data_6FOI
# 
_entry.id   6FOI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.311 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6FOI         
WWPDB D_1200008683 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6FOI 
_pdbx_database_status.recvd_initial_deposition_date   2018-02-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wright, G.S.A.' 1 0000-0002-3756-9634 
'Sala, F.A.'     2 0000-0002-0287-3054 
'Antonyuk, S.V.' 3 0000-0002-2779-9946 
'Garratt, R.C.'  4 ?                   
'Hasnain, S.S.'  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            'Plos Biol.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-7885 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            17 
_citation.language                  ? 
_citation.page_first                e3000141 
_citation.page_last                 e3000141 
_citation.title                     
'Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1371/journal.pbio.3000141 
_citation.pdbx_database_id_PubMed   30735496 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sala, F.A.'     1 ?                   
primary 'Wright, G.S.A.' 2 0000-0002-3756-9634 
primary 'Antonyuk, S.V.' 3 0000-0002-2779-9946 
primary 'Garratt, R.C.'  4 0000-0002-2016-3179 
primary 'Hasnain, S.S.'  5 0000-0002-2854-4718 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6FOI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.650 
_cell.length_a_esd                 ? 
_cell.length_b                     162.959 
_cell.length_b_esd                 ? 
_cell.length_c                     174.601 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6FOI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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]' 15763.432 12   1.15.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                     65.409    12   ?        ? ? ? 
3 non-polymer syn 'SULFATE ION'                  96.063    13   ?        ? ? ? 
4 water       nat water                          18.015    1064 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGATSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLAAGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGATSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLAAGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F,D,G,I,K,M,O,Q,S,U,W 
_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   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  ALA n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 ALA n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   153 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           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 6FOI A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2  1 6FOI F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3  1 6FOI D 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4  1 6FOI G 1 ? 153 ? P00441 2 ? 154 ? 1 153 
5  1 6FOI I 1 ? 153 ? P00441 2 ? 154 ? 1 153 
6  1 6FOI K 1 ? 153 ? P00441 2 ? 154 ? 1 153 
7  1 6FOI M 1 ? 153 ? P00441 2 ? 154 ? 1 153 
8  1 6FOI O 1 ? 153 ? P00441 2 ? 154 ? 1 153 
9  1 6FOI Q 1 ? 153 ? P00441 2 ? 154 ? 1 153 
10 1 6FOI S 1 ? 153 ? P00441 2 ? 154 ? 1 153 
11 1 6FOI U 1 ? 153 ? P00441 2 ? 154 ? 1 153 
12 1 6FOI W 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1  6FOI ALA A 57  ? UNP P00441 CYS 58  'engineered mutation' 57  1  
1  6FOI ALA A 146 ? UNP P00441 CYS 147 'engineered mutation' 146 2  
2  6FOI ALA F 57  ? UNP P00441 CYS 58  'engineered mutation' 57  3  
2  6FOI ALA F 146 ? UNP P00441 CYS 147 'engineered mutation' 146 4  
3  6FOI ALA D 57  ? UNP P00441 CYS 58  'engineered mutation' 57  5  
3  6FOI ALA D 146 ? UNP P00441 CYS 147 'engineered mutation' 146 6  
4  6FOI ALA G 57  ? UNP P00441 CYS 58  'engineered mutation' 57  7  
4  6FOI ALA G 146 ? UNP P00441 CYS 147 'engineered mutation' 146 8  
5  6FOI ALA I 57  ? UNP P00441 CYS 58  'engineered mutation' 57  9  
5  6FOI ALA I 146 ? UNP P00441 CYS 147 'engineered mutation' 146 10 
6  6FOI ALA K 57  ? UNP P00441 CYS 58  'engineered mutation' 57  11 
6  6FOI ALA K 146 ? UNP P00441 CYS 147 'engineered mutation' 146 12 
7  6FOI ALA M 57  ? UNP P00441 CYS 58  'engineered mutation' 57  13 
7  6FOI ALA M 146 ? UNP P00441 CYS 147 'engineered mutation' 146 14 
8  6FOI ALA O 57  ? UNP P00441 CYS 58  'engineered mutation' 57  15 
8  6FOI ALA O 146 ? UNP P00441 CYS 147 'engineered mutation' 146 16 
9  6FOI ALA Q 57  ? UNP P00441 CYS 58  'engineered mutation' 57  17 
9  6FOI ALA Q 146 ? UNP P00441 CYS 147 'engineered mutation' 146 18 
10 6FOI ALA S 57  ? UNP P00441 CYS 58  'engineered mutation' 57  19 
10 6FOI ALA S 146 ? UNP P00441 CYS 147 'engineered mutation' 146 20 
11 6FOI ALA U 57  ? UNP P00441 CYS 58  'engineered mutation' 57  21 
11 6FOI ALA U 146 ? UNP P00441 CYS 147 'engineered mutation' 146 22 
12 6FOI ALA W 57  ? UNP P00441 CYS 58  'engineered mutation' 57  23 
12 6FOI ALA W 146 ? UNP P00441 CYS 147 'engineered mutation' 146 24 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6FOI 
_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            2.77 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         55.6 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8 
_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    
;0.2 M Lithium sulphate
24% w/v PEG 4000
0.1 M Tris-HCl pH 8.0
;
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-09-27 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            27.7 
_reflns.entry_id                         6FOI 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.0 
_reflns.d_resolution_low                 81.48 
_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                       144348 
_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                  6.1 
_reflns.pdbx_Rmerge_I_obs                0.084 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            12.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.102 
_reflns.pdbx_Rpim_I_all                  0.056 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.998 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.0 
_reflns_shell.d_res_low                   2.03 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.9 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           7089 
_reflns_shell.percent_possible_all        100 
_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                0.832 
_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             5.7 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             0.101 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.783 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            -0.91 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            2.34 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.43 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               44.674 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.924 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. TLS REFINEMENT USED THROUGHOUT. ALL CHAINS WERE NCS RESTRAINED TO CHAIN F IN EARLY STAGES.
;
_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                                 6FOI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             81.48 
_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                     136979 
_refine.ls_number_reflns_R_free                  7261 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.22270 
_refine.ls_R_factor_R_free                       0.25941 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22076 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2c9v 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.192 
_refine.pdbx_overall_ESU_R_Free                  0.171 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             10.245 
_refine.overall_SU_ML                            0.154 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        13259 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_refine_hist.number_atoms_solvent             1064 
_refine_hist.number_atoms_total               14400 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        81.48 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  0.019  13567 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  12348 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.149  1.947  18334 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.841  3.000  28796 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.179  5.000  1833  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 40.000 25.571 578   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.013 15.000 2183  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.582 15.000 50    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.064  0.200  2032  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  15673 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  2473  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.726  7341  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.726  7340  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 0.152  1.089  9159  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.152  1.089  9160  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.771  6226  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.113  0.760  6212  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.135  1.138  9153  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.120  10.217 14185 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.036  9.355  13955 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             579 
_refine_ls_shell.number_reflns_R_work             10011 
_refine_ls_shell.percent_reflns_obs               99.98 
_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                  0.316 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.306 
_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                     6FOI 
_struct.title                        'Human Cys57/156Ala superoxide dismutase-1 (SOD1), as isolated.' 
_struct.pdbx_descriptor              'Copper chaperone for superoxide dismutase' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6FOI 
_struct_keywords.text            'zinc, copper, disulphide mutant, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 1 ? 
L  N N 1 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 2 ? 
CA N N 2 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 2 ? 
GA N N 3 ? 
HA N N 2 ? 
IA N N 3 ? 
JA N N 2 ? 
KA N N 3 ? 
LA N N 4 ? 
MA N N 4 ? 
NA N N 4 ? 
OA N N 4 ? 
PA N N 4 ? 
QA N N 4 ? 
RA N N 4 ? 
SA N N 4 ? 
TA N N 4 ? 
UA N N 4 ? 
VA N N 4 ? 
WA N N 4 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  AA2 ASN A 131 ? THR A 135 ? ASN A 131 THR A 135 5 ? 5 
HELX_P HELX_P3  AA3 ALA B 55  ? GLY B 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P4  AA4 ASN B 131 ? THR B 135 ? ASN F 131 THR F 135 5 ? 5 
HELX_P HELX_P5  AA5 ALA C 55  ? GLY C 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P6  AA6 SER C 107 ? CYS C 111 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P7  AA7 ALA D 55  ? GLY D 61  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P8  AA8 ALA E 55  ? GLY E 61  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P9  AA9 ALA F 55  ? GLY F 61  ? ALA K 55  GLY K 61  5 ? 7 
HELX_P HELX_P10 AB1 ALA G 55  ? GLY G 61  ? ALA M 55  GLY M 61  5 ? 7 
HELX_P HELX_P11 AB2 ASN G 131 ? THR G 135 ? ASN M 131 THR M 135 5 ? 5 
HELX_P HELX_P12 AB3 ALA H 55  ? GLY H 61  ? ALA O 55  GLY O 61  5 ? 7 
HELX_P HELX_P13 AB4 ALA I 55  ? GLY I 61  ? ALA Q 55  GLY Q 61  5 ? 7 
HELX_P HELX_P14 AB5 GLU I 133 ? GLY I 138 ? GLU Q 133 GLY Q 138 1 ? 6 
HELX_P HELX_P15 AB6 ALA K 55  ? ALA K 60  ? ALA U 55  ALA U 60  5 ? 6 
HELX_P HELX_P16 AB7 SER K 107 ? CYS K 111 ? SER U 107 CYS U 111 5 ? 5 
HELX_P HELX_P17 AB8 ALA L 57  ? GLY L 61  ? ALA W 57  GLY W 61  5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1  metalc ? ? A HIS 63 ND1 ? ? ? 1_555 M  ZN . ZN ? ? A HIS 63 A ZN 201 1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc2  metalc ? ? A HIS 71 ND1 ? ? ? 1_555 M  ZN . ZN ? ? A HIS 71 A ZN 201 1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc3  metalc ? ? A HIS 80 ND1 ? ? ? 1_555 M  ZN . ZN ? ? A HIS 80 A ZN 201 1_555 ? ? ? ? ? ? ? 2.171 ? 
metalc4  metalc ? ? A ASP 83 OD1 ? ? ? 1_555 M  ZN . ZN ? ? A ASP 83 A ZN 201 1_555 ? ? ? ? ? ? ? 1.894 ? 
metalc5  metalc ? ? B HIS 63 ND1 ? ? ? 1_555 O  ZN . ZN ? ? F HIS 63 F ZN 201 1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc6  metalc ? ? B HIS 71 ND1 ? ? ? 1_555 O  ZN . ZN ? ? F HIS 71 F ZN 201 1_555 ? ? ? ? ? ? ? 2.099 ? 
metalc7  metalc ? ? B HIS 80 ND1 ? ? ? 1_555 O  ZN . ZN ? ? F HIS 80 F ZN 201 1_555 ? ? ? ? ? ? ? 2.207 ? 
metalc8  metalc ? ? B ASP 83 OD1 ? ? ? 1_555 O  ZN . ZN ? ? F ASP 83 F ZN 201 1_555 ? ? ? ? ? ? ? 1.800 ? 
metalc9  metalc ? ? C HIS 63 ND1 ? ? ? 1_555 R  ZN . ZN ? ? D HIS 63 D ZN 201 1_555 ? ? ? ? ? ? ? 2.019 ? 
metalc10 metalc ? ? C HIS 71 ND1 ? ? ? 1_555 R  ZN . ZN ? ? D HIS 71 D ZN 201 1_555 ? ? ? ? ? ? ? 2.045 ? 
metalc11 metalc ? ? C HIS 80 ND1 ? ? ? 1_555 R  ZN . ZN ? ? D HIS 80 D ZN 201 1_555 ? ? ? ? ? ? ? 2.140 ? 
metalc12 metalc ? ? C ASP 83 OD1 ? ? ? 1_555 R  ZN . ZN ? ? D ASP 83 D ZN 201 1_555 ? ? ? ? ? ? ? 1.972 ? 
metalc13 metalc ? ? D HIS 63 ND1 ? ? ? 1_555 T  ZN . ZN ? ? G HIS 63 G ZN 201 1_555 ? ? ? ? ? ? ? 2.083 ? 
metalc14 metalc ? ? D HIS 71 ND1 ? ? ? 1_555 T  ZN . ZN ? ? G HIS 71 G ZN 201 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc15 metalc ? ? D HIS 80 ND1 ? ? ? 1_555 T  ZN . ZN ? ? G HIS 80 G ZN 201 1_555 ? ? ? ? ? ? ? 2.190 ? 
metalc16 metalc ? ? D ASP 83 OD1 ? ? ? 1_555 T  ZN . ZN ? ? G ASP 83 G ZN 201 1_555 ? ? ? ? ? ? ? 1.791 ? 
metalc17 metalc ? ? E HIS 63 ND1 ? ? ? 1_555 V  ZN . ZN ? ? I HIS 63 I ZN 201 1_555 ? ? ? ? ? ? ? 2.002 ? 
metalc18 metalc ? ? E HIS 71 ND1 ? ? ? 1_555 V  ZN . ZN ? ? I HIS 71 I ZN 201 1_555 ? ? ? ? ? ? ? 2.155 ? 
metalc19 metalc ? ? E HIS 80 ND1 ? ? ? 1_555 V  ZN . ZN ? ? I HIS 80 I ZN 201 1_555 ? ? ? ? ? ? ? 2.208 ? 
metalc20 metalc ? ? E ASP 83 OD1 ? ? ? 1_555 V  ZN . ZN ? ? I ASP 83 I ZN 201 1_555 ? ? ? ? ? ? ? 1.928 ? 
metalc21 metalc ? ? F HIS 63 ND1 ? ? ? 1_555 X  ZN . ZN ? ? K HIS 63 K ZN 201 1_555 ? ? ? ? ? ? ? 2.088 ? 
metalc22 metalc ? ? F HIS 71 ND1 ? ? ? 1_555 X  ZN . ZN ? ? K HIS 71 K ZN 201 1_555 ? ? ? ? ? ? ? 1.938 ? 
metalc23 metalc ? ? F HIS 80 ND1 ? ? ? 1_555 X  ZN . ZN ? ? K HIS 80 K ZN 201 1_555 ? ? ? ? ? ? ? 1.994 ? 
metalc24 metalc ? ? F ASP 83 OD1 ? ? ? 1_555 X  ZN . ZN ? ? K ASP 83 K ZN 201 1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc25 metalc ? ? G HIS 63 ND1 ? ? ? 1_555 Z  ZN . ZN ? ? M HIS 63 M ZN 201 1_555 ? ? ? ? ? ? ? 2.168 ? 
metalc26 metalc ? ? G HIS 71 ND1 ? ? ? 1_555 Z  ZN . ZN ? ? M HIS 71 M ZN 201 1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc27 metalc ? ? G HIS 80 ND1 ? ? ? 1_555 Z  ZN . ZN ? ? M HIS 80 M ZN 201 1_555 ? ? ? ? ? ? ? 2.080 ? 
metalc28 metalc ? ? G ASP 83 OD1 ? ? ? 1_555 Z  ZN . ZN ? ? M ASP 83 M ZN 201 1_555 ? ? ? ? ? ? ? 1.881 ? 
metalc29 metalc ? ? H HIS 63 ND1 ? ? ? 1_555 BA ZN . ZN ? ? O HIS 63 O ZN 201 1_555 ? ? ? ? ? ? ? 2.164 ? 
metalc30 metalc ? ? H HIS 71 ND1 ? ? ? 1_555 BA ZN . ZN ? ? O HIS 71 O ZN 201 1_555 ? ? ? ? ? ? ? 2.275 ? 
metalc31 metalc ? ? H HIS 80 ND1 ? ? ? 1_555 BA ZN . ZN ? ? O HIS 80 O ZN 201 1_555 ? ? ? ? ? ? ? 2.228 ? 
metalc32 metalc ? ? H ASP 83 OD1 ? ? ? 1_555 BA ZN . ZN ? ? O ASP 83 O ZN 201 1_555 ? ? ? ? ? ? ? 2.082 ? 
metalc33 metalc ? ? I HIS 63 ND1 ? ? ? 1_555 CA ZN . ZN ? ? Q HIS 63 Q ZN 201 1_555 ? ? ? ? ? ? ? 2.156 ? 
metalc34 metalc ? ? I HIS 71 ND1 ? ? ? 1_555 CA ZN . ZN ? ? Q HIS 71 Q ZN 201 1_555 ? ? ? ? ? ? ? 2.088 ? 
metalc35 metalc ? ? I HIS 80 ND1 ? ? ? 1_555 CA ZN . ZN ? ? Q HIS 80 Q ZN 201 1_555 ? ? ? ? ? ? ? 2.031 ? 
metalc36 metalc ? ? I ASP 83 OD1 ? ? ? 1_555 CA ZN . ZN ? ? Q ASP 83 Q ZN 201 1_555 ? ? ? ? ? ? ? 1.808 ? 
metalc37 metalc ? ? J HIS 63 ND1 ? ? ? 1_555 FA ZN . ZN ? ? S HIS 63 S ZN 201 1_555 ? ? ? ? ? ? ? 2.220 ? 
metalc38 metalc ? ? J HIS 71 ND1 ? ? ? 1_555 FA ZN . ZN ? ? S HIS 71 S ZN 201 1_555 ? ? ? ? ? ? ? 2.122 ? 
metalc39 metalc ? ? J HIS 80 ND1 ? ? ? 1_555 FA ZN . ZN ? ? S HIS 80 S ZN 201 1_555 ? ? ? ? ? ? ? 2.123 ? 
metalc40 metalc ? ? J ASP 83 OD1 ? ? ? 1_555 FA ZN . ZN ? ? S ASP 83 S ZN 201 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc41 metalc ? ? K HIS 63 ND1 ? ? ? 1_555 HA ZN . ZN ? ? U HIS 63 U ZN 201 1_555 ? ? ? ? ? ? ? 2.261 ? 
metalc42 metalc ? ? K HIS 71 ND1 ? ? ? 1_555 HA ZN . ZN ? ? U HIS 71 U ZN 201 1_555 ? ? ? ? ? ? ? 2.251 ? 
metalc43 metalc ? ? K HIS 80 ND1 ? ? ? 1_555 HA ZN . ZN ? ? U HIS 80 U ZN 201 1_555 ? ? ? ? ? ? ? 2.224 ? 
metalc44 metalc ? ? K ASP 83 OD1 ? ? ? 1_555 HA ZN . ZN ? ? U ASP 83 U ZN 201 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc45 metalc ? ? L HIS 63 ND1 ? ? ? 1_555 JA ZN . ZN ? ? W HIS 63 W ZN 201 1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc46 metalc ? ? L HIS 71 ND1 ? ? ? 1_555 JA ZN . ZN ? ? W HIS 71 W ZN 201 1_555 ? ? ? ? ? ? ? 2.026 ? 
metalc47 metalc ? ? L HIS 80 ND1 ? ? ? 1_555 JA ZN . ZN ? ? W HIS 80 W ZN 201 1_555 ? ? ? ? ? ? ? 2.209 ? 
metalc48 metalc ? ? L ASP 83 OD1 ? ? ? 1_555 JA ZN . ZN ? ? W ASP 83 W ZN 201 1_555 ? ? ? ? ? ? ? 1.857 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 8 ? 
AB1 ? 6 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 4 ? 
AC1 ? 5 ? 
AC2 ? 4 ? 
AC3 ? 5 ? 
AC4 ? 4 ? 
AC5 ? 8 ? 
AC6 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AA9 7 8 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC3 4 5 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC5 5 6 ? anti-parallel 
AC5 6 7 ? anti-parallel 
AC5 7 8 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC6 4 5 ? anti-parallel 
AC6 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA1 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA1 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA1 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
AA1 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
AA2 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AA2 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AA2 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AA2 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
AA3 1 ALA B 95  ? ASP B 101 ? ALA F 95  ASP F 101 
AA3 2 VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
AA3 3 GLN B 15  ? GLN B 22  ? GLN F 15  GLN F 22  
AA3 4 THR B 2   ? LEU B 8   ? THR F 2   LEU F 8   
AA3 5 GLY B 150 ? ILE B 151 ? GLY F 150 ILE F 151 
AA4 1 ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
AA4 2 GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
AA4 3 THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
AA4 4 ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 148 
AA5 1 ALA C 95  ? ASP C 101 ? ALA D 95  ASP D 101 
AA5 2 VAL C 29  ? LYS C 36  ? VAL D 29  LYS D 36  
AA5 3 GLN C 15  ? GLN C 22  ? GLN D 15  GLN D 22  
AA5 4 THR C 2   ? LEU C 8   ? THR D 2   LEU D 8   
AA5 5 GLY C 150 ? ILE C 151 ? GLY D 150 ILE D 151 
AA6 1 ASP C 83  ? ALA C 89  ? ASP D 83  ALA D 89  
AA6 2 GLY C 41  ? HIS C 48  ? GLY D 41  HIS D 48  
AA6 3 THR C 116 ? HIS C 120 ? THR D 116 HIS D 120 
AA6 4 ARG C 143 ? VAL C 148 ? ARG D 143 VAL D 148 
AA7 1 ALA D 95  ? ASP D 101 ? ALA G 95  ASP G 101 
AA7 2 VAL D 29  ? LYS D 36  ? VAL G 29  LYS G 36  
AA7 3 GLN D 15  ? GLN D 22  ? GLN G 15  GLN G 22  
AA7 4 THR D 2   ? LEU D 8   ? THR G 2   LEU G 8   
AA7 5 GLY D 150 ? ILE D 151 ? GLY G 150 ILE G 151 
AA8 1 ASP D 83  ? ALA D 89  ? ASP G 83  ALA G 89  
AA8 2 GLY D 41  ? HIS D 48  ? GLY G 41  HIS G 48  
AA8 3 THR D 116 ? HIS D 120 ? THR G 116 HIS G 120 
AA8 4 ARG D 143 ? VAL D 148 ? ARG G 143 VAL G 148 
AA9 1 ASP E 83  ? ALA E 89  ? ASP I 83  ALA I 89  
AA9 2 GLY E 41  ? HIS E 48  ? GLY I 41  HIS I 48  
AA9 3 THR E 116 ? HIS E 120 ? THR I 116 HIS I 120 
AA9 4 ARG E 143 ? VAL E 148 ? ARG I 143 VAL I 148 
AA9 5 THR E 2   ? GLY E 10  ? THR I 2   GLY I 10  
AA9 6 GLN E 15  ? GLN E 22  ? GLN I 15  GLN I 22  
AA9 7 VAL E 29  ? LYS E 36  ? VAL I 29  LYS I 36  
AA9 8 ALA E 95  ? ASP E 101 ? ALA I 95  ASP I 101 
AB1 1 ASP E 83  ? ALA E 89  ? ASP I 83  ALA I 89  
AB1 2 GLY E 41  ? HIS E 48  ? GLY I 41  HIS I 48  
AB1 3 THR E 116 ? HIS E 120 ? THR I 116 HIS I 120 
AB1 4 ARG E 143 ? VAL E 148 ? ARG I 143 VAL I 148 
AB1 5 THR E 2   ? GLY E 10  ? THR I 2   GLY I 10  
AB1 6 GLY E 150 ? ALA E 152 ? GLY I 150 ALA I 152 
AB2 1 ALA F 95  ? ASP F 101 ? ALA K 95  ASP K 101 
AB2 2 VAL F 29  ? LYS F 36  ? VAL K 29  LYS K 36  
AB2 3 GLN F 15  ? GLN F 22  ? GLN K 15  GLN K 22  
AB2 4 THR F 2   ? LEU F 8   ? THR K 2   LEU K 8   
AB2 5 GLY F 150 ? ALA F 152 ? GLY K 150 ALA K 152 
AB3 1 ASP F 83  ? ALA F 89  ? ASP K 83  ALA K 89  
AB3 2 GLY F 41  ? HIS F 48  ? GLY K 41  HIS K 48  
AB3 3 THR F 116 ? HIS F 120 ? THR K 116 HIS K 120 
AB3 4 ARG F 143 ? VAL F 148 ? ARG K 143 VAL K 148 
AB4 1 ALA G 95  ? ASP G 101 ? ALA M 95  ASP M 101 
AB4 2 VAL G 29  ? LYS G 36  ? VAL M 29  LYS M 36  
AB4 3 GLN G 15  ? GLN G 22  ? GLN M 15  GLN M 22  
AB4 4 THR G 2   ? LEU G 8   ? THR M 2   LEU M 8   
AB4 5 GLY G 150 ? ILE G 151 ? GLY M 150 ILE M 151 
AB5 1 ASP G 83  ? ALA G 89  ? ASP M 83  ALA M 89  
AB5 2 GLY G 41  ? HIS G 48  ? GLY M 41  HIS M 48  
AB5 3 THR G 116 ? HIS G 120 ? THR M 116 HIS M 120 
AB5 4 ARG G 143 ? VAL G 148 ? ARG M 143 VAL M 148 
AB6 1 ALA H 95  ? ASP H 101 ? ALA O 95  ASP O 101 
AB6 2 VAL H 29  ? LYS H 36  ? VAL O 29  LYS O 36  
AB6 3 GLN H 15  ? GLN H 22  ? GLN O 15  GLN O 22  
AB6 4 THR H 2   ? LEU H 8   ? THR O 2   LEU O 8   
AB6 5 GLY H 150 ? ILE H 151 ? GLY O 150 ILE O 151 
AB7 1 ASP H 83  ? ALA H 89  ? ASP O 83  ALA O 89  
AB7 2 GLY H 41  ? HIS H 48  ? GLY O 41  HIS O 48  
AB7 3 THR H 116 ? HIS H 120 ? THR O 116 HIS O 120 
AB7 4 ARG H 143 ? VAL H 148 ? ARG O 143 VAL O 148 
AB8 1 ALA I 95  ? ASP I 101 ? ALA Q 95  ASP Q 101 
AB8 2 VAL I 29  ? LYS I 36  ? VAL Q 29  LYS Q 36  
AB8 3 GLN I 15  ? GLN I 22  ? GLN Q 15  GLN Q 22  
AB8 4 THR I 2   ? LEU I 8   ? THR Q 2   LEU Q 8   
AB8 5 GLY I 150 ? ALA I 152 ? GLY Q 150 ALA Q 152 
AB9 1 ASP I 83  ? ALA I 89  ? ASP Q 83  ALA Q 89  
AB9 2 GLY I 41  ? HIS I 48  ? GLY Q 41  HIS Q 48  
AB9 3 THR I 116 ? HIS I 120 ? THR Q 116 HIS Q 120 
AB9 4 ARG I 143 ? VAL I 148 ? ARG Q 143 VAL Q 148 
AC1 1 ALA J 95  ? ASP J 101 ? ALA S 95  ASP S 101 
AC1 2 VAL J 29  ? LYS J 36  ? VAL S 29  LYS S 36  
AC1 3 GLN J 15  ? GLN J 22  ? GLN S 15  GLN S 22  
AC1 4 THR J 2   ? LEU J 8   ? THR S 2   LEU S 8   
AC1 5 GLY J 150 ? ILE J 151 ? GLY S 150 ILE S 151 
AC2 1 ASP J 83  ? ALA J 89  ? ASP S 83  ALA S 89  
AC2 2 GLY J 41  ? HIS J 48  ? GLY S 41  HIS S 48  
AC2 3 THR J 116 ? HIS J 120 ? THR S 116 HIS S 120 
AC2 4 ARG J 143 ? VAL J 148 ? ARG S 143 VAL S 148 
AC3 1 VAL K 94  ? ASP K 101 ? VAL U 94  ASP U 101 
AC3 2 VAL K 29  ? LYS K 36  ? VAL U 29  LYS U 36  
AC3 3 GLN K 15  ? GLN K 22  ? GLN U 15  GLN U 22  
AC3 4 THR K 2   ? LYS K 9   ? THR U 2   LYS U 9   
AC3 5 GLY K 150 ? ILE K 151 ? GLY U 150 ILE U 151 
AC4 1 ASP K 83  ? ASN K 86  ? ASP U 83  ASN U 86  
AC4 2 GLY K 44  ? HIS K 48  ? GLY U 44  HIS U 48  
AC4 3 THR K 116 ? HIS K 120 ? THR U 116 HIS U 120 
AC4 4 ARG K 143 ? VAL K 148 ? ARG U 143 VAL U 148 
AC5 1 ASP L 83  ? ALA L 89  ? ASP W 83  ALA W 89  
AC5 2 GLY L 41  ? HIS L 48  ? GLY W 41  HIS W 48  
AC5 3 THR L 116 ? HIS L 120 ? THR W 116 HIS W 120 
AC5 4 ARG L 143 ? VAL L 148 ? ARG W 143 VAL W 148 
AC5 5 LYS L 3   ? GLY L 10  ? LYS W 3   GLY W 10  
AC5 6 GLN L 15  ? GLU L 21  ? GLN W 15  GLU W 21  
AC5 7 VAL L 29  ? LYS L 36  ? VAL W 29  LYS W 36  
AC5 8 ALA L 95  ? ASP L 101 ? ALA W 95  ASP W 101 
AC6 1 ASP L 83  ? ALA L 89  ? ASP W 83  ALA W 89  
AC6 2 GLY L 41  ? HIS L 48  ? GLY W 41  HIS W 48  
AC6 3 THR L 116 ? HIS L 120 ? THR W 116 HIS W 120 
AC6 4 ARG L 143 ? VAL L 148 ? ARG W 143 VAL W 148 
AC6 5 LYS L 3   ? GLY L 10  ? LYS W 3   GLY W 10  
AC6 6 GLY L 150 ? ALA L 152 ? GLY W 150 ALA W 152 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 95  ? O ALA A 95  N ILE A 35  ? N ILE A 35  
AA1 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
AA1 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
AA1 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AA2 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
AA2 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AA2 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
AA3 1 2 O ILE B 99  ? O ILE F 99  N VAL B 31  ? N VAL F 31  
AA3 2 3 O TRP B 32  ? O TRP F 32  N ASN B 19  ? N ASN F 19  
AA3 3 4 O GLY B 16  ? O GLY F 16  N LEU B 8   ? N LEU F 8   
AA3 4 5 N VAL B 5   ? N VAL F 5   O GLY B 150 ? O GLY F 150 
AA4 1 2 O ALA B 89  ? O ALA F 89  N GLY B 41  ? N GLY F 41  
AA4 2 3 N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
AA4 3 4 N LEU B 117 ? N LEU F 117 O GLY B 147 ? O GLY F 147 
AA5 1 2 O ILE C 99  ? O ILE D 99  N VAL C 31  ? N VAL D 31  
AA5 2 3 O TRP C 32  ? O TRP D 32  N ASN C 19  ? N ASN D 19  
AA5 3 4 O PHE C 20  ? O PHE D 20  N ALA C 4   ? N ALA D 4   
AA5 4 5 N VAL C 5   ? N VAL D 5   O GLY C 150 ? O GLY D 150 
AA6 1 2 O ALA C 89  ? O ALA D 89  N GLY C 41  ? N GLY D 41  
AA6 2 3 N HIS C 48  ? N HIS D 48  O THR C 116 ? O THR D 116 
AA6 3 4 N VAL C 119 ? N VAL D 119 O ALA C 145 ? O ALA D 145 
AA7 1 2 O ILE D 99  ? O ILE G 99  N VAL D 31  ? N VAL G 31  
AA7 2 3 O TRP D 32  ? O TRP G 32  N ASN D 19  ? N ASN G 19  
AA7 3 4 O GLN D 22  ? O GLN G 22  N THR D 2   ? N THR G 2   
AA7 4 5 N VAL D 5   ? N VAL G 5   O GLY D 150 ? O GLY G 150 
AA8 1 2 O ALA D 89  ? O ALA G 89  N GLY D 41  ? N GLY G 41  
AA8 2 3 N HIS D 48  ? N HIS G 48  O THR D 116 ? O THR G 116 
AA8 3 4 N LEU D 117 ? N LEU G 117 O GLY D 147 ? O GLY G 147 
AA9 1 2 O GLY E 85  ? O GLY I 85  N PHE E 45  ? N PHE I 45  
AA9 2 3 N HIS E 48  ? N HIS I 48  O THR E 116 ? O THR I 116 
AA9 3 4 N LEU E 117 ? N LEU I 117 O GLY E 147 ? O GLY I 147 
AA9 4 5 O ALA E 146 ? O ALA I 146 N LYS E 9   ? N LYS I 9   
AA9 5 6 N ALA E 4   ? N ALA I 4   O PHE E 20  ? O PHE I 20  
AA9 6 7 N ASN E 19  ? N ASN I 19  O TRP E 32  ? O TRP I 32  
AA9 7 8 N GLY E 33  ? N GLY I 33  O VAL E 97  ? O VAL I 97  
AB1 1 2 O GLY E 85  ? O GLY I 85  N PHE E 45  ? N PHE I 45  
AB1 2 3 N HIS E 48  ? N HIS I 48  O THR E 116 ? O THR I 116 
AB1 3 4 N LEU E 117 ? N LEU I 117 O GLY E 147 ? O GLY I 147 
AB1 4 5 O ALA E 146 ? O ALA I 146 N LYS E 9   ? N LYS I 9   
AB1 5 6 N VAL E 5   ? N VAL I 5   O GLY E 150 ? O GLY I 150 
AB2 1 2 O ILE F 99  ? O ILE K 99  N VAL F 31  ? N VAL K 31  
AB2 2 3 O TRP F 32  ? O TRP K 32  N ASN F 19  ? N ASN K 19  
AB2 3 4 O GLY F 16  ? O GLY K 16  N LEU F 8   ? N LEU K 8   
AB2 4 5 N VAL F 5   ? N VAL K 5   O GLY F 150 ? O GLY K 150 
AB3 1 2 O ALA F 89  ? O ALA K 89  N GLY F 41  ? N GLY K 41  
AB3 2 3 N HIS F 48  ? N HIS K 48  O THR F 116 ? O THR K 116 
AB3 3 4 N VAL F 119 ? N VAL K 119 O ALA F 145 ? O ALA K 145 
AB4 1 2 O ILE G 99  ? O ILE M 99  N VAL G 31  ? N VAL M 31  
AB4 2 3 O TRP G 32  ? O TRP M 32  N ASN G 19  ? N ASN M 19  
AB4 3 4 O PHE G 20  ? O PHE M 20  N ALA G 4   ? N ALA M 4   
AB4 4 5 N VAL G 5   ? N VAL M 5   O GLY G 150 ? O GLY M 150 
AB5 1 2 O ALA G 89  ? O ALA M 89  N GLY G 41  ? N GLY M 41  
AB5 2 3 N HIS G 48  ? N HIS M 48  O THR G 116 ? O THR M 116 
AB5 3 4 N LEU G 117 ? N LEU M 117 O GLY G 147 ? O GLY M 147 
AB6 1 2 O ILE H 99  ? O ILE O 99  N VAL H 31  ? N VAL O 31  
AB6 2 3 O LYS H 30  ? O LYS O 30  N GLU H 21  ? N GLU O 21  
AB6 3 4 O GLY H 16  ? O GLY O 16  N LEU H 8   ? N LEU O 8   
AB6 4 5 N VAL H 5   ? N VAL O 5   O GLY H 150 ? O GLY O 150 
AB7 1 2 O ALA H 89  ? O ALA O 89  N GLY H 41  ? N GLY O 41  
AB7 2 3 N HIS H 46  ? N HIS O 46  O VAL H 118 ? O VAL O 118 
AB7 3 4 N VAL H 119 ? N VAL O 119 O ALA H 145 ? O ALA O 145 
AB8 1 2 O ASP I 101 ? O ASP Q 101 N VAL I 29  ? N VAL Q 29  
AB8 2 3 O TRP I 32  ? O TRP Q 32  N ASN I 19  ? N ASN Q 19  
AB8 3 4 O GLY I 16  ? O GLY Q 16  N LEU I 8   ? N LEU Q 8   
AB8 4 5 N VAL I 5   ? N VAL Q 5   O GLY I 150 ? O GLY Q 150 
AB9 1 2 O ALA I 89  ? O ALA Q 89  N GLY I 41  ? N GLY Q 41  
AB9 2 3 N HIS I 48  ? N HIS Q 48  O THR I 116 ? O THR Q 116 
AB9 3 4 N VAL I 119 ? N VAL Q 119 O ALA I 145 ? O ALA Q 145 
AC1 1 2 O ALA J 95  ? O ALA S 95  N ILE J 35  ? N ILE S 35  
AC1 2 3 O TRP J 32  ? O TRP S 32  N ASN J 19  ? N ASN S 19  
AC1 3 4 O GLY J 16  ? O GLY S 16  N LEU J 8   ? N LEU S 8   
AC1 4 5 N VAL J 5   ? N VAL S 5   O GLY J 150 ? O GLY S 150 
AC2 1 2 O ALA J 89  ? O ALA S 89  N GLY J 41  ? N GLY S 41  
AC2 2 3 N HIS J 48  ? N HIS S 48  O THR J 116 ? O THR S 116 
AC2 3 4 N VAL J 119 ? N VAL S 119 O ALA J 145 ? O ALA S 145 
AC3 1 2 O ASP K 101 ? O ASP U 101 N VAL K 29  ? N VAL U 29  
AC3 2 3 O LYS K 36  ? O LYS U 36  N GLN K 15  ? N GLN U 15  
AC3 3 4 O ILE K 18  ? O ILE U 18  N CYS K 6   ? N CYS U 6   
AC3 4 5 N VAL K 5   ? N VAL U 5   O GLY K 150 ? O GLY U 150 
AC4 1 2 O GLY K 85  ? O GLY U 85  N PHE K 45  ? N PHE U 45  
AC4 2 3 N HIS K 48  ? N HIS U 48  O THR K 116 ? O THR U 116 
AC4 3 4 N VAL K 119 ? N VAL U 119 O ALA K 145 ? O ALA U 145 
AC5 1 2 O VAL L 87  ? O VAL W 87  N HIS L 43  ? N HIS W 43  
AC5 2 3 N HIS L 46  ? N HIS W 46  O VAL L 118 ? O VAL W 118 
AC5 3 4 N VAL L 119 ? N VAL W 119 O ALA L 145 ? O ALA W 145 
AC5 4 5 O ALA L 146 ? O ALA W 146 N LYS L 9   ? N LYS W 9   
AC5 5 6 N LEU L 8   ? N LEU W 8   O GLY L 16  ? O GLY W 16  
AC5 6 7 N GLN L 15  ? N GLN W 15  O LYS L 36  ? O LYS W 36  
AC5 7 8 N VAL L 31  ? N VAL W 31  O ILE L 99  ? O ILE W 99  
AC6 1 2 O VAL L 87  ? O VAL W 87  N HIS L 43  ? N HIS W 43  
AC6 2 3 N HIS L 46  ? N HIS W 46  O VAL L 118 ? O VAL W 118 
AC6 3 4 N VAL L 119 ? N VAL W 119 O ALA L 145 ? O ALA W 145 
AC6 4 5 O ALA L 146 ? O ALA W 146 N LYS L 9   ? N LYS W 9   
AC6 5 6 N VAL L 5   ? N VAL W 5   O GLY L 150 ? O GLY W 150 
# 
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 ZN  201 ? 5 'binding site for residue ZN A 201'  
AC2 Software A SO4 202 ? 7 'binding site for residue SO4 A 202' 
AC3 Software F ZN  201 ? 4 'binding site for residue ZN F 201'  
AC4 Software F SO4 202 ? 8 'binding site for residue SO4 F 202' 
AC5 Software F SO4 203 ? 6 'binding site for residue SO4 F 203' 
AC6 Software D ZN  201 ? 4 'binding site for residue ZN D 201'  
AC7 Software D SO4 202 ? 6 'binding site for residue SO4 D 202' 
AC8 Software G ZN  201 ? 4 'binding site for residue ZN G 201'  
AC9 Software G SO4 202 ? 3 'binding site for residue SO4 G 202' 
AD1 Software I ZN  201 ? 4 'binding site for residue ZN I 201'  
AD2 Software I SO4 202 ? 5 'binding site for residue SO4 I 202' 
AD3 Software K ZN  201 ? 4 'binding site for residue ZN K 201'  
AD4 Software K SO4 202 ? 5 'binding site for residue SO4 K 202' 
AD5 Software M ZN  201 ? 4 'binding site for residue ZN M 201'  
AD6 Software M SO4 202 ? 4 'binding site for residue SO4 M 202' 
AD7 Software O ZN  201 ? 4 'binding site for residue ZN O 201'  
AD8 Software Q ZN  201 ? 4 'binding site for residue ZN Q 201'  
AD9 Software Q SO4 202 ? 4 'binding site for residue SO4 Q 202' 
AE1 Software Q SO4 203 ? 5 'binding site for residue SO4 Q 203' 
AE2 Software S ZN  201 ? 5 'binding site for residue ZN S 201'  
AE3 Software S SO4 202 ? 4 'binding site for residue SO4 S 202' 
AE4 Software U ZN  201 ? 4 'binding site for residue ZN U 201'  
AE5 Software U SO4 202 ? 4 'binding site for residue SO4 U 202' 
AE6 Software W ZN  201 ? 4 'binding site for residue ZN W 201'  
AE7 Software W SO4 202 ? 5 'binding site for residue SO4 W 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 5 HIS A  63  ? HIS A 63  . ? 1_555 ? 
2   AC1 5 HIS A  71  ? HIS A 71  . ? 1_555 ? 
3   AC1 5 HIS A  80  ? HIS A 80  . ? 1_555 ? 
4   AC1 5 ASP A  83  ? ASP A 83  . ? 1_555 ? 
5   AC1 5 LYS A  136 ? LYS A 136 . ? 1_555 ? 
6   AC2 7 HIS A  120 ? HIS A 120 . ? 1_555 ? 
7   AC2 7 THR A  137 ? THR A 137 . ? 1_555 ? 
8   AC2 7 ARG A  143 ? ARG A 143 . ? 1_555 ? 
9   AC2 7 HOH LA .   ? HOH A 304 . ? 1_555 ? 
10  AC2 7 HOH LA .   ? HOH A 308 . ? 1_555 ? 
11  AC2 7 HOH LA .   ? HOH A 313 . ? 1_555 ? 
12  AC2 7 HOH LA .   ? HOH A 340 . ? 1_555 ? 
13  AC3 4 HIS B  63  ? HIS F 63  . ? 1_555 ? 
14  AC3 4 HIS B  71  ? HIS F 71  . ? 1_555 ? 
15  AC3 4 HIS B  80  ? HIS F 80  . ? 1_555 ? 
16  AC3 4 ASP B  83  ? ASP F 83  . ? 1_555 ? 
17  AC4 8 HIS B  120 ? HIS F 120 . ? 1_555 ? 
18  AC4 8 THR B  137 ? THR F 137 . ? 1_555 ? 
19  AC4 8 ARG B  143 ? ARG F 143 . ? 1_555 ? 
20  AC4 8 HOH MA .   ? HOH F 316 . ? 1_555 ? 
21  AC4 8 HOH MA .   ? HOH F 332 . ? 1_555 ? 
22  AC4 8 HOH MA .   ? HOH F 340 . ? 1_555 ? 
23  AC4 8 HOH MA .   ? HOH F 349 . ? 1_555 ? 
24  AC4 8 HOH MA .   ? HOH F 389 . ? 1_555 ? 
25  AC5 6 LYS B  128 ? LYS F 128 . ? 1_555 ? 
26  AC5 6 HOH MA .   ? HOH F 345 . ? 1_555 ? 
27  AC5 6 HOH MA .   ? HOH F 357 . ? 1_555 ? 
28  AC5 6 LYS F  75  ? LYS K 75  . ? 1_555 ? 
29  AC5 6 LYS F  128 ? LYS K 128 . ? 1_555 ? 
30  AC5 6 LYS G  128 ? LYS M 128 . ? 1_555 ? 
31  AC6 4 HIS C  63  ? HIS D 63  . ? 1_555 ? 
32  AC6 4 HIS C  71  ? HIS D 71  . ? 1_555 ? 
33  AC6 4 HIS C  80  ? HIS D 80  . ? 1_555 ? 
34  AC6 4 ASP C  83  ? ASP D 83  . ? 1_555 ? 
35  AC7 6 HIS C  48  ? HIS D 48  . ? 1_555 ? 
36  AC7 6 HIS C  120 ? HIS D 120 . ? 1_555 ? 
37  AC7 6 THR C  137 ? THR D 137 . ? 1_555 ? 
38  AC7 6 ARG C  143 ? ARG D 143 . ? 1_555 ? 
39  AC7 6 HOH NA .   ? HOH D 306 . ? 1_555 ? 
40  AC7 6 HOH NA .   ? HOH D 310 . ? 1_555 ? 
41  AC8 4 HIS D  63  ? HIS G 63  . ? 1_555 ? 
42  AC8 4 HIS D  71  ? HIS G 71  . ? 1_555 ? 
43  AC8 4 HIS D  80  ? HIS G 80  . ? 1_555 ? 
44  AC8 4 ASP D  83  ? ASP G 83  . ? 1_555 ? 
45  AC9 3 THR D  137 ? THR G 137 . ? 1_555 ? 
46  AC9 3 GLY D  141 ? GLY G 141 . ? 1_555 ? 
47  AC9 3 ARG D  143 ? ARG G 143 . ? 1_555 ? 
48  AD1 4 HIS E  63  ? HIS I 63  . ? 1_555 ? 
49  AD1 4 HIS E  71  ? HIS I 71  . ? 1_555 ? 
50  AD1 4 HIS E  80  ? HIS I 80  . ? 1_555 ? 
51  AD1 4 ASP E  83  ? ASP I 83  . ? 1_555 ? 
52  AD2 5 HIS E  48  ? HIS I 48  . ? 1_555 ? 
53  AD2 5 HIS E  120 ? HIS I 120 . ? 1_555 ? 
54  AD2 5 THR E  137 ? THR I 137 . ? 1_555 ? 
55  AD2 5 ARG E  143 ? ARG I 143 . ? 1_555 ? 
56  AD2 5 HOH PA .   ? HOH I 315 . ? 1_555 ? 
57  AD3 4 HIS F  63  ? HIS K 63  . ? 1_555 ? 
58  AD3 4 HIS F  71  ? HIS K 71  . ? 1_555 ? 
59  AD3 4 HIS F  80  ? HIS K 80  . ? 1_555 ? 
60  AD3 4 ASP F  83  ? ASP K 83  . ? 1_555 ? 
61  AD4 5 HIS F  48  ? HIS K 48  . ? 1_555 ? 
62  AD4 5 HIS F  120 ? HIS K 120 . ? 1_555 ? 
63  AD4 5 THR F  137 ? THR K 137 . ? 1_555 ? 
64  AD4 5 ARG F  143 ? ARG K 143 . ? 1_555 ? 
65  AD4 5 HOH QA .   ? HOH K 301 . ? 1_555 ? 
66  AD5 4 HIS G  63  ? HIS M 63  . ? 1_555 ? 
67  AD5 4 HIS G  71  ? HIS M 71  . ? 1_555 ? 
68  AD5 4 HIS G  80  ? HIS M 80  . ? 1_555 ? 
69  AD5 4 ASP G  83  ? ASP M 83  . ? 1_555 ? 
70  AD6 4 HIS G  120 ? HIS M 120 . ? 1_555 ? 
71  AD6 4 THR G  137 ? THR M 137 . ? 1_555 ? 
72  AD6 4 GLY G  141 ? GLY M 141 . ? 1_555 ? 
73  AD6 4 ARG G  143 ? ARG M 143 . ? 1_555 ? 
74  AD7 4 HIS H  63  ? HIS O 63  . ? 1_555 ? 
75  AD7 4 HIS H  71  ? HIS O 71  . ? 1_555 ? 
76  AD7 4 HIS H  80  ? HIS O 80  . ? 1_555 ? 
77  AD7 4 ASP H  83  ? ASP O 83  . ? 1_555 ? 
78  AD8 4 HIS I  63  ? HIS Q 63  . ? 1_555 ? 
79  AD8 4 HIS I  71  ? HIS Q 71  . ? 1_555 ? 
80  AD8 4 HIS I  80  ? HIS Q 80  . ? 1_555 ? 
81  AD8 4 ASP I  83  ? ASP Q 83  . ? 1_555 ? 
82  AD9 4 THR I  137 ? THR Q 137 . ? 1_555 ? 
83  AD9 4 GLY I  141 ? GLY Q 141 . ? 1_555 ? 
84  AD9 4 ARG I  143 ? ARG Q 143 . ? 1_555 ? 
85  AD9 4 HOH TA .   ? HOH Q 355 . ? 1_555 ? 
86  AE1 5 LYS D  128 ? LYS G 128 . ? 1_555 ? 
87  AE1 5 LYS I  75  ? LYS Q 75  . ? 1_555 ? 
88  AE1 5 LYS I  128 ? LYS Q 128 . ? 1_555 ? 
89  AE1 5 LYS L  128 ? LYS W 128 . ? 1_555 ? 
90  AE1 5 HOH WA .   ? HOH W 330 . ? 1_555 ? 
91  AE2 5 HIS J  63  ? HIS S 63  . ? 1_555 ? 
92  AE2 5 HIS J  71  ? HIS S 71  . ? 1_555 ? 
93  AE2 5 HIS J  80  ? HIS S 80  . ? 1_555 ? 
94  AE2 5 ASP J  83  ? ASP S 83  . ? 1_555 ? 
95  AE2 5 LYS J  136 ? LYS S 136 . ? 1_555 ? 
96  AE3 4 HIS J  48  ? HIS S 48  . ? 1_555 ? 
97  AE3 4 HIS J  120 ? HIS S 120 . ? 1_555 ? 
98  AE3 4 THR J  137 ? THR S 137 . ? 1_555 ? 
99  AE3 4 ARG J  143 ? ARG S 143 . ? 1_555 ? 
100 AE4 4 HIS K  63  ? HIS U 63  . ? 1_555 ? 
101 AE4 4 HIS K  71  ? HIS U 71  . ? 1_555 ? 
102 AE4 4 HIS K  80  ? HIS U 80  . ? 1_555 ? 
103 AE4 4 ASP K  83  ? ASP U 83  . ? 1_555 ? 
104 AE5 4 HIS K  48  ? HIS U 48  . ? 1_555 ? 
105 AE5 4 HIS K  120 ? HIS U 120 . ? 1_555 ? 
106 AE5 4 THR K  137 ? THR U 137 . ? 1_555 ? 
107 AE5 4 ARG K  143 ? ARG U 143 . ? 1_555 ? 
108 AE6 4 HIS L  63  ? HIS W 63  . ? 1_555 ? 
109 AE6 4 HIS L  71  ? HIS W 71  . ? 1_555 ? 
110 AE6 4 HIS L  80  ? HIS W 80  . ? 1_555 ? 
111 AE6 4 ASP L  83  ? ASP W 83  . ? 1_555 ? 
112 AE7 5 HIS L  48  ? HIS W 48  . ? 1_555 ? 
113 AE7 5 HIS L  120 ? HIS W 120 . ? 1_555 ? 
114 AE7 5 THR L  137 ? THR W 137 . ? 1_555 ? 
115 AE7 5 GLY L  141 ? GLY W 141 . ? 1_555 ? 
116 AE7 5 ARG L  143 ? ARG W 143 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6FOI 
_atom_sites.fract_transf_matrix[1][1]   0.013396 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006137 
_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]   0.005727 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ALA A  1 1   ? 8.393   43.812  31.245  1.00 43.06  ? 1   ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 9.445   44.006  30.198  1.00 40.93  ? 1   ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 10.264  42.732  30.009  1.00 38.63  ? 1   ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 10.557  42.046  30.978  1.00 38.86  ? 1   ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 10.359  45.167  30.571  1.00 41.55  ? 1   ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 10.614  42.417  28.766  1.00 36.72  ? 2   THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 11.499  41.288  28.459  1.00 34.66  ? 2   THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 12.922  41.833  28.321  1.00 33.58  ? 2   THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 13.122  42.923  27.774  1.00 33.72  ? 2   THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 11.046  40.568  27.170  1.00 33.63  ? 2   THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 9.633   40.324  27.238  1.00 35.08  ? 2   THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 11.744  39.249  26.997  1.00 32.15  ? 2   THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 13.893  41.077  28.841  1.00 32.62  ? 3   LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 15.306  41.465  28.834  1.00 31.86  ? 3   LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 16.178  40.326  28.318  1.00 30.09  ? 3   LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 15.903  39.152  28.581  1.00 29.76  ? 3   LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 15.756  41.865  30.236  1.00 33.29  ? 3   LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 15.157  43.177  30.722  1.00 35.22  ? 3   LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 15.614  43.542  32.125  1.00 36.92  ? 3   LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 17.049  44.053  32.147  0.50 36.82  ? 3   LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 17.521  44.340  33.528  0.50 38.67  ? 3   LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 17.210  40.680  27.560  1.00 29.08  ? 4   ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 18.192  39.714  27.069  1.00 27.76  ? 4   ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 19.584  40.311  27.114  1.00 27.74  ? 4   ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 19.746  41.530  27.237  1.00 28.46  ? 4   ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 17.855  39.249  25.660  1.00 26.65  ? 4   ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 20.579  39.434  27.010  1.00 27.06  ? 5   VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 21.981  39.833  27.098  1.00 27.33  ? 5   VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 22.847  38.951  26.192  1.00 26.40  ? 5   VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 22.523  37.777  25.956  1.00 25.73  ? 5   VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 22.473  39.812  28.567  1.00 28.57  ? 5   VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 22.513  38.393  29.124  1.00 28.41  ? 5   VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 23.834  40.496  28.708  1.00 29.31  ? 5   VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 23.920  39.539  25.667  1.00 26.53  ? 6   CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 24.877  38.824  24.826  1.00 26.07  ? 6   CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 26.301  39.205  25.211  1.00 27.06  ? 6   CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 26.628  40.386  25.257  1.00 27.72  ? 6   CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 24.647  39.165  23.364  1.00 25.29  ? 6   CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 25.680  38.220  22.215  1.00 24.94  ? 6   CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 27.129  38.200  25.490  1.00 27.44  ? 7   VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 28.571  38.385  25.722  1.00 28.67  ? 7   VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 29.310  38.095  24.407  1.00 28.39  ? 7   VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 29.340  36.958  23.955  1.00 27.94  ? 7   VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 29.079  37.450  26.834  1.00 29.58  ? 7   VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 30.582  37.627  27.054  1.00 31.03  ? 7   VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 28.303  37.702  28.120  1.00 30.13  ? 7   VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 29.882  39.125  23.793  1.00 28.94  ? 8   LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 30.614  38.982  22.533  1.00 29.01  ? 8   LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 32.059  38.592  22.796  1.00 30.62  ? 8   LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 32.760  39.306  23.499  1.00 31.92  ? 8   LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 30.590  40.292  21.750  1.00 29.02  ? 8   LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 29.217  40.767  21.264  1.00 27.91  ? 8   LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 29.314  42.210  20.811  1.00 28.46  ? 8   LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 28.715  39.893  20.132  1.00 26.83  ? 8   LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 32.488  37.457  22.239  1.00 30.85  ? 9   LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 33.865  36.989  22.349  1.00 32.66  ? 9   LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 34.352  36.417  21.026  1.00 32.63  ? 9   LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 33.550  35.923  20.222  1.00 31.24  ? 9   LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 33.987  35.891  23.415  1.00 33.57  ? 9   LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 33.667  36.319  24.836  1.00 34.27  ? 9   LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 34.719  37.263  25.388  1.00 36.27  ? 9   LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 34.442  37.624  26.838  1.00 37.23  ? 9   LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 34.724  36.480  27.750  1.00 38.28  ? 9   LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 35.675  36.461  20.835  1.00 34.20  ? 10  GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 36.322  35.885  19.652  1.00 34.77  ? 10  GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 37.758  35.470  19.898  1.00 37.06  ? 10  GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 38.197  35.374  21.044  1.00 38.05  ? 10  GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 38.486  35.252  18.803  1.00 38.06  ? 11  ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 39.878  34.808  18.843  1.00 40.57  ? 11  ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? 40.875  35.946  19.110  1.00 42.10  ? 11  ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? 41.973  35.694  19.604  1.00 44.32  ? 11  ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 40.244  34.095  17.529  1.00 41.37  ? 11  ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? 39.362  32.883  17.256  1.00 40.48  ? 11  ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? 39.070  32.116  18.202  1.00 40.56  ? 11  ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? 38.943  32.703  16.090  1.00 40.07  ? 11  ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? 40.499  37.182  18.772  1.00 41.07  ? 12  GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? 41.352  38.362  18.976  1.00 42.56  ? 12  GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? 40.986  39.144  20.233  1.00 42.33  ? 12  GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? 40.417  38.583  21.165  1.00 41.56  ? 12  GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? 41.310  40.454  20.267  1.00 43.10  ? 13  PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? 41.005  41.301  21.420  1.00 43.29  ? 13  PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? 39.560  41.848  21.461  1.00 40.93  ? 13  PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? 39.182  42.478  22.450  1.00 41.14  ? 13  PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? 41.997  42.449  21.260  1.00 45.56  ? 13  PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? 42.140  42.597  19.783  1.00 45.15  ? 13  PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? 41.960  41.225  19.189  1.00 44.04  ? 13  PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 38.757  41.616  20.424  1.00 38.89  ? 14  VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 37.418  42.206  20.380  1.00 37.05  ? 14  VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 36.515  41.464  21.366  1.00 35.90  ? 14  VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 36.408  40.239  21.316  1.00 35.28  ? 14  VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 36.819  42.210  18.955  1.00 35.59  ? 14  VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 35.413  42.798  18.959  1.00 34.00  ? 14  VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 37.716  43.004  18.013  1.00 36.90  ? 14  VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 35.908  42.213  22.282  1.00 35.92  ? 15  GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 34.963  41.652  23.252  1.00 35.04  ? 15  GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 34.032  42.721  23.807  1.00 34.75  ? 15  GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 34.382  43.899  23.867  1.00 35.90  ? 15  GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 35.698  40.950  24.398  1.00 36.54  ? 15  GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 36.766  41.798  25.067  1.00 39.03  ? 15  GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? 37.369  41.161  26.311  1.00 40.73  ? 15  GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? 37.896  41.859  27.160  1.00 42.84  ? 15  GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? 37.308  39.841  26.417  1.00 40.26  ? 15  GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 32.839  42.303  24.209  1.00 33.39  ? 16  GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 31.844  43.244  24.709  1.00 33.25  ? 16  GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 30.617  42.586  25.297  1.00 32.06  ? 16  GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 30.460  41.369  25.224  1.00 31.08  ? 16  GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 29.766  43.415  25.895  1.00 32.30  ? 17  ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 28.499  42.993  26.484  1.00 31.51  ? 17  ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 27.401  43.858  25.886  1.00 30.89  ? 17  ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 27.468  45.082  25.967  1.00 31.94  ? 17  ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 28.508  43.146  28.021  1.00 33.04  ? 17  ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 29.587  42.233  28.626  1.00 33.77  ? 17  ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 27.120  42.830  28.591  1.00 32.54  ? 17  ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 29.809  42.376  30.118  1.00 35.60  ? 17  ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 26.396  43.222  25.286  1.00 29.39  ? 18  ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 25.258  43.938  24.716  1.00 29.00  ? 18  ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 23.987  43.516  25.440  1.00 28.83  ? 18  ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 23.734  42.323  25.634  1.00 28.08  ? 18  ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 25.124  43.687  23.199  1.00 27.76  ? 18  ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 26.394  44.137  22.459  1.00 28.10  ? 18  ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 23.895  44.404  22.631  1.00 27.62  ? 18  ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 26.668  45.630  22.487  1.00 29.43  ? 18  ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 23.204  44.514  25.834  1.00 29.71  ? 19  ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 21.948  44.325  26.541  1.00 29.99  ? 19  ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 20.800  44.621  25.598  1.00 29.46  ? 19  ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 20.922  45.468  24.725  1.00 29.49  ? 19  ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 21.881  45.265  27.737  1.00 31.90  ? 19  ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 23.043  45.069  28.689  1.00 32.76  ? 19  ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 23.093  44.080  29.430  1.00 32.60  ? 19  ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 23.997  45.999  28.658  1.00 33.81  ? 19  ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 19.696  43.907  25.791  1.00 29.19  ? 20  PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 18.454  44.115  25.046  1.00 29.08  ? 20  PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 17.310  44.266  26.046  1.00 30.37  ? 20  PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 17.281  43.573  27.068  1.00 30.56  ? 20  PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 18.140  42.935  24.148  1.00 27.65  ? 20  PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 19.229  42.583  23.171  1.00 26.56  ? 20  PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 20.342  41.854  23.580  1.00 26.14  ? 20  PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 19.119  42.935  21.828  1.00 26.13  ? 20  PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 21.329  41.502  22.672  1.00 25.38  ? 20  PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 20.117  42.606  20.921  1.00 25.31  ? 20  PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 21.212  41.877  21.344  1.00 24.96  ? 20  PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 16.382  45.173  25.751  1.00 31.38  ? 21  GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 15.193  45.355  26.574  1.00 32.92  ? 21  GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 13.998  45.790  25.725  1.00 33.40  ? 21  GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 14.100  46.723  24.933  1.00 33.65  ? 21  GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 15.463  46.367  27.682  1.00 34.88  ? 21  GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 14.292  46.552  28.643  1.00 36.86  ? 21  GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 14.676  47.227  29.955  1.00 38.87  ? 21  GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 15.821  47.723  30.090  1.00 39.09  ? 21  GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 13.821  47.261  30.865  1.00 40.59  ? 21  GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 12.873  45.107  25.917  1.00 33.68  ? 22  GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 11.654  45.365  25.173  1.00 34.42  ? 22  GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 10.493  45.487  26.163  1.00 36.41  ? 22  GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 10.084  44.496  26.765  1.00 36.35  ? 22  GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 11.421  44.233  24.178  1.00 32.92  ? 22  GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 10.273  44.483  23.211  1.00 33.73  ? 22  GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 10.029  43.308  22.279  1.00 32.56  ? 22  GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 10.393  42.175  22.588  1.00 31.46  ? 22  GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 9.395   43.574  21.138  1.00 32.94  ? 22  GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 9.973   46.706  26.312  1.00 38.36  ? 23  LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 9.016   47.037  27.374  1.00 40.73  ? 23  LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 7.644   46.388  27.149  1.00 41.44  ? 23  LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 6.991   45.961  28.107  1.00 42.64  ? 23  LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 8.895   48.560  27.515  1.00 42.93  ? 23  LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 8.177   49.023  28.775  1.00 45.71  ? 23  LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 8.347   50.517  29.036  1.00 47.95  ? 23  LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 7.590   51.408  28.049  1.00 49.29  ? 23  LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 6.127   51.486  28.321  1.00 51.76  ? 23  LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 7.219   46.322  25.887  1.00 40.88  ? 24  GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 6.023   45.577  25.487  1.00 41.48  ? 24  GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 6.301   44.748  24.252  1.00 39.36  ? 24  GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 7.094   45.140  23.402  1.00 38.06  ? 24  GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 4.843   46.515  25.207  1.00 44.16  ? 24  GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 4.142   47.026  26.454  1.00 46.86  ? 24  GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 4.756   48.287  27.035  1.00 47.97  ? 24  GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 5.249   49.142  26.263  1.00 47.74  ? 24  GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 4.715   48.435  28.280  1.00 49.41  ? 24  GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 5.603   43.620  24.149  1.00 39.26  ? 25  SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 5.815   42.637  23.081  1.00 37.56  ? 25  SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 5.564   43.182  21.674  1.00 37.69  ? 25  SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 6.114   42.653  20.707  1.00 36.17  ? 25  SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 4.919   41.423  23.312  1.00 38.21  ? 25  SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 3.556   41.821  23.369  1.00 40.74  ? 25  SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 4.729   44.218  21.559  1.00 39.70  ? 26  ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 4.504   44.895  20.275  1.00 40.18  ? 26  ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 5.217   46.251  20.155  1.00 40.26  ? 26  ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 4.883   47.050  19.287  1.00 41.32  ? 26  ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 2.993   45.000  19.968  1.00 42.70  ? 26  ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 2.263   45.982  20.868  1.00 45.18  ? 26  ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 2.627   46.178  22.028  1.00 45.12  ? 26  ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 1.213   46.596  20.332  1.00 47.58  ? 26  ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 6.213   46.484  21.011  1.00 39.35  ? 27  GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 6.990   47.731  21.029  1.00 39.61  ? 27  GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 8.440   47.500  20.613  1.00 37.26  ? 27  GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 8.844   46.357  20.371  1.00 35.44  ? 27  GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 9.234   48.584  20.527  1.00 37.51  ? 28  PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 10.624  48.455  20.074  1.00 35.62  ? 28  PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 11.542  47.782  21.090  1.00 34.46  ? 28  PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 11.226  47.709  22.283  1.00 35.28  ? 28  PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 11.058  49.905  19.824  1.00 36.75  ? 28  PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 10.142  50.738  20.647  1.00 39.21  ? 28  PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 8.852   49.987  20.775  1.00 39.82  ? 28  PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 12.667  47.281  20.590  1.00 32.77  ? 29  VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 13.723  46.723  21.420  1.00 31.82  ? 29  VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 14.830  47.763  21.565  1.00 32.25  ? 29  VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 15.365  48.241  20.563  1.00 31.88  ? 29  VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 14.318  45.451  20.800  1.00 29.90  ? 29  VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 15.382  44.853  21.718  1.00 29.12  ? 29  VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 13.215  44.430  20.524  1.00 29.83  ? 29  VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 15.171  48.098  22.807  1.00 33.22  ? 30  LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 16.378  48.884  23.090  1.00 33.70  ? 30  LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 17.569  47.944  23.158  1.00 32.12  ? 30  LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 17.500  46.910  23.810  1.00 31.45  ? 30  LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 16.251  49.642  24.405  1.00 35.72  ? 30  LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 15.185  50.709  24.361  1.00 37.81  ? 30  LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 15.071  51.449  25.684  0.75 40.07  ? 30  LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 13.854  52.350  25.688  0.75 42.33  ? 30  LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 13.883  53.342  24.577  0.75 42.93  ? 30  LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 18.647  48.321  22.478  1.00 31.76  ? 31  VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 19.896  47.567  22.431  1.00 30.63  ? 31  VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 21.017  48.508  22.866  1.00 31.82  ? 31  VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 21.183  49.582  22.274  1.00 32.66  ? 31  VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 20.192  47.075  20.997  1.00 29.26  ? 31  VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 21.406  46.144  20.976  1.00 28.24  ? 31  VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 18.964  46.398  20.398  1.00 28.65  ? 31  VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 21.777  48.128  23.893  1.00 32.19  ? 32  TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 22.865  48.979  24.374  1.00 33.64  ? 32  TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 23.979  48.215  25.079  1.00 33.50  ? 32  TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 23.768  47.135  25.624  1.00 32.73  ? 32  TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 22.329  50.081  25.299  1.00 35.84  ? 32  TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 22.102  49.641  26.719  1.00 36.67  ? 32  TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 22.937  49.835  27.783  1.00 38.10  ? 32  TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 20.974  48.918  27.220  1.00 36.34  ? 32  TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 22.397  49.281  28.916  1.00 38.63  ? 32  TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 21.190  48.713  28.601  1.00 37.51  ? 32  TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 19.798  48.422  26.634  1.00 35.38  ? 32  TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 20.269  48.043  29.417  1.00 37.67  ? 32  TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 18.877  47.742  27.444  1.00 35.58  ? 32  TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 19.121  47.565  28.825  1.00 36.70  ? 32  TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 25.156  48.822  25.099  1.00 34.54  ? 33  GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 26.315  48.247  25.772  1.00 34.91  ? 33  GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 27.599  48.791  25.194  1.00 35.62  ? 33  GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 27.616  49.890  24.658  1.00 36.47  ? 33  GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 28.661  48.000  25.286  1.00 35.49  ? 34  SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 29.999  48.423  24.886  1.00 36.56  ? 34  SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 30.803  47.270  24.285  1.00 35.47  ? 34  SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 30.686  46.130  24.727  1.00 34.68  ? 34  SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 30.737  48.981  26.092  1.00 38.91  ? 34  SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 31.793  49.806  25.663  1.00 40.50  ? 34  SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 31.609  47.585  23.274  1.00 35.65  ? 35  ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 32.508  46.621  22.633  1.00 35.10  ? 35  ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 33.864  47.295  22.548  1.00 37.01  ? 35  ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 33.948  48.426  22.079  1.00 37.86  ? 35  ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 32.040  46.237  21.208  1.00 33.42  ? 35  ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 30.566  45.802  21.217  1.00 31.78  ? 35  ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 32.923  45.133  20.628  1.00 33.10  ? 35  ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 29.982  45.588  19.838  1.00 30.46  ? 35  ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 34.909  46.612  23.012  1.00 37.92  ? 36  LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 36.282  47.151  22.978  1.00 40.12  ? 36  LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 37.159  46.303  22.064  1.00 39.86  ? 36  LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 36.734  45.244  21.596  1.00 38.06  ? 36  LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 36.879  47.251  24.388  1.00 42.23  ? 36  LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 37.074  45.938  25.129  1.00 42.00  ? 36  LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? 37.481  46.204  26.569  1.00 44.26  ? 36  LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? 37.580  44.914  27.363  1.00 44.13  ? 36  LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? 37.783  45.168  28.816  1.00 46.26  ? 36  LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 38.373  46.785  21.808  1.00 41.84  ? 37  GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? 39.341  46.087  20.961  1.00 42.20  ? 37  GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 39.192  46.263  19.458  1.00 41.21  ? 37  GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? 39.891  45.600  18.694  1.00 41.53  ? 37  GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 38.304  47.161  19.026  1.00 40.27  ? 38  LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 38.008  47.360  17.603  1.00 39.30  ? 38  LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 38.894  48.431  16.996  1.00 41.28  ? 38  LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 39.369  49.324  17.698  1.00 43.07  ? 38  LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 36.558  47.818  17.425  1.00 37.57  ? 38  LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 35.487  46.802  17.798  1.00 35.52  ? 38  LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 34.156  47.499  18.028  1.00 34.64  ? 38  LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 35.373  45.743  16.711  1.00 34.24  ? 38  LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 39.073  48.364  15.678  1.00 41.04  ? 39  THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 39.691  49.459  14.945  1.00 42.80  ? 39  THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 38.723  50.630  14.922  1.00 42.44  ? 39  THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 37.510  50.432  14.908  1.00 40.48  ? 39  THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 40.054  49.072  13.498  1.00 42.75  ? 39  THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 38.882  48.634  12.799  1.00 40.50  ? 39  THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? 41.109  47.974  13.480  1.00 43.63  ? 39  THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 39.259  51.844  14.937  1.00 44.60  ? 40  GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 38.454  53.062  14.832  1.00 44.83  ? 40  GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 37.596  53.042  13.555  1.00 43.23  ? 40  GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 38.067  52.642  12.491  1.00 43.16  ? 40  GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 39.366  54.296  14.840  1.00 47.83  ? 40  GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 38.625  55.628  14.843  1.00 48.61  ? 40  GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 39.541  56.828  14.977  1.00 51.88  ? 40  GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 40.783  56.671  14.898  1.00 53.62  ? 40  GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? 39.009  57.944  15.159  1.00 52.99  ? 40  GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 36.332  53.448  13.685  1.00 42.14  ? 41  GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 35.395  53.507  12.557  1.00 40.87  ? 41  GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 34.226  52.537  12.669  1.00 38.45  ? 41  GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 33.864  52.097  13.765  1.00 37.76  ? 41  GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 33.647  52.201  11.518  1.00 37.38  ? 42  LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 32.380  51.475  11.446  1.00 35.38  ? 42  LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 32.594  49.968  11.393  1.00 34.02  ? 42  LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 33.527  49.483  10.744  1.00 34.54  ? 42  LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 31.572  51.929  10.227  1.00 35.26  ? 42  LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 31.111  53.389  10.219  1.00 36.65  ? 42  LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 30.465  53.748  8.891   1.00 36.73  ? 42  LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 30.139  53.658  11.354  1.00 36.33  ? 42  LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 31.720  49.244  12.090  1.00 32.48  ? 43  HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 31.746  47.793  12.135  1.00 31.24  ? 43  HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 30.329  47.241  12.029  1.00 29.69  ? 43  HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 29.452  47.642  12.791  1.00 29.34  ? 43  HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 32.390  47.335  13.440  1.00 31.51  ? 43  HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 33.831  47.708  13.553  1.00 33.22  ? 43  HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 34.842  46.894  13.100  1.00 33.70  ? 43  HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 34.429  48.829  14.026  1.00 34.90  ? 43  HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 36.006  47.485  13.311  1.00 35.57  ? 43  HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 35.783  48.661  13.871  1.00 36.29  ? 43  HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 30.123  46.324  11.084  1.00 28.96  ? 44  GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 28.857  45.632  10.920  1.00 27.74  ? 44  GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 28.400  44.947  12.189  1.00 26.91  ? 44  GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 29.215  44.445  12.963  1.00 27.03  ? 44  GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 27.087  44.918  12.391  1.00 26.25  ? 45  PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 26.507  44.516  13.663  1.00 25.72  ? 45  PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 25.198  43.802  13.337  1.00 24.87  ? 45  PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 24.225  44.452  12.982  1.00 25.02  ? 45  PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 26.312  45.778  14.516  1.00 26.55  ? 45  PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 25.940  45.520  15.953  1.00 26.50  ? 45  PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 26.813  44.862  16.809  1.00 26.61  ? 45  PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 24.743  45.996  16.467  1.00 26.68  ? 45  PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 26.487  44.659  18.140  1.00 26.70  ? 45  PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 24.405  45.788  17.799  1.00 26.81  ? 45  PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 25.281  45.122  18.634  1.00 26.80  ? 45  PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 25.197  42.470  13.392  1.00 24.18  ? 46  HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 24.093  41.683  12.851  1.00 23.72  ? 46  HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 23.659  40.572  13.788  1.00 23.15  ? 46  HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 24.476  40.001  14.512  1.00 23.12  ? 46  HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 24.456  41.046  11.498  1.00 23.91  ? 46  HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 25.097  41.988  10.531  1.00 24.62  ? 46  HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 26.320  41.737  9.952   1.00 25.14  ? 46  HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 24.694  43.189  10.056  1.00 25.13  ? 46  HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 26.638  42.737  9.151   1.00 25.86  ? 46  HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 25.669  43.635  9.198   1.00 25.86  ? 46  HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 22.370  40.258  13.751  1.00 22.85  ? 47  VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 21.883  39.030  14.341  1.00 22.51  ? 47  VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 21.898  37.963  13.248  1.00 22.57  ? 47  VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 21.257  38.126  12.207  1.00 22.74  ? 47  VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 20.471  39.195  14.940  1.00 22.57  ? 47  VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 19.975  37.876  15.519  1.00 22.40  ? 47  VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 20.477  40.295  15.995  1.00 22.80  ? 47  VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 22.643  36.884  13.482  1.00 22.58  ? 48  HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 22.693  35.752  12.551  1.00 23.02  ? 48  HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 21.710  34.680  12.998  1.00 23.21  ? 48  HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 21.285  34.667  14.153  1.00 22.91  ? 48  HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 24.121  35.208  12.430  1.00 23.34  ? 48  HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 25.059  36.140  11.723  1.00 23.56  ? 48  HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 25.712  35.800  10.557  1.00 24.27  ? 48  HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 25.447  37.403  12.013  1.00 23.42  ? 48  HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 26.466  36.810  10.164  1.00 24.48  ? 48  HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 26.322  37.796  11.029  1.00 23.99  ? 48  HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 21.346  33.792  12.081  1.00 23.98  ? 49  GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 20.198  32.899  12.266  1.00 24.56  ? 49  GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 20.324  31.909  13.433  1.00 24.62  ? 49  GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 19.373  31.722  14.191  1.00 24.54  ? 49  GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 19.908  32.122  10.977  1.00 25.65  ? 49  GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 18.579  31.376  10.991  1.00 26.48  ? 49  GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 18.325  30.574  9.732   1.00 27.89  ? 49  GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 19.073  30.717  8.740   1.00 28.42  ? 49  GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 17.364  29.784  9.736   1.00 28.99  ? 49  GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 21.491  31.289  13.576  1.00 24.92  ? 50  PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 21.669  30.202  14.532  1.00 25.35  ? 50  PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 22.487  30.617  15.750  1.00 25.00  ? 50  PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 23.438  31.401  15.629  1.00 24.88  ? 50  PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 22.328  29.023  13.815  1.00 26.43  ? 50  PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 21.562  28.568  12.602  1.00 27.27  ? 50  PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 20.269  28.067  12.735  1.00 27.70  ? 50  PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 22.115  28.652  11.332  1.00 27.90  ? 50  PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 19.545  27.657  11.623  1.00 28.75  ? 50  PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 21.395  28.242  10.217  1.00 28.88  ? 50  PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 20.109  27.745  10.365  1.00 29.33  ? 50  PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 22.117  30.082  16.915  1.00 25.07  ? 51  GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 22.881  30.241  18.150  1.00 25.07  ? 51  GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 23.875  29.099  18.330  1.00 26.00  ? 51  GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 23.962  28.504  19.406  1.00 26.35  ? 51  GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 24.616  28.813  17.259  1.00 26.59  ? 52  ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 25.518  27.692  17.170  1.00 27.90  ? 52  ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 26.943  28.276  17.080  1.00 28.38  ? 52  ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 27.318  28.848  16.054  1.00 28.19  ? 52  ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 25.175  26.844  15.940  1.00 28.61  ? 52  ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 26.014  25.582  15.843  1.00 30.18  ? 52  ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 27.121  25.564  16.427  1.00 30.63  ? 52  ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 25.571  24.603  15.197  1.00 31.14  ? 52  ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 27.700  28.134  18.167  1.00 29.16  ? 53  ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 29.099  28.592  18.249  1.00 30.12  ? 53  ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 30.073  27.398  18.297  1.00 31.78  ? 53  ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 31.170  27.497  18.862  1.00 32.83  ? 53  ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 29.269  29.501  19.480  1.00 29.99  ? 53  ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 30.501  30.400  19.398  1.00 30.79  ? 53  ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 30.591  31.302  18.547  1.00 30.90  ? 53  ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 31.434  30.187  20.301  1.00 31.90  ? 53  ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 29.686  26.274  17.693  1.00 32.46  ? 54  THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 30.520  25.067  17.695  1.00 34.40  ? 54  THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 31.777  25.219  16.829  1.00 35.70  ? 54  THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 32.816  24.644  17.139  1.00 37.39  ? 54  THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 29.734  23.827  17.237  1.00 34.98  ? 54  THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 29.146  24.080  15.958  1.00 34.47  ? 54  THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 28.649  23.482  18.256  1.00 34.32  ? 54  THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 31.673  25.988  15.750  1.00 35.30  ? 55  ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 32.840  26.363  14.936  1.00 36.55  ? 55  ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 33.035  27.876  15.007  1.00 35.53  ? 55  ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 33.214  28.541  13.981  1.00 35.62  ? 55  ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 32.651  25.897  13.495  1.00 37.27  ? 55  ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 33.000  28.417  16.224  1.00 34.90  ? 56  GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 33.099  29.857  16.424  1.00 34.04  ? 56  GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 31.911  30.585  15.827  1.00 32.52  ? 56  GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 30.802  30.041  15.779  1.00 31.90  ? 56  GLY A O   1 
ATOM   415   N  N   . ALA A  1 57  ? 32.147  31.813  15.368  1.00 32.16  ? 57  ALA A N   1 
ATOM   416   C  CA  . ALA A  1 57  ? 31.107  32.648  14.769  1.00 30.91  ? 57  ALA A CA  1 
ATOM   417   C  C   . ALA A  1 57  ? 30.625  32.144  13.394  1.00 31.07  ? 57  ALA A C   1 
ATOM   418   O  O   . ALA A  1 57  ? 29.522  32.510  12.960  1.00 30.14  ? 57  ALA A O   1 
ATOM   419   C  CB  . ALA A  1 57  ? 31.603  34.082  14.648  1.00 30.87  ? 57  ALA A CB  1 
ATOM   420   N  N   . THR A  1 58  ? 31.451  31.333  12.718  1.00 32.32  ? 58  THR A N   1 
ATOM   421   C  CA  . THR A  1 58  ? 31.138  30.795  11.384  1.00 32.88  ? 58  THR A CA  1 
ATOM   422   C  C   . THR A  1 58  ? 29.871  29.946  11.366  1.00 32.29  ? 58  THR A C   1 
ATOM   423   O  O   . THR A  1 58  ? 29.077  30.050  10.424  1.00 32.31  ? 58  THR A O   1 
ATOM   424   C  CB  . THR A  1 58  ? 32.309  29.943  10.841  1.00 34.96  ? 58  THR A CB  1 
ATOM   425   O  OG1 . THR A  1 58  ? 33.505  30.727  10.851  1.00 35.77  ? 58  THR A OG1 1 
ATOM   426   C  CG2 . THR A  1 58  ? 32.047  29.472  9.413   1.00 35.89  ? 58  THR A CG2 1 
ATOM   427   N  N   . SER A  1 59  ? 29.660  29.147  12.415  1.00 31.95  ? 59  SER A N   1 
ATOM   428   C  CA  . SER A  1 59  ? 28.492  28.241  12.490  1.00 31.61  ? 59  SER A CA  1 
ATOM   429   C  C   . SER A  1 59  ? 27.140  28.932  12.789  1.00 29.90  ? 59  SER A C   1 
ATOM   430   O  O   . SER A  1 59  ? 26.099  28.272  12.806  1.00 29.87  ? 59  SER A O   1 
ATOM   431   C  CB  . SER A  1 59  ? 28.756  27.118  13.507  1.00 32.36  ? 59  SER A CB  1 
ATOM   432   O  OG  . SER A  1 59  ? 29.318  27.626  14.703  1.00 32.00  ? 59  SER A OG  1 
ATOM   433   N  N   . ALA A  1 60  ? 27.164  30.246  13.017  1.00 28.59  ? 60  ALA A N   1 
ATOM   434   C  CA  . ALA A  1 60  ? 25.956  31.036  13.215  1.00 27.31  ? 60  ALA A CA  1 
ATOM   435   C  C   . ALA A  1 60  ? 25.099  31.180  11.947  1.00 27.23  ? 60  ALA A C   1 
ATOM   436   O  O   . ALA A  1 60  ? 23.953  31.622  12.027  1.00 26.63  ? 60  ALA A O   1 
ATOM   437   C  CB  . ALA A  1 60  ? 26.328  32.410  13.747  1.00 26.58  ? 60  ALA A CB  1 
ATOM   438   N  N   . GLY A  1 61  ? 25.659  30.846  10.784  1.00 27.97  ? 61  GLY A N   1 
ATOM   439   C  CA  . GLY A  1 61  ? 24.920  30.890  9.543   1.00 28.26  ? 61  GLY A CA  1 
ATOM   440   C  C   . GLY A  1 61  ? 24.695  32.317  9.074   1.00 27.51  ? 61  GLY A C   1 
ATOM   441   O  O   . GLY A  1 61  ? 25.411  33.245  9.500   1.00 27.00  ? 61  GLY A O   1 
ATOM   442   N  N   . PRO A  1 62  ? 23.701  32.511  8.194   1.00 27.58  ? 62  PRO A N   1 
ATOM   443   C  CA  . PRO A  1 62  ? 23.518  33.818  7.565   1.00 27.22  ? 62  PRO A CA  1 
ATOM   444   C  C   . PRO A  1 62  ? 22.790  34.798  8.477   1.00 26.01  ? 62  PRO A C   1 
ATOM   445   O  O   . PRO A  1 62  ? 22.499  34.467  9.625   1.00 25.39  ? 62  PRO A O   1 
ATOM   446   C  CB  . PRO A  1 62  ? 22.700  33.485  6.316   1.00 28.27  ? 62  PRO A CB  1 
ATOM   447   C  CG  . PRO A  1 62  ? 21.911  32.273  6.696   1.00 28.64  ? 62  PRO A CG  1 
ATOM   448   C  CD  . PRO A  1 62  ? 22.696  31.529  7.733   1.00 28.36  ? 62  PRO A CD  1 
ATOM   449   N  N   . HIS A  1 63  ? 22.507  35.996  7.974   1.00 25.78  ? 63  HIS A N   1 
ATOM   450   C  CA  . HIS A  1 63  ? 21.716  36.969  8.741   1.00 25.07  ? 63  HIS A CA  1 
ATOM   451   C  C   . HIS A  1 63  ? 20.315  36.434  9.008   1.00 25.05  ? 63  HIS A C   1 
ATOM   452   O  O   . HIS A  1 63  ? 19.739  35.743  8.161   1.00 25.72  ? 63  HIS A O   1 
ATOM   453   C  CB  . HIS A  1 63  ? 21.617  38.299  8.019   1.00 25.35  ? 63  HIS A CB  1 
ATOM   454   C  CG  . HIS A  1 63  ? 22.930  38.993  7.867   1.00 25.42  ? 63  HIS A CG  1 
ATOM   455   N  ND1 . HIS A  1 63  ? 23.060  40.199  7.225   1.00 25.86  ? 63  HIS A ND1 1 
ATOM   456   C  CD2 . HIS A  1 63  ? 24.174  38.646  8.272   1.00 25.34  ? 63  HIS A CD2 1 
ATOM   457   C  CE1 . HIS A  1 63  ? 24.327  40.574  7.244   1.00 25.99  ? 63  HIS A CE1 1 
ATOM   458   N  NE2 . HIS A  1 63  ? 25.024  39.645  7.869   1.00 25.73  ? 63  HIS A NE2 1 
ATOM   459   N  N   . PHE A  1 64  ? 19.799  36.713  10.200  1.00 24.43  ? 64  PHE A N   1 
ATOM   460   C  CA  . PHE A  1 64  ? 18.462  36.260  10.568  1.00 24.72  ? 64  PHE A CA  1 
ATOM   461   C  C   . PHE A  1 64  ? 17.464  36.909  9.611   1.00 25.53  ? 64  PHE A C   1 
ATOM   462   O  O   . PHE A  1 64  ? 17.357  38.138  9.564   1.00 25.50  ? 64  PHE A O   1 
ATOM   463   C  CB  . PHE A  1 64  ? 18.161  36.591  12.034  1.00 24.14  ? 64  PHE A CB  1 
ATOM   464   C  CG  . PHE A  1 64  ? 16.780  36.188  12.491  1.00 24.55  ? 64  PHE A CG  1 
ATOM   465   C  CD1 . PHE A  1 64  ? 16.234  34.946  12.150  1.00 25.13  ? 64  PHE A CD1 1 
ATOM   466   C  CD2 . PHE A  1 64  ? 16.036  37.040  13.294  1.00 24.60  ? 64  PHE A CD2 1 
ATOM   467   C  CE1 . PHE A  1 64  ? 14.967  34.585  12.581  1.00 25.79  ? 64  PHE A CE1 1 
ATOM   468   C  CE2 . PHE A  1 64  ? 14.774  36.678  13.737  1.00 25.30  ? 64  PHE A CE2 1 
ATOM   469   C  CZ  . PHE A  1 64  ? 14.234  35.452  13.376  1.00 25.85  ? 64  PHE A CZ  1 
ATOM   470   N  N   . ASN A  1 65  ? 16.775  36.075  8.831   1.00 26.53  ? 65  ASN A N   1 
ATOM   471   C  CA  . ASN A  1 65  ? 15.993  36.538  7.676   1.00 27.68  ? 65  ASN A CA  1 
ATOM   472   C  C   . ASN A  1 65  ? 14.707  35.717  7.442   1.00 28.91  ? 65  ASN A C   1 
ATOM   473   O  O   . ASN A  1 65  ? 14.551  35.061  6.401   1.00 30.01  ? 65  ASN A O   1 
ATOM   474   C  CB  . ASN A  1 65  ? 16.906  36.503  6.437   1.00 28.06  ? 65  ASN A CB  1 
ATOM   475   C  CG  . ASN A  1 65  ? 16.267  37.117  5.212   1.00 29.23  ? 65  ASN A CG  1 
ATOM   476   O  OD1 . ASN A  1 65  ? 15.373  37.969  5.309   1.00 29.58  ? 65  ASN A OD1 1 
ATOM   477   N  ND2 . ASN A  1 65  ? 16.734  36.697  4.040   1.00 30.03  ? 65  ASN A ND2 1 
ATOM   478   N  N   . PRO A  1 66  ? 13.767  35.761  8.402   1.00 29.04  ? 66  PRO A N   1 
ATOM   479   C  CA  . PRO A  1 66  ? 12.536  34.955  8.305   1.00 30.39  ? 66  PRO A CA  1 
ATOM   480   C  C   . PRO A  1 66  ? 11.517  35.405  7.236   1.00 32.10  ? 66  PRO A C   1 
ATOM   481   O  O   . PRO A  1 66  ? 10.631  34.628  6.879   1.00 33.47  ? 66  PRO A O   1 
ATOM   482   C  CB  . PRO A  1 66  ? 11.941  35.070  9.712   1.00 30.03  ? 66  PRO A CB  1 
ATOM   483   C  CG  . PRO A  1 66  ? 12.405  36.403  10.198  1.00 29.09  ? 66  PRO A CG  1 
ATOM   484   C  CD  . PRO A  1 66  ? 13.794  36.571  9.636   1.00 28.19  ? 66  PRO A CD  1 
ATOM   485   N  N   . LEU A  1 67  ? 11.636  36.637  6.740   1.00 32.21  ? 67  LEU A N   1 
ATOM   486   C  CA  . LEU A  1 67  ? 10.785  37.139  5.658   1.00 33.99  ? 67  LEU A CA  1 
ATOM   487   C  C   . LEU A  1 67  ? 11.428  37.009  4.267   1.00 34.58  ? 67  LEU A C   1 
ATOM   488   O  O   . LEU A  1 67  ? 10.837  37.452  3.282   1.00 36.02  ? 67  LEU A O   1 
ATOM   489   C  CB  . LEU A  1 67  ? 10.415  38.599  5.926   1.00 34.15  ? 67  LEU A CB  1 
ATOM   490   C  CG  . LEU A  1 67  ? 9.727   38.875  7.267   1.00 34.07  ? 67  LEU A CG  1 
ATOM   491   C  CD1 . LEU A  1 67  ? 9.480   40.364  7.441   1.00 34.48  ? 67  LEU A CD1 1 
ATOM   492   C  CD2 . LEU A  1 67  ? 8.417   38.101  7.368   1.00 35.69  ? 67  LEU A CD2 1 
ATOM   493   N  N   . SER A  1 68  ? 12.619  36.401  4.185   1.00 33.65  ? 68  SER A N   1 
ATOM   494   C  CA  . SER A  1 68  ? 13.314  36.172  2.911   1.00 34.43  ? 68  SER A CA  1 
ATOM   495   C  C   . SER A  1 68  ? 13.513  37.461  2.099   1.00 34.88  ? 68  SER A C   1 
ATOM   496   O  O   . SER A  1 68  ? 13.214  37.519  0.904   1.00 36.34  ? 68  SER A O   1 
ATOM   497   C  CB  . SER A  1 68  ? 12.576  35.114  2.081   1.00 36.35  ? 68  SER A CB  1 
ATOM   498   O  OG  . SER A  1 68  ? 12.388  33.947  2.843   1.00 36.21  ? 68  SER A OG  1 
ATOM   499   N  N   . ARG A  1 69  ? 14.008  38.490  2.776   1.00 33.80  ? 69  ARG A N   1 
ATOM   500   C  CA  . ARG A  1 69  ? 14.317  39.768  2.154   1.00 34.29  ? 69  ARG A CA  1 
ATOM   501   C  C   . ARG A  1 69  ? 15.804  39.816  1.787   1.00 33.50  ? 69  ARG A C   1 
ATOM   502   O  O   . ARG A  1 69  ? 16.576  38.898  2.102   1.00 32.65  ? 69  ARG A O   1 
ATOM   503   C  CB  . ARG A  1 69  ? 13.996  40.912  3.119   1.00 33.98  ? 69  ARG A CB  1 
ATOM   504   C  CG  . ARG A  1 69  ? 12.560  40.963  3.623   1.00 35.12  ? 69  ARG A CG  1 
ATOM   505   C  CD  . ARG A  1 69  ? 11.673  41.703  2.657   1.00 37.24  ? 69  ARG A CD  1 
ATOM   506   N  NE  . ARG A  1 69  ? 10.257  41.644  3.007   1.00 38.80  ? 69  ARG A NE  1 
ATOM   507   C  CZ  . ARG A  1 69  ? 9.628   42.409  3.909   1.00 39.13  ? 69  ARG A CZ  1 
ATOM   508   N  NH1 . ARG A  1 69  ? 10.276  43.324  4.637   1.00 38.15  ? 69  ARG A NH1 1 
ATOM   509   N  NH2 . ARG A  1 69  ? 8.319   42.236  4.099   1.00 40.67  ? 69  ARG A NH2 1 
ATOM   510   N  N   . LYS A  1 70  ? 16.181  40.897  1.112   1.00 33.88  ? 70  LYS A N   1 
ATOM   511   C  CA  . LYS A  1 70  ? 17.577  41.206  0.813   1.00 33.35  ? 70  LYS A CA  1 
ATOM   512   C  C   . LYS A  1 70  ? 18.161  42.053  1.911   1.00 32.01  ? 70  LYS A C   1 
ATOM   513   O  O   . LYS A  1 70  ? 17.426  42.713  2.655   1.00 31.77  ? 70  LYS A O   1 
ATOM   514   C  CB  . LYS A  1 70  ? 17.696  41.948  -0.532  1.00 34.86  ? 70  LYS A CB  1 
ATOM   515   C  CG  . LYS A  1 70  ? 17.235  41.130  -1.730  1.00 36.52  ? 70  LYS A CG  1 
ATOM   516   C  CD  . LYS A  1 70  ? 18.104  39.897  -1.918  1.00 36.45  ? 70  LYS A CD  1 
ATOM   517   C  CE  . LYS A  1 70  ? 17.690  39.078  -3.129  1.00 38.43  ? 70  LYS A CE  1 
ATOM   518   N  NZ  . LYS A  1 70  ? 18.210  37.683  -3.006  1.00 38.38  ? 70  LYS A NZ  1 
ATOM   519   N  N   . HIS A  1 71  ? 19.493  42.034  2.003   1.00 31.27  ? 71  HIS A N   1 
ATOM   520   C  CA  . HIS A  1 71  ? 20.209  42.785  3.023   1.00 30.22  ? 71  HIS A CA  1 
ATOM   521   C  C   . HIS A  1 71  ? 20.001  44.281  2.826   1.00 30.91  ? 71  HIS A C   1 
ATOM   522   O  O   . HIS A  1 71  ? 19.896  44.756  1.700   1.00 32.17  ? 71  HIS A O   1 
ATOM   523   C  CB  . HIS A  1 71  ? 21.709  42.468  2.972   1.00 29.81  ? 71  HIS A CB  1 
ATOM   524   C  CG  . HIS A  1 71  ? 22.515  43.176  4.008   1.00 29.03  ? 71  HIS A CG  1 
ATOM   525   N  ND1 . HIS A  1 71  ? 22.477  42.840  5.345   1.00 27.97  ? 71  HIS A ND1 1 
ATOM   526   C  CD2 . HIS A  1 71  ? 23.384  44.208  3.902   1.00 29.37  ? 71  HIS A CD2 1 
ATOM   527   C  CE1 . HIS A  1 71  ? 23.289  43.638  6.016   1.00 27.79  ? 71  HIS A CE1 1 
ATOM   528   N  NE2 . HIS A  1 71  ? 23.853  44.473  5.164   1.00 28.62  ? 71  HIS A NE2 1 
ATOM   529   N  N   . GLY A  1 72  ? 19.948  45.012  3.932   1.00 30.40  ? 72  GLY A N   1 
ATOM   530   C  CA  . GLY A  1 72  ? 19.961  46.468  3.900   1.00 31.18  ? 72  GLY A CA  1 
ATOM   531   C  C   . GLY A  1 72  ? 20.401  47.033  5.234   1.00 30.58  ? 72  GLY A C   1 
ATOM   532   O  O   . GLY A  1 72  ? 20.909  46.301  6.088   1.00 29.54  ? 72  GLY A O   1 
ATOM   533   N  N   . GLY A  1 73  ? 20.224  48.340  5.399   1.00 31.51  ? 73  GLY A N   1 
ATOM   534   C  CA  . GLY A  1 73  ? 20.446  49.001  6.678   1.00 31.42  ? 73  GLY A CA  1 
ATOM   535   C  C   . GLY A  1 73  ? 19.198  48.950  7.549   1.00 31.51  ? 73  GLY A C   1 
ATOM   536   O  O   . GLY A  1 73  ? 18.094  48.689  7.051   1.00 31.92  ? 73  GLY A O   1 
ATOM   537   N  N   . PRO A  1 74  ? 19.348  49.227  8.854   1.00 31.34  ? 74  PRO A N   1 
ATOM   538   C  CA  . PRO A  1 74  ? 18.209  49.117  9.789   1.00 31.51  ? 74  PRO A CA  1 
ATOM   539   C  C   . PRO A  1 74  ? 16.997  50.015  9.466   1.00 33.16  ? 74  PRO A C   1 
ATOM   540   O  O   . PRO A  1 74  ? 15.859  49.647  9.780   1.00 33.37  ? 74  PRO A O   1 
ATOM   541   C  CB  . PRO A  1 74  ? 18.829  49.477  11.148  1.00 31.33  ? 74  PRO A CB  1 
ATOM   542   C  CG  . PRO A  1 74  ? 20.086  50.217  10.833  1.00 31.68  ? 74  PRO A CG  1 
ATOM   543   C  CD  . PRO A  1 74  ? 20.581  49.647  9.539   1.00 31.21  ? 74  PRO A CD  1 
ATOM   544   N  N   . LYS A  1 75  ? 17.238  51.151  8.818   1.00 34.48  ? 75  LYS A N   1 
ATOM   545   C  CA  . LYS A  1 75  ? 16.167  52.069  8.416   1.00 36.41  ? 75  LYS A CA  1 
ATOM   546   C  C   . LYS A  1 75  ? 15.463  51.703  7.098   1.00 36.93  ? 75  LYS A C   1 
ATOM   547   O  O   . LYS A  1 75  ? 14.480  52.344  6.746   1.00 38.49  ? 75  LYS A O   1 
ATOM   548   C  CB  . LYS A  1 75  ? 16.711  53.502  8.333   1.00 37.90  ? 75  LYS A CB  1 
ATOM   549   C  CG  . LYS A  1 75  ? 17.318  53.999  9.639   1.00 38.02  ? 75  LYS A CG  1 
ATOM   550   C  CD  . LYS A  1 75  ? 17.760  55.455  9.554   1.00 39.93  ? 75  LYS A CD  1 
ATOM   551   C  CE  . LYS A  1 75  ? 19.046  55.619  8.759   1.00 39.72  ? 75  LYS A CE  1 
ATOM   552   N  NZ  . LYS A  1 75  ? 19.553  57.021  8.797   1.00 41.66  ? 75  LYS A NZ  1 
ATOM   553   N  N   . ASP A  1 76  ? 15.948  50.679  6.386   1.00 35.88  ? 76  ASP A N   1 
ATOM   554   C  CA  . ASP A  1 76  ? 15.398  50.304  5.070   1.00 36.61  ? 76  ASP A CA  1 
ATOM   555   C  C   . ASP A  1 76  ? 14.208  49.353  5.189   1.00 36.64  ? 76  ASP A C   1 
ATOM   556   O  O   . ASP A  1 76  ? 14.163  48.499  6.079   1.00 35.49  ? 76  ASP A O   1 
ATOM   557   C  CB  . ASP A  1 76  ? 16.470  49.625  4.196   1.00 35.84  ? 76  ASP A CB  1 
ATOM   558   C  CG  . ASP A  1 76  ? 17.608  50.561  3.815   1.00 36.24  ? 76  ASP A CG  1 
ATOM   559   O  OD1 . ASP A  1 76  ? 17.340  51.717  3.470   1.00 37.73  ? 76  ASP A OD1 1 
ATOM   560   O  OD2 . ASP A  1 76  ? 18.780  50.132  3.848   1.00 35.39  ? 76  ASP A OD2 1 
ATOM   561   N  N   . GLU A  1 77  ? 13.256  49.502  4.272   1.00 38.15  ? 77  GLU A N   1 
ATOM   562   C  CA  . GLU A  1 77  ? 12.120  48.590  4.182   1.00 38.53  ? 77  GLU A CA  1 
ATOM   563   C  C   . GLU A  1 77  ? 12.609  47.208  3.751   1.00 37.14  ? 77  GLU A C   1 
ATOM   564   O  O   . GLU A  1 77  ? 12.202  46.189  4.326   1.00 36.56  ? 77  GLU A O   1 
ATOM   565   C  CB  . GLU A  1 77  ? 11.075  49.128  3.193   1.00 40.88  ? 77  GLU A CB  1 
ATOM   566   C  CG  . GLU A  1 77  ? 9.763   48.355  3.179   1.00 41.97  ? 77  GLU A CG  1 
ATOM   567   C  CD  . GLU A  1 77  ? 9.013   48.454  4.492   0.50 42.12  ? 77  GLU A CD  1 
ATOM   568   O  OE1 . GLU A  1 77  ? 8.223   49.410  4.657   0.50 43.95  ? 77  GLU A OE1 1 
ATOM   569   O  OE2 . GLU A  1 77  ? 9.213   47.573  5.354   0.50 40.63  ? 77  GLU A OE2 1 
ATOM   570   N  N   . GLU A  1 78  ? 13.482  47.185  2.744   1.00 36.85  ? 78  GLU A N   1 
ATOM   571   C  CA  . GLU A  1 78  ? 14.146  45.958  2.319   1.00 35.76  ? 78  GLU A CA  1 
ATOM   572   C  C   . GLU A  1 78  ? 15.368  45.711  3.212   1.00 33.64  ? 78  GLU A C   1 
ATOM   573   O  O   . GLU A  1 78  ? 16.446  46.286  3.004   1.00 33.31  ? 78  GLU A O   1 
ATOM   574   C  CB  . GLU A  1 78  ? 14.535  46.031  0.832   1.00 36.95  ? 78  GLU A CB  1 
ATOM   575   C  CG  . GLU A  1 78  ? 14.942  44.696  0.219   1.00 36.78  ? 78  GLU A CG  1 
ATOM   576   C  CD  . GLU A  1 78  ? 13.796  43.694  0.105   1.00 37.72  ? 78  GLU A CD  1 
ATOM   577   O  OE1 . GLU A  1 78  ? 12.604  44.099  0.148   1.00 39.15  ? 78  GLU A OE1 1 
ATOM   578   O  OE2 . GLU A  1 78  ? 14.085  42.488  -0.050  1.00 37.41  ? 78  GLU A OE2 1 
ATOM   579   N  N   . ARG A  1 79  ? 15.165  44.871  4.224   1.00 32.29  ? 79  ARG A N   1 
ATOM   580   C  CA  . ARG A  1 79  ? 16.228  44.426  5.121   1.00 30.53  ? 79  ARG A CA  1 
ATOM   581   C  C   . ARG A  1 79  ? 15.920  43.041  5.675   1.00 29.69  ? 79  ARG A C   1 
ATOM   582   O  O   . ARG A  1 79  ? 14.763  42.587  5.677   1.00 30.36  ? 79  ARG A O   1 
ATOM   583   C  CB  . ARG A  1 79  ? 16.401  45.396  6.289   1.00 30.12  ? 79  ARG A CB  1 
ATOM   584   C  CG  . ARG A  1 79  ? 15.146  45.586  7.136   1.00 30.60  ? 79  ARG A CG  1 
ATOM   585   C  CD  . ARG A  1 79  ? 15.413  46.419  8.375   1.00 30.32  ? 79  ARG A CD  1 
ATOM   586   N  NE  . ARG A  1 79  ? 15.871  45.591  9.489   1.00 29.03  ? 79  ARG A NE  1 
ATOM   587   C  CZ  . ARG A  1 79  ? 15.953  45.992  10.756  1.00 28.84  ? 79  ARG A CZ  1 
ATOM   588   N  NH1 . ARG A  1 79  ? 15.627  47.237  11.112  1.00 29.91  ? 79  ARG A NH1 1 
ATOM   589   N  NH2 . ARG A  1 79  ? 16.371  45.139  11.682  1.00 27.80  ? 79  ARG A NH2 1 
ATOM   590   N  N   . HIS A  1 80  ? 16.968  42.390  6.152   1.00 28.35  ? 80  HIS A N   1 
ATOM   591   C  CA  . HIS A  1 80  ? 16.845  41.201  6.990   1.00 27.49  ? 80  HIS A CA  1 
ATOM   592   C  C   . HIS A  1 80  ? 16.436  41.661  8.394   1.00 26.97  ? 80  HIS A C   1 
ATOM   593   O  O   . HIS A  1 80  ? 16.774  42.777  8.803   1.00 26.87  ? 80  HIS A O   1 
ATOM   594   C  CB  . HIS A  1 80  ? 18.181  40.456  7.080   1.00 26.63  ? 80  HIS A CB  1 
ATOM   595   C  CG  . HIS A  1 80  ? 18.732  40.027  5.758   1.00 27.21  ? 80  HIS A CG  1 
ATOM   596   N  ND1 . HIS A  1 80  ? 20.084  39.984  5.483   1.00 26.96  ? 80  HIS A ND1 1 
ATOM   597   C  CD2 . HIS A  1 80  ? 18.105  39.622  4.631   1.00 28.25  ? 80  HIS A CD2 1 
ATOM   598   C  CE1 . HIS A  1 80  ? 20.259  39.554  4.244   1.00 27.89  ? 80  HIS A CE1 1 
ATOM   599   N  NE2 . HIS A  1 80  ? 19.074  39.333  3.704   1.00 28.62  ? 80  HIS A NE2 1 
ATOM   600   N  N   . VAL A  1 81  ? 15.736  40.801  9.134   1.00 26.71  ? 81  VAL A N   1 
ATOM   601   C  CA  . VAL A  1 81  ? 15.392  41.107  10.526  1.00 26.41  ? 81  VAL A CA  1 
ATOM   602   C  C   . VAL A  1 81  ? 16.656  41.402  11.340  1.00 25.48  ? 81  VAL A C   1 
ATOM   603   O  O   . VAL A  1 81  ? 16.665  42.342  12.120  1.00 25.53  ? 81  VAL A O   1 
ATOM   604   C  CB  . VAL A  1 81  ? 14.539  39.996  11.188  1.00 26.46  ? 81  VAL A CB  1 
ATOM   605   C  CG1 . VAL A  1 81  ? 14.418  40.193  12.696  1.00 26.12  ? 81  VAL A CG1 1 
ATOM   606   C  CG2 . VAL A  1 81  ? 13.146  39.979  10.566  1.00 27.82  ? 81  VAL A CG2 1 
ATOM   607   N  N   . GLY A  1 82  ? 17.728  40.639  11.104  1.00 24.88  ? 82  GLY A N   1 
ATOM   608   C  CA  . GLY A  1 82  ? 18.996  40.832  11.820  1.00 24.29  ? 82  GLY A CA  1 
ATOM   609   C  C   . GLY A  1 82  ? 19.895  41.995  11.412  1.00 24.56  ? 82  GLY A C   1 
ATOM   610   O  O   . GLY A  1 82  ? 21.008  42.122  11.949  1.00 24.23  ? 82  GLY A O   1 
ATOM   611   N  N   . ASP A  1 83  ? 19.446  42.843  10.486  1.00 25.29  ? 83  ASP A N   1 
ATOM   612   C  CA  . ASP A  1 83  ? 20.263  43.959  9.996   1.00 25.82  ? 83  ASP A CA  1 
ATOM   613   C  C   . ASP A  1 83  ? 20.230  45.174  10.928  1.00 26.38  ? 83  ASP A C   1 
ATOM   614   O  O   . ASP A  1 83  ? 19.392  46.064  10.763  1.00 27.22  ? 83  ASP A O   1 
ATOM   615   C  CB  . ASP A  1 83  ? 19.816  44.374  8.590   1.00 26.60  ? 83  ASP A CB  1 
ATOM   616   C  CG  . ASP A  1 83  ? 20.168  43.350  7.534   1.00 26.51  ? 83  ASP A CG  1 
ATOM   617   O  OD1 . ASP A  1 83  ? 21.015  42.449  7.768   1.00 25.79  ? 83  ASP A OD1 1 
ATOM   618   O  OD2 . ASP A  1 83  ? 19.576  43.441  6.439   1.00 27.28  ? 83  ASP A OD2 1 
ATOM   619   N  N   . LEU A  1 84  ? 21.161  45.220  11.886  1.00 26.24  ? 84  LEU A N   1 
ATOM   620   C  CA  . LEU A  1 84  ? 21.266  46.353  12.821  1.00 27.03  ? 84  LEU A CA  1 
ATOM   621   C  C   . LEU A  1 84  ? 22.358  47.364  12.441  1.00 27.89  ? 84  LEU A C   1 
ATOM   622   O  O   . LEU A  1 84  ? 22.696  48.251  13.233  1.00 28.71  ? 84  LEU A O   1 
ATOM   623   C  CB  . LEU A  1 84  ? 21.442  45.848  14.257  1.00 26.63  ? 84  LEU A CB  1 
ATOM   624   C  CG  . LEU A  1 84  ? 20.340  44.887  14.726  1.00 26.20  ? 84  LEU A CG  1 
ATOM   625   C  CD1 . LEU A  1 84  ? 20.691  44.260  16.063  1.00 25.89  ? 84  LEU A CD1 1 
ATOM   626   C  CD2 . LEU A  1 84  ? 18.996  45.599  14.818  1.00 27.06  ? 84  LEU A CD2 1 
ATOM   627   N  N   . GLY A  1 85  ? 22.888  47.249  11.225  1.00 28.09  ? 85  GLY A N   1 
ATOM   628   C  CA  . GLY A  1 85  ? 23.716  48.295  10.640  1.00 29.16  ? 85  GLY A CA  1 
ATOM   629   C  C   . GLY A  1 85  ? 25.138  48.260  11.157  1.00 29.37  ? 85  GLY A C   1 
ATOM   630   O  O   . GLY A  1 85  ? 25.773  47.186  11.195  1.00 28.70  ? 85  GLY A O   1 
ATOM   631   N  N   . ASN A  1 86  ? 25.631  49.437  11.547  1.00 30.57  ? 86  ASN A N   1 
ATOM   632   C  CA  . ASN A  1 86  ? 26.999  49.612  12.004  1.00 31.25  ? 86  ASN A CA  1 
ATOM   633   C  C   . ASN A  1 86  ? 27.045  50.176  13.419  1.00 31.96  ? 86  ASN A C   1 
ATOM   634   O  O   . ASN A  1 86  ? 26.246  51.048  13.775  1.00 32.75  ? 86  ASN A O   1 
ATOM   635   C  CB  . ASN A  1 86  ? 27.743  50.576  11.077  1.00 32.58  ? 86  ASN A CB  1 
ATOM   636   C  CG  . ASN A  1 86  ? 28.025  49.973  9.716   1.00 32.30  ? 86  ASN A CG  1 
ATOM   637   O  OD1 . ASN A  1 86  ? 28.754  48.987  9.605   1.00 31.84  ? 86  ASN A OD1 1 
ATOM   638   N  ND2 . ASN A  1 86  ? 27.455  50.564  8.673   1.00 32.78  ? 86  ASN A ND2 1 
ATOM   639   N  N   . VAL A  1 87  ? 27.996  49.681  14.209  1.00 31.99  ? 87  VAL A N   1 
ATOM   640   C  CA  . VAL A  1 87  ? 28.421  50.359  15.431  1.00 33.17  ? 87  VAL A CA  1 
ATOM   641   C  C   . VAL A  1 87  ? 29.712  51.097  15.126  1.00 34.68  ? 87  VAL A C   1 
ATOM   642   O  O   . VAL A  1 87  ? 30.458  50.710  14.220  1.00 34.56  ? 87  VAL A O   1 
ATOM   643   C  CB  . VAL A  1 87  ? 28.595  49.408  16.637  1.00 32.62  ? 87  VAL A CB  1 
ATOM   644   C  CG1 . VAL A  1 87  ? 27.298  48.659  16.903  1.00 31.29  ? 87  VAL A CG1 1 
ATOM   645   C  CG2 . VAL A  1 87  ? 29.770  48.448  16.459  1.00 32.40  ? 87  VAL A CG2 1 
ATOM   646   N  N   . THR A  1 88  ? 29.951  52.173  15.870  1.00 36.32  ? 88  THR A N   1 
ATOM   647   C  CA  . THR A  1 88  ? 31.103  53.035  15.662  1.00 38.20  ? 88  THR A CA  1 
ATOM   648   C  C   . THR A  1 88  ? 32.062  52.946  16.830  1.00 39.28  ? 88  THR A C   1 
ATOM   649   O  O   . THR A  1 88  ? 31.680  53.232  17.966  1.00 39.85  ? 88  THR A O   1 
ATOM   650   C  CB  . THR A  1 88  ? 30.676  54.508  15.520  1.00 39.87  ? 88  THR A CB  1 
ATOM   651   O  OG1 . THR A  1 88  ? 29.718  54.622  14.467  1.00 39.12  ? 88  THR A OG1 1 
ATOM   652   C  CG2 . THR A  1 88  ? 31.890  55.403  15.215  1.00 42.00  ? 88  THR A CG2 1 
ATOM   653   N  N   . ALA A  1 89  ? 33.307  52.573  16.545  1.00 39.84  ? 89  ALA A N   1 
ATOM   654   C  CA  . ALA A  1 89  ? 34.356  52.544  17.557  1.00 41.39  ? 89  ALA A CA  1 
ATOM   655   C  C   . ALA A  1 89  ? 35.128  53.863  17.533  1.00 43.99  ? 89  ALA A C   1 
ATOM   656   O  O   . ALA A  1 89  ? 35.476  54.365  16.460  1.00 44.55  ? 89  ALA A O   1 
ATOM   657   C  CB  . ALA A  1 89  ? 35.292  51.375  17.320  1.00 40.94  ? 89  ALA A CB  1 
ATOM   658   N  N   . ASP A  1 90  ? 35.399  54.403  18.721  1.00 45.75  ? 90  ASP A N   1 
ATOM   659   C  CA  . ASP A  1 90  ? 36.140  55.660  18.879  1.00 48.67  ? 90  ASP A CA  1 
ATOM   660   C  C   . ASP A  1 90  ? 37.663  55.454  18.713  1.00 50.25  ? 90  ASP A C   1 
ATOM   661   O  O   . ASP A  1 90  ? 38.098  54.380  18.306  1.00 49.03  ? 90  ASP A O   1 
ATOM   662   C  CB  . ASP A  1 90  ? 35.759  56.338  20.217  1.00 50.24  ? 90  ASP A CB  1 
ATOM   663   C  CG  . ASP A  1 90  ? 36.294  55.611  21.456  1.00 50.71  ? 90  ASP A CG  1 
ATOM   664   O  OD1 . ASP A  1 90  ? 37.014  54.598  21.343  1.00 49.97  ? 90  ASP A OD1 1 
ATOM   665   O  OD2 . ASP A  1 90  ? 35.982  56.077  22.571  1.00 52.12  ? 90  ASP A OD2 1 
ATOM   666   N  N   . LYS A  1 91  ? 38.459  56.477  19.016  1.00 53.21  ? 91  LYS A N   1 
ATOM   667   C  CA  . LYS A  1 91  ? 39.930  56.405  18.875  1.00 55.26  ? 91  LYS A CA  1 
ATOM   668   C  C   . LYS A  1 91  ? 40.649  55.391  19.790  1.00 55.48  ? 91  LYS A C   1 
ATOM   669   O  O   . LYS A  1 91  ? 41.753  54.951  19.461  1.00 56.50  ? 91  LYS A O   1 
ATOM   670   C  CB  . LYS A  1 91  ? 40.550  57.794  19.066  1.00 58.72  ? 91  LYS A CB  1 
ATOM   671   C  CG  . LYS A  1 91  ? 40.515  58.316  20.498  1.00 60.75  ? 91  LYS A CG  1 
ATOM   672   C  CD  . LYS A  1 91  ? 40.602  59.836  20.542  1.00 63.77  ? 91  LYS A CD  1 
ATOM   673   C  CE  . LYS A  1 91  ? 40.827  60.354  21.953  1.00 66.51  ? 91  LYS A CE  1 
ATOM   674   N  NZ  . LYS A  1 91  ? 42.275  60.480  22.286  1.00 69.68  ? 91  LYS A NZ  1 
ATOM   675   N  N   . ASP A  1 92  ? 40.041  55.048  20.928  1.00 54.79  ? 92  ASP A N   1 
ATOM   676   C  CA  . ASP A  1 92  ? 40.574  54.019  21.841  1.00 54.89  ? 92  ASP A CA  1 
ATOM   677   C  C   . ASP A  1 92  ? 40.099  52.599  21.493  1.00 51.77  ? 92  ASP A C   1 
ATOM   678   O  O   . ASP A  1 92  ? 40.519  51.631  22.133  1.00 51.73  ? 92  ASP A O   1 
ATOM   679   C  CB  . ASP A  1 92  ? 40.184  54.326  23.296  1.00 56.03  ? 92  ASP A CB  1 
ATOM   680   C  CG  . ASP A  1 92  ? 40.764  55.633  23.805  1.00 59.59  ? 92  ASP A CG  1 
ATOM   681   O  OD1 . ASP A  1 92  ? 41.987  55.860  23.659  1.00 62.02  ? 92  ASP A OD1 1 
ATOM   682   O  OD2 . ASP A  1 92  ? 39.995  56.428  24.383  1.00 60.25  ? 92  ASP A OD2 1 
ATOM   683   N  N   . GLY A  1 93  ? 39.221  52.476  20.499  1.00 49.40  ? 93  GLY A N   1 
ATOM   684   C  CA  . GLY A  1 93  ? 38.704  51.186  20.055  1.00 46.63  ? 93  GLY A CA  1 
ATOM   685   C  C   . GLY A  1 93  ? 37.434  50.731  20.752  1.00 44.67  ? 93  GLY A C   1 
ATOM   686   O  O   . GLY A  1 93  ? 37.037  49.565  20.620  1.00 42.68  ? 93  GLY A O   1 
ATOM   687   N  N   . VAL A  1 94  ? 36.788  51.649  21.473  1.00 45.39  ? 94  VAL A N   1 
ATOM   688   C  CA  . VAL A  1 94  ? 35.555  51.362  22.192  1.00 43.98  ? 94  VAL A CA  1 
ATOM   689   C  C   . VAL A  1 94  ? 34.361  51.816  21.355  1.00 42.55  ? 94  VAL A C   1 
ATOM   690   O  O   . VAL A  1 94  ? 34.327  52.962  20.893  1.00 43.70  ? 94  VAL A O   1 
ATOM   691   C  CB  . VAL A  1 94  ? 35.511  52.074  23.559  1.00 45.98  ? 94  VAL A CB  1 
ATOM   692   C  CG1 . VAL A  1 94  ? 34.201  51.769  24.282  1.00 44.67  ? 94  VAL A CG1 1 
ATOM   693   C  CG2 . VAL A  1 94  ? 36.710  51.668  24.411  1.00 47.77  ? 94  VAL A CG2 1 
ATOM   694   N  N   . ALA A  1 95  ? 33.397  50.914  21.165  1.00 40.26  ? 95  ALA A N   1 
ATOM   695   C  CA  . ALA A  1 95  ? 32.123  51.237  20.528  1.00 39.10  ? 95  ALA A CA  1 
ATOM   696   C  C   . ALA A  1 95  ? 31.014  51.219  21.570  1.00 38.90  ? 95  ALA A C   1 
ATOM   697   O  O   . ALA A  1 95  ? 30.625  50.150  22.043  1.00 37.58  ? 95  ALA A O   1 
ATOM   698   C  CB  . ALA A  1 95  ? 31.811  50.245  19.412  1.00 36.97  ? 95  ALA A CB  1 
ATOM   699   N  N   . ASP A  1 96  ? 30.526  52.399  21.942  1.00 40.49  ? 96  ASP A N   1 
ATOM   700   C  CA  . ASP A  1 96  ? 29.374  52.499  22.827  1.00 40.68  ? 96  ASP A CA  1 
ATOM   701   C  C   . ASP A  1 96  ? 28.122  52.334  21.969  1.00 39.14  ? 96  ASP A C   1 
ATOM   702   O  O   . ASP A  1 96  ? 27.849  53.143  21.090  1.00 39.54  ? 96  ASP A O   1 
ATOM   703   C  CB  . ASP A  1 96  ? 29.365  53.823  23.596  1.00 43.32  ? 96  ASP A CB  1 
ATOM   704   C  CG  . ASP A  1 96  ? 30.522  53.932  24.595  1.00 45.31  ? 96  ASP A CG  1 
ATOM   705   O  OD1 . ASP A  1 96  ? 30.833  52.935  25.292  1.00 44.76  ? 96  ASP A OD1 1 
ATOM   706   O  OD2 . ASP A  1 96  ? 31.127  55.021  24.688  1.00 47.71  ? 96  ASP A OD2 1 
ATOM   707   N  N   . VAL A  1 97  ? 27.391  51.259  22.221  1.00 37.61  ? 97  VAL A N   1 
ATOM   708   C  CA  . VAL A  1 97  ? 26.224  50.880  21.423  1.00 36.21  ? 97  VAL A CA  1 
ATOM   709   C  C   . VAL A  1 97  ? 24.961  51.448  22.068  1.00 37.10  ? 97  VAL A C   1 
ATOM   710   O  O   . VAL A  1 97  ? 24.759  51.312  23.271  1.00 37.74  ? 97  VAL A O   1 
ATOM   711   C  CB  . VAL A  1 97  ? 26.137  49.345  21.293  1.00 34.24  ? 97  VAL A CB  1 
ATOM   712   C  CG1 . VAL A  1 97  ? 24.898  48.917  20.508  1.00 32.95  ? 97  VAL A CG1 1 
ATOM   713   C  CG2 . VAL A  1 97  ? 27.403  48.814  20.627  1.00 33.83  ? 97  VAL A CG2 1 
ATOM   714   N  N   . SER A  1 98  ? 24.131  52.100  21.261  1.00 37.46  ? 98  SER A N   1 
ATOM   715   C  CA  . SER A  1 98  ? 22.840  52.609  21.716  1.00 38.52  ? 98  SER A CA  1 
ATOM   716   C  C   . SER A  1 98  ? 21.887  52.699  20.525  1.00 37.95  ? 98  SER A C   1 
ATOM   717   O  O   . SER A  1 98  ? 21.910  53.671  19.781  1.00 39.15  ? 98  SER A O   1 
ATOM   718   C  CB  . SER A  1 98  ? 23.009  53.970  22.388  1.00 41.15  ? 98  SER A CB  1 
ATOM   719   O  OG  . SER A  1 98  ? 21.793  54.373  23.002  1.00 42.42  ? 98  SER A OG  1 
ATOM   720   N  N   . ILE A  1 99  ? 21.053  51.673  20.367  1.00 36.51  ? 99  ILE A N   1 
ATOM   721   C  CA  . ILE A  1 99  ? 20.191  51.486  19.206  1.00 35.77  ? 99  ILE A CA  1 
ATOM   722   C  C   . ILE A  1 99  ? 18.763  51.274  19.704  1.00 36.04  ? 99  ILE A C   1 
ATOM   723   O  O   . ILE A  1 99  ? 18.542  50.754  20.810  1.00 35.98  ? 99  ILE A O   1 
ATOM   724   C  CB  . ILE A  1 99  ? 20.640  50.223  18.413  1.00 33.90  ? 99  ILE A CB  1 
ATOM   725   C  CG1 . ILE A  1 99  ? 21.975  50.465  17.712  1.00 33.89  ? 99  ILE A CG1 1 
ATOM   726   C  CG2 . ILE A  1 99  ? 19.616  49.780  17.374  1.00 33.31  ? 99  ILE A CG2 1 
ATOM   727   C  CD1 . ILE A  1 99  ? 22.656  49.180  17.277  1.00 32.38  ? 99  ILE A CD1 1 
ATOM   728   N  N   . GLU A  1 100 ? 17.802  51.680  18.883  1.00 36.37  ? 100 GLU A N   1 
ATOM   729   C  CA  . GLU A  1 100 ? 16.423  51.244  19.036  1.00 36.44  ? 100 GLU A CA  1 
ATOM   730   C  C   . GLU A  1 100 ? 15.965  50.645  17.707  1.00 35.13  ? 100 GLU A C   1 
ATOM   731   O  O   . GLU A  1 100 ? 16.208  51.235  16.651  1.00 35.24  ? 100 GLU A O   1 
ATOM   732   C  CB  . GLU A  1 100 ? 15.525  52.407  19.442  1.00 38.94  ? 100 GLU A CB  1 
ATOM   733   C  CG  . GLU A  1 100 ? 14.164  51.942  19.937  1.00 39.68  ? 100 GLU A CG  1 
ATOM   734   C  CD  . GLU A  1 100 ? 13.278  53.075  20.390  1.00 42.44  ? 100 GLU A CD  1 
ATOM   735   O  OE1 . GLU A  1 100 ? 13.442  53.527  21.550  1.00 43.89  ? 100 GLU A OE1 1 
ATOM   736   O  OE2 . GLU A  1 100 ? 12.405  53.494  19.594  1.00 43.55  ? 100 GLU A OE2 1 
ATOM   737   N  N   . ASP A  1 101 ? 15.308  49.484  17.771  1.00 33.89  ? 101 ASP A N   1 
ATOM   738   C  CA  . ASP A  1 101 ? 14.830  48.780  16.573  1.00 32.99  ? 101 ASP A CA  1 
ATOM   739   C  C   . ASP A  1 101 ? 13.444  48.145  16.768  1.00 33.26  ? 101 ASP A C   1 
ATOM   740   O  O   . ASP A  1 101 ? 13.183  47.501  17.791  1.00 33.01  ? 101 ASP A O   1 
ATOM   741   C  CB  . ASP A  1 101 ? 15.823  47.692  16.161  1.00 31.18  ? 101 ASP A CB  1 
ATOM   742   C  CG  . ASP A  1 101 ? 15.607  47.225  14.735  1.00 30.80  ? 101 ASP A CG  1 
ATOM   743   O  OD1 . ASP A  1 101 ? 16.047  47.949  13.816  1.00 31.25  ? 101 ASP A OD1 1 
ATOM   744   O  OD2 . ASP A  1 101 ? 14.990  46.150  14.524  1.00 30.29  ? 101 ASP A OD2 1 
ATOM   745   N  N   . SER A  1 102 ? 12.584  48.315  15.765  1.00 33.80  ? 102 SER A N   1 
ATOM   746   C  CA  . SER A  1 102 ? 11.198  47.837  15.809  1.00 34.59  ? 102 SER A CA  1 
ATOM   747   C  C   . SER A  1 102 ? 10.946  46.599  14.951  1.00 33.49  ? 102 SER A C   1 
ATOM   748   O  O   . SER A  1 102 ? 9.812   46.130  14.879  1.00 34.37  ? 102 SER A O   1 
ATOM   749   C  CB  . SER A  1 102 ? 10.256  48.954  15.374  1.00 36.74  ? 102 SER A CB  1 
ATOM   750   O  OG  . SER A  1 102 ? 10.329  50.019  16.291  1.00 38.08  ? 102 SER A OG  1 
ATOM   751   N  N   . VAL A  1 103 ? 11.991  46.068  14.317  1.00 31.76  ? 103 VAL A N   1 
ATOM   752   C  CA  . VAL A  1 103 ? 11.882  44.883  13.467  1.00 30.94  ? 103 VAL A CA  1 
ATOM   753   C  C   . VAL A  1 103 ? 12.268  43.626  14.258  1.00 29.57  ? 103 VAL A C   1 
ATOM   754   O  O   . VAL A  1 103 ? 11.544  42.630  14.232  1.00 29.71  ? 103 VAL A O   1 
ATOM   755   C  CB  . VAL A  1 103 ? 12.722  45.054  12.181  1.00 30.43  ? 103 VAL A CB  1 
ATOM   756   C  CG1 . VAL A  1 103 ? 12.769  43.759  11.382  1.00 29.81  ? 103 VAL A CG1 1 
ATOM   757   C  CG2 . VAL A  1 103 ? 12.142  46.185  11.338  1.00 31.96  ? 103 VAL A CG2 1 
ATOM   758   N  N   . ILE A  1 104 ? 13.403  43.670  14.955  1.00 28.45  ? 104 ILE A N   1 
ATOM   759   C  CA  . ILE A  1 104 ? 13.744  42.618  15.929  1.00 27.51  ? 104 ILE A CA  1 
ATOM   760   C  C   . ILE A  1 104 ? 12.746  42.625  17.095  1.00 28.33  ? 104 ILE A C   1 
ATOM   761   O  O   . ILE A  1 104 ? 12.097  43.628  17.368  1.00 29.49  ? 104 ILE A O   1 
ATOM   762   C  CB  . ILE A  1 104 ? 15.189  42.731  16.487  1.00 26.55  ? 104 ILE A CB  1 
ATOM   763   C  CG1 . ILE A  1 104 ? 15.449  44.090  17.150  1.00 27.30  ? 104 ILE A CG1 1 
ATOM   764   C  CG2 . ILE A  1 104 ? 16.220  42.491  15.386  1.00 25.77  ? 104 ILE A CG2 1 
ATOM   765   C  CD1 . ILE A  1 104 ? 16.621  44.087  18.117  1.00 26.80  ? 104 ILE A CD1 1 
ATOM   766   N  N   . SER A  1 105 ? 12.636  41.490  17.763  1.00 27.87  ? 105 SER A N   1 
ATOM   767   C  CA  . SER A  1 105 ? 11.816  41.359  18.969  1.00 28.73  ? 105 SER A CA  1 
ATOM   768   C  C   . SER A  1 105 ? 12.489  40.380  19.915  1.00 27.86  ? 105 SER A C   1 
ATOM   769   O  O   . SER A  1 105 ? 13.388  39.637  19.508  1.00 26.76  ? 105 SER A O   1 
ATOM   770   C  CB  . SER A  1 105 ? 10.407  40.866  18.606  1.00 29.83  ? 105 SER A CB  1 
ATOM   771   O  OG  . SER A  1 105 ? 9.513   41.029  19.694  1.00 31.08  ? 105 SER A OG  1 
ATOM   772   N  N   . LEU A  1 106 ? 12.076  40.415  21.176  1.00 28.61  ? 106 LEU A N   1 
ATOM   773   C  CA  . LEU A  1 106 ? 12.468  39.428  22.171  1.00 28.24  ? 106 LEU A CA  1 
ATOM   774   C  C   . LEU A  1 106 ? 11.355  38.400  22.439  1.00 29.08  ? 106 LEU A C   1 
ATOM   775   O  O   . LEU A  1 106 ? 11.449  37.617  23.385  1.00 29.14  ? 106 LEU A O   1 
ATOM   776   C  CB  . LEU A  1 106 ? 12.884  40.129  23.464  1.00 28.71  ? 106 LEU A CB  1 
ATOM   777   C  CG  . LEU A  1 106 ? 13.945  41.228  23.339  1.00 28.38  ? 106 LEU A CG  1 
ATOM   778   C  CD1 . LEU A  1 106 ? 14.295  41.744  24.722  1.00 29.20  ? 106 LEU A CD1 1 
ATOM   779   C  CD2 . LEU A  1 106 ? 15.208  40.754  22.608  1.00 26.94  ? 106 LEU A CD2 1 
ATOM   780   N  N   . SER A  1 107 ? 10.315  38.391  21.605  1.00 29.95  ? 107 SER A N   1 
ATOM   781   C  CA  . SER A  1 107 ? 9.302   37.325  21.626  1.00 30.88  ? 107 SER A CA  1 
ATOM   782   C  C   . SER A  1 107 ? 8.694   37.152  20.241  1.00 31.36  ? 107 SER A C   1 
ATOM   783   O  O   . SER A  1 107 ? 8.920   37.980  19.360  1.00 31.10  ? 107 SER A O   1 
ATOM   784   C  CB  . SER A  1 107 ? 8.209   37.637  22.654  1.00 32.56  ? 107 SER A CB  1 
ATOM   785   O  OG  . SER A  1 107 ? 7.568   38.866  22.369  1.00 33.70  ? 107 SER A OG  1 
ATOM   786   N  N   . GLY A  1 108 ? 7.949   36.063  20.055  1.00 32.28  ? 108 GLY A N   1 
ATOM   787   C  CA  . GLY A  1 108 ? 7.208   35.813  18.816  1.00 33.29  ? 108 GLY A CA  1 
ATOM   788   C  C   . GLY A  1 108 ? 8.089   35.504  17.619  1.00 32.33  ? 108 GLY A C   1 
ATOM   789   O  O   . GLY A  1 108 ? 9.239   35.087  17.783  1.00 30.86  ? 108 GLY A O   1 
ATOM   790   N  N   . ASP A  1 109 ? 7.565   35.733  16.414  1.00 33.31  ? 109 ASP A N   1 
ATOM   791   C  CA  . ASP A  1 109 ? 8.230   35.258  15.185  1.00 32.88  ? 109 ASP A CA  1 
ATOM   792   C  C   . ASP A  1 109 ? 9.573   35.910  14.858  1.00 31.25  ? 109 ASP A C   1 
ATOM   793   O  O   . ASP A  1 109 ? 10.436  35.248  14.295  1.00 30.62  ? 109 ASP A O   1 
ATOM   794   C  CB  . ASP A  1 109 ? 7.304   35.364  13.966  1.00 34.62  ? 109 ASP A CB  1 
ATOM   795   C  CG  . ASP A  1 109 ? 6.171   34.346  13.997  1.00 36.52  ? 109 ASP A CG  1 
ATOM   796   O  OD1 . ASP A  1 109 ? 6.401   33.172  14.400  1.00 36.54  ? 109 ASP A OD1 1 
ATOM   797   O  OD2 . ASP A  1 109 ? 5.047   34.722  13.614  1.00 38.37  ? 109 ASP A OD2 1 
ATOM   798   N  N   . HIS A  1 110 ? 9.758   37.182  15.210  1.00 30.92  ? 110 HIS A N   1 
ATOM   799   C  CA  . HIS A  1 110 ? 11.050  37.861  15.000  1.00 29.58  ? 110 HIS A CA  1 
ATOM   800   C  C   . HIS A  1 110 ? 11.953  37.811  16.242  1.00 28.39  ? 110 HIS A C   1 
ATOM   801   O  O   . HIS A  1 110 ? 12.860  38.636  16.382  1.00 27.74  ? 110 HIS A O   1 
ATOM   802   C  CB  . HIS A  1 110 ? 10.820  39.313  14.556  1.00 30.23  ? 110 HIS A CB  1 
ATOM   803   C  CG  . HIS A  1 110 ? 10.208  39.434  13.195  1.00 31.27  ? 110 HIS A CG  1 
ATOM   804   N  ND1 . HIS A  1 110 ? 10.054  40.645  12.554  1.00 31.95  ? 110 HIS A ND1 1 
ATOM   805   C  CD2 . HIS A  1 110 ? 9.728   38.491  12.346  1.00 31.95  ? 110 HIS A CD2 1 
ATOM   806   C  CE1 . HIS A  1 110 ? 9.498   40.442  11.372  1.00 32.97  ? 110 HIS A CE1 1 
ATOM   807   N  NE2 . HIS A  1 110 ? 9.289   39.144  11.223  1.00 32.96  ? 110 HIS A NE2 1 
ATOM   808   N  N   . CYS A  1 111 ? 11.722  36.838  17.129  1.00 28.26  ? 111 CYS A N   1 
ATOM   809   C  CA  . CYS A  1 111 ? 12.476  36.737  18.360  1.00 27.50  ? 111 CYS A CA  1 
ATOM   810   C  C   . CYS A  1 111 ? 13.918  36.378  18.039  1.00 26.07  ? 111 CYS A C   1 
ATOM   811   O  O   . CYS A  1 111 ? 14.161  35.434  17.294  1.00 25.83  ? 111 CYS A O   1 
ATOM   812   C  CB  . CYS A  1 111 ? 11.904  35.673  19.287  1.00 28.10  ? 111 CYS A CB  1 
ATOM   813   S  SG  . CYS A  1 111 ? 12.767  35.647  20.863  1.00 27.88  ? 111 CYS A SG  1 
ATOM   814   N  N   . ILE A  1 112 ? 14.842  37.143  18.601  1.00 25.31  ? 112 ILE A N   1 
ATOM   815   C  CA  . ILE A  1 112 ? 16.280  36.937  18.399  1.00 24.33  ? 112 ILE A CA  1 
ATOM   816   C  C   . ILE A  1 112 ? 16.965  36.201  19.564  1.00 23.98  ? 112 ILE A C   1 
ATOM   817   O  O   . ILE A  1 112 ? 18.161  35.921  19.487  1.00 23.48  ? 112 ILE A O   1 
ATOM   818   C  CB  . ILE A  1 112 ? 17.016  38.267  18.113  1.00 24.13  ? 112 ILE A CB  1 
ATOM   819   C  CG1 . ILE A  1 112 ? 16.879  39.250  19.287  1.00 24.61  ? 112 ILE A CG1 1 
ATOM   820   C  CG2 . ILE A  1 112 ? 16.507  38.876  16.811  1.00 24.40  ? 112 ILE A CG2 1 
ATOM   821   C  CD1 . ILE A  1 112 ? 17.777  40.456  19.170  1.00 24.67  ? 112 ILE A CD1 1 
ATOM   822   N  N   . ILE A  1 113 ? 16.226  35.890  20.633  1.00 24.36  ? 113 ILE A N   1 
ATOM   823   C  CA  . ILE A  1 113 ? 16.779  35.104  21.740  1.00 24.30  ? 113 ILE A CA  1 
ATOM   824   C  C   . ILE A  1 113 ? 17.168  33.714  21.220  1.00 23.98  ? 113 ILE A C   1 
ATOM   825   O  O   . ILE A  1 113 ? 16.454  33.128  20.413  1.00 24.11  ? 113 ILE A O   1 
ATOM   826   C  CB  . ILE A  1 113 ? 15.804  35.038  22.948  1.00 25.21  ? 113 ILE A CB  1 
ATOM   827   C  CG1 . ILE A  1 113 ? 15.735  36.425  23.603  1.00 25.67  ? 113 ILE A CG1 1 
ATOM   828   C  CG2 . ILE A  1 113 ? 16.251  33.996  23.980  1.00 25.38  ? 113 ILE A CG2 1 
ATOM   829   C  CD1 . ILE A  1 113 ? 14.587  36.623  24.561  1.00 26.84  ? 113 ILE A CD1 1 
ATOM   830   N  N   . GLY A  1 114 ? 18.327  33.218  21.649  1.00 23.63  ? 114 GLY A N   1 
ATOM   831   C  CA  . GLY A  1 114 ? 18.872  31.957  21.139  1.00 23.61  ? 114 GLY A CA  1 
ATOM   832   C  C   . GLY A  1 114 ? 19.552  32.021  19.772  1.00 23.22  ? 114 GLY A C   1 
ATOM   833   O  O   . GLY A  1 114 ? 19.954  30.987  19.233  1.00 23.43  ? 114 GLY A O   1 
ATOM   834   N  N   . ARG A  1 115 ? 19.679  33.222  19.210  1.00 22.85  ? 115 ARG A N   1 
ATOM   835   C  CA  . ARG A  1 115 ? 20.400  33.442  17.959  1.00 22.66  ? 115 ARG A CA  1 
ATOM   836   C  C   . ARG A  1 115 ? 21.731  34.109  18.298  1.00 22.49  ? 115 ARG A C   1 
ATOM   837   O  O   . ARG A  1 115 ? 22.039  34.294  19.488  1.00 22.54  ? 115 ARG A O   1 
ATOM   838   C  CB  . ARG A  1 115 ? 19.529  34.259  17.006  1.00 22.66  ? 115 ARG A CB  1 
ATOM   839   C  CG  . ARG A  1 115 ? 18.205  33.549  16.748  1.00 23.19  ? 115 ARG A CG  1 
ATOM   840   C  CD  . ARG A  1 115 ? 17.442  34.111  15.572  1.00 23.49  ? 115 ARG A CD  1 
ATOM   841   N  NE  . ARG A  1 115 ? 16.084  33.565  15.496  1.00 24.24  ? 115 ARG A NE  1 
ATOM   842   C  CZ  . ARG A  1 115 ? 15.724  32.413  14.928  1.00 24.91  ? 115 ARG A CZ  1 
ATOM   843   N  NH1 . ARG A  1 115 ? 16.613  31.614  14.348  1.00 24.93  ? 115 ARG A NH1 1 
ATOM   844   N  NH2 . ARG A  1 115 ? 14.430  32.061  14.909  1.00 25.82  ? 115 ARG A NH2 1 
ATOM   845   N  N   . THR A  1 116 ? 22.527  34.448  17.277  1.00 22.48  ? 116 THR A N   1 
ATOM   846   C  CA  . THR A  1 116 ? 23.894  34.944  17.494  1.00 22.62  ? 116 THR A CA  1 
ATOM   847   C  C   . THR A  1 116 ? 24.039  36.384  17.072  1.00 22.54  ? 116 THR A C   1 
ATOM   848   O  O   . THR A  1 116 ? 23.674  36.740  15.955  1.00 22.55  ? 116 THR A O   1 
ATOM   849   C  CB  . THR A  1 116 ? 24.934  34.082  16.752  1.00 23.07  ? 116 THR A CB  1 
ATOM   850   O  OG1 . THR A  1 116 ? 24.851  32.737  17.230  1.00 23.39  ? 116 THR A OG1 1 
ATOM   851   C  CG2 . THR A  1 116 ? 26.363  34.606  16.977  1.00 23.50  ? 116 THR A CG2 1 
ATOM   852   N  N   . LEU A  1 117 ? 24.550  37.211  17.979  1.00 22.71  ? 117 LEU A N   1 
ATOM   853   C  CA  . LEU A  1 117 ? 24.926  38.586  17.668  1.00 22.94  ? 117 LEU A CA  1 
ATOM   854   C  C   . LEU A  1 117 ? 26.396  38.553  17.231  1.00 23.41  ? 117 LEU A C   1 
ATOM   855   O  O   . LEU A  1 117 ? 27.206  37.906  17.884  1.00 23.75  ? 117 LEU A O   1 
ATOM   856   C  CB  . LEU A  1 117 ? 24.756  39.479  18.901  1.00 23.28  ? 117 LEU A CB  1 
ATOM   857   C  CG  . LEU A  1 117 ? 24.992  40.976  18.728  1.00 23.82  ? 117 LEU A CG  1 
ATOM   858   C  CD1 . LEU A  1 117 ? 24.016  41.604  17.743  1.00 23.63  ? 117 LEU A CD1 1 
ATOM   859   C  CD2 . LEU A  1 117 ? 24.909  41.653  20.080  1.00 24.51  ? 117 LEU A CD2 1 
ATOM   860   N  N   . VAL A  1 118 ? 26.719  39.237  16.136  1.00 23.61  ? 118 VAL A N   1 
ATOM   861   C  CA  . VAL A  1 118 ? 28.071  39.259  15.580  1.00 24.34  ? 118 VAL A CA  1 
ATOM   862   C  C   . VAL A  1 118 ? 28.495  40.698  15.313  1.00 24.97  ? 118 VAL A C   1 
ATOM   863   O  O   . VAL A  1 118 ? 27.684  41.518  14.846  1.00 24.73  ? 118 VAL A O   1 
ATOM   864   C  CB  . VAL A  1 118 ? 28.172  38.477  14.248  1.00 24.36  ? 118 VAL A CB  1 
ATOM   865   C  CG1 . VAL A  1 118 ? 29.617  38.480  13.723  1.00 25.32  ? 118 VAL A CG1 1 
ATOM   866   C  CG2 . VAL A  1 118 ? 27.679  37.047  14.415  1.00 24.04  ? 118 VAL A CG2 1 
ATOM   867   N  N   . VAL A  1 119 ? 29.761  40.994  15.615  1.00 25.96  ? 119 VAL A N   1 
ATOM   868   C  CA  . VAL A  1 119 ? 30.390  42.272  15.261  1.00 26.92  ? 119 VAL A CA  1 
ATOM   869   C  C   . VAL A  1 119 ? 31.531  41.968  14.270  1.00 27.78  ? 119 VAL A C   1 
ATOM   870   O  O   . VAL A  1 119 ? 32.303  41.010  14.449  1.00 28.13  ? 119 VAL A O   1 
ATOM   871   C  CB  . VAL A  1 119 ? 30.844  43.100  16.492  1.00 27.78  ? 119 VAL A CB  1 
ATOM   872   C  CG1 . VAL A  1 119 ? 31.938  42.407  17.290  1.00 28.59  ? 119 VAL A CG1 1 
ATOM   873   C  CG2 . VAL A  1 119 ? 31.307  44.481  16.059  1.00 28.85  ? 119 VAL A CG2 1 
ATOM   874   N  N   . HIS A  1 120 ? 31.591  42.761  13.207  1.00 28.25  ? 120 HIS A N   1 
ATOM   875   C  CA  . HIS A  1 120 ? 32.383  42.424  12.031  1.00 29.14  ? 120 HIS A CA  1 
ATOM   876   C  C   . HIS A  1 120 ? 33.619  43.296  11.862  1.00 30.78  ? 120 HIS A C   1 
ATOM   877   O  O   . HIS A  1 120 ? 33.739  44.373  12.451  1.00 31.29  ? 120 HIS A O   1 
ATOM   878   C  CB  . HIS A  1 120 ? 31.513  42.525  10.766  1.00 28.65  ? 120 HIS A CB  1 
ATOM   879   C  CG  . HIS A  1 120 ? 30.607  41.355  10.563  1.00 27.68  ? 120 HIS A CG  1 
ATOM   880   N  ND1 . HIS A  1 120 ? 30.924  40.310  9.723   1.00 28.04  ? 120 HIS A ND1 1 
ATOM   881   C  CD2 . HIS A  1 120 ? 29.385  41.073  11.075  1.00 26.63  ? 120 HIS A CD2 1 
ATOM   882   C  CE1 . HIS A  1 120 ? 29.940  39.427  9.737   1.00 27.25  ? 120 HIS A CE1 1 
ATOM   883   N  NE2 . HIS A  1 120 ? 28.994  39.866  10.547  1.00 26.36  ? 120 HIS A NE2 1 
ATOM   884   N  N   . GLU A  1 121 ? 34.509  42.798  11.010  1.00 31.88  ? 121 GLU A N   1 
ATOM   885   C  CA  . GLU A  1 121 ? 35.793  43.401  10.689  1.00 33.75  ? 121 GLU A CA  1 
ATOM   886   C  C   . GLU A  1 121 ? 35.667  44.853  10.234  1.00 34.31  ? 121 GLU A C   1 
ATOM   887   O  O   . GLU A  1 121 ? 36.399  45.720  10.719  1.00 35.60  ? 121 GLU A O   1 
ATOM   888   C  CB  . GLU A  1 121 ? 36.456  42.562  9.586   1.00 34.72  ? 121 GLU A CB  1 
ATOM   889   C  CG  . GLU A  1 121 ? 37.870  42.967  9.157   1.00 36.94  ? 121 GLU A CG  1 
ATOM   890   C  CD  . GLU A  1 121 ? 38.342  42.219  7.913   1.00 37.97  ? 121 GLU A CD  1 
ATOM   891   O  OE1 . GLU A  1 121 ? 37.670  41.252  7.473   1.00 37.16  ? 121 GLU A OE1 1 
ATOM   892   O  OE2 . GLU A  1 121 ? 39.394  42.602  7.353   1.00 39.96  ? 121 GLU A OE2 1 
ATOM   893   N  N   . LYS A  1 122 ? 34.737  45.117  9.317   1.00 33.52  ? 122 LYS A N   1 
ATOM   894   C  CA  . LYS A  1 122 ? 34.642  46.426  8.677   1.00 34.25  ? 122 LYS A CA  1 
ATOM   895   C  C   . LYS A  1 122 ? 33.186  46.878  8.460   1.00 32.97  ? 122 LYS A C   1 
ATOM   896   O  O   . LYS A  1 122 ? 32.252  46.271  9.004   1.00 31.47  ? 122 LYS A O   1 
ATOM   897   C  CB  . LYS A  1 122 ? 35.475  46.404  7.388   1.00 35.72  ? 122 LYS A CB  1 
ATOM   898   C  CG  . LYS A  1 122 ? 35.054  45.361  6.366   1.00 35.21  ? 122 LYS A CG  1 
ATOM   899   C  CD  . LYS A  1 122 ? 36.122  45.234  5.299   1.00 36.99  ? 122 LYS A CD  1 
ATOM   900   C  CE  . LYS A  1 122 ? 35.677  44.357  4.140   1.00 36.87  ? 122 LYS A CE  1 
ATOM   901   N  NZ  . LYS A  1 122 ? 36.860  44.017  3.297   1.00 38.84  ? 122 LYS A NZ  1 
ATOM   902   N  N   . ALA A  1 123 ? 33.003  47.976  7.726   1.00 33.60  ? 123 ALA A N   1 
ATOM   903   C  CA  . ALA A  1 123 ? 31.686  48.587  7.558   1.00 32.90  ? 123 ALA A CA  1 
ATOM   904   C  C   . ALA A  1 123 ? 30.687  47.703  6.790   1.00 31.72  ? 123 ALA A C   1 
ATOM   905   O  O   . ALA A  1 123 ? 31.035  47.066  5.795   1.00 32.05  ? 123 ALA A O   1 
ATOM   906   C  CB  . ALA A  1 123 ? 31.827  49.938  6.873   1.00 34.26  ? 123 ALA A CB  1 
ATOM   907   N  N   . ASP A  1 124 ? 29.460  47.650  7.299   1.00 30.61  ? 124 ASP A N   1 
ATOM   908   C  CA  . ASP A  1 124 ? 28.297  47.171  6.557   1.00 29.91  ? 124 ASP A CA  1 
ATOM   909   C  C   . ASP A  1 124 ? 27.954  48.267  5.548   1.00 30.84  ? 124 ASP A C   1 
ATOM   910   O  O   . ASP A  1 124 ? 27.670  49.395  5.932   1.00 31.29  ? 124 ASP A O   1 
ATOM   911   C  CB  . ASP A  1 124 ? 27.122  46.937  7.531   1.00 28.89  ? 124 ASP A CB  1 
ATOM   912   C  CG  . ASP A  1 124 ? 25.904  46.259  6.882   1.00 28.38  ? 124 ASP A CG  1 
ATOM   913   O  OD1 . ASP A  1 124 ? 25.696  46.339  5.651   1.00 29.00  ? 124 ASP A OD1 1 
ATOM   914   O  OD2 . ASP A  1 124 ? 25.118  45.653  7.636   1.00 27.57  ? 124 ASP A OD2 1 
ATOM   915   N  N   . ASP A  1 125 ? 27.989  47.927  4.260   1.00 31.29  ? 125 ASP A N   1 
ATOM   916   C  CA  . ASP A  1 125 ? 27.613  48.864  3.185   1.00 32.40  ? 125 ASP A CA  1 
ATOM   917   C  C   . ASP A  1 125 ? 26.089  49.055  3.006   1.00 32.15  ? 125 ASP A C   1 
ATOM   918   O  O   . ASP A  1 125 ? 25.662  49.716  2.061   1.00 33.14  ? 125 ASP A O   1 
ATOM   919   C  CB  . ASP A  1 125 ? 28.295  48.476  1.845   1.00 33.33  ? 125 ASP A CB  1 
ATOM   920   C  CG  . ASP A  1 125 ? 27.765  47.162  1.237   1.00 32.82  ? 125 ASP A CG  1 
ATOM   921   O  OD1 . ASP A  1 125 ? 26.601  46.770  1.470   1.00 31.97  ? 125 ASP A OD1 1 
ATOM   922   O  OD2 . ASP A  1 125 ? 28.532  46.514  0.498   1.00 33.46  ? 125 ASP A OD2 1 
ATOM   923   N  N   . LEU A  1 126 ? 25.288  48.438  3.882   1.00 31.03  ? 126 LEU A N   1 
ATOM   924   C  CA  . LEU A  1 126 ? 23.831  48.618  3.942   1.00 31.01  ? 126 LEU A CA  1 
ATOM   925   C  C   . LEU A  1 126 ? 23.099  48.214  2.650   1.00 31.61  ? 126 LEU A C   1 
ATOM   926   O  O   . LEU A  1 126 ? 22.022  48.733  2.354   1.00 32.28  ? 126 LEU A O   1 
ATOM   927   C  CB  . LEU A  1 126 ? 23.486  50.057  4.353   1.00 31.88  ? 126 LEU A CB  1 
ATOM   928   C  CG  . LEU A  1 126 ? 24.295  50.644  5.517   1.00 31.88  ? 126 LEU A CG  1 
ATOM   929   C  CD1 . LEU A  1 126 ? 23.822  52.064  5.803   1.00 33.13  ? 126 LEU A CD1 1 
ATOM   930   C  CD2 . LEU A  1 126 ? 24.208  49.781  6.766   1.00 30.56  ? 126 LEU A CD2 1 
ATOM   931   N  N   . GLY A  1 127 ? 23.673  47.269  1.902   1.00 31.66  ? 127 GLY A N   1 
ATOM   932   C  CA  . GLY A  1 127 ? 23.091  46.803  0.637   1.00 32.53  ? 127 GLY A CA  1 
ATOM   933   C  C   . GLY A  1 127 ? 23.335  47.670  -0.582  1.00 34.17  ? 127 GLY A C   1 
ATOM   934   O  O   . GLY A  1 127 ? 22.800  47.377  -1.649  1.00 35.14  ? 127 GLY A O   1 
ATOM   935   N  N   . LYS A  1 128 ? 24.174  48.701  -0.448  1.00 34.74  ? 128 LYS A N   1 
ATOM   936   C  CA  . LYS A  1 128 ? 24.445  49.660  -1.524  1.00 36.45  ? 128 LYS A CA  1 
ATOM   937   C  C   . LYS A  1 128 ? 25.806  49.443  -2.192  1.00 37.12  ? 128 LYS A C   1 
ATOM   938   O  O   . LYS A  1 128 ? 26.262  50.294  -2.947  1.00 38.57  ? 128 LYS A O   1 
ATOM   939   C  CB  . LYS A  1 128 ? 24.374  51.089  -0.971  1.00 37.07  ? 128 LYS A CB  1 
ATOM   940   C  CG  . LYS A  1 128 ? 23.093  51.389  -0.198  1.00 36.73  ? 128 LYS A CG  1 
ATOM   941   C  CD  . LYS A  1 128 ? 23.031  52.845  0.249   0.50 37.73  ? 128 LYS A CD  1 
ATOM   942   C  CE  . LYS A  1 128 ? 21.619  53.265  0.637   0.50 38.07  ? 128 LYS A CE  1 
ATOM   943   N  NZ  . LYS A  1 128 ? 21.111  52.555  1.845   0.50 36.60  ? 128 LYS A NZ  1 
ATOM   944   N  N   . GLY A  1 129 ? 26.443  48.307  -1.924  1.00 36.27  ? 129 GLY A N   1 
ATOM   945   C  CA  . GLY A  1 129 ? 27.774  48.012  -2.443  1.00 37.05  ? 129 GLY A CA  1 
ATOM   946   C  C   . GLY A  1 129 ? 27.873  47.697  -3.923  1.00 38.52  ? 129 GLY A C   1 
ATOM   947   O  O   . GLY A  1 129 ? 28.953  47.796  -4.482  1.00 39.73  ? 129 GLY A O   1 
ATOM   948   N  N   . GLY A  1 130 ? 26.772  47.298  -4.560  1.00 38.71  ? 130 GLY A N   1 
ATOM   949   C  CA  . GLY A  1 130 ? 26.776  47.031  -6.005  1.00 40.39  ? 130 GLY A CA  1 
ATOM   950   C  C   . GLY A  1 130 ? 27.324  45.680  -6.459  1.00 40.73  ? 130 GLY A C   1 
ATOM   951   O  O   . GLY A  1 130 ? 27.563  45.492  -7.651  1.00 42.47  ? 130 GLY A O   1 
ATOM   952   N  N   . ASN A  1 131 ? 27.514  44.742  -5.529  1.00 39.28  ? 131 ASN A N   1 
ATOM   953   C  CA  . ASN A  1 131 ? 27.868  43.351  -5.862  1.00 39.70  ? 131 ASN A CA  1 
ATOM   954   C  C   . ASN A  1 131 ? 26.902  42.377  -5.186  1.00 38.41  ? 131 ASN A C   1 
ATOM   955   O  O   . ASN A  1 131 ? 26.081  42.792  -4.357  1.00 36.99  ? 131 ASN A O   1 
ATOM   956   C  CB  . ASN A  1 131 ? 29.334  43.031  -5.499  1.00 39.86  ? 131 ASN A CB  1 
ATOM   957   C  CG  . ASN A  1 131 ? 29.692  43.371  -4.057  1.00 38.21  ? 131 ASN A CG  1 
ATOM   958   O  OD1 . ASN A  1 131 ? 28.923  43.145  -3.119  1.00 36.58  ? 131 ASN A OD1 1 
ATOM   959   N  ND2 . ASN A  1 131 ? 30.888  43.908  -3.877  1.00 38.82  ? 131 ASN A ND2 1 
ATOM   960   N  N   . GLU A  1 132 ? 27.004  41.091  -5.538  1.00 39.08  ? 132 GLU A N   1 
ATOM   961   C  CA  . GLU A  1 132 ? 26.130  40.058  -4.958  1.00 38.27  ? 132 GLU A CA  1 
ATOM   962   C  C   . GLU A  1 132 ? 26.212  40.029  -3.440  1.00 36.37  ? 132 GLU A C   1 
ATOM   963   O  O   . GLU A  1 132 ? 25.200  39.945  -2.765  1.00 35.26  ? 132 GLU A O   1 
ATOM   964   C  CB  . GLU A  1 132 ? 26.458  38.656  -5.479  1.00 39.45  ? 132 GLU A CB  1 
ATOM   965   C  CG  . GLU A  1 132 ? 25.373  37.639  -5.132  1.00 39.04  ? 132 GLU A CG  1 
ATOM   966   C  CD  . GLU A  1 132 ? 25.727  36.203  -5.470  1.00 40.28  ? 132 GLU A CD  1 
ATOM   967   O  OE1 . GLU A  1 132 ? 26.735  35.954  -6.166  1.00 41.71  ? 132 GLU A OE1 1 
ATOM   968   O  OE2 . GLU A  1 132 ? 24.970  35.313  -5.025  1.00 39.97  ? 132 GLU A OE2 1 
ATOM   969   N  N   . GLU A  1 133 ? 27.428  40.102  -2.916  1.00 36.30  ? 133 GLU A N   1 
ATOM   970   C  CA  . GLU A  1 133 ? 27.653  40.011  -1.474  1.00 34.84  ? 133 GLU A CA  1 
ATOM   971   C  C   . GLU A  1 133 ? 27.068  41.204  -0.677  1.00 33.59  ? 133 GLU A C   1 
ATOM   972   O  O   . GLU A  1 133 ? 26.758  41.063  0.517   1.00 32.34  ? 133 GLU A O   1 
ATOM   973   C  CB  . GLU A  1 133 ? 29.154  39.822  -1.196  1.00 35.48  ? 133 GLU A CB  1 
ATOM   974   C  CG  . GLU A  1 133 ? 29.485  39.104  0.100   1.00 34.59  ? 133 GLU A CG  1 
ATOM   975   C  CD  . GLU A  1 133 ? 28.891  37.707  0.163   1.00 34.72  ? 133 GLU A CD  1 
ATOM   976   O  OE1 . GLU A  1 133 ? 29.030  36.939  -0.819  1.00 36.37  ? 133 GLU A OE1 1 
ATOM   977   O  OE2 . GLU A  1 133 ? 28.247  37.388  1.183   1.00 33.66  ? 133 GLU A OE2 1 
ATOM   978   N  N   . SER A  1 134 ? 26.904  42.360  -1.318  1.00 34.19  ? 134 SER A N   1 
ATOM   979   C  CA  . SER A  1 134 ? 26.201  43.494  -0.698  1.00 33.45  ? 134 SER A CA  1 
ATOM   980   C  C   . SER A  1 134 ? 24.762  43.121  -0.298  1.00 32.73  ? 134 SER A C   1 
ATOM   981   O  O   . SER A  1 134 ? 24.299  43.506  0.773   1.00 31.60  ? 134 SER A O   1 
ATOM   982   C  CB  . SER A  1 134 ? 26.183  44.704  -1.632  1.00 34.66  ? 134 SER A CB  1 
ATOM   983   O  OG  . SER A  1 134 ? 25.741  45.864  -0.948  1.00 34.15  ? 134 SER A OG  1 
ATOM   984   N  N   . THR A  1 135 ? 24.098  42.327  -1.139  1.00 33.55  ? 135 THR A N   1 
ATOM   985   C  CA  . THR A  1 135 ? 22.702  41.921  -0.924  1.00 33.38  ? 135 THR A CA  1 
ATOM   986   C  C   . THR A  1 135 ? 22.514  40.835  0.152   1.00 32.43  ? 135 THR A C   1 
ATOM   987   O  O   . THR A  1 135 ? 21.375  40.570  0.584   1.00 32.12  ? 135 THR A O   1 
ATOM   988   C  CB  . THR A  1 135 ? 22.035  41.466  -2.247  1.00 34.92  ? 135 THR A CB  1 
ATOM   989   O  OG1 . THR A  1 135 ? 22.570  40.207  -2.681  1.00 35.42  ? 135 THR A OG1 1 
ATOM   990   C  CG2 . THR A  1 135 ? 22.232  42.504  -3.340  1.00 36.23  ? 135 THR A CG2 1 
ATOM   991   N  N   . LYS A  1 136 ? 23.626  40.239  0.596   1.00 32.11  ? 136 LYS A N   1 
ATOM   992   C  CA  . LYS A  1 136 ? 23.634  39.118  1.514   1.00 31.39  ? 136 LYS A CA  1 
ATOM   993   C  C   . LYS A  1 136 ? 24.183  39.524  2.884   1.00 30.14  ? 136 LYS A C   1 
ATOM   994   O  O   . LYS A  1 136 ? 23.471  39.431  3.880   1.00 29.29  ? 136 LYS A O   1 
ATOM   995   C  CB  . LYS A  1 136 ? 24.453  37.981  0.899   1.00 32.38  ? 136 LYS A CB  1 
ATOM   996   C  CG  . LYS A  1 136 ? 23.817  37.422  -0.366  1.00 33.94  ? 136 LYS A CG  1 
ATOM   997   C  CD  . LYS A  1 136 ? 24.752  36.518  -1.147  1.00 35.39  ? 136 LYS A CD  1 
ATOM   998   C  CE  . LYS A  1 136 ? 24.958  35.182  -0.455  1.00 35.27  ? 136 LYS A CE  1 
ATOM   999   N  NZ  . LYS A  1 136 ? 25.767  34.281  -1.319  1.00 37.06  ? 136 LYS A NZ  1 
ATOM   1000  N  N   . THR A  1 137 ? 25.435  39.985  2.915   1.00 30.30  ? 137 THR A N   1 
ATOM   1001  C  CA  . THR A  1 137 ? 26.146  40.320  4.161   1.00 29.45  ? 137 THR A CA  1 
ATOM   1002  C  C   . THR A  1 137 ? 26.464  41.810  4.352   1.00 29.39  ? 137 THR A C   1 
ATOM   1003  O  O   . THR A  1 137 ? 26.763  42.231  5.460   1.00 28.87  ? 137 THR A O   1 
ATOM   1004  C  CB  . THR A  1 137 ? 27.481  39.563  4.241   1.00 30.02  ? 137 THR A CB  1 
ATOM   1005  O  OG1 . THR A  1 137 ? 28.337  39.982  3.171   1.00 31.23  ? 137 THR A OG1 1 
ATOM   1006  C  CG2 . THR A  1 137 ? 27.248  38.059  4.144   1.00 30.29  ? 137 THR A CG2 1 
ATOM   1007  N  N   . GLY A  1 138 ? 26.415  42.596  3.281   1.00 30.11  ? 138 GLY A N   1 
ATOM   1008  C  CA  . GLY A  1 138 ? 26.823  43.990  3.332   1.00 30.44  ? 138 GLY A CA  1 
ATOM   1009  C  C   . GLY A  1 138 ? 28.327  44.215  3.273   1.00 31.06  ? 138 GLY A C   1 
ATOM   1010  O  O   . GLY A  1 138 ? 28.785  45.321  3.549   1.00 31.34  ? 138 GLY A O   1 
ATOM   1011  N  N   . ASN A  1 139 ? 29.083  43.174  2.910   1.00 31.44  ? 139 ASN A N   1 
ATOM   1012  C  CA  . ASN A  1 139 ? 30.547  43.233  2.742   1.00 32.54  ? 139 ASN A CA  1 
ATOM   1013  C  C   . ASN A  1 139 ? 31.296  43.686  4.005   1.00 32.31  ? 139 ASN A C   1 
ATOM   1014  O  O   . ASN A  1 139 ? 32.275  44.416  3.916   1.00 33.37  ? 139 ASN A O   1 
ATOM   1015  C  CB  . ASN A  1 139 ? 30.915  44.115  1.523   1.00 33.98  ? 139 ASN A CB  1 
ATOM   1016  C  CG  . ASN A  1 139 ? 30.537  43.468  0.206   1.00 34.78  ? 139 ASN A CG  1 
ATOM   1017  O  OD1 . ASN A  1 139 ? 31.024  42.382  -0.118  1.00 35.36  ? 139 ASN A OD1 1 
ATOM   1018  N  ND2 . ASN A  1 139 ? 29.669  44.122  -0.561  1.00 35.05  ? 139 ASN A ND2 1 
ATOM   1019  N  N   . ALA A  1 140 ? 30.831  43.241  5.173   1.00 31.16  ? 140 ALA A N   1 
ATOM   1020  C  CA  . ALA A  1 140 ? 31.384  43.700  6.457   1.00 31.10  ? 140 ALA A CA  1 
ATOM   1021  C  C   . ALA A  1 140 ? 32.578  42.865  6.948   1.00 31.72  ? 140 ALA A C   1 
ATOM   1022  O  O   . ALA A  1 140 ? 33.095  43.116  8.038   1.00 31.80  ? 140 ALA A O   1 
ATOM   1023  C  CB  . ALA A  1 140 ? 30.295  43.752  7.518   1.00 29.83  ? 140 ALA A CB  1 
ATOM   1024  N  N   . GLY A  1 141 ? 33.020  41.893  6.144   1.00 32.38  ? 141 GLY A N   1 
ATOM   1025  C  CA  . GLY A  1 141 ? 34.275  41.188  6.389   1.00 33.43  ? 141 GLY A CA  1 
ATOM   1026  C  C   . GLY A  1 141 ? 34.087  40.093  7.412   1.00 32.63  ? 141 GLY A C   1 
ATOM   1027  O  O   . GLY A  1 141 ? 32.977  39.625  7.622   1.00 31.46  ? 141 GLY A O   1 
ATOM   1028  N  N   . SER A  1 142 ? 35.176  39.690  8.055   1.00 33.56  ? 142 SER A N   1 
ATOM   1029  C  CA  . SER A  1 142 ? 35.147  38.545  8.959   1.00 33.15  ? 142 SER A CA  1 
ATOM   1030  C  C   . SER A  1 142 ? 34.395  38.865  10.246  1.00 31.68  ? 142 SER A C   1 
ATOM   1031  O  O   . SER A  1 142 ? 34.161  40.032  10.584  1.00 31.22  ? 142 SER A O   1 
ATOM   1032  C  CB  . SER A  1 142 ? 36.568  38.081  9.286   1.00 34.95  ? 142 SER A CB  1 
ATOM   1033  O  OG  . SER A  1 142 ? 37.257  39.098  9.977   1.00 35.62  ? 142 SER A OG  1 
ATOM   1034  N  N   . ARG A  1 143 ? 34.042  37.800  10.956  1.00 31.05  ? 143 ARG A N   1 
ATOM   1035  C  CA  . ARG A  1 143 ? 33.305  37.879  12.207  1.00 29.86  ? 143 ARG A CA  1 
ATOM   1036  C  C   . ARG A  1 143 ? 34.323  37.989  13.338  1.00 30.64  ? 143 ARG A C   1 
ATOM   1037  O  O   . ARG A  1 143 ? 34.959  36.993  13.682  1.00 31.49  ? 143 ARG A O   1 
ATOM   1038  C  CB  . ARG A  1 143 ? 32.414  36.633  12.353  1.00 29.14  ? 143 ARG A CB  1 
ATOM   1039  C  CG  . ARG A  1 143 ? 31.451  36.478  11.172  1.00 28.69  ? 143 ARG A CG  1 
ATOM   1040  C  CD  . ARG A  1 143 ? 30.619  35.210  11.170  1.00 28.39  ? 143 ARG A CD  1 
ATOM   1041  N  NE  . ARG A  1 143 ? 29.844  35.105  9.922   1.00 28.42  ? 143 ARG A NE  1 
ATOM   1042  C  CZ  . ARG A  1 143 ? 28.768  34.330  9.726   1.00 28.09  ? 143 ARG A CZ  1 
ATOM   1043  N  NH1 . ARG A  1 143 ? 28.270  33.556  10.696  1.00 27.71  ? 143 ARG A NH1 1 
ATOM   1044  N  NH2 . ARG A  1 143 ? 28.166  34.343  8.538   1.00 28.37  ? 143 ARG A NH2 1 
ATOM   1045  N  N   . LEU A  1 144 ? 34.485  39.190  13.899  1.00 30.59  ? 144 LEU A N   1 
ATOM   1046  C  CA  . LEU A  1 144 ? 35.497  39.433  14.947  1.00 31.75  ? 144 LEU A CA  1 
ATOM   1047  C  C   . LEU A  1 144 ? 35.121  38.881  16.315  1.00 31.17  ? 144 LEU A C   1 
ATOM   1048  O  O   . LEU A  1 144 ? 35.990  38.390  17.039  1.00 32.26  ? 144 LEU A O   1 
ATOM   1049  C  CB  . LEU A  1 144 ? 35.793  40.929  15.105  1.00 32.44  ? 144 LEU A CB  1 
ATOM   1050  C  CG  . LEU A  1 144 ? 36.380  41.684  13.916  1.00 33.38  ? 144 LEU A CG  1 
