 37.707 -0.752  -9.598  1.00 31.68  ? 439 HOH A O   1 
HETATM 1756 O O   . HOH H 3 .   ? 15.749 -8.182  11.209  1.00 47.63  ? 440 HOH A O   1 
HETATM 1757 O O   . HOH I 3 .   ? 21.352 0.177   11.789  1.00 41.59  ? 301 HOH B O   1 
HETATM 1758 O O   . HOH I 3 .   ? 23.274 -0.210  34.670  1.00 39.10  ? 302 HOH B O   1 
HETATM 1759 O O   . HOH I 3 .   ? 45.156 -13.948 13.848  1.00 39.93  ? 303 HOH B O   1 
HETATM 1760 O O   . HOH I 3 .   ? 42.497 -11.426 16.234  1.00 28.57  ? 304 HOH B O   1 
HETATM 1761 O O   . HOH I 3 .   ? 28.495 -22.454 21.707  1.00 166.80 ? 305 HOH B O   1 
HETATM 1762 O O   . HOH I 3 .   ? 16.749 -18.676 22.256  1.00 36.27  ? 306 HOH B O   1 
HETATM 1763 O O   . HOH I 3 .   ? 27.315 -15.015 31.295  1.00 38.59  ? 307 HOH B O   1 
HETATM 1764 O O   . HOH I 3 .   ? 44.276 -14.253 18.862  1.00 45.69  ? 308 HOH B O   1 
HETATM 1765 O O   . HOH I 3 .   ? 24.639 -3.014  35.082  1.00 35.38  ? 309 HOH B O   1 
HETATM 1766 O O   . HOH I 3 .   ? 6.032  -3.423  34.368  1.00 56.84  ? 310 HOH B O   1 
HETATM 1767 O O   . HOH I 3 .   ? 26.513 -17.442 31.832  1.00 30.43  ? 311 HOH B O   1 
HETATM 1768 O O   . HOH I 3 .   ? 35.850 -17.262 14.718  1.00 31.92  ? 312 HOH B O   1 
HETATM 1769 O O   . HOH I 3 .   ? 12.945 3.371   18.074  1.00 40.09  ? 313 HOH B O   1 
HETATM 1770 O O   . HOH I 3 .   ? 11.021 -1.312  19.392  1.00 26.47  ? 314 HOH B O   1 
HETATM 1771 O O   . HOH I 3 .   ? 14.012 -10.406 32.559  1.00 18.48  ? 315 HOH B O   1 
HETATM 1772 O O   . HOH I 3 .   ? 21.163 -13.427 31.749  1.00 20.80  ? 316 HOH B O   1 
HETATM 1773 O O   . HOH I 3 .   ? 40.210 -7.068  24.422  1.00 31.08  ? 317 HOH B O   1 
HETATM 1774 O O   . HOH I 3 .   ? 28.983 2.576   28.973  1.00 17.53  ? 318 HOH B O   1 
HETATM 1775 O O   . HOH I 3 .   ? 21.187 15.182  30.271  1.00 59.40  ? 319 HOH B O   1 
HETATM 1776 O O   . HOH I 3 .   ? 25.603 11.531  22.234  1.00 20.62  ? 320 HOH B O   1 
HETATM 1777 O O   . HOH I 3 .   ? 18.952 -11.420 15.894  1.00 13.62  ? 321 HOH B O   1 
HETATM 1778 O O   . HOH I 3 .   ? 26.992 -21.923 19.696  1.00 25.68  ? 322 HOH B O   1 
HETATM 1779 O O   . HOH I 3 .   ? 34.712 -21.628 22.845  1.00 27.35  ? 323 HOH B O   1 
HETATM 1780 O O   . HOH I 3 .   ? 28.954 6.229   30.832  1.00 69.19  ? 324 HOH B O   1 
HETATM 1781 O O   . HOH I 3 .   ? 15.185 -10.033 17.634  1.00 22.27  ? 325 HOH B O   1 
HETATM 1782 O O   . HOH I 3 .   ? 39.664 -7.440  17.573  1.00 56.08  ? 326 HOH B O   1 
HETATM 1783 O O   . HOH I 3 .   ? 32.040 -20.037 14.428  1.00 47.45  ? 327 HOH B O   1 
HETATM 1784 O O   . HOH I 3 .   ? 26.851 5.690   23.902  1.00 15.66  ? 328 HOH B O   1 
HETATM 1785 O O   . HOH I 3 .   ? 15.275 -12.430 21.796  1.00 24.20  ? 329 HOH B O   1 
HETATM 1786 O O   . HOH I 3 .   ? 15.066 3.731   33.037  1.00 21.73  ? 330 HOH B O   1 
HETATM 1787 O O   . HOH I 3 .   ? 15.054 2.022   28.150  1.00 16.05  ? 331 HOH B O   1 
HETATM 1788 O O   . HOH I 3 .   ? 34.292 -0.965  17.027  1.00 35.91  ? 332 HOH B O   1 
HETATM 1789 O O   . HOH I 3 .   ? 7.802  -2.341  20.592  1.00 55.09  ? 333 HOH B O   1 
HETATM 1790 O O   . HOH I 3 .   ? 37.921 -15.648 22.334  1.00 21.54  ? 334 HOH B O   1 
HETATM 1791 O O   . HOH I 3 .   ? 20.993 -17.331 25.561  1.00 12.42  ? 335 HOH B O   1 
HETATM 1792 O O   . HOH I 3 .   ? 12.720 2.751   26.784  1.00 21.31  ? 336 HOH B O   1 
HETATM 1793 O O   . HOH I 3 .   ? 29.119 -1.979  27.211  1.00 16.77  ? 337 HOH B O   1 
HETATM 1794 O O   . HOH I 3 .   ? 29.841 -21.368 16.888  1.00 26.64  ? 338 HOH B O   1 
HETATM 1795 O O   . HOH I 3 .   ? 20.243 -20.701 28.202  1.00 38.60  ? 339 HOH B O   1 
HETATM 1796 O O   . HOH I 3 .   ? 16.692 7.981   32.762  1.00 30.36  ? 340 HOH B O   1 
HETATM 1797 O O   . HOH I 3 .   ? 20.565 -11.750 13.582  1.00 23.18  ? 341 HOH B O   1 
HETATM 1798 O O   . HOH I 3 .   ? 27.755 2.452   25.390  1.00 15.24  ? 342 HOH B O   1 
HETATM 1799 O O   . HOH I 3 .   ? 24.291 -15.768 31.671  1.00 16.80  ? 343 HOH B O   1 
HETATM 1800 O O   . HOH I 3 .   ? 19.343 -18.150 22.728  1.00 13.47  ? 344 HOH B O   1 
HETATM 1801 O O   . HOH I 3 .   ? 32.101 -16.498 27.575  1.00 45.72  ? 345 HOH B O   1 
HETATM 1802 O O   . HOH I 3 .   ? 16.133 3.895   36.768  1.00 51.01  ? 346 HOH B O   1 
HETATM 1803 O O   . HOH I 3 .   ? 15.781 -15.155 22.775  1.00 24.05  ? 347 HOH B O   1 
HETATM 1804 O O   . HOH I 3 .   ? 24.083 9.381   29.434  1.00 23.97  ? 348 HOH B O   1 
HETATM 1805 O O   . HOH I 3 .   ? 32.726 -7.228  29.674  1.00 16.98  ? 349 HOH B O   1 
HETATM 1806 O O   . HOH I 3 .   ? 39.974 -12.510 16.766  1.00 21.22  ? 350 HOH B O   1 
HETATM 1807 O O   . HOH I 3 .   ? 32.383 -17.540 24.774  1.00 19.84  ? 351 HOH B O   1 
HETATM 1808 O O   . HOH I 3 .   ? 20.502 -1.320  33.693  1.00 16.82  ? 352 HOH B O   1 
HETATM 1809 O O   . HOH I 3 .   ? 24.643 -21.714 29.639  1.00 44.30  ? 353 HOH B O   1 
HETATM 1810 O O   . HOH I 3 .   ? 37.395 -20.063 21.410  1.00 30.89  ? 354 HOH B O   1 
HETATM 1811 O O   . HOH I 3 .   ? 35.452 -11.631 11.010  1.00 35.53  ? 355 HOH B O   1 
HETATM 1812 O O   . HOH I 3 .   ? 29.031 -19.779 6.852   1.00 42.12  ? 356 HOH B O   1 
HETATM 1813 O O   . HOH I 3 .   ? 40.820 -13.924 23.202  1.00 23.21  ? 357 HOH B O   1 
HETATM 1814 O O   . HOH I 3 .   ? 12.540 -9.312  21.658  1.00 44.35  ? 358 HOH B O   1 
HETATM 1815 O O   . HOH I 3 .   ? 27.711 3.081   16.235  1.00 21.25  ? 359 HOH B O   1 
HETATM 1816 O O   . HOH I 3 .   ? 15.619 -3.596  33.134  1.00 19.31  ? 360 HOH B O   1 
HETATM 1817 O O   . HOH I 3 .   ? 33.404 -6.771  27.144  1.00 15.34  ? 361 HOH B O   1 
HETATM 1818 O O   . HOH I 3 .   ? 25.462 7.700   22.544  1.00 27.58  ? 362 HOH B O   1 
HETATM 1819 O O   . HOH I 3 .   ? 22.227 14.331  22.790  1.00 30.75  ? 363 HOH B O   1 
HETATM 1820 O O   . HOH I 3 .   ? 11.731 -3.355  36.897  1.00 60.78  ? 364 HOH B O   1 
HETATM 1821 O O   . HOH I 3 .   ? 31.278 0.849   23.948  1.00 15.87  ? 365 HOH B O   1 
HETATM 1822 O O   . HOH I 3 .   ? 14.642 -4.315  16.227  1.00 30.01  ? 366 HOH B O   1 
HETATM 1823 O O   . HOH I 3 .   ? 22.583 -23.722 27.592  1.00 43.07  ? 367 HOH B O   1 
HETATM 1824 O O   . HOH I 3 .   ? 26.731 -6.542  32.278  1.00 33.20  ? 368 HOH B O   1 
HETATM 1825 O O   . HOH I 3 .   ? 12.910 -9.208  25.157  1.00 41.11  ? 369 HOH B O   1 
HETATM 1826 O O   . HOH I 3 .   ? 16.445 -12.465 17.494  1.00 21.80  ? 370 HOH B O   1 
HETATM 1827 O O   . HOH I 3 .   ? 19.019 16.972  21.604  1.00 35.88  ? 371 HOH B O   1 