ATOM   1051  C  CD1 . LEU A  1 144 ? 36.531  43.149  14.294  1.00 34.14  ? 144 LEU A CD1 1 
ATOM   1052  C  CD2 . LEU A  1 144 ? 37.716  41.111  13.485  1.00 35.11  ? 144 LEU A CD2 1 
ATOM   1053  N  N   . ALA A  1 145 ? 33.843  39.002  16.687  1.00 29.54  ? 145 ALA A N   1 
ATOM   1054  C  CA  . ALA A  1 145 ? 33.364  38.474  17.966  1.00 29.07  ? 145 ALA A CA  1 
ATOM   1055  C  C   . ALA A  1 145 ? 31.882  38.177  17.896  1.00 27.43  ? 145 ALA A C   1 
ATOM   1056  O  O   . ALA A  1 145 ? 31.144  38.823  17.147  1.00 26.69  ? 145 ALA A O   1 
ATOM   1057  C  CB  . ALA A  1 145 ? 33.648  39.454  19.091  1.00 29.83  ? 145 ALA A CB  1 
ATOM   1058  N  N   . ALA A  1 146 ? 31.459  37.193  18.676  1.00 27.02  ? 146 ALA A N   1 
ATOM   1059  C  CA  . ALA A  1 146 ? 30.081  36.718  18.632  1.00 25.77  ? 146 ALA A CA  1 
ATOM   1060  C  C   . ALA A  1 146 ? 29.654  36.161  19.980  1.00 25.71  ? 146 ALA A C   1 
ATOM   1061  O  O   . ALA A  1 146 ? 30.486  35.824  20.830  1.00 26.60  ? 146 ALA A O   1 
ATOM   1062  C  CB  . ALA A  1 146 ? 29.930  35.667  17.547  1.00 25.53  ? 146 ALA A CB  1 
ATOM   1063  N  N   . GLY A  1 147 ? 28.343  36.101  20.179  1.00 24.81  ? 147 GLY A N   1 
ATOM   1064  C  CA  . GLY A  1 147 ? 27.782  35.429  21.339  1.00 24.83  ? 147 GLY A CA  1 
ATOM   1065  C  C   . GLY A  1 147 ? 26.343  35.047  21.093  1.00 23.98  ? 147 GLY A C   1 
ATOM   1066  O  O   . GLY A  1 147 ? 25.670  35.645  20.253  1.00 23.40  ? 147 GLY A O   1 
ATOM   1067  N  N   . VAL A  1 148 ? 25.873  34.059  21.840  1.00 24.09  ? 148 VAL A N   1 
ATOM   1068  C  CA  . VAL A  1 148 ? 24.472  33.659  21.787  1.00 23.66  ? 148 VAL A CA  1 
ATOM   1069  C  C   . VAL A  1 148 ? 23.656  34.621  22.669  1.00 23.68  ? 148 VAL A C   1 
ATOM   1070  O  O   . VAL A  1 148 ? 24.046  34.951  23.797  1.00 24.21  ? 148 VAL A O   1 
ATOM   1071  C  CB  . VAL A  1 148 ? 24.280  32.191  22.212  1.00 24.03  ? 148 VAL A CB  1 
ATOM   1072  C  CG1 . VAL A  1 148 ? 22.811  31.766  22.083  1.00 23.79  ? 148 VAL A CG1 1 
ATOM   1073  C  CG2 . VAL A  1 148 ? 25.171  31.277  21.379  1.00 24.39  ? 148 VAL A CG2 1 
ATOM   1074  N  N   . ILE A  1 149 ? 22.525  35.068  22.139  1.00 23.34  ? 149 ILE A N   1 
ATOM   1075  C  CA  . ILE A  1 149 ? 21.659  36.017  22.834  1.00 23.65  ? 149 ILE A CA  1 
ATOM   1076  C  C   . ILE A  1 149 ? 20.806  35.223  23.827  1.00 24.07  ? 149 ILE A C   1 
ATOM   1077  O  O   . ILE A  1 149 ? 20.055  34.336  23.434  1.00 23.94  ? 149 ILE A O   1 
ATOM   1078  C  CB  . ILE A  1 149 ? 20.769  36.804  21.844  1.00 23.39  ? 149 ILE A CB  1 
ATOM   1079  C  CG1 . ILE A  1 149 ? 21.646  37.567  20.845  1.00 23.16  ? 149 ILE A CG1 1 
ATOM   1080  C  CG2 . ILE A  1 149 ? 19.835  37.751  22.604  1.00 23.95  ? 149 ILE A CG2 1 
ATOM   1081  C  CD1 . ILE A  1 149 ? 20.892  38.165  19.675  1.00 23.02  ? 149 ILE A CD1 1 
ATOM   1082  N  N   . GLY A  1 150 ? 20.942  35.532  25.111  1.00 24.80  ? 150 GLY A N   1 
ATOM   1083  C  CA  . GLY A  1 150 ? 20.277  34.764  26.165  1.00 25.47  ? 150 GLY A CA  1 
ATOM   1084  C  C   . GLY A  1 150 ? 19.318  35.598  26.980  1.00 26.26  ? 150 GLY A C   1 
ATOM   1085  O  O   . GLY A  1 150 ? 19.410  36.823  26.999  1.00 26.47  ? 150 GLY A O   1 
ATOM   1086  N  N   . ILE A  1 151 ? 18.411  34.916  27.671  1.00 26.98  ? 151 ILE A N   1 
ATOM   1087  C  CA  . ILE A  1 151 ? 17.397  35.560  28.502  1.00 28.10  ? 151 ILE A CA  1 
ATOM   1088  C  C   . ILE A  1 151 ? 18.051  36.111  29.757  1.00 29.12  ? 151 ILE A C   1 
ATOM   1089  O  O   . ILE A  1 151 ? 18.778  35.396  30.430  1.00 29.40  ? 151 ILE A O   1 
ATOM   1090  C  CB  . ILE A  1 151 ? 16.261  34.589  28.911  1.00 28.74  ? 151 ILE A CB  1 
ATOM   1091  C  CG1 . ILE A  1 151 ? 15.550  34.064  27.659  1.00 28.19  ? 151 ILE A CG1 1 
ATOM   1092  C  CG2 . ILE A  1 151 ? 15.254  35.302  29.809  1.00 30.07  ? 151 ILE A CG2 1 
ATOM   1093  C  CD1 . ILE A  1 151 ? 14.537  32.966  27.904  1.00 28.93  ? 151 ILE A CD1 1 
ATOM   1094  N  N   . ALA A  1 152 ? 17.766  37.373  30.064  1.00 29.98  ? 152 ALA A N   1 
ATOM   1095  C  CA  . ALA A  1 152 ? 18.329  38.061  31.223  1.00 31.41  ? 152 ALA A CA  1 
ATOM   1096  C  C   . ALA A  1 152 ? 17.249  38.336  32.268  1.00 33.11  ? 152 ALA A C   1 
ATOM   1097  O  O   . ALA A  1 152 ? 16.053  38.362  31.954  1.00 33.17  ? 152 ALA A O   1 
ATOM   1098  C  CB  . ALA A  1 152 ? 18.976  39.366  30.789  1.00 31.46  ? 152 ALA A CB  1 
ATOM   1099  N  N   . GLN A  1 153 ? 17.692  38.549  33.504  1.00 34.73  ? 153 GLN A N   1 
ATOM   1100  C  CA  . GLN A  1 153 ? 16.795  38.879  34.612  1.00 36.80  ? 153 GLN A CA  1 
ATOM   1101  C  C   . GLN A  1 153 ? 16.312  40.326  34.510  1.00 37.97  ? 153 GLN A C   1 
ATOM   1102  O  O   . GLN A  1 153 ? 17.075  41.244  34.198  1.00 38.10  ? 153 GLN A O   1 
ATOM   1103  C  CB  . GLN A  1 153 ? 17.496  38.673  35.957  1.00 38.27  ? 153 GLN A CB  1 
ATOM   1104  C  CG  . GLN A  1 153 ? 16.546  38.696  37.152  1.00 40.34  ? 153 GLN A CG  1 
ATOM   1105  C  CD  . GLN A  1 153 ? 17.267  38.577  38.474  1.00 42.03  ? 153 GLN A CD  1 
ATOM   1106  O  OE1 . GLN A  1 153 ? 18.217  39.312  38.740  1.00 42.81  ? 153 GLN A OE1 1 
ATOM   1107  N  NE2 . GLN A  1 153 ? 16.821  37.653  39.313  1.00 42.90  ? 153 GLN A NE2 1 
ATOM   1108  O  OXT . GLN A  1 153 ? 15.139  40.613  34.769  1.00 39.24  ? 153 GLN A OXT 1 
ATOM   1109  N  N   . ALA B  1 1   ? 12.876  17.678  13.981  1.00 39.57  ? 1   ALA F N   1 
ATOM   1110  C  CA  . ALA B  1 1   ? 12.312  19.044  13.741  1.00 39.37  ? 1   ALA F CA  1 
ATOM   1111  C  C   . ALA B  1 1   ? 13.169  20.110  14.447  1.00 36.98  ? 1   ALA F C   1 
ATOM   1112  O  O   . ALA B  1 1   ? 14.243  20.445  13.933  1.00 36.78  ? 1   ALA F O   1 
ATOM   1113  C  CB  . ALA B  1 1   ? 10.843  19.104  14.157  1.00 40.33  ? 1   ALA F CB  1 
ATOM   1114  N  N   . THR B  1 2   ? 12.752  20.598  15.622  1.00 35.44  ? 2   THR F N   1 
ATOM   1115  C  CA  . THR B  1 2   ? 13.460  21.689  16.306  1.00 33.35  ? 2   THR F CA  1 
ATOM   1116  C  C   . THR B  1 2   ? 14.776  21.164  16.926  1.00 31.60  ? 2   THR F C   1 
ATOM   1117  O  O   . THR B  1 2   ? 14.807  20.087  17.542  1.00 31.21  ? 2   THR F O   1 
ATOM   1118  C  CB  . THR B  1 2   ? 12.584  22.380  17.386  1.00 32.93  ? 2   THR F CB  1 
ATOM   1119  O  OG1 . THR B  1 2   ? 11.208  22.380  16.983  1.00 34.83  ? 2   THR F OG1 1 
ATOM   1120  C  CG2 . THR B  1 2   ? 13.006  23.817  17.585  1.00 32.17  ? 2   THR F CG2 1 
ATOM   1121  N  N   . LYS B  1 3   ? 15.852  21.922  16.719  1.00 30.43  ? 3   LYS F N   1 
ATOM   1122  C  CA  . LYS B  1 3   ? 17.179  21.569  17.222  1.00 29.16  ? 3   LYS F CA  1 
ATOM   1123  C  C   . LYS B  1 3   ? 17.798  22.752  17.933  1.00 27.63  ? 3   LYS F C   1 
ATOM   1124  O  O   . LYS B  1 3   ? 17.556  23.912  17.567  1.00 27.69  ? 3   LYS F O   1 
ATOM   1125  C  CB  . LYS B  1 3   ? 18.111  21.112  16.099  1.00 30.06  ? 3   LYS F CB  1 
ATOM   1126  C  CG  . LYS B  1 3   ? 17.689  19.809  15.450  1.00 31.61  ? 3   LYS F CG  1 
ATOM   1127  C  CD  . LYS B  1 3   ? 18.663  19.375  14.360  1.00 32.75  ? 3   LYS F CD  1 
ATOM   1128  C  CE  . LYS B  1 3   ? 18.023  18.344  13.441  1.00 34.80  ? 3   LYS F CE  1 
ATOM   1129  N  NZ  . LYS B  1 3   ? 19.018  17.594  12.620  1.00 36.04  ? 3   LYS F NZ  1 
ATOM   1130  N  N   . ALA B  1 4   ? 18.600  22.433  18.946  1.00 26.24  ? 4   ALA F N   1 
ATOM   1131  C  CA  . ALA B  1 4   ? 19.366  23.413  19.685  1.00 25.16  ? 4   ALA F CA  1 
ATOM   1132  C  C   . ALA B  1 4   ? 20.737  22.830  20.005  1.00 24.63  ? 4   ALA F C   1 
ATOM   1133  O  O   . ALA B  1 4   ? 20.962  21.616  19.896  1.00 24.76  ? 4   ALA F O   1 
ATOM   1134  C  CB  . ALA B  1 4   ? 18.651  23.806  20.966  1.00 24.43  ? 4   ALA F CB  1 
ATOM   1135  N  N   . VAL B  1 5   ? 21.637  23.707  20.419  1.00 24.14  ? 5   VAL F N   1 
ATOM   1136  C  CA  . VAL B  1 5   ? 23.010  23.321  20.702  1.00 23.96  ? 5   VAL F CA  1 
ATOM   1137  C  C   . VAL B  1 5   ? 23.587  24.232  21.770  1.00 23.37  ? 5   VAL F C   1 
ATOM   1138  O  O   . VAL B  1 5   ? 23.167  25.384  21.902  1.00 23.21  ? 5   VAL F O   1 
ATOM   1139  C  CB  . VAL B  1 5   ? 23.853  23.368  19.412  1.00 24.90  ? 5   VAL F CB  1 
ATOM   1140  C  CG1 . VAL B  1 5   ? 24.063  24.804  18.931  1.00 25.24  ? 5   VAL F CG1 1 
ATOM   1141  C  CG2 . VAL B  1 5   ? 25.183  22.637  19.594  1.00 25.05  ? 5   VAL F CG2 1 
ATOM   1142  N  N   . CYS B  1 6   ? 24.541  23.695  22.530  1.00 23.19  ? 6   CYS F N   1 
ATOM   1143  C  CA  . CYS B  1 6   ? 25.189  24.425  23.609  1.00 22.97  ? 6   CYS F CA  1 
ATOM   1144  C  C   . CYS B  1 6   ? 26.671  24.061  23.699  1.00 23.28  ? 6   CYS F C   1 
ATOM   1145  O  O   . CYS B  1 6   ? 27.022  22.873  23.785  1.00 23.36  ? 6   CYS F O   1 
ATOM   1146  C  CB  . CYS B  1 6   ? 24.487  24.120  24.933  1.00 22.44  ? 6   CYS F CB  1 
ATOM   1147  S  SG  . CYS B  1 6   ? 25.167  25.014  26.347  1.00 22.60  ? 6   CYS F SG  1 
ATOM   1148  N  N   . VAL B  1 7   ? 27.523  25.089  23.666  1.00 23.70  ? 7   VAL F N   1 
ATOM   1149  C  CA  . VAL B  1 7   ? 28.961  24.944  23.883  1.00 24.28  ? 7   VAL F CA  1 
ATOM   1150  C  C   . VAL B  1 7   ? 29.253  25.245  25.352  1.00 24.05  ? 7   VAL F C   1 
ATOM   1151  O  O   . VAL B  1 7   ? 29.062  26.370  25.813  1.00 24.17  ? 7   VAL F O   1 
ATOM   1152  C  CB  . VAL B  1 7   ? 29.772  25.895  22.982  1.00 25.25  ? 7   VAL F CB  1 
ATOM   1153  C  CG1 . VAL B  1 7   ? 31.273  25.679  23.184  1.00 26.09  ? 7   VAL F CG1 1 
ATOM   1154  C  CG2 . VAL B  1 7   ? 29.393  25.692  21.521  1.00 25.70  ? 7   VAL F CG2 1 
ATOM   1155  N  N   . LEU B  1 8   ? 29.708  24.233  26.081  1.00 24.03  ? 8   LEU F N   1 
ATOM   1156  C  CA  . LEU B  1 8   ? 30.025  24.362  27.503  1.00 23.96  ? 8   LEU F CA  1 
ATOM   1157  C  C   . LEU B  1 8   ? 31.491  24.761  27.673  1.00 25.02  ? 8   LEU F C   1 
ATOM   1158  O  O   . LEU B  1 8   ? 32.369  24.101  27.126  1.00 25.51  ? 8   LEU F O   1 
ATOM   1159  C  CB  . LEU B  1 8   ? 29.770  23.039  28.205  1.00 23.65  ? 8   LEU F CB  1 
ATOM   1160  C  CG  . LEU B  1 8   ? 28.313  22.582  28.249  1.00 22.89  ? 8   LEU F CG  1 
ATOM   1161  C  CD1 . LEU B  1 8   ? 28.260  21.112  28.620  1.00 22.97  ? 8   LEU F CD1 1 
ATOM   1162  C  CD2 . LEU B  1 8   ? 27.536  23.380  29.271  1.00 22.52  ? 8   LEU F CD2 1 
ATOM   1163  N  N   . LYS B  1 9   ? 31.724  25.867  28.385  1.00 25.41  ? 9   LYS F N   1 
ATOM   1164  C  CA  . LYS B  1 9   ? 33.063  26.388  28.687  1.00 26.73  ? 9   LYS F CA  1 
ATOM   1165  C  C   . LYS B  1 9   ? 33.072  26.918  30.118  1.00 26.80  ? 9   LYS F C   1 
ATOM   1166  O  O   . LYS B  1 9   ? 32.044  27.373  30.635  1.00 26.01  ? 9   LYS F O   1 
ATOM   1167  C  CB  . LYS B  1 9   ? 33.450  27.547  27.756  1.00 27.76  ? 9   LYS F CB  1 
ATOM   1168  C  CG  . LYS B  1 9   ? 33.518  27.196  26.281  1.00 28.06  ? 9   LYS F CG  1 
ATOM   1169  C  CD  . LYS B  1 9   ? 34.051  28.364  25.452  1.00 29.33  ? 9   LYS F CD  1 
ATOM   1170  C  CE  . LYS B  1 9   ? 33.959  28.084  23.957  0.50 29.56  ? 9   LYS F CE  1 
ATOM   1171  N  NZ  . LYS B  1 9   ? 34.782  26.906  23.562  0.50 30.14  ? 9   LYS F NZ  1 
ATOM   1172  N  N   . GLY B  1 10  ? 34.235  26.860  30.749  1.00 27.71  ? 10  GLY F N   1 
ATOM   1173  C  CA  . GLY B  1 10  ? 34.412  27.457  32.071  1.00 28.30  ? 10  GLY F CA  1 
ATOM   1174  C  C   . GLY B  1 10  ? 35.827  27.958  32.274  1.00 30.00  ? 10  GLY F C   1 
ATOM   1175  O  O   . GLY B  1 10  ? 36.569  28.148  31.307  1.00 30.62  ? 10  GLY F O   1 
ATOM   1176  N  N   . ASP B  1 11  ? 36.171  28.160  33.545  1.00 30.83  ? 11  ASP F N   1 
ATOM   1177  C  CA  A ASP B  1 11  ? 37.515  28.618  33.919  0.50 32.91  ? 11  ASP F CA  1 
ATOM   1178  C  CA  B ASP B  1 11  ? 37.494  28.609  33.981  0.50 32.85  ? 11  ASP F CA  1 
ATOM   1179  C  C   . ASP B  1 11  ? 38.482  27.444  34.037  1.00 33.46  ? 11  ASP F C   1 
ATOM   1180  O  O   . ASP B  1 11  ? 39.690  27.628  33.902  1.00 35.23  ? 11  ASP F O   1 
ATOM   1181  C  CB  A ASP B  1 11  ? 37.483  29.418  35.224  0.50 34.02  ? 11  ASP F CB  1 
ATOM   1182  C  CB  B ASP B  1 11  ? 37.369  29.234  35.375  0.50 33.71  ? 11  ASP F CB  1 
ATOM   1183  C  CG  A ASP B  1 11  ? 36.789  30.763  35.071  0.50 34.19  ? 11  ASP F CG  1 
ATOM   1184  C  CG  B ASP B  1 11  ? 38.614  29.973  35.798  0.50 36.10  ? 11  ASP F CG  1 
ATOM   1185  O  OD1 A ASP B  1 11  ? 36.842  31.357  33.967  0.50 34.28  ? 11  ASP F OD1 1 
ATOM   1186  O  OD1 B ASP B  1 11  ? 39.019  30.901  35.070  0.50 37.05  ? 11  ASP F OD1 1 
ATOM   1187  O  OD2 A ASP B  1 11  ? 36.189  31.226  36.065  0.50 34.45  ? 11  ASP F OD2 1 
ATOM   1188  O  OD2 B ASP B  1 11  ? 39.184  29.629  36.858  0.50 37.20  ? 11  ASP F OD2 1 
ATOM   1189  N  N   . GLY B  1 12  ? 37.955  26.252  34.296  1.00 32.20  ? 12  GLY F N   1 
ATOM   1190  C  CA  . GLY B  1 12  ? 38.741  25.032  34.380  1.00 32.78  ? 12  GLY F CA  1 
ATOM   1191  C  C   . GLY B  1 12  ? 38.788  24.283  33.051  1.00 32.20  ? 12  GLY F C   1 
ATOM   1192  O  O   . GLY B  1 12  ? 38.542  24.880  31.968  1.00 31.78  ? 12  GLY F O   1 
ATOM   1193  N  N   . PRO B  1 13  ? 39.082  22.964  33.126  1.00 32.33  ? 13  PRO F N   1 
ATOM   1194  C  CA  . PRO B  1 13  ? 39.261  22.150  31.925  1.00 32.28  ? 13  PRO F CA  1 
ATOM   1195  C  C   . PRO B  1 13  ? 37.973  21.587  31.302  1.00 30.53  ? 13  PRO F C   1 
ATOM   1196  O  O   . PRO B  1 13  ? 38.060  20.917  30.273  1.00 30.60  ? 13  PRO F O   1 
ATOM   1197  C  CB  . PRO B  1 13  ? 40.133  20.996  32.432  1.00 33.54  ? 13  PRO F CB  1 
ATOM   1198  C  CG  . PRO B  1 13  ? 39.688  20.811  33.839  1.00 33.16  ? 13  PRO F CG  1 
ATOM   1199  C  CD  . PRO B  1 13  ? 39.373  22.188  34.350  1.00 32.95  ? 13  PRO F CD  1 
ATOM   1200  N  N   . VAL B  1 14  ? 36.805  21.838  31.893  1.00 29.21  ? 14  VAL F N   1 
ATOM   1201  C  CA  . VAL B  1 14  ? 35.584  21.226  31.379  1.00 27.91  ? 14  VAL F CA  1 
ATOM   1202  C  C   . VAL B  1 14  ? 35.172  21.904  30.083  1.00 27.56  ? 14  VAL F C   1 
ATOM   1203  O  O   . VAL B  1 14  ? 34.954  23.116  30.047  1.00 27.43  ? 14  VAL F O   1 
ATOM   1204  C  CB  . VAL B  1 14  ? 34.398  21.281  32.373  1.00 26.77  ? 14  VAL F CB  1 
ATOM   1205  C  CG1 . VAL B  1 14  ? 33.158  20.655  31.744  1.00 25.57  ? 14  VAL F CG1 1 
ATOM   1206  C  CG2 . VAL B  1 14  ? 34.745  20.562  33.671  1.00 27.36  ? 14  VAL F CG2 1 
ATOM   1207  N  N   . GLN B  1 15  ? 35.062  21.118  29.021  1.00 27.72  ? 15  GLN F N   1 
ATOM   1208  C  CA  . GLN B  1 15  ? 34.560  21.632  27.747  1.00 27.48  ? 15  GLN F CA  1 
ATOM   1209  C  C   . GLN B  1 15  ? 33.743  20.582  27.003  1.00 26.76  ? 15  GLN F C   1 
ATOM   1210  O  O   . GLN B  1 15  ? 33.967  19.384  27.125  1.00 27.09  ? 15  GLN F O   1 
ATOM   1211  C  CB  . GLN B  1 15  ? 35.692  22.225  26.871  1.00 29.15  ? 15  GLN F CB  1 
ATOM   1212  C  CG  . GLN B  1 15  ? 36.987  21.484  26.860  1.00 30.89  ? 15  GLN F CG  1 
ATOM   1213  C  CD  . GLN B  1 15  ? 38.128  22.221  26.158  1.00 32.69  ? 15  GLN F CD  1 
ATOM   1214  O  OE1 . GLN B  1 15  ? 37.918  23.111  25.322  1.00 33.20  ? 15  GLN F OE1 1 
ATOM   1215  N  NE2 . GLN B  1 15  ? 39.338  21.839  26.485  1.00 34.19  ? 15  GLN F NE2 1 
ATOM   1216  N  N   . GLY B  1 16  ? 32.755  21.043  26.256  1.00 25.89  ? 16  GLY F N   1 
ATOM   1217  C  CA  . GLY B  1 16  ? 31.878  20.115  25.575  1.00 25.44  ? 16  GLY F CA  1 
ATOM   1218  C  C   . GLY B  1 16  ? 30.855  20.788  24.711  1.00 24.73  ? 16  GLY F C   1 
ATOM   1219  O  O   . GLY B  1 16  ? 30.672  22.007  24.774  1.00 24.38  ? 16  GLY F O   1 
ATOM   1220  N  N   . ILE B  1 17  ? 30.203  19.961  23.902  1.00 24.68  ? 17  ILE F N   1 
ATOM   1221  C  CA  . ILE B  1 17  ? 29.121  20.372  23.026  1.00 24.25  ? 17  ILE F CA  1 
ATOM   1222  C  C   . ILE B  1 17  ? 27.948  19.458  23.323  1.00 23.70  ? 17  ILE F C   1 
ATOM   1223  O  O   . ILE B  1 17  ? 28.088  18.228  23.299  1.00 24.20  ? 17  ILE F O   1 
ATOM   1224  C  CB  . ILE B  1 17  ? 29.522  20.256  21.542  1.00 25.39  ? 17  ILE F CB  1 
ATOM   1225  C  CG1 . ILE B  1 17  ? 30.629  21.274  21.227  1.00 26.02  ? 17  ILE F CG1 1 
ATOM   1226  C  CG2 . ILE B  1 17  ? 28.308  20.451  20.628  1.00 25.33  ? 17  ILE F CG2 1 
ATOM   1227  C  CD1 . ILE B  1 17  ? 31.266  21.113  19.858  1.00 27.46  ? 17  ILE F CD1 1 
ATOM   1228  N  N   . ILE B  1 18  ? 26.797  20.064  23.600  1.00 22.81  ? 18  ILE F N   1 
ATOM   1229  C  CA  . ILE B  1 18  ? 25.577  19.322  23.892  1.00 22.53  ? 18  ILE F CA  1 
ATOM   1230  C  C   . ILE B  1 18  ? 24.525  19.726  22.871  1.00 22.71  ? 18  ILE F C   1 
ATOM   1231  O  O   . ILE B  1 18  ? 24.272  20.912  22.673  1.00 22.33  ? 18  ILE F O   1 
ATOM   1232  C  CB  . ILE B  1 18  ? 25.093  19.577  25.339  1.00 21.67  ? 18  ILE F CB  1 
ATOM   1233  C  CG1 . ILE B  1 18  ? 26.094  18.994  26.350  1.00 21.69  ? 18  ILE F CG1 1 
ATOM   1234  C  CG2 . ILE B  1 18  ? 23.710  18.978  25.588  1.00 21.59  ? 18  ILE F CG2 1 
ATOM   1235  C  CD1 . ILE B  1 18  ? 26.287  17.485  26.269  1.00 22.36  ? 18  ILE F CD1 1 
ATOM   1236  N  N   . ASN B  1 19  ? 23.950  18.713  22.228  1.00 23.48  ? 19  ASN F N   1 
ATOM   1237  C  CA  . ASN B  1 19  ? 22.887  18.861  21.243  1.00 24.09  ? 19  ASN F CA  1 
ATOM   1238  C  C   . ASN B  1 19  ? 21.527  18.556  21.850  1.00 23.94  ? 19  ASN F C   1 
ATOM   1239  O  O   . ASN B  1 19  ? 21.409  17.708  22.734  1.00 23.81  ? 19  ASN F O   1 
ATOM   1240  C  CB  . ASN B  1 19  ? 23.108  17.887  20.094  1.00 25.44  ? 19  ASN F CB  1 
ATOM   1241  C  CG  . ASN B  1 19  ? 24.437  18.086  19.424  1.00 26.00  ? 19  ASN F CG  1 
ATOM   1242  O  OD1 . ASN B  1 19  ? 24.641  19.063  18.699  1.00 26.26  ? 19  ASN F OD1 1 
ATOM   1243  N  ND2 . ASN B  1 19  ? 25.354  17.162  19.659  1.00 26.44  ? 19  ASN F ND2 1 
ATOM   1244  N  N   . PHE B  1 20  ? 20.505  19.241  21.346  1.00 24.20  ? 20  PHE F N   1 
ATOM   1245  C  CA  . PHE B  1 20  ? 19.119  19.002  21.728  1.00 24.49  ? 20  PHE F CA  1 
ATOM   1246  C  C   . PHE B  1 20  ? 18.301  18.780  20.458  1.00 25.78  ? 20  PHE F C   1 
ATOM   1247  O  O   . PHE B  1 20  ? 18.473  19.508  19.480  1.00 25.99  ? 20  PHE F O   1 
ATOM   1248  C  CB  . PHE B  1 20  ? 18.542  20.202  22.482  1.00 23.81  ? 20  PHE F CB  1 
ATOM   1249  C  CG  . PHE B  1 20  ? 19.289  20.562  23.738  1.00 22.82  ? 20  PHE F CG  1 
ATOM   1250  C  CD1 . PHE B  1 20  ? 20.425  21.354  23.684  1.00 22.42  ? 20  PHE F CD1 1 
ATOM   1251  C  CD2 . PHE B  1 20  ? 18.839  20.130  24.975  1.00 22.57  ? 20  PHE F CD2 1 
ATOM   1252  C  CE1 . PHE B  1 20  ? 21.117  21.694  24.841  1.00 21.76  ? 20  PHE F CE1 1 
ATOM   1253  C  CE2 . PHE B  1 20  ? 19.519  20.466  26.137  1.00 21.87  ? 20  PHE F CE2 1 
ATOM   1254  C  CZ  . PHE B  1 20  ? 20.650  21.258  26.073  1.00 21.47  ? 20  PHE F CZ  1 
ATOM   1255  N  N   . GLU B  1 21  ? 17.409  17.796  20.477  1.00 26.78  ? 21  GLU F N   1 
ATOM   1256  C  CA  . GLU B  1 21  ? 16.472  17.587  19.368  1.00 28.44  ? 21  GLU F CA  1 
ATOM   1257  C  C   . GLU B  1 21  ? 15.080  17.207  19.877  1.00 29.17  ? 21  GLU F C   1 
ATOM   1258  O  O   . GLU B  1 21  ? 14.941  16.330  20.724  1.00 29.16  ? 21  GLU F O   1 
ATOM   1259  C  CB  . GLU B  1 21  ? 17.007  16.511  18.421  1.00 29.81  ? 21  GLU F CB  1 
ATOM   1260  C  CG  . GLU B  1 21  ? 16.220  16.382  17.126  1.00 31.74  ? 21  GLU F CG  1 
ATOM   1261  C  CD  . GLU B  1 21  ? 16.880  15.472  16.102  1.00 33.31  ? 21  GLU F CD  1 
ATOM   1262  O  OE1 . GLU B  1 21  ? 17.919  14.853  16.408  1.00 33.21  ? 21  GLU F OE1 1 
ATOM   1263  O  OE2 . GLU B  1 21  ? 16.355  15.367  14.982  1.00 35.10  ? 21  GLU F OE2 1 
ATOM   1264  N  N   . GLN B  1 22  ? 14.055  17.862  19.339  1.00 30.02  ? 22  GLN F N   1 
ATOM   1265  C  CA  . GLN B  1 22  ? 12.673  17.563  19.680  1.00 31.16  ? 22  GLN F CA  1 
ATOM   1266  C  C   . GLN B  1 22  ? 11.901  17.444  18.377  1.00 33.27  ? 22  GLN F C   1 
ATOM   1267  O  O   . GLN B  1 22  ? 11.607  18.448  17.729  1.00 33.46  ? 22  GLN F O   1 
ATOM   1268  C  CB  . GLN B  1 22  ? 12.118  18.665  20.573  1.00 30.24  ? 22  GLN F CB  1 
ATOM   1269  C  CG  . GLN B  1 22  ? 10.732  18.397  21.135  1.00 31.25  ? 22  GLN F CG  1 
ATOM   1270  C  CD  . GLN B  1 22  ? 10.239  19.526  22.025  1.00 30.54  ? 22  GLN F CD  1 
ATOM   1271  O  OE1 . GLN B  1 22  ? 10.547  20.689  21.784  1.00 29.81  ? 22  GLN F OE1 1 
ATOM   1272  N  NE2 . GLN B  1 22  ? 9.476   19.184  23.068  1.00 30.86  ? 22  GLN F NE2 1 
ATOM   1273  N  N   . LYS B  1 23  ? 11.611  16.207  17.986  1.00 35.13  ? 23  LYS F N   1 
ATOM   1274  C  CA  . LYS B  1 23  ? 10.939  15.919  16.713  1.00 37.62  ? 23  LYS F CA  1 
ATOM   1275  C  C   . LYS B  1 23  ? 9.505   16.440  16.648  1.00 39.07  ? 23  LYS F C   1 
ATOM   1276  O  O   . LYS B  1 23  ? 9.036   16.800  15.569  1.00 40.54  ? 23  LYS F O   1 
ATOM   1277  C  CB  . LYS B  1 23  ? 10.954  14.413  16.416  1.00 39.32  ? 23  LYS F CB  1 
ATOM   1278  C  CG  . LYS B  1 23  ? 12.346  13.854  16.142  0.50 38.83  ? 23  LYS F CG  1 
ATOM   1279  C  CD  . LYS B  1 23  ? 12.300  12.366  15.834  0.50 40.85  ? 23  LYS F CD  1 
ATOM   1280  C  CE  . LYS B  1 23  ? 13.632  11.874  15.290  0.50 40.92  ? 23  LYS F CE  1 
ATOM   1281  N  NZ  . LYS B  1 23  ? 14.772  12.335  16.129  0.50 38.52  ? 23  LYS F NZ  1 
ATOM   1282  N  N   . GLU B  1 24  ? 8.817   16.472  17.791  1.00 39.03  ? 24  GLU F N   1 
ATOM   1283  C  CA  . GLU B  1 24  ? 7.438   16.979  17.870  1.00 40.54  ? 24  GLU F CA  1 
ATOM   1284  C  C   . GLU B  1 24  ? 7.245   17.783  19.146  1.00 39.16  ? 24  GLU F C   1 
ATOM   1285  O  O   . GLU B  1 24  ? 7.822   17.447  20.181  1.00 37.74  ? 24  GLU F O   1 
ATOM   1286  C  CB  . GLU B  1 24  ? 6.436   15.820  17.808  1.00 43.05  ? 24  GLU F CB  1 
ATOM   1287  C  CG  . GLU B  1 24  ? 6.211   15.225  16.413  1.00 45.51  ? 24  GLU F CG  1 
ATOM   1288  C  CD  . GLU B  1 24  ? 5.526   16.171  15.424  1.00 46.89  ? 24  GLU F CD  1 
ATOM   1289  O  OE1 . GLU B  1 24  ? 5.211   17.338  15.764  1.00 46.16  ? 24  GLU F OE1 1 
ATOM   1290  O  OE2 . GLU B  1 24  ? 5.293   15.744  14.275  1.00 49.18  ? 24  GLU F OE2 1 
ATOM   1291  N  N   . SER B  1 25  ? 6.423   18.836  19.084  1.00 39.82  ? 25  SER F N   1 
ATOM   1292  C  CA  . SER B  1 25  ? 6.343   19.801  20.203  1.00 38.59  ? 25  SER F CA  1 
ATOM   1293  C  C   . SER B  1 25  ? 5.696   19.218  21.459  1.00 38.87  ? 25  SER F C   1 
ATOM   1294  O  O   . SER B  1 25  ? 6.007   19.639  22.565  1.00 37.63  ? 25  SER F O   1 
ATOM   1295  C  CB  . SER B  1 25  ? 5.622   21.091  19.788  1.00 39.44  ? 25  SER F CB  1 
ATOM   1296  O  OG  . SER B  1 25  ? 4.262   20.846  19.488  1.00 41.83  ? 25  SER F OG  1 
ATOM   1297  N  N   . ASN B  1 26  ? 4.841   18.217  21.297  1.00 40.81  ? 26  ASN F N   1 
ATOM   1298  C  CA  . ASN B  1 26  ? 4.224   17.547  22.457  1.00 41.43  ? 26  ASN F CA  1 
ATOM   1299  C  C   . ASN B  1 26  ? 5.083   16.373  22.957  1.00 40.51  ? 26  ASN F C   1 
ATOM   1300  O  O   . ASN B  1 26  ? 4.550   15.427  23.559  1.00 41.97  ? 26  ASN F O   1 
ATOM   1301  C  CB  . ASN B  1 26  ? 2.800   17.071  22.105  1.00 44.41  ? 26  ASN F CB  1 
ATOM   1302  C  CG  . ASN B  1 26  ? 2.781   15.936  21.084  1.00 46.11  ? 26  ASN F CG  1 
ATOM   1303  O  OD1 . ASN B  1 26  ? 3.784   15.656  20.410  1.00 45.34  ? 26  ASN F OD1 1 
ATOM   1304  N  ND2 . ASN B  1 26  ? 1.649   15.275  20.976  1.00 48.71  ? 26  ASN F ND2 1 
ATOM   1305  N  N   . GLY B  1 27  ? 6.395   16.437  22.722  1.00 38.43  ? 27  GLY F N   1 
ATOM   1306  C  CA  . GLY B  1 27  ? 7.231   15.243  22.717  1.00 37.98  ? 27  GLY F CA  1 
ATOM   1307  C  C   . GLY B  1 27  ? 8.561   15.393  23.432  1.00 35.42  ? 27  GLY F C   1 
ATOM   1308  O  O   . GLY B  1 27  ? 8.974   16.504  23.782  1.00 33.81  ? 27  GLY F O   1 
ATOM   1309  N  N   . PRO B  1 28  ? 9.244   14.259  23.653  1.00 35.16  ? 28  PRO F N   1 
ATOM   1310  C  CA  . PRO B  1 28  ? 10.494  14.287  24.395  1.00 33.20  ? 28  PRO F CA  1 
ATOM   1311  C  C   . PRO B  1 28  ? 11.626  14.999  23.636  1.00 31.71  ? 28  PRO F C   1 
ATOM   1312  O  O   . PRO B  1 28  ? 11.629  15.033  22.399  1.00 32.36  ? 28  PRO F O   1 
ATOM   1313  C  CB  . PRO B  1 28  ? 10.814  12.801  24.613  1.00 34.13  ? 28  PRO F CB  1 
ATOM   1314  C  CG  . PRO B  1 28  ? 10.099  12.081  23.530  1.00 36.32  ? 28  PRO F CG  1 
ATOM   1315  C  CD  . PRO B  1 28  ? 8.881   12.898  23.210  1.00 37.13  ? 28  PRO F CD  1 
ATOM   1316  N  N   . VAL B  1 29  ? 12.539  15.588  24.405  1.00 29.80  ? 29  VAL F N   1 
ATOM   1317  C  CA  . VAL B  1 29  ? 13.753  16.211  23.893  1.00 28.55  ? 29  VAL F CA  1 
ATOM   1318  C  C   . VAL B  1 29  ? 14.912  15.260  24.125  1.00 28.16  ? 29  VAL F C   1 
ATOM   1319  O  O   . VAL B  1 29  ? 15.169  14.872  25.263  1.00 27.73  ? 29  VAL F O   1 
ATOM   1320  C  CB  . VAL B  1 29  ? 14.082  17.527  24.630  1.00 27.06  ? 29  VAL F CB  1 
ATOM   1321  C  CG1 . VAL B  1 29  ? 15.350  18.154  24.056  1.00 26.12  ? 29  VAL F CG1 1 
ATOM   1322  C  CG2 . VAL B  1 29  ? 12.893  18.483  24.550  1.00 27.57  ? 29  VAL F CG2 1 
ATOM   1323  N  N   . LYS B  1 30  ? 15.606  14.893  23.056  1.00 28.53  ? 30  LYS F N   1 
ATOM   1324  C  CA  . LYS B  1 30  ? 16.821  14.078  23.173  1.00 28.37  ? 30  LYS F CA  1 
ATOM   1325  C  C   . LYS B  1 30  ? 17.991  15.008  23.408  1.00 26.81  ? 30  LYS F C   1 
ATOM   1326  O  O   . LYS B  1 30  ? 18.121  16.020  22.733  1.00 26.32  ? 30  LYS F O   1 
ATOM   1327  C  CB  . LYS B  1 30  ? 17.031  13.229  21.925  1.00 29.90  ? 30  LYS F CB  1 
ATOM   1328  C  CG  . LYS B  1 30  ? 15.971  12.147  21.774  0.50 31.73  ? 30  LYS F CG  1 
ATOM   1329  C  CD  . LYS B  1 30  ? 15.975  11.528  20.389  0.50 33.53  ? 30  LYS F CD  1 
ATOM   1330  C  CE  . LYS B  1 30  ? 15.310  10.165  20.400  0.50 35.56  ? 30  LYS F CE  1 
ATOM   1331  N  NZ  . LYS B  1 30  ? 15.201  9.602   19.029  0.50 37.65  ? 30  LYS F NZ  1 
ATOM   1332  N  N   . VAL B  1 31  ? 18.826  14.661  24.384  1.00 26.16  ? 31  VAL F N   1 
ATOM   1333  C  CA  . VAL B  1 31  ? 19.954  15.481  24.790  1.00 24.95  ? 31  VAL F CA  1 
ATOM   1334  C  C   . VAL B  1 31  ? 21.202  14.612  24.692  1.00 25.38  ? 31  VAL F C   1 
ATOM   1335  O  O   . VAL B  1 31  ? 21.288  13.586  25.365  1.00 25.82  ? 31  VAL F O   1 
ATOM   1336  C  CB  . VAL B  1 31  ? 19.791  15.992  26.239  1.00 24.00  ? 31  VAL F CB  1 
ATOM   1337  C  CG1 . VAL B  1 31  ? 20.933  16.935  26.611  1.00 23.05  ? 31  VAL F CG1 1 
ATOM   1338  C  CG2 . VAL B  1 31  ? 18.438  16.681  26.415  1.00 23.98  ? 31  VAL F CG2 1 
ATOM   1339  N  N   . TRP B  1 32  ? 22.157  15.010  23.859  1.00 25.39  ? 32  TRP F N   1 
ATOM   1340  C  CA  . TRP B  1 32  ? 23.356  14.210  23.682  1.00 26.16  ? 32  TRP F CA  1 
ATOM   1341  C  C   . TRP B  1 32  ? 24.564  15.023  23.282  1.00 25.88  ? 32  TRP F C   1 
ATOM   1342  O  O   . TRP B  1 32  ? 24.447  16.112  22.721  1.00 25.39  ? 32  TRP F O   1 
ATOM   1343  C  CB  . TRP B  1 32  ? 23.120  13.078  22.673  1.00 27.78  ? 32  TRP F CB  1 
ATOM   1344  C  CG  . TRP B  1 32  ? 23.263  13.476  21.243  1.00 28.48  ? 32  TRP F CG  1 
ATOM   1345  C  CD1 . TRP B  1 32  ? 24.358  13.279  20.438  1.00 29.35  ? 32  TRP F CD1 1 
ATOM   1346  C  CD2 . TRP B  1 32  ? 22.293  14.146  20.443  1.00 28.58  ? 32  TRP F CD2 1 
ATOM   1347  N  NE1 . TRP B  1 32  ? 24.119  13.786  19.190  1.00 29.98  ? 32  TRP F NE1 1 
ATOM   1348  C  CE2 . TRP B  1 32  ? 22.860  14.322  19.161  1.00 29.51  ? 32  TRP F CE2 1 
ATOM   1349  C  CE3 . TRP B  1 32  ? 20.994  14.615  20.681  1.00 28.23  ? 32  TRP F CE3 1 
ATOM   1350  C  CZ2 . TRP B  1 32  ? 22.171  14.938  18.116  1.00 30.04  ? 32  TRP F CZ2 1 
ATOM   1351  C  CZ3 . TRP B  1 32  ? 20.305  15.234  19.639  1.00 28.74  ? 32  TRP F CZ3 1 
ATOM   1352  C  CH2 . TRP B  1 32  ? 20.901  15.392  18.373  1.00 29.63  ? 32  TRP F CH2 1 
ATOM   1353  N  N   . GLY B  1 33  ? 25.731  14.456  23.571  1.00 26.45  ? 33  GLY F N   1 
ATOM   1354  C  CA  . GLY B  1 33  ? 26.999  15.065  23.207  1.00 26.64  ? 33  GLY F CA  1 
ATOM   1355  C  C   . GLY B  1 33  ? 28.107  14.598  24.120  1.00 26.99  ? 33  GLY F C   1 
ATOM   1356  O  O   . GLY B  1 33  ? 27.912  13.700  24.946  1.00 27.27  ? 33  GLY F O   1 
ATOM   1357  N  N   . SER B  1 34  ? 29.276  15.203  23.969  1.00 27.26  ? 34  SER F N   1 
ATOM   1358  C  CA  . SER B  1 34  ? 30.451  14.791  24.725  1.00 27.89  ? 34  SER F CA  1 
ATOM   1359  C  C   . SER B  1 34  ? 30.959  15.944  25.584  1.00 27.05  ? 34  SER F C   1 
ATOM   1360  O  O   . SER B  1 34  ? 31.066  17.068  25.105  1.00 26.87  ? 34  SER F O   1 
ATOM   1361  C  CB  . SER B  1 34  ? 31.532  14.315  23.773  1.00 29.46  ? 34  SER F CB  1 
ATOM   1362  O  OG  . SER B  1 34  ? 32.556  13.675  24.504  1.00 30.48  ? 34  SER F OG  1 
ATOM   1363  N  N   . ILE B  1 35  ? 31.229  15.675  26.858  1.00 26.80  ? 35  ILE F N   1 
ATOM   1364  C  CA  . ILE B  1 35  ? 31.876  16.655  27.739  1.00 26.39  ? 35  ILE F CA  1 
ATOM   1365  C  C   . ILE B  1 35  ? 33.186  16.031  28.207  1.00 27.60  ? 35  ILE F C   1 
ATOM   1366  O  O   . ILE B  1 35  ? 33.197  14.892  28.678  1.00 28.20  ? 35  ILE F O   1 
ATOM   1367  C  CB  . ILE B  1 35  ? 30.992  17.035  28.949  1.00 25.29  ? 35  ILE F CB  1 
ATOM   1368  C  CG1 . ILE B  1 35  ? 29.586  17.449  28.485  1.00 24.36  ? 35  ILE F CG1 1 
ATOM   1369  C  CG2 . ILE B  1 35  ? 31.625  18.165  29.756  1.00 25.15  ? 35  ILE F CG2 1 
ATOM   1370  C  CD1 . ILE B  1 35  ? 28.623  17.744  29.616  1.00 23.60  ? 35  ILE F CD1 1 
ATOM   1371  N  N   . LYS B  1 36  ? 34.282  16.772  28.067  1.00 28.15  ? 36  LYS F N   1 
ATOM   1372  C  CA  . LYS B  1 36  ? 35.589  16.307  28.518  1.00 29.50  ? 36  LYS F CA  1 
ATOM   1373  C  C   . LYS B  1 36  ? 36.114  17.214  29.629  1.00 29.36  ? 36  LYS F C   1 
ATOM   1374  O  O   . LYS B  1 36  ? 35.543  18.268  29.905  1.00 28.25  ? 36  LYS F O   1 
ATOM   1375  C  CB  . LYS B  1 36  ? 36.573  16.199  27.342  1.00 31.02  ? 36  LYS F CB  1 
ATOM   1376  C  CG  . LYS B  1 36  ? 36.836  17.495  26.597  1.00 31.03  ? 36  LYS F CG  1 
ATOM   1377  C  CD  . LYS B  1 36  ? 37.800  17.284  25.443  1.00 32.78  ? 36  LYS F CD  1 
ATOM   1378  C  CE  . LYS B  1 36  ? 38.157  18.615  24.809  1.00 32.99  ? 36  LYS F CE  1 
ATOM   1379  N  NZ  . LYS B  1 36  ? 38.901  18.404  23.547  1.00 34.71  ? 36  LYS F NZ  1 
ATOM   1380  N  N   . GLY B  1 37  ? 37.183  16.771  30.283  1.00 30.63  ? 37  GLY F N   1 
ATOM   1381  C  CA  . GLY B  1 37  ? 37.813  17.517  31.375  1.00 31.09  ? 37  GLY F CA  1 
ATOM   1382  C  C   . GLY B  1 37  ? 37.187  17.339  32.749  1.00 30.48  ? 37  GLY F C   1 
ATOM   1383  O  O   . GLY B  1 37  ? 37.543  18.060  33.684  1.00 30.89  ? 37  GLY F O   1 
ATOM   1384  N  N   . LEU B  1 38  ? 36.265  16.383  32.884  1.00 29.77  ? 38  LEU F N   1 
ATOM   1385  C  CA  . LEU B  1 38  ? 35.581  16.112  34.159  1.00 29.30  ? 38  LEU F CA  1 
ATOM   1386  C  C   . LEU B  1 38  ? 36.368  15.113  35.011  1.00 30.79  ? 38  LEU F C   1 
ATOM   1387  O  O   . LEU B  1 38  ? 37.136  14.321  34.482  1.00 31.94  ? 38  LEU F O   1 
ATOM   1388  C  CB  . LEU B  1 38  ? 34.173  15.556  33.898  1.00 28.12  ? 38  LEU F CB  1 
ATOM   1389  C  CG  . LEU B  1 38  ? 33.195  16.513  33.207  1.00 26.69  ? 38  LEU F CG  1 
ATOM   1390  C  CD1 . LEU B  1 38  ? 32.036  15.757  32.570  1.00 26.05  ? 38  LEU F CD1 1 
ATOM   1391  C  CD2 . LEU B  1 38  ? 32.694  17.566  34.174  1.00 26.06  ? 38  LEU F CD2 1 
ATOM   1392  N  N   . THR B  1 39  ? 36.181  15.165  36.329  1.00 30.91  ? 39  THR F N   1 
ATOM   1393  C  CA  . THR B  1 39  ? 36.657  14.112  37.227  1.00 32.26  ? 39  THR F CA  1 
ATOM   1394  C  C   . THR B  1 39  ? 35.743  12.910  37.055  1.00 31.94  ? 39  THR F C   1 
ATOM   1395  O  O   . THR B  1 39  ? 34.542  13.071  36.767  1.00 30.46  ? 39  THR F O   1 
ATOM   1396  C  CB  . THR B  1 39  ? 36.620  14.549  38.705  1.00 32.66  ? 39  THR F CB  1 
ATOM   1397  O  OG1 . THR B  1 39  ? 35.308  15.045  39.043  1.00 31.26  ? 39  THR F OG1 1 
ATOM   1398  C  CG2 . THR B  1 39  ? 37.643  15.632  38.964  1.00 33.59  ? 39  THR F CG2 1 
ATOM   1399  N  N   . GLU B  1 40  ? 36.292  11.717  37.241  1.00 33.40  ? 40  GLU F N   1 
ATOM   1400  C  CA  . GLU B  1 40  ? 35.518  10.490  37.070  1.00 33.61  ? 40  GLU F CA  1 
ATOM   1401  C  C   . GLU B  1 40  ? 34.342  10.464  38.044  1.00 32.79  ? 40  GLU F C   1 
ATOM   1402  O  O   . GLU B  1 40  ? 34.500  10.800  39.216  1.00 33.14  ? 40  GLU F O   1 
ATOM   1403  C  CB  . GLU B  1 40  ? 36.393  9.238   37.265  1.00 35.76  ? 40  GLU F CB  1 
ATOM   1404  C  CG  . GLU B  1 40  ? 35.651  7.932   36.971  1.00 36.29  ? 40  GLU F CG  1 
ATOM   1405  C  CD  . GLU B  1 40  ? 36.501  6.676   37.145  1.00 38.70  ? 40  GLU F CD  1 
ATOM   1406  O  OE1 . GLU B  1 40  ? 37.705  6.773   37.438  1.00 40.01  ? 40  GLU F OE1 1 
ATOM   1407  O  OE2 . GLU B  1 40  ? 35.938  5.572   36.991  1.00 39.55  ? 40  GLU F OE2 1 
ATOM   1408  N  N   . GLY B  1 41  ? 33.165  10.083  37.547  1.00 31.91  ? 41  GLY F N   1 
ATOM   1409  C  CA  . GLY B  1 41  ? 31.969  9.955   38.379  1.00 31.39  ? 41  GLY F CA  1 
ATOM   1410  C  C   . GLY B  1 41  ? 30.838  10.884  37.993  1.00 29.71  ? 41  GLY F C   1 
ATOM   1411  O  O   . GLY B  1 41  ? 30.812  11.415  36.887  1.00 28.83  ? 41  GLY F O   1 
ATOM   1412  N  N   . LEU B  1 42  ? 29.912  11.079  38.932  1.00 29.41  ? 42  LEU F N   1 
ATOM   1413  C  CA  . LEU B  1 42  ? 28.659  11.792  38.686  1.00 28.15  ? 42  LEU F CA  1 
ATOM   1414  C  C   . LEU B  1 42  ? 28.807  13.296  38.780  1.00 27.17  ? 42  LEU F C   1 
ATOM   1415  O  O   . LEU B  1 42  ? 29.478  13.801  39.671  1.00 27.70  ? 42  LEU F O   1 
ATOM   1416  C  CB  . LEU B  1 42  ? 27.587  11.343  39.692  1.00 28.61  ? 42  LEU F CB  1 
ATOM   1417  C  CG  . LEU B  1 42  ? 27.224  9.863   39.597  1.00 29.73  ? 42  LEU F CG  1 
ATOM   1418  C  CD1 . LEU B  1 42  ? 26.524  9.381   40.863  1.00 30.64  ? 42  LEU F CD1 1 
ATOM   1419  C  CD2 . LEU B  1 42  ? 26.368  9.629   38.365  1.00 29.20  ? 42  LEU F CD2 1 
ATOM   1420  N  N   . HIS B  1 43  ? 28.153  13.996  37.858  1.00 25.99  ? 43  HIS F N   1 
ATOM   1421  C  CA  . HIS B  1 43  ? 28.118  15.456  37.822  1.00 25.16  ? 43  HIS F CA  1 
ATOM   1422  C  C   . HIS B  1 43  ? 26.708  15.949  37.547  1.00 24.29  ? 43  HIS F C   1 
ATOM   1423  O  O   . HIS B  1 43  ? 26.099  15.536  36.569  1.00 23.89  ? 43  HIS F O   1 
ATOM   1424  C  CB  . HIS B  1 43  ? 29.063  15.957  36.732  1.00 24.96  ? 43  HIS F CB  1 
ATOM   1425  C  CG  . HIS B  1 43  ? 30.496  15.667  37.033  1.00 25.98  ? 43  HIS F CG  1 
ATOM   1426  N  ND1 . HIS B  1 43  ? 31.268  16.502  37.805  1.00 26.51  ? 43  HIS F ND1 1 
ATOM   1427  C  CD2 . HIS B  1 43  ? 31.266  14.591  36.753  1.00 26.90  ? 43  HIS F CD2 1 
ATOM   1428  C  CE1 . HIS B  1 43  ? 32.472  15.978  37.945  1.00 27.68  ? 43  HIS F CE1 1 
ATOM   1429  N  NE2 . HIS B  1 43  ? 32.496  14.813  37.323  1.00 27.94  ? 43  HIS F NE2 1 
ATOM   1430  N  N   . GLY B  1 44  ? 26.201  16.830  38.412  1.00 24.22  ? 44  GLY F N   1 
ATOM   1431  C  CA  . GLY B  1 44  ? 24.906  17.485  38.208  1.00 23.69  ? 44  GLY F CA  1 
ATOM   1432  C  C   . GLY B  1 44  ? 24.880  18.238  36.893  1.00 22.92  ? 44  GLY F C   1 
ATOM   1433  O  O   . GLY B  1 44  ? 25.906  18.799  36.448  1.00 22.71  ? 44  GLY F O   1 
ATOM   1434  N  N   . PHE B  1 45  ? 23.706  18.237  36.272  1.00 22.57  ? 45  PHE F N   1 
ATOM   1435  C  CA  . PHE B  1 45  ? 23.545  18.642  34.890  1.00 22.09  ? 45  PHE F CA  1 
ATOM   1436  C  C   . PHE B  1 45  ? 22.180  19.315  34.821  1.00 21.97  ? 45  PHE F C   1 
ATOM   1437  O  O   . PHE B  1 45  ? 21.158  18.639  34.933  1.00 22.09  ? 45  PHE F O   1 
ATOM   1438  C  CB  . PHE B  1 45  ? 23.620  17.383  34.022  1.00 22.34  ? 45  PHE F CB  1 
ATOM   1439  C  CG  . PHE B  1 45  ? 23.701  17.637  32.536  1.00 22.13  ? 45  PHE F CG  1 
ATOM   1440  C  CD1 . PHE B  1 45  ? 24.812  18.272  31.978  1.00 22.04  ? 45  PHE F CD1 1 
ATOM   1441  C  CD2 . PHE B  1 45  ? 22.701  17.188  31.683  1.00 22.32  ? 45  PHE F CD2 1 
ATOM   1442  C  CE1 . PHE B  1 45  ? 24.907  18.478  30.612  1.00 21.94  ? 45  PHE F CE1 1 
ATOM   1443  C  CE2 . PHE B  1 45  ? 22.794  17.392  30.307  1.00 22.31  ? 45  PHE F CE2 1 
ATOM   1444  C  CZ  . PHE B  1 45  ? 23.910  18.030  29.776  1.00 22.10  ? 45  PHE F CZ  1 
ATOM   1445  N  N   . HIS B  1 46  ? 22.168  20.649  34.711  1.00 21.82  ? 46  HIS F N   1 
ATOM   1446  C  CA  . HIS B  1 46  ? 20.933  21.411  34.885  1.00 22.04  ? 46  HIS F CA  1 
ATOM   1447  C  C   . HIS B  1 46  ? 20.790  22.521  33.876  1.00 21.68  ? 46  HIS F C   1 
ATOM   1448  O  O   . HIS B  1 46  ? 21.788  23.083  33.426  1.00 21.50  ? 46  HIS F O   1 
ATOM   1449  C  CB  . HIS B  1 46  ? 20.857  22.054  36.276  1.00 22.70  ? 46  HIS F CB  1 
ATOM   1450  C  CG  . HIS B  1 46  ? 21.158  21.121  37.396  1.00 23.28  ? 46  HIS F CG  1 
ATOM   1451  N  ND1 . HIS B  1 46  ? 22.190  21.341  38.281  1.00 23.79  ? 46  HIS F ND1 1 
ATOM   1452  C  CD2 . HIS B  1 46  ? 20.585  19.952  37.765  1.00 23.69  ? 46  HIS F CD2 1 
ATOM   1453  C  CE1 . HIS B  1 46  ? 22.229  20.353  39.158  1.00 24.33  ? 46  HIS F CE1 1 
ATOM   1454  N  NE2 . HIS B  1 46  ? 21.269  19.493  38.863  1.00 24.24  ? 46  HIS F NE2 1 
ATOM   1455  N  N   . VAL B  1 47  ? 19.542  22.847  33.550  1.00 21.72  ? 47  VAL F N   1 
ATOM   1456  C  CA  . VAL B  1 47  ? 19.241  24.075  32.851  1.00 21.72  ? 47  VAL F CA  1 
ATOM   1457  C  C   . VAL B  1 47  ? 18.911  25.126  33.894  1.00 22.25  ? 47  VAL F C   1 
ATOM   1458  O  O   . VAL B  1 47  ? 18.031  24.917  34.738  1.00 22.69  ? 47  VAL F O   1 
ATOM   1459  C  CB  . VAL B  1 47  ? 18.090  23.934  31.852  1.00 21.88  ? 47  VAL F CB  1 
ATOM   1460  C  CG1 . VAL B  1 47  ? 17.889  25.250  31.103  1.00 22.09  ? 47  VAL F CG1 1 
ATOM   1461  C  CG2 . VAL B  1 47  ? 18.378  22.808  30.877  1.00 21.64  ? 47  VAL F CG2 1 
ATOM   1462  N  N   . HIS B  1 48  ? 19.634  26.242  33.834  1.00 22.36  ? 48  HIS F N   1 
ATOM   1463  C  CA  . HIS B  1 48  ? 19.423  27.373  34.726  1.00 23.26  ? 48  HIS F CA  1 
ATOM   1464  C  C   . HIS B  1 48  ? 18.646  28.451  33.988  1.00 23.78  ? 48  HIS F C   1 
ATOM   1465  O  O   . HIS B  1 48  ? 18.653  28.507  32.752  1.00 23.45  ? 48  HIS F O   1 
ATOM   1466  C  CB  . HIS B  1 48  ? 20.760  27.940  35.213  1.00 23.45  ? 48  HIS F CB  1 
ATOM   1467  C  CG  . HIS B  1 48  ? 21.459  27.069  36.202  1.00 23.39  ? 48  HIS F CG  1 
ATOM   1468  N  ND1 . HIS B  1 48  ? 21.712  27.472  37.495  1.00 24.26  ? 48  HIS F ND1 1 
ATOM   1469  C  CD2 . HIS B  1 48  ? 21.922  25.800  36.105  1.00 22.81  ? 48  HIS F CD2 1 
ATOM   1470  C  CE1 . HIS B  1 48  ? 22.326  26.498  38.143  1.00 24.18  ? 48  HIS F CE1 1 
ATOM   1471  N  NE2 . HIS B  1 48  ? 22.468  25.473  37.322  1.00 23.27  ? 48  HIS F NE2 1 
ATOM   1472  N  N   . GLU B  1 49  ? 18.049  29.341  34.766  1.00 24.84  ? 49  GLU F N   1 
ATOM   1473  C  CA  . GLU B  1 49  ? 17.012  30.244  34.282  1.00 25.67  ? 49  GLU F CA  1 
ATOM   1474  C  C   . GLU B  1 49  ? 17.468  31.245  33.225  1.00 25.79  ? 49  GLU F C   1 
ATOM   1475  O  O   . GLU B  1 49  ? 16.756  31.463  32.245  1.00 25.82  ? 49  GLU F O   1 
ATOM   1476  C  CB  . GLU B  1 49  ? 16.378  30.997  35.459  1.00 27.07  ? 49  GLU F CB  1 
ATOM   1477  C  CG  . GLU B  1 49  ? 15.087  31.690  35.099  1.00 28.17  ? 49  GLU F CG  1 
ATOM   1478  C  CD  . GLU B  1 49  ? 14.481  32.483  36.234  1.00 29.88  ? 49  GLU F CD  1 
ATOM   1479  O  OE1 . GLU B  1 49  ? 14.914  32.352  37.407  1.00 30.40  ? 49  GLU F OE1 1 
ATOM   1480  O  OE2 . GLU B  1 49  ? 13.566  33.259  35.929  1.00 30.99  ? 49  GLU F OE2 1 
ATOM   1481  N  N   . PHE B  1 50  ? 18.631  31.863  33.431  1.00 26.01  ? 50  PHE F N   1 
ATOM   1482  C  CA  . PHE B  1 50  ? 19.066  32.974  32.590  1.00 26.69  ? 50  PHE F CA  1 
ATOM   1483  C  C   . PHE B  1 50  ? 20.213  32.581  31.659  1.00 25.93  ? 50  PHE F C   1 
ATOM   1484  O  O   . PHE B  1 50  ? 21.126  31.874  32.070  1.00 25.33  ? 50  PHE F O   1 
ATOM   1485  C  CB  . PHE B  1 50  ? 19.461  34.166  33.459  1.00 28.08  ? 50  PHE F CB  1 
ATOM   1486  C  CG  . PHE B  1 50  ? 18.381  34.589  34.410  1.00 29.27  ? 50  PHE F CG  1 
ATOM   1487  C  CD1 . PHE B  1 50  ? 17.143  35.009  33.928  1.00 29.92  ? 50  PHE F CD1 1 
ATOM   1488  C  CD2 . PHE B  1 50  ? 18.584  34.547  35.785  1.00 29.96  ? 50  PHE F CD2 1 
ATOM   1489  C  CE1 . PHE B  1 50  ? 16.131  35.382  34.796  1.00 31.25  ? 50  PHE F CE1 1 
ATOM   1490  C  CE2 . PHE B  1 50  ? 17.575  34.919  36.660  1.00 31.24  ? 50  PHE F CE2 1 
ATOM   1491  C  CZ  . PHE B  1 50  ? 16.346  35.335  36.169  1.00 31.91  ? 50  PHE F CZ  1 
ATOM   1492  N  N   . GLY B  1 51  ? 20.140  33.043  30.409  1.00 26.14  ? 51  GLY F N   1 
ATOM   1493  C  CA  . GLY B  1 51  ? 21.232  32.929  29.440  1.00 25.97  ? 51  GLY F CA  1 
ATOM   1494  C  C   . GLY B  1 51  ? 22.212  34.079  29.554  1.00 27.13  ? 51  GLY F C   1 
ATOM   1495  O  O   . GLY B  1 51  ? 22.595  34.686  28.552  1.00 27.57  ? 51  GLY F O   1 
ATOM   1496  N  N   . ASP B  1 52  ? 22.618  34.361  30.788  1.00 27.91  ? 52  ASP F N   1 
ATOM   1497  C  CA  . ASP B  1 52  ? 23.433  35.501  31.126  1.00 29.49  ? 52  ASP F CA  1 
ATOM   1498  C  C   . ASP B  1 52  ? 24.787  34.934  31.568  1.00 29.58  ? 52  ASP F C   1 
ATOM   1499  O  O   . ASP B  1 52  ? 24.908  34.355  32.655  1.00 29.36  ? 52  ASP F O   1 
ATOM   1500  C  CB  . ASP B  1 52  ? 22.746  36.312  32.232  1.00 30.60  ? 52  ASP F CB  1 
ATOM   1501  C  CG  . ASP B  1 52  ? 23.513  37.568  32.617  1.00 32.36  ? 52  ASP F CG  1 
ATOM   1502  O  OD1 . ASP B  1 52  ? 24.733  37.637  32.367  1.00 32.47  ? 52  ASP F OD1 1 
ATOM   1503  O  OD2 . ASP B  1 52  ? 22.889  38.495  33.174  1.00 33.72  ? 52  ASP F OD2 1 
ATOM   1504  N  N   . ASN B  1 53  ? 25.782  35.077  30.696  1.00 30.18  ? 53  ASN F N   1 
ATOM   1505  C  CA  . ASN B  1 53  ? 27.140  34.604  30.949  1.00 30.62  ? 53  ASN F CA  1 
ATOM   1506  C  C   . ASN B  1 53  ? 28.094  35.759  31.300  1.00 32.42  ? 53  ASN F C   1 
ATOM   1507  O  O   . ASN B  1 53  ? 29.304  35.590  31.219  1.00 32.90  ? 53  ASN F O   1 
ATOM   1508  C  CB  . ASN B  1 53  ? 27.665  33.851  29.712  1.00 30.20  ? 53  ASN F CB  1 
ATOM   1509  C  CG  . ASN B  1 53  ? 28.880  32.984  30.014  1.00 30.39  ? 53  ASN F CG  1 
ATOM   1510  O  OD1 . ASN B  1 53  ? 29.980  33.224  29.502  1.00 31.50  ? 53  ASN F OD1 1 
ATOM   1511  N  ND2 . ASN B  1 53  ? 28.689  31.976  30.860  1.00 29.95  ? 53  ASN F ND2 1 
ATOM   1512  N  N   . THR B  1 54  ? 27.569  36.912  31.712  1.00 33.66  ? 54  THR F N   1 
ATOM   1513  C  CA  . THR B  1 54  ? 28.411  38.091  31.955  1.00 35.79  ? 54  THR F CA  1 
ATOM   1514  C  C   . THR B  1 54  ? 29.354  37.916  33.156  1.00 36.80  ? 54  THR F C   1 
ATOM   1515  O  O   . THR B  1 54  ? 30.414  38.546  33.198  1.00 38.35  ? 54  THR F O   1 
ATOM   1516  C  CB  . THR B  1 54  ? 27.582  39.383  32.153  1.00 37.15  ? 54  THR F CB  1 
ATOM   1517  O  OG1 . THR B  1 54  ? 26.650  39.208  33.222  1.00 36.87  ? 54  THR F OG1 1 
ATOM   1518  C  CG2 . THR B  1 54  ? 26.837  39.745  30.884  1.00 36.85  ? 54  THR F CG2 1 
ATOM   1519  N  N   . ALA B  1 55  ? 28.956  37.080  34.122  1.00 36.03  ? 55  ALA F N   1 
ATOM   1520  C  CA  . ALA B  1 55  ? 29.819  36.698  35.242  1.00 36.88  ? 55  ALA F CA  1 
ATOM   1521  C  C   . ALA B  1 55  ? 30.044  35.188  35.236  1.00 35.33  ? 55  ALA F C   1 
ATOM   1522  O  O   . ALA B  1 55  ? 30.061  34.546  36.289  1.00 35.42  ? 55  ALA F O   1 
ATOM   1523  C  CB  . ALA B  1 55  ? 29.195  37.144  36.552  1.00 37.92  ? 55  ALA F CB  1 
ATOM   1524  N  N   . GLY B  1 56  ? 30.217  34.623  34.044  1.00 34.22  ? 56  GLY F N   1 
ATOM   1525  C  CA  . GLY B  1 56  ? 30.351  33.181  33.891  1.00 32.70  ? 56  GLY F CA  1 
ATOM   1526  C  C   . GLY B  1 56  ? 29.048  32.453  34.157  1.00 31.23  ? 56  GLY F C   1 
ATOM   1527  O  O   . GLY B  1 56  ? 27.955  32.999  33.949  1.00 31.24  ? 56  GLY F O   1 
ATOM   1528  N  N   . ALA B  1 57  ? 29.169  31.214  34.618  1.00 30.22  ? 57  ALA F N   1 
ATOM   1529  C  CA  . ALA B  1 57  ? 28.024  30.406  35.028  1.00 28.96  ? 57  ALA F CA  1 
ATOM   1530  C  C   . ALA B  1 57  ? 27.237  31.008  36.209  1.00 29.50  ? 57  ALA F C   1 
ATOM   1531  O  O   . ALA B  1 57  ? 26.042  30.744  36.349  1.00 28.80  ? 57  ALA F O   1 
ATOM   1532  C  CB  . ALA B  1 57  ? 28.486  28.997  35.372  1.00 28.38  ? 57  ALA F CB  1 
ATOM   1533  N  N   . THR B  1 58  ? 27.906  31.796  37.051  1.00 30.75  ? 58  THR F N   1 
ATOM   1534  C  CA  . THR B  1 58  ? 27.276  32.418  38.226  1.00 31.69  ? 58  THR F CA  1 
ATOM   1535  C  C   . THR B  1 58  ? 26.075  33.318  37.897  1.00 31.60  ? 58  THR F C   1 
ATOM   1536  O  O   . THR B  1 58  ? 25.070  33.279  38.604  1.00 31.84  ? 58  THR F O   1 
ATOM   1537  C  CB  . THR B  1 58  ? 28.305  33.236  39.026  1.00 33.73  ? 58  THR F CB  1 
ATOM   1538  O  OG1 . THR B  1 58  ? 29.439  32.411  39.299  1.00 33.91  ? 58  THR F OG1 1 
ATOM   1539  C  CG2 . THR B  1 58  ? 27.719  33.736  40.355  1.00 35.16  ? 58  THR F CG2 1 
ATOM   1540  N  N   . SER B  1 59  ? 26.164  34.096  36.820  1.00 31.31  ? 59  SER F N   1 
ATOM   1541  C  CA  . SER B  1 59  ? 25.070  35.006  36.428  1.00 31.47  ? 59  SER F CA  1 
ATOM   1542  C  C   . SER B  1 59  ? 23.852  34.299  35.776  1.00 29.79  ? 59  SER F C   1 
ATOM   1543  O  O   . SER B  1 59  ? 22.842  34.952  35.471  1.00 30.33  ? 59  SER F O   1 
ATOM   1544  C  CB  . SER B  1 59  ? 25.609  36.117  35.524  1.00 32.34  ? 59  SER F CB  1 
ATOM   1545  O  OG  . SER B  1 59  ? 26.412  35.582  34.489  1.00 31.44  ? 59  SER F OG  1 
ATOM   1546  N  N   . ALA B  1 60  ? 23.923  32.979  35.601  1.00 28.03  ? 60  ALA F N   1 
ATOM   1547  C  CA  . ALA B  1 60  ? 22.813  32.193  35.058  1.00 26.72  ? 60  ALA F CA  1 
ATOM   1548  C  C   . ALA B  1 60  ? 21.624  31.983  36.012  1.00 26.83  ? 60  ALA F C   1 
ATOM   1549  O  O   . ALA B  1 60  ? 20.618  31.418  35.603  1.00 26.12  ? 60  ALA F O   1 
ATOM   1550  C  CB  . ALA B  1 60  ? 23.319  30.838  34.582  1.00 25.44  ? 60  ALA F CB  1 
ATOM   1551  N  N   . GLY B  1 61  ? 21.750  32.396  37.272  1.00 27.77  ? 61  GLY F N   1 
ATOM   1552  C  CA  . GLY B  1 61  ? 20.669  32.286  38.228  1.00 28.32  ? 61  GLY F CA  1 
ATOM   1553  C  C   . GLY B  1 61  ? 20.426  30.854  38.665  1.00 27.36  ? 61  GLY F C   1 
ATOM   1554  O  O   . GLY B  1 61  ? 21.294  29.978  38.485  1.00 26.41  ? 61  GLY F O   1 
ATOM   1555  N  N   . PRO B  1 62  ? 19.241  30.595  39.241  1.00 27.68  ? 62  PRO F N   1 
ATOM   1556  C  CA  . PRO B  1 62  ? 18.970  29.261  39.750  1.00 27.13  ? 62  PRO F CA  1 
ATOM   1557  C  C   . PRO B  1 62  ? 18.493  28.324  38.646  1.00 25.81  ? 62  PRO F C   1 
ATOM   1558  O  O   . PRO B  1 62  ? 18.373  28.726  37.489  1.00 25.25  ? 62  PRO F O   1 
ATOM   1559  C  CB  . PRO B  1 62  ? 17.852  29.510  40.762  1.00 28.47  ? 62  PRO F CB  1 
ATOM   1560  C  CG  . PRO B  1 62  ? 17.080  30.633  40.154  1.00 29.13  ? 62  PRO F CG  1 
ATOM   1561  C  CD  . PRO B  1 62  ? 18.102  31.505  39.465  1.00 28.91  ? 62  PRO F CD  1 
ATOM   1562  N  N   . HIS B  1 63  ? 18.191  27.091  39.026  1.00 25.50  ? 63  HIS F N   1 
ATOM   1563  C  CA  . HIS B  1 63  ? 17.584  26.132  38.105  1.00 24.73  ? 63  HIS F CA  1 
ATOM   1564  C  C   . HIS B  1 63  ? 16.300  26.702  37.511  1.00 25.15  ? 63  HIS F C   1 
ATOM   1565  O  O   . HIS B  1 63  ? 15.539  27.380  38.201  1.00 26.27  ? 63  HIS F O   1 
ATOM   1566  C  CB  . HIS B  1 63  ? 17.287  24.800  38.787  1.00 24.82  ? 63  HIS F CB  1 
ATOM   1567  C  CG  . HIS B  1 63  ? 18.505  24.115  39.314  1.00 24.54  ? 63  HIS F CG  1 
ATOM   1568  N  ND1 . HIS B  1 63  ? 18.442  22.954  40.041  1.00 24.83  ? 63  HIS F ND1 1 
ATOM   1569  C  CD2 . HIS B  1 63  ? 19.818  24.448  39.251  1.00 24.23  ? 63  HIS F CD2 1 
ATOM   1570  C  CE1 . HIS B  1 63  ? 19.659  22.587  40.393  1.00 24.67  ? 63  HIS F CE1 1 
ATOM   1571  N  NE2 . HIS B  1 63  ? 20.513  23.476  39.921  1.00 24.32  ? 63  HIS F NE2 1 
ATOM   1572  N  N   . PHE B  1 64  ? 16.104  26.464  36.219  1.00 24.46  ? 64  PHE F N   1 
ATOM   1573  C  CA  . PHE B  1 64  ? 14.907  26.916  35.511  1.00 25.04  ? 64  PHE F CA  1 
ATOM   1574  C  C   . PHE B  1 64  ? 13.714  26.235  36.163  1.00 25.92  ? 64  PHE F C   1 
ATOM   1575  O  O   . PHE B  1 64  ? 13.633  25.005  36.159  1.00 25.58  ? 64  PHE F O   1 
ATOM   1576  C  CB  . PHE B  1 64  ? 15.016  26.565  34.019  1.00 24.24  ? 64  PHE F CB  1 
ATOM   1577  C  CG  . PHE B  1 64  ? 13.821  26.963  33.191  1.00 24.92  ? 64  PHE F CG  1 
ATOM   1578  C  CD1 . PHE B  1 64  ? 13.227  28.221  33.327  1.00 25.90  ? 64  PHE F CD1 1 
ATOM   1579  C  CD2 . PHE B  1 64  ? 13.320  26.090  32.224  1.00 24.77  ? 64  PHE F CD2 1 
ATOM   1580  C  CE1 . PHE B  1 64  ? 12.134  28.578  32.550  1.00 26.71  ? 64  PHE F CE1 1 
ATOM   1581  C  CE2 . PHE B  1 64  ? 12.237  26.449  31.439  1.00 25.59  ? 64  PHE F CE2 1 
ATOM   1582  C  CZ  . PHE B  1 64  ? 11.650  27.698  31.597  1.00 26.55  ? 64  PHE F CZ  1 
ATOM   1583  N  N   . ASN B  1 65  ? 12.832  27.044  36.752  1.00 27.29  ? 65  ASN F N   1 
ATOM   1584  C  CA  . ASN B  1 65  ? 11.773  26.561  37.639  1.00 28.56  ? 65  ASN F CA  1 
ATOM   1585  C  C   . ASN B  1 65  ? 10.472  27.373  37.441  1.00 30.12  ? 65  ASN F C   1 
ATOM   1586  O  O   . ASN B  1 65  ? 9.988   28.033  38.375  1.00 31.40  ? 65  ASN F O   1 
ATOM   1587  C  CB  . ASN B  1 65  ? 12.255  26.637  39.097  1.00 29.06  ? 65  ASN F CB  1 
ATOM   1588  C  CG  . ASN B  1 65  ? 11.291  25.984  40.086  1.00 30.31  ? 65  ASN F CG  1 
ATOM   1589  O  OD1 . ASN B  1 65  ? 10.447  25.161  39.722  1.00 30.55  ? 65  ASN F OD1 1 
ATOM   1590  N  ND2 . ASN B  1 65  ? 11.438  26.331  41.349  1.00 31.29  ? 65  ASN F ND2 1 
ATOM   1591  N  N   . PRO B  1 66  ? 9.905   27.329  36.221  1.00 30.22  ? 66  PRO F N   1 
ATOM   1592  C  CA  . PRO B  1 66  ? 8.685   28.110  35.951  1.00 31.88  ? 66  PRO F CA  1 
ATOM   1593  C  C   . PRO B  1 66  ? 7.465   27.697  36.785  1.00 33.76  ? 66  PRO F C   1 
ATOM   1594  O  O   . PRO B  1 66  ? 6.570   28.518  36.975  1.00 35.45  ? 66  PRO F O   1 
ATOM   1595  C  CB  . PRO B  1 66  ? 8.431   27.872  34.453  1.00 31.38  ? 66  PRO F CB  1 
ATOM   1596  C  CG  . PRO B  1 66  ? 9.115   26.587  34.148  1.00 29.98  ? 66  PRO F CG  1 
ATOM   1597  C  CD  . PRO B  1 66  ? 10.315  26.529  35.051  1.00 28.97  ? 66  PRO F CD  1 
ATOM   1598  N  N   . LEU B  1 67  ? 7.428   26.459  37.284  1.00 33.79  ? 67  LEU F N   1 
ATOM   1599  C  CA  . LEU B  1 67  ? 6.306   25.989  38.116  1.00 35.72  ? 67  LEU F CA  1 
ATOM   1600  C  C   . LEU B  1 67  ? 6.539   26.084  39.638  1.00 36.43  ? 67  LEU F C   1 
ATOM   1601  O  O   . LEU B  1 67  ? 5.724   25.577  40.421  1.00 37.97  ? 67  LEU F O   1 
ATOM   1602  C  CB  . LEU B  1 67  ? 5.928   24.557  37.707  1.00 35.77  ? 67  LEU F CB  1 
ATOM   1603  C  CG  . LEU B  1 67  ? 5.563   24.349  36.228  1.00 35.62  ? 67  LEU F CG  1 
ATOM   1604  C  CD1 . LEU B  1 67  ? 5.105   22.920  35.988  1.00 36.17  ? 67  LEU F CD1 1 
ATOM   1605  C  CD2 . LEU B  1 67  ? 4.468   25.300  35.767  1.00 37.24  ? 67  LEU F CD2 1 
ATOM   1606  N  N   . SER B  1 68  ? 7.603   26.767  40.062  1.00 35.59  ? 68  SER F N   1 
ATOM   1607  C  CA  . SER B  1 68  ? 7.896   26.973  41.490  1.00 36.46  ? 68  SER F CA  1 
ATOM   1608  C  C   . SER B  1 68  ? 7.813   25.694  42.336  1.00 36.70  ? 68  SER F C   1 
ATOM   1609  O  O   . SER B  1 68  ? 7.138   25.658  43.371  1.00 38.38  ? 68  SER F O   1 
ATOM   1610  C  CB  . SER B  1 68  ? 6.982   28.061  42.069  1.00 38.72  ? 68  SER F CB  1 
ATOM   1611  O  OG  . SER B  1 68  ? 7.238   29.301  41.438  1.00 38.73  ? 68  SER F OG  1 
ATOM   1612  N  N   . ARG B  1 69  ? 8.488   24.648  41.861  1.00 35.05  ? 69  ARG F N   1 
ATOM   1613  C  CA  A ARG B  1 69  ? 8.577   23.363  42.558  0.50 35.25  ? 69  ARG F CA  1 
ATOM   1614  C  CA  B ARG B  1 69  ? 8.569   23.376  42.580  0.50 35.24  ? 69  ARG F CA  1 
ATOM   1615  C  C   . ARG B  1 69  ? 9.891   23.284  43.333  1.00 34.43  ? 69  ARG F C   1 
ATOM   1616  O  O   . ARG B  1 69  ? 10.769  24.148  43.184  1.00 33.63  ? 69  ARG F O   1 
ATOM   1617  C  CB  A ARG B  1 69  ? 8.535   22.216  41.544  0.50 34.38  ? 69  ARG F CB  1 
ATOM   1618  C  CB  B ARG B  1 69  ? 8.463   22.211  41.599  0.50 34.41  ? 69  ARG F CB  1 
ATOM   1619  C  CG  A ARG B  1 69  ? 7.389   22.262  40.541  0.50 35.10  ? 69  ARG F CG  1 
ATOM   1620  C  CG  B ARG B  1 69  ? 7.196   22.200  40.761  0.50 35.34  ? 69  ARG F CG  1 
ATOM   1621  C  CD  A ARG B  1 69  ? 6.390   21.144  40.756  0.50 36.58  ? 69  ARG F CD  1 
ATOM   1622  C  CD  B ARG B  1 69  ? 5.944   22.027  41.597  0.50 37.62  ? 69  ARG F CD  1 
ATOM   1623  N  NE  A ARG B  1 69  ? 5.224   21.292  39.891  0.50 37.68  ? 69  ARG F NE  1 
ATOM   1624  N  NE  B ARG B  1 69  ? 4.811   21.772  40.718  0.50 38.62  ? 69  ARG F NE  1 
ATOM   1625  C  CZ  A ARG B  1 69  ? 4.702   20.325  39.137  0.50 38.10  ? 69  ARG F CZ  1 
ATOM   1626  C  CZ  B ARG B  1 69  ? 3.745   22.556  40.610  0.50 40.15  ? 69  ARG F CZ  1 
ATOM   1627  N  NH1 A ARG B  1 69  ? 5.238   19.109  39.128  0.50 37.55  ? 69  ARG F NH1 1 
ATOM   1628  N  NH1 B ARG B  1 69  ? 3.627   23.639  41.365  0.50 41.01  ? 69  ARG F NH1 1 
ATOM   1629  N  NH2 A ARG B  1 69  ? 3.630   20.577  38.394  0.50 39.28  ? 69  ARG F NH2 1 
ATOM   1630  N  NH2 B ARG B  1 69  ? 2.791   22.237  39.755  0.50 41.09  ? 69  ARG F NH2 1 
ATOM   1631  N  N   . LYS B  1 70  ? 10.032  22.235  44.136  1.00 34.76  ? 70  LYS F N   1 
ATOM   1632  C  CA  . LYS B  1 70  ? 11.307  21.908  44.767  1.00 33.98  ? 70  LYS F CA  1 
ATOM   1633  C  C   . LYS B  1 70  ? 12.181  21.110  43.799  1.00 32.09  ? 70  LYS F C   1 
ATOM   1634  O  O   . LYS B  1 70  ? 11.689  20.502  42.842  1.00 31.60  ? 70  LYS F O   1 
ATOM   1635  C  CB  . LYS B  1 70  ? 11.096  21.103  46.046  1.00 35.48  ? 70  LYS F CB  1 
ATOM   1636  C  CG  . LYS B  1 70  ? 10.318  21.847  47.118  1.00 37.56  ? 70  LYS F CG  1 
ATOM   1637  C  CD  . LYS B  1 70  ? 10.329  21.129  48.466  1.00 39.15  ? 70  LYS F CD  1 
ATOM   1638  C  CE  . LYS B  1 70  ? 9.694   19.743  48.429  0.50 39.72  ? 70  LYS F CE  1 
ATOM   1639  N  NZ  . LYS B  1 70  ? 8.276   19.766  47.972  0.50 40.77  ? 70  LYS F NZ  1 
ATOM   1640  N  N   . HIS B  1 71  ? 13.486  21.127  44.059  1.00 31.12  ? 71  HIS F N   1 
ATOM   1641  C  CA  . HIS B  1 71  ? 14.457  20.363  43.282  1.00 29.61  ? 71  HIS F CA  1 
ATOM   1642  C  C   . HIS B  1 71  ? 14.243  18.854  43.417  1.00 30.00  ? 71  HIS F C   1 
ATOM   1643  O  O   . HIS B  1 71  ? 14.016  18.335  44.506  1.00 31.14  ? 71  HIS F O   1 
ATOM   1644  C  CB  . HIS B  1 71  ? 15.872  20.695  43.741  1.00 29.11  ? 71  HIS F CB  1 
ATOM   1645  C  CG  . HIS B  1 71  ? 16.929  19.960  42.990  1.00 27.85  ? 71  HIS F CG  1 
ATOM   1646  N  ND1 . HIS B  1 71  ? 17.322  20.319  41.720  1.00 26.60  ? 71  HIS F ND1 1 
ATOM   1647  C  CD2 . HIS B  1 71  ? 17.632  18.848  43.307  1.00 27.85  ? 71  HIS F CD2 1 
ATOM   1648  C  CE1 . HIS B  1 71  ? 18.258  19.483  41.306  1.00 25.99  ? 71  HIS F CE1 1 
ATOM   1649  N  NE2 . HIS B  1 71  ? 18.450  18.573  42.243  1.00 26.71  ? 71  HIS F NE2 1 
ATOM   1650  N  N   . GLY B  1 72  ? 14.334  18.157  42.298  1.00 29.21  ? 72  GLY F N   1 
ATOM   1651  C  CA  . GLY B  1 72  ? 14.286  16.704  42.293  1.00 29.74  ? 72  GLY F CA  1 
ATOM   1652  C  C   . GLY B  1 72  ? 15.119  16.128  41.177  1.00 28.68  ? 72  GLY F C   1 
ATOM   1653  O  O   . GLY B  1 72  ? 15.923  16.835  40.539  1.00 27.50  ? 72  GLY F O   1 
ATOM   1654  N  N   . GLY B  1 73  ? 14.947  14.828  40.963  1.00 29.34  ? 73  GLY F N   1 
ATOM   1655  C  CA  . GLY B  1 73  ? 15.573  14.146  39.845  1.00 28.69  ? 73  GLY F CA  1 
ATOM   1656  C  C   . GLY B  1 73  ? 14.637  14.219  38.644  1.00 28.73  ? 73  GLY F C   1 
ATOM   1657  O  O   . GLY B  1 73  ? 13.460  14.551  38.805  1.00 29.33  ? 73  GLY F O   1 
ATOM   1658  N  N   . PRO B  1 74  ? 15.155  13.918  37.434  1.00 28.12  ? 74  PRO F N   1 
ATOM   1659  C  CA  . PRO B  1 74  ? 14.357  13.943  36.204  1.00 28.30  ? 74  PRO F CA  1 
ATOM   1660  C  C   . PRO B  1 74  ? 13.112  13.036  36.200  1.00 30.04  ? 74  PRO F C   1 
ATOM   1661  O  O   . PRO B  1 74  ? 12.124  13.377  35.553  1.00 30.37  ? 74  PRO F O   1 
ATOM   1662  C  CB  . PRO B  1 74  ? 15.355  13.506  35.114  1.00 27.64  ? 74  PRO F CB  1 
ATOM   1663  C  CG  . PRO B  1 74  ? 16.542  12.969  35.826  1.00 27.46  ? 74  PRO F CG  1 
ATOM   1664  C  CD  . PRO B  1 74  ? 16.580  13.649  37.157  1.00 27.32  ? 74  PRO F CD  1 
ATOM   1665  N  N   . LYS B  1 75  ? 13.167  11.909  36.916  1.00 31.18  ? 75  LYS F N   1 
ATOM   1666  C  CA  . LYS B  1 75  ? 12.046  10.979  37.003  1.00 33.23  ? 75  LYS F CA  1 
ATOM   1667  C  C   . LYS B  1 75  ? 10.945  11.428  37.976  1.00 34.24  ? 75  LYS F C   1 
ATOM   1668  O  O   . LYS B  1 75  ? 9.883   10.835  37.981  1.00 35.97  ? 75  LYS F O   1 
ATOM   1669  C  CB  . LYS B  1 75  ? 12.530  9.587   37.422  1.00 34.35  ? 75  LYS F CB  1 
ATOM   1670  C  CG  . LYS B  1 75  ? 13.548  8.955   36.474  1.00 34.01  ? 75  LYS F CG  1 
ATOM   1671  C  CD  . LYS B  1 75  ? 14.309  7.819   37.142  1.00 34.90  ? 75  LYS F CD  1 
ATOM   1672  C  CE  . LYS B  1 75  ? 13.415  6.641   37.461  1.00 37.23  ? 75  LYS F CE  1 
ATOM   1673  N  NZ  . LYS B  1 75  ? 14.187  5.530   38.075  1.00 38.29  ? 75  LYS F NZ  1 
ATOM   1674  N  N   . ASP B  1 76  ? 11.202  12.451  38.794  1.00 33.57  ? 76  ASP F N   1 
ATOM   1675  C  CA  . ASP B  1 76  ? 10.265  12.883  39.834  1.00 34.87  ? 76  ASP F CA  1 
ATOM   1676  C  C   . ASP B  1 76  ? 9.233   13.838  39.265  1.00 35.11  ? 76  ASP F C   1 
ATOM   1677  O  O   . ASP B  1 76  ? 9.554   14.687  38.430  1.00 33.78  ? 76  ASP F O   1 
ATOM   1678  C  CB  . ASP B  1 76  ? 11.005  13.617  40.971  1.00 34.29  ? 76  ASP F CB  1 
ATOM   1679  C  CG  . ASP B  1 76  ? 11.968  12.723  41.731  1.00 34.47  ? 76  ASP F CG  1 
ATOM   1680  O  OD1 . ASP B  1 76  ? 11.593  11.593  42.100  1.00 36.02  ? 76  ASP F OD1 1 
ATOM   1681  O  OD2 . ASP B  1 76  ? 13.104  13.164  41.989  1.00 33.41  ? 76  ASP F OD2 1 
ATOM   1682  N  N   . GLU B  1 77  ? 8.010   13.737  39.765  1.00 36.95  ? 77  GLU F N   1 
ATOM   1683  C  CA  . GLU B  1 77  ? 6.984   14.728  39.478  1.00 37.59  ? 77  GLU F CA  1 
ATOM   1684  C  C   . GLU B  1 77  ? 7.349   16.082  40.098  1.00 36.66  ? 77  GLU F C   1 
ATOM   1685  O  O   . GLU B  1 77  ? 7.195   17.138  39.455  1.00 36.06  ? 77  GLU F O   1 
ATOM   1686  C  CB  . GLU B  1 77  ? 5.627   14.251  39.997  1.00 40.18  ? 77  GLU F CB  1 
ATOM   1687  C  CG  . GLU B  1 77  ? 4.456   15.111  39.550  1.00 41.34  ? 77  GLU F CG  1 
ATOM   1688  C  CD  . GLU B  1 77  ? 3.991   14.815  38.133  0.75 41.68  ? 77  GLU F CD  1 
ATOM   1689  O  OE1 . GLU B  1 77  ? 4.790   14.329  37.305  0.75 40.62  ? 77  GLU F OE1 1 
ATOM   1690  O  OE2 . GLU B  1 77  ? 2.813   15.083  37.843  0.75 43.43  ? 77  GLU F OE2 1 
ATOM   1691  N  N   . GLU B  1 78  ? 7.826   16.043  41.342  1.00 36.77  ? 78  GLU F N   1 
ATOM   1692  C  CA  . GLU B  1 78  ? 8.320   17.237  42.028  1.00 36.15  ? 78  GLU F CA  1 
ATOM   1693  C  C   . GLU B  1 78  ? 9.768   17.475  41.597  1.00 33.82  ? 78  GLU F C   1 
ATOM   1694  O  O   . GLU B  1 78  ? 10.697  16.832  42.091  1.00 33.52  ? 78  GLU F O   1 
ATOM   1695  C  CB  . GLU B  1 78  ? 8.192   17.076  43.551  1.00 37.80  ? 78  GLU F CB  1 
ATOM   1696  C  CG  . GLU B  1 78  ? 8.497   18.330  44.366  1.00 37.98  ? 78  GLU F CG  1 
ATOM   1697  C  CD  . GLU B  1 78  ? 7.449   19.427  44.237  1.00 39.09  ? 78  GLU F CD  1 
ATOM   1698  O  OE1 . GLU B  1 78  ? 6.293   19.153  43.857  1.00 40.52  ? 78  GLU F OE1 1 
ATOM   1699  O  OE2 . GLU B  1 78  ? 7.789   20.592  44.529  1.00 39.03  ? 78  GLU F OE2 1 
ATOM   1700  N  N   . ARG B  1 79  ? 9.937   18.370  40.631  1.00 32.35  ? 79  ARG F N   1 
ATOM   1701  C  CA  . ARG B  1 79  ? 11.250  18.749  40.122  1.00 30.40  ? 79  ARG F CA  1 
ATOM   1702  C  C   . ARG B  1 79  ? 11.138  20.120  39.487  1.00 29.72  ? 79  ARG F C   1 
ATOM   1703  O  O   . ARG B  1 79  ? 10.042  20.568  39.142  1.00 30.44  ? 79  ARG F O   1 
ATOM   1704  C  CB  . ARG B  1 79  ? 11.752  17.753  39.069  1.00 29.50  ? 79  ARG F CB  1 
ATOM   1705  C  CG  . ARG B  1 79  ? 10.808  17.584  37.876  1.00 29.87  ? 79  ARG F CG  1 
ATOM   1706  C  CD  . ARG B  1 79  ? 11.400  16.731  36.766  1.00 29.12  ? 79  ARG F CD  1 
ATOM   1707  N  NE  . ARG B  1 79  ? 12.137  17.552  35.802  1.00 27.75  ? 79  ARG F NE  1 
ATOM   1708  C  CZ  . ARG B  1 79  ? 12.574  17.133  34.615  1.00 27.18  ? 79  ARG F CZ  1 
ATOM   1709  N  NH1 . ARG B  1 79  ? 12.377  15.884  34.202  1.00 27.89  ? 79  ARG F NH1 1 
ATOM   1710  N  NH2 . ARG B  1 79  ? 13.208  17.981  33.822  1.00 26.20  ? 79  ARG F NH2 1 
ATOM   1711  N  N   . HIS B  1 80  ? 12.283  20.763  39.333  1.00 28.30  ? 80  HIS F N   1 
ATOM   1712  C  CA  . HIS B  1 80  ? 12.418  21.926  38.475  1.00 27.59  ? 80  HIS F CA  1 
ATOM   1713  C  C   . HIS B  1 80  ? 12.404  21.441  37.024  1.00 26.79  ? 80  HIS F C   1 
ATOM   1714  O  O   . HIS B  1 80  ? 12.840  20.320  36.736  1.00 26.31  ? 80  HIS F O   1 
ATOM   1715  C  CB  . HIS B  1 80  ? 13.719  22.689  38.786  1.00 26.76  ? 80  HIS F CB  1 
ATOM   1716  C  CG  . HIS B  1 80  ? 13.827  23.133  40.209  1.00 27.66  ? 80  HIS F CG  1 
ATOM   1717  N  ND1 . HIS B  1 80  ? 15.022  23.247  40.879  1.00 27.39  ? 80  HIS F ND1 1 
ATOM   1718  C  CD2 . HIS B  1 80  ? 12.869  23.483  41.095  1.00 29.13  ? 80  HIS F CD2 1 
ATOM   1719  C  CE1 . HIS B  1 80  ? 14.797  23.653  42.114  1.00 28.63  ? 80  HIS F CE1 1 
ATOM   1720  N  NE2 . HIS B  1 80  ? 13.498  23.810  42.270  1.00 29.70  ? 80  HIS F NE2 1 
ATOM   1721  N  N   . VAL B  1 81  ? 11.902  22.273  36.112  1.00 26.78  ? 81  VAL F N   1 
ATOM   1722  C  CA  . VAL B  1 81  ? 11.978  21.953  34.673  1.00 26.21  ? 81  VAL F CA  1 
ATOM   1723  C  C   . VAL B  1 81  ? 13.433  21.678  34.257  1.00 24.88  ? 81  VAL F C   1 
ATOM   1724  O  O   . VAL B  1 81  ? 13.703  20.751  33.488  1.00 24.60  ? 81  VAL F O   1 
ATOM   1725  C  CB  . VAL B  1 81  ? 11.363  23.072  33.796  1.00 26.53  ? 81  VAL F CB  1 
ATOM   1726  C  CG1 . VAL B  1 81  ? 11.703  22.889  32.317  1.00 25.92  ? 81  VAL F CG1 1 
ATOM   1727  C  CG2 . VAL B  1 81  ? 9.858   23.090  33.967  1.00 28.11  ? 81  VAL F CG2 1 
ATOM   1728  N  N   . GLY B  1 82  ? 14.364  22.466  34.794  1.00 24.29  ? 82  GLY F N   1 
ATOM   1729  C  CA  . GLY B  1 82  ? 15.778  22.318  34.474  1.00 23.31  ? 82  GLY F CA  1 
ATOM   1730  C  C   . GLY B  1 82  ? 16.510  21.141  35.109  1.00 23.16  ? 82  GLY F C   1 
ATOM   1731  O  O   . GLY B  1 82  ? 17.701  20.988  34.872  1.00 22.51  ? 82  GLY F O   1 
ATOM   1732  N  N   . ASP B  1 83  ? 15.819  20.306  35.896  1.00 23.86  ? 83  ASP F N   1 
ATOM   1733  C  CA  . ASP B  1 83  ? 16.465  19.209  36.611  1.00 23.97  ? 83  ASP F CA  1 
ATOM   1734  C  C   . ASP B  1 83  ? 16.709  17.996  35.708  1.00 23.98  ? 83  ASP F C   1 
ATOM   1735  O  O   . ASP B  1 83  ? 15.895  17.082  35.659  1.00 24.74  ? 83  ASP F O   1 
ATOM   1736  C  CB  . ASP B  1 83  ? 15.644  18.786  37.833  1.00 24.91  ? 83  ASP F CB  1 
ATOM   1737  C  CG  . ASP B  1 83  ? 15.658  19.819  38.977  1.00 25.23  ? 83  ASP F CG  1 
ATOM   1738  O  OD1 . ASP B  1 83  ? 16.546  20.720  39.095  1.00 24.40  ? 83  ASP F OD1 1 
ATOM   1739  O  OD2 . ASP B  1 83  ? 14.737  19.694  39.819  1.00 26.17  ? 83  ASP F OD2 1 
ATOM   1740  N  N   . LEU B  1 84  ? 17.865  17.965  35.038  1.00 23.44  ? 84  LEU F N   1 
ATOM   1741  C  CA  . LEU B  1 84  ? 18.217  16.823  34.171  1.00 23.67  ? 84  LEU F CA  1 
ATOM   1742  C  C   . LEU B  1 84  ? 19.059  15.728  34.851  1.00 24.14  ? 84  LEU F C   1 
ATOM   1743  O  O   . LEU B  1 84  ? 19.482  14.768  34.186  1.00 24.63  ? 84  LEU F O   1 
ATOM   1744  C  CB  . LEU B  1 84  ? 18.871  17.318  32.872  1.00 23.06  ? 84  LEU F CB  1 
ATOM   1745  C  CG  . LEU B  1 84  ? 18.000  18.309  32.093  1.00 22.98  ? 84  LEU F CG  1 
ATOM   1746  C  CD1 . LEU B  1 84  ? 18.772  18.929  30.945  1.00 22.48  ? 84  LEU F CD1 1 
ATOM   1747  C  CD2 . LEU B  1 84  ? 16.731  17.640  31.574  1.00 23.82  ? 84  LEU F CD2 1 
ATOM   1748  N  N   . GLY B  1 85  ? 19.287  15.848  36.162  1.00 24.35  ? 85  GLY F N   1 
ATOM   1749  C  CA  . GLY B  1 85  ? 19.890  14.775  36.945  1.00 24.93  ? 85  GLY F CA  1 
ATOM   1750  C  C   . GLY B  1 85  ? 21.402  14.824  36.891  1.00 24.55  ? 85  GLY F C   1 
ATOM   1751  O  O   . GLY B  1 85  ? 21.988  15.897  37.035  1.00 23.92  ? 85  GLY F O   1 
ATOM   1752  N  N   . ASN B  1 86  ? 22.021  13.659  36.696  1.00 25.07  ? 86  ASN F N   1 
ATOM   1753  C  CA  . ASN B  1 86  ? 23.473  13.538  36.601  1.00 25.09  ? 86  ASN F CA  1 
ATOM   1754  C  C   . ASN B  1 86  ? 23.905  13.046  35.220  1.00 25.08  ? 86  ASN F C   1 
ATOM   1755  O  O   . ASN B  1 86  ? 23.129  12.402  34.499  1.00 25.33  ? 86  ASN F O   1 
ATOM   1756  C  CB  . ASN B  1 86  ? 23.996  12.572  37.666  1.00 26.13  ? 86  ASN F CB  1 
ATOM   1757  C  CG  . ASN B  1 86  ? 23.900  13.149  39.058  1.00 26.35  ? 86  ASN F CG  1 
ATOM   1758  O  OD1 . ASN B  1 86  ? 24.513  14.179  39.352  1.00 25.94  ? 86  ASN F OD1 1 
ATOM   1759  N  ND2 . ASN B  1 86  ? 23.108  12.510  39.917  1.00 27.18  ? 86  ASN F ND2 1 
ATOM   1760  N  N   . VAL B  1 87  ? 25.142  13.388  34.868  1.00 24.87  ? 87  VAL F N   1 
ATOM   1761  C  CA  . VAL B  1 87  ? 25.881  12.729  33.792  1.00 25.38  ? 87  VAL F CA  1 
ATOM   1762  C  C   . VAL B  1 87  ? 27.098  12.080  34.425  1.00 26.29  ? 87  VAL F C   1 
ATOM   1763  O  O   . VAL B  1 87  ? 27.579  12.536  35.462  1.00 26.34  ? 87  VAL F O   1 
ATOM   1764  C  CB  . VAL B  1 87  ? 26.299  13.686  32.649  1.00 24.70  ? 87  VAL F CB  1 
ATOM   1765  C  CG1 . VAL B  1 87  ? 25.063  14.255  31.964  1.00 24.12  ? 87  VAL F CG1 1 
ATOM   1766  C  CG2 . VAL B  1 87  ? 27.218  14.806  33.138  1.00 24.29  ? 87  VAL F CG2 1 
ATOM   1767  N  N   . THR B  1 88  ? 27.591  11.026  33.791  1.00 27.32  ? 88  THR F N   1 
ATOM   1768  C  CA  . THR B  1 88  ? 28.680  10.225  34.323  1.00 28.61  ? 88  THR F CA  1 
ATOM   1769  C  C   . THR B  1 88  ? 29.918  10.373  33.435  1.00 29.07  ? 88  THR F C   1 
ATOM   1770  O  O   . THR B  1 88  ? 29.868  10.057  32.242  1.00 29.44  ? 88  THR F O   1 
ATOM   1771  C  CB  . THR B  1 88  ? 28.283  8.734   34.409  1.00 29.93  ? 88  THR F CB  1 
ATOM   1772  O  OG1 . THR B  1 88  ? 27.075  8.596   35.164  1.00 29.71  ? 88  THR F OG1 1 
ATOM   1773  C  CG2 . THR B  1 88  ? 29.374  7.902   35.087  1.00 31.38  ? 88  THR F CG2 1 
ATOM   1774  N  N   . ALA B  1 89  ? 31.012  10.869  34.014  1.00 29.30  ? 89  ALA F N   1 
ATOM   1775  C  CA  . ALA B  1 89  ? 32.310  10.875  33.344  1.00 30.20  ? 89  ALA F CA  1 
ATOM   1776  C  C   . ALA B  1 89  ? 33.013  9.546   33.573  1.00 32.02  ? 89  ALA F C   1 
ATOM   1777  O  O   . ALA B  1 89  ? 33.000  9.011   34.684  1.00 32.60  ? 89  ALA F O   1 
ATOM   1778  C  CB  . ALA B  1 89  ? 33.177  12.014  33.850  1.00 29.95  ? 89  ALA F CB  1 
ATOM   1779  N  N   . ASP B  1 90  ? 33.639  9.030   32.518  1.00 33.15  ? 90  ASP F N   1 
ATOM   1780  C  CA  . ASP B  1 90  ? 34.384  7.778   32.589  1.00 35.24  ? 90  ASP F CA  1 
ATOM   1781  C  C   . ASP B  1 90  ? 35.788  8.038   33.161  1.00 36.26  ? 90  ASP F C   1 
ATOM   1782  O  O   . ASP B  1 90  ? 36.106  9.161   33.544  1.00 35.38  ? 90  ASP F O   1 
ATOM   1783  C  CB  . ASP B  1 90  ? 34.429  7.100   31.207  1.00 36.30  ? 90  ASP F CB  1 
ATOM   1784  C  CG  . ASP B  1 90  ? 35.256  7.878   30.163  1.00 36.47  ? 90  ASP F CG  1 
ATOM   1785  O  OD1 . ASP B  1 90  ? 36.041  8.805   30.498  1.00 36.09  ? 90  ASP F OD1 1 
ATOM   1786  O  OD2 . ASP B  1 90  ? 35.104  7.538   28.973  1.00 37.20  ? 90  ASP F OD2 1 
ATOM   1787  N  N   . LYS B  1 91  ? 36.622  7.005   33.205  1.00 38.37  ? 91  LYS F N   1 
ATOM   1788  C  CA  . LYS B  1 91  ? 37.974  7.113   33.782  1.00 39.80  ? 91  LYS F CA  1 
ATOM   1789  C  C   . LYS B  1 91  ? 38.932  8.076   33.057  1.00 39.86  ? 91  LYS F C   1 
ATOM   1790  O  O   . LYS B  1 91  ? 39.923  8.507   33.649  1.00 40.65  ? 91  LYS F O   1 
ATOM   1791  C  CB  . LYS B  1 91  ? 38.606  5.724   33.907  1.00 42.35  ? 91  LYS F CB  1 
ATOM   1792  C  CG  . LYS B  1 91  ? 38.930  5.041   32.589  1.00 43.79  ? 91  LYS F CG  1 
ATOM   1793  C  CD  . LYS B  1 91  ? 39.159  3.548   32.790  1.00 46.23  ? 91  LYS F CD  1 
ATOM   1794  C  CE  . LYS B  1 91  ? 39.931  2.935   31.629  1.00 48.39  ? 91  LYS F CE  1 
ATOM   1795  N  NZ  . LYS B  1 91  ? 39.313  3.262   30.307  1.00 47.47  ? 91  LYS F NZ  1 
ATOM   1796  N  N   . ASP B  1 92  ? 38.630  8.411   31.799  1.00 39.12  ? 92  ASP F N   1 
ATOM   1797  C  CA  . ASP B  1 92  ? 39.368  9.437   31.044  1.00 39.08  ? 92  ASP F CA  1 
ATOM   1798  C  C   . ASP B  1 92  ? 38.764  10.843  31.166  1.00 36.79  ? 92  ASP F C   1 
ATOM   1799  O  O   . ASP B  1 92  ? 39.184  11.758  30.473  1.00 36.62  ? 92  ASP F O   1 
ATOM   1800  C  CB  . ASP B  1 92  ? 39.443  9.059   29.558  1.00 39.95  ? 92  ASP F CB  1 
ATOM   1801  C  CG  . ASP B  1 92  ? 40.181  7.749   29.307  1.00 42.56  ? 92  ASP F CG  1 
ATOM   1802  O  OD1 . ASP B  1 92  ? 41.157  7.406   30.020  1.00 44.20  ? 92  ASP F OD1 1 
ATOM   1803  O  OD2 . ASP B  1 92  ? 39.784  7.062   28.350  1.00 43.33  ? 92  ASP F OD2 1 
ATOM   1804  N  N   . GLY B  1 93  ? 37.785  11.018  32.044  1.00 35.20  ? 93  GLY F N   1 
ATOM   1805  C  CA  . GLY B  1 93  ? 37.154  12.302  32.243  1.00 33.35  ? 93  GLY F CA  1 
ATOM   1806  C  C   . GLY B  1 93  ? 36.118  12.704  31.205  1.00 31.86  ? 93  GLY F C   1 
ATOM   1807  O  O   . GLY B  1 93  ? 35.745  13.873  31.151  1.00 30.63  ? 93  GLY F O   1 
ATOM   1808  N  N   . VAL B  1 94  ? 35.644  11.750  30.398  1.00 32.11  ? 94  VAL F N   1 
ATOM   1809  C  CA  . VAL B  1 94  ? 34.675  12.036  29.332  1.00 31.06  ? 94  VAL F CA  1 
ATOM   1810  C  C   . VAL B  1 94  ? 33.261  11.562  29.708  1.00 30.09  ? 94  VAL F C   1 
ATOM   1811  O  O   . VAL B  1 94  ? 33.061  10.392  30.042  1.00 30.92  ? 94  VAL F O   1 
ATOM   1812  C  CB  . VAL B  1 94  ? 35.106  11.403  27.982  1.00 32.38  ? 94  VAL F CB  1 
ATOM   1813  C  CG1 . VAL B  1 94  ? 34.079  11.690  26.882  1.00 31.55  ? 94  VAL F CG1 1 
ATOM   1814  C  CG2 . VAL B  1 94  ? 36.472  11.920  27.564  1.00 33.47  ? 94  VAL F CG2 1 
ATOM   1815  N  N   . ALA B  1 95  ? 32.298  12.479  29.651  1.00 28.54  ? 95  ALA F N   1 
ATOM   1816  C  CA  . ALA B  1 95  ? 30.884  12.141  29.769  1.00 27.89  ? 95  ALA F CA  1 
ATOM   1817  C  C   . ALA B  1 95  ? 30.261  12.126  28.384  1.00 27.90  ? 95  ALA F C   1 
ATOM   1818  O  O   . ALA B  1 95  ? 30.094  13.182  27.753  1.00 27.10  ? 95  ALA F O   1 
ATOM   1819  C  CB  . ALA B  1 95  ? 30.155  13.131  30.664  1.00 26.48  ? 95  ALA F CB  1 
ATOM   1820  N  N   . ASP B  1 96  ? 29.948  10.926  27.906  1.00 29.02  ? 96  ASP F N   1 
ATOM   1821  C  CA  . ASP B  1 96  ? 29.178  10.760  26.687  1.00 29.40  ? 96  ASP F CA  1 
ATOM   1822  C  C   . ASP B  1 96  ? 27.691  10.857  27.042  1.00 28.56  ? 96  ASP F C   1 
ATOM   1823  O  O   . ASP B  1 96  ? 27.049  9.868   27.341  1.00 29.22  ? 96  ASP F O   1 
ATOM   1824  C  CB  . ASP B  1 96  ? 29.508  9.430   26.013  1.00 31.34  ? 96  ASP F CB  1 
ATOM   1825  C  CG  . ASP B  1 96  ? 30.873  9.443   25.365  1.00 32.48  ? 96  ASP F CG  1 
ATOM   1826  O  OD1 . ASP B  1 96  ? 31.180  10.429  24.658  1.00 32.13  ? 96  ASP F OD1 1 
ATOM   1827  O  OD2 . ASP B  1 96  ? 31.645  8.484   25.564  1.00 34.07  ? 96  ASP F OD2 1 
ATOM   1828  N  N   . VAL B  1 97  ? 27.168  12.071  27.007  1.00 27.34  ? 97  VAL F N   1 
ATOM   1829  C  CA  . VAL B  1 97  ? 25.808  12.344  27.490  1.00 26.71  ? 97  VAL F CA  1 
ATOM   1830  C  C   . VAL B  1 97  ? 24.777  11.777  26.510  1.00 27.60  ? 97  VAL F C   1 
ATOM   1831  O  O   . VAL B  1 97  ? 24.903  11.947  25.305  1.00 27.97  ? 97  VAL F O   1 
ATOM   1832  C  CB  . VAL B  1 97  ? 25.581  13.862  27.678  1.00 25.34  ? 97  VAL F CB  1 
ATOM   1833  C  CG1 . VAL B  1 97  ? 24.149  14.163  28.129  1.00 24.76  ? 97  VAL F CG1 1 
ATOM   1834  C  CG2 . VAL B  1 97  ? 26.595  14.427  28.664  1.00 24.91  ? 97  VAL F CG2 1 
ATOM   1835  N  N   . SER B  1 98  ? 23.783  11.073  27.041  1.00 28.32  ? 98  SER F N   1 
ATOM   1836  C  CA  . SER B  1 98  ? 22.624  10.650  26.264  1.00 29.33  ? 98  SER F CA  1 
ATOM   1837  C  C   . SER B  1 98  ? 21.447  10.563  27.222  1.00 29.38  ? 98  SER F C   1 
ATOM   1838  O  O   . SER B  1 98  ? 21.380  9.658   28.039  1.00 30.11  ? 98  SER F O   1 
ATOM   1839  C  CB  . SER B  1 98  ? 22.867  9.315   25.552  1.00 31.19  ? 98  SER F CB  1 
ATOM   1840  O  OG  . SER B  1 98  ? 21.815  9.033   24.630  1.00 32.14  ? 98  SER F OG  1 
ATOM   1841  N  N   . ILE B  1 99  ? 20.562  11.553  27.134  1.00 28.83  ? 99  ILE F N   1 
ATOM   1842  C  CA  . ILE B  1 99  ? 19.421  11.716  28.024  1.00 28.88  ? 99  ILE F CA  1 
ATOM   1843  C  C   . ILE B  1 99  ? 18.200  12.005  27.144  1.00 29.49  ? 99  ILE F C   1 
ATOM   1844  O  O   . ILE B  1 99  ? 18.322  12.620  26.082  1.00 29.27  ? 99  ILE F O   1 
ATOM   1845  C  CB  . ILE B  1 99  ? 19.672  12.875  29.028  1.00 27.60  ? 99  ILE F CB  1 
ATOM   1846  C  CG1 . ILE B  1 99  ? 20.603  12.404  30.145  1.00 27.62  ? 99  ILE F CG1 1 
ATOM   1847  C  CG2 . ILE B  1 99  ? 18.377  13.386  29.655  1.00 27.60  ? 99  ILE F CG2 1 
ATOM   1848  C  CD1 . ILE B  1 99  ? 21.183  13.536  30.976  1.00 26.55  ? 99  ILE F CD1 1 
ATOM   1849  N  N   . GLU B  1 100 ? 17.042  11.523  27.585  1.00 30.43  ? 100 GLU F N   1 
ATOM   1850  C  CA  . GLU B  1 100 ? 15.754  11.887  27.009  1.00 31.15  ? 100 GLU F CA  1 
ATOM   1851  C  C   . GLU B  1 100 ? 14.891  12.436  28.134  1.00 30.70  ? 100 GLU F C   1 
ATOM   1852  O  O   . GLU B  1 100 ? 14.784  11.823  29.196  1.00 31.03  ? 100 GLU F O   1 
ATOM   1853  C  CB  . GLU B  1 100 ? 15.080  10.676  26.370  1.00 33.29  ? 100 GLU F CB  1 
ATOM   1854  C  CG  . GLU B  1 100 ? 13.769  11.009  25.679  1.00 34.50  ? 100 GLU F CG  1 
ATOM   1855  C  CD  . GLU B  1 100 ? 13.176  9.832   24.923  1.00 36.96  ? 100 GLU F CD  1 
ATOM   1856  O  OE1 . GLU B  1 100 ? 12.147  9.273   25.369  1.00 38.49  ? 100 GLU F OE1 1 
ATOM   1857  O  OE2 . GLU B  1 100 ? 13.745  9.461   23.878  1.00 37.91  ? 100 GLU F OE2 1 
ATOM   1858  N  N   . ASP B  1 101 ? 14.277  13.590  27.897  1.00 30.08  ? 101 ASP F N   1 
ATOM   1859  C  CA  . ASP B  1 101 ? 13.453  14.246  28.900  1.00 29.76  ? 101 ASP F CA  1 
ATOM   1860  C  C   . ASP B  1 101 ? 12.213  14.845  28.258  1.00 30.42  ? 101 ASP F C   1 
ATOM   1861  O  O   . ASP B  1 101 ? 12.295  15.449  27.182  1.00 30.22  ? 101 ASP F O   1 
ATOM   1862  C  CB  . ASP B  1 101 ? 14.237  15.345  29.615  1.00 28.23  ? 101 ASP F CB  1 
ATOM   1863  C  CG  . ASP B  1 101 ? 13.536  15.817  30.883  1.00 28.41  ? 101 ASP F CG  1 
ATOM   1864  O  OD1 . ASP B  1 101 ? 13.591  15.067  31.891  1.00 28.92  ? 101 ASP F OD1 1 
ATOM   1865  O  OD2 . ASP B  1 101 ? 12.910  16.910  30.874  1.00 28.09  ? 101 ASP F OD2 1 
ATOM   1866  N  N   . SER B  1 102 ? 11.080  14.695  28.946  1.00 31.28  ? 102 SER F N   1 
ATOM   1867  C  CA  . SER B  1 102 ? 9.781   15.157  28.466  1.00 32.27  ? 102 SER F CA  1 
ATOM   1868  C  C   . SER B  1 102 ? 9.277   16.411  29.177  1.00 31.66  ? 102 SER F C   1 
ATOM   1869  O  O   . SER B  1 102 ? 8.167   16.862  28.906  1.00 32.76  ? 102 SER F O   1 
ATOM   1870  C  CB  . SER B  1 102 ? 8.765   14.039  28.641  1.00 34.37  ? 102 SER F CB  1 
ATOM   1871  O  OG  . SER B  1 102 ? 9.102   12.962  27.805  1.00 35.31  ? 102 SER F OG  1 
ATOM   1872  N  N   . VAL B  1 103 ? 10.075  16.970  30.081  1.00 30.02  ? 103 VAL F N   1 
ATOM   1873  C  CA  . VAL B  1 103 ? 9.662   18.127  30.863  1.00 29.70  ? 103 VAL F CA  1 
ATOM   1874  C  C   . VAL B  1 103 ? 10.272  19.402  30.276  1.00 28.35  ? 103 VAL F C   1 
ATOM   1875  O  O   . VAL B  1 103 ? 9.561   20.388  30.086  1.00 28.79  ? 103 VAL F O   1 
ATOM   1876  C  CB  . VAL B  1 103 ? 9.987   17.922  32.361  1.00 29.52  ? 103 VAL F CB  1 
ATOM   1877  C  CG1 . VAL B  1 103 ? 9.822   19.217  33.146  1.00 29.35  ? 103 VAL F CG1 1 
ATOM   1878  C  CG2 . VAL B  1 103 ? 9.074   16.835  32.940  1.00 31.14  ? 103 VAL F CG2 1 
ATOM   1879  N  N   . ILE B  1 104 ? 11.571  19.384  29.973  1.00 26.86  ? 104 ILE F N   1 
ATOM   1880  C  CA  . ILE B  1 104 ? 12.151  20.428  29.122  1.00 25.92  ? 104 ILE F CA  1 
ATOM   1881  C  C   . ILE B  1 104 ? 11.504  20.382  27.726  1.00 26.63  ? 104 ILE F C   1 
ATOM   1882  O  O   . ILE B  1 104 ? 10.953  19.350  27.304  1.00 27.53  ? 104 ILE F O   1 
ATOM   1883  C  CB  . ILE B  1 104 ? 13.690  20.345  28.986  1.00 24.68  ? 104 ILE F CB  1 
ATOM   1884  C  CG1 . ILE B  1 104 ? 14.144  18.989  28.419  1.00 24.83  ? 104 ILE F CG1 1 
ATOM   1885  C  CG2 . ILE B  1 104 ? 14.352  20.629  30.333  1.00 24.04  ? 104 ILE F CG2 1 
ATOM   1886  C  CD1 . ILE B  1 104 ? 15.530  18.997  27.832  1.00 23.94  ? 104 ILE F CD1 1 
ATOM   1887  N  N   . SER B  1 105 ? 11.549  21.515  27.040  1.00 26.29  ? 105 SER F N   1 
ATOM   1888  C  CA  . SER B  1 105 ? 11.046  21.614  25.678  1.00 27.06  ? 105 SER F CA  1 
ATOM   1889  C  C   . SER B  1 105 ? 11.874  22.616  24.882  1.00 26.38  ? 105 SER F C   1 
ATOM   1890  O  O   . SER B  1 105 ? 12.627  23.399  25.455  1.00 25.45  ? 105 SER F O   1 
ATOM   1891  C  CB  . SER B  1 105 ? 9.563   22.022  25.681  1.00 28.43  ? 105 SER F CB  1 
ATOM   1892  O  OG  . SER B  1 105 ? 8.996   21.793  24.411  1.00 29.47  ? 105 SER F OG  1 
ATOM   1893  N  N   . LEU B  1 106 ? 11.733  22.571  23.563  1.00 27.08  ? 106 LEU F N   1 
ATOM   1894  C  CA  . LEU B  1 106 ? 12.341  23.568  22.683  1.00 26.90  ? 106 LEU F CA  1 
ATOM   1895  C  C   . LEU B  1 106 ? 11.304  24.537  22.131  1.00 28.08  ? 106 LEU F C   1 
ATOM   1896  O  O   . LEU B  1 106 ? 11.577  25.249  21.168  1.00 28.43  ? 106 LEU F O   1 
ATOM   1897  C  CB  . LEU B  1 106 ? 13.120  22.888  21.549  1.00 26.97  ? 106 LEU F CB  1 
ATOM   1898  C  CG  . LEU B  1 106 ? 14.196  21.893  21.973  1.00 26.08  ? 106 LEU F CG  1 
ATOM   1899  C  CD1 . LEU B  1 106 ? 14.952  21.408  20.749  1.00 26.48  ? 106 LEU F CD1 1 
ATOM   1900  C  CD2 . LEU B  1 106 ? 15.162  22.491  22.978  1.00 24.78  ? 106 LEU F CD2 1 
ATOM   1901  N  N   . SER B  1 107 ? 10.118  24.566  22.746  1.00 28.93  ? 107 SER F N   1 
ATOM   1902  C  CA  . SER B  1 107 ? 9.109   25.581  22.452  1.00 30.20  ? 107 SER F CA  1 
ATOM   1903  C  C   . SER B  1 107 ? 8.149   25.718  23.640  1.00 30.77  ? 107 SER F C   1 
ATOM   1904  O  O   . SER B  1 107 ? 8.159   24.891  24.556  1.00 30.25  ? 107 SER F O   1 
ATOM   1905  C  CB  . SER B  1 107 ? 8.336   25.238  21.168  1.00 31.80  ? 107 SER F CB  1 
ATOM   1906  O  OG  . SER B  1 107 ? 7.480   24.134  21.363  1.00 32.79  ? 107 SER F OG  1 
ATOM   1907  N  N   . GLY B  1 108 ? 7.344   26.771  23.618  1.00 31.97  ? 108 GLY F N   1 
ATOM   1908  C  CA  . GLY B  1 108 ? 6.333   27.001  24.654  1.00 33.07  ? 108 GLY F CA  1 
ATOM   1909  C  C   . GLY B  1 108 ? 6.917   27.454  25.978  1.00 32.15  ? 108 GLY F C   1 
ATOM   1910  O  O   . GLY B  1 108 ? 8.059   27.924  26.035  1.00 30.97  ? 108 GLY F O   1 
ATOM   1911  N  N   . ASP B  1 109 ? 6.154   27.262  27.050  1.00 33.04  ? 109 ASP F N   1 
ATOM   1912  C  CA  . ASP B  1 109 ? 6.492   27.807  28.369  1.00 32.76  ? 109 ASP F CA  1 
ATOM   1913  C  C   . ASP B  1 109 ? 7.741   27.197  29.004  1.00 30.95  ? 109 ASP F C   1 
ATOM   1914  O  O   . ASP B  1 109 ? 8.448   27.886  29.728  1.00 30.40  ? 109 ASP F O   1 
ATOM   1915  C  CB  . ASP B  1 109 ? 5.317   27.667  29.347  1.00 34.41  ? 109 ASP F CB  1 
ATOM   1916  C  CG  . ASP B  1 109 ? 4.181   28.624  29.042  1.00 36.53  ? 109 ASP F CG  1 
ATOM   1917  O  OD1 . ASP B  1 109 ? 4.397   29.650  28.357  1.00 36.90  ? 109 ASP F OD1 1 
ATOM   1918  O  OD2 . ASP B  1 109 ? 3.052   28.348  29.481  1.00 38.26  ? 109 ASP F OD2 1 
ATOM   1919  N  N   . HIS B  1 110 ? 7.992   25.918  28.736  1.00 30.35  ? 110 HIS F N   1 
ATOM   1920  C  CA  . HIS B  1 110 ? 9.166   25.211  29.252  1.00 28.89  ? 110 HIS F CA  1 
ATOM   1921  C  C   . HIS B  1 110 ? 10.357  25.246  28.281  1.00 27.57  ? 110 HIS F C   1 
ATOM   1922  O  O   . HIS B  1 110 ? 11.296  24.431  28.406  1.00 26.54  ? 110 HIS F O   1 
ATOM   1923  C  CB  . HIS B  1 110 ? 8.802   23.756  29.576  1.00 29.32  ? 110 HIS F CB  1 
ATOM   1924  C  CG  . HIS B  1 110 ? 7.799   23.615  30.675  1.00 30.66  ? 110 HIS F CG  1 
ATOM   1925  N  ND1 . HIS B  1 110 ? 7.439   22.389  31.195  1.00 31.33  ? 110 HIS F ND1 1 
ATOM   1926  C  CD2 . HIS B  1 110 ? 7.097   24.542  31.370  1.00 31.72  ? 110 HIS F CD2 1 
ATOM   1927  C  CE1 . HIS B  1 110 ? 6.526   22.568  32.136  1.00 32.69  ? 110 HIS F CE1 1 
ATOM   1928  N  NE2 . HIS B  1 110 ? 6.304   23.865  32.264  1.00 32.92  ? 110 HIS F NE2 1 
ATOM   1929  N  N   . CYS B  1 111 ? 10.331  26.178  27.327  1.00 27.74  ? 111 CYS F N   1 
ATOM   1930  C  CA  . CYS B  1 111 ? 11.423  26.314  26.371  1.00 26.85  ? 111 CYS F CA  1 
ATOM   1931  C  C   . CYS B  1 111 ? 12.741  26.654  27.082  1.00 25.42  ? 111 CYS F C   1 
ATOM   1932  O  O   . CYS B  1 111 ? 12.787  27.521  27.950  1.00 25.44  ? 111 CYS F O   1 
ATOM   1933  C  CB  . CYS B  1 111 ? 11.122  27.371  25.307  1.00 27.69  ? 111 CYS F CB  1 
ATOM   1934  S  SG  . CYS B  1 111 ? 12.345  27.309  23.986  1.00 27.31  ? 111 CYS F SG  1 
ATOM   1935  N  N   . ILE B  1 112 ? 13.799  25.960  26.699  1.00 24.40  ? 112 ILE F N   1 
ATOM   1936  C  CA  . ILE B  1 112 ? 15.130  26.161  27.301  1.00 23.33  ? 112 ILE F CA  1 
ATOM   1937  C  C   . ILE B  1 112 ? 16.096  26.926  26.401  1.00 23.04  ? 112 ILE F C   1 
ATOM   1938  O  O   . ILE B  1 112 ? 17.220  27.238  26.817  1.00 22.50  ? 112 ILE F O   1 
ATOM   1939  C  CB  . ILE B  1 112 ? 15.750  24.827  27.760  1.00 22.70  ? 112 ILE F CB  1 
ATOM   1940  C  CG1 . ILE B  1 112 ? 15.980  23.864  26.590  1.00 22.74  ? 112 ILE F CG1 1 
ATOM   1941  C  CG2 . ILE B  1 112 ? 14.858  24.198  28.828  1.00 23.09  ? 112 ILE F CG2 1 
ATOM   1942  C  CD1 . ILE B  1 112 ? 16.683  22.589  26.995  1.00 22.36  ? 112 ILE F CD1 1 
ATOM   1943  N  N   . ILE B  1 113 ? 15.666  27.234  25.177  1.00 23.49  ? 113 ILE F N   1 
ATOM   1944  C  CA  . ILE B  1 113 ? 16.478  28.024  24.260  1.00 23.45  ? 113 ILE F CA  1 
ATOM   1945  C  C   . ILE B  1 113 ? 16.636  29.419  24.863  1.00 23.63  ? 113 ILE F C   1 
ATOM   1946  O  O   . ILE B  1 113 ? 15.654  30.024  25.332  1.00 24.17  ? 113 ILE F O   1 
ATOM   1947  C  CB  . ILE B  1 113 ? 15.837  28.086  22.859  1.00 24.36  ? 113 ILE F CB  1 
ATOM   1948  C  CG1 . ILE B  1 113 ? 16.005  26.732  22.163  1.00 24.27  ? 113 ILE F CG1 1 
ATOM   1949  C  CG2 . ILE B  1 113 ? 16.437  29.209  22.006  1.00 24.81  ? 113 ILE F CG2 1 
ATOM   1950  C  CD1 . ILE B  1 113 ? 15.043  26.510  21.018  1.00 25.43  ? 113 ILE F CD1 1 
ATOM   1951  N  N   . GLY B  1 114 ? 17.874  29.911  24.870  1.00 23.17  ? 114 GLY F N   1 
ATOM   1952  C  CA  . GLY B  1 114 ? 18.195  31.194  25.483  1.00 23.59  ? 114 GLY F CA  1 
ATOM   1953  C  C   . GLY B  1 114 ? 18.470  31.119  26.982  1.00 23.19  ? 114 GLY F C   1 
ATOM   1954  O  O   . GLY B  1 114 ? 18.682  32.147  27.623  1.00 23.76  ? 114 GLY F O   1 
ATOM   1955  N  N   . ARG B  1 115 ? 18.453  29.914  27.541  1.00 22.39  ? 115 ARG F N   1 
ATOM   1956  C  CA  . ARG B  1 115 ? 18.804  29.702  28.930  1.00 22.19  ? 115 ARG F CA  1 
ATOM   1957  C  C   . ARG B  1 115 ? 20.202  29.050  28.960  1.00 21.56  ? 115 ARG F C   1 
ATOM   1958  O  O   . ARG B  1 115 ? 20.838  28.869  27.903  1.00 21.39  ? 115 ARG F O   1 
ATOM   1959  C  CB  . ARG B  1 115 ? 17.701  28.890  29.609  1.00 22.16  ? 115 ARG F CB  1 
ATOM   1960  C  CG  . ARG B  1 115 ? 16.322  29.569  29.454  1.00 23.09  ? 115 ARG F CG  1 
ATOM   1961  C  CD  . ARG B  1 115 ? 15.228  28.950  30.314  1.00 23.43  ? 115 ARG F CD  1 
ATOM   1962  N  NE  . ARG B  1 115 ? 13.919  29.544  30.025  1.00 24.57  ? 115 ARG F NE  1 
ATOM   1963  C  CZ  . ARG B  1 115 ? 13.435  30.684  30.539  1.00 25.61  ? 115 ARG F CZ  1 
ATOM   1964  N  NH1 . ARG B  1 115 ? 14.123  31.420  31.420  1.00 25.77  ? 115 ARG F NH1 1 
ATOM   1965  N  NH2 . ARG B  1 115 ? 12.227  31.086  30.178  1.00 26.74  ? 115 ARG F NH2 1 
ATOM   1966  N  N   . THR B  1 116 ? 20.695  28.739  30.152  1.00 21.46  ? 116 THR F N   1 
ATOM   1967  C  CA  . THR B  1 116 ? 22.056  28.245  30.329  1.00 21.15  ? 116 THR F CA  1 
ATOM   1968  C  C   . THR B  1 116 ? 22.079  26.800  30.788  1.00 20.63  ? 116 THR F C   1 
ATOM   1969  O  O   . THR B  1 116 ? 21.392  26.445  31.744  1.00 20.75  ? 116 THR F O   1 
ATOM   1970  C  CB  . THR B  1 116 ? 22.810  29.120  31.332  1.00 21.78  ? 116 THR F CB  1 
ATOM   1971  O  OG1 . THR B  1 116 ? 22.916  30.449  30.811  1.00 22.49  ? 116 THR F OG1 1 
ATOM   1972  C  CG2 . THR B  1 116 ? 24.215  28.587  31.594  1.00 21.70  ? 116 THR F CG2 1 
ATOM   1973  N  N   . LEU B  1 117 ? 22.860  25.968  30.099  1.00 20.27  ? 117 LEU F N   1 
ATOM   1974  C  CA  . LEU B  1 117 ? 23.131  24.607  30.544  1.00 20.03  ? 117 LEU F CA  1 
ATOM   1975  C  C   . LEU B  1 117 ? 24.369  24.656  31.431  1.00 20.27  ? 117 LEU F C   1 
ATOM   1976  O  O   . LEU B  1 117 ? 25.336  25.320  31.081  1.00 20.47  ? 117 LEU F O   1 
ATOM   1977  C  CB  . LEU B  1 117 ? 23.376  23.694  29.344  1.00 19.95  ? 117 LEU F CB  1 
ATOM   1978  C  CG  . LEU B  1 117 ? 23.539  22.208  29.654  1.00 19.96  ? 117 LEU F CG  1 
ATOM   1979  C  CD1 . LEU B  1 117 ? 22.241  21.615  30.179  1.00 19.99  ? 117 LEU F CD1 1 
ATOM   1980  C  CD2 . LEU B  1 117 ? 24.023  21.447  28.430  1.00 20.20  ? 117 LEU F CD2 1 
ATOM   1981  N  N   . VAL B  1 118 ? 24.333  23.968  32.568  1.00 20.39  ? 118 VAL F N   1 
ATOM   1982  C  CA  . VAL B  1 118 ? 25.459  23.948  33.503  1.00 20.92  ? 118 VAL F CA  1 
ATOM   1983  C  C   . VAL B  1 118 ? 25.798  22.516  33.896  1.00 21.04  ? 118 VAL F C   1 
ATOM   1984  O  O   . VAL B  1 118 ? 24.902  21.733  34.200  1.00 20.85  ? 118 VAL F O   1 
ATOM   1985  C  CB  . VAL B  1 118 ? 25.163  24.752  34.786  1.00 21.42  ? 118 VAL F CB  1 
ATOM   1986  C  CG1 . VAL B  1 118 ? 26.366  24.737  35.732  1.00 22.10  ? 118 VAL F CG1 1 
ATOM   1987  C  CG2 . VAL B  1 118 ? 24.744  26.178  34.450  1.00 21.70  ? 118 VAL F CG2 1 
ATOM   1988  N  N   . VAL B  1 119 ? 27.095  22.199  33.920  1.00 21.66  ? 119 VAL F N   1 
ATOM   1989  C  CA  . VAL B  1 119 ? 27.587  20.946  34.496  1.00 22.17  ? 119 VAL F CA  1 
ATOM   1990  C  C   . VAL B  1 119 ? 28.372  21.257  35.773  1.00 23.05  ? 119 VAL F C   1 
ATOM   1991  O  O   . VAL B  1 119 ? 29.169  22.191  35.818  1.00 23.54  ? 119 VAL F O   1 
ATOM   1992  C  CB  . VAL B  1 119 ? 28.415  20.078  33.510  1.00 22.44  ? 119 VAL F CB  1 
ATOM   1993  C  CG1 . VAL B  1 119 ? 29.689  20.776  33.032  1.00 22.99  ? 119 VAL F CG1 1 
ATOM   1994  C  CG2 . VAL B  1 119 ? 28.762  18.734  34.154  1.00 22.97  ? 119 VAL F CG2 1 
ATOM   1995  N  N   . HIS B  1 120 ? 28.120  20.461  36.803  1.00 23.46  ? 120 HIS F N   1 
ATOM   1996  C  CA  . HIS B  1 120 ? 28.519  20.788  38.156  1.00 24.39  ? 120 HIS F CA  1 
ATOM   1997  C  C   . HIS B  1 120 ? 29.700  19.963  38.652  1.00 25.35  ? 120 HIS F C   1 
ATOM   1998  O  O   . HIS B  1 120 ? 30.047  18.928  38.080  1.00 25.23  ? 120 HIS F O   1 
ATOM   1999  C  CB  . HIS B  1 120 ? 27.313  20.640  39.090  1.00 24.43  ? 120 HIS F CB  1 
ATOM   2000  C  CG  . HIS B  1 120 ? 26.362  21.792  39.023  1.00 24.12  ? 120 HIS F CG  1 
ATOM   2001  N  ND1 . HIS B  1 120 ? 26.391  22.831  39.928  1.00 24.92  ? 120 HIS F ND1 1 
ATOM   2002  C  CD2 . HIS B  1 120 ? 25.375  22.086  38.145  1.00 23.41  ? 120 HIS F CD2 1 
ATOM   2003  C  CE1 . HIS B  1 120 ? 25.447  23.704  39.624  1.00 24.63  ? 120 HIS F CE1 1 
ATOM   2004  N  NE2 . HIS B  1 120 ? 24.818  23.278  38.545  1.00 23.68  ? 120 HIS F NE2 1 
ATOM   2005  N  N   . GLU B  1 121 ? 30.294  20.462  39.732  1.00 26.50  ? 121 GLU F N   1 
ATOM   2006  C  CA  . GLU B  1 121 ? 31.449  19.862  40.391  1.00 27.85  ? 121 GLU F CA  1 
ATOM   2007  C  C   . GLU B  1 121 ? 31.229  18.420  40.819  1.00 28.16  ? 121 GLU F C   1 
ATOM   2008  O  O   . GLU B  1 121 ? 32.108  17.586  40.653  1.00 28.75  ? 121 GLU F O   1 
ATOM   2009  C  CB  . GLU B  1 121 ? 31.808  20.686  41.623  1.00 29.10  ? 121 GLU F CB  1 
ATOM   2010  C  CG  . GLU B  1 121 ? 33.023  20.202  42.405  1.00 30.76  ? 121 GLU F CG  1 
ATOM   2011  C  CD  . GLU B  1 121 ? 33.211  20.963  43.704  1.00 32.19  ? 121 GLU F CD  1 
ATOM   2012  O  OE1 . GLU B  1 121 ? 32.299  21.727  44.101  1.00 32.00  ? 121 GLU F OE1 1 
ATOM   2013  O  OE2 . GLU B  1 121 ? 34.272  20.799  44.324  1.00 33.74  ? 121 GLU F OE2 1 
ATOM   2014  N  N   . LYS B  1 122 ? 30.067  18.130  41.391  1.00 27.95  ? 122 LYS F N   1 
ATOM   2015  C  CA  . LYS B  1 122 ? 29.835  16.802  41.956  1.00 28.60  ? 122 LYS F CA  1 
ATOM   2016  C  C   . LYS B  1 122 ? 28.397  16.346  41.750  1.00 27.74  ? 122 LYS F C   1 
ATOM   2017  O  O   . LYS B  1 122 ? 27.650  16.993  41.016  1.00 26.68  ? 122 LYS F O   1 
ATOM   2018  C  CB  . LYS B  1 122 ? 30.296  16.782  43.416  1.00 30.23  ? 122 LYS F CB  1 
ATOM   2019  C  CG  . LYS B  1 122 ? 29.689  17.844  44.311  1.00 30.61  ? 122 LYS F CG  1 
ATOM   2020  C  CD  . LYS B  1 122 ? 30.649  18.191  45.439  1.00 32.35  ? 122 LYS F CD  1 
ATOM   2021  C  CE  . LYS B  1 122 ? 29.930  18.837  46.613  1.00 33.22  ? 122 LYS F CE  1 
ATOM   2022  N  NZ  . LYS B  1 122 ? 30.920  19.050  47.710  1.00 35.23  ? 122 LYS F NZ  1 
ATOM   2023  N  N   . ALA B  1 123 ? 28.044  15.208  42.343  1.00 28.30  ? 123 ALA F N   1 
ATOM   2024  C  CA  . ALA B  1 123 ? 26.749  14.580  42.153  1.00 27.89  ? 123 ALA F CA  1 
ATOM   2025  C  C   . ALA B  1 123 ? 25.590  15.447  42.636  1.00 27.47  ? 123 ALA F C   1 
ATOM   2026  O  O   . ALA B  1 123 ? 25.648  16.054  43.703  1.00 28.16  ? 123 ALA F O   1 
ATOM   2027  C  CB  . ALA B  1 123 ? 26.720  13.235  42.876  1.00 29.11  ? 123 ALA F CB  1 
ATOM   2028  N  N   . ASP B  1 124 ? 24.551  15.513  41.815  1.00 26.56  ? 124 ASP F N   1 
ATOM   2029  C  CA  . ASP B  1 124 ? 23.240  15.990  42.224  1.00 26.50  ? 124 ASP F CA  1 
ATOM   2030  C  C   . ASP B  1 124 ? 22.623  14.862  43.073  1.00 27.53  ? 124 ASP F C   1 
ATOM   2031  O  O   . ASP B  1 124 ? 22.511  13.734  42.606  1.00 27.68  ? 124 ASP F O   1 
ATOM   2032  C  CB  . ASP B  1 124 ? 22.420  16.281  40.950  1.00 25.54  ? 124 ASP F CB  1 
ATOM   2033  C  CG  . ASP B  1 124 ? 21.047  16.884  41.215  1.00 25.68  ? 124 ASP F CG  1 
ATOM   2034  O  OD1 . ASP B  1 124 ? 20.473  16.729  42.313  1.00 26.53  ? 124 ASP F OD1 1 
ATOM   2035  O  OD2 . ASP B  1 124 ? 20.526  17.507  40.264  1.00 25.04  ? 124 ASP F OD2 1 
ATOM   2036  N  N   . ASP B  1 125 ? 22.250  15.167  44.321  1.00 28.40  ? 125 ASP F N   1 
ATOM   2037  C  CA  . ASP B  1 125 ? 21.587  14.189  45.211  1.00 29.67  ? 125 ASP F CA  1 
ATOM   2038  C  C   . ASP B  1 125 ? 20.087  13.978  44.913  1.00 29.81  ? 125 ASP F C   1 
ATOM   2039  O  O   . ASP B  1 125 ? 19.414  13.219  45.622  1.00 31.02  ? 125 ASP F O   1 
ATOM   2040  C  CB  . ASP B  1 125 ? 21.825  14.514  46.713  1.00 30.91  ? 125 ASP F CB  1 
ATOM   2041  C  CG  . ASP B  1 125 ? 21.114  15.798  47.197  1.00 31.01  ? 125 ASP F CG  1 
ATOM   2042  O  OD1 . ASP B  1 125 ? 20.181  16.305  46.533  1.00 30.23  ? 125 ASP F OD1 1 
ATOM   2043  O  OD2 . ASP B  1 125 ? 21.498  16.301  48.279  1.00 32.01  ? 125 ASP F OD2 1 
ATOM   2044  N  N   . LEU B  1 126 ? 19.575  14.681  43.899  1.00 28.78  ? 126 LEU F N   1 
ATOM   2045  C  CA  . LEU B  1 126 ? 18.226  14.506  43.365  1.00 28.91  ? 126 LEU F CA  1 
ATOM   2046  C  C   . LEU B  1 126 ? 17.149  14.833  44.396  1.00 30.11  ? 126 LEU F C   1 
ATOM   2047  O  O   . LEU B  1 126 ? 16.054  14.274  44.356  1.00 30.96  ? 126 LEU F O   1 
ATOM   2048  C  CB  . LEU B  1 126 ? 18.058  13.096  42.772  1.00 29.31  ? 126 LEU F CB  1 
ATOM   2049  C  CG  . LEU B  1 126 ? 19.186  12.629  41.826  1.00 28.53  ? 126 LEU F CG  1 
ATOM   2050  C  CD1 . LEU B  1 126 ? 18.940  11.200  41.371  1.00 29.42  ? 126 LEU F CD1 1 
ATOM   2051  C  CD2 . LEU B  1 126 ? 19.332  13.530  40.616  1.00 27.16  ? 126 LEU F CD2 1 
ATOM   2052  N  N   . GLY B  1 127 ? 17.467  15.755  45.306  1.00 30.43  ? 127 GLY F N   1 
ATOM   2053  C  CA  . GLY B  1 127 ? 16.543  16.178  46.353  1.00 31.84  ? 127 GLY F CA  1 
ATOM   2054  C  C   . GLY B  1 127 ? 16.427  15.265  47.564  1.00 33.54  ? 127 GLY F C   1 
ATOM   2055  O  O   . GLY B  1 127 ? 15.571  15.491  48.401  1.00 34.85  ? 127 GLY F O   1 
ATOM   2056  N  N   . LYS B  1 128 ? 17.311  14.271  47.680  1.00 33.75  ? 128 LYS F N   1 
ATOM   2057  C  CA  . LYS B  1 128 ? 17.230  13.259  48.739  1.00 35.57  ? 128 LYS F CA  1 
ATOM   2058  C  C   . LYS B  1 128 ? 18.302  13.435  49.828  1.00 36.32  ? 128 LYS F C   1 
ATOM   2059  O  O   . LYS B  1 128 ? 18.599  12.493  50.563  1.00 37.56  ? 128 LYS F O   1 
ATOM   2060  C  CB  . LYS B  1 128 ? 17.320  11.859  48.118  1.00 35.74  ? 128 LYS F CB  1 
ATOM   2061  C  CG  . LYS B  1 128 ? 16.220  11.573  47.108  1.00 35.57  ? 128 LYS F CG  1 
ATOM   2062  C  CD  . LYS B  1 128 ? 16.572  10.426  46.174  1.00 35.43  ? 128 LYS F CD  1 
ATOM   2063  C  CE  . LYS B  1 128 ? 16.653  9.098   46.902  1.00 37.34  ? 128 LYS F CE  1 
ATOM   2064  N  NZ  . LYS B  1 128 ? 16.099  7.988   46.070  1.00 38.08  ? 128 LYS F NZ  1 
ATOM   2065  N  N   . GLY B  1 129 ? 18.855  14.643  49.947  1.00 35.79  ? 129 GLY F N   1 
ATOM   2066  C  CA  . GLY B  1 129 ? 19.963  14.915  50.879  1.00 36.69  ? 129 GLY F CA  1 
ATOM   2067  C  C   . GLY B  1 129 ? 19.569  15.260  52.304  1.00 38.74  ? 129 GLY F C   1 
ATOM   2068  O  O   . GLY B  1 129 ? 20.407  15.229  53.200  1.00 39.79  ? 129 GLY F O   1 
ATOM   2069  N  N   . GLY B  1 130 ? 18.299  15.599  52.518  1.00 39.51  ? 130 GLY F N   1 
ATOM   2070  C  CA  . GLY B  1 130 ? 17.804  15.915  53.846  1.00 41.80  ? 130 GLY F CA  1 
ATOM   2071  C  C   . GLY B  1 130 ? 18.203  17.265  54.407  1.00 42.50  ? 130 GLY F C   1 
ATOM   2072  O  O   . GLY B  1 130 ? 18.116  17.468  55.613  1.00 44.55  ? 130 GLY F O   1 
ATOM   2073  N  N   . ASN B  1 131 ? 18.634  18.188  53.551  1.00 41.24  ? 131 ASN F N   1 
ATOM   2074  C  CA  . ASN B  1 131 ? 18.886  19.574  53.955  1.00 42.10  ? 131 ASN F CA  1 
ATOM   2075  C  C   . ASN B  1 131 ? 18.179  20.524  53.001  1.00 41.19  ? 131 ASN F C   1 
ATOM   2076  O  O   . ASN B  1 131 ? 17.735  20.116  51.926  1.00 39.67  ? 131 ASN F O   1 
ATOM   2077  C  CB  . ASN B  1 131 ? 20.395  19.880  54.070  1.00 41.93  ? 131 ASN F CB  1 
ATOM   2078  C  CG  . ASN B  1 131 ? 21.173  19.657  52.775  1.00 39.73  ? 131 ASN F CG  1 
ATOM   2079  O  OD1 . ASN B  1 131 ? 20.643  19.755  51.673  1.00 38.08  ? 131 ASN F OD1 1 
ATOM   2080  N  ND2 . ASN B  1 131 ? 22.461  19.385  52.919  1.00 39.79  ? 131 ASN F ND2 1 
ATOM   2081  N  N   . GLU B  1 132 ? 18.073  21.787  53.403  1.00 42.50  ? 132 GLU F N   1 
ATOM   2082  C  CA  . GLU B  1 132 ? 17.427  22.821  52.582  1.00 42.06  ? 132 GLU F CA  1 
ATOM   2083  C  C   . GLU B  1 132 ? 18.071  22.939  51.202  1.00 39.79  ? 132 GLU F C   1 
ATOM   2084  O  O   . GLU B  1 132 ? 17.383  23.127  50.197  1.00 38.76  ? 132 GLU F O   1 
ATOM   2085  C  CB  . GLU B  1 132 ? 17.494  24.173  53.297  1.00 43.99  ? 132 GLU F CB  1 
ATOM   2086  C  CG  . GLU B  1 132 ? 16.814  25.319  52.555  1.00 43.90  ? 132 GLU F CG  1 
ATOM   2087  C  CD  . GLU B  1 132 ? 16.850  26.635  53.319  1.00 46.15  ? 132 GLU F CD  1 
ATOM   2088  O  OE1 . GLU B  1 132 ? 17.641  26.770  54.284  1.00 47.84  ? 132 GLU F OE1 1 
ATOM   2089  O  OE2 . GLU B  1 132 ? 16.093  27.553  52.932  1.00 46.73  ? 132 GLU F OE2 1 
ATOM   2090  N  N   . GLU B  1 133 ? 19.394  22.831  51.161  1.00 39.30  ? 133 GLU F N   1 
ATOM   2091  C  CA  . GLU B  1 133 ? 20.140  22.954  49.910  1.00 37.41  ? 133 GLU F CA  1 
ATOM   2092  C  C   . GLU B  1 133 ? 19.809  21.818  48.920  1.00 35.48  ? 133 GLU F C   1 
ATOM   2093  O  O   . GLU B  1 133 ? 19.792  22.045  47.718  1.00 33.90  ? 133 GLU F O   1 
ATOM   2094  C  CB  . GLU B  1 133 ? 21.643  23.026  50.220  1.00 38.00  ? 133 GLU F CB  1 
ATOM   2095  C  CG  . GLU B  1 133 ? 22.560  23.379  49.061  1.00 36.81  ? 133 GLU F CG  1 
ATOM   2096  C  CD  . GLU B  1 133 ? 22.397  24.803  48.539  1.00 36.97  ? 133 GLU F CD  1 
ATOM   2097  O  OE1 . GLU B  1 133 ? 21.612  25.597  49.101  1.00 38.37  ? 133 GLU F OE1 1 
ATOM   2098  O  OE2 . GLU B  1 133 ? 23.078  25.126  47.539  1.00 36.25  ? 133 GLU F OE2 1 
ATOM   2099  N  N   . SER B  1 134 ? 19.499  20.622  49.425  1.00 35.67  ? 134 SER F N   1 
ATOM   2100  C  CA  . SER B  1 134 ? 19.110  19.497  48.566  1.00 34.43  ? 134 SER F CA  1 
ATOM   2101  C  C   . SER B  1 134 ? 17.864  19.788  47.729  1.00 33.78  ? 134 SER F C   1 
ATOM   2102  O  O   . SER B  1 134 ? 17.799  19.390  46.574  1.00 32.34  ? 134 SER F O   1 
ATOM   2103  C  CB  . SER B  1 134 ? 18.873  18.236  49.395  1.00 35.52  ? 134 SER F CB  1 
ATOM   2104  O  OG  . SER B  1 134 ? 18.523  17.152  48.563  1.00 34.62  ? 134 SER F OG  1 
ATOM   2105  N  N   . THR B  1 135 ? 16.898  20.489  48.326  1.00 34.97  ? 135 THR F N   1 
ATOM   2106  C  CA  . THR B  1 135 ? 15.641  20.855  47.665  1.00 34.94  ? 135 THR F CA  1 
ATOM   2107  C  C   . THR B  1 135 ? 15.720  22.147  46.836  1.00 34.10  ? 135 THR F C   1 
ATOM   2108  O  O   . THR B  1 135 ? 14.723  22.539  46.218  1.00 34.15  ? 135 THR F O   1 
ATOM   2109  C  CB  . THR B  1 135 ? 14.502  20.999  48.690  1.00 36.97  ? 135 THR F CB  1 
ATOM   2110  O  OG1 . THR B  1 135 ? 14.813  22.047  49.613  1.00 38.18  ? 135 THR F OG1 1 
ATOM   2111  C  CG2 . THR B  1 135 ? 14.296  19.699  49.458  1.00 38.05  ? 135 THR F CG2 1 
ATOM   2112  N  N   . LYS B  1 136 ? 16.883  22.801  46.836  1.00 33.57  ? 136 LYS F N   1 
ATOM   2113  C  CA  . LYS B  1 136 ? 17.160  23.947  45.977  1.00 32.82  ? 136 LYS F CA  1 
ATOM   2114  C  C   . LYS B  1 136 ? 18.086  23.581  44.817  1.00 31.00  ? 136 LYS F C   1 
ATOM   2115  O  O   . LYS B  1 136 ? 17.727  23.770  43.647  1.00 30.07  ? 136 LYS F O   1 
ATOM   2116  C  CB  . LYS B  1 136 ? 17.788  25.077  46.787  1.00 34.03  ? 136 LYS F CB  1 
ATOM   2117  C  CG  . LYS B  1 136 ? 16.857  25.691  47.813  1.00 36.04  ? 136 LYS F CG  1 
ATOM   2118  C  CD  . LYS B  1 136 ? 17.600  26.682  48.697  0.50 37.47  ? 136 LYS F CD  1 
ATOM   2119  C  CE  . LYS B  1 136 ? 16.642  27.433  49.602  0.50 39.65  ? 136 LYS F CE  1 
ATOM   2120  N  NZ  . LYS B  1 136 ? 17.369  28.326  50.544  0.50 41.42  ? 136 LYS F NZ  1 
ATOM   2121  N  N   . THR B  1 137 ? 19.277  23.079  45.142  1.00 30.75  ? 137 THR F N   1 
ATOM   2122  C  CA  . THR B  1 137 ? 20.328  22.819  44.145  1.00 29.33  ? 137 THR F CA  1 
ATOM   2123  C  C   . THR B  1 137 ? 20.719  21.353  43.961  1.00 28.68  ? 137 THR F C   1 
ATOM   2124  O  O   . THR B  1 137 ? 21.411  21.034  43.004  1.00 27.71  ? 137 THR F O   1 
ATOM   2125  C  CB  . THR B  1 137 ? 21.613  23.599  44.493  1.00 29.83  ? 137 THR F CB  1 
ATOM   2126  O  OG1 . THR B  1 137 ? 22.071  23.202  45.786  1.00 31.02  ? 137 THR F OG1 1 
ATOM   2127  C  CG2 . THR B  1 137 ? 21.349  25.111  44.491  1.00 30.47  ? 137 THR F CG2 1 
ATOM   2128  N  N   . GLY B  1 138 ? 20.309  20.471  44.868  1.00 29.39  ? 138 GLY F N   1 
ATOM   2129  C  CA  . GLY B  1 138 ? 20.793  19.089  44.873  1.00 29.25  ? 138 GLY F CA  1 
ATOM   2130  C  C   . GLY B  1 138 ? 22.216  18.863  45.401  1.00 29.61  ? 138 GLY F C   1 
ATOM   2131  O  O   . GLY B  1 138 ? 22.761  17.759  45.248  1.00 29.41  ? 138 GLY F O   1 
ATOM   2132  N  N   . ASN B  1 139 ? 22.804  19.886  46.035  1.00 30.20  ? 139 ASN F N   1 
ATOM   2133  C  CA  . ASN B  1 139 ? 24.158  19.824  46.610  1.00 30.97  ? 139 ASN F CA  1 
ATOM   2134  C  C   . ASN B  1 139 ? 25.225  19.401  45.582  1.00 30.03  ? 139 ASN F C   1 
ATOM   2135  O  O   . ASN B  1 139 ? 26.145  18.655  45.908  1.00 30.68  ? 139 ASN F O   1 
ATOM   2136  C  CB  . ASN B  1 139 ? 24.186  18.919  47.863  1.00 32.43  ? 139 ASN F CB  1 
ATOM   2137  C  CG  . ASN B  1 139 ? 23.350  19.477  49.005  1.00 33.83  ? 139 ASN F CG  1 
ATOM   2138  O  OD1 . ASN B  1 139 ? 23.656  20.540  49.544  1.00 34.71  ? 139 ASN F OD1 1 
ATOM   2139  N  ND2 . ASN B  1 139 ? 22.288  18.767  49.376  1.00 34.27  ? 139 ASN F ND2 1 
ATOM   2140  N  N   . ALA B  1 140 ? 25.094  19.898  44.349  1.00 28.73  ? 140 ALA F N   1 
ATOM   2141  C  CA  . ALA B  1 140 ? 25.989  19.518  43.243  1.00 27.93  ? 140 ALA F CA  1 
ATOM   2142  C  C   . ALA B  1 140 ? 27.277  20.333  43.193  1.00 28.28  ? 140 ALA F C   1 
ATOM   2143  O  O   . ALA B  1 140 ? 28.097  20.125  42.303  1.00 27.96  ? 140 ALA F O   1 
ATOM   2144  C  CB  . ALA B  1 140 ? 25.262  19.612  41.905  1.00 26.64  ? 140 ALA F CB  1 
ATOM   2145  N  N   . GLY B  1 141 ? 27.461  21.262  44.127  1.00 29.21  ? 141 GLY F N   1 
ATOM   2146  C  CA  . GLY B  1 141 ? 28.702  22.007  44.232  1.00 29.89  ? 141 GLY F CA  1 
ATOM   2147  C  C   . GLY B  1 141 ? 28.786  23.097  43.187  1.00 29.09  ? 141 GLY F C   1 
ATOM   2148  O  O   . GLY B  1 141 ? 27.767  23.589  42.686  1.00 28.25  ? 141 GLY F O   1 
ATOM   2149  N  N   . SER B  1 142 ? 30.008  23.458  42.832  1.00 29.43  ? 142 SER F N   1 
ATOM   2150  C  CA  . SER B  1 142 ? 30.235  24.615  41.981  1.00 29.16  ? 142 SER F CA  1 
ATOM   2151  C  C   . SER B  1 142 ? 29.846  24.335  40.522  1.00 27.52  ? 142 SER F C   1 
ATOM   2152  O  O   . SER B  1 142 ? 29.678  23.186  40.093  1.00 26.65  ? 142 SER F O   1 
ATOM   2153  C  CB  . SER B  1 142 ? 31.691  25.083  42.096  1.00 30.59  ? 142 SER F CB  1 
ATOM   2154  O  OG  . SER B  1 142 ? 32.558  24.109  41.574  1.00 30.54  ? 142 SER F OG  1 
ATOM   2155  N  N   . ARG B  1 143 ? 29.673  25.419  39.787  1.00 27.20  ? 143 ARG F N   1 
ATOM   2156  C  CA  . ARG B  1 143 ? 29.342  25.380  38.374  1.00 25.99  ? 143 ARG F CA  1 
ATOM   2157  C  C   . ARG B  1 143 ? 30.669  25.340  37.622  1.00 26.31  ? 143 ARG F C   1 
ATOM   2158  O  O   . ARG B  1 143 ? 31.433  26.291  37.689  1.00 27.37  ? 143 ARG F O   1 
ATOM   2159  C  CB  . ARG B  1 143 ? 28.542  26.636  38.022  1.00 25.87  ? 143 ARG F CB  1 
ATOM   2160  C  CG  . ARG B  1 143 ? 27.265  26.760  38.847  1.00 25.84  ? 143 ARG F CG  1 
ATOM   2161  C  CD  . ARG B  1 143 ? 26.492  28.035  38.591  1.00 26.06  ? 143 ARG F CD  1 
ATOM   2162  N  NE  . ARG B  1 143 ? 25.368  28.141  39.531  1.00 26.45  ? 143 ARG F NE  1 
ATOM   2163  C  CZ  . ARG B  1 143 ? 24.334  28.979  39.424  1.00 26.61  ? 143 ARG F CZ  1 
ATOM   2164  N  NH1 . ARG B  1 143 ? 24.228  29.830  38.406  1.00 26.44  ? 143 ARG F NH1 1 
ATOM   2165  N  NH2 . ARG B  1 143 ? 23.389  28.960  40.359  1.00 27.15  ? 143 ARG F NH2 1 
ATOM   2166  N  N   . LEU B  1 144 ? 30.961  24.222  36.954  1.00 25.73  ? 144 LEU F N   1 
ATOM   2167  C  CA  . LEU B  1 144 ? 32.280  24.003  36.324  1.00 26.32  ? 144 LEU F CA  1 
ATOM   2168  C  C   . LEU B  1 144 ? 32.337  24.545  34.904  1.00 25.76  ? 144 LEU F C   1 
ATOM   2169  O  O   . LEU B  1 144 ? 33.364  25.032  34.461  1.00 26.56  ? 144 LEU F O   1 
ATOM   2170  C  CB  . LEU B  1 144 ? 32.627  22.509  36.280  1.00 26.39  ? 144 LEU F CB  1 
ATOM   2171  C  CG  . LEU B  1 144 ? 32.836  21.736  37.582  1.00 27.16  ? 144 LEU F CG  1 
ATOM   2172  C  CD1 . LEU B  1 144 ? 33.143  20.279  37.248  1.00 27.27  ? 144 LEU F CD1 1 
ATOM   2173  C  CD2 . LEU B  1 144 ? 33.944  22.332  38.438  1.00 28.71  ? 144 LEU F CD2 1 
ATOM   2174  N  N   . ALA B  1 145 ? 31.235  24.417  34.181  1.00 24.51  ? 145 ALA F N   1 
ATOM   2175  C  CA  . ALA B  1 145 ? 31.155  24.922  32.827  1.00 24.11  ? 145 ALA F CA  1 
ATOM   2176  C  C   . ALA B  1 145 ? 29.718  25.196  32.474  1.00 23.09  ? 145 ALA F C   1 
ATOM   2177  O  O   . ALA B  1 145 ? 28.785  24.600  33.052  1.00 22.55  ? 145 ALA F O   1 
ATOM   2178  C  CB  . ALA B  1 145 ? 31.771  23.935  31.844  1.00 24.13  ? 145 ALA F CB  1 
ATOM   2179  N  N   . ALA B  1 146 ? 29.547  26.132  31.548  1.00 23.04  ? 146 ALA F N   1 
ATOM   2180  C  CA  . ALA B  1 146 ? 28.230  26.629  31.193  1.00 22.44  ? 146 ALA F CA  1 
ATOM   2181  C  C   . ALA B  1 146 ? 28.224  27.135  29.759  1.00 22.44  ? 146 ALA F C   1 
ATOM   2182  O  O   . ALA B  1 146 ? 29.269  27.402  29.177  1.00 22.97  ? 146 ALA F O   1 
ATOM   2183  C  CB  . ALA B  1 146 ? 27.831  27.738  32.154  1.00 22.92  ? 146 ALA F CB  1 
ATOM   2184  N  N   . GLY B  1 147 ? 27.025  27.229  29.195  1.00 21.94  ? 147 GLY F N   1 
ATOM   2185  C  CA  . GLY B  1 147 ? 26.820  27.847  27.888  1.00 22.12  ? 147 GLY F CA  1 
ATOM   2186  C  C   . GLY B  1 147 ? 25.363  28.190  27.659  1.00 21.81  ? 147 GLY F C   1 
ATOM   2187  O  O   . GLY B  1 147 ? 24.469  27.598  28.279  1.00 21.22  ? 147 GLY F O   1 
ATOM   2188  N  N   . VAL B  1 148 ? 25.135  29.146  26.761  1.00 22.30  ? 148 VAL F N   1 
ATOM   2189  C  CA  . VAL B  1 148 ? 23.795  29.537  26.378  1.00 22.37  ? 148 VAL F CA  1 
ATOM   2190  C  C   . VAL B  1 148 ? 23.287  28.558  25.309  1.00 22.11  ? 148 VAL F C   1 
ATOM   2191  O  O   . VAL B  1 148 ? 23.984  28.234  24.341  1.00 22.27  ? 148 VAL F O   1 
ATOM   2192  C  CB  . VAL B  1 148 ? 23.732  30.991  25.874  1.00 23.31  ? 148 VAL F CB  1 
ATOM   2193  C  CG1 . VAL B  1 148 ? 22.284  31.411  25.649  1.00 23.52  ? 148 VAL F CG1 1 
ATOM   2194  C  CG2 . VAL B  1 148 ? 24.424  31.946  26.852  1.00 23.96  ? 148 VAL F CG2 1 
ATOM   2195  N  N   . ILE B  1 149 ? 22.064  28.087  25.500  1.00 21.92  ? 149 ILE F N   1 
ATOM   2196  C  CA  . ILE B  1 149 ? 21.441  27.137  24.587  1.00 21.97  ? 149 ILE F CA  1 
ATOM   2197  C  C   . ILE B  1 149 ? 20.893  27.932  23.399  1.00 22.68  ? 149 ILE F C   1 
ATOM   2198  O  O   . ILE B  1 149 ? 19.998  28.755  23.565  1.00 23.01  ? 149 ILE F O   1 
ATOM   2199  C  CB  . ILE B  1 149 ? 20.330  26.336  25.295  1.00 21.78  ? 149 ILE F CB  1 
ATOM   2200  C  CG1 . ILE B  1 149 ? 20.931  25.546  26.469  1.00 21.27  ? 149 ILE F CG1 1 
ATOM   2201  C  CG2 . ILE B  1 149 ? 19.628  25.390  24.319  1.00 22.10  ? 149 ILE F CG2 1 
ATOM   2202  C  CD1 . ILE B  1 149 ? 19.893  25.024  27.449  1.00 21.24  ? 149 ILE F CD1 1 
ATOM   2203  N  N   . GLY B  1 150 ? 21.464  27.710  22.219  1.00 23.07  ? 150 GLY F N   1 
ATOM   2204  C  CA  . GLY B  1 150 ? 21.073  28.438  21.012  1.00 24.05  ? 150 GLY F CA  1 
ATOM   2205  C  C   . GLY B  1 150 ? 20.329  27.570  20.023  1.00 24.56  ? 150 GLY F C   1 
ATOM   2206  O  O   . GLY B  1 150 ? 20.418  26.352  20.081  1.00 24.20  ? 150 GLY F O   1 
ATOM   2207  N  N   . ILE B  1 151 ? 19.614  28.223  19.111  1.00 25.62  ? 151 ILE F N   1 
ATOM   2208  C  CA  . ILE B  1 151 ? 18.888  27.560  18.023  1.00 26.61  ? 151 ILE F CA  1 
ATOM   2209  C  C   . ILE B  1 151 ? 19.907  27.010  17.024  1.00 27.22  ? 151 ILE F C   1 
ATOM   2210  O  O   . ILE B  1 151 ? 20.831  27.713  16.646  1.00 27.35  ? 151 ILE F O   1 
ATOM   2211  C  CB  . ILE B  1 151 ? 17.934  28.552  17.304  1.00 27.77  ? 151 ILE F CB  1 
ATOM   2212  C  CG1 . ILE B  1 151 ? 16.866  29.053  18.281  1.00 27.64  ? 151 ILE F CG1 1 
ATOM   2213  C  CG2 . ILE B  1 151 ? 17.279  27.902  16.093  1.00 28.97  ? 151 ILE F CG2 1 
ATOM   2214  C  CD1 . ILE B  1 151 ? 16.033  30.226  17.792  1.00 28.86  ? 151 ILE F CD1 1 
ATOM   2215  N  N   . ALA B  1 152 ? 19.739  25.748  16.624  1.00 27.75  ? 152 ALA F N   1 
ATOM   2216  C  CA  . ALA B  1 152 ? 20.638  25.094  15.671  1.00 28.67  ? 152 ALA F CA  1 
ATOM   2217  C  C   . ALA B  1 152 ? 19.926  24.770  14.358  1.00 30.47  ? 152 ALA F C   1 
ATOM   2218  O  O   . ALA B  1 152 ? 18.702  24.672  14.303  1.00 30.86  ? 152 ALA F O   1 
ATOM   2219  C  CB  . ALA B  1 152 ? 21.226  23.828  16.284  1.00 28.08  ? 152 ALA F CB  1 
ATOM   2220  N  N   . GLN B  1 153 ? 20.708  24.590  13.301  1.00 31.89  ? 153 GLN F N   1 
ATOM   2221  C  CA  . GLN B  1 153 ? 20.157  24.233  11.997  1.00 33.93  ? 153 GLN F CA  1 
ATOM   2222  C  C   . GLN B  1 153 ? 19.700  22.775  12.000  1.00 34.57  ? 153 GLN F C   1 
ATOM   2223  O  O   . GLN B  1 153 ? 20.385  21.895  12.528  1.00 34.29  ? 153 GLN F O   1 
ATOM   2224  C  CB  . GLN B  1 153 ? 21.189  24.432  10.897  1.00 35.23  ? 153 GLN F CB  1 
ATOM   2225  C  CG  . GLN B  1 153 ? 20.605  24.240  9.506   1.00 37.37  ? 153 GLN F CG  1 
ATOM   2226  C  CD  . GLN B  1 153 ? 21.569  24.619  8.415   1.00 38.85  ? 153 GLN F CD  1 
ATOM   2227  O  OE1 . GLN B  1 153 ? 22.780  24.470  8.564   1.00 38.76  ? 153 GLN F OE1 1 
ATOM   2228  N  NE2 . GLN B  1 153 ? 21.042  25.117  7.314   1.00 40.65  ? 153 GLN F NE2 1 
ATOM   2229  O  OXT . GLN B  1 153 ? 18.639  22.463  11.462  1.00 35.92  ? 153 GLN F OXT 1 
ATOM   2230  N  N   . ALA C  1 1   ? 0.631   33.812  12.479  1.00 39.44  ? 1   ALA D N   1 
ATOM   2231  C  CA  . ALA C  1 1   ? -0.360  34.907  12.716  1.00 37.72  ? 1   ALA D CA  1 
ATOM   2232  C  C   . ALA C  1 1   ? -1.360  34.509  13.805  1.00 36.05  ? 1   ALA D C   1 
ATOM   2233  O  O   . ALA C  1 1   ? -1.579  33.325  14.046  1.00 36.34  ? 1   ALA D O   1 
ATOM   2234  C  CB  . ALA C  1 1   ? -1.092  35.249  11.420  1.00 38.15  ? 1   ALA D CB  1 
ATOM   2235  N  N   . THR C  1 2   ? -1.946  35.505  14.455  1.00 34.56  ? 2   THR D N   1 
ATOM   2236  C  CA  . THR C  1 2   ? -2.984  35.304  15.475  1.00 33.06  ? 2   THR D CA  1 
ATOM   2237  C  C   . THR C  1 2   ? -4.267  35.964  14.971  1.00 32.16  ? 2   THR D C   1 
ATOM   2238  O  O   . THR C  1 2   ? -4.203  37.027  14.344  1.00 32.23  ? 2   THR D O   1 
ATOM   2239  C  CB  . THR C  1 2   ? -2.544  35.904  16.827  1.00 32.37  ? 2   THR D CB  1 
ATOM   2240  O  OG1 . THR C  1 2   ? -1.215  35.466  17.124  1.00 33.63  ? 2   THR D OG1 1 
ATOM   2241  C  CG2 . THR C  1 2   ? -3.440  35.451  17.953  1.00 31.41  ? 2   THR D CG2 1 
ATOM   2242  N  N   . LYS C  1 3   ? -5.411  35.308  15.205  1.00 31.47  ? 3   LYS D N   1 
ATOM   2243  C  CA  . LYS C  1 3   ? -6.736  35.838  14.853  1.00 30.89  ? 3   LYS D CA  1 
ATOM   2244  C  C   . LYS C  1 3   ? -7.682  35.818  16.060  1.00 29.63  ? 3   LYS D C   1 
ATOM   2245  O  O   . LYS C  1 3   ? -7.606  34.937  16.917  1.00 29.37  ? 3   LYS D O   1 
ATOM   2246  C  CB  . LYS C  1 3   ? -7.379  35.046  13.701  1.00 31.96  ? 3   LYS D CB  1 
ATOM   2247  C  CG  . LYS C  1 3   ? -6.741  35.295  12.341  1.00 33.36  ? 3   LYS D CG  1 
ATOM   2248  C  CD  . LYS C  1 3   ? -7.392  34.486  11.225  1.00 34.64  ? 3   LYS D CD  1 
ATOM   2249  C  CE  . LYS C  1 3   ? -6.790  34.878  9.883   1.00 36.18  ? 3   LYS D CE  1 
ATOM   2250  N  NZ  . LYS C  1 3   ? -7.188  34.034  8.720   1.00 37.87  ? 3   LYS D NZ  1 
ATOM   2251  N  N   . ALA C  1 4   ? -8.568  36.801  16.113  1.00 28.91  ? 4   ALA D N   1 
ATOM   2252  C  CA  . ALA C  1 4   ? -9.591  36.864  17.151  1.00 28.05  ? 4   ALA D CA  1 
ATOM   2253  C  C   . ALA C  1 4   ? -10.901 37.348  16.545  1.00 28.20  ? 4   ALA D C   1 
ATOM   2254  O  O   . ALA C  1 4   ? -10.925 37.820  15.409  1.00 28.72  ? 4   ALA D O   1 
ATOM   2255  C  CB  . ALA C  1 4   ? -9.157  37.759  18.303  1.00 27.16  ? 4   ALA D CB  1 
ATOM   2256  N  N   . VAL C  1 5   ? -11.978 37.205  17.316  1.00 27.88  ? 5   VAL D N   1 
ATOM   2257  C  CA  . VAL C  1 5   ? -13.325 37.531  16.851  1.00 28.34  ? 5   VAL D CA  1 
ATOM   2258  C  C   . VAL C  1 5   ? -14.181 37.951  18.037  1.00 27.89  ? 5   VAL D C   1 
ATOM   2259  O  O   . VAL C  1 5   ? -13.933 37.532  19.175  1.00 27.42  ? 5   VAL D O   1 
ATOM   2260  C  CB  . VAL C  1 5   ? -13.951 36.349  16.064  1.00 29.40  ? 5   VAL D CB  1 
ATOM   2261  C  CG1 . VAL C  1 5   ? -14.284 35.177  16.971  1.00 29.41  ? 5   VAL D CG1 1 
ATOM   2262  C  CG2 . VAL C  1 5   ? -15.179 36.787  15.277  1.00 30.26  ? 5   VAL D CG2 1 
ATOM   2263  N  N   . CYS C  1 6   ? -15.155 38.813  17.764  1.00 28.28  ? 6   CYS D N   1 
ATOM   2264  C  CA  . CYS C  1 6   ? -16.072 39.310  18.767  1.00 28.16  ? 6   CYS D CA  1 
ATOM   2265  C  C   . CYS C  1 6   ? -17.475 39.456  18.184  1.00 29.22  ? 6   CYS D C   1 
ATOM   2266  O  O   . CYS C  1 6   ? -17.659 40.102  17.146  1.00 29.79  ? 6   CYS D O   1 
ATOM   2267  C  CB  . CYS C  1 6   ? -15.595 40.663  19.267  1.00 27.55  ? 6   CYS D CB  1 
ATOM   2268  S  SG  . CYS C  1 6   ? -16.611 41.323  20.600  1.00 27.60  ? 6   CYS D SG  1 
ATOM   2269  N  N   . VAL C  1 7   ? -18.454 38.856  18.855  1.00 29.71  ? 7   VAL D N   1 
ATOM   2270  C  CA  . VAL C  1 7   ? -19.863 39.021  18.497  1.00 31.01  ? 7   VAL D CA  1 
ATOM   2271  C  C   . VAL C  1 7   ? -20.441 40.099  19.410  1.00 30.94  ? 7   VAL D C   1 
ATOM   2272  O  O   . VAL C  1 7   ? -20.517 39.902  20.630  1.00 30.53  ? 7   VAL D O   1 
ATOM   2273  C  CB  . VAL C  1 7   ? -20.654 37.709  18.655  1.00 31.98  ? 7   VAL D CB  1 
ATOM   2274  C  CG1 . VAL C  1 7   ? -22.116 37.901  18.247  1.00 33.54  ? 7   VAL D CG1 1 
ATOM   2275  C  CG2 . VAL C  1 7   ? -20.011 36.596  17.829  1.00 32.23  ? 7   VAL D CG2 1 
ATOM   2276  N  N   . LEU C  1 8   ? -20.814 41.236  18.823  1.00 31.46  ? 8   LEU D N   1 
ATOM   2277  C  CA  . LEU C  1 8   ? -21.429 42.336  19.572  1.00 31.74  ? 8   LEU D CA  1 
ATOM   2278  C  C   . LEU C  1 8   ? -22.934 42.144  19.668  1.00 33.27  ? 8   LEU D C   1 
ATOM   2279  O  O   . LEU C  1 8   ? -23.592 41.957  18.654  1.00 34.56  ? 8   LEU D O   1 
ATOM   2280  C  CB  . LEU C  1 8   ? -21.110 43.681  18.918  1.00 31.79  ? 8   LEU D CB  1 
ATOM   2281  C  CG  . LEU C  1 8   ? -19.628 44.048  18.925  1.00 30.59  ? 8   LEU D CG  1 
ATOM   2282  C  CD1 . LEU C  1 8   ? -19.328 45.108  17.880  1.00 31.12  ? 8   LEU D CD1 1 
ATOM   2283  C  CD2 . LEU C  1 8   ? -19.183 44.522  20.297  1.00 29.71  ? 8   LEU D CD2 1 
ATOM   2284  N  N   . LYS C  1 9   ? -23.457 42.167  20.895  1.00 33.45  ? 9   LYS D N   1 
ATOM   2285  C  CA  . LYS C  1 9   ? -24.900 42.103  21.179  1.00 35.18  ? 9   LYS D CA  1 
ATOM   2286  C  C   . LYS C  1 9   ? -25.260 43.020  22.351  1.00 35.16  ? 9   LYS D C   1 
ATOM   2287  O  O   . LYS C  1 9   ? -24.410 43.343  23.181  1.00 33.83  ? 9   LYS D O   1 
ATOM   2288  C  CB  . LYS C  1 9   ? -25.349 40.679  21.555  1.00 35.95  ? 9   LYS D CB  1 
ATOM   2289  C  CG  . LYS C  1 9   ? -25.316 39.662  20.435  1.00 36.64  ? 9   LYS D CG  1 
ATOM   2290  C  CD  . LYS C  1 9   ? -26.105 38.409  20.819  1.00 38.04  ? 9   LYS D CD  1 
ATOM   2291  C  CE  . LYS C  1 9   ? -25.815 37.235  19.891  1.00 38.44  ? 9   LYS D CE  1 
ATOM   2292  N  NZ  . LYS C  1 9   ? -26.383 37.436  18.530  1.00 39.87  ? 9   LYS D NZ  1 
ATOM   2293  N  N   . GLY C  1 10  ? -26.533 43.399  22.416  1.00 36.76  ? 10  GLY D N   1 
ATOM   2294  C  CA  . GLY C  1 10  ? -27.081 44.155  23.547  1.00 37.31  ? 10  GLY D CA  1 
ATOM   2295  C  C   . GLY C  1 10  ? -28.586 43.979  23.689  1.00 39.55  ? 10  GLY D C   1 
ATOM   2296  O  O   . GLY C  1 10  ? -29.164 43.029  23.156  1.00 40.49  ? 10  GLY D O   1 
ATOM   2297  N  N   . ASP C  1 11  ? -29.209 44.907  24.411  1.00 40.54  ? 11  ASP D N   1 
ATOM   2298  C  CA  . ASP C  1 11  ? -30.653 44.875  24.684  1.00 43.04  ? 11  ASP D CA  1 
ATOM   2299  C  C   . ASP C  1 11  ? -31.504 45.576  23.611  1.00 44.69  ? 11  ASP D C   1 
ATOM   2300  O  O   . ASP C  1 11  ? -32.727 45.471  23.638  1.00 46.99  ? 11  ASP D O   1 
ATOM   2301  C  CB  . ASP C  1 11  ? -30.939 45.504  26.053  1.00 43.72  ? 11  ASP D CB  1 
ATOM   2302  C  CG  . ASP C  1 11  ? -30.243 44.771  27.197  1.00 42.64  ? 11  ASP D CG  1 
ATOM   2303  O  OD1 . ASP C  1 11  ? -30.311 43.518  27.258  1.00 42.86  ? 11  ASP D OD1 1 
ATOM   2304  O  OD2 . ASP C  1 11  ? -29.619 45.453  28.041  1.00 41.91  ? 11  ASP D OD2 1 
ATOM   2305  N  N   . GLY C  1 12  ? -30.855 46.280  22.681  1.00 43.67  ? 12  GLY D N   1 
ATOM   2306  C  CA  . GLY C  1 12  ? -31.525 47.001  21.596  1.00 45.31  ? 12  GLY D CA  1 
ATOM   2307  C  C   . GLY C  1 12  ? -31.233 46.373  20.245  1.00 45.10  ? 12  GLY D C   1 
ATOM   2308  O  O   . GLY C  1 12  ? -30.792 45.227  20.188  1.00 44.09  ? 12  GLY D O   1 
ATOM   2309  N  N   . PRO C  1 13  ? -31.439 47.126  19.148  1.00 46.19  ? 13  PRO D N   1 
ATOM   2310  C  CA  . PRO C  1 13  ? -31.216 46.585  17.798  1.00 46.48  ? 13  PRO D CA  1 
ATOM   2311  C  C   . PRO C  1 13  ? -29.749 46.415  17.349  1.00 44.14  ? 13  PRO D C   1 
ATOM   2312  O  O   . PRO C  1 13  ? -29.503 45.778  16.320  1.00 44.32  ? 13  PRO D O   1 
ATOM   2313  C  CB  . PRO C  1 13  ? -31.901 47.617  16.903  1.00 48.69  ? 13  PRO D CB  1 
ATOM   2314  C  CG  . PRO C  1 13  ? -31.784 48.891  17.656  1.00 48.34  ? 13  PRO D CG  1 
ATOM   2315  C  CD  . PRO C  1 13  ? -31.921 48.520  19.100  1.00 47.56  ? 13  PRO D CD  1 
ATOM   2316  N  N   . VAL C  1 14  ? -28.796 46.993  18.080  1.00 42.23  ? 14  VAL D N   1 
ATOM   2317  C  CA  . VAL C  1 14  ? -27.398 47.020  17.637  1.00 40.37  ? 14  VAL D CA  1 
ATOM   2318  C  C   . VAL C  1 14  ? -26.744 45.644  17.799  1.00 39.04  ? 14  VAL D C   1 
ATOM   2319  O  O   . VAL C  1 14  ? -26.729 45.082  18.894  1.00 38.29  ? 14  VAL D O   1 
ATOM   2320  C  CB  . VAL C  1 14  ? -26.583 48.128  18.353  1.00 39.03  ? 14  VAL D CB  1 
ATOM   2321  C  CG1 . VAL C  1 14  ? -25.102 48.064  17.982  1.00 37.21  ? 14  VAL D CG1 1 
ATOM   2322  C  CG2 . VAL C  1 14  ? -27.138 49.492  17.981  1.00 40.61  ? 14  VAL D CG2 1 
ATOM   2323  N  N   . GLN C  1 15  ? -26.238 45.111  16.687  1.00 39.07  ? 15  GLN D N   1 
ATOM   2324  C  CA  . GLN C  1 15  ? -25.479 43.857  16.683  1.00 37.97  ? 15  GLN D CA  1 
ATOM   2325  C  C   . GLN C  1 15  ? -24.462 43.808  15.542  1.00 37.43  ? 15  GLN D C   1 
ATOM   2326  O  O   . GLN C  1 15  ? -24.619 44.485  14.516  1.00 38.53  ? 15  GLN D O   1 
ATOM   2327  C  CB  . GLN C  1 15  ? -26.410 42.638  16.648  1.00 39.39  ? 15  GLN D CB  1 
ATOM   2328  C  CG  . GLN C  1 15  ? -27.467 42.624  15.554  1.00 41.94  ? 15  GLN D CG  1 
ATOM   2329  C  CD  . GLN C  1 15  ? -28.653 41.727  15.900  1.00 43.73  ? 15  GLN D CD  1 
ATOM   2330  O  OE1 . GLN C  1 15  ? -28.490 40.651  16.479  1.00 43.37  ? 15  GLN D OE1 1 
ATOM   2331  N  NE2 . GLN C  1 15  ? -29.848 42.170  15.556  1.00 46.11  ? 15  GLN D NE2 1 
ATOM   2332  N  N   . GLY C  1 16  ? -23.409 43.020  15.741  1.00 35.88  ? 16  GLY D N   1 
ATOM   2333  C  CA  . GLY C  1 16  ? -22.359 42.886  14.740  1.00 35.46  ? 16  GLY D CA  1 
ATOM   2334  C  C   . GLY C  1 16  ? -21.301 41.848  15.050  1.00 34.08  ? 16  GLY D C   1 
ATOM   2335  O  O   . GLY C  1 16  ? -21.332 41.195  16.100  1.00 33.26  ? 16  GLY D O   1 
ATOM   2336  N  N   . ILE C  1 17  ? -20.378 41.689  14.104  1.00 33.99  ? 17  ILE D N   1 
ATOM   2337  C  CA  . ILE C  1 17  ? -19.251 40.769  14.228  1.00 32.93  ? 17  ILE D CA  1 
ATOM   2338  C  C   . ILE C  1 17  ? -17.992 41.524  13.846  1.00 32.23  ? 17  ILE D C   1 
ATOM   2339  O  O   . ILE C  1 17  ? -17.944 42.139  12.783  1.00 33.22  ? 17  ILE D O   1 
ATOM   2340  C  CB  . ILE C  1 17  ? -19.396 39.544  13.307  1.00 34.05  ? 17  ILE D CB  1 
ATOM   2341  C  CG1 . ILE C  1 17  ? -20.663 38.749  13.656  1.00 35.00  ? 17  ILE D CG1 1 
ATOM   2342  C  CG2 . ILE C  1 17  ? -18.158 38.653  13.409  1.00 33.19  ? 17  ILE D CG2 1 
ATOM   2343  C  CD1 . ILE C  1 17  ? -21.019 37.685  12.646  1.00 36.54  ? 17  ILE D CD1 1 
ATOM   2344  N  N   . ILE C  1 18  ? -16.978 41.466  14.705  1.00 30.77  ? 18  ILE D N   1 
ATOM   2345  C  CA  . ILE C  1 18  ? -15.716 42.159  14.468  1.00 30.25  ? 18  ILE D CA  1 
ATOM   2346  C  C   . ILE C  1 18  ? -14.579 41.141  14.496  1.00 29.71  ? 18  ILE D C   1 
ATOM   2347  O  O   . ILE C  1 18  ? -14.499 40.323  15.407  1.00 28.98  ? 18  ILE D O   1 
ATOM   2348  C  CB  . ILE C  1 18  ? -15.495 43.291  15.502  1.00 29.35  ? 18  ILE D CB  1 
ATOM   2349  C  CG1 . ILE C  1 18  ? -16.631 44.325  15.420  1.00 30.09  ? 18  ILE D CG1 1 
ATOM   2350  C  CG2 . ILE C  1 18  ? -14.146 43.977  15.297  1.00 29.06  ? 18  ILE D CG2 1 
ATOM   2351  C  CD1 . ILE C  1 18  ? -16.714 45.092  14.116  1.00 31.36  ? 18  ILE D CD1 1 
ATOM   2352  N  N   . ASN C  1 19  ? -13.723 41.203  13.478  1.00 30.27  ? 19  ASN D N   1 
ATOM   2353  C  CA  . ASN C  1 19  ? -12.591 40.299  13.308  1.00 30.22  ? 19  ASN D CA  1 
ATOM   2354  C  C   . ASN C  1 19  ? -11.284 41.028  13.611  1.00 29.72  ? 19  ASN D C   1 
ATOM   2355  O  O   . ASN C  1 19  ? -11.163 42.222  13.354  1.00 29.86  ? 19  ASN D O   1 
ATOM   2356  C  CB  . ASN C  1 19  ? -12.553 39.784  11.873  1.00 31.68  ? 19  ASN D CB  1 
ATOM   2357  C  CG  . ASN C  1 19  ? -13.813 39.031  11.486  1.00 32.53  ? 19  ASN D CG  1 
ATOM   2358  O  OD1 . ASN C  1 19  ? -14.033 37.895  11.918  1.00 32.40  ? 19  ASN D OD1 1 
ATOM   2359  N  ND2 . ASN C  1 19  ? -14.645 39.660  10.649  1.00 33.65  ? 19  ASN D ND2 1 
ATOM   2360  N  N   . PHE C  1 20  ? -10.321 40.299  14.170  1.00 29.29  ? 20  PHE D N   1 
ATOM   2361  C  CA  . PHE C  1 20  ? -9.000  40.834  14.494  1.00 29.10  ? 20  PHE D CA  1 
ATOM   2362  C  C   . PHE C  1 20  ? -7.948  39.904  13.891  1.00 29.91  ? 20  PHE D C   1 
ATOM   2363  O  O   . PHE C  1 20  ? -8.092  38.680  13.951  1.00 29.91  ? 20  PHE D O   1 
ATOM   2364  C  CB  . PHE C  1 20  ? -8.768  40.907  16.004  1.00 28.02  ? 20  PHE D CB  1 
ATOM   2365  C  CG  . PHE C  1 20  ? -9.766  41.747  16.758  1.00 27.35  ? 20  PHE D CG  1 
ATOM   2366  C  CD1 . PHE C  1 20  ? -10.999 41.226  17.122  1.00 27.12  ? 20  PHE D CD1 1 
ATOM   2367  C  CD2 . PHE C  1 20  ? -9.439  43.037  17.171  1.00 27.13  ? 20  PHE D CD2 1 
ATOM   2368  C  CE1 . PHE C  1 20  ? -11.911 41.992  17.837  1.00 26.73  ? 20  PHE D CE1 1 
ATOM   2369  C  CE2 . PHE C  1 20  ? -10.342 43.803  17.888  1.00 26.71  ? 20  PHE D CE2 1 
ATOM   2370  C  CZ  . PHE C  1 20  ? -11.581 43.285  18.216  1.00 26.51  ? 20  PHE D CZ  1 
ATOM   2371  N  N   . GLU C  1 21  ? -6.903  40.486  13.309  1.00 30.70  ? 21  GLU D N   1 
ATOM   2372  C  CA  . GLU C  1 21  ? -5.789  39.710  12.750  1.00 31.77  ? 21  GLU D CA  1 
ATOM   2373  C  C   . GLU C  1 21  ? -4.470  40.434  12.973  1.00 32.04  ? 21  GLU D C   1 
ATOM   2374  O  O   . GLU C  1 21  ? -4.385  41.634  12.749  1.00 32.14  ? 21  GLU D O   1 
ATOM   2375  C  CB  . GLU C  1 21  ? -5.976  39.455  11.257  1.00 33.36  ? 21  GLU D CB  1 
ATOM   2376  C  CG  . GLU C  1 21  ? -4.969  38.447  10.706  1.00 34.72  ? 21  GLU D CG  1 
ATOM   2377  C  CD  . GLU C  1 21  ? -5.052  38.245  9.204   1.00 36.61  ? 21  GLU D CD  1 
ATOM   2378  O  OE1 . GLU C  1 21  ? -5.238  39.232  8.436   1.00 37.44  ? 21  GLU D OE1 1 
ATOM   2379  O  OE2 . GLU C  1 21  ? -4.890  37.082  8.786   1.00 37.66  ? 21  GLU D OE2 1 
ATOM   2380  N  N   . GLN C  1 22  ? -3.450  39.675  13.382  1.00 32.31  ? 22  GLN D N   1 
ATOM   2381  C  CA  . GLN C  1 22  ? -2.114  40.198  13.626  1.00 32.99  ? 22  GLN D CA  1 
ATOM   2382  C  C   . GLN C  1 22  ? -1.087  39.191  13.099  1.00 34.47  ? 22  GLN D C   1 
ATOM   2383  O  O   . GLN C  1 22  ? -0.933  38.095  13.650  1.00 34.28  ? 22  GLN D O   1 
ATOM   2384  C  CB  . GLN C  1 22  ? -1.929  40.451  15.121  1.00 31.89  ? 22  GLN D CB  1 
ATOM   2385  C  CG  . GLN C  1 22  ? -0.706  41.279  15.477  1.00 32.59  ? 22  GLN D CG  1 
ATOM   2386  C  CD  . GLN C  1 22  ? -0.465  41.356  16.975  1.00 31.83  ? 22  GLN D CD  1 
ATOM   2387  O  OE1 . GLN C  1 22  ? -0.951  40.517  17.741  1.00 30.97  ? 22  GLN D OE1 1 
ATOM   2388  N  NE2 . GLN C  1 22  ? 0.282   42.374  17.404  1.00 32.22  ? 22  GLN D NE2 1 
ATOM   2389  N  N   . LYS C  1 23  ? -0.402  39.573  12.025  1.00 36.07  ? 23  LYS D N   1 
ATOM   2390  C  CA  . LYS C  1 23  ? 0.518   38.690  11.320  1.00 37.85  ? 23  LYS D CA  1 
ATOM   2391  C  C   . LYS C  1 23  ? 1.764   38.392  12.159  1.00 38.37  ? 23  LYS D C   1 
ATOM   2392  O  O   . LYS C  1 23  ? 2.202   37.250  12.218  1.00 39.07  ? 23  LYS D O   1 
ATOM   2393  C  CB  . LYS C  1 23  ? 0.896   39.304  9.971   1.00 39.70  ? 23  LYS D CB  1 
ATOM   2394  C  CG  . LYS C  1 23  ? 1.574   38.348  9.004   1.00 41.81  ? 23  LYS D CG  1 
ATOM   2395  C  CD  . LYS C  1 23  ? 1.695   38.979  7.619   1.00 43.67  ? 23  LYS D CD  1 
ATOM   2396  C  CE  . LYS C  1 23  ? 2.691   38.257  6.730   1.00 46.20  ? 23  LYS D CE  1 
ATOM   2397  N  NZ  . LYS C  1 23  ? 4.025   38.934  6.715   1.00 47.87  ? 23  LYS D NZ  1 
ATOM   2398  N  N   . GLU C  1 24  ? 2.312   39.415  12.816  1.00 38.21  ? 24  GLU D N   1 
ATOM   2399  C  CA  . GLU C  1 24  ? 3.467   39.250  13.706  1.00 38.91  ? 24  GLU D CA  1 
ATOM   2400  C  C   . GLU C  1 24  ? 3.207   39.866  15.077  1.00 37.31  ? 24  GLU D C   1 
ATOM   2401  O  O   . GLU C  1 24  ? 2.517   40.877  15.191  1.00 36.19  ? 24  GLU D O   1 
ATOM   2402  C  CB  . GLU C  1 24  ? 4.729   39.867  13.088  1.00 41.19  ? 24  GLU D CB  1 
ATOM   2403  C  CG  . GLU C  1 24  ? 5.378   39.029  11.982  1.00 43.36  ? 24  GLU D CG  1 
ATOM   2404  C  CD  . GLU C  1 24  ? 5.038   39.473  10.562  1.00 44.34  ? 24  GLU D CD  1 
ATOM   2405  O  OE1 . GLU C  1 24  ? 4.360   40.506  10.389  1.00 43.62  ? 24  GLU D OE1 1 
ATOM   2406  O  OE2 . GLU C  1 24  ? 5.467   38.785  9.603   1.00 46.23  ? 24  GLU D OE2 1 
ATOM   2407  N  N   . SER C  1 25  ? 3.784   39.254  16.111  1.00 37.37  ? 25  SER D N   1 
ATOM   2408  C  CA  . SER C  1 25  ? 3.603   39.690  17.502  1.00 36.25  ? 25  SER D CA  1 
ATOM   2409  C  C   . SER C  1 25  ? 4.028   41.142  17.767  1.00 36.51  ? 25  SER D C   1 
ATOM   2410  O  O   . SER C  1 25  ? 3.491   41.777  18.678  1.00 35.30  ? 25  SER D O   1 
ATOM   2411  C  CB  . SER C  1 25  ? 4.364   38.763  18.451  1.00 37.02  ? 25  SER D CB  1 
ATOM   2412  O  OG  . SER C  1 25  ? 5.750   38.816  18.176  1.00 39.13  ? 25  SER D OG  1 
ATOM   2413  N  N   . ASN C  1 26  ? 4.980   41.655  16.980  1.00 38.21  ? 26  ASN D N   1 
ATOM   2414  C  CA  . ASN C  1 26  ? 5.392   43.066  17.070  1.00 38.83  ? 26  ASN D CA  1 
ATOM   2415  C  C   . ASN C  1 26  ? 4.882   43.958  15.914  1.00 38.90  ? 26  ASN D C   1 
ATOM   2416  O  O   . ASN C  1 26  ? 5.409   45.048  15.688  1.00 39.98  ? 26  ASN D O   1 
ATOM   2417  C  CB  . ASN C  1 26  ? 6.926   43.180  17.252  1.00 41.14  ? 26  ASN D CB  1 
ATOM   2418  C  CG  . ASN C  1 26  ? 7.705   42.781  16.016  1.00 43.13  ? 26  ASN D CG  1 
ATOM   2419  O  OD1 . ASN C  1 26  ? 7.208   42.041  15.166  1.00 42.84  ? 26  ASN D OD1 1 
ATOM   2420  N  ND2 . ASN C  1 26  ? 8.944   43.264  15.914  1.00 45.42  ? 26  ASN D ND2 1 
ATOM   2421  N  N   . GLY C  1 27  ? 3.836   43.506  15.220  1.00 37.93  ? 27  GLY D N   1 
ATOM   2422  C  CA  . GLY C  1 27  ? 3.253   44.237  14.090  1.00 38.17  ? 27  GLY D CA  1 
ATOM   2423  C  C   . GLY C  1 27  ? 1.831   44.698  14.378  1.00 36.29  ? 27  GLY D C   1 
ATOM   2424  O  O   . GLY C  1 27  ? 1.295   44.428  15.452  1.00 34.77  ? 27  GLY D O   1 
ATOM   2425  N  N   . PRO C  1 28  ? 1.204   45.396  13.409  1.00 36.57  ? 28  PRO D N   1 
ATOM   2426  C  CA  . PRO C  1 28  ? -0.136  45.948  13.627  1.00 35.12  ? 28  PRO D CA  1 
ATOM   2427  C  C   . PRO C  1 28  ? -1.231  44.890  13.668  1.00 33.87  ? 28  PRO D C   1 
ATOM   2428  O  O   . PRO C  1 28  ? -1.034  43.780  13.162  1.00 34.32  ? 28  PRO D O   1 
ATOM   2429  C  CB  . PRO C  1 28  ? -0.340  46.874  12.424  1.00 36.32  ? 28  PRO D CB  1 
ATOM   2430  C  CG  . PRO C  1 28  ? 0.584   46.375  11.374  1.00 38.16  ? 28  PRO D CG  1 
ATOM   2431  C  CD  . PRO C  1 28  ? 1.743   45.738  12.079  1.00 38.51  ? 28  PRO D CD  1 
ATOM   2432  N  N   . VAL C  1 29  ? -2.361  45.249  14.285  1.00 32.51  ? 29  VAL D N   1 
ATOM   2433  C  CA  . VAL C  1 29  ? -3.561  44.414  14.326  1.00 31.51  ? 29  VAL D CA  1 
ATOM   2434  C  C   . VAL C  1 29  ? -4.603  45.024  13.397  1.00 31.81  ? 29  VAL D C   1 
ATOM   2435  O  O   . VAL C  1 29  ? -4.950  46.197  13.540  1.00 31.76  ? 29  VAL D O   1 
ATOM   2436  C  CB  . VAL C  1 29  ? -4.173  44.322  15.741  1.00 30.04  ? 29  VAL D CB  1 
ATOM   2437  C  CG1 . VAL C  1 29  ? -5.354  43.362  15.752  1.00 29.28  ? 29  VAL D CG1 1 
ATOM   2438  C  CG2 . VAL C  1 29  ? -3.128  43.874  16.763  1.00 30.02  ? 29  VAL D CG2 1 
ATOM   2439  N  N   . LYS C  1 30  ? -5.084  44.238  12.442  1.00 32.35  ? 30  LYS D N   1 
ATOM   2440  C  CA  . LYS C  1 30  ? -6.172  44.665  11.568  1.00 32.87  ? 30  LYS D CA  1 
ATOM   2441  C  C   . LYS C  1 30  ? -7.483  44.339  12.258  1.00 31.67  ? 30  LYS D C   1 
ATOM   2442  O  O   . LYS C  1 30  ? -7.631  43.255  12.812  1.00 30.96  ? 30  LYS D O   1 
ATOM   2443  C  CB  . LYS C  1 30  ? -6.104  43.957  10.224  1.00 34.33  ? 30  LYS D CB  1 
ATOM   2444  C  CG  . LYS C  1 30  ? -4.870  44.306  9.419   1.00 35.97  ? 30  LYS D CG  1 
ATOM   2445  C  CD  . LYS C  1 30  ? -4.753  43.418  8.201   1.00 37.50  ? 30  LYS D CD  1 
ATOM   2446  C  CE  . LYS C  1 30  ? -3.679  43.927  7.261   1.00 39.53  ? 30  LYS D CE  1 
ATOM   2447  N  NZ  . LYS C  1 30  ? -3.626  43.100  6.033   1.00 41.28  ? 30  LYS D NZ  1 
ATOM   2448  N  N   . VAL C  1 31  ? -8.416  45.288  12.221  1.00 31.64  ? 31  VAL D N   1 
ATOM   2449  C  CA  . VAL C  1 31  ? -9.714  45.163  12.858  1.00 30.78  ? 31  VAL D CA  1 
ATOM   2450  C  C   . VAL C  1 31  ? -10.744 45.423  11.768  1.00 31.92  ? 31  VAL D C   1 
ATOM   2451  O  O   . VAL C  1 31  ? -10.747 46.503  11.178  1.00 32.85  ? 31  VAL D O   1 
ATOM   2452  C  CB  . VAL C  1 31  ? -9.880  46.190  13.995  1.00 29.93  ? 31  VAL D CB  1 
ATOM   2453  C  CG1 . VAL C  1 31  ? -11.254 46.073  14.643  1.00 29.34  ? 31  VAL D CG1 1 
ATOM   2454  C  CG2 . VAL C  1 31  ? -8.779  46.031  15.036  1.00 29.16  ? 31  VAL D CG2 1 
ATOM   2455  N  N   . TRP C  1 32  ? -11.601 44.440  11.486  1.00 32.07  ? 32  TRP D N   1 
ATOM   2456  C  CA  . TRP C  1 32  ? -12.621 44.606  10.447  1.00 33.47  ? 32  TRP D CA  1 
ATOM   2457  C  C   . TRP C  1 32  ? -13.905 43.836  10.723  1.00 33.39  ? 32  TRP D C   1 
ATOM   2458  O  O   . TRP C  1 32  ? -13.894 42.797  11.380  1.00 32.46  ? 32  TRP D O   1 
ATOM   2459  C  CB  . TRP C  1 32  ? -12.073 44.195  9.074   1.00 34.97  ? 32  TRP D CB  1 
ATOM   2460  C  CG  . TRP C  1 32  ? -11.841 42.710  8.931   1.00 34.97  ? 32  TRP D CG  1 
ATOM   2461  C  CD1 . TRP C  1 32  ? -10.764 42.000  9.379   1.00 34.26  ? 32  TRP D CD1 1 
ATOM   2462  C  CD2 . TRP C  1 32  ? -12.716 41.759  8.307   1.00 35.89  ? 32  TRP D CD2 1 
ATOM   2463  N  NE1 . TRP C  1 32  ? -10.912 40.671  9.069   1.00 34.69  ? 32  TRP D NE1 1 
ATOM   2464  C  CE2 . TRP C  1 32  ? -12.100 40.495  8.409   1.00 35.66  ? 32  TRP D CE2 1 
ATOM   2465  C  CE3 . TRP C  1 32  ? -13.961 41.856  7.673   1.00 37.12  ? 32  TRP D CE3 1 
ATOM   2466  C  CZ2 . TRP C  1 32  ? -12.680 39.331  7.896   1.00 36.60  ? 32  TRP D CZ2 1 
ATOM   2467  C  CZ3 . TRP C  1 32  ? -14.546 40.696  7.161   1.00 38.09  ? 32  TRP D CZ3 1 
ATOM   2468  C  CH2 . TRP C  1 32  ? -13.900 39.447  7.278   1.00 37.79  ? 32  TRP D CH2 1 
ATOM   2469  N  N   . GLY C  1 33  ? -14.999 44.335  10.158  1.00 34.63  ? 33  GLY D N   1 
ATOM   2470  C  CA  . GLY C  1 33  ? -16.293 43.680  10.268  1.00 35.08  ? 33  GLY D CA  1 
ATOM   2471  C  C   . GLY C  1 33  ? -17.427 44.649  10.031  1.00 36.25  ? 33  GLY D C   1 
ATOM   2472  O  O   . GLY C  1 33  ? -17.249 45.685  9.395   1.00 37.12  ? 33  GLY D O   1 
ATOM   2473  N  N   . SER C  1 34  ? -18.594 44.310  10.557  1.00 36.50  ? 34  SER D N   1 
ATOM   2474  C  CA  . SER C  1 34  ? -19.798 45.089  10.311  1.00 38.00  ? 34  SER D CA  1 
ATOM   2475  C  C   . SER C  1 34  ? -20.684 45.128  11.546  1.00 37.39  ? 34  SER D C   1 
ATOM   2476  O  O   . SER C  1 34  ? -20.836 44.123  12.242  1.00 36.61  ? 34  SER D O   1 
ATOM   2477  C  CB  . SER C  1 34  ? -20.561 44.494  9.140   1.00 40.10  ? 34  SER D CB  1 
ATOM   2478  O  OG  . SER C  1 34  ? -21.600 45.367  8.741   1.00 41.93  ? 34  SER D OG  1 
ATOM   2479  N  N   . ILE C  1 35  ? -21.255 46.300  11.808  1.00 37.94  ? 35  ILE D N   1 
ATOM   2480  C  CA  . ILE C  1 35  ? -22.187 46.502  12.908  1.00 37.80  ? 35  ILE D CA  1 
ATOM   2481  C  C   . ILE C  1 35  ? -23.434 47.137  12.312  1.00 40.06  ? 35  ILE D C   1 
ATOM   2482  O  O   . ILE C  1 35  ? -23.340 48.184  11.669  1.00 41.04  ? 35  ILE D O   1 
ATOM   2483  C  CB  . ILE C  1 35  ? -21.603 47.420  14.007  1.00 36.35  ? 35  ILE D CB  1 
ATOM   2484  C  CG1 . ILE C  1 35  ? -20.233 46.910  14.485  1.00 34.48  ? 35  ILE D CG1 1 
ATOM   2485  C  CG2 . ILE C  1 35  ? -22.553 47.494  15.202  1.00 36.28  ? 35  ILE D CG2 1 
ATOM   2486  C  CD1 . ILE C  1 35  ? -19.492 47.901  15.361  1.00 33.42  ? 35  ILE D CD1 1 
ATOM   2487  N  N   . LYS C  1 36  ? -24.586 46.497  12.519  1.00 41.15  ? 36  LYS D N   1 
ATOM   2488  C  CA  . LYS C  1 36  ? -25.888 47.008  12.049  1.00 43.62  ? 36  LYS D CA  1 
ATOM   2489  C  C   . LYS C  1 36  ? -26.759 47.453  13.220  1.00 43.81  ? 36  LYS D C   1 
ATOM   2490  O  O   . LYS C  1 36  ? -26.461 47.150  14.369  1.00 42.06  ? 36  LYS D O   1 
ATOM   2491  C  CB  . LYS C  1 36  ? -26.637 45.947  11.222  1.00 45.39  ? 36  LYS D CB  1 
ATOM   2492  C  CG  . LYS C  1 36  ? -26.932 44.641  11.954  1.00 44.74  ? 36  LYS D CG  1 
ATOM   2493  C  CD  . LYS C  1 36  ? -27.894 43.751  11.189  1.00 47.02  ? 36  LYS D CD  1 
ATOM   2494  C  CE  . LYS C  1 36  ? -28.101 42.450  11.944  1.00 46.43  ? 36  LYS D CE  1 
ATOM   2495  N  NZ  . LYS C  1 36  ? -28.957 41.489  11.208  1.00 48.72  ? 36  LYS D NZ  1 
ATOM   2496  N  N   . GLY C  1 37  ? -27.851 48.154  12.906  1.00 46.20  ? 37  GLY D N   1 
ATOM   2497  C  CA  . GLY C  1 37  ? -28.819 48.615  13.905  1.00 47.02  ? 37  GLY D CA  1 
ATOM   2498  C  C   . GLY C  1 37  ? -28.495 49.957  14.544  1.00 46.55  ? 37  GLY D C   1 
ATOM   2499  O  O   . GLY C  1 37  ? -29.206 50.389  15.453  1.00 47.14  ? 37  GLY D O   1 
ATOM   2500  N  N   . LEU C  1 38  ? -27.443 50.626  14.065  1.00 45.80  ? 38  LEU D N   1 
ATOM   2501  C  CA  . LEU C  1 38  ? -26.967 51.876  14.663  1.00 45.26  ? 38  LEU D CA  1 
ATOM   2502  C  C   . LEU C  1 38  ? -27.698 53.059  14.060  1.00 47.80  ? 38  LEU D C   1 
ATOM   2503  O  O   . LEU C  1 38  ? -28.269 52.956  12.979  1.00 49.82  ? 38  LEU D O   1 
ATOM   2504  C  CB  . LEU C  1 38  ? -25.464 52.054  14.428  1.00 43.46  ? 38  LEU D CB  1 
ATOM   2505  C  CG  . LEU C  1 38  ? -24.521 51.126  15.192  1.00 40.98  ? 38  LEU D CG  1 
ATOM   2506  C  CD1 . LEU C  1 38  ? -23.154 51.068  14.523  1.00 39.93  ? 38  LEU D CD1 1 
ATOM   2507  C  CD2 . LEU C  1 38  ? -24.383 51.561  16.640  1.00 39.84  ? 38  LEU D CD2 1 
ATOM   2508  N  N   . THR C  1 39  ? -27.683 54.182  14.773  1.00 47.93  ? 39  THR D N   1 
ATOM   2509  C  CA  . THR C  1 39  ? -28.111 55.458  14.212  1.00 50.18  ? 39  THR D CA  1 
ATOM   2510  C  C   . THR C  1 39  ? -27.012 55.958  13.278  1.00 49.87  ? 39  THR D C   1 
ATOM   2511  O  O   . THR C  1 39  ? -25.836 55.685  13.516  1.00 47.68  ? 39  THR D O   1 
ATOM   2512  C  CB  . THR C  1 39  ? -28.349 56.514  15.313  1.00 50.42  ? 39  THR D CB  1 
ATOM   2513  O  OG1 . THR C  1 39  ? -27.164 56.655  16.107  1.00 48.00  ? 39  THR D OG1 1 
ATOM   2514  C  CG2 . THR C  1 39  ? -29.512 56.111  16.214  1.00 51.23  ? 39  THR D CG2 1 
ATOM   2515  N  N   . GLU C  1 40  ? -27.393 56.674  12.218  1.00 52.31  ? 40  GLU D N   1 
ATOM   2516  C  CA  . GLU C  1 40  ? -26.424 57.305  11.313  1.00 52.57  ? 40  GLU D CA  1 
ATOM   2517  C  C   . GLU C  1 40  ? -25.491 58.244  12.094  1.00 51.20  ? 40  GLU D C   1 
ATOM   2518  O  O   . GLU C  1 40  ? -25.947 59.008  12.946  1.00 51.61  ? 40  GLU D O   1 
ATOM   2519  C  CB  . GLU C  1 40  ? -27.135 58.091  10.197  1.00 55.89  ? 40  GLU D CB  1 
ATOM   2520  C  CG  . GLU C  1 40  ? -26.177 58.753  9.209   1.00 56.58  ? 40  GLU D CG  1 
ATOM   2521  C  CD  . GLU C  1 40  ? -26.862 59.351  7.994   1.00 60.10  ? 40  GLU D CD  1 
ATOM   2522  O  OE1 . GLU C  1 40  ? -27.986 59.887  8.118   1.00 62.24  ? 40  GLU D OE1 1 
ATOM   2523  O  OE2 . GLU C  1 40  ? -26.256 59.297  6.902   1.00 60.97  ? 40  GLU D OE2 1 