HETATM 1828 O O   . HOH I 3 .   ? 22.273 5.605   34.844  1.00 21.15  ? 372 HOH B O   1 
HETATM 1829 O O   . HOH I 3 .   ? 28.038 -19.972 25.098  1.00 27.77  ? 373 HOH B O   1 
HETATM 1830 O O   . HOH I 3 .   ? 17.862 -2.986  35.556  1.00 34.48  ? 374 HOH B O   1 
HETATM 1831 O O   . HOH I 3 .   ? 41.757 -19.856 13.844  1.00 36.93  ? 375 HOH B O   1 
HETATM 1832 O O   . HOH I 3 .   ? 33.071 -15.484 5.248   1.00 55.64  ? 376 HOH B O   1 
HETATM 1833 O O   . HOH I 3 .   ? 38.351 -9.520  16.137  1.00 39.99  ? 377 HOH B O   1 
HETATM 1834 O O   . HOH I 3 .   ? 34.942 -18.269 25.533  1.00 31.82  ? 378 HOH B O   1 
HETATM 1835 O O   . HOH I 3 .   ? 9.583  -7.071  39.097  1.00 36.35  ? 379 HOH B O   1 
HETATM 1836 O O   . HOH I 3 .   ? 29.326 -22.167 27.470  1.00 47.83  ? 380 HOH B O   1 
HETATM 1837 O O   . HOH I 3 .   ? 11.012 0.463   26.659  1.00 32.74  ? 381 HOH B O   1 
HETATM 1838 O O   . HOH I 3 .   ? 20.948 0.198   15.412  1.00 35.13  ? 382 HOH B O   1 
HETATM 1839 O O   . HOH I 3 .   ? 16.780 -3.287  15.139  1.00 23.13  ? 383 HOH B O   1 
HETATM 1840 O O   . HOH I 3 .   ? 10.421 -0.763  29.450  1.00 48.71  ? 384 HOH B O   1 
HETATM 1841 O O   . HOH I 3 .   ? 13.809 -10.874 20.064  1.00 35.05  ? 385 HOH B O   1 
HETATM 1842 O O   . HOH I 3 .   ? 11.057 -7.962  28.860  1.00 34.74  ? 386 HOH B O   1 
HETATM 1843 O O   . HOH I 3 .   ? 23.536 13.248  26.387  1.00 27.34  ? 387 HOH B O   1 
HETATM 1844 O O   . HOH I 3 .   ? 21.941 -13.587 10.895  1.00 36.13  ? 388 HOH B O   1 
HETATM 1845 O O   . HOH I 3 .   ? 36.549 -1.463  19.636  1.00 48.46  ? 389 HOH B O   1 
HETATM 1846 O O   . HOH I 3 .   ? 26.407 -4.321  33.777  1.00 22.70  ? 390 HOH B O   1 
HETATM 1847 O O   . HOH I 3 .   ? 13.211 -3.311  34.760  1.00 96.41  ? 391 HOH B O   1 
HETATM 1848 O O   . HOH I 3 .   ? 15.839 -8.767  40.882  1.00 42.60  ? 392 HOH B O   1 
HETATM 1849 O O   . HOH I 3 .   ? 17.584 -0.355  15.717  1.00 154.67 ? 393 HOH B O   1 
HETATM 1850 O O   . HOH I 3 .   ? 12.256 1.594   31.169  1.00 52.81  ? 394 HOH B O   1 
HETATM 1851 O O   . HOH I 3 .   ? 8.496  -3.665  34.581  1.00 53.38  ? 395 HOH B O   1 
HETATM 1852 O O   . HOH I 3 .   ? 6.976  -2.046  28.803  1.00 64.62  ? 396 HOH B O   1 
HETATM 1853 O O   . HOH I 3 .   ? 39.521 -3.769  24.800  1.00 18.72  ? 397 HOH B O   1 
HETATM 1854 O O   . HOH I 3 .   ? 34.591 -2.700  18.179  1.00 25.54  ? 398 HOH B O   1 
HETATM 1855 O O   . HOH I 3 .   ? 14.956 -12.249 26.680  1.00 48.72  ? 399 HOH B O   1 
HETATM 1856 O O   . HOH I 3 .   ? 30.541 -6.205  33.351  1.00 13.19  ? 400 HOH B O   1 
HETATM 1857 O O   . HOH I 3 .   ? 29.140 5.329   24.342  1.00 160.38 ? 401 HOH B O   1 
HETATM 1858 O O   . HOH I 3 .   ? 36.787 -24.441 23.026  1.00 67.48  ? 402 HOH B O   1 
HETATM 1859 O O   . HOH I 3 .   ? 37.892 -17.917 12.969  1.00 59.36  ? 403 HOH B O   1 
HETATM 1860 O O   . HOH I 3 .   ? 20.246 9.845   33.894  1.00 65.86  ? 404 HOH B O   1 
HETATM 1861 O O   . HOH I 3 .   ? 14.900 -6.958  41.944  1.00 76.73  ? 405 HOH B O   1 
HETATM 1862 O O   . HOH I 3 .   ? 28.555 -14.842 3.665   1.00 55.34  ? 406 HOH B O   1 
HETATM 1863 O O   . HOH I 3 .   ? 38.502 -17.966 23.692  1.00 50.07  ? 407 HOH B O   1 