ATOM   2524  N  N   . GLY C  1 41  ? -24.191 58.152  11.811  1.00 49.71  ? 41  GLY D N   1 
ATOM   2525  C  CA  . GLY C  1 41  ? -23.187 59.015  12.430  1.00 48.59  ? 41  GLY D CA  1 
ATOM   2526  C  C   . GLY C  1 41  ? -22.129 58.241  13.191  1.00 45.74  ? 41  GLY D C   1 
ATOM   2527  O  O   . GLY C  1 41  ? -21.988 57.027  13.034  1.00 44.54  ? 41  GLY D O   1 
ATOM   2528  N  N   . LEU C  1 42  ? -21.392 58.963  14.029  1.00 44.80  ? 42  LEU D N   1 
ATOM   2529  C  CA  . LEU C  1 42  ? -20.232 58.414  14.723  1.00 42.41  ? 42  LEU D CA  1 
ATOM   2530  C  C   . LEU C  1 42  ? -20.621 57.704  16.020  1.00 40.79  ? 42  LEU D C   1 
ATOM   2531  O  O   . LEU C  1 42  ? -21.526 58.141  16.733  1.00 41.43  ? 42  LEU D O   1 
ATOM   2532  C  CB  . LEU C  1 42  ? -19.222 59.531  15.014  1.00 42.52  ? 42  LEU D CB  1 
ATOM   2533  C  CG  . LEU C  1 42  ? -18.653 60.287  13.804  1.00 44.14  ? 42  LEU D CG  1 
ATOM   2534  C  CD1 . LEU C  1 42  ? -17.586 61.270  14.254  1.00 44.12  ? 42  LEU D CD1 1 
ATOM   2535  C  CD2 . LEU C  1 42  ? -18.072 59.328  12.776  1.00 43.82  ? 42  LEU D CD2 1 
ATOM   2536  N  N   . HIS C  1 43  ? -19.913 56.614  16.314  1.00 38.80  ? 43  HIS D N   1 
ATOM   2537  C  CA  . HIS C  1 43  ? -20.128 55.828  17.521  1.00 37.31  ? 43  HIS D CA  1 
ATOM   2538  C  C   . HIS C  1 43  ? -18.800 55.409  18.137  1.00 35.43  ? 43  HIS D C   1 
ATOM   2539  O  O   . HIS C  1 43  ? -17.937 54.852  17.446  1.00 34.80  ? 43  HIS D O   1 
ATOM   2540  C  CB  . HIS C  1 43  ? -20.965 54.596  17.184  1.00 37.35  ? 43  HIS D CB  1 
ATOM   2541  C  CG  . HIS C  1 43  ? -22.366 54.929  16.800  1.00 39.31  ? 43  HIS D CG  1 
ATOM   2542  N  ND1 . HIS C  1 43  ? -23.353 55.158  17.733  1.00 39.94  ? 43  HIS D ND1 1 
ATOM   2543  C  CD2 . HIS C  1 43  ? -22.938 55.129  15.587  1.00 41.11  ? 43  HIS D CD2 1 
ATOM   2544  C  CE1 . HIS C  1 43  ? -24.479 55.460  17.112  1.00 41.94  ? 43  HIS D CE1 1 
ATOM   2545  N  NE2 . HIS C  1 43  ? -24.254 55.454  15.809  1.00 42.69  ? 43  HIS D NE2 1 
ATOM   2546  N  N   . GLY C  1 44  ? -18.645 55.693  19.432  1.00 34.66  ? 44  GLY D N   1 
ATOM   2547  C  CA  . GLY C  1 44  ? -17.470 55.292  20.198  1.00 33.11  ? 44  GLY D CA  1 
ATOM   2548  C  C   . GLY C  1 44  ? -17.233 53.799  20.116  1.00 31.86  ? 44  GLY D C   1 
ATOM   2549  O  O   . GLY C  1 44  ? -18.180 53.013  20.137  1.00 31.90  ? 44  GLY D O   1 
ATOM   2550  N  N   . PHE C  1 45  ? -15.963 53.419  20.021  1.00 30.91  ? 45  PHE D N   1 
ATOM   2551  C  CA  . PHE C  1 45  ? -15.560 52.047  19.742  1.00 29.94  ? 45  PHE D CA  1 
ATOM   2552  C  C   . PHE C  1 45  ? -14.339 51.770  20.608  1.00 28.89  ? 45  PHE D C   1 
ATOM   2553  O  O   . PHE C  1 45  ? -13.251 52.270  20.319  1.00 29.04  ? 45  PHE D O   1 
ATOM   2554  C  CB  . PHE C  1 45  ? -15.255 51.929  18.241  1.00 30.57  ? 45  PHE D CB  1 
ATOM   2555  C  CG  . PHE C  1 45  ? -15.143 50.515  17.723  1.00 30.11  ? 45  PHE D CG  1 
ATOM   2556  C  CD1 . PHE C  1 45  ? -16.177 49.601  17.895  1.00 30.06  ? 45  PHE D CD1 1 
ATOM   2557  C  CD2 . PHE C  1 45  ? -14.022 50.120  16.991  1.00 30.05  ? 45  PHE D CD2 1 
ATOM   2558  C  CE1 . PHE C  1 45  ? -16.077 48.308  17.386  1.00 29.84  ? 45  PHE D CE1 1 
ATOM   2559  C  CE2 . PHE C  1 45  ? -13.916 48.831  16.477  1.00 29.82  ? 45  PHE D CE2 1 
ATOM   2560  C  CZ  . PHE C  1 45  ? -14.945 47.921  16.677  1.00 29.68  ? 45  PHE D CZ  1 
ATOM   2561  N  N   . HIS C  1 46  ? -14.532 51.017  21.692  1.00 28.08  ? 46  HIS D N   1 
ATOM   2562  C  CA  . HIS C  1 46  ? -13.480 50.803  22.695  1.00 27.36  ? 46  HIS D CA  1 
ATOM   2563  C  C   . HIS C  1 46  ? -13.339 49.355  23.129  1.00 26.54  ? 46  HIS D C   1 
ATOM   2564  O  O   . HIS C  1 46  ? -14.331 48.611  23.173  1.00 26.46  ? 46  HIS D O   1 
ATOM   2565  C  CB  . HIS C  1 46  ? -13.774 51.596  23.965  1.00 27.65  ? 46  HIS D CB  1 
ATOM   2566  C  CG  . HIS C  1 46  ? -14.197 53.009  23.729  1.00 28.61  ? 46  HIS D CG  1 
ATOM   2567  N  ND1 . HIS C  1 46  ? -15.369 53.522  24.242  1.00 29.27  ? 46  HIS D ND1 1 
ATOM   2568  C  CD2 . HIS C  1 46  ? -13.598 54.023  23.063  1.00 29.23  ? 46  HIS D CD2 1 
ATOM   2569  C  CE1 . HIS C  1 46  ? -15.476 54.790  23.893  1.00 30.22  ? 46  HIS D CE1 1 
ATOM   2570  N  NE2 . HIS C  1 46  ? -14.417 55.118  23.174  1.00 30.20  ? 46  HIS D NE2 1 
ATOM   2571  N  N   . VAL C  1 47  ? -12.107 48.982  23.482  1.00 26.04  ? 47  VAL D N   1 
ATOM   2572  C  CA  . VAL C  1 47  ? -11.837 47.774  24.228  1.00 25.53  ? 47  VAL D CA  1 
ATOM   2573  C  C   . VAL C  1 47  ? -11.834 48.147  25.707  1.00 25.63  ? 47  VAL D C   1 
ATOM   2574  O  O   . VAL C  1 47  ? -11.046 48.990  26.139  1.00 25.97  ? 47  VAL D O   1 
ATOM   2575  C  CB  . VAL C  1 47  ? -10.480 47.128  23.871  1.00 25.36  ? 47  VAL D CB  1 
ATOM   2576  C  CG1 . VAL C  1 47  ? -10.288 45.846  24.681  1.00 25.09  ? 47  VAL D CG1 1 
ATOM   2577  C  CG2 . VAL C  1 47  ? -10.388 46.831  22.383  1.00 25.47  ? 47  VAL D CG2 1 
ATOM   2578  N  N   . HIS C  1 48  ? -12.706 47.509  26.477  1.00 25.57  ? 48  HIS D N   1 
ATOM   2579  C  CA  . HIS C  1 48  ? -12.807 47.733  27.921  1.00 25.93  ? 48  HIS D CA  1 
ATOM   2580  C  C   . HIS C  1 48  ? -12.053 46.626  28.642  1.00 25.93  ? 48  HIS D C   1 
ATOM   2581  O  O   . HIS C  1 48  ? -11.862 45.540  28.099  1.00 25.58  ? 48  HIS D O   1 
ATOM   2582  C  CB  . HIS C  1 48  ? -14.281 47.777  28.365  1.00 26.28  ? 48  HIS D CB  1 
ATOM   2583  C  CG  . HIS C  1 48  ? -14.997 49.028  27.951  1.00 26.68  ? 48  HIS D CG  1 
ATOM   2584  N  ND1 . HIS C  1 48  ? -15.521 49.921  28.863  1.00 27.40  ? 48  HIS D ND1 1 
ATOM   2585  C  CD2 . HIS C  1 48  ? -15.250 49.549  26.727  1.00 26.70  ? 48  HIS D CD2 1 
ATOM   2586  C  CE1 . HIS C  1 48  ? -16.086 50.925  28.216  1.00 27.87  ? 48  HIS D CE1 1 
ATOM   2587  N  NE2 . HIS C  1 48  ? -15.930 50.728  26.920  1.00 27.47  ? 48  HIS D NE2 1 
ATOM   2588  N  N   . GLU C  1 49  ? -11.653 46.905  29.876  1.00 26.55  ? 49  GLU D N   1 
ATOM   2589  C  CA  . GLU C  1 49  ? -10.705 46.058  30.592  1.00 26.88  ? 49  GLU D CA  1 
ATOM   2590  C  C   . GLU C  1 49  ? -11.126 44.600  30.794  1.00 26.82  ? 49  GLU D C   1 
ATOM   2591  O  O   . GLU C  1 49  ? -10.337 43.695  30.511  1.00 26.68  ? 49  GLU D O   1 
ATOM   2592  C  CB  . GLU C  1 49  ? -10.343 46.682  31.945  1.00 27.87  ? 49  GLU D CB  1 
ATOM   2593  C  CG  . GLU C  1 49  ? -9.177  45.976  32.630  1.00 28.50  ? 49  GLU D CG  1 
ATOM   2594  C  CD  . GLU C  1 49  ? -8.729  46.638  33.910  1.00 29.71  ? 49  GLU D CD  1 
ATOM   2595  O  OE1 . GLU C  1 49  ? -9.368  47.615  34.361  1.00 30.27  ? 49  GLU D OE1 1 
ATOM   2596  O  OE2 . GLU C  1 49  ? -7.727  46.158  34.470  1.00 30.47  ? 49  GLU D OE2 1 
ATOM   2597  N  N   . PHE C  1 50  ? -12.347 44.362  31.269  1.00 27.10  ? 50  PHE D N   1 
ATOM   2598  C  CA  . PHE C  1 50  ? -12.733 43.011  31.680  1.00 27.46  ? 50  PHE D CA  1 
ATOM   2599  C  C   . PHE C  1 50  ? -13.646 42.327  30.664  1.00 27.20  ? 50  PHE D C   1 
ATOM   2600  O  O   . PHE C  1 50  ? -14.524 42.972  30.091  1.00 27.09  ? 50  PHE D O   1 
ATOM   2601  C  CB  . PHE C  1 50  ? -13.388 43.044  33.064  1.00 28.43  ? 50  PHE D CB  1 
ATOM   2602  C  CG  . PHE C  1 50  ? -12.558 43.726  34.109  1.00 29.07  ? 50  PHE D CG  1 
ATOM   2603  C  CD1 . PHE C  1 50  ? -11.331 43.191  34.501  1.00 29.40  ? 50  PHE D CD1 1 
ATOM   2604  C  CD2 . PHE C  1 50  ? -12.985 44.910  34.696  1.00 29.61  ? 50  PHE D CD2 1 
ATOM   2605  C  CE1 . PHE C  1 50  ? -10.556 43.824  35.465  1.00 30.28  ? 50  PHE D CE1 1 
ATOM   2606  C  CE2 . PHE C  1 50  ? -12.220 45.538  35.669  1.00 30.44  ? 50  PHE D CE2 1 
ATOM   2607  C  CZ  . PHE C  1 50  ? -11.003 44.996  36.049  1.00 30.78  ? 50  PHE D CZ  1 
ATOM   2608  N  N   . GLY C  1 51  ? -13.446 41.019  30.469  1.00 27.35  ? 51  GLY D N   1 
ATOM   2609  C  CA  . GLY C  1 51  ? -14.316 40.182  29.643  1.00 27.50  ? 51  GLY D CA  1 
ATOM   2610  C  C   . GLY C  1 51  ? -15.494 39.625  30.428  1.00 28.57  ? 51  GLY D C   1 
ATOM   2611  O  O   . GLY C  1 51  ? -15.835 38.453  30.291  1.00 28.99  ? 51  GLY D O   1 
ATOM   2612  N  N   . ASP C  1 52  ? -16.105 40.480  31.244  1.00 29.30  ? 52  ASP D N   1 
ATOM   2613  C  CA  . ASP C  1 52  ? -17.135 40.104  32.197  1.00 30.67  ? 52  ASP D CA  1 
ATOM   2614  C  C   . ASP C  1 52  ? -18.442 40.669  31.653  1.00 31.29  ? 52  ASP D C   1 
ATOM   2615  O  O   . ASP C  1 52  ? -18.639 41.884  31.635  1.00 31.12  ? 52  ASP D O   1 
ATOM   2616  C  CB  . ASP C  1 52  ? -16.809 40.690  33.573  1.00 31.23  ? 52  ASP D CB  1 
ATOM   2617  C  CG  . ASP C  1 52  ? -17.802 40.273  34.654  1.00 32.68  ? 52  ASP D CG  1 
ATOM   2618  O  OD1 . ASP C  1 52  ? -18.926 39.851  34.319  1.00 33.17  ? 52  ASP D OD1 1 
ATOM   2619  O  OD2 . ASP C  1 52  ? -17.455 40.364  35.844  1.00 33.41  ? 52  ASP D OD2 1 
ATOM   2620  N  N   . ASN C  1 53  ? -19.304 39.768  31.189  1.00 32.33  ? 53  ASN D N   1 
ATOM   2621  C  CA  . ASN C  1 53  ? -20.594 40.125  30.606  1.00 33.33  ? 53  ASN D CA  1 
ATOM   2622  C  C   . ASN C  1 53  ? -21.771 39.738  31.506  1.00 34.95  ? 53  ASN D C   1 
ATOM   2623  O  O   . ASN C  1 53  ? -22.906 39.635  31.026  1.00 35.80  ? 53  ASN D O   1 
ATOM   2624  C  CB  . ASN C  1 53  ? -20.737 39.444  29.240  1.00 33.45  ? 53  ASN D CB  1 
ATOM   2625  C  CG  . ASN C  1 53  ? -21.497 40.296  28.255  1.00 33.98  ? 53  ASN D CG  1 
ATOM   2626  O  OD1 . ASN C  1 53  ? -20.963 41.285  27.755  1.00 33.93  ? 53  ASN D OD1 1 
ATOM   2627  N  ND2 . ASN C  1 53  ? -22.738 39.932  27.972  1.00 35.43  ? 53  ASN D ND2 1 
ATOM   2628  N  N   . THR C  1 54  ? -21.501 39.543  32.802  1.00 35.53  ? 54  THR D N   1 
ATOM   2629  C  CA  . THR C  1 54  ? -22.496 39.057  33.753  1.00 37.37  ? 54  THR D CA  1 
ATOM   2630  C  C   . THR C  1 54  ? -23.659 40.034  33.915  1.00 38.56  ? 54  THR D C   1 
ATOM   2631  O  O   . THR C  1 54  ? -24.809 39.613  34.043  1.00 40.24  ? 54  THR D O   1 
ATOM   2632  C  CB  . THR C  1 54  ? -21.884 38.783  35.145  1.00 37.94  ? 54  THR D CB  1 
ATOM   2633  O  OG1 . THR C  1 54  ? -21.191 39.945  35.610  1.00 37.31  ? 54  THR D OG1 1 
ATOM   2634  C  CG2 . THR C  1 54  ? -20.934 37.594  35.101  1.00 37.48  ? 54  THR D CG2 1 
ATOM   2635  N  N   . ALA C  1 55  ? -23.352 41.328  33.908  1.00 37.99  ? 55  ALA D N   1 
ATOM   2636  C  CA  . ALA C  1 55  ? -24.368 42.384  33.922  1.00 39.08  ? 55  ALA D CA  1 
ATOM   2637  C  C   . ALA C  1 55  ? -24.315 43.149  32.600  1.00 38.06  ? 55  ALA D C   1 
ATOM   2638  O  O   . ALA C  1 55  ? -24.326 44.382  32.578  1.00 38.07  ? 55  ALA D O   1 
ATOM   2639  C  CB  . ALA C  1 55  ? -24.131 43.316  35.104  1.00 39.64  ? 55  ALA D CB  1 
ATOM   2640  N  N   . GLY C  1 56  ? -24.244 42.404  31.500  1.00 37.48  ? 56  GLY D N   1 
ATOM   2641  C  CA  . GLY C  1 56  ? -24.109 42.989  30.172  1.00 36.69  ? 56  GLY D CA  1 
ATOM   2642  C  C   . GLY C  1 56  ? -22.793 43.720  29.976  1.00 35.19  ? 56  GLY D C   1 
ATOM   2643  O  O   . GLY C  1 56  ? -21.770 43.374  30.586  1.00 34.52  ? 56  GLY D O   1 
ATOM   2644  N  N   . ALA C  1 57  ? -22.828 44.743  29.123  1.00 34.92  ? 57  ALA D N   1 
ATOM   2645  C  CA  . ALA C  1 57  ? -21.669 45.586  28.848  1.00 33.68  ? 57  ALA D CA  1 
ATOM   2646  C  C   . ALA C  1 57  ? -21.167 46.360  30.075  1.00 33.71  ? 57  ALA D C   1 
ATOM   2647  O  O   . ALA C  1 57  ? -19.988 46.708  30.133  1.00 32.86  ? 57  ALA D O   1 
ATOM   2648  C  CB  . ALA C  1 57  ? -21.999 46.556  27.725  1.00 33.87  ? 57  ALA D CB  1 
ATOM   2649  N  N   . THR C  1 58  ? -22.068 46.636  31.027  1.00 34.97  ? 58  THR D N   1 
ATOM   2650  C  CA  . THR C  1 58  ? -21.771 47.379  32.261  1.00 35.40  ? 58  THR D CA  1 
ATOM   2651  C  C   . THR C  1 58  ? -20.657 46.753  33.109  1.00 34.67  ? 58  THR D C   1 
ATOM   2652  O  O   . THR C  1 58  ? -19.834 47.478  33.669  1.00 34.63  ? 58  THR D O   1 
ATOM   2653  C  CB  . THR C  1 58  ? -23.042 47.542  33.134  1.00 37.38  ? 58  THR D CB  1 
ATOM   2654  O  OG1 . THR C  1 58  ? -24.166 47.867  32.304  1.00 38.30  ? 58  THR D OG1 1 
ATOM   2655  C  CG2 . THR C  1 58  ? -22.869 48.640  34.173  1.00 38.19  ? 58  THR D CG2 1 
ATOM   2656  N  N   . SER C  1 59  ? -20.601 45.421  33.172  1.00 34.26  ? 59  SER D N   1 
ATOM   2657  C  CA  . SER C  1 59  ? -19.568 44.715  33.952  1.00 33.76  ? 59  SER D CA  1 
ATOM   2658  C  C   . SER C  1 59  ? -18.176 44.642  33.282  1.00 32.14  ? 59  SER D C   1 
ATOM   2659  O  O   . SER C  1 59  ? -17.236 44.119  33.881  1.00 31.99  ? 59  SER D O   1 
ATOM   2660  C  CB  . SER C  1 59  ? -20.052 43.312  34.317  1.00 34.48  ? 59  SER D CB  1 
ATOM   2661  O  OG  . SER C  1 59  ? -20.691 42.683  33.216  1.00 34.33  ? 59  SER D OG  1 
ATOM   2662  N  N   . ALA C  1 60  ? -18.039 45.187  32.073  1.00 31.04  ? 60  ALA D N   1 
ATOM   2663  C  CA  . ALA C  1 60  ? -16.766 45.229  31.370  1.00 29.81  ? 60  ALA D CA  1 
ATOM   2664  C  C   . ALA C  1 60  ? -15.738 46.168  31.984  1.00 29.65  ? 60  ALA D C   1 
ATOM   2665  O  O   . ALA C  1 60  ? -14.583 46.139  31.580  1.00 29.03  ? 60  ALA D O   1 
ATOM   2666  C  CB  . ALA C  1 60  ? -16.973 45.601  29.911  1.00 29.22  ? 60  ALA D CB  1 
ATOM   2667  N  N   . GLY C  1 61  ? -16.155 47.028  32.909  1.00 30.35  ? 61  GLY D N   1 
ATOM   2668  C  CA  . GLY C  1 61  ? -15.245 47.966  33.557  1.00 30.50  ? 61  GLY D CA  1 
ATOM   2669  C  C   . GLY C  1 61  ? -14.864 49.121  32.640  1.00 29.93  ? 61  GLY D C   1 
ATOM   2670  O  O   . GLY C  1 61  ? -15.546 49.380  31.650  1.00 29.56  ? 61  GLY D O   1 
ATOM   2671  N  N   . PRO C  1 62  ? -13.756 49.821  32.958  1.00 29.98  ? 62  PRO D N   1 
ATOM   2672  C  CA  . PRO C  1 62  ? -13.369 50.984  32.169  1.00 29.77  ? 62  PRO D CA  1 
ATOM   2673  C  C   . PRO C  1 62  ? -12.618 50.571  30.911  1.00 28.74  ? 62  PRO D C   1 
ATOM   2674  O  O   . PRO C  1 62  ? -12.490 49.375  30.630  1.00 28.12  ? 62  PRO D O   1 
ATOM   2675  C  CB  . PRO C  1 62  ? -12.466 51.755  33.131  1.00 30.64  ? 62  PRO D CB  1 
ATOM   2676  C  CG  . PRO C  1 62  ? -11.793 50.679  33.919  1.00 30.74  ? 62  PRO D CG  1 
ATOM   2677  C  CD  . PRO C  1 62  ? -12.798 49.563  34.051  1.00 30.49  ? 62  PRO D CD  1 
ATOM   2678  N  N   . HIS C  1 63  ? -12.120 51.553  30.165  1.00 28.68  ? 63  HIS D N   1 
ATOM   2679  C  CA  . HIS C  1 63  ? -11.284 51.269  29.001  1.00 28.01  ? 63  HIS D CA  1 
ATOM   2680  C  C   . HIS C  1 63  ? -9.997  50.548  29.427  1.00 27.81  ? 63  HIS D C   1 
ATOM   2681  O  O   . HIS C  1 63  ? -9.445  50.828  30.487  1.00 28.36  ? 63  HIS D O   1 
ATOM   2682  C  CB  . HIS C  1 63  ? -10.909 52.549  28.244  1.00 28.46  ? 63  HIS D CB  1 
ATOM   2683  C  CG  . HIS C  1 63  ? -12.074 53.299  27.689  1.00 28.75  ? 63  HIS D CG  1 
ATOM   2684  N  ND1 . HIS C  1 63  ? -11.951 54.558  27.147  1.00 29.48  ? 63  HIS D ND1 1 
ATOM   2685  C  CD2 . HIS C  1 63  ? -13.387 52.988  27.616  1.00 28.75  ? 63  HIS D CD2 1 
ATOM   2686  C  CE1 . HIS C  1 63  ? -13.134 54.986  26.752  1.00 29.84  ? 63  HIS D CE1 1 
ATOM   2687  N  NE2 . HIS C  1 63  ? -14.026 54.058  27.037  1.00 29.42  ? 63  HIS D NE2 1 
ATOM   2688  N  N   . PHE C  1 64  ? -9.541  49.616  28.597  1.00 27.16  ? 64  PHE D N   1 
ATOM   2689  C  CA  . PHE C  1 64  ? -8.289  48.900  28.842  1.00 27.25  ? 64  PHE D CA  1 
ATOM   2690  C  C   . PHE C  1 64  ? -7.163  49.919  28.822  1.00 27.91  ? 64  PHE D C   1 
ATOM   2691  O  O   . PHE C  1 64  ? -6.953  50.592  27.810  1.00 27.85  ? 64  PHE D O   1 
ATOM   2692  C  CB  . PHE C  1 64  ? -8.095  47.810  27.789  1.00 26.68  ? 64  PHE D CB  1 
ATOM   2693  C  CG  . PHE C  1 64  ? -6.839  46.996  27.946  1.00 26.98  ? 64  PHE D CG  1 
ATOM   2694  C  CD1 . PHE C  1 64  ? -6.434  46.507  29.188  1.00 27.51  ? 64  PHE D CD1 1 
ATOM   2695  C  CD2 . PHE C  1 64  ? -6.082  46.672  26.826  1.00 27.02  ? 64  PHE D CD2 1 
ATOM   2696  C  CE1 . PHE C  1 64  ? -5.286  45.741  29.304  1.00 28.02  ? 64  PHE D CE1 1 
ATOM   2697  C  CE2 . PHE C  1 64  ? -4.934  45.901  26.934  1.00 27.48  ? 64  PHE D CE2 1 
ATOM   2698  C  CZ  . PHE C  1 64  ? -4.541  45.432  28.173  1.00 28.01  ? 64  PHE D CZ  1 
ATOM   2699  N  N   . ASN C  1 65  ? -6.487  50.052  29.964  1.00 28.71  ? 65  ASN D N   1 
ATOM   2700  C  CA  . ASN C  1 65  ? -5.532  51.135  30.191  1.00 29.80  ? 65  ASN D CA  1 
ATOM   2701  C  C   . ASN C  1 65  ? -4.320  50.706  31.052  1.00 30.84  ? 65  ASN D C   1 
ATOM   2702  O  O   . ASN C  1 65  ? -4.071  51.274  32.119  1.00 31.83  ? 65  ASN D O   1 
ATOM   2703  C  CB  . ASN C  1 65  ? -6.271  52.314  30.836  1.00 30.24  ? 65  ASN D CB  1 
ATOM   2704  C  CG  . ASN C  1 65  ? -5.413  53.562  30.939  1.00 31.44  ? 65  ASN D CG  1 
ATOM   2705  O  OD1 . ASN C  1 65  ? -4.451  53.748  30.172  1.00 31.68  ? 65  ASN D OD1 1 
ATOM   2706  N  ND2 . ASN C  1 65  ? -5.771  54.443  31.875  1.00 32.22  ? 65  ASN D ND2 1 
ATOM   2707  N  N   . PRO C  1 66  ? -3.541  49.718  30.574  1.00 30.86  ? 66  PRO D N   1 
ATOM   2708  C  CA  . PRO C  1 66  ? -2.427  49.188  31.382  1.00 32.03  ? 66  PRO D CA  1 
ATOM   2709  C  C   . PRO C  1 66  ? -1.260  50.162  31.627  1.00 33.65  ? 66  PRO D C   1 
ATOM   2710  O  O   . PRO C  1 66  ? -0.519  49.973  32.595  1.00 34.91  ? 66  PRO D O   1 
ATOM   2711  C  CB  . PRO C  1 66  ? -1.968  47.959  30.590  1.00 31.63  ? 66  PRO D CB  1 
ATOM   2712  C  CG  . PRO C  1 66  ? -2.367  48.249  29.183  1.00 30.72  ? 66  PRO D CG  1 
ATOM   2713  C  CD  . PRO C  1 66  ? -3.639  49.047  29.265  1.00 30.01  ? 66  PRO D CD  1 
ATOM   2714  N  N   . LEU C  1 67  ? -1.122  51.194  30.791  1.00 33.84  ? 67  LEU D N   1 
ATOM   2715  C  CA  . LEU C  1 67  ? -0.103  52.236  30.983  1.00 35.60  ? 67  LEU D CA  1 
ATOM   2716  C  C   . LEU C  1 67  ? -0.609  53.473  31.751  1.00 36.27  ? 67  LEU D C   1 
ATOM   2717  O  O   . LEU C  1 67  ? 0.105   54.468  31.838  1.00 37.69  ? 67  LEU D O   1 
ATOM   2718  C  CB  . LEU C  1 67  ? 0.492   52.642  29.622  1.00 35.85  ? 67  LEU D CB  1 
ATOM   2719  C  CG  . LEU C  1 67  ? 1.165   51.507  28.832  1.00 35.75  ? 67  LEU D CG  1 
ATOM   2720  C  CD1 . LEU C  1 67  ? 1.608   51.960  27.443  1.00 36.13  ? 67  LEU D CD1 1 
ATOM   2721  C  CD2 . LEU C  1 67  ? 2.359   50.953  29.593  1.00 37.28  ? 67  LEU D CD2 1 
ATOM   2722  N  N   . SER C  1 68  ? -1.825  53.407  32.310  1.00 35.49  ? 68  SER D N   1 
ATOM   2723  C  CA  . SER C  1 68  ? -2.397  54.488  33.131  1.00 36.26  ? 68  SER D CA  1 
ATOM   2724  C  C   . SER C  1 68  ? -2.296  55.863  32.458  1.00 36.89  ? 68  SER D C   1 
ATOM   2725  O  O   . SER C  1 68  ? -1.835  56.829  33.065  1.00 38.37  ? 68  SER D O   1 
ATOM   2726  C  CB  . SER C  1 68  ? -1.719  54.522  34.517  1.00 37.97  ? 68  SER D CB  1 
ATOM   2727  O  OG  . SER C  1 68  ? -1.862  53.280  35.186  1.00 37.69  ? 68  SER D OG  1 
ATOM   2728  N  N   . ARG C  1 69  ? -2.704  55.922  31.197  1.00 35.92  ? 69  ARG D N   1 
ATOM   2729  C  CA  . ARG C  1 69  ? -2.750  57.159  30.423  1.00 36.59  ? 69  ARG D CA  1 
ATOM   2730  C  C   . ARG C  1 69  ? -4.174  57.752  30.466  1.00 35.97  ? 69  ARG D C   1 
ATOM   2731  O  O   . ARG C  1 69  ? -5.099  57.145  31.014  1.00 35.01  ? 69  ARG D O   1 
ATOM   2732  C  CB  . ARG C  1 69  ? -2.349  56.877  28.966  1.00 36.34  ? 69  ARG D CB  1 
ATOM   2733  C  CG  . ARG C  1 69  ? -0.956  56.268  28.759  1.00 37.27  ? 69  ARG D CG  1 
ATOM   2734  C  CD  . ARG C  1 69  ? 0.102   57.326  28.493  1.00 39.36  ? 69  ARG D CD  1 
ATOM   2735  N  NE  . ARG C  1 69  ? 1.467   56.778  28.423  1.00 40.65  ? 69  ARG D NE  1 
ATOM   2736  C  CZ  . ARG C  1 69  ? 2.051   56.234  27.348  1.00 40.81  ? 69  ARG D CZ  1 
ATOM   2737  N  NH1 . ARG C  1 69  ? 1.416   56.114  26.176  1.00 39.91  ? 69  ARG D NH1 1 
ATOM   2738  N  NH2 . ARG C  1 69  ? 3.300   55.782  27.449  1.00 42.19  ? 69  ARG D NH2 1 
ATOM   2739  N  N   . LYS C  1 70  ? -4.325  58.946  29.900  1.00 36.64  ? 70  LYS D N   1 
ATOM   2740  C  CA  . LYS C  1 70  ? -5.632  59.580  29.721  1.00 36.32  ? 70  LYS D CA  1 
ATOM   2741  C  C   . LYS C  1 70  ? -6.262  59.126  28.412  1.00 35.08  ? 70  LYS D C   1 
ATOM   2742  O  O   . LYS C  1 70  ? -5.567  58.670  27.501  1.00 34.69  ? 70  LYS D O   1 
ATOM   2743  C  CB  . LYS C  1 70  ? -5.506  61.104  29.728  1.00 38.02  ? 70  LYS D CB  1 
ATOM   2744  C  CG  . LYS C  1 70  ? -5.238  61.686  31.106  1.00 39.41  ? 70  LYS D CG  1 
ATOM   2745  C  CD  . LYS C  1 70  ? -5.298  63.206  31.113  1.00 41.18  ? 70  LYS D CD  1 
ATOM   2746  C  CE  . LYS C  1 70  ? -4.235  63.826  30.214  1.00 42.29  ? 70  LYS D CE  1 
ATOM   2747  N  NZ  . LYS C  1 70  ? -3.673  65.087  30.766  1.00 44.56  ? 70  LYS D NZ  1 
ATOM   2748  N  N   . HIS C  1 71  ? -7.583  59.266  28.328  1.00 34.55  ? 71  HIS D N   1 
ATOM   2749  C  CA  . HIS C  1 71  ? -8.328  58.895  27.122  1.00 33.71  ? 71  HIS D CA  1 
ATOM   2750  C  C   . HIS C  1 71  ? -7.971  59.793  25.936  1.00 34.62  ? 71  HIS D C   1 
ATOM   2751  O  O   . HIS C  1 71  ? -7.770  60.991  26.092  1.00 35.95  ? 71  HIS D O   1 
ATOM   2752  C  CB  . HIS C  1 71  ? -9.838  58.957  27.365  1.00 33.40  ? 71  HIS D CB  1 
ATOM   2753  C  CG  . HIS C  1 71  ? -10.649 58.563  26.171  1.00 32.80  ? 71  HIS D CG  1 
ATOM   2754  N  ND1 . HIS C  1 71  ? -10.815 57.251  25.779  1.00 31.60  ? 71  HIS D ND1 1 
ATOM   2755  C  CD2 . HIS C  1 71  ? -11.294 59.317  25.252  1.00 33.47  ? 71  HIS D CD2 1 
ATOM   2756  C  CE1 . HIS C  1 71  ? -11.558 57.217  24.685  1.00 31.61  ? 71  HIS D CE1 1 
ATOM   2757  N  NE2 . HIS C  1 71  ? -11.860 58.457  24.346  1.00 32.70  ? 71  HIS D NE2 1 
ATOM   2758  N  N   . GLY C  1 72  ? -7.904  59.196  24.751  1.00 34.17  ? 72  GLY D N   1 
ATOM   2759  C  CA  . GLY C  1 72  ? -7.608  59.933  23.524  1.00 35.24  ? 72  GLY D CA  1 
ATOM   2760  C  C   . GLY C  1 72  ? -8.191  59.233  22.318  1.00 34.71  ? 72  GLY D C   1 
ATOM   2761  O  O   . GLY C  1 72  ? -8.901  58.242  22.456  1.00 33.52  ? 72  GLY D O   1 
ATOM   2762  N  N   . GLY C  1 73  ? -7.908  59.767  21.136  1.00 35.87  ? 73  GLY D N   1 
ATOM   2763  C  CA  . GLY C  1 73  ? -8.217  59.078  19.892  1.00 35.75  ? 73  GLY D CA  1 
ATOM   2764  C  C   . GLY C  1 73  ? -7.119  58.075  19.575  1.00 35.41  ? 73  GLY D C   1 
ATOM   2765  O  O   . GLY C  1 73  ? -6.042  58.129  20.174  1.00 35.65  ? 73  GLY D O   1 
ATOM   2766  N  N   . PRO C  1 74  ? -7.369  57.157  18.622  1.00 35.18  ? 74  PRO D N   1 
ATOM   2767  C  CA  . PRO C  1 74  ? -6.359  56.143  18.275  1.00 34.97  ? 74  PRO D CA  1 
ATOM   2768  C  C   . PRO C  1 74  ? -5.020  56.703  17.768  1.00 36.60  ? 74  PRO D C   1 
ATOM   2769  O  O   . PRO C  1 74  ? -3.986  56.060  17.971  1.00 36.57  ? 74  PRO D O   1 
ATOM   2770  C  CB  . PRO C  1 74  ? -7.061  55.290  17.199  1.00 34.66  ? 74  PRO D CB  1 
ATOM   2771  C  CG  . PRO C  1 74  ? -8.190  56.131  16.696  1.00 35.33  ? 74  PRO D CG  1 
ATOM   2772  C  CD  . PRO C  1 74  ? -8.620  56.963  17.863  1.00 35.12  ? 74  PRO D CD  1 
ATOM   2773  N  N   . LYS C  1 75  ? -5.033  57.887  17.155  1.00 38.29  ? 75  LYS D N   1 
ATOM   2774  C  CA  . LYS C  1 75  ? -3.817  58.509  16.622  1.00 40.25  ? 75  LYS D CA  1 
ATOM   2775  C  C   . LYS C  1 75  ? -3.018  59.341  17.645  1.00 41.08  ? 75  LYS D C   1 
ATOM   2776  O  O   . LYS C  1 75  ? -1.925  59.792  17.340  1.00 42.63  ? 75  LYS D O   1 
ATOM   2777  C  CB  . LYS C  1 75  ? -4.166  59.376  15.410  1.00 41.94  ? 75  LYS D CB  1 
ATOM   2778  C  CG  . LYS C  1 75  ? -4.909  58.623  14.314  1.00 41.75  ? 75  LYS D CG  1 
ATOM   2779  C  CD  . LYS C  1 75  ? -5.065  59.453  13.048  1.00 43.87  ? 75  LYS D CD  1 
ATOM   2780  C  CE  . LYS C  1 75  ? -6.079  60.571  13.231  1.00 44.49  ? 75  LYS D CE  1 
ATOM   2781  N  NZ  . LYS C  1 75  ? -6.313  61.320  11.965  1.00 46.71  ? 75  LYS D NZ  1 
ATOM   2782  N  N   . ASP C  1 76  ? -3.565  59.555  18.840  1.00 40.40  ? 76  ASP D N   1 
ATOM   2783  C  CA  . ASP C  1 76  ? -2.878  60.314  19.891  1.00 41.32  ? 76  ASP D CA  1 
ATOM   2784  C  C   . ASP C  1 76  ? -1.806  59.452  20.556  1.00 41.05  ? 76  ASP D C   1 
ATOM   2785  O  O   . ASP C  1 76  ? -1.974  58.236  20.674  1.00 39.83  ? 76  ASP D O   1 
ATOM   2786  C  CB  . ASP C  1 76  ? -3.874  60.780  20.957  1.00 40.73  ? 76  ASP D CB  1 
ATOM   2787  C  CG  . ASP C  1 76  ? -4.891  61.773  20.424  1.00 41.52  ? 76  ASP D CG  1 
ATOM   2788  O  OD1 . ASP C  1 76  ? -4.524  62.629  19.600  1.00 43.25  ? 76  ASP D OD1 1 
ATOM   2789  O  OD2 . ASP C  1 76  ? -6.068  61.710  20.845  1.00 40.73  ? 76  ASP D OD2 1 
ATOM   2790  N  N   . GLU C  1 77  ? -0.709  60.079  20.985  1.00 42.52  ? 77  GLU D N   1 
ATOM   2791  C  CA  . GLU C  1 77  ? 0.265   59.404  21.854  1.00 42.49  ? 77  GLU D CA  1 
ATOM   2792  C  C   . GLU C  1 77  ? -0.357  59.171  23.240  1.00 40.99  ? 77  GLU D C   1 
ATOM   2793  O  O   . GLU C  1 77  ? -0.200  58.095  23.815  1.00 39.97  ? 77  GLU D O   1 
ATOM   2794  C  CB  . GLU C  1 77  ? 1.577   60.200  21.969  1.00 45.04  ? 77  GLU D CB  1 
ATOM   2795  C  CG  . GLU C  1 77  ? 2.644   59.476  22.787  1.00 45.62  ? 77  GLU D CG  1 
ATOM   2796  C  CD  . GLU C  1 77  ? 4.061   59.810  22.367  1.00 48.19  ? 77  GLU D CD  1 
ATOM   2797  O  OE1 . GLU C  1 77  ? 4.428   61.012  22.330  1.00 50.23  ? 77  GLU D OE1 1 
ATOM   2798  O  OE2 . GLU C  1 77  ? 4.820   58.858  22.077  1.00 48.66  ? 77  GLU D OE2 1 
ATOM   2799  N  N   . GLU C  1 78  ? -1.064  60.182  23.751  1.00 40.91  ? 78  GLU D N   1 
ATOM   2800  C  CA  . GLU C  1 78  ? -1.810  60.069  25.005  1.00 39.78  ? 78  GLU D CA  1 
ATOM   2801  C  C   . GLU C  1 78  ? -3.160  59.392  24.732  1.00 37.65  ? 78  GLU D C   1 
ATOM   2802  O  O   . GLU C  1 78  ? -4.129  60.043  24.316  1.00 37.65  ? 78  GLU D O   1 
ATOM   2803  C  CB  . GLU C  1 78  ? -2.009  61.447  25.656  1.00 41.21  ? 78  GLU D CB  1 
ATOM   2804  C  CG  . GLU C  1 78  ? -2.546  61.409  27.084  1.00 40.94  ? 78  GLU D CG  1 
ATOM   2805  C  CD  . GLU C  1 78  ? -1.563  60.838  28.108  1.00 41.48  ? 78  GLU D CD  1 
ATOM   2806  O  OE1 . GLU C  1 78  ? -0.349  60.726  27.806  1.00 42.65  ? 78  GLU D OE1 1 
ATOM   2807  O  OE2 . GLU C  1 78  ? -2.010  60.495  29.229  1.00 41.10  ? 78  GLU D OE2 1 
ATOM   2808  N  N   . ARG C  1 79  ? -3.196  58.079  24.942  1.00 35.94  ? 79  ARG D N   1 
ATOM   2809  C  CA  . ARG C  1 79  ? -4.417  57.296  24.787  1.00 34.16  ? 79  ARG D CA  1 
ATOM   2810  C  C   . ARG C  1 79  ? -4.357  56.067  25.662  1.00 33.03  ? 79  ARG D C   1 
ATOM   2811  O  O   . ARG C  1 79  ? -3.275  55.635  26.078  1.00 33.38  ? 79  ARG D O   1 
ATOM   2812  C  CB  . ARG C  1 79  ? -4.632  56.864  23.335  1.00 33.69  ? 79  ARG D CB  1 
ATOM   2813  C  CG  . ARG C  1 79  ? -3.501  56.027  22.757  1.00 33.81  ? 79  ARG D CG  1 
ATOM   2814  C  CD  . ARG C  1 79  ? -3.850  55.453  21.400  1.00 33.40  ? 79  ARG D CD  1 
ATOM   2815  N  NE  . ARG C  1 79  ? -4.500  54.145  21.503  1.00 31.93  ? 79  ARG D NE  1 
ATOM   2816  C  CZ  . ARG C  1 79  ? -4.701  53.314  20.483  1.00 31.53  ? 79  ARG D CZ  1 
ATOM   2817  N  NH1 . ARG C  1 79  ? -4.324  53.643  19.252  1.00 32.50  ? 79  ARG D NH1 1 
ATOM   2818  N  NH2 . ARG C  1 79  ? -5.283  52.140  20.698  1.00 30.36  ? 79  ARG D NH2 1 
ATOM   2819  N  N   . HIS C  1 80  ? -5.536  55.520  25.935  1.00 31.75  ? 80  HIS D N   1 
ATOM   2820  C  CA  . HIS C  1 80  ? -5.664  54.182  26.495  1.00 30.68  ? 80  HIS D CA  1 
ATOM   2821  C  C   . HIS C  1 80  ? -5.398  53.173  25.378  1.00 29.99  ? 80  HIS D C   1 
ATOM   2822  O  O   . HIS C  1 80  ? -5.688  53.449  24.208  1.00 29.90  ? 80  HIS D O   1 
ATOM   2823  C  CB  . HIS C  1 80  ? -7.077  53.937  27.047  1.00 29.93  ? 80  HIS D CB  1 
ATOM   2824  C  CG  . HIS C  1 80  ? -7.524  54.935  28.066  1.00 30.65  ? 80  HIS D CG  1 
ATOM   2825  N  ND1 . HIS C  1 80  ? -8.847  55.284  28.245  1.00 30.56  ? 80  HIS D ND1 1 
ATOM   2826  C  CD2 . HIS C  1 80  ? -6.819  55.652  28.967  1.00 31.69  ? 80  HIS D CD2 1 
ATOM   2827  C  CE1 . HIS C  1 80  ? -8.931  56.168  29.224  1.00 31.49  ? 80  HIS D CE1 1 
ATOM   2828  N  NE2 . HIS C  1 80  ? -7.714  56.413  29.673  1.00 32.16  ? 80  HIS D NE2 1 
ATOM   2829  N  N   . VAL C  1 81  ? -4.872  52.005  25.747  1.00 29.57  ? 81  VAL D N   1 
ATOM   2830  C  CA  . VAL C  1 81  ? -4.693  50.898  24.796  1.00 29.06  ? 81  VAL D CA  1 
ATOM   2831  C  C   . VAL C  1 81  ? -6.012  50.597  24.088  1.00 28.23  ? 81  VAL D C   1 
ATOM   2832  O  O   . VAL C  1 81  ? -6.044  50.457  22.870  1.00 28.30  ? 81  VAL D O   1 
ATOM   2833  C  CB  . VAL C  1 81  ? -4.125  49.620  25.475  1.00 28.87  ? 81  VAL D CB  1 
ATOM   2834  C  CG1 . VAL C  1 81  ? -4.200  48.407  24.550  1.00 28.34  ? 81  VAL D CG1 1 
ATOM   2835  C  CG2 . VAL C  1 81  ? -2.678  49.840  25.900  1.00 30.05  ? 81  VAL D CG2 1 
ATOM   2836  N  N   . GLY C  1 82  ? -7.106  50.565  24.845  1.00 27.74  ? 82  GLY D N   1 
ATOM   2837  C  CA  . GLY C  1 82  ? -8.425  50.291  24.282  1.00 27.26  ? 82  GLY D CA  1 
ATOM   2838  C  C   . GLY C  1 82  ? -9.094  51.368  23.442  1.00 27.74  ? 82  GLY D C   1 
ATOM   2839  O  O   . GLY C  1 82  ? -10.239 51.186  23.034  1.00 27.54  ? 82  GLY D O   1 
ATOM   2840  N  N   . ASP C  1 83  ? -8.407  52.476  23.161  1.00 28.63  ? 83  ASP D N   1 
ATOM   2841  C  CA  . ASP C  1 83  ? -9.024  53.612  22.456  1.00 29.43  ? 83  ASP D CA  1 
ATOM   2842  C  C   . ASP C  1 83  ? -8.985  53.465  20.932  1.00 29.83  ? 83  ASP D C   1 
ATOM   2843  O  O   . ASP C  1 83  ? -8.048  53.935  20.283  1.00 30.55  ? 83  ASP D O   1 
ATOM   2844  C  CB  . ASP C  1 83  ? -8.342  54.929  22.859  1.00 30.46  ? 83  ASP D CB  1 
ATOM   2845  C  CG  . ASP C  1 83  ? -8.684  55.367  24.262  1.00 30.51  ? 83  ASP D CG  1 
ATOM   2846  O  OD1 . ASP C  1 83  ? -9.651  54.837  24.857  1.00 29.96  ? 83  ASP D OD1 1 
ATOM   2847  O  OD2 . ASP C  1 83  ? -7.991  56.270  24.778  1.00 31.36  ? 83  ASP D OD2 1 
ATOM   2848  N  N   . LEU C  1 84  ? -10.027 52.849  20.370  1.00 29.56  ? 84  LEU D N   1 
ATOM   2849  C  CA  . LEU C  1 84  ? -10.133 52.668  18.909  1.00 30.18  ? 84  LEU D CA  1 
ATOM   2850  C  C   . LEU C  1 84  ? -10.999 53.725  18.210  1.00 31.26  ? 84  LEU D C   1 
ATOM   2851  O  O   . LEU C  1 84  ? -11.355 53.551  17.052  1.00 31.96  ? 84  LEU D O   1 
ATOM   2852  C  CB  . LEU C  1 84  ? -10.614 51.247  18.574  1.00 29.49  ? 84  LEU D CB  1 
ATOM   2853  C  CG  . LEU C  1 84  ? -9.696  50.130  19.069  1.00 28.77  ? 84  LEU D CG  1 
ATOM   2854  C  CD1 . LEU C  1 84  ? -10.297 48.767  18.778  1.00 28.30  ? 84  LEU D CD1 1 
ATOM   2855  C  CD2 . LEU C  1 84  ? -8.306  50.233  18.452  1.00 29.39  ? 84  LEU D CD2 1 
ATOM   2856  N  N   . GLY C  1 85  ? -11.312 54.822  18.900  1.00 31.74  ? 85  GLY D N   1 
ATOM   2857  C  CA  . GLY C  1 85  ? -11.931 55.989  18.276  1.00 33.14  ? 85  GLY D CA  1 
ATOM   2858  C  C   . GLY C  1 85  ? -13.400 55.789  17.946  1.00 33.45  ? 85  GLY D C   1 
ATOM   2859  O  O   . GLY C  1 85  ? -14.175 55.330  18.797  1.00 32.76  ? 85  GLY D O   1 
ATOM   2860  N  N   . ASN C  1 86  ? -13.773 56.136  16.715  1.00 34.70  ? 86  ASN D N   1 
ATOM   2861  C  CA  . ASN C  1 86  ? -15.159 56.099  16.265  1.00 35.51  ? 86  ASN D CA  1 
ATOM   2862  C  C   . ASN C  1 86  ? -15.309 55.216  15.038  1.00 35.97  ? 86  ASN D C   1 
ATOM   2863  O  O   . ASN C  1 86  ? -14.429 55.188  14.176  1.00 36.48  ? 86  ASN D O   1 
ATOM   2864  C  CB  . ASN C  1 86  ? -15.654 57.508  15.926  1.00 37.23  ? 86  ASN D CB  1 
ATOM   2865  C  CG  . ASN C  1 86  ? -15.972 58.330  17.161  1.00 37.18  ? 86  ASN D CG  1 
ATOM   2866  O  OD1 . ASN C  1 86  ? -16.733 57.891  18.025  1.00 36.51  ? 86  ASN D OD1 1 
ATOM   2867  N  ND2 . ASN C  1 86  ? -15.394 59.528  17.252  1.00 38.05  ? 86  ASN D ND2 1 
ATOM   2868  N  N   . VAL C  1 87  ? -16.433 54.501  14.978  1.00 36.06  ? 87  VAL D N   1 
ATOM   2869  C  CA  . VAL C  1 87  ? -16.904 53.863  13.742  1.00 37.06  ? 87  VAL D CA  1 
ATOM   2870  C  C   . VAL C  1 87  ? -18.068 54.695  13.225  1.00 38.99  ? 87  VAL D C   1 
ATOM   2871  O  O   . VAL C  1 87  ? -18.778 55.318  14.012  1.00 39.24  ? 87  VAL D O   1 
ATOM   2872  C  CB  . VAL C  1 87  ? -17.322 52.381  13.932  1.00 36.08  ? 87  VAL D CB  1 
ATOM   2873  C  CG1 . VAL C  1 87  ? -16.127 51.543  14.360  1.00 34.50  ? 87  VAL D CG1 1 
ATOM   2874  C  CG2 . VAL C  1 87  ? -18.485 52.220  14.911  1.00 35.83  ? 87  VAL D CG2 1 
ATOM   2875  N  N   . THR C  1 88  ? -18.253 54.703  11.906  1.00 40.65  ? 88  THR D N   1 
ATOM   2876  C  CA  . THR C  1 88  ? -19.260 55.543  11.246  1.00 42.88  ? 88  THR D CA  1 
ATOM   2877  C  C   . THR C  1 88  ? -20.361 54.682  10.635  1.00 43.88  ? 88  THR D C   1 
ATOM   2878  O  O   . THR C  1 88  ? -20.080 53.836  9.787   1.00 44.12  ? 88  THR D O   1 
ATOM   2879  C  CB  . THR C  1 88  ? -18.620 56.391  10.127  1.00 44.55  ? 88  THR D CB  1 
ATOM   2880  O  OG1 . THR C  1 88  ? -17.544 57.158  10.674  1.00 43.82  ? 88  THR D OG1 1 
ATOM   2881  C  CG2 . THR C  1 88  ? -19.648 57.342  9.487   1.00 47.09  ? 88  THR D CG2 1 
ATOM   2882  N  N   . ALA C  1 89  ? -21.601 54.904  11.066  1.00 44.69  ? 89  ALA D N   1 
ATOM   2883  C  CA  . ALA C  1 89  ? -22.759 54.208  10.509  1.00 46.12  ? 89  ALA D CA  1 
ATOM   2884  C  C   . ALA C  1 89  ? -23.326 55.012  9.345   1.00 48.97  ? 89  ALA D C   1 
ATOM   2885  O  O   . ALA C  1 89  ? -23.486 56.231  9.453   1.00 50.04  ? 89  ALA D O   1 
ATOM   2886  C  CB  . ALA C  1 89  ? -23.827 54.022  11.575  1.00 45.92  ? 89  ALA D CB  1 
ATOM   2887  N  N   . ASP C  1 90  ? -23.631 54.328  8.240   1.00 50.38  ? 90  ASP D N   1 
ATOM   2888  C  CA  . ASP C  1 90  ? -24.282 54.959  7.085   1.00 53.46  ? 90  ASP D CA  1 
ATOM   2889  C  C   . ASP C  1 90  ? -25.750 55.292  7.397   1.00 55.22  ? 90  ASP D C   1 
ATOM   2890  O  O   . ASP C  1 90  ? -26.216 55.081  8.521   1.00 54.01  ? 90  ASP D O   1 
ATOM   2891  C  CB  . ASP C  1 90  ? -24.118 54.105  5.799   1.00 54.66  ? 90  ASP D CB  1 
ATOM   2892  C  CG  . ASP C  1 90  ? -24.865 52.764  5.837   1.00 54.55  ? 90  ASP D CG  1 
ATOM   2893  O  OD1 . ASP C  1 90  ? -25.720 52.527  6.716   1.00 54.12  ? 90  ASP D OD1 1 
ATOM   2894  O  OD2 . ASP C  1 90  ? -24.587 51.929  4.956   1.00 55.08  ? 90  ASP D OD2 1 
ATOM   2895  N  N   . LYS C  1 91  ? -26.464 55.826  6.410   1.00 58.33  ? 91  LYS D N   1 
ATOM   2896  C  CA  . LYS C  1 91  ? -27.895 56.156  6.547   1.00 60.61  ? 91  LYS D CA  1 
ATOM   2897  C  C   . LYS C  1 91  ? -28.811 54.966  6.889   1.00 60.50  ? 91  LYS D C   1 
ATOM   2898  O  O   . LYS C  1 91  ? -29.871 55.155  7.492   1.00 61.52  ? 91  LYS D O   1 
ATOM   2899  C  CB  . LYS C  1 91  ? -28.399 56.845  5.270   1.00 64.29  ? 91  LYS D CB  1 
ATOM   2900  C  CG  . LYS C  1 91  ? -28.431 55.952  4.035   1.00 65.81  ? 91  LYS D CG  1 
ATOM   2901  C  CD  . LYS C  1 91  ? -28.064 56.700  2.756   1.00 68.41  ? 91  LYS D CD  1 
ATOM   2902  C  CE  . LYS C  1 91  ? -28.994 57.866  2.446   1.00 71.78  ? 91  LYS D CE  1 
ATOM   2903  N  NZ  . LYS C  1 91  ? -30.377 57.423  2.118   1.00 74.50  ? 91  LYS D NZ  1 
ATOM   2904  N  N   . ASP C  1 92  ? -28.406 53.756  6.494   1.00 59.47  ? 92  ASP D N   1 
ATOM   2905  C  CA  . ASP C  1 92  ? -29.152 52.528  6.802   1.00 59.32  ? 92  ASP D CA  1 
ATOM   2906  C  C   . ASP C  1 92  ? -28.766 51.894  8.142   1.00 56.10  ? 92  ASP D C   1 
ATOM   2907  O  O   . ASP C  1 92  ? -29.265 50.822  8.485   1.00 55.79  ? 92  ASP D O   1 
ATOM   2908  C  CB  . ASP C  1 92  ? -28.988 51.506  5.663   1.00 60.29  ? 92  ASP D CB  1 
ATOM   2909  C  CG  . ASP C  1 92  ? -29.575 51.999  4.349   1.00 63.96  ? 92  ASP D CG  1 
ATOM   2910  O  OD1 . ASP C  1 92  ? -30.761 52.396  4.328   1.00 66.46  ? 92  ASP D OD1 1 
ATOM   2911  O  OD2 . ASP C  1 92  ? -28.854 51.990  3.332   1.00 64.64  ? 92  ASP D OD2 1 
ATOM   2912  N  N   . GLY C  1 93  ? -27.887 52.553  8.896   1.00 53.93  ? 93  GLY D N   1 
ATOM   2913  C  CA  . GLY C  1 93  ? -27.492 52.099  10.220  1.00 51.15  ? 93  GLY D CA  1 
ATOM   2914  C  C   . GLY C  1 93  ? -26.417 51.035  10.256  1.00 48.83  ? 93  GLY D C   1 
ATOM   2915  O  O   . GLY C  1 93  ? -26.280 50.345  11.266  1.00 47.00  ? 93  GLY D O   1 
ATOM   2916  N  N   . VAL C  1 94  ? -25.642 50.918  9.177   1.00 49.10  ? 94  VAL D N   1 
ATOM   2917  C  CA  . VAL C  1 94  ? -24.571 49.931  9.071   1.00 47.31  ? 94  VAL D CA  1 
ATOM   2918  C  C   . VAL C  1 94  ? -23.203 50.631  9.086   1.00 46.02  ? 94  VAL D C   1 
ATOM   2919  O  O   . VAL C  1 94  ? -22.942 51.523  8.272   1.00 47.49  ? 94  VAL D O   1 
ATOM   2920  C  CB  . VAL C  1 94  ? -24.730 49.070  7.797   1.00 48.90  ? 94  VAL D CB  1 
ATOM   2921  C  CG1 . VAL C  1 94  ? -23.540 48.137  7.610   1.00 47.28  ? 94  VAL D CG1 1 
ATOM   2922  C  CG2 . VAL C  1 94  ? -26.021 48.268  7.868   1.00 50.22  ? 94  VAL D CG2 1 
ATOM   2923  N  N   . ALA C  1 95  ? -22.346 50.230  10.020  1.00 43.60  ? 95  ALA D N   1 
ATOM   2924  C  CA  . ALA C  1 95  ? -20.965 50.704  10.078  1.00 42.39  ? 95  ALA D CA  1 
ATOM   2925  C  C   . ALA C  1 95  ? -20.029 49.584  9.645   1.00 41.55  ? 95  ALA D C   1 
ATOM   2926  O  O   . ALA C  1 95  ? -19.850 48.610  10.376  1.00 40.03  ? 95  ALA D O   1 
ATOM   2927  C  CB  . ALA C  1 95  ? -20.616 51.168  11.487  1.00 40.58  ? 95  ALA D CB  1 
ATOM   2928  N  N   . ASP C  1 96  ? -19.445 49.720  8.454   1.00 42.78  ? 96  ASP D N   1 
ATOM   2929  C  CA  . ASP C  1 96  ? -18.395 48.809  7.997   1.00 42.23  ? 96  ASP D CA  1 
ATOM   2930  C  C   . ASP C  1 96  ? -17.076 49.240  8.640   1.00 40.62  ? 96  ASP D C   1 
ATOM   2931  O  O   . ASP C  1 96  ? -16.598 50.342  8.406   1.00 41.23  ? 96  ASP D O   1 
ATOM   2932  C  CB  . ASP C  1 96  ? -18.295 48.802  6.466   1.00 44.50  ? 96  ASP D CB  1 
ATOM   2933  C  CG  . ASP C  1 96  ? -19.546 48.215  5.793   1.00 46.36  ? 96  ASP D CG  1 
ATOM   2934  O  OD1 . ASP C  1 96  ? -20.117 47.232  6.316   1.00 45.71  ? 96  ASP D OD1 1 
ATOM   2935  O  OD2 . ASP C  1 96  ? -19.960 48.728  4.732   1.00 48.77  ? 96  ASP D OD2 1 
ATOM   2936  N  N   . VAL C  1 97  ? -16.511 48.370  9.468   1.00 38.78  ? 97  VAL D N   1 
ATOM   2937  C  CA  . VAL C  1 97  ? -15.303 48.677  10.234  1.00 37.33  ? 97  VAL D CA  1 
ATOM   2938  C  C   . VAL C  1 97  ? -14.088 48.142  9.482   1.00 37.59  ? 97  VAL D C   1 
ATOM   2939  O  O   . VAL C  1 97  ? -14.096 46.996  9.032   1.00 37.67  ? 97  VAL D O   1 
ATOM   2940  C  CB  . VAL C  1 97  ? -15.370 48.045  11.636  1.00 35.47  ? 97  VAL D CB  1 
ATOM   2941  C  CG1 . VAL C  1 97  ? -14.188 48.494  12.499  1.00 34.27  ? 97  VAL D CG1 1 
ATOM   2942  C  CG2 . VAL C  1 97  ? -16.697 48.391  12.312  1.00 35.51  ? 97  VAL D CG2 1 
ATOM   2943  N  N   . SER C  1 98  ? -13.067 48.988  9.332   1.00 37.89  ? 98  SER D N   1 
ATOM   2944  C  CA  . SER C  1 98  ? -11.807 48.620  8.680   1.00 38.41  ? 98  SER D CA  1 
ATOM   2945  C  C   . SER C  1 98  ? -10.677 49.497  9.233   1.00 38.07  ? 98  SER D C   1 
ATOM   2946  O  O   . SER C  1 98  ? -10.391 50.570  8.713   1.00 39.36  ? 98  SER D O   1 
ATOM   2947  C  CB  . SER C  1 98  ? -11.922 48.744  7.161   1.00 40.65  ? 98  SER D CB  1 
ATOM   2948  O  OG  . SER C  1 98  ? -10.751 48.263  6.515   1.00 41.32  ? 98  SER D OG  1 
ATOM   2949  N  N   . ILE C  1 99  ? -10.054 49.007  10.301  1.00 36.55  ? 99  ILE D N   1 
ATOM   2950  C  CA  . ILE C  1 99  ? -9.109  49.748  11.116  1.00 36.10  ? 99  ILE D CA  1 
ATOM   2951  C  C   . ILE C  1 99  ? -7.784  48.986  11.166  1.00 35.94  ? 99  ILE D C   1 
ATOM   2952  O  O   . ILE C  1 99  ? -7.749  47.754  11.061  1.00 35.53  ? 99  ILE D O   1 
ATOM   2953  C  CB  . ILE C  1 99  ? -9.661  49.893  12.562  1.00 34.62  ? 99  ILE D CB  1 
ATOM   2954  C  CG1 . ILE C  1 99  ? -10.902 50.788  12.579  1.00 35.07  ? 99  ILE D CG1 1 
ATOM   2955  C  CG2 . ILE C  1 99  ? -8.612  50.442  13.532  1.00 34.13  ? 99  ILE D CG2 1 
ATOM   2956  C  CD1 . ILE C  1 99  ? -11.633 50.776  13.908  1.00 33.83  ? 99  ILE D CD1 1 
ATOM   2957  N  N   . GLU C  1 100 ? -6.699  49.734  11.340  1.00 36.42  ? 100 GLU D N   1 
ATOM   2958  C  CA  . GLU C  1 100 ? -5.413  49.160  11.722  1.00 36.22  ? 100 GLU D CA  1 
ATOM   2959  C  C   . GLU C  1 100 ? -4.888  49.900  12.948  1.00 35.39  ? 100 GLU D C   1 
ATOM   2960  O  O   . GLU C  1 100 ? -4.975  51.133  13.016  1.00 35.91  ? 100 GLU D O   1 
ATOM   2961  C  CB  . GLU C  1 100 ? -4.435  49.246  10.558  1.00 38.26  ? 100 GLU D CB  1 
ATOM   2962  C  CG  . GLU C  1 100 ? -3.377  48.166  10.588  1.00 38.57  ? 100 GLU D CG  1 
ATOM   2963  C  CD  . GLU C  1 100 ? -2.595  48.097  9.304   1.00 40.80  ? 100 GLU D CD  1 
ATOM   2964  O  OE1 . GLU C  1 100 ? -3.102  47.498  8.322   1.00 41.67  ? 100 GLU D OE1 1 
ATOM   2965  O  OE2 . GLU C  1 100 ? -1.476  48.646  9.280   1.00 42.08  ? 100 GLU D OE2 1 
ATOM   2966  N  N   . ASP C  1 101 ? -4.366  49.148  13.917  1.00 34.19  ? 101 ASP D N   1 
ATOM   2967  C  CA  . ASP C  1 101 ? -3.866  49.724  15.167  1.00 33.59  ? 101 ASP D CA  1 
ATOM   2968  C  C   . ASP C  1 101 ? -2.607  48.990  15.642  1.00 33.66  ? 101 ASP D C   1 
ATOM   2969  O  O   . ASP C  1 101 ? -2.560  47.746  15.629  1.00 33.09  ? 101 ASP D O   1 
ATOM   2970  C  CB  . ASP C  1 101 ? -4.951  49.665  16.247  1.00 32.11  ? 101 ASP D CB  1 
ATOM   2971  C  CG  . ASP C  1 101 ? -4.650  50.581  17.431  1.00 31.96  ? 101 ASP D CG  1 
ATOM   2972  O  OD1 . ASP C  1 101 ? -4.876  51.808  17.303  1.00 32.61  ? 101 ASP D OD1 1 
ATOM   2973  O  OD2 . ASP C  1 101 ? -4.169  50.088  18.481  1.00 31.36  ? 101 ASP D OD2 1 
ATOM   2974  N  N   . SER C  1 102 ? -1.604  49.768  16.059  1.00 34.38  ? 102 SER D N   1 
ATOM   2975  C  CA  . SER C  1 102 ? -0.314  49.239  16.528  1.00 34.96  ? 102 SER D CA  1 
ATOM   2976  C  C   . SER C  1 102 ? -0.119  49.331  18.049  1.00 34.14  ? 102 SER D C   1 
ATOM   2977  O  O   . SER C  1 102 ? 0.977   49.055  18.547  1.00 34.97  ? 102 SER D O   1 
ATOM   2978  C  CB  . SER C  1 102 ? 0.820   49.984  15.828  1.00 37.02  ? 102 SER D CB  1 
ATOM   2979  O  OG  . SER C  1 102 ? 0.758   49.763  14.433  1.00 38.08  ? 102 SER D OG  1 
ATOM   2980  N  N   . VAL C  1 103 ? -1.156  49.734  18.780  1.00 32.75  ? 103 VAL D N   1 
ATOM   2981  C  CA  . VAL C  1 103 ? -1.096  49.815  20.238  1.00 32.12  ? 103 VAL D CA  1 
ATOM   2982  C  C   . VAL C  1 103 ? -1.709  48.572  20.865  1.00 30.77  ? 103 VAL D C   1 
ATOM   2983  O  O   . VAL C  1 103 ? -1.123  47.999  21.792  1.00 30.85  ? 103 VAL D O   1 
ATOM   2984  C  CB  . VAL C  1 103 ? -1.770  51.089  20.769  1.00 31.93  ? 103 VAL D CB  1 
ATOM   2985  C  CG1 . VAL C  1 103 ? -1.784  51.091  22.296  1.00 31.53  ? 103 VAL D CG1 1 
ATOM   2986  C  CG2 . VAL C  1 103 ? -1.041  52.318  20.234  1.00 33.46  ? 103 VAL D CG2 1 
ATOM   2987  N  N   . ILE C  1 104 ? -2.889  48.175  20.386  1.00 29.70  ? 104 ILE D N   1 
ATOM   2988  C  CA  . ILE C  1 104 ? -3.460  46.871  20.754  1.00 28.72  ? 104 ILE D CA  1 
ATOM   2989  C  C   . ILE C  1 104 ? -2.599  45.726  20.209  1.00 29.21  ? 104 ILE D C   1 
ATOM   2990  O  O   . ILE C  1 104 ? -1.817  45.904  19.273  1.00 30.14  ? 104 ILE D O   1 
ATOM   2991  C  CB  . ILE C  1 104 ? -4.927  46.673  20.288  1.00 27.87  ? 104 ILE D CB  1 
ATOM   2992  C  CG1 . ILE C  1 104 ? -5.089  46.811  18.773  1.00 28.45  ? 104 ILE D CG1 1 
ATOM   2993  C  CG2 . ILE C  1 104 ? -5.849  47.652  21.002  1.00 27.45  ? 104 ILE D CG2 1 
ATOM   2994  C  CD1 . ILE C  1 104 ? -6.381  46.217  18.244  1.00 27.97  ? 104 ILE D CD1 1 
ATOM   2995  N  N   . SER C  1 105 ? -2.765  44.558  20.814  1.00 28.69  ? 105 SER D N   1 
ATOM   2996  C  CA  . SER C  1 105 ? -2.109  43.347  20.366  1.00 29.27  ? 105 SER D CA  1 
ATOM   2997  C  C   . SER C  1 105 ? -3.011  42.151  20.646  1.00 28.51  ? 105 SER D C   1 
ATOM   2998  O  O   . SER C  1 105 ? -3.968  42.246  21.411  1.00 27.68  ? 105 SER D O   1 
ATOM   2999  C  CB  . SER C  1 105 ? -0.742  43.197  21.059  1.00 30.27  ? 105 SER D CB  1 
ATOM   3000  O  OG  . SER C  1 105 ? 0.048   42.192  20.451  1.00 31.16  ? 105 SER D OG  1 
ATOM   3001  N  N   . LEU C  1 106 ? -2.722  41.039  19.980  1.00 29.04  ? 106 LEU D N   1 
ATOM   3002  C  CA  . LEU C  1 106 ? -3.396  39.776  20.240  1.00 28.67  ? 106 LEU D CA  1 
ATOM   3003  C  C   . LEU C  1 106 ? -2.464  38.823  20.997  1.00 29.39  ? 106 LEU D C   1 
ATOM   3004  O  O   . LEU C  1 106 ? -2.744  37.627  21.091  1.00 29.54  ? 106 LEU D O   1 
ATOM   3005  C  CB  . LEU C  1 106 ? -3.876  39.155  18.928  1.00 28.91  ? 106 LEU D CB  1 
ATOM   3006  C  CG  . LEU C  1 106 ? -4.840  39.989  18.077  1.00 28.54  ? 106 LEU D CG  1 
ATOM   3007  C  CD1 . LEU C  1 106 ? -5.248  39.202  16.839  1.00 29.12  ? 106 LEU D CD1 1 
ATOM   3008  C  CD2 . LEU C  1 106 ? -6.076  40.416  18.857  1.00 27.51  ? 106 LEU D CD2 1 
ATOM   3009  N  N   . SER C  1 107 ? -1.363  39.358  21.527  1.00 30.13  ? 107 SER D N   1 
ATOM   3010  C  CA  . SER C  1 107 ? -0.493  38.635  22.462  1.00 31.02  ? 107 SER D CA  1 
ATOM   3011  C  C   . SER C  1 107 ? 0.286   39.625  23.340  1.00 31.53  ? 107 SER D C   1 
ATOM   3012  O  O   . SER C  1 107 ? 0.341   40.821  23.044  1.00 31.30  ? 107 SER D O   1 
ATOM   3013  C  CB  . SER C  1 107 ? 0.456   37.687  21.713  1.00 32.35  ? 107 SER D CB  1 
ATOM   3014  O  OG  . SER C  1 107 ? 1.240   38.362  20.739  1.00 33.23  ? 107 SER D OG  1 
ATOM   3015  N  N   . GLY C  1 108 ? 0.844   39.116  24.436  1.00 32.38  ? 108 GLY D N   1 
ATOM   3016  C  CA  . GLY C  1 108 ? 1.646   39.909  25.374  1.00 33.31  ? 108 GLY D CA  1 
ATOM   3017  C  C   . GLY C  1 108 ? 0.853   40.912  26.204  1.00 32.48  ? 108 GLY D C   1 
ATOM   3018  O  O   . GLY C  1 108 ? -0.356  40.746  26.420  1.00 31.22  ? 108 GLY D O   1 
ATOM   3019  N  N   . ASP C  1 109 ? 1.525   41.970  26.649  1.00 33.34  ? 109 ASP D N   1 
ATOM   3020  C  CA  . ASP C  1 109 ? 0.946   42.889  27.639  1.00 33.09  ? 109 ASP D CA  1 
ATOM   3021  C  C   . ASP C  1 109 ? -0.267  43.694  27.178  1.00 31.53  ? 109 ASP D C   1 
ATOM   3022  O  O   . ASP C  1 109 ? -1.101  44.018  28.001  1.00 31.01  ? 109 ASP D O   1 
ATOM   3023  C  CB  . ASP C  1 109 ? 1.993   43.853  28.198  1.00 34.69  ? 109 ASP D CB  1 
ATOM   3024  C  CG  . ASP C  1 109 ? 2.926   43.174  29.190  1.00 36.54  ? 109 ASP D CG  1 
ATOM   3025  O  OD1 . ASP C  1 109 ? 2.408   42.580  30.183  1.00 36.66  ? 109 ASP D OD1 1 
ATOM   3026  O  OD2 . ASP C  1 109 ? 4.148   43.221  28.963  1.00 38.07  ? 109 ASP D OD2 1 
ATOM   3027  N  N   . HIS C  1 110 ? -0.332  44.036  25.894  1.00 31.12  ? 110 HIS D N   1 
ATOM   3028  C  CA  . HIS C  1 110 ? -1.455  44.794  25.336  1.00 30.01  ? 110 HIS D CA  1 
ATOM   3029  C  C   . HIS C  1 110 ? -2.479  43.880  24.654  1.00 28.91  ? 110 HIS D C   1 
ATOM   3030  O  O   . HIS C  1 110 ? -3.265  44.349  23.827  1.00 28.37  ? 110 HIS D O   1 
ATOM   3031  C  CB  . HIS C  1 110 ? -0.931  45.870  24.376  1.00 30.60  ? 110 HIS D CB  1 
ATOM   3032  C  CG  . HIS C  1 110 ? -0.210  46.985  25.065  1.00 31.61  ? 110 HIS D CG  1 
ATOM   3033  N  ND1 . HIS C  1 110 ? 0.236   48.107  24.400  1.00 32.37  ? 110 HIS D ND1 1 
ATOM   3034  C  CD2 . HIS C  1 110 ? 0.123   47.163  26.366  1.00 32.19  ? 110 HIS D CD2 1 
ATOM   3035  C  CE1 . HIS C  1 110 ? 0.839   48.913  25.254  1.00 33.36  ? 110 HIS D CE1 1 
ATOM   3036  N  NE2 . HIS C  1 110 ? 0.777   48.368  26.457  1.00 33.27  ? 110 HIS D NE2 1 
ATOM   3037  N  N   . CYS C  1 111 ? -2.476  42.592  25.017  1.00 28.77  ? 111 CYS D N   1 
ATOM   3038  C  CA  . CYS C  1 111 ? -3.388  41.617  24.448  1.00 28.00  ? 111 CYS D CA  1 
ATOM   3039  C  C   . CYS C  1 111 ? -4.814  41.977  24.849  1.00 26.88  ? 111 CYS D C   1 
ATOM   3040  O  O   . CYS C  1 111 ? -5.079  42.256  26.020  1.00 26.81  ? 111 CYS D O   1 
ATOM   3041  C  CB  . CYS C  1 111 ? -3.075  40.208  24.927  1.00 28.53  ? 111 CYS D CB  1 
ATOM   3042  S  SG  . CYS C  1 111 ? -4.053  38.937  24.102  1.00 28.27  ? 111 CYS D SG  1 
ATOM   3043  N  N   . ILE C  1 112 ? -5.709  41.970  23.871  1.00 26.17  ? 112 ILE D N   1 
ATOM   3044  C  CA  . ILE C  1 112 ? -7.124  42.292  24.097  1.00 25.39  ? 112 ILE D CA  1 
ATOM   3045  C  C   . ILE C  1 112 ? -8.037  41.068  24.112  1.00 25.10  ? 112 ILE D C   1 
ATOM   3046  O  O   . ILE C  1 112 ? -9.230  41.203  24.380  1.00 24.77  ? 112 ILE D O   1 
ATOM   3047  C  CB  . ILE C  1 112 ? -7.653  43.324  23.077  1.00 25.23  ? 112 ILE D CB  1 
ATOM   3048  C  CG1 . ILE C  1 112 ? -7.562  42.805  21.636  1.00 25.47  ? 112 ILE D CG1 1 
ATOM   3049  C  CG2 . ILE C  1 112 ? -6.890  44.637  23.234  1.00 25.59  ? 112 ILE D CG2 1 
ATOM   3050  C  CD1 . ILE C  1 112 ? -8.194  43.726  20.614  1.00 25.60  ? 112 ILE D CD1 1 
ATOM   3051  N  N   . ILE C  1 113 ? -7.493  39.886  23.820  1.00 25.33  ? 113 ILE D N   1 
ATOM   3052  C  CA  . ILE C  1 113 ? -8.259  38.645  23.877  1.00 25.31  ? 113 ILE D CA  1 
ATOM   3053  C  C   . ILE C  1 113 ? -8.721  38.436  25.325  1.00 25.26  ? 113 ILE D C   1 
ATOM   3054  O  O   . ILE C  1 113 ? -7.964  38.667  26.269  1.00 25.41  ? 113 ILE D O   1 
ATOM   3055  C  CB  . ILE C  1 113 ? -7.441  37.441  23.341  1.00 25.99  ? 113 ILE D CB  1 
ATOM   3056  C  CG1 . ILE C  1 113 ? -7.264  37.574  21.814  1.00 26.17  ? 113 ILE D CG1 1 
ATOM   3057  C  CG2 . ILE C  1 113 ? -8.104  36.114  23.690  1.00 26.29  ? 113 ILE D CG2 1 
ATOM   3058  C  CD1 . ILE C  1 113 ? -6.177  36.696  21.221  1.00 27.01  ? 113 ILE D CD1 1 
ATOM   3059  N  N   . GLY C  1 114 ? -9.989  38.054  25.486  1.00 25.08  ? 114 GLY D N   1 
ATOM   3060  C  CA  . GLY C  1 114 ? -10.589 37.894  26.802  1.00 25.30  ? 114 GLY D CA  1 
ATOM   3061  C  C   . GLY C  1 114 ? -11.082 39.177  27.450  1.00 25.02  ? 114 GLY D C   1 
ATOM   3062  O  O   . GLY C  1 114 ? -11.521 39.156  28.586  1.00 25.38  ? 114 GLY D O   1 
ATOM   3063  N  N   . ARG C  1 115 ? -10.983 40.295  26.751  1.00 24.60  ? 115 ARG D N   1 
ATOM   3064  C  CA  . ARG C  1 115 ? -11.540 41.550  27.207  1.00 24.58  ? 115 ARG D CA  1 
ATOM   3065  C  C   . ARG C  1 115 ? -12.814 41.797  26.378  1.00 24.53  ? 115 ARG D C   1 
ATOM   3066  O  O   . ARG C  1 115 ? -13.235 40.918  25.626  1.00 24.61  ? 115 ARG D O   1 
ATOM   3067  C  CB  . ARG C  1 115 ? -10.485 42.651  27.076  1.00 24.50  ? 115 ARG D CB  1 
ATOM   3068  C  CG  . ARG C  1 115 ? -9.188  42.272  27.795  1.00 24.88  ? 115 ARG D CG  1 
ATOM   3069  C  CD  . ARG C  1 115 ? -8.235  43.448  27.966  1.00 25.14  ? 115 ARG D CD  1 
ATOM   3070  N  NE  . ARG C  1 115 ? -6.974  43.006  28.554  1.00 25.76  ? 115 ARG D NE  1 
ATOM   3071  C  CZ  . ARG C  1 115 ? -6.707  42.873  29.852  1.00 26.43  ? 115 ARG D CZ  1 
ATOM   3072  N  NH1 . ARG C  1 115 ? -7.598  43.177  30.794  1.00 26.56  ? 115 ARG D NH1 1 
ATOM   3073  N  NH2 . ARG C  1 115 ? -5.496  42.455  30.218  1.00 27.23  ? 115 ARG D NH2 1 
ATOM   3074  N  N   . THR C  1 116 ? -13.431 42.962  26.529  1.00 24.61  ? 116 THR D N   1 
ATOM   3075  C  CA  . THR C  1 116 ? -14.723 43.240  25.901  1.00 24.91  ? 116 THR D CA  1 
ATOM   3076  C  C   . THR C  1 116 ? -14.615 44.397  24.919  1.00 24.85  ? 116 THR D C   1 
ATOM   3077  O  O   . THR C  1 116 ? -14.073 45.436  25.260  1.00 24.80  ? 116 THR D O   1 
ATOM   3078  C  CB  . THR C  1 116 ? -15.784 43.586  26.967  1.00 25.45  ? 116 THR D CB  1 
ATOM   3079  O  OG1 . THR C  1 116 ? -16.002 42.448  27.810  1.00 25.76  ? 116 THR D OG1 1 
ATOM   3080  C  CG2 . THR C  1 116 ? -17.120 43.988  26.322  1.00 26.02  ? 116 THR D CG2 1 
ATOM   3081  N  N   . LEU C  1 117 ? -15.142 44.207  23.714  1.00 25.08  ? 117 LEU D N   1 
ATOM   3082  C  CA  . LEU C  1 117 ? -15.288 45.286  22.748  1.00 25.44  ? 117 LEU D CA  1 
ATOM   3083  C  C   . LEU C  1 117 ? -16.667 45.905  22.942  1.00 26.16  ? 117 LEU D C   1 
ATOM   3084  O  O   . LEU C  1 117 ? -17.640 45.183  23.085  1.00 26.52  ? 117 LEU D O   1 
ATOM   3085  C  CB  . LEU C  1 117 ? -15.159 44.745  21.333  1.00 25.68  ? 117 LEU D CB  1 
ATOM   3086  C  CG  . LEU C  1 117 ? -15.229 45.725  20.161  1.00 26.30  ? 117 LEU D CG  1 
ATOM   3087  C  CD1 . LEU C  1 117 ? -14.065 46.703  20.170  1.00 26.14  ? 117 LEU D CD1 1 
ATOM   3088  C  CD2 . LEU C  1 117 ? -15.233 44.925  18.876  1.00 26.77  ? 117 LEU D CD2 1 
ATOM   3089  N  N   . VAL C  1 118 ? -16.743 47.233  22.947  1.00 26.54  ? 118 VAL D N   1 
ATOM   3090  C  CA  . VAL C  1 118 ? -17.998 47.941  23.168  1.00 27.52  ? 118 VAL D CA  1 
ATOM   3091  C  C   . VAL C  1 118 ? -18.214 48.969  22.065  1.00 28.35  ? 118 VAL D C   1 
ATOM   3092  O  O   . VAL C  1 118 ? -17.299 49.704  21.719  1.00 28.18  ? 118 VAL D O   1 
ATOM   3093  C  CB  . VAL C  1 118 ? -18.027 48.640  24.544  1.00 27.56  ? 118 VAL D CB  1 
ATOM   3094  C  CG1 . VAL C  1 118 ? -19.352 49.361  24.762  1.00 28.72  ? 118 VAL D CG1 1 
ATOM   3095  C  CG2 . VAL C  1 118 ? -17.791 47.637  25.664  1.00 27.12  ? 118 VAL D CG2 1 
ATOM   3096  N  N   . VAL C  1 119 ? -19.429 49.015  21.527  1.00 29.55  ? 119 VAL D N   1 
ATOM   3097  C  CA  . VAL C  1 119 ? -19.843 50.087  20.612  1.00 30.78  ? 119 VAL D CA  1 
ATOM   3098  C  C   . VAL C  1 119 ? -20.880 50.942  21.331  1.00 31.94  ? 119 VAL D C   1 
ATOM   3099  O  O   . VAL C  1 119 ? -21.769 50.419  22.014  1.00 32.27  ? 119 VAL D O   1 
ATOM   3100  C  CB  . VAL C  1 119 ? -20.354 49.569  19.240  1.00 31.61  ? 119 VAL D CB  1 
ATOM   3101  C  CG1 . VAL C  1 119 ? -21.584 48.672  19.371  1.00 32.34  ? 119 VAL D CG1 1 
ATOM   3102  C  CG2 . VAL C  1 119 ? -20.641 50.735  18.303  1.00 32.92  ? 119 VAL D CG2 1 
ATOM   3103  N  N   . HIS C  1 120 ? -20.758 52.257  21.160  1.00 32.80  ? 120 HIS D N   1 
ATOM   3104  C  CA  . HIS C  1 120 ? -21.427 53.238  22.021  1.00 33.84  ? 120 HIS D CA  1 
ATOM   3105  C  C   . HIS C  1 120 ? -22.517 54.030  21.322  1.00 35.80  ? 120 HIS D C   1 
ATOM   3106  O  O   . HIS C  1 120 ? -22.577 54.099  20.097  1.00 36.41  ? 120 HIS D O   1 
ATOM   3107  C  CB  . HIS C  1 120 ? -20.390 54.213  22.601  1.00 33.39  ? 120 HIS D CB  1 
ATOM   3108  C  CG  . HIS C  1 120 ? -19.649 53.673  23.781  1.00 32.19  ? 120 HIS D CG  1 
ATOM   3109  N  ND1 . HIS C  1 120 ? -20.041 53.922  25.077  1.00 32.55  ? 120 HIS D ND1 1 
ATOM   3110  C  CD2 . HIS C  1 120 ? -18.547 52.890  23.862  1.00 30.93  ? 120 HIS D CD2 1 
ATOM   3111  C  CE1 . HIS C  1 120 ? -19.215 53.312  25.908  1.00 31.53  ? 120 HIS D CE1 1 
ATOM   3112  N  NE2 . HIS C  1 120 ? -18.298 52.680  25.198  1.00 30.52  ? 120 HIS D NE2 1 
ATOM   3113  N  N   . GLU C  1 121 ? -23.353 54.645  22.155  1.00 37.04  ? 121 GLU D N   1 
ATOM   3114  C  CA  . GLU C  1 121 ? -24.506 55.458  21.743  1.00 39.26  ? 121 GLU D CA  1 
ATOM   3115  C  C   . GLU C  1 121 ? -24.168 56.627  20.823  1.00 40.21  ? 121 GLU D C   1 
ATOM   3116  O  O   . GLU C  1 121 ? -24.922 56.927  19.899  1.00 41.85  ? 121 GLU D O   1 
ATOM   3117  C  CB  . GLU C  1 121 ? -25.195 56.006  22.998  1.00 40.25  ? 121 GLU D CB  1 
ATOM   3118  C  CG  . GLU C  1 121 ? -26.448 56.839  22.772  1.00 42.74  ? 121 GLU D CG  1 
ATOM   3119  C  CD  . GLU C  1 121 ? -26.967 57.467  24.051  1.00 43.78  ? 121 GLU D CD  1 
ATOM   3120  O  OE1 . GLU C  1 121 ? -26.290 57.364  25.099  1.00 42.66  ? 121 GLU D OE1 1 
ATOM   3121  O  OE2 . GLU C  1 121 ? -28.058 58.076  24.011  1.00 46.04  ? 121 GLU D OE2 1 
ATOM   3122  N  N   . LYS C  1 122 ? -23.073 57.319  21.108  1.00 39.49  ? 122 LYS D N   1 
ATOM   3123  C  CA  . LYS C  1 122 ? -22.729 58.524  20.353  1.00 40.62  ? 122 LYS D CA  1 
ATOM   3124  C  C   . LYS C  1 122 ? -21.219 58.650  20.199  1.00 39.21  ? 122 LYS D C   1 
ATOM   3125  O  O   . LYS C  1 122 ? -20.482 57.729  20.550  1.00 37.44  ? 122 LYS D O   1 
ATOM   3126  C  CB  . LYS C  1 122 ? -23.381 59.753  21.007  1.00 42.41  ? 122 LYS D CB  1 
ATOM   3127  C  CG  . LYS C  1 122 ? -23.119 59.905  22.494  1.00 41.81  ? 122 LYS D CG  1 
ATOM   3128  C  CD  . LYS C  1 122 ? -23.769 61.171  23.023  1.00 43.81  ? 122 LYS D CD  1 
ATOM   3129  C  CE  . LYS C  1 122 ? -23.572 61.304  24.524  1.00 43.48  ? 122 LYS D CE  1 
ATOM   3130  N  NZ  . LYS C  1 122 ? -23.855 62.690  24.995  1.00 45.37  ? 122 LYS D NZ  1 
ATOM   3131  N  N   . ALA C  1 123 ? -20.780 59.767  19.622  1.00 40.15  ? 123 ALA D N   1 
ATOM   3132  C  CA  . ALA C  1 123 ? -19.381 59.991  19.294  1.00 39.33  ? 123 ALA D CA  1 
ATOM   3133  C  C   . ALA C  1 123 ? -18.466 60.052  20.515  1.00 38.00  ? 123 ALA D C   1 
ATOM   3134  O  O   . ALA C  1 123 ? -18.784 60.673  21.525  1.00 38.39  ? 123 ALA D O   1 
ATOM   3135  C  CB  . ALA C  1 123 ? -19.235 61.277  18.489  1.00 41.14  ? 123 ALA D CB  1 
ATOM   3136  N  N   . ASP C  1 124 ? -17.333 59.373  20.390  1.00 36.57  ? 124 ASP D N   1 
ATOM   3137  C  CA  . ASP C  1 124 ? -16.169 59.567  21.246  1.00 35.71  ? 124 ASP D CA  1 
ATOM   3138  C  C   . ASP C  1 124 ? -15.568 60.948  20.916  1.00 37.01  ? 124 ASP D C   1 
ATOM   3139  O  O   . ASP C  1 124 ? -15.159 61.182  19.784  1.00 37.62  ? 124 ASP D O   1 
ATOM   3140  C  CB  . ASP C  1 124 ? -15.174 58.439  20.947  1.00 34.29  ? 124 ASP D CB  1 
ATOM   3141  C  CG  . ASP C  1 124 ? -13.999 58.384  21.910  1.00 33.53  ? 124 ASP D CG  1 
ATOM   3142  O  OD1 . ASP C  1 124 ? -13.661 59.398  22.549  1.00 34.21  ? 124 ASP D OD1 1 
ATOM   3143  O  OD2 . ASP C  1 124 ? -13.390 57.297  21.997  1.00 32.42  ? 124 ASP D OD2 1 
ATOM   3144  N  N   . ASP C  1 125 ? -15.509 61.852  21.900  1.00 37.57  ? 125 ASP D N   1 
ATOM   3145  C  CA  . ASP C  1 125 ? -14.885 63.186  21.696  1.00 39.01  ? 125 ASP D CA  1 
ATOM   3146  C  C   . ASP C  1 125 ? -13.337 63.167  21.664  1.00 38.56  ? 125 ASP D C   1 
ATOM   3147  O  O   . ASP C  1 125 ? -12.707 64.228  21.646  1.00 39.79  ? 125 ASP D O   1 
ATOM   3148  C  CB  . ASP C  1 125 ? -15.425 64.245  22.696  1.00 40.19  ? 125 ASP D CB  1 
ATOM   3149  C  CG  . ASP C  1 125 ? -15.037 63.979  24.170  1.00 39.38  ? 125 ASP D CG  1 
ATOM   3150  O  OD1 . ASP C  1 125 ? -14.079 63.236  24.464  1.00 38.08  ? 125 ASP D OD1 1 
ATOM   3151  O  OD2 . ASP C  1 125 ? -15.703 64.557  25.063  1.00 40.31  ? 125 ASP D OD2 1 
ATOM   3152  N  N   . LEU C  1 126 ? -12.745 61.969  21.708  1.00 36.98  ? 126 LEU D N   1 
ATOM   3153  C  CA  . LEU C  1 126 ? -11.299 61.754  21.560  1.00 36.70  ? 126 LEU D CA  1 
ATOM   3154  C  C   . LEU C  1 126 ? -10.471 62.457  22.638  1.00 37.18  ? 126 LEU D C   1 
ATOM   3155  O  O   . LEU C  1 126 ? -9.325  62.817  22.402  1.00 37.84  ? 126 LEU D O   1 
ATOM   3156  C  CB  . LEU C  1 126 ? -10.830 62.154  20.150  1.00 37.78  ? 126 LEU D CB  1 
ATOM   3157  C  CG  . LEU C  1 126 ? -11.677 61.601  18.996  1.00 37.77  ? 126 LEU D CG  1 
ATOM   3158  C  CD1 . LEU C  1 126 ? -11.052 61.972  17.658  1.00 39.06  ? 126 LEU D CD1 1 
ATOM   3159  C  CD2 . LEU C  1 126 ? -11.858 60.090  19.098  1.00 35.98  ? 126 LEU D CD2 1 
ATOM   3160  N  N   . GLY C  1 127 ? -11.053 62.630  23.823  1.00 37.06  ? 127 GLY D N   1 
ATOM   3161  C  CA  . GLY C  1 127 ? -10.379 63.324  24.913  1.00 37.82  ? 127 GLY D CA  1 
ATOM   3162  C  C   . GLY C  1 127 ? -10.289 64.837  24.782  1.00 39.81  ? 127 GLY D C   1 
ATOM   3163  O  O   . GLY C  1 127 ? -9.580  65.468  25.564  1.00 40.75  ? 127 GLY D O   1 
ATOM   3164  N  N   . LYS C  1 128 ? -11.026 65.426  23.835  1.00 40.71  ? 128 LYS D N   1 
ATOM   3165  C  CA  . LYS C  1 128 ? -10.976 66.876  23.565  1.00 42.83  ? 128 LYS D CA  1 
ATOM   3166  C  C   . LYS C  1 128 ? -12.248 67.613  23.999  1.00 43.73  ? 128 LYS D C   1 
ATOM   3167  O  O   . LYS C  1 128 ? -12.487 68.741  23.567  1.00 45.55  ? 128 LYS D O   1 
ATOM   3168  C  CB  . LYS C  1 128 ? -10.710 67.120  22.070  1.00 43.73  ? 128 LYS D CB  1 
ATOM   3169  C  CG  . LYS C  1 128 ? -9.372  66.572  21.599  1.00 43.35  ? 128 LYS D CG  1 
ATOM   3170  C  CD  . LYS C  1 128 ? -8.947  67.153  20.253  1.00 44.97  ? 128 LYS D CD  1 
ATOM   3171  C  CE  . LYS C  1 128 ? -7.437  67.064  20.049  1.00 45.41  ? 128 LYS D CE  1 
ATOM   3172  N  NZ  . LYS C  1 128 ? -6.944  65.657  20.096  1.00 43.57  ? 128 LYS D NZ  1 
ATOM   3173  N  N   . GLY C  1 129 ? -13.040 66.989  24.872  1.00 42.63  ? 129 GLY D N   1 
ATOM   3174  C  CA  . GLY C  1 129 ? -14.319 67.543  25.311  1.00 43.57  ? 129 GLY D CA  1 
ATOM   3175  C  C   . GLY C  1 129 ? -14.232 68.635  26.361  1.00 45.05  ? 129 GLY D C   1 
ATOM   3176  O  O   . GLY C  1 129 ? -15.234 69.286  26.648  1.00 46.31  ? 129 GLY D O   1 
ATOM   3177  N  N   . GLY C  1 130 ? -13.053 68.819  26.958  1.00 45.02  ? 130 GLY D N   1 
ATOM   3178  C  CA  . GLY C  1 130 ? -12.843 69.864  27.959  1.00 46.67  ? 130 GLY D CA  1 
ATOM   3179  C  C   . GLY C  1 130 ? -13.584 69.622  29.266  1.00 46.54  ? 130 GLY D C   1 
ATOM   3180  O  O   . GLY C  1 130 ? -14.024 70.569  29.903  1.00 48.31  ? 130 GLY D O   1 
ATOM   3181  N  N   . ASN C  1 131 ? -13.740 68.357  29.653  1.00 44.62  ? 131 ASN D N   1 
ATOM   3182  C  CA  . ASN C  1 131 ? -14.316 68.008  30.951  1.00 44.60  ? 131 ASN D CA  1 
ATOM   3183  C  C   . ASN C  1 131 ? -13.688 66.727  31.510  1.00 42.84  ? 131 ASN D C   1 
ATOM   3184  O  O   . ASN C  1 131 ? -12.912 66.046  30.826  1.00 41.45  ? 131 ASN D O   1 
ATOM   3185  C  CB  . ASN C  1 131 ? -15.864 67.941  30.878  1.00 44.95  ? 131 ASN D CB  1 
ATOM   3186  C  CG  . ASN C  1 131 ? -16.381 66.931  29.861  1.00 43.37  ? 131 ASN D CG  1 
ATOM   3187  O  OD1 . ASN C  1 131 ? -15.975 65.774  29.848  1.00 41.57  ? 131 ASN D OD1 1 
ATOM   3188  N  ND2 . ASN C  1 131 ? -17.316 67.367  29.022  1.00 44.26  ? 131 ASN D ND2 1 
ATOM   3189  N  N   . GLU C  1 132 ? -14.050 66.405  32.747  1.00 43.08  ? 132 GLU D N   1 
ATOM   3190  C  CA  . GLU C  1 132 ? -13.457 65.298  33.496  1.00 41.97  ? 132 GLU D CA  1 
ATOM   3191  C  C   . GLU C  1 132 ? -13.709 63.944  32.814  1.00 39.96  ? 132 GLU D C   1 
ATOM   3192  O  O   . GLU C  1 132 ? -12.773 63.150  32.636  1.00 38.72  ? 132 GLU D O   1 
ATOM   3193  C  CB  . GLU C  1 132 ? -13.980 65.285  34.942  1.00 43.03  ? 132 GLU D CB  1 
ATOM   3194  C  CG  . GLU C  1 132 ? -13.651 66.543  35.762  1.00 45.25  ? 132 GLU D CG  1 
ATOM   3195  C  CD  . GLU C  1 132 ? -14.696 67.671  35.673  1.00 46.97  ? 132 GLU D CD  1 
ATOM   3196  O  OE1 . GLU C  1 132 ? -15.477 67.712  34.690  1.00 46.51  ? 132 GLU D OE1 1 
ATOM   3197  O  OE2 . GLU C  1 132 ? -14.725 68.533  36.586  1.00 48.93  ? 132 GLU D OE2 1 
ATOM   3198  N  N   . GLU C  1 133 ? -14.957 63.700  32.403  1.00 39.79  ? 133 GLU D N   1 
ATOM   3199  C  CA  . GLU C  1 133 ? -15.307 62.450  31.716  1.00 38.18  ? 133 GLU D CA  1 
ATOM   3200  C  C   . GLU C  1 133 ? -14.665 62.287  30.328  1.00 37.25  ? 133 GLU D C   1 
ATOM   3201  O  O   . GLU C  1 133 ? -14.461 61.153  29.881  1.00 35.77  ? 133 GLU D O   1 
ATOM   3202  C  CB  . GLU C  1 133 ? -16.832 62.270  31.594  1.00 38.60  ? 133 GLU D CB  1 
ATOM   3203  C  CG  . GLU C  1 133 ? -17.542 61.906  32.892  1.00 39.26  ? 133 GLU D CG  1 
ATOM   3204  C  CD  . GLU C  1 133 ? -17.106 60.575  33.484  1.00 38.03  ? 133 GLU D CD  1 
ATOM   3205  O  OE1 . GLU C  1 133 ? -16.735 59.655  32.731  1.00 36.58  ? 133 GLU D OE1 1 
ATOM   3206  O  OE2 . GLU C  1 133 ? -17.140 60.443  34.725  1.00 38.82  ? 133 GLU D OE2 1 
ATOM   3207  N  N   . SER C  1 134 ? -14.351 63.393  29.650  1.00 38.26  ? 134 SER D N   1 
ATOM   3208  C  CA  . SER C  1 134 ? -13.690 63.313  28.340  1.00 37.74  ? 134 SER D CA  1 
ATOM   3209  C  C   . SER C  1 134 ? -12.323 62.625  28.432  1.00 36.79  ? 134 SER D C   1 
ATOM   3210  O  O   . SER C  1 134 ? -11.955 61.850  27.547  1.00 35.67  ? 134 SER D O   1 
ATOM   3211  C  CB  . SER C  1 134 ? -13.522 64.699  27.714  1.00 39.35  ? 134 SER D CB  1 
ATOM   3212  O  OG  . SER C  1 134 ? -12.893 64.583  26.452  1.00 38.99  ? 134 SER D OG  1 
ATOM   3213  N  N   . THR C  1 135 ? -11.602 62.894  29.522  1.00 37.42  ? 135 THR D N   1 
ATOM   3214  C  CA  . THR C  1 135 ? -10.297 62.269  29.774  1.00 36.93  ? 135 THR D CA  1 
ATOM   3215  C  C   . THR C  1 135 ? -10.373 60.808  30.258  1.00 35.48  ? 135 THR D C   1 
ATOM   3216  O  O   . THR C  1 135 ? -9.327  60.174  30.402  1.00 35.03  ? 135 THR D O   1 
ATOM   3217  C  CB  . THR C  1 135 ? -9.465  63.085  30.794  1.00 38.41  ? 135 THR D CB  1 
ATOM   3218  O  OG1 . THR C  1 135 ? -10.071 63.006  32.091  1.00 38.81  ? 135 THR D OG1 1 
ATOM   3219  C  CG2 . THR C  1 135 ? -9.368  64.548  30.380  1.00 40.11  ? 135 THR D CG2 1 
ATOM   3220  N  N   . LYS C  1 136 ? -11.582 60.293  30.514  1.00 34.96  ? 136 LYS D N   1 
ATOM   3221  C  CA  . LYS C  1 136 ? -11.801 58.911  30.964  1.00 33.86  ? 136 LYS D CA  1 
ATOM   3222  C  C   . LYS C  1 136 ? -12.554 58.048  29.945  1.00 32.72  ? 136 LYS D C   1 
ATOM   3223  O  O   . LYS C  1 136 ? -12.103 56.946  29.604  1.00 31.71  ? 136 LYS D O   1 
ATOM   3224  C  CB  . LYS C  1 136 ? -12.574 58.917  32.284  1.00 34.60  ? 136 LYS D CB  1 
ATOM   3225  C  CG  . LYS C  1 136 ? -11.784 59.502  33.439  1.00 35.84  ? 136 LYS D CG  1 
ATOM   3226  C  CD  . LYS C  1 136 ? -12.606 59.514  34.716  1.00 36.80  ? 136 LYS D CD  1 
ATOM   3227  C  CE  . LYS C  1 136 ? -11.907 60.313  35.801  1.00 38.41  ? 136 LYS D CE  1 
ATOM   3228  N  NZ  . LYS C  1 136 ? -10.580 59.735  36.148  1.00 38.25  ? 136 LYS D NZ  1 
ATOM   3229  N  N   . THR C  1 137 ? -13.706 58.530  29.479  1.00 33.16  ? 137 THR D N   1 
ATOM   3230  C  CA  . THR C  1 137 ? -14.546 57.764  28.537  1.00 32.44  ? 137 THR D CA  1 
ATOM   3231  C  C   . THR C  1 137 ? -14.679 58.366  27.136  1.00 32.77  ? 137 THR D C   1 
ATOM   3232  O  O   . THR C  1 137 ? -15.075 57.667  26.214  1.00 32.25  ? 137 THR D O   1 
ATOM   3233  C  CB  . THR C  1 137 ? -15.979 57.597  29.076  1.00 32.92  ? 137 THR D CB  1 
ATOM   3234  O  OG1 . THR C  1 137 ? -16.612 58.874  29.131  1.00 34.35  ? 137 THR D OG1 1 
ATOM   3235  C  CG2 . THR C  1 137 ? -15.966 56.972  30.458  1.00 32.88  ? 137 THR D CG2 1 
ATOM   3236  N  N   . GLY C  1 138 ? -14.386 59.651  26.976  1.00 33.87  ? 138 GLY D N   1 
ATOM   3237  C  CA  . GLY C  1 138 ? -14.720 60.355  25.740  1.00 34.67  ? 138 GLY D CA  1 
ATOM   3238  C  C   . GLY C  1 138 ? -16.191 60.761  25.570  1.00 35.66  ? 138 GLY D C   1 
ATOM   3239  O  O   . GLY C  1 138 ? -16.583 61.196  24.487  1.00 36.38  ? 138 GLY D O   1 
ATOM   3240  N  N   . ASN C  1 139 ? -17.004 60.627  26.626  1.00 35.93  ? 139 ASN D N   1 
ATOM   3241  C  CA  . ASN C  1 139 ? -18.426 61.022  26.610  1.00 37.19  ? 139 ASN D CA  1 
ATOM   3242  C  C   . ASN C  1 139 ? -19.260 60.385  25.481  1.00 37.14  ? 139 ASN D C   1 
ATOM   3243  O  O   . ASN C  1 139 ? -20.119 61.046  24.890  1.00 38.50  ? 139 ASN D O   1 
ATOM   3244  C  CB  . ASN C  1 139 ? -18.555 62.555  26.559  1.00 39.00  ? 139 ASN D CB  1 
ATOM   3245  C  CG  . ASN C  1 139 ? -18.007 63.226  27.795  1.00 39.54  ? 139 ASN D CG  1 
ATOM   3246  O  OD1 . ASN C  1 139 ? -18.545 63.050  28.892  1.00 39.90  ? 139 ASN D OD1 1 
ATOM   3247  N  ND2 . ASN C  1 139 ? -16.948 64.013  27.630  1.00 39.83  ? 139 ASN D ND2 1 
ATOM   3248  N  N   . ALA C  1 140 ? -19.019 59.103  25.205  1.00 35.70  ? 140 ALA D N   1 
ATOM   3249  C  CA  . ALA C  1 140 ? -19.689 58.399  24.103  1.00 35.74  ? 140 ALA D CA  1 
ATOM   3250  C  C   . ALA C  1 140 ? -21.089 57.864  24.435  1.00 36.43  ? 140 ALA D C   1 
ATOM   3251  O  O   . ALA C  1 140 ? -21.716 57.231  23.582  1.00 36.67  ? 140 ALA D O   1 
ATOM   3252  C  CB  . ALA C  1 140 ? -18.814 57.262  23.596  1.00 34.19  ? 140 ALA D CB  1 
ATOM   3253  N  N   . GLY C  1 141 ? -21.582 58.100  25.652  1.00 37.01  ? 141 GLY D N   1 
ATOM   3254  C  CA  . GLY C  1 141 ? -22.933 57.686  26.028  1.00 37.97  ? 141 GLY D CA  1 
ATOM   3255  C  C   . GLY C  1 141 ? -23.007 56.228  26.446  1.00 36.85  ? 141 GLY D C   1 
ATOM   3256  O  O   . GLY C  1 141 ? -22.017 55.636  26.882  1.00 35.38  ? 141 GLY D O   1 
ATOM   3257  N  N   . SER C  1 142 ? -24.187 55.636  26.303  1.00 37.74  ? 142 SER D N   1 
ATOM   3258  C  CA  . SER C  1 142 ? -24.416 54.296  26.823  1.00 37.12  ? 142 SER D CA  1 
ATOM   3259  C  C   . SER C  1 142 ? -23.657 53.237  26.022  1.00 35.51  ? 142 SER D C   1 
ATOM   3260  O  O   . SER C  1 142 ? -23.232 53.469  24.887  1.00 35.15  ? 142 SER D O   1 
ATOM   3261  C  CB  . SER C  1 142 ? -25.909 53.986  26.869  1.00 38.88  ? 142 SER D CB  1 
ATOM   3262  O  OG  . SER C  1 142 ? -26.462 53.992  25.568  1.00 39.70  ? 142 SER D OG  1 
ATOM   3263  N  N   . ARG C  1 143 ? -23.473 52.082  26.645  1.00 34.68  ? 143 ARG D N   1 
ATOM   3264  C  CA  . ARG C  1 143 ? -22.890 50.919  25.977  1.00 33.45  ? 143 ARG D CA  1 
ATOM   3265  C  C   . ARG C  1 143 ? -24.043 50.226  25.261  1.00 34.39  ? 143 ARG D C   1 
ATOM   3266  O  O   . ARG C  1 143 ? -24.923 49.690  25.919  1.00 35.36  ? 143 ARG D O   1 
ATOM   3267  C  CB  . ARG C  1 143 ? -22.215 50.002  27.007  1.00 32.49  ? 143 ARG D CB  1 
ATOM   3268  C  CG  . ARG C  1 143 ? -21.156 50.746  27.818  1.00 31.96  ? 143 ARG D CG  1 
ATOM   3269  C  CD  . ARG C  1 143 ? -20.448 49.900  28.863  1.00 31.30  ? 143 ARG D CD  1 
ATOM   3270  N  NE  . ARG C  1 143 ? -19.583 50.735  29.702  1.00 31.20  ? 143 ARG D NE  1 
ATOM   3271  C  CZ  . ARG C  1 143 ? -18.648 50.292  30.540  1.00 30.65  ? 143 ARG D CZ  1 
ATOM   3272  N  NH1 . ARG C  1 143 ? -18.408 48.994  30.694  1.00 30.10  ? 143 ARG D NH1 1 
ATOM   3273  N  NH2 . ARG C  1 143 ? -17.929 51.172  31.229  1.00 30.90  ? 143 ARG D NH2 1 
ATOM   3274  N  N   . LEU C  1 144 ? -24.062 50.286  23.929  1.00 34.45  ? 144 LEU D N   1 
ATOM   3275  C  CA  . LEU C  1 144 ? -25.174 49.752  23.132  1.00 35.70  ? 144 LEU D CA  1 
ATOM   3276  C  C   . LEU C  1 144 ? -25.075 48.252  22.906  1.00 34.99  ? 144 LEU D C   1 
ATOM   3277  O  O   . LEU C  1 144 ? -26.073 47.540  23.013  1.00 36.08  ? 144 LEU D O   1 
ATOM   3278  C  CB  . LEU C  1 144 ? -25.264 50.445  21.771  1.00 36.52  ? 144 LEU D CB  1 
ATOM   3279  C  CG  . LEU C  1 144 ? -25.663 51.918  21.743  1.00 37.84  ? 144 LEU D CG  1 
ATOM   3280  C  CD1 . LEU C  1 144 ? -25.776 52.363  20.294  1.00 38.87  ? 144 LEU D CD1 1 
ATOM   3281  C  CD2 . LEU C  1 144 ? -26.965 52.169  22.482  1.00 39.57  ? 144 LEU D CD2 1 
ATOM   3282  N  N   . ALA C  1 145 ? -23.881 47.789  22.545  1.00 33.33  ? 145 ALA D N   1 
ATOM   3283  C  CA  . ALA C  1 145 ? -23.631 46.364  22.363  1.00 32.68  ? 145 ALA D CA  1 
ATOM   3284  C  C   . ALA C  1 145 ? -22.192 46.036  22.696  1.00 30.91  ? 145 ALA D C   1 
ATOM   3285  O  O   . ALA C  1 145 ? -21.294 46.871  22.557  1.00 30.24  ? 145 ALA D O   1 
ATOM   3286  C  CB  . ALA C  1 145 ? -23.951 45.930  20.940  1.00 33.39  ? 145 ALA D CB  1 
ATOM   3287  N  N   . ALA C  1 146 ? -21.989 44.806  23.129  1.00 30.37  ? 146 ALA D N   1 
ATOM   3288  C  CA  . ALA C  1 146 ? -20.693 44.367  23.575  1.00 29.01  ? 146 ALA D CA  1 
ATOM   3289  C  C   . ALA C  1 146 ? -20.563 42.873  23.430  1.00 28.84  ? 146 ALA D C   1 
ATOM   3290  O  O   . ALA C  1 146 ? -21.560 42.148  23.293  1.00 29.75  ? 146 ALA D O   1 
ATOM   3291  C  CB  . ALA C  1 146 ? -20.480 44.767  25.017  1.00 28.78  ? 146 ALA D CB  1 
ATOM   3292  N  N   . GLY C  1 147 ? -19.312 42.429  23.456  1.00 27.77  ? 147 GLY D N   1 
ATOM   3293  C  CA  . GLY C  1 147 ? -18.983 41.012  23.409  1.00 27.65  ? 147 GLY D CA  1 
ATOM   3294  C  C   . GLY C  1 147 ? -17.546 40.771  23.838  1.00 26.68  ? 147 GLY D C   1 
ATOM   3295  O  O   . GLY C  1 147 ? -16.698 41.669  23.758  1.00 26.03  ? 147 GLY D O   1 
ATOM   3296  N  N   . VAL C  1 148 ? -17.279 39.544  24.265  1.00 26.73  ? 148 VAL D N   1 
ATOM   3297  C  CA  . VAL C  1 148 ? -15.955 39.156  24.700  1.00 26.19  ? 148 VAL D CA  1 
ATOM   3298  C  C   . VAL C  1 148 ? -15.126 38.784  23.460  1.00 25.97  ? 148 VAL D C   1 
ATOM   3299  O  O   . VAL C  1 148 ? -15.600 38.088  22.565  1.00 26.56  ? 148 VAL D O   1 
ATOM   3300  C  CB  . VAL C  1 148 ? -16.013 37.997  25.704  1.00 26.64  ? 148 VAL D CB  1 
ATOM   3301  C  CG1 . VAL C  1 148 ? -14.616 37.646  26.200  1.00 26.30  ? 148 VAL D CG1 1 
ATOM   3302  C  CG2 . VAL C  1 148 ? -16.930 38.352  26.879  1.00 27.18  ? 148 VAL D CG2 1 
ATOM   3303  N  N   . ILE C  1 149 ? -13.892 39.261  23.420  1.00 25.42  ? 149 ILE D N   1 
ATOM   3304  C  CA  . ILE C  1 149 ? -12.983 39.009  22.303  1.00 25.38  ? 149 ILE D CA  1 
ATOM   3305  C  C   . ILE C  1 149 ? -12.371 37.631  22.511  1.00 25.63  ? 149 ILE D C   1 
ATOM   3306  O  O   . ILE C  1 149 ? -11.691 37.390  23.510  1.00 25.54  ? 149 ILE D O   1 
ATOM   3307  C  CB  . ILE C  1 149 ? -11.907 40.100  22.208  1.00 25.02  ? 149 ILE D CB  1 
ATOM   3308  C  CG1 . ILE C  1 149 ? -12.582 41.467  21.989  1.00 24.97  ? 149 ILE D CG1 1 
ATOM   3309  C  CG2 . ILE C  1 149 ? -10.922 39.807  21.075  1.00 25.27  ? 149 ILE D CG2 1 
ATOM   3310  C  CD1 . ILE C  1 149 ? -11.668 42.652  22.228  1.00 24.80  ? 149 ILE D CD1 1 
ATOM   3311  N  N   . GLY C  1 150 ? -12.644 36.723  21.584  1.00 26.14  ? 150 GLY D N   1 
ATOM   3312  C  CA  . GLY C  1 150 ? -12.185 35.348  21.693  1.00 26.72  ? 150 GLY D CA  1 
ATOM   3313  C  C   . GLY C  1 150 ? -11.214 34.969  20.590  1.00 27.14  ? 150 GLY D C   1 
ATOM   3314  O  O   . GLY C  1 150 ? -11.153 35.619  19.551  1.00 27.04  ? 150 GLY D O   1 
ATOM   3315  N  N   . ILE C  1 151 ? -10.491 33.878  20.826  1.00 27.78  ? 151 ILE D N   1 
ATOM   3316  C  CA  . ILE C  1 151 ? -9.497  33.374  19.890  1.00 28.55  ? 151 ILE D CA  1 
ATOM   3317  C  C   . ILE C  1 151 ? -10.243 32.705  18.747  1.00 29.40  ? 151 ILE D C   1 
ATOM   3318  O  O   . ILE C  1 151 ? -11.173 31.925  18.987  1.00 29.73  ? 151 ILE D O   1 
ATOM   3319  C  CB  . ILE C  1 151 ? -8.531  32.355  20.545  1.00 29.17  ? 151 ILE D CB  1 
ATOM   3320  C  CG1 . ILE C  1 151 ? -7.851  32.979  21.768  1.00 28.75  ? 151 ILE D CG1 1 
ATOM   3321  C  CG2 . ILE C  1 151 ? -7.462  31.927  19.536  1.00 30.04  ? 151 ILE D CG2 1 
ATOM   3322  C  CD1 . ILE C  1 151 ? -7.096  32.007  22.646  1.00 29.54  ? 151 ILE D CD1 1 
ATOM   3323  N  N   . ALA C  1 152 ? -9.838  33.024  17.517  1.00 29.98  ? 152 ALA D N   1 
ATOM   3324  C  CA  . ALA C  1 152 ? -10.468 32.494  16.309  1.00 31.13  ? 152 ALA D CA  1 
ATOM   3325  C  C   . ALA C  1 152 ? -9.510  31.643  15.495  1.00 32.48  ? 152 ALA D C   1 
ATOM   3326  O  O   . ALA C  1 152 ? -8.288  31.760  15.631  1.00 32.52  ? 152 ALA D O   1 
ATOM   3327  C  CB  . ALA C  1 152 ? -10.990 33.627  15.455  1.00 31.03  ? 152 ALA D CB  1 
ATOM   3328  N  N   . GLN C  1 153 ? -10.091 30.788  14.653  1.00 33.90  ? 153 GLN D N   1 
ATOM   3329  C  CA  . GLN C  1 153 ? -9.356  30.000  13.678  1.00 35.53  ? 153 GLN D CA  1 
ATOM   3330  C  C   . GLN C  1 153 ? -9.140  30.847  12.439  1.00 36.23  ? 153 GLN D C   1 
ATOM   3331  O  O   . GLN C  1 153 ? -10.074 31.497  11.921  1.00 36.39  ? 153 GLN D O   1 
ATOM   3332  C  CB  . GLN C  1 153 ? -10.137 28.750  13.289  1.00 36.86  ? 153 GLN D CB  1 
ATOM   3333  C  CG  . GLN C  1 153 ? -9.288  27.660  12.649  1.00 38.46  ? 153 GLN D CG  1 
ATOM   3334  C  CD  . GLN C  1 153 ? -10.123 26.535  12.071  1.00 40.04  ? 153 GLN D CD  1 
ATOM   3335  O  OE1 . GLN C  1 153 ? -11.124 26.779  11.401  1.00 40.60  ? 153 GLN D OE1 1 
ATOM   3336  N  NE2 . GLN C  1 153 ? -9.709  25.300  12.313  1.00 41.10  ? 153 GLN D NE2 1 
ATOM   3337  O  OXT . GLN C  1 153 ? -8.024  30.882  11.929  1.00 37.03  ? 153 GLN D OXT 1 
ATOM   3338  N  N   . ALA D  1 1   ? -3.581  35.739  41.786  0.70 45.81  ? 1   ALA G N   1 
ATOM   3339  C  CA  . ALA D  1 1   ? -4.947  36.329  41.900  0.70 44.87  ? 1   ALA G CA  1 
ATOM   3340  C  C   . ALA D  1 1   ? -5.582  36.578  40.526  0.70 42.72  ? 1   ALA G C   1 
ATOM   3341  O  O   . ALA D  1 1   ? -6.280  37.574  40.330  0.70 42.72  ? 1   ALA G O   1 
ATOM   3342  C  CB  . ALA D  1 1   ? -4.900  37.620  42.720  0.70 47.11  ? 1   ALA G CB  1 
ATOM   3343  N  N   . THR D  1 2   ? -5.361  35.661  39.584  1.00 41.09  ? 2   THR G N   1 
ATOM   3344  C  CA  . THR D  1 2   ? -5.951  35.773  38.256  1.00 39.11  ? 2   THR G CA  1 
ATOM   3345  C  C   . THR D  1 2   ? -7.385  35.209  38.333  1.00 37.29  ? 2   THR G C   1 
ATOM   3346  O  O   . THR D  1 2   ? -7.635  34.158  38.950  1.00 36.82  ? 2   THR G O   1 
ATOM   3347  C  CB  . THR D  1 2   ? -5.097  35.061  37.185  1.00 38.53  ? 2   THR G CB  1 
ATOM   3348  O  OG1 . THR D  1 2   ? -3.711  35.249  37.477  1.00 40.60  ? 2   THR G OG1 1 
ATOM   3349  C  CG2 . THR D  1 2   ? -5.343  35.636  35.815  1.00 37.65  ? 2   THR G CG2 1 
ATOM   3350  N  N   . LYS D  1 3   ? -8.321  35.947  37.746  1.00 36.29  ? 3   LYS G N   1 
ATOM   3351  C  CA  . LYS D  1 3   ? -9.725  35.568  37.743  1.00 34.85  ? 3   LYS G CA  1 
ATOM   3352  C  C   . LYS D  1 3   ? -10.289 35.692  36.345  1.00 33.23  ? 3   LYS G C   1 
ATOM   3353  O  O   . LYS D  1 3   ? -9.870  36.553  35.569  1.00 33.50  ? 3   LYS G O   1 
ATOM   3354  C  CB  . LYS D  1 3   ? -10.532 36.442  38.713  1.00 35.97  ? 3   LYS G CB  1 
ATOM   3355  C  CG  . LYS D  1 3   ? -10.254 36.143  40.176  1.00 37.45  ? 3   LYS G CG  1 
ATOM   3356  C  CD  . LYS D  1 3   ? -10.897 37.157  41.101  1.00 39.02  ? 3   LYS G CD  1 
ATOM   3357  C  CE  . LYS D  1 3   ? -10.294 37.110  42.497  1.00 41.11  ? 3   LYS G CE  1 
ATOM   3358  N  NZ  . LYS D  1 3   ? -11.190 37.776  43.489  1.00 42.49  ? 3   LYS G NZ  1 
ATOM   3359  N  N   . ALA D  1 4   ? -11.242 34.818  36.044  1.00 31.61  ? 4   ALA G N   1 
ATOM   3360  C  CA  . ALA D  1 4   ? -11.979 34.864  34.800  1.00 30.35  ? 4   ALA G CA  1 
ATOM   3361  C  C   . ALA D  1 4   ? -13.448 34.508  35.062  1.00 29.55  ? 4   ALA G C   1 
ATOM   3362  O  O   . ALA D  1 4   ? -13.802 34.031  36.142  1.00 29.67  ? 4   ALA G O   1 
ATOM   3363  C  CB  . ALA D  1 4   ? -11.346 33.931  33.777  1.00 29.40  ? 4   ALA G CB  1 
ATOM   3364  N  N   . VAL D  1 5   ? -14.288 34.771  34.070  1.00 28.87  ? 5   VAL G N   1 
ATOM   3365  C  CA  . VAL D  1 5   ? -15.737 34.566  34.184  1.00 28.41  ? 5   VAL G CA  1 
ATOM   3366  C  C   . VAL D  1 5   ? -16.285 34.207  32.811  1.00 27.50  ? 5   VAL G C   1 
ATOM   3367  O  O   . VAL D  1 5   ? -15.711 34.586  31.775  1.00 27.42  ? 5   VAL G O   1 
ATOM   3368  C  CB  . VAL D  1 5   ? -16.436 35.822  34.771  1.00 29.54  ? 5   VAL G CB  1 
ATOM   3369  C  CG1 . VAL D  1 5   ? -16.321 37.013  33.825  1.00 30.09  ? 5   VAL G CG1 1 
ATOM   3370  C  CG2 . VAL D  1 5   ? -17.888 35.554  35.133  1.00 29.39  ? 5   VAL G CG2 1 
ATOM   3371  N  N   . CYS D  1 6   ? -17.377 33.452  32.818  1.00 26.90  ? 6   CYS G N   1 
ATOM   3372  C  CA  . CYS D  1 6   ? -18.033 33.021  31.600  1.00 26.32  ? 6   CYS G CA  1 
ATOM   3373  C  C   . CYS D  1 6   ? -19.558 33.023  31.797  1.00 26.42  ? 6   CYS G C   1 
ATOM   3374  O  O   . CYS D  1 6   ? -20.054 32.454  32.764  1.00 26.29  ? 6   CYS G O   1 
ATOM   3375  C  CB  . CYS D  1 6   ? -17.569 31.623  31.248  1.00 25.43  ? 6   CYS G CB  1 
ATOM   3376  S  SG  . CYS D  1 6   ? -18.242 31.034  29.688  1.00 25.07  ? 6   CYS G SG  1 
ATOM   3377  N  N   . VAL D  1 7   ? -20.274 33.696  30.903  1.00 26.89  ? 7   VAL G N   1 
ATOM   3378  C  CA  . VAL D  1 7   ? -21.740 33.627  30.857  1.00 27.27  ? 7   VAL G CA  1 
ATOM   3379  C  C   . VAL D  1 7   ? -22.116 32.583  29.822  1.00 26.69  ? 7   VAL G C   1 
ATOM   3380  O  O   . VAL D  1 7   ? -21.828 32.761  28.633  1.00 26.62  ? 7   VAL G O   1 
ATOM   3381  C  CB  . VAL D  1 7   ? -22.376 34.974  30.471  1.00 28.40  ? 7   VAL G CB  1 
ATOM   3382  C  CG1 . VAL D  1 7   ? -23.906 34.881  30.501  1.00 28.85  ? 7   VAL G CG1 1 
ATOM   3383  C  CG2 . VAL D  1 7   ? -21.880 36.077  31.394  1.00 29.35  ? 7   VAL G CG2 1 
ATOM   3384  N  N   . LEU D  1 8   ? -22.739 31.494  30.277  1.00 26.49  ? 8   LEU G N   1 
ATOM   3385  C  CA  . LEU D  1 8   ? -23.229 30.450  29.382  1.00 26.24  ? 8   LEU G CA  1 
ATOM   3386  C  C   . LEU D  1 8   ? -24.633 30.802  28.898  1.00 27.29  ? 8   LEU G C   1 
ATOM   3387  O  O   . LEU D  1 8   ? -25.525 31.049  29.703  1.00 27.79  ? 8   LEU G O   1 
ATOM   3388  C  CB  . LEU D  1 8   ? -23.243 29.099  30.091  1.00 25.64  ? 8   LEU G CB  1 
ATOM   3389  C  CG  . LEU D  1 8   ? -21.865 28.574  30.515  1.00 25.05  ? 8   LEU G CG  1 
ATOM   3390  C  CD1 . LEU D  1 8   ? -21.991 27.541  31.619  1.00 24.93  ? 8   LEU G CD1 1 
ATOM   3391  C  CD2 . LEU D  1 8   ? -21.138 27.978  29.327  1.00 24.58  ? 8   LEU G CD2 1 
ATOM   3392  N  N   . LYS D  1 9   ? -24.801 30.850  27.578  1.00 27.88  ? 9   LYS G N   1 
ATOM   3393  C  CA  . LYS D  1 9   ? -26.097 31.056  26.943  1.00 29.11  ? 9   LYS G CA  1 
ATOM   3394  C  C   . LYS D  1 9   ? -26.287 30.104  25.784  1.00 28.99  ? 9   LYS G C   1 
ATOM   3395  O  O   . LYS D  1 9   ? -25.330 29.660  25.167  1.00 28.28  ? 9   LYS G O   1 
ATOM   3396  C  CB  . LYS D  1 9   ? -26.218 32.477  26.394  1.00 30.51  ? 9   LYS G CB  1 
ATOM   3397  C  CG  . LYS D  1 9   ? -25.892 33.561  27.398  1.00 31.12  ? 9   LYS G CG  1 
ATOM   3398  C  CD  . LYS D  1 9   ? -26.449 34.908  26.950  1.00 32.78  ? 9   LYS G CD  1 
ATOM   3399  C  CE  . LYS D  1 9   ? -26.383 35.939  28.074  1.00 33.58  ? 9   LYS G CE  1 
ATOM   3400  N  NZ  . LYS D  1 9   ? -27.302 35.571  29.194  1.00 33.92  ? 9   LYS G NZ  1 
ATOM   3401  N  N   . GLY D  1 10  ? -27.548 29.835  25.467  1.00 29.87  ? 10  GLY G N   1 
ATOM   3402  C  CA  . GLY D  1 10  ? -27.887 29.026  24.308  1.00 30.29  ? 10  GLY G CA  1 
ATOM   3403  C  C   . GLY D  1 10  ? -29.302 29.278  23.841  1.00 31.87  ? 10  GLY G C   1 
ATOM   3404  O  O   . GLY D  1 10  ? -29.962 30.216  24.278  1.00 32.63  ? 10  GLY G O   1 
ATOM   3405  N  N   . ASP D  1 11  ? -29.764 28.404  22.963  1.00 32.62  ? 11  ASP G N   1 
ATOM   3406  C  CA  . ASP D  1 11  ? -31.065 28.548  22.336  1.00 34.52  ? 11  ASP G CA  1 
ATOM   3407  C  C   . ASP D  1 11  ? -32.193 28.085  23.259  1.00 34.77  ? 11  ASP G C   1 
ATOM   3408  O  O   . ASP D  1 11  ? -33.320 28.523  23.085  1.00 36.34  ? 11  ASP G O   1 
ATOM   3409  C  CB  . ASP D  1 11  ? -31.087 27.782  21.015  1.00 35.49  ? 11  ASP G CB  1 
ATOM   3410  C  CG  . ASP D  1 11  ? -30.009 28.267  20.049  1.00 35.80  ? 11  ASP G CG  1 
ATOM   3411  O  OD1 . ASP D  1 11  ? -29.867 29.497  19.863  1.00 36.61  ? 11  ASP G OD1 1 
ATOM   3412  O  OD2 . ASP D  1 11  ? -29.278 27.414  19.494  1.00 35.78  ? 11  ASP G OD2 1 
ATOM   3413  N  N   . GLY D  1 12  ? -31.882 27.215  24.229  1.00 33.35  ? 12  GLY G N   1 
ATOM   3414  C  CA  . GLY D  1 12  ? -32.868 26.671  25.164  1.00 33.69  ? 12  GLY G CA  1 
ATOM   3415  C  C   . GLY D  1 12  ? -32.850 27.343  26.527  1.00 33.23  ? 12  GLY G C   1 
ATOM   3416  O  O   . GLY D  1 12  ? -32.410 28.481  26.642  1.00 33.18  ? 12  GLY G O   1 
ATOM   3417  N  N   . PRO D  1 13  ? -33.322 26.636  27.576  1.00 33.01  ? 13  PRO G N   1 
ATOM   3418  C  CA  . PRO D  1 13  ? -33.370 27.206  28.921  1.00 32.88  ? 13  PRO G CA  1 
ATOM   3419  C  C   . PRO D  1 13  ? -32.034 27.153  29.691  1.00 31.29  ? 13  PRO G C   1 
ATOM   3420  O  O   . PRO D  1 13  ? -31.953 27.719  30.783  1.00 31.44  ? 13  PRO G O   1 
ATOM   3421  C  CB  . PRO D  1 13  ? -34.431 26.343  29.611  1.00 33.72  ? 13  PRO G CB  1 
ATOM   3422  C  CG  . PRO D  1 13  ? -34.248 25.004  28.995  1.00 33.22  ? 13  PRO G CG  1 
ATOM   3423  C  CD  . PRO D  1 13  ? -33.849 25.255  27.562  1.00 33.16  ? 13  PRO G CD  1 
ATOM   3424  N  N   . VAL D  1 14  ? -31.000 26.508  29.142  1.00 29.92  ? 14  VAL G N   1 
ATOM   3425  C  CA  . VAL D  1 14  ? -29.716 26.396  29.851  1.00 28.67  ? 14  VAL G CA  1 
ATOM   3426  C  C   . VAL D  1 14  ? -29.012 27.754  29.889  1.00 28.59  ? 14  VAL G C   1 
ATOM   3427  O  O   . VAL D  1 14  ? -28.793 28.378  28.857  1.00 28.62  ? 14  VAL G O   1 
ATOM   3428  C  CB  . VAL D  1 14  ? -28.761 25.341  29.248  1.00 27.59  ? 14  VAL G CB  1 
ATOM   3429  C  CG1 . VAL D  1 14  ? -27.494 25.219  30.100  1.00 26.67  ? 14  VAL G CG1 1 
ATOM   3430  C  CG2 . VAL D  1 14  ? -29.448 23.982  29.124  1.00 27.81  ? 14  VAL G CG2 1 
ATOM   3431  N  N   . GLN D  1 15  ? -28.690 28.206  31.097  1.00 28.65  ? 15  GLN G N   1 
ATOM   3432  C  CA  . GLN D  1 15  ? -27.932 29.428  31.296  1.00 28.78  ? 15  GLN G CA  1 
ATOM   3433  C  C   . GLN D  1 15  ? -27.273 29.443  32.668  1.00 28.47  ? 15  GLN G C   1 
ATOM   3434  O  O   . GLN D  1 15  ? -27.760 28.823  33.615  1.00 28.72  ? 15  GLN G O   1 
ATOM   3435  C  CB  . GLN D  1 15  ? -28.801 30.681  31.104  1.00 30.27  ? 15  GLN G CB  1 
ATOM   3436  C  CG  . GLN D  1 15  ? -29.979 30.806  32.058  1.00 31.63  ? 15  GLN G CG  1 
ATOM   3437  C  CD  . GLN D  1 15  ? -30.925 31.932  31.686  1.00 33.26  ? 15  GLN G CD  1 
ATOM   3438  O  OE1 . GLN D  1 15  ? -32.144 31.781  31.745  1.00 34.68  ? 15  GLN G OE1 1 
ATOM   3439  N  NE2 . GLN D  1 15  ? -30.371 33.069  31.302  1.00 33.83  ? 15  GLN G NE2 1 
ATOM   3440  N  N   . GLY D  1 16  ? -26.151 30.149  32.756  1.00 28.00  ? 16  GLY G N   1 
ATOM   3441  C  CA  . GLY D  1 16  ? -25.452 30.292  34.018  1.00 27.94  ? 16  GLY G CA  1 
ATOM   3442  C  C   . GLY D  1 16  ? -24.215 31.159  33.937  1.00 27.70  ? 16  GLY G C   1 
ATOM   3443  O  O   . GLY D  1 16  ? -23.868 31.673  32.873  1.00 27.41  ? 16  GLY G O   1 
ATOM   3444  N  N   . ILE D  1 17  ? -23.582 31.334  35.092  1.00 27.92  ? 17  ILE G N   1 
ATOM   3445  C  CA  . ILE D  1 17  ? -22.340 32.083  35.219  1.00 28.01  ? 17  ILE G CA  1 
ATOM   3446  C  C   . ILE D  1 17  ? -21.334 31.168  35.896  1.00 27.53  ? 17  ILE G C   1 
ATOM   3447  O  O   . ILE D  1 17  ? -21.617 30.616  36.954  1.00 27.91  ? 17  ILE G O   1 
ATOM   3448  C  CB  . ILE D  1 17  ? -22.526 33.376  36.039  1.00 29.37  ? 17  ILE G CB  1 
ATOM   3449  C  CG1 . ILE D  1 17  ? -23.387 34.373  35.254  1.00 29.95  ? 17  ILE G CG1 1 
ATOM   3450  C  CG2 . ILE D  1 17  ? -21.176 34.009  36.385  1.00 29.78  ? 17  ILE G CG2 1 
ATOM   3451  C  CD1 . ILE D  1 17  ? -23.983 35.481  36.100  1.00 31.51  ? 17  ILE G CD1 1 
ATOM   3452  N  N   . ILE D  1 18  ? -20.168 31.017  35.282  1.00 26.91  ? 18  ILE G N   1 
ATOM   3453  C  CA  . ILE D  1 18  ? -19.086 30.217  35.845  1.00 26.73  ? 18  ILE G CA  1 
ATOM   3454  C  C   . ILE D  1 18  ? -17.899 31.125  36.105  1.00 27.44  ? 18  ILE G C   1 
ATOM   3455  O  O   . ILE D  1 18  ? -17.463 31.857  35.211  1.00 27.32  ? 18  ILE G O   1 
ATOM   3456  C  CB  . ILE D  1 18  ? -18.683 29.069  34.898  1.00 25.70  ? 18  ILE G CB  1 
ATOM   3457  C  CG1 . ILE D  1 18  ? -19.853 28.088  34.715  1.00 25.21  ? 18  ILE G CG1 1 
ATOM   3458  C  CG2 . ILE D  1 18  ? -17.428 28.345  35.402  1.00 25.81  ? 18  ILE G CG2 1 
ATOM   3459  C  CD1 . ILE D  1 18  ? -20.276 27.340  35.967  1.00 25.65  ? 18  ILE G CD1 1 
ATOM   3460  N  N   . ASN D  1 19  ? -17.384 31.050  37.334  1.00 28.26  ? 19  ASN G N   1 
ATOM   3461  C  CA  . ASN D  1 19  ? -16.194 31.782  37.762  1.00 29.18  ? 19  ASN G CA  1 
ATOM   3462  C  C   . ASN D  1 19  ? -14.961 30.883  37.716  1.00 29.00  ? 19  ASN G C   1 
ATOM   3463  O  O   . ASN D  1 19  ? -15.057 29.662  37.880  1.00 28.46  ? 19  ASN G O   1 
ATOM   3464  C  CB  . ASN D  1 19  ? -16.375 32.298  39.192  1.00 30.65  ? 19  ASN G CB  1 
ATOM   3465  C  CG  . ASN D  1 19  ? -17.626 33.140  39.355  1.00 31.11  ? 19  ASN G CG  1 
ATOM   3466  O  OD1 . ASN D  1 19  ? -17.694 34.270  38.874  1.00 31.51  ? 19  ASN G OD1 1 
ATOM   3467  N  ND2 . ASN D  1 19  ? -18.623 32.590  40.049  1.00 31.24  ? 19  ASN G ND2 1 
ATOM   3468  N  N   . PHE D  1 20  ? -13.811 31.513  37.493  1.00 29.60  ? 20  PHE G N   1 
ATOM   3469  C  CA  . PHE D  1 20  ? -12.507 30.853  37.506  1.00 29.87  ? 20  PHE G CA  1 
ATOM   3470  C  C   . PHE D  1 20  ? -11.581 31.676  38.365  1.00 31.65  ? 20  PHE G C   1 
ATOM   3471  O  O   . PHE D  1 20  ? -11.549 32.895  38.228  1.00 32.18  ? 20  PHE G O   1 
ATOM   3472  C  CB  . PHE D  1 20  ? -11.907 30.792  36.106  1.00 29.05  ? 20  PHE G CB  1 
ATOM   3473  C  CG  . PHE D  1 20  ? -12.746 30.055  35.111  1.00 27.59  ? 20  PHE G CG  1 
ATOM   3474  C  CD1 . PHE D  1 20  ? -13.793 30.697  34.458  1.00 27.07  ? 20  PHE G CD1 1 
ATOM   3475  C  CD2 . PHE D  1 20  ? -12.491 28.722  34.826  1.00 26.94  ? 20  PHE G CD2 1 
ATOM   3476  C  CE1 . PHE D  1 20  ? -14.562 30.022  33.528  1.00 26.02  ? 20  PHE G CE1 1 
ATOM   3477  C  CE2 . PHE D  1 20  ? -13.257 28.043  33.898  1.00 25.84  ? 20  PHE G CE2 1 
ATOM   3478  C  CZ  . PHE D  1 20  ? -14.289 28.691  33.248  1.00 25.39  ? 20  PHE G CZ  1 
ATOM   3479  N  N   . GLU D  1 21  ? -10.816 31.015  39.232  1.00 32.75  ? 21  GLU G N   1 
ATOM   3480  C  CA  . GLU D  1 21  ? -9.812  31.692  40.037  1.00 34.80  ? 21  GLU G CA  1 
ATOM   3481  C  C   . GLU D  1 21  ? -8.555  30.828  40.178  1.00 35.59  ? 21  GLU G C   1 
ATOM   3482  O  O   . GLU D  1 21  ? -8.634  29.637  40.485  1.00 35.23  ? 21  GLU G O   1 
ATOM   3483  C  CB  . GLU D  1 21  ? -10.369 32.079  41.407  1.00 36.16  ? 21  GLU G CB  1 
ATOM   3484  C  CG  . GLU D  1 21  ? -9.398  32.929  42.222  1.00 38.46  ? 21  GLU G CG  1 
ATOM   3485  C  CD  . GLU D  1 21  ? -9.948  33.376  43.558  1.00 40.10  ? 21  GLU G CD  1 
ATOM   3486  O  OE1 . GLU D  1 21  ? -11.171 33.520  43.704  1.00 39.70  ? 21  GLU G OE1 1 
ATOM   3487  O  OE2 . GLU D  1 21  ? -9.149  33.599  44.472  1.00 42.24  ? 21  GLU G OE2 1 
ATOM   3488  N  N   . GLN D  1 22  ? -7.409  31.453  39.939  1.00 36.91  ? 22  GLN G N   1 
ATOM   3489  C  CA  . GLN D  1 22  ? -6.098  30.805  40.052  1.00 38.12  ? 22  GLN G CA  1 
ATOM   3490  C  C   . GLN D  1 22  ? -5.190  31.708  40.886  1.00 40.78  ? 22  GLN G C   1 
ATOM   3491  O  O   . GLN D  1 22  ? -4.693  32.728  40.409  1.00 41.33  ? 22  GLN G O   1 
ATOM   3492  C  CB  . GLN D  1 22  ? -5.514  30.560  38.659  1.00 37.08  ? 22  GLN G CB  1 
ATOM   3493  C  CG  . GLN D  1 22  ? -4.307  29.630  38.625  1.00 37.88  ? 22  GLN G CG  1 
ATOM   3494  C  CD  . GLN D  1 22  ? -3.751  29.415  37.221  1.00 37.08  ? 22  GLN G CD  1 
ATOM   3495  O  OE1 . GLN D  1 22  ? -3.949  30.285  36.320  1.00 36.44  ? 22  GLN G OE1 1 
ATOM   3496  N  NE2 . GLN D  1 22  ? -3.051  28.245  37.024  1.00 37.27  ? 22  GLN G NE2 1 
ATOM   3497  N  N   . LYS D  1 23  ? -4.995  31.333  42.143  1.00 42.73  ? 23  LYS G N   1 
ATOM   3498  C  CA  . LYS D  1 23  ? -4.222  32.144  43.082  1.00 45.66  ? 23  LYS G CA  1 
ATOM   3499  C  C   . LYS D  1 23  ? -2.750  32.252  42.688  1.00 47.20  ? 23  LYS G C   1 
ATOM   3500  O  O   . LYS D  1 23  ? -2.141  33.301  42.861  1.00 48.79  ? 23  LYS G O   1 
ATOM   3501  C  CB  . LYS D  1 23  ? -4.342  31.586  44.506  1.00 47.33  ? 23  LYS G CB  1 
ATOM   3502  C  CG  . LYS D  1 23  ? -5.730  31.767  45.098  1.00 46.91  ? 23  LYS G CG  1 
ATOM   3503  C  CD  . LYS D  1 23  ? -5.740  31.534  46.607  1.00 49.22  ? 23  LYS G CD  1 
ATOM   3504  C  CE  . LYS D  1 23  ? -6.937  32.203  47.267  1.00 49.45  ? 23  LYS G CE  1 
ATOM   3505  N  NZ  . LYS D  1 23  ? -8.211  31.926  46.549  1.00 46.95  ? 23  LYS G NZ  1 
ATOM   3506  N  N   . GLU D  1 24  ? -2.205  31.172  42.144  1.00 46.94  ? 24  GLU G N   1 
ATOM   3507  C  CA  . GLU D  1 24  ? -0.833  31.145  41.664  1.00 48.48  ? 24  GLU G CA  1 
ATOM   3508  C  C   . GLU D  1 24  ? -0.783  30.577  40.266  1.00 46.68  ? 24  GLU G C   1 
ATOM   3509  O  O   . GLU D  1 24  ? -1.458  29.598  39.978  1.00 44.89  ? 24  GLU G O   1 
ATOM   3510  C  CB  . GLU D  1 24  ? 0.020   30.266  42.579  1.00 50.65  ? 24  GLU G CB  1 
ATOM   3511  C  CG  . GLU D  1 24  ? 0.057   30.702  44.035  1.00 53.16  ? 24  GLU G CG  1 
ATOM   3512  C  CD  . GLU D  1 24  ? 0.797   32.009  44.261  1.00 55.50  ? 24  GLU G CD  1 
ATOM   3513  O  OE1 . GLU D  1 24  ? 1.517   32.485  43.345  1.00 55.81  ? 24  GLU G OE1 1 
ATOM   3514  O  OE2 . GLU D  1 24  ? 0.676   32.556  45.381  1.00 57.52  ? 24  GLU G OE2 1 
ATOM   3515  N  N   . SER D  1 25  ? 0.073   31.148  39.419  1.00 47.50  ? 25  SER G N   1 
ATOM   3516  C  CA  . SER D  1 25  ? 0.271   30.643  38.049  1.00 46.29  ? 25  SER G CA  1 
ATOM   3517  C  C   . SER D  1 25  ? 0.723   29.172  37.985  1.00 46.32  ? 25  SER G C   1 
ATOM   3518  O  O   . SER D  1 25  ? 0.441   28.482  36.993  1.00 44.91  ? 25  SER G O   1 
ATOM   3519  C  CB  . SER D  1 25  ? 1.255   31.536  37.284  1.00 47.46  ? 25  SER G CB  1 
ATOM   3520  O  OG  . SER D  1 25  ? 2.397   31.823  38.066  1.00 50.16  ? 25  SER G OG  1 
ATOM   3521  N  N   . ASN D  1 26  ? 1.397   28.692  39.040  1.00 48.34  ? 26  ASN G N   1 
ATOM   3522  C  CA  . ASN D  1 26  ? 1.762   27.265  39.152  1.00 48.58  ? 26  ASN G CA  1 
ATOM   3523  C  C   . ASN D  1 26  ? 0.659   26.373  39.763  1.00 47.24  ? 26  ASN G C   1 
ATOM   3524  O  O   . ASN D  1 26  ? 0.901   25.191  40.054  1.00 48.03  ? 26  ASN G O   1 
ATOM   3525  C  CB  . ASN D  1 26  ? 3.070   27.100  39.943  1.00 51.59  ? 26  ASN G CB  1 
ATOM   3526  C  CG  . ASN D  1 26  ? 2.898   27.238  41.461  1.00 53.30  ? 26  ASN G CG  1 
ATOM   3527  O  OD1 . ASN D  1 26  ? 1.974   27.887  41.950  1.00 52.82  ? 26  ASN G OD1 1 
ATOM   3528  N  ND2 . ASN D  1 26  ? 3.799   26.610  42.212  1.00 55.60  ? 26  ASN G ND2 1 
ATOM   3529  N  N   . GLY D  1 27  ? -0.530  26.922  39.971  1.00 45.44  ? 27  GLY G N   1 
ATOM   3530  C  CA  . GLY D  1 27  ? -1.491  26.297  40.861  1.00 44.73  ? 27  GLY G CA  1 
ATOM   3531  C  C   . GLY D  1 27  ? -2.775  25.867  40.190  1.00 41.87  ? 27  GLY G C   1 
ATOM   3532  O  O   . GLY D  1 27  ? -2.975  26.097  38.991  1.00 40.24  ? 27  GLY G O   1 
ATOM   3533  N  N   . PRO D  1 28  ? -3.658  25.228  40.973  1.00 41.29  ? 28  PRO G N   1 
ATOM   3534  C  CA  . PRO D  1 28  ? -4.930  24.793  40.447  1.00 38.95  ? 28  PRO G CA  1 
ATOM   3535  C  C   . PRO D  1 28  ? -5.823  25.977  40.107  1.00 37.55  ? 28  PRO G C   1 
ATOM   3536  O  O   . PRO D  1 28  ? -5.664  27.063  40.667  1.00 38.57  ? 28  PRO G O   1 
ATOM   3537  C  CB  . PRO D  1 28  ? -5.530  23.973  41.594  1.00 39.61  ? 28  PRO G CB  1 
ATOM   3538  C  CG  . PRO D  1 28  ? -4.846  24.457  42.817  1.00 42.01  ? 28  PRO G CG  1 
ATOM   3539  C  CD  . PRO D  1 28  ? -3.482  24.861  42.391  1.00 43.16  ? 28  PRO G CD  1 
ATOM   3540  N  N   . VAL D  1 29  ? -6.733  25.759  39.168  1.00 35.35  ? 29  VAL G N   1 
ATOM   3541  C  CA  . VAL D  1 29  ? -7.769  26.724  38.858  1.00 34.11  ? 29  VAL G CA  1 
ATOM   3542  C  C   . VAL D  1 29  ? -9.043  26.214  39.523  1.00 33.42  ? 29  VAL G C   1 
ATOM   3543  O  O   . VAL D  1 29  ? -9.471  25.090  39.266  1.00 32.53  ? 29  VAL G O   1 
ATOM   3544  C  CB  . VAL D  1 29  ? -8.000  26.862  37.343  1.00 32.56  ? 29  VAL G CB  1 
ATOM   3545  C  CG1 . VAL D  1 29  ? -9.089  27.896  37.060  1.00 31.74  ? 29  VAL G CG1 1 
ATOM   3546  C  CG2 . VAL D  1 29  ? -6.693  27.221  36.630  1.00 33.25  ? 29  VAL G CG2 1 
ATOM   3547  N  N   . LYS D  1 30  ? -9.626  27.031  40.389  1.00 33.93  ? 30  LYS G N   1 
ATOM   3548  C  CA  . LYS D  1 30  ? -10.942 26.722  40.951  1.00 33.47  ? 30  LYS G CA  1 
ATOM   3549  C  C   . LYS D  1 30  ? -12.019 27.205  39.999  1.00 31.74  ? 30  LYS G C   1 
ATOM   3550  O  O   . LYS D  1 30  ? -11.977 28.341  39.538  1.00 31.55  ? 30  LYS G O   1 
ATOM   3551  C  CB  . LYS D  1 30  ? -11.106 27.352  42.330  1.00 35.26  ? 30  LYS G CB  1 
ATOM   3552  C  CG  . LYS D  1 30  ? -10.288 26.636  43.386  1.00 37.04  ? 30  LYS G CG  1 
ATOM   3553  C  CD  . LYS D  1 30  ? -10.144 27.476  44.639  1.00 39.20  ? 30  LYS G CD  1 
ATOM   3554  C  CE  . LYS D  1 30  ? -9.354  26.742  45.710  1.00 41.23  ? 30  LYS G CE  1 
ATOM   3555  N  NZ  . LYS D  1 30  ? -8.721  27.698  46.658  1.00 43.61  ? 30  LYS G NZ  1 
ATOM   3556  N  N   . VAL D  1 31  ? -12.977 26.319  39.718  1.00 30.56  ? 31  VAL G N   1 
ATOM   3557  C  CA  . VAL D  1 31  ? -14.075 26.564  38.793  1.00 29.17  ? 31  VAL G CA  1 
ATOM   3558  C  C   . VAL D  1 31  ? -15.384 26.364  39.564  1.00 29.22  ? 31  VAL G C   1 
ATOM   3559  O  O   . VAL D  1 31  ? -15.627 25.291  40.134  1.00 29.34  ? 31  VAL G O   1 
ATOM   3560  C  CB  . VAL D  1 31  ? -14.017 25.599  37.584  1.00 27.93  ? 31  VAL G CB  1 
ATOM   3561  C  CG1 . VAL D  1 31  ? -15.019 25.997  36.510  1.00 26.87  ? 31  VAL G CG1 1 
ATOM   3562  C  CG2 . VAL D  1 31  ? -12.610 25.548  36.996  1.00 28.14  ? 31  VAL G CG2 1 
ATOM   3563  N  N   . TRP D  1 32  ? -16.212 27.402  39.609  1.00 29.27  ? 32  TRP G N   1 
ATOM   3564  C  CA  . TRP D  1 32  ? -17.492 27.313  40.320  1.00 29.55  ? 32  TRP G CA  1 
ATOM   3565  C  C   . TRP D  1 32  ? -18.541 28.294  39.827  1.00 29.35  ? 32  TRP G C   1 
ATOM   3566  O  O   . TRP D  1 32  ? -18.228 29.332  39.253  1.00 29.24  ? 32  TRP G O   1 
ATOM   3567  C  CB  . TRP D  1 32  ? -17.298 27.494  41.836  1.00 31.11  ? 32  TRP G CB  1 
ATOM   3568  C  CG  . TRP D  1 32  ? -17.163 28.923  42.266  1.00 32.15  ? 32  TRP G CG  1 
ATOM   3569  C  CD1 . TRP D  1 32  ? -18.134 29.712  42.806  1.00 32.94  ? 32  TRP G CD1 1 
ATOM   3570  C  CD2 . TRP D  1 32  ? -15.992 29.740  42.166  1.00 32.73  ? 32  TRP G CD2 1 
ATOM   3571  N  NE1 . TRP D  1 32  ? -17.641 30.969  43.056  1.00 34.00  ? 32  TRP G NE1 1 
ATOM   3572  C  CE2 . TRP D  1 32  ? -16.327 31.014  42.674  1.00 33.89  ? 32  TRP G CE2 1 
ATOM   3573  C  CE3 . TRP D  1 32  ? -14.692 29.518  41.698  1.00 32.56  ? 32  TRP G CE3 1 
ATOM   3574  C  CZ2 . TRP D  1 32  ? -15.404 32.064  42.741  1.00 34.90  ? 32  TRP G CZ2 1 
ATOM   3575  C  CZ3 . TRP D  1 32  ? -13.771 30.569  41.761  1.00 33.58  ? 32  TRP G CZ3 1 
ATOM   3576  C  CH2 . TRP D  1 32  ? -14.141 31.828  42.276  1.00 34.70  ? 32  TRP G CH2 1 
ATOM   3577  N  N   . GLY D  1 33  ? -19.792 27.949  40.113  1.00 29.55  ? 33  GLY G N   1 
ATOM   3578  C  CA  . GLY D  1 33  ? -20.942 28.787  39.796  1.00 29.77  ? 33  GLY G CA  1 
ATOM   3579  C  C   . GLY D  1 33  ? -22.159 27.935  39.538  1.00 29.46  ? 33  GLY G C   1 
ATOM   3580  O  O   . GLY D  1 33  ? -22.128 26.715  39.699  1.00 29.28  ? 33  GLY G O   1 
ATOM   3581  N  N   . SER D  1 34  ? -23.240 28.585  39.123  1.00 29.77  ? 34  SER G N   1 
ATOM   3582  C  CA  . SER D  1 34  ? -24.533 27.931  38.986  1.00 29.72  ? 34  SER G CA  1 
ATOM   3583  C  C   . SER D  1 34  ? -24.977 27.949  37.533  1.00 28.64  ? 34  SER G C   1 
ATOM   3584  O  O   . SER D  1 34  ? -24.940 29.000  36.893  1.00 28.76  ? 34  SER G O   1 
ATOM   3585  C  CB  . SER D  1 34  ? -25.563 28.646  39.843  1.00 31.36  ? 34  SER G CB  1 
ATOM   3586  O  OG  . SER D  1 34  ? -25.284 28.404  41.214  1.00 32.69  ? 34  SER G OG  1 
ATOM   3587  N  N   . ILE D  1 35  ? -25.374 26.787  37.020  1.00 27.76  ? 35  ILE G N   1 
ATOM   3588  C  CA  . ILE D  1 35  ? -26.027 26.676  35.710  1.00 27.09  ? 35  ILE G CA  1 
ATOM   3589  C  C   . ILE D  1 35  ? -27.436 26.131  35.938  1.00 27.55  ? 35  ILE G C   1 
ATOM   3590  O  O   . ILE D  1 35  ? -27.590 25.101  36.576  1.00 27.70  ? 35  ILE G O   1 
ATOM   3591  C  CB  . ILE D  1 35  ? -25.292 25.706  34.753  1.00 26.01  ? 35  ILE G CB  1 
ATOM   3592  C  CG1 . ILE D  1 35  ? -23.790 25.995  34.723  1.00 25.55  ? 35  ILE G CG1 1 
ATOM   3593  C  CG2 . ILE D  1 35  ? -25.897 25.782  33.351  1.00 25.79  ? 35  ILE G CG2 1 
ATOM   3594  C  CD1 . ILE D  1 35  ? -22.985 24.989  33.929  1.00 24.77  ? 35  ILE G CD1 1 
ATOM   3595  N  N   . LYS D  1 36  ? -28.441 26.814  35.409  1.00 27.89  ? 36  LYS G N   1 
ATOM   3596  C  CA  . LYS D  1 36  ? -29.837 26.360  35.528  1.00 28.63  ? 36  LYS G CA  1 
ATOM   3597  C  C   . LYS D  1 36  ? -30.358 25.863  34.173  1.00 28.04  ? 36  LYS G C   1 
ATOM   3598  O  O   . LYS D  1 36  ? -29.703 26.040  33.145  1.00 27.13  ? 36  LYS G O   1 
ATOM   3599  C  CB  . LYS D  1 36  ? -30.719 27.461  36.129  1.00 30.14  ? 36  LYS G CB  1 
ATOM   3600  C  CG  . LYS D  1 36  ? -30.796 28.757  35.333  1.00 30.60  ? 36  LYS G CG  1 
ATOM   3601  C  CD  . LYS D  1 36  ? -31.936 29.617  35.838  1.00 32.44  ? 36  LYS G CD  1 
ATOM   3602  C  CE  . LYS D  1 36  ? -32.050 30.921  35.068  1.00 33.08  ? 36  LYS G CE  1 
ATOM   3603  N  NZ  . LYS D  1 36  ? -33.152 31.742  35.625  1.00 34.99  ? 36  LYS G NZ  1 
ATOM   3604  N  N   . GLY D  1 37  ? -31.512 25.201  34.189  1.00 28.56  ? 37  GLY G N   1 
ATOM   3605  C  CA  . GLY D  1 37  ? -32.174 24.733  32.972  1.00 28.59  ? 37  GLY G CA  1 
ATOM   3606  C  C   . GLY D  1 37  ? -31.708 23.405  32.404  1.00 27.68  ? 37  GLY G C   1 
ATOM   3607  O  O   . GLY D  1 37  ? -32.069 23.054  31.276  1.00 27.77  ? 37  GLY G O   1 
ATOM   3608  N  N   . LEU D  1 38  ? -30.922 22.660  33.184  1.00 26.95  ? 38  LEU G N   1 
ATOM   3609  C  CA  . LEU D  1 38  ? -30.312 21.400  32.737  1.00 26.23  ? 38  LEU G CA  1 
ATOM   3610  C  C   . LEU D  1 38  ? -31.163 20.235  33.212  1.00 26.98  ? 38  LEU G C   1 
ATOM   3611  O  O   . LEU D  1 38  ? -31.711 20.290  34.304  1.00 27.63  ? 38  LEU G O   1 
ATOM   3612  C  CB  . LEU D  1 38  ? -28.896 21.239  33.323  1.00 25.32  ? 38  LEU G CB  1 
ATOM   3613  C  CG  . LEU D  1 38  ? -27.796 22.123  32.736  1.00 24.54  ? 38  LEU G CG  1 
ATOM   3614  C  CD1 . LEU D  1 38  ? -26.606 22.194  33.679  1.00 24.15  ? 38  LEU G CD1 1 
ATOM   3615  C  CD2 . LEU D  1 38  ? -27.372 21.602  31.373  1.00 24.00  ? 38  LEU G CD2 1 
ATOM   3616  N  N   . THR D  1 39  ? -31.244 19.174  32.416  1.00 26.98  ? 39  THR G N   1 
ATOM   3617  C  CA  . THR D  1 39  ? -31.926 17.958  32.863  1.00 27.86  ? 39  THR G CA  1 
ATOM   3618  C  C   . THR D  1 39  ? -31.152 17.378  34.045  1.00 27.64  ? 39  THR G C   1 
ATOM   3619  O  O   . THR D  1 39  ? -29.914 17.376  34.058  1.00 26.58  ? 39  THR G O   1 
ATOM   3620  C  CB  . THR D  1 39  ? -32.027 16.893  31.759  1.00 28.00  ? 39  THR G CB  1 
ATOM   3621  O  OG1 . THR D  1 39  ? -30.715 16.583  31.277  1.00 26.94  ? 39  THR G OG1 1 
ATOM   3622  C  CG2 . THR D  1 39  ? -32.879 17.388  30.610  1.00 28.67  ? 39  THR G CG2 1 
ATOM   3623  N  N   . GLU D  1 40  ? -31.882 16.909  35.046  1.00 28.76  ? 40  GLU G N   1 
ATOM   3624  C  CA  . GLU D  1 40  ? -31.272 16.259  36.208  1.00 29.01  ? 40  GLU G CA  1 
ATOM   3625  C  C   . GLU D  1 40  ? -30.264 15.182  35.775  1.00 28.33  ? 40  GLU G C   1 
ATOM   3626  O  O   . GLU D  1 40  ? -30.574 14.350  34.926  1.00 28.47  ? 40  GLU G O   1 
ATOM   3627  C  CB  . GLU D  1 40  ? -32.368 15.625  37.070  1.00 30.62  ? 40  GLU G CB  1 
ATOM   3628  C  CG  . GLU D  1 40  ? -31.854 14.918  38.322  1.00 31.21  ? 40  GLU G CG  1 
ATOM   3629  C  CD  . GLU D  1 40  ? -32.975 14.325  39.145  1.00 32.97  ? 40  GLU G CD  1 
ATOM   3630  O  OE1 . GLU D  1 40  ? -33.976 13.847  38.571  1.00 33.76  ? 40  GLU G OE1 1 
ATOM   3631  O  OE2 . GLU D  1 40  ? -32.836 14.317  40.382  1.00 33.94  ? 40  GLU G OE2 1 
ATOM   3632  N  N   . GLY D  1 41  ? -29.067 15.211  36.365  1.00 27.79  ? 41  GLY G N   1 
ATOM   3633  C  CA  . GLY D  1 41  ? -28.024 14.223  36.081  1.00 27.40  ? 41  GLY G CA  1 
ATOM   3634  C  C   . GLY D  1 41  ? -26.779 14.848  35.475  1.00 26.25  ? 41  GLY G C   1 
ATOM   3635  O  O   . GLY D  1 41  ? -26.568 16.054  35.581  1.00 25.76  ? 41  GLY G O   1 
ATOM   3636  N  N   . LEU D  1 42  ? -25.974 14.015  34.817  1.00 25.99  ? 42  LEU G N   1 
ATOM   3637  C  CA  . LEU D  1 42  ? -24.618 14.391  34.355  1.00 25.18  ? 42  LEU G CA  1 
ATOM   3638  C  C   . LEU D  1 42  ? -24.608 15.129  33.010  1.00 24.40  ? 42  LEU G C   1 
ATOM   3639  O  O   . LEU D  1 42  ? -25.362 14.771  32.092  1.00 24.64  ? 42  LEU G O   1 
ATOM   3640  C  CB  . LEU D  1 42  ? -23.734 13.142  34.256  1.00 25.52  ? 42  LEU G CB  1 
ATOM   3641  C  CG  . LEU D  1 42  ? -23.381 12.425  35.555  1.00 26.42  ? 42  LEU G CG  1 
ATOM   3642  C  CD1 . LEU D  1 42  ? -22.860 11.014  35.287  1.00 27.03  ? 42  LEU G CD1 1 
ATOM   3643  C  CD2 . LEU D  1 42  ? -22.338 13.208  36.335  1.00 26.26  ? 42  LEU G CD2 1 
ATOM   3644  N  N   . HIS D  1 43  ? -23.770 16.164  32.911  1.00 23.66  ? 43  HIS G N   1 
ATOM   3645  C  CA  . HIS D  1 43  ? -23.601 16.943  31.673  1.00 23.08  ? 43  HIS G CA  1 
ATOM   3646  C  C   . HIS D  1 43  ? -22.148 17.249  31.403  1.00 22.61  ? 43  HIS G C   1 
ATOM   3647  O  O   . HIS D  1 43  ? -21.465 17.815  32.257  1.00 22.56  ? 43  HIS G O   1 
ATOM   3648  C  CB  . HIS D  1 43  ? -24.384 18.253  31.753  1.00 23.01  ? 43  HIS G CB  1 
ATOM   3649  C  CG  . HIS D  1 43  ? -25.856 18.043  31.788  1.00 23.60  ? 43  HIS G CG  1 
ATOM   3650  N  ND1 . HIS D  1 43  ? -26.604 17.909  30.642  1.00 23.84  ? 43  HIS G ND1 1 
ATOM   3651  C  CD2 . HIS D  1 43  ? -26.711 17.870  32.823  1.00 24.24  ? 43  HIS G CD2 1 
ATOM   3652  C  CE1 . HIS D  1 43  ? -27.864 17.691  30.965  1.00 24.62  ? 43  HIS G CE1 1 
ATOM   3653  N  NE2 . HIS D  1 43  ? -27.958 17.664  32.283  1.00 24.85  ? 43  HIS G NE2 1 
ATOM   3654  N  N   . GLY D  1 44  ? -21.687 16.887  30.207  1.00 22.46  ? 44  GLY G N   1 
ATOM   3655  C  CA  . GLY D  1 44  ? -20.351 17.211  29.735  1.00 22.16  ? 44  GLY G CA  1 
ATOM   3656  C  C   . GLY D  1 44  ? -20.049 18.689  29.879  1.00 21.83  ? 44  GLY G C   1 
ATOM   3657  O  O   . GLY D  1 44  ? -20.926 19.531  29.678  1.00 21.67  ? 44  GLY G O   1 
ATOM   3658  N  N   . PHE D  1 45  ? -18.811 18.989  30.273  1.00 21.80  ? 45  PHE G N   1 
ATOM   3659  C  CA  . PHE D  1 45  ? -18.415 20.342  30.652  1.00 21.74  ? 45  PHE G CA  1 
ATOM   3660  C  C   . PHE D  1 45  ? -16.990 20.538  30.155  1.00 21.84  ? 45  PHE G C   1 
ATOM   3661  O  O   . PHE D  1 45  ? -16.066 19.984  30.737  1.00 22.16  ? 45  PHE G O   1 
ATOM   3662  C  CB  . PHE D  1 45  ? -18.509 20.466  32.175  1.00 22.06  ? 45  PHE G CB  1 
ATOM   3663  C  CG  . PHE D  1 45  ? -18.400 21.870  32.707  1.00 22.17  ? 45  PHE G CG  1 
ATOM   3664  C  CD1 . PHE D  1 45  ? -19.353 22.821  32.398  1.00 22.11  ? 45  PHE G CD1 1 
ATOM   3665  C  CD2 . PHE D  1 45  ? -17.376 22.217  33.571  1.00 22.65  ? 45  PHE G CD2 1 
ATOM   3666  C  CE1 . PHE D  1 45  ? -19.275 24.101  32.908  1.00 22.39  ? 45  PHE G CE1 1 
ATOM   3667  C  CE2 . PHE D  1 45  ? -17.293 23.496  34.097  1.00 23.00  ? 45  PHE G CE2 1 
ATOM   3668  C  CZ  . PHE D  1 45  ? -18.254 24.438  33.763  1.00 22.85  ? 45  PHE G CZ  1 
ATOM   3669  N  N   . HIS D  1 46  ? -16.815 21.276  29.058  1.00 21.76  ? 46  HIS G N   1 
ATOM   3670  C  CA  . HIS D  1 46  ? -15.514 21.324  28.362  1.00 22.03  ? 46  HIS G CA  1 
ATOM   3671  C  C   . HIS D  1 46  ? -15.103 22.723  27.956  1.00 22.09  ? 46  HIS G C   1 
ATOM   3672  O  O   . HIS D  1 46  ? -15.961 23.585  27.709  1.00 22.00  ? 46  HIS G O   1 
ATOM   3673  C  CB  . HIS D  1 46  ? -15.536 20.462  27.101  1.00 22.23  ? 46  HIS G CB  1 
ATOM   3674  C  CG  . HIS D  1 46  ? -16.069 19.083  27.312  1.00 22.39  ? 46  HIS G CG  1 
ATOM   3675  N  ND1 . HIS D  1 46  ? -17.123 18.577  26.582  1.00 22.48  ? 46  HIS G ND1 1 
ATOM   3676  C  CD2 . HIS D  1 46  ? -15.692 18.100  28.163  1.00 22.69  ? 46  HIS G CD2 1 
ATOM   3677  C  CE1 . HIS D  1 46  ? -17.372 17.341  26.976  1.00 22.77  ? 46  HIS G CE1 1 
ATOM   3678  N  NE2 . HIS D  1 46  ? -16.517 17.026  27.933  1.00 22.86  ? 46  HIS G NE2 1 
ATOM   3679  N  N   . VAL D  1 47  ? -13.791 22.941  27.877  1.00 22.43  ? 47  VAL G N   1 
ATOM   3680  C  CA  . VAL D  1 47  ? -13.252 24.128  27.233  1.00 22.72  ? 47  VAL G CA  1 
ATOM   3681  C  C   . VAL D  1 47  ? -12.920 23.768  25.791  1.00 22.96  ? 47  VAL G C   1 
ATOM   3682  O  O   . VAL D  1 47  ? -12.114 22.861  25.536  1.00 23.25  ? 47  VAL G O   1 
ATOM   3683  C  CB  . VAL D  1 47  ? -12.018 24.698  27.949  1.00 23.30  ? 47  VAL G CB  1 
ATOM   3684  C  CG1 . VAL D  1 47  ? -11.536 25.951  27.241  1.00 23.75  ? 47  VAL G CG1 1 
ATOM   3685  C  CG2 . VAL D  1 47  ? -12.334 25.006  29.412  1.00 23.30  ? 47  VAL G CG2 1 
ATOM   3686  N  N   . HIS D  1 48  ? -13.564 24.474  24.860  1.00 23.00  ? 48  HIS G N   1 
ATOM   3687  C  CA  . HIS D  1 48  ? -13.338 24.282  23.431  1.00 23.54  ? 48  HIS G CA  1 
ATOM   3688  C  C   . HIS D  1 48  ? -12.328 25.292  22.920  1.00 24.26  ? 48  HIS G C   1 
ATOM   3689  O  O   . HIS D  1 48  ? -12.168 26.369  23.498  1.00 24.23  ? 48  HIS G O   1 
ATOM   3690  C  CB  . HIS D  1 48  ? -14.657 24.375  22.655  1.00 23.48  ? 48  HIS G CB  1 
ATOM   3691  C  CG  . HIS D  1 48  ? -15.541 23.189  22.853  1.00 23.09  ? 48  HIS G CG  1 
ATOM   3692  N  ND1 . HIS D  1 48  ? -15.864 22.326  21.831  1.00 23.50  ? 48  HIS G ND1 1 
ATOM   3693  C  CD2 . HIS D  1 48  ? -16.124 22.687  23.967  1.00 22.57  ? 48  HIS G CD2 1 
ATOM   3694  C  CE1 . HIS D  1 48  ? -16.635 21.362  22.298  1.00 23.22  ? 48  HIS G CE1 1 
ATOM   3695  N  NE2 . HIS D  1 48  ? -16.810 21.556  23.591  1.00 22.63  ? 48  HIS G NE2 1 
ATOM   3696  N  N   . GLU D  1 49  ? -11.671 24.943  21.821  1.00 25.07  ? 49  GLU G N   1 
ATOM   3697  C  CA  . GLU D  1 49  ? -10.467 25.644  21.382  1.00 26.07  ? 49  GLU G CA  1 
ATOM   3698  C  C   . GLU D  1 49  ? -10.664 27.140  21.112  1.00 26.47  ? 49  GLU G C   1 
ATOM   3699  O  O   . GLU D  1 49  ? -9.835  27.966  21.544  1.00 26.80  ? 49  GLU G O   1 
ATOM   3700  C  CB  . GLU D  1 49  ? -9.890  24.964  20.137  1.00 27.03  ? 49  GLU G CB  1 
ATOM   3701  C  CG  . GLU D  1 49  ? -8.565  25.532  19.690  1.00 28.18  ? 49  GLU G CG  1 
ATOM   3702  C  CD  . GLU D  1 49  ? -7.951  24.779  18.532  1.00 29.33  ? 49  GLU G CD  1 
ATOM   3703  O  OE1 . GLU D  1 49  ? -8.564  23.820  18.021  1.00 29.40  ? 49  GLU G OE1 1 
ATOM   3704  O  OE2 . GLU D  1 49  ? -6.852  25.175  18.120  1.00 30.42  ? 49  GLU G OE2 1 
ATOM   3705  N  N   . PHE D  1 50  ? -11.740 27.474  20.399  1.00 26.52  ? 50  PHE G N   1 
ATOM   3706  C  CA  . PHE D  1 50  ? -11.953 28.829  19.893  1.00 27.28  ? 50  PHE G CA  1 
ATOM   3707  C  C   . PHE D  1 50  ? -13.033 29.576  20.649  1.00 26.90  ? 50  PHE G C   1 
ATOM   3708  O  O   . PHE D  1 50  ? -14.068 28.999  20.990  1.00 26.29  ? 50  PHE G O   1 
ATOM   3709  C  CB  . PHE D  1 50  ? -12.296 28.791  18.395  1.00 28.13  ? 50  PHE G CB  1 
ATOM   3710  C  CG  . PHE D  1 50  ? -11.272 28.060  17.572  1.00 28.87  ? 50  PHE G CG  1 
ATOM   3711  C  CD1 . PHE D  1 50  ? -9.958  28.511  17.524  1.00 29.58  ? 50  PHE G CD1 1 
ATOM   3712  C  CD2 . PHE D  1 50  ? -11.607 26.898  16.881  1.00 28.99  ? 50  PHE G CD2 1 
ATOM   3713  C  CE1 . PHE D  1 50  ? -9.000  27.825  16.791  1.00 30.46  ? 50  PHE G CE1 1 
ATOM   3714  C  CE2 . PHE D  1 50  ? -10.652 26.211  16.150  1.00 29.86  ? 50  PHE G CE2 1 
ATOM   3715  C  CZ  . PHE D  1 50  ? -9.347  26.673  16.103  1.00 30.58  ? 50  PHE G CZ  1 
ATOM   3716  N  N   . GLY D  1 51  ? -12.798 30.868  20.870  1.00 27.61  ? 51  GLY G N   1 
ATOM   3717  C  CA  . GLY D  1 51  ? -13.772 31.777  21.465  1.00 27.74  ? 51  GLY G CA  1 
ATOM   3718  C  C   . GLY D  1 51  ? -14.590 32.453  20.390  1.00 28.78  ? 51  GLY G C   1 
ATOM   3719  O  O   . GLY D  1 51  ? -14.704 33.679  20.361  1.00 29.51  ? 51  GLY G O   1 
ATOM   3720  N  N   . ASP D  1 52  ? -15.159 31.633  19.510  1.00 29.11  ? 52  ASP G N   1 
ATOM   3721  C  CA  . ASP D  1 52  ? -15.835 32.081  18.307  1.00 30.42  ? 52  ASP G CA  1 
ATOM   3722  C  C   . ASP D  1 52  ? -17.288 31.623  18.456  1.00 30.36  ? 52  ASP G C   1 
ATOM   3723  O  O   . ASP D  1 52  ? -17.573 30.423  18.389  1.00 29.76  ? 52  ASP G O   1 
ATOM   3724  C  CB  . ASP D  1 52  ? -15.151 31.461  17.074  1.00 31.08  ? 52  ASP G CB  1 
ATOM   3725  C  CG  . ASP D  1 52  ? -15.743 31.941  15.748  1.00 32.49  ? 52  ASP G CG  1 
ATOM   3726  O  OD1 . ASP D  1 52  ? -16.888 32.444  15.723  1.00 32.75  ? 52  ASP G OD1 1 
ATOM   3727  O  OD2 . ASP D  1 52  ? -15.046 31.817  14.718  1.00 33.48  ? 52  ASP G OD2 1 
ATOM   3728  N  N   . ASN D  1 53  ? -18.175 32.587  18.710  1.00 31.24  ? 53  ASN G N   1 
ATOM   3729  C  CA  . ASN D  1 53  ? -19.618 32.355  18.836  1.00 31.68  ? 53  ASN G CA  1 
ATOM   3730  C  C   . ASN D  1 53  ? -20.406 32.924  17.646  1.00 33.33  ? 53  ASN G C   1 
ATOM   3731  O  O   . ASN D  1 53  ? -21.595 33.214  17.775  1.00 33.94  ? 53  ASN G O   1 
ATOM   3732  C  CB  . ASN D  1 53  ? -20.137 32.975  20.144  1.00 31.52  ? 53  ASN G CB  1 
ATOM   3733  C  CG  . ASN D  1 53  ? -21.423 32.332  20.635  1.00 31.43  ? 53  ASN G CG  1 
ATOM   3734  O  OD1 . ASN D  1 53  ? -22.470 32.969  20.676  1.00 32.44  ? 53  ASN G OD1 1 
ATOM   3735  N  ND2 . ASN D  1 53  ? -21.346 31.063  21.022  1.00 30.86  ? 53  ASN G ND2 1 
ATOM   3736  N  N   . THR D  1 54  ? -19.763 33.071  16.487  1.00 34.43  ? 54  THR G N   1 
ATOM   3737  C  CA  . THR D  1 54  ? -20.447 33.571  15.292  1.00 36.29  ? 54  THR G CA  1 
ATOM   3738  C  C   . THR D  1 54  ? -21.568 32.630  14.830  1.00 36.86  ? 54  THR G C   1 
ATOM   3739  O  O   . THR D  1 54  ? -22.606 33.095  14.359  1.00 38.16  ? 54  THR G O   1 
ATOM   3740  C  CB  . THR D  1 54  ? -19.479 33.808  14.122  1.00 37.35  ? 54  THR G CB  1 
ATOM   3741  O  OG1 . THR D  1 54  ? -18.695 32.632  13.897  1.00 36.60  ? 54  THR G OG1 1 
ATOM   3742  C  CG2 . THR D  1 54  ? -18.563 34.986  14.416  1.00 37.60  ? 54  THR G CG2 1 
ATOM   3743  N  N   . ALA D  1 55  ? -21.355 31.322  14.971  1.00 36.16  ? 55  ALA G N   1 
ATOM   3744  C  CA  . ALA D  1 55  ? -22.378 30.316  14.671  1.00 36.75  ? 55  ALA G CA  1 
ATOM   3745  C  C   . ALA D  1 55  ? -22.797 29.592  15.948  1.00 35.46  ? 55  ALA G C   1 
ATOM   3746  O  O   . ALA D  1 55  ? -22.952 28.364  15.957  1.00 35.42  ? 55  ALA G O   1 
ATOM   3747  C  CB  . ALA D  1 55  ? -21.851 29.330  13.634  1.00 37.37  ? 55  ALA G CB  1 
ATOM   3748  N  N   . GLY D  1 56  ? -22.982 30.350  17.032  1.00 34.75  ? 56  GLY G N   1 
ATOM   3749  C  CA  . GLY D  1 56  ? -23.302 29.766  18.334  1.00 33.36  ? 56  GLY G CA  1 
ATOM   3750  C  C   . GLY D  1 56  ? -22.149 28.927  18.868  1.00 31.94  ? 56  GLY G C   1 
ATOM   3751  O  O   . GLY D  1 56  ? -20.979 29.208  18.582  1.00 31.96  ? 56  GLY G O   1 
ATOM   3752  N  N   . ALA D  1 57  ? -22.485 27.894  19.636  1.00 30.83  ? 57  ALA G N   1 
ATOM   3753  C  CA  . ALA D  1 57  ? -21.500 26.972  20.191  1.00 29.64  ? 57  ALA G CA  1 
ATOM   3754  C  C   . ALA D  1 57  ? -20.738 26.166  19.119  1.00 29.82  ? 57  ALA G C   1 
ATOM   3755  O  O   . ALA D  1 57  ? -19.604 25.752  19.353  1.00 29.25  ? 57  ALA G O   1 
ATOM   3756  C  CB  . ALA D  1 57  ? -22.176 26.025  21.174  1.00 28.99  ? 57  ALA G CB  1 
ATOM   3757  N  N   . THR D  1 58  ? -21.370 25.923  17.972  1.00 30.66  ? 58  THR G N   1 
ATOM   3758  C  CA  . THR D  1 58  ? -20.748 25.177  16.863  1.00 31.20  ? 58  THR G CA  1 
ATOM   3759  C  C   . THR D  1 58  ? -19.377 25.718  16.420  1.00 31.12  ? 58  THR G C   1 
ATOM   3760  O  O   . THR D  1 58  ? -18.439 24.941  16.240  1.00 31.11  ? 58  THR G O   1 
ATOM   3761  C  CB  . THR D  1 58  ? -21.688 25.146  15.650  1.00 32.86  ? 58  THR G CB  1 
ATOM   3762  O  OG1 . THR D  1 58  ? -22.969 24.659  16.069  1.00 32.92  ? 58  THR G OG1 1 
ATOM   3763  C  CG2 . THR D  1 58  ? -21.135 24.245  14.532  1.00 33.86  ? 58  THR G CG2 1 
ATOM   3764  N  N   . SER D  1 59  ? -19.249 27.041  16.295  1.00 31.14  ? 59  SER G N   1 
ATOM   3765  C  CA  . SER D  1 59  ? -17.998 27.663  15.826  1.00 31.31  ? 59  SER G CA  1 
ATOM   3766  C  C   . SER D  1 59  ? -16.837 27.618  16.842  1.00 29.97  ? 59  SER G C   1 
ATOM   3767  O  O   . SER D  1 59  ? -15.718 28.002  16.511  1.00 30.41  ? 59  SER G O   1 
ATOM   3768  C  CB  . SER D  1 59  ? -18.255 29.110  15.340  1.00 32.31  ? 59  SER G CB  1 
ATOM   3769  O  OG  . SER D  1 59  ? -19.051 29.849  16.255  1.00 31.82  ? 59  SER G OG  1 
ATOM   3770  N  N   . ALA D  1 60  ? -17.092 27.128  18.056  1.00 28.55  ? 60  ALA G N   1 
ATOM   3771  C  CA  . ALA D  1 60  ? -16.056 26.975  19.080  1.00 27.55  ? 60  ALA G CA  1 
ATOM   3772  C  C   . ALA D  1 60  ? -15.019 25.897  18.775  1.00 27.43  ? 60  ALA G C   1 
ATOM   3773  O  O   . ALA D  1 60  ? -14.000 25.817  19.464  1.00 27.01  ? 60  ALA G O   1 
ATOM   3774  C  CB  . ALA D  1 60  ? -16.699 26.695  20.430  1.00 26.58  ? 60  ALA G CB  1 
ATOM   3775  N  N   . GLY D  1 61  ? -15.277 25.055  17.775  1.00 27.85  ? 61  GLY G N   1 
ATOM   3776  C  CA  . GLY D  1 61  ? -14.319 24.029  17.371  1.00 28.10  ? 61  GLY G CA  1 
ATOM   3777  C  C   . GLY D  1 61  ? -14.288 22.876  18.359  1.00 27.14  ? 61  GLY G C   1 
ATOM   3778  O  O   . GLY D  1 61  ? -15.233 22.688  19.134  1.00 26.40  ? 61  GLY G O   1 
ATOM   3779  N  N   . PRO D  1 62  ? -13.209 22.082  18.331  1.00 27.30  ? 62  PRO G N   1 
ATOM   3780  C  CA  . PRO D  1 62  ? -13.133 20.913  19.193  1.00 26.68  ? 62  PRO G CA  1 
ATOM   3781  C  C   . PRO D  1 62  ? -12.652 21.266  20.596  1.00 25.79  ? 62  PRO G C   1 
ATOM   3782  O  O   . PRO D  1 62  ? -12.407 22.442  20.900  1.00 25.60  ? 62  PRO G O   1 
ATOM   3783  C  CB  . PRO D  1 62  ? -12.122 20.033  18.473  1.00 27.71  ? 62  PRO G CB  1 
ATOM   3784  C  CG  . PRO D  1 62  ? -11.191 21.002  17.838  1.00 28.45  ? 62  PRO G CG  1 
ATOM   3785  C  CD  . PRO D  1 62  ? -12.043 22.175  17.433  1.00 28.36  ? 62  PRO G CD  1 
ATOM   3786  N  N   . HIS D  1 63  ? -12.529 20.252  21.443  1.00 25.34  ? 63  HIS G N   1 
ATOM   3787  C  CA  . HIS D  1 63  ? -11.983 20.448  22.787  1.00 24.85  ? 63  HIS G CA  1 
ATOM   3788  C  C   . HIS D  1 63  ? -10.576 21.021  22.682  1.00 25.34  ? 63  HIS G C   1 
ATOM   3789  O  O   . HIS D  1 63  ? -9.834  20.649  21.796  1.00 26.06  ? 63  HIS G O   1 
ATOM   3790  C  CB  . HIS D  1 63  ? -11.938 19.137  23.555  1.00 24.87  ? 63  HIS G CB  1 
ATOM   3791  C  CG  . HIS D  1 63  ? -13.285 18.546  23.816  1.00 24.43  ? 63  HIS G CG  1 
ATOM   3792  N  ND1 . HIS D  1 63  ? -13.451 17.326  24.424  1.00 24.53  ? 63  HIS G ND1 1 
ATOM   3793  C  CD2 . HIS D  1 63  ? -14.530 18.995  23.524  1.00 24.06  ? 63  HIS G CD2 1 
ATOM   3794  C  CE1 . HIS D  1 63  ? -14.740 17.058  24.525  1.00 24.21  ? 63  HIS G CE1 1 
ATOM   3795  N  NE2 . HIS D  1 63  ? -15.415 18.051  23.972  1.00 23.93  ? 63  HIS G NE2 1 
ATOM   3796  N  N   . PHE D  1 64  ? -10.250 21.964  23.563  1.00 25.04  ? 64  PHE G N   1 
ATOM   3797  C  CA  . PHE D  1 64  ? -8.931  22.597  23.602  1.00 25.68  ? 64  PHE G CA  1 
ATOM   3798  C  C   . PHE D  1 64  ? -7.912  21.504  23.879  1.00 26.33  ? 64  PHE G C   1 
ATOM   3799  O  O   . PHE D  1 64  ? -8.030  20.792  24.882  1.00 26.06  ? 64  PHE G O   1 
ATOM   3800  C  CB  . PHE D  1 64  ? -8.932  23.692  24.675  1.00 25.40  ? 64  PHE G CB  1 
ATOM   3801  C  CG  . PHE D  1 64  ? -7.620  24.400  24.861  1.00 26.29  ? 64  PHE G CG  1 
ATOM   3802  C  CD1 . PHE D  1 64  ? -6.859  24.820  23.776  1.00 27.13  ? 64  PHE G CD1 1 
ATOM   3803  C  CD2 . PHE D  1 64  ? -7.176  24.700  26.148  1.00 26.49  ? 64  PHE G CD2 1 
ATOM   3804  C  CE1 . PHE D  1 64  ? -5.652  25.479  23.979  1.00 28.17  ? 64  PHE G CE1 1 
ATOM   3805  C  CE2 . PHE D  1 64  ? -5.983  25.373  26.357  1.00 27.57  ? 64  PHE G CE2 1 
ATOM   3806  C  CZ  . PHE D  1 64  ? -5.220  25.765  25.272  1.00 28.37  ? 64  PHE G CZ  1 
ATOM   3807  N  N   . ASN D  1 65  ? -6.964  21.334  22.954  1.00 27.25  ? 65  ASN G N   1 
ATOM   3808  C  CA  . ASN D  1 65  ? -6.096  20.158  22.925  1.00 28.13  ? 65  ASN G CA  1 
ATOM   3809  C  C   . ASN D  1 65  ? -4.690  20.506  22.384  1.00 29.53  ? 65  ASN G C   1 
ATOM   3810  O  O   . ASN D  1 65  ? -4.258  19.942  21.391  1.00 30.37  ? 65  ASN G O   1 
ATOM   3811  C  CB  . ASN D  1 65  ? -6.763  19.062  22.081  1.00 28.05  ? 65  ASN G CB  1 
ATOM   3812  C  CG  . ASN D  1 65  ? -6.055  17.717  22.171  1.00 28.95  ? 65  ASN G CG  1 
ATOM   3813  O  OD1 . ASN D  1 65  ? -5.335  17.427  23.126  1.00 29.31  ? 65  ASN G OD1 1 
ATOM   3814  N  ND2 . ASN D  1 65  ? -6.270  16.880  21.169  1.00 29.47  ? 65  ASN G ND2 1 
ATOM   3815  N  N   . PRO D  1 66  ? -3.977  21.433  23.054  1.00 29.97  ? 66  PRO G N   1 
ATOM   3816  C  CA  . PRO D  1 66  ? -2.655  21.864  22.582  1.00 31.54  ? 66  PRO G CA  1 
ATOM   3817  C  C   . PRO D  1 66  ? -1.577  20.771  22.583  1.00 32.98  ? 66  PRO G C   1 
ATOM   3818  O  O   . PRO D  1 66  ? -0.572  20.926  21.898  1.00 34.34  ? 66  PRO G O   1 
ATOM   3819  C  CB  . PRO D  1 66  ? -2.270  22.986  23.554  1.00 31.61  ? 66  PRO G CB  1 
ATOM   3820  C  CG  . PRO D  1 66  ? -3.053  22.705  24.789  1.00 30.53  ? 66  PRO G CG  1 
ATOM   3821  C  CD  . PRO D  1 66  ? -4.331  22.053  24.347  1.00 29.30  ? 66  PRO G CD  1 
ATOM   3822  N  N   . LEU D  1 67  ? -1.778  19.703  23.354  1.00 32.90  ? 67  LEU G N   1 
ATOM   3823  C  CA  . LEU D  1 67  ? -0.831  18.584  23.415  1.00 34.47  ? 67  LEU G CA  1 
ATOM   3824  C  C   . LEU D  1 67  ? -1.214  17.397  22.517  1.00 34.63  ? 67  LEU G C   1 
ATOM   3825  O  O   . LEU D  1 67  ? -0.552  16.357  22.563  1.00 35.78  ? 67  LEU G O   1 
ATOM   3826  C  CB  . LEU D  1 67  ? -0.662  18.135  24.880  1.00 34.69  ? 67  LEU G CB  1 
ATOM   3827  C  CG  . LEU D  1 67  ? -0.019  19.187  25.801  1.00 35.25  ? 67  LEU G CG  1 
ATOM   3828  C  CD1 . LEU D  1 67  ? -0.060  18.731  27.253  1.00 35.46  ? 67  LEU G CD1 1 
ATOM   3829  C  CD2 . LEU D  1 67  ? 1.410   19.512  25.389  1.00 37.15  ? 67  LEU G CD2 1 
ATOM   3830  N  N   . SER D  1 68  ? -2.256  17.557  21.693  1.00 33.70  ? 68  SER G N   1 
ATOM   3831  C  CA  . SER D  1 68  ? -2.680  16.539  20.720  1.00 34.08  ? 68  SER G CA  1 
ATOM   3832  C  C   . SER D  1 68  ? -2.879  15.152  21.350  1.00 34.29  ? 68  SER G C   1 
ATOM   3833  O  O   . SER D  1 68  ? -2.429  14.132  20.815  1.00 35.44  ? 68  SER G O   1 
ATOM   3834  C  CB  . SER D  1 68  ? -1.695  16.486  19.542  1.00 35.84  ? 68  SER G CB  1 
ATOM   3835  O  OG  . SER D  1 68  ? -1.521  17.768  18.953  1.00 35.89  ? 68  SER G OG  1 
ATOM   3836  N  N   . ARG D  1 69  ? -3.567  15.139  22.494  1.00 33.27  ? 69  ARG G N   1 
ATOM   3837  C  CA  . ARG D  1 69  ? -3.879  13.919  23.232  1.00 33.50  ? 69  ARG G CA  1 
ATOM   3838  C  C   . ARG D  1 69  ? -5.287  13.415  22.872  1.00 32.41  ? 69  ARG G C   1 
ATOM   3839  O  O   . ARG D  1 69  ? -6.033  14.083  22.155  1.00 31.50  ? 69  ARG G O   1 
ATOM   3840  C  CB  . ARG D  1 69  ? -3.816  14.211  24.736  1.00 33.36  ? 69  ARG G CB  1 
ATOM   3841  C  CG  . ARG D  1 69  ? -2.465  14.717  25.251  1.00 34.84  ? 69  ARG G CG  1 
ATOM   3842  C  CD  . ARG D  1 69  ? -1.648  13.584  25.840  1.00 36.65  ? 69  ARG G CD  1 
ATOM   3843  N  NE  . ARG D  1 69  ? -0.292  13.958  26.258  1.00 38.48  ? 69  ARG G NE  1 
ATOM   3844  C  CZ  . ARG D  1 69  ? 0.107   14.347  27.481  1.00 39.00  ? 69  ARG G CZ  1 
ATOM   3845  N  NH1 . ARG D  1 69  ? -0.747  14.501  28.491  1.00 38.06  ? 69  ARG G NH1 1 
ATOM   3846  N  NH2 . ARG D  1 69  ? 1.403   14.624  27.679  1.00 40.83  ? 69  ARG G NH2 1 
ATOM   3847  N  N   . LYS D  1 70  ? -5.639  12.235  23.382  1.00 32.53  ? 70  LYS G N   1 
ATOM   3848  C  CA  . LYS D  1 70  ? -7.012  11.715  23.297  1.00 31.64  ? 70  LYS G CA  1 
ATOM   3849  C  C   . LYS D  1 70  ? -7.879  12.248  24.425  1.00 30.12  ? 70  LYS G C   1 
ATOM   3850  O  O   . LYS D  1 70  ? -7.378  12.672  25.466  1.00 29.91  ? 70  LYS G O   1 
ATOM   3851  C  CB  . LYS D  1 70  ? -7.018  10.188  23.331  1.00 32.81  ? 70  LYS G CB  1 
ATOM   3852  C  CG  . LYS D  1 70  ? -6.439  9.570   22.073  1.00 34.36  ? 70  LYS G CG  1 
ATOM   3853  C  CD  . LYS D  1 70  ? -6.559  8.056   22.090  1.00 35.64  ? 70  LYS G CD  1 
ATOM   3854  C  CE  . LYS D  1 70  ? -5.740  7.440   23.218  1.00 36.59  ? 70  LYS G CE  1 
ATOM   3855  N  NZ  . LYS D  1 70  ? -5.128  6.147   22.827  1.00 38.63  ? 70  LYS G NZ  1 
ATOM   3856  N  N   . HIS D  1 71  ? -9.191  12.210  24.204  1.00 29.13  ? 71  HIS G N   1 
ATOM   3857  C  CA  . HIS D  1 71  ? -10.173 12.635  25.203  1.00 27.94  ? 71  HIS G CA  1 
ATOM   3858  C  C   . HIS D  1 71  ? -10.143 11.732  26.435  1.00 28.36  ? 71  HIS G C   1 
ATOM   3859  O  O   . HIS D  1 71  ? -10.025 10.519  26.311  1.00 29.26  ? 71  HIS G O   1 
ATOM   3860  C  CB  . HIS D  1 71  ? -11.587 12.605  24.622  1.00 27.24  ? 71  HIS G CB  1 
ATOM   3861  C  CG  . HIS D  1 71  ? -12.634 13.080  25.578  1.00 26.19  ? 71  HIS G CG  1 
ATOM   3862  N  ND1 . HIS D  1 71  ? -12.796 14.409  25.898  1.00 25.33  ? 71  HIS G ND1 1 
ATOM   3863  C  CD2 . HIS D  1 71  ? -13.541 12.397  26.317  1.00 26.02  ? 71  HIS G CD2 1 
ATOM   3864  C  CE1 . HIS D  1 71  ? -13.779 14.526  26.777  1.00 24.76  ? 71  HIS G CE1 1 
ATOM   3865  N  NE2 . HIS D  1 71  ? -14.241 13.320  27.054  1.00 25.14  ? 71  HIS G NE2 1 
ATOM   3866  N  N   . GLY D  1 72  ? -10.269 12.343  27.609  1.00 27.91  ? 72  GLY G N   1 
ATOM   3867  C  CA  . GLY D  1 72  ? -10.376 11.617  28.874  1.00 28.41  ? 72  GLY G CA  1 
ATOM   3868  C  C   . GLY D  1 72  ? -11.142 12.422  29.911  1.00 27.63  ? 72  GLY G C   1 
ATOM   3869  O  O   . GLY D  1 72  ? -11.707 13.477  29.610  1.00 26.71  ? 72  GLY G O   1 
ATOM   3870  N  N   . GLY D  1 73  ? -11.178 11.910  31.132  1.00 28.26  ? 73  GLY G N   1 
ATOM   3871  C  CA  . GLY D  1 73  ? -11.692 12.667  32.265  1.00 27.90  ? 73  GLY G CA  1 
ATOM   3872  C  C   . GLY D  1 73  ? -10.604 13.542  32.868  1.00 28.43  ? 73  GLY G C   1 
ATOM   3873  O  O   . GLY D  1 73  ? -9.415  13.336  32.595  1.00 29.26  ? 73  GLY G O   1 
ATOM   3874  N  N   . PRO D  1 74  ? -10.991 14.517  33.715  1.00 28.20  ? 74  PRO G N   1 
ATOM   3875  C  CA  . PRO D  1 74  ? -9.995  15.405  34.328  1.00 28.85  ? 74  PRO G CA  1 
ATOM   3876  C  C   . PRO D  1 74  ? -8.936  14.708  35.187  1.00 30.56  ? 74  PRO G C   1 
ATOM   3877  O  O   . PRO D  1 74  ? -7.855  15.251  35.356  1.00 31.28  ? 74  PRO G O   1 
ATOM   3878  C  CB  . PRO D  1 74  ? -10.838 16.356  35.192  1.00 28.39  ? 74  PRO G CB  1 
ATOM   3879  C  CG  . PRO D  1 74  ? -12.140 15.663  35.381  1.00 27.93  ? 74  PRO G CG  1 
ATOM   3880  C  CD  . PRO D  1 74  ? -12.361 14.860  34.135  1.00 27.43  ? 74  PRO G CD  1 
ATOM   3881  N  N   . LYS D  1 75  ? -9.250  13.528  35.717  1.00 31.37  ? 75  LYS G N   1 
ATOM   3882  C  CA  . LYS D  1 75  ? -8.302  12.759  36.525  1.00 33.27  ? 75  LYS G CA  1 
ATOM   3883  C  C   . LYS D  1 75  ? -7.267  11.979  35.684  1.00 34.14  ? 75  LYS G C   1 
ATOM   3884  O  O   . LYS D  1 75  ? -6.286  11.499  36.235  1.00 35.72  ? 75  LYS G O   1 
ATOM   3885  C  CB  . LYS D  1 75  ? -9.046  11.785  37.446  1.00 34.00  ? 75  LYS G CB  1 
ATOM   3886  C  CG  . LYS D  1 75  ? -9.985  12.446  38.457  1.00 33.79  ? 75  LYS G CG  1 
ATOM   3887  C  CD  . LYS D  1 75  ? -10.904 11.434  39.139  1.00 34.39  ? 75  LYS G CD  1 
ATOM   3888  C  CE  . LYS D  1 75  ? -10.147 10.446  40.014  1.00 36.51  ? 75  LYS G CE  1 
ATOM   3889  N  NZ  . LYS D  1 75  ? -11.076 9.510   40.714  1.00 37.22  ? 75  LYS G NZ  1 
ATOM   3890  N  N   . ASP D  1 76  ? -7.484  11.841  34.372  1.00 33.30  ? 76  ASP G N   1 
ATOM   3891  C  CA  . ASP D  1 76  ? -6.576  11.066  33.522  1.00 34.32  ? 76  ASP G CA  1 
ATOM   3892  C  C   . ASP D  1 76  ? -5.351  11.874  33.095  1.00 34.92  ? 76  ASP G C   1 
ATOM   3893  O  O   . ASP D  1 76  ? -5.438  13.106  32.928  1.00 34.05  ? 76  ASP G O   1 
ATOM   3894  C  CB  . ASP D  1 76  ? -7.275  10.581  32.249  1.00 33.44  ? 76  ASP G CB  1 
ATOM   3895  C  CG  . ASP D  1 76  ? -8.458  9.680   32.530  1.00 33.22  ? 76  ASP G CG  1 
ATOM   3896  O  OD1 . ASP D  1 76  ? -8.295  8.699   33.269  1.00 34.47  ? 76  ASP G OD1 1 
ATOM   3897  O  OD2 . ASP D  1 76  ? -9.559  9.954   32.008  1.00 31.97  ? 76  ASP G OD2 1 
ATOM   3898  N  N   . GLU D  1 77  ? -4.233  11.164  32.916  1.00 36.52  ? 77  GLU G N   1 
ATOM   3899  C  CA  A GLU D  1 77  ? -3.047  11.743  32.282  0.50 37.28  ? 77  GLU G CA  1 
ATOM   3900  C  CA  B GLU D  1 77  ? -3.035  11.709  32.275  0.50 37.33  ? 77  GLU G CA  1 
ATOM   3901  C  C   . GLU D  1 77  ? -3.348  11.975  30.802  1.00 36.17  ? 77  GLU G C   1 
ATOM   3902  O  O   . GLU D  1 77  ? -3.056  13.049  30.277  1.00 35.74  ? 77  GLU G O   1 
ATOM   3903  C  CB  A GLU D  1 77  ? -1.806  10.856  32.451  0.50 39.57  ? 77  GLU G CB  1 
ATOM   3904  C  CB  B GLU D  1 77  ? -1.853  10.732  32.389  0.50 39.63  ? 77  GLU G CB  1 
ATOM   3905  C  CG  A GLU D  1 77  ? -0.506  11.518  31.992  0.50 40.71  ? 77  GLU G CG  1 
ATOM   3906  C  CG  B GLU D  1 77  ? -1.316  10.522  33.801  0.50 41.29  ? 77  GLU G CG  1 
ATOM   3907  C  CD  A GLU D  1 77  ? 0.735   10.722  32.355  0.50 43.29  ? 77  GLU G CD  1 
ATOM   3908  C  CD  B GLU D  1 77  ? -0.677  9.152   33.999  0.50 43.43  ? 77  GLU G CD  1 
ATOM   3909  O  OE1 A GLU D  1 77  ? 0.707   9.990   33.368  0.50 44.41  ? 77  GLU G OE1 1 
ATOM   3910  O  OE1 B GLU D  1 77  ? 0.310   8.828   33.303  0.50 44.77  ? 77  GLU G OE1 1 
ATOM   3911  O  OE2 A GLU D  1 77  ? 1.753   10.832  31.636  0.50 44.49  ? 77  GLU G OE2 1 
ATOM   3912  O  OE2 B GLU D  1 77  ? -1.154  8.391   34.868  0.50 44.00  ? 77  GLU G OE2 1 
ATOM   3913  N  N   . GLU D  1 78  ? -3.944  10.977  30.147  1.00 35.80  ? 78  GLU G N   1 
ATOM   3914  C  CA  . GLU D  1 78  ? -4.398  11.105  28.762  1.00 34.77  ? 78  GLU G CA  1 
ATOM   3915  C  C   . GLU D  1 78  ? -5.742  11.862  28.723  1.00 32.61  ? 78  GLU G C   1 
ATOM   3916  O  O   . GLU D  1 78  ? -6.817  11.299  28.952  1.00 32.08  ? 78  GLU G O   1 
ATOM   3917  C  CB  . GLU D  1 78  ? -4.507  9.729   28.088  1.00 35.67  ? 78  GLU G CB  1 
ATOM   3918  C  CG  . GLU D  1 78  ? -4.749  9.760   26.576  1.00 35.42  ? 78  GLU G CG  1 
ATOM   3919  C  CD  . GLU D  1 78  ? -3.553  10.244  25.757  1.00 36.43  ? 78  GLU G CD  1 
ATOM   3920  O  OE1 . GLU D  1 78  ? -2.410  10.300  26.268  1.00 37.73  ? 78  GLU G OE1 1 
ATOM   3921  O  OE2 . GLU D  1 78  ? -3.754  10.563  24.565  1.00 36.22  ? 78  GLU G OE2 1 
ATOM   3922  N  N   . ARG D  1 79  ? -5.651  13.159  28.468  1.00 31.55  ? 79  ARG G N   1 
ATOM   3923  C  CA  . ARG D  1 79  ? -6.814  14.015  28.335  1.00 29.79  ? 79  ARG G CA  1 
ATOM   3924  C  C   . ARG D  1 79  ? -6.470  15.220  27.479  1.00 29.27  ? 79  ARG G C   1 
ATOM   3925  O  O   . ARG D  1 79  ? -5.298  15.586  27.322  1.00 30.04  ? 79  ARG G O   1 
ATOM   3926  C  CB  . ARG D  1 79  ? -7.317  14.496  29.703  1.00 29.26  ? 79  ARG G CB  1 
ATOM   3927  C  CG  . ARG D  1 79  ? -6.285  15.264  30.514  1.00 30.03  ? 79  ARG G CG  1 
ATOM   3928  C  CD  . ARG D  1 79  ? -6.877  15.855  31.783  1.00 29.65  ? 79  ARG G CD  1 
ATOM   3929  N  NE  . ARG D  1 79  ? -7.392  17.202  31.561  1.00 28.63  ? 79  ARG G NE  1 
ATOM   3930  C  CZ  . ARG D  1 79  ? -7.770  18.039  32.521  1.00 28.45  ? 79  ARG G CZ  1 
ATOM   3931  N  NH1 . ARG D  1 79  ? -7.718  17.689  33.807  1.00 29.27  ? 79  ARG G NH1 1 
ATOM   3932  N  NH2 . ARG D  1 79  ? -8.179  19.249  32.195  1.00 27.71  ? 79  ARG G NH2 1 
ATOM   3933  N  N   . HIS D  1 80  ? -7.511  15.830  26.941  1.00 27.87  ? 80  HIS G N   1 
ATOM   3934  C  CA  . HIS D  1 80  ? -7.423  17.165  26.372  1.00 27.41  ? 80  HIS G CA  1 
ATOM   3935  C  C   . HIS D  1 80  ? -7.292  18.157  27.534  1.00 27.13  ? 80  HIS G C   1 
ATOM   3936  O  O   . HIS D  1 80  ? -7.834  17.913  28.629  1.00 26.79  ? 80  HIS G O   1 
ATOM   3937  C  CB  . HIS D  1 80  ? -8.692  17.480  25.550  1.00 26.41  ? 80  HIS G CB  1 
ATOM   3938  C  CG  . HIS D  1 80  ? -8.946  16.516  24.430  1.00 26.78  ? 80  HIS G CG  1 
ATOM   3939  N  ND1 . HIS D  1 80  ? -10.202 16.235  23.943  1.00 26.22  ? 80  HIS G ND1 1 
ATOM   3940  C  CD2 . HIS D  1 80  ? -8.085  15.791  23.680  1.00 27.89  ? 80  HIS G CD2 1 
ATOM   3941  C  CE1 . HIS D  1 80  ? -10.104 15.366  22.954  1.00 26.99  ? 80  HIS G CE1 1 
ATOM   3942  N  NE2 . HIS D  1 80  ? -8.828  15.088  22.767  1.00 27.97  ? 80  HIS G NE2 1 
ATOM   3943  N  N   . VAL D  1 81  ? -6.592  19.269  27.317  1.00 27.35  ? 81  VAL G N   1 
ATOM   3944  C  CA  . VAL D  1 81  ? -6.527  20.326  28.335  1.00 27.28  ? 81  VAL G CA  1 
ATOM   3945  C  C   . VAL D  1 81  ? -7.938  20.804  28.739  1.00 26.08  ? 81  VAL G C   1 
ATOM   3946  O  O   . VAL D  1 81  ? -8.203  21.061  29.910  1.00 25.97  ? 81  VAL G O   1 
ATOM   3947  C  CB  . VAL D  1 81  ? -5.658  21.521  27.880  1.00 27.87  ? 81  VAL G CB  1 
ATOM   3948  C  CG1 . VAL D  1 81  ? -5.840  22.727  28.795  1.00 27.76  ? 81  VAL G CG1 1 
ATOM   3949  C  CG2 . VAL D  1 81  ? -4.191  21.122  27.847  1.00 29.38  ? 81  VAL G CG2 1 
ATOM   3950  N  N   . GLY D  1 82  ? -8.837  20.906  27.766  1.00 25.32  ? 82  GLY G N   1 
ATOM   3951  C  CA  . GLY D  1 82  ? -10.198 21.323  28.030  1.00 24.41  ? 82  GLY G CA  1 
ATOM   3952  C  C   . GLY D  1 82  ? -11.138 20.317  28.677  1.00 24.03  ? 82  GLY G C   1 
ATOM   3953  O  O   . GLY D  1 82  ? -12.303 20.652  28.880  1.00 23.37  ? 82  GLY G O   1 
ATOM   3954  N  N   . ASP D  1 83  ? -10.668 19.103  28.986  1.00 24.55  ? 83  ASP G N   1 
ATOM   3955  C  CA  . ASP D  1 83  ? -11.527 18.034  29.535  1.00 24.39  ? 83  ASP G CA  1 
ATOM   3956  C  C   . ASP D  1 83  ? -11.806 18.181  31.042  1.00 24.61  ? 83  ASP G C   1 
ATOM   3957  O  O   . ASP D  1 83  ? -11.126 17.566  31.891  1.00 25.33  ? 83  ASP G O   1 
ATOM   3958  C  CB  . ASP D  1 83  ? -10.920 16.649  29.261  1.00 25.03  ? 83  ASP G CB  1 
ATOM   3959  C  CG  . ASP D  1 83  ? -10.959 16.245  27.787  1.00 25.01  ? 83  ASP G CG  1 
ATOM   3960  O  OD1 . ASP D  1 83  ? -11.707 16.842  26.954  1.00 24.31  ? 83  ASP G OD1 1 
ATOM   3961  O  OD2 . ASP D  1 83  ? -10.221 15.281  27.440  1.00 25.72  ? 83  ASP G OD2 1 
ATOM   3962  N  N   . LEU D  1 84  ? -12.837 18.962  31.372  1.00 24.16  ? 84  LEU G N   1 
ATOM   3963  C  CA  . LEU D  1 84  ? -13.219 19.181  32.760  1.00 24.53  ? 84  LEU G CA  1 
ATOM   3964  C  C   . LEU D  1 84  ? -14.254 18.190  33.286  1.00 24.57  ? 84  LEU G C   1 
ATOM   3965  O  O   . LEU D  1 84  ? -14.713 18.327  34.421  1.00 24.99  ? 84  LEU G O   1 
ATOM   3966  C  CB  . LEU D  1 84  ? -13.678 20.634  32.980  1.00 24.31  ? 84  LEU G CB  1 
ATOM   3967  C  CG  . LEU D  1 84  ? -12.593 21.691  32.744  1.00 24.67  ? 84  LEU G CG  1 
ATOM   3968  C  CD1 . LEU D  1 84  ? -13.201 23.082  32.778  1.00 24.47  ? 84  LEU G CD1 1 
ATOM   3969  C  CD2 . LEU D  1 84  ? -11.470 21.580  33.768  1.00 25.78  ? 84  LEU G CD2 1 
ATOM   3970  N  N   . GLY D  1 85  ? -14.614 17.187  32.483  1.00 24.36  ? 85  GLY G N   1 
ATOM   3971  C  CA  . GLY D  1 85  ? -15.470 16.094  32.945  1.00 24.51  ? 85  GLY G CA  1 
ATOM   3972  C  C   . GLY D  1 85  ? -16.962 16.380  32.887  1.00 23.92  ? 85  GLY G C   1 
ATOM   3973  O  O   . GLY D  1 85  ? -17.475 16.897  31.897  1.00 23.48  ? 85  GLY G O   1 
ATOM   3974  N  N   . ASN D  1 86  ? -17.659 16.004  33.947  1.00 24.18  ? 86  ASN G N   1 
ATOM   3975  C  CA  . ASN D  1 86  ? -19.092 16.245  34.075  1.00 23.88  ? 86  ASN G CA  1 
ATOM   3976  C  C   . ASN D  1 86  ? -19.396 17.243  35.171  1.00 23.97  ? 86  ASN G C   1 
ATOM   3977  O  O   . ASN D  1 86  ? -18.602 17.442  36.094  1.00 24.37  ? 86  ASN G O   1 
ATOM   3978  C  CB  . ASN D  1 86  ? -19.818 14.929  34.361  1.00 24.40  ? 86  ASN G CB  1 
ATOM   3979  C  CG  . ASN D  1 86  ? -19.899 14.052  33.137  1.00 24.33  ? 86  ASN G CG  1 
ATOM   3980  O  OD1 . ASN D  1 86  ? -20.415 14.481  32.108  1.00 23.87  ? 86  ASN G OD1 1 
ATOM   3981  N  ND2 . ASN D  1 86  ? -19.396 12.822  33.234  1.00 24.92  ? 86  ASN G ND2 1 
ATOM   3982  N  N   . VAL D  1 87  ? -20.564 17.868  35.030  1.00 23.66  ? 87  VAL G N   1 
ATOM   3983  C  CA  . VAL D  1 87  ? -21.210 18.614  36.093  1.00 24.04  ? 87  VAL G CA  1 
ATOM   3984  C  C   . VAL D  1 87  ? -22.583 17.986  36.302  1.00 24.34  ? 87  VAL G C   1 
ATOM   3985  O  O   . VAL D  1 87  ? -23.181 17.478  35.352  1.00 24.15  ? 87  VAL G O   1 
ATOM   3986  C  CB  . VAL D  1 87  ? -21.284 20.137  35.807  1.00 23.75  ? 87  VAL G CB  1 
ATOM   3987  C  CG1 . VAL D  1 87  ? -19.873 20.734  35.770  1.00 23.65  ? 87  VAL G CG1 1 
ATOM   3988  C  CG2 . VAL D  1 87  ? -22.036 20.456  34.526  1.00 23.26  ? 87  VAL G CG2 1 
ATOM   3989  N  N   . THR D  1 88  ? -23.069 18.009  37.541  1.00 24.99  ? 88  THR G N   1 
ATOM   3990  C  CA  . THR D  1 88  ? -24.317 17.355  37.897  1.00 25.57  ? 88  THR G CA  1 
ATOM   3991  C  C   . THR D  1 88  ? -25.401 18.383  38.214  1.00 25.87  ? 88  THR G C   1 
ATOM   3992  O  O   . THR D  1 88  ? -25.230 19.220  39.100  1.00 26.27  ? 88  THR G O   1 
ATOM   3993  C  CB  . THR D  1 88  ? -24.122 16.412  39.100  1.00 26.57  ? 88  THR G CB  1 
ATOM   3994  O  OG1 . THR D  1 88  ? -23.150 15.407  38.772  1.00 26.36  ? 88  THR G OG1 1 
ATOM   3995  C  CG2 . THR D  1 88  ? -25.433 15.733  39.488  1.00 27.42  ? 88  THR G CG2 1 
ATOM   3996  N  N   . ALA D  1 89  ? -26.507 18.298  37.474  1.00 25.77  ? 89  ALA G N   1 
ATOM   3997  C  CA  . ALA D  1 89  ? -27.715 19.065  37.760  1.00 26.43  ? 89  ALA G CA  1 