HETATM 1864 O O   . HOH I 3 .   ? 11.695 -0.729  32.083  1.00 52.93  ? 408 HOH B O   1 
HETATM 1865 O O   . HOH I 3 .   ? 30.108 3.677   26.623  1.00 30.90  ? 409 HOH B O   1 
HETATM 1866 O O   . HOH I 3 .   ? 27.684 9.892   20.619  1.00 36.62  ? 410 HOH B O   1 
HETATM 1867 O O   . HOH I 3 .   ? 29.127 -0.099  25.229  1.00 15.35  ? 411 HOH B O   1 
HETATM 1868 O O   . HOH I 3 .   ? 30.011 6.616   26.988  1.00 43.00  ? 412 HOH B O   1 
HETATM 1869 O O   . HOH I 3 .   ? 15.081 6.107   34.031  1.00 41.96  ? 413 HOH B O   1 
HETATM 1870 O O   . HOH I 3 .   ? 18.491 -0.333  11.170  1.00 39.85  ? 414 HOH B O   1 
HETATM 1871 O O   . HOH I 3 .   ? 24.958 8.102   31.695  1.00 42.20  ? 415 HOH B O   1 
HETATM 1872 O O   . HOH I 3 .   ? 23.973 8.016   34.236  1.00 42.00  ? 416 HOH B O   1 
HETATM 1873 O O   . HOH I 3 .   ? 24.285 17.762  26.311  1.00 45.91  ? 417 HOH B O   1 
HETATM 1874 O O   . HOH I 3 .   ? 12.543 2.746   33.242  1.00 45.91  ? 418 HOH B O   1 
HETATM 1875 O O   . HOH I 3 .   ? 46.237 -11.114 13.210  1.00 50.81  ? 419 HOH B O   1 
HETATM 1876 O O   . HOH I 3 .   ? 26.027 10.157  27.398  1.00 34.75  ? 420 HOH B O   1 
HETATM 1877 O O   . HOH I 3 .   ? 25.730 -24.658 20.044  1.00 41.50  ? 421 HOH B O   1 
HETATM 1878 O O   . HOH I 3 .   ? 13.251 -6.637  15.109  1.00 34.88  ? 422 HOH B O   1 
HETATM 1879 O O   . HOH I 3 .   ? 16.483 -4.106  12.226  1.00 39.71  ? 423 HOH B 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   ALA 1   1   1   ALA ALA A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  HIS 30  30  30  HIS HIS A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   ASN 6   6   6   ASN ASN B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   THR 8   8   8   THR THR B . n 
B 1 9   ALA 9   9   9   ALA ALA B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  VAL 17  17  17  VAL VAL B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  SER 22  22  22  SER SER B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  SER 27  27  27  SER SER B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  HIS 30  30  30  HIS HIS B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  GLU 41  41  41  GLU GLU B . n 
B 1 42  LYS 42  42  42  LYS LYS B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  SER 49  49  49  SER SER B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  ILE 56  56  56  ILE ILE B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  GLN 60  60  60  GLN GLN B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  VAL 69  69  69  VAL VAL B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  PRO 77  77  77  PRO PRO B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  ILE 81  81  81  ILE ILE B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  PHE 84  84  84  PHE PHE B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  GLN 86  86  86  GLN GLN B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  GLY 91  91  91  GLY GLY B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 THR 103 103 103 THR THR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 PHE 109 109 109 PHE PHE B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 HIS 112 112 112 HIS HIS B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GOL 1   201 1   GOL GOL A . 
D 2 GOL 1   202 3   GOL GOL A . 
E 2 GOL 1   203 5   GOL GOL A . 
F 2 GOL 1   201 2   GOL GOL B . 
G 2 GOL 1   202 4   GOL GOL B . 
H 3 HOH 1   301 200 HOH HOH A . 
H 3 HOH 2   302 152 HOH HOH A . 
H 3 HOH 3   303 315 HOH HOH A . 
H 3 HOH 4   304 121 HOH HOH A . 
H 3 HOH 5   305 180 HOH HOH A . 
H 3 HOH 6   306 314 HOH HOH A . 
H 3 HOH 7   307 7   HOH HOH A . 
H 3 HOH 8   308 119 HOH HOH A . 
H 3 HOH 9   309 173 HOH HOH A . 
H 3 HOH 10  310 29  HOH HOH A . 
H 3 HOH 11  311 69  HOH HOH A . 
H 3 HOH 12  312 86  HOH HOH A . 
H 3 HOH 13  313 82  HOH HOH A . 
H 3 HOH 14  314 38  HOH HOH A . 
H 3 HOH 15  315 66  HOH HOH A . 
H 3 HOH 16  316 127 HOH HOH A . 
H 3 HOH 17  317 72  HOH HOH A . 
H 3 HOH 18  318 91  HOH HOH A . 
H 3 HOH 19  319 11  HOH HOH A . 
H 3 HOH 20  320 5   HOH HOH A . 
H 3 HOH 21  321 30  HOH HOH A . 
H 3 HOH 22  322 87  HOH HOH A . 
H 3 HOH 23  323 156 HOH HOH A . 
H 3 HOH 24  324 186 HOH HOH A . 
H 3 HOH 25  325 115 HOH HOH A . 
H 3 HOH 26  326 3   HOH HOH A . 
H 3 HOH 27  327 227 HOH HOH A . 
H 3 HOH 28  328 97  HOH HOH A . 
H 3 HOH 29  329 103 HOH HOH A . 
H 3 HOH 30  330 191 HOH HOH A . 
H 3 HOH 31  331 183 HOH HOH A . 
H 3 HOH 32  332 210 HOH HOH A . 
H 3 HOH 33  333 41  HOH HOH A . 
H 3 HOH 34  334 74  HOH HOH A . 
H 3 HOH 35  335 12  HOH HOH A . 
H 3 HOH 36  336 71  HOH HOH A . 
H 3 HOH 37  337 64  HOH HOH A . 
H 3 HOH 38  338 8   HOH HOH A . 
H 3 HOH 39  339 2   HOH HOH A . 
H 3 HOH 40  340 26  HOH HOH A . 
H 3 HOH 41  341 108 HOH HOH A . 
H 3 HOH 42  342 194 HOH HOH A . 
H 3 HOH 43  343 37  HOH HOH A . 
H 3 HOH 44  344 245 HOH HOH A . 
H 3 HOH 45  345 84  HOH HOH A . 
H 3 HOH 46  346 16  HOH HOH A . 
H 3 HOH 47  347 158 HOH HOH A . 
H 3 HOH 48  348 312 HOH HOH A . 
H 3 HOH 49  349 55  HOH HOH A . 
H 3 HOH 50  350 42  HOH HOH A . 
H 3 HOH 51  351 167 HOH HOH A . 
H 3 HOH 52  352 77  HOH HOH A . 
H 3 HOH 53  353 22  HOH HOH A . 
H 3 HOH 54  354 145 HOH HOH A . 
H 3 HOH 55  355 110 HOH HOH A . 
H 3 HOH 56  356 49  HOH HOH A . 
H 3 HOH 57  357 52  HOH HOH A . 
H 3 HOH 58  358 238 HOH HOH A . 
H 3 HOH 59  359 106 HOH HOH A . 
H 3 HOH 60  360 116 HOH HOH A . 
H 3 HOH 61  361 270 HOH HOH A . 
H 3 HOH 62  362 92  HOH HOH A . 
H 3 HOH 63  363 243 HOH HOH A . 