ATOM   3998  C  C   . ALA D  1 89  ? -28.577 18.315  38.781  1.00 27.62  ? 89  ALA G C   1 
ATOM   3999  O  O   . ALA D  1 89  ? -28.770 17.106  38.671  1.00 27.84  ? 89  ALA G O   1 
ATOM   4000  C  CB  . ALA D  1 89  ? -28.501 19.322  36.481  1.00 26.09  ? 89  ALA G CB  1 
ATOM   4001  N  N   . ASP D  1 90  ? -29.080 19.043  39.772  1.00 28.57  ? 90  ASP G N   1 
ATOM   4002  C  CA  . ASP D  1 90  ? -29.927 18.469  40.819  1.00 30.04  ? 90  ASP G CA  1 
ATOM   4003  C  C   . ASP D  1 90  ? -31.383 18.329  40.311  1.00 30.71  ? 90  ASP G C   1 
ATOM   4004  O  O   . ASP D  1 90  ? -31.672 18.617  39.151  1.00 29.99  ? 90  ASP G O   1 
ATOM   4005  C  CB  . ASP D  1 90  ? -29.820 19.303  42.117  1.00 31.06  ? 90  ASP G CB  1 
ATOM   4006  C  CG  . ASP D  1 90  ? -30.443 20.717  42.007  1.00 31.37  ? 90  ASP G CG  1 
ATOM   4007  O  OD1 . ASP D  1 90  ? -31.236 21.009  41.061  1.00 31.07  ? 90  ASP G OD1 1 
ATOM   4008  O  OD2 . ASP D  1 90  ? -30.131 21.544  42.895  1.00 32.07  ? 90  ASP G OD2 1 
ATOM   4009  N  N   . LYS D  1 91  ? -32.293 17.909  41.182  1.00 32.26  ? 91  LYS G N   1 
ATOM   4010  C  CA  . LYS D  1 91  ? -33.694 17.703  40.796  1.00 33.26  ? 91  LYS G CA  1 
ATOM   4011  C  C   . LYS D  1 91  ? -34.442 18.967  40.310  1.00 33.46  ? 91  LYS G C   1 
ATOM   4012  O  O   . LYS D  1 91  ? -35.492 18.841  39.686  1.00 34.08  ? 91  LYS G O   1 
ATOM   4013  C  CB  . LYS D  1 91  ? -34.470 17.051  41.943  1.00 35.12  ? 91  LYS G CB  1 
ATOM   4014  C  CG  . LYS D  1 91  ? -34.706 17.952  43.146  1.00 36.39  ? 91  LYS G CG  1 
ATOM   4015  C  CD  . LYS D  1 91  ? -35.361 17.176  44.272  1.00 38.36  ? 91  LYS G CD  1 
ATOM   4016  C  CE  . LYS D  1 91  ? -35.446 18.007  45.544  1.00 39.80  ? 91  LYS G CE  1 
ATOM   4017  N  NZ  . LYS D  1 91  ? -36.193 19.282  45.354  1.00 40.32  ? 91  LYS G NZ  1 
ATOM   4018  N  N   . ASP D  1 92  ? -33.928 20.158  40.630  1.00 33.13  ? 92  ASP G N   1 
ATOM   4019  C  CA  . ASP D  1 92  ? -34.472 21.428  40.121  1.00 33.36  ? 92  ASP G CA  1 
ATOM   4020  C  C   . ASP D  1 92  ? -33.840 21.887  38.803  1.00 31.87  ? 92  ASP G C   1 
ATOM   4021  O  O   . ASP D  1 92  ? -34.211 22.937  38.273  1.00 32.07  ? 92  ASP G O   1 
ATOM   4022  C  CB  . ASP D  1 92  ? -34.311 22.537  41.166  1.00 34.15  ? 92  ASP G CB  1 
ATOM   4023  C  CG  . ASP D  1 92  ? -34.972 22.198  42.499  1.00 35.95  ? 92  ASP G CG  1 
ATOM   4024  O  OD1 . ASP D  1 92  ? -36.073 21.609  42.511  1.00 36.96  ? 92  ASP G OD1 1 
ATOM   4025  O  OD2 . ASP D  1 92  ? -34.376 22.534  43.546  1.00 36.48  ? 92  ASP G OD2 1 
ATOM   4026  N  N   . GLY D  1 93  ? -32.886 21.116  38.282  1.00 30.59  ? 93  GLY G N   1 
ATOM   4027  C  CA  . GLY D  1 93  ? -32.194 21.452  37.048  1.00 29.33  ? 93  GLY G CA  1 
ATOM   4028  C  C   . GLY D  1 93  ? -31.007 22.392  37.189  1.00 28.53  ? 93  GLY G C   1 
ATOM   4029  O  O   . GLY D  1 93  ? -30.546 22.974  36.192  1.00 27.72  ? 93  GLY G O   1 
ATOM   4030  N  N   . VAL D  1 94  ? -30.484 22.506  38.411  1.00 28.86  ? 94  VAL G N   1 
ATOM   4031  C  CA  . VAL D  1 94  ? -29.406 23.431  38.725  1.00 28.46  ? 94  VAL G CA  1 
ATOM   4032  C  C   . VAL D  1 94  ? -28.120 22.638  38.969  1.00 27.73  ? 94  VAL G C   1 
ATOM   4033  O  O   . VAL D  1 94  ? -28.125 21.678  39.740  1.00 28.16  ? 94  VAL G O   1 
ATOM   4034  C  CB  . VAL D  1 94  ? -29.760 24.292  39.959  1.00 29.80  ? 94  VAL G CB  1 
ATOM   4035  C  CG1 . VAL D  1 94  ? -28.598 25.203  40.352  1.00 29.64  ? 94  VAL G CG1 1 
ATOM   4036  C  CG2 . VAL D  1 94  ? -31.006 25.115  39.684  1.00 30.71  ? 94  VAL G CG2 1 
ATOM   4037  N  N   . ALA D  1 95  ? -27.042 23.009  38.272  1.00 26.73  ? 95  ALA G N   1 
ATOM   4038  C  CA  . ALA D  1 95  ? -25.716 22.442  38.534  1.00 26.32  ? 95  ALA G CA  1 
ATOM   4039  C  C   . ALA D  1 95  ? -24.947 23.457  39.364  1.00 26.85  ? 95  ALA G C   1 
ATOM   4040  O  O   . ALA D  1 95  ? -24.571 24.506  38.856  1.00 26.50  ? 95  ALA G O   1 
ATOM   4041  C  CB  . ALA D  1 95  ? -24.981 22.148  37.233  1.00 25.13  ? 95  ALA G CB  1 
ATOM   4042  N  N   . ASP D  1 96  ? -24.745 23.161  40.644  1.00 27.91  ? 96  ASP G N   1 
ATOM   4043  C  CA  . ASP D  1 96  ? -23.877 23.986  41.482  1.00 28.73  ? 96  ASP G CA  1 
ATOM   4044  C  C   . ASP D  1 96  ? -22.432 23.521  41.256  1.00 28.22  ? 96  ASP G C   1 
ATOM   4045  O  O   . ASP D  1 96  ? -21.938 22.663  41.960  1.00 28.73  ? 96  ASP G O   1 
ATOM   4046  C  CB  . ASP D  1 96  ? -24.299 23.913  42.956  1.00 30.33  ? 96  ASP G CB  1 
ATOM   4047  C  CG  . ASP D  1 96  ? -25.666 24.553  43.204  1.00 31.23  ? 96  ASP G CG  1 
ATOM   4048  O  OD1 . ASP D  1 96  ? -25.914 25.658  42.672  1.00 31.14  ? 96  ASP G OD1 1 
ATOM   4049  O  OD2 . ASP D  1 96  ? -26.492 23.948  43.915  1.00 32.19  ? 96  ASP G OD2 1 
ATOM   4050  N  N   . VAL D  1 97  ? -21.781 24.090  40.249  1.00 27.45  ? 97  VAL G N   1 
ATOM   4051  C  CA  . VAL D  1 97  ? -20.478 23.587  39.768  1.00 27.02  ? 97  VAL G CA  1 
ATOM   4052  C  C   . VAL D  1 97  ? -19.387 23.854  40.805  1.00 28.14  ? 97  VAL G C   1 
ATOM   4053  O  O   . VAL D  1 97  ? -19.294 24.945  41.346  1.00 28.86  ? 97  VAL G O   1 
ATOM   4054  C  CB  . VAL D  1 97  ? -20.074 24.205  38.408  1.00 26.01  ? 97  VAL G CB  1 
ATOM   4055  C  CG1 . VAL D  1 97  ? -18.714 23.688  37.949  1.00 25.67  ? 97  VAL G CG1 1 
ATOM   4056  C  CG2 . VAL D  1 97  ? -21.139 23.930  37.349  1.00 25.23  ? 97  VAL G CG2 1 
ATOM   4057  N  N   . SER D  1 98  ? -18.605 22.829  41.107  1.00 28.60  ? 98  SER G N   1 
ATOM   4058  C  CA  . SER D  1 98  ? -17.446 22.962  41.995  1.00 29.94  ? 98  SER G CA  1 
ATOM   4059  C  C   . SER D  1 98  ? -16.360 22.022  41.505  1.00 29.81  ? 98  SER G C   1 
ATOM   4060  O  O   . SER D  1 98  ? -16.429 20.816  41.755  1.00 30.10  ? 98  SER G O   1 
ATOM   4061  C  CB  . SER D  1 98  ? -17.843 22.638  43.438  1.00 31.47  ? 98  SER G CB  1 
ATOM   4062  O  OG  . SER D  1 98  ? -16.719 22.643  44.291  1.00 32.83  ? 98  SER G OG  1 
ATOM   4063  N  N   . ILE D  1 99  ? -15.387 22.579  40.778  1.00 29.63  ? 99  ILE G N   1 
ATOM   4064  C  CA  . ILE D  1 99  ? -14.280 21.820  40.179  1.00 29.60  ? 99  ILE G CA  1 
ATOM   4065  C  C   . ILE D  1 99  ? -12.951 22.507  40.528  1.00 30.80  ? 99  ILE G C   1 
ATOM   4066  O  O   . ILE D  1 99  ? -12.866 23.734  40.615  1.00 31.00  ? 99  ILE G O   1 
ATOM   4067  C  CB  . ILE D  1 99  ? -14.430 21.703  38.640  1.00 28.18  ? 99  ILE G CB  1 
ATOM   4068  C  CG1 . ILE D  1 99  ? -15.566 20.737  38.272  1.00 27.47  ? 99  ILE G CG1 1 
ATOM   4069  C  CG2 . ILE D  1 99  ? -13.137 21.232  37.962  1.00 28.23  ? 99  ILE G CG2 1 
ATOM   4070  C  CD1 . ILE D  1 99  ? -16.053 20.905  36.853  1.00 26.29  ? 99  ILE G CD1 1 
ATOM   4071  N  N   . GLU D  1 100 ? -11.925 21.695  40.749  1.00 31.75  ? 100 GLU G N   1 
ATOM   4072  C  CA  . GLU D  1 100 ? -10.569 22.193  40.884  1.00 32.98  ? 100 GLU G CA  1 
ATOM   4073  C  C   . GLU D  1 100 ? -9.719  21.419  39.885  1.00 32.56  ? 100 GLU G C   1 
ATOM   4074  O  O   . GLU D  1 100 ? -9.766  20.187  39.863  1.00 32.65  ? 100 GLU G O   1 
ATOM   4075  C  CB  . GLU D  1 100 ? -10.082 21.999  42.308  1.00 35.07  ? 100 GLU G CB  1 
ATOM   4076  C  CG  . GLU D  1 100 ? -8.816  22.765  42.606  1.00 36.66  ? 100 GLU G CG  1 
ATOM   4077  C  CD  . GLU D  1 100 ? -8.311  22.524  44.011  1.00 39.01  ? 100 GLU G CD  1 
ATOM   4078  O  OE1 . GLU D  1 100 ? -9.102  22.655  44.964  1.00 39.87  ? 100 GLU G OE1 1 
ATOM   4079  O  OE2 . GLU D  1 100 ? -7.123  22.204  44.160  1.00 40.53  ? 100 GLU G OE2 1 
ATOM   4080  N  N   . ASP D  1 101 ? -8.976  22.134  39.042  1.00 32.25  ? 101 ASP G N   1 
ATOM   4081  C  CA  . ASP D  1 101 ? -8.202  21.491  37.988  1.00 31.92  ? 101 ASP G CA  1 
ATOM   4082  C  C   . ASP D  1 101 ? -6.824  22.125  37.816  1.00 32.79  ? 101 ASP G C   1 
ATOM   4083  O  O   . ASP D  1 101 ? -6.682  23.346  37.815  1.00 32.86  ? 101 ASP G O   1 
ATOM   4084  C  CB  . ASP D  1 101 ? -8.961  21.539  36.668  1.00 30.38  ? 101 ASP G CB  1 
ATOM   4085  C  CG  . ASP D  1 101 ? -8.359  20.615  35.620  1.00 30.39  ? 101 ASP G CG  1 
ATOM   4086  O  OD1 . ASP D  1 101 ? -8.598  19.390  35.716  1.00 30.83  ? 101 ASP G OD1 1 
ATOM   4087  O  OD2 . ASP D  1 101 ? -7.637  21.086  34.717  1.00 30.27  ? 101 ASP G OD2 1 
ATOM   4088  N  N   . SER D  1 102 ? -5.817  21.281  37.645  1.00 33.56  ? 102 SER G N   1 
ATOM   4089  C  CA  . SER D  1 102 ? -4.442  21.749  37.506  1.00 34.78  ? 102 SER G CA  1 
ATOM   4090  C  C   . SER D  1 102 ? -3.895  21.695  36.081  1.00 34.07  ? 102 SER G C   1 
ATOM   4091  O  O   . SER D  1 102 ? -2.735  22.050  35.867  1.00 35.10  ? 102 SER G O   1 
ATOM   4092  C  CB  . SER D  1 102 ? -3.549  20.949  38.443  1.00 36.82  ? 102 SER G CB  1 
ATOM   4093  O  OG  . SER D  1 102 ? -3.924  21.224  39.776  1.00 37.82  ? 102 SER G OG  1 
ATOM   4094  N  N   . VAL D  1 103 ? -4.717  21.277  35.115  1.00 32.28  ? 103 VAL G N   1 
ATOM   4095  C  CA  . VAL D  1 103 ? -4.285  21.170  33.719  1.00 31.81  ? 103 VAL G CA  1 
ATOM   4096  C  C   . VAL D  1 103 ? -4.682  22.438  32.963  1.00 30.78  ? 103 VAL G C   1 
ATOM   4097  O  O   . VAL D  1 103 ? -3.875  22.992  32.219  1.00 31.29  ? 103 VAL G O   1 
ATOM   4098  C  CB  . VAL D  1 103 ? -4.837  19.887  33.064  1.00 31.01  ? 103 VAL G CB  1 
ATOM   4099  C  CG1 . VAL D  1 103 ? -4.563  19.869  31.572  1.00 30.63  ? 103 VAL G CG1 1 
ATOM   4100  C  CG2 . VAL D  1 103 ? -4.224  18.659  33.733  1.00 32.34  ? 103 VAL G CG2 1 
ATOM   4101  N  N   . ILE D  1 104 ? -5.912  22.899  33.148  1.00 29.48  ? 104 ILE G N   1 
ATOM   4102  C  CA  . ILE D  1 104 ? -6.271  24.244  32.676  1.00 28.88  ? 104 ILE G CA  1 
ATOM   4103  C  C   . ILE D  1 104 ? -5.476  25.293  33.450  1.00 30.02  ? 104 ILE G C   1 
ATOM   4104  O  O   . ILE D  1 104 ? -5.046  25.056  34.583  1.00 31.05  ? 104 ILE G O   1 
ATOM   4105  C  CB  . ILE D  1 104 ? -7.775  24.574  32.766  1.00 27.64  ? 104 ILE G CB  1 
ATOM   4106  C  CG1 . ILE D  1 104 ? -8.325  24.361  34.186  1.00 27.91  ? 104 ILE G CG1 1 
ATOM   4107  C  CG2 . ILE D  1 104 ? -8.558  23.769  31.737  1.00 26.54  ? 104 ILE G CG2 1 
ATOM   4108  C  CD1 . ILE D  1 104 ? -9.648  25.047  34.438  1.00 27.17  ? 104 ILE G CD1 1 
ATOM   4109  N  N   . SER D  1 105 ? -5.279  26.440  32.818  1.00 29.97  ? 105 SER G N   1 
ATOM   4110  C  CA  . SER D  1 105 ? -4.648  27.583  33.453  1.00 31.16  ? 105 SER G CA  1 
ATOM   4111  C  C   . SER D  1 105 ? -5.320  28.859  32.979  1.00 30.65  ? 105 SER G C   1 
ATOM   4112  O  O   . SER D  1 105 ? -6.118  28.848  32.031  1.00 29.40  ? 105 SER G O   1 
ATOM   4113  C  CB  . SER D  1 105 ? -3.141  27.616  33.142  1.00 32.62  ? 105 SER G CB  1 
ATOM   4114  O  OG  . SER D  1 105 ? -2.484  28.583  33.948  1.00 34.09  ? 105 SER G OG  1 
ATOM   4115  N  N   . LEU D  1 106 ? -5.019  29.945  33.677  1.00 31.80  ? 106 LEU G N   1 
ATOM   4116  C  CA  . LEU D  1 106 ? -5.444  31.283  33.285  1.00 31.86  ? 106 LEU G CA  1 
ATOM   4117  C  C   . LEU D  1 106 ? -4.261  32.100  32.787  1.00 33.23  ? 106 LEU G C   1 
ATOM   4118  O  O   . LEU D  1 106 ? -4.374  33.312  32.618  1.00 33.83  ? 106 LEU G O   1 
ATOM   4119  C  CB  . LEU D  1 106 ? -6.143  31.992  34.452  1.00 32.23  ? 106 LEU G CB  1 
ATOM   4120  C  CG  . LEU D  1 106 ? -7.381  31.302  35.019  1.00 31.15  ? 106 LEU G CG  1 
ATOM   4121  C  CD1 . LEU D  1 106 ? -8.086  32.223  36.004  1.00 31.79  ? 106 LEU G CD1 1 
ATOM   4122  C  CD2 . LEU D  1 106 ? -8.349  30.893  33.919  1.00 29.49  ? 106 LEU G CD2 1 
ATOM   4123  N  N   . SER D  1 107 ? -3.131  31.435  32.544  1.00 34.05  ? 107 SER G N   1 
ATOM   4124  C  CA  . SER D  1 107 ? -1.985  32.052  31.887  1.00 35.38  ? 107 SER G CA  1 
ATOM   4125  C  C   . SER D  1 107 ? -1.106  30.989  31.217  1.00 35.63  ? 107 SER G C   1 
ATOM   4126  O  O   . SER D  1 107 ? -1.251  29.790  31.476  1.00 35.07  ? 107 SER G O   1 
ATOM   4127  C  CB  . SER D  1 107 ? -1.171  32.871  32.890  1.00 37.39  ? 107 SER G CB  1 
ATOM   4128  O  OG  . SER D  1 107 ? -0.406  32.038  33.743  1.00 38.49  ? 107 SER G OG  1 
ATOM   4129  N  N   . GLY D  1 108 ? -0.208  31.437  30.345  1.00 36.62  ? 108 GLY G N   1 
ATOM   4130  C  CA  . GLY D  1 108 ? 0.700   30.536  29.635  1.00 37.15  ? 108 GLY G CA  1 
ATOM   4131  C  C   . GLY D  1 108 ? 0.023   29.683  28.570  1.00 35.60  ? 108 GLY G C   1 
ATOM   4132  O  O   . GLY D  1 108 ? -1.089  29.991  28.122  1.00 34.18  ? 108 GLY G O   1 
ATOM   4133  N  N   . ASP D  1 109 ? 0.694   28.594  28.194  1.00 36.04  ? 109 ASP G N   1 
ATOM   4134  C  CA  . ASP D  1 109 ? 0.298   27.738  27.069  1.00 35.12  ? 109 ASP G CA  1 
ATOM   4135  C  C   . ASP D  1 109 ? -1.081  27.097  27.222  1.00 33.19  ? 109 ASP G C   1 
ATOM   4136  O  O   . ASP D  1 109 ? -1.772  26.902  26.231  1.00 32.26  ? 109 ASP G O   1 
ATOM   4137  C  CB  . ASP D  1 109 ? 1.339   26.622  26.830  1.00 36.32  ? 109 ASP G CB  1 
ATOM   4138  C  CG  . ASP D  1 109 ? 2.673   27.144  26.336  1.00 38.36  ? 109 ASP G CG  1 
ATOM   4139  O  OD1 . ASP D  1 109 ? 2.732   28.283  25.824  1.00 38.82  ? 109 ASP G OD1 1 
ATOM   4140  O  OD2 . ASP D  1 109 ? 3.682   26.408  26.451  1.00 39.75  ? 109 ASP G OD2 1 
ATOM   4141  N  N   . HIS D  1 110 ? -1.473  26.764  28.452  1.00 32.76  ? 110 HIS G N   1 
ATOM   4142  C  CA  . HIS D  1 110 ? -2.776  26.132  28.707  1.00 31.16  ? 110 HIS G CA  1 
ATOM   4143  C  C   . HIS D  1 110 ? -3.854  27.143  29.123  1.00 30.20  ? 110 HIS G C   1 
ATOM   4144  O  O   . HIS D  1 110 ? -4.903  26.747  29.625  1.00 29.16  ? 110 HIS G O   1 
ATOM   4145  C  CB  . HIS D  1 110 ? -2.632  25.026  29.764  1.00 31.45  ? 110 HIS G CB  1 
ATOM   4146  C  CG  . HIS D  1 110 ? -1.827  23.854  29.301  1.00 32.20  ? 110 HIS G CG  1 
ATOM   4147  N  ND1 . HIS D  1 110 ? -1.758  22.678  30.015  1.00 32.52  ? 110 HIS G ND1 1 
ATOM   4148  C  CD2 . HIS D  1 110 ? -1.079  23.664  28.187  1.00 32.90  ? 110 HIS G CD2 1 
ATOM   4149  C  CE1 . HIS D  1 110 ? -0.971  21.827  29.380  1.00 33.40  ? 110 HIS G CE1 1 
ATOM   4150  N  NE2 . HIS D  1 110 ? -0.548  22.400  28.267  1.00 33.64  ? 110 HIS G NE2 1 
ATOM   4151  N  N   . CYS D  1 111 ? -3.601  28.434  28.881  1.00 30.70  ? 111 CYS G N   1 
ATOM   4152  C  CA  . CYS D  1 111 ? -4.548  29.490  29.180  1.00 30.13  ? 111 CYS G CA  1 
ATOM   4153  C  C   . CYS D  1 111 ? -5.872  29.236  28.452  1.00 28.54  ? 111 CYS G C   1 
ATOM   4154  O  O   . CYS D  1 111 ? -5.885  28.972  27.247  1.00 28.26  ? 111 CYS G O   1 
ATOM   4155  C  CB  . CYS D  1 111 ? -4.003  30.872  28.794  1.00 31.20  ? 111 CYS G CB  1 
ATOM   4156  S  SG  . CYS D  1 111 ? -5.072  32.229  29.334  1.00 31.15  ? 111 CYS G SG  1 
ATOM   4157  N  N   . ILE D  1 112 ? -6.965  29.286  29.205  1.00 27.66  ? 112 ILE G N   1 
ATOM   4158  C  CA  . ILE D  1 112 ? -8.322  29.095  28.636  1.00 26.42  ? 112 ILE G CA  1 
ATOM   4159  C  C   . ILE D  1 112 ? -9.088  30.404  28.417  1.00 26.32  ? 112 ILE G C   1 
ATOM   4160  O  O   . ILE D  1 112 ? -10.175 30.392  27.845  1.00 25.54  ? 112 ILE G O   1 
ATOM   4161  C  CB  . ILE D  1 112 ? -9.168  28.100  29.460  1.00 25.66  ? 112 ILE G CB  1 
ATOM   4162  C  CG1 . ILE D  1 112 ? -9.386  28.579  30.905  1.00 26.08  ? 112 ILE G CG1 1 
ATOM   4163  C  CG2 . ILE D  1 112 ? -8.505  26.728  29.425  1.00 25.73  ? 112 ILE G CG2 1 
ATOM   4164  C  CD1 . ILE D  1 112 ? -10.399 27.757  31.683  1.00 25.43  ? 112 ILE G CD1 1 
ATOM   4165  N  N   . ILE D  1 113 ? -8.521  31.527  28.853  1.00 27.24  ? 113 ILE G N   1 
ATOM   4166  C  CA  . ILE D  1 113 ? -9.108  32.836  28.578  1.00 27.51  ? 113 ILE G CA  1 
ATOM   4167  C  C   . ILE D  1 113 ? -9.180  33.070  27.054  1.00 27.42  ? 113 ILE G C   1 
ATOM   4168  O  O   . ILE D  1 113 ? -8.226  32.793  26.326  1.00 27.72  ? 113 ILE G O   1 
ATOM   4169  C  CB  . ILE D  1 113 ? -8.329  33.956  29.289  1.00 28.91  ? 113 ILE G CB  1 
ATOM   4170  C  CG1 . ILE D  1 113 ? -8.579  33.870  30.813  1.00 29.11  ? 113 ILE G CG1 1 
ATOM   4171  C  CG2 . ILE D  1 113 ? -8.712  35.330  28.742  1.00 29.53  ? 113 ILE G CG2 1 
ATOM   4172  C  CD1 . ILE D  1 113 ? -7.619  34.700  31.640  1.00 30.75  ? 113 ILE G CD1 1 
ATOM   4173  N  N   . GLY D  1 114 ? -10.337 33.548  26.587  1.00 26.95  ? 114 GLY G N   1 
ATOM   4174  C  CA  . GLY D  1 114 ? -10.574 33.759  25.156  1.00 27.06  ? 114 GLY G CA  1 
ATOM   4175  C  C   . GLY D  1 114 ? -11.024 32.521  24.393  1.00 26.18  ? 114 GLY G C   1 
ATOM   4176  O  O   . GLY D  1 114 ? -11.198 32.570  23.183  1.00 26.43  ? 114 GLY G O   1 
ATOM   4177  N  N   . ARG D  1 115 ? -11.205 31.410  25.098  1.00 25.35  ? 115 ARG G N   1 
ATOM   4178  C  CA  . ARG D  1 115 ? -11.713 30.180  24.511  1.00 24.66  ? 115 ARG G CA  1 
ATOM   4179  C  C   . ARG D  1 115 ? -13.164 30.045  24.968  1.00 24.03  ? 115 ARG G C   1 
ATOM   4180  O  O   . ARG D  1 115 ? -13.689 30.972  25.592  1.00 24.17  ? 115 ARG G O   1 
ATOM   4181  C  CB  . ARG D  1 115 ? -10.812 29.023  24.923  1.00 24.48  ? 115 ARG G CB  1 
ATOM   4182  C  CG  . ARG D  1 115 ? -9.371  29.286  24.503  1.00 25.39  ? 115 ARG G CG  1 
ATOM   4183  C  CD  . ARG D  1 115 ? -8.494  28.051  24.532  1.00 25.49  ? 115 ARG G CD  1 
ATOM   4184  N  NE  . ARG D  1 115 ? -7.101  28.410  24.272  1.00 26.60  ? 115 ARG G NE  1 
ATOM   4185  C  CZ  . ARG D  1 115 ? -6.513  28.475  23.079  1.00 27.31  ? 115 ARG G CZ  1 
ATOM   4186  N  NH1 . ARG D  1 115 ? -7.164  28.180  21.948  1.00 27.07  ? 115 ARG G NH1 1 
ATOM   4187  N  NH2 . ARG D  1 115 ? -5.234  28.817  23.029  1.00 28.45  ? 115 ARG G NH2 1 
ATOM   4188  N  N   . THR D  1 116 ? -13.826 28.936  24.641  1.00 23.50  ? 116 THR G N   1 
ATOM   4189  C  CA  . THR D  1 116 ? -15.262 28.796  24.907  1.00 23.10  ? 116 THR G CA  1 
ATOM   4190  C  C   . THR D  1 116 ? -15.536 27.685  25.906  1.00 22.52  ? 116 THR G C   1 
ATOM   4191  O  O   . THR D  1 116 ? -15.059 26.566  25.734  1.00 22.38  ? 116 THR G O   1 
ATOM   4192  C  CB  . THR D  1 116 ? -16.040 28.536  23.599  1.00 23.29  ? 116 THR G CB  1 
ATOM   4193  O  OG1 . THR D  1 116 ? -15.898 29.669  22.740  1.00 24.04  ? 116 THR G OG1 1 
ATOM   4194  C  CG2 . THR D  1 116 ? -17.536 28.311  23.857  1.00 23.04  ? 116 THR G CG2 1 
ATOM   4195  N  N   . LEU D  1 117 ? -16.287 28.007  26.955  1.00 22.43  ? 117 LEU G N   1 
ATOM   4196  C  CA  . LEU D  1 117 ? -16.789 27.006  27.886  1.00 22.07  ? 117 LEU G CA  1 
ATOM   4197  C  C   . LEU D  1 117 ? -18.110 26.499  27.328  1.00 21.93  ? 117 LEU G C   1 
ATOM   4198  O  O   . LEU D  1 117 ? -18.916 27.290  26.902  1.00 22.19  ? 117 LEU G O   1 
ATOM   4199  C  CB  . LEU D  1 117 ? -16.977 27.601  29.276  1.00 22.27  ? 117 LEU G CB  1 
ATOM   4200  C  CG  . LEU D  1 117 ? -17.434 26.631  30.367  1.00 22.08  ? 117 LEU G CG  1 
ATOM   4201  C  CD1 . LEU D  1 117 ? -16.416 25.550  30.670  1.00 22.02  ? 117 LEU G CD1 1 
ATOM   4202  C  CD2 . LEU D  1 117 ? -17.798 27.386  31.630  1.00 22.59  ? 117 LEU G CD2 1 
ATOM   4203  N  N   . VAL D  1 118 ? -18.307 25.184  27.327  1.00 21.77  ? 118 VAL G N   1 
ATOM   4204  C  CA  . VAL D  1 118 ? -19.511 24.562  26.780  1.00 21.89  ? 118 VAL G CA  1 
ATOM   4205  C  C   . VAL D  1 118 ? -20.057 23.557  27.771  1.00 21.79  ? 118 VAL G C   1 
ATOM   4206  O  O   . VAL D  1 118 ? -19.302 22.724  28.304  1.00 21.58  ? 118 VAL G O   1 
ATOM   4207  C  CB  . VAL D  1 118 ? -19.243 23.829  25.441  1.00 22.03  ? 118 VAL G CB  1 
ATOM   4208  C  CG1 . VAL D  1 118 ? -20.532 23.237  24.876  1.00 22.33  ? 118 VAL G CG1 1 
ATOM   4209  C  CG2 . VAL D  1 118 ? -18.628 24.781  24.427  1.00 22.43  ? 118 VAL G CG2 1 
ATOM   4210  N  N   . VAL D  1 119 ? -21.373 23.614  27.988  1.00 22.09  ? 119 VAL G N   1 
ATOM   4211  C  CA  . VAL D  1 119 ? -22.060 22.566  28.731  1.00 22.25  ? 119 VAL G CA  1 
ATOM   4212  C  C   . VAL D  1 119 ? -22.930 21.766  27.756  1.00 22.65  ? 119 VAL G C   1 
ATOM   4213  O  O   . VAL D  1 119 ? -23.606 22.330  26.895  1.00 22.99  ? 119 VAL G O   1 
ATOM   4214  C  CB  . VAL D  1 119 ? -22.836 23.088  29.968  1.00 22.51  ? 119 VAL G CB  1 
ATOM   4215  C  CG1 . VAL D  1 119 ? -23.998 23.991  29.579  1.00 22.98  ? 119 VAL G CG1 1 
ATOM   4216  C  CG2 . VAL D  1 119 ? -23.341 21.918  30.804  1.00 22.67  ? 119 VAL G CG2 1 
ATOM   4217  N  N   . HIS D  1 120 ? -22.889 20.445  27.902  1.00 22.84  ? 120 HIS G N   1 
ATOM   4218  C  CA  . HIS D  1 120 ? -23.453 19.526  26.917  1.00 23.43  ? 120 HIS G CA  1 
ATOM   4219  C  C   . HIS D  1 120 ? -24.761 18.830  27.332  1.00 24.05  ? 120 HIS G C   1 
ATOM   4220  O  O   . HIS D  1 120 ? -25.158 18.843  28.501  1.00 23.97  ? 120 HIS G O   1 
ATOM   4221  C  CB  . HIS D  1 120 ? -22.394 18.483  26.557  1.00 23.44  ? 120 HIS G CB  1 
ATOM   4222  C  CG  . HIS D  1 120 ? -21.328 19.003  25.645  1.00 23.38  ? 120 HIS G CG  1 
ATOM   4223  N  ND1 . HIS D  1 120 ? -20.260 19.744  26.096  1.00 23.04  ? 120 HIS G ND1 1 
ATOM   4224  C  CD2 . HIS D  1 120 ? -21.161 18.880  24.308  1.00 23.87  ? 120 HIS G CD2 1 
ATOM   4225  C  CE1 . HIS D  1 120 ? -19.480 20.055  25.076  1.00 23.20  ? 120 HIS G CE1 1 
ATOM   4226  N  NE2 . HIS D  1 120 ? -20.004 19.542  23.979  1.00 23.73  ? 120 HIS G NE2 1 
ATOM   4227  N  N   . GLU D  1 121 ? -25.390 18.220  26.326  1.00 24.81  ? 121 GLU G N   1 
ATOM   4228  C  CA  . GLU D  1 121 ? -26.670 17.517  26.419  1.00 25.80  ? 121 GLU G CA  1 
ATOM   4229  C  C   . GLU D  1 121 ? -26.659 16.374  27.418  1.00 25.89  ? 121 GLU G C   1 
ATOM   4230  O  O   . GLU D  1 121 ? -27.584 16.229  28.208  1.00 26.13  ? 121 GLU G O   1 
ATOM   4231  C  CB  . GLU D  1 121 ? -27.038 16.975  25.037  1.00 26.71  ? 121 GLU G CB  1 
ATOM   4232  C  CG  . GLU D  1 121 ? -28.363 16.230  24.923  1.00 27.97  ? 121 GLU G CG  1 
ATOM   4233  C  CD  . GLU D  1 121 ? -28.572 15.651  23.539  1.00 29.07  ? 121 GLU G CD  1 
ATOM   4234  O  OE1 . GLU D  1 121 ? -27.677 15.775  22.678  1.00 29.04  ? 121 GLU G OE1 1 
ATOM   4235  O  OE2 . GLU D  1 121 ? -29.638 15.069  23.300  1.00 30.44  ? 121 GLU G OE2 1 
ATOM   4236  N  N   . LYS D  1 122 ? -25.609 15.562  27.374  1.00 25.78  ? 122 LYS G N   1 
ATOM   4237  C  CA  . LYS D  1 122 ? -25.562 14.367  28.203  1.00 26.24  ? 122 LYS G CA  1 
ATOM   4238  C  C   . LYS D  1 122 ? -24.180 14.105  28.785  1.00 25.56  ? 122 LYS G C   1 
ATOM   4239  O  O   . LYS D  1 122 ? -23.273 14.927  28.650  1.00 24.83  ? 122 LYS G O   1 
ATOM   4240  C  CB  . LYS D  1 122 ? -26.142 13.171  27.423  1.00 27.49  ? 122 LYS G CB  1 
ATOM   4241  C  CG  . LYS D  1 122 ? -25.474 12.848  26.106  1.00 27.88  ? 122 LYS G CG  1 
ATOM   4242  C  CD  . LYS D  1 122 ? -26.401 11.995  25.246  1.00 29.27  ? 122 LYS G CD  1 
ATOM   4243  C  CE  . LYS D  1 122 ? -25.698 11.533  23.981  1.00 29.90  ? 122 LYS G CE  1 
ATOM   4244  N  NZ  . LYS D  1 122 ? -26.537 10.572  23.207  1.00 31.49  ? 122 LYS G NZ  1 
ATOM   4245  N  N   . ALA D  1 123 ? -24.071 12.993  29.501  1.00 25.87  ? 123 ALA G N   1 
ATOM   4246  C  CA  . ALA D  1 123 ? -22.882 12.628  30.217  1.00 25.68  ? 123 ALA G CA  1 
ATOM   4247  C  C   . ALA D  1 123 ? -21.678 12.486  29.281  1.00 25.41  ? 123 ALA G C   1 
ATOM   4248  O  O   . ALA D  1 123 ? -21.784 11.950  28.179  1.00 25.73  ? 123 ALA G O   1 
ATOM   4249  C  CB  . ALA D  1 123 ? -23.121 11.332  30.972  1.00 26.56  ? 123 ALA G CB  1 
ATOM   4250  N  N   . ASP D  1 124 ? -20.560 13.040  29.720  1.00 24.92  ? 124 ASP G N   1 
ATOM   4251  C  CA  . ASP D  1 124 ? -19.248 12.729  29.165  1.00 24.98  ? 124 ASP G CA  1 
ATOM   4252  C  C   . ASP D  1 124 ? -18.869 11.343  29.705  1.00 25.72  ? 124 ASP G C   1 
ATOM   4253  O  O   . ASP D  1 124 ? -18.844 11.147  30.913  1.00 26.02  ? 124 ASP G O   1 
ATOM   4254  C  CB  . ASP D  1 124 ? -18.255 13.807  29.619  1.00 24.54  ? 124 ASP G CB  1 
ATOM   4255  C  CG  . ASP D  1 124 ? -16.876 13.682  28.966  1.00 24.81  ? 124 ASP G CG  1 
ATOM   4256  O  OD1 . ASP D  1 124 ? -16.500 12.583  28.503  1.00 25.42  ? 124 ASP G OD1 1 
ATOM   4257  O  OD2 . ASP D  1 124 ? -16.161 14.705  28.937  1.00 24.53  ? 124 ASP G OD2 1 
ATOM   4258  N  N   . ASP D  1 125 ? -18.599 10.390  28.815  1.00 26.26  ? 125 ASP G N   1 
ATOM   4259  C  CA  . ASP D  1 125 ? -18.159 9.041   29.212  1.00 27.26  ? 125 ASP G CA  1 
ATOM   4260  C  C   . ASP D  1 125 ? -16.667 8.963   29.629  1.00 27.54  ? 125 ASP G C   1 
ATOM   4261  O  O   . ASP D  1 125 ? -16.170 7.879   29.930  1.00 28.52  ? 125 ASP G O   1 
ATOM   4262  C  CB  . ASP D  1 125 ? -18.503 7.992   28.120  1.00 28.13  ? 125 ASP G CB  1 
ATOM   4263  C  CG  . ASP D  1 125 ? -17.672 8.139   26.815  1.00 28.30  ? 125 ASP G CG  1 
ATOM   4264  O  OD1 . ASP D  1 125 ? -16.596 8.772   26.795  1.00 27.93  ? 125 ASP G OD1 1 
ATOM   4265  O  OD2 . ASP D  1 125 ? -18.104 7.578   25.785  1.00 29.00  ? 125 ASP G OD2 1 
ATOM   4266  N  N   . LEU D  1 126 ? -15.973 10.105  29.619  1.00 26.83  ? 126 LEU G N   1 
ATOM   4267  C  CA  . LEU D  1 126 ? -14.601 10.249  30.124  1.00 27.23  ? 126 LEU G CA  1 
ATOM   4268  C  C   . LEU D  1 126 ? -13.613 9.387   29.343  1.00 28.15  ? 126 LEU G C   1 
ATOM   4269  O  O   . LEU D  1 126 ? -12.630 8.908   29.888  1.00 28.97  ? 126 LEU G O   1 
ATOM   4270  C  CB  . LEU D  1 126 ? -14.524 9.977   31.639  1.00 27.76  ? 126 LEU G CB  1 
ATOM   4271  C  CG  . LEU D  1 126 ? -15.592 10.690  32.487  1.00 27.14  ? 126 LEU G CG  1 
ATOM   4272  C  CD1 . LEU D  1 126 ? -15.429 10.325  33.945  1.00 27.98  ? 126 LEU G CD1 1 
ATOM   4273  C  CD2 . LEU D  1 126 ? -15.563 12.206  32.307  1.00 26.14  ? 126 LEU G CD2 1 
ATOM   4274  N  N   . GLY D  1 127 ? -13.895 9.206   28.055  1.00 28.13  ? 127 GLY G N   1 
ATOM   4275  C  CA  . GLY D  1 127 ? -13.049 8.425   27.181  1.00 29.21  ? 127 GLY G CA  1 
ATOM   4276  C  C   . GLY D  1 127 ? -13.144 6.929   27.363  1.00 30.46  ? 127 GLY G C   1 
ATOM   4277  O  O   . GLY D  1 127 ? -12.295 6.206   26.852  1.00 31.57  ? 127 GLY G O   1 
ATOM   4278  N  N   . LYS D  1 128 ? -14.185 6.454   28.049  1.00 30.42  ? 128 LYS G N   1 
ATOM   4279  C  CA  . LYS D  1 128 ? -14.331 5.021   28.344  1.00 31.78  ? 128 LYS G CA  1 
ATOM   4280  C  C   . LYS D  1 128 ? -15.458 4.368   27.556  1.00 32.02  ? 128 LYS G C   1 
ATOM   4281  O  O   . LYS D  1 128 ? -15.854 3.243   27.863  1.00 33.07  ? 128 LYS G O   1 
ATOM   4282  C  CB  . LYS D  1 128 ? -14.552 4.797   29.847  1.00 32.08  ? 128 LYS G CB  1 
ATOM   4283  C  CG  . LYS D  1 128 ? -13.512 5.461   30.728  1.00 32.07  ? 128 LYS G CG  1 
ATOM   4284  C  CD  . LYS D  1 128 ? -13.918 5.454   32.188  1.00 32.31  ? 128 LYS G CD  1 
ATOM   4285  C  CE  . LYS D  1 128 ? -13.691 4.105   32.823  1.00 34.08  ? 128 LYS G CE  1 
ATOM   4286  N  NZ  . LYS D  1 128 ? -14.019 4.202   34.267  1.00 34.45  ? 128 LYS G NZ  1 
ATOM   4287  N  N   . GLY D  1 129 ? -15.961 5.058   26.537  1.00 31.28  ? 129 GLY G N   1 
ATOM   4288  C  CA  . GLY D  1 129 ? -17.066 4.557   25.729  1.00 31.72  ? 129 GLY G CA  1 
ATOM   4289  C  C   . GLY D  1 129 ? -16.681 3.482   24.738  1.00 33.25  ? 129 GLY G C   1 
ATOM   4290  O  O   . GLY D  1 129 ? -17.548 2.753   24.261  1.00 34.05  ? 129 GLY G O   1 
ATOM   4291  N  N   . GLY D  1 130 ? -15.388 3.391   24.409  1.00 33.79  ? 130 GLY G N   1 
ATOM   4292  C  CA  . GLY D  1 130 ? -14.895 2.354   23.513  1.00 35.54  ? 130 GLY G CA  1 
ATOM   4293  C  C   . GLY D  1 130 ? -15.204 2.547   22.031  1.00 36.00  ? 130 GLY G C   1 
ATOM   4294  O  O   . GLY D  1 130 ? -14.997 1.625   21.254  1.00 37.61  ? 130 GLY G O   1 
ATOM   4295  N  N   . ASN D  1 131 ? -15.690 3.727   21.638  1.00 34.78  ? 131 ASN G N   1 
ATOM   4296  C  CA  . ASN D  1 131 ? -15.921 4.037   20.228  1.00 35.36  ? 131 ASN G CA  1 
ATOM   4297  C  C   . ASN D  1 131 ? -15.067 5.229   19.847  1.00 34.61  ? 131 ASN G C   1 
ATOM   4298  O  O   . ASN D  1 131 ? -14.516 5.897   20.720  1.00 33.44  ? 131 ASN G O   1 
ATOM   4299  C  CB  . ASN D  1 131 ? -17.429 4.233   19.901  1.00 35.16  ? 131 ASN G CB  1 
ATOM   4300  C  CG  . ASN D  1 131 ? -18.063 5.447   20.577  1.00 33.41  ? 131 ASN G CG  1 
ATOM   4301  O  OD1 . ASN D  1 131 ? -17.419 6.215   21.290  1.00 32.18  ? 131 ASN G OD1 1 
ATOM   4302  N  ND2 . ASN D  1 131 ? -19.368 5.619   20.340  1.00 33.50  ? 131 ASN G ND2 1 
ATOM   4303  N  N   . GLU D  1 132 ? -14.968 5.502   18.549  1.00 35.49  ? 132 GLU G N   1 
ATOM   4304  C  CA  . GLU D  1 132 ? -14.150 6.616   18.050  1.00 35.13  ? 132 GLU G CA  1 
ATOM   4305  C  C   . GLU D  1 132 ? -14.499 7.910   18.734  1.00 33.40  ? 132 GLU G C   1 
ATOM   4306  O  O   . GLU D  1 132 ? -13.620 8.652   19.157  1.00 32.69  ? 132 GLU G O   1 
ATOM   4307  C  CB  . GLU D  1 132 ? -14.325 6.804   16.543  1.00 36.30  ? 132 GLU G CB  1 
ATOM   4308  C  CG  . GLU D  1 132 ? -13.723 5.697   15.701  1.00 38.41  ? 132 GLU G CG  1 
ATOM   4309  C  CD  . GLU D  1 132 ? -13.953 5.905   14.216  0.75 39.78  ? 132 GLU G CD  1 
ATOM   4310  O  OE1 . GLU D  1 132 ? -14.229 7.050   13.795  0.75 39.10  ? 132 GLU G OE1 1 
ATOM   4311  O  OE2 . GLU D  1 132 ? -13.858 4.912   13.468  0.75 41.77  ? 132 GLU G OE2 1 
ATOM   4312  N  N   . GLU D  1 133 ? -15.796 8.160   18.860  1.00 32.99  ? 133 GLU G N   1 
ATOM   4313  C  CA  . GLU D  1 133 ? -16.287 9.401   19.419  1.00 31.64  ? 133 GLU G CA  1 
ATOM   4314  C  C   . GLU D  1 133 ? -15.946 9.560   20.913  1.00 30.40  ? 133 GLU G C   1 
ATOM   4315  O  O   . GLU D  1 133 ? -15.710 10.678  21.382  1.00 29.12  ? 133 GLU G O   1 
ATOM   4316  C  CB  . GLU D  1 133 ? -17.797 9.485   19.200  1.00 31.93  ? 133 GLU G CB  1 
ATOM   4317  C  CG  . GLU D  1 133 ? -18.395 10.850  19.455  1.00 31.03  ? 133 GLU G CG  1 
ATOM   4318  C  CD  . GLU D  1 133 ? -18.033 11.887  18.402  1.00 31.46  ? 133 GLU G CD  1 
ATOM   4319  O  OE1 . GLU D  1 133 ? -17.515 11.546  17.311  1.00 32.94  ? 133 GLU G OE1 1 
ATOM   4320  O  OE2 . GLU D  1 133 ? -18.274 13.075  18.677  1.00 30.89  ? 133 GLU G OE2 1 
ATOM   4321  N  N   . SER D  1 134 ? -15.900 8.453   21.649  1.00 30.85  ? 134 SER G N   1 
ATOM   4322  C  CA  . SER D  1 134 ? -15.495 8.504   23.053  1.00 30.26  ? 134 SER G CA  1 
ATOM   4323  C  C   . SER D  1 134 ? -14.114 9.150   23.214  1.00 30.15  ? 134 SER G C   1 
ATOM   4324  O  O   . SER D  1 134 ? -13.937 9.988   24.105  1.00 29.17  ? 134 SER G O   1 
ATOM   4325  C  CB  . SER D  1 134 ? -15.494 7.114   23.692  1.00 31.17  ? 134 SER G CB  1 
ATOM   4326  O  OG  . SER D  1 134 ? -15.094 7.202   25.049  1.00 30.74  ? 134 SER G OG  1 
ATOM   4327  N  N   . THR D  1 135 ? -13.187 8.800   22.312  1.00 31.27  ? 135 THR G N   1 
ATOM   4328  C  CA  . THR D  1 135 ? -11.817 9.349   22.305  1.00 31.57  ? 135 THR G CA  1 
ATOM   4329  C  C   . THR D  1 135 ? -11.700 10.775  21.768  1.00 30.89  ? 135 THR G C   1 
ATOM   4330  O  O   . THR D  1 135 ? -10.616 11.350  21.840  1.00 31.02  ? 135 THR G O   1 
ATOM   4331  C  CB  . THR D  1 135 ? -10.830 8.519   21.451  1.00 33.23  ? 135 THR G CB  1 
ATOM   4332  O  OG1 . THR D  1 135 ? -11.009 8.827   20.054  1.00 33.87  ? 135 THR G OG1 1 
ATOM   4333  C  CG2 . THR D  1 135 ? -10.981 7.040   21.680  1.00 34.35  ? 135 THR G CG2 1 
ATOM   4334  N  N   . LYS D  1 136 ? -12.781 11.334  21.214  1.00 30.41  ? 136 LYS G N   1 
ATOM   4335  C  CA  . LYS D  1 136 ? -12.791 12.716  20.710  1.00 29.87  ? 136 LYS G CA  1 
ATOM   4336  C  C   . LYS D  1 136 ? -13.625 13.654  21.562  1.00 28.54  ? 136 LYS G C   1 
ATOM   4337  O  O   . LYS D  1 136 ? -13.140 14.716  21.963  1.00 27.98  ? 136 LYS G O   1 
ATOM   4338  C  CB  . LYS D  1 136 ? -13.293 12.747  19.262  1.00 30.79  ? 136 LYS G CB  1 
ATOM   4339  C  CG  . LYS D  1 136 ? -12.299 12.173  18.268  1.00 32.32  ? 136 LYS G CG  1 
ATOM   4340  C  CD  . LYS D  1 136 ? -12.939 11.872  16.914  1.00 33.55  ? 136 LYS G CD  1 
ATOM   4341  C  CE  . LYS D  1 136 ? -13.455 13.124  16.220  0.50 33.26  ? 136 LYS G CE  1 
ATOM   4342  N  NZ  . LYS D  1 136 ? -13.789 12.848  14.795  0.50 34.81  ? 136 LYS G NZ  1 
ATOM   4343  N  N   . THR D  1 137 ? -14.889 13.288  21.804  1.00 28.15  ? 137 THR G N   1 
ATOM   4344  C  CA  . THR D  1 137 ? -15.834 14.144  22.536  1.00 27.01  ? 137 THR G CA  1 
ATOM   4345  C  C   . THR D  1 137 ? -16.356 13.578  23.860  1.00 26.37  ? 137 THR G C   1 
ATOM   4346  O  O   . THR D  1 137 ? -16.938 14.316  24.650  1.00 25.61  ? 137 THR G O   1 
ATOM   4347  C  CB  . THR D  1 137 ? -17.069 14.470  21.657  1.00 27.32  ? 137 THR G CB  1 
ATOM   4348  O  OG1 . THR D  1 137 ? -17.808 13.274  21.393  1.00 28.06  ? 137 THR G OG1 1 
ATOM   4349  C  CG2 . THR D  1 137 ? -16.631 15.088  20.340  1.00 27.99  ? 137 THR G CG2 1 
ATOM   4350  N  N   . GLY D  1 138 ? -16.164 12.283  24.095  1.00 26.70  ? 138 GLY G N   1 
ATOM   4351  C  CA  . GLY D  1 138 ? -16.798 11.594  25.202  1.00 26.48  ? 138 GLY G CA  1 
ATOM   4352  C  C   . GLY D  1 138 ? -18.308 11.326  25.060  1.00 26.37  ? 138 GLY G C   1 
ATOM   4353  O  O   . GLY D  1 138 ? -18.959 11.020  26.052  1.00 26.13  ? 138 GLY G O   1 
ATOM   4354  N  N   . ASN D  1 139 ? -18.843 11.423  23.838  1.00 26.62  ? 139 ASN G N   1 
ATOM   4355  C  CA  . ASN D  1 139 ? -20.251 11.123  23.527  1.00 27.00  ? 139 ASN G CA  1 
ATOM   4356  C  C   . ASN D  1 139 ? -21.246 11.978  24.319  1.00 26.20  ? 139 ASN G C   1 
ATOM   4357  O  O   . ASN D  1 139 ? -22.302 11.495  24.701  1.00 26.59  ? 139 ASN G O   1 
ATOM   4358  C  CB  . ASN D  1 139 ? -20.550 9.634   23.741  1.00 27.96  ? 139 ASN G CB  1 
ATOM   4359  C  CG  . ASN D  1 139 ? -19.866 8.760   22.729  1.00 29.06  ? 139 ASN G CG  1 
ATOM   4360  O  OD1 . ASN D  1 139 ? -20.204 8.796   21.554  1.00 29.77  ? 139 ASN G OD1 1 
ATOM   4361  N  ND2 . ASN D  1 139 ? -18.892 7.966   23.178  1.00 29.44  ? 139 ASN G ND2 1 
ATOM   4362  N  N   . ALA D  1 140 ? -20.893 13.235  24.566  1.00 25.29  ? 140 ALA G N   1 
ATOM   4363  C  CA  . ALA D  1 140 ? -21.677 14.111  25.437  1.00 24.72  ? 140 ALA G CA  1 
ATOM   4364  C  C   . ALA D  1 140 ? -22.817 14.826  24.706  1.00 24.95  ? 140 ALA G C   1 
ATOM   4365  O  O   . ALA D  1 140 ? -23.543 15.608  25.322  1.00 24.67  ? 140 ALA G O   1 
ATOM   4366  C  CB  . ALA D  1 140 ? -20.767 15.114  26.148  1.00 23.91  ? 140 ALA G CB  1 
ATOM   4367  N  N   . GLY D  1 141 ? -22.980 14.553  23.408  1.00 25.69  ? 141 GLY G N   1 
ATOM   4368  C  CA  . GLY D  1 141 ? -24.114 15.036  22.634  1.00 26.28  ? 141 GLY G CA  1 
ATOM   4369  C  C   . GLY D  1 141 ? -23.953 16.500  22.283  1.00 25.86  ? 141 GLY G C   1 
ATOM   4370  O  O   . GLY D  1 141 ? -22.845 17.012  22.218  1.00 25.21  ? 141 GLY G O   1 
ATOM   4371  N  N   . SER D  1 142 ? -25.076 17.180  22.088  1.00 26.26  ? 142 SER G N   1 
ATOM   4372  C  CA  . SER D  1 142 ? -25.060 18.527  21.537  1.00 26.28  ? 142 SER G CA  1 
ATOM   4373  C  C   . SER D  1 142 ? -24.608 19.564  22.569  1.00 25.24  ? 142 SER G C   1 
ATOM   4374  O  O   . SER D  1 142 ? -24.608 19.322  23.777  1.00 24.64  ? 142 SER G O   1 
ATOM   4375  C  CB  . SER D  1 142 ? -26.447 18.887  20.996  1.00 27.41  ? 142 SER G CB  1 
ATOM   4376  O  OG  . SER D  1 142 ? -27.361 18.903  22.067  1.00 27.31  ? 142 SER G OG  1 
ATOM   4377  N  N   . ARG D  1 143 ? -24.264 20.733  22.055  1.00 25.23  ? 143 ARG G N   1 
ATOM   4378  C  CA  . ARG D  1 143 ? -23.812 21.861  22.843  1.00 24.56  ? 143 ARG G CA  1 
ATOM   4379  C  C   . ARG D  1 143 ? -25.043 22.658  23.274  1.00 24.92  ? 143 ARG G C   1 
ATOM   4380  O  O   . ARG D  1 143 ? -25.740 23.221  22.432  1.00 25.82  ? 143 ARG G O   1 
ATOM   4381  C  CB  . ARG D  1 143 ? -22.859 22.700  21.991  1.00 24.71  ? 143 ARG G CB  1 
ATOM   4382  C  CG  . ARG D  1 143 ? -21.707 21.858  21.449  1.00 24.67  ? 143 ARG G CG  1 
ATOM   4383  C  CD  . ARG D  1 143 ? -20.656 22.643  20.681  1.00 24.92  ? 143 ARG G CD  1 
ATOM   4384  N  NE  . ARG D  1 143 ? -19.662 21.721  20.129  1.00 25.11  ? 143 ARG G NE  1 
ATOM   4385  C  CZ  . ARG D  1 143 ? -18.545 22.070  19.480  1.00 25.43  ? 143 ARG G CZ  1 
ATOM   4386  N  NH1 . ARG D  1 143 ? -18.214 23.352  19.282  1.00 25.54  ? 143 ARG G NH1 1 
ATOM   4387  N  NH2 . ARG D  1 143 ? -17.739 21.111  19.034  1.00 25.77  ? 143 ARG G NH2 1 
ATOM   4388  N  N   . LEU D  1 144 ? -25.338 22.671  24.574  1.00 24.40  ? 144 LEU G N   1 
ATOM   4389  C  CA  . LEU D  1 144 ? -26.592 23.267  25.070  1.00 24.95  ? 144 LEU G CA  1 
ATOM   4390  C  C   . LEU D  1 144 ? -26.461 24.756  25.366  1.00 24.86  ? 144 LEU G C   1 
ATOM   4391  O  O   . LEU D  1 144 ? -27.412 25.514  25.189  1.00 25.71  ? 144 LEU G O   1 
ATOM   4392  C  CB  . LEU D  1 144 ? -27.079 22.537  26.328  1.00 24.83  ? 144 LEU G CB  1 
ATOM   4393  C  CG  . LEU D  1 144 ? -27.551 21.085  26.177  1.00 25.20  ? 144 LEU G CG  1 
ATOM   4394  C  CD1 . LEU D  1 144 ? -28.070 20.605  27.531  1.00 25.29  ? 144 LEU G CD1 1 
ATOM   4395  C  CD2 . LEU D  1 144 ? -28.630 20.948  25.105  1.00 26.39  ? 144 LEU G CD2 1 
ATOM   4396  N  N   . ALA D  1 145 ? -25.305 25.151  25.877  1.00 23.93  ? 145 ALA G N   1 
ATOM   4397  C  CA  . ALA D  1 145 ? -25.010 26.548  26.170  1.00 23.97  ? 145 ALA G CA  1 
ATOM   4398  C  C   . ALA D  1 145 ? -23.500 26.736  26.180  1.00 23.26  ? 145 ALA G C   1 
ATOM   4399  O  O   . ALA D  1 145 ? -22.762 25.792  26.467  1.00 22.64  ? 145 ALA G O   1 
ATOM   4400  C  CB  . ALA D  1 145 ? -25.585 26.954  27.514  1.00 24.13  ? 145 ALA G CB  1 
ATOM   4401  N  N   . ALA D  1 146 ? -23.075 27.955  25.875  1.00 23.47  ? 146 ALA G N   1 
ATOM   4402  C  CA  . ALA D  1 146 ? -21.671 28.274  25.672  1.00 23.17  ? 146 ALA G CA  1 
ATOM   4403  C  C   . ALA D  1 146 ? -21.442 29.735  25.951  1.00 23.61  ? 146 ALA G C   1 
ATOM   4404  O  O   . ALA D  1 146 ? -22.370 30.545  25.884  1.00 24.28  ? 146 ALA G O   1 
ATOM   4405  C  CB  . ALA D  1 146 ? -21.263 27.961  24.237  1.00 23.38  ? 146 ALA G CB  1 
ATOM   4406  N  N   . GLY D  1 147 ? -20.197 30.065  26.261  1.00 23.39  ? 147 GLY G N   1 
ATOM   4407  C  CA  . GLY D  1 147 ? -19.767 31.452  26.315  1.00 23.99  ? 147 GLY G CA  1 
ATOM   4408  C  C   . GLY D  1 147 ? -18.263 31.559  26.202  1.00 23.91  ? 147 GLY G C   1 
ATOM   4409  O  O   . GLY D  1 147 ? -17.533 30.584  26.438  1.00 23.26  ? 147 GLY G O   1 
ATOM   4410  N  N   . VAL D  1 148 ? -17.805 32.754  25.858  1.00 24.63  ? 148 VAL G N   1 
ATOM   4411  C  CA  . VAL D  1 148 ? -16.383 33.027  25.797  1.00 24.90  ? 148 VAL G CA  1 
ATOM   4412  C  C   . VAL D  1 148 ? -15.901 33.327  27.212  1.00 25.00  ? 148 VAL G C   1 
ATOM   4413  O  O   . VAL D  1 148 ? -16.539 34.073  27.958  1.00 25.37  ? 148 VAL G O   1 
ATOM   4414  C  CB  . VAL D  1 148 ? -16.063 34.195  24.849  1.00 25.89  ? 148 VAL G CB  1 
ATOM   4415  C  CG1 . VAL D  1 148 ? -14.553 34.430  24.761  1.00 26.30  ? 148 VAL G CG1 1 
ATOM   4416  C  CG2 . VAL D  1 148 ? -16.641 33.913  23.467  1.00 26.08  ? 148 VAL G CG2 1 
ATOM   4417  N  N   . ILE D  1 149 ? -14.756 32.753  27.561  1.00 24.87  ? 149 ILE G N   1 
ATOM   4418  C  CA  . ILE D  1 149 ? -14.159 32.944  28.879  1.00 25.26  ? 149 ILE G CA  1 
ATOM   4419  C  C   . ILE D  1 149 ? -13.384 34.255  28.867  1.00 26.37  ? 149 ILE G C   1 
ATOM   4420  O  O   . ILE D  1 149 ? -12.467 34.409  28.089  1.00 26.76  ? 149 ILE G O   1 
ATOM   4421  C  CB  . ILE D  1 149 ? -13.249 31.761  29.255  1.00 24.89  ? 149 ILE G CB  1 
ATOM   4422  C  CG1 . ILE D  1 149 ? -14.058 30.451  29.261  1.00 23.96  ? 149 ILE G CG1 1 
ATOM   4423  C  CG2 . ILE D  1 149 ? -12.604 32.000  30.621  1.00 25.57  ? 149 ILE G CG2 1 
ATOM   4424  C  CD1 . ILE D  1 149 ? -13.200 29.202  29.191  1.00 23.71  ? 149 ILE G CD1 1 
ATOM   4425  N  N   . GLY D  1 150 ? -13.758 35.190  29.730  1.00 27.11  ? 150 GLY G N   1 
ATOM   4426  C  CA  . GLY D  1 150 ? -13.167 36.526  29.742  1.00 28.45  ? 150 GLY G CA  1 
ATOM   4427  C  C   . GLY D  1 150 ? -12.440 36.844  31.033  1.00 29.39  ? 150 GLY G C   1 
ATOM   4428  O  O   . GLY D  1 150 ? -12.698 36.224  32.065  1.00 29.13  ? 150 GLY G O   1 
ATOM   4429  N  N   . ILE D  1 151 ? -11.550 37.831  30.969  1.00 30.73  ? 151 ILE G N   1 
ATOM   4430  C  CA  . ILE D  1 151 ? -10.790 38.296  32.135  1.00 32.09  ? 151 ILE G CA  1 
ATOM   4431  C  C   . ILE D  1 151 ? -11.769 38.952  33.105  1.00 32.78  ? 151 ILE G C   1 
ATOM   4432  O  O   . ILE D  1 151 ? -12.599 39.743  32.680  1.00 33.03  ? 151 ILE G O   1 
ATOM   4433  C  CB  . ILE D  1 151 ? -9.674  39.300  31.725  1.00 33.51  ? 151 ILE G CB  1 
ATOM   4434  C  CG1 . ILE D  1 151 ? -8.648  38.603  30.829  1.00 33.19  ? 151 ILE G CG1 1 
ATOM   4435  C  CG2 . ILE D  1 151 ? -8.997  39.894  32.959  1.00 35.09  ? 151 ILE G CG2 1 
ATOM   4436  C  CD1 . ILE D  1 151 ? -7.639  39.522  30.165  1.00 34.57  ? 151 ILE G CD1 1 
ATOM   4437  N  N   . ALA D  1 152 ? -11.690 38.595  34.388  1.00 33.29  ? 152 ALA G N   1 
ATOM   4438  C  CA  . ALA D  1 152 ? -12.565 39.156  35.436  1.00 34.20  ? 152 ALA G CA  1 
ATOM   4439  C  C   . ALA D  1 152 ? -11.758 39.957  36.437  1.00 36.26  ? 152 ALA G C   1 
ATOM   4440  O  O   . ALA D  1 152 ? -10.548 39.733  36.595  1.00 36.75  ? 152 ALA G O   1 
ATOM   4441  C  CB  . ALA D  1 152 ? -13.316 38.051  36.156  1.00 33.31  ? 152 ALA G CB  1 
ATOM   4442  N  N   . GLN D  1 153 ? -12.433 40.885  37.113  1.00 37.66  ? 153 GLN G N   1 
ATOM   4443  C  CA  . GLN D  1 153 ? -11.793 41.771  38.086  1.00 40.03  ? 153 GLN G CA  1 
ATOM   4444  C  C   . GLN D  1 153 ? -11.430 41.020  39.363  1.00 40.68  ? 153 GLN G C   1 
ATOM   4445  O  O   . GLN D  1 153 ? -12.142 40.109  39.794  1.00 39.86  ? 153 GLN G O   1 
ATOM   4446  C  CB  . GLN D  1 153 ? -12.706 42.954  38.431  1.00 41.40  ? 153 GLN G CB  1 
ATOM   4447  C  CG  . GLN D  1 153 ? -12.018 44.043  39.247  1.00 43.94  ? 153 GLN G CG  1 
ATOM   4448  C  CD  . GLN D  1 153 ? -12.924 45.228  39.521  1.00 45.44  ? 153 GLN G CD  1 
ATOM   4449  O  OE1 . GLN D  1 153 ? -14.109 45.067  39.798  1.00 45.09  ? 153 GLN G OE1 1 
ATOM   4450  N  NE2 . GLN D  1 153 ? -12.363 46.425  39.457  1.00 47.37  ? 153 GLN G NE2 1 
ATOM   4451  O  OXT . GLN D  1 153 ? -10.422 41.336  39.997  1.00 42.40  ? 153 GLN G OXT 1 
ATOM   4452  N  N   . ALA E  1 1   ? 14.253  -21.483 15.111  1.00 78.39  ? 1   ALA I N   1 
ATOM   4453  C  CA  . ALA E  1 1   ? 14.838  -22.660 15.824  1.00 75.18  ? 1   ALA I CA  1 
ATOM   4454  C  C   . ALA E  1 1   ? 15.171  -22.320 17.273  1.00 72.03  ? 1   ALA I C   1 
ATOM   4455  O  O   . ALA E  1 1   ? 15.439  -21.160 17.594  1.00 72.52  ? 1   ALA I O   1 
ATOM   4456  C  CB  . ALA E  1 1   ? 16.083  -23.155 15.097  1.00 76.13  ? 1   ALA I CB  1 
ATOM   4457  N  N   . THR E  1 2   ? 15.134  -23.331 18.139  1.00 69.07  ? 2   THR I N   1 
ATOM   4458  C  CA  . THR E  1 2   ? 15.578  -23.192 19.526  1.00 66.15  ? 2   THR I CA  1 
ATOM   4459  C  C   . THR E  1 2   ? 16.938  -23.869 19.666  1.00 65.00  ? 2   THR I C   1 
ATOM   4460  O  O   . THR E  1 2   ? 17.146  -24.968 19.153  1.00 65.06  ? 2   THR I O   1 
ATOM   4461  C  CB  . THR E  1 2   ? 14.587  -23.821 20.533  1.00 63.86  ? 2   THR I CB  1 
ATOM   4462  O  OG1 . THR E  1 2   ? 13.245  -23.468 20.185  1.00 65.48  ? 2   THR I OG1 1 
ATOM   4463  C  CG2 . THR E  1 2   ? 14.872  -23.330 21.952  1.00 61.56  ? 2   THR I CG2 1 
ATOM   4464  N  N   . LYS E  1 3   ? 17.854  -23.192 20.355  1.00 64.24  ? 3   LYS I N   1 
ATOM   4465  C  CA  . LYS E  1 3   ? 19.179  -23.714 20.657  1.00 63.29  ? 3   LYS I CA  1 
ATOM   4466  C  C   . LYS E  1 3   ? 19.382  -23.773 22.162  1.00 60.50  ? 3   LYS I C   1 
ATOM   4467  O  O   . LYS E  1 3   ? 18.773  -23.004 22.917  1.00 59.77  ? 3   LYS I O   1 
ATOM   4468  C  CB  . LYS E  1 3   ? 20.258  -22.814 20.060  1.00 65.65  ? 3   LYS I CB  1 
ATOM   4469  C  CG  . LYS E  1 3   ? 20.326  -22.829 18.542  1.00 68.78  ? 3   LYS I CG  1 
ATOM   4470  C  CD  . LYS E  1 3   ? 21.707  -22.436 18.027  1.00 70.92  ? 3   LYS I CD  1 
ATOM   4471  C  CE  . LYS E  1 3   ? 22.745  -23.527 18.286  1.00 69.89  ? 3   LYS I CE  1 
ATOM   4472  N  NZ  . LYS E  1 3   ? 23.968  -23.363 17.449  1.00 72.80  ? 3   LYS I NZ  1 
ATOM   4473  N  N   . ALA E  1 4   ? 20.252  -24.686 22.583  1.00 59.14  ? 4   ALA I N   1 
ATOM   4474  C  CA  . ALA E  1 4   ? 20.733  -24.735 23.958  1.00 56.98  ? 4   ALA I CA  1 
ATOM   4475  C  C   . ALA E  1 4   ? 22.154  -25.306 24.011  1.00 57.11  ? 4   ALA I C   1 
ATOM   4476  O  O   . ALA E  1 4   ? 22.647  -25.876 23.036  1.00 58.46  ? 4   ALA I O   1 
ATOM   4477  C  CB  . ALA E  1 4   ? 19.785  -25.551 24.831  1.00 54.64  ? 4   ALA I CB  1 
ATOM   4478  N  N   . VAL E  1 5   ? 22.800  -25.138 25.159  1.00 55.89  ? 5   VAL I N   1 
ATOM   4479  C  CA  . VAL E  1 5   ? 24.177  -25.571 25.350  1.00 56.30  ? 5   VAL I CA  1 
ATOM   4480  C  C   . VAL E  1 5   ? 24.404  -25.992 26.801  1.00 54.18  ? 5   VAL I C   1 
ATOM   4481  O  O   . VAL E  1 5   ? 23.724  -25.511 27.717  1.00 52.83  ? 5   VAL I O   1 
ATOM   4482  C  CB  . VAL E  1 5   ? 25.167  -24.456 24.930  1.00 58.75  ? 5   VAL I CB  1 
ATOM   4483  C  CG1 . VAL E  1 5   ? 25.086  -23.258 25.873  1.00 58.42  ? 5   VAL I CG1 1 
ATOM   4484  C  CG2 . VAL E  1 5   ? 26.595  -24.989 24.831  1.00 59.93  ? 5   VAL I CG2 1 
ATOM   4485  N  N   . CYS E  1 6   ? 25.354  -26.903 26.991  1.00 54.15  ? 6   CYS I N   1 
ATOM   4486  C  CA  . CYS E  1 6   ? 25.712  -27.408 28.303  1.00 52.61  ? 6   CYS I CA  1 
ATOM   4487  C  C   . CYS E  1 6   ? 27.228  -27.574 28.414  1.00 54.06  ? 6   CYS I C   1 
ATOM   4488  O  O   . CYS E  1 6   ? 27.845  -28.205 27.560  1.00 55.43  ? 6   CYS I O   1 
ATOM   4489  C  CB  . CYS E  1 6   ? 25.022  -28.748 28.539  1.00 50.88  ? 6   CYS I CB  1 
ATOM   4490  S  SG  . CYS E  1 6   ? 25.280  -29.418 30.191  1.00 49.15  ? 6   CYS I SG  1 
ATOM   4491  N  N   . VAL E  1 7   ? 27.810  -26.993 29.464  1.00 54.05  ? 7   VAL I N   1 
ATOM   4492  C  CA  . VAL E  1 7   ? 29.225  -27.158 29.791  1.00 55.56  ? 7   VAL I CA  1 
ATOM   4493  C  C   . VAL E  1 7   ? 29.332  -28.237 30.878  1.00 54.03  ? 7   VAL I C   1 
ATOM   4494  O  O   . VAL E  1 7   ? 28.970  -28.002 32.038  1.00 52.69  ? 7   VAL I O   1 
ATOM   4495  C  CB  . VAL E  1 7   ? 29.849  -25.829 30.276  1.00 56.99  ? 7   VAL I CB  1 
ATOM   4496  C  CG1 . VAL E  1 7   ? 31.345  -25.990 30.537  1.00 59.10  ? 7   VAL I CG1 1 
ATOM   4497  C  CG2 . VAL E  1 7   ? 29.589  -24.721 29.259  1.00 58.48  ? 7   VAL I CG2 1 
ATOM   4498  N  N   . LEU E  1 8   ? 29.802  -29.420 30.482  1.00 54.44  ? 8   LEU I N   1 
ATOM   4499  C  CA  . LEU E  1 8   ? 29.999  -30.542 31.404  1.00 53.44  ? 8   LEU I CA  1 
ATOM   4500  C  C   . LEU E  1 8   ? 31.316  -30.380 32.150  1.00 55.15  ? 8   LEU I C   1 
ATOM   4501  O  O   . LEU E  1 8   ? 32.370  -30.259 31.521  1.00 57.59  ? 8   LEU I O   1 
ATOM   4502  C  CB  . LEU E  1 8   ? 30.005  -31.867 30.643  1.00 53.55  ? 8   LEU I CB  1 
ATOM   4503  C  CG  . LEU E  1 8   ? 28.712  -32.249 29.920  1.00 52.16  ? 8   LEU I CG  1 
ATOM   4504  C  CD1 . LEU E  1 8   ? 28.950  -33.446 29.015  1.00 53.04  ? 8   LEU I CD1 1 
ATOM   4505  C  CD2 . LEU E  1 8   ? 27.598  -32.558 30.912  1.00 49.72  ? 8   LEU I CD2 1 
ATOM   4506  N  N   . LYS E  1 9   ? 31.239  -30.348 33.482  1.00 54.19  ? 9   LYS I N   1 
ATOM   4507  C  CA  . LYS E  1 9   ? 32.410  -30.303 34.368  1.00 55.86  ? 9   LYS I CA  1 
ATOM   4508  C  C   . LYS E  1 9   ? 32.187  -31.197 35.582  1.00 54.56  ? 9   LYS I C   1 
ATOM   4509  O  O   . LYS E  1 9   ? 31.044  -31.465 35.961  1.00 52.29  ? 9   LYS I O   1 
ATOM   4510  C  CB  . LYS E  1 9   ? 32.670  -28.873 34.846  1.00 56.85  ? 9   LYS I CB  1 
ATOM   4511  C  CG  . LYS E  1 9   ? 33.000  -27.875 33.749  1.00 58.66  ? 9   LYS I CG  1 
ATOM   4512  C  CD  . LYS E  1 9   ? 34.358  -28.149 33.110  1.00 61.68  ? 9   LYS I CD  1 
ATOM   4513  C  CE  . LYS E  1 9   ? 34.663  -27.156 31.999  1.00 63.74  ? 9   LYS I CE  1 
ATOM   4514  N  NZ  . LYS E  1 9   ? 34.788  -25.766 32.514  1.00 64.67  ? 9   LYS I NZ  1 
ATOM   4515  N  N   . GLY E  1 10  ? 33.281  -31.639 36.198  1.00 56.32  ? 10  GLY I N   1 
ATOM   4516  C  CA  . GLY E  1 10  ? 33.221  -32.530 37.364  1.00 55.67  ? 10  GLY I CA  1 
ATOM   4517  C  C   . GLY E  1 10  ? 34.421  -32.426 38.283  1.00 58.07  ? 10  GLY I C   1 
ATOM   4518  O  O   . GLY E  1 10  ? 35.202  -31.480 38.189  1.00 60.13  ? 10  GLY I O   1 
ATOM   4519  N  N   . ASP E  1 11  ? 34.555  -33.401 39.179  1.00 58.12  ? 11  ASP I N   1 
ATOM   4520  C  CA  . ASP E  1 11  ? 35.695  -33.471 40.103  1.00 60.69  ? 11  ASP I CA  1 
ATOM   4521  C  C   . ASP E  1 11  ? 36.955  -34.012 39.427  1.00 63.48  ? 11  ASP I C   1 
ATOM   4522  O  O   . ASP E  1 11  ? 38.064  -33.651 39.819  1.00 66.37  ? 11  ASP I O   1 
ATOM   4523  C  CB  . ASP E  1 11  ? 35.364  -34.351 41.319  1.00 60.05  ? 11  ASP I CB  1 
ATOM   4524  C  CG  . ASP E  1 11  ? 34.245  -33.780 42.187  1.00 57.96  ? 11  ASP I CG  1 
ATOM   4525  O  OD1 . ASP E  1 11  ? 33.993  -32.552 42.142  1.00 57.69  ? 11  ASP I OD1 1 
ATOM   4526  O  OD2 . ASP E  1 11  ? 33.621  -34.575 42.929  1.00 56.84  ? 11  ASP I OD2 1 
ATOM   4527  N  N   . GLY E  1 12  ? 36.777  -34.891 38.440  1.00 62.86  ? 12  GLY I N   1 
ATOM   4528  C  CA  . GLY E  1 12  ? 37.886  -35.510 37.714  1.00 65.59  ? 12  GLY I CA  1 
ATOM   4529  C  C   . GLY E  1 12  ? 38.275  -34.733 36.466  1.00 66.86  ? 12  GLY I C   1 
ATOM   4530  O  O   . GLY E  1 12  ? 37.975  -33.541 36.363  1.00 66.33  ? 12  GLY I O   1 
ATOM   4531  N  N   . PRO E  1 13  ? 38.935  -35.406 35.497  1.00 68.73  ? 13  PRO I N   1 
ATOM   4532  C  CA  . PRO E  1 13  ? 39.364  -34.756 34.259  1.00 70.44  ? 13  PRO I CA  1 
ATOM   4533  C  C   . PRO E  1 13  ? 38.301  -34.715 33.147  1.00 68.15  ? 13  PRO I C   1 
ATOM   4534  O  O   . PRO E  1 13  ? 38.612  -34.288 32.034  1.00 69.73  ? 13  PRO I O   1 
ATOM   4535  C  CB  . PRO E  1 13  ? 40.551  -35.624 33.827  1.00 73.87  ? 13  PRO I CB  1 
ATOM   4536  C  CG  . PRO E  1 13  ? 40.164  -36.994 34.269  1.00 72.50  ? 13  PRO I CG  1 
ATOM   4537  C  CD  . PRO E  1 13  ? 39.313  -36.833 35.506  1.00 69.67  ? 13  PRO I CD  1 
ATOM   4538  N  N   . VAL E  1 14  ? 37.068  -35.139 33.437  1.00 64.78  ? 14  VAL I N   1 
ATOM   4539  C  CA  . VAL E  1 14  ? 36.018  -35.213 32.420  1.00 62.86  ? 14  VAL I CA  1 
ATOM   4540  C  C   . VAL E  1 14  ? 35.420  -33.820 32.202  1.00 61.86  ? 14  VAL I C   1 
ATOM   4541  O  O   . VAL E  1 14  ? 34.960  -33.172 33.150  1.00 60.39  ? 14  VAL I O   1 
ATOM   4542  C  CB  . VAL E  1 14  ? 34.912  -36.230 32.790  1.00 60.04  ? 14  VAL I CB  1 
ATOM   4543  C  CG1 . VAL E  1 14  ? 33.874  -36.332 31.676  1.00 58.60  ? 14  VAL I CG1 1 
ATOM   4544  C  CG2 . VAL E  1 14  ? 35.521  -37.602 33.062  1.00 61.25  ? 14  VAL I CG2 1 
ATOM   4545  N  N   . GLN E  1 15  ? 35.455  -33.363 30.952  1.00 62.95  ? 15  GLN I N   1 
ATOM   4546  C  CA  . GLN E  1 15  ? 34.864  -32.083 30.570  1.00 62.33  ? 15  GLN I CA  1 
ATOM   4547  C  C   . GLN E  1 15  ? 34.447  -32.082 29.098  1.00 62.76  ? 15  GLN I C   1 
ATOM   4548  O  O   . GLN E  1 15  ? 34.997  -32.837 28.286  1.00 64.50  ? 15  GLN I O   1 
ATOM   4549  C  CB  . GLN E  1 15  ? 35.827  -30.923 30.865  1.00 64.69  ? 15  GLN I CB  1 
ATOM   4550  C  CG  . GLN E  1 15  ? 37.209  -31.059 30.237  1.00 68.48  ? 15  GLN I CG  1 
ATOM   4551  C  CD  . GLN E  1 15  ? 38.112  -29.867 30.513  1.00 71.09  ? 15  GLN I CD  1 
ATOM   4552  O  OE1 . GLN E  1 15  ? 37.649  -28.734 30.643  1.00 70.46  ? 15  GLN I OE1 1 
ATOM   4553  N  NE2 . GLN E  1 15  ? 39.412  -30.119 30.593  1.00 74.38  ? 15  GLN I NE2 1 
ATOM   4554  N  N   . GLY E  1 16  ? 33.469  -31.238 28.769  1.00 61.34  ? 16  GLY I N   1 
ATOM   4555  C  CA  . GLY E  1 16  ? 32.953  -31.146 27.404  1.00 61.84  ? 16  GLY I CA  1 
ATOM   4556  C  C   . GLY E  1 16  ? 31.894  -30.075 27.194  1.00 60.57  ? 16  GLY I C   1 
ATOM   4557  O  O   . GLY E  1 16  ? 31.353  -29.528 28.155  1.00 58.74  ? 16  GLY I O   1 
ATOM   4558  N  N   . ILE E  1 17  ? 31.621  -29.784 25.922  1.00 61.82  ? 17  ILE I N   1 
ATOM   4559  C  CA  . ILE E  1 17  ? 30.567  -28.855 25.505  1.00 61.13  ? 17  ILE I CA  1 
ATOM   4560  C  C   . ILE E  1 17  ? 29.590  -29.626 24.614  1.00 60.41  ? 17  ILE I C   1 
ATOM   4561  O  O   . ILE E  1 17  ? 29.966  -30.074 23.533  1.00 62.38  ? 17  ILE I O   1 
ATOM   4562  C  CB  . ILE E  1 17  ? 31.139  -27.633 24.733  1.00 63.95  ? 17  ILE I CB  1 
ATOM   4563  C  CG1 . ILE E  1 17  ? 31.947  -26.731 25.678  1.00 64.68  ? 17  ILE I CG1 1 
ATOM   4564  C  CG2 . ILE E  1 17  ? 30.021  -26.818 24.073  1.00 63.68  ? 17  ILE I CG2 1 
ATOM   4565  C  CD1 . ILE E  1 17  ? 32.832  -25.718 24.975  1.00 68.10  ? 17  ILE I CD1 1 
ATOM   4566  N  N   . ILE E  1 18  ? 28.348  -29.772 25.081  1.00 57.87  ? 18  ILE I N   1 
ATOM   4567  C  CA  . ILE E  1 18  ? 27.264  -30.377 24.303  1.00 57.28  ? 18  ILE I CA  1 
ATOM   4568  C  C   . ILE E  1 18  ? 26.282  -29.292 23.866  1.00 57.37  ? 18  ILE I C   1 
ATOM   4569  O  O   . ILE E  1 18  ? 25.907  -28.416 24.657  1.00 56.30  ? 18  ILE I O   1 
ATOM   4570  C  CB  . ILE E  1 18  ? 26.523  -31.461 25.119  1.00 54.76  ? 18  ILE I CB  1 
ATOM   4571  C  CG1 . ILE E  1 18  ? 27.493  -32.583 25.537  1.00 54.90  ? 18  ILE I CG1 1 
ATOM   4572  C  CG2 . ILE E  1 18  ? 25.333  -32.023 24.341  1.00 54.43  ? 18  ILE I CG2 1 
ATOM   4573  C  CD1 . ILE E  1 18  ? 28.169  -33.315 24.390  1.00 57.16  ? 18  ILE I CD1 1 
ATOM   4574  N  N   . ASN E  1 19  ? 25.871  -29.370 22.602  1.00 58.88  ? 19  ASN I N   1 
ATOM   4575  C  CA  . ASN E  1 19  ? 24.947  -28.418 21.996  1.00 59.55  ? 19  ASN I CA  1 
ATOM   4576  C  C   . ASN E  1 19  ? 23.631  -29.113 21.698  1.00 58.55  ? 19  ASN I C   1 
ATOM   4577  O  O   . ASN E  1 19  ? 23.605  -30.316 21.424  1.00 58.35  ? 19  ASN I O   1 
ATOM   4578  C  CB  . ASN E  1 19  ? 25.530  -27.866 20.693  1.00 62.79  ? 19  ASN I CB  1 
ATOM   4579  C  CG  . ASN E  1 19  ? 26.890  -27.233 20.888  1.00 64.33  ? 19  ASN I CG  1 
ATOM   4580  O  OD1 . ASN E  1 19  ? 27.008  -26.154 21.468  1.00 64.20  ? 19  ASN I OD1 1 
ATOM   4581  N  ND2 . ASN E  1 19  ? 27.930  -27.903 20.403  1.00 66.04  ? 19  ASN I ND2 1 
ATOM   4582  N  N   . PHE E  1 20  ? 22.548  -28.340 21.752  1.00 58.17  ? 20  PHE I N   1 
ATOM   4583  C  CA  . PHE E  1 20  ? 21.220  -28.796 21.360  1.00 57.91  ? 20  PHE I CA  1 
ATOM   4584  C  C   . PHE E  1 20  ? 20.651  -27.818 20.340  1.00 60.20  ? 20  PHE I C   1 
ATOM   4585  O  O   . PHE E  1 20  ? 20.892  -26.609 20.422  1.00 60.99  ? 20  PHE I O   1 
ATOM   4586  C  CB  . PHE E  1 20  ? 20.283  -28.875 22.564  1.00 55.39  ? 20  PHE I CB  1 
ATOM   4587  C  CG  . PHE E  1 20  ? 20.782  -29.758 23.668  1.00 53.30  ? 20  PHE I CG  1 
ATOM   4588  C  CD1 . PHE E  1 20  ? 21.693  -29.278 24.603  1.00 52.54  ? 20  PHE I CD1 1 
ATOM   4589  C  CD2 . PHE E  1 20  ? 20.337  -31.070 23.781  1.00 52.38  ? 20  PHE I CD2 1 
ATOM   4590  C  CE1 . PHE E  1 20  ? 22.154  -30.091 25.628  1.00 50.92  ? 20  PHE I CE1 1 
ATOM   4591  C  CE2 . PHE E  1 20  ? 20.789  -31.887 24.804  1.00 50.70  ? 20  PHE I CE2 1 
ATOM   4592  C  CZ  . PHE E  1 20  ? 21.701  -31.398 25.728  1.00 49.99  ? 20  PHE I CZ  1 
ATOM   4593  N  N   . GLU E  1 21  ? 19.902  -28.352 19.381  1.00 61.52  ? 21  GLU I N   1 
ATOM   4594  C  CA  . GLU E  1 21  ? 19.258  -27.543 18.356  1.00 64.03  ? 21  GLU I CA  1 
ATOM   4595  C  C   . GLU E  1 21  ? 17.996  -28.247 17.869  1.00 64.45  ? 21  GLU I C   1 
ATOM   4596  O  O   . GLU E  1 21  ? 18.038  -29.414 17.484  1.00 64.61  ? 21  GLU I O   1 
ATOM   4597  C  CB  . GLU E  1 21  ? 20.217  -27.264 17.189  1.00 67.02  ? 21  GLU I CB  1 
ATOM   4598  C  CG  . GLU E  1 21  ? 19.636  -26.327 16.135  1.00 69.98  ? 21  GLU I CG  1 
ATOM   4599  C  CD  . GLU E  1 21  ? 20.664  -25.405 15.489  1.00 72.61  ? 21  GLU I CD  1 
ATOM   4600  O  OE1 . GLU E  1 21  ? 21.782  -25.859 15.171  1.00 73.50  ? 21  GLU I OE1 1 
ATOM   4601  O  OE2 . GLU E  1 21  ? 20.341  -24.212 15.289  1.00 74.10  ? 21  GLU I OE2 1 
ATOM   4602  N  N   . GLN E  1 22  ? 16.878  -27.527 17.912  1.00 64.86  ? 22  GLN I N   1 
ATOM   4603  C  CA  . GLN E  1 22  ? 15.581  -28.045 17.505  1.00 65.64  ? 22  GLN I CA  1 
ATOM   4604  C  C   . GLN E  1 22  ? 14.972  -27.035 16.540  1.00 68.72  ? 22  GLN I C   1 
ATOM   4605  O  O   . GLN E  1 22  ? 14.615  -25.925 16.937  1.00 68.80  ? 22  GLN I O   1 
ATOM   4606  C  CB  . GLN E  1 22  ? 14.700  -28.243 18.736  1.00 63.13  ? 22  GLN I CB  1 
ATOM   4607  C  CG  . GLN E  1 22  ? 13.355  -28.895 18.464  1.00 63.90  ? 22  GLN I CG  1 
ATOM   4608  C  CD  . GLN E  1 22  ? 12.532  -29.088 19.725  1.00 61.67  ? 22  GLN I CD  1 
ATOM   4609  O  OE1 . GLN E  1 22  ? 12.766  -28.432 20.740  1.00 59.90  ? 22  GLN I OE1 1 
ATOM   4610  N  NE2 . GLN E  1 22  ? 11.561  -29.991 19.668  1.00 62.01  ? 22  GLN I NE2 1 
ATOM   4611  N  N   . LYS E  1 23  ? 14.879  -27.430 15.272  1.00 71.50  ? 23  LYS I N   1 
ATOM   4612  C  CA  . LYS E  1 23  ? 14.436  -26.555 14.180  1.00 75.04  ? 23  LYS I CA  1 
ATOM   4613  C  C   . LYS E  1 23  ? 12.989  -26.091 14.346  1.00 75.71  ? 23  LYS I C   1 
ATOM   4614  O  O   . LYS E  1 23  ? 12.688  -24.905 14.180  1.00 77.31  ? 23  LYS I O   1 
ATOM   4615  C  CB  . LYS E  1 23  ? 14.589  -27.294 12.845  1.00 77.92  ? 23  LYS I CB  1 
ATOM   4616  C  CG  . LYS E  1 23  ? 14.379  -26.449 11.597  1.00 82.06  ? 23  LYS I CG  1 
ATOM   4617  C  CD  . LYS E  1 23  ? 14.459  -27.309 10.341  1.00 84.97  ? 23  LYS I CD  1 
ATOM   4618  C  CE  . LYS E  1 23  ? 15.894  -27.628 9.938   1.00 85.45  ? 23  LYS I CE  1 
ATOM   4619  N  NZ  . LYS E  1 23  ? 16.444  -26.601 9.008   1.00 88.90  ? 23  LYS I NZ  1 
ATOM   4620  N  N   . GLU E  1 24  ? 12.104  -27.037 14.652  1.00 74.82  ? 24  GLU I N   1 
ATOM   4621  C  CA  . GLU E  1 24  ? 10.684  -26.761 14.848  1.00 75.66  ? 24  GLU I CA  1 
ATOM   4622  C  C   . GLU E  1 24  ? 10.253  -27.321 16.192  1.00 72.42  ? 24  GLU I C   1 
ATOM   4623  O  O   . GLU E  1 24  ? 10.777  -28.345 16.638  1.00 70.26  ? 24  GLU I O   1 
ATOM   4624  C  CB  . GLU E  1 24  ? 9.863   -27.402 13.730  1.00 78.83  ? 24  GLU I CB  1 
ATOM   4625  N  N   . SER E  1 25  ? 9.288   -26.657 16.822  1.00 72.37  ? 25  SER I N   1 
ATOM   4626  C  CA  . SER E  1 25  ? 8.791   -27.033 18.150  1.00 69.70  ? 25  SER I CA  1 
ATOM   4627  C  C   . SER E  1 25  ? 8.342   -28.496 18.262  1.00 69.03  ? 25  SER I C   1 
ATOM   4628  O  O   . SER E  1 25  ? 8.526   -29.120 19.312  1.00 66.26  ? 25  SER I O   1 
ATOM   4629  C  CB  . SER E  1 25  ? 7.629   -26.121 18.540  1.00 70.91  ? 25  SER I CB  1 
ATOM   4630  O  OG  . SER E  1 25  ? 6.576   -26.237 17.599  1.00 74.29  ? 25  SER I OG  1 
ATOM   4631  N  N   . ASN E  1 26  ? 7.757   -29.024 17.184  1.00 71.76  ? 26  ASN I N   1 
ATOM   4632  C  CA  . ASN E  1 26  ? 7.333   -30.433 17.116  1.00 71.76  ? 26  ASN I CA  1 
ATOM   4633  C  C   . ASN E  1 26  ? 8.331   -31.344 16.365  1.00 71.86  ? 26  ASN I C   1 
ATOM   4634  O  O   . ASN E  1 26  ? 7.969   -32.441 15.926  1.00 72.92  ? 26  ASN I O   1 
ATOM   4635  C  CB  . ASN E  1 26  ? 5.924   -30.536 16.505  1.00 75.07  ? 26  ASN I CB  1 
ATOM   4636  C  CG  . ASN E  1 26  ? 5.877   -30.122 15.045  1.00 78.79  ? 26  ASN I CG  1 
ATOM   4637  O  OD1 . ASN E  1 26  ? 6.670   -29.295 14.592  1.00 79.17  ? 26  ASN I OD1 1 
ATOM   4638  N  ND2 . ASN E  1 26  ? 4.929   -30.684 14.306  1.00 81.86  ? 26  ASN I ND2 1 
ATOM   4639  N  N   . GLY E  1 27  ? 9.583   -30.896 16.252  1.00 70.94  ? 27  GLY I N   1 
ATOM   4640  C  CA  . GLY E  1 27  ? 10.624  -31.594 15.505  1.00 71.43  ? 27  GLY I CA  1 
ATOM   4641  C  C   . GLY E  1 27  ? 11.694  -32.163 16.419  1.00 68.26  ? 27  GLY I C   1 
ATOM   4642  O  O   . GLY E  1 27  ? 11.680  -31.929 17.641  1.00 65.61  ? 27  GLY I O   1 
ATOM   4643  N  N   . PRO E  1 28  ? 12.647  -32.908 15.836  1.00 68.71  ? 28  PRO I N   1 
ATOM   4644  C  CA  . PRO E  1 28  ? 13.659  -33.587 16.636  1.00 66.09  ? 28  PRO I CA  1 
ATOM   4645  C  C   . PRO E  1 28  ? 14.707  -32.629 17.200  1.00 64.63  ? 28  PRO I C   1 
ATOM   4646  O  O   . PRO E  1 28  ? 14.872  -31.519 16.700  1.00 66.06  ? 28  PRO I O   1 
ATOM   4647  C  CB  . PRO E  1 28  ? 14.291  -34.552 15.632  1.00 67.87  ? 28  PRO I CB  1 
ATOM   4648  C  CG  . PRO E  1 28  ? 14.176  -33.845 14.330  1.00 71.22  ? 28  PRO I CG  1 
ATOM   4649  C  CD  . PRO E  1 28  ? 12.890  -33.070 14.390  1.00 71.98  ? 28  PRO I CD  1 
ATOM   4650  N  N   . VAL E  1 29  ? 15.394  -33.066 18.247  1.00 62.03  ? 29  VAL I N   1 
ATOM   4651  C  CA  . VAL E  1 29  ? 16.488  -32.306 18.830  1.00 60.83  ? 29  VAL I CA  1 
ATOM   4652  C  C   . VAL E  1 29  ? 17.802  -32.929 18.364  1.00 61.54  ? 29  VAL I C   1 
ATOM   4653  O  O   . VAL E  1 29  ? 18.110  -34.076 18.710  1.00 60.51  ? 29  VAL I O   1 
ATOM   4654  C  CB  . VAL E  1 29  ? 16.420  -32.313 20.373  1.00 57.80  ? 29  VAL I CB  1 
ATOM   4655  C  CG1 . VAL E  1 29  ? 17.543  -31.467 20.968  1.00 56.89  ? 29  VAL I CG1 1 
ATOM   4656  C  CG2 . VAL E  1 29  ? 15.059  -31.816 20.845  1.00 57.44  ? 29  VAL I CG2 1 
ATOM   4657  N  N   . LYS E  1 30  ? 18.562  -32.182 17.567  1.00 63.54  ? 30  LYS I N   1 
ATOM   4658  C  CA  . LYS E  1 30  ? 19.937  -32.566 17.251  1.00 64.36  ? 30  LYS I CA  1 
ATOM   4659  C  C   . LYS E  1 30  ? 20.795  -32.273 18.475  1.00 62.15  ? 30  LYS I C   1 
ATOM   4660  O  O   . LYS E  1 30  ? 20.729  -31.173 19.031  1.00 61.47  ? 30  LYS I O   1 
ATOM   4661  C  CB  . LYS E  1 30  ? 20.462  -31.805 16.032  1.00 67.53  ? 30  LYS I CB  1 
ATOM   4662  C  CG  . LYS E  1 30  ? 19.789  -32.201 14.730  1.00 70.27  ? 30  LYS I CG  1 
ATOM   4663  C  CD  . LYS E  1 30  ? 20.334  -31.396 13.560  1.00 73.67  ? 30  LYS I CD  1 
ATOM   4664  C  CE  . LYS E  1 30  ? 19.550  -31.645 12.283  1.00 76.69  ? 30  LYS I CE  1 
ATOM   4665  N  NZ  . LYS E  1 30  ? 19.774  -30.554 11.293  1.00 79.96  ? 30  LYS I NZ  1 
ATOM   4666  N  N   . VAL E  1 31  ? 21.563  -33.269 18.909  1.00 61.29  ? 31  VAL I N   1 
ATOM   4667  C  CA  . VAL E  1 31  ? 22.449  -33.153 20.065  1.00 59.52  ? 31  VAL I CA  1 
ATOM   4668  C  C   . VAL E  1 31  ? 23.851  -33.500 19.591  1.00 61.31  ? 31  VAL I C   1 
ATOM   4669  O  O   . VAL E  1 31  ? 24.069  -34.599 19.078  1.00 62.23  ? 31  VAL I O   1 
ATOM   4670  C  CB  . VAL E  1 31  ? 22.032  -34.112 21.198  1.00 56.94  ? 31  VAL I CB  1 
ATOM   4671  C  CG1 . VAL E  1 31  ? 22.912  -33.916 22.430  1.00 55.37  ? 31  VAL I CG1 1 
ATOM   4672  C  CG2 . VAL E  1 31  ? 20.560  -33.923 21.541  1.00 55.73  ? 31  VAL I CG2 1 
ATOM   4673  N  N   . TRP E  1 32  ? 24.791  -32.570 19.749  1.00 62.07  ? 32  TRP I N   1 
ATOM   4674  C  CA  . TRP E  1 32  ? 26.158  -32.775 19.268  1.00 64.26  ? 32  TRP I CA  1 
ATOM   4675  C  C   . TRP E  1 32  ? 27.192  -32.041 20.112  1.00 64.03  ? 32  TRP I C   1 
ATOM   4676  O  O   . TRP E  1 32  ? 26.888  -31.030 20.741  1.00 62.96  ? 32  TRP I O   1 
ATOM   4677  C  CB  . TRP E  1 32  ? 26.278  -32.350 17.803  1.00 67.55  ? 32  TRP I CB  1 
ATOM   4678  C  CG  . TRP E  1 32  ? 26.130  -30.881 17.600  1.00 68.50  ? 32  TRP I CG  1 
ATOM   4679  C  CD1 . TRP E  1 32  ? 24.967  -30.159 17.606  1.00 67.73  ? 32  TRP I CD1 1 
ATOM   4680  C  CD2 . TRP E  1 32  ? 27.184  -29.942 17.380  1.00 70.65  ? 32  TRP I CD2 1 
ATOM   4681  N  NE1 . TRP E  1 32  ? 25.234  -28.828 17.393  1.00 69.21  ? 32  TRP I NE1 1 
ATOM   4682  C  CE2 . TRP E  1 32  ? 26.588  -28.666 17.250  1.00 71.02  ? 32  TRP I CE2 1 
ATOM   4683  C  CE3 . TRP E  1 32  ? 28.578  -30.053 17.275  1.00 72.60  ? 32  TRP I CE3 1 
ATOM   4684  C  CZ2 . TRP E  1 32  ? 27.339  -27.503 17.018  1.00 73.20  ? 32  TRP I CZ2 1 
ATOM   4685  C  CZ3 . TRP E  1 32  ? 29.328  -28.894 17.041  1.00 74.86  ? 32  TRP I CZ3 1 
ATOM   4686  C  CH2 . TRP E  1 32  ? 28.703  -27.638 16.915  1.00 75.10  ? 32  TRP I CH2 1 
ATOM   4687  N  N   . GLY E  1 33  ? 28.417  -32.557 20.104  1.00 65.37  ? 33  GLY I N   1 
ATOM   4688  C  CA  . GLY E  1 33  ? 29.505  -31.988 20.892  1.00 65.62  ? 33  GLY I CA  1 
ATOM   4689  C  C   . GLY E  1 33  ? 30.635  -32.968 21.116  1.00 66.60  ? 33  GLY I C   1 
ATOM   4690  O  O   . GLY E  1 33  ? 30.622  -34.074 20.573  1.00 67.24  ? 33  GLY I O   1 
ATOM   4691  N  N   . SER E  1 34  ? 31.609  -32.553 21.922  1.00 66.96  ? 34  SER I N   1 
ATOM   4692  C  CA  . SER E  1 34  ? 32.775  -33.374 22.262  1.00 68.21  ? 34  SER I CA  1 
ATOM   4693  C  C   . SER E  1 34  ? 32.947  -33.455 23.780  1.00 66.08  ? 34  SER I C   1 
ATOM   4694  O  O   . SER E  1 34  ? 32.685  -32.484 24.494  1.00 64.83  ? 34  SER I O   1 
ATOM   4695  C  CB  . SER E  1 34  ? 34.033  -32.786 21.629  1.00 71.93  ? 34  SER I CB  1 
ATOM   4696  O  OG  . SER E  1 34  ? 35.171  -33.569 21.940  1.00 73.58  ? 34  SER I OG  1 
ATOM   4697  N  N   . ILE E  1 35  ? 33.379  -34.622 24.258  1.00 65.87  ? 35  ILE I N   1 
ATOM   4698  C  CA  . ILE E  1 35  ? 33.681  -34.840 25.676  1.00 64.41  ? 35  ILE I CA  1 
ATOM   4699  C  C   . ILE E  1 35  ? 35.057  -35.498 25.759  1.00 67.02  ? 35  ILE I C   1 
ATOM   4700  O  O   . ILE E  1 35  ? 35.255  -36.568 25.189  1.00 68.08  ? 35  ILE I O   1 
ATOM   4701  C  CB  . ILE E  1 35  ? 32.636  -35.757 26.367  1.00 61.38  ? 35  ILE I CB  1 
ATOM   4702  C  CG1 . ILE E  1 35  ? 31.203  -35.280 26.087  1.00 59.25  ? 35  ILE I CG1 1 
ATOM   4703  C  CG2 . ILE E  1 35  ? 32.893  -35.821 27.873  1.00 60.09  ? 35  ILE I CG2 1 
ATOM   4704  C  CD1 . ILE E  1 35  ? 30.125  -36.226 26.579  1.00 56.81  ? 35  ILE I CD1 1 
ATOM   4705  N  N   . LYS E  1 36  ? 35.991  -34.859 26.467  1.00 68.26  ? 36  LYS I N   1 
ATOM   4706  C  CA  . LYS E  1 36  ? 37.336  -35.408 26.684  1.00 71.07  ? 36  LYS I CA  1 
ATOM   4707  C  C   . LYS E  1 36  ? 37.540  -35.822 28.145  1.00 69.84  ? 36  LYS I C   1 
ATOM   4708  O  O   . LYS E  1 36  ? 36.758  -35.452 29.027  1.00 67.05  ? 36  LYS I O   1 
ATOM   4709  C  CB  . LYS E  1 36  ? 38.422  -34.412 26.241  1.00 74.53  ? 36  LYS I CB  1 
ATOM   4710  C  CG  . LYS E  1 36  ? 38.572  -33.169 27.108  1.00 74.22  ? 36  LYS I CG  1 
ATOM   4711  C  CD  . LYS E  1 36  ? 39.719  -32.297 26.626  1.00 78.19  ? 36  LYS I CD  1 
ATOM   4712  C  CE  . LYS E  1 36  ? 40.066  -31.216 27.638  1.00 78.42  ? 36  LYS I CE  1 
ATOM   4713  N  NZ  . LYS E  1 36  ? 41.345  -30.530 27.302  1.00 82.86  ? 36  LYS I NZ  1 
ATOM   4714  N  N   . GLY E  1 37  ? 38.603  -36.591 28.376  1.00 72.22  ? 37  GLY I N   1 
ATOM   4715  C  CA  . GLY E  1 37  ? 38.967  -37.082 29.708  1.00 71.85  ? 37  GLY I CA  1 
ATOM   4716  C  C   . GLY E  1 37  ? 38.336  -38.405 30.113  1.00 69.86  ? 37  GLY I C   1 
ATOM   4717  O  O   . GLY E  1 37  ? 38.506  -38.839 31.255  1.00 69.43  ? 37  GLY I O   1 
ATOM   4718  N  N   . LEU E  1 38  ? 37.628  -39.054 29.186  1.00 68.93  ? 38  LEU I N   1 
ATOM   4719  C  CA  . LEU E  1 38  ? 36.928  -40.312 29.463  1.00 67.16  ? 38  LEU I CA  1 
ATOM   4720  C  C   . LEU E  1 38  ? 37.823  -41.521 29.208  1.00 69.89  ? 38  LEU I C   1 
ATOM   4721  O  O   . LEU E  1 38  ? 38.802  -41.426 28.477  1.00 73.05  ? 38  LEU I O   1 
ATOM   4722  C  CB  . LEU E  1 38  ? 35.677  -40.426 28.586  1.00 65.10  ? 38  LEU I CB  1 
ATOM   4723  C  CG  . LEU E  1 38  ? 34.570  -39.402 28.835  1.00 62.26  ? 38  LEU I CG  1 
ATOM   4724  C  CD1 . LEU E  1 38  ? 33.579  -39.413 27.682  1.00 61.44  ? 38  LEU I CD1 1 
ATOM   4725  C  CD2 . LEU E  1 38  ? 33.863  -39.671 30.158  1.00 59.63  ? 38  LEU I CD2 1 
ATOM   4726  N  N   . THR E  1 39  ? 37.482  -42.650 29.826  1.00 68.87  ? 39  THR I N   1 
ATOM   4727  C  CA  . THR E  1 39  ? 38.072  -43.945 29.472  1.00 71.19  ? 39  THR I CA  1 
ATOM   4728  C  C   . THR E  1 39  ? 37.428  -44.443 28.176  1.00 71.02  ? 39  THR I C   1 
ATOM   4729  O  O   . THR E  1 39  ? 36.324  -44.022 27.831  1.00 68.57  ? 39  THR I O   1 
ATOM   4730  C  CB  . THR E  1 39  ? 37.867  -44.996 30.588  1.00 70.30  ? 39  THR I CB  1 
ATOM   4731  O  OG1 . THR E  1 39  ? 36.479  -45.074 30.935  1.00 66.75  ? 39  THR I OG1 1 
ATOM   4732  C  CG2 . THR E  1 39  ? 38.669  -44.632 31.830  1.00 71.28  ? 39  THR I CG2 1 
ATOM   4733  N  N   . GLU E  1 40  ? 38.118  -45.329 27.463  1.00 73.89  ? 40  GLU I N   1 
ATOM   4734  C  CA  . GLU E  1 40  ? 37.615  -45.877 26.195  1.00 74.36  ? 40  GLU I CA  1 
ATOM   4735  C  C   . GLU E  1 40  ? 36.371  -46.739 26.416  1.00 71.66  ? 40  GLU I C   1 
ATOM   4736  O  O   . GLU E  1 40  ? 36.319  -47.527 27.365  1.00 71.02  ? 40  GLU I O   1 
ATOM   4737  C  CB  . GLU E  1 40  ? 38.697  -46.718 25.499  1.00 78.42  ? 40  GLU I CB  1 
ATOM   4738  C  CG  . GLU E  1 40  ? 38.335  -47.183 24.089  1.00 79.64  ? 40  GLU I CG  1 
ATOM   4739  C  CD  . GLU E  1 40  ? 39.371  -48.118 23.483  1.00 83.81  ? 40  GLU I CD  1 
ATOM   4740  O  OE1 . GLU E  1 40  ? 40.583  -47.886 23.674  1.00 86.67  ? 40  GLU I OE1 1 
ATOM   4741  O  OE2 . GLU E  1 40  ? 38.969  -49.086 22.801  1.00 84.46  ? 40  GLU I OE2 1 
ATOM   4742  N  N   . GLY E  1 41  ? 35.384  -46.579 25.533  1.00 70.40  ? 41  GLY I N   1 
ATOM   4743  C  CA  . GLY E  1 41  ? 34.154  -47.376 25.559  1.00 68.31  ? 41  GLY I CA  1 
ATOM   4744  C  C   . GLY E  1 41  ? 32.903  -46.583 25.901  1.00 64.93  ? 41  GLY I C   1 
ATOM   4745  O  O   . GLY E  1 41  ? 32.881  -45.352 25.808  1.00 64.26  ? 41  GLY I O   1 
ATOM   4746  N  N   . LEU E  1 42  ? 31.862  -47.307 26.305  1.00 63.05  ? 42  LEU I N   1 
ATOM   4747  C  CA  . LEU E  1 42  ? 30.532  -46.738 26.505  1.00 60.21  ? 42  LEU I CA  1 
ATOM   4748  C  C   . LEU E  1 42  ? 30.427  -45.992 27.832  1.00 58.08  ? 42  LEU I C   1 
ATOM   4749  O  O   . LEU E  1 42  ? 30.934  -46.456 28.853  1.00 58.14  ? 42  LEU I O   1 
ATOM   4750  C  CB  . LEU E  1 42  ? 29.471  -47.841 26.447  1.00 59.49  ? 42  LEU I CB  1 
ATOM   4751  C  CG  . LEU E  1 42  ? 29.385  -48.660 25.151  1.00 61.62  ? 42  LEU I CG  1 
ATOM   4752  C  CD1 . LEU E  1 42  ? 28.609  -49.948 25.377  1.00 61.38  ? 42  LEU I CD1 1 
ATOM   4753  C  CD2 . LEU E  1 42  ? 28.756  -47.860 24.021  1.00 61.68  ? 42  LEU I CD2 1 
ATOM   4754  N  N   . HIS E  1 43  ? 29.768  -44.832 27.800  1.00 56.42  ? 43  HIS I N   1 
ATOM   4755  C  CA  . HIS E  1 43  ? 29.512  -44.024 28.995  1.00 54.43  ? 43  HIS I CA  1 
ATOM   4756  C  C   . HIS E  1 43  ? 28.061  -43.536 28.988  1.00 52.19  ? 43  HIS I C   1 
ATOM   4757  O  O   . HIS E  1 43  ? 27.606  -42.948 28.000  1.00 52.35  ? 43  HIS I O   1 
ATOM   4758  C  CB  . HIS E  1 43  ? 30.470  -42.830 29.050  1.00 55.32  ? 43  HIS I CB  1 
ATOM   4759  C  CG  . HIS E  1 43  ? 31.889  -43.206 29.347  1.00 57.60  ? 43  HIS I CG  1 
ATOM   4760  N  ND1 . HIS E  1 43  ? 32.347  -43.419 30.630  1.00 57.45  ? 43  HIS I ND1 1 
ATOM   4761  C  CD2 . HIS E  1 43  ? 32.952  -43.403 28.531  1.00 60.42  ? 43  HIS I CD2 1 
ATOM   4762  C  CE1 . HIS E  1 43  ? 33.628  -43.739 30.590  1.00 60.08  ? 43  HIS I CE1 1 
ATOM   4763  N  NE2 . HIS E  1 43  ? 34.021  -43.735 29.329  1.00 61.91  ? 43  HIS I NE2 1 
ATOM   4764  N  N   . GLY E  1 44  ? 27.344  -43.779 30.088  1.00 50.39  ? 44  GLY I N   1 
ATOM   4765  C  CA  . GLY E  1 44  ? 25.935  -43.380 30.210  1.00 48.52  ? 44  GLY I CA  1 
ATOM   4766  C  C   . GLY E  1 44  ? 25.732  -41.888 29.993  1.00 47.85  ? 44  GLY I C   1 
ATOM   4767  O  O   . GLY E  1 44  ? 26.549  -41.078 30.440  1.00 48.00  ? 44  GLY I O   1 
ATOM   4768  N  N   . PHE E  1 45  ? 24.645  -41.543 29.300  1.00 47.32  ? 45  PHE I N   1 
ATOM   4769  C  CA  . PHE E  1 45  ? 24.365  -40.179 28.858  1.00 47.10  ? 45  PHE I CA  1 
ATOM   4770  C  C   . PHE E  1 45  ? 22.894  -39.885 29.144  1.00 45.64  ? 45  PHE I C   1 
ATOM   4771  O  O   . PHE E  1 45  ? 22.007  -40.405 28.463  1.00 45.91  ? 45  PHE I O   1 
ATOM   4772  C  CB  . PHE E  1 45  ? 24.690  -40.056 27.362  1.00 48.96  ? 45  PHE I CB  1 
ATOM   4773  C  CG  . PHE E  1 45  ? 24.870  -38.642 26.875  1.00 49.45  ? 45  PHE I CG  1 
ATOM   4774  C  CD1 . PHE E  1 45  ? 25.789  -37.784 27.479  1.00 49.54  ? 45  PHE I CD1 1 
ATOM   4775  C  CD2 . PHE E  1 45  ? 24.162  -38.184 25.768  1.00 50.21  ? 45  PHE I CD2 1 
ATOM   4776  C  CE1 . PHE E  1 45  ? 25.966  -36.488 27.013  1.00 50.25  ? 45  PHE I CE1 1 
ATOM   4777  C  CE2 . PHE E  1 45  ? 24.342  -36.892 25.293  1.00 50.95  ? 45  PHE I CE2 1 
ATOM   4778  C  CZ  . PHE E  1 45  ? 25.245  -36.043 25.915  1.00 50.94  ? 45  PHE I CZ  1 
ATOM   4779  N  N   . HIS E  1 46  ? 22.644  -39.082 30.179  1.00 44.33  ? 46  HIS I N   1 
ATOM   4780  C  CA  . HIS E  1 46  ? 21.290  -38.893 30.711  1.00 43.11  ? 46  HIS I CA  1 
ATOM   4781  C  C   . HIS E  1 46  ? 20.993  -37.434 31.004  1.00 42.53  ? 46  HIS I C   1 
ATOM   4782  O  O   . HIS E  1 46  ? 21.871  -36.703 31.464  1.00 42.53  ? 46  HIS I O   1 
ATOM   4783  C  CB  . HIS E  1 46  ? 21.091  -39.673 32.019  1.00 42.19  ? 46  HIS I CB  1 
ATOM   4784  C  CG  . HIS E  1 46  ? 21.428  -41.133 31.930  1.00 42.85  ? 46  HIS I CG  1 
ATOM   4785  N  ND1 . HIS E  1 46  ? 22.233  -41.763 32.853  1.00 42.88  ? 46  HIS I ND1 1 
ATOM   4786  C  CD2 . HIS E  1 46  ? 21.059  -42.085 31.040  1.00 43.71  ? 46  HIS I CD2 1 
ATOM   4787  C  CE1 . HIS E  1 46  ? 22.354  -43.039 32.531  1.00 43.71  ? 46  HIS I CE1 1 
ATOM   4788  N  NE2 . HIS E  1 46  ? 21.652  -43.259 31.434  1.00 44.21  ? 46  HIS I NE2 1 
ATOM   4789  N  N   . VAL E  1 47  ? 19.748  -37.025 30.751  1.00 42.29  ? 47  VAL I N   1 
ATOM   4790  C  CA  . VAL E  1 47  ? 19.217  -35.792 31.303  1.00 41.66  ? 47  VAL I CA  1 
ATOM   4791  C  C   . VAL E  1 47  ? 18.553  -36.138 32.639  1.00 40.59  ? 47  VAL I C   1 
ATOM   4792  O  O   . VAL E  1 47  ? 17.634  -36.960 32.685  1.00 40.51  ? 47  VAL I O   1 
ATOM   4793  C  CB  . VAL E  1 47  ? 18.191  -35.112 30.364  1.00 42.36  ? 47  VAL I CB  1 
ATOM   4794  C  CG1 . VAL E  1 47  ? 17.576  -33.886 31.037  1.00 41.87  ? 47  VAL I CG1 1 
ATOM   4795  C  CG2 . VAL E  1 47  ? 18.845  -34.719 29.042  1.00 43.73  ? 47  VAL I CG2 1 
ATOM   4796  N  N   . HIS E  1 48  ? 19.025  -35.506 33.714  1.00 40.01  ? 48  HIS I N   1 
ATOM   4797  C  CA  . HIS E  1 48  ? 18.457  -35.676 35.050  1.00 39.27  ? 48  HIS I CA  1 
ATOM   4798  C  C   . HIS E  1 48  ? 17.459  -34.558 35.340  1.00 39.17  ? 48  HIS I C   1 
ATOM   4799  O  O   . HIS E  1 48  ? 17.515  -33.488 34.729  1.00 39.60  ? 48  HIS I O   1 
ATOM   4800  C  CB  . HIS E  1 48  ? 19.574  -35.735 36.106  1.00 39.07  ? 48  HIS I CB  1 
ATOM   4801  C  CG  . HIS E  1 48  ? 20.364  -37.011 36.069  1.00 39.38  ? 48  HIS I CG  1 
ATOM   4802  N  ND1 . HIS E  1 48  ? 20.466  -37.859 37.152  1.00 39.21  ? 48  HIS I ND1 1 
ATOM   4803  C  CD2 . HIS E  1 48  ? 21.061  -37.599 35.066  1.00 40.08  ? 48  HIS I CD2 1 
ATOM   4804  C  CE1 . HIS E  1 48  ? 21.207  -38.903 36.824  1.00 39.80  ? 48  HIS I CE1 1 
ATOM   4805  N  NE2 . HIS E  1 48  ? 21.577  -38.772 35.563  1.00 40.33  ? 48  HIS I NE2 1 
ATOM   4806  N  N   . GLU E  1 49  ? 16.549  -34.816 36.274  1.00 38.86  ? 49  GLU I N   1 
ATOM   4807  C  CA  . GLU E  1 49  ? 15.376  -33.952 36.488  1.00 39.10  ? 49  GLU I CA  1 
ATOM   4808  C  C   . GLU E  1 49  ? 15.696  -32.506 36.874  1.00 39.12  ? 49  GLU I C   1 
ATOM   4809  O  O   . GLU E  1 49  ? 15.071  -31.577 36.357  1.00 39.64  ? 49  GLU I O   1 
ATOM   4810  C  CB  . GLU E  1 49  ? 14.448  -34.567 37.542  1.00 39.09  ? 49  GLU I CB  1 
ATOM   4811  C  CG  . GLU E  1 49  ? 13.076  -33.905 37.629  1.00 39.78  ? 49  GLU I CG  1 
ATOM   4812  C  CD  . GLU E  1 49  ? 12.176  -34.515 38.690  1.00 40.13  ? 49  GLU I CD  1 
ATOM   4813  O  OE1 . GLU E  1 49  ? 12.519  -35.570 39.270  1.00 39.84  ? 49  GLU I OE1 1 
ATOM   4814  O  OE2 . GLU E  1 49  ? 11.105  -33.920 38.940  1.00 41.01  ? 49  GLU I OE2 1 
ATOM   4815  N  N   . PHE E  1 50  ? 16.650  -32.311 37.781  1.00 38.82  ? 50  PHE I N   1 
ATOM   4816  C  CA  . PHE E  1 50  ? 16.913  -30.978 38.338  1.00 39.08  ? 50  PHE I CA  1 
ATOM   4817  C  C   . PHE E  1 50  ? 18.191  -30.347 37.789  1.00 39.43  ? 50  PHE I C   1 
ATOM   4818  O  O   . PHE E  1 50  ? 19.191  -31.036 37.598  1.00 39.37  ? 50  PHE I O   1 
ATOM   4819  C  CB  . PHE E  1 50  ? 16.960  -31.053 39.867  1.00 38.98  ? 50  PHE I CB  1 
ATOM   4820  C  CG  . PHE E  1 50  ? 15.691  -31.595 40.481  1.00 39.04  ? 50  PHE I CG  1 
ATOM   4821  C  CD1 . PHE E  1 50  ? 14.485  -30.913 40.331  1.00 39.58  ? 50  PHE I CD1 1 
ATOM   4822  C  CD2 . PHE E  1 50  ? 15.696  -32.785 41.202  1.00 38.89  ? 50  PHE I CD2 1 
ATOM   4823  C  CE1 . PHE E  1 50  ? 13.309  -31.414 40.884  1.00 39.99  ? 50  PHE I CE1 1 
ATOM   4824  C  CE2 . PHE E  1 50  ? 14.525  -33.286 41.759  1.00 39.25  ? 50  PHE I CE2 1 
ATOM   4825  C  CZ  . PHE E  1 50  ? 13.331  -32.605 41.595  1.00 39.81  ? 50  PHE I CZ  1 
ATOM   4826  N  N   . GLY E  1 51  ? 18.143  -29.035 37.538  1.00 40.01  ? 51  GLY I N   1 
ATOM   4827  C  CA  . GLY E  1 51  ? 19.330  -28.235 37.208  1.00 40.75  ? 51  GLY I CA  1 
ATOM   4828  C  C   . GLY E  1 51  ? 19.989  -27.675 38.457  1.00 41.02  ? 51  GLY I C   1 
ATOM   4829  O  O   . GLY E  1 51  ? 20.307  -26.482 38.530  1.00 41.89  ? 51  GLY I O   1 
ATOM   4830  N  N   . ASP E  1 52  ? 20.205  -28.552 39.433  1.00 40.56  ? 52  ASP I N   1 
ATOM   4831  C  CA  . ASP E  1 52  ? 20.701  -28.191 40.747  1.00 40.97  ? 52  ASP I CA  1 
ATOM   4832  C  C   . ASP E  1 52  ? 22.090  -28.809 40.832  1.00 41.44  ? 52  ASP I C   1 
ATOM   4833  O  O   . ASP E  1 52  ? 22.228  -30.024 40.953  1.00 40.97  ? 52  ASP I O   1 
ATOM   4834  C  CB  . ASP E  1 52  ? 19.759  -28.751 41.823  1.00 40.47  ? 52  ASP I CB  1 
ATOM   4835  C  CG  . ASP E  1 52  ? 20.173  -28.382 43.241  1.00 41.13  ? 52  ASP I CG  1 
ATOM   4836  O  OD1 . ASP E  1 52  ? 21.345  -28.035 43.479  1.00 41.89  ? 52  ASP I OD1 1 
ATOM   4837  O  OD2 . ASP E  1 52  ? 19.304  -28.436 44.134  1.00 41.17  ? 52  ASP I OD2 1 
ATOM   4838  N  N   . ASN E  1 53  ? 23.107  -27.954 40.737  1.00 42.60  ? 53  ASN I N   1 
ATOM   4839  C  CA  . ASN E  1 53  ? 24.502  -28.377 40.770  1.00 43.59  ? 53  ASN I CA  1 
ATOM   4840  C  C   . ASN E  1 53  ? 25.174  -28.000 42.106  1.00 44.61  ? 53  ASN I C   1 
ATOM   4841  O  O   . ASN E  1 53  ? 26.399  -27.967 42.186  1.00 45.94  ? 53  ASN I O   1 
ATOM   4842  C  CB  . ASN E  1 53  ? 25.238  -27.742 39.574  1.00 44.65  ? 53  ASN I CB  1 
ATOM   4843  C  CG  . ASN E  1 53  ? 26.551  -28.441 39.242  1.00 45.77  ? 53  ASN I CG  1 
ATOM   4844  O  OD1 . ASN E  1 53  ? 27.621  -27.831 39.305  1.00 47.47  ? 53  ASN I OD1 1 
ATOM   4845  N  ND2 . ASN E  1 53  ? 26.475  -29.721 38.892  1.00 45.10  ? 53  ASN I ND2 1 
ATOM   4846  N  N   . THR E  1 54  ? 24.377  -27.742 43.152  1.00 44.25  ? 54  THR I N   1 
ATOM   4847  C  CA  . THR E  1 54  ? 24.895  -27.233 44.429  1.00 45.51  ? 54  THR I CA  1 
ATOM   4848  C  C   . THR E  1 54  ? 25.764  -28.256 45.158  1.00 46.25  ? 54  THR I C   1 
ATOM   4849  O  O   . THR E  1 54  ? 26.717  -27.881 45.841  1.00 47.91  ? 54  THR I O   1 
ATOM   4850  C  CB  . THR E  1 54  ? 23.765  -26.780 45.381  1.00 45.19  ? 54  THR I CB  1 
ATOM   4851  O  OG1 . THR E  1 54  ? 22.805  -27.834 45.532  1.00 43.90  ? 54  THR I OG1 1 
ATOM   4852  C  CG2 . THR E  1 54  ? 23.076  -25.539 44.844  1.00 45.15  ? 54  THR I CG2 1 
ATOM   4853  N  N   . ALA E  1 55  ? 25.422  -29.537 45.013  1.00 45.27  ? 55  ALA I N   1 
ATOM   4854  C  CA  . ALA E  1 55  ? 26.265  -30.636 45.474  1.00 46.10  ? 55  ALA I CA  1 
ATOM   4855  C  C   . ALA E  1 55  ? 26.816  -31.397 44.263  1.00 45.92  ? 55  ALA I C   1 
ATOM   4856  O  O   . ALA E  1 55  ? 26.867  -32.626 44.270  1.00 45.67  ? 55  ALA I O   1 
ATOM   4857  C  CB  . ALA E  1 55  ? 25.468  -31.562 46.389  1.00 45.52  ? 55  ALA I CB  1 
ATOM   4858  N  N   . GLY E  1 56  ? 27.238  -30.653 43.235  1.00 46.29  ? 56  GLY I N   1 
ATOM   4859  C  CA  . GLY E  1 56  ? 27.721  -31.236 41.987  1.00 46.40  ? 56  GLY I CA  1 
ATOM   4860  C  C   . GLY E  1 56  ? 26.622  -31.945 41.217  1.00 44.75  ? 56  GLY I C   1 
ATOM   4861  O  O   . GLY E  1 56  ? 25.452  -31.532 41.254  1.00 43.60  ? 56  GLY I O   1 
ATOM   4862  N  N   . ALA E  1 57  ? 26.993  -33.024 40.531  1.00 44.88  ? 57  ALA I N   1 
ATOM   4863  C  CA  . ALA E  1 57  ? 26.039  -33.829 39.777  1.00 43.67  ? 57  ALA I CA  1 
ATOM   4864  C  C   . ALA E  1 57  ? 25.050  -34.579 40.671  1.00 42.72  ? 57  ALA I C   1 
ATOM   4865  O  O   . ALA E  1 57  ? 23.965  -34.924 40.212  1.00 41.75  ? 57  ALA I O   1 
ATOM   4866  C  CB  . ALA E  1 57  ? 26.769  -34.811 38.874  1.00 44.40  ? 57  ALA I CB  1 
ATOM   4867  N  N   . THR E  1 58  ? 25.427  -34.838 41.926  1.00 43.38  ? 58  THR I N   1 
ATOM   4868  C  CA  . THR E  1 58  ? 24.588  -35.573 42.884  1.00 42.91  ? 58  THR I CA  1 
ATOM   4869  C  C   . THR E  1 58  ? 23.220  -34.907 43.112  1.00 41.90  ? 58  THR I C   1 
ATOM   4870  O  O   . THR E  1 58  ? 22.199  -35.590 43.201  1.00 41.32  ? 58  THR I O   1 
ATOM   4871  C  CB  . THR E  1 58  ? 25.311  -35.738 44.246  1.00 44.20  ? 58  THR I CB  1 
ATOM   4872  O  OG1 . THR E  1 58  ? 26.609  -36.318 44.045  1.00 45.58  ? 58  THR I OG1 1 
ATOM   4873  C  CG2 . THR E  1 58  ? 24.519  -36.634 45.191  1.00 44.03  ? 58  THR I CG2 1 
ATOM   4874  N  N   . SER E  1 59  ? 23.205  -33.577 43.180  1.00 41.99  ? 59  SER I N   1 
ATOM   4875  C  CA  . SER E  1 59  ? 21.975  -32.818 43.427  1.00 41.36  ? 59  SER I CA  1 
ATOM   4876  C  C   . SER E  1 59  ? 21.011  -32.722 42.222  1.00 40.45  ? 59  SER I C   1 
ATOM   4877  O  O   . SER E  1 59  ? 19.920  -32.163 42.357  1.00 40.21  ? 59  SER I O   1 
ATOM   4878  C  CB  . SER E  1 59  ? 22.331  -31.418 43.948  1.00 42.10  ? 59  SER I CB  1 
ATOM   4879  O  OG  . SER E  1 59  ? 23.376  -30.831 43.186  1.00 42.75  ? 59  SER I OG  1 
ATOM   4880  N  N   . ALA E  1 60  ? 21.400  -33.271 41.067  1.00 40.24  ? 60  ALA I N   1 
ATOM   4881  C  CA  . ALA E  1 60  ? 20.554  -33.275 39.872  1.00 39.71  ? 60  ALA I CA  1 
ATOM   4882  C  C   . ALA E  1 60  ? 19.331  -34.200 39.954  1.00 39.14  ? 60  ALA I C   1 
ATOM   4883  O  O   . ALA E  1 60  ? 18.422  -34.075 39.139  1.00 38.96  ? 60  ALA I O   1 
ATOM   4884  C  CB  . ALA E  1 60  ? 21.387  -33.638 38.650  1.00 40.09  ? 60  ALA I CB  1 
ATOM   4885  N  N   . GLY E  1 61  ? 19.321  -35.140 40.901  1.00 39.10  ? 61  GLY I N   1 
ATOM   4886  C  CA  . GLY E  1 61  ? 18.171  -36.020 41.107  1.00 38.87  ? 61  GLY I CA  1 
ATOM   4887  C  C   . GLY E  1 61  ? 18.146  -37.178 40.119  1.00 38.80  ? 61  GLY I C   1 
ATOM   4888  O  O   . GLY E  1 61  ? 19.145  -37.440 39.442  1.00 38.94  ? 61  GLY I O   1 
ATOM   4889  N  N   . PRO E  1 62  ? 17.004  -37.884 40.027  1.00 38.83  ? 62  PRO I N   1 
ATOM   4890  C  CA  . PRO E  1 62  ? 16.882  -39.033 39.131  1.00 39.05  ? 62  PRO I CA  1 
ATOM   4891  C  C   . PRO E  1 62  ? 16.752  -38.623 37.660  1.00 39.05  ? 62  PRO I C   1 
ATOM   4892  O  O   . PRO E  1 62  ? 16.786  -37.426 37.346  1.00 38.82  ? 62  PRO I O   1 
ATOM   4893  C  CB  . PRO E  1 62  ? 15.606  -39.713 39.626  1.00 39.48  ? 62  PRO I CB  1 
ATOM   4894  C  CG  . PRO E  1 62  ? 14.764  -38.584 40.106  1.00 39.44  ? 62  PRO I CG  1 
ATOM   4895  C  CD  . PRO E  1 62  ? 15.718  -37.571 40.683  1.00 39.03  ? 62  PRO I CD  1 
ATOM   4896  N  N   . HIS E  1 63  ? 16.612  -39.608 36.771  1.00 39.43  ? 63  HIS I N   1 
ATOM   4897  C  CA  . HIS E  1 63  ? 16.424  -39.325 35.348  1.00 39.83  ? 63  HIS I CA  1 
ATOM   4898  C  C   . HIS E  1 63  ? 15.111  -38.573 35.152  1.00 40.00  ? 63  HIS I C   1 
ATOM   4899  O  O   . HIS E  1 63  ? 14.110  -38.874 35.813  1.00 40.13  ? 63  HIS I O   1 
ATOM   4900  C  CB  . HIS E  1 63  ? 16.419  -40.602 34.501  1.00 40.59  ? 63  HIS I CB  1 
ATOM   4901  C  CG  . HIS E  1 63  ? 17.722  -41.335 34.505  1.00 40.81  ? 63  HIS I CG  1 
ATOM   4902  N  ND1 . HIS E  1 63  ? 17.892  -42.553 33.879  1.00 41.68  ? 63  HIS I ND1 1 
ATOM   4903  C  CD2 . HIS E  1 63  ? 18.909  -41.042 35.085  1.00 40.53  ? 63  HIS I CD2 1 
ATOM   4904  C  CE1 . HIS E  1 63  ? 19.133  -42.967 34.062  1.00 41.87  ? 63  HIS I CE1 1 
ATOM   4905  N  NE2 . HIS E  1 63  ? 19.770  -42.067 34.786  1.00 41.24  ? 63  HIS I NE2 1 
ATOM   4906  N  N   . PHE E  1 64  ? 15.134  -37.575 34.271  1.00 40.20  ? 64  PHE I N   1 
ATOM   4907  C  CA  . PHE E  1 64  ? 13.941  -36.802 33.956  1.00 40.73  ? 64  PHE I CA  1 
ATOM   4908  C  C   . PHE E  1 64  ? 12.884  -37.758 33.397  1.00 41.68  ? 64  PHE I C   1 
ATOM   4909  O  O   . PHE E  1 64  ? 13.092  -38.391 32.359  1.00 42.31  ? 64  PHE I O   1 
ATOM   4910  C  CB  . PHE E  1 64  ? 14.274  -35.664 32.975  1.00 41.14  ? 64  PHE I CB  1 
ATOM   4911  C  CG  . PHE E  1 64  ? 13.082  -34.849 32.542  1.00 42.05  ? 64  PHE I CG  1 
ATOM   4912  C  CD1 . PHE E  1 64  ? 12.142  -34.397 33.468  1.00 42.06  ? 64  PHE I CD1 1 
ATOM   4913  C  CD2 . PHE E  1 64  ? 12.916  -34.503 31.205  1.00 43.21  ? 64  PHE I CD2 1 
ATOM   4914  C  CE1 . PHE E  1 64  ? 11.051  -33.649 33.060  1.00 43.20  ? 64  PHE I CE1 1 
ATOM   4915  C  CE2 . PHE E  1 64  ? 11.827  -33.747 30.797  1.00 44.35  ? 64  PHE I CE2 1 
ATOM   4916  C  CZ  . PHE E  1 64  ? 10.896  -33.321 31.726  1.00 44.35  ? 64  PHE I CZ  1 
ATOM   4917  N  N   . ASN E  1 65  ? 11.776  -37.874 34.127  1.00 41.99  ? 65  ASN I N   1 
ATOM   4918  C  CA  . ASN E  1 65  ? 10.786  -38.923 33.907  1.00 43.10  ? 65  ASN I CA  1 
ATOM   4919  C  C   . ASN E  1 65  ? 9.357   -38.388 34.098  1.00 44.25  ? 65  ASN I C   1 
ATOM   4920  O  O   . ASN E  1 65  ? 8.609   -38.881 34.948  1.00 44.72  ? 65  ASN I O   1 
ATOM   4921  C  CB  . ASN E  1 65  ? 11.084  -40.080 34.871  1.00 42.67  ? 65  ASN I CB  1 
ATOM   4922  C  CG  . ASN E  1 65  ? 10.294  -41.335 34.557  1.00 43.96  ? 65  ASN I CG  1 
ATOM   4923  O  OD1 . ASN E  1 65  ? 9.807   -41.523 33.443  1.00 45.07  ? 65  ASN I OD1 1 
ATOM   4924  N  ND2 . ASN E  1 65  ? 10.181  -42.212 35.539  1.00 44.01  ? 65  ASN I ND2 1 
ATOM   4925  N  N   . PRO E  1 66  ? 8.960   -37.384 33.287  1.00 45.03  ? 66  PRO I N   1 
ATOM   4926  C  CA  . PRO E  1 66  ? 7.628   -36.789 33.446  1.00 46.45  ? 66  PRO I CA  1 
ATOM   4927  C  C   . PRO E  1 66  ? 6.471   -37.762 33.166  1.00 48.34  ? 66  PRO I C   1 
ATOM   4928  O  O   . PRO E  1 66  ? 5.381   -37.557 33.695  1.00 49.60  ? 66  PRO I O   1 
ATOM   4929  C  CB  . PRO E  1 66  ? 7.634   -35.634 32.440  1.00 47.03  ? 66  PRO I CB  1 
ATOM   4930  C  CG  . PRO E  1 66  ? 8.580   -36.078 31.382  1.00 46.74  ? 66  PRO I CG  1 
ATOM   4931  C  CD  . PRO E  1 66  ? 9.637   -36.891 32.074  1.00 45.11  ? 66  PRO I CD  1 
ATOM   4932  N  N   . LEU E  1 67  ? 6.710   -38.802 32.362  1.00 48.80  ? 67  LEU I N   1 
ATOM   4933  C  CA  . LEU E  1 67  ? 5.696   -39.838 32.088  1.00 50.81  ? 67  LEU I CA  1 
ATOM   4934  C  C   . LEU E  1 67  ? 5.681   -41.029 33.066  1.00 50.62  ? 67  LEU I C   1 
ATOM   4935  O  O   . LEU E  1 67  ? 4.871   -41.941 32.892  1.00 52.40  ? 67  LEU I O   1 
ATOM   4936  C  CB  . LEU E  1 67  ? 5.841   -40.352 30.643  1.00 51.94  ? 67  LEU I CB  1 
ATOM   4937  C  CG  . LEU E  1 67  ? 5.391   -39.399 29.530  1.00 53.37  ? 67  LEU I CG  1 
ATOM   4938  C  CD1 . LEU E  1 67  ? 5.756   -39.969 28.166  1.00 54.42  ? 67  LEU I CD1 1 
ATOM   4939  C  CD2 . LEU E  1 67  ? 3.894   -39.120 29.606  1.00 55.69  ? 67  LEU I CD2 1 
ATOM   4940  N  N   . SER E  1 68  ? 6.551   -41.021 34.081  1.00 48.79  ? 68  SER I N   1 
ATOM   4941  C  CA  . SER E  1 68  ? 6.650   -42.109 35.071  1.00 48.68  ? 68  SER I CA  1 
ATOM   4942  C  C   . SER E  1 68  ? 6.827   -43.497 34.431  1.00 49.49  ? 68  SER I C   1 
ATOM   4943  O  O   . SER E  1 68  ? 6.197   -44.467 34.846  1.00 50.79  ? 68  SER I O   1 
ATOM   4944  C  CB  . SER E  1 68  ? 5.437   -42.103 36.015  1.00 50.09  ? 68  SER I CB  1 
ATOM   4945  O  OG  . SER E  1 68  ? 5.253   -40.834 36.616  1.00 49.62  ? 68  SER I OG  1 
ATOM   4946  N  N   . ARG E  1 69  ? 7.692   -43.573 33.423  1.00 48.97  ? 69  ARG I N   1 
ATOM   4947  C  CA  . ARG E  1 69  ? 8.038   -44.834 32.770  1.00 49.76  ? 69  ARG I CA  1 
ATOM   4948  C  C   . ARG E  1 69  ? 9.234   -45.477 33.479  1.00 48.38  ? 69  ARG I C   1 
ATOM   4949  O  O   . ARG E  1 69  ? 9.795   -44.902 34.416  1.00 46.87  ? 69  ARG I O   1 
ATOM   4950  C  CB  . ARG E  1 69  ? 8.380   -44.594 31.294  1.00 50.30  ? 69  ARG I CB  1 
ATOM   4951  C  CG  . ARG E  1 69  ? 7.261   -43.969 30.465  1.00 52.09  ? 69  ARG I CG  1 
ATOM   4952  C  CD  . ARG E  1 69  ? 6.178   -44.972 30.095  1.00 54.61  ? 69  ARG I CD  1 
ATOM   4953  N  NE  . ARG E  1 69  ? 5.327   -44.475 29.007  1.00 56.70  ? 69  ARG I NE  1 
ATOM   4954  C  CZ  . ARG E  1 69  ? 4.212   -43.747 29.143  1.00 58.01  ? 69  ARG I CZ  1 
ATOM   4955  N  NH1 . ARG E  1 69  ? 3.742   -43.383 30.341  1.00 57.52  ? 69  ARG I NH1 1 
ATOM   4956  N  NH2 . ARG E  1 69  ? 3.549   -43.368 28.051  1.00 60.13  ? 69  ARG I NH2 1 
ATOM   4957  N  N   . LYS E  1 70  ? 9.600   -46.678 33.038  1.00 49.13  ? 70  LYS I N   1 
ATOM   4958  C  CA  . LYS E  1 70  ? 10.836  -47.338 33.475  1.00 48.25  ? 70  LYS I CA  1 
ATOM   4959  C  C   . LYS E  1 70  ? 12.000  -46.960 32.556  1.00 47.53  ? 70  LYS I C   1 
ATOM   4960  O  O   . LYS E  1 70  ? 11.787  -46.538 31.408  1.00 48.14  ? 70  LYS I O   1 
ATOM   4961  C  CB  . LYS E  1 70  ? 10.650  -48.857 33.508  1.00 49.76  ? 70  LYS I CB  1 
ATOM   4962  C  CG  . LYS E  1 70  ? 9.557   -49.300 34.467  1.00 50.82  ? 70  LYS I CG  1 
ATOM   4963  C  CD  . LYS E  1 70  ? 9.564   -50.800 34.693  1.00 52.29  ? 70  LYS I CD  1 
ATOM   4964  C  CE  . LYS E  1 70  ? 8.459   -51.198 35.660  1.00 53.65  ? 70  LYS I CE  1 
ATOM   4965  N  NZ  . LYS E  1 70  ? 8.480   -52.648 35.997  1.00 55.24  ? 70  LYS I NZ  1 
ATOM   4966  N  N   . HIS E  1 71  ? 13.223  -47.108 33.073  1.00 46.49  ? 71  HIS I N   1 
ATOM   4967  C  CA  . HIS E  1 71  ? 14.447  -46.778 32.330  1.00 46.06  ? 71  HIS I CA  1 
ATOM   4968  C  C   . HIS E  1 71  ? 14.600  -47.666 31.095  1.00 47.58  ? 71  HIS I C   1 
ATOM   4969  O  O   . HIS E  1 71  ? 14.249  -48.839 31.125  1.00 48.71  ? 71  HIS I O   1 
ATOM   4970  C  CB  . HIS E  1 71  ? 15.693  -46.921 33.220  1.00 45.18  ? 71  HIS I CB  1 
ATOM   4971  C  CG  . HIS E  1 71  ? 16.982  -46.619 32.516  1.00 45.10  ? 71  HIS I CG  1 
ATOM   4972  N  ND1 . HIS E  1 71  ? 17.432  -45.336 32.296  1.00 44.30  ? 71  HIS I ND1 1 
ATOM   4973  C  CD2 . HIS E  1 71  ? 17.909  -47.441 31.970  1.00 46.03  ? 71  HIS I CD2 1 
ATOM   4974  C  CE1 . HIS E  1 71  ? 18.584  -45.380 31.651  1.00 44.79  ? 71  HIS I CE1 1 
ATOM   4975  N  NE2 . HIS E  1 71  ? 18.895  -46.645 31.439  1.00 45.83  ? 71  HIS I NE2 1 
ATOM   4976  N  N   . GLY E  1 72  ? 15.111  -47.080 30.017  1.00 47.83  ? 72  GLY I N   1 
ATOM   4977  C  CA  . GLY E  1 72  ? 15.417  -47.806 28.792  1.00 49.52  ? 72  GLY I CA  1 
ATOM   4978  C  C   . GLY E  1 72  ? 16.505  -47.104 28.009  1.00 49.55  ? 72  GLY I C   1 
ATOM   4979  O  O   . GLY E  1 72  ? 17.078  -46.121 28.479  1.00 48.25  ? 72  GLY I O   1 
ATOM   4980  N  N   . GLY E  1 73  ? 16.805  -47.631 26.826  1.00 51.31  ? 73  GLY I N   1 
ATOM   4981  C  CA  . GLY E  1 73  ? 17.658  -46.941 25.858  1.00 51.96  ? 73  GLY I CA  1 
ATOM   4982  C  C   . GLY E  1 73  ? 16.822  -45.992 25.013  1.00 52.59  ? 73  GLY I C   1 
ATOM   4983  O  O   . GLY E  1 73  ? 15.590  -46.065 25.043  1.00 52.86  ? 73  GLY I O   1 
ATOM   4984  N  N   . PRO E  1 74  ? 17.477  -45.098 24.244  1.00 53.14  ? 74  PRO I N   1 
ATOM   4985  C  CA  . PRO E  1 74  ? 16.753  -44.071 23.473  1.00 53.85  ? 74  PRO I CA  1 
ATOM   4986  C  C   . PRO E  1 74  ? 15.813  -44.618 22.396  1.00 56.13  ? 74  PRO I C   1 
ATOM   4987  O  O   . PRO E  1 74  ? 14.772  -44.020 22.142  1.00 56.62  ? 74  PRO I O   1 
ATOM   4988  C  CB  . PRO E  1 74  ? 17.880  -43.244 22.837  1.00 54.32  ? 74  PRO I CB  1 
ATOM   4989  C  CG  . PRO E  1 74  ? 19.060  -44.160 22.812  1.00 54.84  ? 74  PRO I CG  1 
ATOM   4990  C  CD  . PRO E  1 74  ? 18.934  -44.976 24.063  1.00 53.37  ? 74  PRO I CD  1 
ATOM   4991  N  N   . LYS E  1 75  ? 16.175  -45.741 21.780  1.00 57.85  ? 75  LYS I N   1 
ATOM   4992  C  CA  . LYS E  1 75  ? 15.329  -46.374 20.759  1.00 60.38  ? 75  LYS I CA  1 
ATOM   4993  C  C   . LYS E  1 75  ? 14.097  -47.103 21.316  1.00 60.54  ? 75  LYS I C   1 
ATOM   4994  O  O   . LYS E  1 75  ? 13.179  -47.415 20.550  1.00 62.67  ? 75  LYS I O   1 
ATOM   4995  C  CB  . LYS E  1 75  ? 16.149  -47.352 19.915  1.00 62.35  ? 75  LYS I CB  1 
ATOM   4996  C  CG  . LYS E  1 75  ? 17.250  -46.697 19.096  1.00 63.24  ? 75  LYS I CG  1 
ATOM   4997  C  CD  . LYS E  1 75  ? 18.188  -47.743 18.508  1.00 65.08  ? 75  LYS I CD  1 
ATOM   4998  C  CE  . LYS E  1 75  ? 19.094  -47.149 17.441  1.00 66.87  ? 75  LYS I CE  1 
ATOM   4999  N  NZ  . LYS E  1 75  ? 20.150  -48.113 17.028  1.00 68.61  ? 75  LYS I NZ  1 
ATOM   5000  N  N   . ASP E  1 76  ? 14.076  -47.388 22.622  1.00 58.66  ? 76  ASP I N   1 
ATOM   5001  C  CA  . ASP E  1 76  ? 12.965  -48.128 23.238  1.00 58.97  ? 76  ASP I CA  1 
ATOM   5002  C  C   . ASP E  1 76  ? 11.710  -47.277 23.388  1.00 58.99  ? 76  ASP I C   1 
ATOM   5003  O  O   . ASP E  1 76  ? 11.780  -46.047 23.504  1.00 57.90  ? 76  ASP I O   1 
ATOM   5004  C  CB  . ASP E  1 76  ? 13.357  -48.677 24.616  1.00 57.23  ? 76  ASP I CB  1 
ATOM   5005  C  CG  . ASP E  1 76  ? 14.473  -49.712 24.548  1.00 57.68  ? 76  ASP I CG  1 
ATOM   5006  O  OD1 . ASP E  1 76  ? 14.479  -50.545 23.613  1.00 59.82  ? 76  ASP I OD1 1 
ATOM   5007  O  OD2 . ASP E  1 76  ? 15.340  -49.700 25.450  1.00 56.16  ? 76  ASP I OD2 1 
ATOM   5008  N  N   . GLU E  1 77  ? 10.565  -47.956 23.377  1.00 60.54  ? 77  GLU I N   1 
ATOM   5009  C  CA  . GLU E  1 77  ? 9.272   -47.346 23.667  1.00 60.93  ? 77  GLU I CA  1 
ATOM   5010  C  C   . GLU E  1 77  ? 9.196   -47.033 25.158  1.00 58.58  ? 77  GLU I C   1 
ATOM   5011  O  O   . GLU E  1 77  ? 8.831   -45.921 25.547  1.00 57.69  ? 77  GLU I O   1 
ATOM   5012  C  CB  . GLU E  1 77  ? 8.139   -48.301 23.261  1.00 63.71  ? 77  GLU I CB  1 
ATOM   5013  C  CG  . GLU E  1 77  ? 6.726   -47.739 23.397  1.00 64.98  ? 77  GLU I CG  1 
ATOM   5014  C  CD  . GLU E  1 77  ? 6.409   -46.679 22.362  1.00 66.29  ? 77  GLU I CD  1 
ATOM   5015  O  OE1 . GLU E  1 77  ? 6.049   -47.050 21.221  1.00 69.07  ? 77  GLU I OE1 1 
ATOM   5016  O  OE2 . GLU E  1 77  ? 6.505   -45.477 22.696  1.00 64.81  ? 77  GLU I OE2 1 
ATOM   5017  N  N   . GLU E  1 78  ? 9.549   -48.025 25.979  1.00 57.81  ? 78  GLU I N   1 
ATOM   5018  C  CA  . GLU E  1 78  ? 9.554   -47.889 27.433  1.00 55.81  ? 78  GLU I CA  1 
ATOM   5019  C  C   . GLU E  1 78  ? 10.877  -47.257 27.898  1.00 53.37  ? 78  GLU I C   1 
ATOM   5020  O  O   . GLU E  1 78  ? 11.855  -47.960 28.166  1.00 52.84  ? 78  GLU I O   1 
ATOM   5021  C  CB  . GLU E  1 78  ? 9.323   -49.264 28.085  1.00 56.58  ? 78  GLU I CB  1 
ATOM   5022  C  CG  . GLU E  1 78  ? 9.151   -49.263 29.605  1.00 55.28  ? 78  GLU I CG  1 
ATOM   5023  C  CD  . GLU E  1 78  ? 7.908   -48.528 30.083  1.00 55.67  ? 78  GLU I CD  1 
ATOM   5024  O  OE1 . GLU E  1 78  ? 6.945   -48.378 29.295  1.00 57.61  ? 78  GLU I OE1 1 
ATOM   5025  O  OE2 . GLU E  1 78  ? 7.891   -48.105 31.258  1.00 54.31  ? 78  GLU I OE2 1 
ATOM   5026  N  N   . ARG E  1 79  ? 10.894  -45.925 27.975  1.00 52.14  ? 79  ARG I N   1 
ATOM   5027  C  CA  . ARG E  1 79  ? 12.076  -45.168 28.408  1.00 50.10  ? 79  ARG I CA  1 
ATOM   5028  C  C   . ARG E  1 79  ? 11.692  -43.913 29.179  1.00 48.78  ? 79  ARG I C   1 
ATOM   5029  O  O   . ARG E  1 79  ? 10.575  -43.410 29.051  1.00 49.54  ? 79  ARG I O   1 
ATOM   5030  C  CB  . ARG E  1 79  ? 12.930  -44.764 27.199  1.00 50.58  ? 79  ARG I CB  1 
ATOM   5031  C  CG  . ARG E  1 79  ? 12.171  -44.013 26.115  1.00 51.97  ? 79  ARG I CG  1 
ATOM   5032  C  CD  . ARG E  1 79  ? 13.103  -43.394 25.085  1.00 52.38  ? 79  ARG I CD  1 
ATOM   5033  N  NE  . ARG E  1 79  ? 13.651  -42.115 25.545  1.00 50.86  ? 79  ARG I NE  1 
ATOM   5034  C  CZ  . ARG E  1 79  ? 14.338  -41.254 24.788  1.00 51.23  ? 79  ARG I CZ  1 
ATOM   5035  N  NH1 . ARG E  1 79  ? 14.586  -41.509 23.503  1.00 53.09  ? 79  ARG I NH1 1 
ATOM   5036  N  NH2 . ARG E  1 79  ? 14.777  -40.112 25.322  1.00 49.96  ? 79  ARG I NH2 1 
ATOM   5037  N  N   . HIS E  1 80  ? 12.636  -43.412 29.971  1.00 46.99  ? 80  HIS I N   1 
ATOM   5038  C  CA  . HIS E  1 80  ? 12.524  -42.078 30.564  1.00 45.83  ? 80  HIS I CA  1 
ATOM   5039  C  C   . HIS E  1 80  ? 12.787  -41.058 29.469  1.00 46.22  ? 80  HIS I C   1 
ATOM   5040  O  O   . HIS E  1 80  ? 13.528  -41.350 28.523  1.00 46.85  ? 80  HIS I O   1 
ATOM   5041  C  CB  . HIS E  1 80  ? 13.549  -41.878 31.688  1.00 44.18  ? 80  HIS I CB  1 
ATOM   5042  C  CG  . HIS E  1 80  ? 13.413  -42.851 32.815  1.00 43.92  ? 80  HIS I CG  1 
ATOM   5043  N  ND1 . HIS E  1 80  ? 14.483  -43.261 33.582  1.00 43.12  ? 80  HIS I ND1 1 
ATOM   5044  C  CD2 . HIS E  1 80  ? 12.330  -43.499 33.301  1.00 44.61  ? 80  HIS I CD2 1 
ATOM   5045  C  CE1 . HIS E  1 80  ? 14.058  -44.108 34.502  1.00 43.36  ? 80  HIS I CE1 1 
ATOM   5046  N  NE2 . HIS E  1 80  ? 12.757  -44.272 34.352  1.00 44.24  ? 80  HIS I NE2 1 
ATOM   5047  N  N   . VAL E  1 81  ? 12.203  -39.868 29.596  1.00 46.04  ? 81  VAL I N   1 
ATOM   5048  C  CA  . VAL E  1 81  ? 12.450  -38.787 28.627  1.00 46.59  ? 81  VAL I CA  1 
ATOM   5049  C  C   . VAL E  1 81  ? 13.951  -38.493 28.520  1.00 45.77  ? 81  VAL I C   1 
ATOM   5050  O  O   . VAL E  1 81  ? 14.479  -38.312 27.415  1.00 46.70  ? 81  VAL I O   1 
ATOM   5051  C  CB  . VAL E  1 81  ? 11.650  -37.496 28.968  1.00 46.59  ? 81  VAL I CB  1 
ATOM   5052  C  CG1 . VAL E  1 81  ? 12.153  -36.289 28.175  1.00 47.01  ? 81  VAL I CG1 1 
ATOM   5053  C  CG2 . VAL E  1 81  ? 10.165  -37.721 28.705  1.00 48.15  ? 81  VAL I CG2 1 
ATOM   5054  N  N   . GLY E  1 82  ? 14.633  -38.496 29.664  1.00 44.31  ? 82  GLY I N   1 
ATOM   5055  C  CA  . GLY E  1 82  ? 16.055  -38.195 29.712  1.00 43.80  ? 82  GLY I CA  1 
ATOM   5056  C  C   . GLY E  1 82  ? 17.020  -39.324 29.393  1.00 44.16  ? 82  GLY I C   1 
ATOM   5057  O  O   . GLY E  1 82  ? 18.208  -39.164 29.645  1.00 43.84  ? 82  GLY I O   1 
ATOM   5058  N  N   . ASP E  1 83  ? 16.534  -40.451 28.856  1.00 45.10  ? 83  ASP I N   1 
ATOM   5059  C  CA  . ASP E  1 83  ? 17.394  -41.592 28.482  1.00 45.82  ? 83  ASP I CA  1 
ATOM   5060  C  C   . ASP E  1 83  ? 17.952  -41.421 27.070  1.00 47.34  ? 83  ASP I C   1 
ATOM   5061  O  O   . ASP E  1 83  ? 17.304  -41.787 26.089  1.00 48.69  ? 83  ASP I O   1 
ATOM   5062  C  CB  . ASP E  1 83  ? 16.626  -42.923 28.557  1.00 46.41  ? 83  ASP I CB  1 
ATOM   5063  C  CG  . ASP E  1 83  ? 16.292  -43.344 29.982  1.00 45.34  ? 83  ASP I CG  1 
ATOM   5064  O  OD1 . ASP E  1 83  ? 16.956  -42.885 30.935  1.00 44.29  ? 83  ASP I OD1 1 
ATOM   5065  O  OD2 . ASP E  1 83  ? 15.346  -44.142 30.165  1.00 45.79  ? 83  ASP I OD2 1 
ATOM   5066  N  N   . LEU E  1 84  ? 19.160  -40.870 26.981  1.00 47.39  ? 84  LEU I N   1 
ATOM   5067  C  CA  . LEU E  1 84  ? 19.854  -40.693 25.703  1.00 49.08  ? 84  LEU I CA  1 
ATOM   5068  C  C   . LEU E  1 84  ? 20.907  -41.774 25.443  1.00 50.11  ? 84  LEU I C   1 
ATOM   5069  O  O   . LEU E  1 84  ? 21.716  -41.635 24.523  1.00 51.73  ? 84  LEU I O   1 
ATOM   5070  C  CB  . LEU E  1 84  ? 20.487  -39.298 25.650  1.00 49.03  ? 84  LEU I CB  1 
ATOM   5071  C  CG  . LEU E  1 84  ? 19.492  -38.140 25.773  1.00 48.43  ? 84  LEU I CG  1 
ATOM   5072  C  CD1 . LEU E  1 84  ? 20.225  -36.813 25.894  1.00 48.39  ? 84  LEU I CD1 1 
ATOM   5073  C  CD2 . LEU E  1 84  ? 18.533  -38.124 24.589  1.00 49.93  ? 84  LEU I CD2 1 
ATOM   5074  N  N   . GLY E  1 85  ? 20.899  -42.845 26.241  1.00 49.43  ? 85  GLY I N   1 
ATOM   5075  C  CA  . GLY E  1 85  ? 21.716  -44.023 25.969  1.00 50.64  ? 85  GLY I CA  1 
ATOM   5076  C  C   . GLY E  1 85  ? 23.175  -43.867 26.345  1.00 50.86  ? 85  GLY I C   1 
ATOM   5077  O  O   . GLY E  1 85  ? 23.495  -43.422 27.451  1.00 49.56  ? 85  GLY I O   1 
ATOM   5078  N  N   . ASN E  1 86  ? 24.053  -44.248 25.419  1.00 52.77  ? 86  ASN I N   1 
ATOM   5079  C  CA  . ASN E  1 86  ? 25.492  -44.250 25.639  1.00 53.67  ? 86  ASN I CA  1 
ATOM   5080  C  C   . ASN E  1 86  ? 26.187  -43.376 24.606  1.00 55.29  ? 86  ASN I C   1 
ATOM   5081  O  O   . ASN E  1 86  ? 25.816  -43.383 23.430  1.00 56.55  ? 86  ASN I O   1 
ATOM   5082  C  CB  . ASN E  1 86  ? 26.043  -45.683 25.539  1.00 55.11  ? 86  ASN I CB  1 
ATOM   5083  C  CG  . ASN E  1 86  ? 25.720  -46.526 26.763  1.00 53.84  ? 86  ASN I CG  1 
ATOM   5084  O  OD1 . ASN E  1 86  ? 25.979  -46.120 27.895  1.00 52.56  ? 86  ASN I OD1 1 
ATOM   5085  N  ND2 . ASN E  1 86  ? 25.164  -47.712 26.540  1.00 54.43  ? 86  ASN I ND2 1 
ATOM   5086  N  N   . VAL E  1 87  ? 27.188  -42.626 25.065  1.00 55.45  ? 87  VAL I N   1 
ATOM   5087  C  CA  . VAL E  1 87  ? 28.200  -42.032 24.182  1.00 57.71  ? 87  VAL I CA  1 
ATOM   5088  C  C   . VAL E  1 87  ? 29.440  -42.927 24.211  1.00 59.70  ? 87  VAL I C   1 
ATOM   5089  O  O   . VAL E  1 87  ? 29.721  -43.590 25.217  1.00 58.98  ? 87  VAL I O   1 
ATOM   5090  C  CB  . VAL E  1 87  ? 28.556  -40.562 24.542  1.00 57.25  ? 87  VAL I CB  1 
ATOM   5091  C  CG1 . VAL E  1 87  ? 27.314  -39.683 24.475  1.00 55.60  ? 87  VAL I CG1 1 
ATOM   5092  C  CG2 . VAL E  1 87  ? 29.233  -40.431 25.908  1.00 56.32  ? 87  VAL I CG2 1 
ATOM   5093  N  N   . THR E  1 88  ? 30.169  -42.928 23.096  1.00 62.45  ? 88  THR I N   1 
ATOM   5094  C  CA  . THR E  1 88  ? 31.316  -43.806 22.874  1.00 64.99  ? 88  THR I CA  1 
ATOM   5095  C  C   . THR E  1 88  ? 32.622  -43.006 22.787  1.00 67.06  ? 88  THR I C   1 
ATOM   5096  O  O   . THR E  1 88  ? 32.847  -42.284 21.814  1.00 68.79  ? 88  THR I O   1 
ATOM   5097  C  CB  . THR E  1 88  ? 31.135  -44.599 21.564  1.00 67.20  ? 88  THR I CB  1 
ATOM   5098  O  OG1 . THR E  1 88  ? 30.577  -43.737 20.561  1.00 67.67  ? 88  THR I OG1 1 
ATOM   5099  C  CG2 . THR E  1 88  ? 30.213  -45.798 21.774  1.00 66.04  ? 88  THR I CG2 1 
ATOM   5100  N  N   . ALA E  1 89  ? 33.475  -43.146 23.804  1.00 67.16  ? 89  ALA I N   1 
ATOM   5101  C  CA  . ALA E  1 89  ? 34.791  -42.502 23.825  1.00 69.53  ? 89  ALA I CA  1 
ATOM   5102  C  C   . ALA E  1 89  ? 35.826  -43.382 23.119  1.00 73.12  ? 89  ALA I C   1 
ATOM   5103  O  O   . ALA E  1 89  ? 35.906  -44.585 23.386  1.00 73.41  ? 89  ALA I O   1 
ATOM   5104  C  CB  . ALA E  1 89  ? 35.222  -42.230 25.257  1.00 68.39  ? 89  ALA I CB  1 
ATOM   5105  N  N   . ASP E  1 90  ? 36.616  -42.775 22.231  1.00 76.06  ? 90  ASP I N   1 
ATOM   5106  C  CA  . ASP E  1 90  ? 37.687  -43.483 21.501  1.00 80.06  ? 90  ASP I CA  1 
ATOM   5107  C  C   . ASP E  1 90  ? 38.892  -43.791 22.408  1.00 81.77  ? 90  ASP I C   1 
ATOM   5108  O  O   . ASP E  1 90  ? 38.845  -43.535 23.615  1.00 79.72  ? 90  ASP I O   1 
ATOM   5109  C  CB  . ASP E  1 90  ? 38.105  -42.683 20.244  1.00 82.97  ? 90  ASP I CB  1 
ATOM   5110  C  CG  . ASP E  1 90  ? 38.796  -41.349 20.567  1.00 83.80  ? 90  ASP I CG  1 
ATOM   5111  O  OD1 . ASP E  1 90  ? 39.033  -41.033 21.752  1.00 82.34  ? 90  ASP I OD1 1 
ATOM   5112  O  OD2 . ASP E  1 90  ? 39.099  -40.602 19.614  1.00 86.16  ? 90  ASP I OD2 1 
ATOM   5113  N  N   . LYS E  1 91  ? 39.964  -44.329 21.827  1.00 85.79  ? 91  LYS I N   1 
ATOM   5114  C  CA  . LYS E  1 91  ? 41.197  -44.647 22.565  1.00 88.25  ? 91  LYS I CA  1 
ATOM   5115  C  C   . LYS E  1 91  ? 41.864  -43.433 23.236  1.00 88.69  ? 91  LYS I C   1 
ATOM   5116  O  O   . LYS E  1 91  ? 42.429  -43.563 24.321  1.00 88.91  ? 91  LYS I O   1 
ATOM   5117  C  CB  . LYS E  1 91  ? 42.192  -45.346 21.634  1.00 92.99  ? 91  LYS I CB  1 
ATOM   5118  C  CG  . LYS E  1 91  ? 43.464  -45.841 22.308  1.00 96.12  ? 91  LYS I CG  1 
ATOM   5119  C  CD  . LYS E  1 91  ? 44.236  -46.818 21.429  1.00 100.57 ? 91  LYS I CD  1 
ATOM   5120  C  CE  . LYS E  1 91  ? 44.616  -46.239 20.070  1.00 103.80 ? 91  LYS I CE  1 
ATOM   5121  N  NZ  . LYS E  1 91  ? 45.286  -44.911 20.157  1.00 105.25 ? 91  LYS I NZ  1 
ATOM   5122  N  N   . ASP E  1 92  ? 41.790  -42.265 22.599  1.00 89.05  ? 92  ASP I N   1 
ATOM   5123  C  CA  . ASP E  1 92  ? 42.278  -41.009 23.203  1.00 89.30  ? 92  ASP I CA  1 
ATOM   5124  C  C   . ASP E  1 92  ? 41.390  -40.465 24.333  1.00 84.92  ? 92  ASP I C   1 
ATOM   5125  O  O   . ASP E  1 92  ? 41.767  -39.494 24.994  1.00 84.99  ? 92  ASP I O   1 
ATOM   5126  C  CB  . ASP E  1 92  ? 42.446  -39.920 22.131  1.00 91.29  ? 92  ASP I CB  1 
ATOM   5127  C  CG  . ASP E  1 92  ? 43.554  -40.233 21.144  1.00 96.42  ? 92  ASP I CG  1 
ATOM   5128  O  OD1 . ASP E  1 92  ? 44.653  -40.632 21.584  1.00 99.33  ? 92  ASP I OD1 1 
ATOM   5129  O  OD2 . ASP E  1 92  ? 43.333  -40.065 19.927  1.00 97.83  ? 92  ASP I OD2 1 
ATOM   5130  N  N   . GLY E  1 93  ? 40.220  -41.073 24.542  1.00 81.41  ? 93  GLY I N   1 
ATOM   5131  C  CA  . GLY E  1 93  ? 39.292  -40.671 25.592  1.00 77.42  ? 93  GLY I CA  1 
ATOM   5132  C  C   . GLY E  1 93  ? 38.333  -39.577 25.169  1.00 75.30  ? 93  GLY I C   1 
ATOM   5133  O  O   . GLY E  1 93  ? 37.744  -38.909 26.023  1.00 72.64  ? 93  GLY I O   1 
ATOM   5134  N  N   . VAL E  1 94  ? 38.167  -39.408 23.855  1.00 76.71  ? 94  VAL I N   1 
ATOM   5135  C  CA  . VAL E  1 94  ? 37.348  -38.343 23.281  1.00 75.49  ? 94  VAL I CA  1 
ATOM   5136  C  C   . VAL E  1 94  ? 36.059  -38.946 22.722  1.00 73.38  ? 94  VAL I C   1 
ATOM   5137  O  O   . VAL E  1 94  ? 36.097  -39.726 21.768  1.00 75.09  ? 94  VAL I O   1 
ATOM   5138  C  CB  . VAL E  1 94  ? 38.101  -37.579 22.164  1.00 79.10  ? 94  VAL I CB  1 
ATOM   5139  C  CG1 . VAL E  1 94  ? 37.240  -36.445 21.607  1.00 77.96  ? 94  VAL I CG1 1 
ATOM   5140  C  CG2 . VAL E  1 94  ? 39.425  -37.033 22.689  1.00 81.74  ? 94  VAL I CG2 1 
ATOM   5141  N  N   . ALA E  1 95  ? 34.929  -38.579 23.325  1.00 69.97  ? 95  ALA I N   1 
ATOM   5142  C  CA  . ALA E  1 95  ? 33.610  -39.029 22.881  1.00 68.02  ? 95  ALA I CA  1 
ATOM   5143  C  C   . ALA E  1 95  ? 32.930  -37.943 22.054  1.00 68.01  ? 95  ALA I C   1 
ATOM   5144  O  O   . ALA E  1 95  ? 32.381  -36.991 22.612  1.00 66.08  ? 95  ALA I O   1 
ATOM   5145  C  CB  . ALA E  1 95  ? 32.746  -39.397 24.082  1.00 64.61  ? 95  ALA I CB  1 
ATOM   5146  N  N   . ASP E  1 96  ? 32.981  -38.082 20.728  1.00 70.41  ? 96  ASP I N   1 
ATOM   5147  C  CA  . ASP E  1 96  ? 32.224  -37.199 19.831  1.00 70.69  ? 96  ASP I CA  1 
ATOM   5148  C  C   . ASP E  1 96  ? 30.764  -37.629 19.839  1.00 68.21  ? 96  ASP I C   1 
ATOM   5149  O  O   . ASP E  1 96  ? 30.453  -38.789 19.567  1.00 68.27  ? 96  ASP I O   1 
ATOM   5150  C  CB  . ASP E  1 96  ? 32.773  -37.226 18.397  1.00 74.47  ? 96  ASP I CB  1 
ATOM   5151  C  CG  . ASP E  1 96  ? 33.998  -36.346 18.219  1.00 77.29  ? 96  ASP I CG  1 
ATOM   5152  O  OD1 . ASP E  1 96  ? 34.058  -35.248 18.817  1.00 76.38  ? 96  ASP I OD1 1 
ATOM   5153  O  OD2 . ASP E  1 96  ? 34.901  -36.745 17.457  1.00 80.70  ? 96  ASP I OD2 1 
ATOM   5154  N  N   . VAL E  1 97  ? 29.881  -36.688 20.165  1.00 66.32  ? 97  VAL I N   1 
ATOM   5155  C  CA  . VAL E  1 97  ? 28.453  -36.954 20.284  1.00 64.09  ? 97  VAL I CA  1 
ATOM   5156  C  C   . VAL E  1 97  ? 27.744  -36.404 19.052  1.00 65.59  ? 97  VAL I C   1 
ATOM   5157  O  O   . VAL E  1 97  ? 27.996  -35.271 18.642  1.00 66.86  ? 97  VAL I O   1 
ATOM   5158  C  CB  . VAL E  1 97  ? 27.875  -36.317 21.561  1.00 61.11  ? 97  VAL I CB  1 
ATOM   5159  C  CG1 . VAL E  1 97  ? 26.412  -36.714 21.747  1.00 59.07  ? 97  VAL I CG1 1 
ATOM   5160  C  CG2 . VAL E  1 97  ? 28.711  -36.725 22.772  1.00 60.17  ? 97  VAL I CG2 1 
ATOM   5161  N  N   . SER E  1 98  ? 26.876  -37.227 18.463  1.00 65.73  ? 98  SER I N   1 
ATOM   5162  C  CA  . SER E  1 98  ? 26.050  -36.831 17.320  1.00 67.28  ? 98  SER I CA  1 
ATOM   5163  C  C   . SER E  1 98  ? 24.755  -37.657 17.319  1.00 66.06  ? 98  SER I C   1 
ATOM   5164  O  O   . SER E  1 98  ? 24.678  -38.731 16.717  1.00 67.38  ? 98  SER I O   1 
ATOM   5165  C  CB  . SER E  1 98  ? 26.823  -37.000 16.011  1.00 70.97  ? 98  SER I CB  1 
ATOM   5166  O  OG  . SER E  1 98  ? 26.077  -36.486 14.923  1.00 72.76  ? 98  SER I OG  1 
ATOM   5167  N  N   . ILE E  1 99  ? 23.751  -37.127 18.010  1.00 63.82  ? 99  ILE I N   1 
ATOM   5168  C  CA  . ILE E  1 99  ? 22.511  -37.827 18.326  1.00 62.36  ? 99  ILE I CA  1 
ATOM   5169  C  C   . ILE E  1 99  ? 21.343  -37.017 17.767  1.00 62.88  ? 99  ILE I C   1 
ATOM   5170  O  O   . ILE E  1 99  ? 21.426  -35.791 17.665  1.00 63.19  ? 99  ILE I O   1 
ATOM   5171  C  CB  . ILE E  1 99  ? 22.364  -37.959 19.871  1.00 59.31  ? 99  ILE I CB  1 
ATOM   5172  C  CG1 . ILE E  1 99  ? 23.467  -38.861 20.446  1.00 59.02  ? 99  ILE I CG1 1 
ATOM   5173  C  CG2 . ILE E  1 99  ? 20.985  -38.482 20.282  1.00 57.95  ? 99  ILE I CG2 1 
ATOM   5174  C  CD1 . ILE E  1 99  ? 23.654  -38.722 21.947  1.00 56.53  ? 99  ILE I CD1 1 
ATOM   5175  N  N   . GLU E  1 100 ? 20.269  -37.709 17.395  1.00 63.24  ? 100 GLU I N   1 
ATOM   5176  C  CA  . GLU E  1 100 ? 18.963  -37.083 17.178  1.00 63.42  ? 100 GLU I CA  1 
ATOM   5177  C  C   . GLU E  1 100 ? 17.915  -37.833 17.998  1.00 61.56  ? 100 GLU I C   1 
ATOM   5178  O  O   . GLU E  1 100 ? 17.914  -39.066 18.037  1.00 61.57  ? 100 GLU I O   1 
ATOM   5179  C  CB  . GLU E  1 100 ? 18.592  -37.073 15.699  1.00 66.74  ? 100 GLU I CB  1 
ATOM   5180  C  CG  . GLU E  1 100 ? 19.510  -36.196 14.857  1.00 68.93  ? 100 GLU I CG  1 
ATOM   5181  C  CD  . GLU E  1 100 ? 18.900  -35.772 13.530  1.00 72.20  ? 100 GLU I CD  1 
ATOM   5182  O  OE1 . GLU E  1 100 ? 17.730  -35.329 13.508  1.00 72.33  ? 100 GLU I OE1 1 
ATOM   5183  O  OE2 . GLU E  1 100 ? 19.605  -35.856 12.503  1.00 74.97  ? 100 GLU I OE2 1 
ATOM   5184  N  N   . ASP E  1 101 ? 17.037  -37.082 18.661  1.00 60.13  ? 101 ASP I N   1 
ATOM   5185  C  CA  . ASP E  1 101 ? 16.042  -37.652 19.571  1.00 58.44  ? 101 ASP I CA  1 
ATOM   5186  C  C   . ASP E  1 101 ? 14.724  -36.901 19.422  1.00 59.07  ? 101 ASP I C   1 
ATOM   5187  O  O   . ASP E  1 101 ? 14.723  -35.677 19.321  1.00 59.31  ? 101 ASP I O   1 
ATOM   5188  C  CB  . ASP E  1 101 ? 16.542  -37.548 21.013  1.00 55.62  ? 101 ASP I CB  1 
ATOM   5189  C  CG  . ASP E  1 101 ? 15.808  -38.480 21.960  1.00 54.19  ? 101 ASP I CG  1 
ATOM   5190  O  OD1 . ASP E  1 101 ? 16.146  -39.682 21.990  1.00 54.24  ? 101 ASP I OD1 1 
ATOM   5191  O  OD2 . ASP E  1 101 ? 14.907  -38.017 22.691  1.00 53.18  ? 101 ASP I OD2 1 
ATOM   5192  N  N   . SER E  1 102 ? 13.617  -37.643 19.418  1.00 59.57  ? 102 SER I N   1 
ATOM   5193  C  CA  . SER E  1 102 ? 12.270  -37.085 19.257  1.00 60.66  ? 102 SER I CA  1 
ATOM   5194  C  C   . SER E  1 102 ? 11.401  -37.226 20.517  1.00 58.82  ? 102 SER I C   1 
ATOM   5195  O  O   . SER E  1 102 ? 10.185  -37.038 20.456  1.00 60.00  ? 102 SER I O   1 
ATOM   5196  C  CB  . SER E  1 102 ? 11.578  -37.756 18.063  1.00 63.70  ? 102 SER I CB  1 
ATOM   5197  O  OG  . SER E  1 102 ? 12.281  -37.505 16.855  1.00 65.78  ? 102 SER I OG  1 
ATOM   5198  N  N   . VAL E  1 103 ? 12.019  -37.543 21.654  1.00 56.23  ? 103 VAL I N   1 
ATOM   5199  C  CA  . VAL E  1 103 ? 11.303  -37.642 22.930  1.00 54.57  ? 103 VAL I CA  1 
ATOM   5200  C  C   . VAL E  1 103 ? 11.582  -36.391 23.762  1.00 52.91  ? 103 VAL I C   1 
ATOM   5201  O  O   . VAL E  1 103 ? 10.640  -35.733 24.220  1.00 52.99  ? 103 VAL I O   1 
ATOM   5202  C  CB  . VAL E  1 103 ? 11.673  -38.926 23.693  1.00 53.22  ? 103 VAL I CB  1 
ATOM   5203  C  CG1 . VAL E  1 103 ? 10.920  -39.008 25.017  1.00 51.89  ? 103 VAL I CG1 1 
ATOM   5204  C  CG2 . VAL E  1 103 ? 11.370  -40.145 22.829  1.00 55.09  ? 103 VAL I CG2 1 
ATOM   5205  N  N   . ILE E  1 104 ? 12.865  -36.062 23.941  1.00 51.65  ? 104 ILE I N   1 
ATOM   5206  C  CA  . ILE E  1 104 ? 13.257  -34.774 24.530  1.00 50.56  ? 104 ILE I CA  1 
ATOM   5207  C  C   . ILE E  1 104 ? 12.807  -33.590 23.663  1.00 52.31  ? 104 ILE I C   1 
ATOM   5208  O  O   . ILE E  1 104 ? 12.499  -33.745 22.484  1.00 54.37  ? 104 ILE I O   1 
ATOM   5209  C  CB  . ILE E  1 104 ? 14.782  -34.650 24.793  1.00 49.45  ? 104 ILE I CB  1 
ATOM   5210  C  CG1 . ILE E  1 104 ? 15.611  -34.800 23.505  1.00 51.10  ? 104 ILE I CG1 1 
ATOM   5211  C  CG2 . ILE E  1 104 ? 15.226  -35.652 25.853  1.00 47.73  ? 104 ILE I CG2 1 
ATOM   5212  C  CD1 . ILE E  1 104 ? 16.949  -34.092 23.553  1.00 50.88  ? 104 ILE I CD1 1 
ATOM   5213  N  N   . SER E  1 105 ? 12.772  -32.410 24.267  1.00 51.65  ? 105 SER I N   1 
ATOM   5214  C  CA  . SER E  1 105 ? 12.447  -31.187 23.538  1.00 53.39  ? 105 SER I CA  1 
ATOM   5215  C  C   . SER E  1 105 ? 13.111  -29.988 24.190  1.00 52.41  ? 105 SER I C   1 
ATOM   5216  O  O   . SER E  1 105 ? 13.592  -30.071 25.319  1.00 50.36  ? 105 SER I O   1 
ATOM   5217  C  CB  . SER E  1 105 ? 10.932  -30.990 23.470  1.00 54.71  ? 105 SER I CB  1 
ATOM   5218  O  OG  . SER E  1 105 ? 10.598  -29.925 22.598  1.00 56.93  ? 105 SER I OG  1 
ATOM   5219  N  N   . LEU E  1 106 ? 13.152  -28.885 23.448  1.00 54.09  ? 106 LEU I N   1 
ATOM   5220  C  CA  . LEU E  1 106 ? 13.642  -27.611 23.963  1.00 53.73  ? 106 LEU I CA  1 
ATOM   5221  C  C   . LEU E  1 106 ? 12.478  -26.645 24.248  1.00 54.55  ? 106 LEU I C   1 
ATOM   5222  O  O   . LEU E  1 106 ? 12.702  -25.452 24.444  1.00 54.92  ? 106 LEU I O   1 
ATOM   5223  C  CB  . LEU E  1 106 ? 14.667  -27.008 22.994  1.00 55.26  ? 106 LEU I CB  1 
ATOM   5224  C  CG  . LEU E  1 106 ? 15.823  -27.920 22.548  1.00 55.11  ? 106 LEU I CG  1 
ATOM   5225  C  CD1 . LEU E  1 106 ? 16.786  -27.148 21.661  1.00 57.01  ? 106 LEU I CD1 1 
ATOM   5226  C  CD2 . LEU E  1 106 ? 16.576  -28.536 23.723  1.00 52.68  ? 106 LEU I CD2 1 
ATOM   5227  N  N   . SER E  1 107 ? 11.249  -27.173 24.268  1.00 55.06  ? 107 SER I N   1 
ATOM   5228  C  CA  . SER E  1 107 ? 10.065  -26.461 24.767  1.00 55.82  ? 107 SER I CA  1 
ATOM   5229  C  C   . SER E  1 107 ? 8.968   -27.460 25.189  1.00 55.68  ? 107 SER I C   1 
ATOM   5230  O  O   . SER E  1 107 ? 9.075   -28.660 24.918  1.00 55.29  ? 107 SER I O   1 
ATOM   5231  C  CB  . SER E  1 107 ? 9.536   -25.461 23.720  1.00 58.69  ? 107 SER I CB  1 
ATOM   5232  O  OG  . SER E  1 107 ? 9.393   -26.051 22.436  1.00 60.56  ? 107 SER I OG  1 
ATOM   5233  N  N   . GLY E  1 108 ? 7.948   -26.964 25.890  1.00 56.17  ? 108 GLY I N   1 
ATOM   5234  C  CA  . GLY E  1 108 ? 6.787   -27.776 26.291  1.00 56.63  ? 108 GLY I CA  1 
ATOM   5235  C  C   . GLY E  1 108 ? 7.011   -28.780 27.417  1.00 54.35  ? 108 GLY I C   1 
ATOM   5236  O  O   . GLY E  1 108 ? 7.878   -28.585 28.269  1.00 52.32  ? 108 GLY I O   1 
ATOM   5237  N  N   . ASP E  1 109 ? 6.218   -29.855 27.406  1.00 55.01  ? 109 ASP I N   1 
ATOM   5238  C  CA  . ASP E  1 109 ? 6.163   -30.847 28.505  1.00 53.42  ? 109 ASP I CA  1 
ATOM   5239  C  C   . ASP E  1 109 ? 7.468   -31.593 28.750  1.00 51.13  ? 109 ASP I C   1 
ATOM   5240  O  O   . ASP E  1 109 ? 7.851   -31.836 29.898  1.00 49.38  ? 109 ASP I O   1 
ATOM   5241  C  CB  . ASP E  1 109 ? 5.060   -31.885 28.242  1.00 55.09  ? 109 ASP I CB  1 
ATOM   5242  C  CG  . ASP E  1 109 ? 3.673   -31.312 28.395  1.00 57.40  ? 109 ASP I CG  1 
ATOM   5243  O  OD1 . ASP E  1 109 ? 3.371   -30.799 29.497  1.00 56.90  ? 109 ASP I OD1 1 
ATOM   5244  O  OD2 . ASP E  1 109 ? 2.886   -31.378 27.419  1.00 59.99  ? 109 ASP I OD2 1 
ATOM   5245  N  N   . HIS E  1 110 ? 8.134   -31.962 27.660  1.00 51.46  ? 110 HIS I N   1 
ATOM   5246  C  CA  . HIS E  1 110 ? 9.395   -32.690 27.712  1.00 49.81  ? 110 HIS I CA  1 
ATOM   5247  C  C   . HIS E  1 110 ? 10.595  -31.745 27.568  1.00 49.08  ? 110 HIS I C   1 
ATOM   5248  O  O   . HIS E  1 110 ? 11.681  -32.187 27.175  1.00 48.56  ? 110 HIS I O   1 
ATOM   5249  C  CB  . HIS E  1 110 ? 9.415   -33.771 26.614  1.00 50.96  ? 110 HIS I CB  1 
ATOM   5250  C  CG  . HIS E  1 110 ? 8.407   -34.862 26.816  1.00 51.68  ? 110 HIS I CG  1 
ATOM   5251  N  ND1 . HIS E  1 110 ? 8.319   -35.955 25.980  1.00 52.85  ? 110 HIS I ND1 1 
ATOM   5252  C  CD2 . HIS E  1 110 ? 7.464   -35.044 27.772  1.00 51.64  ? 110 HIS I CD2 1 
ATOM   5253  C  CE1 . HIS E  1 110 ? 7.354   -36.754 26.401  1.00 53.51  ? 110 HIS I CE1 1 
ATOM   5254  N  NE2 . HIS E  1 110 ? 6.817   -36.223 27.486  1.00 52.84  ? 110 HIS I NE2 1 
ATOM   5255  N  N   . CYS E  1 111 ? 10.419  -30.459 27.896  1.00 49.24  ? 111 CYS I N   1 
ATOM   5256  C  CA  . CYS E  1 111 ? 11.518  -29.502 27.804  1.00 48.84  ? 111 CYS I CA  1 
ATOM   5257  C  C   . CYS E  1 111 ? 12.645  -29.898 28.751  1.00 46.73  ? 111 CYS I C   1 
ATOM   5258  O  O   . CYS E  1 111 ? 12.384  -30.212 29.916  1.00 45.58  ? 111 CYS I O   1 
ATOM   5259  C  CB  . CYS E  1 111 ? 11.067  -28.084 28.139  1.00 49.54  ? 111 CYS I CB  1 
ATOM   5260  S  SG  . CYS E  1 111 ? 12.349  -26.858 27.792  1.00 49.89  ? 111 CYS I SG  1 
ATOM   5261  N  N   . ILE E  1 112 ? 13.881  -29.880 28.254  1.00 46.54  ? 112 ILE I N   1 
ATOM   5262  C  CA  . ILE E  1 112 ? 15.065  -30.222 29.067  1.00 45.00  ? 112 ILE I CA  1 
ATOM   5263  C  C   . ILE E  1 112 ? 15.913  -29.013 29.469  1.00 44.86  ? 112 ILE I C   1 
ATOM   5264  O  O   . ILE E  1 112 ? 16.909  -29.169 30.175  1.00 43.91  ? 112 ILE I O   1 
ATOM   5265  C  CB  . ILE E  1 112 ? 15.956  -31.290 28.382  1.00 45.12  ? 112 ILE I CB  1 
ATOM   5266  C  CG1 . ILE E  1 112 ? 16.542  -30.787 27.049  1.00 46.80  ? 112 ILE I CG1 1 
ATOM   5267  C  CG2 . ILE E  1 112 ? 15.158  -32.573 28.177  1.00 45.17  ? 112 ILE I CG2 1 
ATOM   5268  C  CD1 . ILE E  1 112 ? 17.568  -31.717 26.429  1.00 47.18  ? 112 ILE I CD1 1 
ATOM   5269  N  N   . ILE E  1 113 ? 15.526  -27.815 29.031  1.00 46.02  ? 113 ILE I N   1 
ATOM   5270  C  CA  . ILE E  1 113 ? 16.230  -26.594 29.409  1.00 46.24  ? 113 ILE I CA  1 
ATOM   5271  C  C   . ILE E  1 113 ? 16.044  -26.341 30.912  1.00 44.97  ? 113 ILE I C   1 
ATOM   5272  O  O   . ILE E  1 113 ? 14.952  -26.523 31.458  1.00 44.59  ? 113 ILE I O   1 
ATOM   5273  C  CB  . ILE E  1 113 ? 15.773  -25.382 28.556  1.00 48.12  ? 113 ILE I CB  1 
ATOM   5274  C  CG1 . ILE E  1 113 ? 16.271  -25.559 27.115  1.00 49.65  ? 113 ILE I CG1 1 
ATOM   5275  C  CG2 . ILE E  1 113 ? 16.300  -24.068 29.123  1.00 48.44  ? 113 ILE I CG2 1 
ATOM   5276  C  CD1 . ILE E  1 113 ? 15.653  -24.607 26.113  1.00 51.84  ? 113 ILE I CD1 1 
ATOM   5277  N  N   . GLY E  1 114 ? 17.139  -25.956 31.566  1.00 44.57  ? 114 GLY I N   1 
ATOM   5278  C  CA  . GLY E  1 114 ? 17.181  -25.787 33.013  1.00 43.58  ? 114 GLY I CA  1 
ATOM   5279  C  C   . GLY E  1 114 ? 17.324  -27.064 33.825  1.00 42.21  ? 114 GLY I C   1 
ATOM   5280  O  O   . GLY E  1 114 ? 17.241  -27.022 35.056  1.00 41.52  ? 114 GLY I O   1 
ATOM   5281  N  N   . ARG E  1 115 ? 17.532  -28.190 33.148  1.00 42.02  ? 115 ARG I N   1 
ATOM   5282  C  CA  . ARG E  1 115 ? 17.754  -29.476 33.796  1.00 41.02  ? 115 ARG I CA  1 
ATOM   5283  C  C   . ARG E  1 115 ? 19.218  -29.830 33.593  1.00 41.24  ? 115 ARG I C   1 
ATOM   5284  O  O   . ARG E  1 115 ? 19.955  -29.044 33.007  1.00 42.19  ? 115 ARG I O   1 
ATOM   5285  C  CB  . ARG E  1 115 ? 16.812  -30.521 33.206  1.00 40.96  ? 115 ARG I CB  1 
ATOM   5286  C  CG  . ARG E  1 115 ? 15.348  -30.138 33.374  1.00 41.23  ? 115 ARG I CG  1 
ATOM   5287  C  CD  . ARG E  1 115 ? 14.396  -31.257 32.995  1.00 41.38  ? 115 ARG I CD  1 
ATOM   5288  N  NE  . ARG E  1 115 ? 13.001  -30.800 32.988  1.00 42.16  ? 115 ARG I NE  1 
ATOM   5289  C  CZ  . ARG E  1 115 ? 12.180  -30.778 34.042  1.00 41.98  ? 115 ARG I CZ  1 
ATOM   5290  N  NH1 . ARG E  1 115 ? 12.576  -31.188 35.254  1.00 40.95  ? 115 ARG I NH1 1 
ATOM   5291  N  NH2 . ARG E  1 115 ? 10.927  -30.349 33.881  1.00 43.10  ? 115 ARG I NH2 1 
ATOM   5292  N  N   . THR E  1 116 ? 19.654  -30.984 34.088  1.00 40.68  ? 116 THR I N   1 
ATOM   5293  C  CA  . THR E  1 116 ? 21.075  -31.324 34.070  1.00 41.15  ? 116 THR I CA  1 
ATOM   5294  C  C   . THR E  1 116 ? 21.387  -32.457 33.094  1.00 41.61  ? 116 THR I C   1 
ATOM   5295  O  O   . THR E  1 116 ? 20.701  -33.483 33.083  1.00 41.13  ? 116 THR I O   1 
ATOM   5296  C  CB  . THR E  1 116 ? 21.577  -31.704 35.477  1.00 40.62  ? 116 THR I CB  1 
ATOM   5297  O  OG1 . THR E  1 116 ? 21.427  -30.582 36.352  1.00 40.57  ? 116 THR I OG1 1 
ATOM   5298  C  CG2 . THR E  1 116 ? 23.055  -32.092 35.448  1.00 41.45  ? 116 THR I CG2 1 
ATOM   5299  N  N   . LEU E  1 117 ? 22.439  -32.267 32.300  1.00 42.76  ? 117 LEU I N   1 
ATOM   5300  C  CA  . LEU E  1 117 ? 22.992  -33.321 31.469  1.00 43.49  ? 117 LEU I CA  1 
ATOM   5301  C  C   . LEU E  1 117 ? 24.134  -33.978 32.248  1.00 43.68  ? 117 LEU I C   1 
ATOM   5302  O  O   . LEU E  1 117 ? 24.965  -33.283 32.833  1.00 44.11  ? 117 LEU I O   1 
ATOM   5303  C  CB  . LEU E  1 117 ? 23.510  -32.743 30.153  1.00 45.11  ? 117 LEU I CB  1 
ATOM   5304  C  CG  . LEU E  1 117 ? 24.060  -33.742 29.130  1.00 46.31  ? 117 LEU I CG  1 
ATOM   5305  C  CD1 . LEU E  1 117 ? 22.961  -34.680 28.650  1.00 45.85  ? 117 LEU I CD1 1 
ATOM   5306  C  CD2 . LEU E  1 117 ? 24.705  -33.014 27.956  1.00 48.28  ? 117 LEU I CD2 1 
ATOM   5307  N  N   . VAL E  1 118 ? 24.168  -35.311 32.252  1.00 43.58  ? 118 VAL I N   1 
ATOM   5308  C  CA  . VAL E  1 118 ? 25.158  -36.073 33.018  1.00 43.97  ? 118 VAL I CA  1 
ATOM   5309  C  C   . VAL E  1 118 ? 25.807  -37.142 32.140  1.00 45.24  ? 118 VAL I C   1 
ATOM   5310  O  O   . VAL E  1 118 ? 25.120  -37.844 31.393  1.00 45.12  ? 118 VAL I O   1 
ATOM   5311  C  CB  . VAL E  1 118 ? 24.513  -36.749 34.251  1.00 42.72  ? 118 VAL I CB  1 
ATOM   5312  C  CG1 . VAL E  1 118 ? 25.553  -37.535 35.056  1.00 43.39  ? 118 VAL I CG1 1 
ATOM   5313  C  CG2 . VAL E  1 118 ? 23.821  -35.711 35.131  1.00 41.73  ? 118 VAL I CG2 1 
ATOM   5314  N  N   . VAL E  1 119 ? 27.133  -37.253 32.249  1.00 46.72  ? 119 VAL I N   1 
ATOM   5315  C  CA  . VAL E  1 119 ? 27.899  -38.319 31.597  1.00 48.28  ? 119 VAL I CA  1 
ATOM   5316  C  C   . VAL E  1 119 ? 28.471  -39.223 32.691  1.00 48.52  ? 119 VAL I C   1 
ATOM   5317  O  O   . VAL E  1 119 ? 28.958  -38.740 33.716  1.00 48.53  ? 119 VAL I O   1 
ATOM   5318  C  CB  . VAL E  1 119 ? 28.999  -37.794 30.634  1.00 50.44  ? 119 VAL I CB  1 
ATOM   5319  C  CG1 . VAL E  1 119 ? 30.012  -36.895 31.337  1.00 51.33  ? 119 VAL I CG1 1 
ATOM   5320  C  CG2 . VAL E  1 119 ? 29.701  -38.958 29.940  1.00 52.17  ? 119 VAL I CG2 1 
ATOM   5321  N  N   . HIS E  1 120 ? 28.415  -40.531 32.456  1.00 49.03  ? 120 HIS I N   1 
ATOM   5322  C  CA  . HIS E  1 120 ? 28.605  -41.527 33.514  1.00 49.08  ? 120 HIS I CA  1 
ATOM   5323  C  C   . HIS E  1 120 ? 29.928  -42.291 33.447  1.00 51.35  ? 120 HIS I C   1 
ATOM   5324  O  O   . HIS E  1 120 ? 30.639  -42.272 32.433  1.00 53.03  ? 120 HIS I O   1 
ATOM   5325  C  CB  . HIS E  1 120 ? 27.424  -42.507 33.515  1.00 48.00  ? 120 HIS I CB  1 
ATOM   5326  C  CG  . HIS E  1 120 ? 26.236  -42.013 34.279  1.00 46.13  ? 120 HIS I CG  1 
ATOM   5327  N  ND1 . HIS E  1 120 ? 25.961  -42.414 35.569  1.00 45.55  ? 120 HIS I ND1 1 
ATOM   5328  C  CD2 . HIS E  1 120 ? 25.259  -41.138 33.940  1.00 45.01  ? 120 HIS I CD2 1 
ATOM   5329  C  CE1 . HIS E  1 120 ? 24.861  -41.814 35.988  1.00 44.13  ? 120 HIS I CE1 1 
ATOM   5330  N  NE2 . HIS E  1 120 ? 24.417  -41.033 35.020  1.00 43.76  ? 120 HIS I NE2 1 
ATOM   5331  N  N   . GLU E  1 121 ? 30.220  -42.955 34.566  1.00 51.59  ? 121 GLU I N   1 
ATOM   5332  C  CA  . GLU E  1 121 ? 31.440  -43.729 34.790  1.00 53.90  ? 121 GLU I CA  1 
ATOM   5333  C  C   . GLU E  1 121 ? 31.589  -44.884 33.811  1.00 55.17  ? 121 GLU I C   1 
ATOM   5334  O  O   . GLU E  1 121 ? 32.677  -45.120 33.283  1.00 57.58  ? 121 GLU I O   1 
ATOM   5335  C  CB  . GLU E  1 121 ? 31.423  -44.292 36.219  1.00 53.77  ? 121 GLU I CB  1 
ATOM   5336  C  CG  . GLU E  1 121 ? 32.696  -44.999 36.678  1.00 56.38  ? 121 GLU I CG  1 
ATOM   5337  C  CD  . GLU E  1 121 ? 32.515  -45.767 37.982  1.00 56.41  ? 121 GLU I CD  1 
ATOM   5338  O  OE1 . GLU E  1 121 ? 31.514  -45.545 38.700  1.00 54.49  ? 121 GLU I OE1 1 
ATOM   5339  O  OE2 . GLU E  1 121 ? 33.387  -46.600 38.298  1.00 58.66  ? 121 GLU I OE2 1 
ATOM   5340  N  N   . LYS E  1 122 ? 30.499  -45.614 33.599  1.00 53.87  ? 122 LYS I N   1 
ATOM   5341  C  CA  . LYS E  1 122 ? 30.514  -46.798 32.748  1.00 55.10  ? 122 LYS I CA  1 
ATOM   5342  C  C   . LYS E  1 122 ? 29.219  -46.881 31.937  1.00 53.65  ? 122 LYS I C   1 
ATOM   5343  O  O   . LYS E  1 122 ? 28.433  -45.937 31.939  1.00 51.96  ? 122 LYS I O   1 
ATOM   5344  C  CB  . LYS E  1 122 ? 30.779  -48.047 33.607  1.00 56.04  ? 122 LYS I CB  1 
ATOM   5345  C  CG  . LYS E  1 122 ? 29.753  -48.328 34.693  1.00 54.26  ? 122 LYS I CG  1 
ATOM   5346  C  CD  . LYS E  1 122 ? 30.225  -49.476 35.580  1.00 55.70  ? 122 LYS I CD  1 
ATOM   5347  C  CE  . LYS E  1 122 ? 29.224  -49.795 36.680  1.00 54.30  ? 122 LYS I CE  1 
ATOM   5348  N  NZ  . LYS E  1 122 ? 29.753  -50.811 37.633  1.00 55.97  ? 122 LYS I NZ  1 
ATOM   5349  N  N   . ALA E  1 123 ? 29.018  -47.995 31.233  1.00 54.61  ? 123 ALA I N   1 
ATOM   5350  C  CA  . ALA E  1 123 ? 27.919  -48.143 30.274  1.00 53.96  ? 123 ALA I CA  1 
ATOM   5351  C  C   . ALA E  1 123 ? 26.528  -48.217 30.917  1.00 51.85  ? 123 ALA I C   1 
ATOM   5352  O  O   . ALA E  1 123 ? 26.335  -48.843 31.963  1.00 51.42  ? 123 ALA I O   1 
ATOM   5353  C  CB  . ALA E  1 123 ? 28.147  -49.379 29.403  1.00 56.00  ? 123 ALA I CB  1 
ATOM   5354  N  N   . ASP E  1 124 ? 25.571  -47.565 30.265  1.00 50.82  ? 124 ASP I N   1 
ATOM   5355  C  CA  . ASP E  1 124 ? 24.147  -47.760 30.522  1.00 49.48  ? 124 ASP I CA  1 
ATOM   5356  C  C   . ASP E  1 124 ? 23.753  -49.125 29.957  1.00 50.77  ? 124 ASP I C   1 
ATOM   5357  O  O   . ASP E  1 124 ? 24.008  -49.388 28.778  1.00 52.22  ? 124 ASP I O   1 
ATOM   5358  C  CB  . ASP E  1 124 ? 23.362  -46.645 29.815  1.00 48.68  ? 124 ASP I CB  1 
ATOM   5359  C  CG  . ASP E  1 124 ? 21.892  -46.601 30.201  1.00 47.45  ? 124 ASP I CG  1 
ATOM   5360  O  OD1 . ASP E  1 124 ? 21.318  -47.636 30.604  1.00 47.59  ? 124 ASP I OD1 1 
ATOM   5361  O  OD2 . ASP E  1 124 ? 21.303  -45.506 30.074  1.00 46.56  ? 124 ASP I OD2 1 
ATOM   5362  N  N   . ASP E  1 125 ? 23.133  -49.980 30.781  1.00 50.43  ? 125 ASP I N   1 
ATOM   5363  C  CA  . ASP E  1 125 ? 22.636  -51.302 30.315  1.00 51.80  ? 125 ASP I CA  1 
ATOM   5364  C  C   . ASP E  1 125 ? 21.272  -51.256 29.580  1.00 51.69  ? 125 ASP I C   1 
ATOM   5365  O  O   . ASP E  1 125 ? 20.739  -52.303 29.204  1.00 52.94  ? 125 ASP I O   1 
ATOM   5366  C  CB  . ASP E  1 125 ? 22.628  -52.357 31.456  1.00 52.10  ? 125 ASP I CB  1 
ATOM   5367  C  CG  . ASP E  1 125 ? 21.649  -52.032 32.603  1.00 50.55  ? 125 ASP I CG  1 
ATOM   5368  O  OD1 . ASP E  1 125 ? 20.604  -51.377 32.392  1.00 49.55  ? 125 ASP I OD1 1 
ATOM   5369  O  OD2 . ASP E  1 125 ? 21.930  -52.459 33.741  1.00 50.59  ? 125 ASP I OD2 1 
ATOM   5370  N  N   . LEU E  1 126 ? 20.714  -50.053 29.412  1.00 50.43  ? 126 LEU I N   1 
ATOM   5371  C  CA  . LEU E  1 126 ? 19.478  -49.806 28.649  1.00 50.58  ? 126 LEU I CA  1 
ATOM   5372  C  C   . LEU E  1 126 ? 18.236  -50.460 29.272  1.00 50.48  ? 126 LEU I C   1 
ATOM   5373  O  O   . LEU E  1 126 ? 17.277  -50.784 28.570  1.00 51.54  ? 126 LEU I O   1 
ATOM   5374  C  CB  . LEU E  1 126 ? 19.656  -50.220 27.170  1.00 52.54  ? 126 LEU I CB  1 
ATOM   5375  C  CG  . LEU E  1 126 ? 20.925  -49.717 26.461  1.00 53.23  ? 126 LEU I CG  1 
ATOM   5376  C  CD1 . LEU E  1 126 ? 20.869  -50.035 24.974  1.00 55.37  ? 126 LEU I CD1 1 
ATOM   5377  C  CD2 . LEU E  1 126 ? 21.143  -48.222 26.665  1.00 51.79  ? 126 LEU I CD2 1 
ATOM   5378  N  N   . GLY E  1 127 ? 18.254  -50.638 30.593  1.00 49.50  ? 127 GLY I N   1 
ATOM   5379  C  CA  . GLY E  1 127 ? 17.162  -51.303 31.301  1.00 49.68  ? 127 GLY I CA  1 
ATOM   5380  C  C   . GLY E  1 127 ? 17.078  -52.805 31.097  1.00 51.50  ? 127 GLY I C   1 
ATOM   5381  O  O   . GLY E  1 127 ? 16.061  -53.409 31.427  1.00 52.19  ? 127 GLY I O   1 
ATOM   5382  N  N   . LYS E  1 128 ? 18.150  -53.414 30.588  1.00 52.51  ? 128 LYS I N   1 
ATOM   5383  C  CA  . LYS E  1 128 ? 18.171  -54.848 30.273  1.00 54.55  ? 128 LYS I CA  1 
ATOM   5384  C  C   . LYS E  1 128 ? 19.156  -55.608 31.171  1.00 54.91  ? 128 LYS I C   1 
ATOM   5385  O  O   . LYS E  1 128 ? 19.534  -56.737 30.857  1.00 56.77  ? 128 LYS I O   1 
ATOM   5386  C  CB  . LYS E  1 128 ? 18.519  -55.047 28.789  1.00 56.12  ? 128 LYS I CB  1 
ATOM   5387  C  CG  . LYS E  1 128 ? 17.599  -54.292 27.829  1.00 56.14  ? 128 LYS I CG  1 
ATOM   5388  C  CD  . LYS E  1 128 ? 17.952  -54.562 26.372  1.00 58.08  ? 128 LYS I CD  1 
ATOM   5389  C  CE  . LYS E  1 128 ? 16.803  -54.226 25.429  1.00 58.96  ? 128 LYS I CE  1 
ATOM   5390  N  NZ  . LYS E  1 128 ? 16.359  -52.805 25.520  1.00 57.25  ? 128 LYS I NZ  1 
ATOM   5391  N  N   . GLY E  1 129 ? 19.548  -54.996 32.293  1.00 53.38  ? 129 GLY I N   1 
ATOM   5392  C  CA  . GLY E  1 129 ? 20.525  -55.573 33.212  1.00 53.85  ? 129 GLY I CA  1 
ATOM   5393  C  C   . GLY E  1 129 ? 19.988  -56.658 34.130  1.00 54.79  ? 129 GLY I C   1 
ATOM   5394  O  O   . GLY E  1 129 ? 20.774  -57.372 34.753  1.00 55.83  ? 129 GLY I O   1 
ATOM   5395  N  N   . GLY E  1 130 ? 18.662  -56.771 34.232  1.00 54.71  ? 130 GLY I N   1 
ATOM   5396  C  CA  . GLY E  1 130 ? 18.023  -57.826 35.027  1.00 55.99  ? 130 GLY I CA  1 
ATOM   5397  C  C   . GLY E  1 130 ? 18.069  -57.612 36.535  1.00 55.29  ? 130 GLY I C   1 
ATOM   5398  O  O   . GLY E  1 130 ? 18.220  -58.569 37.297  1.00 56.68  ? 130 GLY I O   1 
ATOM   5399  N  N   . ASN E  1 131 ? 17.946  -56.356 36.960  1.00 53.34  ? 131 ASN I N   1 
ATOM   5400  C  CA  . ASN E  1 131 ? 17.824  -56.011 38.381  1.00 52.75  ? 131 ASN I CA  1 
ATOM   5401  C  C   . ASN E  1 131 ? 17.002  -54.724 38.550  1.00 51.00  ? 131 ASN I C   1 
ATOM   5402  O  O   . ASN E  1 131 ? 16.653  -54.074 37.561  1.00 50.19  ? 131 ASN I O   1 
ATOM   5403  C  CB  . ASN E  1 131 ? 19.209  -55.917 39.055  1.00 52.73  ? 131 ASN I CB  1 
ATOM   5404  C  CG  . ASN E  1 131 ? 20.133  -54.886 38.409  1.00 51.46  ? 131 ASN I CG  1 
ATOM   5405  O  OD1 . ASN E  1 131 ? 19.741  -53.756 38.127  1.00 49.85  ? 131 ASN I OD1 1 
ATOM   5406  N  ND2 . ASN E  1 131 ? 21.384  -55.277 38.199  1.00 52.42  ? 131 ASN I ND2 1 
ATOM   5407  N  N   . GLU E  1 132 ? 16.692  -54.369 39.795  1.00 50.66  ? 132 GLU I N   1 
ATOM   5408  C  CA  . GLU E  1 132 ? 15.842  -53.209 40.079  1.00 49.40  ? 132 GLU I CA  1 
ATOM   5409  C  C   . GLU E  1 132 ? 16.492  -51.886 39.685  1.00 47.60  ? 132 GLU I C   1 
ATOM   5410  O  O   . GLU E  1 132 ? 15.816  -51.010 39.136  1.00 46.69  ? 132 GLU I O   1 
ATOM   5411  C  CB  . GLU E  1 132 ? 15.431  -53.173 41.559  1.00 49.82  ? 132 GLU I CB  1 
ATOM   5412  C  CG  . GLU E  1 132 ? 14.380  -52.116 41.911  1.00 49.03  ? 132 GLU I CG  1 
ATOM   5413  C  CD  . GLU E  1 132 ? 13.092  -52.247 41.105  1.00 49.64  ? 132 GLU I CD  1 
ATOM   5414  O  OE1 . GLU E  1 132 ? 12.751  -53.374 40.695  1.00 51.18  ? 132 GLU I OE1 1 
ATOM   5415  O  OE2 . GLU E  1 132 ? 12.420  -51.220 40.878  1.00 48.84  ? 132 GLU I OE2 1 
ATOM   5416  N  N   . GLU E  1 133 ? 17.790  -51.741 39.959  1.00 47.36  ? 133 GLU I N   1 
ATOM   5417  C  CA  . GLU E  1 133 ? 18.522  -50.531 39.554  1.00 46.06  ? 133 GLU I CA  1 
ATOM   5418  C  C   . GLU E  1 133 ? 18.551  -50.332 38.043  1.00 45.79  ? 133 GLU I C   1 
ATOM   5419  O  O   . GLU E  1 133 ? 18.563  -49.192 37.593  1.00 44.67  ? 133 GLU I O   1 
ATOM   5420  C  CB  . GLU E  1 133 ? 19.966  -50.508 40.090  1.00 46.41  ? 133 GLU I CB  1 
ATOM   5421  C  CG  . GLU E  1 133 ? 20.108  -50.077 41.544  1.00 46.35  ? 133 GLU I CG  1 
ATOM   5422  C  CD  . GLU E  1 133 ? 19.563  -48.686 41.834  1.00 44.95  ? 133 GLU I CD  1 
ATOM   5423  O  OE1 . GLU E  1 133 ? 19.604  -47.798 40.949  1.00 43.99  ? 133 GLU I OE1 1 
ATOM   5424  O  OE2 . GLU E  1 133 ? 19.089  -48.482 42.969  1.00 45.12  ? 133 GLU I OE2 1 
ATOM   5425  N  N   . SER E  1 134 ? 18.556  -51.425 37.273  1.00 47.01  ? 134 SER I N   1 
ATOM   5426  C  CA  . SER E  1 134 ? 18.514  -51.337 35.810  1.00 47.20  ? 134 SER I CA  1 
ATOM   5427  C  C   . SER E  1 134 ? 17.265  -50.605 35.302  1.00 46.59  ? 134 SER I C   1 
ATOM   5428  O  O   . SER E  1 134 ? 17.354  -49.804 34.371  1.00 46.13  ? 134 SER I O   1 
ATOM   5429  C  CB  . SER E  1 134 ? 18.599  -52.727 35.174  1.00 48.98  ? 134 SER I CB  1 
ATOM   5430  O  OG  . SER E  1 134 ? 18.718  -52.637 33.766  1.00 49.41  ? 134 SER I OG  1 
ATOM   5431  N  N   . THR E  1 135 ? 16.120  -50.854 35.938  1.00 46.86  ? 135 THR I N   1 
ATOM   5432  C  CA  . THR E  1 135 ? 14.863  -50.179 35.576  1.00 46.68  ? 135 THR I CA  1 
ATOM   5433  C  C   . THR E  1 135 ? 14.797  -48.703 36.018  1.00 45.17  ? 135 THR I C   1 
ATOM   5434  O  O   . THR E  1 135 ? 13.873  -47.998 35.621  1.00 45.07  ? 135 THR I O   1 
ATOM   5435  C  CB  . THR E  1 135 ? 13.613  -50.916 36.129  1.00 47.87  ? 135 THR I CB  1 
ATOM   5436  O  OG1 . THR E  1 135 ? 13.562  -50.809 37.558  1.00 47.52  ? 135 THR I OG1 1 
ATOM   5437  C  CG2 . THR E  1 135 ? 13.615  -52.384 35.728  1.00 49.64  ? 135 THR I CG2 1 
ATOM   5438  N  N   . LYS E  1 136 ? 15.758  -48.246 36.823  1.00 44.31  ? 136 LYS I N   1 
ATOM   5439  C  CA  . LYS E  1 136 ? 15.803  -46.871 37.333  1.00 43.12  ? 136 LYS I CA  1 
ATOM   5440  C  C   . LYS E  1 136 ? 16.927  -46.023 36.728  1.00 42.44  ? 136 LYS I C   1 
ATOM   5441  O  O   . LYS E  1 136 ? 16.678  -44.921 36.235  1.00 41.86  ? 136 LYS I O   1 
ATOM   5442  C  CB  . LYS E  1 136 ? 15.958  -46.900 38.855  1.00 43.00  ? 136 LYS I CB  1 
ATOM   5443  C  CG  . LYS E  1 136 ? 14.794  -47.567 39.569  1.00 43.94  ? 136 LYS I CG  1 
ATOM   5444  C  CD  . LYS E  1 136 ? 14.920  -47.469 41.085  1.00 44.01  ? 136 LYS I CD  1 
ATOM   5445  C  CE  . LYS E  1 136 ? 13.753  -48.151 41.782  1.00 45.30  ? 136 LYS I CE  1 
ATOM   5446  N  NZ  . LYS E  1 136 ? 12.436  -47.610 41.349  1.00 45.47  ? 136 LYS I NZ  1 
ATOM   5447  N  N   . THR E  1 137 ? 18.156  -46.537 36.790  1.00 42.84  ? 137 THR I N   1 
ATOM   5448  C  CA  . THR E  1 137 ? 19.364  -45.806 36.362  1.00 42.60  ? 137 THR I CA  1 
ATOM   5449  C  C   . THR E  1 137 ? 20.148  -46.448 35.211  1.00 43.62  ? 137 THR I C   1 
ATOM   5450  O  O   . THR E  1 137 ? 21.017  -45.807 34.633  1.00 43.69  ? 137 THR I O   1 
ATOM   5451  C  CB  . THR E  1 137 ? 20.352  -45.660 37.544  1.00 42.56  ? 137 THR I CB  1 
ATOM   5452  O  OG1 . THR E  1 137 ? 20.769  -46.960 37.992  1.00 43.60  ? 137 THR I OG1 1 
ATOM   5453  C  CG2 . THR E  1 137 ? 19.706  -44.893 38.703  1.00 41.80  ? 137 THR I CG2 1 
ATOM   5454  N  N   . GLY E  1 138 ? 19.871  -47.710 34.898  1.00 44.71  ? 138 GLY I N   1 
ATOM   5455  C  CA  . GLY E  1 138 ? 20.676  -48.463 33.938  1.00 46.06  ? 138 GLY I CA  1 
ATOM   5456  C  C   . GLY E  1 138 ? 22.088  -48.856 34.383  1.00 46.86  ? 138 GLY I C   1 
ATOM   5457  O  O   . GLY E  1 138 ? 22.904  -49.236 33.540  1.00 48.08  ? 138 GLY I O   1 
ATOM   5458  N  N   . ASN E  1 139 ? 22.379  -48.775 35.686  1.00 46.54  ? 139 ASN I N   1 
ATOM   5459  C  CA  . ASN E  1 139 ? 23.669  -49.212 36.266  1.00 47.68  ? 139 ASN I CA  1 
ATOM   5460  C  C   . ASN E  1 139 ? 24.929  -48.573 35.640  1.00 48.28  ? 139 ASN I C   1 
ATOM   5461  O  O   . ASN E  1 139 ? 25.964  -49.216 35.506  1.00 49.88  ? 139 ASN I O   1 
ATOM   5462  C  CB  . ASN E  1 139 ? 23.755  -50.748 36.238  1.00 49.29  ? 139 ASN I CB  1 
ATOM   5463  C  CG  . ASN E  1 139 ? 22.722  -51.399 37.133  1.00 49.19  ? 139 ASN I CG  1 
ATOM   5464  O  OD1 . ASN E  1 139 ? 22.730  -51.201 38.351  1.00 49.01  ? 139 ASN I OD1 1 
ATOM   5465  N  ND2 . ASN E  1 139 ? 21.826  -52.173 36.540  1.00 49.66  ? 139 ASN I ND2 1 
ATOM   5466  N  N   . ALA E  1 140 ? 24.840  -47.290 35.298  1.00 47.28  ? 140 ALA I N   1 
ATOM   5467  C  CA  . ALA E  1 140 ? 25.943  -46.576 34.638  1.00 48.06  ? 140 ALA I CA  1 
ATOM   5468  C  C   . ALA E  1 140 ? 27.039  -46.065 35.591  1.00 48.60  ? 140 ALA I C   1 
ATOM   5469  O  O   . ALA E  1 140 ? 27.975  -45.398 35.141  1.00 49.46  ? 140 ALA I O   1 
ATOM   5470  C  CB  . ALA E  1 140 ? 25.396  -45.427 33.804  1.00 47.10  ? 140 ALA I CB  1 