H 3 HOH 64  364 124 HOH HOH A . 
H 3 HOH 65  365 247 HOH HOH A . 
H 3 HOH 66  366 177 HOH HOH A . 
H 3 HOH 67  367 111 HOH HOH A . 
H 3 HOH 68  368 239 HOH HOH A . 
H 3 HOH 69  369 57  HOH HOH A . 
H 3 HOH 70  370 262 HOH HOH A . 
H 3 HOH 71  371 17  HOH HOH A . 
H 3 HOH 72  372 27  HOH HOH A . 
H 3 HOH 73  373 122 HOH HOH A . 
H 3 HOH 74  374 185 HOH HOH A . 
H 3 HOH 75  375 137 HOH HOH A . 
H 3 HOH 76  376 90  HOH HOH A . 
H 3 HOH 77  377 19  HOH HOH A . 
H 3 HOH 78  378 98  HOH HOH A . 
H 3 HOH 79  379 33  HOH HOH A . 
H 3 HOH 80  380 23  HOH HOH A . 
H 3 HOH 81  381 62  HOH HOH A . 
H 3 HOH 82  382 175 HOH HOH A . 
H 3 HOH 83  383 32  HOH HOH A . 
H 3 HOH 84  384 102 HOH HOH A . 
H 3 HOH 85  385 46  HOH HOH A . 
H 3 HOH 86  386 305 HOH HOH A . 
H 3 HOH 87  387 104 HOH HOH A . 
H 3 HOH 88  388 78  HOH HOH A . 
H 3 HOH 89  389 143 HOH HOH A . 
H 3 HOH 90  390 118 HOH HOH A . 
H 3 HOH 91  391 54  HOH HOH A . 
H 3 HOH 92  392 107 HOH HOH A . 
H 3 HOH 93  393 201 HOH HOH A . 
H 3 HOH 94  394 187 HOH HOH A . 
H 3 HOH 95  395 267 HOH HOH A . 
H 3 HOH 96  396 193 HOH HOH A . 
H 3 HOH 97  397 132 HOH HOH A . 
H 3 HOH 98  398 123 HOH HOH A . 
H 3 HOH 99  399 230 HOH HOH A . 
H 3 HOH 100 400 202 HOH HOH A . 
H 3 HOH 101 401 248 HOH HOH A . 
H 3 HOH 102 402 178 HOH HOH A . 
H 3 HOH 103 403 50  HOH HOH A . 
H 3 HOH 104 404 109 HOH HOH A . 
H 3 HOH 105 405 174 HOH HOH A . 
H 3 HOH 106 406 20  HOH HOH A . 
H 3 HOH 107 407 209 HOH HOH A . 
H 3 HOH 108 408 79  HOH HOH A . 
H 3 HOH 109 409 172 HOH HOH A . 
H 3 HOH 110 410 164 HOH HOH A . 
H 3 HOH 111 411 301 HOH HOH A . 
H 3 HOH 112 412 241 HOH HOH A . 
H 3 HOH 113 413 140 HOH HOH A . 
H 3 HOH 114 414 197 HOH HOH A . 
H 3 HOH 115 415 265 HOH HOH A . 
H 3 HOH 116 416 179 HOH HOH A . 
H 3 HOH 117 417 229 HOH HOH A . 
H 3 HOH 118 418 83  HOH HOH A . 
H 3 HOH 119 419 231 HOH HOH A . 
H 3 HOH 120 420 284 HOH HOH A . 
H 3 HOH 121 421 182 HOH HOH A . 
H 3 HOH 122 422 217 HOH HOH A . 
H 3 HOH 123 423 226 HOH HOH A . 
H 3 HOH 124 424 285 HOH HOH A . 
H 3 HOH 125 425 196 HOH HOH A . 
H 3 HOH 126 426 184 HOH HOH A . 
H 3 HOH 127 427 100 HOH HOH A . 
H 3 HOH 128 428 287 HOH HOH A . 
H 3 HOH 129 429 244 HOH HOH A . 
H 3 HOH 130 430 138 HOH HOH A . 
H 3 HOH 131 431 99  HOH HOH A . 
H 3 HOH 132 432 295 HOH HOH A . 
H 3 HOH 133 433 199 HOH HOH A . 
H 3 HOH 134 434 141 HOH HOH A . 
H 3 HOH 135 435 288 HOH HOH A . 
H 3 HOH 136 436 286 HOH HOH A . 
H 3 HOH 137 437 221 HOH HOH A . 
H 3 HOH 138 438 218 HOH HOH A . 
H 3 HOH 139 439 162 HOH HOH A . 
H 3 HOH 140 440 219 HOH HOH A . 
I 3 HOH 1   301 277 HOH HOH B . 
I 3 HOH 2   302 256 HOH HOH B . 
I 3 HOH 3   303 155 HOH HOH B . 
I 3 HOH 4   304 148 HOH HOH B . 
I 3 HOH 5   305 307 HOH HOH B . 
I 3 HOH 6   306 211 HOH HOH B . 
I 3 HOH 7   307 304 HOH HOH B . 
I 3 HOH 8   308 308 HOH HOH B . 
I 3 HOH 9   309 205 HOH HOH B . 
I 3 HOH 10  310 235 HOH HOH B . 
I 3 HOH 11  311 95  HOH HOH B . 
I 3 HOH 12  312 112 HOH HOH B . 
I 3 HOH 13  313 213 HOH HOH B . 
I 3 HOH 14  314 133 HOH HOH B . 
I 3 HOH 15  315 40  HOH HOH B . 
I 3 HOH 16  316 65  HOH HOH B . 
I 3 HOH 17  317 24  HOH HOH B . 
I 3 HOH 18  318 4   HOH HOH B . 
I 3 HOH 19  319 242 HOH HOH B . 
I 3 HOH 20  320 47  HOH HOH B . 
I 3 HOH 21  321 6   HOH HOH B . 
I 3 HOH 22  322 31  HOH HOH B . 
I 3 HOH 23  323 96  HOH HOH B . 
I 3 HOH 24  324 157 HOH HOH B . 
I 3 HOH 25  325 43  HOH HOH B . 
I 3 HOH 26  326 268 HOH HOH B . 
I 3 HOH 27  327 228 HOH HOH B . 
I 3 HOH 28  328 9   HOH HOH B . 
I 3 HOH 29  329 80  HOH HOH B . 
I 3 HOH 30  330 67  HOH HOH B . 
I 3 HOH 31  331 48  HOH HOH B . 
I 3 HOH 32  332 204 HOH HOH B . 
I 3 HOH 33  333 233 HOH HOH B . 
I 3 HOH 34  334 53  HOH HOH B . 
I 3 HOH 35  335 14  HOH HOH B . 
I 3 HOH 36  336 34  HOH HOH B . 
I 3 HOH 37  337 45  HOH HOH B . 
I 3 HOH 38  338 70  HOH HOH B . 
I 3 HOH 39  339 144 HOH HOH B . 
I 3 HOH 40  340 85  HOH HOH B . 
I 3 HOH 41  341 18  HOH HOH B . 
I 3 HOH 42  342 13  HOH HOH B . 
I 3 HOH 43  343 73  HOH HOH B . 
I 3 HOH 44  344 1   HOH HOH B . 
I 3 HOH 45  345 249 HOH HOH B . 
I 3 HOH 46  346 303 HOH HOH B . 
I 3 HOH 47  347 89  HOH HOH B . 
I 3 HOH 48  348 36  HOH HOH B . 
I 3 HOH 49  349 51  HOH HOH B . 
I 3 HOH 50  350 59  HOH HOH B . 
I 3 HOH 51  351 44  HOH HOH B . 
I 3 HOH 52  352 21  HOH HOH B . 
I 3 HOH 53  353 153 HOH HOH B . 
I 3 HOH 54  354 117 HOH HOH B . 
I 3 HOH 55  355 214 HOH HOH B . 
I 3 HOH 56  356 165 HOH HOH B . 
I 3 HOH 57  357 39  HOH HOH B . 
I 3 HOH 58  358 139 HOH HOH B . 
I 3 HOH 59  359 63  HOH HOH B . 
I 3 HOH 60  360 61  HOH HOH B . 
I 3 HOH 61  361 35  HOH HOH B . 
I 3 HOH 62  362 163 HOH HOH B . 
I 3 HOH 63  363 149 HOH HOH B . 
I 3 HOH 64  364 302 HOH HOH B . 
I 3 HOH 65  365 10  HOH HOH B . 
I 3 HOH 66  366 76  HOH HOH B . 
I 3 HOH 67  367 170 HOH HOH B . 
I 3 HOH 68  368 120 HOH HOH B . 
I 3 HOH 69  369 311 HOH HOH B . 
I 3 HOH 70  370 28  HOH HOH B . 
I 3 HOH 71  371 60  HOH HOH B . 
I 3 HOH 72  372 25  HOH HOH B . 
I 3 HOH 73  373 93  HOH HOH B . 
I 3 HOH 74  374 266 HOH HOH B . 
I 3 HOH 75  375 131 HOH HOH B . 
I 3 HOH 76  376 212 HOH HOH B . 
I 3 HOH 77  377 101 HOH HOH B . 
I 3 HOH 78  378 151 HOH HOH B . 
I 3 HOH 79  379 154 HOH HOH B . 