ATOM   5471  N  N   . GLY E  1 141 ? 26.938  -46.379 36.887  1.00 48.43  ? 141 GLY I N   1 
ATOM   5472  C  CA  . GLY E  1 141 ? 27.956  -45.998 37.864  1.00 49.27  ? 141 GLY I CA  1 
ATOM   5473  C  C   . GLY E  1 141 ? 27.850  -44.527 38.218  1.00 48.16  ? 141 GLY I C   1 
ATOM   5474  O  O   . GLY E  1 141 ? 26.799  -43.905 38.031  1.00 46.54  ? 141 GLY I O   1 
ATOM   5475  N  N   . SER E  1 142 ? 28.953  -43.968 38.706  1.00 49.31  ? 142 SER I N   1 
ATOM   5476  C  CA  . SER E  1 142 ? 28.969  -42.591 39.199  1.00 48.63  ? 142 SER I CA  1 
ATOM   5477  C  C   . SER E  1 142 ? 28.869  -41.549 38.083  1.00 48.02  ? 142 SER I C   1 
ATOM   5478  O  O   . SER E  1 142 ? 29.107  -41.835 36.907  1.00 48.62  ? 142 SER I O   1 
ATOM   5479  C  CB  . SER E  1 142 ? 30.234  -42.338 40.023  1.00 50.52  ? 142 SER I CB  1 
ATOM   5480  O  OG  . SER E  1 142 ? 31.392  -42.475 39.222  1.00 52.47  ? 142 SER I OG  1 
ATOM   5481  N  N   . ARG E  1 143 ? 28.530  -40.333 38.490  1.00 47.04  ? 143 ARG I N   1 
ATOM   5482  C  CA  . ARG E  1 143 ? 28.333  -39.210 37.584  1.00 46.49  ? 143 ARG I CA  1 
ATOM   5483  C  C   . ARG E  1 143 ? 29.660  -38.454 37.482  1.00 48.19  ? 143 ARG I C   1 
ATOM   5484  O  O   . ARG E  1 143 ? 30.051  -37.759 38.421  1.00 48.61  ? 143 ARG I O   1 
ATOM   5485  C  CB  . ARG E  1 143 ? 27.213  -38.319 38.130  1.00 44.82  ? 143 ARG I CB  1 
ATOM   5486  C  CG  . ARG E  1 143 ? 25.928  -39.085 38.419  1.00 43.49  ? 143 ARG I CG  1 
ATOM   5487  C  CD  . ARG E  1 143 ? 24.846  -38.201 39.020  1.00 42.24  ? 143 ARG I CD  1 
ATOM   5488  N  NE  . ARG E  1 143 ? 23.703  -38.997 39.462  1.00 41.44  ? 143 ARG I NE  1 
ATOM   5489  C  CZ  . ARG E  1 143 ? 22.560  -38.508 39.947  1.00 40.55  ? 143 ARG I CZ  1 
ATOM   5490  N  NH1 . ARG E  1 143 ? 22.361  -37.194 40.065  1.00 40.20  ? 143 ARG I NH1 1 
ATOM   5491  N  NH2 . ARG E  1 143 ? 21.596  -39.351 40.314  1.00 40.23  ? 143 ARG I NH2 1 
ATOM   5492  N  N   . LEU E  1 144 ? 30.369  -38.627 36.364  1.00 49.47  ? 144 LEU I N   1 
ATOM   5493  C  CA  . LEU E  1 144 ? 31.722  -38.074 36.211  1.00 51.67  ? 144 LEU I CA  1 
ATOM   5494  C  C   . LEU E  1 144 ? 31.714  -36.566 35.970  1.00 51.58  ? 144 LEU I C   1 
ATOM   5495  O  O   . LEU E  1 144 ? 32.482  -35.841 36.601  1.00 52.78  ? 144 LEU I O   1 
ATOM   5496  C  CB  . LEU E  1 144 ? 32.492  -38.780 35.086  1.00 53.53  ? 144 LEU I CB  1 
ATOM   5497  C  CG  . LEU E  1 144 ? 32.825  -40.271 35.259  1.00 54.41  ? 144 LEU I CG  1 
ATOM   5498  C  CD1 . LEU E  1 144 ? 33.714  -40.728 34.112  1.00 56.73  ? 144 LEU I CD1 1 
ATOM   5499  C  CD2 . LEU E  1 144 ? 33.495  -40.581 36.593  1.00 55.41  ? 144 LEU I CD2 1 
ATOM   5500  N  N   . ALA E  1 145 ? 30.854  -36.110 35.059  1.00 50.37  ? 145 ALA I N   1 
ATOM   5501  C  CA  . ALA E  1 145 ? 30.701  -34.684 34.763  1.00 50.32  ? 145 ALA I CA  1 
ATOM   5502  C  C   . ALA E  1 145 ? 29.250  -34.327 34.465  1.00 48.21  ? 145 ALA I C   1 
ATOM   5503  O  O   . ALA E  1 145 ? 28.480  -35.157 33.975  1.00 47.24  ? 145 ALA I O   1 
ATOM   5504  C  CB  . ALA E  1 145 ? 31.583  -34.291 33.591  1.00 52.48  ? 145 ALA I CB  1 
ATOM   5505  N  N   . ALA E  1 146 ? 28.895  -33.079 34.759  1.00 47.75  ? 146 ALA I N   1 
ATOM   5506  C  CA  . ALA E  1 146 ? 27.538  -32.589 34.562  1.00 46.11  ? 146 ALA I CA  1 
ATOM   5507  C  C   . ALA E  1 146 ? 27.477  -31.068 34.418  1.00 46.56  ? 146 ALA I C   1 
ATOM   5508  O  O   . ALA E  1 146 ? 28.423  -30.354 34.762  1.00 47.90  ? 146 ALA I O   1 
ATOM   5509  C  CB  . ALA E  1 146 ? 26.651  -33.038 35.715  1.00 44.44  ? 146 ALA I CB  1 
ATOM   5510  N  N   . GLY E  1 147 ? 26.347  -30.590 33.907  1.00 45.64  ? 147 GLY I N   1 
ATOM   5511  C  CA  . GLY E  1 147 ? 26.074  -29.156 33.821  1.00 46.03  ? 147 GLY I CA  1 
ATOM   5512  C  C   . GLY E  1 147 ? 24.616  -28.871 33.506  1.00 44.90  ? 147 GLY I C   1 
ATOM   5513  O  O   . GLY E  1 147 ? 23.902  -29.738 32.992  1.00 44.20  ? 147 GLY I O   1 
ATOM   5514  N  N   . VAL E  1 148 ? 24.182  -27.649 33.799  1.00 44.99  ? 148 VAL I N   1 
ATOM   5515  C  CA  . VAL E  1 148 ? 22.805  -27.240 33.544  1.00 44.32  ? 148 VAL I CA  1 
ATOM   5516  C  C   . VAL E  1 148 ? 22.657  -26.893 32.060  1.00 45.44  ? 148 VAL I C   1 
ATOM   5517  O  O   . VAL E  1 148 ? 23.522  -26.242 31.485  1.00 46.97  ? 148 VAL I O   1 
ATOM   5518  C  CB  . VAL E  1 148 ? 22.389  -26.040 34.424  1.00 44.32  ? 148 VAL I CB  1 
ATOM   5519  C  CG1 . VAL E  1 148 ? 20.936  -25.659 34.161  1.00 43.96  ? 148 VAL I CG1 1 
ATOM   5520  C  CG2 . VAL E  1 148 ? 22.589  -26.363 35.900  1.00 43.54  ? 148 VAL I CG2 1 
ATOM   5521  N  N   . ILE E  1 149 ? 21.558  -27.339 31.454  1.00 44.97  ? 149 ILE I N   1 
ATOM   5522  C  CA  . ILE E  1 149 ? 21.257  -27.058 30.050  1.00 46.27  ? 149 ILE I CA  1 
ATOM   5523  C  C   . ILE E  1 149 ? 20.668  -25.652 29.963  1.00 47.06  ? 149 ILE I C   1 
ATOM   5524  O  O   . ILE E  1 149 ? 19.622  -25.387 30.550  1.00 46.29  ? 149 ILE I O   1 
ATOM   5525  C  CB  . ILE E  1 149 ? 20.265  -28.091 29.462  1.00 45.81  ? 149 ILE I CB  1 
ATOM   5526  C  CG1 . ILE E  1 149 ? 20.878  -29.500 29.503  1.00 45.28  ? 149 ILE I CG1 1 
ATOM   5527  C  CG2 . ILE E  1 149 ? 19.875  -27.712 28.033  1.00 47.49  ? 149 ILE I CG2 1 
ATOM   5528  C  CD1 . ILE E  1 149 ? 19.868  -30.623 29.396  1.00 44.54  ? 149 ILE I CD1 1 
ATOM   5529  N  N   . GLY E  1 150 ? 21.339  -24.763 29.234  1.00 48.85  ? 150 GLY I N   1 
ATOM   5530  C  CA  . GLY E  1 150 ? 20.940  -23.354 29.150  1.00 50.01  ? 150 GLY I CA  1 
ATOM   5531  C  C   . GLY E  1 150 ? 20.687  -22.894 27.730  1.00 52.00  ? 150 GLY I C   1 
ATOM   5532  O  O   . GLY E  1 150 ? 21.222  -23.470 26.783  1.00 52.89  ? 150 GLY I O   1 
ATOM   5533  N  N   . ILE E  1 151 ? 19.889  -21.834 27.592  1.00 52.94  ? 151 ILE I N   1 
ATOM   5534  C  CA  . ILE E  1 151 ? 19.436  -21.352 26.285  1.00 55.05  ? 151 ILE I CA  1 
ATOM   5535  C  C   . ILE E  1 151 ? 20.624  -20.698 25.589  1.00 57.17  ? 151 ILE I C   1 
ATOM   5536  O  O   . ILE E  1 151 ? 21.422  -20.016 26.233  1.00 57.39  ? 151 ILE I O   1 
ATOM   5537  C  CB  . ILE E  1 151 ? 18.270  -20.331 26.402  1.00 55.80  ? 151 ILE I CB  1 
ATOM   5538  C  CG1 . ILE E  1 151 ? 17.065  -20.954 27.129  1.00 54.09  ? 151 ILE I CG1 1 
ATOM   5539  C  CG2 . ILE E  1 151 ? 17.838  -19.839 25.020  1.00 58.32  ? 151 ILE I CG2 1 
ATOM   5540  C  CD1 . ILE E  1 151 ? 16.028  -19.956 27.607  1.00 54.68  ? 151 ILE I CD1 1 
ATOM   5541  N  N   . ALA E  1 152 ? 20.737  -20.923 24.282  1.00 58.98  ? 152 ALA I N   1 
ATOM   5542  C  CA  . ALA E  1 152 ? 21.858  -20.425 23.486  1.00 61.44  ? 152 ALA I CA  1 
ATOM   5543  C  C   . ALA E  1 152 ? 21.349  -19.565 22.343  1.00 64.17  ? 152 ALA I C   1 
ATOM   5544  O  O   . ALA E  1 152 ? 20.182  -19.655 21.954  1.00 64.29  ? 152 ALA I O   1 
ATOM   5545  C  CB  . ALA E  1 152 ? 22.668  -21.592 22.941  1.00 61.54  ? 152 ALA I CB  1 
ATOM   5546  N  N   . GLN E  1 153 ? 22.230  -18.724 21.813  1.00 66.73  ? 153 GLN I N   1 
ATOM   5547  C  CA  . GLN E  1 153 ? 21.918  -17.948 20.612  1.00 69.87  ? 153 GLN I CA  1 
ATOM   5548  C  C   . GLN E  1 153 ? 22.055  -18.847 19.386  1.00 71.24  ? 153 GLN I C   1 
ATOM   5549  O  O   . GLN E  1 153 ? 21.078  -19.092 18.683  1.00 71.95  ? 153 GLN I O   1 
ATOM   5550  C  CB  . GLN E  1 153 ? 22.839  -16.736 20.477  1.00 72.41  ? 153 GLN I CB  1 
ATOM   5551  C  CG  . GLN E  1 153 ? 22.404  -15.763 19.395  1.00 75.73  ? 153 GLN I CG  1 
ATOM   5552  C  CD  . GLN E  1 153 ? 23.186  -14.471 19.433  1.00 78.22  ? 153 GLN I CD  1 
ATOM   5553  O  OE1 . GLN E  1 153 ? 24.412  -14.478 19.532  1.00 79.02  ? 153 GLN I OE1 1 
ATOM   5554  N  NE2 . GLN E  1 153 ? 22.481  -13.349 19.350  1.00 79.73  ? 153 GLN I NE2 1 
ATOM   5555  N  N   . ALA F  1 1   ? 4.553   -23.123 43.279  1.00 45.07  ? 1   ALA K N   1 
ATOM   5556  C  CA  . ALA F  1 1   ? 5.587   -23.835 44.089  1.00 44.80  ? 1   ALA K CA  1 
ATOM   5557  C  C   . ALA F  1 1   ? 6.768   -24.278 43.210  1.00 43.96  ? 1   ALA K C   1 
ATOM   5558  O  O   . ALA F  1 1   ? 7.371   -25.328 43.453  1.00 44.83  ? 1   ALA K O   1 
ATOM   5559  C  CB  . ALA F  1 1   ? 4.960   -25.031 44.807  1.00 47.04  ? 1   ALA K CB  1 
ATOM   5560  N  N   . THR F  1 2   ? 7.092   -23.468 42.199  1.00 42.50  ? 2   THR K N   1 
ATOM   5561  C  CA  . THR F  1 2   ? 8.235   -23.711 41.336  1.00 41.74  ? 2   THR K CA  1 
ATOM   5562  C  C   . THR F  1 2   ? 9.458   -23.155 42.061  1.00 40.00  ? 2   THR K C   1 
ATOM   5563  O  O   . THR F  1 2   ? 9.417   -22.054 42.630  1.00 38.80  ? 2   THR K O   1 
ATOM   5564  C  CB  . THR F  1 2   ? 8.075   -23.036 39.958  1.00 41.44  ? 2   THR K CB  1 
ATOM   5565  O  OG1 . THR F  1 2   ? 6.718   -23.149 39.522  1.00 42.84  ? 2   THR K OG1 1 
ATOM   5566  C  CG2 . THR F  1 2   ? 8.973   -23.690 38.920  1.00 41.98  ? 2   THR K CG2 1 
ATOM   5567  N  N   . LYS F  1 3   ? 10.527  -23.940 42.069  1.00 39.99  ? 3   LYS K N   1 
ATOM   5568  C  CA  . LYS F  1 3   ? 11.788  -23.525 42.658  1.00 38.76  ? 3   LYS K CA  1 
ATOM   5569  C  C   . LYS F  1 3   ? 12.867  -23.574 41.592  1.00 38.40  ? 3   LYS K C   1 
ATOM   5570  O  O   . LYS F  1 3   ? 12.804  -24.381 40.657  1.00 39.39  ? 3   LYS K O   1 
ATOM   5571  C  CB  . LYS F  1 3   ? 12.162  -24.425 43.843  1.00 39.64  ? 3   LYS K CB  1 
ATOM   5572  C  CG  . LYS F  1 3   ? 11.148  -24.389 44.975  1.00 40.22  ? 3   LYS K CG  1 
ATOM   5573  C  CD  . LYS F  1 3   ? 11.608  -25.160 46.208  1.00 41.27  ? 3   LYS K CD  1 
ATOM   5574  C  CE  . LYS F  1 3   ? 10.429  -25.530 47.106  1.00 42.69  ? 3   LYS K CE  1 
ATOM   5575  N  NZ  . LYS F  1 3   ? 10.807  -25.701 48.544  1.00 43.44  ? 3   LYS K NZ  1 
ATOM   5576  N  N   . ALA F  1 4   ? 13.846  -22.688 41.733  1.00 37.10  ? 4   ALA K N   1 
ATOM   5577  C  CA  . ALA F  1 4   ? 15.044  -22.721 40.908  1.00 37.14  ? 4   ALA K CA  1 
ATOM   5578  C  C   . ALA F  1 4   ? 16.288  -22.421 41.740  1.00 36.61  ? 4   ALA K C   1 
ATOM   5579  O  O   . ALA F  1 4   ? 16.199  -21.906 42.858  1.00 35.82  ? 4   ALA K O   1 
ATOM   5580  C  CB  . ALA F  1 4   ? 14.910  -21.755 39.741  1.00 36.51  ? 4   ALA K CB  1 
ATOM   5581  N  N   . VAL F  1 5   ? 17.445  -22.760 41.184  1.00 37.23  ? 5   VAL K N   1 
ATOM   5582  C  CA  . VAL F  1 5   ? 18.715  -22.571 41.871  1.00 37.26  ? 5   VAL K CA  1 
ATOM   5583  C  C   . VAL F  1 5   ? 19.826  -22.257 40.864  1.00 37.70  ? 5   VAL K C   1 
ATOM   5584  O  O   . VAL F  1 5   ? 19.782  -22.700 39.711  1.00 38.54  ? 5   VAL K O   1 
ATOM   5585  C  CB  . VAL F  1 5   ? 19.062  -23.804 42.740  1.00 38.52  ? 5   VAL K CB  1 
ATOM   5586  C  CG1 . VAL F  1 5   ? 19.385  -25.020 41.882  1.00 40.16  ? 5   VAL K CG1 1 
ATOM   5587  C  CG2 . VAL F  1 5   ? 20.199  -23.501 43.708  1.00 38.60  ? 5   VAL K CG2 1 
ATOM   5588  N  N   . CYS F  1 6   ? 20.802  -21.472 41.308  1.00 37.34  ? 6   CYS K N   1 
ATOM   5589  C  CA  . CYS F  1 6   ? 21.941  -21.099 40.474  1.00 38.06  ? 6   CYS K CA  1 
ATOM   5590  C  C   . CYS F  1 6   ? 23.219  -21.125 41.302  1.00 38.75  ? 6   CYS K C   1 
ATOM   5591  O  O   . CYS F  1 6   ? 23.262  -20.529 42.382  1.00 37.87  ? 6   CYS K O   1 
ATOM   5592  C  CB  . CYS F  1 6   ? 21.719  -19.708 39.886  1.00 36.95  ? 6   CYS K CB  1 
ATOM   5593  S  SG  . CYS F  1 6   ? 23.077  -19.111 38.860  1.00 38.12  ? 6   CYS K SG  1 
ATOM   5594  N  N   . VAL F  1 7   ? 24.230  -21.843 40.807  1.00 40.53  ? 7   VAL K N   1 
ATOM   5595  C  CA  . VAL F  1 7   ? 25.577  -21.833 41.387  1.00 41.70  ? 7   VAL K CA  1 
ATOM   5596  C  C   . VAL F  1 7   ? 26.382  -20.761 40.655  1.00 41.96  ? 7   VAL K C   1 
ATOM   5597  O  O   . VAL F  1 7   ? 26.659  -20.893 39.461  1.00 42.98  ? 7   VAL K O   1 
ATOM   5598  C  CB  . VAL F  1 7   ? 26.296  -23.202 41.248  1.00 43.91  ? 7   VAL K CB  1 
ATOM   5599  C  CG1 . VAL F  1 7   ? 27.611  -23.206 42.022  1.00 45.19  ? 7   VAL K CG1 1 
ATOM   5600  C  CG2 . VAL F  1 7   ? 25.403  -24.339 41.728  1.00 43.98  ? 7   VAL K CG2 1 
ATOM   5601  N  N   . LEU F  1 8   ? 26.731  -19.690 41.363  1.00 41.26  ? 8   LEU K N   1 
ATOM   5602  C  CA  . LEU F  1 8   ? 27.590  -18.644 40.816  1.00 41.76  ? 8   LEU K CA  1 
ATOM   5603  C  C   . LEU F  1 8   ? 29.054  -19.043 40.978  1.00 44.06  ? 8   LEU K C   1 
ATOM   5604  O  O   . LEU F  1 8   ? 29.484  -19.392 42.078  1.00 44.57  ? 8   LEU K O   1 
ATOM   5605  C  CB  . LEU F  1 8   ? 27.332  -17.310 41.517  1.00 40.23  ? 8   LEU K CB  1 
ATOM   5606  C  CG  . LEU F  1 8   ? 25.949  -16.703 41.270  1.00 38.31  ? 8   LEU K CG  1 
ATOM   5607  C  CD1 . LEU F  1 8   ? 25.685  -15.550 42.231  1.00 37.09  ? 8   LEU K CD1 1 
ATOM   5608  C  CD2 . LEU F  1 8   ? 25.816  -16.236 39.827  1.00 38.42  ? 8   LEU K CD2 1 
ATOM   5609  N  N   . LYS F  1 9   ? 29.799  -19.004 39.872  1.00 45.75  ? 9   LYS K N   1 
ATOM   5610  C  CA  . LYS F  1 9   ? 31.246  -19.257 39.860  1.00 48.33  ? 9   LYS K CA  1 
ATOM   5611  C  C   . LYS F  1 9   ? 31.935  -18.324 38.870  1.00 49.40  ? 9   LYS K C   1 
ATOM   5612  O  O   . LYS F  1 9   ? 31.342  -17.900 37.876  1.00 48.76  ? 9   LYS K O   1 
ATOM   5613  C  CB  . LYS F  1 9   ? 31.550  -20.697 39.454  1.00 50.38  ? 9   LYS K CB  1 
ATOM   5614  C  CG  . LYS F  1 9   ? 31.104  -21.746 40.453  1.00 50.11  ? 9   LYS K CG  1 
ATOM   5615  C  CD  . LYS F  1 9   ? 31.599  -23.125 40.045  1.00 52.59  ? 9   LYS K CD  1 
ATOM   5616  C  CE  . LYS F  1 9   ? 31.069  -24.217 40.965  1.00 52.41  ? 9   LYS K CE  1 
ATOM   5617  N  NZ  . LYS F  1 9   ? 31.786  -24.266 42.272  1.00 53.12  ? 9   LYS K NZ  1 
ATOM   5618  N  N   . GLY F  1 10  ? 33.194  -18.020 39.146  1.00 51.32  ? 10  GLY K N   1 
ATOM   5619  C  CA  . GLY F  1 10  ? 34.002  -17.200 38.253  1.00 52.95  ? 10  GLY K CA  1 
ATOM   5620  C  C   . GLY F  1 10  ? 35.428  -17.668 38.224  1.00 56.24  ? 10  GLY K C   1 
ATOM   5621  O  O   . GLY F  1 10  ? 35.758  -18.716 38.772  1.00 57.31  ? 10  GLY K O   1 
ATOM   5622  N  N   . ASP F  1 11  ? 36.265  -16.874 37.569  1.00 58.11  ? 11  ASP K N   1 
ATOM   5623  C  CA  . ASP F  1 11  ? 37.705  -17.101 37.518  1.00 61.62  ? 11  ASP K CA  1 
ATOM   5624  C  C   . ASP F  1 11  ? 38.398  -16.653 38.810  1.00 61.86  ? 11  ASP K C   1 
ATOM   5625  O  O   . ASP F  1 11  ? 39.462  -17.160 39.139  1.00 64.58  ? 11  ASP K O   1 
ATOM   5626  C  CB  . ASP F  1 11  ? 38.309  -16.359 36.320  1.00 63.81  ? 11  ASP K CB  1 
ATOM   5627  C  CG  . ASP F  1 11  ? 37.767  -16.857 34.986  1.00 64.36  ? 11  ASP K CG  1 
ATOM   5628  O  OD1 . ASP F  1 11  ? 37.706  -18.090 34.778  1.00 65.46  ? 11  ASP K OD1 1 
ATOM   5629  O  OD2 . ASP F  1 11  ? 37.415  -16.015 34.136  1.00 64.08  ? 11  ASP K OD2 1 
ATOM   5630  N  N   . GLY F  1 12  ? 37.800  -15.697 39.521  1.00 59.30  ? 12  GLY K N   1 
ATOM   5631  C  CA  . GLY F  1 12  ? 38.330  -15.194 40.788  1.00 59.48  ? 12  GLY K CA  1 
ATOM   5632  C  C   . GLY F  1 12  ? 37.632  -15.845 41.965  1.00 57.61  ? 12  GLY K C   1 
ATOM   5633  O  O   . GLY F  1 12  ? 37.050  -16.920 41.807  1.00 57.07  ? 12  GLY K O   1 
ATOM   5634  N  N   . PRO F  1 13  ? 37.640  -15.188 43.146  1.00 56.80  ? 13  PRO K N   1 
ATOM   5635  C  CA  . PRO F  1 13  ? 37.106  -15.796 44.361  1.00 55.60  ? 13  PRO K CA  1 
ATOM   5636  C  C   . PRO F  1 13  ? 35.588  -15.639 44.554  1.00 52.17  ? 13  PRO K C   1 
ATOM   5637  O  O   . PRO F  1 13  ? 35.057  -16.109 45.560  1.00 51.31  ? 13  PRO K O   1 
ATOM   5638  C  CB  . PRO F  1 13  ? 37.851  -15.033 45.457  1.00 56.82  ? 13  PRO K CB  1 
ATOM   5639  C  CG  . PRO F  1 13  ? 38.006  -13.657 44.892  1.00 56.62  ? 13  PRO K CG  1 
ATOM   5640  C  CD  . PRO F  1 13  ? 37.970  -13.771 43.386  1.00 56.82  ? 13  PRO K CD  1 
ATOM   5641  N  N   . VAL F  1 14  ? 34.889  -14.986 43.627  1.00 50.46  ? 14  VAL K N   1 
ATOM   5642  C  CA  . VAL F  1 14  ? 33.455  -14.765 43.803  1.00 47.49  ? 14  VAL K CA  1 
ATOM   5643  C  C   . VAL F  1 14  ? 32.691  -16.052 43.498  1.00 46.75  ? 14  VAL K C   1 
ATOM   5644  O  O   . VAL F  1 14  ? 32.758  -16.572 42.379  1.00 47.36  ? 14  VAL K O   1 
ATOM   5645  C  CB  . VAL F  1 14  ? 32.912  -13.605 42.944  1.00 46.11  ? 14  VAL K CB  1 
ATOM   5646  C  CG1 . VAL F  1 14  ? 31.416  -13.406 43.217  1.00 43.41  ? 14  VAL K CG1 1 
ATOM   5647  C  CG2 . VAL F  1 14  ? 33.679  -12.325 43.246  1.00 46.98  ? 14  VAL K CG2 1 
ATOM   5648  N  N   . GLN F  1 15  ? 31.984  -16.559 44.511  1.00 45.64  ? 15  GLN K N   1 
ATOM   5649  C  CA  . GLN F  1 15  ? 31.154  -17.756 44.361  1.00 45.00  ? 15  GLN K CA  1 
ATOM   5650  C  C   . GLN F  1 15  ? 29.965  -17.744 45.322  1.00 43.05  ? 15  GLN K C   1 
ATOM   5651  O  O   . GLN F  1 15  ? 30.011  -17.132 46.397  1.00 42.81  ? 15  GLN K O   1 
ATOM   5652  C  CB  . GLN F  1 15  ? 31.981  -19.035 44.548  1.00 47.32  ? 15  GLN K CB  1 
ATOM   5653  C  CG  . GLN F  1 15  ? 32.797  -19.081 45.833  1.00 48.81  ? 15  GLN K CG  1 
ATOM   5654  C  CD  . GLN F  1 15  ? 33.557  -20.389 46.036  1.00 51.24  ? 15  GLN K CD  1 
ATOM   5655  O  OE1 . GLN F  1 15  ? 33.131  -21.460 45.594  1.00 51.47  ? 15  GLN K OE1 1 
ATOM   5656  N  NE2 . GLN F  1 15  ? 34.683  -20.306 46.733  1.00 53.34  ? 15  GLN K NE2 1 
ATOM   5657  N  N   . GLY F  1 16  ? 28.902  -18.428 44.925  1.00 41.85  ? 16  GLY K N   1 
ATOM   5658  C  CA  . GLY F  1 16  ? 27.725  -18.514 45.767  1.00 40.34  ? 16  GLY K CA  1 
ATOM   5659  C  C   . GLY F  1 16  ? 26.617  -19.355 45.185  1.00 39.49  ? 16  GLY K C   1 
ATOM   5660  O  O   . GLY F  1 16  ? 26.734  -19.875 44.066  1.00 39.99  ? 16  GLY K O   1 
ATOM   5661  N  N   . ILE F  1 17  ? 25.554  -19.493 45.975  1.00 38.42  ? 17  ILE K N   1 
ATOM   5662  C  CA  . ILE F  1 17  ? 24.345  -20.218 45.586  1.00 37.68  ? 17  ILE K CA  1 
ATOM   5663  C  C   . ILE F  1 17  ? 23.164  -19.281 45.792  1.00 35.89  ? 17  ILE K C   1 
ATOM   5664  O  O   . ILE F  1 17  ? 22.995  -18.727 46.876  1.00 35.53  ? 17  ILE K O   1 
ATOM   5665  C  CB  . ILE F  1 17  ? 24.150  -21.503 46.418  1.00 38.76  ? 17  ILE K CB  1 
ATOM   5666  C  CG1 . ILE F  1 17  ? 25.313  -22.478 46.176  1.00 40.68  ? 17  ILE K CG1 1 
ATOM   5667  C  CG2 . ILE F  1 17  ? 22.823  -22.174 46.072  1.00 38.26  ? 17  ILE K CG2 1 
ATOM   5668  C  CD1 . ILE F  1 17  ? 25.376  -23.628 47.161  1.00 42.07  ? 17  ILE K CD1 1 
ATOM   5669  N  N   . ILE F  1 18  ? 22.370  -19.086 44.743  1.00 34.96  ? 18  ILE K N   1 
ATOM   5670  C  CA  . ILE F  1 18  ? 21.171  -18.263 44.819  1.00 33.56  ? 18  ILE K CA  1 
ATOM   5671  C  C   . ILE F  1 18  ? 19.946  -19.135 44.566  1.00 33.54  ? 18  ILE K C   1 
ATOM   5672  O  O   . ILE F  1 18  ? 19.908  -19.907 43.606  1.00 34.04  ? 18  ILE K O   1 
ATOM   5673  C  CB  . ILE F  1 18  ? 21.212  -17.084 43.820  1.00 32.72  ? 18  ILE K CB  1 
ATOM   5674  C  CG1 . ILE F  1 18  ? 22.410  -16.168 44.116  1.00 32.93  ? 18  ILE K CG1 1 
ATOM   5675  C  CG2 . ILE F  1 18  ? 19.909  -16.289 43.852  1.00 31.49  ? 18  ILE K CG2 1 
ATOM   5676  C  CD1 . ILE F  1 18  ? 22.396  -15.491 45.475  1.00 32.70  ? 18  ILE K CD1 1 
ATOM   5677  N  N   . ASN F  1 19  ? 18.962  -18.996 45.461  1.00 33.15  ? 19  ASN K N   1 
ATOM   5678  C  CA  . ASN F  1 19  ? 17.704  -19.713 45.406  1.00 33.35  ? 19  ASN K CA  1 
ATOM   5679  C  C   . ASN F  1 19  ? 16.621  -18.799 44.867  1.00 32.36  ? 19  ASN K C   1 
ATOM   5680  O  O   . ASN F  1 19  ? 16.624  -17.596 45.145  1.00 31.48  ? 19  ASN K O   1 
ATOM   5681  C  CB  . ASN F  1 19  ? 17.309  -20.178 46.808  1.00 34.06  ? 19  ASN K CB  1 
ATOM   5682  C  CG  . ASN F  1 19  ? 18.378  -21.021 47.459  1.00 35.24  ? 19  ASN K CG  1 
ATOM   5683  O  OD1 . ASN F  1 19  ? 18.606  -22.158 47.058  1.00 36.22  ? 19  ASN K OD1 1 
ATOM   5684  N  ND2 . ASN F  1 19  ? 19.039  -20.467 48.469  1.00 35.41  ? 19  ASN K ND2 1 
ATOM   5685  N  N   . PHE F  1 20  ? 15.705  -19.388 44.101  1.00 32.70  ? 20  PHE K N   1 
ATOM   5686  C  CA  . PHE F  1 20  ? 14.527  -18.712 43.573  1.00 32.17  ? 20  PHE K CA  1 
ATOM   5687  C  C   . PHE F  1 20  ? 13.289  -19.506 43.969  1.00 33.06  ? 20  PHE K C   1 
ATOM   5688  O  O   . PHE F  1 20  ? 13.284  -20.728 43.837  1.00 34.05  ? 20  PHE K O   1 
ATOM   5689  C  CB  . PHE F  1 20  ? 14.565  -18.689 42.057  1.00 32.20  ? 20  PHE K CB  1 
ATOM   5690  C  CG  . PHE F  1 20  ? 15.752  -17.987 41.480  1.00 31.77  ? 20  PHE K CG  1 
ATOM   5691  C  CD1 . PHE F  1 20  ? 16.946  -18.665 41.287  1.00 32.50  ? 20  PHE K CD1 1 
ATOM   5692  C  CD2 . PHE F  1 20  ? 15.666  -16.655 41.100  1.00 30.90  ? 20  PHE K CD2 1 
ATOM   5693  C  CE1 . PHE F  1 20  ? 18.040  -18.017 40.734  1.00 32.44  ? 20  PHE K CE1 1 
ATOM   5694  C  CE2 . PHE F  1 20  ? 16.753  -16.003 40.541  1.00 30.77  ? 20  PHE K CE2 1 
ATOM   5695  C  CZ  . PHE F  1 20  ? 17.943  -16.684 40.361  1.00 31.56  ? 20  PHE K CZ  1 
ATOM   5696  N  N   . GLU F  1 21  ? 12.234  -18.822 44.410  1.00 32.92  ? 21  GLU K N   1 
ATOM   5697  C  CA  . GLU F  1 21  ? 10.943  -19.482 44.656  1.00 34.10  ? 21  GLU K CA  1 
ATOM   5698  C  C   . GLU F  1 21  ? 9.752   -18.621 44.250  1.00 33.93  ? 21  GLU K C   1 
ATOM   5699  O  O   . GLU F  1 21  ? 9.704   -17.431 44.534  1.00 33.06  ? 21  GLU K O   1 
ATOM   5700  C  CB  . GLU F  1 21  ? 10.799  -19.884 46.120  1.00 35.00  ? 21  GLU K CB  1 
ATOM   5701  C  CG  . GLU F  1 21  ? 9.570   -20.745 46.393  1.00 36.63  ? 21  GLU K CG  1 
ATOM   5702  C  CD  . GLU F  1 21  ? 9.580   -21.352 47.772  1.00 37.93  ? 21  GLU K CD  1 
ATOM   5703  O  OE1 . GLU F  1 21  ? 10.060  -20.690 48.718  1.00 37.70  ? 21  GLU K OE1 1 
ATOM   5704  O  OE2 . GLU F  1 21  ? 9.115   -22.499 47.920  1.00 39.51  ? 21  GLU K OE2 1 
ATOM   5705  N  N   . GLN F  1 22  ? 8.777   -19.262 43.617  1.00 35.02  ? 22  GLN K N   1 
ATOM   5706  C  CA  . GLN F  1 22  ? 7.570   -18.591 43.143  1.00 35.38  ? 22  GLN K CA  1 
ATOM   5707  C  C   . GLN F  1 22  ? 6.397   -19.487 43.502  1.00 37.29  ? 22  GLN K C   1 
ATOM   5708  O  O   . GLN F  1 22  ? 6.210   -20.531 42.892  1.00 38.29  ? 22  GLN K O   1 
ATOM   5709  C  CB  . GLN F  1 22  ? 7.661   -18.345 41.630  1.00 35.00  ? 22  GLN K CB  1 
ATOM   5710  C  CG  . GLN F  1 22  ? 6.458   -17.629 41.032  1.00 35.41  ? 22  GLN K CG  1 
ATOM   5711  C  CD  . GLN F  1 22  ? 6.660   -17.251 39.578  1.00 35.15  ? 22  GLN K CD  1 
ATOM   5712  O  OE1 . GLN F  1 22  ? 7.224   -18.022 38.802  1.00 35.42  ? 22  GLN K OE1 1 
ATOM   5713  N  NE2 . GLN F  1 22  ? 6.189   -16.062 39.199  1.00 34.74  ? 22  GLN K NE2 1 
ATOM   5714  N  N   . LYS F  1 23  ? 5.642   -19.083 44.520  1.00 38.11  ? 23  LYS K N   1 
ATOM   5715  C  CA  . LYS F  1 23  ? 4.558   -19.901 45.067  1.00 40.29  ? 23  LYS K CA  1 
ATOM   5716  C  C   . LYS F  1 23  ? 3.405   -20.042 44.079  1.00 41.56  ? 23  LYS K C   1 
ATOM   5717  O  O   . LYS F  1 23  ? 2.875   -21.135 43.904  1.00 43.24  ? 23  LYS K O   1 
ATOM   5718  C  CB  . LYS F  1 23  ? 4.071   -19.334 46.410  1.00 40.98  ? 23  LYS K CB  1 
ATOM   5719  C  CG  . LYS F  1 23  ? 5.108   -19.444 47.516  0.50 40.53  ? 23  LYS K CG  1 
ATOM   5720  C  CD  . LYS F  1 23  ? 4.661   -18.762 48.799  0.50 41.40  ? 23  LYS K CD  1 
ATOM   5721  C  CE  . LYS F  1 23  ? 5.784   -18.749 49.826  0.50 40.99  ? 23  LYS K CE  1 
ATOM   5722  N  NZ  . LYS F  1 23  ? 6.056   -20.102 50.384  0.50 42.27  ? 23  LYS K NZ  1 
ATOM   5723  N  N   . GLU F  1 24  ? 3.050   -18.946 43.417  1.00 41.02  ? 24  GLU K N   1 
ATOM   5724  C  CA  . GLU F  1 24  ? 2.023   -18.948 42.380  1.00 42.28  ? 24  GLU K CA  1 
ATOM   5725  C  C   . GLU F  1 24  ? 2.557   -18.297 41.108  1.00 41.08  ? 24  GLU K C   1 
ATOM   5726  O  O   . GLU F  1 24  ? 3.355   -17.359 41.175  1.00 39.31  ? 24  GLU K O   1 
ATOM   5727  C  CB  . GLU F  1 24  ? 0.790   -18.194 42.876  1.00 43.51  ? 24  GLU K CB  1 
ATOM   5728  C  CG  . GLU F  1 24  ? 0.129   -18.804 44.112  1.00 45.31  ? 24  GLU K CG  1 
ATOM   5729  C  CD  . GLU F  1 24  ? -0.406  -20.207 43.885  0.50 47.31  ? 24  GLU K CD  1 
ATOM   5730  O  OE1 . GLU F  1 24  ? -0.931  -20.488 42.787  0.50 48.19  ? 24  GLU K OE1 1 
ATOM   5731  O  OE2 . GLU F  1 24  ? -0.304  -21.033 44.814  0.50 48.21  ? 24  GLU K OE2 1 
ATOM   5732  N  N   . SER F  1 25  ? 2.102   -18.777 39.947  1.00 42.29  ? 25  SER K N   1 
ATOM   5733  C  CA  . SER F  1 25  ? 2.617   -18.275 38.657  1.00 41.60  ? 25  SER K CA  1 
ATOM   5734  C  C   . SER F  1 25  ? 2.325   -16.789 38.439  1.00 40.89  ? 25  SER K C   1 
ATOM   5735  O  O   . SER F  1 25  ? 3.105   -16.091 37.787  1.00 39.69  ? 25  SER K O   1 
ATOM   5736  C  CB  . SER F  1 25  ? 2.096   -19.112 37.485  1.00 43.43  ? 25  SER K CB  1 
ATOM   5737  O  OG  . SER F  1 25  ? 0.715   -19.377 37.609  1.00 45.47  ? 25  SER K OG  1 
ATOM   5738  N  N   . ASN F  1 26  ? 1.234   -16.303 39.030  1.00 41.86  ? 26  ASN K N   1 
ATOM   5739  C  CA  . ASN F  1 26  ? 0.885   -14.874 38.987  1.00 41.46  ? 26  ASN K CA  1 
ATOM   5740  C  C   . ASN F  1 26  ? 1.569   -13.997 40.055  1.00 39.79  ? 26  ASN K C   1 
ATOM   5741  O  O   . ASN F  1 26  ? 1.182   -12.832 40.230  1.00 39.76  ? 26  ASN K O   1 
ATOM   5742  C  CB  . ASN F  1 26  ? -0.641  -14.706 39.091  1.00 43.68  ? 26  ASN K CB  1 
ATOM   5743  C  CG  . ASN F  1 26  ? -1.202  -15.058 40.472  1.00 44.68  ? 26  ASN K CG  1 
ATOM   5744  O  OD1 . ASN F  1 26  ? -0.574  -15.768 41.258  1.00 44.21  ? 26  ASN K OD1 1 
ATOM   5745  N  ND2 . ASN F  1 26  ? -2.411  -14.578 40.753  1.00 46.50  ? 26  ASN K ND2 1 
ATOM   5746  N  N   . GLY F  1 27  ? 2.574   -14.534 40.751  1.00 38.61  ? 27  GLY K N   1 
ATOM   5747  C  CA  . GLY F  1 27  ? 3.089   -13.908 41.962  1.00 37.57  ? 27  GLY K CA  1 
ATOM   5748  C  C   . GLY F  1 27  ? 4.570   -13.576 41.921  1.00 35.58  ? 27  GLY K C   1 
ATOM   5749  O  O   . GLY F  1 27  ? 5.264   -13.906 40.958  1.00 34.92  ? 27  GLY K O   1 
ATOM   5750  N  N   . PRO F  1 28  ? 5.064   -12.928 42.987  1.00 34.80  ? 28  PRO K N   1 
ATOM   5751  C  CA  . PRO F  1 28  ? 6.458   -12.547 43.057  1.00 33.25  ? 28  PRO K CA  1 
ATOM   5752  C  C   . PRO F  1 28  ? 7.404   -13.754 43.130  1.00 32.95  ? 28  PRO K C   1 
ATOM   5753  O  O   . PRO F  1 28  ? 7.002   -14.844 43.550  1.00 33.88  ? 28  PRO K O   1 
ATOM   5754  C  CB  . PRO F  1 28  ? 6.528   -11.705 44.334  1.00 33.19  ? 28  PRO K CB  1 
ATOM   5755  C  CG  . PRO F  1 28  ? 5.416   -12.191 45.176  1.00 34.79  ? 28  PRO K CG  1 
ATOM   5756  C  CD  . PRO F  1 28  ? 4.332   -12.587 44.225  1.00 35.75  ? 28  PRO K CD  1 
ATOM   5757  N  N   . VAL F  1 29  ? 8.632   -13.551 42.667  1.00 31.83  ? 29  VAL K N   1 
ATOM   5758  C  CA  . VAL F  1 29  ? 9.699   -14.534 42.801  1.00 31.68  ? 29  VAL K CA  1 
ATOM   5759  C  C   . VAL F  1 29  ? 10.593  -14.065 43.944  1.00 31.07  ? 29  VAL K C   1 
ATOM   5760  O  O   . VAL F  1 29  ? 11.097  -12.945 43.915  1.00 30.22  ? 29  VAL K O   1 
ATOM   5761  C  CB  . VAL F  1 29  ? 10.515  -14.685 41.504  1.00 31.31  ? 29  VAL K CB  1 
ATOM   5762  C  CG1 . VAL F  1 29  ? 11.574  -15.771 41.666  1.00 31.53  ? 29  VAL K CG1 1 
ATOM   5763  C  CG2 . VAL F  1 29  ? 9.596   -15.030 40.340  1.00 32.13  ? 29  VAL K CG2 1 
ATOM   5764  N  N   . LYS F  1 30  ? 10.751  -14.903 44.965  1.00 31.70  ? 30  LYS K N   1 
ATOM   5765  C  CA  . LYS F  1 30  ? 11.674  -14.602 46.056  1.00 31.59  ? 30  LYS K CA  1 
ATOM   5766  C  C   . LYS F  1 30  ? 13.053  -15.094 45.650  1.00 31.16  ? 30  LYS K C   1 
ATOM   5767  O  O   . LYS F  1 30  ? 13.191  -16.219 45.169  1.00 31.53  ? 30  LYS K O   1 
ATOM   5768  C  CB  . LYS F  1 30  ? 11.220  -15.237 47.362  1.00 32.89  ? 30  LYS K CB  1 
ATOM   5769  C  CG  . LYS F  1 30  ? 9.906   -14.646 47.864  1.00 33.71  ? 30  LYS K CG  1 
ATOM   5770  C  CD  . LYS F  1 30  ? 9.240   -15.523 48.906  1.00 35.45  ? 30  LYS K CD  1 
ATOM   5771  C  CE  . LYS F  1 30  ? 8.049   -14.812 49.520  1.00 36.53  ? 30  LYS K CE  1 
ATOM   5772  N  NZ  . LYS F  1 30  ? 7.485   -15.565 50.672  1.00 38.56  ? 30  LYS K NZ  1 
ATOM   5773  N  N   . VAL F  1 31  ? 14.057  -14.236 45.830  1.00 30.49  ? 31  VAL K N   1 
ATOM   5774  C  CA  . VAL F  1 31  ? 15.431  -14.531 45.434  1.00 30.40  ? 31  VAL K CA  1 
ATOM   5775  C  C   . VAL F  1 31  ? 16.332  -14.328 46.643  1.00 30.73  ? 31  VAL K C   1 
ATOM   5776  O  O   . VAL F  1 31  ? 16.403  -13.228 47.195  1.00 30.50  ? 31  VAL K O   1 
ATOM   5777  C  CB  . VAL F  1 31  ? 15.895  -13.619 44.276  1.00 29.71  ? 31  VAL K CB  1 
ATOM   5778  C  CG1 . VAL F  1 31  ? 17.319  -13.969 43.833  1.00 30.01  ? 31  VAL K CG1 1 
ATOM   5779  C  CG2 . VAL F  1 31  ? 14.928  -13.711 43.107  1.00 29.61  ? 31  VAL K CG2 1 
ATOM   5780  N  N   . TRP F  1 32  ? 17.010  -15.385 47.066  1.00 31.51  ? 32  TRP K N   1 
ATOM   5781  C  CA  . TRP F  1 32  ? 17.852  -15.300 48.247  1.00 32.21  ? 32  TRP K CA  1 
ATOM   5782  C  C   . TRP F  1 32  ? 18.981  -16.311 48.242  1.00 33.13  ? 32  TRP K C   1 
ATOM   5783  O  O   . TRP F  1 32  ? 18.883  -17.372 47.621  1.00 33.42  ? 32  TRP K O   1 
ATOM   5784  C  CB  . TRP F  1 32  ? 17.018  -15.468 49.526  1.00 32.91  ? 32  TRP K CB  1 
ATOM   5785  C  CG  . TRP F  1 32  ? 16.668  -16.888 49.850  1.00 33.88  ? 32  TRP K CG  1 
ATOM   5786  C  CD1 . TRP F  1 32  ? 17.284  -17.694 50.767  1.00 35.11  ? 32  TRP K CD1 1 
ATOM   5787  C  CD2 . TRP F  1 32  ? 15.635  -17.676 49.254  1.00 33.94  ? 32  TRP K CD2 1 
ATOM   5788  N  NE1 . TRP F  1 32  ? 16.697  -18.932 50.779  1.00 35.91  ? 32  TRP K NE1 1 
ATOM   5789  C  CE2 . TRP F  1 32  ? 15.685  -18.955 49.858  1.00 35.22  ? 32  TRP K CE2 1 
ATOM   5790  C  CE3 . TRP F  1 32  ? 14.671  -17.430 48.263  1.00 33.23  ? 32  TRP K CE3 1 
ATOM   5791  C  CZ2 . TRP F  1 32  ? 14.798  -19.989 49.513  1.00 35.86  ? 32  TRP K CZ2 1 
ATOM   5792  C  CZ3 . TRP F  1 32  ? 13.787  -18.461 47.918  1.00 33.90  ? 32  TRP K CZ3 1 
ATOM   5793  C  CH2 . TRP F  1 32  ? 13.855  -19.722 48.552  1.00 35.21  ? 32  TRP K CH2 1 
ATOM   5794  N  N   . GLY F  1 33  ? 20.034  -15.974 48.980  1.00 33.86  ? 33  GLY K N   1 
ATOM   5795  C  CA  . GLY F  1 33  ? 21.192  -16.845 49.145  1.00 35.10  ? 33  GLY K CA  1 
ATOM   5796  C  C   . GLY F  1 33  ? 22.430  -16.061 49.521  1.00 35.75  ? 33  GLY K C   1 
ATOM   5797  O  O   . GLY F  1 33  ? 22.367  -14.859 49.781  1.00 35.29  ? 33  GLY K O   1 
ATOM   5798  N  N   . SER F  1 34  ? 23.563  -16.750 49.523  1.00 37.10  ? 34  SER K N   1 
ATOM   5799  C  CA  . SER F  1 34  ? 24.829  -16.188 49.975  1.00 38.26  ? 34  SER K CA  1 
ATOM   5800  C  C   . SER F  1 34  ? 25.849  -16.173 48.831  1.00 38.60  ? 34  SER K C   1 
ATOM   5801  O  O   . SER F  1 34  ? 26.036  -17.187 48.151  1.00 39.08  ? 34  SER K O   1 
ATOM   5802  C  CB  . SER F  1 34  ? 25.350  -17.014 51.140  1.00 40.04  ? 34  SER K CB  1 
ATOM   5803  O  OG  . SER F  1 34  ? 26.454  -16.385 51.754  1.00 41.45  ? 34  SER K OG  1 
ATOM   5804  N  N   . ILE F  1 35  ? 26.463  -15.013 48.603  1.00 38.56  ? 35  ILE K N   1 
ATOM   5805  C  CA  . ILE F  1 35  ? 27.602  -14.882 47.682  1.00 39.45  ? 35  ILE K CA  1 
ATOM   5806  C  C   . ILE F  1 35  ? 28.776  -14.336 48.478  1.00 41.05  ? 35  ILE K C   1 
ATOM   5807  O  O   . ILE F  1 35  ? 28.655  -13.298 49.125  1.00 40.78  ? 35  ILE K O   1 
ATOM   5808  C  CB  . ILE F  1 35  ? 27.332  -13.913 46.510  1.00 38.28  ? 35  ILE K CB  1 
ATOM   5809  C  CG1 . ILE F  1 35  ? 25.977  -14.199 45.851  1.00 36.71  ? 35  ILE K CG1 1 
ATOM   5810  C  CG2 . ILE F  1 35  ? 28.440  -14.021 45.468  1.00 39.51  ? 35  ILE K CG2 1 
ATOM   5811  C  CD1 . ILE F  1 35  ? 25.557  -13.156 44.839  1.00 35.67  ? 35  ILE K CD1 1 
ATOM   5812  N  N   . LYS F  1 36  ? 29.910  -15.026 48.402  1.00 43.00  ? 36  LYS K N   1 
ATOM   5813  C  CA  . LYS F  1 36  ? 31.133  -14.614 49.107  1.00 45.02  ? 36  LYS K CA  1 
ATOM   5814  C  C   . LYS F  1 36  ? 32.223  -14.180 48.122  1.00 46.13  ? 36  LYS K C   1 
ATOM   5815  O  O   . LYS F  1 36  ? 32.078  -14.352 46.908  1.00 45.55  ? 36  LYS K O   1 
ATOM   5816  C  CB  . LYS F  1 36  ? 31.631  -15.744 50.014  1.00 46.92  ? 36  LYS K CB  1 
ATOM   5817  C  CG  . LYS F  1 36  ? 32.196  -16.956 49.287  1.00 48.23  ? 36  LYS K CG  1 
ATOM   5818  C  CD  . LYS F  1 36  ? 32.577  -18.062 50.253  1.00 50.12  ? 36  LYS K CD  1 
ATOM   5819  C  CE  . LYS F  1 36  ? 32.679  -19.406 49.542  1.00 50.95  ? 36  LYS K CE  1 
ATOM   5820  N  NZ  . LYS F  1 36  ? 31.337  -19.938 49.145  1.00 49.07  ? 36  LYS K NZ  1 
ATOM   5821  N  N   . GLY F  1 37  ? 33.309  -13.624 48.662  1.00 47.95  ? 37  GLY K N   1 
ATOM   5822  C  CA  . GLY F  1 37  ? 34.441  -13.158 47.862  1.00 49.52  ? 37  GLY K CA  1 
ATOM   5823  C  C   . GLY F  1 37  ? 34.298  -11.802 47.176  1.00 48.62  ? 37  GLY K C   1 
ATOM   5824  O  O   . GLY F  1 37  ? 35.146  -11.435 46.365  1.00 50.05  ? 37  GLY K O   1 
ATOM   5825  N  N   . LEU F  1 38  ? 33.254  -11.046 47.508  1.00 46.52  ? 38  LEU K N   1 
ATOM   5826  C  CA  . LEU F  1 38  ? 33.005  -9.735  46.899  1.00 45.59  ? 38  LEU K CA  1 
ATOM   5827  C  C   . LEU F  1 38  ? 33.673  -8.644  47.716  1.00 46.86  ? 38  LEU K C   1 
ATOM   5828  O  O   . LEU F  1 38  ? 33.896  -8.821  48.908  1.00 47.74  ? 38  LEU K O   1 
ATOM   5829  C  CB  . LEU F  1 38  ? 31.500  -9.460  46.843  1.00 42.99  ? 38  LEU K CB  1 
ATOM   5830  C  CG  . LEU F  1 38  ? 30.687  -10.376 45.930  1.00 41.66  ? 38  LEU K CG  1 
ATOM   5831  C  CD1 . LEU F  1 38  ? 29.211  -10.352 46.308  1.00 39.57  ? 38  LEU K CD1 1 
ATOM   5832  C  CD2 . LEU F  1 38  ? 30.884  -9.993  44.468  1.00 41.75  ? 38  LEU K CD2 1 
ATOM   5833  N  N   . THR F  1 39  ? 34.006  -7.524  47.076  1.00 47.19  ? 39  THR K N   1 
ATOM   5834  C  CA  . THR F  1 39  ? 34.398  -6.314  47.802  1.00 48.18  ? 39  THR K CA  1 
ATOM   5835  C  C   . THR F  1 39  ? 33.163  -5.744  48.495  1.00 46.21  ? 39  THR K C   1 
ATOM   5836  O  O   . THR F  1 39  ? 32.047  -5.829  47.956  1.00 43.99  ? 39  THR K O   1 
ATOM   5837  C  CB  . THR F  1 39  ? 35.015  -5.255  46.860  1.00 49.23  ? 39  THR K CB  1 
ATOM   5838  O  OG1 . THR F  1 39  ? 36.281  -5.726  46.386  1.00 51.65  ? 39  THR K OG1 1 
ATOM   5839  C  CG2 . THR F  1 39  ? 35.241  -3.900  47.567  1.00 50.15  ? 39  THR K CG2 1 
ATOM   5840  N  N   . GLU F  1 40  ? 33.364  -5.184  49.689  1.00 47.24  ? 40  GLU K N   1 
ATOM   5841  C  CA  . GLU F  1 40  ? 32.286  -4.538  50.438  1.00 45.98  ? 40  GLU K CA  1 
ATOM   5842  C  C   . GLU F  1 40  ? 31.646  -3.420  49.617  1.00 44.56  ? 40  GLU K C   1 
ATOM   5843  O  O   . GLU F  1 40  ? 32.349  -2.627  48.994  1.00 45.47  ? 40  GLU K O   1 
ATOM   5844  C  CB  . GLU F  1 40  ? 32.793  -3.977  51.776  1.00 48.06  ? 40  GLU K CB  1 
ATOM   5845  C  CG  . GLU F  1 40  ? 31.753  -3.145  52.531  1.00 47.31  ? 40  GLU K CG  1 
ATOM   5846  C  CD  . GLU F  1 40  ? 32.208  -2.686  53.907  1.00 49.67  ? 40  GLU K CD  1 
ATOM   5847  O  OE1 . GLU F  1 40  ? 33.413  -2.798  54.244  1.00 52.05  ? 40  GLU K OE1 1 
ATOM   5848  O  OE2 . GLU F  1 40  ? 31.335  -2.198  54.656  1.00 49.42  ? 40  GLU K OE2 1 
ATOM   5849  N  N   . GLY F  1 41  ? 30.312  -3.370  49.638  1.00 42.43  ? 41  GLY K N   1 
ATOM   5850  C  CA  . GLY F  1 41  ? 29.550  -2.368  48.900  1.00 41.13  ? 41  GLY K CA  1 
ATOM   5851  C  C   . GLY F  1 41  ? 28.627  -2.988  47.866  1.00 39.07  ? 41  GLY K C   1 
ATOM   5852  O  O   . GLY F  1 41  ? 28.388  -4.201  47.873  1.00 38.42  ? 41  GLY K O   1 
ATOM   5853  N  N   . LEU F  1 42  ? 28.137  -2.138  46.963  1.00 38.24  ? 42  LEU K N   1 
ATOM   5854  C  CA  . LEU F  1 42  ? 27.110  -2.512  45.981  1.00 36.45  ? 42  LEU K CA  1 
ATOM   5855  C  C   . LEU F  1 42  ? 27.705  -3.240  44.786  1.00 36.69  ? 42  LEU K C   1 
ATOM   5856  O  O   . LEU F  1 42  ? 28.777  -2.884  44.308  1.00 38.13  ? 42  LEU K O   1 
ATOM   5857  C  CB  . LEU F  1 42  ? 26.370  -1.267  45.472  1.00 35.80  ? 42  LEU K CB  1 
ATOM   5858  C  CG  . LEU F  1 42  ? 25.533  -0.467  46.471  1.00 35.53  ? 42  LEU K CG  1 
ATOM   5859  C  CD1 . LEU F  1 42  ? 25.153  0.903   45.914  1.00 35.53  ? 42  LEU K CD1 1 
ATOM   5860  C  CD2 . LEU F  1 42  ? 24.276  -1.225  46.863  1.00 34.17  ? 42  LEU K CD2 1 
ATOM   5861  N  N   . HIS F  1 43  ? 26.982  -4.247  44.307  1.00 35.45  ? 43  HIS K N   1 
ATOM   5862  C  CA  . HIS F  1 43  ? 27.356  -5.006  43.118  1.00 35.74  ? 43  HIS K CA  1 
ATOM   5863  C  C   . HIS F  1 43  ? 26.137  -5.251  42.231  1.00 34.28  ? 43  HIS K C   1 
ATOM   5864  O  O   . HIS F  1 43  ? 25.101  -5.679  42.729  1.00 33.04  ? 43  HIS K O   1 
ATOM   5865  C  CB  . HIS F  1 43  ? 27.943  -6.344  43.545  1.00 36.39  ? 43  HIS K CB  1 
ATOM   5866  C  CG  . HIS F  1 43  ? 29.294  -6.227  44.172  1.00 38.27  ? 43  HIS K CG  1 
ATOM   5867  N  ND1 . HIS F  1 43  ? 30.448  -6.148  43.427  1.00 40.03  ? 43  HIS K ND1 1 
ATOM   5868  C  CD2 . HIS F  1 43  ? 29.675  -6.158  45.469  1.00 38.98  ? 43  HIS K CD2 1 
ATOM   5869  C  CE1 . HIS F  1 43  ? 31.488  -6.047  44.237  1.00 41.71  ? 43  HIS K CE1 1 
ATOM   5870  N  NE2 . HIS F  1 43  ? 31.047  -6.054  45.482  1.00 41.11  ? 43  HIS K NE2 1 
ATOM   5871  N  N   . GLY F  1 44  ? 26.272  -5.005  40.928  1.00 34.68  ? 44  GLY K N   1 
ATOM   5872  C  CA  . GLY F  1 44  ? 25.176  -5.216  39.969  1.00 33.74  ? 44  GLY K CA  1 
ATOM   5873  C  C   . GLY F  1 44  ? 24.793  -6.677  39.878  1.00 33.40  ? 44  GLY K C   1 
ATOM   5874  O  O   . GLY F  1 44  ? 25.651  -7.543  39.979  1.00 34.41  ? 44  GLY K O   1 
ATOM   5875  N  N   . PHE F  1 45  ? 23.503  -6.943  39.695  1.00 32.22  ? 45  PHE K N   1 
ATOM   5876  C  CA  . PHE F  1 45  ? 22.938  -8.284  39.855  1.00 31.85  ? 45  PHE K CA  1 
ATOM   5877  C  C   . PHE F  1 45  ? 21.846  -8.449  38.806  1.00 31.42  ? 45  PHE K C   1 
ATOM   5878  O  O   . PHE F  1 45  ? 20.777  -7.870  38.937  1.00 30.52  ? 45  PHE K O   1 
ATOM   5879  C  CB  . PHE F  1 45  ? 22.404  -8.416  41.287  1.00 31.03  ? 45  PHE K CB  1 
ATOM   5880  C  CG  . PHE F  1 45  ? 22.027  -9.819  41.704  1.00 30.97  ? 45  PHE K CG  1 
ATOM   5881  C  CD1 . PHE F  1 45  ? 22.994  -10.796 41.884  1.00 31.98  ? 45  PHE K CD1 1 
ATOM   5882  C  CD2 . PHE F  1 45  ? 20.707  -10.137 42.000  1.00 30.16  ? 45  PHE K CD2 1 
ATOM   5883  C  CE1 . PHE F  1 45  ? 22.646  -12.080 42.304  1.00 32.07  ? 45  PHE K CE1 1 
ATOM   5884  C  CE2 . PHE F  1 45  ? 20.351  -11.411 42.429  1.00 30.31  ? 45  PHE K CE2 1 
ATOM   5885  C  CZ  . PHE F  1 45  ? 21.326  -12.385 42.580  1.00 31.24  ? 45  PHE K CZ  1 
ATOM   5886  N  N   . HIS F  1 46  ? 22.140  -9.202  37.743  1.00 32.35  ? 46  HIS K N   1 
ATOM   5887  C  CA  . HIS F  1 46  ? 21.265  -9.278  36.569  1.00 32.43  ? 46  HIS K CA  1 
ATOM   5888  C  C   . HIS F  1 46  ? 21.059  -10.694 36.065  1.00 33.05  ? 46  HIS K C   1 
ATOM   5889  O  O   . HIS F  1 46  ? 21.941  -11.531 36.192  1.00 33.93  ? 46  HIS K O   1 
ATOM   5890  C  CB  . HIS F  1 46  ? 21.849  -8.462  35.408  1.00 33.58  ? 46  HIS K CB  1 
ATOM   5891  C  CG  . HIS F  1 46  ? 22.310  -7.095  35.795  1.00 33.44  ? 46  HIS K CG  1 
ATOM   5892  N  ND1 . HIS F  1 46  ? 23.571  -6.626  35.494  1.00 34.85  ? 46  HIS K ND1 1 
ATOM   5893  C  CD2 . HIS F  1 46  ? 21.684  -6.097  36.459  1.00 32.38  ? 46  HIS K CD2 1 
ATOM   5894  C  CE1 . HIS F  1 46  ? 23.699  -5.393  35.954  1.00 34.54  ? 46  HIS K CE1 1 
ATOM   5895  N  NE2 . HIS F  1 46  ? 22.571  -5.053  36.551  1.00 33.05  ? 46  HIS K NE2 1 
ATOM   5896  N  N   . VAL F  1 47  ? 19.893  -10.937 35.470  1.00 32.81  ? 47  VAL K N   1 
ATOM   5897  C  CA  . VAL F  1 47  ? 19.668  -12.104 34.634  1.00 33.89  ? 47  VAL K CA  1 
ATOM   5898  C  C   . VAL F  1 47  ? 19.973  -11.720 33.181  1.00 35.38  ? 47  VAL K C   1 
ATOM   5899  O  O   . VAL F  1 47  ? 19.303  -10.853 32.610  1.00 35.22  ? 47  VAL K O   1 
ATOM   5900  C  CB  . VAL F  1 47  ? 18.222  -12.618 34.751  1.00 33.28  ? 47  VAL K CB  1 
ATOM   5901  C  CG1 . VAL F  1 47  ? 18.025  -13.867 33.896  1.00 34.64  ? 47  VAL K CG1 1 
ATOM   5902  C  CG2 . VAL F  1 47  ? 17.880  -12.894 36.208  1.00 32.11  ? 47  VAL K CG2 1 
ATOM   5903  N  N   . HIS F  1 48  ? 20.985  -12.366 32.599  1.00 37.07  ? 48  HIS K N   1 
ATOM   5904  C  CA  . HIS F  1 48  ? 21.354  -12.172 31.195  1.00 39.04  ? 48  HIS K CA  1 
ATOM   5905  C  C   . HIS F  1 48  ? 20.644  -13.200 30.326  1.00 40.30  ? 48  HIS K C   1 
ATOM   5906  O  O   . HIS F  1 48  ? 20.184  -14.225 30.825  1.00 39.85  ? 48  HIS K O   1 
ATOM   5907  C  CB  . HIS F  1 48  ? 22.868  -12.256 31.014  1.00 40.61  ? 48  HIS K CB  1 
ATOM   5908  C  CG  . HIS F  1 48  ? 23.604  -11.083 31.581  1.00 40.07  ? 48  HIS K CG  1 
ATOM   5909  N  ND1 . HIS F  1 48  ? 24.418  -10.279 30.818  1.00 41.62  ? 48  HIS K ND1 1 
ATOM   5910  C  CD2 . HIS F  1 48  ? 23.628  -10.562 32.832  1.00 38.40  ? 48  HIS K CD2 1 
ATOM   5911  C  CE1 . HIS F  1 48  ? 24.929  -9.325  31.575  1.00 40.90  ? 48  HIS K CE1 1 
ATOM   5912  N  NE2 . HIS F  1 48  ? 24.460  -9.468  32.800  1.00 38.94  ? 48  HIS K NE2 1 
ATOM   5913  N  N   . GLU F  1 49  ? 20.571  -12.924 29.024  1.00 42.10  ? 49  GLU K N   1 
ATOM   5914  C  CA  . GLU F  1 49  ? 19.661  -13.640 28.116  1.00 43.39  ? 49  GLU K CA  1 
ATOM   5915  C  C   . GLU F  1 49  ? 19.940  -15.133 27.934  1.00 44.90  ? 49  GLU K C   1 
ATOM   5916  O  O   . GLU F  1 49  ? 19.013  -15.939 27.948  1.00 44.87  ? 49  GLU K O   1 
ATOM   5917  C  CB  . GLU F  1 49  ? 19.639  -12.977 26.734  1.00 45.35  ? 49  GLU K CB  1 
ATOM   5918  C  CG  . GLU F  1 49  ? 18.566  -13.543 25.814  1.00 46.71  ? 49  GLU K CG  1 
ATOM   5919  C  CD  . GLU F  1 49  ? 18.406  -12.778 24.520  1.00 48.68  ? 49  GLU K CD  1 
ATOM   5920  O  OE1 . GLU F  1 49  ? 19.164  -11.812 24.276  1.00 49.13  ? 49  GLU K OE1 1 
ATOM   5921  O  OE2 . GLU F  1 49  ? 17.512  -13.156 23.738  1.00 50.05  ? 49  GLU K OE2 1 
ATOM   5922  N  N   . PHE F  1 50  ? 21.202  -15.488 27.734  1.00 46.52  ? 50  PHE K N   1 
ATOM   5923  C  CA  . PHE F  1 50  ? 21.568  -16.853 27.357  1.00 48.60  ? 50  PHE K CA  1 
ATOM   5924  C  C   . PHE F  1 50  ? 22.165  -17.631 28.536  1.00 47.82  ? 50  PHE K C   1 
ATOM   5925  O  O   . PHE F  1 50  ? 22.903  -17.069 29.347  1.00 46.76  ? 50  PHE K O   1 
ATOM   5926  C  CB  . PHE F  1 50  ? 22.532  -16.815 26.171  1.00 51.61  ? 50  PHE K CB  1 
ATOM   5927  C  CG  . PHE F  1 50  ? 21.989  -16.069 24.982  1.00 52.87  ? 50  PHE K CG  1 
ATOM   5928  C  CD1 . PHE F  1 50  ? 20.859  -16.533 24.313  1.00 53.62  ? 50  PHE K CD1 1 
ATOM   5929  C  CD2 . PHE F  1 50  ? 22.585  -14.891 24.542  1.00 53.48  ? 50  PHE K CD2 1 
ATOM   5930  C  CE1 . PHE F  1 50  ? 20.339  -15.844 23.230  1.00 54.95  ? 50  PHE K CE1 1 
ATOM   5931  C  CE2 . PHE F  1 50  ? 22.069  -14.198 23.455  1.00 54.80  ? 50  PHE K CE2 1 
ATOM   5932  C  CZ  . PHE F  1 50  ? 20.946  -14.677 22.796  1.00 55.54  ? 50  PHE K CZ  1 
ATOM   5933  N  N   . GLY F  1 51  ? 21.827  -18.919 28.621  1.00 48.59  ? 51  GLY K N   1 
ATOM   5934  C  CA  . GLY F  1 51  ? 22.429  -19.852 29.577  1.00 48.52  ? 51  GLY K CA  1 
ATOM   5935  C  C   . GLY F  1 51  ? 23.664  -20.521 28.995  1.00 51.39  ? 51  GLY K C   1 
ATOM   5936  O  O   . GLY F  1 51  ? 23.813  -21.741 29.068  1.00 52.69  ? 51  GLY K O   1 
ATOM   5937  N  N   . ASP F  1 52  ? 24.552  -19.706 28.432  1.00 52.60  ? 52  ASP K N   1 
ATOM   5938  C  CA  . ASP F  1 52  ? 25.701  -20.165 27.664  1.00 55.82  ? 52  ASP K CA  1 
ATOM   5939  C  C   . ASP F  1 52  ? 26.925  -19.765 28.468  1.00 55.71  ? 52  ASP K C   1 
ATOM   5940  O  O   . ASP F  1 52  ? 27.257  -18.579 28.565  1.00 54.95  ? 52  ASP K O   1 
ATOM   5941  C  CB  . ASP F  1 52  ? 25.691  -19.498 26.279  1.00 57.77  ? 52  ASP K CB  1 
ATOM   5942  C  CG  . ASP F  1 52  ? 26.784  -20.017 25.351  1.00 61.61  ? 52  ASP K CG  1 
ATOM   5943  O  OD1 . ASP F  1 52  ? 27.763  -20.620 25.832  1.00 62.64  ? 52  ASP K OD1 1 
ATOM   5944  O  OD2 . ASP F  1 52  ? 26.661  -19.815 24.125  1.00 63.85  ? 52  ASP K OD2 1 
ATOM   5945  N  N   . ASN F  1 53  ? 27.573  -20.761 29.062  1.00 56.70  ? 53  ASN K N   1 
ATOM   5946  C  CA  . ASN F  1 53  ? 28.749  -20.554 29.901  1.00 56.98  ? 53  ASN K CA  1 
ATOM   5947  C  C   . ASN F  1 53  ? 30.006  -21.081 29.207  1.00 60.70  ? 53  ASN K C   1 
ATOM   5948  O  O   . ASN F  1 53  ? 31.012  -21.325 29.868  1.00 61.58  ? 53  ASN K O   1 
ATOM   5949  C  CB  . ASN F  1 53  ? 28.539  -21.253 31.257  1.00 55.33  ? 53  ASN K CB  1 
ATOM   5950  C  CG  . ASN F  1 53  ? 29.398  -20.668 32.370  1.00 54.55  ? 53  ASN K CG  1 
ATOM   5951  O  OD1 . ASN F  1 53  ? 30.310  -21.327 32.874  1.00 56.09  ? 53  ASN K OD1 1 
ATOM   5952  N  ND2 . ASN F  1 53  ? 29.108  -19.438 32.761  1.00 52.51  ? 53  ASN K ND2 1 
ATOM   5953  N  N   . THR F  1 54  ? 29.954  -21.239 27.880  1.00 63.19  ? 54  THR K N   1 
ATOM   5954  C  CA  . THR F  1 54  ? 31.065  -21.810 27.109  1.00 67.24  ? 54  THR K CA  1 
ATOM   5955  C  C   . THR F  1 54  ? 32.297  -20.910 27.152  1.00 68.59  ? 54  THR K C   1 
ATOM   5956  O  O   . THR F  1 54  ? 33.426  -21.404 27.177  1.00 71.30  ? 54  THR K O   1 
ATOM   5957  C  CB  . THR F  1 54  ? 30.691  -22.054 25.628  1.00 69.83  ? 54  THR K CB  1 
ATOM   5958  O  OG1 . THR F  1 54  ? 30.191  -20.846 25.049  1.00 68.85  ? 54  THR K OG1 1 
ATOM   5959  C  CG2 . THR F  1 54  ? 29.644  -23.155 25.494  1.00 69.54  ? 54  THR K CG2 1 
ATOM   5960  N  N   . ALA F  1 55  ? 32.069  -19.596 27.149  1.00 66.92  ? 55  ALA K N   1 
ATOM   5961  C  CA  . ALA F  1 55  ? 33.133  -18.606 27.320  1.00 67.88  ? 55  ALA K CA  1 
ATOM   5962  C  C   . ALA F  1 55  ? 32.956  -17.870 28.648  1.00 64.49  ? 55  ALA K C   1 
ATOM   5963  O  O   . ALA F  1 55  ? 33.173  -16.654 28.728  1.00 63.94  ? 55  ALA K O   1 
ATOM   5964  C  CB  . ALA F  1 55  ? 33.124  -17.628 26.150  1.00 69.38  ? 55  ALA K CB  1 
ATOM   5965  N  N   . GLY F  1 56  ? 32.571  -18.612 29.689  1.00 62.55  ? 56  GLY K N   1 
ATOM   5966  C  CA  . GLY F  1 56  ? 32.230  -18.028 30.984  1.00 59.36  ? 56  GLY K CA  1 
ATOM   5967  C  C   . GLY F  1 56  ? 30.985  -17.162 30.916  1.00 56.54  ? 56  GLY K C   1 
ATOM   5968  O  O   . GLY F  1 56  ? 30.097  -17.393 30.089  1.00 56.52  ? 56  GLY K O   1 
ATOM   5969  N  N   . ALA F  1 57  ? 30.936  -16.147 31.779  1.00 54.42  ? 57  ALA K N   1 
ATOM   5970  C  CA  . ALA F  1 57  ? 29.864  -15.155 31.772  1.00 51.91  ? 57  ALA K CA  1 
ATOM   5971  C  C   . ALA F  1 57  ? 29.768  -14.318 30.487  1.00 53.02  ? 57  ALA K C   1 
ATOM   5972  O  O   . ALA F  1 57  ? 28.695  -13.788 30.187  1.00 51.43  ? 57  ALA K O   1 
ATOM   5973  C  CB  . ALA F  1 57  ? 29.997  -14.233 32.979  1.00 50.02  ? 57  ALA K CB  1 
ATOM   5974  N  N   . THR F  1 58  ? 30.863  -14.189 29.736  1.00 55.92  ? 58  THR K N   1 
ATOM   5975  C  CA  . THR F  1 58  ? 30.881  -13.362 28.521  1.00 57.47  ? 58  THR K CA  1 
ATOM   5976  C  C   . THR F  1 58  ? 29.900  -13.850 27.449  1.00 57.86  ? 58  THR K C   1 
ATOM   5977  O  O   . THR F  1 58  ? 29.273  -13.037 26.756  1.00 57.63  ? 58  THR K O   1 
ATOM   5978  C  CB  . THR F  1 58  ? 32.296  -13.281 27.912  1.00 61.20  ? 58  THR K CB  1 
ATOM   5979  O  OG1 . THR F  1 58  ? 33.260  -13.144 28.964  1.00 61.28  ? 58  THR K OG1 1 
ATOM   5980  C  CG2 . THR F  1 58  ? 32.414  -12.100 26.950  1.00 62.61  ? 58  THR K CG2 1 
ATOM   5981  N  N   . SER F  1 59  ? 29.748  -15.169 27.343  1.00 58.46  ? 59  SER K N   1 
ATOM   5982  C  CA  . SER F  1 59  ? 28.814  -15.786 26.393  1.00 59.11  ? 59  SER K CA  1 
ATOM   5983  C  C   . SER F  1 59  ? 27.320  -15.693 26.800  1.00 55.91  ? 59  SER K C   1 
ATOM   5984  O  O   . SER F  1 59  ? 26.444  -16.070 26.019  1.00 56.45  ? 59  SER K O   1 
ATOM   5985  C  CB  . SER F  1 59  ? 29.218  -17.251 26.152  1.00 61.37  ? 59  SER K CB  1 
ATOM   5986  O  OG  . SER F  1 59  ? 29.521  -17.915 27.375  1.00 60.08  ? 59  SER K OG  1 
ATOM   5987  N  N   . ALA F  1 60  ? 27.027  -15.182 27.997  1.00 52.88  ? 60  ALA K N   1 
ATOM   5988  C  CA  . ALA F  1 60  ? 25.643  -15.033 28.465  1.00 50.08  ? 60  ALA K CA  1 
ATOM   5989  C  C   . ALA F  1 60  ? 24.839  -13.965 27.713  1.00 49.65  ? 60  ALA K C   1 
ATOM   5990  O  O   . ALA F  1 60  ? 23.610  -13.939 27.815  1.00 48.08  ? 60  ALA K O   1 
ATOM   5991  C  CB  . ALA F  1 60  ? 25.627  -14.734 29.955  1.00 47.50  ? 60  ALA K CB  1 
ATOM   5992  N  N   . GLY F  1 61  ? 25.523  -13.078 26.986  1.00 51.19  ? 61  GLY K N   1 
ATOM   5993  C  CA  . GLY F  1 61  ? 24.861  -12.045 26.200  1.00 51.20  ? 61  GLY K CA  1 
ATOM   5994  C  C   . GLY F  1 61  ? 24.431  -10.875 27.069  1.00 48.52  ? 61  GLY K C   1 
ATOM   5995  O  O   . GLY F  1 61  ? 24.936  -10.708 28.180  1.00 47.10  ? 61  GLY K O   1 
ATOM   5996  N  N   . PRO F  1 62  ? 23.488  -10.053 26.571  1.00 47.97  ? 62  PRO K N   1 
ATOM   5997  C  CA  . PRO F  1 62  ? 23.091  -8.850  27.281  1.00 45.87  ? 62  PRO K CA  1 
ATOM   5998  C  C   . PRO F  1 62  ? 22.054  -9.171  28.353  1.00 43.17  ? 62  PRO K C   1 
ATOM   5999  O  O   . PRO F  1 62  ? 21.721  -10.336 28.553  1.00 42.92  ? 62  PRO K O   1 
ATOM   6000  C  CB  . PRO F  1 62  ? 22.485  -7.986  26.169  1.00 46.95  ? 62  PRO K CB  1 
ATOM   6001  C  CG  . PRO F  1 62  ? 21.905  -8.970  25.208  1.00 48.49  ? 62  PRO K CG  1 
ATOM   6002  C  CD  . PRO F  1 62  ? 22.657  -10.268 25.370  1.00 49.43  ? 62  PRO K CD  1 
ATOM   6003  N  N   . HIS F  1 63  ? 21.533  -8.144  29.013  1.00 41.41  ? 63  HIS K N   1 
ATOM   6004  C  CA  . HIS F  1 63  ? 20.466  -8.340  29.992  1.00 39.25  ? 63  HIS K CA  1 
ATOM   6005  C  C   . HIS F  1 63  ? 19.253  -8.943  29.297  1.00 39.46  ? 63  HIS K C   1 
ATOM   6006  O  O   . HIS F  1 63  ? 18.943  -8.575  28.176  1.00 40.76  ? 63  HIS K O   1 
ATOM   6007  C  CB  . HIS F  1 63  ? 20.093  -7.035  30.699  1.00 37.87  ? 63  HIS K CB  1 
ATOM   6008  C  CG  . HIS F  1 63  ? 21.217  -6.439  31.490  1.00 37.80  ? 63  HIS K CG  1 
ATOM   6009  N  ND1 . HIS F  1 63  ? 21.121  -5.222  32.129  1.00 36.93  ? 63  HIS K ND1 1 
ATOM   6010  C  CD2 . HIS F  1 63  ? 22.478  -6.881  31.713  1.00 38.78  ? 63  HIS K CD2 1 
ATOM   6011  C  CE1 . HIS F  1 63  ? 22.266  -4.950  32.729  1.00 37.27  ? 63  HIS K CE1 1 
ATOM   6012  N  NE2 . HIS F  1 63  ? 23.109  -5.936  32.483  1.00 38.45  ? 63  HIS K NE2 1 
ATOM   6013  N  N   . PHE F  1 64  ? 18.607  -9.903  29.955  1.00 38.41  ? 64  PHE K N   1 
ATOM   6014  C  CA  . PHE F  1 64  ? 17.396  -10.526 29.424  1.00 38.76  ? 64  PHE K CA  1 
ATOM   6015  C  C   . PHE F  1 64  ? 16.321  -9.452  29.263  1.00 38.18  ? 64  PHE K C   1 
ATOM   6016  O  O   . PHE F  1 64  ? 15.874  -8.864  30.251  1.00 36.44  ? 64  PHE K O   1 
ATOM   6017  C  CB  . PHE F  1 64  ? 16.925  -11.636 30.367  1.00 37.75  ? 64  PHE K CB  1 
ATOM   6018  C  CG  . PHE F  1 64  ? 15.644  -12.309 29.950  1.00 38.26  ? 64  PHE K CG  1 
ATOM   6019  C  CD1 . PHE F  1 64  ? 15.412  -12.669 28.620  1.00 40.30  ? 64  PHE K CD1 1 
ATOM   6020  C  CD2 . PHE F  1 64  ? 14.675  -12.617 30.901  1.00 37.01  ? 64  PHE K CD2 1 
ATOM   6021  C  CE1 . PHE F  1 64  ? 14.231  -13.295 28.254  1.00 41.02  ? 64  PHE K CE1 1 
ATOM   6022  C  CE2 . PHE F  1 64  ? 13.498  -13.247 30.538  1.00 37.74  ? 64  PHE K CE2 1 
ATOM   6023  C  CZ  . PHE F  1 64  ? 13.278  -13.592 29.217  1.00 39.71  ? 64  PHE K CZ  1 
ATOM   6024  N  N   . ASN F  1 65  ? 15.922  -9.207  28.017  1.00 39.82  ? 65  ASN K N   1 
ATOM   6025  C  CA  . ASN F  1 65  ? 15.116  -8.041  27.660  1.00 39.82  ? 65  ASN K CA  1 
ATOM   6026  C  C   . ASN F  1 65  ? 14.084  -8.399  26.582  1.00 41.46  ? 65  ASN K C   1 
ATOM   6027  O  O   . ASN F  1 65  ? 14.155  -7.894  25.466  1.00 43.15  ? 65  ASN K O   1 
ATOM   6028  C  CB  . ASN F  1 65  ? 16.047  -6.912  27.182  1.00 40.58  ? 65  ASN K CB  1 
ATOM   6029  C  CG  . ASN F  1 65  ? 15.322  -5.599  26.930  1.00 40.58  ? 65  ASN K CG  1 
ATOM   6030  O  OD1 . ASN F  1 65  ? 14.279  -5.317  27.531  1.00 39.43  ? 65  ASN K OD1 1 
ATOM   6031  N  ND2 . ASN F  1 65  ? 15.892  -4.769  26.059  1.00 42.16  ? 65  ASN K ND2 1 
ATOM   6032  N  N   . PRO F  1 66  ? 13.109  -9.265  26.921  1.00 41.12  ? 66  PRO K N   1 
ATOM   6033  C  CA  . PRO F  1 66  ? 12.113  -9.686  25.924  1.00 42.97  ? 66  PRO K CA  1 
ATOM   6034  C  C   . PRO F  1 66  ? 11.126  -8.593  25.474  1.00 43.44  ? 66  PRO K C   1 
ATOM   6035  O  O   . PRO F  1 66  ? 10.516  -8.746  24.418  1.00 45.47  ? 66  PRO K O   1 
ATOM   6036  C  CB  . PRO F  1 66  ? 11.364  -10.817 26.633  1.00 42.35  ? 66  PRO K CB  1 
ATOM   6037  C  CG  . PRO F  1 66  ? 11.490  -10.491 28.080  1.00 39.91  ? 66  PRO K CG  1 
ATOM   6038  C  CD  . PRO F  1 66  ? 12.844  -9.863  28.242  1.00 39.29  ? 66  PRO K CD  1 
ATOM   6039  N  N   . LEU F  1 67  ? 10.965  -7.524  26.259  1.00 41.81  ? 67  LEU K N   1 
ATOM   6040  C  CA  . LEU F  1 67  ? 10.083  -6.394  25.885  1.00 42.37  ? 67  LEU K CA  1 
ATOM   6041  C  C   . LEU F  1 67  ? 10.826  -5.182  25.279  1.00 43.03  ? 67  LEU K C   1 
ATOM   6042  O  O   . LEU F  1 67  ? 10.215  -4.133  25.048  1.00 43.48  ? 67  LEU K O   1 
ATOM   6043  C  CB  . LEU F  1 67  ? 9.249   -5.961  27.103  1.00 40.59  ? 67  LEU K CB  1 
ATOM   6044  C  CG  . LEU F  1 67  ? 8.297   -7.024  27.672  1.00 40.37  ? 67  LEU K CG  1 
ATOM   6045  C  CD1 . LEU F  1 67  ? 7.717   -6.582  29.008  1.00 38.72  ? 67  LEU K CD1 1 
ATOM   6046  C  CD2 . LEU F  1 67  ? 7.173   -7.332  26.690  1.00 42.53  ? 67  LEU K CD2 1 
ATOM   6047  N  N   . SER F  1 68  ? 12.128  -5.327  25.023  1.00 43.39  ? 68  SER K N   1 
ATOM   6048  C  CA  . SER F  1 68  ? 12.930  -4.310  24.331  1.00 44.55  ? 68  SER K CA  1 
ATOM   6049  C  C   . SER F  1 68  ? 12.867  -2.932  25.004  1.00 43.27  ? 68  SER K C   1 
ATOM   6050  O  O   . SER F  1 68  ? 12.641  -1.904  24.349  1.00 44.40  ? 68  SER K O   1 
ATOM   6051  C  CB  . SER F  1 68  ? 12.520  -4.224  22.850  1.00 47.40  ? 68  SER K CB  1 
ATOM   6052  O  OG  . SER F  1 68  ? 12.416  -5.517  22.269  1.00 48.81  ? 68  SER K OG  1 
ATOM   6053  N  N   . ARG F  1 69  ? 13.059  -2.923  26.321  1.00 41.08  ? 69  ARG K N   1 
ATOM   6054  C  CA  . ARG F  1 69  ? 13.043  -1.691  27.114  1.00 39.89  ? 69  ARG K CA  1 
ATOM   6055  C  C   . ARG F  1 69  ? 14.470  -1.212  27.381  1.00 39.55  ? 69  ARG K C   1 
ATOM   6056  O  O   . ARG F  1 69  ? 15.441  -1.903  27.071  1.00 40.17  ? 69  ARG K O   1 
ATOM   6057  C  CB  . ARG F  1 69  ? 12.319  -1.932  28.439  1.00 38.14  ? 69  ARG K CB  1 
ATOM   6058  C  CG  . ARG F  1 69  ? 10.907  -2.521  28.328  1.00 38.60  ? 69  ARG K CG  1 
ATOM   6059  C  CD  . ARG F  1 69  ? 9.867   -1.476  27.956  1.00 39.58  ? 69  ARG K CD  1 
ATOM   6060  N  NE  . ARG F  1 69  ? 8.514   -2.017  27.769  0.70 40.40  ? 69  ARG K NE  1 
ATOM   6061  C  CZ  . ARG F  1 69  ? 7.689   -2.436  28.740  0.70 39.57  ? 69  ARG K CZ  1 
ATOM   6062  N  NH1 . ARG F  1 69  ? 8.049   -2.437  30.027  0.70 37.80  ? 69  ARG K NH1 1 
ATOM   6063  N  NH2 . ARG F  1 69  ? 6.475   -2.884  28.411  0.70 40.77  ? 69  ARG K NH2 1 
ATOM   6064  N  N   . LYS F  1 70  ? 14.588  -0.015  27.945  1.00 38.84  ? 70  LYS K N   1 
ATOM   6065  C  CA  . LYS F  1 70  ? 15.872  0.499   28.440  1.00 38.52  ? 70  LYS K CA  1 
ATOM   6066  C  C   . LYS F  1 70  ? 16.173  -0.080  29.825  1.00 36.58  ? 70  LYS K C   1 
ATOM   6067  O  O   . LYS F  1 70  ? 15.259  -0.490  30.547  1.00 35.32  ? 70  LYS K O   1 
ATOM   6068  C  CB  . LYS F  1 70  ? 15.849  2.028   28.532  1.00 38.82  ? 70  LYS K CB  1 
ATOM   6069  C  CG  . LYS F  1 70  ? 15.591  2.738   27.209  1.00 40.90  ? 70  LYS K CG  1 
ATOM   6070  C  CD  . LYS F  1 70  ? 15.763  4.251   27.321  0.50 41.40  ? 70  LYS K CD  1 
ATOM   6071  C  CE  . LYS F  1 70  ? 14.690  4.918   28.180  0.50 40.20  ? 70  LYS K CE  1 
ATOM   6072  N  NZ  . LYS F  1 70  ? 13.327  4.816   27.589  0.50 40.79  ? 70  LYS K NZ  1 
ATOM   6073  N  N   . HIS F  1 71  ? 17.453  -0.091  30.189  1.00 36.53  ? 71  HIS K N   1 
ATOM   6074  C  CA  . HIS F  1 71  ? 17.897  -0.565  31.498  1.00 35.07  ? 71  HIS K CA  1 
ATOM   6075  C  C   . HIS F  1 71  ? 17.385  0.350   32.614  1.00 33.94  ? 71  HIS K C   1 
ATOM   6076  O  O   . HIS F  1 71  ? 17.429  1.569   32.488  1.00 34.50  ? 71  HIS K O   1 
ATOM   6077  C  CB  . HIS F  1 71  ? 19.428  -0.626  31.558  1.00 35.78  ? 71  HIS K CB  1 
ATOM   6078  C  CG  . HIS F  1 71  ? 19.961  -1.121  32.862  1.00 34.58  ? 71  HIS K CG  1 
ATOM   6079  N  ND1 . HIS F  1 71  ? 20.034  -2.461  33.183  1.00 34.03  ? 71  HIS K ND1 1 
ATOM   6080  C  CD2 . HIS F  1 71  ? 20.437  -0.446  33.933  1.00 33.99  ? 71  HIS K CD2 1 
ATOM   6081  C  CE1 . HIS F  1 71  ? 20.525  -2.583  34.403  1.00 33.27  ? 71  HIS K CE1 1 
ATOM   6082  N  NE2 . HIS F  1 71  ? 20.785  -1.377  34.876  1.00 33.22  ? 71  HIS K NE2 1 
ATOM   6083  N  N   . GLY F  1 72  ? 16.912  -0.255  33.700  1.00 32.61  ? 72  GLY K N   1 
ATOM   6084  C  CA  . GLY F  1 72  ? 16.488  0.483   34.889  1.00 31.75  ? 72  GLY K CA  1 
ATOM   6085  C  C   . GLY F  1 72  ? 16.777  -0.310  36.143  1.00 30.81  ? 72  GLY K C   1 
ATOM   6086  O  O   . GLY F  1 72  ? 17.461  -1.334  36.096  1.00 30.85  ? 72  GLY K O   1 
ATOM   6087  N  N   . GLY F  1 73  ? 16.279  0.183   37.269  1.00 30.28  ? 73  GLY K N   1 
ATOM   6088  C  CA  . GLY F  1 73  ? 16.306  -0.561  38.522  1.00 29.62  ? 73  GLY K CA  1 
ATOM   6089  C  C   . GLY F  1 73  ? 15.069  -1.442  38.613  1.00 29.26  ? 73  GLY K C   1 
ATOM   6090  O  O   . GLY F  1 73  ? 14.115  -1.242  37.849  1.00 29.53  ? 73  GLY K O   1 
ATOM   6091  N  N   . PRO F  1 74  ? 15.062  -2.417  39.547  1.00 28.87  ? 74  PRO K N   1 
ATOM   6092  C  CA  . PRO F  1 74  ? 13.913  -3.322  39.659  1.00 28.74  ? 74  PRO K CA  1 
ATOM   6093  C  C   . PRO F  1 74  ? 12.587  -2.638  40.019  1.00 28.95  ? 74  PRO K C   1 
ATOM   6094  O  O   . PRO F  1 74  ? 11.536  -3.166  39.686  1.00 29.16  ? 74  PRO K O   1 
ATOM   6095  C  CB  . PRO F  1 74  ? 14.329  -4.308  40.764  1.00 28.49  ? 74  PRO K CB  1 
ATOM   6096  C  CG  . PRO F  1 74  ? 15.483  -3.677  41.459  1.00 28.54  ? 74  PRO K CG  1 
ATOM   6097  C  CD  . PRO F  1 74  ? 16.160  -2.817  40.441  1.00 28.79  ? 74  PRO K CD  1 
ATOM   6098  N  N   . LYS F  1 75  ? 12.645  -1.484  40.675  1.00 29.16  ? 75  LYS K N   1 
ATOM   6099  C  CA  . LYS F  1 75  ? 11.447  -0.726  41.025  1.00 29.73  ? 75  LYS K CA  1 
ATOM   6100  C  C   . LYS F  1 75  ? 10.828  0.047   39.841  1.00 30.21  ? 75  LYS K C   1 
ATOM   6101  O  O   . LYS F  1 75  ? 9.704   0.503   39.956  1.00 30.67  ? 75  LYS K O   1 
ATOM   6102  C  CB  . LYS F  1 75  ? 11.752  0.248   42.171  1.00 30.10  ? 75  LYS K CB  1 
ATOM   6103  C  CG  . LYS F  1 75  ? 12.195  -0.436  43.458  1.00 30.10  ? 75  LYS K CG  1 
ATOM   6104  C  CD  . LYS F  1 75  ? 12.883  0.533   44.407  1.00 30.65  ? 75  LYS K CD  1 
ATOM   6105  C  CE  . LYS F  1 75  ? 11.882  1.461   45.089  1.00 31.67  ? 75  LYS K CE  1 
ATOM   6106  N  NZ  . LYS F  1 75  ? 12.571  2.393   46.035  1.00 32.42  ? 75  LYS K NZ  1 
ATOM   6107  N  N   . ASP F  1 76  ? 11.561  0.213   38.734  1.00 30.25  ? 76  ASP K N   1 
ATOM   6108  C  CA  . ASP F  1 76  ? 11.072  0.976   37.585  1.00 31.08  ? 76  ASP K CA  1 
ATOM   6109  C  C   . ASP F  1 76  ? 10.136  0.172   36.688  1.00 31.53  ? 76  ASP K C   1 
ATOM   6110  O  O   . ASP F  1 76  ? 10.304  -1.040  36.500  1.00 31.14  ? 76  ASP K O   1 
ATOM   6111  C  CB  . ASP F  1 76  ? 12.223  1.459   36.696  1.00 31.39  ? 76  ASP K CB  1 
ATOM   6112  C  CG  . ASP F  1 76  ? 13.200  2.338   37.423  1.00 31.40  ? 76  ASP K CG  1 
ATOM   6113  O  OD1 . ASP F  1 76  ? 12.749  3.247   38.151  1.00 31.72  ? 76  ASP K OD1 1 
ATOM   6114  O  OD2 . ASP F  1 76  ? 14.420  2.127   37.248  1.00 31.44  ? 76  ASP K OD2 1 
ATOM   6115  N  N   . GLU F  1 77  ? 9.197   0.891   36.085  1.00 32.51  ? 77  GLU K N   1 
ATOM   6116  C  CA  . GLU F  1 77  ? 8.375   0.365   35.003  1.00 33.47  ? 77  GLU K CA  1 
ATOM   6117  C  C   . GLU F  1 77  ? 9.255   0.150   33.763  1.00 33.66  ? 77  GLU K C   1 
ATOM   6118  O  O   . GLU F  1 77  ? 9.225   -0.922  33.154  1.00 33.88  ? 77  GLU K O   1 
ATOM   6119  C  CB  . GLU F  1 77  ? 7.224   1.328   34.706  1.00 34.89  ? 77  GLU K CB  1 
ATOM   6120  C  CG  . GLU F  1 77  ? 6.067   0.708   33.948  1.00 36.23  ? 77  GLU K CG  1 
ATOM   6121  C  CD  . GLU F  1 77  ? 5.055   1.742   33.514  1.00 37.84  ? 77  GLU K CD  1 
ATOM   6122  O  OE1 . GLU F  1 77  ? 4.483   2.433   34.392  1.00 38.30  ? 77  GLU K OE1 1 
ATOM   6123  O  OE2 . GLU F  1 77  ? 4.827   1.873   32.291  1.00 39.20  ? 77  GLU K OE2 1 
ATOM   6124  N  N   . GLU F  1 78  ? 10.062  1.153   33.422  1.00 33.70  ? 78  GLU K N   1 
ATOM   6125  C  CA  . GLU F  1 78  ? 11.043  1.026   32.340  1.00 34.20  ? 78  GLU K CA  1 
ATOM   6126  C  C   . GLU F  1 78  ? 12.297  0.275   32.833  1.00 33.10  ? 78  GLU K C   1 
ATOM   6127  O  O   . GLU F  1 78  ? 13.189  0.857   33.463  1.00 32.61  ? 78  GLU K O   1 
ATOM   6128  C  CB  . GLU F  1 78  ? 11.404  2.404   31.778  1.00 35.22  ? 78  GLU K CB  1 
ATOM   6129  C  CG  . GLU F  1 78  ? 12.253  2.368   30.509  1.00 36.55  ? 78  GLU K CG  1 
ATOM   6130  C  CD  . GLU F  1 78  ? 11.504  1.890   29.265  1.00 38.06  ? 78  GLU K CD  1 
ATOM   6131  O  OE1 . GLU F  1 78  ? 10.251  1.799   29.270  1.00 38.39  ? 78  GLU K OE1 1 
ATOM   6132  O  OE2 . GLU F  1 78  ? 12.184  1.619   28.253  1.00 39.35  ? 78  GLU K OE2 1 
ATOM   6133  N  N   . ARG F  1 79  ? 12.337  -1.022  32.547  1.00 32.82  ? 79  ARG K N   1 
ATOM   6134  C  CA  . ARG F  1 79  ? 13.462  -1.880  32.901  1.00 32.18  ? 79  ARG K CA  1 
ATOM   6135  C  C   . ARG F  1 79  ? 13.482  -3.106  32.005  1.00 32.91  ? 79  ARG K C   1 
ATOM   6136  O  O   . ARG F  1 79  ? 12.476  -3.454  31.382  1.00 33.59  ? 79  ARG K O   1 
ATOM   6137  C  CB  . ARG F  1 79  ? 13.349  -2.352  34.354  1.00 30.80  ? 79  ARG K CB  1 
ATOM   6138  C  CG  . ARG F  1 79  ? 12.060  -3.107  34.638  1.00 30.58  ? 79  ARG K CG  1 
ATOM   6139  C  CD  . ARG F  1 79  ? 12.006  -3.676  36.034  1.00 29.59  ? 79  ARG K CD  1 
ATOM   6140  N  NE  . ARG F  1 79  ? 12.560  -5.021  36.092  1.00 29.41  ? 79  ARG K NE  1 
ATOM   6141  C  CZ  . ARG F  1 79  ? 12.420  -5.858  37.118  1.00 28.89  ? 79  ARG K CZ  1 
ATOM   6142  N  NH1 . ARG F  1 79  ? 11.724  -5.509  38.204  1.00 28.52  ? 79  ARG K NH1 1 
ATOM   6143  N  NH2 . ARG F  1 79  ? 12.969  -7.068  37.047  1.00 28.94  ? 79  ARG K NH2 1 
ATOM   6144  N  N   . HIS F  1 80  ? 14.630  -3.772  31.980  1.00 32.96  ? 80  HIS K N   1 
ATOM   6145  C  CA  . HIS F  1 80  ? 14.725  -5.120  31.434  1.00 33.59  ? 80  HIS K CA  1 
ATOM   6146  C  C   . HIS F  1 80  ? 14.108  -6.072  32.443  1.00 32.51  ? 80  HIS K C   1 
ATOM   6147  O  O   . HIS F  1 80  ? 14.126  -5.797  33.651  1.00 31.35  ? 80  HIS K O   1 
ATOM   6148  C  CB  . HIS F  1 80  ? 16.175  -5.541  31.217  1.00 34.22  ? 80  HIS K CB  1 
ATOM   6149  C  CG  . HIS F  1 80  ? 16.971  -4.582  30.391  1.00 35.46  ? 80  HIS K CG  1 
ATOM   6150  N  ND1 . HIS F  1 80  ? 18.292  -4.295  30.652  1.00 35.74  ? 80  HIS K ND1 1 
ATOM   6151  C  CD2 . HIS F  1 80  ? 16.626  -3.833  29.319  1.00 36.75  ? 80  HIS K CD2 1 
ATOM   6152  C  CE1 . HIS F  1 80  ? 18.730  -3.426  29.753  1.00 37.16  ? 80  HIS K CE1 1 
ATOM   6153  N  NE2 . HIS F  1 80  ? 17.740  -3.130  28.935  1.00 37.75  ? 80  HIS K NE2 1 
ATOM   6154  N  N   . VAL F  1 81  ? 13.603  -7.201  31.960  1.00 33.09  ? 81  VAL K N   1 
ATOM   6155  C  CA  . VAL F  1 81  ? 13.105  -8.249  32.841  1.00 32.36  ? 81  VAL K CA  1 
ATOM   6156  C  C   . VAL F  1 81  ? 14.214  -8.699  33.790  1.00 31.53  ? 81  VAL K C   1 
ATOM   6157  O  O   . VAL F  1 81  ? 13.967  -8.917  34.974  1.00 30.54  ? 81  VAL K O   1 
ATOM   6158  C  CB  . VAL F  1 81  ? 12.529  -9.440  32.045  1.00 33.60  ? 81  VAL K CB  1 
ATOM   6159  C  CG1 . VAL F  1 81  ? 12.234  -10.631 32.958  1.00 33.14  ? 81  VAL K CG1 1 
ATOM   6160  C  CG2 . VAL F  1 81  ? 11.258  -9.013  31.318  1.00 34.47  ? 81  VAL K CG2 1 
ATOM   6161  N  N   . GLY F  1 82  ? 15.439  -8.793  33.277  1.00 32.07  ? 82  GLY K N   1 
ATOM   6162  C  CA  . GLY F  1 82  ? 16.577  -9.210  34.082  1.00 31.67  ? 82  GLY K CA  1 
ATOM   6163  C  C   . GLY F  1 82  ? 17.188  -8.202  35.042  1.00 30.75  ? 82  GLY K C   1 
ATOM   6164  O  O   . GLY F  1 82  ? 18.196  -8.523  35.665  1.00 30.71  ? 82  GLY K O   1 
ATOM   6165  N  N   . ASP F  1 83  ? 16.612  -6.999  35.168  1.00 30.23  ? 83  ASP K N   1 
ATOM   6166  C  CA  . ASP F  1 83  ? 17.163  -5.952  36.042  1.00 29.63  ? 83  ASP K CA  1 
ATOM   6167  C  C   . ASP F  1 83  ? 16.757  -6.137  37.499  1.00 28.67  ? 83  ASP K C   1 
ATOM   6168  O  O   . ASP F  1 83  ? 15.743  -5.606  37.935  1.00 28.18  ? 83  ASP K O   1 
ATOM   6169  C  CB  . ASP F  1 83  ? 16.735  -4.553  35.562  1.00 29.80  ? 83  ASP K CB  1 
ATOM   6170  C  CG  . ASP F  1 83  ? 17.407  -4.142  34.274  1.00 31.00  ? 83  ASP K CG  1 
ATOM   6171  O  OD1 . ASP F  1 83  ? 18.283  -4.892  33.833  1.00 31.83  ? 83  ASP K OD1 1 
ATOM   6172  O  OD2 . ASP F  1 83  ? 17.073  -3.083  33.691  1.00 31.33  ? 83  ASP K OD2 1 
ATOM   6173  N  N   . LEU F  1 84  ? 17.572  -6.876  38.250  1.00 28.63  ? 84  LEU K N   1 
ATOM   6174  C  CA  . LEU F  1 84  ? 17.347  -7.078  39.681  1.00 28.05  ? 84  LEU K CA  1 
ATOM   6175  C  C   . LEU F  1 84  ? 18.140  -6.102  40.566  1.00 28.04  ? 84  LEU K C   1 
ATOM   6176  O  O   . LEU F  1 84  ? 18.124  -6.239  41.788  1.00 27.96  ? 84  LEU K O   1 
ATOM   6177  C  CB  . LEU F  1 84  ? 17.654  -8.536  40.046  1.00 28.25  ? 84  LEU K CB  1 
ATOM   6178  C  CG  . LEU F  1 84  ? 16.847  -9.574  39.258  1.00 28.51  ? 84  LEU K CG  1 
ATOM   6179  C  CD1 . LEU F  1 84  ? 17.317  -10.984 39.573  1.00 28.97  ? 84  LEU K CD1 1 
ATOM   6180  C  CD2 . LEU F  1 84  ? 15.358  -9.434  39.548  1.00 28.17  ? 84  LEU K CD2 1 
ATOM   6181  N  N   . GLY F  1 85  ? 18.811  -5.118  39.962  1.00 28.37  ? 85  GLY K N   1 
ATOM   6182  C  CA  . GLY F  1 85  ? 19.435  -4.025  40.704  1.00 28.53  ? 85  GLY K CA  1 
ATOM   6183  C  C   . GLY F  1 85  ? 20.786  -4.392  41.303  1.00 29.15  ? 85  GLY K C   1 
ATOM   6184  O  O   . GLY F  1 85  ? 21.624  -5.018  40.637  1.00 29.75  ? 85  GLY K O   1 
ATOM   6185  N  N   . ASN F  1 86  ? 20.985  -4.008  42.567  1.00 29.16  ? 86  ASN K N   1 
ATOM   6186  C  CA  . ASN F  1 86  ? 22.234  -4.255  43.265  1.00 29.97  ? 86  ASN K CA  1 
ATOM   6187  C  C   . ASN F  1 86  ? 22.049  -5.239  44.406  1.00 29.86  ? 86  ASN K C   1 
ATOM   6188  O  O   . ASN F  1 86  ? 20.937  -5.426  44.912  1.00 29.15  ? 86  ASN K O   1 
ATOM   6189  C  CB  . ASN F  1 86  ? 22.805  -2.938  43.792  1.00 30.64  ? 86  ASN K CB  1 
ATOM   6190  C  CG  . ASN F  1 86  ? 23.333  -2.059  42.680  1.00 31.23  ? 86  ASN K CG  1 
ATOM   6191  O  OD1 . ASN F  1 86  ? 24.165  -2.499  41.878  1.00 31.95  ? 86  ASN K OD1 1 
ATOM   6192  N  ND2 . ASN F  1 86  ? 22.866  -0.819  42.620  1.00 31.12  ? 86  ASN K ND2 1 
ATOM   6193  N  N   . VAL F  1 87  ? 23.161  -5.873  44.775  1.00 30.66  ? 87  VAL K N   1 
ATOM   6194  C  CA  . VAL F  1 87  ? 23.275  -6.651  45.995  1.00 31.05  ? 87  VAL K CA  1 
ATOM   6195  C  C   . VAL F  1 87  ? 24.459  -6.065  46.768  1.00 32.36  ? 87  VAL K C   1 
ATOM   6196  O  O   . VAL F  1 87  ? 25.430  -5.626  46.169  1.00 33.11  ? 87  VAL K O   1 
ATOM   6197  C  CB  . VAL F  1 87  ? 23.462  -8.166  45.733  1.00 31.21  ? 87  VAL K CB  1 
ATOM   6198  C  CG1 . VAL F  1 87  ? 22.210  -8.742  45.092  1.00 30.18  ? 87  VAL K CG1 1 
ATOM   6199  C  CG2 . VAL F  1 87  ? 24.692  -8.464  44.876  1.00 32.15  ? 87  VAL K CG2 1 
ATOM   6200  N  N   . THR F  1 88  ? 24.358  -6.053  48.091  1.00 32.88  ? 88  THR K N   1 
ATOM   6201  C  CA  . THR F  1 88  ? 25.331  -5.392  48.951  1.00 34.36  ? 88  THR K CA  1 
ATOM   6202  C  C   . THR F  1 88  ? 26.135  -6.441  49.706  1.00 35.57  ? 88  THR K C   1 
ATOM   6203  O  O   . THR F  1 88  ? 25.561  -7.278  50.412  1.00 35.46  ? 88  THR K O   1 
ATOM   6204  C  CB  . THR F  1 88  ? 24.619  -4.458  49.947  1.00 34.52  ? 88  THR K CB  1 
ATOM   6205  O  OG1 . THR F  1 88  ? 23.977  -3.399  49.228  1.00 33.66  ? 88  THR K OG1 1 
ATOM   6206  C  CG2 . THR F  1 88  ? 25.604  -3.857  50.957  1.00 36.39  ? 88  THR K CG2 1 
ATOM   6207  N  N   . ALA F  1 89  ? 27.455  -6.387  49.551  1.00 36.97  ? 89  ALA K N   1 
ATOM   6208  C  CA  . ALA F  1 89  ? 28.372  -7.251  50.296  1.00 38.57  ? 89  ALA K CA  1 
ATOM   6209  C  C   . ALA F  1 89  ? 28.829  -6.528  51.558  1.00 40.18  ? 89  ALA K C   1 
ATOM   6210  O  O   . ALA F  1 89  ? 29.059  -5.314  51.535  1.00 40.60  ? 89  ALA K O   1 
ATOM   6211  C  CB  . ALA F  1 89  ? 29.558  -7.632  49.434  1.00 39.59  ? 89  ALA K CB  1 
ATOM   6212  N  N   . ASP F  1 90  ? 28.958  -7.274  52.654  1.00 41.29  ? 90  ASP K N   1 
ATOM   6213  C  CA  . ASP F  1 90  ? 29.300  -6.700  53.960  1.00 43.13  ? 90  ASP K CA  1 
ATOM   6214  C  C   . ASP F  1 90  ? 30.830  -6.603  54.131  1.00 45.46  ? 90  ASP K C   1 
ATOM   6215  O  O   . ASP F  1 90  ? 31.579  -6.873  53.186  1.00 45.53  ? 90  ASP K O   1 
ATOM   6216  C  CB  . ASP F  1 90  ? 28.603  -7.475  55.100  1.00 43.51  ? 90  ASP K CB  1 
ATOM   6217  C  CG  . ASP F  1 90  ? 29.116  -8.910  55.276  1.00 44.35  ? 90  ASP K CG  1 
ATOM   6218  O  OD1 . ASP F  1 90  ? 30.167  -9.289  54.706  1.00 45.07  ? 90  ASP K OD1 1 
ATOM   6219  O  OD2 . ASP F  1 90  ? 28.452  -9.665  56.009  1.00 44.45  ? 90  ASP K OD2 1 
ATOM   6220  N  N   . LYS F  1 91  ? 31.287  -6.206  55.317  1.00 47.62  ? 91  LYS K N   1 
ATOM   6221  C  CA  . LYS F  1 91  ? 32.736  -6.083  55.602  1.00 50.29  ? 91  LYS K CA  1 
ATOM   6222  C  C   . LYS F  1 91  ? 33.568  -7.376  55.438  1.00 51.32  ? 91  LYS K C   1 
ATOM   6223  O  O   . LYS F  1 91  ? 34.785  -7.307  55.214  1.00 53.23  ? 91  LYS K O   1 
ATOM   6224  C  CB  . LYS F  1 91  ? 32.964  -5.477  56.996  1.00 52.67  ? 91  LYS K CB  1 
ATOM   6225  C  CG  . LYS F  1 91  ? 32.579  -6.361  58.179  1.00 53.65  ? 91  LYS K CG  1 
ATOM   6226  C  CD  . LYS F  1 91  ? 32.849  -5.649  59.505  1.00 56.35  ? 91  LYS K CD  1 
ATOM   6227  C  CE  . LYS F  1 91  ? 33.021  -6.626  60.662  1.00 58.45  ? 91  LYS K CE  1 
ATOM   6228  N  NZ  . LYS F  1 91  ? 31.843  -7.529  60.812  1.00 56.79  ? 91  LYS K NZ  1 
ATOM   6229  N  N   . ASP F  1 92  ? 32.919  -8.536  55.565  1.00 50.27  ? 92  ASP K N   1 
ATOM   6230  C  CA  . ASP F  1 92  ? 33.546  -9.845  55.303  1.00 51.04  ? 92  ASP K CA  1 
ATOM   6231  C  C   . ASP F  1 92  ? 33.419  -10.299 53.834  1.00 49.23  ? 92  ASP K C   1 
ATOM   6232  O  O   . ASP F  1 92  ? 33.785  -11.424 53.497  1.00 49.65  ? 92  ASP K O   1 
ATOM   6233  C  CB  . ASP F  1 92  ? 32.935  -10.915 56.219  1.00 51.25  ? 92  ASP K CB  1 
ATOM   6234  C  CG  . ASP F  1 92  ? 33.062  -10.579 57.707  1.00 53.44  ? 92  ASP K CG  1 
ATOM   6235  O  OD1 . ASP F  1 92  ? 34.081  -9.982  58.116  1.00 55.71  ? 92  ASP K OD1 1 
ATOM   6236  O  OD2 . ASP F  1 92  ? 32.137  -10.937 58.477  1.00 53.16  ? 92  ASP K OD2 1 
ATOM   6237  N  N   . GLY F  1 93  ? 32.905  -9.431  52.964  1.00 47.42  ? 93  GLY K N   1 
ATOM   6238  C  CA  . GLY F  1 93  ? 32.761  -9.739  51.546  1.00 46.04  ? 93  GLY K CA  1 
ATOM   6239  C  C   . GLY F  1 93  ? 31.581  -10.625 51.167  1.00 43.97  ? 93  GLY K C   1 
ATOM   6240  O  O   . GLY F  1 93  ? 31.558  -11.197 50.071  1.00 43.27  ? 93  GLY K O   1 
ATOM   6241  N  N   . VAL F  1 94  ? 30.594  -10.713 52.057  1.00 43.21  ? 94  VAL K N   1 
ATOM   6242  C  CA  . VAL F  1 94  ? 29.456  -11.611 51.893  1.00 41.68  ? 94  VAL K CA  1 
ATOM   6243  C  C   . VAL F  1 94  ? 28.210  -10.802 51.539  1.00 39.61  ? 94  VAL K C   1 
ATOM   6244  O  O   . VAL F  1 94  ? 27.850  -9.878  52.269  1.00 39.65  ? 94  VAL K O   1 
ATOM   6245  C  CB  . VAL F  1 94  ? 29.200  -12.418 53.186  1.00 42.71  ? 94  VAL K CB  1 
ATOM   6246  C  CG1 . VAL F  1 94  ? 27.922  -13.249 53.074  1.00 41.29  ? 94  VAL K CG1 1 
ATOM   6247  C  CG2 . VAL F  1 94  ? 30.393  -13.314 53.484  1.00 44.91  ? 94  VAL K CG2 1 
ATOM   6248  N  N   . ALA F  1 95  ? 27.569  -11.147 50.422  1.00 38.07  ? 95  ALA K N   1 
ATOM   6249  C  CA  . ALA F  1 95  ? 26.251  -10.613 50.072  1.00 36.27  ? 95  ALA K CA  1 
ATOM   6250  C  C   . ALA F  1 95  ? 25.191  -11.658 50.426  1.00 35.73  ? 95  ALA K C   1 
ATOM   6251  O  O   . ALA F  1 95  ? 25.097  -12.695 49.773  1.00 35.44  ? 95  ALA K O   1 
ATOM   6252  C  CB  . ALA F  1 95  ? 26.178  -10.255 48.599  1.00 35.21  ? 95  ALA K CB  1 
ATOM   6253  N  N   . ASP F  1 96  ? 24.428  -11.387 51.484  1.00 35.90  ? 96  ASP K N   1 
ATOM   6254  C  CA  . ASP F  1 96  ? 23.268  -12.213 51.852  1.00 35.61  ? 96  ASP K CA  1 
ATOM   6255  C  C   . ASP F  1 96  ? 22.047  -11.689 51.094  1.00 34.05  ? 96  ASP K C   1 
ATOM   6256  O  O   . ASP F  1 96  ? 21.325  -10.815 51.568  1.00 33.80  ? 96  ASP K O   1 
ATOM   6257  C  CB  . ASP F  1 96  ? 23.041  -12.185 53.362  1.00 36.94  ? 96  ASP K CB  1 
ATOM   6258  C  CG  . ASP F  1 96  ? 24.151  -12.894 54.135  1.00 38.83  ? 96  ASP K CG  1 
ATOM   6259  O  OD1 . ASP F  1 96  ? 24.528  -14.030 53.752  1.00 39.10  ? 96  ASP K OD1 1 
ATOM   6260  O  OD2 . ASP F  1 96  ? 24.628  -12.314 55.136  1.00 40.23  ? 96  ASP K OD2 1 
ATOM   6261  N  N   . VAL F  1 97  ? 21.829  -12.238 49.909  1.00 33.28  ? 97  VAL K N   1 
ATOM   6262  C  CA  . VAL F  1 97  ? 20.866  -11.680 48.957  1.00 32.09  ? 97  VAL K CA  1 
ATOM   6263  C  C   . VAL F  1 97  ? 19.440  -11.879 49.470  1.00 31.99  ? 97  VAL K C   1 
ATOM   6264  O  O   . VAL F  1 97  ? 19.099  -12.947 49.958  1.00 32.53  ? 97  VAL K O   1 
ATOM   6265  C  CB  . VAL F  1 97  ? 21.047  -12.298 47.548  1.00 31.59  ? 97  VAL K CB  1 
ATOM   6266  C  CG1 . VAL F  1 97  ? 19.982  -11.800 46.574  1.00 30.49  ? 97  VAL K CG1 1 
ATOM   6267  C  CG2 . VAL F  1 97  ? 22.441  -11.981 47.017  1.00 32.11  ? 97  VAL K CG2 1 
ATOM   6268  N  N   . SER F  1 98  ? 18.635  -10.823 49.392  1.00 31.61  ? 98  SER K N   1 
ATOM   6269  C  CA  . SER F  1 98  ? 17.217  -10.883 49.761  1.00 31.78  ? 98  SER K CA  1 
ATOM   6270  C  C   . SER F  1 98  ? 16.477  -9.938  48.842  1.00 31.00  ? 98  SER K C   1 
ATOM   6271  O  O   . SER F  1 98  ? 16.423  -8.725  49.089  1.00 31.09  ? 98  SER K O   1 
ATOM   6272  C  CB  . SER F  1 98  ? 17.009  -10.500 51.229  1.00 32.97  ? 98  SER K CB  1 
ATOM   6273  O  OG  . SER F  1 98  ? 15.643  -10.570 51.595  1.00 33.36  ? 98  SER K OG  1 
ATOM   6274  N  N   . ILE F  1 99  ? 15.964  -10.500 47.751  1.00 30.53  ? 99  ILE K N   1 
ATOM   6275  C  CA  . ILE F  1 99  ? 15.218  -9.756  46.740  1.00 29.93  ? 99  ILE K CA  1 
ATOM   6276  C  C   . ILE F  1 99  ? 13.855  -10.435 46.537  1.00 30.17  ? 99  ILE K C   1 
ATOM   6277  O  O   . ILE F  1 99  ? 13.726  -11.664 46.638  1.00 30.46  ? 99  ILE K O   1 
ATOM   6278  C  CB  . ILE F  1 99  ? 16.030  -9.668  45.422  1.00 29.45  ? 99  ILE K CB  1 
ATOM   6279  C  CG1 . ILE F  1 99  ? 17.165  -8.648  45.588  1.00 29.50  ? 99  ILE K CG1 1 
ATOM   6280  C  CG2 . ILE F  1 99  ? 15.152  -9.300  44.224  1.00 29.07  ? 99  ILE K CG2 1 
ATOM   6281  C  CD1 . ILE F  1 99  ? 18.252  -8.723  44.534  1.00 29.53  ? 99  ILE K CD1 1 
ATOM   6282  N  N   . GLU F  1 100 ? 12.842  -9.608  46.296  1.00 30.13  ? 100 GLU K N   1 
ATOM   6283  C  CA  . GLU F  1 100 ? 11.545  -10.069 45.825  1.00 30.50  ? 100 GLU K CA  1 
ATOM   6284  C  C   . GLU F  1 100 ? 11.206  -9.264  44.573  1.00 29.85  ? 100 GLU K C   1 
ATOM   6285  O  O   . GLU F  1 100 ? 11.289  -8.037  44.584  1.00 29.53  ? 100 GLU K O   1 
ATOM   6286  C  CB  . GLU F  1 100 ? 10.491  -9.885  46.913  1.00 31.68  ? 100 GLU K CB  1 
ATOM   6287  C  CG  . GLU F  1 100 ? 9.249   -10.728 46.693  1.00 32.70  ? 100 GLU K CG  1 
ATOM   6288  C  CD  . GLU F  1 100 ? 8.348   -10.811 47.918  1.00 34.28  ? 100 GLU K CD  1 
ATOM   6289  O  OE1 . GLU F  1 100 ? 8.846   -11.007 49.053  1.00 35.12  ? 100 GLU K OE1 1 
ATOM   6290  O  OE2 . GLU F  1 100 ? 7.131   -10.703 47.740  1.00 35.29  ? 100 GLU K OE2 1 
ATOM   6291  N  N   . ASP F  1 101 ? 10.856  -9.959  43.495  1.00 29.79  ? 101 ASP K N   1 
ATOM   6292  C  CA  . ASP F  1 101 ? 10.611  -9.316  42.202  1.00 29.54  ? 101 ASP K CA  1 
ATOM   6293  C  C   . ASP F  1 101 ? 9.440   -9.960  41.474  1.00 30.11  ? 101 ASP K C   1 
ATOM   6294  O  O   . ASP F  1 101 ? 9.346   -11.187 41.416  1.00 30.54  ? 101 ASP K O   1 
ATOM   6295  C  CB  . ASP F  1 101 ? 11.864  -9.401  41.324  1.00 29.18  ? 101 ASP K CB  1 
ATOM   6296  C  CG  . ASP F  1 101 ? 11.785  -8.483  40.122  1.00 29.26  ? 101 ASP K CG  1 
ATOM   6297  O  OD1 . ASP F  1 101 ? 12.120  -7.283  40.276  1.00 29.13  ? 101 ASP K OD1 1 
ATOM   6298  O  OD2 . ASP F  1 101 ? 11.363  -8.933  39.028  1.00 29.73  ? 101 ASP K OD2 1 
ATOM   6299  N  N   . SER F  1 102 ? 8.575   -9.124  40.898  1.00 30.22  ? 102 SER K N   1 
ATOM   6300  C  CA  . SER F  1 102 ? 7.348   -9.576  40.234  1.00 31.11  ? 102 SER K CA  1 
ATOM   6301  C  C   . SER F  1 102 ? 7.381   -9.443  38.714  1.00 31.22  ? 102 SER K C   1 
ATOM   6302  O  O   . SER F  1 102 ? 6.347   -9.604  38.071  1.00 32.19  ? 102 SER K O   1 
ATOM   6303  C  CB  . SER F  1 102 ? 6.154   -8.793  40.784  1.00 31.84  ? 102 SER K CB  1 
ATOM   6304  O  OG  . SER F  1 102 ? 5.998   -9.064  42.164  1.00 32.13  ? 102 SER K OG  1 
ATOM   6305  N  N   . VAL F  1 103 ? 8.559   -9.152  38.151  1.00 30.38  ? 103 VAL K N   1 
ATOM   6306  C  CA  . VAL F  1 103 ? 8.736   -9.018  36.704  1.00 30.77  ? 103 VAL K CA  1 
ATOM   6307  C  C   . VAL F  1 103 ? 9.411   -10.273 36.152  1.00 31.05  ? 103 VAL K C   1 
ATOM   6308  O  O   . VAL F  1 103 ? 8.954   -10.820 35.152  1.00 32.15  ? 103 VAL K O   1 
ATOM   6309  C  CB  . VAL F  1 103 ? 9.520   -7.740  36.352  1.00 30.25  ? 103 VAL K CB  1 
ATOM   6310  C  CG1 . VAL F  1 103 ? 9.863   -7.694  34.866  1.00 31.06  ? 103 VAL K CG1 1 
ATOM   6311  C  CG2 . VAL F  1 103 ? 8.712   -6.511  36.757  1.00 30.27  ? 103 VAL K CG2 1 
ATOM   6312  N  N   . ILE F  1 104 ? 10.483  -10.735 36.797  1.00 30.31  ? 104 ILE K N   1 
ATOM   6313  C  CA  . ILE F  1 104 ? 10.999  -12.085 36.513  1.00 30.80  ? 104 ILE K CA  1 
ATOM   6314  C  C   . ILE F  1 104 ? 9.942   -13.113 36.898  1.00 31.43  ? 104 ILE K C   1 
ATOM   6315  O  O   . ILE F  1 104 ? 9.080   -12.849 37.737  1.00 31.27  ? 104 ILE K O   1 
ATOM   6316  C  CB  . ILE F  1 104 ? 12.334  -12.427 37.233  1.00 30.17  ? 104 ILE K CB  1 
ATOM   6317  C  CG1 . ILE F  1 104 ? 12.200  -12.363 38.759  1.00 29.48  ? 104 ILE K CG1 1 
ATOM   6318  C  CG2 . ILE F  1 104 ? 13.442  -11.503 36.762  1.00 29.88  ? 104 ILE K CG2 1 
ATOM   6319  C  CD1 . ILE F  1 104 ? 13.351  -12.997 39.509  1.00 29.32  ? 104 ILE K CD1 1 
ATOM   6320  N  N   . SER F  1 105 ? 10.021  -14.278 36.273  1.00 32.37  ? 105 SER K N   1 
ATOM   6321  C  CA  . SER F  1 105 ? 9.153   -15.390 36.603  1.00 33.26  ? 105 SER K CA  1 
ATOM   6322  C  C   . SER F  1 105 ? 9.911   -16.700 36.414  1.00 33.96  ? 105 SER K C   1 
ATOM   6323  O  O   . SER F  1 105 ? 10.987  -16.713 35.812  1.00 33.91  ? 105 SER K O   1 
ATOM   6324  C  CB  . SER F  1 105 ? 7.908   -15.348 35.721  1.00 34.47  ? 105 SER K CB  1 
ATOM   6325  O  OG  . SER F  1 105 ? 6.932   -16.240 36.200  1.00 35.41  ? 105 SER K OG  1 
ATOM   6326  N  N   . LEU F  1 106 ? 9.346   -17.779 36.955  1.00 34.81  ? 106 LEU K N   1 
ATOM   6327  C  CA  . LEU F  1 106 ? 9.840   -19.146 36.749  1.00 35.91  ? 106 LEU K CA  1 
ATOM   6328  C  C   . LEU F  1 106 ? 8.910   -19.958 35.826  1.00 37.86  ? 106 LEU K C   1 
ATOM   6329  O  O   . LEU F  1 106 ? 8.958   -21.194 35.812  1.00 39.07  ? 106 LEU K O   1 
ATOM   6330  C  CB  . LEU F  1 106 ? 10.031  -19.854 38.102  1.00 35.68  ? 106 LEU K CB  1 
ATOM   6331  C  CG  . LEU F  1 106 ? 10.894  -19.131 39.144  1.00 34.19  ? 106 LEU K CG  1 
ATOM   6332  C  CD1 . LEU F  1 106 ? 10.988  -19.945 40.428  1.00 34.48  ? 106 LEU K CD1 1 
ATOM   6333  C  CD2 . LEU F  1 106 ? 12.289  -18.829 38.622  1.00 33.68  ? 106 LEU K CD2 1 
ATOM   6334  N  N   . SER F  1 107 ? 8.075   -19.251 35.060  1.00 38.39  ? 107 SER K N   1 
ATOM   6335  C  CA  . SER F  1 107 ? 7.262   -19.834 33.995  1.00 40.47  ? 107 SER K CA  1 
ATOM   6336  C  C   . SER F  1 107 ? 6.843   -18.734 33.004  1.00 40.76  ? 107 SER K C   1 
ATOM   6337  O  O   . SER F  1 107 ? 6.917   -17.542 33.325  1.00 39.40  ? 107 SER K O   1 
ATOM   6338  C  CB  . SER F  1 107 ? 6.019   -20.506 34.576  1.00 41.61  ? 107 SER K CB  1 
ATOM   6339  O  OG  . SER F  1 107 ? 5.136   -19.547 35.136  1.00 41.05  ? 107 SER K OG  1 
ATOM   6340  N  N   . GLY F  1 108 ? 6.418   -19.142 31.810  1.00 42.78  ? 108 GLY K N   1 
ATOM   6341  C  CA  . GLY F  1 108 ? 5.932   -18.217 30.785  1.00 43.59  ? 108 GLY K CA  1 
ATOM   6342  C  C   . GLY F  1 108 ? 7.029   -17.449 30.064  1.00 43.11  ? 108 GLY K C   1 
ATOM   6343  O  O   . GLY F  1 108 ? 8.204   -17.811 30.140  1.00 42.64  ? 108 GLY K O   1 
ATOM   6344  N  N   . ASP F  1 109 ? 6.642   -16.365 29.396  1.00 43.42  ? 109 ASP K N   1 
ATOM   6345  C  CA  . ASP F  1 109 ? 7.554   -15.581 28.544  1.00 43.49  ? 109 ASP K CA  1 
ATOM   6346  C  C   . ASP F  1 109 ? 8.697   -14.915 29.296  1.00 41.42  ? 109 ASP K C   1 
ATOM   6347  O  O   . ASP F  1 109 ? 9.758   -14.687 28.723  1.00 41.63  ? 109 ASP K O   1 
ATOM   6348  C  CB  . ASP F  1 109 ? 6.787   -14.485 27.788  1.00 44.30  ? 109 ASP K CB  1 
ATOM   6349  C  CG  . ASP F  1 109 ? 5.777   -15.037 26.811  1.00 46.89  ? 109 ASP K CG  1 
ATOM   6350  O  OD1 . ASP F  1 109 ? 5.865   -16.226 26.443  1.00 48.36  ? 109 ASP K OD1 1 
ATOM   6351  O  OD2 . ASP F  1 109 ? 4.883   -14.271 26.403  1.00 47.74  ? 109 ASP K OD2 1 
ATOM   6352  N  N   . HIS F  1 110 ? 8.474   -14.587 30.567  1.00 39.75  ? 110 HIS K N   1 
ATOM   6353  C  CA  . HIS F  1 110 ? 9.489   -13.938 31.388  1.00 37.93  ? 110 HIS K CA  1 
ATOM   6354  C  C   . HIS F  1 110 ? 10.237  -14.954 32.253  1.00 37.27  ? 110 HIS K C   1 
ATOM   6355  O  O   . HIS F  1 110 ? 10.884  -14.570 33.228  1.00 35.79  ? 110 HIS K O   1 
ATOM   6356  C  CB  . HIS F  1 110 ? 8.842   -12.856 32.258  1.00 36.79  ? 110 HIS K CB  1 
ATOM   6357  C  CG  . HIS F  1 110 ? 8.324   -11.683 31.483  1.00 37.38  ? 110 HIS K CG  1 
ATOM   6358  N  ND1 . HIS F  1 110 ? 8.036   -10.475 32.081  1.00 36.48  ? 110 HIS K ND1 1 
ATOM   6359  C  CD2 . HIS F  1 110 ? 8.065   -11.521 30.163  1.00 39.07  ? 110 HIS K CD2 1 
ATOM   6360  C  CE1 . HIS F  1 110 ? 7.603   -9.626  31.166  1.00 37.41  ? 110 HIS K CE1 1 
ATOM   6361  N  NE2 . HIS F  1 110 ? 7.614   -10.234 29.993  1.00 39.01  ? 110 HIS K NE2 1 
ATOM   6362  N  N   . CYS F  1 111 ? 10.163  -16.239 31.888  1.00 38.53  ? 111 CYS K N   1 
ATOM   6363  C  CA  . CYS F  1 111 ? 10.858  -17.288 32.614  1.00 38.30  ? 111 CYS K CA  1 
ATOM   6364  C  C   . CYS F  1 111 ? 12.363  -17.085 32.508  1.00 37.83  ? 111 CYS K C   1 
ATOM   6365  O  O   . CYS F  1 111 ? 12.872  -16.796 31.430  1.00 38.78  ? 111 CYS K O   1 
ATOM   6366  C  CB  . CYS F  1 111 ? 10.478  -18.679 32.104  1.00 40.16  ? 111 CYS K CB  1 
ATOM   6367  S  SG  . CYS F  1 111 ? 11.112  -20.028 33.123  1.00 40.14  ? 111 CYS K SG  1 
ATOM   6368  N  N   . ILE F  1 112 ? 13.047  -17.219 33.642  1.00 36.59  ? 112 ILE K N   1 
ATOM   6369  C  CA  . ILE F  1 112 ? 14.506  -17.069 33.721  1.00 36.33  ? 112 ILE K CA  1 
ATOM   6370  C  C   . ILE F  1 112 ? 15.248  -18.403 33.885  1.00 37.25  ? 112 ILE K C   1 
ATOM   6371  O  O   . ILE F  1 112 ? 16.478  -18.416 33.955  1.00 37.41  ? 112 ILE K O   1 
ATOM   6372  C  CB  . ILE F  1 112 ? 14.924  -16.085 34.846  1.00 34.60  ? 112 ILE K CB  1 
ATOM   6373  C  CG1 . ILE F  1 112 ? 14.483  -16.566 36.235  1.00 33.82  ? 112 ILE K CG1 1 
ATOM   6374  C  CG2 . ILE F  1 112 ? 14.353  -14.694 34.561  1.00 33.93  ? 112 ILE K CG2 1 
ATOM   6375  C  CD1 . ILE F  1 112 ? 15.016  -15.714 37.360  1.00 32.52  ? 112 ILE K CD1 1 
ATOM   6376  N  N   . ILE F  1 113 ? 14.513  -19.511 33.948  1.00 38.01  ? 113 ILE K N   1 
ATOM   6377  C  CA  . ILE F  1 113 ? 15.121  -20.834 33.967  1.00 39.28  ? 113 ILE K CA  1 
ATOM   6378  C  C   . ILE F  1 113 ? 15.799  -21.083 32.616  1.00 41.02  ? 113 ILE K C   1 
ATOM   6379  O  O   . ILE F  1 113 ? 15.216  -20.826 31.562  1.00 41.92  ? 113 ILE K O   1 
ATOM   6380  C  CB  . ILE F  1 113 ? 14.084  -21.925 34.335  1.00 40.03  ? 113 ILE K CB  1 
ATOM   6381  C  CG1 . ILE F  1 113 ? 13.776  -21.842 35.840  1.00 38.67  ? 113 ILE K CG1 1 
ATOM   6382  C  CG2 . ILE F  1 113 ? 14.589  -23.318 33.989  1.00 41.93  ? 113 ILE K CG2 1 
ATOM   6383  C  CD1 . ILE F  1 113 ? 12.464  -22.476 36.255  1.00 39.24  ? 113 ILE K CD1 1 
ATOM   6384  N  N   . GLY F  1 114 ? 17.044  -21.556 32.668  1.00 41.69  ? 114 GLY K N   1 
ATOM   6385  C  CA  . GLY F  1 114 ? 17.860  -21.762 31.474  1.00 43.66  ? 114 GLY K CA  1 
ATOM   6386  C  C   . GLY F  1 114 ? 18.596  -20.525 30.992  1.00 43.32  ? 114 GLY K C   1 
ATOM   6387  O  O   . GLY F  1 114 ? 19.176  -20.541 29.912  1.00 45.17  ? 114 GLY K O   1 
ATOM   6388  N  N   . ARG F  1 115 ? 18.575  -19.457 31.789  1.00 41.22  ? 115 ARG K N   1 
ATOM   6389  C  CA  . ARG F  1 115 ? 19.288  -18.223 31.491  1.00 40.87  ? 115 ARG K CA  1 
ATOM   6390  C  C   . ARG F  1 115 ? 20.379  -18.049 32.541  1.00 40.05  ? 115 ARG K C   1 
ATOM   6391  O  O   . ARG F  1 115 ? 20.555  -18.929 33.372  1.00 39.91  ? 115 ARG K O   1 
ATOM   6392  C  CB  . ARG F  1 115 ? 18.302  -17.059 31.456  1.00 39.48  ? 115 ARG K CB  1 
ATOM   6393  C  CG  . ARG F  1 115 ? 17.225  -17.262 30.401  1.00 40.60  ? 115 ARG K CG  1 
ATOM   6394  C  CD  . ARG F  1 115 ? 16.436  -15.997 30.116  1.00 39.76  ? 115 ARG K CD  1 
ATOM   6395  N  NE  . ARG F  1 115 ? 15.276  -16.298 29.274  1.00 40.90  ? 115 ARG K NE  1 
ATOM   6396  C  CZ  . ARG F  1 115 ? 15.270  -16.349 27.939  1.00 43.00  ? 115 ARG K CZ  1 
ATOM   6397  N  NH1 . ARG F  1 115 ? 16.364  -16.092 27.217  1.00 44.28  ? 115 ARG K NH1 1 
ATOM   6398  N  NH2 . ARG F  1 115 ? 14.138  -16.651 27.311  1.00 44.09  ? 115 ARG K NH2 1 
ATOM   6399  N  N   . THR F  1 116 ? 21.138  -16.953 32.484  1.00 39.78  ? 116 THR K N   1 
ATOM   6400  C  CA  . THR F  1 116 ? 22.330  -16.807 33.329  1.00 39.64  ? 116 THR K CA  1 
ATOM   6401  C  C   . THR F  1 116 ? 22.202  -15.667 34.322  1.00 37.69  ? 116 THR K C   1 
ATOM   6402  O  O   . THR F  1 116 ? 21.926  -14.532 33.934  1.00 37.23  ? 116 THR K O   1 
ATOM   6403  C  CB  . THR F  1 116 ? 23.601  -16.595 32.487  1.00 41.64  ? 116 THR K CB  1 
ATOM   6404  O  OG1 . THR F  1 116 ? 23.814  -17.741 31.667  1.00 43.72  ? 116 THR K OG1 1 
ATOM   6405  C  CG2 . THR F  1 116 ? 24.834  -16.406 33.357  1.00 41.78  ? 116 THR K CG2 1 
ATOM   6406  N  N   . LEU F  1 117 ? 22.418  -15.983 35.598  1.00 36.83  ? 117 LEU K N   1 
ATOM   6407  C  CA  . LEU F  1 117 ? 22.518  -14.981 36.650  1.00 35.38  ? 117 LEU K CA  1 
ATOM   6408  C  C   . LEU F  1 117 ? 23.970  -14.527 36.723  1.00 36.36  ? 117 LEU K C   1 
ATOM   6409  O  O   . LEU F  1 117 ? 24.874  -15.361 36.723  1.00 37.72  ? 117 LEU K O   1 
ATOM   6410  C  CB  . LEU F  1 117 ? 22.089  -15.570 37.995  1.00 34.43  ? 117 LEU K CB  1 
ATOM   6411  C  CG  . LEU F  1 117 ? 22.045  -14.592 39.172  1.00 33.20  ? 117 LEU K CG  1 
ATOM   6412  C  CD1 . LEU F  1 117 ? 20.997  -13.506 38.951  1.00 32.01  ? 117 LEU K CD1 1 
ATOM   6413  C  CD2 . LEU F  1 117 ? 21.781  -15.344 40.466  1.00 32.90  ? 117 LEU K CD2 1 
ATOM   6414  N  N   . VAL F  1 118 ? 24.182  -13.213 36.801  1.00 35.81  ? 118 VAL K N   1 
ATOM   6415  C  CA  . VAL F  1 118 ? 25.522  -12.629 36.837  1.00 36.96  ? 118 VAL K CA  1 
ATOM   6416  C  C   . VAL F  1 118 ? 25.623  -11.624 37.973  1.00 35.92  ? 118 VAL K C   1 
ATOM   6417  O  O   . VAL F  1 118 ? 24.729  -10.794 38.147  1.00 34.57  ? 118 VAL K O   1 
ATOM   6418  C  CB  . VAL F  1 118 ? 25.856  -11.911 35.512  1.00 38.11  ? 118 VAL K CB  1 
ATOM   6419  C  CG1 . VAL F  1 118 ? 27.257  -11.296 35.557  1.00 39.59  ? 118 VAL K CG1 1 
ATOM   6420  C  CG2 . VAL F  1 118 ? 25.718  -12.875 34.339  1.00 39.50  ? 118 VAL K CG2 1 
ATOM   6421  N  N   . VAL F  1 119 ? 26.717  -11.697 38.730  1.00 36.81  ? 119 VAL K N   1 
ATOM   6422  C  CA  . VAL F  1 119 ? 27.037  -10.682 39.742  1.00 36.41  ? 119 VAL K CA  1 
ATOM   6423  C  C   . VAL F  1 119 ? 28.228  -9.865  39.231  1.00 38.09  ? 119 VAL K C   1 
ATOM   6424  O  O   . VAL F  1 119 ? 29.213  -10.425 38.731  1.00 39.90  ? 119 VAL K O   1 
ATOM   6425  C  CB  . VAL F  1 119 ? 27.274  -11.284 41.158  1.00 36.35  ? 119 VAL K CB  1 
ATOM   6426  C  CG1 . VAL F  1 119 ? 28.366  -12.347 41.170  1.00 38.17  ? 119 VAL K CG1 1 
ATOM   6427  C  CG2 . VAL F  1 119 ? 27.577  -10.191 42.172  1.00 36.18  ? 119 VAL K CG2 1 
ATOM   6428  N  N   . HIS F  1 120 ? 28.128  -8.543  39.353  1.00 37.70  ? 120 HIS K N   1 
ATOM   6429  C  CA  . HIS F  1 120 ? 29.070  -7.626  38.688  1.00 39.32  ? 120 HIS K CA  1 
ATOM   6430  C  C   . HIS F  1 120 ? 30.080  -6.977  39.632  1.00 40.38  ? 120 HIS K C   1 
ATOM   6431  O  O   . HIS F  1 120 ? 29.929  -7.016  40.860  1.00 39.56  ? 120 HIS K O   1 
ATOM   6432  C  CB  . HIS F  1 120 ? 28.294  -6.548  37.924  1.00 38.58  ? 120 HIS K CB  1 
ATOM   6433  C  CG  . HIS F  1 120 ? 27.661  -7.041  36.660  1.00 38.63  ? 120 HIS K CG  1 
ATOM   6434  N  ND1 . HIS F  1 120 ? 28.248  -6.877  35.424  1.00 40.48  ? 120 HIS K ND1 1 
ATOM   6435  C  CD2 . HIS F  1 120 ? 26.487  -7.679  36.438  1.00 37.36  ? 120 HIS K CD2 1 
ATOM   6436  C  CE1 . HIS F  1 120 ? 27.467  -7.401  34.497  1.00 40.34  ? 120 HIS K CE1 1 
ATOM   6437  N  NE2 . HIS F  1 120 ? 26.395  -7.900  35.085  1.00 38.42  ? 120 HIS K NE2 1 
ATOM   6438  N  N   . GLU F  1 121 ? 31.102  -6.378  39.012  1.00 42.40  ? 121 GLU K N   1 
ATOM   6439  C  CA  . GLU F  1 121 ? 32.235  -5.739  39.683  1.00 44.12  ? 121 GLU K CA  1 
ATOM   6440  C  C   . GLU F  1 121 ? 31.842  -4.578  40.586  1.00 43.12  ? 121 GLU K C   1 
ATOM   6441  O  O   . GLU F  1 121 ? 32.354  -4.452  41.694  1.00 43.73  ? 121 GLU K O   1 
ATOM   6442  C  CB  . GLU F  1 121 ? 33.245  -5.247  38.624  1.00 46.64  ? 121 GLU K CB  1 
ATOM   6443  C  CG  . GLU F  1 121 ? 34.451  -4.467  39.147  1.00 48.84  ? 121 GLU K CG  1 
ATOM   6444  C  CD  . GLU F  1 121 ? 35.352  -3.935  38.039  1.00 51.50  ? 121 GLU K CD  1 
ATOM   6445  O  OE1 . GLU F  1 121 ? 34.842  -3.497  36.989  1.00 51.25  ? 121 GLU K OE1 1 
ATOM   6446  O  OE2 . GLU F  1 121 ? 36.586  -3.938  38.221  1.00 54.22  ? 121 GLU K OE2 1 
ATOM   6447  N  N   . LYS F  1 122 ? 30.972  -3.706  40.095  1.00 41.93  ? 122 LYS K N   1 
ATOM   6448  C  CA  . LYS F  1 122 ? 30.585  -2.511  40.846  1.00 41.28  ? 122 LYS K CA  1 
ATOM   6449  C  C   . LYS F  1 122 ? 29.081  -2.259  40.754  1.00 38.97  ? 122 LYS K C   1 
ATOM   6450  O  O   . LYS F  1 122 ? 28.349  -3.061  40.168  1.00 37.87  ? 122 LYS K O   1 
ATOM   6451  C  CB  . LYS F  1 122 ? 31.413  -1.309  40.383  1.00 43.20  ? 122 LYS K CB  1 
ATOM   6452  C  CG  . LYS F  1 122 ? 31.378  -1.017  38.892  1.00 43.92  ? 122 LYS K CG  1 
ATOM   6453  C  CD  . LYS F  1 122 ? 32.370  0.085   38.538  0.50 46.25  ? 122 LYS K CD  1 
ATOM   6454  C  CE  . LYS F  1 122 ? 32.586  0.181   37.039  0.50 47.65  ? 122 LYS K CE  1 
ATOM   6455  N  NZ  . LYS F  1 122 ? 33.573  1.239   36.691  0.50 50.25  ? 122 LYS K NZ  1 
ATOM   6456  N  N   . ALA F  1 123 ? 28.642  -1.160  41.369  1.00 38.42  ? 123 ALA K N   1 
ATOM   6457  C  CA  . ALA F  1 123 ? 27.234  -0.811  41.479  1.00 36.55  ? 123 ALA K CA  1 
ATOM   6458  C  C   . ALA F  1 123 ? 26.586  -0.584  40.119  1.00 36.03  ? 123 ALA K C   1 
ATOM   6459  O  O   . ALA F  1 123 ? 27.165  0.050   39.240  1.00 37.37  ? 123 ALA K O   1 
ATOM   6460  C  CB  . ALA F  1 123 ? 27.072  0.437   42.345  1.00 36.71  ? 123 ALA K CB  1 
ATOM   6461  N  N   . ASP F  1 124 ? 25.398  -1.154  39.956  1.00 34.38  ? 124 ASP K N   1 
ATOM   6462  C  CA  . ASP F  1 124 ? 24.469  -0.800  38.885  1.00 33.74  ? 124 ASP K CA  1 
ATOM   6463  C  C   . ASP F  1 124 ? 23.951  0.604   39.195  1.00 33.38  ? 124 ASP K C   1 
ATOM   6464  O  O   . ASP F  1 124 ? 23.485  0.851   40.307  1.00 32.73  ? 124 ASP K O   1 
ATOM   6465  C  CB  . ASP F  1 124 ? 23.328  -1.826  38.882  1.00 32.43  ? 124 ASP K CB  1 
ATOM   6466  C  CG  . ASP F  1 124 ? 22.385  -1.699  37.692  1.00 32.22  ? 124 ASP K CG  1 
ATOM   6467  O  OD1 . ASP F  1 124 ? 22.244  -0.609  37.099  1.00 32.64  ? 124 ASP K OD1 1 
ATOM   6468  O  OD2 . ASP F  1 124 ? 21.745  -2.723  37.374  1.00 31.75  ? 124 ASP K OD2 1 
ATOM   6469  N  N   . ASP F  1 125 ? 24.038  1.523   38.230  1.00 34.03  ? 125 ASP K N   1 
ATOM   6470  C  CA  . ASP F  1 125 ? 23.517  2.894   38.416  1.00 33.93  ? 125 ASP K CA  1 
ATOM   6471  C  C   . ASP F  1 125 ? 21.999  3.025   38.167  1.00 32.61  ? 125 ASP K C   1 
ATOM   6472  O  O   . ASP F  1 125 ? 21.443  4.127   38.270  1.00 32.68  ? 125 ASP K O   1 
ATOM   6473  C  CB  . ASP F  1 125 ? 24.326  3.936   37.599  1.00 35.67  ? 125 ASP K CB  1 
ATOM   6474  C  CG  . ASP F  1 125 ? 24.118  3.840   36.076  1.00 36.28  ? 125 ASP K CG  1 
ATOM   6475  O  OD1 . ASP F  1 125 ? 23.126  3.245   35.599  1.00 35.29  ? 125 ASP K OD1 1 
ATOM   6476  O  OD2 . ASP F  1 125 ? 24.957  4.403   35.344  1.00 37.98  ? 125 ASP K OD2 1 
ATOM   6477  N  N   . LEU F  1 126 ? 21.357  1.911   37.802  1.00 31.63  ? 126 LEU K N   1 
ATOM   6478  C  CA  . LEU F  1 126 ? 19.892  1.791   37.723  1.00 30.54  ? 126 LEU K CA  1 
ATOM   6479  C  C   . LEU F  1 126 ? 19.297  2.665   36.608  1.00 31.04  ? 126 LEU K C   1 
ATOM   6480  O  O   . LEU F  1 126 ? 18.157  3.096   36.690  1.00 30.55  ? 126 LEU K O   1 
ATOM   6481  C  CB  . LEU F  1 126 ? 19.237  2.089   39.088  1.00 29.80  ? 126 LEU K CB  1 
ATOM   6482  C  CG  . LEU F  1 126 ? 19.825  1.382   40.323  1.00 29.52  ? 126 LEU K CG  1 
ATOM   6483  C  CD1 . LEU F  1 126 ? 19.038  1.723   41.575  1.00 29.13  ? 126 LEU K CD1 1 
ATOM   6484  C  CD2 . LEU F  1 126 ? 19.891  -0.126  40.153  1.00 29.03  ? 126 LEU K CD2 1 
ATOM   6485  N  N   . GLY F  1 127 ? 20.088  2.910   35.560  1.00 32.19  ? 127 GLY K N   1 
ATOM   6486  C  CA  . GLY F  1 127 ? 19.666  3.733   34.434  1.00 33.08  ? 127 GLY K CA  1 
ATOM   6487  C  C   . GLY F  1 127 ? 19.726  5.231   34.660  1.00 33.72  ? 127 GLY K C   1 
ATOM   6488  O  O   . GLY F  1 127 ? 19.285  5.988   33.808  1.00 34.57  ? 127 GLY K O   1 
ATOM   6489  N  N   . LYS F  1 128 ? 20.307  5.662   35.777  1.00 33.57  ? 128 LYS K N   1 
ATOM   6490  C  CA  . LYS F  1 128 ? 20.307  7.071   36.178  1.00 34.32  ? 128 LYS K CA  1 
ATOM   6491  C  C   . LYS F  1 128 ? 21.639  7.807   35.929  1.00 35.98  ? 128 LYS K C   1 
ATOM   6492  O  O   . LYS F  1 128 ? 21.827  8.929   36.398  1.00 36.72  ? 128 LYS K O   1 
ATOM   6493  C  CB  . LYS F  1 128 ? 19.905  7.158   37.653  1.00 33.44  ? 128 LYS K CB  1 
ATOM   6494  C  CG  . LYS F  1 128 ? 18.531  6.551   37.925  1.00 32.19  ? 128 LYS K CG  1 
ATOM   6495  C  CD  . LYS F  1 128 ? 18.234  6.437   39.407  1.00 31.62  ? 128 LYS K CD  1 
ATOM   6496  C  CE  . LYS F  1 128 ? 17.843  7.769   40.006  1.00 32.43  ? 128 LYS K CE  1 
ATOM   6497  N  NZ  . LYS F  1 128 ? 17.336  7.585   41.391  1.00 32.12  ? 128 LYS K NZ  1 
ATOM   6498  N  N   . GLY F  1 129 ? 22.538  7.188   35.168  1.00 36.82  ? 129 GLY K N   1 
ATOM   6499  C  CA  . GLY F  1 129 ? 23.880  7.732   34.924  1.00 38.78  ? 129 GLY K CA  1 
ATOM   6500  C  C   . GLY F  1 129 ? 24.021  8.781   33.833  1.00 40.67  ? 129 GLY K C   1 
ATOM   6501  O  O   . GLY F  1 129 ? 25.087  9.383   33.699  1.00 42.48  ? 129 GLY K O   1 
ATOM   6502  N  N   . GLY F  1 130 ? 22.971  8.988   33.035  1.00 40.52  ? 130 GLY K N   1 
ATOM   6503  C  CA  . GLY F  1 130 ? 22.963  10.017  32.004  1.00 42.47  ? 130 GLY K CA  1 
ATOM   6504  C  C   . GLY F  1 130 ? 23.851  9.786   30.787  1.00 44.66  ? 130 GLY K C   1 
ATOM   6505  O  O   . GLY F  1 130 ? 24.188  10.742  30.095  1.00 46.63  ? 130 GLY K O   1 
ATOM   6506  N  N   . ASN F  1 131 ? 24.228  8.531   30.529  1.00 44.57  ? 131 ASN K N   1 
ATOM   6507  C  CA  . ASN F  1 131 ? 24.943  8.153   29.306  1.00 46.92  ? 131 ASN K CA  1 
ATOM   6508  C  C   . ASN F  1 131 ? 24.302  6.933   28.654  1.00 46.37  ? 131 ASN K C   1 
ATOM   6509  O  O   . ASN F  1 131 ? 23.447  6.281   29.257  1.00 44.07  ? 131 ASN K O   1 
ATOM   6510  C  CB  . ASN F  1 131 ? 26.453  7.954   29.559  1.00 48.42  ? 131 ASN K CB  1 
ATOM   6511  C  CG  . ASN F  1 131 ? 26.776  6.897   30.615  1.00 46.76  ? 131 ASN K CG  1 
ATOM   6512  O  OD1 . ASN F  1 131 ? 26.021  5.959   30.858  1.00 44.80  ? 131 ASN K OD1 1 
ATOM   6513  N  ND2 . ASN F  1 131 ? 27.946  7.038   31.223  1.00 47.84  ? 131 ASN K ND2 1 
ATOM   6514  N  N   . GLU F  1 132 ? 24.729  6.632   27.426  1.00 48.79  ? 132 GLU K N   1 
ATOM   6515  C  CA  . GLU F  1 132 ? 24.197  5.495   26.648  1.00 48.94  ? 132 GLU K CA  1 
ATOM   6516  C  C   . GLU F  1 132 ? 24.328  4.192   27.413  1.00 47.30  ? 132 GLU K C   1 
ATOM   6517  O  O   . GLU F  1 132 ? 23.409  3.373   27.421  1.00 45.92  ? 132 GLU K O   1 
ATOM   6518  C  CB  . GLU F  1 132 ? 24.931  5.309   25.304  1.00 52.17  ? 132 GLU K CB  1 
ATOM   6519  C  CG  . GLU F  1 132 ? 24.808  6.445   24.307  1.00 54.58  ? 132 GLU K CG  1 
ATOM   6520  C  CD  . GLU F  1 132 ? 25.961  7.430   24.387  1.00 56.65  ? 132 GLU K CD  1 
ATOM   6521  O  OE1 . GLU F  1 132 ? 26.333  7.785   25.530  1.00 55.32  ? 132 GLU K OE1 1 
ATOM   6522  O  OE2 . GLU F  1 132 ? 26.488  7.841   23.321  1.00 59.82  ? 132 GLU K OE2 1 
ATOM   6523  N  N   . GLU F  1 133 ? 25.481  4.023   28.057  1.00 47.81  ? 133 GLU K N   1 
ATOM   6524  C  CA  . GLU F  1 133 ? 25.811  2.813   28.798  1.00 46.73  ? 133 GLU K CA  1 
ATOM   6525  C  C   . GLU F  1 133 ? 24.897  2.607   30.016  1.00 43.79  ? 133 GLU K C   1 
ATOM   6526  O  O   . GLU F  1 133 ? 24.582  1.465   30.367  1.00 42.44  ? 133 GLU K O   1 
ATOM   6527  C  CB  . GLU F  1 133 ? 27.280  2.857   29.244  1.00 48.27  ? 133 GLU K CB  1 
ATOM   6528  C  CG  . GLU F  1 133 ? 27.840  1.522   29.712  1.00 48.01  ? 133 GLU K CG  1 
ATOM   6529  C  CD  . GLU F  1 133 ? 27.923  0.486   28.602  1.00 49.54  ? 133 GLU K CD  1 
ATOM   6530  O  OE1 . GLU F  1 133 ? 28.024  0.881   27.422  1.00 51.75  ? 133 GLU K OE1 1 
ATOM   6531  O  OE2 . GLU F  1 133 ? 27.878  -0.726  28.922  1.00 48.80  ? 133 GLU K OE2 1 
ATOM   6532  N  N   . SER F  1 134 ? 24.467  3.702   30.644  1.00 43.00  ? 134 SER K N   1 
ATOM   6533  C  CA  . SER F  1 134 ? 23.513  3.624   31.766  1.00 40.63  ? 134 SER K CA  1 
ATOM   6534  C  C   . SER F  1 134 ? 22.206  2.952   31.341  1.00 39.63  ? 134 SER K C   1 
ATOM   6535  O  O   . SER F  1 134 ? 21.693  2.076   32.050  1.00 37.98  ? 134 SER K O   1 
ATOM   6536  C  CB  . SER F  1 134 ? 23.229  5.012   32.345  1.00 40.40  ? 134 SER K CB  1 
ATOM   6537  O  OG  . SER F  1 134 ? 22.491  4.918   33.554  1.00 38.40  ? 134 SER K OG  1 
ATOM   6538  N  N   . THR F  1 135 ? 21.706  3.339   30.166  1.00 40.92  ? 135 THR K N   1 
ATOM   6539  C  CA  . THR F  1 135 ? 20.464  2.794   29.611  1.00 40.56  ? 135 THR K CA  1 
ATOM   6540  C  C   . THR F  1 135 ? 20.595  1.394   28.984  1.00 41.11  ? 135 THR K C   1 
ATOM   6541  O  O   . THR F  1 135 ? 19.588  0.850   28.520  1.00 40.85  ? 135 THR K O   1 
ATOM   6542  C  CB  . THR F  1 135 ? 19.856  3.750   28.558  1.00 42.03  ? 135 THR K CB  1 
ATOM   6543  O  OG1 . THR F  1 135 ? 20.801  3.993   27.511  1.00 44.50  ? 135 THR K OG1 1 
ATOM   6544  C  CG2 . THR F  1 135 ? 19.486  5.070   29.183  1.00 41.62  ? 135 THR K CG2 1 
ATOM   6545  N  N   . LYS F  1 136 ? 21.807  0.822   28.968  1.00 42.13  ? 136 LYS K N   1 
ATOM   6546  C  CA  . LYS F  1 136 ? 22.059  -0.549  28.481  1.00 42.85  ? 136 LYS K CA  1 
ATOM   6547  C  C   . LYS F  1 136 ? 22.470  -1.524  29.580  1.00 41.62  ? 136 LYS K C   1 
ATOM   6548  O  O   . LYS F  1 136 ? 21.853  -2.584  29.726  1.00 40.86  ? 136 LYS K O   1 
ATOM   6549  C  CB  . LYS F  1 136 ? 23.142  -0.532  27.397  1.00 45.61  ? 136 LYS K CB  1 
ATOM   6550  C  CG  . LYS F  1 136 ? 22.725  0.195   26.129  0.50 47.44  ? 136 LYS K CG  1 
ATOM   6551  C  CD  . LYS F  1 136 ? 23.786  0.091   25.045  0.50 50.54  ? 136 LYS K CD  1 
ATOM   6552  C  CE  . LYS F  1 136 ? 23.322  0.762   23.764  0.25 52.64  ? 136 LYS K CE  1 
ATOM   6553  N  NZ  . LYS F  1 136 ? 21.962  0.303   23.368  0.25 51.89  ? 136 LYS K NZ  1 
ATOM   6554  N  N   . THR F  1 137 ? 23.523  -1.188  30.334  1.00 41.83  ? 137 THR K N   1 
ATOM   6555  C  CA  . THR F  1 137 ? 24.082  -2.088  31.373  1.00 40.96  ? 137 THR K CA  1 
ATOM   6556  C  C   . THR F  1 137 ? 24.094  -1.548  32.807  1.00 39.36  ? 137 THR K C   1 
ATOM   6557  O  O   . THR F  1 137 ? 24.323  -2.313  33.753  1.00 38.43  ? 137 THR K O   1 
ATOM   6558  C  CB  . THR F  1 137 ? 25.542  -2.458  31.049  1.00 43.13  ? 137 THR K CB  1 
ATOM   6559  O  OG1 . THR F  1 137 ? 26.363  -1.288  31.171  1.00 44.32  ? 137 THR K OG1 1 
ATOM   6560  C  CG2 . THR F  1 137 ? 25.654  -3.027  29.641  1.00 45.17  ? 137 THR K CG2 1 
ATOM   6561  N  N   . GLY F  1 138 ? 23.864  -0.247  32.973  1.00 39.14  ? 138 GLY K N   1 
ATOM   6562  C  CA  . GLY F  1 138 ? 23.984  0.394   34.270  1.00 38.16  ? 138 GLY K CA  1 
ATOM   6563  C  C   . GLY F  1 138 ? 25.409  0.648   34.761  1.00 39.40  ? 138 GLY K C   1 
ATOM   6564  O  O   . GLY F  1 138 ? 25.586  0.946   35.941  1.00 38.84  ? 138 GLY K O   1 
ATOM   6565  N  N   . ASN F  1 139 ? 26.414  0.555   33.879  1.00 41.42  ? 139 ASN K N   1 
ATOM   6566  C  CA  . ASN F  1 139 ? 27.833  0.831   34.222  1.00 43.09  ? 139 ASN K CA  1 
ATOM   6567  C  C   . ASN F  1 139 ? 28.336  -0.001  35.411  1.00 42.46  ? 139 ASN K C   1 
ATOM   6568  O  O   . ASN F  1 139 ? 29.093  0.496   36.252  1.00 43.10  ? 139 ASN K O   1 
ATOM   6569  C  CB  . ASN F  1 139 ? 28.051  2.330   34.515  1.00 43.75  ? 139 ASN K CB  1 
ATOM   6570  C  CG  . ASN F  1 139 ? 27.793  3.210   33.309  1.00 44.98  ? 139 ASN K CG  1 
ATOM   6571  O  OD1 . ASN F  1 139 ? 28.472  3.088   32.296  1.00 47.04  ? 139 ASN K OD1 1 
ATOM   6572  N  ND2 . ASN F  1 139 ? 26.825  4.122   33.424  1.00 43.95  ? 139 ASN K ND2 1 
ATOM   6573  N  N   . ALA F  1 140 ? 27.911  -1.264  35.469  1.00 41.40  ? 140 ALA K N   1 
ATOM   6574  C  CA  . ALA F  1 140 ? 28.203  -2.144  36.609  1.00 40.72  ? 140 ALA K CA  1 
ATOM   6575  C  C   . ALA F  1 140 ? 29.572  -2.826  36.518  1.00 42.68  ? 140 ALA K C   1 
ATOM   6576  O  O   . ALA F  1 140 ? 29.968  -3.534  37.442  1.00 42.50  ? 140 ALA K O   1 
ATOM   6577  C  CB  . ALA F  1 140 ? 27.104  -3.189  36.759  1.00 38.93  ? 140 ALA K CB  1 
ATOM   6578  N  N   . GLY F  1 141 ? 30.288  -2.622  35.411  1.00 44.73  ? 141 GLY K N   1 
ATOM   6579  C  CA  . GLY F  1 141 ? 31.633  -3.156  35.255  1.00 47.10  ? 141 GLY K CA  1 
ATOM   6580  C  C   . GLY F  1 141 ? 31.630  -4.604  34.816  1.00 47.34  ? 141 GLY K C   1 
ATOM   6581  O  O   . GLY F  1 141 ? 30.632  -5.106  34.302  1.00 46.03  ? 141 GLY K O   1 
ATOM   6582  N  N   . SER F  1 142 ? 32.762  -5.277  35.024  1.00 49.24  ? 142 SER K N   1 
ATOM   6583  C  CA  . SER F  1 142 ? 32.956  -6.642  34.536  1.00 50.13  ? 142 SER K CA  1 
ATOM   6584  C  C   . SER F  1 142 ? 32.090  -7.659  35.279  1.00 47.83  ? 142 SER K C   1 
ATOM   6585  O  O   . SER F  1 142 ? 31.573  -7.388  36.366  1.00 45.76  ? 142 SER K O   1 
ATOM   6586  C  CB  . SER F  1 142 ? 34.428  -7.047  34.655  1.00 53.07  ? 142 SER K CB  1 
ATOM   6587  O  OG  . SER F  1 142 ? 34.819  -7.074  36.016  1.00 52.59  ? 142 SER K OG  1 
ATOM   6588  N  N   . ARG F  1 143 ? 31.965  -8.831  34.666  1.00 48.46  ? 143 ARG K N   1 
ATOM   6589  C  CA  . ARG F  1 143 ? 31.150  -9.925  35.165  1.00 46.82  ? 143 ARG K CA  1 
ATOM   6590  C  C   . ARG F  1 143 ? 32.023  -10.811 36.064  1.00 47.77  ? 143 ARG K C   1 
ATOM   6591  O  O   . ARG F  1 143 ? 32.853  -11.578 35.564  1.00 50.07  ? 143 ARG K O   1 
ATOM   6592  C  CB  . ARG F  1 143 ? 30.584  -10.722 33.978  1.00 47.40  ? 143 ARG K CB  1 
ATOM   6593  C  CG  . ARG F  1 143 ? 29.804  -9.867  32.986  1.00 47.01  ? 143 ARG K CG  1 
ATOM   6594  C  CD  . ARG F  1 143 ? 29.183  -10.659 31.843  1.00 47.75  ? 143 ARG K CD  1 
ATOM   6595  N  NE  . ARG F  1 143 ? 28.559  -9.761  30.870  1.00 47.88  ? 143 ARG K NE  1 
ATOM   6596  C  CZ  . ARG F  1 143 ? 27.822  -10.127 29.819  1.00 48.45  ? 143 ARG K CZ  1 
ATOM   6597  N  NH1 . ARG F  1 143 ? 27.576  -11.404 29.553  1.00 49.02  ? 143 ARG K NH1 1 
ATOM   6598  N  NH2 . ARG F  1 143 ? 27.320  -9.191  29.017  1.00 48.71  ? 143 ARG K NH2 1 
ATOM   6599  N  N   . LEU F  1 144 ? 31.850  -10.690 37.382  1.00 46.24  ? 144 LEU K N   1 
ATOM   6600  C  CA  . LEU F  1 144 ? 32.731  -11.368 38.346  1.00 47.35  ? 144 LEU K CA  1 
ATOM   6601  C  C   . LEU F  1 144 ? 32.431  -12.859 38.490  1.00 47.19  ? 144 LEU K C   1 
ATOM   6602  O  O   . LEU F  1 144 ? 33.340  -13.659 38.638  1.00 49.17  ? 144 LEU K O   1 
ATOM   6603  C  CB  . LEU F  1 144 ? 32.664  -10.700 39.725  1.00 46.23  ? 144 LEU K CB  1 
ATOM   6604  C  CG  . LEU F  1 144 ? 33.201  -9.278  39.910  1.00 46.82  ? 144 LEU K CG  1 
ATOM   6605  C  CD1 . LEU F  1 144 ? 33.143  -8.923  41.388  1.00 46.09  ? 144 LEU K CD1 1 
ATOM   6606  C  CD2 . LEU F  1 144 ? 34.622  -9.132  39.396  1.00 49.86  ? 144 LEU K CD2 1 
ATOM   6607  N  N   . ALA F  1 145 ? 31.155  -13.224 38.477  1.00 45.05  ? 145 ALA K N   1 
ATOM   6608  C  CA  . ALA F  1 145 ? 30.756  -14.628 38.572  1.00 44.96  ? 145 ALA K CA  1 
ATOM   6609  C  C   . ALA F  1 145 ? 29.384  -14.823 37.953  1.00 43.26  ? 145 ALA K C   1 
ATOM   6610  O  O   . ALA F  1 145 ? 28.603  -13.879 37.851  1.00 41.66  ? 145 ALA K O   1 
ATOM   6611  C  CB  . ALA F  1 145 ? 30.755  -15.084 40.020  1.00 44.36  ? 145 ALA K CB  1 
ATOM   6612  N  N   . ALA F  1 146 ? 29.110  -16.055 37.539  1.00 43.81  ? 146 ALA K N   1 
ATOM   6613  C  CA  . ALA F  1 146 ? 27.895  -16.370 36.810  1.00 42.79  ? 146 ALA K CA  1 
ATOM   6614  C  C   . ALA F  1 146 ? 27.530  -17.839 36.909  1.00 43.21  ? 146 ALA K C   1 
ATOM   6615  O  O   . ALA F  1 146 ? 28.356  -18.676 37.260  1.00 44.66  ? 146 ALA K O   1 
ATOM   6616  C  CB  . ALA F  1 146 ? 28.053  -15.976 35.349  1.00 44.07  ? 146 ALA K CB  1 
ATOM   6617  N  N   . GLY F  1 147 ? 26.276  -18.133 36.594  1.00 42.07  ? 147 GLY K N   1 
ATOM   6618  C  CA  . GLY F  1 147 ? 25.794  -19.504 36.518  1.00 42.69  ? 147 GLY K CA  1 
ATOM   6619  C  C   . GLY F  1 147 ? 24.483  -19.604 35.784  1.00 41.98  ? 147 GLY K C   1 
ATOM   6620  O  O   . GLY F  1 147 ? 23.760  -18.618 35.664  1.00 40.59  ? 147 GLY K O   1 
ATOM   6621  N  N   . VAL F  1 148 ? 24.170  -20.804 35.311  1.00 43.23  ? 148 VAL K N   1 
ATOM   6622  C  CA  . VAL F  1 148 ? 22.914  -21.066 34.619  1.00 43.04  ? 148 VAL K CA  1 
ATOM   6623  C  C   . VAL F  1 148 ? 21.839  -21.368 35.662  1.00 41.52  ? 148 VAL K C   1 
ATOM   6624  O  O   . VAL F  1 148 ? 22.077  -22.123 36.604  1.00 41.66  ? 148 VAL K O   1 
ATOM   6625  C  CB  . VAL F  1 148 ? 23.041  -22.242 33.635  1.00 45.42  ? 148 VAL K CB  1 
ATOM   6626  C  CG1 . VAL F  1 148 ? 21.726  -22.479 32.902  1.00 45.45  ? 148 VAL K CG1 1 
ATOM   6627  C  CG2 . VAL F  1 148 ? 24.165  -21.986 32.640  1.00 47.44  ? 148 VAL K CG2 1 
ATOM   6628  N  N   . ILE F  1 149 ? 20.655  -20.785 35.483  1.00 40.33  ? 149 ILE K N   1 
ATOM   6629  C  CA  . ILE F  1 149 ? 19.570  -20.943 36.445  1.00 39.09  ? 149 ILE K CA  1 
ATOM   6630  C  C   . ILE F  1 149 ? 18.826  -22.239 36.116  1.00 40.38  ? 149 ILE K C   1 
ATOM   6631  O  O   . ILE F  1 149 ? 18.292  -22.378 35.024  1.00 41.31  ? 149 ILE K O   1 
ATOM   6632  C  CB  . ILE F  1 149 ? 18.607  -19.731 36.422  1.00 37.47  ? 149 ILE K CB  1 
ATOM   6633  C  CG1 . ILE F  1 149 ? 19.377  -18.427 36.690  1.00 36.50  ? 149 ILE K CG1 1 
ATOM   6634  C  CG2 . ILE F  1 149 ? 17.507  -19.917 37.456  1.00 36.50  ? 149 ILE K CG2 1 
ATOM   6635  C  CD1 . ILE F  1 149 ? 18.578  -17.154 36.466  1.00 35.31  ? 149 ILE K CD1 1 
ATOM   6636  N  N   . GLY F  1 150 ? 18.790  -23.179 37.058  1.00 40.76  ? 150 GLY K N   1 
ATOM   6637  C  CA  . GLY F  1 150 ? 18.207  -24.500 36.811  1.00 42.33  ? 150 GLY K CA  1 
ATOM   6638  C  C   . GLY F  1 150 ? 17.001  -24.785 37.674  1.00 41.85  ? 150 GLY K C   1 
ATOM   6639  O  O   . GLY F  1 150 ? 16.783  -24.115 38.689  1.00 40.41  ? 150 GLY K O   1 
ATOM   6640  N  N   . ILE F  1 151 ? 16.226  -25.788 37.264  1.00 43.38  ? 151 ILE K N   1 
ATOM   6641  C  CA  . ILE F  1 151 ? 15.038  -26.221 37.997  1.00 43.52  ? 151 ILE K CA  1 
ATOM   6642  C  C   . ILE F  1 151 ? 15.507  -26.943 39.254  1.00 43.88  ? 151 ILE K C   1 
ATOM   6643  O  O   . ILE F  1 151 ? 16.381  -27.805 39.177  1.00 45.11  ? 151 ILE K O   1 
ATOM   6644  C  CB  . ILE F  1 151 ? 14.144  -27.177 37.163  1.00 45.39  ? 151 ILE K CB  1 
ATOM   6645  C  CG1 . ILE F  1 151 ? 13.576  -26.453 35.938  1.00 45.45  ? 151 ILE K CG1 1 
ATOM   6646  C  CG2 . ILE F  1 151 ? 13.002  -27.743 38.013  1.00 45.78  ? 151 ILE K CG2 1 
ATOM   6647  C  CD1 . ILE F  1 151 ? 13.001  -27.362 34.865  1.00 47.70  ? 151 ILE K CD1 1 
ATOM   6648  N  N   . ALA F  1 152 ? 14.921  -26.583 40.397  1.00 43.10  ? 152 ALA K N   1 
ATOM   6649  C  CA  . ALA F  1 152 ? 15.237  -27.204 41.690  1.00 43.68  ? 152 ALA K CA  1 
ATOM   6650  C  C   . ALA F  1 152 ? 14.021  -27.926 42.254  1.00 44.83  ? 152 ALA K C   1 
ATOM   6651  O  O   . ALA F  1 152 ? 12.884  -27.651 41.861  1.00 44.68  ? 152 ALA K O   1 
ATOM   6652  C  CB  . ALA F  1 152 ? 15.717  -26.152 42.679  1.00 42.19  ? 152 ALA K CB  1 
ATOM   6653  N  N   . GLN F  1 153 ? 14.279  -28.847 43.181  1.00 46.22  ? 153 GLN K N   1 
ATOM   6654  C  CA  . GLN F  1 153 ? 13.225  -29.609 43.849  1.00 47.70  ? 153 GLN K CA  1 
ATOM   6655  C  C   . GLN F  1 153 ? 12.539  -28.754 44.912  1.00 46.95  ? 153 GLN K C   1 
ATOM   6656  O  O   . GLN F  1 153 ? 13.117  -28.413 45.946  1.00 46.61  ? 153 GLN K O   1 
ATOM   6657  C  CB  . GLN F  1 153 ? 13.794  -30.874 44.485  1.00 49.53  ? 153 GLN K CB  1 
ATOM   6658  C  CG  . GLN F  1 153 ? 12.730  -31.868 44.914  1.00 51.42  ? 153 GLN K CG  1 
ATOM   6659  C  CD  . GLN F  1 153 ? 13.312  -33.199 45.325  1.00 53.48  ? 153 GLN K CD  1 
ATOM   6660  O  OE1 . GLN F  1 153 ? 14.380  -33.264 45.931  1.00 53.51  ? 153 GLN K OE1 1 
ATOM   6661  N  NE2 . GLN F  1 153 ? 12.607  -34.274 45.000  1.00 55.57  ? 153 GLN K NE2 1 
ATOM   6662  O  OXT . GLN F  1 153 ? 11.379  -28.376 44.748  1.00 47.10  ? 153 GLN K OXT 1 
ATOM   6663  N  N   . ALA G  1 1   ? -0.661  24.397  66.099  1.00 58.62  ? 1   ALA M N   1 
ATOM   6664  C  CA  . ALA G  1 1   ? 0.528   23.599  65.672  1.00 55.45  ? 1   ALA M CA  1 
ATOM   6665  C  C   . ALA G  1 1   ? 1.158   22.833  66.833  1.00 54.16  ? 1   ALA M C   1 
ATOM   6666  O  O   . ALA G  1 1   ? 1.569   23.437  67.822  1.00 55.39  ? 1   ALA M O   1 
ATOM   6667  C  CB  . ALA G  1 1   ? 1.571   24.507  65.030  1.00 55.41  ? 1   ALA M CB  1 
ATOM   6668  N  N   . THR G  1 2   ? 1.229   21.509  66.711  1.00 51.94  ? 2   THR M N   1 
ATOM   6669  C  CA  . THR G  1 2   ? 1.973   20.691  67.663  1.00 50.61  ? 2   THR M CA  1 
ATOM   6670  C  C   . THR G  1 2   ? 3.465   20.867  67.373  1.00 49.09  ? 2   THR M C   1 
ATOM   6671  O  O   . THR G  1 2   ? 3.889   20.900  66.207  1.00 47.85  ? 2   THR M O   1 
ATOM   6672  C  CB  . THR G  1 2   ? 1.590   19.198  67.577  1.00 49.05  ? 2   THR M CB  1 
ATOM   6673  O  OG1 . THR G  1 2   ? 0.170   19.069  67.522  1.00 50.59  ? 2   THR M OG1 1 
ATOM   6674  C  CG2 . THR G  1 2   ? 2.102   18.432  68.789  1.00 48.63  ? 2   THR M CG2 1 
ATOM   6675  N  N   . LYS G  1 3   ? 4.248   20.994  68.439  1.00 49.39  ? 3   LYS M N   1 
ATOM   6676  C  CA  . LYS G  1 3   ? 5.688   21.168  68.336  1.00 48.43  ? 3   LYS M CA  1 
ATOM   6677  C  C   . LYS G  1 3   ? 6.384   20.119  69.182  1.00 47.31  ? 3   LYS M C   1 
ATOM   6678  O  O   . LYS G  1 3   ? 5.927   19.794  70.277  1.00 48.24  ? 3   LYS M O   1 
ATOM   6679  C  CB  . LYS G  1 3   ? 6.079   22.578  68.776  1.00 50.64  ? 3   LYS M CB  1 
ATOM   6680  C  CG  . LYS G  1 3   ? 5.708   23.636  67.752  1.00 51.70  ? 3   LYS M CG  1 
ATOM   6681  C  CD  . LYS G  1 3   ? 6.008   25.039  68.247  1.00 54.30  ? 3   LYS M CD  1 
ATOM   6682  C  CE  . LYS G  1 3   ? 5.668   26.077  67.193  1.00 55.59  ? 3   LYS M CE  1 
ATOM   6683  N  NZ  . LYS G  1 3   ? 5.983   27.455  67.653  1.00 58.37  ? 3   LYS M NZ  1 
ATOM   6684  N  N   . ALA G  1 4   ? 7.477   19.574  68.658  1.00 45.50  ? 4   ALA M N   1 
ATOM   6685  C  CA  . ALA G  1 4   ? 8.282   18.606  69.392  1.00 44.70  ? 4   ALA M CA  1 
ATOM   6686  C  C   . ALA G  1 4   ? 9.760   18.875  69.167  1.00 44.33  ? 4   ALA M C   1 
ATOM   6687  O  O   . ALA G  1 4   ? 10.133  19.543  68.203  1.00 44.11  ? 4   ALA M O   1 
ATOM   6688  C  CB  . ALA G  1 4   ? 7.914   17.189  68.990  1.00 42.90  ? 4   ALA M CB  1 
ATOM   6689  N  N   . VAL G  1 5   ? 10.594  18.369  70.069  1.00 44.57  ? 5   VAL M N   1 
ATOM   6690  C  CA  . VAL G  1 5   ? 12.032  18.635  70.025  1.00 44.77  ? 5   VAL M CA  1 
ATOM   6691  C  C   . VAL G  1 5   ? 12.835  17.418  70.483  1.00 44.04  ? 5   VAL M C   1 
ATOM   6692  O  O   . VAL G  1 5   ? 12.343  16.598  71.261  1.00 44.14  ? 5   VAL M O   1 
ATOM   6693  C  CB  . VAL G  1 5   ? 12.381  19.894  70.863  1.00 47.25  ? 5   VAL M CB  1 
ATOM   6694  C  CG1 . VAL G  1 5   ? 12.326  19.607  72.363  1.00 48.76  ? 5   VAL M CG1 1 
ATOM   6695  C  CG2 . VAL G  1 5   ? 13.733  20.465  70.460  1.00 47.69  ? 5   VAL M CG2 1 
ATOM   6696  N  N   . CYS G  1 6   ? 14.066  17.311  69.990  1.00 43.59  ? 6   CYS M N   1 
ATOM   6697  C  CA  . CYS G  1 6   ? 14.947  16.201  70.328  1.00 43.21  ? 6   CYS M CA  1 
ATOM   6698  C  C   . CYS G  1 6   ? 16.411  16.643  70.459  1.00 44.40  ? 6   CYS M C   1 
ATOM   6699  O  O   . CYS G  1 6   ? 16.967  17.261  69.549  1.00 44.17  ? 6   CYS M O   1 
ATOM   6700  C  CB  . CYS G  1 6   ? 14.827  15.111  69.267  1.00 41.00  ? 6   CYS M CB  1 
ATOM   6701  S  SG  . CYS G  1 6   ? 15.746  13.618  69.681  1.00 40.73  ? 6   CYS M SG  1 
ATOM   6702  N  N   . VAL G  1 7   ? 17.013  16.333  71.606  1.00 45.94  ? 7   VAL M N   1 
ATOM   6703  C  CA  . VAL G  1 7   ? 18.437  16.562  71.836  1.00 47.40  ? 7   VAL M CA  1 
ATOM   6704  C  C   . VAL G  1 7   ? 19.147  15.259  71.499  1.00 46.33  ? 7   VAL M C   1 
ATOM   6705  O  O   . VAL G  1 7   ? 18.958  14.262  72.185  1.00 46.27  ? 7   VAL M O   1 
ATOM   6706  C  CB  . VAL G  1 7   ? 18.718  16.971  73.297  1.00 50.09  ? 7   VAL M CB  1 
ATOM   6707  C  CG1 . VAL G  1 7   ? 20.199  17.290  73.497  1.00 51.99  ? 7   VAL M CG1 1 
ATOM   6708  C  CG2 . VAL G  1 7   ? 17.851  18.162  73.686  1.00 51.26  ? 7   VAL M CG2 1 
ATOM   6709  N  N   . LEU G  1 8   ? 19.921  15.266  70.415  1.00 45.62  ? 8   LEU M N   1 
ATOM   6710  C  CA  . LEU G  1 8   ? 20.724  14.107  70.013  1.00 45.02  ? 8   LEU M CA  1 
ATOM   6711  C  C   . LEU G  1 8   ? 22.065  14.124  70.744  1.00 47.48  ? 8   LEU M C   1 
ATOM   6712  O  O   . LEU G  1 8   ? 22.774  15.130  70.710  1.00 49.07  ? 8   LEU M O   1 
ATOM   6713  C  CB  . LEU G  1 8   ? 20.956  14.109  68.496  1.00 43.40  ? 8   LEU M CB  1 
ATOM   6714  C  CG  . LEU G  1 8   ? 19.710  13.914  67.621  1.00 41.20  ? 8   LEU M CG  1 
ATOM   6715  C  CD1 . LEU G  1 8   ? 20.031  14.204  66.163  1.00 40.25  ? 8   LEU M CD1 1 
ATOM   6716  C  CD2 . LEU G  1 8   ? 19.148  12.511  67.766  1.00 39.94  ? 8   LEU M CD2 1 
ATOM   6717  N  N   . LYS G  1 9   ? 22.387  13.021  71.422  1.00 48.14  ? 9   LYS M N   1 
ATOM   6718  C  CA  . LYS G  1 9   ? 23.673  12.838  72.111  1.00 50.63  ? 9   LYS M CA  1 
ATOM   6719  C  C   . LYS G  1 9   ? 24.124  11.382  72.005  1.00 50.28  ? 9   LYS M C   1 
ATOM   6720  O  O   . LYS G  1 9   ? 23.293  10.485  71.879  1.00 48.58  ? 9   LYS M O   1 
ATOM   6721  C  CB  . LYS G  1 9   ? 23.540  13.221  73.586  1.00 53.08  ? 9   LYS M CB  1 
ATOM   6722  C  CG  . LYS G  1 9   ? 23.384  14.713  73.835  1.00 54.40  ? 9   LYS M CG  1 
ATOM   6723  C  CD  . LYS G  1 9   ? 23.230  15.017  75.316  1.00 56.97  ? 9   LYS M CD  1 
ATOM   6724  C  CE  . LYS G  1 9   ? 23.187  16.517  75.583  1.00 58.69  ? 9   LYS M CE  1 
ATOM   6725  N  NZ  . LYS G  1 9   ? 24.490  17.192  75.318  1.00 60.63  ? 9   LYS M NZ  1 
ATOM   6726  N  N   . GLY G  1 10  ? 25.436  11.153  72.074  1.00 52.20  ? 10  GLY M N   1 
ATOM   6727  C  CA  . GLY G  1 10  ? 26.001  9.796   72.040  1.00 52.48  ? 10  GLY M CA  1 
ATOM   6728  C  C   . GLY G  1 10  ? 27.333  9.657   72.754  1.00 55.73  ? 10  GLY M C   1 
ATOM   6729  O  O   . GLY G  1 10  ? 27.735  10.538  73.512  1.00 57.98  ? 10  GLY M O   1 
ATOM   6730  N  N   . ASP G  1 11  ? 28.010  8.536   72.509  1.00 56.26  ? 11  ASP M N   1 
ATOM   6731  C  CA  . ASP G  1 11  ? 29.315  8.249   73.129  1.00 59.65  ? 11  ASP M CA  1 
ATOM   6732  C  C   . ASP G  1 11  ? 30.427  9.077   72.499  1.00 60.90  ? 11  ASP M C   1 
ATOM   6733  O  O   . ASP G  1 11  ? 31.285  9.605   73.204  1.00 64.02  ? 11  ASP M O   1 
ATOM   6734  C  CB  . ASP G  1 11  ? 29.662  6.761   73.008  1.00 60.02  ? 11  ASP M CB  1 
ATOM   6735  C  CG  . ASP G  1 11  ? 28.672  5.873   73.735  1.00 59.50  ? 11  ASP M CG  1 
ATOM   6736  O  OD1 . ASP G  1 11  ? 28.504  6.048   74.957  1.00 61.51  ? 11  ASP M OD1 1 
ATOM   6737  O  OD2 . ASP G  1 11  ? 28.049  5.010   73.082  1.00 57.45  ? 11  ASP M OD2 1 
ATOM   6738  N  N   . GLY G  1 12  ? 30.405  9.179   71.172  1.00 58.70  ? 12  GLY M N   1 
ATOM   6739  C  CA  . GLY G  1 12  ? 31.388  9.953   70.411  1.00 59.80  ? 12  GLY M CA  1 
ATOM   6740  C  C   . GLY G  1 12  ? 31.080  11.444  70.347  1.00 59.72  ? 12  GLY M C   1 
ATOM   6741  O  O   . GLY G  1 12  ? 30.401  11.968  71.229  1.00 59.91  ? 12  GLY M O   1 
ATOM   6742  N  N   . PRO G  1 13  ? 31.573  12.138  69.296  1.00 59.65  ? 13  PRO M N   1 
ATOM   6743  C  CA  . PRO G  1 13  ? 31.424  13.592  69.183  1.00 60.12  ? 13  PRO M CA  1 
ATOM   6744  C  C   . PRO G  1 13  ? 30.138  14.079  68.490  1.00 56.97  ? 13  PRO M C   1 
ATOM   6745  O  O   . PRO G  1 13  ? 29.959  15.290  68.346  1.00 57.49  ? 13  PRO M O   1 
ATOM   6746  C  CB  . PRO G  1 13  ? 32.640  13.980  68.344  1.00 61.95  ? 13  PRO M CB  1 
ATOM   6747  C  CG  . PRO G  1 13  ? 32.806  12.830  67.414  1.00 60.34  ? 13  PRO M CG  1 
ATOM   6748  C  CD  . PRO G  1 13  ? 32.340  11.600  68.153  1.00 59.47  ? 13  PRO M CD  1 
ATOM   6749  N  N   . VAL G  1 14  ? 29.256  13.171  68.072  1.00 54.05  ? 14  VAL M N   1 
ATOM   6750  C  CA  . VAL G  1 14  ? 28.047  13.571  67.342  1.00 51.32  ? 14  VAL M CA  1 
ATOM   6751  C  C   . VAL G  1 14  ? 26.955  14.056  68.298  1.00 50.95  ? 14  VAL M C   1 
ATOM   6752  O  O   . VAL G  1 14  ? 26.539  13.324  69.199  1.00 50.86  ? 14  VAL M O   1 
ATOM   6753  C  CB  . VAL G  1 14  ? 27.494  12.439  66.452  1.00 48.62  ? 14  VAL M CB  1 
ATOM   6754  C  CG1 . VAL G  1 14  ? 26.246  12.908  65.709  1.00 46.25  ? 14  VAL M CG1 1 
ATOM   6755  C  CG2 . VAL G  1 14  ? 28.555  11.983  65.462  1.00 49.11  ? 14  VAL M CG2 1 
ATOM   6756  N  N   . GLN G  1 15  ? 26.493  15.286  68.085  1.00 50.95  ? 15  GLN M N   1 
ATOM   6757  C  CA  . GLN G  1 15  ? 25.424  15.864  68.893  1.00 50.78  ? 15  GLN M CA  1 
ATOM   6758  C  C   . GLN G  1 15  ? 24.661  16.945  68.133  1.00 49.81  ? 15  GLN M C   1 
ATOM   6759  O  O   . GLN G  1 15  ? 25.199  17.589  67.224  1.00 50.25  ? 15  GLN M O   1 
ATOM   6760  C  CB  . GLN G  1 15  ? 25.979  16.432  70.206  1.00 53.85  ? 15  GLN M CB  1 
ATOM   6761  C  CG  . GLN G  1 15  ? 26.965  17.581  70.045  1.00 56.39  ? 15  GLN M CG  1 
ATOM   6762  C  CD  . GLN G  1 15  ? 27.643  17.969  71.351  1.00 59.77  ? 15  GLN M CD  1 
ATOM   6763  O  OE1 . GLN G  1 15  ? 27.605  19.132  71.764  1.00 61.65  ? 15  GLN M OE1 1 
ATOM   6764  N  NE2 . GLN G  1 15  ? 28.280  16.997  72.004  1.00 60.84  ? 15  GLN M NE2 1 
ATOM   6765  N  N   . GLY G  1 16  ? 23.411  17.149  68.527  1.00 48.72  ? 16  GLY M N   1 
ATOM   6766  C  CA  . GLY G  1 16  ? 22.587  18.165  67.899  1.00 48.12  ? 16  GLY M CA  1 
ATOM   6767  C  C   . GLY G  1 16  ? 21.208  18.330  68.498  1.00 47.41  ? 16  GLY M C   1 
ATOM   6768  O  O   . GLY G  1 16  ? 20.862  17.680  69.478  1.00 47.44  ? 16  GLY M O   1 
ATOM   6769  N  N   . ILE G  1 17  ? 20.438  19.225  67.887  1.00 47.03  ? 17  ILE M N   1 
ATOM   6770  C  CA  . ILE G  1 17  ? 19.075  19.542  68.290  1.00 46.65  ? 17  ILE M CA  1 
ATOM   6771  C  C   . ILE G  1 17  ? 18.216  19.511  67.029  1.00 44.71  ? 17  ILE M C   1 
ATOM   6772  O  O   . ILE G  1 17  ? 18.552  20.165  66.037  1.00 44.93  ? 17  ILE M O   1 
ATOM   6773  C  CB  . ILE G  1 17  ? 18.990  20.937  68.953  1.00 49.15  ? 17  ILE M CB  1 
ATOM   6774  C  CG1 . ILE G  1 17  ? 19.832  20.976  70.244  1.00 51.35  ? 17  ILE M CG1 1 
ATOM   6775  C  CG2 . ILE G  1 17  ? 17.536  21.307  69.249  1.00 49.00  ? 17  ILE M CG2 1 
ATOM   6776  C  CD1 . ILE G  1 17  ? 20.187  22.371  70.719  1.00 54.25  ? 17  ILE M CD1 1 
ATOM   6777  N  N   . ILE G  1 18  ? 17.135  18.733  67.068  1.00 43.05  ? 18  ILE M N   1 
ATOM   6778  C  CA  . ILE G  1 18  ? 16.185  18.625  65.964  1.00 41.44  ? 18  ILE M CA  1 
ATOM   6779  C  C   . ILE G  1 18  ? 14.808  19.047  66.467  1.00 41.86  ? 18  ILE M C   1 
ATOM   6780  O  O   . ILE G  1 18  ? 14.359  18.597  67.520  1.00 42.10  ? 18  ILE M O   1 
ATOM   6781  C  CB  . ILE G  1 18  ? 16.136  17.191  65.398  1.00 39.31  ? 18  ILE M CB  1 
ATOM   6782  C  CG1 . ILE G  1 18  ? 17.506  16.799  64.811  1.00 39.08  ? 18  ILE M CG1 1 
ATOM   6783  C  CG2 . ILE G  1 18  ? 15.035  17.042  64.341  1.00 37.97  ? 18  ILE M CG2 1 
ATOM   6784  C  CD1 . ILE G  1 18  ? 17.971  17.648  63.637  1.00 39.45  ? 18  ILE M CD1 1 
ATOM   6785  N  N   . ASN G  1 19  ? 14.167  19.926  65.698  1.00 42.17  ? 19  ASN M N   1 
ATOM   6786  C  CA  . ASN G  1 19  ? 12.848  20.459  65.997  1.00 42.93  ? 19  ASN M CA  1 
ATOM   6787  C  C   . ASN G  1 19  ? 11.840  19.814  65.052  1.00 41.40  ? 19  ASN M C   1 
ATOM   6788  O  O   . ASN G  1 19  ? 12.157  19.550  63.894  1.00 40.26  ? 19  ASN M O   1 
ATOM   6789  C  CB  . ASN G  1 19  ? 12.838  21.974  65.781  1.00 44.91  ? 19  ASN M CB  1 
ATOM   6790  C  CG  . ASN G  1 19  ? 13.924  22.689  66.568  1.00 46.73  ? 19  ASN M CG  1 
ATOM   6791  O  OD1 . ASN G  1 19  ? 13.838  22.806  67.783  1.00 47.91  ? 19  ASN M OD1 1 
ATOM   6792  N  ND2 . ASN G  1 19  ? 14.944  23.181  65.870  1.00 47.22  ? 19  ASN M ND2 1 
ATOM   6793  N  N   . PHE G  1 20  ? 10.631  19.573  65.552  1.00 41.62  ? 20  PHE M N   1 
ATOM   6794  C  CA  . PHE G  1 20  ? 9.516   19.073  64.751  1.00 40.75  ? 20  PHE M CA  1 
ATOM   6795  C  C   . PHE G  1 20  ? 8.376   20.067  64.880  1.00 42.62  ? 20  PHE M C   1 
ATOM   6796  O  O   . PHE G  1 20  ? 8.163   20.624  65.955  1.00 44.15  ? 20  PHE M O   1 
ATOM   6797  C  CB  . PHE G  1 20  ? 9.040   17.713  65.252  1.00 39.60  ? 20  PHE M CB  1 
ATOM   6798  C  CG  . PHE G  1 20  ? 10.107  16.654  65.268  1.00 38.15  ? 20  PHE M CG  1 
ATOM   6799  C  CD1 . PHE G  1 20  ? 11.075  16.635  66.272  1.00 38.74  ? 20  PHE M CD1 1 
ATOM   6800  C  CD2 . PHE G  1 20  ? 10.132  15.656  64.299  1.00 36.49  ? 20  PHE M CD2 1 
ATOM   6801  C  CE1 . PHE G  1 20  ? 12.052  15.652  66.296  1.00 37.73  ? 20  PHE M CE1 1 
ATOM   6802  C  CE2 . PHE G  1 20  ? 11.105  14.670  64.320  1.00 35.42  ? 20  PHE M CE2 1 
ATOM   6803  C  CZ  . PHE G  1 20  ? 12.069  14.671  65.318  1.00 36.06  ? 20  PHE M CZ  1 
ATOM   6804  N  N   . GLU G  1 21  ? 7.650   20.293  63.789  1.00 42.74  ? 21  GLU M N   1 
ATOM   6805  C  CA  . GLU G  1 21  ? 6.459   21.142  63.809  1.00 44.74  ? 21  GLU M CA  1 
ATOM   6806  C  C   . GLU G  1 21  ? 5.406   20.556  62.880  1.00 44.28  ? 21  GLU M C   1 
ATOM   6807  O  O   . GLU G  1 21  ? 5.717   20.149  61.761  1.00 43.04  ? 21  GLU M O   1 
ATOM   6808  C  CB  . GLU G  1 21  ? 6.805   22.574  63.395  1.00 46.54  ? 21  GLU M CB  1 
ATOM   6809  C  CG  . GLU G  1 21  ? 5.642   23.552  63.527  1.00 49.03  ? 21  GLU M CG  1 
ATOM   6810  C  CD  . GLU G  1 21  ? 6.056   25.009  63.420  1.00 51.27  ? 21  GLU M CD  1 
ATOM   6811  O  OE1 . GLU G  1 21  ? 7.152   25.304  62.891  1.00 51.00  ? 21  GLU M OE1 1 
ATOM   6812  O  OE2 . GLU G  1 21  ? 5.268   25.867  63.860  1.00 53.67  ? 21  GLU M OE2 1 
ATOM   6813  N  N   . GLN G  1 22  ? 4.166   20.505  63.356  1.00 45.53  ? 22  GLN M N   1 
ATOM   6814  C  CA  . GLN G  1 22  ? 3.056   19.979  62.575  1.00 45.63  ? 22  GLN M CA  1 
ATOM   6815  C  C   . GLN G  1 22  ? 1.849   20.890  62.771  1.00 48.42  ? 22  GLN M C   1 
ATOM   6816  O  O   . GLN G  1 22  ? 1.179   20.819  63.796  1.00 49.53  ? 22  GLN M O   1 
ATOM   6817  C  CB  . GLN G  1 22  ? 2.746   18.544  62.999  1.00 44.22  ? 22  GLN M CB  1 
ATOM   6818  C  CG  . GLN G  1 22  ? 1.763   17.846  62.074  1.00 44.09  ? 22  GLN M CG  1 
ATOM   6819  C  CD  . GLN G  1 22  ? 1.349   16.466  62.546  1.00 43.21  ? 22  GLN M CD  1 
ATOM   6820  O  OE1 . GLN G  1 22  ? 1.386   16.160  63.739  1.00 43.32  ? 22  GLN M OE1 1 
ATOM   6821  N  NE2 . GLN G  1 22  ? 0.945   15.620  61.604  1.00 42.47  ? 22  GLN M NE2 1 
ATOM   6822  N  N   . LYS G  1 23  ? 1.595   21.755  61.793  1.00 49.88  ? 23  LYS M N   1 
ATOM   6823  C  CA  . LYS G  1 23  ? 0.532   22.762  61.904  1.00 52.99  ? 23  LYS M CA  1 
ATOM   6824  C  C   . LYS G  1 23  ? -0.881  22.175  61.947  1.00 54.10  ? 23  LYS M C   1 
ATOM   6825  O  O   . LYS G  1 23  ? -1.718  22.663  62.702  1.00 56.34  ? 23  LYS M O   1 
ATOM   6826  C  CB  . LYS G  1 23  ? 0.634   23.807  60.787  1.00 54.44  ? 23  LYS M CB  1 
ATOM   6827  C  CG  . LYS G  1 23  ? 1.767   24.807  60.987  1.00 54.91  ? 23  LYS M CG  1 
ATOM   6828  C  CD  . LYS G  1 23  ? 1.635   25.997  60.040  1.00 57.25  ? 23  LYS M CD  1 
ATOM   6829  C  CE  . LYS G  1 23  ? 2.383   27.226  60.547  1.00 58.91  ? 23  LYS M CE  1 
ATOM   6830  N  NZ  . LYS G  1 23  ? 3.861   27.058  60.489  1.00 57.07  ? 23  LYS M NZ  1 
ATOM   6831  N  N   . GLU G  1 24  ? -1.133  21.143  61.144  1.00 52.86  ? 24  GLU M N   1 
ATOM   6832  C  CA  . GLU G  1 24  ? -2.437  20.478  61.082  1.00 54.05  ? 24  GLU M CA  1 
ATOM   6833  C  C   . GLU G  1 24  ? -2.243  19.001  61.413  1.00 51.88  ? 24  GLU M C   1 
ATOM   6834  O  O   . GLU G  1 24  ? -1.226  18.418  61.040  1.00 49.35  ? 24  GLU M O   1 
ATOM   6835  C  CB  . GLU G  1 24  ? -3.062  20.613  59.679  1.00 55.22  ? 24  GLU M CB  1 
ATOM   6836  C  CG  . GLU G  1 24  ? -2.989  21.994  59.019  1.00 57.23  ? 24  GLU M CG  1 
ATOM   6837  C  CD  . GLU G  1 24  ? -3.945  23.022  59.608  1.00 60.65  ? 24  GLU M CD  1 
ATOM   6838  O  OE1 . GLU G  1 24  ? -5.171  22.768  59.676  1.00 62.61  ? 24  GLU M OE1 1 
ATOM   6839  O  OE2 . GLU G  1 24  ? -3.474  24.119  59.978  1.00 61.78  ? 24  GLU M OE2 1 
ATOM   6840  N  N   . SER G  1 25  ? -3.222  18.388  62.082  1.00 53.01  ? 25  SER M N   1 
ATOM   6841  C  CA  . SER G  1 25  ? -3.112  16.967  62.470  1.00 51.45  ? 25  SER M CA  1 
ATOM   6842  C  C   . SER G  1 25  ? -3.125  16.009  61.267  1.00 50.22  ? 25  SER M C   1 
ATOM   6843  O  O   . SER G  1 25  ? -2.559  14.926  61.336  1.00 48.34  ? 25  SER M O   1 
ATOM   6844  C  CB  . SER G  1 25  ? -4.194  16.575  63.496  1.00 53.33  ? 25  SER M CB  1 
ATOM   6845  O  OG  . SER G  1 25  ? -5.477  16.400  62.909  1.00 55.27  ? 25  SER M OG  1 
ATOM   6846  N  N   . ASN G  1 26  ? -3.748  16.420  60.164  1.00 51.61  ? 26  ASN M N   1 
ATOM   6847  C  CA  . ASN G  1 26  ? -3.753  15.615  58.932  1.00 50.74  ? 26  ASN M CA  1 
ATOM   6848  C  C   . ASN G  1 26  ? -2.544  15.886  58.024  1.00 48.83  ? 26  ASN M C   1 
ATOM   6849  O  O   . ASN G  1 26  ? -2.532  15.453  56.866  1.00 48.65  ? 26  ASN M O   1 
ATOM   6850  C  CB  . ASN G  1 26  ? -5.057  15.856  58.148  1.00 53.54  ? 26  ASN M CB  1 
ATOM   6851  C  CG  . ASN G  1 26  ? -5.157  17.265  57.559  1.00 55.42  ? 26  ASN M CG  1 
ATOM   6852  O  OD1 . ASN G  1 26  ? -4.413  18.176  57.940  1.00 55.22  ? 26  ASN M OD1 1 
ATOM   6853  N  ND2 . ASN G  1 26  ? -6.090  17.448  56.631  1.00 57.65  ? 26  ASN M ND2 1 
ATOM   6854  N  N   . GLY G  1 27  ? -1.529  16.578  58.543  1.00 47.63  ? 27  GLY M N   1 
ATOM   6855  C  CA  . GLY G  1 27  ? -0.608  17.312  57.693  1.00 46.84  ? 27  GLY M CA  1 
ATOM   6856  C  C   . GLY G  1 27  ? 0.836   16.899  57.822  1.00 44.10  ? 27  GLY M C   1 
ATOM   6857  O  O   . GLY G  1 27  ? 1.186   16.099  58.697  1.00 42.77  ? 27  GLY M O   1 
ATOM   6858  N  N   . PRO G  1 28  ? 1.690   17.451  56.942  1.00 43.45  ? 28  PRO M N   1 
ATOM   6859  C  CA  . PRO G  1 28  ? 3.114   17.158  56.995  1.00 41.30  ? 28  PRO M CA  1 
ATOM   6860  C  C   . PRO G  1 28  ? 3.774   17.665  58.278  1.00 41.04  ? 28  PRO M C   1 
ATOM   6861  O  O   . PRO G  1 28  ? 3.320   18.651  58.868  1.00 42.69  ? 28  PRO M O   1 
ATOM   6862  C  CB  . PRO G  1 28  ? 3.672   17.879  55.762  1.00 41.77  ? 28  PRO M CB  1 
ATOM   6863  C  CG  . PRO G  1 28  ? 2.683   18.937  55.439  1.00 44.32  ? 28  PRO M CG  1 
ATOM   6864  C  CD  . PRO G  1 28  ? 1.354   18.383  55.845  1.00 45.14  ? 28  PRO M CD  1 
ATOM   6865  N  N   . VAL G  1 29  ? 4.816   16.957  58.707  1.00 39.11  ? 29  VAL M N   1 
ATOM   6866  C  CA  . VAL G  1 29  ? 5.664   17.367  59.821  1.00 38.96  ? 29  VAL M CA  1 
ATOM   6867  C  C   . VAL G  1 29  ? 6.950   17.979  59.263  1.00 38.61  ? 29  VAL M C   1 
ATOM   6868  O  O   . VAL G  1 29  ? 7.674   17.317  58.522  1.00 37.22  ? 29  VAL M O   1 
ATOM   6869  C  CB  . VAL G  1 29  ? 6.030   16.166  60.717  1.00 37.59  ? 29  VAL M CB  1 
ATOM   6870  C  CG1 . VAL G  1 29  ? 6.936   16.604  61.875  1.00 37.84  ? 29  VAL M CG1 1 
ATOM   6871  C  CG2 . VAL G  1 29  ? 4.766   15.496  61.243  1.00 38.09  ? 29  VAL M CG2 1 
ATOM   6872  N  N   . LYS G  1 30  ? 7.225   19.236  59.607  1.00 40.06  ? 30  LYS M N   1 
ATOM   6873  C  CA  . LYS G  1 30  ? 8.520   19.848  59.300  1.00 40.12  ? 30  LYS M CA  1 
ATOM   6874  C  C   . LYS G  1 30  ? 9.537   19.393  60.338  1.00 39.22  ? 30  LYS M C   1 
ATOM   6875  O  O   . LYS G  1 30  ? 9.271   19.467  61.538  1.00 39.74  ? 30  LYS M O   1 
ATOM   6876  C  CB  . LYS G  1 30  ? 8.422   21.374  59.275  1.00 42.45  ? 30  LYS M CB  1 
ATOM   6877  C  CG  . LYS G  1 30  ? 7.554   21.898  58.141  1.00 43.72  ? 30  LYS M CG  1 
ATOM   6878  C  CD  . LYS G  1 30  ? 7.461   23.416  58.168  1.00 46.35  ? 30  LYS M CD  1 
ATOM   6879  C  CE  . LYS G  1 30  ? 6.764   23.969  56.930  1.00 47.88  ? 30  LYS M CE  1 
ATOM   6880  N  NZ  . LYS G  1 30  ? 5.277   23.900  57.021  1.00 48.91  ? 30  LYS M NZ  1 
ATOM   6881  N  N   . VAL G  1 31  ? 10.684  18.909  59.865  1.00 38.07  ? 31  VAL M N   1 
ATOM   6882  C  CA  . VAL G  1 31  ? 11.775  18.431  60.709  1.00 37.48  ? 31  VAL M CA  1 
ATOM   6883  C  C   . VAL G  1 31  ? 13.020  19.244  60.359  1.00 38.36  ? 31  VAL M C   1 
ATOM   6884  O  O   . VAL G  1 31  ? 13.470  19.215  59.210  1.00 38.05  ? 31  VAL M O   1 
ATOM   6885  C  CB  . VAL G  1 31  ? 12.062  16.925  60.487  1.00 35.61  ? 31  VAL M CB  1 
ATOM   6886  C  CG1 . VAL G  1 31  ? 13.145  16.432  61.445  1.00 35.43  ? 31  VAL M CG1 1 
ATOM   6887  C  CG2 . VAL G  1 31  ? 10.795  16.101  60.653  1.00 34.96  ? 31  VAL M CG2 1 
ATOM   6888  N  N   . TRP G  1 32  ? 13.576  19.966  61.333  1.00 39.67  ? 32  TRP M N   1 
ATOM   6889  C  CA  . TRP G  1 32  ? 14.753  20.797  61.082  1.00 40.97  ? 32  TRP M CA  1 
ATOM   6890  C  C   . TRP G  1 32  ? 15.626  20.994  62.317  1.00 42.00  ? 32  TRP M C   1 
ATOM   6891  O  O   . TRP G  1 32  ? 15.173  20.831  63.449  1.00 42.18  ? 32  TRP M O   1 
ATOM   6892  C  CB  . TRP G  1 32  ? 14.341  22.158  60.498  1.00 42.79  ? 32  TRP M CB  1 
ATOM   6893  C  CG  . TRP G  1 32  ? 13.915  23.187  61.515  1.00 44.75  ? 32  TRP M CG  1 
ATOM   6894  C  CD1 . TRP G  1 32  ? 14.655  24.245  61.969  1.00 46.89  ? 32  TRP M CD1 1 
ATOM   6895  C  CD2 . TRP G  1 32  ? 12.661  23.252  62.203  1.00 45.05  ? 32  TRP M CD2 1 
ATOM   6896  N  NE1 . TRP G  1 32  ? 13.939  24.965  62.892  1.00 48.45  ? 32  TRP M NE1 1 
ATOM   6897  C  CE2 . TRP G  1 32  ? 12.709  24.382  63.054  1.00 47.38  ? 32  TRP M CE2 1 
ATOM   6898  C  CE3 . TRP G  1 32  ? 11.497  22.468  62.183  1.00 43.84  ? 32  TRP M CE3 1 
ATOM   6899  C  CZ2 . TRP G  1 32  ? 11.633  24.751  63.879  1.00 48.48  ? 32  TRP M CZ2 1 
ATOM   6900  C  CZ3 . TRP G  1 32  ? 10.424  22.835  63.009  1.00 44.96  ? 32  TRP M CZ3 1 
ATOM   6901  C  CH2 . TRP G  1 32  ? 10.504  23.970  63.842  1.00 47.24  ? 32  TRP M CH2 1 
ATOM   6902  N  N   . GLY G  1 33  ? 16.881  21.356  62.070  1.00 42.93  ? 33  GLY M N   1 
ATOM   6903  C  CA  . GLY G  1 33  ? 17.862  21.583  63.128  1.00 44.33  ? 33  GLY M CA  1 
ATOM   6904  C  C   . GLY G  1 33  ? 19.281  21.405  62.625  1.00 44.72  ? 33  GLY M C   1 
ATOM   6905  O  O   . GLY G  1 33  ? 19.533  21.430  61.417  1.00 44.36  ? 33  GLY M O   1 
ATOM   6906  N  N   . SER G  1 34  ? 20.206  21.210  63.559  1.00 45.71  ? 34  SER M N   1 
ATOM   6907  C  CA  . SER G  1 34  ? 21.623  21.079  63.235  1.00 46.59  ? 34  SER M CA  1 
ATOM   6908  C  C   . SER G  1 34  ? 22.269  19.946  64.029  1.00 46.15  ? 34  SER M C   1 
ATOM   6909  O  O   . SER G  1 34  ? 22.051  19.830  65.232  1.00 46.69  ? 34  SER M O   1 
ATOM   6910  C  CB  . SER G  1 34  ? 22.344  22.391  63.505  1.00 49.51  ? 34  SER M CB  1 
ATOM   6911  O  OG  . SER G  1 34  ? 23.646  22.348  62.954  1.00 50.62  ? 34  SER M OG  1 
ATOM   6912  N  N   . ILE G  1 35  ? 23.030  19.102  63.336  1.00 45.35  ? 35  ILE M N   1 
ATOM   6913  C  CA  . ILE G  1 35  ? 23.809  18.037  63.958  1.00 45.36  ? 35  ILE M CA  1 
ATOM   6914  C  C   . ILE G  1 35  ? 25.255  18.264  63.550  1.00 47.18  ? 35  ILE M C   1 
ATOM   6915  O  O   . ILE G  1 35  ? 25.543  18.484  62.370  1.00 47.06  ? 35  ILE M O   1 
ATOM   6916  C  CB  . ILE G  1 35  ? 23.369  16.631  63.499  1.00 42.94  ? 35  ILE M CB  1 
ATOM   6917  C  CG1 . ILE G  1 35  ? 21.851  16.454  63.635  1.00 41.22  ? 35  ILE M CG1 1 
ATOM   6918  C  CG2 . ILE G  1 35  ? 24.101  15.558  64.304  1.00 43.36  ? 35  ILE M CG2 1 
ATOM   6919  C  CD1 . ILE G  1 35  ? 21.294  15.319  62.798  1.00 39.00  ? 35  ILE M CD1 1 
ATOM   6920  N  N   . LYS G  1 36  ? 26.154  18.210  64.530  1.00 49.10  ? 36  LYS M N   1 
ATOM   6921  C  CA  . LYS G  1 36  ? 27.573  18.466  64.312  1.00 51.40  ? 36  LYS M CA  1 
ATOM   6922  C  C   . LYS G  1 36  ? 28.406  17.285  64.802  1.00 51.76  ? 36  LYS M C   1 
ATOM   6923  O  O   . LYS G  1 36  ? 27.894  16.393  65.477  1.00 50.51  ? 36  LYS M O   1 
ATOM   6924  C  CB  . LYS G  1 36  ? 27.991  19.778  64.996  1.00 54.37  ? 36  LYS M CB  1 
ATOM   6925  C  CG  . LYS G  1 36  ? 27.956  19.770  66.519  1.00 55.71  ? 36  LYS M CG  1 
ATOM   6926  C  CD  . LYS G  1 36  ? 27.925  21.184  67.078  1.00 58.19  ? 36  LYS M CD  1 
ATOM   6927  C  CE  . LYS G  1 36  ? 28.275  21.219  68.561  1.00 60.45  ? 36  LYS M CE  1 
ATOM   6928  N  NZ  . LYS G  1 36  ? 29.741  21.143  68.812  1.00 63.31  ? 36  LYS M NZ  1 
ATOM   6929  N  N   . GLY G  1 37  ? 29.688  17.295  64.445  1.00 53.70  ? 37  GLY M N   1 
ATOM   6930  C  CA  . GLY G  1 37  ? 30.609  16.200  64.749  1.00 54.50  ? 37  GLY M CA  1 
ATOM   6931  C  C   . GLY G  1 37  ? 30.501  14.993  63.826  1.00 52.27  ? 37  GLY M C   1 
ATOM   6932  O  O   . GLY G  1 37  ? 31.061  13.937  64.126  1.00 52.68  ? 37  GLY M O   1 
ATOM   6933  N  N   . LEU G  1 38  ? 29.805  15.150  62.697  1.00 50.19  ? 38  LEU M N   1 
ATOM   6934  C  CA  . LEU G  1 38  ? 29.615  14.061  61.735  1.00 48.16  ? 38  LEU M CA  1 
ATOM   6935  C  C   . LEU G  1 38  ? 30.739  14.032  60.702  1.00 49.57  ? 38  LEU M C   1 
ATOM   6936  O  O   . LEU G  1 38  ? 31.373  15.053  60.433  1.00 51.55  ? 38  LEU M O   1 
ATOM   6937  C  CB  . LEU G  1 38  ? 28.272  14.214  61.015  1.00 45.51  ? 38  LEU M CB  1 
ATOM   6938  C  CG  . LEU G  1 38  ? 27.026  13.965  61.870  1.00 43.82  ? 38  LEU M CG  1 
ATOM   6939  C  CD1 . LEU G  1 38  ? 25.808  14.621  61.233  1.00 42.24  ? 38  LEU M CD1 1 
ATOM   6940  C  CD2 . LEU G  1 38  ? 26.790  12.474  62.076  1.00 42.41  ? 38  LEU M CD2 1 
ATOM   6941  N  N   . THR G  1 39  ? 30.972  12.856  60.122  1.00 48.71  ? 39  THR M N   1 
ATOM   6942  C  CA  . THR G  1 39  ? 31.830  12.742  58.939  1.00 49.71  ? 39  THR M CA  1 
ATOM   6943  C  C   . THR G  1 39  ? 31.072  13.330  57.756  1.00 48.23  ? 39  THR M C   1 