I 3 HOH 80  380 168 HOH HOH B . 
I 3 HOH 81  381 75  HOH HOH B . 
I 3 HOH 82  382 105 HOH HOH B . 
I 3 HOH 83  383 56  HOH HOH B . 
I 3 HOH 84  384 246 HOH HOH B . 
I 3 HOH 85  385 136 HOH HOH B . 
I 3 HOH 86  386 130 HOH HOH B . 
I 3 HOH 87  387 129 HOH HOH B . 
I 3 HOH 88  388 147 HOH HOH B . 
I 3 HOH 89  389 225 HOH HOH B . 
I 3 HOH 90  390 58  HOH HOH B . 
I 3 HOH 91  391 198 HOH HOH B . 
I 3 HOH 92  392 310 HOH HOH B . 
I 3 HOH 93  393 150 HOH HOH B . 
I 3 HOH 94  394 166 HOH HOH B . 
I 3 HOH 95  395 236 HOH HOH B . 
I 3 HOH 96  396 276 HOH HOH B . 
I 3 HOH 97  397 128 HOH HOH B . 
I 3 HOH 98  398 142 HOH HOH B . 
I 3 HOH 99  399 313 HOH HOH B . 
I 3 HOH 100 400 126 HOH HOH B . 
I 3 HOH 101 401 234 HOH HOH B . 
I 3 HOH 102 402 309 HOH HOH B . 
I 3 HOH 103 403 169 HOH HOH B . 
I 3 HOH 104 404 254 HOH HOH B . 
I 3 HOH 105 405 306 HOH HOH B . 
I 3 HOH 106 406 192 HOH HOH B . 
I 3 HOH 107 407 203 HOH HOH B . 
I 3 HOH 108 408 255 HOH HOH B . 
I 3 HOH 109 409 88  HOH HOH B . 
I 3 HOH 110 410 224 HOH HOH B . 
I 3 HOH 111 411 15  HOH HOH B . 
I 3 HOH 112 412 222 HOH HOH B . 
I 3 HOH 113 413 259 HOH HOH B . 
I 3 HOH 114 414 278 HOH HOH B . 
I 3 HOH 115 415 279 HOH HOH B . 
I 3 HOH 116 416 237 HOH HOH B . 
I 3 HOH 117 417 291 HOH HOH B . 
I 3 HOH 118 418 283 HOH HOH B . 
I 3 HOH 119 419 208 HOH HOH B . 
I 3 HOH 120 420 113 HOH HOH B . 
I 3 HOH 121 421 293 HOH HOH B . 
I 3 HOH 122 422 94  HOH HOH B . 
I 3 HOH 123 423 220 HOH HOH B . 
# 
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 ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_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_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2017-02-01 
2 'Structure model' 1 1 2018-01-17 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Data collection' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            diffrn_source 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_diffrn_source.pdbx_synchrotron_site' 
# 
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      ? ? ? 5.7.0032 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? iMOSFLM     ? ? ? .        3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
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 O1  B GOL 202 ? ? O   B HOH 301 ? ? 1.58 
2 1 CD  A GLU 85  ? ? O   A HOH 303 ? ? 1.93 
3 1 OE1 A GLU 85  ? ? O   A HOH 301 ? ? 2.05 
4 1 O   B HOH 332 ? ? O   B HOH 398 ? ? 2.10 
5 1 O   B GLY 64  ? ? O   B LYS 87  ? ? 2.13 
6 1 NZ  A LYS 67  ? ? OE2 A GLU 85  ? ? 2.15 
7 1 NE2 A GLN 60  ? ? O   A HOH 302 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     436 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     341 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   6_554 
_pdbx_validate_symm_contact.dist              1.98 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD  A GLU 85 ? ? OE2 A GLU 85 ? ? 1.130 1.252 -0.122 0.011 N 
2 1 CD2 A TRP 96 ? ? CE3 A TRP 96 ? ? 1.303 1.399 -0.096 0.015 N 
3 1 CB  A SER 98 ? ? OG  A SER 98 ? ? 1.319 1.418 -0.099 0.013 N 
4 1 CD  B GLU 85 ? ? OE1 B GLU 85 ? ? 1.154 1.252 -0.098 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 OE1 A GLU 85 ? ? CD A GLU 85 ? ? OE2 A GLU 85 ? ? 110.75 123.30 -12.55 1.20 N 
2 1 CB  B ASP 16 ? ? CG B ASP 16 ? ? OD1 B ASP 16 ? ? 123.74 118.30 5.44   0.90 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     61 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -136.79 
_pdbx_validate_torsion.psi             -139.45 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    48 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    49 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -123.60 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       440 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   . 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          6.55 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
3 water    HOH 
# 