ATOM   6944  O  O   . THR G  1 39  ? 29.836  13.255  57.704  1.00 45.85  ? 39  THR M O   1 
ATOM   6945  C  CB  . THR G  1 39  ? 32.205  11.281  58.615  1.00 49.26  ? 39  THR M CB  1 
ATOM   6946  O  OG1 . THR G  1 39  ? 31.016  10.510  58.410  1.00 46.29  ? 39  THR M OG1 1 
ATOM   6947  C  CG2 . THR G  1 39  ? 33.024  10.663  59.742  1.00 51.18  ? 39  THR M CG2 1 
ATOM   6948  N  N   . GLU G  1 40  ? 31.808  13.919  56.817  1.00 49.92  ? 40  GLU M N   1 
ATOM   6949  C  CA  . GLU G  1 40  ? 31.212  14.547  55.643  1.00 49.13  ? 40  GLU M CA  1 
ATOM   6950  C  C   . GLU G  1 40  ? 30.425  13.506  54.843  1.00 46.58  ? 40  GLU M C   1 
ATOM   6951  O  O   . GLU G  1 40  ? 30.885  12.379  54.661  1.00 46.47  ? 40  GLU M O   1 
ATOM   6952  C  CB  . GLU G  1 40  ? 32.297  15.199  54.769  1.00 51.86  ? 40  GLU M CB  1 
ATOM   6953  C  CG  . GLU G  1 40  ? 31.751  16.005  53.598  1.00 51.64  ? 40  GLU M CG  1 
ATOM   6954  C  CD  . GLU G  1 40  ? 32.819  16.703  52.776  1.00 54.71  ? 40  GLU M CD  1 
ATOM   6955  O  OE1 . GLU G  1 40  ? 34.030  16.587  53.082  1.00 57.14  ? 40  GLU M OE1 1 
ATOM   6956  O  OE2 . GLU G  1 40  ? 32.434  17.385  51.805  1.00 54.95  ? 40  GLU M OE2 1 
ATOM   6957  N  N   . GLY G  1 41  ? 29.221  13.873  54.413  1.00 44.79  ? 41  GLY M N   1 
ATOM   6958  C  CA  . GLY G  1 41  ? 28.400  13.009  53.556  1.00 42.66  ? 41  GLY M CA  1 
ATOM   6959  C  C   . GLY G  1 41  ? 27.101  12.561  54.194  1.00 40.28  ? 41  GLY M C   1 
ATOM   6960  O  O   . GLY G  1 41  ? 26.599  13.201  55.124  1.00 40.13  ? 41  GLY M O   1 
ATOM   6961  N  N   . LEU G  1 42  ? 26.570  11.447  53.690  1.00 38.67  ? 42  LEU M N   1 
ATOM   6962  C  CA  . LEU G  1 42  ? 25.221  10.990  54.019  1.00 36.54  ? 42  LEU M CA  1 
ATOM   6963  C  C   . LEU G  1 42  ? 25.192  10.151  55.287  1.00 36.00  ? 42  LEU M C   1 
ATOM   6964  O  O   . LEU G  1 42  ? 26.058  9.312   55.494  1.00 36.69  ? 42  LEU M O   1 
ATOM   6965  C  CB  . LEU G  1 42  ? 24.643  10.144  52.885  1.00 35.41  ? 42  LEU M CB  1 
ATOM   6966  C  CG  . LEU G  1 42  ? 24.365  10.796  51.535  1.00 35.77  ? 42  LEU M CG  1 
ATOM   6967  C  CD1 . LEU G  1 42  ? 23.931  9.723   50.546  1.00 34.87  ? 42  LEU M CD1 1 
ATOM   6968  C  CD2 . LEU G  1 42  ? 23.301  11.878  51.654  1.00 35.40  ? 42  LEU M CD2 1 
ATOM   6969  N  N   . HIS G  1 43  ? 24.162  10.360  56.105  1.00 34.92  ? 43  HIS M N   1 
ATOM   6970  C  CA  . HIS G  1 43  ? 23.958  9.609   57.342  1.00 34.51  ? 43  HIS M CA  1 
ATOM   6971  C  C   . HIS G  1 43  ? 22.485  9.298   57.506  1.00 32.78  ? 43  HIS M C   1 
ATOM   6972  O  O   . HIS G  1 43  ? 21.662  10.215  57.429  1.00 32.40  ? 43  HIS M O   1 
ATOM   6973  C  CB  . HIS G  1 43  ? 24.414  10.445  58.536  1.00 35.93  ? 43  HIS M CB  1 
ATOM   6974  C  CG  . HIS G  1 43  ? 25.889  10.675  58.577  1.00 38.03  ? 43  HIS M CG  1 
ATOM   6975  N  ND1 . HIS G  1 43  ? 26.776  9.704   58.981  1.00 38.97  ? 43  HIS M ND1 1 
ATOM   6976  C  CD2 . HIS G  1 43  ? 26.635  11.756  58.250  1.00 39.67  ? 43  HIS M CD2 1 
ATOM   6977  C  CE1 . HIS G  1 43  ? 28.005  10.182  58.918  1.00 41.09  ? 43  HIS M CE1 1 
ATOM   6978  N  NE2 . HIS G  1 43  ? 27.948  11.424  58.476  1.00 41.55  ? 43  HIS M NE2 1 
ATOM   6979  N  N   . GLY G  1 44  ? 22.169  8.023   57.750  1.00 31.93  ? 44  GLY M N   1 
ATOM   6980  C  CA  . GLY G  1 44  ? 20.806  7.583   58.026  1.00 30.66  ? 44  GLY M CA  1 
ATOM   6981  C  C   . GLY G  1 44  ? 20.189  8.280   59.229  1.00 30.80  ? 44  GLY M C   1 
ATOM   6982  O  O   . GLY G  1 44  ? 20.869  8.551   60.222  1.00 31.82  ? 44  GLY M O   1 
ATOM   6983  N  N   . PHE G  1 45  ? 18.887  8.546   59.130  1.00 29.92  ? 45  PHE M N   1 
ATOM   6984  C  CA  . PHE G  1 45  ? 18.180  9.433   60.051  1.00 30.26  ? 45  PHE M CA  1 
ATOM   6985  C  C   . PHE G  1 45  ? 16.797  8.831   60.276  1.00 29.47  ? 45  PHE M C   1 
ATOM   6986  O  O   . PHE G  1 45  ? 15.940  8.892   59.393  1.00 28.77  ? 45  PHE M O   1 
ATOM   6987  C  CB  . PHE G  1 45  ? 18.120  10.813  59.412  1.00 30.66  ? 45  PHE M CB  1 
ATOM   6988  C  CG  . PHE G  1 45  ? 17.643  11.906  60.317  1.00 31.46  ? 45  PHE M CG  1 
ATOM   6989  C  CD1 . PHE G  1 45  ? 18.366  12.260  61.453  1.00 32.67  ? 45  PHE M CD1 1 
ATOM   6990  C  CD2 . PHE G  1 45  ? 16.505  12.643  59.990  1.00 31.33  ? 45  PHE M CD2 1 
ATOM   6991  C  CE1 . PHE G  1 45  ? 17.937  13.299  62.270  1.00 33.65  ? 45  PHE M CE1 1 
ATOM   6992  C  CE2 . PHE G  1 45  ? 16.079  13.690  60.796  1.00 32.33  ? 45  PHE M CE2 1 
ATOM   6993  C  CZ  . PHE G  1 45  ? 16.793  14.018  61.941  1.00 33.46  ? 45  PHE M CZ  1 
ATOM   6994  N  N   . HIS G  1 46  ? 16.601  8.205   61.436  1.00 29.82  ? 46  HIS M N   1 
ATOM   6995  C  CA  . HIS G  1 46  ? 15.436  7.339   61.660  1.00 29.34  ? 46  HIS M CA  1 
ATOM   6996  C  C   . HIS G  1 46  ? 14.777  7.568   63.003  1.00 30.11  ? 46  HIS M C   1 
ATOM   6997  O  O   . HIS G  1 46  ? 15.458  7.856   63.992  1.00 31.15  ? 46  HIS M O   1 
ATOM   6998  C  CB  . HIS G  1 46  ? 15.849  5.871   61.606  1.00 29.18  ? 46  HIS M CB  1 
ATOM   6999  C  CG  . HIS G  1 46  ? 16.623  5.505   60.386  1.00 28.74  ? 46  HIS M CG  1 
ATOM   7000  N  ND1 . HIS G  1 46  ? 17.833  4.852   60.445  1.00 29.29  ? 46  HIS M ND1 1 
ATOM   7001  C  CD2 . HIS G  1 46  ? 16.363  5.699   59.074  1.00 28.06  ? 46  HIS M CD2 1 
ATOM   7002  C  CE1 . HIS G  1 46  ? 18.284  4.659   59.220  1.00 28.93  ? 46  HIS M CE1 1 
ATOM   7003  N  NE2 . HIS G  1 46  ? 17.413  5.169   58.369  1.00 28.14  ? 46  HIS M NE2 1 
ATOM   7004  N  N   . VAL G  1 47  ? 13.458  7.405   63.045  1.00 29.91  ? 47  VAL M N   1 
ATOM   7005  C  CA  . VAL G  1 47  ? 12.748  7.272   64.317  1.00 30.84  ? 47  VAL M CA  1 
ATOM   7006  C  C   . VAL G  1 47  ? 12.674  5.794   64.678  1.00 30.96  ? 47  VAL M C   1 
ATOM   7007  O  O   . VAL G  1 47  ? 12.189  4.992   63.897  1.00 30.22  ? 47  VAL M O   1 
ATOM   7008  C  CB  . VAL G  1 47  ? 11.337  7.871   64.276  1.00 31.02  ? 47  VAL M CB  1 
ATOM   7009  C  CG1 . VAL G  1 47  ? 10.684  7.775   65.654  1.00 32.22  ? 47  VAL M CG1 1 
ATOM   7010  C  CG2 . VAL G  1 47  ? 11.397  9.319   63.806  1.00 31.12  ? 47  VAL M CG2 1 
ATOM   7011  N  N   . HIS G  1 48  ? 13.178  5.449   65.861  1.00 32.15  ? 48  HIS M N   1 
ATOM   7012  C  CA  . HIS G  1 48  ? 13.142  4.073   66.366  1.00 32.82  ? 48  HIS M CA  1 
ATOM   7013  C  C   . HIS G  1 48  ? 11.971  3.917   67.323  1.00 33.93  ? 48  HIS M C   1 
ATOM   7014  O  O   . HIS G  1 48  ? 11.464  4.909   67.828  1.00 34.40  ? 48  HIS M O   1 
ATOM   7015  C  CB  . HIS G  1 48  ? 14.472  3.715   67.035  1.00 33.78  ? 48  HIS M CB  1 
ATOM   7016  C  CG  . HIS G  1 48  ? 15.587  3.521   66.056  1.00 33.10  ? 48  HIS M CG  1 
ATOM   7017  N  ND1 . HIS G  1 48  ? 16.231  2.315   65.894  1.00 33.47  ? 48  HIS M ND1 1 
ATOM   7018  C  CD2 . HIS G  1 48  ? 16.131  4.363   65.145  1.00 32.31  ? 48  HIS M CD2 1 
ATOM   7019  C  CE1 . HIS G  1 48  ? 17.159  2.436   64.959  1.00 32.93  ? 48  HIS M CE1 1 
ATOM   7020  N  NE2 . HIS G  1 48  ? 17.112  3.666   64.481  1.00 32.21  ? 48  HIS M NE2 1 
ATOM   7021  N  N   . GLU G  1 49  ? 11.558  2.672   67.559  1.00 34.60  ? 49  GLU M N   1 
ATOM   7022  C  CA  . GLU G  1 49  ? 10.294  2.370   68.240  1.00 35.81  ? 49  GLU M CA  1 
ATOM   7023  C  C   . GLU G  1 49  ? 10.177  2.917   69.674  1.00 37.49  ? 49  GLU M C   1 
ATOM   7024  O  O   . GLU G  1 49  ? 9.164   3.544   70.025  1.00 38.06  ? 49  GLU M O   1 
ATOM   7025  C  CB  . GLU G  1 49  ? 10.039  0.850   68.246  1.00 36.51  ? 49  GLU M CB  1 
ATOM   7026  C  CG  . GLU G  1 49  ? 8.649   0.456   68.749  1.00 37.77  ? 49  GLU M CG  1 
ATOM   7027  C  CD  . GLU G  1 49  ? 8.312   -1.019  68.588  1.00 38.57  ? 49  GLU M CD  1 
ATOM   7028  O  OE1 . GLU G  1 49  ? 9.103   -1.790  68.013  1.00 38.11  ? 49  GLU M OE1 1 
ATOM   7029  O  OE2 . GLU G  1 49  ? 7.224   -1.413  69.054  1.00 40.06  ? 49  GLU M OE2 1 
ATOM   7030  N  N   . PHE G  1 50  ? 11.196  2.673   70.492  1.00 38.54  ? 50  PHE M N   1 
ATOM   7031  C  CA  . PHE G  1 50  ? 11.117  2.943   71.933  1.00 40.58  ? 50  PHE M CA  1 
ATOM   7032  C  C   . PHE G  1 50  ? 11.917  4.179   72.332  1.00 40.91  ? 50  PHE M C   1 
ATOM   7033  O  O   . PHE G  1 50  ? 13.051  4.370   71.876  1.00 40.28  ? 50  PHE M O   1 
ATOM   7034  C  CB  . PHE G  1 50  ? 11.614  1.732   72.720  1.00 42.18  ? 50  PHE M CB  1 
ATOM   7035  C  CG  . PHE G  1 50  ? 10.937  0.448   72.337  1.00 42.26  ? 50  PHE M CG  1 
ATOM   7036  C  CD1 . PHE G  1 50  ? 9.572   0.276   72.556  1.00 42.97  ? 50  PHE M CD1 1 
ATOM   7037  C  CD2 . PHE G  1 50  ? 11.654  -0.588  71.748  1.00 41.93  ? 50  PHE M CD2 1 
ATOM   7038  C  CE1 . PHE G  1 50  ? 8.936   -0.904  72.194  1.00 43.31  ? 50  PHE M CE1 1 
ATOM   7039  C  CE2 . PHE G  1 50  ? 11.023  -1.768  71.383  1.00 42.25  ? 50  PHE M CE2 1 
ATOM   7040  C  CZ  . PHE G  1 50  ? 9.663   -1.925  71.600  1.00 42.93  ? 50  PHE M CZ  1 
ATOM   7041  N  N   . GLY G  1 51  ? 11.334  4.999   73.204  1.00 42.21  ? 51  GLY M N   1 
ATOM   7042  C  CA  . GLY G  1 51  ? 12.044  6.116   73.832  1.00 43.22  ? 51  GLY M CA  1 
ATOM   7043  C  C   . GLY G  1 51  ? 12.832  5.675   75.056  1.00 45.44  ? 51  GLY M C   1 
ATOM   7044  O  O   . GLY G  1 51  ? 12.781  6.332   76.094  1.00 47.19  ? 51  GLY M O   1 
ATOM   7045  N  N   . ASP G  1 52  ? 13.567  4.572   74.916  1.00 45.62  ? 52  ASP M N   1 
ATOM   7046  C  CA  . ASP G  1 52  ? 14.312  3.944   75.991  1.00 48.00  ? 52  ASP M CA  1 
ATOM   7047  C  C   . ASP G  1 52  ? 15.782  4.190   75.697  1.00 48.09  ? 52  ASP M C   1 
ATOM   7048  O  O   . ASP G  1 52  ? 16.313  3.652   74.727  1.00 46.79  ? 52  ASP M O   1 
ATOM   7049  C  CB  . ASP G  1 52  ? 14.007  2.441   76.020  1.00 48.45  ? 52  ASP M CB  1 
ATOM   7050  C  CG  . ASP G  1 52  ? 14.620  1.727   77.221  1.00 51.26  ? 52  ASP M CG  1 
ATOM   7051  O  OD1 . ASP G  1 52  ? 15.534  2.276   77.873  1.00 52.68  ? 52  ASP M OD1 1 
ATOM   7052  O  OD2 . ASP G  1 52  ? 14.173  0.600   77.518  1.00 52.32  ? 52  ASP M OD2 1 
ATOM   7053  N  N   . ASN G  1 53  ? 16.421  5.011   76.528  1.00 49.99  ? 53  ASN M N   1 
ATOM   7054  C  CA  . ASN G  1 53  ? 17.849  5.324   76.405  1.00 50.73  ? 53  ASN M CA  1 
ATOM   7055  C  C   . ASN G  1 53  ? 18.669  4.781   77.596  1.00 53.84  ? 53  ASN M C   1 
ATOM   7056  O  O   . ASN G  1 53  ? 19.716  5.342   77.937  1.00 55.38  ? 53  ASN M O   1 
ATOM   7057  C  CB  . ASN G  1 53  ? 18.024  6.849   76.265  1.00 50.53  ? 53  ASN M CB  1 
ATOM   7058  C  CG  . ASN G  1 53  ? 19.278  7.236   75.495  0.50 50.09  ? 53  ASN M CG  1 
ATOM   7059  O  OD1 . ASN G  1 53  ? 19.379  7.005   74.289  0.50 48.10  ? 53  ASN M OD1 1 
ATOM   7060  N  ND2 . ASN G  1 53  ? 20.226  7.848   76.184  0.50 52.25  ? 53  ASN M ND2 1 
ATOM   7061  N  N   . THR G  1 54  ? 18.211  3.684   78.211  1.00 55.11  ? 54  THR M N   1 
ATOM   7062  C  CA  . THR G  1 54  ? 18.883  3.103   79.391  1.00 58.45  ? 54  THR M CA  1 
ATOM   7063  C  C   . THR G  1 54  ? 20.196  2.420   79.025  1.00 59.22  ? 54  THR M C   1 
ATOM   7064  O  O   . THR G  1 54  ? 21.151  2.450   79.801  1.00 61.83  ? 54  THR M O   1 
ATOM   7065  C  CB  . THR G  1 54  ? 17.997  2.076   80.132  1.00 59.81  ? 54  THR M CB  1 
ATOM   7066  O  OG1 . THR G  1 54  ? 17.517  1.088   79.210  1.00 57.91  ? 54  THR M OG1 1 
ATOM   7067  C  CG2 . THR G  1 54  ? 16.823  2.767   80.806  1.00 60.24  ? 54  THR M CG2 1 
ATOM   7068  N  N   . ALA G  1 55  ? 20.220  1.792   77.851  1.00 57.17  ? 55  ALA M N   1 
ATOM   7069  C  CA  . ALA G  1 55  ? 21.445  1.252   77.264  1.00 57.58  ? 55  ALA M CA  1 
ATOM   7070  C  C   . ALA G  1 55  ? 21.750  2.068   76.014  1.00 55.15  ? 55  ALA M C   1 
ATOM   7071  O  O   . ALA G  1 55  ? 21.917  1.518   74.917  1.00 53.57  ? 55  ALA M O   1 
ATOM   7072  C  CB  . ALA G  1 55  ? 21.270  -0.226  76.935  1.00 57.56  ? 55  ALA M CB  1 
ATOM   7073  N  N   . GLY G  1 56  ? 21.805  3.390   76.195  1.00 55.18  ? 56  GLY M N   1 
ATOM   7074  C  CA  . GLY G  1 56  ? 22.023  4.341   75.104  1.00 53.15  ? 56  GLY M CA  1 
ATOM   7075  C  C   . GLY G  1 56  ? 21.008  4.235   73.979  1.00 50.18  ? 56  GLY M C   1 
ATOM   7076  O  O   . GLY G  1 56  ? 19.830  3.965   74.217  1.00 49.63  ? 56  GLY M O   1 
ATOM   7077  N  N   . ALA G  1 57  ? 21.487  4.440   72.753  1.00 48.51  ? 57  ALA M N   1 
ATOM   7078  C  CA  . ALA G  1 57  ? 20.705  4.259   71.544  1.00 45.84  ? 57  ALA M CA  1 
ATOM   7079  C  C   . ALA G  1 57  ? 20.334  2.798   71.248  1.00 45.33  ? 57  ALA M C   1 
ATOM   7080  O  O   . ALA G  1 57  ? 19.391  2.548   70.485  1.00 43.45  ? 57  ALA M O   1 
ATOM   7081  C  CB  . ALA G  1 57  ? 21.459  4.847   70.356  1.00 44.77  ? 57  ALA M CB  1 
ATOM   7082  N  N   . THR G  1 58  ? 21.072  1.847   71.819  1.00 47.14  ? 58  THR M N   1 
ATOM   7083  C  CA  . THR G  1 58  ? 20.813  0.418   71.600  1.00 47.15  ? 58  THR M CA  1 
ATOM   7084  C  C   . THR G  1 58  ? 19.455  -0.042  72.153  1.00 46.92  ? 58  THR M C   1 
ATOM   7085  O  O   . THR G  1 58  ? 18.804  -0.893  71.550  1.00 46.03  ? 58  THR M O   1 
ATOM   7086  C  CB  . THR G  1 58  ? 21.926  -0.453  72.215  1.00 49.90  ? 58  THR M CB  1 
ATOM   7087  O  OG1 . THR G  1 58  ? 23.206  0.119   71.910  1.00 50.60  ? 58  THR M OG1 1 
ATOM   7088  C  CG2 . THR G  1 58  ? 21.863  -1.889  71.680  1.00 49.95  ? 58  THR M CG2 1 
ATOM   7089  N  N   . SER G  1 59  ? 19.023  0.536   73.274  1.00 47.88  ? 59  SER M N   1 
ATOM   7090  C  CA  . SER G  1 59  ? 17.732  0.186   73.882  1.00 47.99  ? 59  SER M CA  1 
ATOM   7091  C  C   . SER G  1 59  ? 16.498  0.749   73.147  1.00 45.55  ? 59  SER M C   1 
ATOM   7092  O  O   . SER G  1 59  ? 15.373  0.359   73.469  1.00 45.83  ? 59  SER M O   1 
ATOM   7093  C  CB  . SER G  1 59  ? 17.705  0.593   75.363  1.00 50.42  ? 59  SER M CB  1 
ATOM   7094  O  OG  . SER G  1 59  ? 18.194  1.910   75.563  1.00 50.51  ? 59  SER M OG  1 
ATOM   7095  N  N   . ALA G  1 60  ? 16.701  1.632   72.162  1.00 43.43  ? 60  ALA M N   1 
ATOM   7096  C  CA  . ALA G  1 60  ? 15.598  2.223   71.377  1.00 41.31  ? 60  ALA M CA  1 
ATOM   7097  C  C   . ALA G  1 60  ? 14.882  1.264   70.410  1.00 39.85  ? 60  ALA M C   1 
ATOM   7098  O  O   . ALA G  1 60  ? 13.868  1.644   69.819  1.00 38.64  ? 60  ALA M O   1 
ATOM   7099  C  CB  . ALA G  1 60  ? 16.091  3.446   70.609  1.00 40.03  ? 60  ALA M CB  1 
ATOM   7100  N  N   . GLY G  1 61  ? 15.413  0.055   70.223  1.00 40.14  ? 61  GLY M N   1 
ATOM   7101  C  CA  . GLY G  1 61  ? 14.776  -0.966  69.398  1.00 39.25  ? 61  GLY M CA  1 
ATOM   7102  C  C   . GLY G  1 61  ? 14.883  -0.701  67.898  1.00 37.07  ? 61  GLY M C   1 
ATOM   7103  O  O   . GLY G  1 61  ? 15.665  0.149   67.472  1.00 36.36  ? 61  GLY M O   1 
ATOM   7104  N  N   . PRO G  1 62  ? 14.074  -1.412  67.086  1.00 36.15  ? 62  PRO M N   1 
ATOM   7105  C  CA  . PRO G  1 62  ? 14.124  -1.263  65.628  1.00 34.39  ? 62  PRO M CA  1 
ATOM   7106  C  C   . PRO G  1 62  ? 13.447  0.017   65.149  1.00 32.97  ? 62  PRO M C   1 
ATOM   7107  O  O   . PRO G  1 62  ? 12.963  0.811   65.958  1.00 33.30  ? 62  PRO M O   1 
ATOM   7108  C  CB  . PRO G  1 62  ? 13.364  -2.497  65.128  1.00 34.62  ? 62  PRO M CB  1 
ATOM   7109  C  CG  . PRO G  1 62  ? 12.374  -2.772  66.206  1.00 35.92  ? 62  PRO M CG  1 
ATOM   7110  C  CD  . PRO G  1 62  ? 13.027  -2.365  67.500  1.00 37.11  ? 62  PRO M CD  1 
ATOM   7111  N  N   . HIS G  1 63  ? 13.426  0.222   63.840  1.00 31.58  ? 63  HIS M N   1 
ATOM   7112  C  CA  . HIS G  1 63  ? 12.756  1.395   63.281  1.00 30.57  ? 63  HIS M CA  1 
ATOM   7113  C  C   . HIS G  1 63  ? 11.261  1.334   63.621  1.00 30.90  ? 63  HIS M C   1 
ATOM   7114  O  O   . HIS G  1 63  ? 10.665  0.251   63.657  1.00 31.35  ? 63  HIS M O   1 
ATOM   7115  C  CB  . HIS G  1 63  ? 12.949  1.486   61.771  1.00 29.47  ? 63  HIS M CB  1 
ATOM   7116  C  CG  . HIS G  1 63  ? 14.372  1.704   61.353  1.00 29.26  ? 63  HIS M CG  1 
ATOM   7117  N  ND1 . HIS G  1 63  ? 14.761  1.723   60.033  1.00 28.53  ? 63  HIS M ND1 1 
ATOM   7118  C  CD2 . HIS G  1 63  ? 15.501  1.885   62.080  1.00 29.91  ? 63  HIS M CD2 1 
ATOM   7119  C  CE1 . HIS G  1 63  ? 16.064  1.927   59.962  1.00 28.80  ? 63  HIS M CE1 1 
ATOM   7120  N  NE2 . HIS G  1 63  ? 16.539  2.021   61.192  1.00 29.60  ? 63  HIS M NE2 1 
ATOM   7121  N  N   . PHE G  1 64  ? 10.680  2.494   63.913  1.00 30.86  ? 64  PHE M N   1 
ATOM   7122  C  CA  . PHE G  1 64  ? 9.264   2.571   64.233  1.00 31.51  ? 64  PHE M CA  1 
ATOM   7123  C  C   . PHE G  1 64  ? 8.468   2.093   63.023  1.00 31.06  ? 64  PHE M C   1 
ATOM   7124  O  O   . PHE G  1 64  ? 8.548   2.701   61.949  1.00 30.09  ? 64  PHE M O   1 
ATOM   7125  C  CB  . PHE G  1 64  ? 8.886   3.998   64.625  1.00 31.71  ? 64  PHE M CB  1 
ATOM   7126  C  CG  . PHE G  1 64  ? 7.435   4.177   64.973  1.00 32.63  ? 64  PHE M CG  1 
ATOM   7127  C  CD1 . PHE G  1 64  ? 6.773   3.268   65.802  1.00 33.87  ? 64  PHE M CD1 1 
ATOM   7128  C  CD2 . PHE G  1 64  ? 6.728   5.266   64.479  1.00 32.60  ? 64  PHE M CD2 1 
ATOM   7129  C  CE1 . PHE G  1 64  ? 5.430   3.438   66.113  1.00 35.04  ? 64  PHE M CE1 1 
ATOM   7130  C  CE2 . PHE G  1 64  ? 5.385   5.441   64.792  1.00 33.78  ? 64  PHE M CE2 1 
ATOM   7131  C  CZ  . PHE G  1 64  ? 4.740   4.530   65.617  1.00 34.99  ? 64  PHE M CZ  1 
ATOM   7132  N  N   . ASN G  1 65  ? 7.742   0.988   63.207  1.00 31.93  ? 65  ASN M N   1 
ATOM   7133  C  CA  . ASN G  1 65  ? 7.169   0.230   62.101  1.00 31.94  ? 65  ASN M CA  1 
ATOM   7134  C  C   . ASN G  1 65  ? 5.806   -0.408  62.484  1.00 33.45  ? 65  ASN M C   1 
ATOM   7135  O  O   . ASN G  1 65  ? 5.653   -1.627  62.469  1.00 34.19  ? 65  ASN M O   1 
ATOM   7136  C  CB  . ASN G  1 65  ? 8.186   -0.838  61.661  1.00 31.59  ? 65  ASN M CB  1 
ATOM   7137  C  CG  . ASN G  1 65  ? 7.755   -1.606  60.421  1.00 31.60  ? 65  ASN M CG  1 
ATOM   7138  O  OD1 . ASN G  1 65  ? 7.029   -1.092  59.560  1.00 31.38  ? 65  ASN M OD1 1 
ATOM   7139  N  ND2 . ASN G  1 65  ? 8.232   -2.840  60.307  1.00 32.07  ? 65  ASN M ND2 1 
ATOM   7140  N  N   . PRO G  1 66  ? 4.808   0.428   62.825  1.00 34.20  ? 66  PRO M N   1 
ATOM   7141  C  CA  . PRO G  1 66  ? 3.512   -0.111  63.232  1.00 35.98  ? 66  PRO M CA  1 
ATOM   7142  C  C   . PRO G  1 66  ? 2.742   -0.839  62.113  1.00 36.51  ? 66  PRO M C   1 
ATOM   7143  O  O   . PRO G  1 66  ? 1.889   -1.659  62.422  1.00 38.11  ? 66  PRO M O   1 
ATOM   7144  C  CB  . PRO G  1 66  ? 2.752   1.129   63.718  1.00 36.56  ? 66  PRO M CB  1 
ATOM   7145  C  CG  . PRO G  1 66  ? 3.364   2.262   62.980  1.00 35.05  ? 66  PRO M CG  1 
ATOM   7146  C  CD  . PRO G  1 66  ? 4.808   1.903   62.797  1.00 33.68  ? 66  PRO M CD  1 
ATOM   7147  N  N   . LEU G  1 67  ? 3.052   -0.570  60.843  1.00 35.46  ? 67  LEU M N   1 
ATOM   7148  C  CA  . LEU G  1 67  ? 2.379   -1.252  59.724  1.00 36.22  ? 67  LEU M CA  1 
ATOM   7149  C  C   . LEU G  1 67  ? 3.101   -2.517  59.222  1.00 36.04  ? 67  LEU M C   1 
ATOM   7150  O  O   . LEU G  1 67  ? 2.647   -3.135  58.268  1.00 36.60  ? 67  LEU M O   1 
ATOM   7151  C  CB  . LEU G  1 67  ? 2.128   -0.266  58.573  1.00 35.68  ? 67  LEU M CB  1 
ATOM   7152  C  CG  . LEU G  1 67  ? 1.247   0.952   58.901  1.00 36.42  ? 67  LEU M CG  1 
ATOM   7153  C  CD1 . LEU G  1 67  ? 1.092   1.863   57.693  1.00 36.09  ? 67  LEU M CD1 1 
ATOM   7154  C  CD2 . LEU G  1 67  ? -0.116  0.523   59.407  1.00 38.59  ? 67  LEU M CD2 1 
ATOM   7155  N  N   . SER G  1 68  ? 4.199   -2.906  59.875  1.00 35.55  ? 68  SER M N   1 
ATOM   7156  C  CA  . SER G  1 68  ? 4.967   -4.116  59.526  1.00 35.72  ? 68  SER M CA  1 
ATOM   7157  C  C   . SER G  1 68  ? 5.359   -4.209  58.050  1.00 34.99  ? 68  SER M C   1 
ATOM   7158  O  O   . SER G  1 68  ? 5.119   -5.223  57.392  1.00 35.87  ? 68  SER M O   1 
ATOM   7159  C  CB  . SER G  1 68  ? 4.210   -5.372  59.962  1.00 37.71  ? 68  SER M CB  1 
ATOM   7160  O  OG  . SER G  1 68  ? 4.041   -5.353  61.359  1.00 38.70  ? 68  SER M OG  1 
ATOM   7161  N  N   . ARG G  1 69  ? 5.956   -3.131  57.554  1.00 33.65  ? 69  ARG M N   1 
ATOM   7162  C  CA  . ARG G  1 69  ? 6.427   -3.037  56.189  1.00 33.04  ? 69  ARG M CA  1 
ATOM   7163  C  C   . ARG G  1 69  ? 7.936   -3.258  56.180  1.00 32.01  ? 69  ARG M C   1 
ATOM   7164  O  O   . ARG G  1 69  ? 8.580   -3.290  57.227  1.00 31.81  ? 69  ARG M O   1 
ATOM   7165  C  CB  . ARG G  1 69  ? 6.111   -1.648  55.612  1.00 32.66  ? 69  ARG M CB  1 
ATOM   7166  C  CG  . ARG G  1 69  ? 4.647   -1.212  55.687  1.00 34.00  ? 69  ARG M CG  1 
ATOM   7167  C  CD  . ARG G  1 69  ? 3.953   -1.261  54.345  1.00 34.94  ? 69  ARG M CD  1 
ATOM   7168  N  NE  . ARG G  1 69  ? 2.527   -0.896  54.430  1.00 36.65  ? 69  ARG M NE  1 
ATOM   7169  C  CZ  . ARG G  1 69  ? 1.940   0.205   53.933  1.00 37.09  ? 69  ARG M CZ  1 
ATOM   7170  N  NH1 . ARG G  1 69  ? 2.617   1.147   53.274  1.00 36.17  ? 69  ARG M NH1 1 
ATOM   7171  N  NH2 . ARG G  1 69  ? 0.627   0.367   54.102  1.00 38.86  ? 69  ARG M NH2 1 
ATOM   7172  N  N   . LYS G  1 70  ? 8.493   -3.421  54.989  1.00 31.54  ? 70  LYS M N   1 
ATOM   7173  C  CA  . LYS G  1 70  ? 9.945   -3.428  54.815  1.00 30.76  ? 70  LYS M CA  1 
ATOM   7174  C  C   . LYS G  1 70  ? 10.519  -2.017  54.877  1.00 29.57  ? 70  LYS M C   1 
ATOM   7175  O  O   . LYS G  1 70  ? 9.794   -1.027  54.701  1.00 29.22  ? 70  LYS M O   1 
ATOM   7176  C  CB  . LYS G  1 70  ? 10.322  -4.096  53.494  1.00 31.11  ? 70  LYS M CB  1 
ATOM   7177  C  CG  . LYS G  1 70  ? 9.942   -5.571  53.448  1.00 32.49  ? 70  LYS M CG  1 
ATOM   7178  C  CD  . LYS G  1 70  ? 10.354  -6.212  52.129  1.00 33.03  ? 70  LYS M CD  1 
ATOM   7179  C  CE  . LYS G  1 70  ? 9.378   -5.898  51.004  0.70 33.41  ? 70  LYS M CE  1 
ATOM   7180  N  NZ  . LYS G  1 70  ? 9.913   -6.300  49.669  0.70 33.91  ? 70  LYS M NZ  1 
ATOM   7181  N  N   . HIS G  1 71  ? 11.826  -1.942  55.149  1.00 29.07  ? 71  HIS M N   1 
ATOM   7182  C  CA  . HIS G  1 71  ? 12.569  -0.681  55.134  1.00 28.27  ? 71  HIS M CA  1 
ATOM   7183  C  C   . HIS G  1 71  ? 12.586  -0.082  53.730  1.00 28.00  ? 71  HIS M C   1 
ATOM   7184  O  O   . HIS G  1 71  ? 12.720  -0.802  52.747  1.00 28.31  ? 71  HIS M O   1 
ATOM   7185  C  CB  . HIS G  1 71  ? 14.025  -0.884  55.597  1.00 28.30  ? 71  HIS M CB  1 
ATOM   7186  C  CG  . HIS G  1 71  ? 14.822  0.382   55.634  1.00 27.82  ? 71  HIS M CG  1 
ATOM   7187  N  ND1 . HIS G  1 71  ? 14.656  1.336   56.614  1.00 27.68  ? 71  HIS M ND1 1 
ATOM   7188  C  CD2 . HIS G  1 71  ? 15.745  0.879   54.777  1.00 27.70  ? 71  HIS M CD2 1 
ATOM   7189  C  CE1 . HIS G  1 71  ? 15.460  2.356   56.371  1.00 27.52  ? 71  HIS M CE1 1 
ATOM   7190  N  NE2 . HIS G  1 71  ? 16.126  2.105   55.259  1.00 27.55  ? 71  HIS M NE2 1 
ATOM   7191  N  N   . GLY G  1 72  ? 12.447  1.240   53.664  1.00 27.66  ? 72  GLY M N   1 
ATOM   7192  C  CA  . GLY G  1 72  ? 12.531  1.994   52.422  1.00 27.67  ? 72  GLY M CA  1 
ATOM   7193  C  C   . GLY G  1 72  ? 12.977  3.417   52.692  1.00 27.50  ? 72  GLY M C   1 
ATOM   7194  O  O   . GLY G  1 72  ? 13.414  3.746   53.797  1.00 27.41  ? 72  GLY M O   1 
ATOM   7195  N  N   . GLY G  1 73  ? 12.889  4.258   51.673  1.00 27.82  ? 73  GLY M N   1 
ATOM   7196  C  CA  . GLY G  1 73  ? 13.151  5.681   51.833  1.00 28.02  ? 73  GLY M CA  1 
ATOM   7197  C  C   . GLY G  1 73  ? 11.858  6.426   52.121  1.00 28.39  ? 73  GLY M C   1 
ATOM   7198  O  O   . GLY G  1 73  ? 10.770  5.870   51.946  1.00 28.59  ? 73  GLY M O   1 
ATOM   7199  N  N   . PRO G  1 74  ? 11.960  7.705   52.528  1.00 28.73  ? 74  PRO M N   1 
ATOM   7200  C  CA  . PRO G  1 74  ? 10.757  8.478   52.861  1.00 29.27  ? 74  PRO M CA  1 
ATOM   7201  C  C   . PRO G  1 74  ? 9.753   8.649   51.719  1.00 30.08  ? 74  PRO M C   1 
ATOM   7202  O  O   . PRO G  1 74  ? 8.564   8.806   51.991  1.00 30.54  ? 74  PRO M O   1 
ATOM   7203  C  CB  . PRO G  1 74  ? 11.313  9.840   53.309  1.00 29.70  ? 74  PRO M CB  1 
ATOM   7204  C  CG  . PRO G  1 74  ? 12.710  9.894   52.785  1.00 29.60  ? 74  PRO M CG  1 
ATOM   7205  C  CD  . PRO G  1 74  ? 13.192  8.479   52.761  1.00 28.84  ? 74  PRO M CD  1 
ATOM   7206  N  N   . LYS G  1 75  ? 10.225  8.608   50.469  1.00 30.40  ? 75  LYS M N   1 
ATOM   7207  C  CA  . LYS G  1 75  ? 9.355   8.707   49.288  1.00 31.46  ? 75  LYS M CA  1 
ATOM   7208  C  C   . LYS G  1 75  ? 8.623   7.406   48.914  1.00 31.45  ? 75  LYS M C   1 
ATOM   7209  O  O   . LYS G  1 75  ? 7.706   7.439   48.101  1.00 32.38  ? 75  LYS M O   1 
ATOM   7210  C  CB  . LYS G  1 75  ? 10.175  9.166   48.069  1.00 32.14  ? 75  LYS M CB  1 
ATOM   7211  C  CG  . LYS G  1 75  ? 10.838  10.540  48.210  1.00 32.72  ? 75  LYS M CG  1 
ATOM   7212  C  CD  . LYS G  1 75  ? 11.963  10.737  47.197  1.00 33.26  ? 75  LYS M CD  1 
ATOM   7213  C  CE  . LYS G  1 75  ? 11.432  10.823  45.781  1.00 34.63  ? 75  LYS M CE  1 
ATOM   7214  N  NZ  . LYS G  1 75  ? 12.516  11.052  44.789  1.00 35.46  ? 75  LYS M NZ  1 
ATOM   7215  N  N   . ASP G  1 76  ? 9.042   6.268   49.464  1.00 30.55  ? 76  ASP M N   1 
ATOM   7216  C  CA  . ASP G  1 76  ? 8.443   4.983   49.104  1.00 30.92  ? 76  ASP M CA  1 
ATOM   7217  C  C   . ASP G  1 76  ? 7.140   4.754   49.863  1.00 31.40  ? 76  ASP M C   1 
ATOM   7218  O  O   . ASP G  1 76  ? 7.011   5.150   51.028  1.00 30.98  ? 76  ASP M O   1 
ATOM   7219  C  CB  . ASP G  1 76  ? 9.394   3.827   49.424  1.00 30.17  ? 76  ASP M CB  1 
ATOM   7220  C  CG  . ASP G  1 76  ? 10.664  3.857   48.596  1.00 30.05  ? 76  ASP M CG  1 
ATOM   7221  O  OD1 . ASP G  1 76  ? 10.581  4.019   47.364  1.00 30.91  ? 76  ASP M OD1 1 
ATOM   7222  O  OD2 . ASP G  1 76  ? 11.752  3.695   49.176  1.00 29.59  ? 76  ASP M OD2 1 
ATOM   7223  N  N   . GLU G  1 77  ? 6.190   4.098   49.203  1.00 32.44  ? 77  GLU M N   1 
ATOM   7224  C  CA  . GLU G  1 77  ? 5.011   3.564   49.887  1.00 33.18  ? 77  GLU M CA  1 
ATOM   7225  C  C   . GLU G  1 77  ? 5.426   2.449   50.842  1.00 32.28  ? 77  GLU M C   1 
ATOM   7226  O  O   . GLU G  1 77  ? 4.940   2.377   51.973  1.00 32.37  ? 77  GLU M O   1 
ATOM   7227  C  CB  . GLU G  1 77  ? 3.996   3.021   48.878  1.00 34.89  ? 77  GLU M CB  1 
ATOM   7228  C  CG  . GLU G  1 77  ? 2.662   2.642   49.501  1.00 36.29  ? 77  GLU M CG  1 
ATOM   7229  C  CD  . GLU G  1 77  ? 1.769   3.844   49.731  0.75 37.41  ? 77  GLU M CD  1 
ATOM   7230  O  OE1 . GLU G  1 77  ? 1.067   4.241   48.777  0.75 39.04  ? 77  GLU M OE1 1 
ATOM   7231  O  OE2 . GLU G  1 77  ? 1.770   4.383   50.859  0.75 37.05  ? 77  GLU M OE2 1 
ATOM   7232  N  N   . GLU G  1 78  ? 6.303   1.569   50.371  1.00 31.72  ? 78  GLU M N   1 
ATOM   7233  C  CA  . GLU G  1 78  ? 6.869   0.518   51.210  1.00 31.14  ? 78  GLU M CA  1 
ATOM   7234  C  C   . GLU G  1 78  ? 8.029   1.082   52.046  1.00 29.75  ? 78  GLU M C   1 
ATOM   7235  O  O   . GLU G  1 78  ? 9.166   1.188   51.575  1.00 29.18  ? 78  GLU M O   1 
ATOM   7236  C  CB  . GLU G  1 78  ? 7.317   -0.675  50.351  1.00 31.63  ? 78  GLU M CB  1 
ATOM   7237  C  CG  . GLU G  1 78  ? 7.697   -1.937  51.134  1.00 31.78  ? 78  GLU M CG  1 
ATOM   7238  C  CD  . GLU G  1 78  ? 6.543   -2.577  51.897  1.00 32.90  ? 78  GLU M CD  1 
ATOM   7239  O  OE1 . GLU G  1 78  ? 5.371   -2.165  51.715  1.00 33.89  ? 78  GLU M OE1 1 
ATOM   7240  O  OE2 . GLU G  1 78  ? 6.796   -3.515  52.688  1.00 33.21  ? 78  GLU M OE2 1 
ATOM   7241  N  N   . ARG G  1 79  ? 7.711   1.468   53.279  1.00 29.36  ? 79  ARG M N   1 
ATOM   7242  C  CA  . ARG G  1 79  ? 8.686   2.000   54.235  1.00 28.39  ? 79  ARG M CA  1 
ATOM   7243  C  C   . ARG G  1 79  ? 8.169   1.772   55.647  1.00 28.63  ? 79  ARG M C   1 
ATOM   7244  O  O   . ARG G  1 79  ? 6.967   1.546   55.852  1.00 29.40  ? 79  ARG M O   1 
ATOM   7245  C  CB  . ARG G  1 79  ? 8.900   3.508   54.034  1.00 28.07  ? 79  ARG M CB  1 
ATOM   7246  C  CG  . ARG G  1 79  ? 7.627   4.339   54.212  1.00 28.78  ? 79  ARG M CG  1 
ATOM   7247  C  CD  . ARG G  1 79  ? 7.885   5.841   54.142  1.00 28.76  ? 79  ARG M CD  1 
ATOM   7248  N  NE  . ARG G  1 79  ? 8.125   6.426   55.453  1.00 28.58  ? 79  ARG M NE  1 
ATOM   7249  C  CZ  . ARG G  1 79  ? 8.167   7.736   55.714  1.00 28.94  ? 79  ARG M CZ  1 
ATOM   7250  N  NH1 . ARG G  1 79  ? 8.004   8.644   54.749  1.00 29.43  ? 79  ARG M NH1 1 
ATOM   7251  N  NH2 . ARG G  1 79  ? 8.376   8.152   56.965  1.00 29.01  ? 79  ARG M NH2 1 
ATOM   7252  N  N   . HIS G  1 80  ? 9.082   1.871   56.603  1.00 28.05  ? 80  HIS M N   1 
ATOM   7253  C  CA  . HIS G  1 80  ? 8.750   2.000   58.018  1.00 28.45  ? 80  HIS M CA  1 
ATOM   7254  C  C   . HIS G  1 80  ? 8.267   3.446   58.231  1.00 28.44  ? 80  HIS M C   1 
ATOM   7255  O  O   . HIS G  1 80  ? 8.717   4.352   57.523  1.00 27.98  ? 80  HIS M O   1 
ATOM   7256  C  CB  . HIS G  1 80  ? 9.980   1.703   58.909  1.00 28.29  ? 80  HIS M CB  1 
ATOM   7257  C  CG  . HIS G  1 80  ? 10.598  0.353   58.680  1.00 28.47  ? 80  HIS M CG  1 
ATOM   7258  N  ND1 . HIS G  1 80  ? 11.952  0.111   58.780  1.00 28.37  ? 80  HIS M ND1 1 
ATOM   7259  C  CD2 . HIS G  1 80  ? 10.035  -0.830  58.349  1.00 29.05  ? 80  HIS M CD2 1 
ATOM   7260  C  CE1 . HIS G  1 80  ? 12.189  -1.163  58.530  1.00 28.81  ? 80  HIS M CE1 1 
ATOM   7261  N  NE2 . HIS G  1 80  ? 11.042  -1.757  58.269  1.00 29.21  ? 80  HIS M NE2 1 
ATOM   7262  N  N   . VAL G  1 81  ? 7.357   3.664   59.184  1.00 29.10  ? 81  VAL M N   1 
ATOM   7263  C  CA  . VAL G  1 81  ? 6.953   5.026   59.554  1.00 29.40  ? 81  VAL M CA  1 
ATOM   7264  C  C   . VAL G  1 81  ? 8.180   5.876   59.941  1.00 28.87  ? 81  VAL M C   1 
ATOM   7265  O  O   . VAL G  1 81  ? 8.263   7.053   59.594  1.00 28.82  ? 81  VAL M O   1 
ATOM   7266  C  CB  . VAL G  1 81  ? 5.899   5.043   60.695  1.00 30.60  ? 81  VAL M CB  1 
ATOM   7267  C  CG1 . VAL G  1 81  ? 5.678   6.455   61.238  1.00 31.12  ? 81  VAL M CG1 1 
ATOM   7268  C  CG2 . VAL G  1 81  ? 4.566   4.471   60.217  1.00 31.54  ? 81  VAL M CG2 1 
ATOM   7269  N  N   . GLY G  1 82  ? 9.142   5.266   60.629  1.00 28.69  ? 82  GLY M N   1 
ATOM   7270  C  CA  . GLY G  1 82  ? 10.358  5.969   61.066  1.00 28.56  ? 82  GLY M CA  1 
ATOM   7271  C  C   . GLY G  1 82  ? 11.441  6.251   60.028  1.00 27.88  ? 82  GLY M C   1 
ATOM   7272  O  O   . GLY G  1 82  ? 12.509  6.783   60.382  1.00 28.01  ? 82  GLY M O   1 
ATOM   7273  N  N   . ASP G  1 83  ? 11.200  5.919   58.761  1.00 27.40  ? 83  ASP M N   1 
ATOM   7274  C  CA  . ASP G  1 83  ? 12.238  6.026   57.729  1.00 26.99  ? 83  ASP M CA  1 
ATOM   7275  C  C   . ASP G  1 83  ? 12.304  7.427   57.138  1.00 27.28  ? 83  ASP M C   1 
ATOM   7276  O  O   . ASP G  1 83  ? 11.663  7.707   56.133  1.00 27.40  ? 83  ASP M O   1 
ATOM   7277  C  CB  . ASP G  1 83  ? 11.994  5.004   56.615  1.00 26.62  ? 83  ASP M CB  1 
ATOM   7278  C  CG  . ASP G  1 83  ? 12.267  3.575   57.054  1.00 26.58  ? 83  ASP M CG  1 
ATOM   7279  O  OD1 . ASP G  1 83  ? 12.949  3.347   58.098  1.00 26.63  ? 83  ASP M OD1 1 
ATOM   7280  O  OD2 . ASP G  1 83  ? 11.784  2.660   56.332  1.00 26.49  ? 83  ASP M OD2 1 
ATOM   7281  N  N   . LEU G  1 84  ? 13.094  8.301   57.756  1.00 27.74  ? 84  LEU M N   1 
ATOM   7282  C  CA  . LEU G  1 84  ? 13.259  9.663   57.254  1.00 28.34  ? 84  LEU M CA  1 
ATOM   7283  C  C   . LEU G  1 84  ? 14.432  9.826   56.271  1.00 28.45  ? 84  LEU M C   1 
ATOM   7284  O  O   . LEU G  1 84  ? 14.725  10.940  55.855  1.00 29.21  ? 84  LEU M O   1 
ATOM   7285  C  CB  . LEU G  1 84  ? 13.354  10.652  58.418  1.00 29.12  ? 84  LEU M CB  1 
ATOM   7286  C  CG  . LEU G  1 84  ? 12.160  10.626  59.377  1.00 29.46  ? 84  LEU M CG  1 
ATOM   7287  C  CD1 . LEU G  1 84  ? 12.442  11.502  60.596  1.00 30.44  ? 84  LEU M CD1 1 
ATOM   7288  C  CD2 . LEU G  1 84  ? 10.890  11.059  58.679  1.00 29.73  ? 84  LEU M CD2 1 
ATOM   7289  N  N   . GLY G  1 85  ? 15.094  8.731   55.891  1.00 28.02  ? 85  GLY M N   1 
ATOM   7290  C  CA  . GLY G  1 85  ? 16.107  8.780   54.835  1.00 28.25  ? 85  GLY M CA  1 
ATOM   7291  C  C   . GLY G  1 85  ? 17.467  9.172   55.366  1.00 28.90  ? 85  GLY M C   1 
ATOM   7292  O  O   . GLY G  1 85  ? 17.869  8.727   56.439  1.00 29.03  ? 85  GLY M O   1 
ATOM   7293  N  N   . ASN G  1 86  ? 18.166  10.007  54.606  1.00 29.61  ? 86  ASN M N   1 
ATOM   7294  C  CA  . ASN G  1 86  ? 19.482  10.495  54.964  1.00 30.62  ? 86  ASN M CA  1 
ATOM   7295  C  C   . ASN G  1 86  ? 19.460  11.978  55.288  1.00 31.64  ? 86  ASN M C   1 
ATOM   7296  O  O   . ASN G  1 86  ? 18.588  12.718  54.818  1.00 31.65  ? 86  ASN M O   1 
ATOM   7297  C  CB  . ASN G  1 86  ? 20.458  10.236  53.811  1.00 31.14  ? 86  ASN M CB  1 
ATOM   7298  C  CG  . ASN G  1 86  ? 20.835  8.773   53.694  1.00 30.63  ? 86  ASN M CG  1 
ATOM   7299  O  OD1 . ASN G  1 86  ? 21.344  8.186   54.649  1.00 30.77  ? 86  ASN M OD1 1 
ATOM   7300  N  ND2 . ASN G  1 86  ? 20.595  8.177   52.531  1.00 30.22  ? 86  ASN M ND2 1 
ATOM   7301  N  N   . VAL G  1 87  ? 20.421  12.390  56.112  1.00 32.74  ? 87  VAL M N   1 
ATOM   7302  C  CA  . VAL G  1 87  ? 20.820  13.800  56.239  1.00 34.28  ? 87  VAL M CA  1 
ATOM   7303  C  C   . VAL G  1 87  ? 22.264  13.933  55.752  1.00 35.66  ? 87  VAL M C   1 
ATOM   7304  O  O   . VAL G  1 87  ? 23.039  12.972  55.822  1.00 35.57  ? 87  VAL M O   1 
ATOM   7305  C  CB  . VAL G  1 87  ? 20.660  14.355  57.672  1.00 34.89  ? 87  VAL M CB  1 
ATOM   7306  C  CG1 . VAL G  1 87  ? 19.209  14.246  58.108  1.00 33.85  ? 87  VAL M CG1 1 
ATOM   7307  C  CG2 . VAL G  1 87  ? 21.585  13.667  58.671  1.00 35.34  ? 87  VAL M CG2 1 
ATOM   7308  N  N   . THR G  1 88  ? 22.608  15.118  55.249  1.00 37.18  ? 88  THR M N   1 
ATOM   7309  C  CA  . THR G  1 88  ? 23.921  15.371  54.648  1.00 38.88  ? 88  THR M CA  1 
ATOM   7310  C  C   . THR G  1 88  ? 24.730  16.337  55.496  1.00 40.95  ? 88  THR M C   1 
ATOM   7311  O  O   . THR G  1 88  ? 24.280  17.447  55.780  1.00 41.71  ? 88  THR M O   1 
ATOM   7312  C  CB  . THR G  1 88  ? 23.796  15.968  53.235  1.00 39.53  ? 88  THR M CB  1 
ATOM   7313  O  OG1 . THR G  1 88  ? 22.934  15.149  52.444  1.00 37.83  ? 88  THR M OG1 1 
ATOM   7314  C  CG2 . THR G  1 88  ? 25.175  16.055  52.550  1.00 41.38  ? 88  THR M CG2 1 
ATOM   7315  N  N   . ALA G  1 89  ? 25.931  15.904  55.877  1.00 42.13  ? 89  ALA M N   1 
ATOM   7316  C  CA  . ALA G  1 89  ? 26.881  16.731  56.611  1.00 44.56  ? 89  ALA M CA  1 
ATOM   7317  C  C   . ALA G  1 89  ? 27.858  17.378  55.629  1.00 46.77  ? 89  ALA M C   1 
ATOM   7318  O  O   . ALA G  1 89  ? 28.380  16.706  54.732  1.00 46.72  ? 89  ALA M O   1 
ATOM   7319  C  CB  . ALA G  1 89  ? 27.632  15.887  57.622  1.00 44.96  ? 89  ALA M CB  1 
ATOM   7320  N  N   . ASP G  1 90  ? 28.106  18.676  55.806  1.00 48.96  ? 90  ASP M N   1 
ATOM   7321  C  CA  . ASP G  1 90  ? 29.067  19.414  54.972  1.00 51.61  ? 90  ASP M CA  1 
ATOM   7322  C  C   . ASP G  1 90  ? 30.514  19.075  55.378  1.00 53.75  ? 90  ASP M C   1 
ATOM   7323  O  O   . ASP G  1 90  ? 30.733  18.186  56.210  1.00 53.07  ? 90  ASP M O   1 
ATOM   7324  C  CB  . ASP G  1 90  ? 28.773  20.931  55.006  1.00 53.44  ? 90  ASP M CB  1 
ATOM   7325  C  CG  . ASP G  1 90  ? 28.999  21.576  56.384  1.00 54.99  ? 90  ASP M CG  1 
ATOM   7326  O  OD1 . ASP G  1 90  ? 29.601  20.957  57.287  1.00 55.24  ? 90  ASP M OD1 1 
ATOM   7327  O  OD2 . ASP G  1 90  ? 28.564  22.734  56.560  1.00 56.26  ? 90  ASP M OD2 1 
ATOM   7328  N  N   . LYS G  1 91  ? 31.494  19.765  54.793  1.00 56.62  ? 91  LYS M N   1 
ATOM   7329  C  CA  . LYS G  1 91  ? 32.912  19.506  55.100  1.00 59.14  ? 91  LYS M CA  1 
ATOM   7330  C  C   . LYS G  1 91  ? 33.345  19.874  56.535  1.00 60.74  ? 91  LYS M C   1 
ATOM   7331  O  O   . LYS G  1 91  ? 34.335  19.333  57.029  1.00 62.24  ? 91  LYS M O   1 
ATOM   7332  C  CB  . LYS G  1 91  ? 33.827  20.164  54.058  1.00 62.12  ? 91  LYS M CB  1 
ATOM   7333  C  CG  . LYS G  1 91  ? 33.936  21.681  54.123  1.00 64.84  ? 91  LYS M CG  1 
ATOM   7334  C  CD  . LYS G  1 91  ? 34.647  22.218  52.887  1.00 67.49  ? 91  LYS M CD  1 
ATOM   7335  C  CE  . LYS G  1 91  ? 35.290  23.571  53.143  1.00 71.41  ? 91  LYS M CE  1 
ATOM   7336  N  NZ  . LYS G  1 91  ? 34.298  24.607  53.540  1.00 71.07  ? 91  LYS M NZ  1 
ATOM   7337  N  N   . ASP G  1 92  ? 32.599  20.764  57.199  1.00 60.58  ? 92  ASP M N   1 
ATOM   7338  C  CA  . ASP G  1 92  ? 32.810  21.065  58.633  1.00 61.85  ? 92  ASP M CA  1 
ATOM   7339  C  C   . ASP G  1 92  ? 32.147  20.039  59.569  1.00 59.21  ? 92  ASP M C   1 
ATOM   7340  O  O   . ASP G  1 92  ? 32.192  20.203  60.788  1.00 60.13  ? 92  ASP M O   1 
ATOM   7341  C  CB  . ASP G  1 92  ? 32.265  22.457  58.996  1.00 63.09  ? 92  ASP M CB  1 
ATOM   7342  C  CG  . ASP G  1 92  ? 32.896  23.581  58.194  1.00 66.12  ? 92  ASP M CG  1 
ATOM   7343  O  OD1 . ASP G  1 92  ? 33.984  23.390  57.607  1.00 68.03  ? 92  ASP M OD1 1 
ATOM   7344  O  OD2 . ASP G  1 92  ? 32.290  24.673  58.165  1.00 66.85  ? 92  ASP M OD2 1 
ATOM   7345  N  N   . GLY G  1 93  ? 31.524  19.002  59.012  1.00 56.17  ? 93  GLY M N   1 
ATOM   7346  C  CA  . GLY G  1 93  ? 30.834  17.988  59.798  1.00 53.75  ? 93  GLY M CA  1 
ATOM   7347  C  C   . GLY G  1 93  ? 29.450  18.379  60.289  1.00 51.84  ? 93  GLY M C   1 
ATOM   7348  O  O   . GLY G  1 93  ? 28.893  17.692  61.147  1.00 50.43  ? 93  GLY M O   1 
ATOM   7349  N  N   . VAL G  1 94  ? 28.884  19.454  59.735  1.00 51.96  ? 94  VAL M N   1 
ATOM   7350  C  CA  . VAL G  1 94  ? 27.581  19.967  60.165  1.00 50.71  ? 94  VAL M CA  1 
ATOM   7351  C  C   . VAL G  1 94  ? 26.476  19.570  59.178  1.00 48.05  ? 94  VAL M C   1 
ATOM   7352  O  O   . VAL G  1 94  ? 26.551  19.884  57.989  1.00 48.24  ? 94  VAL M O   1 
ATOM   7353  C  CB  . VAL G  1 94  ? 27.599  21.503  60.315  1.00 53.09  ? 94  VAL M CB  1 
ATOM   7354  C  CG1 . VAL G  1 94  ? 26.232  22.017  60.770  1.00 52.03  ? 94  VAL M CG1 1 
ATOM   7355  C  CG2 . VAL G  1 94  ? 28.684  21.931  61.299  1.00 56.03  ? 94  VAL M CG2 1 
ATOM   7356  N  N   . ALA G  1 95  ? 25.455  18.885  59.679  1.00 45.86  ? 95  ALA M N   1 
ATOM   7357  C  CA  . ALA G  1 95  ? 24.251  18.594  58.897  1.00 43.67  ? 95  ALA M CA  1 
ATOM   7358  C  C   . ALA G  1 95  ? 23.149  19.550  59.313  1.00 43.81  ? 95  ALA M C   1 
ATOM   7359  O  O   . ALA G  1 95  ? 22.635  19.452  60.424  1.00 43.54  ? 95  ALA M O   1 
ATOM   7360  C  CB  . ALA G  1 95  ? 23.814  17.151  59.103  1.00 41.41  ? 95  ALA M CB  1 
ATOM   7361  N  N   . ASP G  1 96  ? 22.808  20.491  58.434  1.00 44.58  ? 96  ASP M N   1 
ATOM   7362  C  CA  . ASP G  1 96  ? 21.677  21.395  58.664  1.00 44.91  ? 96  ASP M CA  1 
ATOM   7363  C  C   . ASP G  1 96  ? 20.419  20.713  58.141  1.00 42.65  ? 96  ASP M C   1 
ATOM   7364  O  O   . ASP G  1 96  ? 20.128  20.755  56.948  1.00 42.36  ? 96  ASP M O   1 
ATOM   7365  C  CB  . ASP G  1 96  ? 21.895  22.754  57.995  1.00 47.22  ? 96  ASP M CB  1 
ATOM   7366  C  CG  . ASP G  1 96  ? 22.916  23.607  58.735  1.00 49.93  ? 96  ASP M CG  1 
ATOM   7367  O  OD1 . ASP G  1 96  ? 22.714  23.877  59.944  1.00 50.56  ? 96  ASP M OD1 1 
ATOM   7368  O  OD2 . ASP G  1 96  ? 23.919  24.010  58.113  1.00 51.70  ? 96  ASP M OD2 1 
ATOM   7369  N  N   . VAL G  1 97  ? 19.685  20.079  59.048  1.00 41.33  ? 97  VAL M N   1 
ATOM   7370  C  CA  . VAL G  1 97  ? 18.559  19.231  58.672  1.00 39.30  ? 97  VAL M CA  1 
ATOM   7371  C  C   . VAL G  1 97  ? 17.368  20.103  58.275  1.00 39.80  ? 97  VAL M C   1 
ATOM   7372  O  O   . VAL G  1 97  ? 17.088  21.114  58.914  1.00 41.26  ? 97  VAL M O   1 
ATOM   7373  C  CB  . VAL G  1 97  ? 18.173  18.249  59.803  1.00 38.08  ? 97  VAL M CB  1 
ATOM   7374  C  CG1 . VAL G  1 97  ? 16.988  17.384  59.390  1.00 36.32  ? 97  VAL M CG1 1 
ATOM   7375  C  CG2 . VAL G  1 97  ? 19.364  17.362  60.165  1.00 37.89  ? 97  VAL M CG2 1 
ATOM   7376  N  N   . SER G  1 98  ? 16.719  19.720  57.181  1.00 38.85  ? 98  SER M N   1 
ATOM   7377  C  CA  . SER G  1 98  ? 15.445  20.298  56.773  1.00 39.28  ? 98  SER M CA  1 
ATOM   7378  C  C   . SER G  1 98  ? 14.726  19.248  55.934  1.00 37.68  ? 98  SER M C   1 
ATOM   7379  O  O   . SER G  1 98  ? 15.082  19.003  54.781  1.00 37.49  ? 98  SER M O   1 
ATOM   7380  C  CB  . SER G  1 98  ? 15.629  21.603  55.998  1.00 41.36  ? 98  SER M CB  1 
ATOM   7381  O  OG  . SER G  1 98  ? 14.391  22.279  55.845  1.00 42.23  ? 98  SER M OG  1 
ATOM   7382  N  N   . ILE G  1 99  ? 13.751  18.598  56.561  1.00 36.71  ? 99  ILE M N   1 
ATOM   7383  C  CA  . ILE G  1 99  ? 12.965  17.527  55.959  1.00 35.39  ? 99  ILE M CA  1 
ATOM   7384  C  C   . ILE G  1 99  ? 11.494  17.833  56.229  1.00 35.96  ? 99  ILE M C   1 
ATOM   7385  O  O   . ILE G  1 99  ? 11.158  18.414  57.262  1.00 36.68  ? 99  ILE M O   1 
ATOM   7386  C  CB  . ILE G  1 99  ? 13.376  16.161  56.564  1.00 33.82  ? 99  ILE M CB  1 
ATOM   7387  C  CG1 . ILE G  1 99  ? 14.737  15.729  56.004  1.00 33.46  ? 99  ILE M CG1 1 
ATOM   7388  C  CG2 . ILE G  1 99  ? 12.333  15.077  56.298  1.00 32.75  ? 99  ILE M CG2 1 
ATOM   7389  C  CD1 . ILE G  1 99  ? 15.397  14.615  56.795  1.00 32.51  ? 99  ILE M CD1 1 
ATOM   7390  N  N   . GLU G  1 100 ? 10.637  17.473  55.276  1.00 35.87  ? 100 GLU M N   1 
ATOM   7391  C  CA  . GLU G  1 100 ? 9.187   17.538  55.435  1.00 36.52  ? 100 GLU M CA  1 
ATOM   7392  C  C   . GLU G  1 100 ? 8.671   16.135  55.134  1.00 35.12  ? 100 GLU M C   1 
ATOM   7393  O  O   . GLU G  1 100 ? 9.038   15.552  54.113  1.00 34.53  ? 100 GLU M O   1 
ATOM   7394  C  CB  . GLU G  1 100 ? 8.583   18.573  54.482  1.00 38.42  ? 100 GLU M CB  1 
ATOM   7395  C  CG  . GLU G  1 100 ? 7.130   18.914  54.771  1.00 39.76  ? 100 GLU M CG  1 
ATOM   7396  C  CD  . GLU G  1 100 ? 6.663   20.169  54.046  1.00 42.18  ? 100 GLU M CD  1 
ATOM   7397  O  OE1 . GLU G  1 100 ? 7.231   21.254  54.306  1.00 43.49  ? 100 GLU M OE1 1 
ATOM   7398  O  OE2 . GLU G  1 100 ? 5.723   20.077  53.220  1.00 43.10  ? 100 GLU M OE2 1 
ATOM   7399  N  N   . ASP G  1 101 ? 7.873   15.575  56.040  1.00 34.76  ? 101 ASP M N   1 
ATOM   7400  C  CA  . ASP G  1 101 ? 7.394   14.200  55.901  1.00 33.67  ? 101 ASP M CA  1 
ATOM   7401  C  C   . ASP G  1 101 ? 5.943   14.081  56.346  1.00 34.48  ? 101 ASP M C   1 
ATOM   7402  O  O   . ASP G  1 101 ? 5.550   14.695  57.342  1.00 35.32  ? 101 ASP M O   1 
ATOM   7403  C  CB  . ASP G  1 101 ? 8.253   13.266  56.736  1.00 32.36  ? 101 ASP M CB  1 
ATOM   7404  C  CG  . ASP G  1 101 ? 8.013   11.805  56.404  1.00 31.44  ? 101 ASP M CG  1 
ATOM   7405  O  OD1 . ASP G  1 101 ? 8.444   11.370  55.312  1.00 31.04  ? 101 ASP M OD1 1 
ATOM   7406  O  OD2 . ASP G  1 101 ? 7.399   11.085  57.224  1.00 31.33  ? 101 ASP M OD2 1 
ATOM   7407  N  N   . SER G  1 102 ? 5.173   13.266  55.625  1.00 34.41  ? 102 SER M N   1 
ATOM   7408  C  CA  . SER G  1 102 ? 3.722   13.115  55.846  1.00 35.61  ? 102 SER M CA  1 
ATOM   7409  C  C   . SER G  1 102 ? 3.289   11.759  56.407  1.00 34.98  ? 102 SER M C   1 
ATOM   7410  O  O   . SER G  1 102 ? 2.088   11.528  56.597  1.00 36.22  ? 102 SER M O   1 
ATOM   7411  C  CB  . SER G  1 102 ? 2.984   13.389  54.537  1.00 36.83  ? 102 SER M CB  1 
ATOM   7412  O  OG  . SER G  1 102 ? 2.931   14.781  54.315  1.00 38.23  ? 102 SER M OG  1 
ATOM   7413  N  N   . VAL G  1 103 ? 4.247   10.872  56.663  1.00 33.35  ? 103 VAL M N   1 
ATOM   7414  C  CA  . VAL G  1 103 ? 3.962   9.557   57.231  1.00 32.94  ? 103 VAL M CA  1 
ATOM   7415  C  C   . VAL G  1 103 ? 4.139   9.575   58.757  1.00 32.94  ? 103 VAL M C   1 
ATOM   7416  O  O   . VAL G  1 103 ? 3.292   9.036   59.483  1.00 33.73  ? 103 VAL M O   1 
ATOM   7417  C  CB  . VAL G  1 103 ? 4.830   8.471   56.568  1.00 31.63  ? 103 VAL M CB  1 
ATOM   7418  C  CG1 . VAL G  1 103 ? 4.600   7.115   57.222  1.00 31.48  ? 103 VAL M CG1 1 
ATOM   7419  C  CG2 . VAL G  1 103 ? 4.503   8.398   55.076  1.00 32.00  ? 103 VAL M CG2 1 
ATOM   7420  N  N   . ILE G  1 104 ? 5.230   10.182  59.237  1.00 32.25  ? 104 ILE M N   1 
ATOM   7421  C  CA  . ILE G  1 104 ? 5.363   10.487  60.671  1.00 32.68  ? 104 ILE M CA  1 
ATOM   7422  C  C   . ILE G  1 104 ? 4.303   11.509  61.076  1.00 34.24  ? 104 ILE M C   1 
ATOM   7423  O  O   . ILE G  1 104 ? 3.743   12.209  60.233  1.00 34.90  ? 104 ILE M O   1 
ATOM   7424  C  CB  . ILE G  1 104 ? 6.770   11.014  61.093  1.00 32.09  ? 104 ILE M CB  1 
ATOM   7425  C  CG1 . ILE G  1 104 ? 7.145   12.334  60.392  1.00 32.42  ? 104 ILE M CG1 1 
ATOM   7426  C  CG2 . ILE G  1 104 ? 7.834   9.957   60.844  1.00 30.82  ? 104 ILE M CG2 1 
ATOM   7427  C  CD1 . ILE G  1 104 ? 8.324   13.058  61.011  1.00 32.52  ? 104 ILE M CD1 1 
ATOM   7428  N  N   . SER G  1 105 ? 4.054   11.593  62.374  1.00 35.01  ? 105 SER M N   1 
ATOM   7429  C  CA  . SER G  1 105 ? 3.114   12.556  62.912  1.00 36.79  ? 105 SER M CA  1 
ATOM   7430  C  C   . SER G  1 105 ? 3.474   12.910  64.345  1.00 37.49  ? 105 SER M C   1 
ATOM   7431  O  O   . SER G  1 105 ? 4.274   12.228  64.982  1.00 36.72  ? 105 SER M O   1 
ATOM   7432  C  CB  . SER G  1 105 ? 1.691   11.993  62.841  1.00 37.91  ? 105 SER M CB  1 
ATOM   7433  O  OG  . SER G  1 105 ? 0.747   13.024  63.033  1.00 39.80  ? 105 SER M OG  1 
ATOM   7434  N  N   . LEU G  1 106 ? 2.888   13.998  64.830  1.00 39.20  ? 106 LEU M N   1 
ATOM   7435  C  CA  . LEU G  1 106 ? 2.968   14.368  66.238  1.00 40.41  ? 106 LEU M CA  1 
ATOM   7436  C  C   . LEU G  1 106 ? 1.656   14.051  66.970  1.00 42.15  ? 106 LEU M C   1 
ATOM   7437  O  O   . LEU G  1 106 ? 1.448   14.528  68.080  1.00 43.68  ? 106 LEU M O   1 
ATOM   7438  C  CB  . LEU G  1 106 ? 3.353   15.847  66.383  1.00 41.41  ? 106 LEU M CB  1 
ATOM   7439  C  CG  . LEU G  1 106 ? 4.656   16.247  65.678  1.00 40.12  ? 106 LEU M CG  1 
ATOM   7440  C  CD1 . LEU G  1 106 ? 4.906   17.743  65.814  1.00 41.57  ? 106 LEU M CD1 1 
ATOM   7441  C  CD2 . LEU G  1 106 ? 5.839   15.453  66.215  1.00 38.86  ? 106 LEU M CD2 1 
ATOM   7442  N  N   . SER G  1 107 ? 0.786   13.241  66.350  1.00 42.14  ? 107 SER M N   1 
ATOM   7443  C  CA  . SER G  1 107 ? -0.385  12.659  67.025  1.00 43.82  ? 107 SER M CA  1 
ATOM   7444  C  C   . SER G  1 107 ? -0.901  11.405  66.301  1.00 43.28  ? 107 SER M C   1 
ATOM   7445  O  O   . SER G  1 107 ? -0.452  11.080  65.195  1.00 41.66  ? 107 SER M O   1 
ATOM   7446  C  CB  . SER G  1 107 ? -1.509  13.691  67.170  1.00 46.22  ? 107 SER M CB  1 
ATOM   7447  O  OG  . SER G  1 107 ? -2.172  13.916  65.943  1.00 46.48  ? 107 SER M OG  1 
ATOM   7448  N  N   . GLY G  1 108 ? -1.824  10.693  66.946  1.00 44.83  ? 108 GLY M N   1 
ATOM   7449  C  CA  . GLY G  1 108 ? -2.412  9.470   66.386  1.00 44.87  ? 108 GLY M CA  1 
ATOM   7450  C  C   . GLY G  1 108 ? -1.478  8.272   66.399  1.00 43.12  ? 108 GLY M C   1 
ATOM   7451  O  O   . GLY G  1 108 ? -0.451  8.284   67.074  1.00 42.22  ? 108 GLY M O   1 
ATOM   7452  N  N   . ASP G  1 109 ? -1.826  7.248   65.621  1.00 42.89  ? 109 ASP M N   1 
ATOM   7453  C  CA  . ASP G  1 109 ? -1.101  5.967   65.608  1.00 41.73  ? 109 ASP M CA  1 
ATOM   7454  C  C   . ASP G  1 109 ? 0.365   6.072   65.151  1.00 39.43  ? 109 ASP M C   1 
ATOM   7455  O  O   . ASP G  1 109 ? 1.207   5.314   65.612  1.00 38.79  ? 109 ASP M O   1 
ATOM   7456  C  CB  . ASP G  1 109 ? -1.828  4.945   64.719  1.00 42.18  ? 109 ASP M CB  1 
ATOM   7457  C  CG  . ASP G  1 109 ? -3.198  4.546   65.258  1.00 44.83  ? 109 ASP M CG  1 
ATOM   7458  O  OD1 . ASP G  1 109 ? -3.465  4.736   66.466  1.00 46.25  ? 109 ASP M OD1 1 
ATOM   7459  O  OD2 . ASP G  1 109 ? -4.016  4.035   64.459  1.00 45.73  ? 109 ASP M OD2 1 
ATOM   7460  N  N   . HIS G  1 110 ? 0.655   7.013   64.256  1.00 38.55  ? 110 HIS M N   1 
ATOM   7461  C  CA  . HIS G  1 110 ? 2.011   7.232   63.747  1.00 36.69  ? 110 HIS M CA  1 
ATOM   7462  C  C   . HIS G  1 110 ? 2.754   8.342   64.513  1.00 36.56  ? 110 HIS M C   1 
ATOM   7463  O  O   . HIS G  1 110 ? 3.742   8.886   64.008  1.00 35.39  ? 110 HIS M O   1 
ATOM   7464  C  CB  . HIS G  1 110 ? 1.941   7.550   62.247  1.00 36.11  ? 110 HIS M CB  1 
ATOM   7465  C  CG  . HIS G  1 110 ? 1.426   6.419   61.410  1.00 36.23  ? 110 HIS M CG  1 
ATOM   7466  N  ND1 . HIS G  1 110 ? 1.388   6.474   60.032  1.00 35.95  ? 110 HIS M ND1 1 
ATOM   7467  C  CD2 . HIS G  1 110 ? 0.961   5.193   61.749  1.00 36.94  ? 110 HIS M CD2 1 
ATOM   7468  C  CE1 . HIS G  1 110 ? 0.890   5.344   59.560  1.00 36.32  ? 110 HIS M CE1 1 
ATOM   7469  N  NE2 . HIS G  1 110 ? 0.625   4.548   60.582  1.00 36.96  ? 110 HIS M NE2 1 
ATOM   7470  N  N   . CYS G  1 111 ? 2.290   8.660   65.729  1.00 37.96  ? 111 CYS M N   1 
ATOM   7471  C  CA  . CYS G  1 111 ? 2.930   9.651   66.583  1.00 38.27  ? 111 CYS M CA  1 
ATOM   7472  C  C   . CYS G  1 111 ? 4.330   9.198   66.974  1.00 37.10  ? 111 CYS M C   1 
ATOM   7473  O  O   . CYS G  1 111 ? 4.530   8.044   67.347  1.00 36.93  ? 111 CYS M O   1 
ATOM   7474  C  CB  . CYS G  1 111 ? 2.122   9.903   67.859  1.00 40.37  ? 111 CYS M CB  1 
ATOM   7475  S  SG  . CYS G  1 111 ? 2.743   11.290  68.829  1.00 41.34  ? 111 CYS M SG  1 
ATOM   7476  N  N   . ILE G  1 112 ? 5.278   10.126  66.887  1.00 36.54  ? 112 ILE M N   1 
ATOM   7477  C  CA  . ILE G  1 112 ? 6.686   9.849   67.185  1.00 35.73  ? 112 ILE M CA  1 
ATOM   7478  C  C   . ILE G  1 112 ? 7.161   10.427  68.523  1.00 36.99  ? 112 ILE M C   1 
ATOM   7479  O  O   . ILE G  1 112 ? 8.283   10.149  68.941  1.00 36.78  ? 112 ILE M O   1 
ATOM   7480  C  CB  . ILE G  1 112 ? 7.610   10.296  66.027  1.00 34.33  ? 112 ILE M CB  1 
ATOM   7481  C  CG1 . ILE G  1 112 ? 7.570   11.817  65.804  1.00 34.95  ? 112 ILE M CG1 1 
ATOM   7482  C  CG2 . ILE G  1 112 ? 7.227   9.548   64.756  1.00 33.22  ? 112 ILE M CG2 1 
ATOM   7483  C  CD1 . ILE G  1 112 ? 8.592   12.313  64.804  1.00 34.03  ? 112 ILE M CD1 1 
ATOM   7484  N  N   . ILE G  1 113 ? 6.311   11.209  69.190  1.00 38.54  ? 113 ILE M N   1 
ATOM   7485  C  CA  . ILE G  1 113 ? 6.613   11.729  70.525  1.00 40.14  ? 113 ILE M CA  1 
ATOM   7486  C  C   . ILE G  1 113 ? 6.735   10.557  71.506  1.00 40.74  ? 113 ILE M C   1 
ATOM   7487  O  O   . ILE G  1 113 ? 5.916   9.647   71.495  1.00 40.92  ? 113 ILE M O   1 
ATOM   7488  C  CB  . ILE G  1 113 ? 5.540   12.740  71.001  1.00 41.96  ? 113 ILE M CB  1 
ATOM   7489  C  CG1 . ILE G  1 113 ? 5.604   14.013  70.144  1.00 41.77  ? 113 ILE M CG1 1 
ATOM   7490  C  CG2 . ILE G  1 113 ? 5.745   13.112  72.466  1.00 43.92  ? 113 ILE M CG2 1 
ATOM   7491  C  CD1 . ILE G  1 113 ? 4.462   14.986  70.371  1.00 43.62  ? 113 ILE M CD1 1 
ATOM   7492  N  N   . GLY G  1 114 ? 7.774   10.587  72.337  1.00 41.32  ? 114 GLY M N   1 
ATOM   7493  C  CA  . GLY G  1 114 ? 8.068   9.496   73.262  1.00 42.12  ? 114 GLY M CA  1 
ATOM   7494  C  C   . GLY G  1 114 ? 8.893   8.362   72.674  1.00 40.68  ? 114 GLY M C   1 
ATOM   7495  O  O   . GLY G  1 114 ? 9.117   7.352   73.342  1.00 41.48  ? 114 GLY M O   1 
ATOM   7496  N  N   . ARG G  1 115 ? 9.348   8.516   71.436  1.00 38.82  ? 115 ARG M N   1 
ATOM   7497  C  CA  . ARG G  1 115 ? 10.186  7.519   70.774  1.00 37.56  ? 115 ARG M CA  1 
ATOM   7498  C  C   . ARG G  1 115 ? 11.546  8.161   70.548  1.00 37.18  ? 115 ARG M C   1 
ATOM   7499  O  O   . ARG G  1 115 ? 11.778  9.265   71.048  1.00 38.10  ? 115 ARG M O   1 
ATOM   7500  C  CB  . ARG G  1 115 ? 9.526   7.067   69.475  1.00 36.06  ? 115 ARG M CB  1 
ATOM   7501  C  CG  . ARG G  1 115 ? 8.084   6.616   69.672  1.00 36.76  ? 115 ARG M CG  1 
ATOM   7502  C  CD  . ARG G  1 115 ? 7.512   6.018   68.402  1.00 35.55  ? 115 ARG M CD  1 
ATOM   7503  N  NE  . ARG G  1 115 ? 6.099   5.680   68.569  1.00 36.53  ? 115 ARG M NE  1 
ATOM   7504  C  CZ  . ARG G  1 115 ? 5.625   4.553   69.103  1.00 37.53  ? 115 ARG M CZ  1 
ATOM   7505  N  NH1 . ARG G  1 115 ? 6.433   3.584   69.534  1.00 37.67  ? 115 ARG M NH1 1 
ATOM   7506  N  NH2 . ARG G  1 115 ? 4.312   4.382   69.188  1.00 38.65  ? 115 ARG M NH2 1 
ATOM   7507  N  N   . THR G  1 116 ? 12.445  7.482   69.831  1.00 36.12  ? 116 THR M N   1 
ATOM   7508  C  CA  . THR G  1 116 ? 13.850  7.914   69.726  1.00 36.19  ? 116 THR M CA  1 
ATOM   7509  C  C   . THR G  1 116 ? 14.246  8.270   68.302  1.00 34.65  ? 116 THR M C   1 
ATOM   7510  O  O   . THR G  1 116 ? 14.045  7.479   67.388  1.00 33.43  ? 116 THR M O   1 
ATOM   7511  C  CB  . THR G  1 116 ? 14.803  6.817   70.242  1.00 36.93  ? 116 THR M CB  1 
ATOM   7512  O  OG1 . THR G  1 116 ? 14.487  6.522   71.604  1.00 38.66  ? 116 THR M OG1 1 
ATOM   7513  C  CG2 . THR G  1 116 ? 16.260  7.254   70.162  1.00 37.42  ? 116 THR M CG2 1 
ATOM   7514  N  N   . LEU G  1 117 ? 14.812  9.464   68.134  1.00 34.94  ? 117 LEU M N   1 
ATOM   7515  C  CA  . LEU G  1 117 ? 15.441  9.871   66.882  1.00 34.00  ? 117 LEU M CA  1 
ATOM   7516  C  C   . LEU G  1 117 ? 16.913  9.459   66.934  1.00 34.56  ? 117 LEU M C   1 
ATOM   7517  O  O   . LEU G  1 117 ? 17.584  9.677   67.949  1.00 36.02  ? 117 LEU M O   1 
ATOM   7518  C  CB  . LEU G  1 117 ? 15.325  11.384  66.709  1.00 34.48  ? 117 LEU M CB  1 
ATOM   7519  C  CG  . LEU G  1 117 ? 15.872  12.000  65.425  1.00 33.87  ? 117 LEU M CG  1 
ATOM   7520  C  CD1 . LEU G  1 117 ? 15.078  11.539  64.214  1.00 32.36  ? 117 LEU M CD1 1 
ATOM   7521  C  CD2 . LEU G  1 117 ? 15.872  13.517  65.551  1.00 35.02  ? 117 LEU M CD2 1 
ATOM   7522  N  N   . VAL G  1 118 ? 17.397  8.856   65.850  1.00 33.61  ? 118 VAL M N   1 
ATOM   7523  C  CA  . VAL G  1 118 ? 18.763  8.336   65.771  1.00 34.26  ? 118 VAL M CA  1 
ATOM   7524  C  C   . VAL G  1 118 ? 19.414  8.788   64.474  1.00 33.75  ? 118 VAL M C   1 
ATOM   7525  O  O   . VAL G  1 118 ? 18.821  8.646   63.394  1.00 32.43  ? 118 VAL M O   1 
ATOM   7526  C  CB  . VAL G  1 118 ? 18.799  6.791   65.805  1.00 34.00  ? 118 VAL M CB  1 
ATOM   7527  C  CG1 . VAL G  1 118 ? 20.239  6.284   65.788  1.00 35.02  ? 118 VAL M CG1 1 
ATOM   7528  C  CG2 . VAL G  1 118 ? 18.073  6.266   67.032  1.00 34.75  ? 118 VAL M CG2 1 
ATOM   7529  N  N   . VAL G  1 119 ? 20.633  9.314   64.585  1.00 35.08  ? 119 VAL M N   1 
ATOM   7530  C  CA  . VAL G  1 119 ? 21.475  9.596   63.421  1.00 35.10  ? 119 VAL M CA  1 
ATOM   7531  C  C   . VAL G  1 119 ? 22.566  8.521   63.365  1.00 35.87  ? 119 VAL M C   1 
ATOM   7532  O  O   . VAL G  1 119 ? 23.200  8.209   64.382  1.00 37.25  ? 119 VAL M O   1 
ATOM   7533  C  CB  . VAL G  1 119 ? 22.031  11.048  63.410  1.00 36.37  ? 119 VAL M CB  1 
ATOM   7534  C  CG1 . VAL G  1 119 ? 23.024  11.314  64.545  1.00 38.49  ? 119 VAL M CG1 1 
ATOM   7535  C  CG2 . VAL G  1 119 ? 22.674  11.363  62.065  1.00 36.28  ? 119 VAL M CG2 1 
ATOM   7536  N  N   . HIS G  1 120 ? 22.771  7.962   62.174  1.00 35.21  ? 120 HIS M N   1 
ATOM   7537  C  CA  . HIS G  1 120 ? 23.553  6.732   61.994  1.00 35.80  ? 120 HIS M CA  1 
ATOM   7538  C  C   . HIS G  1 120 ? 24.934  6.966   61.403  1.00 37.26  ? 120 HIS M C   1 
ATOM   7539  O  O   . HIS G  1 120 ? 25.227  8.043   60.882  1.00 37.62  ? 120 HIS M O   1 
ATOM   7540  C  CB  . HIS G  1 120 ? 22.780  5.750   61.109  1.00 34.22  ? 120 HIS M CB  1 
ATOM   7541  C  CG  . HIS G  1 120 ? 21.715  5.000   61.837  1.00 33.63  ? 120 HIS M CG  1 
ATOM   7542  N  ND1 . HIS G  1 120 ? 21.901  3.719   62.309  1.00 34.22  ? 120 HIS M ND1 1 
ATOM   7543  C  CD2 . HIS G  1 120 ? 20.454  5.352   62.180  1.00 32.77  ? 120 HIS M CD2 1 
ATOM   7544  C  CE1 . HIS G  1 120 ? 20.799  3.314   62.916  1.00 33.75  ? 120 HIS M CE1 1 
ATOM   7545  N  NE2 . HIS G  1 120 ? 19.906  4.287   62.852  1.00 32.88  ? 120 HIS M NE2 1 
ATOM   7546  N  N   . GLU G  1 121 ? 25.759  5.919   61.490  1.00 38.40  ? 121 GLU M N   1 
ATOM   7547  C  CA  . GLU G  1 121 ? 27.181  5.916   61.074  1.00 40.26  ? 121 GLU M CA  1 
ATOM   7548  C  C   . GLU G  1 121 ? 27.383  6.298   59.609  1.00 39.74  ? 121 GLU M C   1 
ATOM   7549  O  O   . GLU G  1 121 ? 28.218  7.143   59.288  1.00 41.03  ? 121 GLU M O   1 
ATOM   7550  C  CB  . GLU G  1 121 ? 27.773  4.513   61.310  1.00 41.35  ? 121 GLU M CB  1 
ATOM   7551  C  CG  . GLU G  1 121 ? 29.269  4.330   61.046  1.00 43.75  ? 121 GLU M CG  1 
ATOM   7552  C  CD  . GLU G  1 121 ? 29.670  2.857   60.923  1.00 44.56  ? 121 GLU M CD  1 
ATOM   7553  O  OE1 . GLU G  1 121 ? 28.913  1.961   61.366  1.00 43.82  ? 121 GLU M OE1 1 
ATOM   7554  O  OE2 . GLU G  1 121 ? 30.747  2.584   60.358  1.00 46.26  ? 121 GLU M OE2 1 
ATOM   7555  N  N   . LYS G  1 122 ? 26.613  5.665   58.730  1.00 38.07  ? 122 LYS M N   1 
ATOM   7556  C  CA  . LYS G  1 122 ? 26.795  5.811   57.289  1.00 37.75  ? 122 LYS M CA  1 
ATOM   7557  C  C   . LYS G  1 122 ? 25.455  5.952   56.558  1.00 35.60  ? 122 LYS M C   1 
ATOM   7558  O  O   . LYS G  1 122 ? 24.402  6.072   57.193  1.00 34.45  ? 122 LYS M O   1 
ATOM   7559  C  CB  . LYS G  1 122 ? 27.656  4.652   56.766  1.00 38.85  ? 122 LYS M CB  1 
ATOM   7560  C  CG  . LYS G  1 122 ? 27.092  3.258   56.969  1.00 38.15  ? 122 LYS M CG  1 
ATOM   7561  C  CD  . LYS G  1 122 ? 28.204  2.212   56.912  1.00 40.00  ? 122 LYS M CD  1 
ATOM   7562  C  CE  . LYS G  1 122 ? 27.636  0.797   57.010  1.00 39.55  ? 122 LYS M CE  1 
ATOM   7563  N  NZ  . LYS G  1 122 ? 28.706  -0.229  56.849  1.00 41.57  ? 122 LYS M NZ  1 
ATOM   7564  N  N   . ALA G  1 123 ? 25.506  5.987   55.228  1.00 35.23  ? 123 ALA M N   1 
ATOM   7565  C  CA  . ALA G  1 123 ? 24.318  6.180   54.398  1.00 33.62  ? 123 ALA M CA  1 
ATOM   7566  C  C   . ALA G  1 123 ? 23.255  5.095   54.575  1.00 32.15  ? 123 ALA M C   1 
ATOM   7567  O  O   . ALA G  1 123 ? 23.569  3.914   54.692  1.00 32.46  ? 123 ALA M O   1 
ATOM   7568  C  CB  . ALA G  1 123 ? 24.720  6.269   52.931  1.00 34.08  ? 123 ALA M CB  1 
ATOM   7569  N  N   . ASP G  1 124 ? 21.998  5.530   54.627  1.00 30.85  ? 124 ASP M N   1 
ATOM   7570  C  CA  . ASP G  1 124 ? 20.832  4.664   54.479  1.00 29.61  ? 124 ASP M CA  1 
ATOM   7571  C  C   . ASP G  1 124 ? 20.695  4.416   52.977  1.00 29.30  ? 124 ASP M C   1 
ATOM   7572  O  O   . ASP G  1 124 ? 20.584  5.378   52.214  1.00 29.38  ? 124 ASP M O   1 
ATOM   7573  C  CB  . ASP G  1 124 ? 19.595  5.396   55.038  1.00 28.90  ? 124 ASP M CB  1 
ATOM   7574  C  CG  . ASP G  1 124 ? 18.316  4.564   55.010  1.00 28.14  ? 124 ASP M CG  1 
ATOM   7575  O  OD1 . ASP G  1 124 ? 18.217  3.572   54.253  1.00 28.02  ? 124 ASP M OD1 1 
ATOM   7576  O  OD2 . ASP G  1 124 ? 17.369  4.939   55.747  1.00 27.88  ? 124 ASP M OD2 1 
ATOM   7577  N  N   . ASP G  1 125 ? 20.700  3.145   52.561  1.00 29.09  ? 125 ASP M N   1 
ATOM   7578  C  CA  . ASP G  1 125 ? 20.533  2.782   51.141  1.00 29.11  ? 125 ASP M CA  1 
ATOM   7579  C  C   . ASP G  1 125 ? 19.062  2.792   50.677  1.00 28.25  ? 125 ASP M C   1 
ATOM   7580  O  O   . ASP G  1 125 ? 18.769  2.473   49.520  1.00 28.43  ? 125 ASP M O   1 
ATOM   7581  C  CB  . ASP G  1 125 ? 21.232  1.441   50.797  1.00 29.80  ? 125 ASP M CB  1 
ATOM   7582  C  CG  . ASP G  1 125 ? 20.557  0.207   51.423  1.00 29.43  ? 125 ASP M CG  1 
ATOM   7583  O  OD1 . ASP G  1 125 ? 19.384  0.269   51.865  1.00 28.56  ? 125 ASP M OD1 1 
ATOM   7584  O  OD2 . ASP G  1 125 ? 21.217  -0.858  51.449  1.00 30.23  ? 125 ASP M OD2 1 
ATOM   7585  N  N   . LEU G  1 126 ? 18.153  3.110   51.599  1.00 27.54  ? 126 LEU M N   1 
ATOM   7586  C  CA  . LEU G  1 126 ? 16.742  3.346   51.306  1.00 27.06  ? 126 LEU M CA  1 
ATOM   7587  C  C   . LEU G  1 126 ? 16.041  2.066   50.830  1.00 26.99  ? 126 LEU M C   1 
ATOM   7588  O  O   . LEU G  1 126 ? 15.116  2.127   50.033  1.00 27.07  ? 126 LEU M O   1 
ATOM   7589  C  CB  . LEU G  1 126 ? 16.580  4.495   50.298  1.00 27.40  ? 126 LEU M CB  1 
ATOM   7590  C  CG  . LEU G  1 126 ? 17.400  5.774   50.554  1.00 27.84  ? 126 LEU M CG  1 
ATOM   7591  C  CD1 . LEU G  1 126 ? 17.155  6.780   49.445  1.00 28.46  ? 126 LEU M CD1 1 
ATOM   7592  C  CD2 . LEU G  1 126 ? 17.091  6.391   51.913  1.00 27.53  ? 126 LEU M CD2 1 
ATOM   7593  N  N   . GLY G  1 127 ? 16.483  0.913   51.334  1.00 27.08  ? 127 GLY M N   1 
ATOM   7594  C  CA  . GLY G  1 127 ? 15.905  -0.373  50.963  1.00 27.34  ? 127 GLY M CA  1 
ATOM   7595  C  C   . GLY G  1 127 ? 16.303  -0.940  49.613  1.00 27.97  ? 127 GLY M C   1 
ATOM   7596  O  O   . GLY G  1 127 ? 15.765  -1.969  49.212  1.00 28.41  ? 127 GLY M O   1 
ATOM   7597  N  N   . LYS G  1 128 ? 17.276  -0.329  48.928  1.00 28.25  ? 128 LYS M N   1 
ATOM   7598  C  CA  . LYS G  1 128 ? 17.663  -0.756  47.565  1.00 29.12  ? 128 LYS M CA  1 
ATOM   7599  C  C   . LYS G  1 128 ? 18.987  -1.549  47.507  1.00 29.92  ? 128 LYS M C   1 
ATOM   7600  O  O   . LYS G  1 128 ? 19.529  -1.764  46.428  1.00 30.78  ? 128 LYS M O   1 
ATOM   7601  C  CB  . LYS G  1 128 ? 17.755  0.469   46.648  1.00 29.42  ? 128 LYS M CB  1 
ATOM   7602  C  CG  . LYS G  1 128 ? 16.500  1.342   46.654  1.00 29.00  ? 128 LYS M CG  1 
ATOM   7603  C  CD  . LYS G  1 128 ? 16.738  2.682   45.968  1.00 29.49  ? 128 LYS M CD  1 
ATOM   7604  C  CE  . LYS G  1 128 ? 16.619  2.566   44.464  1.00 30.66  ? 128 LYS M CE  1 
ATOM   7605  N  NZ  . LYS G  1 128 ? 16.704  3.902   43.816  1.00 31.39  ? 128 LYS M NZ  1 
ATOM   7606  N  N   . GLY G  1 129 ? 19.496  -1.984  48.661  1.00 29.82  ? 129 GLY M N   1 
ATOM   7607  C  CA  . GLY G  1 129 ? 20.770  -2.698  48.736  1.00 30.89  ? 129 GLY M CA  1 
ATOM   7608  C  C   . GLY G  1 129 ? 20.759  -4.162  48.316  1.00 31.82  ? 129 GLY M C   1 
ATOM   7609  O  O   . GLY G  1 129 ? 21.828  -4.757  48.129  1.00 33.03  ? 129 GLY M O   1 
ATOM   7610  N  N   . GLY G  1 130 ? 19.575  -4.760  48.198  1.00 31.48  ? 130 GLY M N   1 
ATOM   7611  C  CA  . GLY G  1 130 ? 19.452  -6.154  47.770  1.00 32.66  ? 130 GLY M CA  1 
ATOM   7612  C  C   . GLY G  1 130 ? 19.881  -7.234  48.755  1.00 33.56  ? 130 GLY M C   1 
ATOM   7613  O  O   . GLY G  1 130 ? 19.869  -8.412  48.395  1.00 34.77  ? 130 GLY M O   1 
ATOM   7614  N  N   . ASN G  1 131 ? 20.259  -6.854  49.981  1.00 33.25  ? 131 ASN M N   1 
ATOM   7615  C  CA  . ASN G  1 131 ? 20.567  -7.819  51.045  1.00 34.35  ? 131 ASN M CA  1 
ATOM   7616  C  C   . ASN G  1 131 ? 19.541  -7.720  52.171  1.00 33.67  ? 131 ASN M C   1 
ATOM   7617  O  O   . ASN G  1 131 ? 18.747  -6.778  52.224  1.00 32.26  ? 131 ASN M O   1 
ATOM   7618  C  CB  . ASN G  1 131 ? 22.020  -7.686  51.571  1.00 35.29  ? 131 ASN M CB  1 
ATOM   7619  C  CG  . ASN G  1 131 ? 22.289  -6.390  52.330  1.00 34.30  ? 131 ASN M CG  1 
ATOM   7620  O  OD1 . ASN G  1 131 ? 21.464  -5.480  52.376  1.00 32.80  ? 131 ASN M OD1 1 
ATOM   7621  N  ND2 . ASN G  1 131 ? 23.476  -6.301  52.925  1.00 35.40  ? 131 ASN M ND2 1 
ATOM   7622  N  N   . GLU G  1 132 ? 19.569  -8.709  53.058  1.00 34.97  ? 132 GLU M N   1 
ATOM   7623  C  CA  . GLU G  1 132 ? 18.638  -8.798  54.186  1.00 34.87  ? 132 GLU M CA  1 
ATOM   7624  C  C   . GLU G  1 132 ? 18.640  -7.516  55.020  1.00 33.79  ? 132 GLU M C   1 
ATOM   7625  O  O   . GLU G  1 132 ? 17.586  -6.975  55.356  1.00 32.77  ? 132 GLU M O   1 
ATOM   7626  C  CB  . GLU G  1 132 ? 19.003  -10.000 55.054  1.00 36.74  ? 132 GLU M CB  1 
ATOM   7627  C  CG  . GLU G  1 132 ? 18.097  -10.226 56.245  1.00 37.01  ? 132 GLU M CG  1 
ATOM   7628  C  CD  . GLU G  1 132 ? 18.603  -11.291 57.200  1.00 39.15  ? 132 GLU M CD  1 
ATOM   7629  O  OE1 . GLU G  1 132 ? 19.490  -12.090 56.821  1.00 40.70  ? 132 GLU M OE1 1 
ATOM   7630  O  OE2 . GLU G  1 132 ? 18.093  -11.327 58.342  1.00 39.55  ? 132 GLU M OE2 1 
ATOM   7631  N  N   . GLU G  1 133 ? 19.829  -7.019  55.328  1.00 34.24  ? 133 GLU M N   1 
ATOM   7632  C  CA  . GLU G  1 133 ? 19.962  -5.816  56.143  1.00 33.64  ? 133 GLU M CA  1 
ATOM   7633  C  C   . GLU G  1 133 ? 19.329  -4.564  55.491  1.00 32.09  ? 133 GLU M C   1 
ATOM   7634  O  O   . GLU G  1 133 ? 18.782  -3.701  56.197  1.00 31.27  ? 133 GLU M O   1 
ATOM   7635  C  CB  . GLU G  1 133 ? 21.439  -5.583  56.478  1.00 34.86  ? 133 GLU M CB  1 
ATOM   7636  C  CG  . GLU G  1 133 ? 21.687  -4.682  57.672  1.00 34.96  ? 133 GLU M CG  1 
ATOM   7637  C  CD  . GLU G  1 133 ? 21.073  -5.222  58.950  1.00 35.67  ? 133 GLU M CD  1 
ATOM   7638  O  OE1 . GLU G  1 133 ? 21.399  -6.364  59.338  1.00 37.30  ? 133 GLU M OE1 1 
ATOM   7639  O  OE2 . GLU G  1 133 ? 20.237  -4.511  59.550  1.00 34.92  ? 133 GLU M OE2 1 
ATOM   7640  N  N   . SER G  1 134 ? 19.358  -4.482  54.155  1.00 31.82  ? 134 SER M N   1 
ATOM   7641  C  CA  . SER G  1 134 ? 18.751  -3.346  53.458  1.00 30.70  ? 134 SER M CA  1 
ATOM   7642  C  C   . SER G  1 134 ? 17.253  -3.233  53.746  1.00 30.07  ? 134 SER M C   1 
ATOM   7643  O  O   . SER G  1 134 ? 16.745  -2.126  53.874  1.00 29.28  ? 134 SER M O   1 
ATOM   7644  C  CB  . SER G  1 134 ? 18.985  -3.415  51.943  1.00 30.83  ? 134 SER M CB  1 
ATOM   7645  O  OG  . SER G  1 134 ? 18.493  -2.243  51.308  1.00 29.91  ? 134 SER M OG  1 
ATOM   7646  N  N   . THR G  1 135 ? 16.577  -4.377  53.867  1.00 30.76  ? 135 THR M N   1 
ATOM   7647  C  CA  . THR G  1 135 ? 15.142  -4.437  54.166  1.00 30.64  ? 135 THR M CA  1 
ATOM   7648  C  C   . THR G  1 135 ? 14.790  -4.131  55.623  1.00 30.68  ? 135 THR M C   1 
ATOM   7649  O  O   . THR G  1 135 ? 13.616  -3.950  55.931  1.00 30.56  ? 135 THR M O   1 
ATOM   7650  C  CB  . THR G  1 135 ? 14.546  -5.840  53.887  1.00 31.73  ? 135 THR M CB  1 
ATOM   7651  O  OG1 . THR G  1 135 ? 15.092  -6.799  54.815  1.00 32.80  ? 135 THR M OG1 1 
ATOM   7652  C  CG2 . THR G  1 135 ? 14.804  -6.277  52.463  1.00 32.10  ? 135 THR M CG2 1 
ATOM   7653  N  N   . LYS G  1 136 ? 15.784  -4.102  56.513  1.00 31.14  ? 136 LYS M N   1 
ATOM   7654  C  CA  . LYS G  1 136 ? 15.564  -3.821  57.934  1.00 31.39  ? 136 LYS M CA  1 
ATOM   7655  C  C   . LYS G  1 136 ? 16.064  -2.433  58.329  1.00 30.70  ? 136 LYS M C   1 
ATOM   7656  O  O   . LYS G  1 136 ? 15.307  -1.625  58.860  1.00 30.14  ? 136 LYS M O   1 
ATOM   7657  C  CB  . LYS G  1 136 ? 16.242  -4.896  58.771  1.00 32.91  ? 136 LYS M CB  1 
ATOM   7658  C  CG  . LYS G  1 136 ? 15.658  -6.284  58.544  1.00 33.97  ? 136 LYS M CG  1 
ATOM   7659  C  CD  . LYS G  1 136 ? 16.384  -7.343  59.355  1.00 35.77  ? 136 LYS M CD  1 
ATOM   7660  C  CE  . LYS G  1 136 ? 15.752  -8.710  59.131  1.00 37.07  ? 136 LYS M CE  1 
ATOM   7661  N  NZ  . LYS G  1 136 ? 16.522  -9.798  59.795  1.00 39.12  ? 136 LYS M NZ  1 
ATOM   7662  N  N   . THR G  1 137 ? 17.338  -2.160  58.066  1.00 30.87  ? 137 THR M N   1 
ATOM   7663  C  CA  . THR G  1 137 ? 17.977  -0.920  58.526  1.00 30.69  ? 137 THR M CA  1 
ATOM   7664  C  C   . THR G  1 137 ? 18.482  -0.010  57.421  1.00 30.13  ? 137 THR M C   1 
ATOM   7665  O  O   . THR G  1 137 ? 18.912  1.109   57.707  1.00 30.26  ? 137 THR M O   1 
ATOM   7666  C  CB  . THR G  1 137 ? 19.178  -1.240  59.443  1.00 32.00  ? 137 THR M CB  1 
ATOM   7667  O  OG1 . THR G  1 137 ? 20.129  -2.023  58.717  1.00 32.66  ? 137 THR M OG1 1 
ATOM   7668  C  CG2 . THR G  1 137 ? 18.732  -1.991  60.667  1.00 32.87  ? 137 THR M CG2 1 
ATOM   7669  N  N   . GLY G  1 138 ? 18.476  -0.478  56.177  1.00 29.87  ? 138 GLY M N   1 
ATOM   7670  C  CA  . GLY G  1 138 ? 19.096  0.253   55.081  1.00 29.70  ? 138 GLY M CA  1 
ATOM   7671  C  C   . GLY G  1 138 ? 20.625  0.319   55.121  1.00 30.71  ? 138 GLY M C   1 
ATOM   7672  O  O   . GLY G  1 138 ? 21.215  1.188   54.475  1.00 30.75  ? 138 GLY M O   1 
ATOM   7673  N  N   . ASN G  1 139 ? 21.256  -0.596  55.865  1.00 31.71  ? 139 ASN M N   1 
ATOM   7674  C  CA  . ASN G  1 139 ? 22.721  -0.661  56.027  1.00 33.14  ? 139 ASN M CA  1 
ATOM   7675  C  C   . ASN G  1 139 ? 23.348  0.650   56.512  1.00 33.51  ? 139 ASN M C   1 
ATOM   7676  O  O   . ASN G  1 139 ? 24.416  1.036   56.050  1.00 34.46  ? 139 ASN M O   1 
ATOM   7677  C  CB  . ASN G  1 139 ? 23.380  -1.127  54.716  1.00 33.68  ? 139 ASN M CB  1 
ATOM   7678  C  CG  . ASN G  1 139 ? 23.002  -2.544  54.348  1.00 33.88  ? 139 ASN M CG  1 
ATOM   7679  O  OD1 . ASN G  1 139 ? 23.430  -3.482  54.989  1.00 34.96  ? 139 ASN M OD1 1 
ATOM   7680  N  ND2 . ASN G  1 139 ? 22.199  -2.698  53.313  1.00 33.09  ? 139 ASN M ND2 1 
ATOM   7681  N  N   . ALA G  1 140 ? 22.677  1.332   57.440  1.00 33.00  ? 140 ALA M N   1 
ATOM   7682  C  CA  . ALA G  1 140 ? 23.161  2.620   57.964  1.00 33.54  ? 140 ALA M CA  1 
ATOM   7683  C  C   . ALA G  1 140 ? 24.205  2.475   59.088  1.00 35.30  ? 140 ALA M C   1 
ATOM   7684  O  O   . ALA G  1 140 ? 24.794  3.473   59.528  1.00 36.13  ? 140 ALA M O   1 
ATOM   7685  C  CB  . ALA G  1 140 ? 21.988  3.464   58.436  1.00 32.47  ? 140 ALA M CB  1 
ATOM   7686  N  N   . GLY G  1 141 ? 24.441  1.246   59.551  1.00 36.19  ? 141 GLY M N   1 
ATOM   7687  C  CA  . GLY G  1 141 ? 25.490  0.987   60.539  1.00 38.26  ? 141 GLY M CA  1 
ATOM   7688  C  C   . GLY G  1 141 ? 25.073  1.407   61.936  1.00 38.64  ? 141 GLY M C   1 
ATOM   7689  O  O   . GLY G  1 141 ? 23.883  1.500   62.234  1.00 37.43  ? 141 GLY M O   1 
ATOM   7690  N  N   . SER G  1 142 ? 26.057  1.694   62.780  1.00 40.68  ? 142 SER M N   1 
ATOM   7691  C  CA  . SER G  1 142 ? 25.820  1.948   64.202  1.00 41.61  ? 142 SER M CA  1 
ATOM   7692  C  C   . SER G  1 142 ? 25.150  3.296   64.493  1.00 40.63  ? 142 SER M C   1 
ATOM   7693  O  O   . SER G  1 142 ? 25.105  4.193   63.649  1.00 39.66  ? 142 SER M O   1 
ATOM   7694  C  CB  . SER G  1 142 ? 27.138  1.849   64.966  1.00 44.44  ? 142 SER M CB  1 
ATOM   7695  O  OG  . SER G  1 142 ? 28.071  2.759   64.428  1.00 45.25  ? 142 SER M OG  1 
ATOM   7696  N  N   . ARG G  1 143 ? 24.662  3.419   65.721  1.00 41.15  ? 143 ARG M N   1 
ATOM   7697  C  CA  . ARG G  1 143 ? 23.885  4.564   66.171  1.00 40.47  ? 143 ARG M CA  1 
ATOM   7698  C  C   . ARG G  1 143 ? 24.819  5.581   66.828  1.00 42.24  ? 143 ARG M C   1 
ATOM   7699  O  O   . ARG G  1 143 ? 25.288  5.362   67.941  1.00 44.20  ? 143 ARG M O   1 
ATOM   7700  C  CB  . ARG G  1 143 ? 22.795  4.075   67.137  1.00 40.40  ? 143 ARG M CB  1 
ATOM   7701  C  CG  . ARG G  1 143 ? 21.963  2.945   66.529  1.00 39.09  ? 143 ARG M CG  1 
ATOM   7702  C  CD  . ARG G  1 143 ? 20.866  2.400   67.426  1.00 39.27  ? 143 ARG M CD  1 
ATOM   7703  N  NE  . ARG G  1 143 ? 20.232  1.236   66.793  1.00 38.42  ? 143 ARG M NE  1 
ATOM   7704  C  CZ  . ARG G  1 143 ? 19.155  0.589   67.250  1.00 38.43  ? 143 ARG M CZ  1 
ATOM   7705  N  NH1 . ARG G  1 143 ? 18.544  0.969   68.370  1.00 39.22  ? 143 ARG M NH1 1 
ATOM   7706  N  NH2 . ARG G  1 143 ? 18.678  -0.452  66.569  1.00 37.86  ? 143 ARG M NH2 1 
ATOM   7707  N  N   . LEU G  1 144 ? 25.097  6.681   66.125  1.00 41.77  ? 144 LEU M N   1 
ATOM   7708  C  CA  . LEU G  1 144 ? 26.083  7.676   66.576  1.00 43.73  ? 144 LEU M CA  1 
ATOM   7709  C  C   . LEU G  1 144 ? 25.556  8.601   67.664  1.00 44.31  ? 144 LEU M C   1 
ATOM   7710  O  O   . LEU G  1 144 ? 26.257  8.890   68.626  1.00 46.57  ? 144 LEU M O   1 
ATOM   7711  C  CB  . LEU G  1 144 ? 26.569  8.532   65.408  1.00 43.48  ? 144 LEU M CB  1 
ATOM   7712  C  CG  . LEU G  1 144 ? 27.188  7.845   64.190  1.00 43.08  ? 144 LEU M CG  1 
ATOM   7713  C  CD1 . LEU G  1 144 ? 27.584  8.916   63.182  1.00 43.18  ? 144 LEU M CD1 1 
ATOM   7714  C  CD2 . LEU G  1 144 ? 28.378  6.982   64.565  1.00 45.18  ? 144 LEU M CD2 1 
ATOM   7715  N  N   . ALA G  1 145 ? 24.339  9.102   67.483  1.00 42.46  ? 145 ALA M N   1 
ATOM   7716  C  CA  . ALA G  1 145 ? 23.681  9.918   68.500  1.00 43.04  ? 145 ALA M CA  1 
ATOM   7717  C  C   . ALA G  1 145 ? 22.192  9.640   68.503  1.00 41.13  ? 145 ALA M C   1 
ATOM   7718  O  O   . ALA G  1 145 ? 21.621  9.266   67.475  1.00 39.18  ? 145 ALA M O   1 
ATOM   7719  C  CB  . ALA G  1 145 ? 23.949  11.392  68.260  1.00 43.76  ? 145 ALA M CB  1 
ATOM   7720  N  N   . ALA G  1 146 ? 21.575  9.815   69.668  1.00 41.92  ? 146 ALA M N   1 
ATOM   7721  C  CA  . ALA G  1 146 ? 20.145  9.577   69.834  1.00 40.63  ? 146 ALA M CA  1 
ATOM   7722  C  C   . ALA G  1 146 ? 19.548  10.455  70.918  1.00 41.84  ? 146 ALA M C   1 
ATOM   7723  O  O   . ALA G  1 146 ? 20.260  11.051  71.725  1.00 43.82  ? 146 ALA M O   1 
ATOM   7724  C  CB  . ALA G  1 146 ? 19.893  8.112   70.158  1.00 40.44  ? 146 ALA M CB  1 
ATOM   7725  N  N   . GLY G  1 147 ? 18.224  10.530  70.916  1.00 40.79  ? 147 GLY M N   1 
ATOM   7726  C  CA  . GLY G  1 147 ? 17.489  11.204  71.973  1.00 42.05  ? 147 GLY M CA  1 
ATOM   7727  C  C   . GLY G  1 147 ? 16.004  10.951  71.864  1.00 40.96  ? 147 GLY M C   1 
ATOM   7728  O  O   . GLY G  1 147 ? 15.491  10.671  70.773  1.00 39.09  ? 147 GLY M O   1 
ATOM   7729  N  N   . VAL G  1 148 ? 15.314  11.082  72.992  1.00 42.33  ? 148 VAL M N   1 
ATOM   7730  C  CA  . VAL G  1 148 ? 13.876  10.864  73.056  1.00 41.87  ? 148 VAL M CA  1 
ATOM   7731  C  C   . VAL G  1 148 ? 13.192  12.121  72.512  1.00 41.54  ? 148 VAL M C   1 
ATOM   7732  O  O   . VAL G  1 148 ? 13.637  13.240  72.788  1.00 42.68  ? 148 VAL M O   1 
ATOM   7733  C  CB  . VAL G  1 148 ? 13.412  10.556  74.497  1.00 43.91  ? 148 VAL M CB  1 
ATOM   7734  C  CG1 . VAL G  1 148 ? 11.906  10.309  74.553  1.00 43.73  ? 148 VAL M CG1 1 
ATOM   7735  C  CG2 . VAL G  1 148 ? 14.175  9.358   75.053  1.00 44.66  ? 148 VAL M CG2 1 
ATOM   7736  N  N   . ILE G  1 149 ? 12.126  11.935  71.734  1.00 40.22  ? 149 ILE M N   1 
ATOM   7737  C  CA  . ILE G  1 149 ? 11.401  13.053  71.132  1.00 40.06  ? 149 ILE M CA  1 
ATOM   7738  C  C   . ILE G  1 149 ? 10.388  13.578  72.147  1.00 41.86  ? 149 ILE M C   1 
ATOM   7739  O  O   . ILE G  1 149 ? 9.516   12.839  72.595  1.00 42.14  ? 149 ILE M O   1 
ATOM   7740  C  CB  . ILE G  1 149 ? 10.704  12.643  69.811  1.00 38.23  ? 149 ILE M CB  1 
ATOM   7741  C  CG1 . ILE G  1 149 ? 11.746  12.093  68.815  1.00 36.68  ? 149 ILE M CG1 1 
ATOM   7742  C  CG2 . ILE G  1 149 ? 9.971   13.841  69.207  1.00 38.46  ? 149 ILE M CG2 1 
ATOM   7743  C  CD1 . ILE G  1 149 ? 11.179  11.478  67.550  1.00 35.05  ? 149 ILE M CD1 1 
ATOM   7744  N  N   . GLY G  1 150 ? 10.506  14.854  72.501  1.00 43.31  ? 150 GLY M N   1 
ATOM   7745  C  CA  . GLY G  1 150 ? 9.672   15.452  73.541  1.00 45.47  ? 150 GLY M CA  1 
ATOM   7746  C  C   . GLY G  1 150 ? 8.787   16.559  73.019  1.00 45.98  ? 150 GLY M C   1 
ATOM   7747  O  O   . GLY G  1 150 ? 9.068   17.138  71.974  1.00 45.05  ? 150 GLY M O   1 
ATOM   7748  N  N   . ILE G  1 151 ? 7.728   16.857  73.769  1.00 47.78  ? 151 ILE M N   1 
ATOM   7749  C  CA  . ILE G  1 151 ? 6.804   17.946  73.445  1.00 48.90  ? 151 ILE M CA  1 
ATOM   7750  C  C   . ILE G  1 151 ? 7.505   19.276  73.711  1.00 50.48  ? 151 ILE M C   1 
ATOM   7751  O  O   . ILE G  1 151 ? 8.186   19.423  74.727  1.00 51.84  ? 151 ILE M O   1 
ATOM   7752  C  CB  . ILE G  1 151 ? 5.503   17.862  74.284  1.00 50.74  ? 151 ILE M CB  1 
ATOM   7753  C  CG1 . ILE G  1 151 ? 4.733   16.574  73.951  1.00 49.55  ? 151 ILE M CG1 1 
ATOM   7754  C  CG2 . ILE G  1 151 ? 4.614   19.080  74.037  1.00 52.33  ? 151 ILE M CG2 1 
ATOM   7755  C  CD1 . ILE G  1 151 ? 3.709   16.169  74.993  1.00 51.50  ? 151 ILE M CD1 1 
ATOM   7756  N  N   . ALA G  1 152 ? 7.336   20.231  72.797  1.00 50.57  ? 152 ALA M N   1 
ATOM   7757  C  CA  . ALA G  1 152 ? 7.961   21.559  72.898  1.00 52.28  ? 152 ALA M CA  1 
ATOM   7758  C  C   . ALA G  1 152 ? 6.888   22.646  72.905  1.00 54.40  ? 152 ALA M C   1 
ATOM   7759  O  O   . ALA G  1 152 ? 5.749   22.403  72.497  1.00 54.20  ? 152 ALA M O   1 
ATOM   7760  C  CB  . ALA G  1 152 ? 8.938   21.776  71.749  1.00 50.81  ? 152 ALA M CB  1 
ATOM   7761  N  N   . GLN G  1 153 ? 7.257   23.839  73.372  1.00 56.75  ? 153 GLN M N   1 
ATOM   7762  C  CA  . GLN G  1 153 ? 6.310   24.953  73.515  1.00 59.29  ? 153 GLN M CA  1 
ATOM   7763  C  C   . GLN G  1 153 ? 6.005   25.601  72.166  1.00 58.97  ? 153 GLN M C   1 
ATOM   7764  O  O   . GLN G  1 153 ? 6.846   25.620  71.270  1.00 57.56  ? 153 GLN M O   1 
ATOM   7765  C  CB  . GLN G  1 153 ? 6.849   26.010  74.488  1.00 62.16  ? 153 GLN M CB  1 
ATOM   7766  C  CG  . GLN G  1 153 ? 5.805   27.035  74.915  1.00 65.17  ? 153 GLN M CG  1 
ATOM   7767  C  CD  . GLN G  1 153 ? 6.281   27.951  76.026  1.00 68.23  ? 153 GLN M CD  1 
ATOM   7768  O  OE1 . GLN G  1 153 ? 7.428   28.399  76.031  1.00 68.64  ? 153 GLN M OE1 1 
ATOM   7769  N  NE2 . GLN G  1 153 ? 5.394   28.244  76.971  1.00 70.72  ? 153 GLN M NE2 1 
ATOM   7770  O  OXT . GLN G  1 153 ? 4.913   26.126  71.945  1.00 60.39  ? 153 GLN M OXT 1 
ATOM   7771  N  N   . ALA H  1 1   ? -0.447  -3.833  78.566  1.00 57.62  ? 1   ALA O N   1 
ATOM   7772  C  CA  . ALA H  1 1   ? -0.025  -2.726  79.479  1.00 56.83  ? 1   ALA O CA  1 
ATOM   7773  C  C   . ALA H  1 1   ? 0.895   -1.733  78.765  1.00 54.97  ? 1   ALA O C   1 
ATOM   7774  O  O   . ALA H  1 1   ? 1.771   -2.138  77.997  1.00 54.47  ? 1   ALA O O   1 
ATOM   7775  C  CB  . ALA H  1 1   ? 0.666   -3.289  80.715  1.00 57.75  ? 1   ALA O CB  1 
ATOM   7776  N  N   . THR H  1 2   ? 0.686   -0.441  79.016  1.00 54.22  ? 2   THR O N   1 
ATOM   7777  C  CA  . THR H  1 2   ? 1.556   0.610   78.485  1.00 52.67  ? 2   THR O CA  1 
ATOM   7778  C  C   . THR H  1 2   ? 2.720   0.800   79.464  1.00 52.42  ? 2   THR O C   1 
ATOM   7779  O  O   . THR H  1 2   ? 2.510   0.888   80.685  1.00 53.26  ? 2   THR O O   1 
ATOM   7780  C  CB  . THR H  1 2   ? 0.781   1.933   78.282  1.00 52.36  ? 2   THR O CB  1 
ATOM   7781  O  OG1 . THR H  1 2   ? -0.445  1.665   77.596  1.00 53.04  ? 2   THR O OG1 1 
ATOM   7782  C  CG2 . THR H  1 2   ? 1.581   2.929   77.465  1.00 51.11  ? 2   THR O CG2 1 
ATOM   7783  N  N   . LYS H  1 3   ? 3.940   0.828   78.927  1.00 51.46  ? 3   LYS O N   1 
ATOM   7784  C  CA  . LYS H  1 3   ? 5.153   1.024   79.719  1.00 51.41  ? 3   LYS O CA  1 
ATOM   7785  C  C   . LYS H  1 3   ? 5.923   2.240   79.221  1.00 50.25  ? 3   LYS O C   1 
ATOM   7786  O  O   . LYS H  1 3   ? 5.935   2.533   78.019  1.00 49.40  ? 3   LYS O O   1 
ATOM   7787  C  CB  . LYS H  1 3   ? 6.055   -0.202  79.632  1.00 51.95  ? 3   LYS O CB  1 
ATOM   7788  C  CG  . LYS H  1 3   ? 5.410   -1.497  80.089  1.00 53.32  ? 3   LYS O CG  1 
ATOM   7789  C  CD  . LYS H  1 3   ? 6.458   -2.586  80.245  0.70 54.20  ? 3   LYS O CD  1 
ATOM   7790  C  CE  . LYS H  1 3   ? 5.858   -3.897  80.720  0.70 55.88  ? 3   LYS O CE  1 
ATOM   7791  N  NZ  . LYS H  1 3   ? 6.918   -4.853  81.147  0.70 57.13  ? 3   LYS O NZ  1 
ATOM   7792  N  N   . ALA H  1 4   ? 6.559   2.944   80.154  1.00 50.39  ? 4   ALA O N   1 
ATOM   7793  C  CA  . ALA H  1 4   ? 7.450   4.055   79.827  1.00 49.67  ? 4   ALA O CA  1 
ATOM   7794  C  C   . ALA H  1 4   ? 8.721   3.973   80.669  1.00 50.33  ? 4   ALA O C   1 
ATOM   7795  O  O   . ALA H  1 4   ? 8.807   3.167   81.600  1.00 51.38  ? 4   ALA O O   1 
ATOM   7796  C  CB  . ALA H  1 4   ? 6.745   5.391   80.027  1.00 49.46  ? 4   ALA O CB  1 
ATOM   7797  N  N   . VAL H  1 5   ? 9.704   4.798   80.316  1.00 49.95  ? 5   VAL O N   1 
ATOM   7798  C  CA  . VAL H  1 5   ? 10.980  4.853   81.023  1.00 50.83  ? 5   VAL O CA  1 
ATOM   7799  C  C   . VAL H  1 5   ? 11.602  6.245   80.895  1.00 50.69  ? 5   VAL O C   1 
ATOM   7800  O  O   . VAL H  1 5   ? 11.360  6.957   79.912  1.00 49.82  ? 5   VAL O O   1 
ATOM   7801  C  CB  . VAL H  1 5   ? 11.946  3.759   80.510  1.00 51.11  ? 5   VAL O CB  1 
ATOM   7802  C  CG1 . VAL H  1 5   ? 12.420  4.052   79.091  1.00 50.20  ? 5   VAL O CG1 1 
ATOM   7803  C  CG2 . VAL H  1 5   ? 13.130  3.583   81.453  1.00 52.48  ? 5   VAL O CG2 1 
ATOM   7804  N  N   . CYS H  1 6   ? 12.392  6.622   81.898  1.00 51.87  ? 6   CYS O N   1 
ATOM   7805  C  CA  . CYS H  1 6   ? 13.025  7.933   81.952  1.00 52.17  ? 6   CYS O CA  1 
ATOM   7806  C  C   . CYS H  1 6   ? 14.393  7.870   82.630  1.00 53.60  ? 6   CYS O C   1 
ATOM   7807  O  O   . CYS H  1 6   ? 14.501  7.439   83.776  1.00 54.85  ? 6   CYS O O   1 
ATOM   7808  C  CB  . CYS H  1 6   ? 12.128  8.910   82.704  1.00 52.50  ? 6   CYS O CB  1 
ATOM   7809  S  SG  . CYS H  1 6   ? 12.804  10.577  82.825  1.00 53.22  ? 6   CYS O SG  1 
ATOM   7810  N  N   . VAL H  1 7   ? 15.424  8.304   81.906  1.00 53.66  ? 7   VAL O N   1 
ATOM   7811  C  CA  . VAL H  1 7   ? 16.776  8.434   82.439  1.00 55.27  ? 7   VAL O CA  1 
ATOM   7812  C  C   . VAL H  1 7   ? 16.952  9.880   82.892  1.00 56.03  ? 7   VAL O C   1 
ATOM   7813  O  O   . VAL H  1 7   ? 16.852  10.796  82.077  1.00 55.36  ? 7   VAL O O   1 
ATOM   7814  C  CB  . VAL H  1 7   ? 17.841  8.089   81.372  1.00 55.24  ? 7   VAL O CB  1 
ATOM   7815  C  CG1 . VAL H  1 7   ? 19.252  8.199   81.953  1.00 57.19  ? 7   VAL O CG1 1 
ATOM   7816  C  CG2 . VAL H  1 7   ? 17.599  6.692   80.812  1.00 54.62  ? 7   VAL O CG2 1 
ATOM   7817  N  N   . LEU H  1 8   ? 17.211  10.075  84.184  1.00 57.73  ? 8   LEU O N   1 
ATOM   7818  C  CA  . LEU H  1 8   ? 17.426  11.406  84.757  1.00 58.90  ? 8   LEU O CA  1 
ATOM   7819  C  C   . LEU H  1 8   ? 18.915  11.741  84.761  1.00 60.53  ? 8   LEU O C   1 
ATOM   7820  O  O   . LEU H  1 8   ? 19.721  10.980  85.297  1.00 61.90  ? 8   LEU O O   1 
ATOM   7821  C  CB  . LEU H  1 8   ? 16.876  11.470  86.184  1.00 60.19  ? 8   LEU O CB  1 
ATOM   7822  C  CG  . LEU H  1 8   ? 15.370  11.235  86.337  1.00 59.11  ? 8   LEU O CG  1 
ATOM   7823  C  CD1 . LEU H  1 8   ? 15.008  10.959  87.787  1.00 60.80  ? 8   LEU O CD1 1 
ATOM   7824  C  CD2 . LEU H  1 8   ? 14.581  12.422  85.812  1.00 58.23  ? 8   LEU O CD2 1 
ATOM   7825  N  N   . LYS H  1 9   ? 19.270  12.872  84.150  1.00 60.65  ? 9   LYS O N   1 
ATOM   7826  C  CA  . LYS H  1 9   ? 20.651  13.379  84.124  1.00 62.45  ? 9   LYS O CA  1 
ATOM   7827  C  C   . LYS H  1 9   ? 20.661  14.885  84.368  1.00 63.46  ? 9   LYS O C   1 
ATOM   7828  O  O   . LYS H  1 9   ? 19.691  15.570  84.050  1.00 62.43  ? 9   LYS O O   1 
ATOM   7829  C  CB  . LYS H  1 9   ? 21.300  13.072  82.769  1.00 61.74  ? 9   LYS O CB  1 
ATOM   7830  C  CG  . LYS H  1 9   ? 21.763  11.631  82.618  1.00 61.73  ? 9   LYS O CG  1 
ATOM   7831  C  CD  . LYS H  1 9   ? 22.072  11.285  81.169  1.00 60.75  ? 9   LYS O CD  1 
ATOM   7832  C  CE  . LYS H  1 9   ? 22.538  9.843   81.027  1.00 60.98  ? 9   LYS O CE  1 
ATOM   7833  N  NZ  . LYS H  1 9   ? 22.325  9.340   79.640  1.00 59.56  ? 9   LYS O NZ  1 
ATOM   7834  N  N   . GLY H  1 10  ? 21.758  15.396  84.919  1.00 65.74  ? 10  GLY O N   1 
ATOM   7835  C  CA  . GLY H  1 10  ? 21.914  16.835  85.148  1.00 67.12  ? 10  GLY O CA  1 
ATOM   7836  C  C   . GLY H  1 10  ? 23.347  17.297  85.013  1.00 69.28  ? 10  GLY O C   1 
ATOM   7837  O  O   . GLY H  1 10  ? 24.195  16.585  84.472  1.00 69.40  ? 10  GLY O O   1 
ATOM   7838  N  N   . ASP H  1 11  ? 23.607  18.507  85.501  1.00 71.20  ? 11  ASP O N   1 
ATOM   7839  C  CA  . ASP H  1 11  ? 24.968  19.048  85.572  1.00 73.85  ? 11  ASP O CA  1 
ATOM   7840  C  C   . ASP H  1 11  ? 25.755  18.387  86.705  1.00 76.05  ? 11  ASP O C   1 
ATOM   7841  O  O   . ASP H  1 11  ? 26.955  18.145  86.570  1.00 77.79  ? 11  ASP O O   1 
ATOM   7842  C  CB  . ASP H  1 11  ? 24.947  20.571  85.779  1.00 75.53  ? 11  ASP O CB  1 
ATOM   7843  C  CG  . ASP H  1 11  ? 24.287  21.324  84.624  1.00 73.90  ? 11  ASP O CG  1 
ATOM   7844  O  OD1 . ASP H  1 11  ? 24.361  20.864  83.463  1.00 72.28  ? 11  ASP O OD1 1 
ATOM   7845  O  OD2 . ASP H  1 11  ? 23.692  22.391  84.882  1.00 74.51  ? 11  ASP O OD2 1 
ATOM   7846  N  N   . GLY H  1 12  ? 25.072  18.103  87.815  1.00 76.23  ? 12  GLY O N   1 
ATOM   7847  C  CA  . GLY H  1 12  ? 25.685  17.483  88.991  1.00 78.55  ? 12  GLY O CA  1 
ATOM   7848  C  C   . GLY H  1 12  ? 25.803  15.968  88.917  1.00 77.59  ? 12  GLY O C   1 
ATOM   7849  O  O   . GLY H  1 12  ? 25.698  15.388  87.833  1.00 75.38  ? 12  GLY O O   1 
ATOM   7850  N  N   . PRO H  1 13  ? 26.033  15.315  90.076  1.00 79.51  ? 13  PRO O N   1 
ATOM   7851  C  CA  . PRO H  1 13  ? 26.119  13.857  90.143  1.00 79.06  ? 13  PRO O CA  1 
ATOM   7852  C  C   . PRO H  1 13  ? 24.764  13.135  90.293  1.00 76.72  ? 13  PRO O C   1 
ATOM   7853  O  O   . PRO H  1 13  ? 24.753  11.909  90.422  1.00 76.56  ? 13  PRO O O   1 
ATOM   7854  C  CB  . PRO H  1 13  ? 26.991  13.631  91.380  1.00 82.78  ? 13  PRO O CB  1 
ATOM   7855  C  CG  . PRO H  1 13  ? 26.645  14.766  92.278  1.00 84.35  ? 13  PRO O CG  1 
ATOM   7856  C  CD  . PRO H  1 13  ? 26.294  15.932  91.392  1.00 82.66  ? 13  PRO O CD  1 
ATOM   7857  N  N   . VAL H  1 14  ? 23.646  13.867  90.263  1.00 75.15  ? 14  VAL O N   1 
ATOM   7858  C  CA  . VAL H  1 14  ? 22.322  13.276  90.486  1.00 73.34  ? 14  VAL O CA  1 
ATOM   7859  C  C   . VAL H  1 14  ? 21.875  12.536  89.220  1.00 70.33  ? 14  VAL O C   1 
ATOM   7860  O  O   . VAL H  1 14  ? 21.755  13.147  88.155  1.00 68.71  ? 14  VAL O O   1 
ATOM   7861  C  CB  . VAL H  1 14  ? 21.271  14.350  90.875  1.00 73.03  ? 14  VAL O CB  1 
ATOM   7862  C  CG1 . VAL H  1 14  ? 19.883  13.732  91.024  1.00 71.28  ? 14  VAL O CG1 1 
ATOM   7863  C  CG2 . VAL H  1 14  ? 21.676  15.062  92.166  1.00 76.28  ? 14  VAL O CG2 1 
ATOM   7864  N  N   . GLN H  1 15  ? 21.638  11.227  89.343  1.00 69.85  ? 15  GLN O N   1 
ATOM   7865  C  CA  . GLN H  1 15  ? 21.199  10.397  88.215  1.00 67.31  ? 15  GLN O CA  1 
ATOM   7866  C  C   . GLN H  1 15  ? 20.344  9.215   88.656  1.00 66.78  ? 15  GLN O C   1 
ATOM   7867  O  O   . GLN H  1 15  ? 20.378  8.808   89.818  1.00 68.72  ? 15  GLN O O   1 
ATOM   7868  C  CB  . GLN H  1 15  ? 22.402  9.892   87.408  1.00 67.68  ? 15  GLN O CB  1 
ATOM   7869  C  CG  . GLN H  1 15  ? 23.289  8.883   88.138  1.00 70.04  ? 15  GLN O CG  1 
ATOM   7870  C  CD  . GLN H  1 15  ? 24.529  8.498   87.348  1.00 70.78  ? 15  GLN O CD  1 
ATOM   7871  O  OE1 . GLN H  1 15  ? 25.583  8.222   87.922  1.00 73.46  ? 15  GLN O OE1 1 
ATOM   7872  N  NE2 . GLN H  1 15  ? 24.407  8.472   86.028  1.00 68.75  ? 15  GLN O NE2 1 
ATOM   7873  N  N   . GLY H  1 16  ? 19.593  8.661   87.707  1.00 64.38  ? 16  GLY O N   1 
ATOM   7874  C  CA  . GLY H  1 16  ? 18.710  7.531   87.984  1.00 63.83  ? 16  GLY O CA  1 
ATOM   7875  C  C   . GLY H  1 16  ? 17.783  7.142   86.847  1.00 61.21  ? 16  GLY O C   1 
ATOM   7876  O  O   . GLY H  1 16  ? 17.598  7.898   85.891  1.00 59.64  ? 16  GLY O O   1 
ATOM   7877  N  N   . ILE H  1 17  ? 17.201  5.950   86.979  1.00 61.01  ? 17  ILE O N   1 
ATOM   7878  C  CA  . ILE H  1 17  ? 16.244  5.400   86.021  1.00 58.97  ? 17  ILE O CA  1 
ATOM   7879  C  C   . ILE H  1 17  ? 14.889  5.258   86.716  1.00 58.85  ? 17  ILE O C   1 
ATOM   7880  O  O   . ILE H  1 17  ? 14.803  4.642   87.776  1.00 60.49  ? 17  ILE O O   1 
ATOM   7881  C  CB  . ILE H  1 17  ? 16.719  4.022   85.501  1.00 59.16  ? 17  ILE O CB  1 
ATOM   7882  C  CG1 . ILE H  1 17  ? 18.016  4.178   84.691  1.00 59.31  ? 17  ILE O CG1 1 
ATOM   7883  C  CG2 . ILE H  1 17  ? 15.644  3.347   84.653  1.00 57.48  ? 17  ILE O CG2 1 
ATOM   7884  C  CD1 . ILE H  1 17  ? 18.789  2.891   84.503  1.00 60.41  ? 17  ILE O CD1 1 
ATOM   7885  N  N   . ILE H  1 18  ? 13.843  5.831   86.115  1.00 57.16  ? 18  ILE O N   1 
ATOM   7886  C  CA  . ILE H  1 18  ? 12.472  5.737   86.631  1.00 57.10  ? 18  ILE O CA  1 
ATOM   7887  C  C   . ILE H  1 18  ? 11.582  5.038   85.598  1.00 55.52  ? 18  ILE O C   1 
ATOM   7888  O  O   . ILE H  1 18  ? 11.469  5.495   84.452  1.00 53.92  ? 18  ILE O O   1 
ATOM   7889  C  CB  . ILE H  1 18  ? 11.890  7.134   86.961  1.00 57.05  ? 18  ILE O CB  1 
ATOM   7890  C  CG1 . ILE H  1 18  ? 12.707  7.820   88.067  1.00 58.97  ? 18  ILE O CG1 1 
ATOM   7891  C  CG2 . ILE H  1 18  ? 10.415  7.040   87.364  1.00 57.07  ? 18  ILE O CG2 1 
ATOM   7892  C  CD1 . ILE H  1 18  ? 12.471  7.280   89.462  1.00 61.06  ? 18  ILE O CD1 1 
ATOM   7893  N  N   . ASN H  1 19  ? 10.957  3.939   86.021  1.00 56.18  ? 19  ASN O N   1 
ATOM   7894  C  CA  . ASN H  1 19  ? 10.075  3.138   85.172  1.00 55.17  ? 19  ASN O CA  1 
ATOM   7895  C  C   . ASN H  1 19  ? 8.627   3.472   85.475  1.00 55.12  ? 19  ASN O C   1 
ATOM   7896  O  O   . ASN H  1 19  ? 8.291   3.768   86.621  1.00 56.45  ? 19  ASN O O   1 
ATOM   7897  C  CB  . ASN H  1 19  ? 10.302  1.654   85.428  1.00 56.29  ? 19  ASN O CB  1 
ATOM   7898  C  CG  . ASN H  1 19  ? 11.735  1.242   85.188  1.00 56.75  ? 19  ASN O CG  1 
ATOM   7899  O  OD1 . ASN H  1 19  ? 12.204  1.245   84.053  1.00 55.63  ? 19  ASN O OD1 1 
ATOM   7900  N  ND2 . ASN H  1 19  ? 12.444  0.897   86.259  1.00 58.65  ? 19  ASN O ND2 1 
ATOM   7901  N  N   . PHE H  1 20  ? 7.784   3.416   84.444  1.00 53.84  ? 20  PHE O N   1 
ATOM   7902  C  CA  . PHE H  1 20  ? 6.348   3.643   84.575  1.00 53.95  ? 20  PHE O CA  1 
ATOM   7903  C  C   . PHE H  1 20  ? 5.601   2.462   83.981  1.00 53.89  ? 20  PHE O C   1 
ATOM   7904  O  O   . PHE H  1 20  ? 6.013   1.928   82.942  1.00 53.03  ? 20  PHE O O   1 
ATOM   7905  C  CB  . PHE H  1 20  ? 5.916   4.897   83.824  1.00 52.79  ? 20  PHE O CB  1 
ATOM   7906  C  CG  . PHE H  1 20  ? 6.612   6.149   84.264  1.00 52.96  ? 20  PHE O CG  1 
ATOM   7907  C  CD1 . PHE H  1 20  ? 7.878   6.469   83.772  1.00 52.39  ? 20  PHE O CD1 1 
ATOM   7908  C  CD2 . PHE H  1 20  ? 5.995   7.028   85.145  1.00 53.90  ? 20  PHE O CD2 1 
ATOM   7909  C  CE1 . PHE H  1 20  ? 8.521   7.635   84.168  1.00 52.76  ? 20  PHE O CE1 1 
ATOM   7910  C  CE2 . PHE H  1 20  ? 6.632   8.197   85.543  1.00 54.28  ? 20  PHE O CE2 1 
ATOM   7911  C  CZ  . PHE H  1 20  ? 7.896   8.501   85.055  1.00 53.69  ? 20  PHE O CZ  1 
ATOM   7912  N  N   . GLU H  1 21  ? 4.498   2.068   84.619  1.00 55.00  ? 21  GLU O N   1 
ATOM   7913  C  CA  . GLU H  1 21  ? 3.606   1.054   84.051  1.00 55.21  ? 21  GLU O CA  1 
ATOM   7914  C  C   . GLU H  1 21  ? 2.137   1.327   84.370  1.00 55.97  ? 21  GLU O C   1 
ATOM   7915  O  O   . GLU H  1 21  ? 1.788   1.647   85.508  1.00 57.26  ? 21  GLU O O   1 
ATOM   7916  C  CB  . GLU H  1 21  ? 3.997   -0.340  84.526  1.00 56.56  ? 21  GLU O CB  1 
ATOM   7917  C  CG  . GLU H  1 21  ? 3.336   -1.450  83.722  1.00 56.76  ? 21  GLU O CG  1 
ATOM   7918  C  CD  . GLU H  1 21  ? 3.867   -2.830  84.055  1.00 58.18  ? 21  GLU O CD  1 
ATOM   7919  O  OE1 . GLU H  1 21  ? 4.622   -2.973  85.042  1.00 59.29  ? 21  GLU O OE1 1 
ATOM   7920  O  OE2 . GLU H  1 21  ? 3.514   -3.783  83.326  1.00 58.47  ? 21  GLU O OE2 1 
ATOM   7921  N  N   . GLN H  1 22  ? 1.292   1.182   83.348  1.00 55.38  ? 22  GLN O N   1 
ATOM   7922  C  CA  . GLN H  1 22  ? -0.146  1.401   83.452  1.00 56.25  ? 22  GLN O CA  1 
ATOM   7923  C  C   . GLN H  1 22  ? -0.855  0.258   82.715  1.00 56.74  ? 22  GLN O C   1 
ATOM   7924  O  O   . GLN H  1 22  ? -0.874  0.218   81.486  1.00 55.71  ? 22  GLN O O   1 
ATOM   7925  C  CB  . GLN H  1 22  ? -0.509  2.773   82.869  1.00 55.27  ? 22  GLN O CB  1 
ATOM   7926  C  CG  . GLN H  1 22  ? -1.989  3.124   82.922  1.00 56.35  ? 22  GLN O CG  1 
ATOM   7927  C  CD  . GLN H  1 22  ? -2.303  4.527   82.426  1.00 55.70  ? 22  GLN O CD  1 
ATOM   7928  O  OE1 . GLN H  1 22  ? -1.617  5.064   81.556  1.00 54.25  ? 22  GLN O OE1 1 
ATOM   7929  N  NE2 . GLN H  1 22  ? -3.359  5.120   82.965  1.00 57.02  ? 22  GLN O NE2 1 
ATOM   7930  N  N   . LYS H  1 23  ? -1.418  -0.673  83.482  1.00 58.58  ? 23  LYS O N   1 
ATOM   7931  C  CA  . LYS H  1 23  ? -2.018  -1.898  82.942  1.00 59.52  ? 23  LYS O CA  1 
ATOM   7932  C  C   . LYS H  1 23  ? -3.346  -1.659  82.202  1.00 59.87  ? 23  LYS O C   1 
ATOM   7933  O  O   . LYS H  1 23  ? -3.722  -2.460  81.340  1.00 60.24  ? 23  LYS O O   1 
ATOM   7934  C  CB  . LYS H  1 23  ? -2.216  -2.913  84.076  1.00 61.75  ? 23  LYS O CB  1 
ATOM   7935  C  CG  . LYS H  1 23  ? -2.592  -4.323  83.633  1.00 63.02  ? 23  LYS O CG  1 
ATOM   7936  C  CD  . LYS H  1 23  ? -2.475  -5.335  84.773  1.00 65.28  ? 23  LYS O CD  1 
ATOM   7937  C  CE  . LYS H  1 23  ? -3.578  -5.199  85.818  1.00 67.42  ? 23  LYS O CE  1 
ATOM   7938  N  NZ  . LYS H  1 23  ? -4.888  -5.732  85.345  1.00 68.83  ? 23  LYS O NZ  1 
ATOM   7939  N  N   . GLU H  1 24  ? -4.054  -0.582  82.558  1.00 60.07  ? 24  GLU O N   1 
ATOM   7940  C  CA  . GLU H  1 24  ? -5.278  -0.146  81.864  1.00 60.53  ? 24  GLU O CA  1 
ATOM   7941  C  C   . GLU H  1 24  ? -5.312  1.385   81.769  1.00 59.54  ? 24  GLU O C   1 
ATOM   7942  O  O   . GLU H  1 24  ? -4.880  2.079   82.692  1.00 59.42  ? 24  GLU O O   1 
ATOM   7943  C  CB  . GLU H  1 24  ? -6.531  -0.658  82.594  1.00 63.06  ? 24  GLU O CB  1 
ATOM   7944  C  CG  . GLU H  1 24  ? -7.039  -2.024  82.132  1.00 64.39  ? 24  GLU O CG  1 
ATOM   7945  C  CD  . GLU H  1 24  ? -6.523  -3.199  82.955  1.00 65.49  ? 24  GLU O CD  1 
ATOM   7946  O  OE1 . GLU H  1 24  ? -6.683  -3.186  84.199  1.00 66.90  ? 24  GLU O OE1 1 
ATOM   7947  O  OE2 . GLU H  1 24  ? -5.988  -4.158  82.352  1.00 65.21  ? 24  GLU O OE2 1 
ATOM   7948  N  N   . SER H  1 25  ? -5.854  1.901   80.667  1.00 59.10  ? 25  SER O N   1 
ATOM   7949  C  CA  . SER H  1 25  ? -5.816  3.343   80.359  1.00 58.25  ? 25  SER O CA  1 
ATOM   7950  C  C   . SER H  1 25  ? -6.570  4.255   81.340  1.00 59.59  ? 25  SER O C   1 
ATOM   7951  O  O   . SER H  1 25  ? -6.252  5.448   81.440  1.00 58.98  ? 25  SER O O   1 
ATOM   7952  C  CB  . SER H  1 25  ? -6.346  3.596   78.946  1.00 58.04  ? 25  SER O CB  1 
ATOM   7953  O  OG  . SER H  1 25  ? -7.716  3.243   78.855  1.00 59.96  ? 25  SER O OG  1 
ATOM   7954  N  N   . ASN H  1 26  ? -7.565  3.708   82.040  1.00 61.62  ? 26  ASN O N   1 
ATOM   7955  C  CA  . ASN H  1 26  ? -8.297  4.460   83.076  1.00 63.31  ? 26  ASN O CA  1 
ATOM   7956  C  C   . ASN H  1 26  ? -7.868  4.094   84.503  1.00 64.21  ? 26  ASN O C   1 
ATOM   7957  O  O   . ASN H  1 26  ? -8.537  4.481   85.464  1.00 66.08  ? 26  ASN O O   1 
ATOM   7958  C  CB  . ASN H  1 26  ? -9.822  4.310   82.894  1.00 65.50  ? 26  ASN O CB  1 
ATOM   7959  C  CG  . ASN H  1 26  ? -10.331 2.902   83.179  1.00 67.02  ? 26  ASN O CG  1 
ATOM   7960  O  OD1 . ASN H  1 26  ? -9.684  1.907   82.850  1.00 66.09  ? 26  ASN O OD1 1 
ATOM   7961  N  ND2 . ASN H  1 26  ? -11.515 2.818   83.782  1.00 69.60  ? 26  ASN O ND2 1 
ATOM   7962  N  N   . GLY H  1 27  ? -6.745  3.378   84.632  1.00 63.14  ? 27  GLY O N   1 
ATOM   7963  C  CA  . GLY H  1 27  ? -6.249  2.879   85.915  1.00 64.21  ? 27  GLY O CA  1 
ATOM   7964  C  C   . GLY H  1 27  ? -5.021  3.630   86.409  1.00 63.11  ? 27  GLY O C   1 
ATOM   7965  O  O   . GLY H  1 27  ? -4.587  4.602   85.785  1.00 61.49  ? 27  GLY O O   1 
ATOM   7966  N  N   . PRO H  1 28  ? -4.452  3.186   87.545  1.00 64.20  ? 28  PRO O N   1 
ATOM   7967  C  CA  . PRO H  1 28  ? -3.292  3.864   88.124  1.00 63.60  ? 28  PRO O CA  1 
ATOM   7968  C  C   . PRO H  1 28  ? -1.992  3.565   87.375  1.00 61.56  ? 28  PRO O C   1 
ATOM   7969  O  O   . PRO H  1 28  ? -1.837  2.483   86.800  1.00 61.16  ? 28  PRO O O   1 
ATOM   7970  C  CB  . PRO H  1 28  ? -3.233  3.296   89.542  1.00 65.88  ? 28  PRO O CB  1 
ATOM   7971  C  CG  . PRO H  1 28  ? -3.806  1.929   89.410  1.00 66.88  ? 28  PRO O CG  1 
ATOM   7972  C  CD  . PRO H  1 28  ? -4.866  2.022   88.350  1.00 66.34  ? 28  PRO O CD  1 
ATOM   7973  N  N   . VAL H  1 29  ? -1.082  4.537   87.382  1.00 60.55  ? 29  VAL O N   1 
ATOM   7974  C  CA  . VAL H  1 29  ? 0.267   4.371   86.849  1.00 58.99  ? 29  VAL O CA  1 
ATOM   7975  C  C   . VAL H  1 29  ? 1.189   3.995   88.012  1.00 60.21  ? 29  VAL O C   1 
ATOM   7976  O  O   . VAL H  1 29  ? 1.274   4.733   88.998  1.00 61.35  ? 29  VAL O O   1 
ATOM   7977  C  CB  . VAL H  1 29  ? 0.782   5.679   86.203  1.00 57.50  ? 29  VAL O CB  1 
ATOM   7978  C  CG1 . VAL H  1 29  ? 2.176   5.480   85.610  1.00 56.09  ? 29  VAL O CG1 1 
ATOM   7979  C  CG2 . VAL H  1 29  ? -0.197  6.180   85.146  1.00 56.78  ? 29  VAL O CG2 1 
ATOM   7980  N  N   . LYS H  1 30  ? 1.859   2.847   87.900  1.00 60.24  ? 30  LYS O N   1 
ATOM   7981  C  CA  . LYS H  1 30  ? 2.917   2.466   88.839  1.00 61.40  ? 30  LYS O CA  1 
ATOM   7982  C  C   . LYS H  1 30  ? 4.218   3.165   88.439  1.00 60.01  ? 30  LYS O C   1 
ATOM   7983  O  O   . LYS H  1 30  ? 4.570   3.181   87.263  1.00 58.21  ? 30  LYS O O   1 
ATOM   7984  C  CB  . LYS H  1 30  ? 3.113   0.945   88.865  1.00 62.32  ? 30  LYS O CB  1 
ATOM   7985  C  CG  . LYS H  1 30  ? 4.253   0.494   89.768  1.00 63.81  ? 30  LYS O CG  1 
ATOM   7986  C  CD  . LYS H  1 30  ? 4.037   -0.891  90.361  1.00 65.95  ? 30  LYS O CD  1 
ATOM   7987  C  CE  . LYS H  1 30  ? 5.257   -1.349  91.152  1.00 67.53  ? 30  LYS O CE  1 
ATOM   7988  N  NZ  . LYS H  1 30  ? 5.474   -0.585  92.415  1.00 69.26  ? 30  LYS O NZ  1 
ATOM   7989  N  N   . VAL H  1 31  ? 4.918   3.735   89.421  1.00 61.08  ? 31  VAL O N   1 
ATOM   7990  C  CA  . VAL H  1 31  ? 6.172   4.467   89.201  1.00 60.26  ? 31  VAL O CA  1 
ATOM   7991  C  C   . VAL H  1 31  ? 7.246   3.901   90.134  1.00 61.94  ? 31  VAL O C   1 
ATOM   7992  O  O   . VAL H  1 31  ? 7.105   3.997   91.356  1.00 64.03  ? 31  VAL O O   1 
ATOM   7993  C  CB  . VAL H  1 31  ? 6.000   5.982   89.476  1.00 60.29  ? 31  VAL O CB  1 
ATOM   7994  C  CG1 . VAL H  1 31  ? 7.262   6.755   89.093  1.00 59.52  ? 31  VAL O CG1 1 
ATOM   7995  C  CG2 . VAL H  1 31  ? 4.784   6.530   88.736  1.00 59.22  ? 31  VAL O CG2 1 
ATOM   7996  N  N   . TRP H  1 32  ? 8.306   3.313   89.571  1.00 61.30  ? 32  TRP O N   1 
ATOM   7997  C  CA  . TRP H  1 32  ? 9.377   2.718   90.383  1.00 63.12  ? 32  TRP O CA  1 
ATOM   7998  C  C   . TRP H  1 32  ? 10.764  2.785   89.750  1.00 62.39  ? 32  TRP O C   1 
ATOM   7999  O  O   . TRP H  1 32  ? 10.903  2.875   88.531  1.00 60.41  ? 32  TRP O O   1 
ATOM   8000  C  CB  . TRP H  1 32  ? 9.045   1.261   90.732  1.00 64.50  ? 32  TRP O CB  1 
ATOM   8001  C  CG  . TRP H  1 32  ? 9.409   0.263   89.666  1.00 63.42  ? 32  TRP O CG  1 
ATOM   8002  C  CD1 . TRP H  1 32  ? 10.488  -0.575  89.662  1.00 64.35  ? 32  TRP O CD1 1 
ATOM   8003  C  CD2 . TRP H  1 32  ? 8.695   0.005   88.456  1.00 61.52  ? 32  TRP O CD2 1 
ATOM   8004  N  NE1 . TRP H  1 32  ? 10.486  -1.343  88.525  1.00 63.12  ? 32  TRP O NE1 1 
ATOM   8005  C  CE2 . TRP H  1 32  ? 9.396   -1.009  87.765  1.00 61.37  ? 32  TRP O CE2 1 
ATOM   8006  C  CE3 . TRP H  1 32  ? 7.527   0.532   87.885  1.00 60.17  ? 32  TRP O CE3 1 
ATOM   8007  C  CZ2 . TRP H  1 32  ? 8.969   -1.509  86.528  1.00 59.95  ? 32  TRP O CZ2 1 
ATOM   8008  C  CZ3 . TRP H  1 32  ? 7.097   0.036   86.652  1.00 58.75  ? 32  TRP O CZ3 1 
ATOM   8009  C  CH2 . TRP H  1 32  ? 7.820   -0.974  85.987  1.00 58.65  ? 32  TRP O CH2 1 
ATOM   8010  N  N   . GLY H  1 33  ? 11.784  2.713   90.605  1.00 64.28  ? 33  GLY O N   1 
ATOM   8011  C  CA  . GLY H  1 33  ? 13.179  2.757   90.168  1.00 64.19  ? 33  GLY O CA  1 
ATOM   8012  C  C   . GLY H  1 33  ? 14.113  3.230   91.264  1.00 66.47  ? 33  GLY O C   1 
ATOM   8013  O  O   . GLY H  1 33  ? 13.874  2.968   92.444  1.00 68.68  ? 33  GLY O O   1 
ATOM   8014  N  N   . SER H  1 34  ? 15.178  3.926   90.869  1.00 66.17  ? 34  SER O N   1 
ATOM   8015  C  CA  . SER H  1 34  ? 16.181  4.425   91.807  1.00 68.52  ? 34  SER O CA  1 
ATOM   8016  C  C   . SER H  1 34  ? 16.818  5.713   91.307  1.00 67.69  ? 34  SER O C   1 
ATOM   8017  O  O   . SER H  1 34  ? 17.069  5.853   90.114  1.00 65.72  ? 34  SER O O   1 
ATOM   8018  C  CB  . SER H  1 34  ? 17.272  3.375   92.027  1.00 70.41  ? 34  SER O CB  1 
ATOM   8019  O  OG  . SER H  1 34  ? 16.795  2.306   92.820  1.00 72.11  ? 34  SER O OG  1 
ATOM   8020  N  N   . ILE H  1 35  ? 17.075  6.638   92.233  1.00 69.44  ? 35  ILE O N   1 
ATOM   8021  C  CA  . ILE H  1 35  ? 17.838  7.860   91.966  1.00 69.49  ? 35  ILE O CA  1 
ATOM   8022  C  C   . ILE H  1 35  ? 18.994  7.905   92.964  1.00 72.70  ? 35  ILE O C   1 
ATOM   8023  O  O   . ILE H  1 35  ? 18.765  7.785   94.168  1.00 74.95  ? 35  ILE O O   1 
ATOM   8024  C  CB  . ILE H  1 35  ? 16.972  9.134   92.130  1.00 68.89  ? 35  ILE O CB  1 
ATOM   8025  C  CG1 . ILE H  1 35  ? 15.675  9.016   91.319  1.00 66.25  ? 35  ILE O CG1 1 
ATOM   8026  C  CG2 . ILE H  1 35  ? 17.753  10.380  91.709  1.00 68.93  ? 35  ILE O CG2 1 
ATOM   8027  C  CD1 . ILE H  1 35  ? 14.735  10.191  91.477  1.00 65.89  ? 35  ILE O CD1 1 
ATOM   8028  N  N   . LYS H  1 36  ? 20.219  8.080   92.464  1.00 73.14  ? 36  LYS O N   1 
ATOM   8029  C  CA  . LYS H  1 36  ? 21.421  8.146   93.306  1.00 76.39  ? 36  LYS O CA  1 
ATOM   8030  C  C   . LYS H  1 36  ? 22.166  9.463   93.093  1.00 76.94  ? 36  LYS O C   1 
ATOM   8031  O  O   . LYS H  1 36  ? 22.093  10.059  92.014  1.00 74.71  ? 36  LYS O O   1 
ATOM   8032  C  CB  . LYS H  1 36  ? 22.350  6.955   93.037  1.00 77.33  ? 36  LYS O CB  1 
ATOM   8033  C  CG  . LYS H  1 36  ? 22.813  6.803   91.595  1.00 75.21  ? 36  LYS O CG  1 
ATOM   8034  C  CD  . LYS H  1 36  ? 23.935  5.785   91.467  1.00 76.94  ? 36  LYS O CD  1 
ATOM   8035  C  CE  . LYS H  1 36  ? 24.364  5.625   90.016  1.00 75.02  ? 36  LYS O CE  1 
ATOM   8036  N  NZ  . LYS H  1 36  ? 25.621  4.837   89.879  1.00 77.14  ? 36  LYS O NZ  1 
ATOM   8037  N  N   . GLY H  1 37  ? 22.886  9.895   94.130  1.00 80.16  ? 37  GLY O N   1 
ATOM   8038  C  CA  . GLY H  1 37  ? 23.635  11.155  94.121  1.00 81.41  ? 37  GLY O CA  1 
ATOM   8039  C  C   . GLY H  1 37  ? 22.943  12.319  94.813  1.00 82.09  ? 37  GLY O C   1 
ATOM   8040  O  O   . GLY H  1 37  ? 23.410  13.456  94.721  1.00 82.94  ? 37  GLY O O   1 
ATOM   8041  N  N   . LEU H  1 38  ? 21.841  12.043  95.511  1.00 81.99  ? 38  LEU O N   1 
ATOM   8042  C  CA  . LEU H  1 38  ? 21.090  13.070  96.233  1.00 82.92  ? 38  LEU O CA  1 
ATOM   8043  C  C   . LEU H  1 38  ? 21.633  13.219  97.654  1.00 87.11  ? 38  LEU O C   1 
ATOM   8044  O  O   . LEU H  1 38  ? 22.231  12.291  98.196  1.00 89.05  ? 38  LEU O O   1 
ATOM   8045  C  CB  . LEU H  1 38  ? 19.603  12.701  96.300  1.00 81.06  ? 38  LEU O CB  1 
ATOM   8046  C  CG  . LEU H  1 38  ? 18.838  12.573  94.974  1.00 77.16  ? 38  LEU O CG  1 
ATOM   8047  C  CD1 . LEU H  1 38  ? 17.566  11.759  95.160  1.00 76.00  ? 38  LEU O CD1 1 
ATOM   8048  C  CD2 . LEU H  1 38  ? 18.508  13.938  94.387  1.00 76.01  ? 38  LEU O CD2 1 
ATOM   8049  N  N   . THR H  1 39  ? 21.420  14.387  98.254  1.00 88.75  ? 39  THR O N   1 
ATOM   8050  C  CA  . THR H  1 39  ? 21.637  14.557  99.689  1.00 92.83  ? 39  THR O CA  1 
ATOM   8051  C  C   . THR H  1 39  ? 20.524  13.817  100.436 1.00 93.06  ? 39  THR O C   1 
ATOM   8052  O  O   . THR H  1 39  ? 19.458  13.565  99.875  1.00 90.12  ? 39  THR O O   1 
ATOM   8053  C  CB  . THR H  1 39  ? 21.662  16.044  100.098 1.00 94.66  ? 39  THR O CB  1 
ATOM   8054  O  OG1 . THR H  1 39  ? 20.485  16.700  99.615  1.00 92.17  ? 39  THR O OG1 1 
ATOM   8055  C  CG2 . THR H  1 39  ? 22.894  16.736  99.526  1.00 95.35  ? 39  THR O CG2 1 
ATOM   8056  N  N   . GLU H  1 40  ? 20.781  13.458  101.692 1.00 96.80  ? 40  GLU O N   1 
ATOM   8057  C  CA  . GLU H  1 40  ? 19.804  12.724  102.503 1.00 97.69  ? 40  GLU O CA  1 
ATOM   8058  C  C   . GLU H  1 40  ? 18.554  13.573  102.740 1.00 97.16  ? 40  GLU O C   1 
ATOM   8059  O  O   . GLU H  1 40  ? 18.647  14.794  102.905 1.00 98.20  ? 40  GLU O O   1 
ATOM   8060  C  CB  . GLU H  1 40  ? 20.415  12.298  103.847 1.00 102.39 ? 40  GLU O CB  1 
ATOM   8061  C  CG  . GLU H  1 40  ? 19.558  11.324  104.651 1.00 103.61 ? 40  GLU O CG  1 
ATOM   8062  C  CD  . GLU H  1 40  ? 20.222  10.844  105.937 1.00 108.56 ? 40  GLU O CD  1 
ATOM   8063  O  OE1 . GLU H  1 40  ? 21.016  11.599  106.545 1.00 111.69 ? 40  GLU O OE1 1 
ATOM   8064  O  OE2 . GLU H  1 40  ? 19.934  9.699   106.348 1.00 109.53 ? 40  GLU O OE2 1 
ATOM   8065  N  N   . GLY H  1 41  ? 17.394  12.917  102.737 1.00 95.74  ? 41  GLY O N   1 
ATOM   8066  C  CA  . GLY H  1 41  ? 16.113  13.570  103.005 1.00 95.49  ? 41  GLY O CA  1 
ATOM   8067  C  C   . GLY H  1 41  ? 15.202  13.638  101.795 1.00 91.27  ? 41  GLY O C   1 
ATOM   8068  O  O   . GLY H  1 41  ? 15.422  12.953  100.790 1.00 88.45  ? 41  GLY O O   1 
ATOM   8069  N  N   . LEU H  1 42  ? 14.176  14.478  101.904 1.00 91.13  ? 42  LEU O N   1 
ATOM   8070  C  CA  . LEU H  1 42  ? 13.131  14.583  100.886 1.00 87.68  ? 42  LEU O CA  1 
ATOM   8071  C  C   . LEU H  1 42  ? 13.592  15.442  99.702  1.00 85.23  ? 42  LEU O C   1 
ATOM   8072  O  O   . LEU H  1 42  ? 14.290  16.444  99.886  1.00 86.75  ? 42  LEU O O   1 
ATOM   8073  C  CB  . LEU H  1 42  ? 11.847  15.158  101.502 1.00 88.91  ? 42  LEU O CB  1 
ATOM   8074  C  CG  . LEU H  1 42  ? 11.240  14.377  102.678 1.00 91.62  ? 42  LEU O CG  1 
ATOM   8075  C  CD1 . LEU H  1 42  ? 10.184  15.202  103.398 1.00 93.65  ? 42  LEU O CD1 1 
ATOM   8076  C  CD2 . LEU H  1 42  ? 10.649  13.055  102.220 1.00 89.60  ? 42  LEU O CD2 1 
ATOM   8077  N  N   . HIS H  1 43  ? 13.204  15.031  98.496  1.00 81.69  ? 43  HIS O N   1 
ATOM   8078  C  CA  . HIS H  1 43  ? 13.549  15.742  97.261  1.00 79.30  ? 43  HIS O CA  1 
ATOM   8079  C  C   . HIS H  1 43  ? 12.345  15.816  96.327  1.00 76.46  ? 43  HIS O C   1 
ATOM   8080  O  O   . HIS H  1 43  ? 11.736  14.790  96.011  1.00 74.89  ? 43  HIS O O   1 
ATOM   8081  C  CB  . HIS H  1 43  ? 14.713  15.047  96.553  1.00 78.11  ? 43  HIS O CB  1 
ATOM   8082  C  CG  . HIS H  1 43  ? 16.027  15.242  97.237  1.00 80.86  ? 43  HIS O CG  1 
ATOM   8083  N  ND1 . HIS H  1 43  ? 16.791  16.375  97.064  1.00 81.78  ? 43  HIS O ND1 1 
ATOM   8084  C  CD2 . HIS H  1 43  ? 16.706  14.459  98.107  1.00 83.22  ? 43  HIS O CD2 1 
ATOM   8085  C  CE1 . HIS H  1 43  ? 17.889  16.279  97.793  1.00 84.55  ? 43  HIS O CE1 1 
ATOM   8086  N  NE2 . HIS H  1 43  ? 17.861  15.127  98.438  1.00 85.49  ? 43  HIS O NE2 1 
ATOM   8087  N  N   . GLY H  1 44  ? 12.018  17.037  95.895  1.00 76.07  ? 44  GLY O N   1 
ATOM   8088  C  CA  . GLY H  1 44  ? 10.902  17.291  94.984  1.00 73.79  ? 44  GLY O CA  1 
ATOM   8089  C  C   . GLY H  1 44  ? 10.991  16.460  93.718  1.00 70.67  ? 44  GLY O C   1 
ATOM   8090  O  O   . GLY H  1 44  ? 12.087  16.232  93.198  1.00 69.95  ? 44  GLY O O   1 
ATOM   8091  N  N   . PHE H  1 45  ? 9.831   16.021  93.234  1.00 69.07  ? 45  PHE O N   1 
ATOM   8092  C  CA  . PHE H  1 45  ? 9.736   14.998  92.191  1.00 66.52  ? 45  PHE O CA  1 
ATOM   8093  C  C   . PHE H  1 45  ? 8.507   15.268  91.315  1.00 64.87  ? 45  PHE O C   1 
ATOM   8094  O  O   . PHE H  1 45  ? 7.403   14.829  91.640  1.00 65.10  ? 45  PHE O O   1 
ATOM   8095  C  CB  . PHE H  1 45  ? 9.656   13.627  92.876  1.00 67.13  ? 45  PHE O CB  1 
ATOM   8096  C  CG  . PHE H  1 45  ? 9.774   12.448  91.942  1.00 64.97  ? 45  PHE O CG  1 
ATOM   8097  C  CD1 . PHE H  1 45  ? 10.921  12.256  91.180  1.00 63.91  ? 45  PHE O CD1 1 
ATOM   8098  C  CD2 . PHE H  1 45  ? 8.763   11.490  91.878  1.00 64.36  ? 45  PHE O CD2 1 
ATOM   8099  C  CE1 . PHE H  1 45  ? 11.044  11.154  90.345  1.00 62.25  ? 45  PHE O CE1 1 
ATOM   8100  C  CE2 . PHE H  1 45  ? 8.882   10.385  91.053  1.00 62.71  ? 45  PHE O CE2 1 
ATOM   8101  C  CZ  . PHE H  1 45  ? 10.021  10.216  90.282  1.00 61.64  ? 45  PHE O CZ  1 
ATOM   8102  N  N   . HIS H  1 46  ? 8.708   16.005  90.217  1.00 63.50  ? 46  HIS O N   1 
ATOM   8103  C  CA  . HIS H  1 46  ? 7.605   16.510  89.382  1.00 62.41  ? 46  HIS O CA  1 
ATOM   8104  C  C   . HIS H  1 46  ? 7.762   16.181  87.896  1.00 60.03  ? 46  HIS O C   1 
ATOM   8105  O  O   . HIS H  1 46  ? 8.879   15.995  87.405  1.00 59.35  ? 46  HIS O O   1 
ATOM   8106  C  CB  . HIS H  1 46  ? 7.476   18.036  89.510  1.00 63.74  ? 46  HIS O CB  1 
ATOM   8107  C  CG  . HIS H  1 46  ? 7.624   18.550  90.908  1.00 66.40  ? 46  HIS O CG  1 
ATOM   8108  N  ND1 . HIS H  1 46  ? 8.559   19.503  91.252  1.00 67.91  ? 46  HIS O ND1 1 
ATOM   8109  C  CD2 . HIS H  1 46  ? 6.966   18.238  92.048  1.00 68.10  ? 46  HIS O CD2 1 
ATOM   8110  C  CE1 . HIS H  1 46  ? 8.465   19.761  92.544  1.00 70.41  ? 46  HIS O CE1 1 
ATOM   8111  N  NE2 . HIS H  1 46  ? 7.507   19.005  93.051  1.00 70.58  ? 46  HIS O NE2 1 
ATOM   8112  N  N   . VAL H  1 47  ? 6.625   16.121  87.200  1.00 59.05  ? 47  VAL O N   1 
ATOM   8113  C  CA  . VAL H  1 47  ? 6.577   16.095  85.737  1.00 57.25  ? 47  VAL O CA  1 
ATOM   8114  C  C   . VAL H  1 47  ? 6.325   17.518  85.242  1.00 57.75  ? 47  VAL O C   1 
ATOM   8115  O  O   . VAL H  1 47  ? 5.273   18.094  85.519  1.00 58.69  ? 47  VAL O O   1 
ATOM   8116  C  CB  . VAL H  1 47  ? 5.460   15.173  85.202  1.00 56.18  ? 47  VAL O CB  1 
ATOM   8117  C  CG1 . VAL H  1 47  ? 5.440   15.185  83.673  1.00 54.64  ? 47  VAL O CG1 1 
ATOM   8118  C  CG2 . VAL H  1 47  ? 5.636   13.754  85.728  1.00 55.99  ? 47  VAL O CG2 1 
ATOM   8119  N  N   . HIS H  1 48  ? 7.295   18.074  84.520  1.00 57.41  ? 48  HIS O N   1 
ATOM   8120  C  CA  . HIS H  1 48  ? 7.170   19.399  83.901  1.00 58.01  ? 48  HIS O CA  1 
ATOM   8121  C  C   . HIS H  1 48  ? 6.585   19.278  82.494  1.00 56.71  ? 48  HIS O C   1 
ATOM   8122  O  O   . HIS H  1 48  ? 6.691   18.225  81.862  1.00 55.24  ? 48  HIS O O   1 
ATOM   8123  C  CB  . HIS H  1 48  ? 8.529   20.107  83.860  1.00 58.71  ? 48  HIS O CB  1 
ATOM   8124  C  CG  . HIS H  1 48  ? 9.042   20.507  85.208  1.00 60.57  ? 48  HIS O CG  1 
ATOM   8125  N  ND1 . HIS H  1 48  ? 9.375   21.807  85.521  1.00 62.41  ? 48  HIS O ND1 1 
ATOM   8126  C  CD2 . HIS H  1 48  ? 9.262   19.781  86.329  1.00 61.18  ? 48  HIS O CD2 1 
ATOM   8127  C  CE1 . HIS H  1 48  ? 9.787   21.863  86.776  1.00 64.04  ? 48  HIS O CE1 1 
ATOM   8128  N  NE2 . HIS H  1 48  ? 9.730   20.646  87.288  1.00 63.36  ? 48  HIS O NE2 1 
ATOM   8129  N  N   . GLU H  1 49  ? 6.005   20.374  82.008  1.00 57.51  ? 49  GLU O N   1 
ATOM   8130  C  CA  . GLU H  1 49  ? 5.150   20.370  80.813  1.00 56.88  ? 49  GLU O CA  1 
ATOM   8131  C  C   . GLU H  1 49  ? 5.845   19.901  79.518  1.00 55.51  ? 49  GLU O C   1 
ATOM   8132  O  O   . GLU H  1 49  ? 5.311   19.063  78.784  1.00 54.42  ? 49  GLU O O   1 
ATOM   8133  C  CB  . GLU H  1 49  ? 4.544   21.769  80.613  1.00 58.50  ? 49  GLU O CB  1 
ATOM   8134  C  CG  . GLU H  1 49  ? 3.494   21.867  79.512  1.00 58.40  ? 49  GLU O CG  1 
ATOM   8135  C  CD  . GLU H  1 49  ? 2.867   23.248  79.389  1.00 60.38  ? 49  GLU O CD  1 
ATOM   8136  O  OE1 . GLU H  1 49  ? 3.171   24.145  80.208  1.00 61.88  ? 49  GLU O OE1 1 
ATOM   8137  O  OE2 . GLU H  1 49  ? 2.053   23.439  78.464  1.00 60.66  ? 49  GLU O OE2 1 
ATOM   8138  N  N   . PHE H  1 50  ? 7.024   20.449  79.241  1.00 55.80  ? 50  PHE O N   1 
ATOM   8139  C  CA  . PHE H  1 50  ? 7.713   20.199  77.974  1.00 54.93  ? 50  PHE O CA  1 
ATOM   8140  C  C   . PHE H  1 50  ? 8.818   19.159  78.127  1.00 53.94  ? 50  PHE O C   1 
ATOM   8141  O  O   . PHE H  1 50  ? 9.499   19.115  79.151  1.00 54.41  ? 50  PHE O O   1 
ATOM   8142  C  CB  . PHE H  1 50  ? 8.302   21.503  77.431  1.00 56.23  ? 50  PHE O CB  1 
ATOM   8143  C  CG  . PHE H  1 50  ? 7.327   22.645  77.422  1.00 57.68  ? 50  PHE O CG  1 
ATOM   8144  C  CD1 . PHE H  1 50  ? 6.120   22.533  76.735  1.00 57.55  ? 50  PHE O CD1 1 
ATOM   8145  C  CD2 . PHE H  1 50  ? 7.604   23.828  78.102  1.00 59.47  ? 50  PHE O CD2 1 
ATOM   8146  C  CE1 . PHE H  1 50  ? 5.206   23.580  76.726  1.00 59.16  ? 50  PHE O CE1 1 
ATOM   8147  C  CE2 . PHE H  1 50  ? 6.696   24.876  78.098  1.00 61.06  ? 50  PHE O CE2 1 
ATOM   8148  C  CZ  . PHE H  1 50  ? 5.494   24.752  77.412  1.00 60.90  ? 50  PHE O CZ  1 
ATOM   8149  N  N   . GLY H  1 51  ? 8.992   18.338  77.092  1.00 52.80  ? 51  GLY O N   1 
ATOM   8150  C  CA  . GLY H  1 51  ? 10.148  17.450  76.955  1.00 52.14  ? 51  GLY O CA  1 
ATOM   8151  C  C   . GLY H  1 51  ? 11.303  18.133  76.235  1.00 52.83  ? 51  GLY O C   1 
ATOM   8152  O  O   . GLY H  1 51  ? 11.938  17.532  75.358  1.00 52.31  ? 51  GLY O O   1 
ATOM   8153  N  N   . ASP H  1 52  ? 11.578  19.382  76.618  1.00 54.22  ? 52  ASP O N   1 
ATOM   8154  C  CA  . ASP H  1 52  ? 12.585  20.218  75.983  1.00 55.34  ? 52  ASP O CA  1 
ATOM   8155  C  C   . ASP H  1 52  ? 13.797  20.279  76.916  1.00 56.26  ? 52  ASP O C   1 
ATOM   8156  O  O   . ASP H  1 52  ? 13.737  20.873  77.999  1.00 57.23  ? 52  ASP O O   1 
ATOM   8157  C  CB  . ASP H  1 52  ? 12.010  21.611  75.710  1.00 56.64  ? 52  ASP O CB  1 
ATOM   8158  C  CG  . ASP H  1 52  ? 12.931  22.488  74.868  1.00 57.99  ? 52  ASP O CG  1 
ATOM   8159  O  OD1 . ASP H  1 52  ? 14.156  22.233  74.812  1.00 58.24  ? 52  ASP O OD1 1 
ATOM   8160  O  OD2 . ASP H  1 52  ? 12.420  23.458  74.268  1.00 59.04  ? 52  ASP O OD2 1 
ATOM   8161  N  N   . ASN H  1 53  ? 14.883  19.648  76.470  1.00 56.12  ? 53  ASN O N   1 
ATOM   8162  C  CA  . ASN H  1 53  ? 16.115  19.499  77.233  1.00 57.10  ? 53  ASN O CA  1 
ATOM   8163  C  C   . ASN H  1 53  ? 17.259  20.291  76.576  1.00 58.58  ? 53  ASN O C   1 
ATOM   8164  O  O   . ASN H  1 53  ? 18.425  20.109  76.939  1.00 59.54  ? 53  ASN O O   1 
ATOM   8165  C  CB  . ASN H  1 53  ? 16.467  18.003  77.313  1.00 56.04  ? 53  ASN O CB  1 
ATOM   8166  C  CG  . ASN H  1 53  ? 17.341  17.658  78.509  1.00 57.01  ? 53  ASN O CG  1 
ATOM   8167  O  OD1 . ASN H  1 53  ? 16.875  17.635  79.647  1.00 57.29  ? 53  ASN O OD1 1 
ATOM   8168  N  ND2 . ASN H  1 53  ? 18.609  17.369  78.250  1.00 57.83  ? 53  ASN O ND2 1 
ATOM   8169  N  N   . THR H  1 54  ? 16.927  21.167  75.621  1.00 59.00  ? 54  THR O N   1 
ATOM   8170  C  CA  . THR H  1 54  ? 17.932  21.910  74.850  1.00 60.58  ? 54  THR O CA  1 
ATOM   8171  C  C   . THR H  1 54  ? 18.761  22.822  75.750  1.00 62.65  ? 54  THR O C   1 
ATOM   8172  O  O   . THR H  1 54  ? 19.975  22.946  75.562  1.00 64.03  ? 54  THR O O   1 
ATOM   8173  C  CB  . THR H  1 54  ? 17.299  22.765  73.728  1.00 61.03  ? 54  THR O CB  1 
ATOM   8174  O  OG1 . THR H  1 54  ? 16.311  23.644  74.281  1.00 61.43  ? 54  THR O OG1 1 
ATOM   8175  C  CG2 . THR H  1 54  ? 16.662  21.884  72.656  1.00 59.45  ? 54  THR O CG2 1 
ATOM   8176  N  N   . ALA H  1 55  ? 18.091  23.451  76.717  1.00 63.09  ? 55  ALA O N   1 
ATOM   8177  C  CA  . ALA H  1 55  ? 18.738  24.242  77.765  1.00 65.16  ? 55  ALA O CA  1 
ATOM   8178  C  C   . ALA H  1 55  ? 18.653  23.514  79.116  1.00 64.72  ? 55  ALA O C   1 
ATOM   8179  O  O   . ALA H  1 55  ? 18.319  24.121  80.137  1.00 65.86  ? 55  ALA O O   1 
ATOM   8180  C  CB  . ALA H  1 55  ? 18.088  25.619  77.845  1.00 66.57  ? 55  ALA O CB  1 
ATOM   8181  N  N   . GLY H  1 56  ? 18.968  22.217  79.116  1.00 63.38  ? 56  GLY O N   1 
ATOM   8182  C  CA  . GLY H  1 56  ? 18.876  21.378  80.313  1.00 63.01  ? 56  GLY O CA  1 
ATOM   8183  C  C   . GLY H  1 56  ? 17.458  21.246  80.844  1.00 61.87  ? 56  GLY O C   1 
ATOM   8184  O  O   . GLY H  1 56  ? 16.500  21.309  80.081  1.00 60.62  ? 56  GLY O O   1 
ATOM   8185  N  N   . ALA H  1 57  ? 17.336  21.083  82.162  1.00 62.59  ? 57  ALA O N   1 
ATOM   8186  C  CA  . ALA H  1 57  ? 16.034  20.991  82.841  1.00 61.99  ? 57  ALA O CA  1 
ATOM   8187  C  C   . ALA H  1 57  ? 15.231  22.301  82.824  1.00 62.88  ? 57  ALA O C   1 
ATOM   8188  O  O   . ALA H  1 57  ? 14.003  22.271  82.940  1.00 62.14  ? 57  ALA O O   1 
ATOM   8189  C  CB  . ALA H  1 57  ? 16.231  20.528  84.278  1.00 63.06  ? 57  ALA O CB  1 
ATOM   8190  N  N   . THR H  1 58  ? 15.927  23.435  82.694  1.00 64.68  ? 58  THR O N   1 
ATOM   8191  C  CA  . THR H  1 58  ? 15.313  24.772  82.621  1.00 65.98  ? 58  THR O CA  1 
ATOM   8192  C  C   . THR H  1 58  ? 14.263  24.890  81.511  1.00 64.60  ? 58  THR O C   1 
ATOM   8193  O  O   . THR H  1 58  ? 13.170  25.416  81.740  1.00 64.97  ? 58  THR O O   1 
ATOM   8194  C  CB  . THR H  1 58  ? 16.387  25.861  82.378  1.00 68.16  ? 58  THR O CB  1 
ATOM   8195  O  OG1 . THR H  1 58  ? 17.518  25.628  83.229  1.00 69.52  ? 58  THR O OG1 1 
ATOM   8196  C  CG2 . THR H  1 58  ? 15.833  27.265  82.640  1.00 70.15  ? 58  THR O CG2 1 
ATOM   8197  N  N   . SER H  1 59  ? 14.596  24.382  80.323  1.00 63.24  ? 59  SER O N   1 
ATOM   8198  C  CA  . SER H  1 59  ? 13.699  24.440  79.155  1.00 62.12  ? 59  SER O CA  1 
ATOM   8199  C  C   . SER H  1 59  ? 12.441  23.546  79.246  1.00 60.35  ? 59  SER O C   1 
ATOM   8200  O  O   . SER H  1 59  ? 11.548  23.655  78.402  1.00 59.79  ? 59  SER O O   1 
ATOM   8201  C  CB  . SER H  1 59  ? 14.485  24.152  77.859  1.00 61.56  ? 59  SER O CB  1 
ATOM   8202  O  OG  . SER H  1 59  ? 15.429  23.102  78.018  1.00 60.79  ? 59  SER O OG  1 
ATOM   8203  N  N   . ALA H  1 60  ? 12.359  22.691  80.270  1.00 59.76  ? 60  ALA O N   1 
ATOM   8204  C  CA  . ALA H  1 60  ? 11.180  21.843  80.497  1.00 58.44  ? 60  ALA O CA  1 
ATOM   8205  C  C   . ALA H  1 60  ? 9.916   22.592  80.930  1.00 59.32  ? 60  ALA O C   1 
ATOM   8206  O  O   . ALA H  1 60  ? 8.846   21.983  81.007  1.00 58.47  ? 60  ALA O O   1 
ATOM   8207  C  CB  . ALA H  1 60  ? 11.503  20.763  81.515  1.00 58.02  ? 60  ALA O CB  1 
ATOM   8208  N  N   . GLY H  1 61  ? 10.032  23.886  81.241  1.00 61.24  ? 61  GLY O N   1 
ATOM   8209  C  CA  . GLY H  1 61  ? 8.874   24.715  81.571  1.00 62.45  ? 61  GLY O CA  1 
ATOM   8210  C  C   . GLY H  1 61  ? 8.423   24.526  83.013  1.00 63.28  ? 61  GLY O C   1 
ATOM   8211  O  O   . GLY H  1 61  ? 9.174   23.986  83.835  1.00 63.33  ? 61  GLY O O   1 
ATOM   8212  N  N   . PRO H  1 62  ? 7.197   24.980  83.339  1.00 64.18  ? 62  PRO O N   1 
ATOM   8213  C  CA  . PRO H  1 62  ? 6.651   24.798  84.688  1.00 65.19  ? 62  PRO O CA  1 
ATOM   8214  C  C   . PRO H  1 62  ? 6.107   23.383  84.881  1.00 63.53  ? 62  PRO O C   1 
ATOM   8215  O  O   . PRO H  1 62  ? 6.232   22.545  83.982  1.00 61.52  ? 62  PRO O O   1 
ATOM   8216  C  CB  . PRO H  1 62  ? 5.527   25.836  84.748  1.00 66.93  ? 62  PRO O CB  1 
ATOM   8217  C  CG  . PRO H  1 62  ? 5.059   25.958  83.342  1.00 65.94  ? 62  PRO O CG  1 
ATOM   8218  C  CD  . PRO H  1 62  ? 6.247   25.687  82.456  1.00 64.58  ? 62  PRO O CD  1 
ATOM   8219  N  N   . HIS H  1 63  ? 5.513   23.124  86.045  1.00 64.56  ? 63  HIS O N   1 
ATOM   8220  C  CA  . HIS H  1 63  ? 4.906   21.820  86.335  1.00 63.47  ? 63  HIS O CA  1 
ATOM   8221  C  C   . HIS H  1 63  ? 3.761   21.565  85.363  1.00 62.42  ? 63  HIS O C   1 
ATOM   8222  O  O   . HIS H  1 63  ? 3.031   22.497  85.017  1.00 63.45  ? 63  HIS O O   1 
ATOM   8223  C  CB  . HIS H  1 63  ? 4.378   21.742  87.776  1.00 65.32  ? 63  HIS O CB  1 
ATOM   8224  C  CG  . HIS H  1 63  ? 5.441   21.850  88.827  1.00 66.66  ? 63  HIS O CG  1 
ATOM   8225  N  ND1 . HIS H  1 63  ? 5.153   21.864  90.175  1.00 68.71  ? 63  HIS O ND1 1 
ATOM   8226  C  CD2 . HIS H  1 63  ? 6.787   21.966  88.731  1.00 66.50  ? 63  HIS O CD2 1 
ATOM   8227  C  CE1 . HIS H  1 63  ? 6.276   21.968  90.862  1.00 69.77  ? 63  HIS O CE1 1 
ATOM   8228  N  NE2 . HIS H  1 63  ? 7.283   22.036  90.010  1.00 68.45  ? 63  HIS O NE2 1 
ATOM   8229  N  N   . PHE H  1 64  ? 3.619   20.314  84.920  1.00 60.64  ? 64  PHE O N   1 
ATOM   8230  C  CA  . PHE H  1 64  ? 2.544   19.922  83.995  1.00 59.79  ? 64  PHE O CA  1 
ATOM   8231  C  C   . PHE H  1 64  ? 1.186   20.141  84.659  1.00 61.39  ? 64  PHE O C   1 
ATOM   8232  O  O   . PHE H  1 64  ? 0.846   19.447  85.614  1.00 61.88  ? 64  PHE O O   1 
ATOM   8233  C  CB  . PHE H  1 64  ? 2.717   18.457  83.565  1.00 57.91  ? 64  PHE O CB  1 
ATOM   8234  C  CG  . PHE H  1 64  ? 1.642   17.944  82.626  1.00 57.19  ? 64  PHE O CG  1 
ATOM   8235  C  CD1 . PHE H  1 64  ? 1.202   18.701  81.537  1.00 57.31  ? 64  PHE O CD1 1 
ATOM   8236  C  CD2 . PHE H  1 64  ? 1.103   16.669  82.808  1.00 56.61  ? 64  PHE O CD2 1 
ATOM   8237  C  CE1 . PHE H  1 64  ? 0.226   18.208  80.677  1.00 56.93  ? 64  PHE O CE1 1 
ATOM   8238  C  CE2 . PHE H  1 64  ? 0.134   16.173  81.949  1.00 56.20  ? 64  PHE O CE2 1 
ATOM   8239  C  CZ  . PHE H  1 64  ? -0.307  16.943  80.883  1.00 56.37  ? 64  PHE O CZ  1 
ATOM   8240  N  N   . ASN H  1 65  ? 0.433   21.113  84.137  1.00 62.44  ? 65  ASN O N   1 
ATOM   8241  C  CA  . ASN H  1 65  ? -0.771  21.644  84.786  1.00 64.56  ? 65  ASN O CA  1 
ATOM   8242  C  C   . ASN H  1 65  ? -1.878  21.945  83.749  1.00 64.89  ? 65  ASN O C   1 
ATOM   8243  O  O   . ASN H  1 65  ? -2.215  23.109  83.512  1.00 66.43  ? 65  ASN O O   1 
ATOM   8244  C  CB  . ASN H  1 65  ? -0.386  22.905  85.582  1.00 66.61  ? 65  ASN O CB  1 
ATOM   8245  C  CG  . ASN H  1 65  ? -1.533  23.475  86.407  1.00 69.15  ? 65  ASN O CG  1 
ATOM   8246  O  OD1 . ASN H  1 65  ? -2.472  22.768  86.781  1.00 69.53  ? 65  ASN O OD1 1 
ATOM   8247  N  ND2 . ASN H  1 65  ? -1.448  24.764  86.712  1.00 71.16  ? 65  ASN O ND2 1 
ATOM   8248  N  N   . PRO H  1 66  ? -2.444  20.893  83.123  1.00 63.68  ? 66  PRO O N   1 
ATOM   8249  C  CA  . PRO H  1 66  ? -3.493  21.096  82.112  1.00 64.20  ? 66  PRO O CA  1 
ATOM   8250  C  C   . PRO H  1 66  ? -4.828  21.621  82.665  1.00 66.68  ? 66  PRO O C   1 
ATOM   8251  O  O   . PRO H  1 66  ? -5.568  22.278  81.930  1.00 67.85  ? 66  PRO O O   1 
ATOM   8252  C  CB  . PRO H  1 66  ? -3.675  19.696  81.508  1.00 62.47  ? 66  PRO O CB  1 
ATOM   8253  C  CG  . PRO H  1 66  ? -3.261  18.768  82.593  1.00 61.91  ? 66  PRO O CG  1 
ATOM   8254  C  CD  . PRO H  1 66  ? -2.134  19.463  83.303  1.00 62.07  ? 66  PRO O CD  1 
ATOM   8255  N  N   . LEU H  1 67  ? -5.125  21.336  83.935  1.00 67.70  ? 67  LEU O N   1 
ATOM   8256  C  CA  . LEU H  1 67  ? -6.386  21.755  84.564  1.00 70.32  ? 67  LEU O CA  1 
ATOM   8257  C  C   . LEU H  1 67  ? -6.335  23.137  85.246  1.00 72.62  ? 67  LEU O C   1 
ATOM   8258  O  O   . LEU H  1 67  ? -7.338  23.570  85.815  1.00 75.08  ? 67  LEU O O   1 
ATOM   8259  C  CB  . LEU H  1 67  ? -6.850  20.682  85.564  1.00 70.67  ? 67  LEU O CB  1 
ATOM   8260  C  CG  . LEU H  1 67  ? -7.183  19.311  84.957  1.00 69.09  ? 67  LEU O CG  1 
ATOM   8261  C  CD1 . LEU H  1 67  ? -7.280  18.248  86.038  1.00 69.36  ? 67  LEU O CD1 1 
ATOM   8262  C  CD2 . LEU H  1 67  ? -8.475  19.367  84.155  1.00 70.25  ? 67  LEU O CD2 1 
ATOM   8263  N  N   . SER H  1 68  ? -5.188  23.822  85.174  1.00 72.06  ? 68  SER O N   1 
ATOM   8264  C  CA  . SER H  1 68  ? -5.002  25.177  85.734  1.00 74.33  ? 68  SER O CA  1 
ATOM   8265  C  C   . SER H  1 68  ? -5.260  25.260  87.252  1.00 76.44  ? 68  SER O C   1 
ATOM   8266  O  O   . SER H  1 68  ? -5.984  26.135  87.733  1.00 79.21  ? 68  SER O O   1 
ATOM   8267  C  CB  . SER H  1 68  ? -5.839  26.212  84.963  1.00 76.14  ? 68  SER O CB  1 
ATOM   8268  O  OG  . SER H  1 68  ? -5.514  26.191  83.585  1.00 74.49  ? 68  SER O OG  1 
ATOM   8269  N  N   . ARG H  1 69  ? -4.647  24.331  87.983  1.00 75.33  ? 69  ARG O N   1 
ATOM   8270  C  CA  . ARG H  1 69  ? -4.755  24.241  89.438  1.00 77.28  ? 69  ARG O CA  1 
ATOM   8271  C  C   . ARG H  1 69  ? -3.570  24.933  90.119  1.00 77.95  ? 69  ARG O C   1 
ATOM   8272  O  O   . ARG H  1 69  ? -2.625  25.371  89.454  1.00 76.71  ? 69  ARG O O   1 
ATOM   8273  C  CB  . ARG H  1 69  ? -4.789  22.768  89.863  1.00 76.03  ? 69  ARG O CB  1 
ATOM   8274  C  CG  . ARG H  1 69  ? -5.889  21.941  89.214  1.00 75.43  ? 69  ARG O CG  1 
ATOM   8275  C  CD  . ARG H  1 69  ? -7.242  22.223  89.836  1.00 78.39  ? 69  ARG O CD  1 
ATOM   8276  N  NE  . ARG H  1 69  ? -8.292  21.395  89.246  1.00 78.09  ? 69  ARG O NE  1 
ATOM   8277  C  CZ  . ARG H  1 69  ? -8.487  20.096  89.492  1.00 77.35  ? 69  ARG O CZ  1 
ATOM   8278  N  NH1 . ARG H  1 69  ? -7.697  19.414  90.327  1.00 76.79  ? 69  ARG O NH1 1 
ATOM   8279  N  NH2 . ARG H  1 69  ? -9.489  19.462  88.885  1.00 77.40  ? 69  ARG O NH2 1 
ATOM   8280  N  N   . LYS H  1 70  ? -3.647  25.031  91.446  1.00 80.19  ? 70  LYS O N   1 
ATOM   8281  C  CA  . LYS H  1 70  ? -2.516  25.429  92.290  1.00 81.05  ? 70  LYS O CA  1 
ATOM   8282  C  C   . LYS H  1 70  ? -1.671  24.199  92.610  1.00 79.18  ? 70  LYS O C   1 
ATOM   8283  O  O   . LYS H  1 70  ? -2.167  23.071  92.564  1.00 78.08  ? 70  LYS O O   1 
ATOM   8284  C  CB  . LYS H  1 70  ? -3.004  26.045  93.605  1.00 84.69  ? 70  LYS O CB  1 
ATOM   8285  C  CG  . LYS H  1 70  ? -3.890  27.272  93.460  1.00 87.17  ? 70  LYS O CG  1 
ATOM   8286  C  CD  . LYS H  1 70  ? -3.149  28.443  92.832  1.00 87.27  ? 70  LYS O CD  1 
ATOM   8287  C  CE  . LYS H  1 70  ? -3.882  29.755  93.070  1.00 90.69  ? 70  LYS O CE  1 
ATOM   8288  N  NZ  . LYS H  1 70  ? -3.304  30.871  92.272  1.00 90.83  ? 70  LYS O NZ  1 
ATOM   8289  N  N   . HIS H  1 71  ? -0.401  24.430  92.946  1.00 79.11  ? 71  HIS O N   1 
ATOM   8290  C  CA  . HIS H  1 71  ? 0.544   23.356  93.276  1.00 77.70  ? 71  HIS O CA  1 
ATOM   8291  C  C   . HIS H  1 71  ? 0.154   22.648  94.572  1.00 79.55  ? 71  HIS O C   1 
ATOM   8292  O  O   . HIS H  1 71  ? -0.161  23.307  95.570  1.00 82.55  ? 71  HIS O O   1 
ATOM   8293  C  CB  . HIS H  1 71  ? 1.968   23.910  93.427  1.00 77.89  ? 71  HIS O CB  1 
ATOM   8294  C  CG  . HIS H  1 71  ? 2.965   22.895  93.891  1.00 77.06  ? 71  HIS O CG  1 
ATOM   8295  N  ND1 . HIS H  1 71  ? 3.524   21.959  93.049  1.00 74.20  ? 71  HIS O ND1 1 
ATOM   8296  C  CD2 . HIS H  1 71  ? 3.491   22.658  95.117  1.00 78.99  ? 71  HIS O CD2 1 
ATOM   8297  C  CE1 . HIS H  1 71  ? 4.356   21.195  93.732  1.00 74.40  ? 71  HIS O CE1 1 
ATOM   8298  N  NE2 . HIS H  1 71  ? 4.354   21.597  94.990  1.00 77.30  ? 71  HIS O NE2 1 
ATOM   8299  N  N   . GLY H  1 72  ? 0.205   21.315  94.557  1.00 78.00  ? 72  GLY O N   1 
ATOM   8300  C  CA  . GLY H  1 72  ? -0.077  20.513  95.752  1.00 79.78  ? 72  GLY O CA  1 
ATOM   8301  C  C   . GLY H  1 72  ? 0.697   19.212  95.814  1.00 78.24  ? 72  GLY O C   1 
ATOM   8302  O  O   . GLY H  1 72  ? 1.582   18.959  94.990  1.00 75.82  ? 72  GLY O O   1 
ATOM   8303  N  N   . GLY H  1 73  ? 0.361   18.402  96.817  1.00 79.93  ? 73  GLY O N   1 
ATOM   8304  C  CA  . GLY H  1 73  ? 0.909   17.054  96.977  1.00 79.00  ? 73  GLY O CA  1 
ATOM   8305  C  C   . GLY H  1 73  ? 0.041   16.029  96.267  1.00 77.29  ? 73  GLY O C   1 
ATOM   8306  O  O   . GLY H  1 73  ? -1.094  16.337  95.902  1.00 77.45  ? 73  GLY O O   1 
ATOM   8307  N  N   . PRO H  1 74  ? 0.553   14.791  96.099  1.00 75.98  ? 74  PRO O N   1 
ATOM   8308  C  CA  . PRO H  1 74  ? -0.096  13.756  95.277  1.00 74.20  ? 74  PRO O CA  1 
ATOM   8309  C  C   . PRO H  1 74  ? -1.437  13.212  95.803  1.00 76.04  ? 74  PRO O C   1 
ATOM   8310  O  O   . PRO H  1 74  ? -2.162  12.563  95.040  1.00 74.80  ? 74  PRO O O   1 
ATOM   8311  C  CB  . PRO H  1 74  ? 0.956   12.640  95.233  1.00 73.07  ? 74  PRO O CB  1 
ATOM   8312  C  CG  . PRO H  1 74  ? 1.697   12.788  96.507  1.00 75.49  ? 74  PRO O CG  1 
ATOM   8313  C  CD  . PRO H  1 74  ? 1.755   14.266  96.774  1.00 76.61  ? 74  PRO O CD  1 
ATOM   8314  N  N   . LYS H  1 75  ? -1.750  13.461  97.075  1.00 79.17  ? 75  LYS O N   1 
ATOM   8315  C  CA  . LYS H  1 75  ? -3.018  13.039  97.687  1.00 81.49  ? 75  LYS O CA  1 
ATOM   8316  C  C   . LYS H  1 75  ? -4.098  14.132  97.715  1.00 83.01  ? 75  LYS O C   1 
ATOM   8317  O  O   . LYS H  1 75  ? -5.277  13.821  97.908  1.00 84.53  ? 75  LYS O O   1 
ATOM   8318  C  CB  . LYS H  1 75  ? -2.765  12.542  99.115  1.00 84.50  ? 75  LYS O CB  1 
ATOM   8319  C  CG  . LYS H  1 75  ? -1.765  11.395  99.220  1.00 83.68  ? 75  LYS O CG  1 
ATOM   8320  C  CD  . LYS H  1 75  ? -2.182  10.194  98.378  1.00 81.79  ? 75  LYS O CD  1 
ATOM   8321  C  CE  . LYS H  1 75  ? -1.465  8.922   98.804  1.00 82.23  ? 75  LYS O CE  1 
ATOM   8322  N  NZ  . LYS H  1 75  ? -1.946  8.391   100.112 1.00 85.89  ? 75  LYS O NZ  1 
ATOM   8323  N  N   . ASP H  1 76  ? -3.702  15.395  97.524  1.00 82.84  ? 76  ASP O N   1 
ATOM   8324  C  CA  . ASP H  1 76  ? -4.654  16.518  97.477  1.00 84.35  ? 76  ASP O CA  1 
ATOM   8325  C  C   . ASP H  1 76  ? -5.455  16.484  96.175  1.00 82.36  ? 76  ASP O C   1 
ATOM   8326  O  O   . ASP H  1 76  ? -4.994  15.940  95.171  1.00 79.45  ? 76  ASP O O   1 
ATOM   8327  C  CB  . ASP H  1 76  ? -3.928  17.869  97.569  1.00 84.77  ? 76  ASP O CB  1 
ATOM   8328  C  CG  . ASP H  1 76  ? -3.101  18.017  98.835  1.00 87.05  ? 76  ASP O CG  1 
ATOM   8329  O  OD1 . ASP H  1 76  ? -3.600  17.677  99.928  1.00 89.92  ? 76  ASP O OD1 1 
ATOM   8330  O  OD2 . ASP H  1 76  ? -1.947  18.486  98.733  1.00 86.21  ? 76  ASP O OD2 1 
ATOM   8331  N  N   . GLU H  1 77  ? -6.655  17.062  96.201  1.00 84.22  ? 77  GLU O N   1 
ATOM   8332  C  CA  . GLU H  1 77  ? -7.450  17.242  94.988  1.00 82.89  ? 77  GLU O CA  1 
ATOM   8333  C  C   . GLU H  1 77  ? -6.937  18.453  94.213  1.00 81.64  ? 77  GLU O C   1 
ATOM   8334  O  O   . GLU H  1 77  ? -6.772  18.381  92.997  1.00 79.15  ? 77  GLU O O   1 
ATOM   8335  C  CB  . GLU H  1 77  ? -8.939  17.397  95.308  1.00 85.72  ? 77  GLU O CB  1 
ATOM   8336  C  CG  . GLU H  1 77  ? -9.813  17.474  94.058  1.00 84.70  ? 77  GLU O CG  1 
ATOM   8337  C  CD  . GLU H  1 77  ? -11.275 17.142  94.305  1.00 87.26  ? 77  GLU O CD  1 
ATOM   8338  O  OE1 . GLU H  1 77  ? -11.774 17.367  95.432  1.00 90.46  ? 77  GLU O OE1 1 
ATOM   8339  O  OE2 . GLU H  1 77  ? -11.927 16.662  93.352  1.00 86.27  ? 77  GLU O OE2 1 
ATOM   8340  N  N   . GLU H  1 78  ? -6.695  19.559  94.920  1.00 83.64  ? 78  GLU O N   1 
ATOM   8341  C  CA  . GLU H  1 78  ? -6.097  20.759  94.322  1.00 82.90  ? 78  GLU O CA  1 
ATOM   8342  C  C   . GLU H  1 78  ? -4.592  20.537  94.135  1.00 80.59  ? 78  GLU O C   1 
ATOM   8343  O  O   . GLU H  1 78  ? -3.818  20.585  95.098  1.00 81.72  ? 78  GLU O O   1 
ATOM   8344  C  CB  . GLU H  1 78  ? -6.370  21.997  95.191  1.00 86.26  ? 78  GLU O CB  1 
ATOM   8345  C  CG  . GLU H  1 78  ? -5.947  23.335  94.579  1.00 86.16  ? 78  GLU O CG  1 
ATOM   8346  C  CD  . GLU H  1 78  ? -6.758  23.750  93.357  1.00 85.46  ? 78  GLU O CD  1 
ATOM   8347  O  OE1 . GLU H  1 78  ? -7.874  23.226  93.142  1.00 85.91  ? 78  GLU O OE1 1 
ATOM   8348  O  OE2 . GLU H  1 78  ? -6.272  24.621  92.604  1.00 84.70  ? 78  GLU O OE2 1 
ATOM   8349  N  N   . ARG H  1 79  ? -4.196  20.285  92.890  1.00 77.58  ? 79  ARG O N   1 
ATOM   8350  C  CA  . ARG H  1 79  ? -2.822  19.928  92.545  1.00 75.26  ? 79  ARG O CA  1 
ATOM   8351  C  C   . ARG H  1 79  ? -2.631  19.964  91.030  1.00 72.56  ? 79  ARG O C   1 
ATOM   8352  O  O   . ARG H  1 79  ? -3.594  19.814  90.278  1.00 72.15  ? 79  ARG O O   1 
ATOM   8353  C  CB  . ARG H  1 79  ? -2.487  18.520  93.050  1.00 74.59  ? 79  ARG O CB  1 
ATOM   8354  C  CG  . ARG H  1 79  ? -3.489  17.447  92.636  1.00 73.92  ? 79  ARG O CG  1 
ATOM   8355  C  CD  . ARG H  1 79  ? -2.921  16.042  92.764  1.00 72.65  ? 79  ARG O CD  1 
ATOM   8356  N  NE  . ARG H  1 79  ? -1.944  15.741  91.717  1.00 69.80  ? 79  ARG O NE  1 
ATOM   8357  C  CZ  . ARG H  1 79  ? -1.421  14.535  91.469  1.00 68.29  ? 79  ARG O CZ  1 
ATOM   8358  N  NH1 . ARG H  1 79  ? -1.769  13.469  92.190  1.00 69.31  ? 79  ARG O NH1 1 
ATOM   8359  N  NH2 . ARG H  1 79  ? -0.540  14.388  90.477  1.00 65.94  ? 79  ARG O NH2 1 
ATOM   8360  N  N   . HIS H  1 80  ? -1.388  20.139  90.593  1.00 70.94  ? 80  HIS O N   1 
ATOM   8361  C  CA  . HIS H  1 80  ? -1.048  19.997  89.180  1.00 68.40  ? 80  HIS O CA  1 
ATOM   8362  C  C   . HIS H  1 80  ? -0.965  18.504  88.851  1.00 66.44  ? 80  HIS O C   1 
ATOM   8363  O  O   . HIS H  1 80  ? -0.772  17.681  89.747  1.00 66.89  ? 80  HIS O O   1 
ATOM   8364  C  CB  . HIS H  1 80  ? 0.274   20.701  88.843  1.00 67.73  ? 80  HIS O CB  1 
ATOM   8365  C  CG  . HIS H  1 80  ? 0.339   22.127  89.298  1.00 69.93  ? 80  HIS O CG  1 
ATOM   8366  N  ND1 . HIS H  1 80  ? 1.512   22.735  89.698  1.00 70.55  ? 80  HIS O ND1 1 
ATOM   8367  C  CD2 . HIS H  1 80  ? -0.631  23.061  89.428  1.00 71.91  ? 80  HIS O CD2 1 
ATOM   8368  C  CE1 . HIS H  1 80  ? 1.263   23.989  90.030  1.00 72.79  ? 80  HIS O CE1 1 
ATOM   8369  N  NE2 . HIS H  1 80  ? -0.029  24.212  89.877  1.00 73.65  ? 80  HIS O NE2 1 
ATOM   8370  N  N   . VAL H  1 81  ? -1.109  18.159  87.571  1.00 64.50  ? 81  VAL O N   1 
ATOM   8371  C  CA  . VAL H  1 81  ? -1.044  16.753  87.131  1.00 62.75  ? 81  VAL O CA  1 
ATOM   8372  C  C   . VAL H  1 81  ? 0.339   16.135  87.379  1.00 61.60  ? 81  VAL O C   1 
ATOM   8373  O  O   . VAL H  1 81  ? 0.439   14.951  87.710  1.00 61.19  ? 81  VAL O O   1 
ATOM   8374  C  CB  . VAL H  1 81  ? -1.479  16.591  85.651  1.00 61.26  ? 81  VAL O CB  1 
ATOM   8375  C  CG1 . VAL H  1 81  ? -1.178  15.190  85.114  1.00 59.50  ? 81  VAL O CG1 1 
ATOM   8376  C  CG2 . VAL H  1 81  ? -2.970  16.878  85.519  1.00 62.68  ? 81  VAL O CG2 1 
ATOM   8377  N  N   . GLY H  1 82  ? 1.391   16.941  87.240  1.00 61.34  ? 82  GLY O N   1 
ATOM   8378  C  CA  . GLY H  1 82  ? 2.763   16.487  87.469  1.00 60.62  ? 82  GLY O CA  1 
ATOM   8379  C  C   . GLY H  1 82  ? 3.214   16.334  88.916  1.00 62.30  ? 82  GLY O C   1 
ATOM   8380  O  O   . GLY H  1 82  ? 4.284   15.776  89.163  1.00 61.97  ? 82  GLY O O   1 
ATOM   8381  N  N   . ASP H  1 83  ? 2.418   16.809  89.872  1.00 64.34  ? 83  ASP O N   1 
ATOM   8382  C  CA  . ASP H  1 83  ? 2.822   16.810  91.287  1.00 66.43  ? 83  ASP O CA  1 
ATOM   8383  C  C   . ASP H  1 83  ? 2.814   15.417  91.923  1.00 66.68  ? 83  ASP O C   1 
ATOM   8384  O  O   . ASP H  1 83  ? 1.783   14.961  92.434  1.00 67.77  ? 83  ASP O O   1 
ATOM   8385  C  CB  . ASP H  1 83  ? 1.931   17.751  92.092  1.00 68.82  ? 83  ASP O CB  1 
ATOM   8386  C  CG  . ASP H  1 83  ? 2.050   19.189  91.648  1.00 69.16  ? 83  ASP O CG  1 
ATOM   8387  O  OD1 . ASP H  1 83  ? 3.146   19.617  91.218  1.00 68.28  ? 83  ASP O OD1 1 
ATOM   8388  O  OD2 . ASP H  1 83  ? 1.039   19.904  91.730  1.00 70.40  ? 83  ASP O OD2 1 
ATOM   8389  N  N   . LEU H  1 84  ? 3.977   14.760  91.888  1.00 65.95  ? 84  LEU O N   1 
ATOM   8390  C  CA  . LEU H  1 84  ? 4.173   13.433  92.485  1.00 66.42  ? 84  LEU O CA  1 
ATOM   8391  C  C   . LEU H  1 84  ? 4.834   13.486  93.874  1.00 69.00  ? 84  LEU O C   1 
ATOM   8392  O  O   . LEU H  1 84  ? 5.281   12.453  94.385  1.00 69.68  ? 84  LEU O O   1 
ATOM   8393  C  CB  . LEU H  1 84  ? 4.994   12.541  91.539  1.00 64.24  ? 84  LEU O CB  1 
ATOM   8394  C  CG  . LEU H  1 84  ? 4.398   12.288  90.150  1.00 61.95  ? 84  LEU O CG  1 
ATOM   8395  C  CD1 . LEU H  1 84  ? 5.437   11.689  89.215  1.00 60.10  ? 84  LEU O CD1 1 
ATOM   8396  C  CD2 . LEU H  1 84  ? 3.181   11.383  90.256  1.00 62.24  ? 84  LEU O CD2 1 
ATOM   8397  N  N   . GLY H  1 85  ? 4.888   14.675  94.482  1.00 70.75  ? 85  GLY O N   1 
ATOM   8398  C  CA  . GLY H  1 85  ? 5.354   14.832  95.854  1.00 73.63  ? 85  GLY O CA  1 
ATOM   8399  C  C   . GLY H  1 85  ? 6.860   14.731  96.010  1.00 73.86  ? 85  GLY O C   1 
ATOM   8400  O  O   . GLY H  1 85  ? 7.614   15.380  95.278  1.00 72.68  ? 85  GLY O O   1 
ATOM   8401  N  N   . ASN H  1 86  ? 7.287   13.912  96.970  1.00 75.68  ? 86  ASN O N   1 
ATOM   8402  C  CA  . ASN H  1 86  ? 8.690   13.774  97.345  1.00 76.66  ? 86  ASN O CA  1 
ATOM   8403  C  C   . ASN H  1 86  ? 9.166   12.336  97.194  1.00 75.93  ? 86  ASN O C   1 
ATOM   8404  O  O   . ASN H  1 86  ? 8.379   11.391  97.310  1.00 75.84  ? 86  ASN O O   1 
ATOM   8405  C  CB  . ASN H  1 86  ? 8.882   14.202  98.803  1.00 80.40  ? 86  ASN O CB  1 
ATOM   8406  C  CG  . ASN H  1 86  ? 8.688   15.690  99.006  1.00 81.58  ? 86  ASN O CG  1 
ATOM   8407  O  OD1 . ASN H  1 86  ? 9.310   16.504  98.327  1.00 80.54  ? 86  ASN O OD1 1 
ATOM   8408  N  ND2 . ASN H  1 86  ? 7.834   16.055  99.951  1.00 84.03  ? 86  ASN O ND2 1 
ATOM   8409  N  N   . VAL H  1 87  ? 10.463  12.191  96.934  1.00 75.64  ? 87  VAL O N   1 
ATOM   8410  C  CA  . VAL H  1 87  ? 11.171  10.919  97.100  1.00 76.03  ? 87  VAL O CA  1 
ATOM   8411  C  C   . VAL H  1 87  ? 12.214  11.105  98.208  1.00 79.17  ? 87  VAL O C   1 
ATOM   8412  O  O   . VAL H  1 87  ? 12.810  12.178  98.331  1.00 79.99  ? 87  VAL O O   1 
ATOM   8413  C  CB  . VAL H  1 87  ? 11.828  10.410  95.792  1.00 73.27  ? 87  VAL O CB  1 
ATOM   8414  C  CG1 . VAL H  1 87  ? 10.764  10.121  94.740  1.00 70.53  ? 87  VAL O CG1 1 
ATOM   8415  C  CG2 . VAL H  1 87  ? 12.872  11.382  95.246  1.00 72.78  ? 87  VAL O CG2 1 
ATOM   8416  N  N   . THR H  1 88  ? 12.421  10.061  99.008  1.00 81.16  ? 88  THR O N   1 
ATOM   8417  C  CA  . THR H  1 88  ? 13.308  10.119  100.179 1.00 84.73  ? 88  THR O CA  1 
ATOM   8418  C  C   . THR H  1 88  ? 14.616  9.390   99.891  1.00 84.87  ? 88  THR O C   1 
ATOM   8419  O  O   . THR H  1 88  ? 14.608  8.193   99.598  1.00 84.15  ? 88  THR O O   1 
ATOM   8420  C  CB  . THR H  1 88  ? 12.643  9.478   101.413 1.00 87.66  ? 88  THR O CB  1 
ATOM   8421  O  OG1 . THR H  1 88  ? 11.315  9.989   101.561 1.00 87.37  ? 88  THR O OG1 1 
ATOM   8422  C  CG2 . THR H  1 88  ? 13.441  9.766   102.688 1.00 91.79  ? 88  THR O CG2 1 
ATOM   8423  N  N   . ALA H  1 89  ? 15.731  10.113  99.986  1.00 86.06  ? 89  ALA O N   1 
ATOM   8424  C  CA  . ALA H  1 89  ? 17.063  9.535   99.795  1.00 86.79  ? 89  ALA O CA  1 
ATOM   8425  C  C   . ALA H  1 89  ? 17.676  9.128   101.138 1.00 91.09  ? 89  ALA O C   1 
ATOM   8426  O  O   . ALA H  1 89  ? 17.690  9.921   102.084 1.00 93.78  ? 89  ALA O O   1 
ATOM   8427  C  CB  . ALA H  1 89  ? 17.967  10.527  99.085  1.00 85.92  ? 89  ALA O CB  1 
ATOM   8428  N  N   . ASP H  1 90  ? 18.192  7.899   101.205 1.00 91.97  ? 90  ASP O N   1 
ATOM   8429  C  CA  . ASP H  1 90  ? 18.836  7.368   102.421 1.00 96.32  ? 90  ASP O CA  1 
ATOM   8430  C  C   . ASP H  1 90  ? 20.191  8.044   102.690 1.00 98.70  ? 90  ASP O C   1 
ATOM   8431  O  O   . ASP H  1 90  ? 20.590  8.946   101.948 1.00 96.96  ? 90  ASP O O   1 
ATOM   8432  C  CB  . ASP H  1 90  ? 18.974  5.829   102.335 1.00 96.63  ? 90  ASP O CB  1 
ATOM   8433  C  CG  . ASP H  1 90  ? 19.937  5.359   101.235 1.00 94.79  ? 90  ASP O CG  1 
ATOM   8434  O  OD1 . ASP H  1 90  ? 20.478  6.191   100.477 1.00 93.06  ? 90  ASP O OD1 1 
ATOM   8435  O  OD2 . ASP H  1 90  ? 20.150  4.134   101.131 1.00 95.27  ? 90  ASP O OD2 1 
ATOM   8436  N  N   . LYS H  1 91  ? 20.890  7.609   103.741 1.00 102.94 ? 91  LYS O N   1 
ATOM   8437  C  CA  . LYS H  1 91  ? 22.236  8.128   104.072 1.00 105.83 ? 91  LYS O CA  1 
ATOM   8438  C  C   . LYS H  1 91  ? 23.258  8.048   102.924 1.00 103.90 ? 91  LYS O C   1 
ATOM   8439  O  O   . LYS H  1 91  ? 24.115  8.924   102.793 1.00 104.80 ? 91  LYS O O   1 
ATOM   8440  C  CB  . LYS H  1 91  ? 22.804  7.443   105.330 1.00 110.86 ? 91  LYS O CB  1 
ATOM   8441  C  CG  . LYS H  1 91  ? 23.010  5.933   105.236 1.00 111.33 ? 91  LYS O CG  1 
ATOM   8442  C  CD  . LYS H  1 91  ? 23.808  5.418   106.424 1.00 116.78 ? 91  LYS O CD  1 
ATOM   8443  C  CE  . LYS H  1 91  ? 23.936  3.902   106.412 1.00 117.68 ? 91  LYS O CE  1 
ATOM   8444  N  NZ  . LYS H  1 91  ? 22.679  3.212   106.818 1.00 117.42 ? 91  LYS O NZ  1 
ATOM   8445  N  N   . ASP H  1 92  ? 23.154  7.007   102.097 1.00 101.48 ? 92  ASP O N   1 
ATOM   8446  C  CA  . ASP H  1 92  ? 24.021  6.839   100.922 1.00 99.52  ? 92  ASP O CA  1 
ATOM   8447  C  C   . ASP H  1 92  ? 23.643  7.751   99.744  1.00 95.46  ? 92  ASP O C   1 
ATOM   8448  O  O   . ASP H  1 92  ? 24.405  7.859   98.785  1.00 94.12  ? 92  ASP O O   1 
ATOM   8449  C  CB  . ASP H  1 92  ? 24.017  5.373   100.458 1.00 98.66  ? 92  ASP O CB  1 
ATOM   8450  C  CG  . ASP H  1 92  ? 24.523  4.404   101.532 1.00 102.98 ? 92  ASP O CG  1 
ATOM   8451  O  OD1 . ASP H  1 92  ? 25.159  4.848   102.514 1.00 106.77 ? 92  ASP O OD1 1 
ATOM   8452  O  OD2 . ASP H  1 92  ? 24.279  3.186   101.385 1.00 102.77 ? 92  ASP O OD2 1 
ATOM   8453  N  N   . GLY H  1 93  ? 22.474  8.390   99.812  1.00 93.77  ? 93  GLY O N   1 
ATOM   8454  C  CA  . GLY H  1 93  ? 21.993  9.287   98.765  1.00 90.25  ? 93  GLY O CA  1 
ATOM   8455  C  C   . GLY H  1 93  ? 21.131  8.604   97.719  1.00 86.43  ? 93  GLY O C   1 
ATOM   8456  O  O   . GLY H  1 93  ? 20.826  9.201   96.680  1.00 83.49  ? 93  GLY O O   1 
ATOM   8457  N  N   . VAL H  1 94  ? 20.730  7.360   97.995  1.00 86.77  ? 94  VAL O N   1 
ATOM   8458  C  CA  . VAL H  1 94  ? 19.934  6.561   97.071  1.00 83.64  ? 94  VAL O CA  1 
ATOM   8459  C  C   . VAL H  1 94  ? 18.470  6.660   97.479  1.00 82.90  ? 94  VAL O C   1 
ATOM   8460  O  O   . VAL H  1 94  ? 18.128  6.413   98.638  1.00 85.49  ? 94  VAL O O   1 
ATOM   8461  C  CB  . VAL H  1 94  ? 20.373  5.080   97.073  1.00 84.65  ? 94  VAL O CB  1 
ATOM   8462  C  CG1 . VAL H  1 94  ? 19.523  4.258   96.104  1.00 81.59  ? 94  VAL O CG1 1 
ATOM   8463  C  CG2 . VAL H  1 94  ? 21.855  4.964   96.727  1.00 85.86  ? 94  VAL O CG2 1 
ATOM   8464  N  N   . ALA H  1 95  ? 17.618  7.025   96.522  1.00 79.64  ? 95  ALA O N   1 
ATOM   8465  C  CA  . ALA H  1 95  ? 16.175  7.105   96.734  1.00 78.77  ? 95  ALA O CA  1 
ATOM   8466  C  C   . ALA H  1 95  ? 15.471  6.003   95.948  1.00 76.63  ? 95  ALA O C   1 
ATOM   8467  O  O   . ALA H  1 95  ? 15.308  6.108   94.726  1.00 73.77  ? 95  ALA O O   1 
ATOM   8468  C  CB  . ALA H  1 95  ? 15.657  8.477   96.325  1.00 77.17  ? 95  ALA O CB  1 
ATOM   8469  N  N   . ASP H  1 96  ? 15.076  4.939   96.650  1.00 78.34  ? 96  ASP O N   1 
ATOM   8470  C  CA  . ASP H  1 96  ? 14.250  3.877   96.067  1.00 76.84  ? 96  ASP O CA  1 
ATOM   8471  C  C   . ASP H  1 96  ? 12.832  4.418   95.877  1.00 75.25  ? 96  ASP O C   1 
ATOM   8472  O  O   . ASP H  1 96  ? 12.142  4.714   96.852  1.00 77.00  ? 96  ASP O O   1 
ATOM   8473  C  CB  . ASP H  1 96  ? 14.238  2.635   96.973  1.00 79.63  ? 96  ASP O CB  1 
ATOM   8474  C  CG  . ASP H  1 96  ? 13.591  1.412   96.311  1.00 78.38  ? 96  ASP O CG  1 
ATOM   8475  O  OD1 . ASP H  1 96  ? 12.614  1.553   95.548  1.00 75.98  ? 96  ASP O OD1 1 
ATOM   8476  O  OD2 . ASP H  1 96  ? 14.058  0.287   96.574  1.00 80.18  ? 96  ASP O OD2 1 
ATOM   8477  N  N   . VAL H  1 97  ? 12.409  4.547   94.621  1.00 72.21  ? 97  VAL O N   1 
ATOM   8478  C  CA  . VAL H  1 97  ? 11.075  5.055   94.301  1.00 70.73  ? 97  VAL O CA  1 
ATOM   8479  C  C   . VAL H  1 97  ? 10.112  3.887   94.123  1.00 70.47  ? 97  VAL O C   1 
ATOM   8480  O  O   . VAL H  1 97  ? 10.450  2.880   93.505  1.00 69.79  ? 97  VAL O O   1 
ATOM   8481  C  CB  . VAL H  1 97  ? 11.092  5.935   93.037  1.00 67.93  ? 97  VAL O CB  1 
ATOM   8482  C  CG1 . VAL H  1 97  ? 9.694   6.478   92.727  1.00 66.74  ? 97  VAL O CG1 1 
ATOM   8483  C  CG2 . VAL H  1 97  ? 12.091  7.075   93.209  1.00 68.49  ? 97  VAL O CG2 1 
ATOM   8484  N  N   . SER H  1 98  ? 8.926   4.024   94.706  1.00 71.35  ? 98  SER O N   1 
ATOM   8485  C  CA  . SER H  1 98  ? 7.835   3.071   94.516  1.00 71.22  ? 98  SER O CA  1 
ATOM   8486  C  C   . SER H  1 98  ? 6.522   3.779   94.844  1.00 71.50  ? 98  SER O C   1 
ATOM   8487  O  O   . SER H  1 98  ? 6.112   3.857   96.006  1.00 73.98  ? 98  SER O O   1 
ATOM   8488  C  CB  . SER H  1 98  ? 8.027   1.826   95.379  1.00 73.84  ? 98  SER O CB  1 
ATOM   8489  O  OG  . SER H  1 98  ? 7.056   0.850   95.044  1.00 73.70  ? 98  SER O OG  1 
ATOM   8490  N  N   . ILE H  1 99  ? 5.898   4.319   93.802  1.00 69.11  ? 99  ILE O N   1 
ATOM   8491  C  CA  . ILE H  1 99  ? 4.750   5.217   93.913  1.00 69.19  ? 99  ILE O CA  1 
ATOM   8492  C  C   . ILE H  1 99  ? 3.650   4.699   92.990  1.00 67.75  ? 99  ILE O C   1 
ATOM   8493  O  O   . ILE H  1 99  ? 3.928   3.999   92.012  1.00 66.06  ? 99  ILE O O   1 
ATOM   8494  C  CB  . ILE H  1 99  ? 5.179   6.669   93.548  1.00 68.07  ? 99  ILE O CB  1 
ATOM   8495  C  CG1 . ILE H  1 99  ? 5.977   7.281   94.712  1.00 70.32  ? 99  ILE O CG1 1 
ATOM   8496  C  CG2 . ILE H  1 99  ? 3.995   7.580   93.222  1.00 67.53  ? 99  ILE O CG2 1 
ATOM   8497  C  CD1 . ILE H  1 99  ? 6.835   8.469   94.321  1.00 69.41  ? 99  ILE O CD1 1 
ATOM   8498  N  N   . GLU H  1 100 ? 2.405   5.027   93.332  1.00 68.70  ? 100 GLU O N   1 
ATOM   8499  C  CA  . GLU H  1 100 ? 1.245   4.742   92.494  1.00 67.67  ? 100 GLU O CA  1 
ATOM   8500  C  C   . GLU H  1 100 ? 0.331   5.967   92.473  1.00 67.74  ? 100 GLU O C   1 
ATOM   8501  O  O   . GLU H  1 100 ? -0.106  6.430   93.532  1.00 69.93  ? 100 GLU O O   1 
ATOM   8502  C  CB  . GLU H  1 100 ? 0.504   3.524   93.035  1.00 69.60  ? 100 GLU O CB  1 
ATOM   8503  C  CG  . GLU H  1 100 ? -0.471  2.913   92.047  1.00 68.66  ? 100 GLU O CG  1 
ATOM   8504  C  CD  . GLU H  1 100 ? -1.086  1.622   92.554  1.00 70.75  ? 100 GLU O CD  1 
ATOM   8505  O  OE1 . GLU H  1 100 ? -0.346  0.770   93.098  1.00 71.86  ? 100 GLU O OE1 1 
ATOM   8506  O  OE2 . GLU H  1 100 ? -2.315  1.458   92.406  1.00 71.57  ? 100 GLU O OE2 1 
ATOM   8507  N  N   . ASP H  1 101 ? 0.050   6.482   91.271  1.00 65.56  ? 101 ASP O N   1 
ATOM   8508  C  CA  . ASP H  1 101 ? -0.689  7.739   91.092  1.00 65.52  ? 101 ASP O CA  1 
ATOM   8509  C  C   . ASP H  1 101 ? -1.729  7.590   89.984  1.00 64.43  ? 101 ASP O C   1 
ATOM   8510  O  O   . ASP H  1 101 ? -1.462  6.935   88.979  1.00 62.77  ? 101 ASP O O   1 
ATOM   8511  C  CB  . ASP H  1 101 ? 0.291   8.870   90.751  1.00 64.28  ? 101 ASP O CB  1 
ATOM   8512  C  CG  . ASP H  1 101 ? -0.325  10.255  90.910  1.00 65.07  ? 101 ASP O CG  1 
ATOM   8513  O  OD1 . ASP H  1 101 ? -0.323  10.783  92.042  1.00 67.08  ? 101 ASP O OD1 1 
ATOM   8514  O  OD2 . ASP H  1 101 ? -0.796  10.824  89.902  1.00 63.86  ? 101 ASP O OD2 1 
ATOM   8515  N  N   . SER H  1 102 ? -2.899  8.206   90.167  1.00 65.63  ? 102 SER O N   1 
ATOM   8516  C  CA  . SER H  1 102 ? -4.029  8.090   89.222  1.00 65.23  ? 102 SER O CA  1 
ATOM   8517  C  C   . SER H  1 102 ? -4.481  9.430   88.609  1.00 64.82  ? 102 SER O C   1 
ATOM   8518  O  O   . SER H  1 102 ? -5.559  9.504   88.018  1.00 65.18  ? 102 SER O O   1 
ATOM   8519  C  CB  . SER H  1 102 ? -5.215  7.409   89.909  1.00 67.59  ? 102 SER O CB  1 
ATOM   8520  O  OG  . SER H  1 102 ? -4.809  6.223   90.569  1.00 68.37  ? 102 SER O OG  1 
ATOM   8521  N  N   . VAL H  1 103 ? -3.661  10.475  88.751  1.00 64.30  ? 103 VAL O N   1 
ATOM   8522  C  CA  . VAL H  1 103 ? -3.864  11.749  88.049  1.00 63.82  ? 103 VAL O CA  1 
ATOM   8523  C  C   . VAL H  1 103 ? -3.028  11.767  86.761  1.00 61.31  ? 103 VAL O C   1 
ATOM   8524  O  O   . VAL H  1 103 ? -3.516  12.201  85.714  1.00 60.67  ? 103 VAL O O   1 
ATOM   8525  C  CB  . VAL H  1 103 ? -3.504  12.957  88.944  1.00 65.13  ? 103 VAL O CB  1 
ATOM   8526  C  CG1 . VAL H  1 103 ? -3.772  14.272  88.217  1.00 64.99  ? 103 VAL O CG1 1 
ATOM   8527  C  CG2 . VAL H  1 103 ? -4.288  12.901  90.249  1.00 67.86  ? 103 VAL O CG2 1 
ATOM   8528  N  N   . ILE H  1 104 ? -1.770  11.327  86.853  1.00 60.15  ? 104 ILE O N   1 
ATOM   8529  C  CA  . ILE H  1 104 ? -0.941  11.077  85.662  1.00 57.98  ? 104 ILE O CA  1 
ATOM   8530  C  C   . ILE H  1 104 ? -1.438  9.854   84.896  1.00 57.27  ? 104 ILE O C   1 
ATOM   8531  O  O   . ILE H  1 104 ? -2.048  8.950   85.478  1.00 58.29  ? 104 ILE O O   1 
ATOM   8532  C  CB  . ILE H  1 104 ? 0.569   10.878  85.978  1.00 57.25  ? 104 ILE O CB  1 
ATOM   8533  C  CG1 . ILE H  1 104 ? 0.830   9.662   86.890  1.00 57.99  ? 104 ILE O CG1 1 
ATOM   8534  C  CG2 . ILE H  1 104 ? 1.158   12.144  86.587  1.00 58.02  ? 104 ILE O CG2 1 
ATOM   8535  C  CD1 . ILE H  1 104 ? 2.281   9.221   86.923  1.00 57.22  ? 104 ILE O CD1 1 
ATOM   8536  N  N   . SER H  1 105 ? -1.153  9.838   83.593  1.00 55.74  ? 105 SER O N   1 
ATOM   8537  C  CA  . SER H  1 105 ? -1.450  8.698   82.725  1.00 55.05  ? 105 SER O CA  1 
ATOM   8538  C  C   . SER H  1 105 ? -0.373  8.539   81.653  1.00 53.30  ? 105 SER O C   1 
ATOM   8539  O  O   . SER H  1 105 ? 0.427   9.446   81.415  1.00 52.67  ? 105 SER O O   1 
ATOM   8540  C  CB  . SER H  1 105 ? -2.825  8.863   82.070  1.00 55.78  ? 105 SER O CB  1 
ATOM   8541  O  OG  . SER H  1 105 ? -3.288  7.627   81.543  1.00 55.81  ? 105 SER O OG  1 
ATOM   8542  N  N   . LEU H  1 106 ? -0.360  7.372   81.021  1.00 52.74  ? 106 LEU O N   1 
ATOM   8543  C  CA  . LEU H  1 106 ? 0.521   7.101   79.889  1.00 51.37  ? 106 LEU O CA  1 
ATOM   8544  C  C   . LEU H  1 106 ? -0.218  7.184   78.547  1.00 51.15  ? 106 LEU O C   1 
ATOM   8545  O  O   . LEU H  1 106 ? 0.351   6.839   77.515  1.00 50.27  ? 106 LEU O O   1 
ATOM   8546  C  CB  . LEU H  1 106 ? 1.213   5.745   80.081  1.00 51.18  ? 106 LEU O CB  1 
ATOM   8547  C  CG  . LEU H  1 106 ? 2.009   5.613   81.396  1.00 51.68  ? 106 LEU O CG  1 
ATOM   8548  C  CD1 . LEU H  1 106 ? 2.714   4.267   81.462  1.00 51.70  ? 106 LEU O CD1 1 
ATOM   8549  C  CD2 . LEU H  1 106 ? 3.013   6.748   81.581  1.00 51.19  ? 106 LEU O CD2 1 
ATOM   8550  N  N   . SER H  1 107 ? -1.466  7.665   78.572  1.00 52.20  ? 107 SER O N   1 
ATOM   8551  C  CA  . SER H  1 107 ? -2.244  7.957   77.363  1.00 52.46  ? 107 SER O CA  1 
ATOM   8552  C  C   . SER H  1 107 ? -3.248  9.099   77.595  1.00 53.70  ? 107 SER O C   1 
ATOM   8553  O  O   . SER H  1 107 ? -3.554  9.454   78.738  1.00 54.52  ? 107 SER O O   1 
ATOM   8554  C  CB  . SER H  1 107 ? -2.994  6.704   76.898  1.00 53.02  ? 107 SER O CB  1 
ATOM   8555  O  OG  . SER H  1 107 ? -3.915  6.261   77.883  1.00 54.32  ? 107 SER O OG  1 
ATOM   8556  N  N   . GLY H  1 108 ? -3.732  9.674   76.496  1.00 54.06  ? 108 GLY O N   1 
ATOM   8557  C  CA  . GLY H  1 108 ? -4.782  10.685  76.519  1.00 55.59  ? 108 GLY O CA  1 
ATOM   8558  C  C   . GLY H  1 108 ? -4.389  12.063  77.031  1.00 55.83  ? 108 GLY O C   1 
ATOM   8559  O  O   . GLY H  1 108 ? -3.253  12.503  76.849  1.00 54.75  ? 108 GLY O O   1 
ATOM   8560  N  N   . ASP H  1 109 ? -5.339  12.729  77.690  1.00 57.52  ? 109 ASP O N   1 
ATOM   8561  C  CA  . ASP H  1 109 ? -5.227  14.154  78.047  1.00 58.30  ? 109 ASP O CA  1 
ATOM   8562  C  C   . ASP H  1 109 ? -4.090  14.438  79.016  1.00 57.57  ? 109 ASP O C   1 
ATOM   8563  O  O   . ASP H  1 109 ? -3.347  15.407  78.839  1.00 57.33  ? 109 ASP O O   1 
ATOM   8564  C  CB  . ASP H  1 109 ? -6.522  14.662  78.694  1.00 60.53  ? 109 ASP O CB  1 
ATOM   8565  C  CG  . ASP H  1 109 ? -7.732  14.504  77.800  1.00 61.84  ? 109 ASP O CG  1 
ATOM   8566  O  OD1 . ASP H  1 109 ? -8.157  15.513  77.195  1.00 63.02  ? 109 ASP O OD1 1 
ATOM   8567  O  OD2 . ASP H  1 109 ? -8.245  13.365  77.700  1.00 61.93  ? 109 ASP O OD2 1 
ATOM   8568  N  N   . HIS H  1 110 ? -3.970  13.589  80.037  1.00 57.48  ? 110 HIS O N   1 
ATOM   8569  C  CA  . HIS H  1 110 ? -2.977  13.757  81.100  1.00 57.21  ? 110 HIS O CA  1 
ATOM   8570  C  C   . HIS H  1 110 ? -1.702  12.931  80.847  1.00 55.46  ? 110 HIS O C   1 
ATOM   8571  O  O   . HIS H  1 110 ? -0.976  12.589  81.792  1.00 55.35  ? 110 HIS O O   1 
ATOM   8572  C  CB  . HIS H  1 110 ? -3.614  13.385  82.449  1.00 58.64  ? 110 HIS O CB  1 
ATOM   8573  C  CG  . HIS H  1 110 ? -4.624  14.377  82.935  1.00 60.66  ? 110 HIS O CG  1 
ATOM   8574  N  ND1 . HIS H  1 110 ? -5.195  14.299  84.188  1.00 62.38  ? 110 HIS O ND1 1 
ATOM   8575  C  CD2 . HIS H  1 110 ? -5.138  15.489  82.356  1.00 61.48  ? 110 HIS O CD2 1 
ATOM   8576  C  CE1 . HIS H  1 110 ? -6.032  15.307  84.351  1.00 64.14  ? 110 HIS O CE1 1 
ATOM   8577  N  NE2 . HIS H  1 110 ? -6.014  16.046  83.256  1.00 63.64  ? 110 HIS O NE2 1 
ATOM   8578  N  N   . CYS H  1 111 ? -1.423  12.639  79.575  1.00 54.35  ? 111 CYS O N   1 
ATOM   8579  C  CA  . CYS H  1 111 ? -0.301  11.797  79.201  1.00 52.94  ? 111 CYS O CA  1 
ATOM   8580  C  C   . CYS H  1 111 ? 1.022   12.490  79.501  1.00 52.42  ? 111 CYS O C   1 
ATOM   8581  O  O   . CYS H  1 111 ? 1.225   13.650  79.116  1.00 52.59  ? 111 CYS O O   1 
ATOM   8582  C  CB  . CYS H  1 111 ? -0.357  11.445  77.716  1.00 52.27  ? 111 CYS O CB  1 
ATOM   8583  S  SG  . CYS H  1 111 ? 0.903   10.254  77.229  1.00 50.95  ? 111 CYS O SG  1 
ATOM   8584  N  N   . ILE H  1 112 ? 1.907   11.763  80.181  1.00 51.97  ? 112 ILE O N   1 
ATOM   8585  C  CA  . ILE H  1 112 ? 3.231   12.271  80.566  1.00 51.77  ? 112 ILE O CA  1 
ATOM   8586  C  C   . ILE H  1 112 ? 4.353   11.838  79.617  1.00 50.57  ? 112 ILE O C   1 
ATOM   8587  O  O   . ILE H  1 112 ? 5.450   12.398  79.671  1.00 50.52  ? 112 ILE O O   1 
ATOM   8588  C  CB  . ILE H  1 112 ? 3.590   11.908  82.027  1.00 52.56  ? 112 ILE O CB  1 
ATOM   8589  C  CG1 . ILE H  1 112 ? 3.670   10.386  82.252  1.00 52.29  ? 112 ILE O CG1 1 
ATOM   8590  C  CG2 . ILE H  1 112 ? 2.575   12.537  82.973  1.00 54.03  ? 112 ILE O CG2 1 
ATOM   8591  C  CD1 . ILE H  1 112 ? 4.168   10.005  83.631  1.00 53.32  ? 112 ILE O CD1 1 
ATOM   8592  N  N   . ILE H  1 113 ? 4.084   10.858  78.755  1.00 49.86  ? 113 ILE O N   1 
ATOM   8593  C  CA  . ILE H  1 113 ? 5.036   10.468  77.706  1.00 48.95  ? 113 ILE O CA  1 
ATOM   8594  C  C   . ILE H  1 113 ? 5.301   11.681  76.812  1.00 48.89  ? 113 ILE O C   1 
ATOM   8595  O  O   . ILE H  1 113 ? 4.364   12.336  76.350  1.00 49.29  ? 113 ILE O O   1 
ATOM   8596  C  CB  . ILE H  1 113 ? 4.521   9.277   76.863  1.00 48.54  ? 113 ILE O CB  1 
ATOM   8597  C  CG1 . ILE H  1 113 ? 4.482   7.998   77.711  1.00 48.73  ? 113 ILE O CG1 1 
ATOM   8598  C  CG2 . ILE H  1 113 ? 5.417   9.047   75.647  1.00 47.94  ? 113 ILE O CG2 1 
ATOM   8599  C  CD1 . ILE H  1 113 ? 3.693   6.866   77.088  1.00 48.77  ? 113 ILE O CD1 1 
ATOM   8600  N  N   . GLY H  1 114 ? 6.579   11.981  76.599  1.00 48.65  ? 114 GLY O N   1 
ATOM   8601  C  CA  . GLY H  1 114 ? 6.996   13.151  75.838  1.00 48.90  ? 114 GLY O CA  1 
ATOM   8602  C  C   . GLY H  1 114 ? 7.246   14.392  76.672  1.00 49.72  ? 114 GLY O C   1 
ATOM   8603  O  O   . GLY H  1 114 ? 7.612   15.432  76.130  1.00 50.23  ? 114 GLY O O   1 
ATOM   8604  N  N   . ARG H  1 115 ? 7.052   14.295  77.983  1.00 50.13  ? 115 ARG O N   1 
ATOM   8605  C  CA  . ARG H  1 115 ? 7.291   15.404  78.894  1.00 51.19  ? 115 ARG O CA  1 
ATOM   8606  C  C   . ARG H  1 115 ? 8.492   15.036  79.772  1.00 51.46  ? 115 ARG O C   1 
ATOM   8607  O  O   . ARG H  1 115 ? 9.068   13.952  79.608  1.00 50.82  ? 115 ARG O O   1 
ATOM   8608  C  CB  . ARG H  1 115 ? 6.021   15.688  79.703  1.00 51.92  ? 115 ARG O CB  1 
ATOM   8609  C  CG  . ARG H  1 115 ? 4.782   15.861  78.833  1.00 51.85  ? 115 ARG O CG  1 
ATOM   8610  C  CD  . ARG H  1 115 ? 3.573   16.355  79.607  1.00 53.00  ? 115 ARG O CD  1 
ATOM   8611  N  NE  . ARG H  1 115 ? 2.372   16.421  78.759  1.00 53.18  ? 115 ARG O NE  1 
ATOM   8612  C  CZ  . ARG H  1 115 ? 2.027   17.440  77.965  1.00 53.86  ? 115 ARG O CZ  1 
ATOM   8613  N  NH1 . ARG H  1 115 ? 2.776   18.537  77.861  1.00 54.43  ? 115 ARG O NH1 1 
ATOM   8614  N  NH2 . ARG H  1 115 ? 0.905   17.364  77.259  1.00 54.27  ? 115 ARG O NH2 1 
ATOM   8615  N  N   . THR H  1 116 ? 8.875   15.937  80.679  1.00 52.63  ? 116 THR O N   1 
ATOM   8616  C  CA  . THR H  1 116 ? 10.109  15.804  81.458  1.00 53.29  ? 116 THR O CA  1 
ATOM   8617  C  C   . THR H  1 116 ? 9.839   15.506  82.932  1.00 54.29  ? 116 THR O C   1 
ATOM   8618  O  O   . THR H  1 116 ? 9.133   16.267  83.591  1.00 55.31  ? 116 THR O O   1 
ATOM   8619  C  CB  . THR H  1 116 ? 10.941  17.101  81.353  1.00 54.35  ? 116 THR O CB  1 
ATOM   8620  O  OG1 . THR H  1 116 ? 11.320  17.316  79.990  1.00 53.68  ? 116 THR O OG1 1 
ATOM   8621  C  CG2 . THR H  1 116 ? 12.204  17.037  82.202  1.00 55.43  ? 116 THR O CG2 1 
ATOM   8622  N  N   . LEU H  1 117 ? 10.412  14.411  83.440  1.00 54.27  ? 117 LEU O N   1 
ATOM   8623  C  CA  . LEU H  1 117 ? 10.443  14.124  84.885  1.00 55.65  ? 117 LEU O CA  1 
ATOM   8624  C  C   . LEU H  1 117 ? 11.646  14.840  85.492  1.00 57.14  ? 117 LEU O C   1 
ATOM   8625  O  O   . LEU H  1 117 ? 12.733  14.810  84.918  1.00 56.93  ? 117 LEU O O   1 
ATOM   8626  C  CB  . LEU H  1 117 ? 10.551  12.617  85.139  1.00 55.30  ? 117 LEU O CB  1 
ATOM   8627  C  CG  . LEU H  1 117 ? 10.594  12.112  86.584  1.00 56.91  ? 117 LEU O CG  1 
ATOM   8628  C  CD1 . LEU H  1 117 ? 9.288   12.407  87.306  1.00 57.65  ? 117 LEU O CD1 1 
ATOM   8629  C  CD2 . LEU H  1 117 ? 10.900  10.622  86.606  1.00 56.65  ? 117 LEU O CD2 1 
ATOM   8630  N  N   . VAL H  1 118 ? 11.453  15.464  86.656  1.00 58.91  ? 118 VAL O N   1 
ATOM   8631  C  CA  . VAL H  1 118 ? 12.493  16.265  87.300  1.00 60.74  ? 118 VAL O CA  1 
ATOM   8632  C  C   . VAL H  1 118 ? 12.646  15.854  88.765  1.00 62.69  ? 118 VAL O C   1 
ATOM   8633  O  O   . VAL H  1 118 ? 11.661  15.528  89.434  1.00 63.08  ? 118 VAL O O   1 
ATOM   8634  C  CB  . VAL H  1 118 ? 12.183  17.781  87.192  1.00 61.55  ? 118 VAL O CB  1 
ATOM   8635  C  CG1 . VAL H  1 118 ? 13.238  18.621  87.905  1.00 63.75  ? 118 VAL O CG1 1 
ATOM   8636  C  CG2 . VAL H  1 118 ? 12.096  18.199  85.731  1.00 60.03  ? 118 VAL O CG2 1 
ATOM   8637  N  N   . VAL H  1 119 ? 13.892  15.863  89.241  1.00 64.15  ? 119 VAL O N   1 
ATOM   8638  C  CA  . VAL H  1 119 ? 14.204  15.690  90.662  1.00 66.57  ? 119 VAL O CA  1 
ATOM   8639  C  C   . VAL H  1 119 ? 14.914  16.960  91.144  1.00 68.73  ? 119 VAL O C   1 
ATOM   8640  O  O   . VAL H  1 119 ? 15.766  17.512  90.442  1.00 68.55  ? 119 VAL O O   1 
ATOM   8641  C  CB  . VAL H  1 119 ? 15.014  14.393  90.947  1.00 66.94  ? 119 VAL O CB  1 
ATOM   8642  C  CG1 . VAL H  1 119 ? 16.351  14.370  90.215  1.00 66.75  ? 119 VAL O CG1 1 
ATOM   8643  C  CG2 . VAL H  1 119 ? 15.220  14.201  92.446  1.00 69.73  ? 119 VAL O CG2 1 
ATOM   8644  N  N   . HIS H  1 120 ? 14.551  17.410  92.344  1.00 70.99  ? 120 HIS O N   1 
ATOM   8645  C  CA  . HIS H  1 120 ? 14.867  18.762  92.820  1.00 73.19  ? 120 HIS O CA  1 
ATOM   8646  C  C   . HIS H  1 120 ? 15.918  18.798  93.937  1.00 76.23  ? 120 HIS O C   1 
ATOM   8647  O  O   . HIS H  1 120 ? 16.324  17.760  94.467  1.00 76.85  ? 120 HIS O O   1 
ATOM   8648  C  CB  . HIS H  1 120 ? 13.572  19.452  93.272  1.00 73.80  ? 120 HIS O CB  1 
ATOM   8649  C  CG  . HIS H  1 120 ? 12.767  20.022  92.147  1.00 71.81  ? 120 HIS O CG  1 
ATOM   8650  N  ND1 . HIS H  1 120 ? 12.895  21.330  91.730  1.00 72.49  ? 120 HIS O ND1 1 
ATOM   8651  C  CD2 . HIS H  1 120 ? 11.827  19.463  91.346  1.00 69.44  ? 120 HIS O CD2 1 
ATOM   8652  C  CE1 . HIS H  1 120 ? 12.068  21.552  90.723  1.00 70.60  ? 120 HIS O CE1 1 
ATOM   8653  N  NE2 . HIS H  1 120 ? 11.409  20.436  90.471  1.00 68.73  ? 120 HIS O NE2 1 
ATOM   8654  N  N   . GLU H  1 121 ? 16.348  20.015  94.269  1.00 78.35  ? 121 GLU O N   1 
ATOM   8655  C  CA  . GLU H  1 121 ? 17.379  20.269  95.277  1.00 81.64  ? 121 GLU O CA  1 
ATOM   8656  C  C   . GLU H  1 121 ? 16.863  20.067  96.700  1.00 84.11  ? 121 GLU O C   1 
ATOM   8657  O  O   . GLU H  1 121 ? 17.507  19.389  97.508  1.00 86.01  ? 121 GLU O O   1 
ATOM   8658  C  CB  . GLU H  1 121 ? 17.899  21.707  95.128  1.00 83.29  ? 121 GLU O CB  1 
ATOM   8659  C  CG  . GLU H  1 121 ? 19.119  22.057  95.977  1.00 86.83  ? 121 GLU O CG  1 
ATOM   8660  C  CD  . GLU H  1 121 ? 19.376  23.554  96.064  1.00 89.04  ? 121 GLU O CD  1 
ATOM   8661  O  OE1 . GLU H  1 121 ? 18.937  24.309  95.166  1.00 87.55  ? 121 GLU O OE1 1 
ATOM   8662  O  OE2 . GLU H  1 121 ? 20.028  23.979  97.039  1.00 92.57  ? 121 GLU O OE2 1 
ATOM   8663  N  N   . LYS H  1 122 ? 15.725  20.693  97.004  1.00 84.38  ? 122 LYS O N   1 
ATOM   8664  C  CA  . LYS H  1 122 ? 15.114  20.648  98.340  1.00 86.99  ? 122 LYS O CA  1 
ATOM   8665  C  C   . LYS H  1 122 ? 13.787  19.883  98.297  1.00 85.20  ? 122 LYS O C   1 
ATOM   8666  O  O   . LYS H  1 122 ? 13.392  19.362  97.248  1.00 81.97  ? 122 LYS O O   1 
ATOM   8667  C  CB  . LYS H  1 122 ? 14.900  22.069  98.874  1.00 89.56  ? 122 LYS O CB  1 
ATOM   8668  N  N   . ALA H  1 123 ? 13.117  19.813  99.447  1.00 87.53  ? 123 ALA O N   1 
ATOM   8669  C  CA  . ALA H  1 123 ? 11.840  19.108  99.571  1.00 86.53  ? 123 ALA O CA  1 
ATOM   8670  C  C   . ALA H  1 123 ? 10.682  19.923  98.996  1.00 85.29  ? 123 ALA O C   1 
ATOM   8671  O  O   . ALA H  1 123 ? 10.687  21.153  99.051  1.00 86.58  ? 123 ALA O O   1 
ATOM   8672  C  CB  . ALA H  1 123 ? 11.566  18.775  101.031 1.00 89.94  ? 123 ALA O CB  1 
ATOM   8673  N  N   . ASP H  1 124 ? 9.698   19.220  98.440  1.00 83.00  ? 124 ASP O N   1 
ATOM   8674  C  CA  . ASP H  1 124 ? 8.430   19.820  98.031  1.00 82.25  ? 124 ASP O CA  1 
ATOM   8675  C  C   . ASP H  1 124 ? 7.560   19.957  99.280  1.00 85.25  ? 124 ASP O C   1 
ATOM   8676  O  O   . ASP H  1 124 ? 7.241   18.955  99.920  1.00 85.98  ? 124 ASP O O   1 
ATOM   8677  C  CB  . ASP H  1 124 ? 7.740   18.926  96.988  1.00 79.00  ? 124 ASP O CB  1 
ATOM   8678  C  CG  . ASP H  1 124 ? 6.513   19.575  96.348  1.00 78.11  ? 124 ASP O CG  1 
ATOM   8679  O  OD1 . ASP H  1 124 ? 6.015   20.608  96.849  1.00 80.22  ? 124 ASP O OD1 1 
ATOM   8680  O  OD2 . ASP H  1 124 ? 6.036   19.028  95.333  1.00 75.51  ? 124 ASP O OD2 1 
ATOM   8681  N  N   . ASP H  1 125 ? 7.172   21.190  99.611  1.00 87.17  ? 125 ASP O N   1 
ATOM   8682  C  CA  . ASP H  1 125 ? 6.307   21.454  100.781 1.00 90.38  ? 125 ASP O CA  1 
ATOM   8683  C  C   . ASP H  1 125 ? 4.805   21.182  100.552 1.00 89.59  ? 125 ASP O C   1 
ATOM   8684  O  O   . ASP H  1 125 ? 3.992   21.402  101.455 1.00 92.30  ? 125 ASP O O   1 
ATOM   8685  C  CB  . ASP H  1 125 ? 6.535   22.878  101.343 1.00 93.40  ? 125 ASP O CB  1 
ATOM   8686  C  CG  . ASP H  1 125 ? 6.179   23.997  100.355 1.00 92.18  ? 125 ASP O CG  1 
ATOM   8687  O  OD1 . ASP H  1 125 ? 5.391   23.781  99.409  1.00 89.60  ? 125 ASP O OD1 1 
ATOM   8688  O  OD2 . ASP H  1 125 ? 6.702   25.118  100.542 1.00 94.11  ? 125 ASP O OD2 1 
ATOM   8689  N  N   . LEU H  1 126 ? 4.451   20.727  99.346  1.00 86.12  ? 126 LEU O N   1 
ATOM   8690  C  CA  . LEU H  1 126 ? 3.102   20.253  99.008  1.00 85.16  ? 126 LEU O CA  1 
ATOM   8691  C  C   . LEU H  1 126 ? 2.050   21.371  99.029  1.00 86.66  ? 126 LEU O C   1 
ATOM   8692  O  O   . LEU H  1 126 ? 0.881   21.129  99.343  0.75 87.72  ? 126 LEU O O   1 
ATOM   8693  C  CB  . LEU H  1 126 ? 2.688   19.067  99.902  1.00 86.46  ? 126 LEU O CB  1 
ATOM   8694  C  CG  . LEU H  1 126 ? 3.712   17.932  100.080 1.00 85.72  ? 126 LEU O CG  1 
ATOM   8695  C  CD1 . LEU H  1 126 ? 3.282   16.993  101.196 1.00 88.08  ? 126 LEU O CD1 1 
ATOM   8696  C  CD2 . LEU H  1 126 ? 3.935   17.152  98.788  1.00 81.92  ? 126 LEU O CD2 1 
ATOM   8697  N  N   . GLY H  1 127 ? 2.473   22.582  98.660  0.75 86.89  ? 127 GLY O N   1 
ATOM   8698  C  CA  . GLY H  1 127 ? 1.599   23.752  98.623  0.75 88.55  ? 127 GLY O CA  1 
ATOM   8699  C  C   . GLY H  1 127 ? 1.041   24.182  99.968  0.75 92.58  ? 127 GLY O C   1 
ATOM   8700  O  O   . GLY H  1 127 ? -0.074  24.700  100.031 0.75 94.03  ? 127 GLY O O   1 
ATOM   8701  N  N   . LYS H  1 128 ? 1.809   23.970  101.038 1.00 94.64  ? 128 LYS O N   1 
ATOM   8702  C  CA  . LYS H  1 128 ? 1.389   24.324  102.407 1.00 98.89  ? 128 LYS O CA  1 
ATOM   8703  C  C   . LYS H  1 128 ? 2.276   25.388  103.079 1.00 101.74 ? 128 LYS O C   1 
ATOM   8704  O  O   . LYS H  1 128 ? 2.147   25.630  104.282 1.00 105.54 ? 128 LYS O O   1 
ATOM   8705  C  CB  . LYS H  1 128 ? 1.310   23.057  103.268 0.75 99.76  ? 128 LYS O CB  1 
ATOM   8706  C  CG  . LYS H  1 128 ? 0.219   22.095  102.819 0.75 98.01  ? 128 LYS O CG  1 
ATOM   8707  C  CD  . LYS H  1 128 ? -0.050  21.008  103.849 0.75 99.95  ? 128 LYS O CD  1 
ATOM   8708  C  CE  . LYS H  1 128 ? -1.341  20.264  103.546 0.75 99.20  ? 128 LYS O CE  1 
ATOM   8709  N  NZ  . LYS H  1 128 ? -1.303  19.578  102.225 0.75 94.91  ? 128 LYS O NZ  1 
ATOM   8710  N  N   . GLY H  1 129 ? 3.152   26.035  102.307 1.00 100.21 ? 129 GLY O N   1 
ATOM   8711  C  CA  . GLY H  1 129 ? 3.961   27.154  102.803 1.00 102.97 ? 129 GLY O CA  1 
ATOM   8712  C  C   . GLY H  1 129 ? 3.180   28.455  102.806 1.00 105.20 ? 129 GLY O C   1 
ATOM   8713  O  O   . GLY H  1 129 ? 2.051   28.510  102.314 1.00 104.37 ? 129 GLY O O   1 
ATOM   8714  N  N   . GLY H  1 130 ? 3.789   29.506  103.349 0.50 108.28 ? 130 GLY O N   1 
ATOM   8715  C  CA  . GLY H  1 130 ? 3.146   30.818  103.467 0.50 111.08 ? 130 GLY O CA  1 
ATOM   8716  C  C   . GLY H  1 130 ? 3.654   31.815  102.445 0.50 109.99 ? 130 GLY O C   1 
ATOM   8717  O  O   . GLY H  1 130 ? 4.131   32.890  102.815 0.50 112.95 ? 130 GLY O O   1 
ATOM   8718  N  N   . ASN H  1 131 ? 3.546   31.464  101.163 0.50 106.00 ? 131 ASN O N   1 
ATOM   8719  C  CA  . ASN H  1 131 ? 4.040   32.322  100.077 0.75 104.80 ? 131 ASN O CA  1 
ATOM   8720  C  C   . ASN H  1 131 ? 3.472   31.973  98.694  0.75 101.00 ? 131 ASN O C   1 
ATOM   8721  O  O   . ASN H  1 131 ? 2.930   30.886  98.480  0.75 98.63  ? 131 ASN O O   1 
ATOM   8722  C  CB  . ASN H  1 131 ? 5.577   32.300  100.035 0.75 104.38 ? 131 ASN O CB  1 
ATOM   8723  C  CG  . ASN H  1 131 ? 6.148   30.892  99.972  0.75 101.52 ? 131 ASN O CG  1 
ATOM   8724  O  OD1 . ASN H  1 131 ? 6.076   30.224  98.940  0.75 97.82  ? 131 ASN O OD1 1 
ATOM   8725  N  ND2 . ASN H  1 131 ? 6.735   30.441  101.078 0.75 103.48 ? 131 ASN O ND2 1 
ATOM   8726  N  N   . GLU H  1 132 ? 3.618   32.924  97.771  0.75 100.76 ? 132 GLU O N   1 
ATOM   8727  C  CA  . GLU H  1 132 ? 3.193   32.787  96.372  0.75 97.63  ? 132 GLU O CA  1 
ATOM   8728  C  C   . GLU H  1 132 ? 3.923   31.654  95.641  0.75 93.69  ? 132 GLU O C   1 
ATOM   8729  O  O   . GLU H  1 132 ? 3.334   30.973  94.798  0.75 90.92  ? 132 GLU O O   1 
ATOM   8730  C  CB  . GLU H  1 132 ? 3.431   34.119  95.636  0.75 98.81  ? 132 GLU O CB  1 
ATOM   8731  C  CG  . GLU H  1 132 ? 3.013   34.172  94.167  0.75 96.25  ? 132 GLU O CG  1 
ATOM   8732  C  CD  . GLU H  1 132 ? 1.516   34.029  93.958  0.75 96.24  ? 132 GLU O CD  1 
ATOM   8733  O  OE1 . GLU H  1 132 ? 0.741   34.701  94.671  0.75 99.43  ? 132 GLU O OE1 1 
ATOM   8734  O  OE2 . GLU H  1 132 ? 1.117   33.252  93.067  0.75 93.22  ? 132 GLU O OE2 1 
ATOM   8735  N  N   . GLU H  1 133 ? 5.203   31.466  95.964  0.75 93.72  ? 133 GLU O N   1 
ATOM   8736  C  CA  . GLU H  1 133 ? 6.046   30.466  95.302  0.75 90.40  ? 133 GLU O CA  1 
ATOM   8737  C  C   . GLU H  1 133 ? 5.656   29.022  95.649  0.75 88.61  ? 133 GLU O C   1 
ATOM   8738  O  O   . GLU H  1 133 ? 5.835   28.125  94.821  0.75 85.43  ? 133 GLU O O   1 
ATOM   8739  C  CB  . GLU H  1 133 ? 7.524   30.724  95.635  0.75 91.52  ? 133 GLU O CB  1 
ATOM   8740  C  CG  . GLU H  1 133 ? 8.536   29.956  94.791  0.75 88.53  ? 133 GLU O CG  1 
ATOM   8741  C  CD  . GLU H  1 133 ? 8.452   30.266  93.303  0.75 86.26  ? 133 GLU O CD  1 
ATOM   8742  O  OE1 . GLU H  1 133 ? 8.094   31.405  92.937  0.75 87.70  ? 133 GLU O OE1 1 
ATOM   8743  O  OE2 . GLU H  1 133 ? 8.752   29.367  92.492  0.75 83.24  ? 133 GLU O OE2 1 
ATOM   8744  N  N   . SER H  1 134 ? 5.122   28.803  96.854  0.75 90.86  ? 134 SER O N   1 
ATOM   8745  C  CA  . SER H  1 134 ? 4.642   27.476  97.270  0.75 89.72  ? 134 SER O CA  1 
ATOM   8746  C  C   . SER H  1 134 ? 3.418   27.010  96.472  0.75 87.60  ? 134 SER O C   1 
ATOM   8747  O  O   . SER H  1 134 ? 3.267   25.814  96.216  0.75 85.34  ? 134 SER O O   1 
ATOM   8748  C  CB  . SER H  1 134 ? 4.315   27.452  98.766  0.75 93.17  ? 134 SER O CB  1 
ATOM   8749  O  OG  . SER H  1 134 ? 3.997   26.136  99.193  0.75 92.29  ? 134 SER O OG  1 
ATOM   8750  N  N   . THR H  1 135 ? 2.560   27.952  96.080  0.75 88.57  ? 135 THR O N   1 
ATOM   8751  C  CA  . THR H  1 135 ? 1.393   27.645  95.244  0.75 86.92  ? 135 THR O CA  1 
ATOM   8752  C  C   . THR H  1 135 ? 1.737   27.374  93.768  0.75 83.51  ? 135 THR O C   1 
ATOM   8753  O  O   . THR H  1 135 ? 0.889   26.867  93.030  0.75 81.83  ? 135 THR O O   1 
ATOM   8754  C  CB  . THR H  1 135 ? 0.341   28.772  95.294  0.75 89.47  ? 135 THR O CB  1 
ATOM   8755  O  OG1 . THR H  1 135 ? 0.905   29.987  94.786  0.75 90.26  ? 135 THR O OG1 1 
ATOM   8756  C  CG2 . THR H  1 135 ? -0.152  28.990  96.718  0.75 93.06  ? 135 THR O CG2 1 
ATOM   8757  N  N   . LYS H  1 136 ? 2.956   27.716  93.340  0.75 82.75  ? 136 LYS O N   1 
ATOM   8758  C  CA  . LYS H  1 136 ? 3.422   27.462  91.972  0.75 79.79  ? 136 LYS O CA  1 
ATOM   8759  C  C   . LYS H  1 136 ? 4.382   26.274  91.872  0.75 77.50  ? 136 LYS O C   1 
ATOM   8760  O  O   . LYS H  1 136 ? 4.162   25.368  91.068  0.75 74.92  ? 136 LYS O O   1 
ATOM   8761  C  CB  . LYS H  1 136 ? 4.095   28.715  91.409  0.75 80.71  ? 136 LYS O CB  1 
ATOM   8762  C  CG  . LYS H  1 136 ? 3.152   29.904  91.281  0.75 82.92  ? 136 LYS O CG  1 
ATOM   8763  C  CD  . LYS H  1 136 ? 3.549   30.828  90.138  0.75 82.73  ? 136 LYS O CD  1 
ATOM   8764  C  CE  . LYS H  1 136 ? 2.433   31.794  89.772  0.75 84.53  ? 136 LYS O CE  1 
ATOM   8765  N  NZ  . LYS H  1 136 ? 2.596   32.294  88.378  0.75 83.58  ? 136 LYS O NZ  1 
ATOM   8766  N  N   . THR H  1 137 ? 5.450   26.299  92.668  1.00 78.70  ? 137 THR O N   1 
ATOM   8767  C  CA  . THR H  1 137 ? 6.509   25.270  92.623  1.00 77.04  ? 137 THR O CA  1 
ATOM   8768  C  C   . THR H  1 137 ? 6.643   24.396  93.878  1.00 78.15  ? 137 THR O C   1 
ATOM   8769  O  O   . THR H  1 137 ? 7.231   23.313  93.808  1.00 76.65  ? 137 THR O O   1 
ATOM   8770  C  CB  . THR H  1 137 ? 7.887   25.916  92.376  1.00 77.55  ? 137 THR O CB  1 
ATOM   8771  O  OG1 . THR H  1 137 ? 8.138   26.906  93.382  1.00 80.85  ? 137 THR O OG1 1 
ATOM   8772  C  CG2 . THR H  1 137 ? 7.940   26.559  90.999  1.00 76.20  ? 137 THR O CG2 1 
ATOM   8773  N  N   . GLY H  1 138 ? 6.126   24.863  95.014  1.00 81.02  ? 138 GLY O N   1 
ATOM   8774  C  CA  . GLY H  1 138 ? 6.281   24.164  96.291  1.00 82.74  ? 138 GLY O CA  1 
ATOM   8775  C  C   . GLY H  1 138 ? 7.645   24.325  96.946  1.00 84.38  ? 138 GLY O C   1 
ATOM   8776  O  O   . GLY H  1 138 ? 8.014   23.520  97.805  1.00 85.36  ? 138 GLY O O   1 
ATOM   8777  N  N   . ASN H  1 139 ? 8.389   25.361  96.544  1.00 84.96  ? 139 ASN O N   1 
ATOM   8778  C  CA  . ASN H  1 139 ? 9.701   25.700  97.121  1.00 86.95  ? 139 ASN O CA  1 
ATOM   8779  C  C   . ASN H  1 139 ? 10.691  24.525  97.180  1.00 85.80  ? 139 ASN O C   1 
ATOM   8780  O  O   . ASN H  1 139 ? 11.390  24.341  98.179  1.00 88.15  ? 139 ASN O O   1 
ATOM   8781  C  CB  . ASN H  1 139 ? 9.517   26.333  98.512  1.00 91.02  ? 139 ASN O CB  1 
ATOM   8782  C  CG  . ASN H  1 139 ? 8.711   27.619  98.469  1.00 92.67  ? 139 ASN O CG  1 
ATOM   8783  O  OD1 . ASN H  1 139 ? 8.908   28.458  97.591  1.00 92.02  ? 139 ASN O OD1 1 
ATOM   8784  N  ND2 . ASN H  1 139 ? 7.805   27.785  99.426  1.00 95.10  ? 139 ASN O ND2 1 
ATOM   8785  N  N   . ALA H  1 140 ? 10.754  23.744  96.101  1.00 82.42  ? 140 ALA O N   1 
ATOM   8786  C  CA  . ALA H  1 140 ? 11.677  22.605  96.022  1.00 81.25  ? 140 ALA O CA  1 
ATOM   8787  C  C   . ALA H  1 140 ? 13.065  22.973  95.479  1.00 81.21  ? 140 ALA O C   1 
ATOM   8788  O  O   . ALA H  1 140 ? 13.919  22.096  95.343  1.00 80.44  ? 140 ALA O O   1 
ATOM   8789  C  CB  . ALA H  1 140 ? 11.063  21.486  95.200  1.00 78.01  ? 140 ALA O CB  1 
ATOM   8790  N  N   . GLY H  1 141 ? 13.297  24.253  95.178  1.00 82.27  ? 141 GLY O N   1 
ATOM   8791  C  CA  . GLY H  1 141 ? 14.614  24.725  94.754  1.00 82.86  ? 141 GLY O CA  1 
ATOM   8792  C  C   . GLY H  1 141 ? 14.927  24.403  93.304  1.00 79.79  ? 141 GLY O C   1 
ATOM   8793  O  O   . GLY H  1 141 ? 14.020  24.189  92.496  1.00 77.37  ? 141 GLY O O   1 
ATOM   8794  N  N   . SER H  1 142 ? 16.220  24.362  92.984  1.00 80.13  ? 142 SER O N   1 
ATOM   8795  C  CA  . SER H  1 142 ? 16.688  24.150  91.611  1.00 77.76  ? 142 SER O CA  1 
ATOM   8796  C  C   . SER H  1 142 ? 16.500  22.703  91.141  1.00 74.98  ? 142 SER O C   1 
ATOM   8797  O  O   . SER H  1 142 ? 16.272  21.795  91.948  1.00 75.18  ? 142 SER O O   1 
ATOM   8798  C  CB  . SER H  1 142 ? 18.159  24.566  91.478  1.00 79.46  ? 142 SER O CB  1 
ATOM   8799  O  OG  . SER H  1 142 ? 18.951  23.983  92.498  1.00 81.39  ? 142 SER O OG  1 
ATOM   8800  N  N   . ARG H  1 143 ? 16.608  22.509  89.829  1.00 72.65  ? 143 ARG O N   1 
ATOM   8801  C  CA  . ARG H  1 143 ? 16.354  21.217  89.194  1.00 70.00  ? 143 ARG O CA  1 
ATOM   8802  C  C   . ARG H  1 143 ? 17.652  20.419  89.073  1.00 70.14  ? 143 ARG O C   1 
ATOM   8803  O  O   . ARG H  1 143 ? 18.499  20.724  88.233  1.00 70.06  ? 143 ARG O O   1 
ATOM   8804  C  CB  . ARG H  1 143 ? 15.707  21.436  87.823  1.00 67.73  ? 143 ARG O CB  1 
ATOM   8805  C  CG  . ARG H  1 143 ? 14.408  22.227  87.909  1.00 67.83  ? 143 ARG O CG  1 
ATOM   8806  C  CD  . ARG H  1 143 ? 13.836  22.591  86.550  1.00 66.13  ? 143 ARG O CD  1 
ATOM   8807  N  NE  . ARG H  1 143 ? 12.796  23.614  86.675  1.00 67.00  ? 143 ARG O NE  1 
ATOM   8808  C  CZ  . ARG H  1 143 ? 12.037  24.067  85.676  1.00 66.07  ? 143 ARG O CZ  1 
ATOM   8809  N  NH1 . ARG H  1 143 ? 12.162  23.589  84.435  1.00 64.17  ? 143 ARG O NH1 1 
ATOM   8810  N  NH2 . ARG H  1 143 ? 11.126  25.005  85.929  1.00 67.31  ? 143 ARG O NH2 1 
ATOM   8811  N  N   . LEU H  1 144 ? 17.795  19.400  89.923  1.00 70.63  ? 144 LEU O N   1 
ATOM   8812  C  CA  . LEU H  1 144 ? 19.041  18.628  90.041  1.00 71.42  ? 144 LEU O CA  1 
ATOM   8813  C  C   . LEU H  1 144 ? 19.302  17.729  88.830  1.00 69.03  ? 144 LEU O C   1 
ATOM   8814  O  O   . LEU H  1 144 ? 20.422  17.676  88.320  1.00 69.51  ? 144 LEU O O   1 
ATOM   8815  C  CB  . LEU H  1 144 ? 19.027  17.781  91.321  1.00 72.92  ? 144 LEU O CB  1 
ATOM   8816  N  N   . ALA H  1 145 ? 18.270  17.016  88.388  1.00 66.70  ? 145 ALA O N   1 
ATOM   8817  C  CA  . ALA H  1 145 ? 18.371  16.154  87.210  1.00 64.50  ? 145 ALA O CA  1 
ATOM   8818  C  C   . ALA H  1 145 ? 17.023  16.020  86.510  1.00 62.17  ? 145 ALA O C   1 
ATOM   8819  O  O   . ALA H  1 145 ? 15.966  16.131  87.139  1.00 62.18  ? 145 ALA O O   1 
ATOM   8820  C  CB  . ALA H  1 145 ? 18.915  14.787  87.592  1.00 64.82  ? 145 ALA O CB  1 
ATOM   8821  N  N   . ALA H  1 146 ? 17.078  15.790  85.201  1.00 60.41  ? 146 ALA O N   1 
ATOM   8822  C  CA  . ALA H  1 146 ? 15.883  15.721  84.370  1.00 58.41  ? 146 ALA O CA  1 
ATOM   8823  C  C   . ALA H  1 146 ? 16.074  14.767  83.199  1.00 56.74  ? 146 ALA O C   1 
ATOM   8824  O  O   . ALA H  1 146 ? 17.200  14.445  82.814  1.00 57.14  ? 146 ALA O O   1 
ATOM   8825  C  CB  . ALA H  1 146 ? 15.517  17.109  83.865  1.00 58.56  ? 146 ALA O CB  1 
ATOM   8826  N  N   . GLY H  1 147 ? 14.956  14.307  82.655  1.00 55.12  ? 147 GLY O N   1 
ATOM   8827  C  CA  . GLY H  1 147 ? 14.957  13.461  81.472  1.00 53.64  ? 147 GLY O CA  1 
ATOM   8828  C  C   . GLY H  1 147 ? 13.581  13.376  80.853  1.00 52.24  ? 147 GLY O C   1 
ATOM   8829  O  O   . GLY H  1 147 ? 12.575  13.505  81.549  1.00 52.34  ? 147 GLY O O   1 
ATOM   8830  N  N   . VAL H  1 148 ? 13.546  13.142  79.546  1.00 51.18  ? 148 VAL O N   1 
ATOM   8831  C  CA  . VAL H  1 148 ? 12.291  13.045  78.806  1.00 50.10  ? 148 VAL O CA  1 
ATOM   8832  C  C   . VAL H  1 148 ? 11.697  11.646  79.017  1.00 49.41  ? 148 VAL O C   1 
ATOM   8833  O  O   . VAL H  1 148 ? 12.414  10.644  78.982  1.00 49.40  ? 148 VAL O O   1 
ATOM   8834  C  CB  . VAL H  1 148 ? 12.496  13.332  77.301  1.00 49.63  ? 148 VAL O CB  1 
ATOM   8835  C  CG1 . VAL H  1 148 ? 11.167  13.256  76.552  1.00 48.86  ? 148 VAL O CG1 1 
ATOM   8836  C  CG2 . VAL H  1 148 ? 13.158  14.699  77.104  1.00 50.57  ? 148 VAL O CG2 1 
ATOM   8837  N  N   . ILE H  1 149 ? 10.388  11.590  79.247  1.00 49.10  ? 149 ILE O N   1 
ATOM   8838  C  CA  . ILE H  1 149 ? 9.691   10.322  79.456  1.00 48.70  ? 149 ILE O CA  1 
ATOM   8839  C  C   . ILE H  1 149 ? 9.379   9.728   78.082  1.00 47.76  ? 149 ILE O C   1 
ATOM   8840  O  O   . ILE H  1 149 ? 8.727   10.377  77.259  1.00 47.45  ? 149 ILE O O   1 
ATOM   8841  C  CB  . ILE H  1 149 ? 8.403   10.505  80.288  1.00 49.13  ? 149 ILE O CB  1 
ATOM   8842  C  CG1 . ILE H  1 149 ? 8.741   11.133  81.651  1.00 50.35  ? 149 ILE O CG1 1 
ATOM   8843  C  CG2 . ILE H  1 149 ? 7.694   9.164   80.476  1.00 49.01  ? 149 ILE O CG2 1 
ATOM   8844  C  CD1 . ILE H  1 149 ? 7.553   11.651  82.436  1.00 51.11  ? 149 ILE O CD1 1 
ATOM   8845  N  N   . GLY H  1 150 ? 9.863   8.509   77.841  1.00 47.53  ? 150 GLY O N   1 
ATOM   8846  C  CA  . GLY H  1 150 ? 9.708   7.821   76.556  1.00 46.92  ? 150 GLY O CA  1 
ATOM   8847  C  C   . GLY H  1 150 ? 9.013   6.477   76.677  1.00 46.88  ? 150 GLY O C   1 
ATOM   8848  O  O   . GLY H  1 150 ? 8.958   5.895   77.757  1.00 47.32  ? 150 GLY O O   1 
ATOM   8849  N  N   . ILE H  1 151 ? 8.486   5.998   75.547  1.00 46.54  ? 151 ILE O N   1 
ATOM   8850  C  CA  . ILE H  1 151 ? 7.755   4.727   75.452  1.00 46.71  ? 151 ILE O CA  1 
ATOM   8851  C  C   . ILE H  1 151 ? 8.763   3.588   75.590  1.00 47.09  ? 151 ILE O C   1 
ATOM   8852  O  O   . ILE H  1 151 ? 9.853   3.668   75.033  1.00 47.08  ? 151 ILE O O   1 
ATOM   8853  C  CB  . ILE H  1 151 ? 7.004   4.597   74.091  1.00 46.57  ? 151 ILE O CB  1 
ATOM   8854  C  CG1 . ILE H  1 151 ? 5.952   5.707   73.931  1.00 46.52  ? 151 ILE O CG1 1 
ATOM   8855  C  CG2 . ILE H  1 151 ? 6.335   3.227   73.951  1.00 47.03  ? 151 ILE O CG2 1 
ATOM   8856  C  CD1 . ILE H  1 151 ? 5.464   5.916   72.507  1.00 46.62  ? 151 ILE O CD1 1 
ATOM   8857  N  N   . ALA H  1 152 ? 8.392   2.536   76.321  1.00 47.68  ? 152 ALA O N   1 
ATOM   8858  C  CA  . ALA H  1 152 ? 9.274   1.395   76.585  1.00 48.41  ? 152 ALA O CA  1 
ATOM   8859  C  C   . ALA H  1 152 ? 8.633   0.089   76.141  1.00 48.95  ? 152 ALA O C   1 
ATOM   8860  O  O   . ALA H  1 152 ? 7.415   0.007   76.005  1.00 48.91  ? 152 ALA O O   1 
ATOM   8861  C  CB  . ALA H  1 152 ? 9.606   1.333   78.065  1.00 49.18  ? 152 ALA O CB  1 
ATOM   8862  N  N   . GLN H  1 153 ? 9.463   -0.929  75.921  1.00 49.70  ? 153 GLN O N   1 
ATOM   8863  C  CA  . GLN H  1 153 ? 8.989   -2.261  75.516  1.00 50.59  ? 153 GLN O CA  1 
ATOM   8864  C  C   . GLN H  1 153 ? 8.397   -3.014  76.700  1.00 51.65  ? 153 GLN O C   1 
ATOM   8865  O  O   . GLN H  1 153 ? 8.937   -2.979  77.807  1.00 52.19  ? 153 GLN O O   1 
ATOM   8866  C  CB  . GLN H  1 153 ? 10.135  -3.090  74.929  1.00 51.35  ? 153 GLN O CB  1 
ATOM   8867  C  CG  . GLN H  1 153 ? 9.690   -4.385  74.257  1.00 52.37  ? 153 GLN O CG  1 
ATOM   8868  C  CD  . GLN H  1 153 ? 10.858  -5.213  73.754  1.00 53.42  ? 153 GLN O CD  1 
ATOM   8869  O  OE1 . GLN H  1 153 ? 11.853  -5.388  74.456  1.00 54.09  ? 153 GLN O OE1 1 
ATOM   8870  N  NE2 . GLN H  1 153 ? 10.740  -5.733  72.537  1.00 53.84  ? 153 GLN O NE2 1 
ATOM   8871  O  OXT . GLN H  1 153 ? 7.380   -3.692  76.563  1.00 52.25  ? 153 GLN O OXT 1 
ATOM   8872  N  N   . ALA I  1 1   ? -8.606  -12.795 64.288  1.00 70.60  ? 1   ALA Q N   1 
ATOM   8873  C  CA  . ALA I  1 1   ? -9.304  -11.831 63.394  1.00 66.51  ? 1   ALA Q CA  1 
ATOM   8874  C  C   . ALA I  1 1   ? -10.412 -11.080 64.134  1.00 65.71  ? 1   ALA Q C   1 
ATOM   8875  O  O   . ALA I  1 1   ? -11.290 -11.704 64.743  1.00 67.73  ? 1   ALA Q O   1 
ATOM   8876  C  CB  . ALA I  1 1   ? -9.887  -12.554 62.184  1.00 65.67  ? 1   ALA Q CB  1 
ATOM   8877  N  N   . THR I  1 2   ? -10.371 -9.749  64.071  1.00 62.98  ? 2   THR Q N   1 
ATOM   8878  C  CA  . THR I  1 2   ? -11.412 -8.923  64.665  1.00 62.09  ? 2   THR Q CA  1 
ATOM   8879  C  C   . THR I  1 2   ? -12.595 -8.952  63.707  1.00 59.67  ? 2   THR Q C   1 
ATOM   8880  O  O   . THR I  1 2   ? -12.407 -8.928  62.488  1.00 57.34  ? 2   THR Q O   1 
ATOM   8881  C  CB  . THR I  1 2   ? -10.955 -7.465  64.878  1.00 60.51  ? 2   THR Q CB  1 
ATOM   8882  O  OG1 . THR I  1 2   ? -9.651  -7.446  65.463  1.00 62.50  ? 2   THR Q OG1 1 
ATOM   8883  C  CG2 . THR I  1 2   ? -11.913 -6.730  65.801  1.00 61.05  ? 2   THR Q CG2 1 
ATOM   8884  N  N   . LYS I  1 3   ? -13.798 -9.044  64.269  1.00 60.35  ? 3   LYS Q N   1 
ATOM   8885  C  CA  . LYS I  1 3   ? -15.030 -9.044  63.491  1.00 58.59  ? 3   LYS Q CA  1 
ATOM   8886  C  C   . LYS I  1 3   ? -15.964 -7.967  64.009  1.00 57.69  ? 3   LYS Q C   1 
ATOM   8887  O  O   . LYS I  1 3   ? -15.956 -7.641  65.196  1.00 59.54  ? 3   LYS Q O   1 
ATOM   8888  C  CB  . LYS I  1 3   ? -15.719 -10.403 63.574  1.00 61.08  ? 3   LYS Q CB  1 
ATOM   8889  C  CG  . LYS I  1 3   ? -14.941 -11.535 62.926  1.00 62.14  ? 3   LYS Q CG  1 
ATOM   8890  C  CD  . LYS I  1 3   ? -15.706 -12.842 63.058  1.00 65.01  ? 3   LYS Q CD  1 
ATOM   8891  C  CE  . LYS I  1 3   ? -14.864 -14.049 62.681  1.00 67.12  ? 3   LYS Q CE  1 
ATOM   8892  N  NZ  . LYS I  1 3   ? -15.449 -15.301 63.236  1.00 70.97  ? 3   LYS Q NZ  1 
ATOM   8893  N  N   . ALA I  1 4   ? -16.761 -7.411  63.107  1.00 55.05  ? 4   ALA Q N   1 
ATOM   8894  C  CA  . ALA I  1 4   ? -17.798 -6.469  63.482  1.00 54.51  ? 4   ALA Q CA  1 
ATOM   8895  C  C   . ALA I  1 4   ? -19.071 -6.792  62.717  1.00 53.78  ? 4   ALA Q C   1 
ATOM   8896  O  O   . ALA I  1 4   ? -19.052 -7.568  61.761  1.00 53.15  ? 4   ALA Q O   1 
ATOM   8897  C  CB  . ALA I  1 4   ? -17.342 -5.043  63.230  1.00 52.09  ? 4   ALA Q CB  1 
ATOM   8898  N  N   . VAL I  1 5   ? -20.182 -6.224  63.171  1.00 54.29  ? 5   VAL Q N   1 
ATOM   8899  C  CA  . VAL I  1 5   ? -21.481 -6.467  62.541  1.00 54.02  ? 5   VAL Q CA  1 
ATOM   8900  C  C   . VAL I  1 5   ? -22.365 -5.237  62.669  1.00 53.21  ? 5   VAL Q C   1 
ATOM   8901  O  O   . VAL I  1 5   ? -22.260 -4.479  63.639  1.00 54.27  ? 5   VAL Q O   1 
ATOM   8902  C  CB  . VAL I  1 5   ? -22.175 -7.722  63.131  1.00 57.34  ? 5   VAL Q CB  1 
ATOM   8903  C  CG1 . VAL I  1 5   ? -22.644 -7.489  64.567  1.00 60.19  ? 5   VAL Q CG1 1 
ATOM   8904  C  CG2 . VAL I  1 5   ? -23.332 -8.177  62.243  1.00 57.08  ? 5   VAL Q CG2 1 
ATOM   8905  N  N   . CYS I  1 6   ? -23.223 -5.046  61.671  1.00 51.65  ? 6   CYS Q N   1 
ATOM   8906  C  CA  . CYS I  1 6   ? -24.152 -3.930  61.625  1.00 50.96  ? 6   CYS Q CA  1 
ATOM   8907  C  C   . CYS I  1 6   ? -25.503 -4.433  61.107  1.00 51.58  ? 6   CYS Q C   1 
ATOM   8908  O  O   . CYS I  1 6   ? -25.564 -5.153  60.103  1.00 50.69  ? 6   CYS Q O   1 
ATOM   8909  C  CB  . CYS I  1 6   ? -23.598 -2.826  60.720  1.00 47.87  ? 6   CYS Q CB  1 
ATOM   8910  S  SG  . CYS I  1 6   ? -24.519 -1.264  60.784  1.00 47.42  ? 6   CYS Q SG  1 
ATOM   8911  N  N   . VAL I  1 7   ? -26.568 -4.091  61.830  1.00 53.45  ? 7   VAL Q N   1 
ATOM   8912  C  CA  . VAL I  1 7   ? -27.937 -4.326  61.365  1.00 54.17  ? 7   VAL Q CA  1 
ATOM   8913  C  C   . VAL I  1 7   ? -28.454 -3.027  60.745  1.00 52.19  ? 7   VAL Q C   1 
ATOM   8914  O  O   . VAL I  1 7   ? -28.509 -1.996  61.404  1.00 52.61  ? 7   VAL Q O   1 
ATOM   8915  C  CB  . VAL I  1 7   ? -28.861 -4.865  62.490  1.00 58.05  ? 7   VAL Q CB  1 
ATOM   8916  C  CG1 . VAL I  1 7   ? -28.227 -6.083  63.147  1.00 60.10  ? 7   VAL Q CG1 1 
ATOM   8917  C  CG2 . VAL I  1 7   ? -29.196 -3.814  63.549  1.00 59.57  ? 7   VAL Q CG2 1 
ATOM   8918  N  N   . LEU I  1 8   ? -28.780 -3.068  59.460  1.00 50.24  ? 8   LEU Q N   1 
ATOM   8919  C  CA  . LEU I  1 8   ? -29.269 -1.891  58.754  1.00 48.53  ? 8   LEU Q CA  1 
ATOM   8920  C  C   . LEU I  1 8   ? -30.791 -1.876  58.859  1.00 50.61  ? 8   LEU Q C   1 
ATOM   8921  O  O   . LEU I  1 8   ? -31.444 -2.840  58.479  1.00 51.67  ? 8   LEU Q O   1 
ATOM   8922  C  CB  . LEU I  1 8   ? -28.827 -1.912  57.288  1.00 45.74  ? 8   LEU Q CB  1 
ATOM   8923  C  CG  . LEU I  1 8   ? -27.312 -1.869  57.049  1.00 43.76  ? 8   LEU Q CG  1 
ATOM   8924  C  CD1 . LEU I  1 8   ? -26.991 -2.075  55.572  1.00 41.71  ? 8   LEU Q CD1 1 
ATOM   8925  C  CD2 . LEU I  1 8   ? -26.716 -0.553  57.534  1.00 42.83  ? 8   LEU Q CD2 1 
ATOM   8926  N  N   . LYS I  1 9   ? -31.327 -0.794  59.422  1.00 51.49  ? 9   LYS Q N   1 
ATOM   8927  C  CA  . LYS I  1 9   ? -32.761 -0.574  59.523  1.00 53.64  ? 9   LYS Q CA  1 
ATOM   8928  C  C   . LYS I  1 9   ? -33.096 0.891   59.266  1.00 52.83  ? 9   LYS Q C   1 
ATOM   8929  O  O   . LYS I  1 9   ? -32.284 1.784   59.532  1.00 51.64  ? 9   LYS Q O   1 
ATOM   8930  C  CB  . LYS I  1 9   ? -33.257 -0.984  60.907  1.00 57.33  ? 9   LYS Q CB  1 
ATOM   8931  C  CG  . LYS I  1 9   ? -33.192 -2.481  61.191  1.00 59.02  ? 9   LYS Q CG  1 
ATOM   8932  C  CD  . LYS I  1 9   ? -34.186 -3.274  60.346  1.00 59.83  ? 9   LYS Q CD  1 
ATOM   8933  C  CE  . LYS I  1 9   ? -34.072 -4.774  60.591  1.00 61.73  ? 9   LYS Q CE  1 
ATOM   8934  N  NZ  . LYS I  1 9   ? -32.859 -5.373  59.962  1.00 59.42  ? 9   LYS Q NZ  1 
ATOM   8935  N  N   . GLY I  1 10  ? -34.291 1.120   58.732  1.00 53.70  ? 10  GLY Q N   1 
ATOM   8936  C  CA  . GLY I  1 10  ? -34.803 2.463   58.466  1.00 53.61  ? 10  GLY Q CA  1 
ATOM   8937  C  C   . GLY I  1 10  ? -36.310 2.519   58.633  1.00 56.56  ? 10  GLY Q C   1 
ATOM   8938  O  O   . GLY I  1 10  ? -36.917 1.590   59.169  1.00 58.93  ? 10  GLY Q O   1 
ATOM   8939  N  N   . ASP I  1 11  ? -36.911 3.614   58.181  1.00 56.68  ? 11  ASP Q N   1 
ATOM   8940  C  CA  . ASP I  1 11  ? -38.369 3.790   58.272  1.00 59.69  ? 11  ASP Q CA  1 
ATOM   8941  C  C   . ASP I  1 11  ? -39.074 3.092   57.110  1.00 59.20  ? 11  ASP Q C   1 
ATOM   8942  O  O   . ASP I  1 11  ? -40.256 2.758   57.212  1.00 62.03  ? 11  ASP Q O   1 
ATOM   8943  C  CB  . ASP I  1 11  ? -38.753 5.274   58.282  1.00 60.54  ? 11  ASP Q CB  1 
ATOM   8944  C  CG  . ASP I  1 11  ? -38.017 6.062   59.352  1.00 61.19  ? 11  ASP Q CG  1 
ATOM   8945  O  OD1 . ASP I  1 11  ? -38.101 5.654   60.554  1.00 63.79  ? 11  ASP Q OD1 1 
ATOM   8946  O  OD2 . ASP I  1 11  ? -37.341 7.082   58.985  1.00 59.49  ? 11  ASP Q OD2 1 
ATOM   8947  N  N   . GLY I  1 12  ? -38.350 2.894   56.007  1.00 55.88  ? 12  GLY Q N   1 
ATOM   8948  C  CA  . GLY I  1 12  ? -38.884 2.262   54.807  1.00 55.40  ? 12  GLY Q CA  1 
ATOM   8949  C  C   . GLY I  1 12  ? -38.538 0.752   54.754  1.00 55.23  ? 12  GLY Q C   1 
ATOM   8950  O  O   . GLY I  1 12  ? -38.082 0.103   55.782  1.00 56.04  ? 12  GLY Q O   1 
ATOM   8951  N  N   . PRO I  1 13  ? -38.614 0.237   53.450  1.00 53.98  ? 13  PRO Q N   1 
ATOM   8952  C  CA  . PRO I  1 13  ? -38.493 -1.200  53.233  1.00 54.54  ? 13  PRO Q CA  1 
ATOM   8953  C  C   . PRO I  1 13  ? -37.061 -1.737  53.252  1.00 52.30  ? 13  PRO Q C   1 
ATOM   8954  O  O   . PRO I  1 13  ? -36.881 -2.957  53.190  1.00 53.16  ? 13  PRO Q O   1 
ATOM   8955  C  CB  . PRO I  1 13  ? -39.105 -1.383  51.843  1.00 54.49  ? 13  PRO Q CB  1 
ATOM   8956  C  CG  . PRO I  1 13  ? -38.769 -0.117  51.131  1.00 52.16  ? 13  PRO Q CG  1 
ATOM   8957  C  CD  . PRO I  1 13  ? -38.723 0.972   52.171  1.00 52.33  ? 13  PRO Q CD  1 
ATOM   8958  N  N   . VAL I  1 14  ? -36.066 -0.853  53.358  1.00 49.77  ? 14  VAL Q N   1 
ATOM   8959  C  CA  . VAL I  1 14  ? -34.662 -1.267  53.323  1.00 47.75  ? 14  VAL Q CA  1 
ATOM   8960  C  C   . VAL I  1 14  ? -34.214 -1.808  54.687  1.00 49.00  ? 14  VAL Q C   1 
ATOM   8961  O  O   . VAL I  1 14  ? -34.254 -1.094  55.695  1.00 49.71  ? 14  VAL Q O   1 
ATOM   8962  C  CB  . VAL I  1 14  ? -33.726 -0.116  52.884  1.00 44.89  ? 14  VAL Q CB  1 
ATOM   8963  C  CG1 . VAL I  1 14  ? -32.279 -0.596  52.777  1.00 43.07  ? 14  VAL Q CG1 1 
ATOM   8964  C  CG2 . VAL I  1 14  ? -34.184 0.446   51.546  1.00 43.95  ? 14  VAL Q CG2 1 
ATOM   8965  N  N   . GLN I  1 15  ? -33.783 -3.069  54.690  1.00 49.53  ? 15  GLN Q N   1 
ATOM   8966  C  CA  . GLN I  1 15  ? -33.196 -3.709  55.863  1.00 50.77  ? 15  GLN Q CA  1 
ATOM   8967  C  C   . GLN I  1 15  ? -32.141 -4.729  55.442  1.00 49.81  ? 15  GLN Q C   1 
ATOM   8968  O  O   . GLN I  1 15  ? -32.204 -5.279  54.339  1.00 49.32  ? 15  GLN Q O   1 
ATOM   8969  C  CB  . GLN I  1 15  ? -34.268 -4.379  56.730  1.00 54.49  ? 15  GLN Q CB  1 
ATOM   8970  C  CG  . GLN I  1 15  ? -35.296 -5.223  55.986  1.00 56.28  ? 15  GLN Q CG  1 
ATOM   8971  C  CD  . GLN I  1 15  ? -36.387 -5.758  56.904  1.00 60.22  ? 15  GLN Q CD  1 
ATOM   8972  O  OE1 . GLN I  1 15  ? -36.120 -6.139  58.044  1.00 62.08  ? 15  GLN Q OE1 1 
ATOM   8973  N  NE2 . GLN I  1 15  ? -37.627 -5.787  56.410  1.00 61.90  ? 15  GLN Q NE2 1 
ATOM   8974  N  N   . GLY I  1 16  ? -31.169 -4.969  56.321  1.00 49.76  ? 16  GLY Q N   1 
ATOM   8975  C  CA  . GLY I  1 16  ? -30.134 -5.959  56.048  1.00 49.33  ? 16  GLY Q CA  1 
ATOM   8976  C  C   . GLY I  1 16  ? -29.109 -6.130  57.150  1.00 49.73  ? 16  GLY Q C   1 
ATOM   8977  O  O   . GLY I  1 16  ? -29.147 -5.429  58.167  1.00 50.26  ? 16  GLY Q O   1 
ATOM   8978  N  N   . ILE I  1 17  ? -28.196 -7.074  56.924  1.00 49.72  ? 17  ILE Q N   1 
ATOM   8979  C  CA  . ILE I  1 17  ? -27.150 -7.441  57.871  1.00 50.49  ? 17  ILE Q CA  1 
ATOM   8980  C  C   . ILE I  1 17  ? -25.811 -7.402  57.137  1.00 48.18  ? 17  ILE Q C   1 
ATOM   8981  O  O   . ILE I  1 17  ? -25.637 -8.094  56.138  1.00 47.89  ? 17  ILE Q O   1 
ATOM   8982  C  CB  . ILE I  1 17  ? -27.374 -8.867  58.431  1.00 53.83  ? 17  ILE Q CB  1 
ATOM   8983  C  CG1 . ILE I  1 17  ? -28.776 -9.009  59.047  1.00 56.49  ? 17  ILE Q CG1 1 
ATOM   8984  C  CG2 . ILE I  1 17  ? -26.282 -9.245  59.436  1.00 54.97  ? 17  ILE Q CG2 1 
ATOM   8985  C  CD1 . ILE I  1 17  ? -29.029 -8.178  60.289  1.00 57.44  ? 17  ILE Q CD1 1 
ATOM   8986  N  N   . ILE I  1 18  ? -24.879 -6.590  57.627  1.00 46.83  ? 18  ILE Q N   1 
ATOM   8987  C  CA  . ILE I  1 18  ? -23.538 -6.499  57.042  1.00 44.99  ? 18  ILE Q CA  1 
ATOM   8988  C  C   . ILE I  1 18  ? -22.508 -6.935  58.077  1.00 46.39  ? 18  ILE Q C   1 
ATOM   8989  O  O   . ILE I  1 18  ? -22.540 -6.472  59.218  1.00 47.37  ? 18  ILE Q O   1 
ATOM   8990  C  CB  . ILE I  1 18  ? -23.235 -5.070  56.546  1.00 42.18  ? 18  ILE Q CB  1 
ATOM   8991  C  CG1 . ILE I  1 18  ? -24.213 -4.679  55.428  1.00 40.98  ? 18  ILE Q CG1 1 
ATOM   8992  C  CG2 . ILE I  1 18  ? -21.788 -4.947  56.063  1.00 40.71  ? 18  ILE Q CG2 1 
ATOM   8993  C  CD1 . ILE I  1 18  ? -24.161 -5.557  54.189  1.00 40.79  ? 18  ILE Q CD1 1 
ATOM   8994  N  N   . ASN I  1 19  ? -21.608 -7.825  57.655  1.00 46.79  ? 19  ASN Q N   1 
ATOM   8995  C  CA  . ASN I  1 19  ? -20.494 -8.320  58.469  1.00 48.24  ? 19  ASN Q CA  1 
ATOM   8996  C  C   . ASN I  1 19  ? -19.184 -7.646  58.063  1.00 46.34  ? 19  ASN Q C   1 
ATOM   8997  O  O   . ASN I  1 19  ? -19.068 -7.118  56.955  1.00 44.06  ? 19  ASN Q O   1 
ATOM   8998  C  CB  . ASN I  1 19  ? -20.353 -9.826  58.274  1.00 50.53  ? 19  ASN Q CB  1 
ATOM   8999  C  CG  . ASN I  1 19  ? -21.620 -10.581 58.636  1.00 52.92  ? 19  ASN Q CG  1 
ATOM   9000  O  OD1 . ASN I  1 19  ? -22.047 -10.572 59.789  1.00 54.75  ? 19  ASN Q OD1 1 
ATOM   9001  N  ND2 . ASN I  1 19  ? -22.225 -11.237 57.652  1.00 53.19  ? 19  ASN Q ND2 1 
ATOM   9002  N  N   . PHE I  1 20  ? -18.211 -7.665  58.975  1.00 47.52  ? 20  PHE Q N   1 
ATOM   9003  C  CA  . PHE I  1 20  ? -16.848 -7.199  58.715  1.00 46.40  ? 20  PHE Q CA  1 
ATOM   9004  C  C   . PHE I  1 20  ? -15.872 -8.207  59.313  1.00 48.95  ? 20  PHE Q C   1 
ATOM   9005  O  O   . PHE I  1 20  ? -16.155 -8.785  60.365  1.00 51.43  ? 20  PHE Q O   1 
ATOM   9006  C  CB  . PHE I  1 20  ? -16.585 -5.841  59.366  1.00 45.39  ? 20  PHE Q CB  1 
ATOM   9007  C  CG  . PHE I  1 20  ? -17.556 -4.766  58.972  1.00 43.50  ? 20  PHE Q CG  1 
ATOM   9008  C  CD1 . PHE I  1 20  ? -18.823 -4.707  59.551  1.00 44.52  ? 20  PHE Q CD1 1 
ATOM   9009  C  CD2 . PHE I  1 20  ? -17.201 -3.793  58.050  1.00 41.04  ? 20  PHE Q CD2 1 
ATOM   9010  C  CE1 . PHE I  1 20  ? -19.722 -3.714  59.198  1.00 43.05  ? 20  PHE Q CE1 1 
ATOM   9011  C  CE2 . PHE I  1 20  ? -18.094 -2.793  57.703  1.00 39.60  ? 20  PHE Q CE2 1 
ATOM   9012  C  CZ  . PHE I  1 20  ? -19.353 -2.751  58.281  1.00 40.59  ? 20  PHE Q CZ  1 
ATOM   9013  N  N   . GLU I  1 21  ? -14.734 -8.413  58.651  1.00 48.62  ? 21  GLU Q N   1 
ATOM   9014  C  CA  . GLU I  1 21  ? -13.681 -9.298  59.162  1.00 51.15  ? 21  GLU Q CA  1 
ATOM   9015  C  C   . GLU I  1 21  ? -12.308 -8.814  58.701  1.00 50.21  ? 21  GLU Q C   1 
ATOM   9016  O  O   . GLU I  1 21  ? -12.107 -8.543  57.516  1.00 48.39  ? 21  GLU Q O   1 
ATOM   9017  C  CB  . GLU I  1 21  ? -13.913 -10.749 58.725  1.00 53.29  ? 21  GLU Q CB  1 
ATOM   9018  C  CG  . GLU I  1 21  ? -12.797 -11.709 59.146  1.00 56.18  ? 21  GLU Q CG  1 
ATOM   9019  C  CD  . GLU I  1 21  ? -13.254 -13.150 59.326  1.00 59.43  ? 21  GLU Q CD  1 
ATOM   9020  O  OE1 . GLU I  1 21  ? -14.202 -13.580 58.633  1.00 59.35  ? 21  GLU Q OE1 1 
ATOM   9021  O  OE2 . GLU I  1 21  ? -12.659 -13.863 60.166  1.00 62.48  ? 21  GLU Q OE2 1 
ATOM   9022  N  N   . GLN I  1 22  ? -11.385 -8.698  59.656  1.00 51.75  ? 22  GLN Q N   1 
ATOM   9023  C  CA  . GLN I  1 22  ? -10.024 -8.227  59.406  1.00 51.44  ? 22  GLN Q CA  1 
ATOM   9024  C  C   . GLN I  1 22  ? -9.070  -9.221  60.041  1.00 54.80  ? 22  GLN Q C   1 
ATOM   9025  O  O   . GLN I  1 22  ? -8.955  -9.269  61.265  1.00 56.73  ? 22  GLN Q O   1 
ATOM   9026  C  CB  . GLN I  1 22  ? -9.833  -6.826  60.003  1.00 50.10  ? 22  GLN Q CB  1 
ATOM   9027  C  CG  . GLN I  1 22  ? -8.598  -6.091  59.498  1.00 49.10  ? 22  GLN Q CG  1 
ATOM   9028  C  CD  . GLN I  1 22  ? -8.368  -4.752  60.181  1.00 48.43  ? 22  GLN Q CD  1 
ATOM   9029  O  OE1 . GLN I  1 22  ? -8.823  -4.522  61.304  1.00 49.52  ? 22  GLN Q OE1 1 
ATOM   9030  N  NE2 . GLN I  1 22  ? -7.655  -3.856  59.500  1.00 46.88  ? 22  GLN Q NE2 1 
ATOM   9031  N  N   . LYS I  1 23  ? -8.409  -10.027 59.214  1.00 55.91  ? 23  LYS Q N   1 
ATOM   9032  C  CA  . LYS I  1 23  ? -7.495  -11.062 59.715  1.00 59.53  ? 23  LYS Q CA  1 
ATOM   9033  C  C   . LYS I  1 23  ? -6.256  -10.460 60.369  1.00 60.47  ? 23  LYS Q C   1 
ATOM   9034  O  O   . LYS I  1 23  ? -5.935  -10.783 61.516  1.00 63.04  ? 23  LYS Q O   1 
ATOM   9035  C  CB  . LYS I  1 23  ? -7.084  -12.028 58.598  1.00 60.61  ? 23  LYS Q CB  1 
ATOM   9036  C  CG  . LYS I  1 23  ? -8.244  -12.831 58.018  1.00 60.79  ? 23  LYS Q CG  1 
ATOM   9037  C  CD  . LYS I  1 23  ? -7.760  -14.096 57.318  1.00 63.47  ? 23  LYS Q CD  1 
ATOM   9038  C  CE  . LYS I  1 23  ? -8.896  -14.806 56.591  1.00 63.65  ? 23  LYS Q CE  1 
ATOM   9039  N  NZ  . LYS I  1 23  ? -9.789  -15.554 57.521  1.00 65.81  ? 23  LYS Q NZ  1 
ATOM   9040  N  N   . GLU I  1 24  ? -5.574  -9.584  59.636  1.00 58.68  ? 24  GLU Q N   1 
ATOM   9041  C  CA  . GLU I  1 24  ? -4.380  -8.906  60.143  1.00 59.59  ? 24  GLU Q CA  1 
ATOM   9042  C  C   . GLU I  1 24  ? -4.730  -7.495  60.590  1.00 57.61  ? 24  GLU Q C   1 
ATOM   9043  O  O   . GLU I  1 24  ? -5.426  -6.772  59.882  1.00 54.76  ? 24  GLU Q O   1 
ATOM   9044  C  CB  . GLU I  1 24  ? -3.278  -8.843  59.074  1.00 59.45  ? 24  GLU Q CB  1 
ATOM   9045  C  CG  . GLU I  1 24  ? -2.271  -9.986  59.121  1.00 62.95  ? 24  GLU Q CG  1 
ATOM   9046  C  CD  . GLU I  1 24  ? -2.892  -11.356 58.912  1.00 64.67  ? 24  GLU Q CD  1 
ATOM   9047  O  OE1 . GLU I  1 24  ? -3.939  -11.453 58.238  1.00 62.86  ? 24  GLU Q OE1 1 
ATOM   9048  O  OE2 . GLU I  1 24  ? -2.316  -12.346 59.419  1.00 68.18  ? 24  GLU Q OE2 1 
ATOM   9049  N  N   . SER I  1 25  ? -4.245  -7.113  61.770  1.00 59.48  ? 25  SER Q N   1 
ATOM   9050  C  CA  . SER I  1 25  ? -4.154  -5.703  62.161  1.00 58.35  ? 25  SER Q CA  1 
ATOM   9051  C  C   . SER I  1 25  ? -3.578  -4.901  60.990  1.00 56.18  ? 25  SER Q C   1 
ATOM   9052  O  O   . SER I  1 25  ? -2.612  -5.332  60.368  1.00 57.22  ? 25  SER Q O   1 
ATOM   9053  C  CB  . SER I  1 25  ? -3.249  -5.567  63.398  1.00 61.42  ? 25  SER Q CB  1 
ATOM   9054  O  OG  . SER I  1 25  ? -2.761  -4.245  63.566  1.00 60.77  ? 25  SER Q OG  1 
ATOM   9055  N  N   . ASN I  1 26  ? -4.186  -3.765  60.669  1.00 53.66  ? 26  ASN Q N   1 
ATOM   9056  C  CA  . ASN I  1 26  ? -3.741  -2.924  59.550  1.00 51.66  ? 26  ASN Q CA  1 
ATOM   9057  C  C   . ASN I  1 26  ? -3.695  -3.670  58.192  1.00 50.72  ? 26  ASN Q C   1 
ATOM   9058  O  O   . ASN I  1 26  ? -2.853  -3.376  57.336  1.00 50.66  ? 26  ASN Q O   1 
ATOM   9059  C  CB  . ASN I  1 26  ? -2.372  -2.300  59.860  1.00 53.20  ? 26  ASN Q CB  1 
ATOM   9060  C  CG  . ASN I  1 26  ? -2.295  -1.713  61.264  1.00 54.92  ? 26  ASN Q CG  1 
ATOM   9061  O  OD1 . ASN I  1 26  ? -1.487  -2.147  62.089  1.00 57.68  ? 26  ASN Q OD1 1 
ATOM   9062  N  ND2 . ASN I  1 26  ? -3.143  -0.728  61.543  1.00 53.59  ? 26  ASN Q ND2 1 
ATOM   9063  N  N   . GLY I  1 27  ? -4.599  -4.632  58.013  1.00 50.35  ? 27  GLY Q N   1 
ATOM   9064  C  CA  . GLY I  1 27  ? -4.711  -5.406  56.780  1.00 49.59  ? 27  GLY Q CA  1 
ATOM   9065  C  C   . GLY I  1 27  ? -6.103  -5.188  56.223  1.00 46.96  ? 27  GLY Q C   1 
ATOM   9066  O  O   . GLY I  1 27  ? -6.894  -4.454  56.818  1.00 45.74  ? 27  GLY Q O   1 
ATOM   9067  N  N   . PRO I  1 28  ? -6.411  -5.820  55.077  1.00 46.23  ? 28  PRO Q N   1 
ATOM   9068  C  CA  . PRO I  1 28  ? -7.693  -5.587  54.417  1.00 44.00  ? 28  PRO Q CA  1 
ATOM   9069  C  C   . PRO I  1 28  ? -8.898  -6.106  55.219  1.00 44.22  ? 28  PRO Q C   1 
ATOM   9070  O  O   . PRO I  1 28  ? -8.809  -7.152  55.872  1.00 46.39  ? 28  PRO Q O   1 
ATOM   9071  C  CB  . PRO I  1 28  ? -7.544  -6.330  53.083  1.00 44.36  ? 28  PRO Q CB  1 
ATOM   9072  C  CG  . PRO I  1 28  ? -6.514  -7.360  53.327  1.00 47.21  ? 28  PRO Q CG  1 
ATOM   9073  C  CD  . PRO I  1 28  ? -5.565  -6.762  54.322  1.00 47.93  ? 28  PRO Q CD  1 
ATOM   9074  N  N   . VAL I  1 29  ? -9.997  -5.354  55.169  1.00 42.13  ? 29  VAL Q N   1 
ATOM   9075  C  CA  . VAL I  1 29  ? -11.250 -5.700  55.849  1.00 42.42  ? 29  VAL Q CA  1 
ATOM   9076  C  C   . VAL I  1 29  ? -12.235 -6.232  54.815  1.00 41.66  ? 29  VAL Q C   1 
ATOM   9077  O  O   . VAL I  1 29  ? -12.553 -5.523  53.862  1.00 39.69  ? 29  VAL Q O   1 
ATOM   9078  C  CB  . VAL I  1 29  ? -11.867 -4.466  56.547  1.00 41.16  ? 29  VAL Q CB  1 
ATOM   9079  C  CG1 . VAL I  1 29  ? -13.206 -4.804  57.197  1.00 41.82  ? 29  VAL Q CG1 1 
ATOM   9080  C  CG2 . VAL I  1 29  ? -10.902 -3.897  57.579  1.00 42.17  ? 29  VAL Q CG2 1 
ATOM   9081  N  N   . LYS I  1 30  ? -12.702 -7.468  54.985  1.00 43.50  ? 30  LYS Q N   1 
ATOM   9082  C  CA  . LYS I  1 30  ? -13.780 -8.007  54.139  1.00 43.29  ? 30  LYS Q CA  1 
ATOM   9083  C  C   . LYS I  1 30  ? -15.142 -7.547  54.660  1.00 42.55  ? 30  LYS Q C   1 
ATOM   9084  O  O   . LYS I  1 30  ? -15.402 -7.600  55.859  1.00 43.68  ? 30  LYS Q O   1 
ATOM   9085  C  CB  . LYS I  1 30  ? -13.734 -9.534  54.059  1.00 46.03  ? 30  LYS Q CB  1 
ATOM   9086  C  CG  . LYS I  1 30  ? -12.593 -10.068 53.204  1.00 46.97  ? 30  LYS Q CG  1 
ATOM   9087  C  CD  . LYS I  1 30  ? -12.854 -11.500 52.761  0.50 49.57  ? 30  LYS Q CD  1 
ATOM   9088  C  CE  . LYS I  1 30  ? -11.708 -12.050 51.929  0.50 50.95  ? 30  LYS Q CE  1 
ATOM   9089  N  NZ  . LYS I  1 30  ? -10.500 -12.302 52.759  0.50 52.68  ? 30  LYS Q NZ  1 
ATOM   9090  N  N   . VAL I  1 31  ? -15.995 -7.093  53.748  1.00 40.92  ? 31  VAL Q N   1 
ATOM   9091  C  CA  . VAL I  1 31  ? -17.329 -6.590  54.073  1.00 40.32  ? 31  VAL Q CA  1 
ATOM   9092  C  C   . VAL I  1 31  ? -18.332 -7.371  53.222  1.00 40.95  ? 31  VAL Q C   1 
ATOM   9093  O  O   . VAL I  1 31  ? -18.284 -7.299  51.991  1.00 39.98  ? 31  VAL Q O   1 
ATOM   9094  C  CB  . VAL I  1 31  ? -17.451 -5.075  53.779  1.00 37.88  ? 31  VAL Q CB  1 
ATOM   9095  C  CG1 . VAL I  1 31  ? -18.743 -4.511  54.368  1.00 37.79  ? 31  VAL Q CG1 1 
ATOM   9096  C  CG2 . VAL I  1 31  ? -16.240 -4.315  54.313  1.00 37.40  ? 31  VAL Q CG2 1 
ATOM   9097  N  N   . TRP I  1 32  ? -19.222 -8.127  53.867  1.00 42.87  ? 32  TRP Q N   1 
ATOM   9098  C  CA  . TRP I  1 32  ? -20.197 -8.946  53.147  1.00 43.96  ? 32  TRP Q CA  1 
ATOM   9099  C  C   . TRP I  1 32  ? -21.503 -9.166  53.910  1.00 45.36  ? 32  TRP Q C   1 
ATOM   9100  O  O   . TRP I  1 32  ? -21.552 -9.088  55.139  1.00 46.33  ? 32  TRP Q O   1 
ATOM   9101  C  CB  . TRP I  1 32  ? -19.595 -10.302 52.748  1.00 46.18  ? 32  TRP Q CB  1 
ATOM   9102  C  CG  . TRP I  1 32  ? -19.659 -11.337 53.833  1.00 49.12  ? 32  TRP Q CG  1 
ATOM   9103  C  CD1 . TRP I  1 32  ? -20.581 -12.344 53.959  1.00 51.63  ? 32  TRP Q CD1 1 
ATOM   9104  C  CD2 . TRP I  1 32  ? -18.785 -11.452 54.957  1.00 50.17  ? 32  TRP Q CD2 1 
ATOM   9105  N  NE1 . TRP I  1 32  ? -20.329 -13.078 55.087  1.00 54.17  ? 32  TRP Q NE1 1 
ATOM   9106  C  CE2 . TRP I  1 32  ? -19.231 -12.556 55.721  1.00 53.35  ? 32  TRP Q CE2 1 
ATOM   9107  C  CE3 . TRP I  1 32  ? -17.665 -10.731 55.394  1.00 49.00  ? 32  TRP Q CE3 1 
ATOM   9108  C  CZ2 . TRP I  1 32  ? -18.594 -12.959 56.900  1.00 55.36  ? 32  TRP Q CZ2 1 
ATOM   9109  C  CZ3 . TRP I  1 32  ? -17.031 -11.130 56.566  1.00 50.98  ? 32  TRP Q CZ3 1 
ATOM   9110  C  CH2 . TRP I  1 32  ? -17.499 -12.237 57.306  1.00 54.13  ? 32  TRP Q CH2 1 
ATOM   9111  N  N   . GLY I  1 33  ? -22.544 -9.475  53.146  1.00 45.74  ? 33  GLY Q N   1 
ATOM   9112  C  CA  . GLY I  1 33  ? -23.884 -9.690  53.683  1.00 47.28  ? 33  GLY Q CA  1 
ATOM   9113  C  C   . GLY I  1 33  ? -24.944 -9.369  52.649  1.00 46.54  ? 33  GLY Q C   1 
ATOM   9114  O  O   . GLY I  1 33  ? -24.637 -9.190  51.463  1.00 45.25  ? 33  GLY Q O   1 
ATOM   9115  N  N   . SER I  1 34  ? -26.189 -9.281  53.109  1.00 47.64  ? 34  SER Q N   1 
ATOM   9116  C  CA  . SER I  1 34  ? -27.341 -9.081  52.232  1.00 47.55  ? 34  SER Q CA  1 
ATOM   9117  C  C   . SER I  1 34  ? -28.167 -7.878  52.681  1.00 46.50  ? 34  SER Q C   1 
ATOM   9118  O  O   . SER I  1 34  ? -28.412 -7.696  53.877  1.00 47.47  ? 34  SER Q O   1 
ATOM   9119  C  CB  . SER I  1 34  ? -28.200 -10.335 52.211  1.00 50.75  ? 34  SER Q CB  1 
ATOM   9120  O  OG  . SER I  1 34  ? -29.005 -10.364 51.048  1.00 50.95  ? 34  SER Q OG  1 
ATOM   9121  N  N   . ILE I  1 35  ? -28.555 -7.046  51.714  1.00 44.74  ? 35  ILE Q N   1 
ATOM   9122  C  CA  . ILE I  1 35  ? -29.474 -5.934  51.938  1.00 44.14  ? 35  ILE Q CA  1 
ATOM   9123  C  C   . ILE I  1 35  ? -30.672 -6.150  51.015  1.00 45.13  ? 35  ILE Q C   1 
ATOM   9124  O  O   . ILE I  1 35  ? -30.494 -6.318  49.809  1.00 44.46  ? 35  ILE Q O   1 
ATOM   9125  C  CB  . ILE I  1 35  ? -28.821 -4.570  51.627  1.00 41.33  ? 35  ILE Q CB  1 
ATOM   9126  C  CG1 . ILE I  1 35  ? -27.436 -4.466  52.275  1.00 40.32  ? 35  ILE Q CG1 1 
ATOM   9127  C  CG2 . ILE I  1 35  ? -29.713 -3.422  52.101  1.00 41.28  ? 35  ILE Q CG2 1 
ATOM   9128  C  CD1 . ILE I  1 35  ? -26.725 -3.169  51.967  1.00 37.89  ? 35  ILE Q CD1 1 
ATOM   9129  N  N   . LYS I  1 36  ? -31.876 -6.149  51.591  1.00 47.00  ? 36  LYS Q N   1 
ATOM   9130  C  CA  . LYS I  1 36  ? -33.130 -6.312  50.844  1.00 48.41  ? 36  LYS Q CA  1 
ATOM   9131  C  C   . LYS I  1 36  ? -33.919 -5.007  50.826  1.00 47.63  ? 36  LYS Q C   1 
ATOM   9132  O  O   . LYS I  1 36  ? -33.589 -4.062  51.547  1.00 46.50  ? 36  LYS Q O   1 
ATOM   9133  C  CB  . LYS I  1 36  ? -33.983 -7.412  51.479  1.00 51.86  ? 36  LYS Q CB  1 
ATOM   9134  C  CG  . LYS I  1 36  ? -33.347 -8.790  51.429  1.00 53.28  ? 36  LYS Q CG  1 
ATOM   9135  C  CD  . LYS I  1 36  ? -34.272 -9.852  52.002  1.00 57.07  ? 36  LYS Q CD  1 
ATOM   9136  C  CE  . LYS I  1 36  ? -33.789 -11.254 51.655  1.00 58.90  ? 36  LYS Q CE  1 
ATOM   9137  N  NZ  . LYS I  1 36  ? -32.393 -11.502 52.108  1.00 57.78  ? 36  LYS Q NZ  1 
ATOM   9138  N  N   . GLY I  1 37  ? -34.955 -4.970  49.991  1.00 48.57  ? 37  GLY Q N   1 
ATOM   9139  C  CA  . GLY I  1 37  ? -35.856 -3.820  49.883  1.00 48.42  ? 37  GLY Q CA  1 
ATOM   9140  C  C   . GLY I  1 37  ? -35.368 -2.632  49.067  1.00 45.70  ? 37  GLY Q C   1 
ATOM   9141  O  O   . GLY I  1 37  ? -35.988 -1.571  49.114  1.00 45.69  ? 37  GLY Q O   1 
ATOM   9142  N  N   . LEU I  1 38  ? -34.276 -2.802  48.316  1.00 43.71  ? 38  LEU Q N   1 
ATOM   9143  C  CA  . LEU I  1 38  ? -33.683 -1.714  47.516  1.00 41.27  ? 38  LEU Q CA  1 
ATOM   9144  C  C   . LEU I  1 38  ? -34.264 -1.652  46.104  1.00 41.61  ? 38  LEU Q C   1 
ATOM   9145  O  O   . LEU I  1 38  ? -34.723 -2.659  45.573  1.00 43.29  ? 38  LEU Q O   1 
ATOM   9146  C  CB  . LEU I  1 38  ? -32.170 -1.901  47.422  1.00 39.32  ? 38  LEU Q CB  1 
ATOM   9147  C  CG  . LEU I  1 38  ? -31.380 -1.618  48.696  1.00 38.52  ? 38  LEU Q CG  1 
ATOM   9148  C  CD1 . LEU I  1 38  ? -30.021 -2.301  48.637  1.00 37.57  ? 38  LEU Q CD1 1 
ATOM   9149  C  CD2 . LEU I  1 38  ? -31.226 -0.120  48.918  1.00 37.10  ? 38  LEU Q CD2 1 
ATOM   9150  N  N   . THR I  1 39  ? -34.247 -0.465  45.500  1.00 40.30  ? 39  THR Q N   1 
ATOM   9151  C  CA  . THR I  1 39  ? -34.548 -0.337  44.073  1.00 40.51  ? 39  THR Q CA  1 
ATOM   9152  C  C   . THR I  1 39  ? -33.374 -0.928  43.311  1.00 39.41  ? 39  THR Q C   1 
ATOM   9153  O  O   . THR I  1 39  ? -32.220 -0.797  43.744  1.00 37.68  ? 39  THR Q O   1 
ATOM   9154  C  CB  . THR I  1 39  ? -34.749 1.129   43.616  1.00 39.62  ? 39  THR Q CB  1 
ATOM   9155  O  OG1 . THR I  1 39  ? -33.631 1.933   44.028  1.00 37.45  ? 39  THR Q OG1 1 
ATOM   9156  C  CG2 . THR I  1 39  ? -36.043 1.703   44.187  1.00 41.26  ? 39  THR Q CG2 1 
ATOM   9157  N  N   . GLU I  1 40  ? -33.670 -1.580  42.189  1.00 40.69  ? 40  GLU Q N   1 
ATOM   9158  C  CA  . GLU I  1 40  ? -32.641 -2.180  41.338  1.00 40.28  ? 40  GLU Q CA  1 
ATOM   9159  C  C   . GLU I  1 40  ? -31.588 -1.131  40.959  1.00 37.94  ? 40  GLU Q C   1 
ATOM   9160  O  O   . GLU I  1 40  ? -31.932 0.002   40.630  1.00 37.29  ? 40  GLU Q O   1 
ATOM   9161  C  CB  . GLU I  1 40  ? -33.274 -2.764  40.072  1.00 42.40  ? 40  GLU Q CB  1 
ATOM   9162  C  CG  . GLU I  1 40  ? -32.315 -3.536  39.178  1.00 42.77  ? 40  GLU Q CG  1 
ATOM   9163  C  CD  . GLU I  1 40  ? -32.974 -4.083  37.920  1.00 45.32  ? 40  GLU Q CD  1 
ATOM   9164  O  OE1 . GLU I  1 40  ? -34.142 -3.748  37.633  1.00 46.67  ? 40  GLU Q OE1 1 
ATOM   9165  O  OE2 . GLU I  1 40  ? -32.316 -4.863  37.205  1.00 46.37  ? 40  GLU Q OE2 1 
ATOM   9166  N  N   . GLY I  1 41  ? -30.316 -1.514  41.045  1.00 36.90  ? 41  GLY Q N   1 
ATOM   9167  C  CA  . GLY I  1 41  ? -29.204 -0.650  40.641  1.00 35.10  ? 41  GLY Q CA  1 
ATOM   9168  C  C   . GLY I  1 41  ? -28.274 -0.265  41.774  1.00 33.43  ? 41  GLY Q C   1 
ATOM   9169  O  O   . GLY I  1 41  ? -28.268 -0.896  42.846  1.00 33.67  ? 41  GLY Q O   1 
ATOM   9170  N  N   . LEU I  1 42  ? -27.492 0.786   41.522  1.00 31.97  ? 42  LEU Q N   1 
ATOM   9171  C  CA  . LEU I  1 42  ? -26.405 1.198   42.414  1.00 30.53  ? 42  LEU Q CA  1 
ATOM   9172  C  C   . LEU I  1 42  ? -26.912 1.997   43.603  1.00 30.07  ? 42  LEU Q C   1 
ATOM   9173  O  O   . LEU I  1 42  ? -27.822 2.821   43.463  1.00 30.28  ? 42  LEU Q O   1 
ATOM   9174  C  CB  . LEU I  1 42  ? -25.374 2.044   41.654  1.00 29.56  ? 42  LEU Q CB  1 
ATOM   9175  C  CG  . LEU I  1 42  ? -24.560 1.359   40.553  1.00 30.12  ? 42  LEU Q CG  1 
ATOM   9176  C  CD1 . LEU I  1 42  ? -23.797 2.390   39.738  1.00 29.53  ? 42  LEU Q CD1 1 
ATOM   9177  C  CD2 . LEU I  1 42  ? -23.582 0.353   41.127  1.00 30.23  ? 42  LEU Q CD2 1 
ATOM   9178  N  N   . HIS I  1 43  ? -26.302 1.757   44.762  1.00 29.67  ? 43  HIS Q N   1 
ATOM   9179  C  CA  . HIS I  1 43  ? -26.617 2.488   45.995  1.00 29.58  ? 43  HIS Q CA  1 
ATOM   9180  C  C   . HIS I  1 43  ? -25.350 2.815   46.773  1.00 28.61  ? 43  HIS Q C   1 
ATOM   9181  O  O   . HIS I  1 43  ? -24.553 1.923   47.058  1.00 28.60  ? 43  HIS Q O   1 
ATOM   9182  C  CB  . HIS I  1 43  ? -27.563 1.665   46.872  1.00 31.05  ? 43  HIS Q CB  1 
ATOM   9183  C  CG  . HIS I  1 43  ? -28.927 1.507   46.284  1.00 32.30  ? 43  HIS Q CG  1 
ATOM   9184  N  ND1 . HIS I  1 43  ? -29.943 2.408   46.517  1.00 32.95  ? 43  HIS Q ND1 1 
ATOM   9185  C  CD2 . HIS I  1 43  ? -29.431 0.580   45.438  1.00 33.37  ? 43  HIS Q CD2 1 
ATOM   9186  C  CE1 . HIS I  1 43  ? -31.021 2.031   45.852  1.00 34.24  ? 43  HIS Q CE1 1 
ATOM   9187  N  NE2 . HIS I  1 43  ? -30.735 0.929   45.182  1.00 34.51  ? 43  HIS Q NE2 1 
ATOM   9188  N  N   . GLY I  1 44  ? -25.188 4.089   47.130  1.00 28.08  ? 44  GLY Q N   1 
ATOM   9189  C  CA  . GLY I  1 44  ? -24.077 4.538   47.967  1.00 27.57  ? 44  GLY Q CA  1 
ATOM   9190  C  C   . GLY I  1 44  ? -24.055 3.792   49.292  1.00 28.38  ? 44  GLY Q C   1 
ATOM   9191  O  O   . GLY I  1 44  ? -25.105 3.514   49.880  1.00 29.51  ? 44  GLY Q O   1 
ATOM   9192  N  N   . PHE I  1 45  ? -22.846 3.476   49.744  1.00 28.07  ? 45  PHE Q N   1 
ATOM   9193  C  CA  . PHE I  1 45  ? -22.615 2.554   50.840  1.00 29.06  ? 45  PHE Q CA  1 
ATOM   9194  C  C   . PHE I  1 45  ? -21.437 3.123   51.625  1.00 28.93  ? 45  PHE Q C   1 
ATOM   9195  O  O   . PHE I  1 45  ? -20.297 3.061   51.163  1.00 28.15  ? 45  PHE Q O   1 
ATOM   9196  C  CB  . PHE I  1 45  ? -22.308 1.183   50.250  1.00 29.29  ? 45  PHE Q CB  1 
ATOM   9197  C  CG  . PHE I  1 45  ? -22.243 0.074   51.258  1.00 30.67  ? 45  PHE Q CG  1 
ATOM   9198  C  CD1 . PHE I  1 45  ? -23.389 -0.353  51.915  1.00 32.05  ? 45  PHE Q CD1 1 
ATOM   9199  C  CD2 . PHE I  1 45  ? -21.048 -0.587  51.507  1.00 30.89  ? 45  PHE Q CD2 1 
ATOM   9200  C  CE1 . PHE I  1 45  ? -23.337 -1.399  52.824  1.00 33.67  ? 45  PHE Q CE1 1 
ATOM   9201  C  CE2 . PHE I  1 45  ? -20.992 -1.633  52.411  1.00 32.47  ? 45  PHE Q CE2 1 
ATOM   9202  C  CZ  . PHE I  1 45  ? -22.135 -2.041  53.072  1.00 33.86  ? 45  PHE Q CZ  1 
ATOM   9203  N  N   . HIS I  1 46  ? -21.726 3.718   52.779  1.00 29.89  ? 46  HIS Q N   1 
ATOM   9204  C  CA  . HIS I  1 46  ? -20.764 4.572   53.479  1.00 30.08  ? 46  HIS Q CA  1 
ATOM   9205  C  C   . HIS I  1 46  ? -20.758 4.364   54.979  1.00 31.80  ? 46  HIS Q C   1 
ATOM   9206  O  O   . HIS I  1 46  ? -21.820 4.114   55.581  1.00 33.00  ? 46  HIS Q O   1 
ATOM   9207  C  CB  . HIS I  1 46  ? -21.088 6.043   53.234  1.00 29.87  ? 46  HIS Q CB  1 
ATOM   9208  C  CG  . HIS I  1 46  ? -21.195 6.405   51.794  1.00 28.68  ? 46  HIS Q CG  1 
ATOM   9209  N  ND1 . HIS I  1 46  ? -22.304 7.029   51.270  1.00 28.79  ? 46  HIS Q ND1 1 
ATOM   9210  C  CD2 . HIS I  1 46  ? -20.338 6.229   50.762  1.00 27.64  ? 46  HIS Q CD2 1 
ATOM   9211  C  CE1 . HIS I  1 46  ? -22.123 7.229   49.977  1.00 27.80  ? 46  HIS Q CE1 1 
ATOM   9212  N  NE2 . HIS I  1 46  ? -20.944 6.744   49.641  1.00 27.11  ? 46  HIS Q NE2 1 
ATOM   9213  N  N   . VAL I  1 47  ? -19.569 4.484   55.577  1.00 32.16  ? 47  VAL Q N   1 
ATOM   9214  C  CA  . VAL I  1 47  ? -19.438 4.633   57.025  1.00 34.07  ? 47  VAL Q CA  1 
ATOM   9215  C  C   . VAL I  1 47  ? -19.482 6.121   57.380  1.00 34.62  ? 47  VAL Q C   1 
ATOM   9216  O  O   . VAL I  1 47  ? -18.699 6.910   56.861  1.00 33.70  ? 47  VAL Q O   1 
ATOM   9217  C  CB  . VAL I  1 47  ? -18.154 4.000   57.575  1.00 34.67  ? 47  VAL Q CB  1 
ATOM   9218  C  CG1 . VAL I  1 47  ? -18.075 4.177   59.091  1.00 36.92  ? 47  VAL Q CG1 1 
ATOM   9219  C  CG2 . VAL I  1 47  ? -18.094 2.522   57.203  1.00 34.57  ? 47  VAL Q CG2 1 
ATOM   9220  N  N   . HIS I  1 48  ? -20.414 6.491   58.258  1.00 36.45  ? 48  HIS Q N   1 
ATOM   9221  C  CA  . HIS I  1 48  ? -20.567 7.873   58.726  1.00 37.71  ? 48  HIS Q CA  1 
ATOM   9222  C  C   . HIS I  1 48  ? -19.923 8.033   60.103  1.00 40.10  ? 48  HIS Q C   1 
ATOM   9223  O  O   . HIS I  1 48  ? -19.761 7.052   60.819  1.00 41.04  ? 48  HIS Q O   1 
ATOM   9224  C  CB  . HIS I  1 48  ? -22.050 8.250   58.757  1.00 38.59  ? 48  HIS Q CB  1 
ATOM   9225  C  CG  . HIS I  1 48  ? -22.665 8.378   57.397  1.00 36.75  ? 48  HIS Q CG  1 
ATOM   9226  N  ND1 . HIS I  1 48  ? -23.158 9.570   56.910  1.00 36.82  ? 48  HIS Q ND1 1 
ATOM   9227  C  CD2 . HIS I  1 48  ? -22.845 7.470   56.409  1.00 35.13  ? 48  HIS Q CD2 1 
ATOM   9228  C  CE1 . HIS I  1 48  ? -23.636 9.386   55.693  1.00 35.25  ? 48  HIS Q CE1 1 
ATOM   9229  N  NE2 . HIS I  1 48  ? -23.454 8.121   55.363  1.00 34.24  ? 48  HIS Q NE2 1 
ATOM   9230  N  N   . GLU I  1 49  ? -19.576 9.272   60.462  1.00 41.40  ? 49  GLU Q N   1 
ATOM   9231  C  CA  . GLU I  1 49  ? -18.704 9.565   61.619  1.00 43.75  ? 49  GLU Q CA  1 
ATOM   9232  C  C   . GLU I  1 49  ? -19.216 9.096   62.977  1.00 46.71  ? 49  GLU Q C   1 
ATOM   9233  O  O   . GLU I  1 49  ? -18.462 8.496   63.740  1.00 47.91  ? 49  GLU Q O   1 
ATOM   9234  C  CB  . GLU I  1 49  ? -18.401 11.068  61.704  1.00 44.80  ? 49  GLU Q CB  1 
ATOM   9235  C  CG  . GLU I  1 49  ? -17.409 11.453  62.806  1.00 47.21  ? 49  GLU Q CG  1 
ATOM   9236  C  CD  . GLU I  1 49  ? -16.985 12.909  62.744  1.00 48.35  ? 49  GLU Q CD  1 
ATOM   9237  O  OE1 . GLU I  1 49  ? -17.569 13.677  61.943  1.00 47.53  ? 49  GLU Q OE1 1 
ATOM   9238  O  OE2 . GLU I  1 49  ? -16.069 13.294  63.511  1.00 50.43  ? 49  GLU Q OE2 1 
ATOM   9239  N  N   . PHE I  1 50  ? -20.482 9.386   63.280  1.00 48.28  ? 50  PHE Q N   1 
ATOM   9240  C  CA  . PHE I  1 50  ? -21.042 9.164   64.618  1.00 51.73  ? 50  PHE Q CA  1 
ATOM   9241  C  C   . PHE I  1 50  ? -21.966 7.954   64.635  1.00 51.93  ? 50  PHE Q C   1 
ATOM   9242  O  O   . PHE I  1 50  ? -22.749 7.759   63.701  1.00 50.36  ? 50  PHE Q O   1 
ATOM   9243  C  CB  . PHE I  1 50  ? -21.809 10.410  65.062  1.00 54.04  ? 50  PHE Q CB  1 
ATOM   9244  C  CG  . PHE I  1 50  ? -20.984 11.663  65.016  1.00 54.46  ? 50  PHE Q CG  1 
ATOM   9245  C  CD1 . PHE I  1 50  ? -19.862 11.797  65.828  1.00 56.07  ? 50  PHE Q CD1 1 
ATOM   9246  C  CD2 . PHE I  1 50  ? -21.309 12.699  64.144  1.00 53.51  ? 50  PHE Q CD2 1 
ATOM   9247  C  CE1 . PHE I  1 50  ? -19.087 12.946  65.780  1.00 56.74  ? 50  PHE Q CE1 1 
ATOM   9248  C  CE2 . PHE I  1 50  ? -20.533 13.850  64.088  1.00 54.17  ? 50  PHE Q CE2 1 
ATOM   9249  C  CZ  . PHE I  1 50  ? -19.421 13.974  64.908  1.00 55.80  ? 50  PHE Q CZ  1 
ATOM   9250  N  N   . GLY I  1 51  ? -21.878 7.153   65.695  1.00 54.37  ? 51  GLY Q N   1 
ATOM   9251  C  CA  . GLY I  1 51  ? -22.819 6.060   65.954  1.00 55.52  ? 51  GLY Q CA  1 
ATOM   9252  C  C   . GLY I  1 51  ? -24.038 6.553   66.715  1.00 58.74  ? 51  GLY Q C   1 
ATOM   9253  O  O   . GLY I  1 51  ? -24.475 5.925   67.682  1.00 61.53  ? 51  GLY Q O   1 
ATOM   9254  N  N   . ASP I  1 52  ? -24.592 7.670   66.251  1.00 58.65  ? 52  ASP Q N   1 
ATOM   9255  C  CA  . ASP I  1 52  ? -25.665 8.377   66.911  1.00 61.97  ? 52  ASP Q CA  1 
ATOM   9256  C  C   . ASP I  1 52  ? -26.883 8.180   66.028  1.00 60.98  ? 52  ASP Q C   1 
ATOM   9257  O  O   . ASP I  1 52  ? -26.907 8.671   64.897  1.00 58.52  ? 52  ASP Q O   1 
ATOM   9258  C  CB  . ASP I  1 52  ? -25.310 9.865   67.037  1.00 62.85  ? 52  ASP Q CB  1 
ATOM   9259  C  CG  . ASP I  1 52  ? -26.345 10.665  67.828  1.00 66.70  ? 52  ASP Q CG  1 
ATOM   9260  O  OD1 . ASP I  1 52  ? -27.462 10.167  68.070  1.00 68.25  ? 52  ASP Q OD1 1 
ATOM   9261  O  OD2 . ASP I  1 52  ? -26.028 11.809  68.212  1.00 68.50  ? 52  ASP Q OD2 1 
ATOM   9262  N  N   . ASN I  1 53  ? -27.869 7.451   66.547  1.00 63.39  ? 53  ASN Q N   1 
ATOM   9263  C  CA  . ASN I  1 53  ? -29.131 7.192   65.851  1.00 63.12  ? 53  ASN Q CA  1 
ATOM   9264  C  C   . ASN I  1 53  ? -30.337 7.756   66.628  1.00 67.08  ? 53  ASN Q C   1 
ATOM   9265  O  O   . ASN I  1 53  ? -31.455 7.234   66.522  1.00 68.21  ? 53  ASN Q O   1 
ATOM   9266  C  CB  . ASN I  1 53  ? -29.280 5.680   65.618  1.00 62.42  ? 53  ASN Q CB  1 
ATOM   9267  C  CG  . ASN I  1 53  ? -30.250 5.349   64.497  1.00 60.95  ? 53  ASN Q CG  1 
ATOM   9268  O  OD1 . ASN I  1 53  ? -29.895 5.374   63.311  1.00 57.78  ? 53  ASN Q OD1 1 
ATOM   9269  N  ND2 . ASN I  1 53  ? -31.476 5.018   64.867  1.00 63.55  ? 53  ASN Q ND2 1 
ATOM   9270  N  N   . THR I  1 54  ? -30.114 8.827   67.400  1.00 69.46  ? 54  THR Q N   1 
ATOM   9271  C  CA  . THR I  1 54  ? -31.189 9.492   68.144  1.00 73.56  ? 54  THR Q CA  1 
ATOM   9272  C  C   . THR I  1 54  ? -32.212 10.120  67.200  1.00 72.92  ? 54  THR Q C   1 
ATOM   9273  O  O   . THR I  1 54  ? -33.407 10.097  67.488  1.00 75.68  ? 54  THR Q O   1 
ATOM   9274  C  CB  . THR I  1 54  ? -30.669 10.592  69.100  1.00 76.47  ? 54  THR Q CB  1 
ATOM   9275  O  OG1 . THR I  1 54  ? -29.868 11.534  68.377  1.00 73.92  ? 54  THR Q OG1 1 
ATOM   9276  C  CG2 . THR I  1 54  ? -29.856 9.991   70.244  1.00 78.37  ? 54  THR Q CG2 1 
ATOM   9277  N  N   . ALA I  1 55  ? -31.732 10.683  66.089  1.00 69.56  ? 55  ALA Q N   1 
ATOM   9278  C  CA  . ALA I  1 55  ? -32.582 11.178  65.005  1.00 68.50  ? 55  ALA Q CA  1 
ATOM   9279  C  C   . ALA I  1 55  ? -32.367 10.298  63.774  1.00 64.49  ? 55  ALA Q C   1 
ATOM   9280  O  O   . ALA I  1 55  ? -32.015 10.785  62.684  1.00 61.78  ? 55  ALA Q O   1 
ATOM   9281  C  CB  . ALA I  1 55  ? -32.257 12.636  64.705  1.00 68.53  ? 55  ALA Q CB  1 
ATOM   9282  N  N   . GLY I  1 56  ? -32.556 8.989   63.967  1.00 64.49  ? 56  GLY Q N   1 
ATOM   9283  C  CA  . GLY I  1 56  ? -32.279 7.982   62.935  1.00 61.10  ? 56  GLY Q CA  1 
ATOM   9284  C  C   . GLY I  1 56  ? -30.907 8.120   62.288  1.00 57.73  ? 56  GLY Q C   1 
ATOM   9285  O  O   . GLY I  1 56  ? -29.940 8.565   62.924  1.00 58.20  ? 56  GLY Q O   1 
ATOM   9286  N  N   . ALA I  1 57  ? -30.826 7.761   61.010  1.00 54.61  ? 57  ALA Q N   1 
ATOM   9287  C  CA  . ALA I  1 57  ? -29.592 7.893   60.244  1.00 51.40  ? 57  ALA Q CA  1 
ATOM   9288  C  C   . ALA I  1 57  ? -29.098 9.345   60.094  1.00 51.12  ? 57  ALA Q C   1 
ATOM   9289  O  O   . ALA I  1 57  ? -27.913 9.563   59.798  1.00 49.28  ? 57  ALA Q O   1 
ATOM   9290  C  CB  . ALA I  1 57  ? -29.761 7.253   58.874  1.00 48.84  ? 57  ALA Q CB  1 
ATOM   9291  N  N   . THR I  1 58  ? -29.990 10.322  60.289  1.00 53.08  ? 58  THR Q N   1 
ATOM   9292  C  CA  . THR I  1 58  ? -29.651 11.745  60.160  1.00 53.41  ? 58  THR Q CA  1 
ATOM   9293  C  C   . THR I  1 58  ? -28.596 12.242  61.162  1.00 54.48  ? 58  THR Q C   1 
ATOM   9294  O  O   . THR I  1 58  ? -27.739 13.060  60.803  1.00 53.74  ? 58  THR Q O   1 
ATOM   9295  C  CB  . THR I  1 58  ? -30.906 12.634  60.298  1.00 56.23  ? 58  THR Q CB  1 
ATOM   9296  O  OG1 . THR I  1 58  ? -32.034 11.974  59.705  1.00 56.14  ? 58  THR Q OG1 1 
ATOM   9297  C  CG2 . THR I  1 58  ? -30.685 13.986  59.617  1.00 55.94  ? 58  THR Q CG2 1 
ATOM   9298  N  N   . SER I  1 59  ? -28.640 11.727  62.388  1.00 56.42  ? 59  SER Q N   1 
ATOM   9299  C  CA  . SER I  1 59  ? -27.727 12.153  63.457  1.00 58.08  ? 59  SER Q CA  1 
ATOM   9300  C  C   . SER I  1 59  ? -26.305 11.561  63.387  1.00 55.68  ? 59  SER Q C   1 
ATOM   9301  O  O   . SER I  1 59  ? -25.439 11.956  64.180  1.00 57.15  ? 59  SER Q O   1 
ATOM   9302  C  CB  . SER I  1 59  ? -28.343 11.827  64.820  1.00 61.89  ? 59  SER Q CB  1 
ATOM   9303  O  OG  . SER I  1 59  ? -28.767 10.475  64.863  1.00 61.48  ? 59  SER Q OG  1 
ATOM   9304  N  N   . ALA I  1 60  ? -26.065 10.633  62.454  1.00 52.32  ? 60  ALA Q N   1 
ATOM   9305  C  CA  . ALA I  1 60  ? -24.750 10.009  62.277  1.00 50.12  ? 60  ALA Q CA  1 
ATOM   9306  C  C   . ALA I  1 60  ? -23.687 10.941  61.687  1.00 48.48  ? 60  ALA Q C   1 
ATOM   9307  O  O   . ALA I  1 60  ? -22.515 10.565  61.613  1.00 47.30  ? 60  ALA Q O   1 
ATOM   9308  C  CB  . ALA I  1 60  ? -24.877 8.757   61.423  1.00 47.70  ? 60  ALA Q CB  1 
ATOM   9309  N  N   . GLY I  1 61  ? -24.091 12.130  61.239  1.00 48.63  ? 61  GLY Q N   1 
ATOM   9310  C  CA  . GLY I  1 61  ? -23.159 13.141  60.771  1.00 47.75  ? 61  GLY Q CA  1 
ATOM   9311  C  C   . GLY I  1 61  ? -22.640 12.814  59.387  1.00 44.25  ? 61  GLY Q C   1 
ATOM   9312  O  O   . GLY I  1 61  ? -23.209 11.956  58.692  1.00 42.70  ? 61  GLY Q O   1 
ATOM   9313  N  N   . PRO I  1 62  ? -21.546 13.478  58.974  1.00 43.21  ? 62  PRO Q N   1 
ATOM   9314  C  CA  . PRO I  1 62  ? -21.011 13.276  57.637  1.00 40.29  ? 62  PRO Q CA  1 
ATOM   9315  C  C   . PRO I  1 62  ? -20.299 11.923  57.495  1.00 38.37  ? 62  PRO Q C   1 
ATOM   9316  O  O   . PRO I  1 62  ? -20.303 11.119  58.433  1.00 39.23  ? 62  PRO Q O   1 
ATOM   9317  C  CB  . PRO I  1 62  ? -20.031 14.440  57.490  1.00 40.87  ? 62  PRO Q CB  1 
ATOM   9318  C  CG  . PRO I  1 62  ? -19.519 14.645  58.872  1.00 43.32  ? 62  PRO Q CG  1 
ATOM   9319  C  CD  . PRO I  1 62  ? -20.679 14.364  59.776  1.00 45.18  ? 62  PRO Q CD  1 
ATOM   9320  N  N   . HIS I  1 63  ? -19.727 11.664  56.321  1.00 35.94  ? 63  HIS Q N   1 
ATOM   9321  C  CA  . HIS I  1 63  ? -18.906 10.464  56.122  1.00 34.47  ? 63  HIS Q CA  1 
ATOM   9322  C  C   . HIS I  1 63  ? -17.699 10.509  57.046  1.00 35.47  ? 63  HIS Q C   1 
ATOM   9323  O  O   . HIS I  1 63  ? -17.127 11.578  57.270  1.00 36.43  ? 63  HIS Q O   1 
ATOM   9324  C  CB  . HIS I  1 63  ? -18.438 10.332  54.668  1.00 32.36  ? 63  HIS Q CB  1 
ATOM   9325  C  CG  . HIS I  1 63  ? -19.549 10.064  53.701  1.00 31.25  ? 63  HIS Q CG  1 
ATOM   9326  N  ND1 . HIS I  1 63  ? -19.365 10.066  52.340  1.00 29.73  ? 63  HIS Q ND1 1 
ATOM   9327  C  CD2 . HIS I  1 63  ? -20.866 9.819   53.901  1.00 31.75  ? 63  HIS Q CD2 1 
ATOM   9328  C  CE1 . HIS I  1 63  ? -20.510 9.802   51.739  1.00 29.41  ? 63  HIS Q CE1 1 
ATOM   9329  N  NE2 . HIS I  1 63  ? -21.442 9.657   52.666  1.00 30.55  ? 63  HIS Q NE2 1 
ATOM   9330  N  N   . PHE I  1 64  ? -17.326 9.350   57.581  1.00 35.52  ? 64  PHE Q N   1 
ATOM   9331  C  CA  . PHE I  1 64  ? -16.168 9.232   58.461  1.00 36.73  ? 64  PHE Q CA  1 
ATOM   9332  C  C   . PHE I  1 64  ? -14.916 9.681   57.706  1.00 35.86  ? 64  PHE Q C   1 
ATOM   9333  O  O   . PHE I  1 64  ? -14.512 9.046   56.721  1.00 34.19  ? 64  PHE Q O   1 
ATOM   9334  C  CB  . PHE I  1 64  ? -16.039 7.789   58.977  1.00 37.00  ? 64  PHE Q CB  1 
ATOM   9335  C  CG  . PHE I  1 64  ? -14.870 7.555   59.910  1.00 38.54  ? 64  PHE Q CG  1 
ATOM   9336  C  CD1 . PHE I  1 64  ? -14.531 8.474   60.906  1.00 40.61  ? 64  PHE Q CD1 1 
ATOM   9337  C  CD2 . PHE I  1 64  ? -14.126 6.383   59.811  1.00 38.25  ? 64  PHE Q CD2 1 
ATOM   9338  C  CE1 . PHE I  1 64  ? -13.455 8.241   61.752  1.00 42.32  ? 64  PHE Q CE1 1 
ATOM   9339  C  CE2 . PHE I  1 64  ? -13.056 6.142   60.668  1.00 39.93  ? 64  PHE Q CE2 1 
ATOM   9340  C  CZ  . PHE I  1 64  ? -12.724 7.070   61.642  1.00 41.94  ? 64  PHE Q CZ  1 
ATOM   9341  N  N   . ASN I  1 65  ? -14.336 10.789  58.171  1.00 37.26  ? 65  ASN Q N   1 
ATOM   9342  C  CA  . ASN I  1 65  ? -13.331 11.537  57.432  1.00 36.91  ? 65  ASN Q CA  1 
ATOM   9343  C  C   . ASN I  1 65  ? -12.244 12.088  58.368  1.00 39.18  ? 65  ASN Q C   1 
ATOM   9344  O  O   . ASN I  1 65  ? -12.052 13.302  58.456  1.00 40.39  ? 65  ASN Q O   1 
ATOM   9345  C  CB  . ASN I  1 65  ? -14.017 12.674  56.663  1.00 36.46  ? 65  ASN Q CB  1 
ATOM   9346  C  CG  . ASN I  1 65  ? -13.086 13.402  55.708  1.00 35.98  ? 65  ASN Q CG  1 
ATOM   9347  O  OD1 . ASN I  1 65  ? -12.098 12.845  55.216  1.00 35.18  ? 65  ASN Q OD1 1 
ATOM   9348  N  ND2 . ASN I  1 65  ? -13.418 14.654  55.415  1.00 36.67  ? 65  ASN Q ND2 1 
ATOM   9349  N  N   . PRO I  1 66  ? -11.515 11.192  59.061  1.00 40.08  ? 66  PRO Q N   1 
ATOM   9350  C  CA  . PRO I  1 66  ? -10.460 11.645  59.993  1.00 42.56  ? 66  PRO Q CA  1 
ATOM   9351  C  C   . PRO I  1 66  ? -9.279  12.404  59.352  1.00 42.82  ? 66  PRO Q C   1 
ATOM   9352  O  O   . PRO I  1 66  ? -8.610  13.163  60.051  1.00 45.04  ? 66  PRO Q O   1 
ATOM   9353  C  CB  . PRO I  1 66  ? -9.975  10.340  60.648  1.00 43.06  ? 66  PRO Q CB  1 
ATOM   9354  C  CG  . PRO I  1 66  ? -10.345 9.263   59.686  1.00 40.62  ? 66  PRO Q CG  1 
ATOM   9355  C  CD  . PRO I  1 66  ? -11.599 9.720   58.991  1.00 39.09  ? 66  PRO Q CD  1 
ATOM   9356  N  N   . LEU I  1 67  ? -9.036  12.213  58.050  1.00 40.89  ? 67  LEU Q N   1 
ATOM   9357  C  CA  . LEU I  1 67  ? -7.938  12.896  57.354  1.00 41.32  ? 67  LEU Q CA  1 
ATOM   9358  C  C   . LEU I  1 67  ? -8.358  14.193  56.644  1.00 41.35  ? 67  LEU Q C   1 
ATOM   9359  O  O   . LEU I  1 67  ? -7.525  14.834  56.009  1.00 41.81  ? 67  LEU Q O   1 
ATOM   9360  C  CB  . LEU I  1 67  ? -7.269  11.934  56.358  1.00 39.76  ? 67  LEU Q CB  1 
ATOM   9361  C  CG  . LEU I  1 67  ? -6.762  10.608  56.952  1.00 40.17  ? 67  LEU Q CG  1 
ATOM   9362  C  CD1 . LEU I  1 67  ? -6.055  9.767   55.896  1.00 39.08  ? 67  LEU Q CD1 1 
ATOM   9363  C  CD2 . LEU I  1 67  ? -5.836  10.832  58.139  1.00 42.78  ? 67  LEU Q CD2 1 
ATOM   9364  N  N   . SER I  1 68  ? -9.634  14.575  56.764  1.00 41.23  ? 68  SER Q N   1 
ATOM   9365  C  CA  . SER I  1 68  ? -10.184 15.805  56.160  1.00 41.55  ? 68  SER Q CA  1 
ATOM   9366  C  C   . SER I  1 68  ? -9.966  15.899  54.655  1.00 39.94  ? 68  SER Q C   1 
ATOM   9367  O  O   . SER I  1 68  ? -9.604  16.948  54.129  1.00 40.88  ? 68  SER Q O   1 
ATOM   9368  C  CB  . SER I  1 68  ? -9.649  17.052  56.862  1.00 44.43  ? 68  SER Q CB  1 
ATOM   9369  O  OG  . SER I  1 68  ? -9.957  17.008  58.239  1.00 46.40  ? 68  SER Q OG  1 
ATOM   9370  N  N   . ARG I  1 69  ? -10.218 14.786  53.978  1.00 37.94  ? 69  ARG Q N   1 
ATOM   9371  C  CA  . ARG I  1 69  ? -10.092 14.679  52.534  1.00 36.49  ? 69  ARG Q CA  1 
ATOM   9372  C  C   . ARG I  1 69  ? -11.464 14.897  51.900  1.00 35.18  ? 69  ARG Q C   1 
ATOM   9373  O  O   . ARG I  1 69  ? -12.483 14.902  52.595  1.00 35.28  ? 69  ARG Q O   1 
ATOM   9374  C  CB  . ARG I  1 69  ? -9.575  13.283  52.177  1.00 35.59  ? 69  ARG Q CB  1 
ATOM   9375  C  CG  . ARG I  1 69  ? -8.233  12.896  52.812  1.00 37.11  ? 69  ARG Q CG  1 
ATOM   9376  C  CD  . ARG I  1 69  ? -7.062  13.069  51.860  1.00 37.74  ? 69  ARG Q CD  1 
ATOM   9377  N  NE  . ARG I  1 69  ? -5.790  12.598  52.433  1.00 39.34  ? 69  ARG Q NE  1 
ATOM   9378  C  CZ  . ARG I  1 69  ? -5.138  11.464  52.122  1.00 39.30  ? 69  ARG Q CZ  1 
ATOM   9379  N  NH1 . ARG I  1 69  ? -5.585  10.600  51.202  1.00 37.83  ? 69  ARG Q NH1 1 
ATOM   9380  N  NH2 . ARG I  1 69  ? -3.984  11.192  52.738  1.00 41.09  ? 69  ARG Q NH2 1 
ATOM   9381  N  N   . LYS I  1 70  ? -11.493 15.094  50.588  1.00 34.11  ? 70  LYS Q N   1 
ATOM   9382  C  CA  . LYS I  1 70  ? -12.762 15.158  49.859  1.00 32.96  ? 70  LYS Q CA  1 
ATOM   9383  C  C   . LYS I  1 70  ? -13.294 13.743  49.610  1.00 31.02  ? 70  LYS Q C   1 
ATOM   9384  O  O   . LYS I  1 70  ? -12.553 12.763  49.688  1.00 30.47  ? 70  LYS Q O   1 
ATOM   9385  C  CB  . LYS I  1 70  ? -12.600 15.882  48.524  1.00 33.16  ? 70  LYS Q CB  1 
ATOM   9386  C  CG  . LYS I  1 70  ? -12.002 17.283  48.621  1.00 35.26  ? 70  LYS Q CG  1 
ATOM   9387  C  CD  . LYS I  1 70  ? -11.954 17.959  47.256  1.00 35.62  ? 70  LYS Q CD  1 
ATOM   9388  C  CE  . LYS I  1 70  ? -10.861 17.393  46.355  1.00 35.34  ? 70  LYS Q CE  1 
ATOM   9389  N  NZ  . LYS I  1 70  ? -11.364 17.196  44.964  0.75 34.65  ? 70  LYS Q NZ  1 
ATOM   9390  N  N   . HIS I  1 71  ? -14.590 13.658  49.316  1.00 30.08  ? 71  HIS Q N   1 
ATOM   9391  C  CA  . HIS I  1 71  ? -15.245 12.394  48.956  1.00 28.60  ? 71  HIS Q CA  1 
ATOM   9392  C  C   . HIS I  1 71  ? -14.660 11.792  47.678  1.00 27.65  ? 71  HIS Q C   1 
ATOM   9393  O  O   . HIS I  1 71  ? -14.381 12.518  46.731  1.00 27.92  ? 71  HIS Q O   1 
ATOM   9394  C  CB  . HIS I  1 71  ? -16.755 12.613  48.728  1.00 28.36  ? 71  HIS Q CB  1 
ATOM   9395  C  CG  . HIS I  1 71  ? -17.502 11.357  48.414  1.00 27.38  ? 71  HIS Q CG  1 
ATOM   9396  N  ND1 . HIS I  1 71  ? -17.758 10.386  49.355  1.00 27.38  ? 71  HIS Q ND1 1 
ATOM   9397  C  CD2 . HIS I  1 71  ? -18.016 10.898  47.249  1.00 26.74  ? 71  HIS Q CD2 1 
ATOM   9398  C  CE1 . HIS I  1 71  ? -18.419 9.392   48.788  1.00 26.79  ? 71  HIS Q CE1 1 
ATOM   9399  N  NE2 . HIS I  1 71  ? -18.586 9.678   47.510  1.00 26.37  ? 71  HIS Q NE2 1 
ATOM   9400  N  N   . GLY I  1 72  ? -14.541 10.467  47.646  1.00 26.85  ? 72  GLY Q N   1 
ATOM   9401  C  CA  . GLY I  1 72  ? -14.082 9.742   46.466  1.00 26.39  ? 72  GLY Q CA  1 
ATOM   9402  C  C   . GLY I  1 72  ? -14.641 8.335   46.412  1.00 25.83  ? 72  GLY Q C   1 
ATOM   9403  O  O   . GLY I  1 72  ? -15.495 7.976   47.208  1.00 25.75  ? 72  GLY Q O   1 
ATOM   9404  N  N   . GLY I  1 73  ? -14.161 7.543   45.461  1.00 25.82  ? 73  GLY Q N   1 
ATOM   9405  C  CA  . GLY I  1 73  ? -14.462 6.118   45.425  1.00 25.82  ? 73  GLY Q CA  1 
ATOM   9406  C  C   . GLY I  1 73  ? -13.462 5.344   46.280  1.00 26.40  ? 73  GLY Q C   1 
ATOM   9407  O  O   . GLY I  1 73  ? -12.403 5.880   46.637  1.00 26.71  ? 73  GLY Q O   1 
ATOM   9408  N  N   . PRO I  1 74  ? -13.766 4.066   46.582  1.00 26.70  ? 74  PRO Q N   1 
ATOM   9409  C  CA  . PRO I  1 74  ? -12.854 3.253   47.394  1.00 27.56  ? 74  PRO Q CA  1 
ATOM   9410  C  C   . PRO I  1 74  ? -11.437 3.124   46.810  1.00 28.39  ? 74  PRO Q C   1 
ATOM   9411  O  O   . PRO I  1 74  ? -10.459 3.080   47.561  1.00 28.99  ? 74  PRO Q O   1 
ATOM   9412  C  CB  . PRO I  1 74  ? -13.548 1.881   47.469  1.00 28.02  ? 74  PRO Q CB  1 
ATOM   9413  C  CG  . PRO I  1 74  ? -14.674 1.909   46.499  1.00 27.48  ? 74  PRO Q CG  1 
ATOM   9414  C  CD  . PRO I  1 74  ? -14.992 3.338   46.203  1.00 26.57  ? 74  PRO Q CD  1 
ATOM   9415  N  N   . LYS I  1 75  ? -11.341 3.110   45.482  1.00 28.60  ? 75  LYS Q N   1 
ATOM   9416  C  CA  . LYS I  1 75  ? -10.071 3.000   44.782  1.00 29.77  ? 75  LYS Q CA  1 
ATOM   9417  C  C   . LYS I  1 75  ? -9.228  4.282   44.775  1.00 29.81  ? 75  LYS Q C   1 
ATOM   9418  O  O   . LYS I  1 75  ? -8.059  4.231   44.397  1.00 30.82  ? 75  LYS Q O   1 
ATOM   9419  C  CB  . LYS I  1 75  ? -10.311 2.572   43.324  1.00 30.41  ? 75  LYS Q CB  1 
ATOM   9420  C  CG  . LYS I  1 75  ? -11.039 1.236   43.158  1.00 31.03  ? 75  LYS Q CG  1 
ATOM   9421  C  CD  . LYS I  1 75  ? -11.560 1.061   41.730  1.00 31.60  ? 75  LYS Q CD  1 
ATOM   9422  C  CE  . LYS I  1 75  ? -10.446 0.785   40.736  1.00 33.31  ? 75  LYS Q CE  1 
ATOM   9423  N  NZ  . LYS I  1 75  ? -10.959 0.685   39.340  1.00 34.15  ? 75  LYS Q NZ  1 
ATOM   9424  N  N   . ASP I  1 76  ? -9.808  5.425   45.135  1.00 28.96  ? 76  ASP Q N   1 
ATOM   9425  C  CA  . ASP I  1 76  ? -9.075  6.698   45.100  1.00 29.45  ? 76  ASP Q CA  1 
ATOM   9426  C  C   . ASP I  1 76  ? -8.192  6.905   46.337  1.00 30.19  ? 76  ASP Q C   1 
ATOM   9427  O  O   . ASP I  1 76  ? -8.549  6.482   47.452  1.00 30.06  ? 76  ASP Q O   1 
ATOM   9428  C  CB  . ASP I  1 76  ? -10.048 7.872   45.020  1.00 28.71  ? 76  ASP Q CB  1 
ATOM   9429  C  CG  . ASP I  1 76  ? -10.822 7.913   43.722  1.00 28.41  ? 76  ASP Q CG  1 
ATOM   9430  O  OD1 . ASP I  1 76  ? -10.200 7.890   42.653  1.00 29.27  ? 76  ASP Q OD1 1 
ATOM   9431  O  OD2 . ASP I  1 76  ? -12.060 8.024   43.770  1.00 27.77  ? 76  ASP Q OD2 1 
ATOM   9432  N  N   . GLU I  1 77  ? -7.076  7.603   46.148  1.00 31.19  ? 77  GLU Q N   1 
ATOM   9433  C  CA  . GLU I  1 77  ? -6.273  8.089   47.279  1.00 32.17  ? 77  GLU Q CA  1 
ATOM   9434  C  C   . GLU I  1 77  ? -7.014  9.235   47.990  1.00 31.71  ? 77  GLU Q C   1 
ATOM   9435  O  O   . GLU I  1 77  ? -7.036  9.288   49.217  1.00 32.11  ? 77  GLU Q O   1 
ATOM   9436  C  CB  . GLU I  1 77  ? -4.871  8.544   46.831  1.00 33.77  ? 77  GLU Q CB  1 
ATOM   9437  C  CG  . GLU I  1 77  ? -3.856  8.569   47.970  1.00 35.24  ? 77  GLU Q CG  1 
ATOM   9438  C  CD  . GLU I  1 77  ? -2.501  9.128   47.575  0.50 37.10  ? 77  GLU Q CD  1 
ATOM   9439  O  OE1 . GLU I  1 77  ? -2.200  9.223   46.365  0.50 37.47  ? 77  GLU Q OE1 1 
ATOM   9440  O  OE2 . GLU I  1 77  ? -1.723  9.470   48.490  0.50 38.51  ? 77  GLU Q OE2 1 
ATOM   9441  N  N   . GLU I  1 78  ? -7.608  10.145  47.217  1.00 31.20  ? 78  GLU Q N   1 
ATOM   9442  C  CA  . GLU I  1 78  ? -8.419  11.231  47.778  1.00 31.05  ? 78  GLU Q CA  1 
ATOM   9443  C  C   . GLU I  1 78  ? -9.829  10.677  48.030  1.00 29.59  ? 78  GLU Q C   1 
ATOM   9444  O  O   . GLU I  1 78  ? -10.654 10.614  47.123  1.00 28.75  ? 78  GLU Q O   1 
ATOM   9445  C  CB  . GLU I  1 78  ? -8.437  12.443  46.829  1.00 31.65  ? 78  GLU Q CB  1 
ATOM   9446  C  CG  . GLU I  1 78  ? -9.117  13.700  47.366  1.00 32.23  ? 78  GLU Q CG  1 
ATOM   9447  C  CD  . GLU I  1 78  ? -8.401  14.342  48.549  1.00 33.85  ? 78  GLU Q CD  1 
ATOM   9448  O  OE1 . GLU I  1 78  ? -7.224  14.028  48.813  1.00 34.94  ? 78  GLU Q OE1 1 
ATOM   9449  O  OE2 . GLU I  1 78  ? -9.024  15.179  49.237  1.00 34.57  ? 78  GLU Q OE2 1 
ATOM   9450  N  N   . ARG I  1 79  ? -10.058 10.222  49.259  1.00 29.47  ? 79  ARG Q N   1 
ATOM   9451  C  CA  . ARG I  1 79  ? -11.353 9.679   49.688  1.00 28.55  ? 79  ARG Q CA  1 
ATOM   9452  C  C   . ARG I  1 79  ? -11.507 9.880   51.193  1.00 29.29  ? 79  ARG Q C   1 
ATOM   9453  O  O   . ARG I  1 79  ? -10.522 10.060  51.912  1.00 30.35  ? 79  ARG Q O   1 
ATOM   9454  C  CB  . ARG I  1 79  ? -11.459 8.180   49.381  1.00 27.94  ? 79  ARG Q CB  1 
ATOM   9455  C  CG  . ARG I  1 79  ? -10.348 7.340   50.019  1.00 28.83  ? 79  ARG Q CG  1 
ATOM   9456  C  CD  . ARG I  1 79  ? -10.568 5.852   49.830  1.00 28.62  ? 79  ARG Q CD  1 
ATOM   9457  N  NE  . ARG I  1 79  ? -11.413 5.305   50.892  1.00 28.75  ? 79  ARG Q NE  1 
ATOM   9458  C  CZ  . ARG I  1 79  ? -11.648 4.009   51.096  1.00 29.02  ? 79  ARG Q CZ  1 
ATOM   9459  N  NH1 . ARG I  1 79  ? -11.130 3.081   50.290  1.00 29.18  ? 79  ARG Q NH1 1 
ATOM   9460  N  NH2 . ARG I  1 79  ? -12.423 3.643   52.119  1.00 29.45  ? 79  ARG Q NH2 1 
ATOM   9461  N  N   . HIS I  1 80  ? -12.748 9.829   51.651  1.00 28.84  ? 80  HIS Q N   1 
ATOM   9462  C  CA  . HIS I  1 80  ? -13.060 9.698   53.072  1.00 29.80  ? 80  HIS Q CA  1 
ATOM   9463  C  C   . HIS I  1 80  ? -12.722 8.255   53.469  1.00 29.72  ? 80  HIS Q C   1 
ATOM   9464  O  O   . HIS I  1 80  ? -12.848 7.364   52.642  1.00 28.71  ? 80  HIS Q O   1 
ATOM   9465  C  CB  . HIS I  1 80  ? -14.559 9.984   53.342  1.00 29.78  ? 80  HIS Q CB  1 
ATOM   9466  C  CG  . HIS I  1 80  ? -15.023 11.337  52.892  1.00 30.02  ? 80  HIS Q CG  1 
ATOM   9467  N  ND1 . HIS I  1 80  ? -16.295 11.586  52.406  1.00 29.69  ? 80  HIS Q ND1 1 
ATOM   9468  C  CD2 . HIS I  1 80  ? -14.378 12.524  52.872  1.00 30.95  ? 80  HIS Q CD2 1 
ATOM   9469  C  CE1 . HIS I  1 80  ? -16.405 12.871  52.119  1.00 30.32  ? 80  HIS Q CE1 1 
ATOM   9470  N  NE2 . HIS I  1 80  ? -15.256 13.463  52.392  1.00 31.08  ? 80  HIS Q NE2 1 
ATOM   9471  N  N   . VAL I  1 81  ? -12.297 8.021   54.716  1.00 31.02  ? 81  VAL Q N   1 
ATOM   9472  C  CA  . VAL I  1 81  ? -12.103 6.651   55.217  1.00 31.42  ? 81  VAL Q CA  1 
ATOM   9473  C  C   . VAL I  1 81  ? -13.379 5.816   55.025  1.00 30.72  ? 81  VAL Q C   1 
ATOM   9474  O  O   . VAL I  1 81  ? -13.315 4.662   54.589  1.00 30.38  ? 81  VAL Q O   1 
ATOM   9475  C  CB  . VAL I  1 81  ? -11.638 6.623   56.699  1.00 33.42  ? 81  VAL Q CB  1 
ATOM   9476  C  CG1 . VAL I  1 81  ? -11.769 5.230   57.315  1.00 34.17  ? 81  VAL Q CG1 1 
ATOM   9477  C  CG2 . VAL I  1 81  ? -10.197 7.101   56.808  1.00 34.36  ? 81  VAL Q CG2 1 
ATOM   9478  N  N   . GLY I  1 82  ? -14.533 6.414   55.307  1.00 30.73  ? 82  GLY Q N   1 
ATOM   9479  C  CA  . GLY I  1 82  ? -15.814 5.727   55.154  1.00 30.39  ? 82  GLY Q CA  1 
ATOM   9480  C  C   . GLY I  1 82  ? -16.364 5.508   53.747  1.00 28.85  ? 82  GLY Q C   1 
ATOM   9481  O  O   . GLY I  1 82  ? -17.480 4.980   53.607  1.00 28.78  ? 82  GLY Q O   1 
ATOM   9482  N  N   . ASP I  1 83  ? -15.619 5.894   52.712  1.00 27.90  ? 83  ASP Q N   1 
ATOM   9483  C  CA  . ASP I  1 83  ? -16.099 5.789   51.322  1.00 26.78  ? 83  ASP Q CA  1 
ATOM   9484  C  C   . ASP I  1 83  ? -15.922 4.390   50.739  1.00 26.75  ? 83  ASP Q C   1 
ATOM   9485  O  O   . ASP I  1 83  ? -14.887 4.091   50.152  1.00 26.78  ? 83  ASP Q O   1 
ATOM   9486  C  CB  . ASP I  1 83  ? -15.385 6.809   50.432  1.00 26.17  ? 83  ASP Q CB  1 
ATOM   9487  C  CG  . ASP I  1 83  ? -15.812 8.240   50.708  1.00 26.37  ? 83  ASP Q CG  1 
ATOM   9488  O  OD1 . ASP I  1 83  ? -16.909 8.495   51.337  1.00 26.67  ? 83  ASP Q OD1 1 
ATOM   9489  O  OD2 . ASP I  1 83  ? -15.045 9.134   50.261  1.00 26.24  ? 83  ASP Q OD2 1 
ATOM   9490  N  N   . LEU I  1 84  ? -16.938 3.545   50.887  1.00 27.13  ? 84  LEU Q N   1 
ATOM   9491  C  CA  . LEU I  1 84  ? -16.893 2.179   50.352  1.00 27.51  ? 84  LEU Q CA  1 
ATOM   9492  C  C   . LEU I  1 84  ? -17.555 2.022   48.971  1.00 26.99  ? 84  LEU Q C   1 
ATOM   9493  O  O   . LEU I  1 84  ? -17.666 0.901   48.464  1.00 27.61  ? 84  LEU Q O   1 
ATOM   9494  C  CB  . LEU I  1 84  ? -17.484 1.190   51.365  1.00 28.73  ? 84  LEU Q CB  1 
ATOM   9495  C  CG  . LEU I  1 84  ? -16.765 1.106   52.714  1.00 29.80  ? 84  LEU Q CG  1 
ATOM   9496  C  CD1 . LEU I  1 84  ? -17.513 0.199   53.678  1.00 31.29  ? 84  LEU Q CD1 1 
ATOM   9497  C  CD2 . LEU I  1 84  ? -15.327 0.618   52.557  1.00 30.18  ? 84  LEU Q CD2 1 
ATOM   9498  N  N   . GLY I  1 85  ? -17.985 3.128   48.356  1.00 26.20  ? 85  GLY Q N   1 
ATOM   9499  C  CA  . GLY I  1 85  ? -18.460 3.099   46.987  1.00 25.90  ? 85  GLY Q CA  1 
ATOM   9500  C  C   . GLY I  1 85  ? -19.924 2.735   46.883  1.00 26.23  ? 85  GLY Q C   1 
ATOM   9501  O  O   . GLY I  1 85  ? -20.747 3.257   47.638  1.00 26.36  ? 85  GLY Q O   1 
ATOM   9502  N  N   . ASN I  1 86  ? -20.241 1.844   45.943  1.00 26.66  ? 86  ASN Q N   1 
ATOM   9503  C  CA  . ASN I  1 86  ? -21.611 1.416   45.702  1.00 27.31  ? 86  ASN Q CA  1 
ATOM   9504  C  C   . ASN I  1 86  ? -21.782 -0.057  45.963  1.00 28.56  ? 86  ASN Q C   1 
ATOM   9505  O  O   . ASN I  1 86  ? -20.830 -0.837  45.884  1.00 28.93  ? 86  ASN Q O   1 
ATOM   9506  C  CB  . ASN I  1 86  ? -22.009 1.686   44.250  1.00 27.28  ? 86  ASN Q CB  1 
ATOM   9507  C  CG  . ASN I  1 86  ? -22.219 3.150   43.974  1.00 26.51  ? 86  ASN Q CG  1 
ATOM   9508  O  OD1 . ASN I  1 86  ? -23.087 3.781   44.585  1.00 26.53  ? 86  ASN Q OD1 1 
ATOM   9509  N  ND2 . ASN I  1 86  ? -21.427 3.707   43.065  1.00 26.05  ? 86  ASN Q ND2 1 
ATOM   9510  N  N   . VAL I  1 87  ? -23.024 -0.413  46.266  1.00 29.43  ? 87  VAL Q N   1 
ATOM   9511  C  CA  . VAL I  1 87  ? -23.487 -1.790  46.244  1.00 31.05  ? 87  VAL Q CA  1 
ATOM   9512  C  C   . VAL I  1 87  ? -24.537 -1.835  45.145  1.00 31.62  ? 87  VAL Q C   1 
ATOM   9513  O  O   . VAL I  1 87  ? -25.092 -0.798  44.770  1.00 30.87  ? 87  VAL Q O   1 
ATOM   9514  C  CB  . VAL I  1 87  ? -24.020 -2.263  47.621  1.00 32.10  ? 87  VAL Q CB  1 
ATOM   9515  C  CG1 . VAL I  1 87  ? -22.896 -2.223  48.646  1.00 31.83  ? 87  VAL Q CG1 1 
ATOM   9516  C  CG2 . VAL I  1 87  ? -25.198 -1.430  48.109  1.00 32.10  ? 87  VAL Q CG2 1 
ATOM   9517  N  N   . THR I  1 88  ? -24.779 -3.025  44.612  1.00 33.21  ? 88  THR Q N   1 
ATOM   9518  C  CA  . THR I  1 88  ? -25.689 -3.205  43.497  1.00 34.23  ? 88  THR Q CA  1 
ATOM   9519  C  C   . THR I  1 88  ? -26.840 -4.096  43.937  1.00 36.19  ? 88  THR Q C   1 
ATOM   9520  O  O   . THR I  1 88  ? -26.618 -5.227  44.359  1.00 37.54  ? 88  THR Q O   1 
ATOM   9521  C  CB  . THR I  1 88  ? -24.969 -3.828  42.279  1.00 35.00  ? 88  THR Q CB  1 
ATOM   9522  O  OG1 . THR I  1 88  ? -23.947 -2.936  41.814  1.00 33.49  ? 88  THR Q OG1 1 
ATOM   9523  C  CG2 . THR I  1 88  ? -25.953 -4.100  41.125  1.00 36.51  ? 88  THR Q CG2 1 
ATOM   9524  N  N   . ALA I  1 89  ? -28.062 -3.572  43.835  1.00 36.60  ? 89  ALA Q N   1 
ATOM   9525  C  CA  . ALA I  1 89  ? -29.269 -4.360  44.042  1.00 38.84  ? 89  ALA Q CA  1 
ATOM   9526  C  C   . ALA I  1 89  ? -29.731 -4.955  42.721  1.00 40.53  ? 89  ALA Q C   1 
ATOM   9527  O  O   . ALA I  1 89  ? -29.811 -4.257  41.717  1.00 39.96  ? 89  ALA Q O   1 
ATOM   9528  C  CB  . ALA I  1 89  ? -30.373 -3.503  44.641  1.00 38.79  ? 89  ALA Q CB  1 
ATOM   9529  N  N   . ASP I  1 90  ? -30.066 -6.243  42.744  1.00 43.00  ? 90  ASP Q N   1 
ATOM   9530  C  CA  . ASP I  1 90  ? -30.546 -6.951  41.563  1.00 45.22  ? 90  ASP Q CA  1 
ATOM   9531  C  C   . ASP I  1 90  ? -32.026 -6.623  41.299  1.00 46.55  ? 90  ASP Q C   1 
ATOM   9532  O  O   . ASP I  1 90  ? -32.630 -5.800  42.000  1.00 45.68  ? 90  ASP Q O   1 
ATOM   9533  C  CB  . ASP I  1 90  ? -30.272 -8.470  41.687  1.00 47.65  ? 90  ASP Q CB  1 
ATOM   9534  C  CG  . ASP I  1 90  ? -31.107 -9.173  42.779  1.00 49.48  ? 90  ASP Q CG  1 
ATOM   9535  O  OD1 . ASP I  1 90  ? -32.138 -8.635  43.251  1.00 49.47  ? 90  ASP Q OD1 1 
ATOM   9536  O  OD2 . ASP I  1 90  ? -30.712 -10.301 43.157  1.00 51.20  ? 90  ASP Q OD2 1 
ATOM   9537  N  N   . LYS I  1 91  ? -32.604 -7.271  40.292  1.00 48.99  ? 91  LYS Q N   1 
ATOM   9538  C  CA  . LYS I  1 91  ? -33.996 -7.035  39.899  1.00 50.69  ? 91  LYS Q CA  1 
ATOM   9539  C  C   . LYS I  1 91  ? -35.037 -7.353  40.989  1.00 52.12  ? 91  LYS Q C   1 
ATOM   9540  O  O   . LYS I  1 91  ? -36.142 -6.806  40.969  1.00 52.86  ? 91  LYS Q O   1 
ATOM   9541  C  CB  . LYS I  1 91  ? -34.310 -7.830  38.627  1.00 53.51  ? 91  LYS Q CB  1 
ATOM   9542  C  CG  . LYS I  1 91  ? -35.611 -7.427  37.957  1.00 55.23  ? 91  LYS Q CG  1 
ATOM   9543  C  CD  . LYS I  1 91  ? -35.542 -7.544  36.439  1.00 56.77  ? 91  LYS Q CD  1 
ATOM   9544  C  CE  . LYS I  1 91  ? -36.651 -6.743  35.771  1.00 57.69  ? 91  LYS Q CE  1 
ATOM   9545  N  NZ  . LYS I  1 91  ? -36.475 -5.270  35.959  1.00 54.74  ? 91  LYS Q NZ  1 
ATOM   9546  N  N   . ASP I  1 92  ? -34.676 -8.231  41.928  1.00 52.77  ? 92  ASP Q N   1 
ATOM   9547  C  CA  . ASP I  1 92  ? -35.529 -8.582  43.070  1.00 54.33  ? 92  ASP Q CA  1 
ATOM   9548  C  C   . ASP I  1 92  ? -35.241 -7.772  44.340  1.00 52.15  ? 92  ASP Q C   1 
ATOM   9549  O  O   . ASP I  1 92  ? -35.699 -8.141  45.428  1.00 53.49  ? 92  ASP Q O   1 
ATOM   9550  C  CB  . ASP I  1 92  ? -35.396 -10.081 43.342  1.00 57.03  ? 92  ASP Q CB  1 
ATOM   9551  C  CG  . ASP I  1 92  ? -35.826 -10.913 42.153  1.00 59.86  ? 92  ASP Q CG  1 
ATOM   9552  O  OD1 . ASP I  1 92  ? -37.044 -10.927 41.845  1.00 61.99  ? 92  ASP Q OD1 1 
ATOM   9553  O  OD2 . ASP I  1 92  ? -34.952 -11.544 41.522  1.00 60.23  ? 92  ASP Q OD2 1 
ATOM   9554  N  N   . GLY I  1 93  ? -34.501 -6.667  44.200  1.00 49.11  ? 93  GLY Q N   1 
ATOM   9555  C  CA  . GLY I  1 93  ? -34.239 -5.746  45.297  1.00 47.20  ? 93  GLY Q CA  1 
ATOM   9556  C  C   . GLY I  1 93  ? -33.206 -6.199  46.313  1.00 46.51  ? 93  GLY Q C   1 
ATOM   9557  O  O   . GLY I  1 93  ? -33.139 -5.637  47.408  1.00 45.75  ? 93  GLY Q O   1 
ATOM   9558  N  N   . VAL I  1 94  ? -32.388 -7.187  45.943  1.00 46.97  ? 94  VAL Q N   1 
ATOM   9559  C  CA  . VAL I  1 94  ? -31.397 -7.774  46.842  1.00 46.86  ? 94  VAL Q CA  1 
ATOM   9560  C  C   . VAL I  1 94  ? -29.993 -7.376  46.395  1.00 44.54  ? 94  VAL Q C   1 
ATOM   9561  O  O   . VAL I  1 94  ? -29.589 -7.664  45.264  1.00 44.59  ? 94  VAL Q O   1 
ATOM   9562  C  CB  . VAL I  1 94  ? -31.506 -9.313  46.869  1.00 49.82  ? 94  VAL Q CB  1 
ATOM   9563  C  CG1 . VAL I  1 94  ? -30.445 -9.924  47.788  1.00 49.94  ? 94  VAL Q CG1 1 
ATOM   9564  C  CG2 . VAL I  1 94  ? -32.905 -9.728  47.310  1.00 52.52  ? 94  VAL Q CG2 1 
ATOM   9565  N  N   . ALA I  1 95  ? -29.264 -6.703  47.283  1.00 42.81  ? 95  ALA Q N   1 
ATOM   9566  C  CA  . ALA I  1 95  ? -27.842 -6.458  47.097  1.00 41.04  ? 95  ALA Q CA  1 
ATOM   9567  C  C   . ALA I  1 95  ? -27.054 -7.425  47.980  1.00 42.18  ? 95  ALA Q C   1 
ATOM   9568  O  O   . ALA I  1 95  ? -27.061 -7.299  49.206  1.00 42.29  ? 95  ALA Q O   1 
ATOM   9569  C  CB  . ALA I  1 95  ? -27.501 -5.018  47.429  1.00 38.63  ? 95  ALA Q CB  1 
ATOM   9570  N  N   . ASP I  1 96  ? -26.420 -8.410  47.341  1.00 43.37  ? 96  ASP Q N   1 
ATOM   9571  C  CA  . ASP I  1 96  ? -25.457 -9.293  47.998  1.00 44.53  ? 96  ASP Q CA  1 
ATOM   9572  C  C   . ASP I  1 96  ? -24.101 -8.591  48.048  1.00 42.44  ? 96  ASP Q C   1 
ATOM   9573  O  O   . ASP I  1 96  ? -23.303 -8.688  47.115  1.00 42.10  ? 96  ASP Q O   1 
ATOM   9574  C  CB  . ASP I  1 96  ? -25.350 -10.629 47.262  1.00 47.06  ? 96  ASP Q CB  1 
ATOM   9575  C  CG  . ASP I  1 96  ? -26.606 -11.482 47.418  1.00 49.83  ? 96  ASP Q CG  1 
ATOM   9576  O  OD1 . ASP I  1 96  ? -26.910 -11.895 48.564  1.00 51.21  ? 96  ASP Q OD1 1 
ATOM   9577  O  OD2 . ASP I  1 96  ? -27.285 -11.738 46.397  1.00 50.88  ? 96  ASP Q OD2 1 
ATOM   9578  N  N   . VAL I  1 97  ? -23.859 -7.889  49.152  1.00 41.37  ? 97  VAL Q N   1 
ATOM   9579  C  CA  . VAL I  1 97  ? -22.678 -7.049  49.307  1.00 39.46  ? 97  VAL Q CA  1 
ATOM   9580  C  C   . VAL I  1 97  ? -21.444 -7.932  49.473  1.00 40.55  ? 97  VAL Q C   1 
ATOM   9581  O  O   . VAL I  1 97  ? -21.460 -8.887  50.240  1.00 42.55  ? 97  VAL Q O   1 
ATOM   9582  C  CB  . VAL I  1 97  ? -22.814 -6.093  50.512  1.00 38.55  ? 97  VAL Q CB  1 
ATOM   9583  C  CG1 . VAL I  1 97  ? -21.546 -5.256  50.694  1.00 36.90  ? 97  VAL Q CG1 1 
ATOM   9584  C  CG2 . VAL I  1 97  ? -24.038 -5.199  50.333  1.00 37.82  ? 97  VAL Q CG2 1 
ATOM   9585  N  N   . SER I  1 98  ? -20.401 -7.635  48.705  1.00 39.57  ? 98  SER Q N   1 
ATOM   9586  C  CA  . SER I  1 98  ? -19.107 -8.306  48.848  1.00 40.64  ? 98  SER Q CA  1 
ATOM   9587  C  C   . SER I  1 98  ? -18.015 -7.333  48.433  1.00 38.80  ? 98  SER Q C   1 
ATOM   9588  O  O   . SER I  1 98  ? -17.813 -7.081  47.248  1.00 38.31  ? 98  SER Q O   1 
ATOM   9589  C  CB  . SER I  1 98  ? -19.043 -9.590  48.024  1.00 42.95  ? 98  SER Q CB  1 
ATOM   9590  O  OG  . SER I  1 98  ? -17.900 -10.340 48.395  1.00 44.50  ? 98  SER Q OG  1 
ATOM   9591  N  N   . ILE I  1 99  ? -17.359 -6.755  49.432  1.00 38.08  ? 99  ILE Q N   1 
ATOM   9592  C  CA  . ILE I  1 99  ? -16.373 -5.698  49.244  1.00 36.46  ? 99  ILE Q CA  1 
ATOM   9593  C  C   . ILE I  1 99  ? -15.133 -6.060  50.057  1.00 37.42  ? 99  ILE Q C   1 
ATOM   9594  O  O   . ILE I  1 99  ? -15.243 -6.715  51.102  1.00 38.81  ? 99  ILE Q O   1 
ATOM   9595  C  CB  . ILE I  1 99  ? -16.951 -4.334  49.701  1.00 34.66  ? 99  ILE Q CB  1 
ATOM   9596  C  CG1 . ILE I  1 99  ? -18.007 -3.842  48.704  1.00 33.73  ? 99  ILE Q CG1 1 
ATOM   9597  C  CG2 . ILE I  1 99  ? -15.863 -3.267  49.820  1.00 33.56  ? 99  ILE Q CG2 1 
ATOM   9598  C  CD1 . ILE I  1 99  ? -18.862 -2.701  49.226  1.00 32.55  ? 99  ILE Q CD1 1 
ATOM   9599  N  N   . GLU I  1 100 ? -13.961 -5.654  49.560  1.00 36.92  ? 100 GLU Q N   1 
ATOM   9600  C  CA  . GLU I  1 100 ? -12.719 -5.694  50.334  1.00 37.69  ? 100 GLU Q CA  1 
ATOM   9601  C  C   . GLU I  1 100 ? -12.075 -4.307  50.304  1.00 35.91  ? 100 GLU Q C   1 
ATOM   9602  O  O   . GLU I  1 100 ? -11.826 -3.759  49.234  1.00 34.93  ? 100 GLU Q O   1 
ATOM   9603  C  CB  . GLU I  1 100 ? -11.758 -6.742  49.780  1.00 39.76  ? 100 GLU Q CB  1 
ATOM   9604  C  CG  . GLU I  1 100 ? -10.520 -6.941  50.644  1.00 41.21  ? 100 GLU Q CG  1 
ATOM   9605  C  CD  . GLU I  1 100 ? -9.533  -7.922  50.053  1.00 43.50  ? 100 GLU Q CD  1 
ATOM   9606  O  OE1 . GLU I  1 100 ? -9.759  -9.146  50.184  1.00 45.69  ? 100 GLU Q OE1 1 
ATOM   9607  O  OE2 . GLU I  1 100 ? -8.515  -7.461  49.480  1.00 43.51  ? 100 GLU Q OE2 1 
ATOM   9608  N  N   . ASP I  1 101 ? -11.808 -3.748  51.481  1.00 35.71  ? 101 ASP Q N   1 
ATOM   9609  C  CA  . ASP I  1 101 ? -11.218 -2.418  51.591  1.00 34.44  ? 101 ASP Q CA  1 
ATOM   9610  C  C   . ASP I  1 101 ? -10.060 -2.400  52.588  1.00 35.61  ? 101 ASP Q C   1 
ATOM   9611  O  O   . ASP I  1 101 ? -10.121 -3.046  53.639  1.00 37.03  ? 101 ASP Q O   1 
ATOM   9612  C  CB  . ASP I  1 101 ? -12.275 -1.413  52.028  1.00 33.13  ? 101 ASP Q CB  1 
ATOM   9613  C  CG  . ASP I  1 101 ? -11.819 0.010   51.845  1.00 32.04  ? 101 ASP Q CG  1 
ATOM   9614  O  OD1 . ASP I  1 101 ? -11.742 0.444   50.677  1.00 31.24  ? 101 ASP Q OD1 1 
ATOM   9615  O  OD2 . ASP I  1 101 ? -11.513 0.690   52.849  1.00 32.36  ? 101 ASP Q OD2 1 
ATOM   9616  N  N   . SER I  1 102 ? -9.029  -1.629  52.260  1.00 35.21  ? 102 SER Q N   1 
ATOM   9617  C  CA  . SER I  1 102 ? -7.814  -1.542  53.063  1.00 36.55  ? 102 SER Q CA  1 
ATOM   9618  C  C   . SER I  1 102 ? -7.638  -0.196  53.762  1.00 35.89  ? 102 SER Q C   1 
ATOM   9619  O  O   . SER I  1 102 ? -6.622  0.021   54.402  1.00 37.18  ? 102 SER Q O   1 
ATOM   9620  C  CB  . SER I  1 102 ? -6.611  -1.835  52.173  1.00 37.46  ? 102 SER Q CB  1 
ATOM   9621  O  OG  . SER I  1 102 ? -6.612  -3.204  51.814  1.00 38.87  ? 102 SER Q OG  1 
ATOM   9622  N  N   . VAL I  1 103 ? -8.618  0.699   53.648  1.00 34.14  ? 103 VAL Q N   1 
ATOM   9623  C  CA  . VAL I  1 103 ? -8.564  2.008   54.300  1.00 33.86  ? 103 VAL Q CA  1 
ATOM   9624  C  C   . VAL I  1 103 ? -9.380  1.996   55.603  1.00 34.47  ? 103 VAL Q C   1 
ATOM   9625  O  O   . VAL I  1 103 ? -8.921  2.515   56.620  1.00 35.67  ? 103 VAL Q O   1 
ATOM   9626  C  CB  . VAL I  1 103 ? -9.029  3.125   53.348  1.00 32.16  ? 103 VAL Q CB  1 
ATOM   9627  C  CG1 . VAL I  1 103 ? -9.082  4.466   54.069  1.00 32.34  ? 103 VAL Q CG1 1 
ATOM   9628  C  CG2 . VAL I  1 103 ? -8.089  3.203   52.147  1.00 32.02  ? 103 VAL Q CG2 1 
ATOM   9629  N  N   . ILE I  1 104 ? -10.588 1.426   55.569  1.00 33.88  ? 104 ILE Q N   1 
ATOM   9630  C  CA  . ILE I  1 104 ? -11.304 1.130   56.814  1.00 35.02  ? 104 ILE Q CA  1 
ATOM   9631  C  C   . ILE I  1 104 ? -10.509 0.094   57.615  1.00 37.04  ? 104 ILE Q C   1 
ATOM   9632  O  O   . ILE I  1 104 ? -9.792  -0.730  57.039  1.00 37.38  ? 104 ILE Q O   1 
ATOM   9633  C  CB  . ILE I  1 104 ? -12.755 0.638   56.604  1.00 34.43  ? 104 ILE Q CB  1 
ATOM   9634  C  CG1 . ILE I  1 104 ? -12.827 -0.622  55.736  1.00 34.29  ? 104 ILE Q CG1 1 
ATOM   9635  C  CG2 . ILE I  1 104 ? -13.603 1.745   55.999  1.00 32.82  ? 104 ILE Q CG2 1 
ATOM   9636  C  CD1 . ILE I  1 104 ? -14.102 -1.401  55.924  1.00 34.77  ? 104 ILE Q CD1 1 
ATOM   9637  N  N   . SER I  1 105 ? -10.622 0.167   58.932  1.00 38.65  ? 105 SER Q N   1 
ATOM   9638  C  CA  . SER I  1 105 ? -10.032 -0.820  59.823  1.00 40.99  ? 105 SER Q CA  1 
ATOM   9639  C  C   . SER I  1 105 ? -10.976 -1.124  60.991  1.00 42.58  ? 105 SER Q C   1 
ATOM   9640  O  O   . SER I  1 105 ? -11.938 -0.395  61.227  1.00 42.03  ? 105 SER Q O   1 
ATOM   9641  C  CB  . SER I  1 105 ? -8.697  -0.309  60.353  1.00 42.28  ? 105 SER Q CB  1 
ATOM   9642  O  OG  . SER I  1 105 ? -7.989  -1.354  60.980  1.00 44.57  ? 105 SER Q OG  1 
ATOM   9643  N  N   . LEU I  1 106 ? -10.695 -2.218  61.691  1.00 44.83  ? 106 LEU Q N   1 
ATOM   9644  C  CA  . LEU I  1 106 ? -11.376 -2.563  62.942  1.00 47.10  ? 106 LEU Q CA  1 
ATOM   9645  C  C   . LEU I  1 106 ? -10.490 -2.290  64.175  1.00 49.67  ? 106 LEU Q C   1 
ATOM   9646  O  O   . LEU I  1 106 ? -10.791 -2.765  65.268  1.00 52.19  ? 106 LEU Q O   1 
ATOM   9647  C  CB  . LEU I  1 106 ? -11.844 -4.024  62.898  1.00 48.30  ? 106 LEU Q CB  1 
ATOM   9648  C  CG  . LEU I  1 106 ? -12.769 -4.391  61.731  1.00 46.31  ? 106 LEU Q CG  1 
ATOM   9649  C  CD1 . LEU I  1 106 ? -13.172 -5.852  61.810  1.00 48.15  ? 106 LEU Q CD1 1 
ATOM   9650  C  CD2 . LEU I  1 106 ? -14.005 -3.503  61.687  1.00 44.95  ? 106 LEU Q CD2 1 
ATOM   9651  N  N   . SER I  1 107 ? -9.417  -1.517  63.988  1.00 49.26  ? 107 SER Q N   1 
ATOM   9652  C  CA  . SER I  1 107 ? -8.632  -0.965  65.097  1.00 51.67  ? 107 SER Q CA  1 
ATOM   9653  C  C   . SER I  1 107 ? -7.829  0.257   64.637  1.00 50.48  ? 107 SER Q C   1 
ATOM   9654  O  O   . SER I  1 107 ? -7.775  0.560   63.445  1.00 47.94  ? 107 SER Q O   1 
ATOM   9655  C  CB  . SER I  1 107 ? -7.691  -2.023  65.672  1.00 54.38  ? 107 SER Q CB  1 
ATOM   9656  O  OG  . SER I  1 107 ? -6.706  -2.386  64.724  1.00 53.54  ? 107 SER Q OG  1 
ATOM   9657  N  N   . GLY I  1 108 ? -7.226  0.961   65.590  1.00 52.59  ? 108 GLY Q N   1 
ATOM   9658  C  CA  . GLY I  1 108 ? -6.457  2.170   65.291  1.00 52.09  ? 108 GLY Q CA  1 
ATOM   9659  C  C   . GLY I  1 108 ? -7.328  3.363   64.938  1.00 50.34  ? 108 GLY Q C   1 
ATOM   9660  O  O   . GLY I  1 108 ? -8.536  3.367   65.196  1.00 50.07  ? 108 GLY Q O   1 
ATOM   9661  N  N   . ASP I  1 109 ? -6.712  4.369   64.325  1.00 49.41  ? 109 ASP Q N   1 
ATOM   9662  C  CA  . ASP I  1 109 ? -7.371  5.651   64.056  1.00 48.35  ? 109 ASP Q CA  1 
ATOM   9663  C  C   . ASP I  1 109 ? -8.534  5.559   63.077  1.00 45.54  ? 109 ASP Q C   1 
ATOM   9664  O  O   . ASP I  1 109 ? -9.484  6.334   63.187  1.00 45.30  ? 109 ASP Q O   1 
ATOM   9665  C  CB  . ASP I  1 109 ? -6.365  6.683   63.527  1.00 48.23  ? 109 ASP Q CB  1 
ATOM   9666  C  CG  . ASP I  1 109 ? -5.345  7.095   64.564  1.00 51.41  ? 109 ASP Q CG  1 
ATOM   9667  O  OD1 . ASP I  1 109 ? -5.667  7.120   65.768  1.00 53.83  ? 109 ASP Q OD1 1 
ATOM   9668  O  OD2 . ASP I  1 109 ? -4.206  7.407   64.170  1.00 51.85  ? 109 ASP Q OD2 1 
ATOM   9669  N  N   . HIS I  1 110 ? -8.453  4.615   62.136  1.00 43.77  ? 110 HIS Q N   1 
ATOM   9670  C  CA  . HIS I  1 110 ? -9.459  4.442   61.090  1.00 41.27  ? 110 HIS Q CA  1 
ATOM   9671  C  C   . HIS I  1 110 ? -10.491 3.376   61.480  1.00 41.52  ? 110 HIS Q C   1 
ATOM   9672  O  O   . HIS I  1 110 ? -11.182 2.841   60.621  1.00 39.76  ? 110 HIS Q O   1 
ATOM   9673  C  CB  . HIS I  1 110 ? -8.777  4.084   59.754  1.00 39.55  ? 110 HIS Q CB  1 
ATOM   9674  C  CG  . HIS I  1 110 ? -7.913  5.176   59.200  1.00 39.23  ? 110 HIS Q CG  1 
ATOM   9675  N  ND1 . HIS I  1 110 ? -7.257  5.064   57.989  1.00 38.05  ? 110 HIS Q ND1 1 
ATOM   9676  C  CD2 . HIS I  1 110 ? -7.609  6.406   59.679  1.00 40.24  ? 110 HIS Q CD2 1 
ATOM   9677  C  CE1 . HIS I  1 110 ? -6.569  6.169   57.760  1.00 38.29  ? 110 HIS Q CE1 1 
ATOM   9678  N  NE2 . HIS I  1 110 ? -6.769  7.000   58.768  1.00 39.63  ? 110 HIS Q NE2 1 
ATOM   9679  N  N   . CYS I  1 111 ? -10.596 3.082   62.778  1.00 43.95  ? 111 CYS Q N   1 
ATOM   9680  C  CA  . CYS I  1 111 ? -11.527 2.084   63.275  1.00 44.82  ? 111 CYS Q CA  1 
ATOM   9681  C  C   . CYS I  1 111 ? -12.963 2.537   63.035  1.00 43.73  ? 111 CYS Q C   1 
ATOM   9682  O  O   . CYS I  1 111 ? -13.308 3.680   63.332  1.00 43.96  ? 111 CYS Q O   1 
ATOM   9683  C  CB  . CYS I  1 111 ? -11.316 1.831   64.766  1.00 48.09  ? 111 CYS Q CB  1 
ATOM   9684  S  SG  . CYS I  1 111 ? -12.318 0.468   65.379  1.00 49.70  ? 111 CYS Q SG  1 
ATOM   9685  N  N   . ILE I  1 112 ? -13.779 1.635   62.498  1.00 42.83  ? 112 ILE Q N   1 
ATOM   9686  C  CA  . ILE I  1 112 ? -15.186 1.940   62.176  1.00 41.98  ? 112 ILE Q CA  1 
ATOM   9687  C  C   . ILE I  1 112 ? -16.195 1.446   63.220  1.00 44.28  ? 112 ILE Q C   1 
ATOM   9688  O  O   . ILE I  1 112 ? -17.390 1.710   63.086  1.00 44.01  ? 112 ILE Q O   1 
ATOM   9689  C  CB  . ILE I  1 112 ? -15.581 1.439   60.761  1.00 39.54  ? 112 ILE Q CB  1 
ATOM   9690  C  CG1 . ILE I  1 112 ? -15.490 -0.089  60.637  1.00 40.16  ? 112 ILE Q CG1 1 
ATOM   9691  C  CG2 . ILE I  1 112 ? -14.715 2.126   59.714  1.00 37.56  ? 112 ILE Q CG2 1 
ATOM   9692  C  CD1 . ILE I  1 112 ? -16.015 -0.618  59.323  1.00 38.39  ? 112 ILE Q CD1 1 
ATOM   9693  N  N   . ILE I  1 113 ? -15.711 0.758   64.255  1.00 46.84  ? 113 ILE Q N   1 
ATOM   9694  C  CA  . ILE I  1 113 ? -16.558 0.285   65.351  1.00 49.63  ? 113 ILE Q CA  1 
ATOM   9695  C  C   . ILE I  1 113 ? -17.079 1.482   66.160  1.00 51.13  ? 113 ILE Q C   1 
ATOM   9696  O  O   . ILE I  1 113 ? -16.323 2.396   66.495  1.00 51.57  ? 113 ILE Q O   1 
ATOM   9697  C  CB  . ILE I  1 113 ? -15.802 -0.714  66.257  1.00 52.24  ? 113 ILE Q CB  1 
ATOM   9698  C  CG1 . ILE I  1 113 ? -15.490 -2.002  65.477  1.00 51.37  ? 113 ILE Q CG1 1 
ATOM   9699  C  CG2 . ILE I  1 113 ? -16.613 -1.038  67.503  1.00 55.55  ? 113 ILE Q CG2 1 
ATOM   9700  C  CD1 . ILE I  1 113 ? -14.431 -2.871  66.120  1.00 53.62  ? 113 ILE Q CD1 1 
ATOM   9701  N  N   . GLY I  1 114 ? -18.379 1.472   66.449  1.00 52.21  ? 114 GLY Q N   1 
ATOM   9702  C  CA  . GLY I  1 114 ? -19.044 2.583   67.136  1.00 53.88  ? 114 GLY Q CA  1 
ATOM   9703  C  C   . GLY I  1 114 ? -19.459 3.725   66.219  1.00 51.63  ? 114 GLY Q C   1 
ATOM   9704  O  O   . GLY I  1 114 ? -19.906 4.768   66.694  1.00 52.94  ? 114 GLY Q O   1 
ATOM   9705  N  N   . ARG I  1 115 ? -19.306 3.534   64.908  1.00 48.54  ? 115 ARG Q N   1 
ATOM   9706  C  CA  . ARG I  1 115 ? -19.742 4.503   63.914  1.00 46.46  ? 115 ARG Q CA  1 
ATOM   9707  C  C   . ARG I  1 115 ? -20.889 3.861   63.110  1.00 45.29  ? 115 ARG Q C   1 
ATOM   9708  O  O   . ARG I  1 115 ? -21.269 2.717   63.374  1.00 46.23  ? 115 ARG Q O   1 
ATOM   9709  C  CB  . ARG I  1 115 ? -18.551 4.927   63.049  1.00 44.24  ? 115 ARG Q CB  1 
ATOM   9710  C  CG  . ARG I  1 115 ? -17.313 5.294   63.870  1.00 45.77  ? 115 ARG Q CG  1 
ATOM   9711  C  CD  . ARG I  1 115 ? -16.199 5.906   63.041  1.00 43.96  ? 115 ARG Q CD  1 
ATOM   9712  N  NE  . ARG I  1 115 ? -15.046 6.277   63.872  1.00 45.79  ? 115 ARG Q NE  1 
ATOM   9713  C  CZ  . ARG I  1 115 ? -14.887 7.436   64.520  1.00 47.52  ? 115 ARG Q CZ  1 
ATOM   9714  N  NH1 . ARG I  1 115 ? -15.805 8.403   64.463  1.00 47.78  ? 115 ARG Q NH1 1 
ATOM   9715  N  NH2 . ARG I  1 115 ? -13.786 7.636   65.234  1.00 49.32  ? 115 ARG Q NH2 1 
ATOM   9716  N  N   . THR I  1 116 ? -21.457 4.600   62.158  1.00 43.59  ? 116 THR Q N   1 
ATOM   9717  C  CA  . THR I  1 116 ? -22.693 4.179   61.465  1.00 42.96  ? 116 THR Q CA  1 
ATOM   9718  C  C   . THR I  1 116 ? -22.441 3.778   60.011  1.00 40.14  ? 116 THR Q C   1 
ATOM   9719  O  O   . THR I  1 116 ? -21.845 4.544   59.256  1.00 38.51  ? 116 THR Q O   1 
ATOM   9720  C  CB  . THR I  1 116 ? -23.756 5.307   61.499  1.00 43.75  ? 116 THR Q CB  1 
ATOM   9721  O  OG1 . THR I  1 116 ? -23.998 5.698   62.853  1.00 46.71  ? 116 THR Q OG1 1 
ATOM   9722  C  CG2 . THR I  1 116 ? -25.094 4.873   60.879  1.00 43.58  ? 116 THR Q CG2 1 
ATOM   9723  N  N   . LEU I  1 117 ? -22.881 2.578   59.630  1.00 39.96  ? 117 LEU Q N   1 
ATOM   9724  C  CA  . LEU I  1 117 ? -22.963 2.194   58.219  1.00 37.78  ? 117 LEU Q CA  1 
ATOM   9725  C  C   . LEU I  1 117 ? -24.308 2.654   57.686  1.00 37.66  ? 117 LEU Q C   1 
ATOM   9726  O  O   . LEU I  1 117 ? -25.322 2.553   58.389  1.00 39.54  ? 117 LEU Q O   1 
ATOM   9727  C  CB  . LEU I  1 117 ? -22.856 0.681   58.060  1.00 38.18  ? 117 LEU Q CB  1 
ATOM   9728  C  CG  . LEU I  1 117 ? -22.817 0.122   56.638  1.00 36.49  ? 117 LEU Q CG  1 
ATOM   9729  C  CD1 . LEU I  1 117 ? -21.577 0.583   55.887  1.00 34.63  ? 117 LEU Q CD1 1 
ATOM   9730  C  CD2 . LEU I  1 117 ? -22.869 -1.395  56.697  1.00 37.74  ? 117 LEU Q CD2 1 
ATOM   9731  N  N   . VAL I  1 118 ? -24.314 3.144   56.451  1.00 35.70  ? 118 VAL Q N   1 
ATOM   9732  C  CA  . VAL I  1 118 ? -25.515 3.688   55.813  1.00 35.59  ? 118 VAL Q CA  1 
ATOM   9733  C  C   . VAL I  1 118 ? -25.568 3.255   54.345  1.00 33.97  ? 118 VAL Q C   1 
ATOM   9734  O  O   . VAL I  1 118 ? -24.566 3.378   53.625  1.00 32.33  ? 118 VAL Q O   1 
ATOM   9735  C  CB  . VAL I  1 118 ? -25.545 5.237   55.892  1.00 35.48  ? 118 VAL Q CB  1 
ATOM   9736  C  CG1 . VAL I  1 118 ? -26.793 5.802   55.220  1.00 35.67  ? 118 VAL Q CG1 1 
ATOM   9737  C  CG2 . VAL I  1 118 ? -25.458 5.714   57.334  1.00 37.48  ? 118 VAL Q CG2 1 
ATOM   9738  N  N   . VAL I  1 119 ? -26.728 2.743   53.921  1.00 34.68  ? 119 VAL Q N   1 
ATOM   9739  C  CA  . VAL I  1 119 ? -27.021 2.493   52.504  1.00 33.66  ? 119 VAL Q CA  1 
ATOM   9740  C  C   . VAL I  1 119 ? -27.983 3.573   52.019  1.00 33.86  ? 119 VAL Q C   1 
ATOM   9741  O  O   . VAL I  1 119 ? -28.970 3.898   52.692  1.00 35.45  ? 119 VAL Q O   1 
ATOM   9742  C  CB  . VAL I  1 119 ? -27.544 1.061   52.213  1.00 34.61  ? 119 VAL Q CB  1 
ATOM   9743  C  CG1 . VAL I  1 119 ? -28.888 0.775   52.877  1.00 36.75  ? 119 VAL Q CG1 1 
ATOM   9744  C  CG2 . VAL I  1 119 ? -27.646 0.818   50.713  1.00 33.68  ? 119 VAL Q CG2 1 
ATOM   9745  N  N   . HIS I  1 120 ? -27.688 4.109   50.839  1.00 32.60  ? 120 HIS Q N   1 
ATOM   9746  C  CA  . HIS I  1 120 ? -28.290 5.341   50.356  1.00 32.71  ? 120 HIS Q CA  1 
ATOM   9747  C  C   . HIS I  1 120 ? -29.263 5.140   49.210  1.00 33.07  ? 120 HIS Q C   1 
ATOM   9748  O  O   . HIS I  1 120 ? -29.283 4.092   48.567  1.00 32.97  ? 120 HIS Q O   1 
ATOM   9749  C  CB  . HIS I  1 120 ? -27.191 6.300   49.908  1.00 31.30  ? 120 HIS Q CB  1 
ATOM   9750  C  CG  . HIS I  1 120 ? -26.446 6.925   51.038  1.00 31.57  ? 120 HIS Q CG  1 
ATOM   9751  N  ND1 . HIS I  1 120 ? -26.757 8.173   51.526  1.00 32.52  ? 120 HIS Q ND1 1 
ATOM   9752  C  CD2 . HIS I  1 120 ? -25.397 6.483   51.768  1.00 31.38  ? 120 HIS Q CD2 1 
ATOM   9753  C  CE1 . HIS I  1 120 ? -25.932 8.473   52.513  1.00 32.89  ? 120 HIS Q CE1 1 
ATOM   9754  N  NE2 . HIS I  1 120 ? -25.095 7.465   52.678  1.00 32.17  ? 120 HIS Q NE2 1 
ATOM   9755  N  N   . GLU I  1 121 ? -30.027 6.200   48.960  1.00 33.75  ? 121 GLU Q N   1 
ATOM   9756  C  CA  . GLU I  1 121 ? -31.085 6.254   47.951  1.00 34.56  ? 121 GLU Q CA  1 
ATOM   9757  C  C   . GLU I  1 121 ? -30.625 5.912   46.532  1.00 33.38  ? 121 GLU Q C   1 
ATOM   9758  O  O   . GLU I  1 121 ? -31.319 5.200   45.804  1.00 34.06  ? 121 GLU Q O   1 
ATOM   9759  C  CB  . GLU I  1 121 ? -31.688 7.671   47.948  1.00 35.53  ? 121 GLU Q CB  1 
ATOM   9760  C  CG  . GLU I  1 121 ? -32.932 7.876   47.095  1.00 36.95  ? 121 GLU Q CG  1 
ATOM   9761  C  CD  . GLU I  1 121 ? -33.317 9.347   46.944  1.00 37.91  ? 121 GLU Q CD  1 
ATOM   9762  O  OE1 . GLU I  1 121 ? -32.638 10.254  47.490  1.00 37.69  ? 121 GLU Q OE1 1 
ATOM   9763  O  OE2 . GLU I  1 121 ? -34.314 9.601   46.252  1.00 39.37  ? 121 GLU Q OE2 1 
ATOM   9764  N  N   . LYS I  1 122 ? -29.476 6.440   46.131  1.00 31.86  ? 122 LYS Q N   1 
ATOM   9765  C  CA  . LYS I  1 122 ? -29.029 6.270   44.748  1.00 31.12  ? 122 LYS Q CA  1 
ATOM   9766  C  C   . LYS I  1 122 ? -27.516 6.124   44.640  1.00 29.53  ? 122 LYS Q C   1 
ATOM   9767  O  O   . LYS I  1 122 ? -26.826 5.984   45.664  1.00 28.94  ? 122 LYS Q O   1 
ATOM   9768  C  CB  . LYS I  1 122 ? -29.602 7.399   43.882  1.00 31.79  ? 122 LYS Q CB  1 
ATOM   9769  C  CG  . LYS I  1 122 ? -29.156 8.800   44.255  1.00 31.62  ? 122 LYS Q CG  1 
ATOM   9770  C  CD  . LYS I  1 122 ? -30.283 9.808   44.044  1.00 33.15  ? 122 LYS Q CD  1 
ATOM   9771  C  CE  . LYS I  1 122 ? -29.728 11.224  43.948  1.00 33.18  ? 122 LYS Q CE  1 
ATOM   9772  N  NZ  . LYS I  1 122 ? -30.843 12.202  43.890  1.00 35.01  ? 122 LYS Q NZ  1 
ATOM   9773  N  N   . ALA I  1 123 ? -27.022 6.092   43.402  1.00 28.91  ? 123 ALA Q N   1 
ATOM   9774  C  CA  . ALA I  1 123 ? -25.615 5.877   43.133  1.00 27.84  ? 123 ALA Q CA  1 
ATOM   9775  C  C   . ALA I  1 123 ? -24.729 6.955   43.766  1.00 26.98  ? 123 ALA Q C   1 
ATOM   9776  O  O   . ALA I  1 123 ? -25.052 8.146   43.746  1.00 27.21  ? 123 ALA Q O   1 
ATOM   9777  C  CB  . ALA I  1 123 ? -25.363 5.817   41.634  1.00 28.00  ? 123 ALA Q CB  1 
ATOM   9778  N  N   . ASP I  1 124 ? -23.637 6.496   44.358  1.00 26.22  ? 124 ASP Q N   1 
ATOM   9779  C  CA  . ASP I  1 124 ? -22.500 7.327   44.667  1.00 25.56  ? 124 ASP Q CA  1 
ATOM   9780  C  C   . ASP I  1 124 ? -21.740 7.566   43.341  1.00 25.14  ? 124 ASP Q C   1 
ATOM   9781  O  O   . ASP I  1 124 ? -21.341 6.612   42.674  1.00 25.18  ? 124 ASP Q O   1 
ATOM   9782  C  CB  . ASP I  1 124 ? -21.619 6.589   45.684  1.00 25.41  ? 124 ASP Q CB  1 
ATOM   9783  C  CG  . ASP I  1 124 ? -20.443 7.414   46.183  1.00 25.24  ? 124 ASP Q CG  1 
ATOM   9784  O  OD1 . ASP I  1 124 ? -20.042 8.412   45.553  1.00 25.13  ? 124 ASP Q OD1 1 
ATOM   9785  O  OD2 . ASP I  1 124 ? -19.902 7.040   47.242  1.00 25.57  ? 124 ASP Q OD2 1 
ATOM   9786  N  N   . ASP I  1 125 ? -21.534 8.833   42.992  1.00 25.01  ? 125 ASP Q N   1 
ATOM   9787  C  CA  . ASP I  1 125 ? -20.795 9.219   41.782  1.00 25.05  ? 125 ASP Q CA  1 
ATOM   9788  C  C   . ASP I  1 125 ? -19.263 9.214   41.983  1.00 24.74  ? 125 ASP Q C   1 
ATOM   9789  O  O   . ASP I  1 125 ? -18.507 9.590   41.076  1.00 25.06  ? 125 ASP Q O   1 
ATOM   9790  C  CB  . ASP I  1 125 ? -21.302 10.569  41.235  1.00 25.63  ? 125 ASP Q CB  1 
ATOM   9791  C  CG  . ASP I  1 125 ? -20.907 11.772  42.098  1.00 25.76  ? 125 ASP Q CG  1 
ATOM   9792  O  OD1 . ASP I  1 125 ? -20.004 11.677  42.969  1.00 25.35  ? 125 ASP Q OD1 1 
ATOM   9793  O  OD2 . ASP I  1 125 ? -21.490 12.846  41.874  1.00 26.48  ? 125 ASP Q OD2 1 
ATOM   9794  N  N   . LEU I  1 126 ? -18.824 8.819   43.185  1.00 24.33  ? 126 LEU Q N   1 
ATOM   9795  C  CA  . LEU I  1 126 ? -17.419 8.580   43.505  1.00 24.22  ? 126 LEU Q CA  1 
ATOM   9796  C  C   . LEU I  1 126 ? -16.580 9.854   43.421  1.00 24.48  ? 126 LEU Q C   1 
ATOM   9797  O  O   . LEU I  1 126 ? -15.397 9.799   43.144  1.00 24.72  ? 126 LEU Q O   1 
ATOM   9798  C  CB  . LEU I  1 126 ? -16.838 7.442   42.635  1.00 24.44  ? 126 LEU Q CB  1 
ATOM   9799  C  CG  . LEU I  1 126 ? -17.684 6.160   42.522  1.00 24.55  ? 126 LEU Q CG  1 
ATOM   9800  C  CD1 . LEU I  1 126 ? -16.994 5.152   41.617  1.00 25.24  ? 126 LEU Q CD1 1 
ATOM   9801  C  CD2 . LEU I  1 126 ? -17.965 5.518   43.869  1.00 24.39  ? 126 LEU Q CD2 1 
ATOM   9802  N  N   . GLY I  1 127 ? -17.205 10.999  43.696  1.00 24.72  ? 127 GLY Q N   1 
ATOM   9803  C  CA  . GLY I  1 127 ? -16.538 12.292  43.639  1.00 25.42  ? 127 GLY Q CA  1 
ATOM   9804  C  C   . GLY I  1 127 ? -16.331 12.876  42.256  1.00 25.97  ? 127 GLY Q C   1 
ATOM   9805  O  O   . GLY I  1 127 ? -15.673 13.897  42.134  1.00 26.82  ? 127 GLY Q O   1 
ATOM   9806  N  N   . LYS I  1 128 ? -16.938 12.276  41.227  1.00 25.83  ? 128 LYS Q N   1 
ATOM   9807  C  CA  . LYS I  1 128 ? -16.725 12.682  39.824  1.00 26.71  ? 128 LYS Q CA  1 
ATOM   9808  C  C   . LYS I  1 128 ? -17.905 13.463  39.208  1.00 27.26  ? 128 LYS Q C   1 
ATOM   9809  O  O   . LYS I  1 128 ? -17.955 13.670  37.983  1.00 28.07  ? 128 LYS Q O   1 
ATOM   9810  C  CB  . LYS I  1 128 ? -16.443 11.442  38.984  1.00 26.78  ? 128 LYS Q CB  1 
ATOM   9811  C  CG  . LYS I  1 128 ? -15.242 10.633  39.474  1.00 26.66  ? 128 LYS Q CG  1 
ATOM   9812  C  CD  . LYS I  1 128 ? -15.201 9.267   38.820  1.00 26.92  ? 128 LYS Q CD  1 
ATOM   9813  C  CE  . LYS I  1 128 ? -14.919 9.359   37.339  1.00 28.29  ? 128 LYS Q CE  1 
ATOM   9814  N  NZ  . LYS I  1 128 ? -14.576 8.022   36.790  1.00 28.99  ? 128 LYS Q NZ  1 
ATOM   9815  N  N   . GLY I  1 129 ? -18.837 13.906  40.051  1.00 27.00  ? 129 GLY Q N   1 
ATOM   9816  C  CA  . GLY I  1 129 ? -20.040 14.593  39.575  1.00 27.78  ? 129 GLY Q CA  1 
ATOM   9817  C  C   . GLY I  1 129 ? -19.856 16.053  39.222  1.00 29.15  ? 129 GLY Q C   1 
ATOM   9818  O  O   . GLY I  1 129 ? -20.706 16.627  38.559  1.00 30.11  ? 129 GLY Q O   1 
ATOM   9819  N  N   . GLY I  1 130 ? -18.772 16.667  39.702  1.00 29.44  ? 130 GLY Q N   1 
ATOM   9820  C  CA  . GLY I  1 130 ? -18.461 18.061  39.382  1.00 31.17  ? 130 GLY Q CA  1 
ATOM   9821  C  C   . GLY I  1 130 ? -19.324 19.133  40.034  1.00 32.37  ? 130 GLY Q C   1 
ATOM   9822  O  O   . GLY I  1 130 ? -19.209 20.311  39.676  1.00 34.11  ? 130 GLY Q O   1 
ATOM   9823  N  N   . ASN I  1 131 ? -20.190 18.746  40.977  1.00 31.77  ? 131 ASN Q N   1 
ATOM   9824  C  CA  . ASN I  1 131 ? -20.916 19.711  41.795  1.00 33.23  ? 131 ASN Q CA  1 
ATOM   9825  C  C   . ASN I  1 131 ? -20.391 19.664  43.235  1.00 33.06  ? 131 ASN Q C   1 
ATOM   9826  O  O   . ASN I  1 131 ? -19.601 18.780  43.588  1.00 31.55  ? 131 ASN Q O   1 
ATOM   9827  C  CB  . ASN I  1 131 ? -22.460 19.537  41.695  1.00 33.51  ? 131 ASN Q CB  1 
ATOM   9828  C  CG  . ASN I  1 131 ? -22.980 18.252  42.324  1.00 31.94  ? 131 ASN Q CG  1 
ATOM   9829  O  OD1 . ASN I  1 131 ? -22.234 17.312  42.593  1.00 30.43  ? 131 ASN Q OD1 1 
ATOM   9830  N  ND2 . ASN I  1 131 ? -24.295 18.213  42.560  1.00 32.57  ? 131 ASN Q ND2 1 
ATOM   9831  N  N   . GLU I  1 132 ? -20.811 20.639  44.040  1.00 34.89  ? 132 GLU Q N   1 
ATOM   9832  C  CA  . GLU I  1 132 ? -20.389 20.742  45.445  1.00 35.45  ? 132 GLU Q CA  1 
ATOM   9833  C  C   . GLU I  1 132 ? -20.641 19.430  46.178  1.00 33.84  ? 132 GLU Q C   1 
ATOM   9834  O  O   . GLU I  1 132 ? -19.781 18.914  46.880  1.00 33.14  ? 132 GLU Q O   1 
ATOM   9835  C  CB  . GLU I  1 132 ? -21.159 21.851  46.157  1.00 37.90  ? 132 GLU Q CB  1 
ATOM   9836  C  CG  . GLU I  1 132 ? -20.811 23.264  45.708  1.00 40.28  ? 132 GLU Q CG  1 
ATOM   9837  C  CD  . GLU I  1 132 ? -21.826 24.304  46.158  1.00 42.99  ? 132 GLU Q CD  1 
ATOM   9838  O  OE1 . GLU I  1 132 ? -22.792 23.942  46.865  1.00 43.14  ? 132 GLU Q OE1 1 
ATOM   9839  O  OE2 . GLU I  1 132 ? -21.656 25.495  45.806  1.00 45.34  ? 132 GLU Q OE2 1 
ATOM   9840  N  N   . GLU I  1 133 ? -21.827 18.885  45.960  1.00 33.53  ? 133 GLU Q N   1 
ATOM   9841  C  CA  . GLU I  1 133 ? -22.287 17.704  46.671  1.00 32.55  ? 133 GLU Q CA  1 
ATOM   9842  C  C   . GLU I  1 133 ? -21.462 16.434  46.346  1.00 30.48  ? 133 GLU Q C   1 
ATOM   9843  O  O   . GLU I  1 133 ? -21.216 15.604  47.240  1.00 29.75  ? 133 GLU Q O   1 
ATOM   9844  C  CB  . GLU I  1 133 ? -23.786 17.525  46.395  1.00 33.17  ? 133 GLU Q CB  1 
ATOM   9845  C  CG  . GLU I  1 133 ? -24.511 16.586  47.329  1.00 33.10  ? 133 GLU Q CG  1 
ATOM   9846  C  CD  . GLU I  1 133 ? -24.445 17.032  48.776  1.00 34.60  ? 133 GLU Q CD  1 
ATOM   9847  O  OE1 . GLU I  1 133 ? -24.827 18.180  49.082  1.00 36.77  ? 133 GLU Q OE1 1 
ATOM   9848  O  OE2 . GLU I  1 133 ? -23.996 16.233  49.611  1.00 34.10  ? 133 GLU Q OE2 1 
ATOM   9849  N  N   . SER I  1 134 ? -20.983 16.308  45.105  1.00 29.76  ? 134 SER Q N   1 
ATOM   9850  C  CA  . SER I  1 134 ? -20.102 15.184  44.730  1.00 28.31  ? 134 SER Q CA  1 
ATOM   9851  C  C   . SER I  1 134 ? -18.902 15.011  45.666  1.00 28.19  ? 134 SER Q C   1 
ATOM   9852  O  O   . SER I  1 134 ? -18.599 13.894  46.072  1.00 27.20  ? 134 SER Q O   1 
ATOM   9853  C  CB  . SER I  1 134 ? -19.586 15.321  43.297  1.00 28.23  ? 134 SER Q CB  1 
ATOM   9854  O  OG  . SER I  1 134 ? -19.004 14.106  42.874  1.00 27.03  ? 134 SER Q OG  1 
ATOM   9855  N  N   . THR I  1 135 ? -18.269 16.127  46.025  1.00 29.51  ? 135 THR Q N   1 
ATOM   9856  C  CA  . THR I  1 135 ? -17.099 16.148  46.922  1.00 29.99  ? 135 THR Q CA  1 
ATOM   9857  C  C   . THR I  1 135 ? -17.414 15.885  48.413  1.00 30.37  ? 135 THR Q C   1 
ATOM   9858  O  O   . THR I  1 135 ? -16.491 15.724  49.209  1.00 30.72  ? 135 THR Q O   1 
ATOM   9859  C  CB  . THR I  1 135 ? -16.362 17.513  46.847  1.00 31.71  ? 135 THR Q CB  1 
ATOM   9860  O  OG1 . THR I  1 135 ? -17.266 18.563  47.206  1.00 33.32  ? 135 THR Q OG1 1 
ATOM   9861  C  CG2 . THR I  1 135 ? -15.842 17.798  45.461  1.00 31.81  ? 135 THR Q CG2 1 
ATOM   9862  N  N   . LYS I  1 136 ? -18.695 15.876  48.780  1.00 30.69  ? 136 LYS Q N   1 
ATOM   9863  C  CA  . LYS I  1 136 ? -19.159 15.602  50.150  1.00 31.44  ? 136 LYS Q CA  1 
ATOM   9864  C  C   . LYS I  1 136 ? -19.781 14.221  50.294  1.00 30.22  ? 136 LYS Q C   1 
ATOM   9865  O  O   . LYS I  1 136 ? -19.386 13.455  51.164  1.00 30.08  ? 136 LYS Q O   1 
ATOM   9866  C  CB  . LYS I  1 136 ? -20.192 16.644  50.573  1.00 33.34  ? 136 LYS Q CB  1 
ATOM   9867  C  CG  . LYS I  1 136 ? -19.639 18.053  50.661  1.00 35.20  ? 136 LYS Q CG  1 
ATOM   9868  C  CD  . LYS I  1 136 ? -20.735 19.064  50.913  1.00 37.33  ? 136 LYS Q CD  1 
ATOM   9869  C  CE  . LYS I  1 136 ? -20.154 20.463  50.997  1.00 39.52  ? 136 LYS Q CE  1 
ATOM   9870  N  NZ  . LYS I  1 136 ? -21.210 21.471  51.293  1.00 42.04  ? 136 LYS Q NZ  1 
ATOM   9871  N  N   . THR I  1 137 ? -20.774 13.923  49.456  1.00 29.58  ? 137 THR Q N   1 
ATOM   9872  C  CA  . THR I  1 137 ? -21.582 12.708  49.597  1.00 28.95  ? 137 THR Q CA  1 
ATOM   9873  C  C   . THR I  1 137 ? -21.613 11.803  48.383  1.00 27.52  ? 137 THR Q C   1 
ATOM   9874  O  O   . THR I  1 137 ? -22.184 10.710  48.453  1.00 27.35  ? 137 THR Q O   1 
ATOM   9875  C  CB  . THR I  1 137 ? -23.045 13.082  49.900  1.00 30.21  ? 137 THR Q CB  1 
ATOM   9876  O  OG1 . THR I  1 137 ? -23.544 13.903  48.841  1.00 30.39  ? 137 THR Q OG1 1 
ATOM   9877  C  CG2 . THR I  1 137 ? -23.152 13.825  51.223  1.00 32.07  ? 137 THR Q CG2 1 
ATOM   9878  N  N   . GLY I  1 138 ? -21.048 12.246  47.266  1.00 26.90  ? 138 GLY Q N   1 
ATOM   9879  C  CA  . GLY I  1 138 ? -21.193 11.545  46.007  1.00 26.01  ? 138 GLY Q CA  1 
ATOM   9880  C  C   . GLY I  1 138 ? -22.578 11.602  45.372  1.00 26.33  ? 138 GLY Q C   1 
ATOM   9881  O  O   . GLY I  1 138 ? -22.901 10.760  44.537  1.00 25.87  ? 138 GLY Q O   1 
ATOM   9882  N  N   . ASN I  1 139 ? -23.393 12.583  45.765  1.00 27.33  ? 139 ASN Q N   1 
ATOM   9883  C  CA  . ASN I  1 139 ? -24.786 12.704  45.307  1.00 28.09  ? 139 ASN Q CA  1 
ATOM   9884  C  C   . ASN I  1 139 ? -25.615 11.427  45.511  1.00 27.92  ? 139 ASN Q C   1 
ATOM   9885  O  O   . ASN I  1 139 ? -26.481 11.110  44.706  1.00 28.22  ? 139 ASN Q O   1 
ATOM   9886  C  CB  . ASN I  1 139 ? -24.812 13.142  43.835  1.00 28.16  ? 139 ASN Q CB  1 
ATOM   9887  C  CG  . ASN I  1 139 ? -24.330 14.559  43.652  1.00 28.96  ? 139 ASN Q CG  1 
ATOM   9888  O  OD1 . ASN I  1 139 ? -25.024 15.502  44.024  1.00 30.30  ? 139 ASN Q OD1 1 
ATOM   9889  N  ND2 . ASN I  1 139 ? -23.146 14.721  43.075  1.00 28.41  ? 139 ASN Q ND2 1 
ATOM   9890  N  N   . ALA I  1 140 ? -25.351 10.712  46.602  1.00 27.73  ? 140 ALA Q N   1 
ATOM   9891  C  CA  . ALA I  1 140 ? -26.009 9.432   46.870  1.00 27.89  ? 140 ALA Q CA  1 
ATOM   9892  C  C   . ALA I  1 140 ? -27.431 9.551   47.436  1.00 29.37  ? 140 ALA Q C   1 
ATOM   9893  O  O   . ALA I  1 140 ? -28.115 8.543   47.554  1.00 29.77  ? 140 ALA Q O   1 
ATOM   9894  C  CB  . ALA I  1 140 ? -25.159 8.590   47.799  1.00 27.43  ? 140 ALA Q CB  1 
ATOM   9895  N  N   . GLY I  1 141 ? -27.864 10.760  47.791  1.00 30.52  ? 141 GLY Q N   1 
ATOM   9896  C  CA  . GLY I  1 141 ? -29.259 11.008  48.169  1.00 32.36  ? 141 GLY Q CA  1 
ATOM   9897  C  C   . GLY I  1 141 ? -29.549 10.674  49.618  1.00 33.54  ? 141 GLY Q C   1 
ATOM   9898  O  O   . GLY I  1 141 ? -28.663 10.711  50.457  1.00 33.26  ? 141 GLY Q O   1 
ATOM   9899  N  N   . SER I  1 142 ? -30.801 10.348  49.919  1.00 35.25  ? 142 SER Q N   1 
ATOM   9900  C  CA  . SER I  1 142 ? -31.221 10.135  51.312  1.00 37.00  ? 142 SER Q CA  1 
ATOM   9901  C  C   . SER I  1 142 ? -30.669 8.836   51.916  1.00 36.41  ? 142 SER Q C   1 
ATOM   9902  O  O   . SER I  1 142 ? -30.249 7.920   51.202  1.00 34.90  ? 142 SER Q O   1 
ATOM   9903  C  CB  . SER I  1 142 ? -32.749 10.160  51.419  1.00 39.25  ? 142 SER Q CB  1 
ATOM   9904  O  OG  . SER I  1 142 ? -33.315 9.063   50.733  1.00 39.01  ? 142 SER Q OG  1 
ATOM   9905  N  N   . ARG I  1 143 ? -30.705 8.773   53.244  1.00 38.00  ? 143 ARG Q N   1 
ATOM   9906  C  CA  . ARG I  1 143 ? -30.240 7.615   54.005  1.00 38.08  ? 143 ARG Q CA  1 
ATOM   9907  C  C   . ARG I  1 143 ? -31.404 6.654   54.220  1.00 39.71  ? 143 ARG Q C   1 
ATOM   9908  O  O   . ARG I  1 143 ? -32.299 6.918   55.033  1.00 42.13  ? 143 ARG Q O   1 
ATOM   9909  C  CB  . ARG I  1 143 ? -29.648 8.075   55.335  1.00 39.31  ? 143 ARG Q CB  1 
ATOM   9910  C  CG  . ARG I  1 143 ? -28.583 9.143   55.157  1.00 38.29  ? 143 ARG Q CG  1 
ATOM   9911  C  CD  . ARG I  1 143 ? -27.937 9.595   56.457  1.00 39.75  ? 143 ARG Q CD  1 
ATOM   9912  N  NE  . ARG I  1 143 ? -27.058 10.738  56.197  1.00 39.17  ? 143 ARG Q NE  1 
ATOM   9913  C  CZ  . ARG I  1 143 ? -26.234 11.305  57.078  1.00 40.16  ? 143 ARG Q CZ  1 
ATOM   9914  N  NH1 . ARG I  1 143 ? -26.136 10.851  58.329  1.00 41.86  ? 143 ARG Q NH1 1 
ATOM   9915  N  NH2 . ARG I  1 143 ? -25.499 12.344  56.696  1.00 39.73  ? 143 ARG Q NH2 1 
ATOM   9916  N  N   . LEU I  1 144 ? -31.402 5.552   53.474  1.00 38.76  ? 144 LEU Q N   1 
ATOM   9917  C  CA  . LEU I  1 144 ? -32.508 4.586   53.485  1.00 40.40  ? 144 LEU Q CA  1 
ATOM   9918  C  C   . LEU I  1 144 ? -32.490 3.658   54.693  1.00 41.99  ? 144 LEU Q C   1 
ATOM   9919  O  O   . LEU I  1 144 ? -33.545 3.307   55.225  1.00 44.34  ? 144 LEU Q O   1 
ATOM   9920  C  CB  . LEU I  1 144 ? -32.469 3.717   52.229  1.00 39.25  ? 144 LEU Q CB  1 
ATOM   9921  C  CG  . LEU I  1 144 ? -32.576 4.403   50.868  1.00 38.05  ? 144 LEU Q CG  1 
ATOM   9922  C  CD1 . LEU I  1 144 ? -32.696 3.325   49.801  1.00 37.76  ? 144 LEU Q CD1 1 
ATOM   9923  C  CD2 . LEU I  1 144 ? -33.771 5.342   50.817  1.00 39.61  ? 144 LEU Q CD2 1 
ATOM   9924  N  N   . ALA I  1 145 ? -31.297 3.221   55.091  1.00 40.87  ? 145 ALA Q N   1 
ATOM   9925  C  CA  . ALA I  1 145 ? -31.159 2.335   56.240  1.00 42.50  ? 145 ALA Q CA  1 
ATOM   9926  C  C   . ALA I  1 145 ? -29.788 2.489   56.870  1.00 41.60  ? 145 ALA Q C   1 
ATOM   9927  O  O   . ALA I  1 145 ? -28.799 2.756   56.177  1.00 39.32  ? 145 ALA Q O   1 
ATOM   9928  C  CB  . ALA I  1 145 ? -31.392 0.895   55.827  1.00 42.92  ? 145 ALA Q CB  1 
ATOM   9929  N  N   . ALA I  1 146 ? -29.741 2.320   58.189  1.00 43.65  ? 146 ALA Q N   1 
ATOM   9930  C  CA  . ALA I  1 146 ? -28.530 2.570   58.958  1.00 43.42  ? 146 ALA Q CA  1 
ATOM   9931  C  C   . ALA I  1 146 ? -28.461 1.715   60.198  1.00 45.84  ? 146 ALA Q C   1 
ATOM   9932  O  O   . ALA I  1 146 ? -29.471 1.167   60.661  1.00 48.10  ? 146 ALA Q O   1 
ATOM   9933  C  CB  . ALA I  1 146 ? -28.457 4.037   59.352  1.00 43.71  ? 146 ALA Q CB  1 
ATOM   9934  N  N   . GLY I  1 147 ? -27.250 1.616   60.734  1.00 45.57  ? 147 GLY Q N   1 
ATOM   9935  C  CA  . GLY I  1 147 ? -27.017 0.964   62.021  1.00 48.14  ? 147 GLY Q CA  1 
ATOM   9936  C  C   . GLY I  1 147 ? -25.659 1.332   62.575  1.00 47.82  ? 147 GLY Q C   1 
ATOM   9937  O  O   . GLY I  1 147 ? -24.768 1.754   61.831  1.00 45.36  ? 147 GLY Q O   1 
ATOM   9938  N  N   . VAL I  1 148 ? -25.495 1.157   63.878  1.00 50.56  ? 148 VAL Q N   1 
ATOM   9939  C  CA  . VAL I  1 148 ? -24.198 1.334   64.514  1.00 50.85  ? 148 VAL Q CA  1 
ATOM   9940  C  C   . VAL I  1 148 ? -23.390 0.050   64.304  1.00 50.40  ? 148 VAL Q C   1 
ATOM   9941  O  O   . VAL I  1 148 ? -23.929 -1.051  64.441  1.00 51.79  ? 148 VAL Q O   1 
ATOM   9942  C  CB  . VAL I  1 148 ? -24.340 1.647   66.019  1.00 54.42  ? 148 VAL Q CB  1 
ATOM   9943  C  CG1 . VAL I  1 148 ? -22.964 1.795   66.671  1.00 54.92  ? 148 VAL Q CG1 1 
ATOM   9944  C  CG2 . VAL I  1 148 ? -25.178 2.910   66.225  1.00 55.34  ? 148 VAL Q CG2 1 
ATOM   9945  N  N   . ILE I  1 149 ? -22.104 0.195   63.976  1.00 48.81  ? 149 ILE Q N   1 
ATOM   9946  C  CA  . ILE I  1 149 ? -21.213 -0.961  63.800  1.00 48.70  ? 149 ILE Q CA  1 
ATOM   9947  C  C   . ILE I  1 149 ? -20.671 -1.405  65.157  1.00 51.80  ? 149 ILE Q C   1 
ATOM   9948  O  O   . ILE I  1 149 ? -20.053 -0.613  65.878  1.00 52.69  ? 149 ILE Q O   1 
ATOM   9949  C  CB  . ILE I  1 149 ? -20.046 -0.660  62.835  1.00 45.98  ? 149 ILE Q CB  1 
ATOM   9950  C  CG1 . ILE I  1 149 ? -20.587 -0.246  61.460  1.00 43.25  ? 149 ILE Q CG1 1 
ATOM   9951  C  CG2 . ILE I  1 149 ? -19.138 -1.883  62.700  1.00 46.31  ? 149 ILE Q CG2 1 
ATOM   9952  C  CD1 . ILE I  1 149 ? -19.572 0.431   60.564  1.00 40.85  ? 149 ILE Q CD1 1 
ATOM   9953  N  N   . GLY I  1 150 ? -20.892 -2.674  65.488  1.00 53.73  ? 150 GLY Q N   1 
ATOM   9954  C  CA  . GLY I  1 150 ? -20.552 -3.217  66.802  1.00 57.23  ? 150 GLY Q CA  1 
ATOM   9955  C  C   . GLY I  1 150 ? -19.639 -4.419  66.707  1.00 57.86  ? 150 GLY Q C   1 
ATOM   9956  O  O   . GLY I  1 150 ? -19.596 -5.095  65.678  1.00 56.20  ? 150 GLY Q O   1 
ATOM   9957  N  N   . ILE I  1 151 ? -18.917 -4.679  67.797  1.00 60.63  ? 151 ILE Q N   1 
ATOM   9958  C  CA  . ILE I  1 151 ? -17.987 -5.805  67.885  1.00 61.95  ? 151 ILE Q CA  1 
ATOM   9959  C  C   . ILE I  1 151 ? -18.785 -7.108  67.834  1.00 63.80  ? 151 ILE Q C   1 
ATOM   9960  O  O   . ILE I  1 151 ? -19.752 -7.270  68.585  1.00 66.27  ? 151 ILE Q O   1 
ATOM   9961  C  CB  . ILE I  1 151 ? -17.158 -5.766  69.198  1.00 65.09  ? 151 ILE Q CB  1 
ATOM   9962  C  CG1 . ILE I  1 151 ? -16.260 -4.523  69.240  1.00 63.71  ? 151 ILE Q CG1 1 
ATOM   9963  C  CG2 . ILE I  1 151 ? -16.314 -7.031  69.364  1.00 66.99  ? 151 ILE Q CG2 1 
ATOM   9964  C  CD1 . ILE I  1 151 ? -15.880 -4.095  70.644  1.00 67.10  ? 151 ILE Q CD1 1 
ATOM   9965  N  N   . ALA I  1 152 ? -18.366 -8.014  66.952  1.00 62.95  ? 152 ALA Q N   1 
ATOM   9966  C  CA  . ALA I  1 152 ? -18.951 -9.346  66.810  1.00 64.96  ? 152 ALA Q CA  1 
ATOM   9967  C  C   . ALA I  1 152 ? -18.012 -10.374 67.407  1.00 67.98  ? 152 ALA Q C   1 
ATOM   9968  O  O   . ALA I  1 152 ? -16.838 -10.079 67.639  1.00 67.77  ? 152 ALA Q O   1 
ATOM   9969  C  CB  . ALA I  1 152 ? -19.178 -9.660  65.345  1.00 62.31  ? 152 ALA Q CB  1 
ATOM   9970  N  N   . GLN I  1 153 ? -18.531 -11.583 67.628  1.00 71.02  ? 153 GLN Q N   1 
ATOM   9971  C  CA  . GLN I  1 153 ? -17.748 -12.687 68.202  1.00 74.49  ? 153 GLN Q CA  1 
ATOM   9972  C  C   . GLN I  1 153 ? -16.868 -13.322 67.141  1.00 73.25  ? 153 GLN Q C   1 
ATOM   9973  O  O   . GLN I  1 153 ? -17.358 -13.618 66.051  1.00 71.61  ? 153 GLN Q O   1 
ATOM   9974  C  CB  . GLN I  1 153 ? -18.648 -13.777 68.779  1.00 78.50  ? 153 GLN Q CB  1 
ATOM   9975  C  CG  . GLN I  1 153 ? -19.743 -13.285 69.704  1.00 80.23  ? 153 GLN Q CG  1 
ATOM   9976  C  CD  . GLN I  1 153 ? -20.217 -14.362 70.649  1.00 85.28  ? 153 GLN Q CD  1 
ATOM   9977  O  OE1 . GLN I  1 153 ? -19.451 -14.865 71.471  1.00 88.34  ? 153 GLN Q OE1 1 
ATOM   9978  N  NE2 . GLN I  1 153 ? -21.489 -14.725 70.539  1.00 86.52  ? 153 GLN Q NE2 1 
ATOM   9979  O  OXT . GLN I  1 153 ? -15.677 -13.569 67.350  1.00 74.21  ? 153 GLN Q OXT 1 
ATOM   9980  N  N   . ALA J  1 1   ? -12.671 16.227  75.622  1.00 61.13  ? 1   ALA S N   1 
ATOM   9981  C  CA  . ALA J  1 1   ? -13.821 15.482  76.224  1.00 58.66  ? 1   ALA S CA  1 
ATOM   9982  C  C   . ALA J  1 1   ? -14.438 14.484  75.237  1.00 56.42  ? 1   ALA S C   1 
ATOM   9983  O  O   . ALA J  1 1   ? -15.005 14.891  74.217  1.00 56.90  ? 1   ALA S O   1 
ATOM   9984  C  CB  . ALA J  1 1   ? -14.886 16.458  76.712  1.00 59.78  ? 1   ALA S CB  1 
ATOM   9985  N  N   . THR J  1 2   ? -14.324 13.189  75.546  1.00 54.27  ? 2   THR S N   1 
ATOM   9986  C  CA  . THR J  1 2   ? -14.939 12.131  74.738  1.00 52.28  ? 2   THR S CA  1 
ATOM   9987  C  C   . THR J  1 2   ? -16.411 12.009  75.107  1.00 51.19  ? 2   THR S C   1 
ATOM   9988  O  O   . THR J  1 2   ? -16.749 11.987  76.292  1.00 50.93  ? 2   THR S O   1 
ATOM   9989  C  CB  . THR J  1 2   ? -14.259 10.767  74.976  1.00 50.87  ? 2   THR S CB  1 
ATOM   9990  O  OG1 . THR J  1 2   ? -12.872 10.860  74.646  1.00 52.18  ? 2   THR S OG1 1 
ATOM   9991  C  CG2 . THR J  1 2   ? -14.891 9.671   74.118  1.00 49.27  ? 2   THR S CG2 1 
ATOM   9992  N  N   . LYS J  1 3   ? -17.276 11.924  74.095  1.00 50.81  ? 3   LYS S N   1 
ATOM   9993  C  CA  . LYS J  1 3   ? -18.715 11.716  74.297  1.00 50.04  ? 3   LYS S CA  1 
ATOM   9994  C  C   . LYS J  1 3   ? -19.210 10.504  73.506  1.00 48.53  ? 3   LYS S C   1 
ATOM   9995  O  O   . LYS J  1 3   ? -18.742 10.257  72.385  1.00 48.66  ? 3   LYS S O   1 
ATOM   9996  C  CB  . LYS J  1 3   ? -19.500 12.960  73.868  1.00 51.81  ? 3   LYS S CB  1 
ATOM   9997  C  CG  . LYS J  1 3   ? -19.306 14.173  74.764  1.00 53.65  ? 3   LYS S CG  1 
ATOM   9998  C  CD  . LYS J  1 3   ? -19.991 15.395  74.174  1.00 55.84  ? 3   LYS S CD  1 
ATOM   9999  C  CE  . LYS J  1 3   ? -19.801 16.620  75.054  1.00 58.11  ? 3   LYS S CE  1 
ATOM   10000 N  NZ  . LYS J  1 3   ? -20.170 17.877  74.343  1.00 60.78  ? 3   LYS S NZ  1 
ATOM   10001 N  N   . ALA J  1 4   ? -20.150 9.762   74.092  1.00 47.40  ? 4   ALA S N   1 
ATOM   10002 C  CA  . ALA J  1 4   ? -20.874 8.693   73.398  1.00 46.46  ? 4   ALA S CA  1 
ATOM   10003 C  C   . ALA J  1 4   ? -22.385 8.785   73.667  1.00 46.75  ? 4   ALA S C   1 
ATOM   10004 O  O   . ALA J  1 4   ? -22.826 9.465   74.603  1.00 47.36  ? 4   ALA S O   1 
ATOM   10005 C  CB  . ALA J  1 4   ? -20.340 7.327   73.809  1.00 45.09  ? 4   ALA S CB  1 
ATOM   10006 N  N   . VAL J  1 5   ? -23.169 8.091   72.842  1.00 46.57  ? 5   VAL S N   1 
ATOM   10007 C  CA  . VAL J  1 5   ? -24.640 8.085   72.960  1.00 47.20  ? 5   VAL S CA  1 
ATOM   10008 C  C   . VAL J  1 5   ? -25.200 6.690   72.629  1.00 46.52  ? 5   VAL S C   1 
ATOM   10009 O  O   . VAL J  1 5   ? -24.555 5.894   71.937  1.00 45.87  ? 5   VAL S O   1 
ATOM   10010 C  CB  . VAL J  1 5   ? -25.272 9.208   72.084  1.00 48.89  ? 5   VAL S CB  1 
ATOM   10011 C  CG1 . VAL J  1 5   ? -25.139 8.906   70.596  1.00 49.11  ? 5   VAL S CG1 1 
ATOM   10012 C  CG2 . VAL J  1 5   ? -26.726 9.474   72.461  1.00 50.03  ? 5   VAL S CG2 1 
ATOM   10013 N  N   . CYS J  1 6   ? -26.377 6.387   73.172  1.00 46.95  ? 6   CYS S N   1 
ATOM   10014 C  CA  . CYS J  1 6   ? -27.035 5.110   72.933  1.00 46.82  ? 6   CYS S CA  1 
ATOM   10015 C  C   . CYS J  1 6   ? -28.565 5.246   72.934  1.00 48.32  ? 6   CYS S C   1 
ATOM   10016 O  O   . CYS J  1 6   ? -29.152 5.795   73.881  1.00 49.01  ? 6   CYS S O   1 
ATOM   10017 C  CB  . CYS J  1 6   ? -26.608 4.097   73.992  1.00 45.77  ? 6   CYS S CB  1 
ATOM   10018 S  SG  . CYS J  1 6   ? -27.313 2.456   73.737  1.00 45.98  ? 6   CYS S SG  1 
ATOM   10019 N  N   . VAL J  1 7   ? -29.191 4.735   71.872  1.00 49.10  ? 7   VAL S N   1 
ATOM   10020 C  CA  . VAL J  1 7   ? -30.648 4.657   71.759  1.00 50.83  ? 7   VAL S CA  1 
ATOM   10021 C  C   . VAL J  1 7   ? -31.104 3.273   72.236  1.00 50.83  ? 7   VAL S C   1 
ATOM   10022 O  O   . VAL J  1 7   ? -30.756 2.251   71.633  1.00 50.38  ? 7   VAL S O   1 
ATOM   10023 C  CB  . VAL J  1 7   ? -31.117 4.906   70.306  1.00 52.15  ? 7   VAL S CB  1 
ATOM   10024 C  CG1 . VAL J  1 7   ? -32.640 4.949   70.224  1.00 54.32  ? 7   VAL S CG1 1 
ATOM   10025 C  CG2 . VAL J  1 7   ? -30.515 6.206   69.776  1.00 52.34  ? 7   VAL S CG2 1 
ATOM   10026 N  N   . LEU J  1 8   ? -31.883 3.260   73.317  1.00 51.63  ? 8   LEU S N   1 
ATOM   10027 C  CA  . LEU J  1 8   ? -32.425 2.031   73.903  1.00 52.14  ? 8   LEU S CA  1 
ATOM   10028 C  C   . LEU J  1 8   ? -33.759 1.681   73.253  1.00 54.40  ? 8   LEU S C   1 
ATOM   10029 O  O   . LEU J  1 8   ? -34.676 2.496   73.270  1.00 56.05  ? 8   LEU S O   1 
ATOM   10030 C  CB  . LEU J  1 8   ? -32.611 2.212   75.411  1.00 52.22  ? 8   LEU S CB  1 
ATOM   10031 C  CG  . LEU J  1 8   ? -31.312 2.421   76.200  1.00 50.35  ? 8   LEU S CG  1 
ATOM   10032 C  CD1 . LEU J  1 8   ? -31.624 2.845   77.627  1.00 50.93  ? 8   LEU S CD1 1 
ATOM   10033 C  CD2 . LEU J  1 8   ? -30.453 1.160   76.173  1.00 49.14  ? 8   LEU S CD2 1 
ATOM   10034 N  N   . LYS J  1 9   ? -33.849 0.484   72.667  1.00 54.83  ? 9   LYS S N   1 
ATOM   10035 C  CA  . LYS J  1 9   ? -35.067 -0.007  71.998  1.00 57.29  ? 9   LYS S CA  1 
ATOM   10036 C  C   . LYS J  1 9   ? -35.259 -1.503  72.234  1.00 58.02  ? 9   LYS S C   1 
ATOM   10037 O  O   . LYS J  1 9   ? -34.279 -2.250  72.356  1.00 56.50  ? 9   LYS S O   1 
ATOM   10038 C  CB  . LYS J  1 9   ? -34.994 0.227   70.482  1.00 57.78  ? 9   LYS S CB  1 
ATOM   10039 C  CG  . LYS J  1 9   ? -34.899 1.680   70.039  1.00 57.73  ? 9   LYS S CG  1 
ATOM   10040 C  CD  . LYS J  1 9   ? -36.196 2.440   70.278  1.00 60.08  ? 9   LYS S CD  1 
ATOM   10041 C  CE  . LYS J  1 9   ? -36.107 3.865   69.745  1.00 60.45  ? 9   LYS S CE  1 
ATOM   10042 N  NZ  . LYS J  1 9   ? -37.361 4.638   69.969  1.00 63.08  ? 9   LYS S NZ  1 
ATOM   10043 N  N   . GLY J  1 10  ? -36.524 -1.928  72.274  1.00 60.66  ? 10  GLY S N   1 
ATOM   10044 C  CA  . GLY J  1 10  ? -36.889 -3.344  72.392  1.00 62.17  ? 10  GLY S CA  1 
ATOM   10045 C  C   . GLY J  1 10  ? -38.280 -3.662  71.858  1.00 65.57  ? 10  GLY S C   1 
ATOM   10046 O  O   . GLY J  1 10  ? -38.890 -2.849  71.159  1.00 66.68  ? 10  GLY S O   1 
ATOM   10047 N  N   . ASP J  1 11  ? -38.775 -4.850  72.201  1.00 67.50  ? 11  ASP S N   1 
ATOM   10048 C  CA  . ASP J  1 11  ? -40.078 -5.341  71.718  1.00 71.22  ? 11  ASP S CA  1 
ATOM   10049 C  C   . ASP J  1 11  ? -41.272 -4.647  72.379  1.00 73.42  ? 11  ASP S C   1 
ATOM   10050 O  O   . ASP J  1 11  ? -42.270 -4.363  71.712  1.00 76.07  ? 11  ASP S O   1 
ATOM   10051 C  CB  . ASP J  1 11  ? -40.197 -6.859  71.925  1.00 72.96  ? 11  ASP S CB  1 
ATOM   10052 C  CG  . ASP J  1 11  ? -39.192 -7.652  71.095  1.00 71.80  ? 11  ASP S CG  1 
ATOM   10053 O  OD1 . ASP J  1 11  ? -38.200 -7.068  70.610  1.00 69.10  ? 11  ASP S OD1 1 
ATOM   10054 O  OD2 . ASP J  1 11  ? -39.399 -8.871  70.934  1.00 73.94  ? 11  ASP S OD2 1 
ATOM   10055 N  N   . GLY J  1 12  ? -41.170 -4.398  73.686  1.00 72.63  ? 12  GLY S N   1 
ATOM   10056 C  CA  . GLY J  1 12  ? -42.211 -3.700  74.444  1.00 74.74  ? 12  GLY S CA  1 
ATOM   10057 C  C   . GLY J  1 12  ? -42.103 -2.181  74.351  1.00 73.59  ? 12  GLY S C   1 
ATOM   10058 O  O   . GLY J  1 12  ? -41.505 -1.657  73.408  1.00 71.93  ? 12  GLY S O   1 
ATOM   10059 N  N   . PRO J  1 13  ? -42.672 -1.458  75.338  1.00 74.71  ? 13  PRO S N   1 
ATOM   10060 C  CA  . PRO J  1 13  ? -42.662 0.009   75.342  1.00 74.23  ? 13  PRO S CA  1 
ATOM   10061 C  C   . PRO J  1 13  ? -41.412 0.665   75.967  1.00 70.79  ? 13  PRO S C   1 
ATOM   10062 O  O   . PRO J  1 13  ? -41.373 1.898   76.063  1.00 70.64  ? 13  PRO S O   1 
ATOM   10063 C  CB  . PRO J  1 13  ? -43.892 0.339   76.185  1.00 77.61  ? 13  PRO S CB  1 
ATOM   10064 C  CG  . PRO J  1 13  ? -43.910 -0.748  77.206  1.00 77.99  ? 13  PRO S CG  1 
ATOM   10065 C  CD  . PRO J  1 13  ? -43.389 -1.985  76.518  1.00 76.92  ? 13  PRO S CD  1 
ATOM   10066 N  N   . VAL J  1 14  ? -40.415 -0.128  76.379  1.00 68.38  ? 14  VAL S N   1 
ATOM   10067 C  CA  . VAL J  1 14  ? -39.222 0.409   77.049  1.00 65.45  ? 14  VAL S CA  1 
ATOM   10068 C  C   . VAL J  1 14  ? -38.276 1.031   76.020  1.00 63.15  ? 14  VAL S C   1 
ATOM   10069 O  O   . VAL J  1 14  ? -37.801 0.341   75.112  1.00 62.27  ? 14  VAL S O   1 
ATOM   10070 C  CB  . VAL J  1 14  ? -38.459 -0.659  77.869  1.00 64.05  ? 14  VAL S CB  1 
ATOM   10071 C  CG1 . VAL J  1 14  ? -37.239 -0.043  78.555  1.00 61.38  ? 14  VAL S CG1 1 
ATOM   10072 C  CG2 . VAL J  1 14  ? -39.379 -1.293  78.904  1.00 66.55  ? 14  VAL S CG2 1 
ATOM   10073 N  N   . GLN J  1 15  ? -38.013 2.329   76.181  1.00 62.52  ? 15  GLN S N   1 
ATOM   10074 C  CA  . GLN J  1 15  ? -37.142 3.077   75.274  1.00 60.77  ? 15  GLN S CA  1 
ATOM   10075 C  C   . GLN J  1 15  ? -36.548 4.324   75.930  1.00 59.80  ? 15  GLN S C   1 
ATOM   10076 O  O   . GLN J  1 15  ? -37.104 4.862   76.889  1.00 61.14  ? 15  GLN S O   1 
ATOM   10077 C  CB  . GLN J  1 15  ? -37.904 3.464   74.000  1.00 62.63  ? 15  GLN S CB  1 
ATOM   10078 C  CG  . GLN J  1 15  ? -39.034 4.472   74.210  1.00 65.41  ? 15  GLN S CG  1 
ATOM   10079 C  CD  . GLN J  1 15  ? -40.022 4.529   73.054  1.00 67.95  ? 15  GLN S CD  1 
ATOM   10080 O  OE1 . GLN J  1 15  ? -41.107 5.099   73.183  1.00 70.79  ? 15  GLN S OE1 1 
ATOM   10081 N  NE2 . GLN J  1 15  ? -39.655 3.936   71.919  1.00 67.22  ? 15  GLN S NE2 1 
ATOM   10082 N  N   . GLY J  1 16  ? -35.420 4.777   75.392  1.00 57.73  ? 16  GLY S N   1 
ATOM   10083 C  CA  . GLY J  1 16  ? -34.746 5.963   75.903  1.00 57.02  ? 16  GLY S CA  1 
ATOM   10084 C  C   . GLY J  1 16  ? -33.433 6.297   75.213  1.00 54.98  ? 16  GLY S C   1 
ATOM   10085 O  O   . GLY J  1 16  ? -32.908 5.502   74.426  1.00 53.70  ? 16  GLY S O   1 
ATOM   10086 N  N   . ILE J  1 17  ? -32.925 7.492   75.519  1.00 54.94  ? 17  ILE S N   1 
ATOM   10087 C  CA  . ILE J  1 17  ? -31.622 7.979   75.046  1.00 53.41  ? 17  ILE S CA  1 
ATOM   10088 C  C   . ILE J  1 17  ? -30.709 8.095   76.272  1.00 52.24  ? 17  ILE S C   1 
ATOM   10089 O  O   . ILE J  1 17  ? -31.094 8.716   77.272  1.00 53.30  ? 17  ILE S O   1 
ATOM   10090 C  CB  . ILE J  1 17  ? -31.743 9.358   74.339  1.00 54.92  ? 17  ILE S CB  1 
ATOM   10091 C  CG1 . ILE J  1 17  ? -32.677 9.260   73.119  1.00 56.36  ? 17  ILE S CG1 1 
ATOM   10092 C  CG2 . ILE J  1 17  ? -30.368 9.871   73.913  1.00 53.75  ? 17  ILE S CG2 1 
ATOM   10093 C  CD1 . ILE J  1 17  ? -33.049 10.589  72.491  1.00 58.49  ? 17  ILE S CD1 1 
ATOM   10094 N  N   . ILE J  1 18  ? -29.515 7.496   76.187  1.00 50.27  ? 18  ILE S N   1 
ATOM   10095 C  CA  . ILE J  1 18  ? -28.518 7.529   77.267  1.00 49.27  ? 18  ILE S CA  1 
ATOM   10096 C  C   . ILE J  1 18  ? -27.217 8.132   76.734  1.00 48.52  ? 18  ILE S C   1 
ATOM   10097 O  O   . ILE J  1 18  ? -26.627 7.607   75.790  1.00 47.61  ? 18  ILE S O   1 
ATOM   10098 C  CB  . ILE J  1 18  ? -28.285 6.111   77.861  1.00 48.08  ? 18  ILE S CB  1 
ATOM   10099 C  CG1 . ILE J  1 18  ? -29.524 5.658   78.658  1.00 49.25  ? 18  ILE S CG1 1 
ATOM   10100 C  CG2 . ILE J  1 18  ? -27.036 6.057   78.740  1.00 47.07  ? 18  ILE S CG2 1 
ATOM   10101 C  CD1 . ILE J  1 18  ? -29.718 6.323   80.012  1.00 50.22  ? 18  ILE S CD1 1 
ATOM   10102 N  N   . ASN J  1 19  ? -26.785 9.231   77.351  1.00 49.23  ? 19  ASN S N   1 
ATOM   10103 C  CA  . ASN J  1 19  ? -25.561 9.941   76.973  1.00 49.09  ? 19  ASN S CA  1 
ATOM   10104 C  C   . ASN J  1 19  ? -24.395 9.522   77.880  1.00 48.04  ? 19  ASN S C   1 
ATOM   10105 O  O   . ASN J  1 19  ? -24.608 9.132   79.034  1.00 47.90  ? 19  ASN S O   1 
ATOM   10106 C  CB  . ASN J  1 19  ? -25.770 11.458  77.088  1.00 51.08  ? 19  ASN S CB  1 
ATOM   10107 C  CG  . ASN J  1 19  ? -26.989 11.946  76.323  1.00 52.58  ? 19  ASN S CG  1 
ATOM   10108 O  OD1 . ASN J  1 19  ? -26.993 11.976  75.093  1.00 52.63  ? 19  ASN S OD1 1 
ATOM   10109 N  ND2 . ASN J  1 19  ? -28.027 12.341  77.053  1.00 54.08  ? 19  ASN S ND2 1 
ATOM   10110 N  N   . PHE J  1 20  ? -23.173 9.607   77.342  1.00 47.52  ? 20  PHE S N   1 
ATOM   10111 C  CA  . PHE J  1 20  ? -21.936 9.346   78.091  1.00 46.94  ? 20  PHE S CA  1 
ATOM   10112 C  C   . PHE J  1 20  ? -20.958 10.485  77.837  1.00 48.03  ? 20  PHE S C   1 
ATOM   10113 O  O   . PHE J  1 20  ? -20.819 10.918  76.692  1.00 48.46  ? 20  PHE S O   1 
ATOM   10114 C  CB  . PHE J  1 20  ? -21.248 8.064   77.625  1.00 45.51  ? 20  PHE S CB  1 
ATOM   10115 C  CG  . PHE J  1 20  ? -22.092 6.831   77.713  1.00 44.67  ? 20  PHE S CG  1 
ATOM   10116 C  CD1 . PHE J  1 20  ? -23.084 6.582   76.771  1.00 44.76  ? 20  PHE S CD1 1 
ATOM   10117 C  CD2 . PHE J  1 20  ? -21.851 5.880   78.693  1.00 44.10  ? 20  PHE S CD2 1 
ATOM   10118 C  CE1 . PHE J  1 20  ? -23.840 5.423   76.824  1.00 44.35  ? 20  PHE S CE1 1 
ATOM   10119 C  CE2 . PHE J  1 20  ? -22.604 4.717   78.755  1.00 43.69  ? 20  PHE S CE2 1 
ATOM   10120 C  CZ  . PHE J  1 20  ? -23.597 4.487   77.817  1.00 43.85  ? 20  PHE S CZ  1 
ATOM   10121 N  N   . GLU J  1 21  ? -20.264 10.945  78.877  1.00 48.67  ? 21  GLU S N   1 
ATOM   10122 C  CA  . GLU J  1 21  ? -19.193 11.934  78.709  1.00 50.05  ? 21  GLU S CA  1 
ATOM   10123 C  C   . GLU J  1 21  ? -18.015 11.632  79.638  1.00 50.03  ? 21  GLU S C   1 
ATOM   10124 O  O   . GLU J  1 21  ? -18.215 11.308  80.812  1.00 49.91  ? 21  GLU S O   1 
ATOM   10125 C  CB  . GLU J  1 21  ? -19.719 13.355  78.942  1.00 52.20  ? 21  GLU S CB  1 
ATOM   10126 C  CG  . GLU J  1 21  ? -18.741 14.450  78.528  1.00 54.11  ? 21  GLU S CG  1 
ATOM   10127 C  CD  . GLU J  1 21  ? -19.354 15.844  78.481  1.00 56.59  ? 21  GLU S CD  1 
ATOM   10128 O  OE1 . GLU J  1 21  ? -20.527 16.023  78.877  1.00 56.99  ? 21  GLU S OE1 1 
ATOM   10129 O  OE2 . GLU J  1 21  ? -18.649 16.778  78.037  1.00 58.51  ? 21  GLU S OE2 1 
ATOM   10130 N  N   . GLN J  1 22  ? -16.799 11.745  79.103  1.00 50.45  ? 22  GLN S N   1 
ATOM   10131 C  CA  . GLN J  1 22  ? -15.562 11.505  79.861  1.00 50.90  ? 22  GLN S CA  1 
ATOM   10132 C  C   . GLN J  1 22  ? -14.550 12.613  79.530  1.00 53.07  ? 22  GLN S C   1 
ATOM   10133 O  O   . GLN J  1 22  ? -13.957 12.615  78.442  1.00 53.30  ? 22  GLN S O   1 
ATOM   10134 C  CB  . GLN J  1 22  ? -14.998 10.118  79.531  1.00 49.31  ? 22  GLN S CB  1 
ATOM   10135 C  CG  . GLN J  1 22  ? -14.002 9.602   80.558  1.00 49.65  ? 22  GLN S CG  1 
ATOM   10136 C  CD  . GLN J  1 22  ? -13.241 8.360   80.104  1.00 48.77  ? 22  GLN S CD  1 
ATOM   10137 O  OE1 . GLN J  1 22  ? -13.419 7.879   78.984  1.00 47.94  ? 22  GLN S OE1 1 
ATOM   10138 N  NE2 . GLN J  1 22  ? -12.383 7.835   80.982  1.00 49.21  ? 22  GLN S NE2 1 
ATOM   10139 N  N   . LYS J  1 23  ? -14.373 13.558  80.456  1.00 54.96  ? 23  LYS S N   1 
ATOM   10140 C  CA  . LYS J  1 23  ? -13.538 14.749  80.198  1.00 57.61  ? 23  LYS S CA  1 
ATOM   10141 C  C   . LYS J  1 23  ? -12.057 14.412  79.990  1.00 58.27  ? 23  LYS S C   1 
ATOM   10142 O  O   . LYS J  1 23  ? -11.403 14.997  79.127  1.00 59.76  ? 23  LYS S O   1 
ATOM   10143 C  CB  . LYS J  1 23  ? -13.682 15.795  81.315  1.00 59.87  ? 23  LYS S CB  1 
ATOM   10144 C  CG  . LYS J  1 23  ? -15.001 16.561  81.305  1.00 60.47  ? 23  LYS S CG  1 
ATOM   10145 C  CD  . LYS J  1 23  ? -14.802 18.019  81.719  1.00 63.90  ? 23  LYS S CD  1 
ATOM   10146 C  CE  . LYS J  1 23  ? -16.095 18.679  82.168  1.00 64.84  ? 23  LYS S CE  1 
ATOM   10147 N  NZ  . LYS J  1 23  ? -16.387 18.391  83.601  1.00 64.82  ? 23  LYS S NZ  1 
ATOM   10148 N  N   . GLU J  1 24  ? -11.549 13.475  80.788  1.00 57.43  ? 24  GLU S N   1 
ATOM   10149 C  CA  . GLU J  1 24  ? -10.186 12.966  80.654  1.00 58.10  ? 24  GLU S CA  1 
ATOM   10150 C  C   . GLU J  1 24  ? -10.204 11.441  80.536  1.00 55.73  ? 24  GLU S C   1 
ATOM   10151 O  O   . GLU J  1 24  ? -11.000 10.773  81.200  1.00 54.09  ? 24  GLU S O   1 
ATOM   10152 C  CB  . GLU J  1 24  ? -9.339  13.402  81.857  1.00 60.33  ? 24  GLU S CB  1 
ATOM   10153 C  CG  . GLU J  1 24  ? -8.701  14.784  81.722  1.00 63.59  ? 24  GLU S CG  1 
ATOM   10154 C  CD  . GLU J  1 24  ? -9.628  15.958  82.020  1.00 64.74  ? 24  GLU S CD  1 
ATOM   10155 O  OE1 . GLU J  1 24  ? -10.599 15.801  82.790  1.00 63.60  ? 24  GLU S OE1 1 
ATOM   10156 O  OE2 . GLU J  1 24  ? -9.366  17.061  81.487  1.00 67.13  ? 24  GLU S OE2 1 
ATOM   10157 N  N   . SER J  1 25  ? -9.309  10.894  79.711  1.00 55.90  ? 25  SER S N   1 
ATOM   10158 C  CA  . SER J  1 25  ? -9.238  9.442   79.463  1.00 54.14  ? 25  SER S CA  1 
ATOM   10159 C  C   . SER J  1 25  ? -9.006  8.595   80.725  1.00 53.82  ? 25  SER S C   1 
ATOM   10160 O  O   . SER J  1 25  ? -9.494  7.464   80.803  1.00 52.13  ? 25  SER S O   1 
ATOM   10161 C  CB  . SER J  1 25  ? -8.157  9.132   78.417  1.00 55.14  ? 25  SER S CB  1 
ATOM   10162 O  OG  . SER J  1 25  ? -6.904  9.680   78.798  1.00 57.73  ? 25  SER S OG  1 
ATOM   10163 N  N   . ASN J  1 26  ? -8.269  9.147   81.698  1.00 55.73  ? 26  ASN S N   1 
ATOM   10164 C  CA  . ASN J  1 26  ? -8.077  8.514   83.021  1.00 55.85  ? 26  ASN S CA  1 
ATOM   10165 C  C   . ASN J  1 26  ? -9.084  8.978   84.094  1.00 55.54  ? 26  ASN S C   1 
ATOM   10166 O  O   . ASN J  1 26  ? -8.944  8.620   85.267  1.00 56.02  ? 26  ASN S O   1 
ATOM   10167 C  CB  . ASN J  1 26  ? -6.622  8.688   83.517  1.00 58.45  ? 26  ASN S CB  1 
ATOM   10168 C  CG  . ASN J  1 26  ? -6.291  10.115  83.957  1.00 60.90  ? 26  ASN S CG  1 
ATOM   10169 O  OD1 . ASN J  1 26  ? -6.846  11.090  83.451  1.00 61.01  ? 26  ASN S OD1 1 
ATOM   10170 N  ND2 . ASN J  1 26  ? -5.361  10.235  84.900  1.00 63.17  ? 26  ASN S ND2 1 
ATOM   10171 N  N   . GLY J  1 27  ? -10.095 9.753   83.688  1.00 54.98  ? 27  GLY S N   1 
ATOM   10172 C  CA  . GLY J  1 27  ? -11.117 10.288  84.594  1.00 55.03  ? 27  GLY S CA  1 
ATOM   10173 C  C   . GLY J  1 27  ? -12.409 9.487   84.526  1.00 52.75  ? 27  GLY S C   1 
ATOM   10174 O  O   . GLY J  1 27  ? -12.515 8.541   83.739  1.00 51.17  ? 27  GLY S O   1 
ATOM   10175 N  N   . PRO J  1 28  ? -13.404 9.859   85.355  1.00 52.88  ? 28  PRO S N   1 
ATOM   10176 C  CA  . PRO J  1 28  ? -14.672 9.125   85.404  1.00 51.17  ? 28  PRO S CA  1 
ATOM   10177 C  C   . PRO J  1 28  ? -15.559 9.389   84.184  1.00 50.15  ? 28  PRO S C   1 
ATOM   10178 O  O   . PRO J  1 28  ? -15.405 10.417  83.528  1.00 51.06  ? 28  PRO S O   1 
ATOM   10179 C  CB  . PRO J  1 28  ? -15.331 9.667   86.676  1.00 52.35  ? 28  PRO S CB  1 
ATOM   10180 C  CG  . PRO J  1 28  ? -14.807 11.060  86.802  1.00 54.54  ? 28  PRO S CG  1 
ATOM   10181 C  CD  . PRO J  1 28  ? -13.404 11.025  86.261  1.00 55.05  ? 28  PRO S CD  1 
ATOM   10182 N  N   . VAL J  1 29  ? -16.467 8.457   83.891  1.00 48.57  ? 29  VAL S N   1 
ATOM   10183 C  CA  . VAL J  1 29  ? -17.483 8.648   82.847  1.00 47.87  ? 29  VAL S CA  1 
ATOM   10184 C  C   . VAL J  1 29  ? -18.839 9.020   83.462  1.00 48.33  ? 29  VAL S C   1 
ATOM   10185 O  O   . VAL J  1 29  ? -19.449 8.210   84.181  1.00 47.85  ? 29  VAL S O   1 
ATOM   10186 C  CB  . VAL J  1 29  ? -17.687 7.387   81.973  1.00 46.19  ? 29  VAL S CB  1 
ATOM   10187 C  CG1 . VAL J  1 29  ? -18.648 7.693   80.825  1.00 45.81  ? 29  VAL S CG1 1 
ATOM   10188 C  CG2 . VAL J  1 29  ? -16.357 6.870   81.434  1.00 46.04  ? 29  VAL S CG2 1 
ATOM   10189 N  N   . LYS J  1 30  ? -19.313 10.232  83.162  1.00 49.56  ? 30  LYS S N   1 
ATOM   10190 C  CA  . LYS J  1 30  ? -20.691 10.627  83.487  1.00 50.25  ? 30  LYS S CA  1 
ATOM   10191 C  C   . LYS J  1 30  ? -21.671 9.954   82.517  1.00 49.06  ? 30  LYS S C   1 
ATOM   10192 O  O   . LYS J  1 30  ? -21.515 10.058  81.297  1.00 48.60  ? 30  LYS S O   1 
ATOM   10193 C  CB  . LYS J  1 30  ? -20.877 12.153  83.448  1.00 52.35  ? 30  LYS S CB  1 
ATOM   10194 C  CG  . LYS J  1 30  ? -20.425 12.860  84.719  1.00 54.22  ? 30  LYS S CG  1 
ATOM   10195 C  CD  . LYS J  1 30  ? -21.166 14.175  84.941  1.00 56.61  ? 30  LYS S CD  1 
ATOM   10196 C  CE  . LYS J  1 30  ? -20.986 14.691  86.361  1.00 58.57  ? 30  LYS S CE  1 
ATOM   10197 N  NZ  . LYS J  1 30  ? -19.645 15.285  86.600  1.00 59.86  ? 30  LYS S NZ  1 
ATOM   10198 N  N   . VAL J  1 31  ? -22.667 9.266   83.075  1.00 48.82  ? 31  VAL S N   1 
ATOM   10199 C  CA  . VAL J  1 31  ? -23.709 8.585   82.306  1.00 48.13  ? 31  VAL S CA  1 
ATOM   10200 C  C   . VAL J  1 31  ? -25.044 9.243   82.655  1.00 49.68  ? 31  VAL S C   1 
ATOM   10201 O  O   . VAL J  1 31  ? -25.404 9.292   83.837  1.00 50.60  ? 31  VAL S O   1 
ATOM   10202 C  CB  . VAL J  1 31  ? -23.746 7.081   82.669  1.00 46.99  ? 31  VAL S CB  1 
ATOM   10203 C  CG1 . VAL J  1 31  ? -24.905 6.366   81.967  1.00 46.73  ? 31  VAL S CG1 1 
ATOM   10204 C  CG2 . VAL J  1 31  ? -22.398 6.424   82.360  1.00 45.83  ? 31  VAL S CG2 1 
ATOM   10205 N  N   . TRP J  1 32  ? -25.769 9.764   81.658  1.00 50.20  ? 32  TRP S N   1 
ATOM   10206 C  CA  . TRP J  1 32  ? -27.070 10.400  81.930  1.00 52.06  ? 32  TRP S CA  1 
ATOM   10207 C  C   . TRP J  1 32  ? -28.044 10.392  80.752  1.00 52.39  ? 32  TRP S C   1 
ATOM   10208 O  O   . TRP J  1 32  ? -27.635 10.370  79.595  1.00 51.57  ? 32  TRP S O   1 
ATOM   10209 C  CB  . TRP J  1 32  ? -26.883 11.841  82.461  1.00 54.05  ? 32  TRP S CB  1 
ATOM   10210 C  CG  . TRP J  1 32  ? -26.723 12.905  81.394  1.00 54.99  ? 32  TRP S CG  1 
ATOM   10211 C  CD1 . TRP J  1 32  ? -27.692 13.753  80.928  1.00 56.96  ? 32  TRP S CD1 1 
ATOM   10212 C  CD2 . TRP J  1 32  ? -25.528 13.230  80.670  1.00 54.36  ? 32  TRP S CD2 1 
ATOM   10213 N  NE1 . TRP J  1 32  ? -27.175 14.580  79.959  1.00 57.55  ? 32  TRP S NE1 1 
ATOM   10214 C  CE2 . TRP J  1 32  ? -25.849 14.285  79.783  1.00 56.00  ? 32  TRP S CE2 1 
ATOM   10215 C  CE3 . TRP J  1 32  ? -24.216 12.735  80.685  1.00 52.89  ? 32  TRP S CE3 1 
ATOM   10216 C  CZ2 . TRP J  1 32  ? -24.903 14.855  78.915  1.00 56.18  ? 32  TRP S CZ2 1 
ATOM   10217 C  CZ3 . TRP J  1 32  ? -23.273 13.303  79.820  1.00 53.09  ? 32  TRP S CZ3 1 
ATOM   10218 C  CH2 . TRP J  1 32  ? -23.626 14.352  78.947  1.00 54.71  ? 32  TRP S CH2 1 
ATOM   10219 N  N   . GLY J  1 33  ? -29.334 10.441  81.083  1.00 53.88  ? 33  GLY S N   1 
ATOM   10220 C  CA  . GLY J  1 33  ? -30.418 10.461  80.095  1.00 54.80  ? 33  GLY S CA  1 
ATOM   10221 C  C   . GLY J  1 33  ? -31.772 10.131  80.705  1.00 56.41  ? 33  GLY S C   1 
ATOM   10222 O  O   . GLY J  1 33  ? -31.969 10.301  81.908  1.00 57.40  ? 33  GLY S O   1 
ATOM   10223 N  N   . SER J  1 34  ? -32.696 9.654   79.869  1.00 56.92  ? 34  SER S N   1 
ATOM   10224 C  CA  . SER J  1 34  ? -34.062 9.309   80.287  1.00 58.87  ? 34  SER S CA  1 
ATOM   10225 C  C   . SER J  1 34  ? -34.520 8.005   79.638  1.00 58.19  ? 34  SER S C   1 
ATOM   10226 O  O   . SER J  1 34  ? -34.338 7.822   78.436  1.00 57.46  ? 34  SER S O   1 
ATOM   10227 C  CB  . SER J  1 34  ? -35.027 10.422  79.885  1.00 61.65  ? 34  SER S CB  1 
ATOM   10228 O  OG  . SER J  1 34  ? -34.605 11.674  80.393  1.00 62.69  ? 34  SER S OG  1 
ATOM   10229 N  N   . ILE J  1 35  ? -35.110 7.112   80.434  1.00 58.74  ? 35  ILE S N   1 
ATOM   10230 C  CA  . ILE J  1 35  ? -35.695 5.855   79.945  1.00 58.79  ? 35  ILE S CA  1 
ATOM   10231 C  C   . ILE J  1 35  ? -37.152 5.818   80.405  1.00 61.84  ? 35  ILE S C   1 
ATOM   10232 O  O   . ILE J  1 35  ? -37.435 6.139   81.555  1.00 63.03  ? 35  ILE S O   1 
ATOM   10233 C  CB  . ILE J  1 35  ? -34.951 4.615   80.493  1.00 56.94  ? 35  ILE S CB  1 
ATOM   10234 C  CG1 . ILE J  1 35  ? -33.453 4.704   80.171  1.00 54.28  ? 35  ILE S CG1 1 
ATOM   10235 C  CG2 . ILE J  1 35  ? -35.550 3.325   79.926  1.00 57.39  ? 35  ILE S CG2 1 
ATOM   10236 C  CD1 . ILE J  1 35  ? -32.598 3.709   80.920  1.00 52.81  ? 35  ILE S CD1 1 
ATOM   10237 N  N   . LYS J  1 36  ? -38.058 5.424   79.506  1.00 63.30  ? 36  LYS S N   1 
ATOM   10238 C  CA  . LYS J  1 36  ? -39.502 5.416   79.772  1.00 66.69  ? 36  LYS S CA  1 
ATOM   10239 C  C   . LYS J  1 36  ? -40.134 4.079   79.384  1.00 67.55  ? 36  LYS S C   1 
ATOM   10240 O  O   . LYS J  1 36  ? -39.490 3.241   78.754  1.00 65.58  ? 36  LYS S O   1 
ATOM   10241 C  CB  . LYS J  1 36  ? -40.192 6.584   79.050  1.00 68.80  ? 36  LYS S CB  1 
ATOM   10242 C  CG  . LYS J  1 36  ? -39.964 6.643   77.550  1.00 67.99  ? 36  LYS S CG  1 
ATOM   10243 C  CD  . LYS J  1 36  ? -40.708 7.816   76.938  1.00 70.58  ? 36  LYS S CD  1 
ATOM   10244 C  CE  . LYS J  1 36  ? -40.482 7.898   75.437  1.00 70.04  ? 36  LYS S CE  1 
ATOM   10245 N  NZ  . LYS J  1 36  ? -41.304 8.978   74.828  1.00 73.04  ? 36  LYS S NZ  1 
ATOM   10246 N  N   . GLY J  1 37  ? -41.392 3.891   79.783  1.00 70.82  ? 37  GLY S N   1 
ATOM   10247 C  CA  . GLY J  1 37  ? -42.118 2.634   79.568  1.00 72.43  ? 37  GLY S CA  1 
ATOM   10248 C  C   . GLY J  1 37  ? -41.738 1.493   80.506  1.00 71.69  ? 37  GLY S C   1 
ATOM   10249 O  O   . GLY J  1 37  ? -42.044 0.331   80.218  1.00 72.51  ? 37  GLY S O   1 
ATOM   10250 N  N   . LEU J  1 38  ? -41.085 1.823   81.628  1.00 70.51  ? 38  LEU S N   1 
ATOM   10251 C  CA  . LEU J  1 38  ? -40.654 0.834   82.623  1.00 69.93  ? 38  LEU S CA  1 
ATOM   10252 C  C   . LEU J  1 38  ? -41.704 0.677   83.713  1.00 73.34  ? 38  LEU S C   1 
ATOM   10253 O  O   . LEU J  1 38  ? -42.505 1.580   83.959  1.00 75.62  ? 38  LEU S O   1 
ATOM   10254 C  CB  . LEU J  1 38  ? -39.325 1.251   83.272  1.00 67.03  ? 38  LEU S CB  1 
ATOM   10255 C  CG  . LEU J  1 38  ? -38.069 1.244   82.387  1.00 63.68  ? 38  LEU S CG  1 
ATOM   10256 C  CD1 . LEU J  1 38  ? -36.961 2.070   83.024  1.00 61.70  ? 38  LEU S CD1 1 
ATOM   10257 C  CD2 . LEU J  1 38  ? -37.596 -0.179  82.111  1.00 62.63  ? 38  LEU S CD2 1 
ATOM   10258 N  N   . THR J  1 39  ? -41.695 -0.480  84.365  1.00 73.98  ? 39  THR S N   1 
ATOM   10259 C  CA  . THR J  1 39  ? -42.469 -0.678  85.583  1.00 77.05  ? 39  THR S CA  1 
ATOM   10260 C  C   . THR J  1 39  ? -41.768 0.093   86.707  1.00 75.90  ? 39  THR S C   1 
ATOM   10261 O  O   . THR J  1 39  ? -40.533 0.164   86.736  1.00 72.72  ? 39  THR S O   1 
ATOM   10262 C  CB  . THR J  1 39  ? -42.593 -2.173  85.935  1.00 78.26  ? 39  THR S CB  1 
ATOM   10263 O  OG1 . THR J  1 39  ? -41.290 -2.760  86.024  1.00 75.13  ? 39  THR S OG1 1 
ATOM   10264 C  CG2 . THR J  1 39  ? -43.389 -2.908  84.863  1.00 80.09  ? 39  THR S CG2 1 
ATOM   10265 N  N   . GLU J  1 40  ? -42.551 0.691   87.603  1.00 78.73  ? 40  GLU S N   1 
ATOM   10266 C  CA  . GLU J  1 40  ? -42.005 1.459   88.730  1.00 78.31  ? 40  GLU S CA  1 
ATOM   10267 C  C   . GLU J  1 40  ? -41.020 0.602   89.530  1.00 76.52  ? 40  GLU S C   1 
ATOM   10268 O  O   . GLU J  1 40  ? -41.306 -0.560  89.822  1.00 77.76  ? 40  GLU S O   1 
ATOM   10269 C  CB  . GLU J  1 40  ? -43.143 1.955   89.642  1.00 82.49  ? 40  GLU S CB  1 
ATOM   10270 C  CG  . GLU J  1 40  ? -42.695 2.811   90.827  1.00 82.75  ? 40  GLU S CG  1 
ATOM   10271 C  CD  . GLU J  1 40  ? -43.841 3.302   91.703  1.00 87.23  ? 40  GLU S CD  1 
ATOM   10272 O  OE1 . GLU J  1 40  ? -45.023 3.159   91.320  1.00 90.24  ? 40  GLU S OE1 1 
ATOM   10273 O  OE2 . GLU J  1 40  ? -43.553 3.842   92.791  1.00 88.00  ? 40  GLU S OE2 1 
ATOM   10274 N  N   . GLY J  1 41  ? -39.859 1.173   89.855  1.00 73.89  ? 41  GLY S N   1 
ATOM   10275 C  CA  . GLY J  1 41  ? -38.881 0.525   90.736  1.00 72.53  ? 41  GLY S CA  1 
ATOM   10276 C  C   . GLY J  1 41  ? -37.487 0.423   90.142  1.00 68.67  ? 41  GLY S C   1 
ATOM   10277 O  O   . GLY J  1 41  ? -37.132 1.171   89.224  1.00 66.94  ? 41  GLY S O   1 
ATOM   10278 N  N   . LEU J  1 42  ? -36.700 -0.513  90.671  1.00 67.65  ? 42  LEU S N   1 
ATOM   10279 C  CA  . LEU J  1 42  ? -35.288 -0.667  90.293  1.00 64.37  ? 42  LEU S CA  1 
ATOM   10280 C  C   . LEU J  1 42  ? -35.167 -1.600  89.089  1.00 63.06  ? 42  LEU S C   1 
ATOM   10281 O  O   . LEU J  1 42  ? -35.900 -2.587  88.987  1.00 64.73  ? 42  LEU S O   1 
ATOM   10282 C  CB  . LEU J  1 42  ? -34.460 -1.197  91.475  1.00 64.33  ? 42  LEU S CB  1 
ATOM   10283 C  CG  . LEU J  1 42  ? -34.223 -0.243  92.665  1.00 65.22  ? 42  LEU S CG  1 
ATOM   10284 C  CD1 . LEU J  1 42  ? -35.513 0.155   93.373  1.00 68.51  ? 42  LEU S CD1 1 
ATOM   10285 C  CD2 . LEU J  1 42  ? -33.254 -0.856  93.668  1.00 64.98  ? 42  LEU S CD2 1 
ATOM   10286 N  N   . HIS J  1 43  ? -34.244 -1.276  88.181  1.00 60.34  ? 43  HIS S N   1 
ATOM   10287 C  CA  . HIS J  1 43  ? -34.022 -2.047  86.954  1.00 59.09  ? 43  HIS S CA  1 
ATOM   10288 C  C   . HIS J  1 43  ? -32.526 -2.138  86.648  1.00 56.35  ? 43  HIS S C   1 
ATOM   10289 O  O   . HIS J  1 43  ? -31.848 -1.113  86.562  1.00 54.84  ? 43  HIS S O   1 
ATOM   10290 C  CB  . HIS J  1 43  ? -34.744 -1.383  85.770  1.00 59.24  ? 43  HIS S CB  1 
ATOM   10291 C  CG  . HIS J  1 43  ? -36.236 -1.496  85.829  1.00 62.20  ? 43  HIS S CG  1 
ATOM   10292 N  ND1 . HIS J  1 43  ? -36.939 -2.449  85.123  1.00 63.52  ? 43  HIS S ND1 1 
ATOM   10293 C  CD2 . HIS J  1 43  ? -37.161 -0.783  86.519  1.00 64.47  ? 43  HIS S CD2 1 
ATOM   10294 C  CE1 . HIS J  1 43  ? -38.230 -2.316  85.371  1.00 66.44  ? 43  HIS S CE1 1 
ATOM   10295 N  NE2 . HIS J  1 43  ? -38.392 -1.314  86.218  1.00 67.05  ? 43  HIS S NE2 1 
ATOM   10296 N  N   . GLY J  1 44  ? -32.028 -3.363  86.479  1.00 56.00  ? 44  GLY S N   1 
ATOM   10297 C  CA  . GLY J  1 44  ? -30.624 -3.604  86.156  1.00 53.91  ? 44  GLY S CA  1 
ATOM   10298 C  C   . GLY J  1 44  ? -30.171 -2.845  84.915  1.00 52.04  ? 44  GLY S C   1 
ATOM   10299 O  O   . GLY J  1 44  ? -30.912 -2.742  83.935  1.00 52.35  ? 44  GLY S O   1 
ATOM   10300 N  N   . PHE J  1 45  ? -28.953 -2.312  84.975  1.00 50.39  ? 45  PHE S N   1 
ATOM   10301 C  CA  . PHE J  1 45  ? -28.415 -1.410  83.954  1.00 48.88  ? 45  PHE S CA  1 
ATOM   10302 C  C   . PHE J  1 45  ? -26.987 -1.860  83.650  1.00 47.44  ? 45  PHE S C   1 
ATOM   10303 O  O   . PHE J  1 45  ? -26.089 -1.690  84.483  1.00 47.07  ? 45  PHE S O   1 
ATOM   10304 C  CB  . PHE J  1 45  ? -28.467 0.027   84.501  1.00 49.01  ? 45  PHE S CB  1 
ATOM   10305 C  CG  . PHE J  1 45  ? -28.338 1.107   83.456  1.00 48.25  ? 45  PHE S CG  1 
ATOM   10306 C  CD1 . PHE J  1 45  ? -29.203 1.159   82.365  1.00 48.66  ? 45  PHE S CD1 1 
ATOM   10307 C  CD2 . PHE J  1 45  ? -27.387 2.114   83.600  1.00 47.50  ? 45  PHE S CD2 1 
ATOM   10308 C  CE1 . PHE J  1 45  ? -29.092 2.170   81.418  1.00 48.24  ? 45  PHE S CE1 1 
ATOM   10309 C  CE2 . PHE J  1 45  ? -27.274 3.128   82.661  1.00 47.15  ? 45  PHE S CE2 1 
ATOM   10310 C  CZ  . PHE J  1 45  ? -28.126 3.157   81.568  1.00 47.49  ? 45  PHE S CZ  1 
ATOM   10311 N  N   . HIS J  1 46  ? -26.792 -2.462  82.472  1.00 46.92  ? 46  HIS S N   1 
ATOM   10312 C  CA  . HIS J  1 46  ? -25.563 -3.214  82.160  1.00 46.16  ? 46  HIS S CA  1 
ATOM   10313 C  C   . HIS J  1 46  ? -24.987 -2.905  80.779  1.00 45.10  ? 46  HIS S C   1 
ATOM   10314 O  O   . HIS J  1 46  ? -25.735 -2.739  79.806  1.00 45.25  ? 46  HIS S O   1 
ATOM   10315 C  CB  . HIS J  1 46  ? -25.828 -4.730  82.221  1.00 47.33  ? 46  HIS S CB  1 
ATOM   10316 C  CG  . HIS J  1 46  ? -26.380 -5.201  83.526  1.00 48.74  ? 46  HIS S CG  1 
ATOM   10317 N  ND1 . HIS J  1 46  ? -27.554 -5.913  83.619  1.00 50.44  ? 46  HIS S ND1 1 
ATOM   10318 C  CD2 . HIS J  1 46  ? -25.926 -5.055  84.792  1.00 49.00  ? 46  HIS S CD2 1 
ATOM   10319 C  CE1 . HIS J  1 46  ? -27.800 -6.190  84.886  1.00 51.67  ? 46  HIS S CE1 1 
ATOM   10320 N  NE2 . HIS J  1 46  ? -26.827 -5.680  85.619  1.00 50.80  ? 46  HIS S NE2 1 
ATOM   10321 N  N   . VAL J  1 47  ? -23.657 -2.852  80.696  1.00 44.28  ? 47  VAL S N   1 
ATOM   10322 C  CA  . VAL J  1 47  ? -22.959 -2.873  79.408  1.00 43.66  ? 47  VAL S CA  1 
ATOM   10323 C  C   . VAL J  1 47  ? -22.576 -4.321  79.103  1.00 44.27  ? 47  VAL S C   1 
ATOM   10324 O  O   . VAL J  1 47  ? -21.815 -4.939  79.841  1.00 44.57  ? 47  VAL S O   1 
ATOM   10325 C  CB  . VAL J  1 47  ? -21.711 -1.968  79.398  1.00 42.91  ? 47  VAL S CB  1 
ATOM   10326 C  CG1 . VAL J  1 47  ? -21.000 -2.041  78.047  1.00 42.62  ? 47  VAL S CG1 1 
ATOM   10327 C  CG2 . VAL J  1 47  ? -22.099 -0.531  79.737  1.00 42.69  ? 47  VAL S CG2 1 
ATOM   10328 N  N   . HIS J  1 48  ? -23.130 -4.862  78.023  1.00 44.76  ? 48  HIS S N   1 
ATOM   10329 C  CA  . HIS J  1 48  ? -22.823 -6.222  77.595  1.00 45.76  ? 48  HIS S CA  1 
ATOM   10330 C  C   . HIS J  1 48  ? -21.702 -6.171  76.560  1.00 45.41  ? 48  HIS S C   1 
ATOM   10331 O  O   . HIS J  1 48  ? -21.423 -5.116  75.999  1.00 44.45  ? 48  HIS S O   1 
ATOM   10332 C  CB  . HIS J  1 48  ? -24.079 -6.919  77.069  1.00 47.01  ? 48  HIS S CB  1 
ATOM   10333 C  CG  . HIS J  1 48  ? -25.111 -7.174  78.131  1.00 47.94  ? 48  HIS S CG  1 
ATOM   10334 N  ND1 . HIS J  1 48  ? -25.616 -8.431  78.394  1.00 49.72  ? 48  HIS S ND1 1 
ATOM   10335 C  CD2 . HIS J  1 48  ? -25.712 -6.335  79.010  1.00 47.61  ? 48  HIS S CD2 1 
ATOM   10336 C  CE1 . HIS J  1 48  ? -26.494 -8.352  79.379  1.00 50.47  ? 48  HIS S CE1 1 
ATOM   10337 N  NE2 . HIS J  1 48  ? -26.570 -7.092  79.772  1.00 49.20  ? 48  HIS S NE2 1 
ATOM   10338 N  N   . GLU J  1 49  ? -21.072 -7.322  76.327  1.00 46.46  ? 49  GLU S N   1 
ATOM   10339 C  CA  . GLU J  1 49  ? -19.783 -7.407  75.635  1.00 46.54  ? 49  GLU S CA  1 
ATOM   10340 C  C   . GLU J  1 49  ? -19.840 -6.943  74.172  1.00 46.41  ? 49  GLU S C   1 
ATOM   10341 O  O   . GLU J  1 49  ? -19.024 -6.116  73.728  1.00 45.70  ? 49  GLU S O   1 
ATOM   10342 C  CB  . GLU J  1 49  ? -19.259 -8.853  75.706  1.00 48.21  ? 49  GLU S CB  1 
ATOM   10343 C  CG  . GLU J  1 49  ? -17.814 -9.041  75.255  1.00 48.72  ? 49  GLU S CG  1 
ATOM   10344 C  CD  . GLU J  1 49  ? -17.339 -10.484 75.342  1.00 50.78  ? 49  GLU S CD  1 
ATOM   10345 O  OE1 . GLU J  1 49  ? -17.996 -11.308 76.010  1.00 51.77  ? 49  GLU S OE1 1 
ATOM   10346 O  OE2 . GLU J  1 49  ? -16.299 -10.805 74.730  1.00 51.76  ? 49  GLU S OE2 1 
ATOM   10347 N  N   . PHE J  1 50  ? -20.812 -7.478  73.443  1.00 47.29  ? 50  PHE S N   1 
ATOM   10348 C  CA  . PHE J  1 50  ? -20.870 -7.325  72.000  1.00 47.74  ? 50  PHE S CA  1 
ATOM   10349 C  C   . PHE J  1 50  ? -21.875 -6.250  71.602  1.00 47.07  ? 50  PHE S C   1 
ATOM   10350 O  O   . PHE J  1 50  ? -22.903 -6.044  72.286  1.00 46.94  ? 50  PHE S O   1 
ATOM   10351 C  CB  . PHE J  1 50  ? -21.191 -8.676  71.350  1.00 49.68  ? 50  PHE S CB  1 
ATOM   10352 C  CG  . PHE J  1 50  ? -20.264 -9.779  71.791  1.00 50.83  ? 50  PHE S CG  1 
ATOM   10353 C  CD1 . PHE J  1 50  ? -18.913 -9.732  71.468  1.00 50.96  ? 50  PHE S CD1 1 
ATOM   10354 C  CD2 . PHE J  1 50  ? -20.729 -10.845 72.555  1.00 52.10  ? 50  PHE S CD2 1 
ATOM   10355 C  CE1 . PHE J  1 50  ? -18.043 -10.737 71.881  1.00 52.35  ? 50  PHE S CE1 1 
ATOM   10356 C  CE2 . PHE J  1 50  ? -19.866 -11.856 72.974  1.00 53.48  ? 50  PHE S CE2 1 
ATOM   10357 C  CZ  . PHE J  1 50  ? -18.520 -11.804 72.637  1.00 53.60  ? 50  PHE S CZ  1 
ATOM   10358 N  N   . GLY J  1 51  ? -21.552 -5.574  70.495  1.00 46.93  ? 51  GLY S N   1 
ATOM   10359 C  CA  . GLY J  1 51  ? -22.429 -4.605  69.842  1.00 46.76  ? 51  GLY S CA  1 
ATOM   10360 C  C   . GLY J  1 51  ? -23.253 -5.248  68.738  1.00 48.26  ? 51  GLY S C   1 
ATOM   10361 O  O   . GLY J  1 51  ? -23.527 -4.619  67.714  1.00 48.60  ? 51  GLY S O   1 
ATOM   10362 N  N   . ASP J  1 52  ? -23.661 -6.497  68.969  1.00 49.40  ? 52  ASP S N   1 
ATOM   10363 C  CA  . ASP J  1 52  ? -24.368 -7.313  68.003  1.00 51.30  ? 52  ASP S CA  1 
ATOM   10364 C  C   . ASP J  1 52  ? -25.853 -7.316  68.390  1.00 52.00  ? 52  ASP S C   1 
ATOM   10365 O  O   . ASP J  1 52  ? -26.243 -7.906  69.409  1.00 52.27  ? 52  ASP S O   1 
ATOM   10366 C  CB  . ASP J  1 52  ? -23.781 -8.728  68.029  1.00 52.64  ? 52  ASP S CB  1 
ATOM   10367 C  CG  . ASP J  1 52  ? -24.385 -9.645  66.991  1.00 54.99  ? 52  ASP S CG  1 
ATOM   10368 O  OD1 . ASP J  1 52  ? -25.514 -9.389  66.531  1.00 55.70  ? 52  ASP S OD1 1 
ATOM   10369 O  OD2 . ASP J  1 52  ? -23.725 -10.645 66.646  1.00 56.46  ? 52  ASP S OD2 1 
ATOM   10370 N  N   . ASN J  1 53  ? -26.668 -6.643  67.576  1.00 52.56  ? 53  ASN S N   1 
ATOM   10371 C  CA  . ASN J  1 53  ? -28.121 -6.592  67.767  1.00 53.72  ? 53  ASN S CA  1 
ATOM   10372 C  C   . ASN J  1 53  ? -28.879 -7.421  66.709  1.00 56.19  ? 53  ASN S C   1 
ATOM   10373 O  O   . ASN J  1 53  ? -30.054 -7.151  66.438  1.00 57.45  ? 53  ASN S O   1 
ATOM   10374 C  CB  . ASN J  1 53  ? -28.597 -5.126  67.759  1.00 52.91  ? 53  ASN S CB  1 
ATOM   10375 C  CG  . ASN J  1 53  ? -29.891 -4.922  68.540  1.00 53.71  ? 53  ASN S CG  1 
ATOM   10376 O  OD1 . ASN J  1 53  ? -29.918 -5.062  69.767  1.00 53.15  ? 53  ASN S OD1 1 
ATOM   10377 N  ND2 . ASN J  1 53  ? -30.969 -4.585  67.832  1.00 55.28  ? 53  ASN S ND2 1 
ATOM   10378 N  N   . THR J  1 54  ? -28.224 -8.436  66.135  1.00 57.20  ? 54  THR S N   1 
ATOM   10379 C  CA  . THR J  1 54  ? -28.824 -9.248  65.064  1.00 59.87  ? 54  THR S CA  1 
ATOM   10380 C  C   . THR J  1 54  ? -29.985 -10.099 65.565  1.00 61.98  ? 54  THR S C   1 
ATOM   10381 O  O   . THR J  1 54  ? -30.940 -10.335 64.826  1.00 64.27  ? 54  THR S O   1 
ATOM   10382 C  CB  . THR J  1 54  ? -27.788 -10.153 64.358  1.00 60.80  ? 54  THR S CB  1 
ATOM   10383 O  OG1 . THR J  1 54  ? -27.108 -10.964 65.317  1.00 60.41  ? 54  THR S OG1 1 
ATOM   10384 C  CG2 . THR J  1 54  ? -26.767 -9.314  63.595  1.00 59.50  ? 54  THR S CG2 1 
ATOM   10385 N  N   . ALA J  1 55  ? -29.884 -10.568 66.808  1.00 61.55  ? 55  ALA S N   1 
ATOM   10386 C  CA  . ALA J  1 55  ? -30.996 -11.204 67.518  1.00 63.45  ? 55  ALA S CA  1 
ATOM   10387 C  C   . ALA J  1 55  ? -31.396 -10.325 68.706  1.00 61.80  ? 55  ALA S C   1 
ATOM   10388 O  O   . ALA J  1 55  ? -31.482 -10.797 69.843  1.00 61.94  ? 55  ALA S O   1 
ATOM   10389 C  CB  . ALA J  1 55  ? -30.596 -12.597 67.975  1.00 64.97  ? 55  ALA S CB  1 
ATOM   10390 N  N   . GLY J  1 56  ? -31.638 -9.042  68.426  1.00 60.56  ? 56  GLY S N   1 
ATOM   10391 C  CA  . GLY J  1 56  ? -32.020 -8.057  69.445  1.00 59.24  ? 56  GLY S CA  1 
ATOM   10392 C  C   . GLY J  1 56  ? -30.997 -7.928  70.563  1.00 57.09  ? 56  GLY S C   1 
ATOM   10393 O  O   . GLY J  1 56  ? -29.791 -7.972  70.317  1.00 55.75  ? 56  GLY S O   1 
ATOM   10394 N  N   . ALA J  1 57  ? -31.481 -7.794  71.796  1.00 57.08  ? 57  ALA S N   1 
ATOM   10395 C  CA  . ALA J  1 57  ? -30.611 -7.755  72.974  1.00 55.47  ? 57  ALA S CA  1 
ATOM   10396 C  C   . ALA J  1 57  ? -29.973 -9.120  73.340  1.00 56.33  ? 57  ALA S C   1 
ATOM   10397 O  O   . ALA J  1 57  ? -29.038 -9.151  74.143  1.00 55.05  ? 57  ALA S O   1 
ATOM   10398 C  CB  . ALA J  1 57  ? -31.375 -7.190  74.165  1.00 55.54  ? 57  ALA S CB  1 
ATOM   10399 N  N   . THR J  1 58  ? -30.460 -10.226 72.763  1.00 58.78  ? 58  THR S N   1 
ATOM   10400 C  CA  . THR J  1 58  ? -29.948 -11.579 73.065  1.00 60.21  ? 58  THR S CA  1 
ATOM   10401 C  C   . THR J  1 58  ? -28.512 -11.814 72.584  1.00 59.11  ? 58  THR S C   1 
ATOM   10402 O  O   . THR J  1 58  ? -27.670 -12.297 73.344  1.00 58.78  ? 58  THR S O   1 
ATOM   10403 C  CB  . THR J  1 58  ? -30.849 -12.678 72.451  1.00 63.57  ? 58  THR S CB  1 
ATOM   10404 O  OG1 . THR J  1 58  ? -32.223 -12.393 72.745  1.00 64.94  ? 58  THR S OG1 1 
ATOM   10405 C  CG2 . THR J  1 58  ? -30.495 -14.063 73.001  1.00 65.54  ? 58  THR S CG2 1 
ATOM   10406 N  N   . SER J  1 59  ? -28.244 -11.462 71.328  1.00 58.82  ? 59  SER S N   1 
ATOM   10407 C  CA  . SER J  1 59  ? -26.913 -11.641 70.711  1.00 58.18  ? 59  SER S CA  1 
ATOM   10408 C  C   . SER J  1 59  ? -25.777 -10.766 71.296  1.00 55.56  ? 59  SER S C   1 
ATOM   10409 O  O   . SER J  1 59  ? -24.603 -11.000 70.993  1.00 55.37  ? 59  SER S O   1 
ATOM   10410 C  CB  . SER J  1 59  ? -27.007 -11.432 69.187  1.00 58.87  ? 59  SER S CB  1 
ATOM   10411 O  OG  . SER J  1 59  ? -27.751 -10.268 68.858  1.00 57.91  ? 59  SER S OG  1 
ATOM   10412 N  N   . ALA J  1 60  ? -26.118 -9.768  72.115  1.00 53.90  ? 60  ALA S N   1 
ATOM   10413 C  CA  . ALA J  1 60  ? -25.118 -8.915  72.793  1.00 51.73  ? 60  ALA S CA  1 
ATOM   10414 C  C   . ALA J  1 60  ? -24.153 -9.641  73.762  1.00 51.76  ? 60  ALA S C   1 
ATOM   10415 O  O   . ALA J  1 60  ? -23.093 -9.095  74.105  1.00 50.43  ? 60  ALA S O   1 
ATOM   10416 C  CB  . ALA J  1 60  ? -25.816 -7.766  73.520  1.00 50.56  ? 60  ALA S CB  1 
ATOM   10417 N  N   . GLY J  1 61  ? -24.531 -10.836 74.221  1.00 53.52  ? 61  GLY S N   1 
ATOM   10418 C  CA  . GLY J  1 61  ? -23.663 -11.671 75.051  1.00 54.11  ? 61  GLY S CA  1 
ATOM   10419 C  C   . GLY J  1 61  ? -23.789 -11.368 76.535  1.00 53.42  ? 61  GLY S C   1 
ATOM   10420 O  O   . GLY J  1 61  ? -24.813 -10.830 76.972  1.00 53.09  ? 61  GLY S O   1 
ATOM   10421 N  N   . PRO J  1 62  ? -22.752 -11.724 77.328  1.00 53.42  ? 62  PRO S N   1 
ATOM   10422 C  CA  . PRO J  1 62  ? -22.780 -11.490 78.771  1.00 53.04  ? 62  PRO S CA  1 
ATOM   10423 C  C   . PRO J  1 62  ? -22.346 -10.065 79.131  1.00 50.72  ? 62  PRO S C   1 
ATOM   10424 O  O   . PRO J  1 62  ? -22.083 -9.239  78.235  1.00 49.37  ? 62  PRO S O   1 
ATOM   10425 C  CB  . PRO J  1 62  ? -21.771 -12.515 79.301  1.00 54.45  ? 62  PRO S CB  1 
ATOM   10426 C  CG  . PRO J  1 62  ? -20.761 -12.629 78.210  1.00 54.38  ? 62  PRO S CG  1 
ATOM   10427 C  CD  . PRO J  1 62  ? -21.473 -12.335 76.909  1.00 54.04  ? 62  PRO S CD  1 
ATOM   10428 N  N   . HIS J  1 63  ? -22.272 -9.785  80.434  1.00 50.46  ? 63  HIS S N   1 
ATOM   10429 C  CA  . HIS J  1 63  ? -21.777 -8.488  80.912  1.00 48.74  ? 63  HIS S CA  1 
ATOM   10430 C  C   . HIS J  1 63  ? -20.307 -8.328  80.504  1.00 48.11  ? 63  HIS S C   1 
ATOM   10431 O  O   . HIS J  1 63  ? -19.532 -9.292  80.539  1.00 49.19  ? 63  HIS S O   1 
ATOM   10432 C  CB  . HIS J  1 63  ? -21.929 -8.322  82.433  1.00 49.08  ? 63  HIS S CB  1 
ATOM   10433 C  CG  . HIS J  1 63  ? -23.346 -8.409  82.923  1.00 49.95  ? 63  HIS S CG  1 
ATOM   10434 N  ND1 . HIS J  1 63  ? -23.673 -8.349  84.261  1.00 50.70  ? 63  HIS S ND1 1 
ATOM   10435 C  CD2 . HIS J  1 63  ? -24.515 -8.580  82.258  1.00 50.51  ? 63  HIS S CD2 1 
ATOM   10436 C  CE1 . HIS J  1 63  ? -24.982 -8.459  84.398  1.00 51.69  ? 63  HIS S CE1 1 
ATOM   10437 N  NE2 . HIS J  1 63  ? -25.516 -8.611  83.199  1.00 51.63  ? 63  HIS S NE2 1 
ATOM   10438 N  N   . PHE J  1 64  ? -19.945 -7.120  80.084  1.00 46.65  ? 64  PHE S N   1 
ATOM   10439 C  CA  . PHE J  1 64  ? -18.566 -6.828  79.696  1.00 46.30  ? 64  PHE S CA  1 
ATOM   10440 C  C   . PHE J  1 64  ? -17.653 -7.061  80.911  1.00 46.96  ? 64  PHE S C   1 
ATOM   10441 O  O   . PHE J  1 64  ? -17.853 -6.471  81.983  1.00 46.65  ? 64  PHE S O   1 
ATOM   10442 C  CB  . PHE J  1 64  ? -18.450 -5.397  79.138  1.00 44.94  ? 64  PHE S CB  1 
ATOM   10443 C  CG  . PHE J  1 64  ? -17.072 -5.030  78.624  1.00 44.87  ? 64  PHE S CG  1 
ATOM   10444 C  CD1 . PHE J  1 64  ? -16.282 -5.947  77.919  1.00 45.80  ? 64  PHE S CD1 1 
ATOM   10445 C  CD2 . PHE J  1 64  ? -16.577 -3.737  78.821  1.00 44.21  ? 64  PHE S CD2 1 
ATOM   10446 C  CE1 . PHE J  1 64  ? -15.027 -5.588  77.456  1.00 46.10  ? 64  PHE S CE1 1 
ATOM   10447 C  CE2 . PHE J  1 64  ? -15.320 -3.375  78.357  1.00 44.52  ? 64  PHE S CE2 1 
ATOM   10448 C  CZ  . PHE J  1 64  ? -14.545 -4.303  77.675  1.00 45.47  ? 64  PHE S CZ  1 
ATOM   10449 N  N   . ASN J  1 65  ? -16.689 -7.962  80.731  1.00 48.15  ? 65  ASN S N   1 
ATOM   10450 C  CA  . ASN J  1 65  ? -15.873 -8.476  81.819  1.00 49.40  ? 65  ASN S CA  1 
ATOM   10451 C  C   . ASN J  1 65  ? -14.477 -8.905  81.313  1.00 50.48  ? 65  ASN S C   1 
ATOM   10452 O  O   . ASN J  1 65  ? -14.150 -10.101 81.308  1.00 52.27  ? 65  ASN S O   1 
ATOM   10453 C  CB  . ASN J  1 65  ? -16.616 -9.645  82.483  1.00 50.79  ? 65  ASN S CB  1 
ATOM   10454 C  CG  . ASN J  1 65  ? -15.906 -10.182 83.714  1.00 52.30  ? 65  ASN S CG  1 
ATOM   10455 O  OD1 . ASN J  1 65  ? -15.298 -9.428  84.478  1.00 51.98  ? 65  ASN S OD1 1 
ATOM   10456 N  ND2 . ASN J  1 65  ? -15.992 -11.496 83.917  1.00 54.27  ? 65  ASN S ND2 1 
ATOM   10457 N  N   . PRO J  1 66  ? -13.652 -7.928  80.878  1.00 49.78  ? 66  PRO S N   1 
ATOM   10458 C  CA  . PRO J  1 66  ? -12.318 -8.247  80.347  1.00 51.03  ? 66  PRO S CA  1 
ATOM   10459 C  C   . PRO J  1 66  ? -11.314 -8.705  81.419  1.00 52.72  ? 66  PRO S C   1 
ATOM   10460 O  O   . PRO J  1 66  ? -10.380 -9.438  81.095  1.00 54.47  ? 66  PRO S O   1 
ATOM   10461 C  CB  . PRO J  1 66  ? -11.874 -6.929  79.701  1.00 49.96  ? 66  PRO S CB  1 
ATOM   10462 C  CG  . PRO J  1 66  ? -12.585 -5.872  80.469  1.00 48.56  ? 66  PRO S CG  1 
ATOM   10463 C  CD  . PRO J  1 66  ? -13.903 -6.471  80.886  1.00 48.20  ? 66  PRO S CD  1 
ATOM   10464 N  N   . LEU J  1 67  ? -11.515 -8.290  82.673  1.00 52.48  ? 67  LEU S N   1 
ATOM   10465 C  CA  . LEU J  1 67  ? -10.647 -8.705  83.793  1.00 54.30  ? 67  LEU S CA  1 
ATOM   10466 C  C   . LEU J  1 67  ? -11.028 -10.049 84.457  1.00 55.89  ? 67  LEU S C   1 
ATOM   10467 O  O   . LEU J  1 67  ? -10.323 -10.488 85.368  1.00 57.72  ? 67  LEU S O   1 
ATOM   10468 C  CB  . LEU J  1 67  ? -10.592 -7.598  84.864  1.00 53.71  ? 67  LEU S CB  1 
ATOM   10469 C  CG  . LEU J  1 67  ? -9.934  -6.265  84.486  1.00 53.02  ? 67  LEU S CG  1 
ATOM   10470 C  CD1 . LEU J  1 67  ? -10.116 -5.250  85.609  1.00 52.68  ? 67  LEU S CD1 1 
ATOM   10471 C  CD2 . LEU J  1 67  ? -8.453  -6.444  84.163  1.00 54.84  ? 67  LEU S CD2 1 
ATOM   10472 N  N   . SER J  1 68  ? -12.122 -10.684 84.016  1.00 55.52  ? 68  SER S N   1 
ATOM   10473 C  CA  . SER J  1 68  ? -12.567 -12.011 84.516  1.00 57.38  ? 68  SER S CA  1 
ATOM   10474 C  C   . SER J  1 68  ? -12.967 -12.038 86.008  1.00 58.00  ? 68  SER S C   1 
ATOM   10475 O  O   . SER J  1 68  ? -12.661 -12.995 86.726  1.00 60.21  ? 68  SER S O   1 
ATOM   10476 C  CB  . SER J  1 68  ? -11.515 -13.102 84.227  1.00 59.92  ? 68  SER S CB  1 
ATOM   10477 O  OG  . SER J  1 68  ? -11.079 -13.061 82.883  1.00 59.67  ? 68  SER S OG  1 
ATOM   10478 N  N   . ARG J  1 69  ? -13.662 -10.988 86.451  1.00 56.29  ? 69  ARG S N   1 
ATOM   10479 C  CA  . ARG J  1 69  ? -14.164 -10.884 87.832  1.00 56.87  ? 69  ARG S CA  1 
ATOM   10480 C  C   . ARG J  1 69  ? -15.586 -11.442 87.903  1.00 56.96  ? 69  ARG S C   1 
ATOM   10481 O  O   . ARG J  1 69  ? -16.190 -11.749 86.871  1.00 56.38  ? 69  ARG S O   1 
ATOM   10482 C  CB  . ARG J  1 69  ? -14.183 -9.426  88.312  1.00 55.41  ? 69  ARG S CB  1 
ATOM   10483 C  CG  . ARG J  1 69  ? -12.890 -8.642  88.127  1.00 55.29  ? 69  ARG S CG  1 
ATOM   10484 C  CD  . ARG J  1 69  ? -11.831 -8.992  89.160  1.00 57.53  ? 69  ARG S CD  1 
ATOM   10485 N  NE  . ARG J  1 69  ? -10.604 -8.214  88.954  1.00 57.75  ? 69  ARG S NE  1 
ATOM   10486 C  CZ  . ARG J  1 69  ? -10.420 -6.933  89.301  1.00 57.06  ? 69  ARG S CZ  1 
ATOM   10487 N  NH1 . ARG J  1 69  ? -11.385 -6.222  89.894  1.00 56.06  ? 69  ARG S NH1 1 
ATOM   10488 N  NH2 . ARG J  1 69  ? -9.245  -6.347  89.050  1.00 57.67  ? 69  ARG S NH2 1 
ATOM   10489 N  N   . LYS J  1 70  ? -16.106 -11.563 89.126  1.00 57.89  ? 70  LYS S N   1 
ATOM   10490 C  CA  . LYS J  1 70  ? -17.510 -11.909 89.363  1.00 58.21  ? 70  LYS S CA  1 
ATOM   10491 C  C   . LYS J  1 70  ? -18.399 -10.670 89.231  1.00 56.11  ? 70  LYS S C   1 
ATOM   10492 O  O   . LYS J  1 70  ? -17.896 -9.544  89.109  1.00 54.55  ? 70  LYS S O   1 
ATOM   10493 C  CB  . LYS J  1 70  ? -17.684 -12.537 90.752  1.00 60.53  ? 70  LYS S CB  1 
ATOM   10494 C  CG  . LYS J  1 70  ? -16.971 -13.870 90.925  1.00 63.11  ? 70  LYS S CG  1 
ATOM   10495 C  CD  . LYS J  1 70  ? -17.068 -14.368 92.357  1.00 65.57  ? 70  LYS S CD  1 
ATOM   10496 C  CE  . LYS J  1 70  ? -16.563 -15.799 92.479  1.00 68.61  ? 70  LYS S CE  1 
ATOM   10497 N  NZ  . LYS J  1 70  ? -16.470 -16.252 93.893  1.00 71.25  ? 70  LYS S NZ  1 
ATOM   10498 N  N   . HIS J  1 71  ? -19.717 -10.887 89.246  1.00 56.38  ? 71  HIS S N   1 
ATOM   10499 C  CA  . HIS J  1 71  ? -20.695 -9.792  89.179  1.00 54.92  ? 71  HIS S CA  1 
ATOM   10500 C  C   . HIS J  1 71  ? -20.781 -9.045  90.513  1.00 55.28  ? 71  HIS S C   1 
ATOM   10501 O  O   . HIS J  1 71  ? -20.688 -9.649  91.580  1.00 57.18  ? 71  HIS S O   1 
ATOM   10502 C  CB  . HIS J  1 71  ? -22.087 -10.307 88.795  1.00 55.63  ? 71  HIS S CB  1 
ATOM   10503 C  CG  . HIS J  1 71  ? -23.115 -9.224  88.667  1.00 54.53  ? 71  HIS S CG  1 
ATOM   10504 N  ND1 . HIS J  1 71  ? -23.203 -8.401  87.566  1.00 52.63  ? 71  HIS S ND1 1 
ATOM   10505 C  CD2 . HIS J  1 71  ? -24.082 -8.812  89.521  1.00 55.36  ? 71  HIS S CD2 1 
ATOM   10506 C  CE1 . HIS J  1 71  ? -24.188 -7.538  87.738  1.00 52.39  ? 71  HIS S CE1 1 
ATOM   10507 N  NE2 . HIS J  1 71  ? -24.738 -7.767  88.916  1.00 54.03  ? 71  HIS S NE2 1 
ATOM   10508 N  N   . GLY J  1 72  ? -20.972 -7.731  90.428  1.00 53.72  ? 72  GLY S N   1 
ATOM   10509 C  CA  . GLY J  1 72  ? -21.105 -6.881  91.594  1.00 54.18  ? 72  GLY S CA  1 
ATOM   10510 C  C   . GLY J  1 72  ? -21.872 -5.609  91.305  1.00 53.00  ? 72  GLY S C   1 
ATOM   10511 O  O   . GLY J  1 72  ? -22.437 -5.433  90.225  1.00 51.87  ? 72  GLY S O   1 
ATOM   10512 N  N   . GLY J  1 73  ? -21.920 -4.741  92.311  1.00 53.59  ? 73  GLY S N   1 
ATOM   10513 C  CA  . GLY J  1 73  ? -22.443 -3.395  92.156  1.00 52.85  ? 73  GLY S CA  1 
ATOM   10514 C  C   . GLY J  1 73  ? -21.383 -2.479  91.562  1.00 51.46  ? 73  GLY S C   1 
ATOM   10515 O  O   . GLY J  1 73  ? -20.213 -2.876  91.444  1.00 51.24  ? 73  GLY S O   1 
ATOM   10516 N  N   . PRO J  1 74  ? -21.781 -1.244  91.187  1.00 50.83  ? 74  PRO S N   1 
ATOM   10517 C  CA  . PRO J  1 74  ? -20.834 -0.265  90.638  1.00 49.88  ? 74  PRO S CA  1 
ATOM   10518 C  C   . PRO J  1 74  ? -19.741 0.205   91.619  1.00 50.85  ? 74  PRO S C   1 
ATOM   10519 O  O   . PRO J  1 74  ? -18.644 0.537   91.174  1.00 50.36  ? 74  PRO S O   1 
ATOM   10520 C  CB  . PRO J  1 74  ? -21.736 0.903   90.199  1.00 49.61  ? 74  PRO S CB  1 
ATOM   10521 C  CG  . PRO J  1 74  ? -22.993 0.747   90.978  1.00 50.89  ? 74  PRO S CG  1 
ATOM   10522 C  CD  . PRO J  1 74  ? -23.164 -0.727  91.190  1.00 51.28  ? 74  PRO S CD  1 
ATOM   10523 N  N   . LYS J  1 75  ? -20.029 0.215   92.925  1.00 52.48  ? 75  LYS S N   1 
ATOM   10524 C  CA  . LYS J  1 75  ? -19.048 0.617   93.945  1.00 53.79  ? 75  LYS S CA  1 
ATOM   10525 C  C   . LYS J  1 75  ? -18.245 -0.546  94.558  1.00 54.69  ? 75  LYS S C   1 
ATOM   10526 O  O   . LYS J  1 75  ? -17.453 -0.318  95.475  1.00 56.12  ? 75  LYS S O   1 
ATOM   10527 C  CB  . LYS J  1 75  ? -19.736 1.421   95.065  1.00 55.48  ? 75  LYS S CB  1 
ATOM   10528 C  CG  . LYS J  1 75  ? -20.632 2.559   94.588  1.00 55.16  ? 75  LYS S CG  1 
ATOM   10529 C  CD  . LYS J  1 75  ? -19.857 3.664   93.873  1.00 54.51  ? 75  LYS S CD  1 
ATOM   10530 C  CE  . LYS J  1 75  ? -20.708 4.343   92.812  1.00 53.53  ? 75  LYS S CE  1 
ATOM   10531 N  NZ  . LYS J  1 75  ? -19.980 5.456   92.144  1.00 53.30  ? 75  LYS S NZ  1 
ATOM   10532 N  N   . ASP J  1 76  ? -18.436 -1.773  94.067  1.00 54.18  ? 76  ASP S N   1 
ATOM   10533 C  CA  . ASP J  1 76  ? -17.647 -2.926  94.523  1.00 55.28  ? 76  ASP S CA  1 
ATOM   10534 C  C   . ASP J  1 76  ? -16.349 -3.044  93.728  1.00 54.64  ? 76  ASP S C   1 
ATOM   10535 O  O   . ASP J  1 76  ? -16.331 -2.791  92.514  1.00 53.04  ? 76  ASP S O   1 
ATOM   10536 C  CB  . ASP J  1 76  ? -18.440 -4.228  94.375  1.00 55.56  ? 76  ASP S CB  1 
ATOM   10537 C  CG  . ASP J  1 76  ? -19.717 -4.235  95.195  1.00 56.71  ? 76  ASP S CG  1 
ATOM   10538 O  OD1 . ASP J  1 76  ? -19.712 -3.708  96.328  1.00 58.09  ? 76  ASP S OD1 1 
ATOM   10539 O  OD2 . ASP J  1 76  ? -20.732 -4.776  94.706  1.00 56.47  ? 76  ASP S OD2 1 
ATOM   10540 N  N   . GLU J  1 77  ? -15.273 -3.435  94.415  1.00 56.16  ? 77  GLU S N   1 
ATOM   10541 C  CA  . GLU J  1 77  ? -14.006 -3.784  93.762  1.00 56.16  ? 77  GLU S CA  1 
ATOM   10542 C  C   . GLU J  1 77  ? -14.215 -4.994  92.841  1.00 55.48  ? 77  GLU S C   1 
ATOM   10543 O  O   . GLU J  1 77  ? -13.835 -4.962  91.662  1.00 54.29  ? 77  GLU S O   1 
ATOM   10544 C  CB  . GLU J  1 77  ? -12.931 -4.100  94.809  1.00 58.54  ? 77  GLU S CB  1 
ATOM   10545 C  CG  . GLU J  1 77  ? -11.530 -4.286  94.244  1.00 59.13  ? 77  GLU S CG  1 
ATOM   10546 C  CD  . GLU J  1 77  ? -10.890 -2.972  93.859  1.00 58.70  ? 77  GLU S CD  1 
ATOM   10547 O  OE1 . GLU J  1 77  ? -10.260 -2.338  94.738  1.00 60.41  ? 77  GLU S OE1 1 
ATOM   10548 O  OE2 . GLU J  1 77  ? -11.017 -2.577  92.683  1.00 57.02  ? 77  GLU S OE2 1 
ATOM   10549 N  N   . GLU J  1 78  ? -14.826 -6.046  93.393  1.00 56.47  ? 78  GLU S N   1 
ATOM   10550 C  CA  . GLU J  1 78  ? -15.216 -7.234  92.627  1.00 56.28  ? 78  GLU S CA  1 
ATOM   10551 C  C   . GLU J  1 78  ? -16.473 -6.949  91.789  1.00 54.43  ? 78  GLU S C   1 
ATOM   10552 O  O   . GLU J  1 78  ? -17.600 -6.986  92.302  1.00 54.77  ? 78  GLU S O   1 
ATOM   10553 C  CB  . GLU J  1 78  ? -15.449 -8.428  93.570  1.00 58.55  ? 78  GLU S CB  1 
ATOM   10554 C  CG  . GLU J  1 78  ? -15.631 -9.775  92.875  1.00 59.22  ? 78  GLU S CG  1 
ATOM   10555 C  CD  . GLU J  1 78  ? -14.382 -10.283 92.163  1.00 59.66  ? 78  GLU S CD  1 
ATOM   10556 O  OE1 . GLU J  1 78  ? -13.274 -9.743  92.378  1.00 59.94  ? 78  GLU S OE1 1 
ATOM   10557 O  OE2 . GLU J  1 78  ? -14.516 -11.247 91.377  1.00 60.07  ? 78  GLU S OE2 1 
ATOM   10558 N  N   . ARG J  1 79  ? -16.264 -6.658  90.504  1.00 52.71  ? 79  ARG S N   1 
ATOM   10559 C  CA  . ARG J  1 79  ? -17.358 -6.374  89.566  1.00 51.12  ? 79  ARG S CA  1 
ATOM   10560 C  C   . ARG J  1 79  ? -16.922 -6.581  88.122  1.00 50.04  ? 79  ARG S C   1 
ATOM   10561 O  O   . ARG J  1 79  ? -15.731 -6.519  87.814  1.00 50.16  ? 79  ARG S O   1 
ATOM   10562 C  CB  . ARG J  1 79  ? -17.851 -4.925  89.728  1.00 50.06  ? 79  ARG S CB  1 
ATOM   10563 C  CG  . ARG J  1 79  ? -16.814 -3.853  89.384  1.00 49.32  ? 79  ARG S CG  1 
ATOM   10564 C  CD  . ARG J  1 79  ? -17.417 -2.459  89.278  1.00 48.42  ? 79  ARG S CD  1 
ATOM   10565 N  NE  . ARG J  1 79  ? -17.878 -2.122  87.925  1.00 46.96  ? 79  ARG S NE  1 
ATOM   10566 C  CZ  . ARG J  1 79  ? -18.288 -0.907  87.542  1.00 46.27  ? 79  ARG S CZ  1 
ATOM   10567 N  NH1 . ARG J  1 79  ? -18.318 0.107   88.409  1.00 46.92  ? 79  ARG S NH1 1 
ATOM   10568 N  NH2 . ARG J  1 79  ? -18.676 -0.696  86.285  1.00 45.18  ? 79  ARG S NH2 1 
ATOM   10569 N  N   . HIS J  1 80  ? -17.898 -6.793  87.242  1.00 49.23  ? 80  HIS S N   1 
ATOM   10570 C  CA  . HIS J  1 80  ? -17.666 -6.750  85.794  1.00 48.16  ? 80  HIS S CA  1 
ATOM   10571 C  C   . HIS J  1 80  ? -17.555 -5.263  85.418  1.00 46.67  ? 80  HIS S C   1 
ATOM   10572 O  O   . HIS J  1 80  ? -18.158 -4.411  86.093  1.00 46.34  ? 80  HIS S O   1 
ATOM   10573 C  CB  . HIS J  1 80  ? -18.818 -7.410  85.011  1.00 48.17  ? 80  HIS S CB  1 
ATOM   10574 C  CG  . HIS J  1 80  ? -19.111 -8.829  85.409  1.00 50.01  ? 80  HIS S CG  1 
ATOM   10575 N  ND1 . HIS J  1 80  ? -20.370 -9.390  85.323  1.00 50.69  ? 80  HIS S ND1 1 
ATOM   10576 C  CD2 . HIS J  1 80  ? -18.304 -9.798  85.896  1.00 51.59  ? 80  HIS S CD2 1 
ATOM   10577 C  CE1 . HIS J  1 80  ? -20.316 -10.649 85.720  1.00 52.65  ? 80  HIS S CE1 1 
ATOM   10578 N  NE2 . HIS J  1 80  ? -19.076 -10.920 86.079  1.00 53.19  ? 80  HIS S NE2 1 
ATOM   10579 N  N   . VAL J  1 81  ? -16.796 -4.943  84.360  1.00 45.99  ? 81  VAL S N   1 
ATOM   10580 C  CA  . VAL J  1 81  ? -16.721 -3.545  83.874  1.00 44.90  ? 81  VAL S CA  1 
ATOM   10581 C  C   . VAL J  1 81  ? -18.117 -3.041  83.476  1.00 44.07  ? 81  VAL S C   1 
ATOM   10582 O  O   . VAL J  1 81  ? -18.441 -1.874  83.705  1.00 43.73  ? 81  VAL S O   1 
ATOM   10583 C  CB  . VAL J  1 81  ? -15.718 -3.339  82.703  1.00 44.64  ? 81  VAL S CB  1 
ATOM   10584 C  CG1 . VAL J  1 81  ? -15.840 -1.933  82.104  1.00 43.77  ? 81  VAL S CG1 1 
ATOM   10585 C  CG2 . VAL J  1 81  ? -14.291 -3.568  83.177  1.00 45.76  ? 81  VAL S CG2 1 
ATOM   10586 N  N   . GLY J  1 82  ? -18.949 -3.922  82.924  1.00 44.12  ? 82  GLY S N   1 
ATOM   10587 C  CA  . GLY J  1 82  ? -20.304 -3.550  82.530  1.00 43.75  ? 82  GLY S CA  1 
ATOM   10588 C  C   . GLY J  1 82  ? -21.336 -3.303  83.629  1.00 44.27  ? 82  GLY S C   1 
ATOM   10589 O  O   . GLY J  1 82  ? -22.472 -2.925  83.323  1.00 44.21  ? 82  GLY S O   1 
ATOM   10590 N  N   . ASP J  1 83  ? -20.961 -3.508  84.892  1.00 45.01  ? 83  ASP S N   1 
ATOM   10591 C  CA  . ASP J  1 83  ? -21.900 -3.401  86.019  1.00 45.94  ? 83  ASP S CA  1 
ATOM   10592 C  C   . ASP J  1 83  ? -22.135 -1.959  86.477  1.00 45.79  ? 83  ASP S C   1 
ATOM   10593 O  O   . ASP J  1 83  ? -21.399 -1.440  87.329  1.00 46.10  ? 83  ASP S O   1 
ATOM   10594 C  CB  . ASP J  1 83  ? -21.396 -4.248  87.186  1.00 47.13  ? 83  ASP S CB  1 
ATOM   10595 C  CG  . ASP J  1 83  ? -21.383 -5.727  86.871  1.00 47.90  ? 83  ASP S CG  1 
ATOM   10596 O  OD1 . ASP J  1 83  ? -22.051 -6.161  85.903  1.00 47.69  ? 83  ASP S OD1 1 
ATOM   10597 O  OD2 . ASP J  1 83  ? -20.697 -6.472  87.598  1.00 48.94  ? 83  ASP S OD2 1 
ATOM   10598 N  N   . LEU J  1 84  ? -23.167 -1.323  85.912  0.75 45.64  ? 84  LEU S N   1 
ATOM   10599 C  CA  . LEU J  1 84  ? -23.566 0.044   86.289  0.75 45.92  ? 84  LEU S CA  1 
ATOM   10600 C  C   . LEU J  1 84  ? -24.744 0.098   87.275  0.75 47.41  ? 84  LEU S C   1 
ATOM   10601 O  O   . LEU J  1 84  ? -25.300 1.174   87.512  0.75 47.99  ? 84  LEU S O   1 
ATOM   10602 C  CB  . LEU J  1 84  ? -23.857 0.879   85.030  0.75 45.15  ? 84  LEU S CB  1 
ATOM   10603 C  CG  . LEU J  1 84  ? -22.658 1.089   84.090  0.75 44.06  ? 84  LEU S CG  1 
ATOM   10604 C  CD1 . LEU J  1 84  ? -23.066 1.859   82.840  0.75 43.62  ? 84  LEU S CD1 1 
ATOM   10605 C  CD2 . LEU J  1 84  ? -21.521 1.807   84.807  0.75 44.23  ? 84  LEU S CD2 1 
ATOM   10606 N  N   . GLY J  1 85  ? -25.113 -1.053  87.849  1.00 48.38  ? 85  GLY S N   1 
ATOM   10607 C  CA  . GLY J  1 85  ? -26.006 -1.105  89.000  1.00 50.15  ? 85  GLY S CA  1 
ATOM   10608 C  C   . GLY J  1 85  ? -27.488 -1.117  88.669  1.00 51.19  ? 85  GLY S C   1 
ATOM   10609 O  O   . GLY J  1 85  ? -27.980 -2.067  88.056  1.00 51.45  ? 85  GLY S O   1 
ATOM   10610 N  N   . ASN J  1 86  ? -28.196 -0.070  89.097  1.00 52.17  ? 86  ASN S N   1 
ATOM   10611 C  CA  . ASN J  1 86  ? -29.644 0.043   88.926  1.00 53.65  ? 86  ASN S CA  1 
ATOM   10612 C  C   . ASN J  1 86  ? -30.033 1.454   88.480  1.00 53.71  ? 86  ASN S C   1 
ATOM   10613 O  O   . ASN J  1 86  ? -29.416 2.438   88.900  1.00 53.56  ? 86  ASN S O   1 
ATOM   10614 C  CB  . ASN J  1 86  ? -30.357 -0.284  90.249  1.00 55.98  ? 86  ASN S CB  1 
ATOM   10615 C  CG  . ASN J  1 86  ? -30.435 -1.779  90.525  1.00 56.73  ? 86  ASN S CG  1 
ATOM   10616 O  OD1 . ASN J  1 86  ? -30.953 -2.548  89.707  1.00 56.86  ? 86  ASN S OD1 1 
ATOM   10617 N  ND2 . ASN J  1 86  ? -29.932 -2.198  91.685  1.00 57.51  ? 86  ASN S ND2 1 
ATOM   10618 N  N   . VAL J  1 87  ? -31.047 1.542   87.618  1.00 54.26  ? 87  VAL S N   1 
ATOM   10619 C  CA  . VAL J  1 87  ? -31.753 2.807   87.371  1.00 55.25  ? 87  VAL S CA  1 
ATOM   10620 C  C   . VAL J  1 87  ? -33.124 2.686   88.041  1.00 57.92  ? 87  VAL S C   1 
ATOM   10621 O  O   . VAL J  1 87  ? -33.706 1.594   88.083  1.00 58.75  ? 87  VAL S O   1 
ATOM   10622 C  CB  . VAL J  1 87  ? -31.853 3.190   85.866  1.00 54.29  ? 87  VAL S CB  1 
ATOM   10623 C  CG1 . VAL J  1 87  ? -30.459 3.382   85.267  1.00 52.00  ? 87  VAL S CG1 1 
ATOM   10624 C  CG2 . VAL J  1 87  ? -32.651 2.177   85.047  1.00 54.68  ? 87  VAL S CG2 1 
ATOM   10625 N  N   . THR J  1 88  ? -33.612 3.796   88.595  1.00 59.56  ? 88  THR S N   1 
ATOM   10626 C  CA  . THR J  1 88  ? -34.891 3.827   89.317  1.00 62.53  ? 88  THR S CA  1 
ATOM   10627 C  C   . THR J  1 88  ? -35.975 4.453   88.443  1.00 63.92  ? 88  THR S C   1 
ATOM   10628 O  O   . THR J  1 88  ? -35.885 5.631   88.096  1.00 63.99  ? 88  THR S O   1 
ATOM   10629 C  CB  . THR J  1 88  ? -34.780 4.641   90.627  1.00 64.11  ? 88  THR S CB  1 
ATOM   10630 O  OG1 . THR J  1 88  ? -33.596 4.262   91.334  1.00 62.67  ? 88  THR S OG1 1 
ATOM   10631 C  CG2 . THR J  1 88  ? -36.003 4.415   91.521  1.00 67.40  ? 88  THR S CG2 1 
ATOM   10632 N  N   . ALA J  1 89  ? -36.989 3.664   88.088  1.00 65.32  ? 89  ALA S N   1 
ATOM   10633 C  CA  . ALA J  1 89  ? -38.181 4.180   87.403  1.00 67.44  ? 89  ALA S CA  1 
ATOM   10634 C  C   . ALA J  1 89  ? -39.168 4.745   88.430  1.00 70.93  ? 89  ALA S C   1 
ATOM   10635 O  O   . ALA J  1 89  ? -39.456 4.091   89.435  1.00 72.38  ? 89  ALA S O   1 
ATOM   10636 C  CB  . ALA J  1 89  ? -38.844 3.083   86.583  1.00 67.86  ? 89  ALA S CB  1 
ATOM   10637 N  N   . ASP J  1 90  ? -39.684 5.947   88.165  1.00 72.55  ? 90  ASP S N   1 
ATOM   10638 C  CA  . ASP J  1 90  ? -40.696 6.589   89.028  1.00 76.37  ? 90  ASP S CA  1 
ATOM   10639 C  C   . ASP J  1 90  ? -42.098 5.964   88.839  1.00 79.43  ? 90  ASP S C   1 
ATOM   10640 O  O   . ASP J  1 90  ? -42.233 4.945   88.150  1.00 78.54  ? 90  ASP S O   1 
ATOM   10641 C  CB  . ASP J  1 90  ? -40.697 8.125   88.815  1.00 77.37  ? 90  ASP S CB  1 
ATOM   10642 C  CG  . ASP J  1 90  ? -41.181 8.558   87.420  1.00 77.58  ? 90  ASP S CG  1 
ATOM   10643 O  OD1 . ASP J  1 90  ? -41.587 7.709   86.597  1.00 77.11  ? 90  ASP S OD1 1 
ATOM   10644 O  OD2 . ASP J  1 90  ? -41.147 9.776   87.146  1.00 78.47  ? 90  ASP S OD2 1 
ATOM   10645 N  N   . LYS J  1 91  ? -43.125 6.560   89.452  1.00 83.32  ? 91  LYS S N   1 
ATOM   10646 C  CA  . LYS J  1 91  ? -44.525 6.119   89.281  1.00 86.92  ? 91  LYS S CA  1 
ATOM   10647 C  C   . LYS J  1 91  ? -45.007 6.169   87.825  1.00 86.89  ? 91  LYS S C   1 
ATOM   10648 O  O   . LYS J  1 91  ? -45.735 5.277   87.375  1.00 88.21  ? 91  LYS S O   1 
ATOM   10649 C  CB  . LYS J  1 91  ? -45.467 6.955   90.155  1.00 91.33  ? 91  LYS S CB  1 
ATOM   10650 N  N   . ASP J  1 92  ? -44.580 7.199   87.093  1.00 85.62  ? 92  ASP S N   1 
ATOM   10651 C  CA  . ASP J  1 92  ? -44.897 7.344   85.662  1.00 85.43  ? 92  ASP S CA  1 
ATOM   10652 C  C   . ASP J  1 92  ? -44.056 6.436   84.735  1.00 81.56  ? 92  ASP S C   1 
ATOM   10653 O  O   . ASP J  1 92  ? -44.205 6.504   83.512  1.00 81.18  ? 92  ASP S O   1 
ATOM   10654 C  CB  . ASP J  1 92  ? -44.725 8.808   85.219  1.00 85.83  ? 92  ASP S CB  1 
ATOM   10655 C  CG  . ASP J  1 92  ? -45.562 9.786   86.039  1.00 90.04  ? 92  ASP S CG  1 
ATOM   10656 O  OD1 . ASP J  1 92  ? -46.433 9.353   86.832  1.00 93.06  ? 92  ASP S OD1 1 
ATOM   10657 O  OD2 . ASP J  1 92  ? -45.339 11.006  85.881  1.00 90.65  ? 92  ASP S OD2 1 
ATOM   10658 N  N   . GLY J  1 93  ? -43.178 5.605   85.305  1.00 78.96  ? 93  GLY S N   1 
ATOM   10659 C  CA  . GLY J  1 93  ? -42.381 4.643   84.542  1.00 75.74  ? 93  GLY S CA  1 
ATOM   10660 C  C   . GLY J  1 93  ? -41.124 5.212   83.902  1.00 72.23  ? 93  GLY S C   1 
ATOM   10661 O  O   . GLY J  1 93  ? -40.499 4.544   83.075  1.00 69.83  ? 93  GLY S O   1 
ATOM   10662 N  N   . VAL J  1 94  ? -40.751 6.431   84.299  1.00 72.26  ? 94  VAL S N   1 
ATOM   10663 C  CA  . VAL J  1 94  ? -39.618 7.155   83.730  1.00 69.64  ? 94  VAL S CA  1 
ATOM   10664 C  C   . VAL J  1 94  ? -38.436 7.088   84.702  1.00 67.56  ? 94  VAL S C   1 
ATOM   10665 O  O   . VAL J  1 94  ? -38.557 7.521   85.855  1.00 69.03  ? 94  VAL S O   1 
ATOM   10666 C  CB  . VAL J  1 94  ? -39.980 8.635   83.452  1.00 71.57  ? 94  VAL S CB  1 
ATOM   10667 C  CG1 . VAL J  1 94  ? -38.799 9.380   82.832  1.00 69.17  ? 94  VAL S CG1 1 
ATOM   10668 C  CG2 . VAL J  1 94  ? -41.209 8.723   82.549  1.00 74.14  ? 94  VAL S CG2 1 
ATOM   10669 N  N   . ALA J  1 95  ? -37.315 6.530   84.233  1.00 64.42  ? 95  ALA S N   1 
ATOM   10670 C  CA  . ALA J  1 95  ? -36.068 6.469   84.999  1.00 62.41  ? 95  ALA S CA  1 
ATOM   10671 C  C   . ALA J  1 95  ? -35.090 7.528   84.500  1.00 61.05  ? 95  ALA S C   1 
ATOM   10672 O  O   . ALA J  1 95  ? -34.472 7.358   83.442  1.00 59.16  ? 95  ALA S O   1 
ATOM   10673 C  CB  . ALA J  1 95  ? -35.444 5.079   84.905  1.00 60.31  ? 95  ALA S CB  1 
ATOM   10674 N  N   . ASP J  1 96  ? -34.965 8.623   85.253  1.00 62.37  ? 96  ASP S N   1 
ATOM   10675 C  CA  . ASP J  1 96  ? -33.987 9.676   84.953  1.00 61.56  ? 96  ASP S CA  1 
ATOM   10676 C  C   . ASP J  1 96  ? -32.617 9.241   85.475  1.00 59.31  ? 96  ASP S C   1 
ATOM   10677 O  O   . ASP J  1 96  ? -32.383 9.226   86.687  1.00 59.95  ? 96  ASP S O   1 
ATOM   10678 C  CB  . ASP J  1 96  ? -34.412 11.016  85.569  1.00 64.34  ? 96  ASP S CB  1 
ATOM   10679 C  CG  . ASP J  1 96  ? -35.720 11.545  84.983  1.00 66.96  ? 96  ASP S CG  1 
ATOM   10680 O  OD1 . ASP J  1 96  ? -35.911 11.479  83.748  1.00 66.38  ? 96  ASP S OD1 1 
ATOM   10681 O  OD2 . ASP J  1 96  ? -36.564 12.036  85.758  1.00 69.88  ? 96  ASP S OD2 1 
ATOM   10682 N  N   . VAL J  1 97  ? -31.727 8.878   84.550  1.00 56.96  ? 97  VAL S N   1 
ATOM   10683 C  CA  . VAL J  1 97  ? -30.425 8.292   84.880  1.00 54.90  ? 97  VAL S CA  1 
ATOM   10684 C  C   . VAL J  1 97  ? -29.374 9.390   85.078  1.00 54.89  ? 97  VAL S C   1 
ATOM   10685 O  O   . VAL J  1 97  ? -29.339 10.377  84.339  1.00 55.44  ? 97  VAL S O   1 
ATOM   10686 C  CB  . VAL J  1 97  ? -29.959 7.294   83.786  1.00 52.75  ? 97  VAL S CB  1 
ATOM   10687 C  CG1 . VAL J  1 97  ? -28.651 6.618   84.183  1.00 51.02  ? 97  VAL S CG1 1 
ATOM   10688 C  CG2 . VAL J  1 97  ? -31.040 6.249   83.519  1.00 53.19  ? 97  VAL S CG2 1 
ATOM   10689 N  N   . SER J  1 98  ? -28.532 9.206   86.091  1.00 54.55  ? 98  SER S N   1 
ATOM   10690 C  CA  . SER J  1 98  ? -27.418 10.111  86.374  1.00 54.76  ? 98  SER S CA  1 
ATOM   10691 C  C   . SER J  1 98  ? -26.366 9.375   87.219  1.00 53.77  ? 98  SER S C   1 
ATOM   10692 O  O   . SER J  1 98  ? -26.405 9.397   88.451  1.00 54.99  ? 98  SER S O   1 
ATOM   10693 C  CB  . SER J  1 98  ? -27.912 11.396  87.055  1.00 57.42  ? 98  SER S CB  1 
ATOM   10694 O  OG  . SER J  1 98  ? -28.897 11.121  88.035  1.00 58.96  ? 98  SER S OG  1 
ATOM   10695 N  N   . ILE J  1 99  ? -25.450 8.706   86.526  1.00 51.85  ? 99  ILE S N   1 
ATOM   10696 C  CA  . ILE J  1 99  ? -24.416 7.854   87.132  1.00 50.94  ? 99  ILE S CA  1 
ATOM   10697 C  C   . ILE J  1 99  ? -23.041 8.484   86.870  1.00 50.67  ? 99  ILE S C   1 
ATOM   10698 O  O   . ILE J  1 99  ? -22.841 9.156   85.848  1.00 50.44  ? 99  ILE S O   1 
ATOM   10699 C  CB  . ILE J  1 99  ? -24.496 6.403   86.551  1.00 49.35  ? 99  ILE S CB  1 
ATOM   10700 C  CG1 . ILE J  1 99  ? -25.749 5.688   87.071  1.00 50.13  ? 99  ILE S CG1 1 
ATOM   10701 C  CG2 . ILE J  1 99  ? -23.254 5.560   86.872  1.00 48.43  ? 99  ILE S CG2 1 
ATOM   10702 C  CD1 . ILE J  1 99  ? -26.193 4.519   86.213  1.00 49.12  ? 99  ILE S CD1 1 
ATOM   10703 N  N   . GLU J  1 100 ? -22.115 8.288   87.811  1.00 50.96  ? 100 GLU S N   1 
ATOM   10704 C  CA  . GLU J  1 100 ? -20.687 8.514   87.575  1.00 50.68  ? 100 GLU S CA  1 
ATOM   10705 C  C   . GLU J  1 100 ? -19.939 7.221   87.890  1.00 49.68  ? 100 GLU S C   1 
ATOM   10706 O  O   . GLU J  1 100 ? -20.138 6.625   88.950  1.00 50.17  ? 100 GLU S O   1 
ATOM   10707 C  CB  . GLU J  1 100 ? -20.153 9.669   88.421  1.00 52.72  ? 100 GLU S CB  1 
ATOM   10708 C  CG  . GLU J  1 100 ? -18.741 10.098  88.032  1.00 52.97  ? 100 GLU S CG  1 
ATOM   10709 C  CD  . GLU J  1 100 ? -18.244 11.313  88.798  1.00 55.41  ? 100 GLU S CD  1 
ATOM   10710 O  OE1 . GLU J  1 100 ? -18.996 12.306  88.930  1.00 56.86  ? 100 GLU S OE1 1 
ATOM   10711 O  OE2 . GLU J  1 100 ? -17.083 11.277  89.260  1.00 56.19  ? 100 GLU S OE2 1 
ATOM   10712 N  N   . ASP J  1 101 ? -19.082 6.797   86.960  1.00 48.54  ? 101 ASP S N   1 
ATOM   10713 C  CA  . ASP J  1 101 ? -18.378 5.514   87.053  1.00 47.75  ? 101 ASP S CA  1 
ATOM   10714 C  C   . ASP J  1 101 ? -16.931 5.629   86.554  1.00 47.74  ? 101 ASP S C   1 
ATOM   10715 O  O   . ASP J  1 101 ? -16.681 6.132   85.449  1.00 47.40  ? 101 ASP S O   1 
ATOM   10716 C  CB  . ASP J  1 101 ? -19.126 4.455   86.237  1.00 46.43  ? 101 ASP S CB  1 
ATOM   10717 C  CG  . ASP J  1 101 ? -18.710 3.038   86.592  1.00 46.16  ? 101 ASP S CG  1 
ATOM   10718 O  OD1 . ASP J  1 101 ? -19.287 2.478   87.547  1.00 46.77  ? 101 ASP S OD1 1 
ATOM   10719 O  OD2 . ASP J  1 101 ? -17.813 2.484   85.920  1.00 45.63  ? 101 ASP S OD2 1 
ATOM   10720 N  N   . SER J  1 102 ? -15.999 5.130   87.371  1.00 48.39  ? 102 SER S N   1 
ATOM   10721 C  CA  . SER J  1 102 ? -14.555 5.186   87.103  1.00 48.92  ? 102 SER S CA  1 
ATOM   10722 C  C   . SER J  1 102 ? -13.950 3.854   86.626  1.00 48.14  ? 102 SER S C   1 
ATOM   10723 O  O   . SER J  1 102 ? -12.722 3.721   86.585  1.00 48.95  ? 102 SER S O   1 
ATOM   10724 C  CB  . SER J  1 102 ? -13.821 5.639   88.369  1.00 50.81  ? 102 SER S CB  1 
ATOM   10725 O  OG  . SER J  1 102 ? -14.326 6.878   88.820  1.00 51.87  ? 102 SER S OG  1 
ATOM   10726 N  N   . VAL J  1 103 ? -14.798 2.880   86.272  1.00 46.84  ? 103 VAL S N   1 
ATOM   10727 C  CA  . VAL J  1 103 ? -14.344 1.575   85.765  1.00 46.38  ? 103 VAL S CA  1 
ATOM   10728 C  C   . VAL J  1 103 ? -14.548 1.494   84.243  1.00 45.25  ? 103 VAL S C   1 
ATOM   10729 O  O   . VAL J  1 103 ? -13.625 1.126   83.513  1.00 45.36  ? 103 VAL S O   1 
ATOM   10730 C  CB  . VAL J  1 103 ? -15.060 0.413   86.482  1.00 46.32  ? 103 VAL S CB  1 
ATOM   10731 C  CG1 . VAL J  1 103 ? -14.541 -0.932  85.984  1.00 46.35  ? 103 VAL S CG1 1 
ATOM   10732 C  CG2 . VAL J  1 103 ? -14.879 0.549   87.992  1.00 47.63  ? 103 VAL S CG2 1 
ATOM   10733 N  N   . ILE J  1 104 ? -15.756 1.827   83.776  1.00 44.37  ? 104 ILE S N   1 
ATOM   10734 C  CA  . ILE J  1 104 ? -15.998 2.010   82.334  1.00 43.59  ? 104 ILE S CA  1 
ATOM   10735 C  C   . ILE J  1 104 ? -15.194 3.203   81.805  1.00 44.12  ? 104 ILE S C   1 
ATOM   10736 O  O   . ILE J  1 104 ? -14.899 4.156   82.546  1.00 44.97  ? 104 ILE S O   1 
ATOM   10737 C  CB  . ILE J  1 104 ? -17.498 2.211   81.964  1.00 42.89  ? 104 ILE S CB  1 
ATOM   10738 C  CG1 . ILE J  1 104 ? -18.095 3.478   82.618  1.00 43.39  ? 104 ILE S CG1 1 
ATOM   10739 C  CG2 . ILE J  1 104 ? -18.311 0.961   82.315  1.00 42.67  ? 104 ILE S CG2 1 
ATOM   10740 C  CD1 . ILE J  1 104 ? -19.223 4.108   81.824  1.00 43.14  ? 104 ILE S CD1 1 
ATOM   10741 N  N   . SER J  1 105 ? -14.835 3.127   80.527  1.00 43.91  ? 105 SER S N   1 
ATOM   10742 C  CA  . SER J  1 105 ? -14.124 4.200   79.835  1.00 44.65  ? 105 SER S CA  1 
ATOM   10743 C  C   . SER J  1 105 ? -14.690 4.349   78.429  1.00 44.15  ? 105 SER S C   1 
ATOM   10744 O  O   . SER J  1 105 ? -15.343 3.443   77.912  1.00 43.28  ? 105 SER S O   1 
ATOM   10745 C  CB  . SER J  1 105 ? -12.629 3.883   79.773  1.00 45.66  ? 105 SER S CB  1 
ATOM   10746 O  OG  . SER J  1 105 ? -11.884 4.988   79.294  1.00 46.77  ? 105 SER S OG  1 
ATOM   10747 N  N   . LEU J  1 106 ? -14.440 5.507   77.828  1.00 44.97  ? 106 LEU S N   1 
ATOM   10748 C  CA  . LEU J  1 106 ? -14.755 5.742   76.424  1.00 44.97  ? 106 LEU S CA  1 
ATOM   10749 C  C   . LEU J  1 106 ? -13.499 5.663   75.540  1.00 46.03  ? 106 LEU S C   1 
ATOM   10750 O  O   . LEU J  1 106 ? -13.532 6.071   74.372  1.00 46.44  ? 106 LEU S O   1 
ATOM   10751 C  CB  . LEU J  1 106 ? -15.480 7.086   76.263  1.00 45.48  ? 106 LEU S CB  1 
ATOM   10752 C  CG  . LEU J  1 106 ? -16.766 7.255   77.090  1.00 44.95  ? 106 LEU S CG  1 
ATOM   10753 C  CD1 . LEU J  1 106 ? -17.459 8.574   76.750  1.00 45.87  ? 106 LEU S CD1 1 
ATOM   10754 C  CD2 . LEU J  1 106 ? -17.717 6.074   76.909  1.00 43.72  ? 106 LEU S CD2 1 
ATOM   10755 N  N   . SER J  1 107 ? -12.407 5.131   76.098  1.00 46.73  ? 107 SER S N   1 
ATOM   10756 C  CA  . SER J  1 107 ? -11.214 4.765   75.325  1.00 47.95  ? 107 SER S CA  1 
ATOM   10757 C  C   . SER J  1 107 ? -10.444 3.645   76.036  1.00 48.27  ? 107 SER S C   1 
ATOM   10758 O  O   . SER J  1 107 ? -10.723 3.338   77.199  1.00 47.73  ? 107 SER S O   1 
ATOM   10759 C  CB  . SER J  1 107 ? -10.317 5.989   75.113  1.00 49.78  ? 107 SER S CB  1 
ATOM   10760 O  OG  . SER J  1 107 ? -9.955  6.582   76.353  1.00 50.57  ? 107 SER S OG  1 
ATOM   10761 N  N   . GLY J  1 108 ? -9.505  3.024   75.319  1.00 49.40  ? 108 GLY S N   1 
ATOM   10762 C  CA  . GLY J  1 108 ? -8.649  1.954   75.863  1.00 50.31  ? 108 GLY S CA  1 
ATOM   10763 C  C   . GLY J  1 108 ? -9.312  0.593   76.039  1.00 49.41  ? 108 GLY S C   1 
ATOM   10764 O  O   . GLY J  1 108 ? -10.339 0.315   75.420  1.00 48.23  ? 108 GLY S O   1 
ATOM   10765 N  N   . ASP J  1 109 ? -8.708  -0.245  76.894  1.00 50.34  ? 109 ASP S N   1 
ATOM   10766 C  CA  . ASP J  1 109 ? -9.158  -1.637  77.167  1.00 50.11  ? 109 ASP S CA  1 
ATOM   10767 C  C   . ASP J  1 109 ? -10.562 -1.738  77.788  1.00 48.52  ? 109 ASP S C   1 
ATOM   10768 O  O   . ASP J  1 109 ? -11.292 -2.694  77.518  1.00 48.15  ? 109 ASP S O   1 
ATOM   10769 C  CB  . ASP J  1 109 ? -8.190  -2.356  78.128  1.00 51.68  ? 109 ASP S CB  1 
ATOM   10770 C  CG  . ASP J  1 109 ? -6.781  -2.512  77.568  1.00 53.88  ? 109 ASP S CG  1 
ATOM   10771 O  OD1 . ASP J  1 109 ? -6.603  -2.555  76.326  1.00 54.35  ? 109 ASP S OD1 1 
ATOM   10772 O  OD2 . ASP J  1 109 ? -5.842  -2.608  78.390  1.00 55.46  ? 109 ASP S OD2 1 
ATOM   10773 N  N   . HIS J  1 110 ? -10.920 -0.764  78.631  1.00 48.00  ? 110 HIS S N   1 
ATOM   10774 C  CA  . HIS J  1 110 ? -12.261 -0.691  79.242  1.00 46.77  ? 110 HIS S CA  1 
ATOM   10775 C  C   . HIS J  1 110 ? -13.258 0.151   78.422  1.00 45.73  ? 110 HIS S C   1 
ATOM   10776 O  O   . HIS J  1 110 ? -14.280 0.625   78.958  1.00 45.02  ? 110 HIS S O   1 
ATOM   10777 C  CB  . HIS J  1 110 ? -12.158 -0.166  80.687  1.00 47.14  ? 110 HIS S CB  1 
ATOM   10778 C  CG  . HIS J  1 110 ? -11.578 -1.158  81.648  1.00 48.14  ? 110 HIS S CG  1 
ATOM   10779 N  ND1 . HIS J  1 110 ? -11.780 -1.079  83.010  1.00 48.47  ? 110 HIS S ND1 1 
ATOM   10780 C  CD2 . HIS J  1 110 ? -10.830 -2.269  81.441  1.00 49.14  ? 110 HIS S CD2 1 
ATOM   10781 C  CE1 . HIS J  1 110 ? -11.163 -2.088  83.601  1.00 49.60  ? 110 HIS S CE1 1 
ATOM   10782 N  NE2 . HIS J  1 110 ? -10.580 -2.825  82.671  1.00 50.05  ? 110 HIS S NE2 1 
ATOM   10783 N  N   . CYS J  1 111 ? -12.985 0.310   77.123  1.00 45.86  ? 111 CYS S N   1 
ATOM   10784 C  CA  . CYS J  1 111 ? -13.862 1.087   76.263  1.00 45.20  ? 111 CYS S CA  1 
ATOM   10785 C  C   . CYS J  1 111 ? -15.176 0.331   76.034  1.00 44.24  ? 111 CYS S C   1 
ATOM   10786 O  O   . CYS J  1 111 ? -15.182 -0.891  75.785  1.00 44.36  ? 111 CYS S O   1 
ATOM   10787 C  CB  . CYS J  1 111 ? -13.191 1.450   74.940  1.00 46.00  ? 111 CYS S CB  1 
ATOM   10788 S  SG  . CYS J  1 111 ? -14.132 2.647   73.964  1.00 45.82  ? 111 CYS S SG  1 
ATOM   10789 N  N   . ILE J  1 112 ? -16.274 1.079   76.141  1.00 43.53  ? 112 ILE S N   1 
ATOM   10790 C  CA  . ILE J  1 112 ? -17.638 0.550   75.943  1.00 42.96  ? 112 ILE S CA  1 
ATOM   10791 C  C   . ILE J  1 112 ? -18.295 1.005   74.630  1.00 42.88  ? 112 ILE S C   1 
ATOM   10792 O  O   . ILE J  1 112 ? -19.410 0.571   74.323  1.00 42.77  ? 112 ILE S O   1 
ATOM   10793 C  CB  . ILE J  1 112 ? -18.558 0.870   77.149  1.00 42.67  ? 112 ILE S CB  1 
ATOM   10794 C  CG1 . ILE J  1 112 ? -18.694 2.385   77.386  1.00 42.79  ? 112 ILE S CG1 1 
ATOM   10795 C  CG2 . ILE J  1 112 ? -18.024 0.171   78.393  1.00 42.87  ? 112 ILE S CG2 1 
ATOM   10796 C  CD1 . ILE J  1 112 ? -19.765 2.747   78.395  1.00 42.87  ? 112 ILE S CD1 1 
ATOM   10797 N  N   . ILE J  1 113 ? -17.608 1.866   73.869  1.00 43.16  ? 113 ILE S N   1 
ATOM   10798 C  CA  . ILE J  1 113 ? -18.043 2.248   72.527  1.00 43.42  ? 113 ILE S CA  1 
ATOM   10799 C  C   . ILE J  1 113 ? -17.988 1.003   71.646  1.00 43.60  ? 113 ILE S C   1 
ATOM   10800 O  O   . ILE J  1 113 ? -17.042 0.222   71.718  1.00 43.84  ? 113 ILE S O   1 
ATOM   10801 C  CB  . ILE J  1 113 ? -17.171 3.388   71.936  1.00 44.18  ? 113 ILE S CB  1 
ATOM   10802 C  CG1 . ILE J  1 113 ? -17.388 4.689   72.727  1.00 44.34  ? 113 ILE S CG1 1 
ATOM   10803 C  CG2 . ILE J  1 113 ? -17.492 3.629   70.460  1.00 44.81  ? 113 ILE S CG2 1 
ATOM   10804 C  CD1 . ILE J  1 113 ? -16.297 5.730   72.541  1.00 45.43  ? 113 ILE S CD1 1 
ATOM   10805 N  N   . GLY J  1 114 ? -19.029 0.813   70.841  1.00 43.75  ? 114 GLY S N   1 
ATOM   10806 C  CA  . GLY J  1 114 ? -19.182 -0.394  70.034  1.00 44.28  ? 114 GLY S CA  1 
ATOM   10807 C  C   . GLY J  1 114 ? -19.656 -1.620  70.790  1.00 44.11  ? 114 GLY S C   1 
ATOM   10808 O  O   . GLY J  1 114 ? -19.605 -2.730  70.253  1.00 44.84  ? 114 GLY S O   1 
ATOM   10809 N  N   . ARG J  1 115 ? -20.121 -1.419  72.027  1.00 43.48  ? 115 ARG S N   1 
ATOM   10810 C  CA  . ARG J  1 115 ? -20.735 -2.464  72.845  1.00 43.60  ? 115 ARG S CA  1 
ATOM   10811 C  C   . ARG J  1 115 ? -22.189 -2.039  73.123  1.00 43.66  ? 115 ARG S C   1 
ATOM   10812 O  O   . ARG J  1 115 ? -22.624 -0.979  72.653  1.00 43.52  ? 115 ARG S O   1 
ATOM   10813 C  CB  . ARG J  1 115 ? -19.935 -2.668  74.140  1.00 43.21  ? 115 ARG S CB  1 
ATOM   10814 C  CG  . ARG J  1 115 ? -18.425 -2.690  73.937  1.00 43.39  ? 115 ARG S CG  1 
ATOM   10815 C  CD  . ARG J  1 115 ? -17.671 -3.315  75.110  1.00 43.59  ? 115 ARG S CD  1 
ATOM   10816 N  NE  . ARG J  1 115 ? -16.249 -3.513  74.797  1.00 44.24  ? 115 ARG S NE  1 
ATOM   10817 C  CZ  . ARG J  1 115 ? -15.691 -4.623  74.288  1.00 45.31  ? 115 ARG S CZ  1 
ATOM   10818 N  NH1 . ARG J  1 115 ? -16.399 -5.725  74.012  1.00 45.88  ? 115 ARG S NH1 1 
ATOM   10819 N  NH2 . ARG J  1 115 ? -14.376 -4.633  74.055  1.00 46.16  ? 115 ARG S NH2 1 
ATOM   10820 N  N   . THR J  1 116 ? -22.935 -2.855  73.873  1.00 44.12  ? 116 THR S N   1 
ATOM   10821 C  CA  . THR J  1 116 ? -24.381 -2.635  74.062  1.00 44.67  ? 116 THR S CA  1 
ATOM   10822 C  C   . THR J  1 116 ? -24.788 -2.329  75.497  1.00 44.46  ? 116 THR S C   1 
ATOM   10823 O  O   . THR J  1 116 ? -24.473 -3.092  76.411  1.00 44.57  ? 116 THR S O   1 
ATOM   10824 C  CB  . THR J  1 116 ? -25.223 -3.857  73.628  1.00 46.06  ? 116 THR S CB  1 
ATOM   10825 O  OG1 . THR J  1 116 ? -24.639 -5.055  74.147  1.00 46.49  ? 116 THR S OG1 1 
ATOM   10826 C  CG2 . THR J  1 116 ? -25.293 -3.943  72.145  1.00 46.70  ? 116 THR S CG2 1 
ATOM   10827 N  N   . LEU J  1 117 ? -25.517 -1.225  75.663  1.00 44.44  ? 117 LEU S N   1 
ATOM   10828 C  CA  . LEU J  1 117 ? -26.201 -0.900  76.910  1.00 44.73  ? 117 LEU S CA  1 
ATOM   10829 C  C   . LEU J  1 117 ? -27.504 -1.702  76.950  1.00 46.01  ? 117 LEU S C   1 
ATOM   10830 O  O   . LEU J  1 117 ? -28.205 -1.791  75.940  1.00 46.70  ? 117 LEU S O   1 
ATOM   10831 C  CB  . LEU J  1 117 ? -26.503 0.604   76.966  1.00 44.73  ? 117 LEU S CB  1 
ATOM   10832 C  CG  . LEU J  1 117 ? -26.989 1.208   78.291  1.00 45.21  ? 117 LEU S CG  1 
ATOM   10833 C  CD1 . LEU J  1 117 ? -25.852 1.233   79.298  1.00 44.48  ? 117 LEU S CD1 1 
ATOM   10834 C  CD2 . LEU J  1 117 ? -27.555 2.612   78.102  1.00 45.85  ? 117 LEU S CD2 1 
ATOM   10835 N  N   . VAL J  1 118 ? -27.817 -2.282  78.106  1.00 46.58  ? 118 VAL S N   1 
ATOM   10836 C  CA  . VAL J  1 118 ? -29.059 -3.052  78.302  1.00 48.27  ? 118 VAL S CA  1 
ATOM   10837 C  C   . VAL J  1 118 ? -29.775 -2.595  79.589  1.00 49.09  ? 118 VAL S C   1 
ATOM   10838 O  O   . VAL J  1 118 ? -29.150 -2.465  80.649  1.00 48.55  ? 118 VAL S O   1 
ATOM   10839 C  CB  . VAL J  1 118 ? -28.778 -4.583  78.348  1.00 48.89  ? 118 VAL S CB  1 
ATOM   10840 C  CG1 . VAL J  1 118 ? -30.057 -5.378  78.626  1.00 51.04  ? 118 VAL S CG1 1 
ATOM   10841 C  CG2 . VAL J  1 118 ? -28.124 -5.054  77.048  1.00 48.47  ? 118 VAL S CG2 1 
ATOM   10842 N  N   . VAL J  1 119 ? -31.080 -2.336  79.478  1.00 50.64  ? 119 VAL S N   1 
ATOM   10843 C  CA  . VAL J  1 119 ? -31.945 -2.127  80.648  1.00 52.11  ? 119 VAL S CA  1 
ATOM   10844 C  C   . VAL J  1 119 ? -32.790 -3.394  80.829  1.00 54.13  ? 119 VAL S C   1 
ATOM   10845 O  O   . VAL J  1 119 ? -33.204 -4.021  79.839  1.00 54.87  ? 119 VAL S O   1 
ATOM   10846 C  CB  . VAL J  1 119 ? -32.788 -0.818  80.569  1.00 52.92  ? 119 VAL S CB  1 
ATOM   10847 C  CG1 . VAL J  1 119 ? -33.794 -0.828  79.422  1.00 54.23  ? 119 VAL S CG1 1 
ATOM   10848 C  CG2 . VAL J  1 119 ? -33.497 -0.555  81.894  1.00 54.50  ? 119 VAL S CG2 1 
ATOM   10849 N  N   . HIS J  1 120 ? -33.026 -3.759  82.092  1.00 55.25  ? 120 HIS S N   1 
ATOM   10850 C  CA  . HIS J  1 120 ? -33.538 -5.087  82.463  1.00 57.24  ? 120 HIS S CA  1 
ATOM   10851 C  C   . HIS J  1 120 ? -34.933 -5.089  83.098  1.00 60.03  ? 120 HIS S C   1 
ATOM   10852 O  O   . HIS J  1 120 ? -35.432 -4.059  83.563  1.00 60.45  ? 120 HIS S O   1 
ATOM   10853 C  CB  . HIS J  1 120 ? -32.549 -5.775  83.417  1.00 56.70  ? 120 HIS S CB  1 
ATOM   10854 C  CG  . HIS J  1 120 ? -31.423 -6.472  82.723  1.00 55.31  ? 120 HIS S CG  1 
ATOM   10855 N  ND1 . HIS J  1 120 ? -31.481 -7.800  82.359  1.00 56.62  ? 120 HIS S ND1 1 
ATOM   10856 C  CD2 . HIS J  1 120 ? -30.211 -6.025  82.324  1.00 53.10  ? 120 HIS S CD2 1 
ATOM   10857 C  CE1 . HIS J  1 120 ? -30.350 -8.142  81.768  1.00 55.24  ? 120 HIS S CE1 1 
ATOM   10858 N  NE2 . HIS J  1 120 ? -29.562 -7.082  81.733  1.00 53.09  ? 120 HIS S NE2 1 
ATOM   10859 N  N   . GLU J  1 121 ? -35.523 -6.288  83.111  1.00 62.22  ? 121 GLU S N   1 
ATOM   10860 C  CA  . GLU J  1 121 ? -36.858 -6.569  83.651  1.00 65.47  ? 121 GLU S CA  1 
ATOM   10861 C  C   . GLU J  1 121 ? -37.021 -6.120  85.098  1.00 66.30  ? 121 GLU S C   1 
ATOM   10862 O  O   . GLU J  1 121 ? -38.004 -5.459  85.435  1.00 68.08  ? 121 GLU S O   1 
ATOM   10863 C  CB  . GLU J  1 121 ? -37.130 -8.079  83.562  1.00 67.62  ? 121 GLU S CB  1 
ATOM   10864 C  CG  . GLU J  1 121 ? -38.532 -8.536  83.947  1.00 71.49  ? 121 GLU S CG  1 
ATOM   10865 C  CD  . GLU J  1 121 ? -38.611 -10.035 84.182  1.00 73.81  ? 121 GLU S CD  1 
ATOM   10866 O  OE1 . GLU J  1 121 ? -37.794 -10.785 83.609  1.00 72.71  ? 121 GLU S OE1 1 
ATOM   10867 O  OE2 . GLU J  1 121 ? -39.496 -10.467 84.951  1.00 77.04  ? 121 GLU S OE2 1 
ATOM   10868 N  N   . LYS J  1 122 ? -36.059 -6.493  85.941  1.00 65.30  ? 122 LYS S N   1 
ATOM   10869 C  CA  . LYS J  1 122 ? -36.172 -6.314  87.394  1.00 66.55  ? 122 LYS S CA  1 
ATOM   10870 C  C   . LYS J  1 122 ? -34.835 -5.908  88.020  1.00 64.12  ? 122 LYS S C   1 
ATOM   10871 O  O   . LYS J  1 122 ? -33.845 -5.714  87.302  1.00 61.53  ? 122 LYS S O   1 
ATOM   10872 C  CB  . LYS J  1 122 ? -36.742 -7.591  88.028  1.00 69.60  ? 122 LYS S CB  1 
ATOM   10873 C  CG  . LYS J  1 122 ? -36.000 -8.874  87.686  1.00 69.29  ? 122 LYS S CG  1 
ATOM   10874 C  CD  . LYS J  1 122 ? -36.680 -10.076 88.325  1.00 72.89  ? 122 LYS S CD  1 
ATOM   10875 C  CE  . LYS J  1 122 ? -36.191 -11.383 87.721  1.00 73.29  ? 122 LYS S CE  1 
ATOM   10876 N  NZ  . LYS J  1 122 ? -36.739 -12.553 88.460  1.00 77.02  ? 122 LYS S NZ  1 
ATOM   10877 N  N   . ALA J  1 123 ? -34.823 -5.750  89.346  1.00 65.23  ? 123 ALA S N   1 
ATOM   10878 C  CA  . ALA J  1 123 ? -33.661 -5.232  90.076  1.00 63.49  ? 123 ALA S CA  1 
ATOM   10879 C  C   . ALA J  1 123 ? -32.400 -6.099  89.945  1.00 61.99  ? 123 ALA S C   1 
ATOM   10880 O  O   . ALA J  1 123 ? -32.460 -7.321  90.068  1.00 63.37  ? 123 ALA S O   1 
ATOM   10881 C  CB  . ALA J  1 123 ? -34.011 -5.047  91.547  1.00 65.61  ? 123 ALA S CB  1 
ATOM   10882 N  N   . ASP J  1 124 ? -31.269 -5.448  89.678  1.00 59.48  ? 124 ASP S N   1 
ATOM   10883 C  CA  . ASP J  1 124 ? -29.953 -6.066  89.814  1.00 58.36  ? 124 ASP S CA  1 
ATOM   10884 C  C   . ASP J  1 124 ? -29.640 -6.166  91.315  1.00 59.71  ? 124 ASP S C   1 
ATOM   10885 O  O   . ASP J  1 124 ? -29.597 -5.141  92.003  1.00 59.63  ? 124 ASP S O   1 
ATOM   10886 C  CB  . ASP J  1 124 ? -28.899 -5.211  89.092  1.00 55.68  ? 124 ASP S CB  1 
ATOM   10887 C  CG  . ASP J  1 124 ? -27.501 -5.835  89.100  1.00 54.70  ? 124 ASP S CG  1 
ATOM   10888 O  OD1 . ASP J  1 124 ? -27.212 -6.713  89.950  1.00 56.01  ? 124 ASP S OD1 1 
ATOM   10889 O  OD2 . ASP J  1 124 ? -26.677 -5.425  88.254  1.00 52.82  ? 124 ASP S OD2 1 
ATOM   10890 N  N   . ASP J  1 125 ? -29.415 -7.390  91.807  1.00 61.18  ? 125 ASP S N   1 
ATOM   10891 C  CA  . ASP J  1 125 ? -29.105 -7.625  93.238  1.00 62.86  ? 125 ASP S CA  1 
ATOM   10892 C  C   . ASP J  1 125 ? -27.640 -7.361  93.651  1.00 61.54  ? 125 ASP S C   1 
ATOM   10893 O  O   . ASP J  1 125 ? -27.296 -7.518  94.826  1.00 62.98  ? 125 ASP S O   1 
ATOM   10894 C  CB  . ASP J  1 125 ? -29.566 -9.033  93.697  1.00 65.60  ? 125 ASP S CB  1 
ATOM   10895 C  CG  . ASP J  1 125 ? -28.735 -10.187 93.106  1.00 65.30  ? 125 ASP S CG  1 
ATOM   10896 O  OD1 . ASP J  1 125 ? -27.641 -9.971  92.545  1.00 63.07  ? 125 ASP S OD1 1 
ATOM   10897 O  OD2 . ASP J  1 125 ? -29.201 -11.341 93.216  1.00 67.64  ? 125 ASP S OD2 1 
ATOM   10898 N  N   . LEU J  1 126 ? -26.795 -6.982  92.686  1.00 59.19  ? 126 LEU S N   1 
ATOM   10899 C  CA  . LEU J  1 126 ? -25.419 -6.530  92.935  1.00 57.98  ? 126 LEU S CA  1 
ATOM   10900 C  C   . LEU J  1 126 ? -24.517 -7.657  93.479  1.00 59.15  ? 126 LEU S C   1 
ATOM   10901 O  O   . LEU J  1 126 ? -23.627 -7.409  94.297  1.00 59.51  ? 126 LEU S O   1 
ATOM   10902 C  CB  . LEU J  1 126 ? -25.405 -5.302  93.873  1.00 58.19  ? 126 LEU S CB  1 
ATOM   10903 C  CG  . LEU J  1 126 ? -26.442 -4.189  93.644  1.00 58.00  ? 126 LEU S CG  1 
ATOM   10904 C  CD1 . LEU J  1 126 ? -26.475 -3.236  94.832  1.00 59.18  ? 126 LEU S CD1 1 
ATOM   10905 C  CD2 . LEU J  1 126 ? -26.177 -3.435  92.349  1.00 55.70  ? 126 LEU S CD2 1 
ATOM   10906 N  N   . GLY J  1 127 ? -24.754 -8.888  93.021  1.00 60.10  ? 127 GLY S N   1 
ATOM   10907 C  CA  . GLY J  1 127 ? -23.973 -10.048 93.453  1.00 61.62  ? 127 GLY S CA  1 
ATOM   10908 C  C   . GLY J  1 127 ? -24.166 -10.422 94.912  1.00 64.22  ? 127 GLY S C   1 
ATOM   10909 O  O   . GLY J  1 127 ? -23.244 -10.941 95.547  1.00 65.32  ? 127 GLY S O   1 
ATOM   10910 N  N   . LYS J  1 128 ? -25.364 -10.155 95.438  1.00 65.49  ? 128 LYS S N   1 
ATOM   10911 C  CA  . LYS J  1 128 ? -25.710 -10.429 96.837  1.00 68.25  ? 128 LYS S CA  1 
ATOM   10912 C  C   . LYS J  1 128 ? -27.029 -11.217 96.920  1.00 70.70  ? 128 LYS S C   1 
ATOM   10913 O  O   . LYS J  1 128 ? -27.843 -11.000 97.823  1.00 72.69  ? 128 LYS S O   1 
ATOM   10914 C  CB  . LYS J  1 128 ? -25.786 -9.108  97.624  1.00 67.90  ? 128 LYS S CB  1 
ATOM   10915 C  CG  . LYS J  1 128 ? -24.448 -8.382  97.743  1.00 66.29  ? 128 LYS S CG  1 
ATOM   10916 C  CD  . LYS J  1 128 ? -24.603 -6.907  98.094  1.00 65.51  ? 128 LYS S CD  1 
ATOM   10917 C  CE  . LYS J  1 128 ? -23.283 -6.167  97.922  1.00 63.80  ? 128 LYS S CE  1 
ATOM   10918 N  NZ  . LYS J  1 128 ? -23.415 -4.708  98.177  1.00 63.25  ? 128 LYS S NZ  1 
ATOM   10919 N  N   . GLY J  1 129 ? -27.214 -12.143 95.974  1.00 70.87  ? 129 GLY S N   1 
ATOM   10920 C  CA  . GLY J  1 129 ? -28.395 -13.013 95.905  1.00 73.49  ? 129 GLY S CA  1 
ATOM   10921 C  C   . GLY J  1 129 ? -28.202 -14.388 96.526  1.00 76.68  ? 129 GLY S C   1 
ATOM   10922 O  O   . GLY J  1 129 ? -29.176 -15.010 96.957  1.00 79.72  ? 129 GLY S O   1 
ATOM   10923 N  N   . GLY J  1 130 ? -26.958 -14.874 96.549  1.00 76.33  ? 130 GLY S N   1 
ATOM   10924 C  CA  . GLY J  1 130 ? -26.608 -16.138 97.211  1.00 79.56  ? 130 GLY S CA  1 
ATOM   10925 C  C   . GLY J  1 130 ? -26.719 -17.365 96.321  1.00 80.98  ? 130 GLY S C   1 
ATOM   10926 O  O   . GLY J  1 130 ? -27.114 -18.440 96.784  1.00 84.58  ? 130 GLY S O   1 
ATOM   10927 N  N   . ASN J  1 131 ? -26.354 -17.206 95.051  0.75 78.46  ? 131 ASN S N   1 
ATOM   10928 C  CA  . ASN J  1 131 ? -26.403 -18.293 94.070  0.75 79.70  ? 131 ASN S CA  1 
ATOM   10929 C  C   . ASN J  1 131 ? -25.488 -17.986 92.881  0.75 76.70  ? 131 ASN S C   1 
ATOM   10930 O  O   . ASN J  1 131 ? -24.947 -16.877 92.773  0.75 73.63  ? 131 ASN S O   1 
ATOM   10931 C  CB  . ASN J  1 131 ? -27.851 -18.542 93.613  0.75 81.17  ? 131 ASN S CB  1 
ATOM   10932 C  CG  . ASN J  1 131 ? -28.555 -17.274 93.151  0.75 78.42  ? 131 ASN S CG  1 
ATOM   10933 O  OD1 . ASN J  1 131 ? -28.137 -16.624 92.193  0.75 75.34  ? 131 ASN S OD1 1 
ATOM   10934 N  ND2 . ASN J  1 131 ? -29.642 -16.928 93.825  0.75 79.85  ? 131 ASN S ND2 1 
ATOM   10935 N  N   . GLU J  1 132 ? -25.317 -18.970 91.998  0.75 77.91  ? 132 GLU S N   1 
ATOM   10936 C  CA  . GLU J  1 132 ? -24.440 -18.822 90.831  0.75 75.66  ? 132 GLU S CA  1 
ATOM   10937 C  C   . GLU J  1 132 ? -24.936 -17.760 89.839  0.75 72.51  ? 132 GLU S C   1 
ATOM   10938 O  O   . GLU J  1 132 ? -24.121 -17.062 89.237  0.75 69.78  ? 132 GLU S O   1 
ATOM   10939 C  CB  . GLU J  1 132 ? -24.247 -20.163 90.111  0.75 78.22  ? 132 GLU S CB  1 
ATOM   10940 C  CG  . GLU J  1 132 ? -23.119 -20.149 89.082  0.75 76.56  ? 132 GLU S CG  1 
ATOM   10941 C  CD  . GLU J  1 132 ? -22.928 -21.480 88.382  0.75 79.48  ? 132 GLU S CD  1 
ATOM   10942 O  OE1 . GLU J  1 132 ? -22.999 -22.538 89.048  0.75 83.09  ? 132 GLU S OE1 1 
ATOM   10943 O  OE2 . GLU J  1 132 ? -22.692 -21.463 87.157  0.75 78.37  ? 132 GLU S OE2 1 
ATOM   10944 N  N   . GLU J  1 133 ? -26.256 -17.645 89.674  1.00 73.19  ? 133 GLU S N   1 
ATOM   10945 C  CA  . GLU J  1 133 ? -26.842 -16.629 88.783  1.00 70.63  ? 133 GLU S CA  1 
ATOM   10946 C  C   . GLU J  1 133 ? -26.661 -15.200 89.319  1.00 67.93  ? 133 GLU S C   1 
ATOM   10947 O  O   . GLU J  1 133 ? -26.546 -14.257 88.526  1.00 65.25  ? 133 GLU S O   1 
ATOM   10948 C  CB  . GLU J  1 133 ? -28.330 -16.921 88.523  1.00 72.63  ? 133 GLU S CB  1 
ATOM   10949 C  CG  . GLU J  1 133 ? -28.955 -16.124 87.372  1.00 70.68  ? 133 GLU S CG  1 
ATOM   10950 C  CD  . GLU J  1 133 ? -28.305 -16.398 86.022  1.00 69.57  ? 133 GLU S CD  1 
ATOM   10951 O  OE1 . GLU J  1 133 ? -27.890 -17.547 85.765  1.00 71.57  ? 133 GLU S OE1 1 
ATOM   10952 O  OE2 . GLU J  1 133 ? -28.205 -15.464 85.204  1.00 67.00  ? 133 GLU S OE2 1 
ATOM   10953 N  N   . SER J  1 134 ? -26.631 -15.047 90.649  1.00 68.90  ? 134 SER S N   1 
ATOM   10954 C  CA  . SER J  1 134 ? -26.357 -13.753 91.294  1.00 66.88  ? 134 SER S CA  1 
ATOM   10955 C  C   . SER J  1 134 ? -24.923 -13.271 91.056  1.00 64.62  ? 134 SER S C   1 
ATOM   10956 O  O   . SER J  1 134 ? -24.697 -12.075 90.866  1.00 62.30  ? 134 SER S O   1 
ATOM   10957 C  CB  . SER J  1 134 ? -26.615 -13.823 92.800  1.00 68.96  ? 134 SER S CB  1 
ATOM   10958 O  OG  . SER J  1 134 ? -26.514 -12.535 93.379  1.00 67.33  ? 134 SER S OG  1 
ATOM   10959 N  N   . THR J  1 135 ? -23.969 -14.206 91.062  1.00 65.69  ? 135 THR S N   1 
ATOM   10960 C  CA  . THR J  1 135 ? -22.561 -13.915 90.740  1.00 64.10  ? 135 THR S CA  1 
ATOM   10961 C  C   . THR J  1 135 ? -22.265 -13.702 89.232  1.00 62.13  ? 135 THR S C   1 
ATOM   10962 O  O   . THR J  1 135 ? -21.147 -13.309 88.880  1.00 60.73  ? 135 THR S O   1 
ATOM   10963 C  CB  . THR J  1 135 ? -21.622 -15.021 91.282  1.00 66.39  ? 135 THR S CB  1 
ATOM   10964 O  OG1 . THR J  1 135 ? -21.968 -16.287 90.701  1.00 68.50  ? 135 THR S OG1 1 
ATOM   10965 C  CG2 . THR J  1 135 ? -21.719 -15.115 92.802  1.00 68.33  ? 135 THR S CG2 1 
ATOM   10966 N  N   . LYS J  1 136 ? -23.253 -13.949 88.361  1.00 62.30  ? 136 LYS S N   1 
ATOM   10967 C  CA  . LYS J  1 136 ? -23.123 -13.764 86.909  1.00 60.78  ? 136 LYS S CA  1 
ATOM   10968 C  C   . LYS J  1 136 ? -23.907 -12.558 86.395  1.00 58.76  ? 136 LYS S C   1 
ATOM   10969 O  O   . LYS J  1 136 ? -23.329 -11.637 85.815  1.00 56.59  ? 136 LYS S O   1 
ATOM   10970 C  CB  . LYS J  1 136 ? -23.604 -15.021 86.174  1.00 62.92  ? 136 LYS S CB  1 
ATOM   10971 C  CG  . LYS J  1 136 ? -22.674 -16.216 86.320  1.00 65.03  ? 136 LYS S CG  1 
ATOM   10972 C  CD  . LYS J  1 136 ? -23.276 -17.483 85.735  1.00 67.76  ? 136 LYS S CD  1 
ATOM   10973 C  CE  . LYS J  1 136 ? -23.410 -17.401 84.222  1.00 66.79  ? 136 LYS S CE  1 
ATOM   10974 N  NZ  . LYS J  1 136 ? -23.735 -18.730 83.637  1.00 69.87  ? 136 LYS S NZ  1 
ATOM   10975 N  N   . THR J  1 137 ? -25.226 -12.581 86.583  1.00 59.82  ? 137 THR S N   1 
ATOM   10976 C  CA  . THR J  1 137 ? -26.119 -11.541 86.037  1.00 58.47  ? 137 THR S CA  1 
ATOM   10977 C  C   . THR J  1 137 ? -26.723 -10.585 87.079  1.00 58.32  ? 137 THR S C   1 
ATOM   10978 O  O   . THR J  1 137 ? -27.227 -9.519  86.714  1.00 57.03  ? 137 THR S O   1 
ATOM   10979 C  CB  . THR J  1 137 ? -27.284 -12.174 85.242  1.00 60.07  ? 137 THR S CB  1 
ATOM   10980 O  OG1 . THR J  1 137 ? -27.977 -13.115 86.068  1.00 62.91  ? 137 THR S OG1 1 
ATOM   10981 C  CG2 . THR J  1 137 ? -26.772 -12.874 83.984  1.00 60.09  ? 137 THR S CG2 1 
ATOM   10982 N  N   . GLY J  1 138 ? -26.690 -10.962 88.357  1.00 59.85  ? 138 GLY S N   1 
ATOM   10983 C  CA  . GLY J  1 138 ? -27.380 -10.212 89.398  1.00 60.40  ? 138 GLY S CA  1 
ATOM   10984 C  C   . GLY J  1 138 ? -28.884 -10.465 89.490  1.00 62.50  ? 138 GLY S C   1 
ATOM   10985 O  O   . GLY J  1 138 ? -29.594 -9.719  90.173  1.00 63.01  ? 138 GLY S O   1 
ATOM   10986 N  N   . ASN J  1 139 ? -29.366 -11.511 88.810  1.00 63.99  ? 139 ASN S N   1 
ATOM   10987 C  CA  . ASN J  1 139 ? -30.784 -11.902 88.801  1.00 66.47  ? 139 ASN S CA  1 
ATOM   10988 C  C   . ASN J  1 139 ? -31.736 -10.784 88.332  1.00 65.69  ? 139 ASN S C   1 
ATOM   10989 O  O   . ASN J  1 139 ? -32.854 -10.645 88.836  1.00 67.71  ? 139 ASN S O   1 
ATOM   10990 C  CB  . ASN J  1 139 ? -31.184 -12.448 90.180  1.00 69.31  ? 139 ASN S CB  1 
ATOM   10991 C  CG  . ASN J  1 139 ? -30.293 -13.596 90.633  1.00 70.55  ? 139 ASN S CG  1 
ATOM   10992 O  OD1 . ASN J  1 139 ? -30.069 -14.548 89.888  1.00 71.30  ? 139 ASN S OD1 1 
ATOM   10993 N  ND2 . ASN J  1 139 ? -29.783 -13.512 91.855  1.00 71.05  ? 139 ASN S ND2 1 
ATOM   10994 N  N   . ALA J  1 140 ? -31.290 -10.019 87.335  1.00 63.07  ? 140 ALA S N   1 
ATOM   10995 C  CA  . ALA J  1 140 ? -32.047 -8.874  86.808  1.00 62.29  ? 140 ALA S CA  1 
ATOM   10996 C  C   . ALA J  1 140 ? -33.151 -9.247  85.793  1.00 63.78  ? 140 ALA S C   1 
ATOM   10997 O  O   . ALA J  1 140 ? -33.893 -8.365  85.348  1.00 63.65  ? 140 ALA S O   1 
ATOM   10998 C  CB  . ALA J  1 140 ? -31.091 -7.859  86.186  1.00 59.21  ? 140 ALA S CB  1 
ATOM   10999 N  N   . GLY J  1 141 ? -33.257 -10.527 85.425  1.00 65.43  ? 141 GLY S N   1 
ATOM   11000 C  CA  . GLY J  1 141 ? -34.272 -10.982 84.476  1.00 67.24  ? 141 GLY S CA  1 
ATOM   11001 C  C   . GLY J  1 141 ? -33.918 -10.656 83.033  1.00 65.26  ? 141 GLY S C   1 
ATOM   11002 O  O   . GLY J  1 141 ? -32.755 -10.355 82.711  1.00 62.69  ? 141 GLY S O   1 
ATOM   11003 N  N   . SER J  1 142 ? -34.934 -10.700 82.169  1.00 66.67  ? 142 SER S N   1 
ATOM   11004 C  CA  . SER J  1 142 ? -34.759 -10.526 80.719  1.00 65.48  ? 142 SER S CA  1 
ATOM   11005 C  C   . SER J  1 142 ? -34.338 -9.101  80.328  1.00 62.53  ? 142 SER S C   1 
ATOM   11006 O  O   . SER J  1 142 ? -34.344 -8.188  81.160  1.00 61.65  ? 142 SER S O   1 
ATOM   11007 C  CB  . SER J  1 142 ? -36.045 -10.913 79.977  1.00 68.34  ? 142 SER S CB  1 
ATOM   11008 O  OG  . SER J  1 142 ? -37.086 -9.992  80.249  1.00 69.19  ? 142 SER S OG  1 
ATOM   11009 N  N   . ARG J  1 143 ? -33.982 -8.932  79.054  1.00 61.29  ? 143 ARG S N   1 
ATOM   11010 C  CA  . ARG J  1 143 ? -33.485 -7.664  78.519  1.00 58.73  ? 143 ARG S CA  1 
ATOM   11011 C  C   . ARG J  1 143 ? -34.617 -6.933  77.792  1.00 59.74  ? 143 ARG S C   1 
ATOM   11012 O  O   . ARG J  1 143 ? -35.039 -7.355  76.711  1.00 60.91  ? 143 ARG S O   1 
ATOM   11013 C  CB  . ARG J  1 143 ? -32.303 -7.935  77.582  1.00 57.08  ? 143 ARG S CB  1 
ATOM   11014 C  CG  . ARG J  1 143 ? -31.229 -8.804  78.229  1.00 56.61  ? 143 ARG S CG  1 
ATOM   11015 C  CD  . ARG J  1 143 ? -30.098 -9.170  77.287  1.00 55.52  ? 143 ARG S CD  1 
ATOM   11016 N  NE  . ARG J  1 143 ? -29.195 -10.145 77.907  1.00 55.79  ? 143 ARG S NE  1 
ATOM   11017 C  CZ  . ARG J  1 143 ? -28.033 -10.557 77.394  1.00 55.10  ? 143 ARG S CZ  1 
ATOM   11018 N  NH1 . ARG J  1 143 ? -27.587 -10.086 76.226  1.00 54.02  ? 143 ARG S NH1 1 
ATOM   11019 N  NH2 . ARG J  1 143 ? -27.297 -11.446 78.064  1.00 55.73  ? 143 ARG S NH2 1 
ATOM   11020 N  N   . LEU J  1 144 ? -35.105 -5.848  78.399  1.00 59.54  ? 144 LEU S N   1 
ATOM   11021 C  CA  . LEU J  1 144 ? -36.278 -5.111  77.899  1.00 61.04  ? 144 LEU S CA  1 
ATOM   11022 C  C   . LEU J  1 144 ? -35.966 -4.186  76.718  1.00 59.60  ? 144 LEU S C   1 
ATOM   11023 O  O   . LEU J  1 144 ? -36.797 -4.034  75.819  1.00 61.20  ? 144 LEU S O   1 
ATOM   11024 C  CB  . LEU J  1 144 ? -36.913 -4.269  79.013  1.00 61.83  ? 144 LEU S CB  1 
ATOM   11025 C  CG  . LEU J  1 144 ? -37.352 -4.941  80.324  1.00 63.57  ? 144 LEU S CG  1 
ATOM   11026 C  CD1 . LEU J  1 144 ? -37.893 -3.881  81.278  1.00 64.28  ? 144 LEU S CD1 1 
ATOM   11027 C  CD2 . LEU J  1 144 ? -38.384 -6.035  80.082  1.00 66.71  ? 144 LEU S CD2 1 
ATOM   11028 N  N   . ALA J  1 145 ? -34.797 -3.541  76.746  1.00 56.90  ? 145 ALA S N   1 
ATOM   11029 C  CA  . ALA J  1 145 ? -34.399 -2.599  75.692  1.00 55.62  ? 145 ALA S CA  1 
ATOM   11030 C  C   . ALA J  1 145 ? -32.884 -2.391  75.648  1.00 52.96  ? 145 ALA S C   1 
ATOM   11031 O  O   . ALA J  1 145 ? -32.216 -2.298  76.686  1.00 51.81  ? 145 ALA S O   1 
ATOM   11032 C  CB  . ALA J  1 145 ? -35.101 -1.261  75.870  1.00 56.30  ? 145 ALA S CB  1 
ATOM   11033 N  N   . ALA J  1 146 ? -32.359 -2.308  74.431  1.00 52.18  ? 146 ALA S N   1 
ATOM   11034 C  CA  . ALA J  1 146 ? -30.934 -2.218  74.220  1.00 50.12  ? 146 ALA S CA  1 
ATOM   11035 C  C   . ALA J  1 146 ? -30.608 -1.319  73.038  1.00 49.60  ? 146 ALA S C   1 
ATOM   11036 O  O   . ALA J  1 146 ? -31.479 -0.954  72.235  1.00 50.81  ? 146 ALA S O   1 
ATOM   11037 C  CB  . ALA J  1 146 ? -30.352 -3.610  74.007  1.00 50.16  ? 146 ALA S CB  1 
ATOM   11038 N  N   . GLY J  1 147 ? -29.335 -0.955  72.969  1.00 47.95  ? 147 GLY S N   1 
ATOM   11039 C  CA  . GLY J  1 147 ? -28.789 -0.188  71.866  1.00 47.53  ? 147 GLY S CA  1 
ATOM   11040 C  C   . GLY J  1 147 ? -27.290 -0.347  71.884  1.00 46.11  ? 147 GLY S C   1 
ATOM   11041 O  O   . GLY J  1 147 ? -26.711 -0.592  72.951  1.00 45.22  ? 147 GLY S O   1 
ATOM   11042 N  N   . VAL J  1 148 ? -26.668 -0.204  70.712  1.00 46.05  ? 148 VAL S N   1 
ATOM   11043 C  CA  . VAL J  1 148 ? -25.214 -0.247  70.600  1.00 45.09  ? 148 VAL S CA  1 
ATOM   11044 C  C   . VAL J  1 148 ? -24.696 1.163   70.924  1.00 44.48  ? 148 VAL S C   1 
ATOM   11045 O  O   . VAL J  1 148 ? -25.272 2.167   70.490  1.00 45.11  ? 148 VAL S O   1 
ATOM   11046 C  CB  . VAL J  1 148 ? -24.753 -0.721  69.202  1.00 45.76  ? 148 VAL S CB  1 
ATOM   11047 C  CG1 . VAL J  1 148 ? -23.232 -0.816  69.136  1.00 45.12  ? 148 VAL S CG1 1 
ATOM   11048 C  CG2 . VAL J  1 148 ? -25.380 -2.072  68.846  1.00 46.85  ? 148 VAL S CG2 1 
ATOM   11049 N  N   . ILE J  1 149 ? -23.630 1.233   71.711  1.00 43.56  ? 149 ILE S N   1 
ATOM   11050 C  CA  . ILE J  1 149 ? -23.059 2.508   72.142  1.00 43.26  ? 149 ILE S CA  1 
ATOM   11051 C  C   . ILE J  1 149 ? -22.175 3.016   70.998  1.00 43.55  ? 149 ILE S C   1 
ATOM   11052 O  O   . ILE J  1 149 ? -21.398 2.245   70.434  1.00 43.55  ? 149 ILE S O   1 
ATOM   11053 C  CB  . ILE J  1 149 ? -22.230 2.364   73.450  1.00 42.54  ? 149 ILE S CB  1 
ATOM   11054 C  CG1 . ILE J  1 149 ? -23.111 1.824   74.595  1.00 42.49  ? 149 ILE S CG1 1 
ATOM   11055 C  CG2 . ILE J  1 149 ? -21.596 3.706   73.835  1.00 42.63  ? 149 ILE S CG2 1 
ATOM   11056 C  CD1 . ILE J  1 149 ? -22.353 1.300   75.805  1.00 42.04  ? 149 ILE S CD1 1 
ATOM   11057 N  N   . GLY J  1 150 ? -22.298 4.302   70.676  1.00 44.08  ? 150 GLY S N   1 
ATOM   11058 C  CA  . GLY J  1 150 ? -21.615 4.895   69.532  1.00 44.83  ? 150 GLY S CA  1 
ATOM   11059 C  C   . GLY J  1 150 ? -21.133 6.302   69.814  1.00 45.38  ? 150 GLY S C   1 
ATOM   11060 O  O   . GLY J  1 150 ? -21.624 6.979   70.721  1.00 45.42  ? 150 GLY S O   1 
ATOM   11061 N  N   . ILE J  1 151 ? -20.180 6.741   69.009  1.00 46.09  ? 151 ILE S N   1 
ATOM   11062 C  CA  . ILE J  1 151 ? -19.492 8.010   69.235  1.00 47.03  ? 151 ILE S CA  1 
ATOM   11063 C  C   . ILE J  1 151 ? -20.455 9.169   68.951  1.00 48.23  ? 151 ILE S C   1 
ATOM   11064 O  O   . ILE J  1 151 ? -21.184 9.135   67.954  1.00 48.88  ? 151 ILE S O   1 
ATOM   11065 C  CB  . ILE J  1 151 ? -18.213 8.112   68.357  1.00 47.93  ? 151 ILE S CB  1 
ATOM   11066 C  CG1 . ILE J  1 151 ? -17.229 6.992   68.733  1.00 47.10  ? 151 ILE S CG1 1 
ATOM   11067 C  CG2 . ILE J  1 151 ? -17.547 9.483   68.508  1.00 49.39  ? 151 ILE S CG2 1 
ATOM   11068 C  CD1 . ILE J  1 151 ? -16.144 6.729   67.707  1.00 48.11  ? 151 ILE S CD1 1 
ATOM   11069 N  N   . ALA J  1 152 ? -20.466 10.169  69.834  1.00 48.77  ? 152 ALA S N   1 
ATOM   11070 C  CA  . ALA J  1 152 ? -21.309 11.360  69.678  1.00 50.37  ? 152 ALA S CA  1 
ATOM   11071 C  C   . ALA J  1 152 ? -20.447 12.584  69.425  1.00 52.18  ? 152 ALA S C   1 
ATOM   11072 O  O   . ALA J  1 152 ? -19.267 12.603  69.780  1.00 52.11  ? 152 ALA S O   1 
ATOM   11073 C  CB  . ALA J  1 152 ? -22.156 11.573  70.923  1.00 50.18  ? 152 ALA S CB  1 
ATOM   11074 N  N   . GLN J  1 153 ? -21.039 13.610  68.822  1.00 54.13  ? 153 GLN S N   1 
ATOM   11075 C  CA  . GLN J  1 153 ? -20.335 14.875  68.586  1.00 56.43  ? 153 GLN S CA  1 
ATOM   11076 C  C   . GLN J  1 153 ? -20.147 15.653  69.898  1.00 57.16  ? 153 GLN S C   1 
ATOM   11077 O  O   . GLN J  1 153 ? -20.876 15.462  70.877  1.00 56.40  ? 153 GLN S O   1 
ATOM   11078 C  CB  . GLN J  1 153 ? -21.076 15.735  67.553  1.00 58.63  ? 153 GLN S CB  1 
ATOM   11079 C  CG  . GLN J  1 153 ? -20.259 16.919  67.043  1.00 61.28  ? 153 GLN S CG  1 
ATOM   11080 C  CD  . GLN J  1 153 ? -20.918 17.647  65.886  1.00 63.63  ? 153 GLN S CD  1 
ATOM   11081 O  OE1 . GLN J  1 153 ? -22.144 17.687  65.777  1.00 63.90  ? 153 GLN S OE1 1 
ATOM   11082 N  NE2 . GLN J  1 153 ? -20.101 18.239  65.020  1.00 65.64  ? 153 GLN S NE2 1 
ATOM   11083 O  OXT . GLN J  1 153 ? -19.250 16.495  70.018  1.00 58.87  ? 153 GLN S OXT 1 
ATOM   11084 N  N   . ALA K  1 1   ? -2.138  -31.157 27.897  0.75 71.72  ? 1   ALA U N   1 
ATOM   11085 C  CA  . ALA K  1 1   ? -2.444  -31.421 26.455  1.00 70.35  ? 1   ALA U CA  1 
ATOM   11086 C  C   . ALA K  1 1   ? -3.177  -30.247 25.805  1.00 68.01  ? 1   ALA U C   1 
ATOM   11087 O  O   . ALA K  1 1   ? -4.280  -29.889 26.223  1.00 68.21  ? 1   ALA U O   1 
ATOM   11088 C  CB  . ALA K  1 1   ? -3.267  -32.693 26.310  1.00 72.23  ? 1   ALA U CB  1 
ATOM   11089 N  N   . THR K  1 2   ? -2.562  -29.653 24.784  1.00 66.07  ? 2   THR U N   1 
ATOM   11090 C  CA  . THR K  1 2   ? -3.188  -28.569 24.031  1.00 63.96  ? 2   THR U CA  1 
ATOM   11091 C  C   . THR K  1 2   ? -4.271  -29.136 23.111  1.00 63.95  ? 2   THR U C   1 
ATOM   11092 O  O   . THR K  1 2   ? -4.116  -30.230 22.551  1.00 64.97  ? 2   THR U O   1 
ATOM   11093 C  CB  . THR K  1 2   ? -2.157  -27.793 23.187  1.00 62.32  ? 2   THR U CB  1 
ATOM   11094 O  OG1 . THR K  1 2   ? -0.982  -27.552 23.971  1.00 62.94  ? 2   THR U OG1 1 
ATOM   11095 C  CG2 . THR K  1 2   ? -2.732  -26.457 22.703  1.00 60.40  ? 2   THR U CG2 1 
ATOM   11096 N  N   . LYS K  1 3   ? -5.359  -28.382 22.969  1.00 63.02  ? 3   LYS U N   1 
ATOM   11097 C  CA  . LYS K  1 3   ? -6.511  -28.773 22.156  1.00 63.20  ? 3   LYS U CA  1 
ATOM   11098 C  C   . LYS K  1 3   ? -6.983  -27.594 21.317  1.00 61.21  ? 3   LYS U C   1 
ATOM   11099 O  O   . LYS K  1 3   ? -6.788  -26.431 21.694  1.00 60.01  ? 3   LYS U O   1 
ATOM   11100 C  CB  . LYS K  1 3   ? -7.662  -29.235 23.049  1.00 65.11  ? 3   LYS U CB  1 
ATOM   11101 C  CG  . LYS K  1 3   ? -7.326  -30.405 23.955  1.00 67.44  ? 3   LYS U CG  1 
ATOM   11102 C  CD  . LYS K  1 3   ? -8.557  -30.837 24.728  1.00 69.65  ? 3   LYS U CD  1 
ATOM   11103 C  CE  . LYS K  1 3   ? -8.301  -32.092 25.543  1.00 72.37  ? 3   LYS U CE  1 
ATOM   11104 N  NZ  . LYS K  1 3   ? -9.540  -32.552 26.230  1.00 74.93  ? 3   LYS U NZ  1 
ATOM   11105 N  N   . ALA K  1 4   ? -7.613  -27.900 20.187  1.00 61.09  ? 4   ALA U N   1 
ATOM   11106 C  CA  . ALA K  1 4   ? -8.193  -26.868 19.331  1.00 59.59  ? 4   ALA U CA  1 
ATOM   11107 C  C   . ALA K  1 4   ? -9.429  -27.373 18.593  1.00 60.54  ? 4   ALA U C   1 
ATOM   11108 O  O   . ALA K  1 4   ? -9.678  -28.583 18.530  1.00 62.29  ? 4   ALA U O   1 
ATOM   11109 C  CB  . ALA K  1 4   ? -7.145  -26.332 18.355  1.00 58.00  ? 4   ALA U CB  1 
ATOM   11110 N  N   . VAL K  1 5   ? -10.201 -26.425 18.058  1.00 59.59  ? 5   VAL U N   1 
ATOM   11111 C  CA  . VAL K  1 5   ? -11.442 -26.722 17.340  1.00 60.62  ? 5   VAL U CA  1 
ATOM   11112 C  C   . VAL K  1 5   ? -11.681 -25.709 16.213  1.00 59.19  ? 5   VAL U C   1 
ATOM   11113 O  O   . VAL K  1 5   ? -11.240 -24.551 16.289  1.00 57.53  ? 5   VAL U O   1 
ATOM   11114 C  CB  . VAL K  1 5   ? -12.658 -26.785 18.311  1.00 62.21  ? 5   VAL U CB  1 
ATOM   11115 C  CG1 . VAL K  1 5   ? -13.055 -25.396 18.803  1.00 61.13  ? 5   VAL U CG1 1 
ATOM   11116 C  CG2 . VAL K  1 5   ? -13.846 -27.494 17.669  1.00 64.11  ? 5   VAL U CG2 1 
ATOM   11117 N  N   . CYS K  1 6   ? -12.368 -26.175 15.171  1.00 60.12  ? 6   CYS U N   1 
ATOM   11118 C  CA  . CYS K  1 6   ? -12.738 -25.356 14.020  1.00 59.28  ? 6   CYS U CA  1 
ATOM   11119 C  C   . CYS K  1 6   ? -14.170 -25.673 13.585  1.00 61.05  ? 6   CYS U C   1 
ATOM   11120 O  O   . CYS K  1 6   ? -14.554 -26.842 13.515  1.00 62.92  ? 6   CYS U O   1 
ATOM   11121 C  CB  . CYS K  1 6   ? -11.781 -25.606 12.854  1.00 58.72  ? 6   CYS U CB  1 
ATOM   11122 S  SG  . CYS K  1 6   ? -12.151 -24.603 11.395  1.00 58.01  ? 6   CYS U SG  1 
ATOM   11123 N  N   . VAL K  1 7   ? -14.940 -24.618 13.308  1.00 60.60  ? 7   VAL U N   1 
ATOM   11124 C  CA  . VAL K  1 7   ? -16.312 -24.726 12.825  1.00 62.37  ? 7   VAL U CA  1 
ATOM   11125 C  C   . VAL K  1 7   ? -16.308 -24.317 11.356  1.00 61.96  ? 7   VAL U C   1 
ATOM   11126 O  O   . VAL K  1 7   ? -16.222 -23.130 11.038  1.00 60.57  ? 7   VAL U O   1 
ATOM   11127 C  CB  . VAL K  1 7   ? -17.272 -23.820 13.630  1.00 62.62  ? 7   VAL U CB  1 
ATOM   11128 C  CG1 . VAL K  1 7   ? -18.707 -23.955 13.119  1.00 64.82  ? 7   VAL U CG1 1 
ATOM   11129 C  CG2 . VAL K  1 7   ? -17.182 -24.144 15.120  1.00 63.13  ? 7   VAL U CG2 1 
ATOM   11130 N  N   . LEU K  1 8   ? -16.387 -25.307 10.471  1.00 63.42  ? 8   LEU U N   1 
ATOM   11131 C  CA  . LEU K  1 8   ? -16.359 -25.071 9.031   1.00 63.50  ? 8   LEU U CA  1 
ATOM   11132 C  C   . LEU K  1 8   ? -17.739 -24.636 8.562   1.00 64.97  ? 8   LEU U C   1 
ATOM   11133 O  O   . LEU K  1 8   ? -18.721 -25.323 8.836   1.00 67.21  ? 8   LEU U O   1 
ATOM   11134 C  CB  . LEU K  1 8   ? -15.930 -26.343 8.290   1.00 64.92  ? 8   LEU U CB  1 
ATOM   11135 C  CG  . LEU K  1 8   ? -14.555 -26.914 8.665   1.00 63.93  ? 8   LEU U CG  1 
ATOM   11136 C  CD1 . LEU K  1 8   ? -14.340 -28.276 8.026   1.00 65.95  ? 8   LEU U CD1 1 
ATOM   11137 C  CD2 . LEU K  1 8   ? -13.448 -25.958 8.259   1.00 61.71  ? 8   LEU U CD2 1 
ATOM   11138 N  N   . LYS K  1 9   ? -17.807 -23.480 7.892   1.00 63.98  ? 9   LYS U N   1 
ATOM   11139 C  CA  . LYS K  1 9   ? -19.043 -22.966 7.272   1.00 65.45  ? 9   LYS U CA  1 
ATOM   11140 C  C   . LYS K  1 9   ? -18.738 -22.269 5.942   1.00 64.97  ? 9   LYS U C   1 
ATOM   11141 O  O   . LYS K  1 9   ? -17.644 -21.721 5.751   1.00 63.01  ? 9   LYS U O   1 
ATOM   11142 C  CB  . LYS K  1 9   ? -19.754 -21.961 8.188   1.00 65.05  ? 9   LYS U CB  1 
ATOM   11143 C  CG  . LYS K  1 9   ? -20.197 -22.489 9.544   1.00 65.91  ? 9   LYS U CG  1 
ATOM   11144 C  CD  . LYS K  1 9   ? -21.341 -23.491 9.447   1.00 69.06  ? 9   LYS U CD  1 
ATOM   11145 C  CE  . LYS K  1 9   ? -21.655 -24.091 10.812  1.00 70.12  ? 9   LYS U CE  1 
ATOM   11146 N  NZ  . LYS K  1 9   ? -22.269 -23.099 11.741  1.00 69.97  ? 9   LYS U NZ  1 
ATOM   11147 N  N   . GLY K  1 10  ? -19.719 -22.281 5.040   1.00 67.03  ? 10  GLY U N   1 
ATOM   11148 C  CA  . GLY K  1 10  ? -19.596 -21.646 3.724   1.00 67.18  ? 10  GLY U CA  1 
ATOM   11149 C  C   . GLY K  1 10  ? -20.907 -21.089 3.203   1.00 69.07  ? 10  GLY U C   1 
ATOM   11150 O  O   . GLY K  1 10  ? -21.868 -20.931 3.959   1.00 69.90  ? 10  GLY U O   1 
ATOM   11151 N  N   . ASP K  1 11  ? -20.937 -20.781 1.907   1.00 70.01  ? 11  ASP U N   1 
ATOM   11152 C  CA  . ASP K  1 11  ? -22.144 -20.250 1.260   1.00 72.14  ? 11  ASP U CA  1 
ATOM   11153 C  C   . ASP K  1 11  ? -23.176 -21.354 1.046   1.00 75.34  ? 11  ASP U C   1 
ATOM   11154 O  O   . ASP K  1 11  ? -24.356 -21.173 1.351   1.00 77.08  ? 11  ASP U O   1 
ATOM   11155 C  CB  . ASP K  1 11  ? -21.806 -19.592 -0.085  1.00 72.44  ? 11  ASP U CB  1 
ATOM   11156 C  CG  . ASP K  1 11  ? -20.910 -18.363 0.057   1.00 69.83  ? 11  ASP U CG  1 
ATOM   11157 O  OD1 . ASP K  1 11  ? -20.607 -17.941 1.196   1.00 67.79  ? 11  ASP U OD1 1 
ATOM   11158 O  OD2 . ASP K  1 11  ? -20.511 -17.811 -0.991  1.00 70.10  ? 11  ASP U OD2 1 
ATOM   11159 N  N   . GLY K  1 12  ? -22.722 -22.493 0.524   1.00 76.36  ? 12  GLY U N   1 
ATOM   11160 C  CA  . GLY K  1 12  ? -23.578 -23.652 0.282   1.00 79.66  ? 12  GLY U CA  1 
ATOM   11161 C  C   . GLY K  1 12  ? -23.894 -24.451 1.541   1.00 80.01  ? 12  GLY U C   1 
ATOM   11162 O  O   . GLY K  1 12  ? -23.804 -23.923 2.653   1.00 78.07  ? 12  GLY U O   1 
ATOM   11163 N  N   . PRO K  1 13  ? -24.277 -25.736 1.377   1.00 82.80  ? 13  PRO U N   1 
ATOM   11164 C  CA  . PRO K  1 13  ? -24.632 -26.593 2.514   1.00 83.77  ? 13  PRO U CA  1 
ATOM   11165 C  C   . PRO K  1 13  ? -23.459 -27.283 3.244   1.00 81.80  ? 13  PRO U C   1 
ATOM   11166 O  O   . PRO K  1 13  ? -23.697 -27.927 4.270   1.00 82.53  ? 13  PRO U O   1 
ATOM   11167 C  CB  . PRO K  1 13  ? -25.546 -27.640 1.874   1.00 88.05  ? 13  PRO U CB  1 
ATOM   11168 C  CG  . PRO K  1 13  ? -25.029 -27.775 0.485   1.00 88.57  ? 13  PRO U CG  1 
ATOM   11169 C  CD  . PRO K  1 13  ? -24.497 -26.425 0.089   1.00 85.68  ? 13  PRO U CD  1 
ATOM   11170 N  N   . VAL K  1 14  ? -22.227 -27.155 2.741   1.00 79.63  ? 14  VAL U N   1 
ATOM   11171 C  CA  . VAL K  1 14  ? -21.067 -27.823 3.353   1.00 78.04  ? 14  VAL U CA  1 
ATOM   11172 C  C   . VAL K  1 14  ? -20.762 -27.182 4.702   1.00 75.41  ? 14  VAL U C   1 
ATOM   11173 O  O   . VAL K  1 14  ? -20.612 -25.962 4.789   1.00 73.29  ? 14  VAL U O   1 
ATOM   11174 C  CB  . VAL K  1 14  ? -19.802 -27.774 2.456   1.00 76.63  ? 14  VAL U CB  1 
ATOM   11175 C  CG1 . VAL K  1 14  ? -18.589 -28.360 3.174   1.00 74.99  ? 14  VAL U CG1 1 
ATOM   11176 C  CG2 . VAL K  1 14  ? -20.038 -28.536 1.160   1.00 79.57  ? 14  VAL U CG2 1 
ATOM   11177 N  N   . GLN K  1 15  ? -20.688 -28.011 5.743   1.00 75.88  ? 15  GLN U N   1 
ATOM   11178 C  CA  . GLN K  1 15  ? -20.344 -27.551 7.088   1.00 73.80  ? 15  GLN U CA  1 
ATOM   11179 C  C   . GLN K  1 15  ? -19.923 -28.698 7.999   1.00 74.49  ? 15  GLN U C   1 
ATOM   11180 O  O   . GLN K  1 15  ? -20.207 -29.863 7.716   1.00 77.08  ? 15  GLN U O   1 
ATOM   11181 C  CB  . GLN K  1 15  ? -21.516 -26.791 7.723   1.00 74.44  ? 15  GLN U CB  1 
ATOM   11182 C  CG  . GLN K  1 15  ? -22.830 -27.562 7.793   1.00 78.14  ? 15  GLN U CG  1 
ATOM   11183 C  CD  . GLN K  1 15  ? -23.958 -26.744 8.397   1.00 78.94  ? 15  GLN U CD  1 
ATOM   11184 O  OE1 . GLN K  1 15  ? -23.779 -25.579 8.754   1.00 76.71  ? 15  GLN U OE1 1 
ATOM   11185 N  NE2 . GLN K  1 15  ? -25.130 -27.354 8.514   1.00 82.43  ? 15  GLN U NE2 1 
ATOM   11186 N  N   . GLY K  1 16  ? -19.255 -28.356 9.099   1.00 72.40  ? 16  GLY U N   1 
ATOM   11187 C  CA  . GLY K  1 16  ? -18.779 -29.359 10.048  1.00 72.99  ? 16  GLY U CA  1 
ATOM   11188 C  C   . GLY K  1 16  ? -17.999 -28.807 11.225  1.00 70.64  ? 16  GLY U C   1 
ATOM   11189 O  O   . GLY K  1 16  ? -17.756 -27.600 11.310  1.00 68.40  ? 16  GLY U O   1 
ATOM   11190 N  N   . ILE K  1 17  ? -17.611 -29.709 12.127  1.00 71.42  ? 17  ILE U N   1 
ATOM   11191 C  CA  . ILE K  1 17  ? -16.820 -29.376 13.320  1.00 69.67  ? 17  ILE U CA  1 
ATOM   11192 C  C   . ILE K  1 17  ? -15.569 -30.269 13.378  1.00 69.40  ? 17  ILE U C   1 
ATOM   11193 O  O   . ILE K  1 17  ? -15.655 -31.454 13.725  1.00 71.60  ? 17  ILE U O   1 
ATOM   11194 C  CB  . ILE K  1 17  ? -17.643 -29.535 14.629  1.00 71.32  ? 17  ILE U CB  1 
ATOM   11195 C  CG1 . ILE K  1 17  ? -18.998 -28.800 14.545  1.00 72.29  ? 17  ILE U CG1 1 
ATOM   11196 C  CG2 . ILE K  1 17  ? -16.835 -29.065 15.839  1.00 69.62  ? 17  ILE U CG2 1 
ATOM   11197 C  CD1 . ILE K  1 17  ? -18.920 -27.285 14.508  1.00 69.81  ? 17  ILE U CD1 1 
ATOM   11198 N  N   . ILE K  1 18  ? -14.416 -29.696 13.025  1.00 66.97  ? 18  ILE U N   1 
ATOM   11199 C  CA  . ILE K  1 18  ? -13.125 -30.395 13.089  1.00 66.62  ? 18  ILE U CA  1 
ATOM   11200 C  C   . ILE K  1 18  ? -12.414 -30.060 14.408  1.00 65.39  ? 18  ILE U C   1 
ATOM   11201 O  O   . ILE K  1 18  ? -12.340 -28.891 14.805  1.00 63.57  ? 18  ILE U O   1 
ATOM   11202 C  CB  . ILE K  1 18  ? -12.210 -30.033 11.886  1.00 65.22  ? 18  ILE U CB  1 
ATOM   11203 C  CG1 . ILE K  1 18  ? -12.874 -30.406 10.548  1.00 66.74  ? 18  ILE U CG1 1 
ATOM   11204 C  CG2 . ILE K  1 18  ? -10.842 -30.708 12.008  1.00 65.10  ? 18  ILE U CG2 1 
ATOM   11205 C  CD1 . ILE K  1 18  ? -13.091 -31.895 10.317  1.00 69.57  ? 18  ILE U CD1 1 
ATOM   11206 N  N   . ASN K  1 19  ? -11.889 -31.100 15.060  1.00 66.61  ? 19  ASN U N   1 
ATOM   11207 C  CA  . ASN K  1 19  ? -11.187 -30.991 16.338  1.00 66.01  ? 19  ASN U CA  1 
ATOM   11208 C  C   . ASN K  1 19  ? -9.690  -31.239 16.148  1.00 65.12  ? 19  ASN U C   1 
ATOM   11209 O  O   . ASN K  1 19  ? -9.248  -31.704 15.093  1.00 65.36  ? 19  ASN U O   1 
ATOM   11210 C  CB  . ASN K  1 19  ? -11.767 -31.996 17.343  1.00 68.59  ? 19  ASN U CB  1 
ATOM   11211 C  CG  . ASN K  1 19  ? -13.276 -31.869 17.494  1.00 70.04  ? 19  ASN U CG  1 
ATOM   11212 O  OD1 . ASN K  1 19  ? -13.772 -30.908 18.084  1.00 69.23  ? 19  ASN U OD1 1 
ATOM   11213 N  ND2 . ASN K  1 19  ? -14.012 -32.839 16.959  1.00 72.44  ? 19  ASN U ND2 1 
ATOM   11214 N  N   . PHE K  1 20  ? -8.919  -30.895 17.174  1.00 64.30  ? 20  PHE U N   1 
ATOM   11215 C  CA  . PHE K  1 20  ? -7.462  -31.043 17.173  1.00 63.68  ? 20  PHE U CA  1 
ATOM   11216 C  C   . PHE K  1 20  ? -6.991  -31.379 18.587  1.00 64.53  ? 20  PHE U C   1 
ATOM   11217 O  O   . PHE K  1 20  ? -7.521  -30.836 19.560  1.00 64.43  ? 20  PHE U O   1 
ATOM   11218 C  CB  . PHE K  1 20  ? -6.775  -29.741 16.745  1.00 61.30  ? 20  PHE U CB  1 
ATOM   11219 C  CG  . PHE K  1 20  ? -7.112  -29.278 15.349  1.00 60.48  ? 20  PHE U CG  1 
ATOM   11220 C  CD1 . PHE K  1 20  ? -8.234  -28.486 15.113  1.00 59.86  ? 20  PHE U CD1 1 
ATOM   11221 C  CD2 . PHE K  1 20  ? -6.286  -29.597 14.276  1.00 60.55  ? 20  PHE U CD2 1 
ATOM   11222 C  CE1 . PHE K  1 20  ? -8.540  -28.044 13.831  1.00 59.32  ? 20  PHE U CE1 1 
ATOM   11223 C  CE2 . PHE K  1 20  ? -6.588  -29.159 12.992  1.00 60.07  ? 20  PHE U CE2 1 
ATOM   11224 C  CZ  . PHE K  1 20  ? -7.715  -28.379 12.770  1.00 59.42  ? 20  PHE U CZ  1 
ATOM   11225 N  N   . GLU K  1 21  ? -5.994  -32.257 18.703  1.00 65.57  ? 21  GLU U N   1 
ATOM   11226 C  CA  . GLU K  1 21  ? -5.392  -32.584 20.004  1.00 66.55  ? 21  GLU U CA  1 
ATOM   11227 C  C   . GLU K  1 21  ? -3.904  -32.909 19.863  1.00 66.64  ? 21  GLU U C   1 
ATOM   11228 O  O   . GLU K  1 21  ? -3.496  -33.560 18.895  1.00 67.19  ? 21  GLU U O   1 
ATOM   11229 C  CB  . GLU K  1 21  ? -6.133  -33.750 20.674  1.00 69.23  ? 21  GLU U CB  1 
ATOM   11230 C  CG  . GLU K  1 21  ? -5.758  -33.962 22.141  1.00 70.45  ? 21  GLU U CG  1 
ATOM   11231 C  CD  . GLU K  1 21  ? -6.754  -34.818 22.910  1.00 73.13  ? 21  GLU U CD  1 
ATOM   11232 O  OE1 . GLU K  1 21  ? -7.970  -34.729 22.645  1.00 73.52  ? 21  GLU U OE1 1 
ATOM   11233 O  OE2 . GLU K  1 21  ? -6.321  -35.578 23.801  1.00 75.13  ? 21  GLU U OE2 1 
ATOM   11234 N  N   . GLN K  1 22  ? -3.114  -32.445 20.836  1.00 66.35  ? 22  GLN U N   1 
ATOM   11235 C  CA  . GLN K  1 22  ? -1.660  -32.632 20.865  1.00 66.64  ? 22  GLN U CA  1 
ATOM   11236 C  C   . GLN K  1 22  ? -1.223  -32.829 22.318  1.00 67.96  ? 22  GLN U C   1 
ATOM   11237 O  O   . GLN K  1 22  ? -1.185  -31.876 23.104  1.00 67.12  ? 22  GLN U O   1 
ATOM   11238 C  CB  . GLN K  1 22  ? -0.960  -31.421 20.231  1.00 64.54  ? 22  GLN U CB  1 
ATOM   11239 C  CG  . GLN K  1 22  ? 0.517   -31.622 19.918  1.00 65.04  ? 22  GLN U CG  1 
ATOM   11240 C  CD  . GLN K  1 22  ? 1.147   -30.411 19.239  1.00 63.31  ? 22  GLN U CD  1 
ATOM   11241 O  OE1 . GLN K  1 22  ? 0.879   -29.267 19.604  1.00 61.90  ? 22  GLN U OE1 1 
ATOM   11242 N  NE2 . GLN K  1 22  ? 1.994   -30.660 18.248  1.00 63.69  ? 22  GLN U NE2 1 
ATOM   11243 N  N   . LYS K  1 23  ? -0.901  -34.072 22.666  1.00 70.26  ? 23  LYS U N   1 
ATOM   11244 C  CA  . LYS K  1 23  ? -0.647  -34.467 24.060  1.00 72.10  ? 23  LYS U CA  1 
ATOM   11245 C  C   . LYS K  1 23  ? 0.723   -34.028 24.596  1.00 72.07  ? 23  LYS U C   1 
ATOM   11246 O  O   . LYS K  1 23  ? 0.903   -33.914 25.810  1.00 73.11  ? 23  LYS U O   1 
ATOM   11247 C  CB  . LYS K  1 23  ? -0.832  -35.982 24.219  1.00 74.93  ? 23  LYS U CB  1 
ATOM   11248 C  CG  . LYS K  1 23  ? -2.252  -36.441 23.905  1.00 75.57  ? 23  LYS U CG  1 
ATOM   11249 C  CD  . LYS K  1 23  ? -2.429  -37.943 24.055  1.00 78.71  ? 23  LYS U CD  1 
ATOM   11250 C  CE  . LYS K  1 23  ? -3.884  -38.340 23.857  1.00 79.72  ? 23  LYS U CE  1 
ATOM   11251 N  NZ  . LYS K  1 23  ? -4.096  -39.807 24.000  1.00 83.11  ? 23  LYS U NZ  1 
ATOM   11252 N  N   . GLU K  1 24  ? 1.678   -33.806 23.694  1.00 71.18  ? 24  GLU U N   1 
ATOM   11253 C  CA  . GLU K  1 24  ? 2.947   -33.158 24.021  1.00 71.02  ? 24  GLU U CA  1 
ATOM   11254 C  C   . GLU K  1 24  ? 3.373   -32.283 22.844  1.00 69.03  ? 24  GLU U C   1 
ATOM   11255 O  O   . GLU K  1 24  ? 3.181   -32.669 21.691  1.00 68.68  ? 24  GLU U O   1 
ATOM   11256 C  CB  . GLU K  1 24  ? 4.042   -34.194 24.303  1.00 73.50  ? 24  GLU U CB  1 
ATOM   11257 C  CG  . GLU K  1 24  ? 3.941   -34.919 25.647  1.00 75.87  ? 24  GLU U CG  1 
ATOM   11258 C  CD  . GLU K  1 24  ? 3.305   -36.298 25.561  1.00 77.81  ? 24  GLU U CD  1 
ATOM   11259 O  OE1 . GLU K  1 24  ? 3.774   -37.133 24.757  1.00 78.78  ? 24  GLU U OE1 1 
ATOM   11260 O  OE2 . GLU K  1 24  ? 2.352   -36.561 26.324  1.00 78.70  ? 24  GLU U OE2 1 
ATOM   11261 N  N   . SER K  1 25  ? 3.983   -31.134 23.132  1.00 68.05  ? 25  SER U N   1 
ATOM   11262 C  CA  . SER K  1 25  ? 4.419   -30.181 22.089  1.00 66.42  ? 25  SER U CA  1 
ATOM   11263 C  C   . SER K  1 25  ? 5.321   -30.782 20.992  1.00 67.23  ? 25  SER U C   1 
ATOM   11264 O  O   . SER K  1 25  ? 5.321   -30.303 19.854  1.00 66.03  ? 25  SER U O   1 
ATOM   11265 C  CB  . SER K  1 25  ? 5.143   -28.992 22.727  1.00 66.06  ? 25  SER U CB  1 
ATOM   11266 O  OG  . SER K  1 25  ? 6.381   -29.398 23.293  1.00 68.11  ? 25  SER U OG  1 
ATOM   11267 N  N   . ASN K  1 26  ? 6.101   -31.801 21.356  1.00 69.45  ? 26  ASN U N   1 
ATOM   11268 C  CA  . ASN K  1 26  ? 6.959   -32.528 20.411  1.00 70.78  ? 26  ASN U CA  1 
ATOM   11269 C  C   . ASN K  1 26  ? 6.255   -33.698 19.700  1.00 71.50  ? 26  ASN U C   1 
ATOM   11270 O  O   . ASN K  1 26  ? 6.771   -34.208 18.707  1.00 72.42  ? 26  ASN U O   1 
ATOM   11271 C  CB  . ASN K  1 26  ? 8.241   -33.015 21.107  1.00 73.15  ? 26  ASN U CB  1 
ATOM   11272 C  CG  . ASN K  1 26  ? 7.984   -34.113 22.121  1.00 75.02  ? 26  ASN U CG  1 
ATOM   11273 O  OD1 . ASN K  1 26  ? 6.946   -34.134 22.780  1.00 74.43  ? 26  ASN U OD1 1 
ATOM   11274 N  ND2 . ASN K  1 26  ? 8.934   -35.028 22.255  1.00 77.56  ? 26  ASN U ND2 1 
ATOM   11275 N  N   . GLY K  1 27  ? 5.101   -34.126 20.216  1.00 71.42  ? 27  GLY U N   1 
ATOM   11276 C  CA  . GLY K  1 27  ? 4.319   -35.217 19.631  1.00 72.37  ? 27  GLY U CA  1 
ATOM   11277 C  C   . GLY K  1 27  ? 3.421   -34.790 18.477  1.00 70.68  ? 27  GLY U C   1 
ATOM   11278 O  O   . GLY K  1 27  ? 3.388   -33.610 18.111  1.00 68.65  ? 27  GLY U O   1 
ATOM   11279 N  N   . PRO K  1 28  ? 2.680   -35.753 17.892  1.00 71.77  ? 28  PRO U N   1 
ATOM   11280 C  CA  . PRO K  1 28  ? 1.844   -35.476 16.720  1.00 70.65  ? 28  PRO U CA  1 
ATOM   11281 C  C   . PRO K  1 28  ? 0.517   -34.794 17.063  1.00 69.05  ? 28  PRO U C   1 
ATOM   11282 O  O   . PRO K  1 28  ? 0.068   -34.842 18.212  1.00 69.35  ? 28  PRO U O   1 
ATOM   11283 C  CB  . PRO K  1 28  ? 1.599   -36.870 16.134  1.00 73.02  ? 28  PRO U CB  1 
ATOM   11284 C  CG  . PRO K  1 28  ? 1.650   -37.782 17.312  1.00 74.97  ? 28  PRO U CG  1 
ATOM   11285 C  CD  . PRO K  1 28  ? 2.620   -37.174 18.287  1.00 74.44  ? 28  PRO U CD  1 
ATOM   11286 N  N   . VAL K  1 29  ? -0.088  -34.167 16.055  1.00 67.65  ? 29  VAL U N   1 
ATOM   11287 C  CA  . VAL K  1 29  ? -1.412  -33.548 16.167  1.00 66.37  ? 29  VAL U CA  1 
ATOM   11288 C  C   . VAL K  1 29  ? -2.471  -34.548 15.680  1.00 67.96  ? 29  VAL U C   1 
ATOM   11289 O  O   . VAL K  1 29  ? -2.506  -34.896 14.495  1.00 68.51  ? 29  VAL U O   1 
ATOM   11290 C  CB  . VAL K  1 29  ? -1.504  -32.244 15.334  1.00 64.17  ? 29  VAL U CB  1 
ATOM   11291 C  CG1 . VAL K  1 29  ? -2.860  -31.570 15.517  1.00 63.05  ? 29  VAL U CG1 1 
ATOM   11292 C  CG2 . VAL K  1 29  ? -0.392  -31.282 15.718  1.00 63.00  ? 29  VAL U CG2 1 
ATOM   11293 N  N   . LYS K  1 30  ? -3.313  -35.023 16.599  1.00 69.00  ? 30  LYS U N   1 
ATOM   11294 C  CA  . LYS K  1 30  ? -4.483  -35.826 16.238  1.00 70.63  ? 30  LYS U CA  1 
ATOM   11295 C  C   . LYS K  1 30  ? -5.565  -34.879 15.708  1.00 69.08  ? 30  LYS U C   1 
ATOM   11296 O  O   . LYS K  1 30  ? -5.899  -33.893 16.366  1.00 67.52  ? 30  LYS U O   1 
ATOM   11297 C  CB  . LYS K  1 30  ? -5.004  -36.611 17.448  1.00 72.61  ? 30  LYS U CB  1 
ATOM   11298 C  CG  . LYS K  1 30  ? -6.120  -37.601 17.133  1.00 75.01  ? 30  LYS U CG  1 
ATOM   11299 C  CD  . LYS K  1 30  ? -5.583  -38.861 16.463  1.00 77.31  ? 30  LYS U CD  1 
ATOM   11300 C  CE  . LYS K  1 30  ? -6.648  -39.594 15.665  1.00 79.35  ? 30  LYS U CE  1 
ATOM   11301 N  NZ  . LYS K  1 30  ? -6.035  -40.686 14.866  1.00 81.47  ? 30  LYS U NZ  1 
ATOM   11302 N  N   . VAL K  1 31  ? -6.094  -35.188 14.525  1.00 69.73  ? 31  VAL U N   1 
ATOM   11303 C  CA  . VAL K  1 31  ? -7.123  -34.386 13.862  1.00 68.67  ? 31  VAL U CA  1 
ATOM   11304 C  C   . VAL K  1 31  ? -8.320  -35.292 13.590  1.00 71.08  ? 31  VAL U C   1 
ATOM   11305 O  O   . VAL K  1 31  ? -8.180  -36.298 12.896  1.00 73.07  ? 31  VAL U O   1 
ATOM   11306 C  CB  . VAL K  1 31  ? -6.601  -33.815 12.520  1.00 67.49  ? 31  VAL U CB  1 
ATOM   11307 C  CG1 . VAL K  1 31  ? -7.667  -32.971 11.823  1.00 66.61  ? 31  VAL U CG1 1 
ATOM   11308 C  CG2 . VAL K  1 31  ? -5.321  -33.013 12.739  1.00 65.63  ? 31  VAL U CG2 1 
ATOM   11309 N  N   . TRP K  1 32  ? -9.487  -34.948 14.136  1.00 71.22  ? 32  TRP U N   1 
ATOM   11310 C  CA  . TRP K  1 32  ? -10.708 -35.738 13.910  1.00 73.80  ? 32  TRP U CA  1 
ATOM   11311 C  C   . TRP K  1 32  ? -11.978 -34.872 13.971  1.00 73.27  ? 32  TRP U C   1 
ATOM   11312 O  O   . TRP K  1 32  ? -11.986 -33.795 14.585  1.00 71.21  ? 32  TRP U O   1 
ATOM   11313 C  CB  . TRP K  1 32  ? -10.782 -36.919 14.899  1.00 76.44  ? 32  TRP U CB  1 
ATOM   11314 C  CG  . TRP K  1 32  ? -11.409 -36.577 16.205  1.00 76.59  ? 32  TRP U CG  1 
ATOM   11315 C  CD1 . TRP K  1 32  ? -12.665 -36.911 16.622  1.00 78.82  ? 32  TRP U CD1 1 
ATOM   11316 C  CD2 . TRP K  1 32  ? -10.827 -35.805 17.255  1.00 74.73  ? 32  TRP U CD2 1 
ATOM   11317 N  NE1 . TRP K  1 32  ? -12.897 -36.404 17.875  1.00 78.48  ? 32  TRP U NE1 1 
ATOM   11318 C  CE2 . TRP K  1 32  ? -11.786 -35.717 18.288  1.00 75.96  ? 32  TRP U CE2 1 
ATOM   11319 C  CE3 . TRP K  1 32  ? -9.582  -35.181 17.429  1.00 72.44  ? 32  TRP U CE3 1 
ATOM   11320 C  CZ2 . TRP K  1 32  ? -11.540 -35.028 19.485  1.00 74.93  ? 32  TRP U CZ2 1 
ATOM   11321 C  CZ3 . TRP K  1 32  ? -9.337  -34.490 18.620  1.00 71.41  ? 32  TRP U CZ3 1 
ATOM   11322 C  CH2 . TRP K  1 32  ? -10.315 -34.421 19.631  1.00 72.64  ? 32  TRP U CH2 1 
ATOM   11323 N  N   . GLY K  1 33  ? -13.040 -35.352 13.324  1.00 75.35  ? 33  GLY U N   1 
ATOM   11324 C  CA  . GLY K  1 33  ? -14.312 -34.629 13.255  1.00 75.39  ? 33  GLY U CA  1 
ATOM   11325 C  C   . GLY K  1 33  ? -15.249 -35.161 12.186  1.00 77.75  ? 33  GLY U C   1 
ATOM   11326 O  O   . GLY K  1 33  ? -15.147 -36.322 11.783  1.00 80.14  ? 33  GLY U O   1 
ATOM   11327 N  N   . SER K  1 34  ? -16.161 -34.302 11.733  1.00 77.29  ? 34  SER U N   1 
ATOM   11328 C  CA  . SER K  1 34  ? -17.169 -34.660 10.730  1.00 79.71  ? 34  SER U CA  1 
ATOM   11329 C  C   . SER K  1 34  ? -17.498 -33.444 9.865   1.00 77.94  ? 34  SER U C   1 
ATOM   11330 O  O   . SER K  1 34  ? -17.637 -32.336 10.389  1.00 75.85  ? 34  SER U O   1 
ATOM   11331 C  CB  . SER K  1 34  ? -18.437 -35.171 11.424  1.00 82.75  ? 34  SER U CB  1 
ATOM   11332 O  OG  . SER K  1 34  ? -19.429 -35.555 10.489  1.00 85.51  ? 34  SER U OG  1 
ATOM   11333 N  N   . ILE K  1 35  ? -17.603 -33.656 8.551   0.75 78.97  ? 35  ILE U N   1 
ATOM   11334 C  CA  . ILE K  1 35  ? -18.025 -32.617 7.599   0.75 78.00  ? 35  ILE U CA  1 
ATOM   11335 C  C   . ILE K  1 35  ? -19.227 -33.162 6.825   0.75 81.47  ? 35  ILE U C   1 
ATOM   11336 O  O   . ILE K  1 35  ? -19.132 -34.218 6.199   0.75 83.87  ? 35  ILE U O   1 
ATOM   11337 C  CB  . ILE K  1 35  ? -16.896 -32.220 6.613   0.75 76.06  ? 35  ILE U CB  1 
ATOM   11338 C  CG1 . ILE K  1 35  ? -15.606 -31.877 7.371   0.75 73.23  ? 35  ILE U CG1 1 
ATOM   11339 C  CG2 . ILE K  1 35  ? -17.317 -31.024 5.760   0.75 75.01  ? 35  ILE U CG2 1 
ATOM   11340 C  CD1 . ILE K  1 35  ? -14.425 -31.545 6.482   0.75 71.71  ? 35  ILE U CD1 1 
ATOM   11341 N  N   . LYS K  1 36  ? -20.341 -32.428 6.867   1.00 81.95  ? 36  LYS U N   1 
ATOM   11342 C  CA  . LYS K  1 36  ? -21.600 -32.831 6.226   1.00 85.50  ? 36  LYS U CA  1 
ATOM   11343 C  C   . LYS K  1 36  ? -21.965 -31.854 5.111   1.00 84.95  ? 36  LYS U C   1 
ATOM   11344 O  O   . LYS K  1 36  ? -21.674 -30.662 5.213   1.00 82.04  ? 36  LYS U O   1 
ATOM   11345 C  CB  . LYS K  1 36  ? -22.740 -32.916 7.254   1.00 87.44  ? 36  LYS U CB  1 
ATOM   11346 C  CG  . LYS K  1 36  ? -23.071 -31.616 7.992   1.00 85.19  ? 36  LYS U CG  1 
ATOM   11347 C  CD  . LYS K  1 36  ? -24.260 -31.769 8.934   1.00 87.77  ? 36  LYS U CD  1 
ATOM   11348 C  CE  . LYS K  1 36  ? -25.591 -31.922 8.203   1.00 91.41  ? 36  LYS U CE  1 
ATOM   11349 N  NZ  . LYS K  1 36  ? -25.916 -30.772 7.314   1.00 90.24  ? 36  LYS U NZ  1 
ATOM   11350 N  N   . GLY K  1 37  ? -22.603 -32.369 4.060   0.75 88.01  ? 37  GLY U N   1 
ATOM   11351 C  CA  . GLY K  1 37  ? -23.012 -31.566 2.903   0.75 88.20  ? 37  GLY U CA  1 
ATOM   11352 C  C   . GLY K  1 37  ? -22.085 -31.612 1.696   0.75 87.59  ? 37  GLY U C   1 
ATOM   11353 O  O   . GLY K  1 37  ? -22.298 -30.871 0.735   0.75 87.59  ? 37  GLY U O   1 
ATOM   11354 N  N   . LEU K  1 38  ? -21.063 -32.469 1.733   0.75 87.31  ? 38  LEU U N   1 
ATOM   11355 C  CA  . LEU K  1 38  ? -20.153 -32.651 0.596   0.75 87.28  ? 38  LEU U CA  1 
ATOM   11356 C  C   . LEU K  1 38  ? -20.754 -33.605 -0.433  0.75 91.56  ? 38  LEU U C   1 
ATOM   11357 O  O   . LEU K  1 38  ? -21.683 -34.357 -0.134  0.75 94.54  ? 38  LEU U O   1 
ATOM   11358 C  CB  . LEU K  1 38  ? -18.799 -33.206 1.059   0.75 85.61  ? 38  LEU U CB  1 
ATOM   11359 C  CG  . LEU K  1 38  ? -17.910 -32.296 1.912   0.75 81.50  ? 38  LEU U CG  1 
ATOM   11360 C  CD1 . LEU K  1 38  ? -16.795 -33.098 2.564   0.75 80.79  ? 38  LEU U CD1 1 
ATOM   11361 C  CD2 . LEU K  1 38  ? -17.328 -31.162 1.082   0.75 79.43  ? 38  LEU U CD2 1 
ATOM   11362 N  N   . THR K  1 39  ? -20.215 -33.556 -1.648  0.75 92.10  ? 39  THR U N   1 
ATOM   11363 C  CA  . THR K  1 39  ? -20.515 -34.551 -2.676  0.75 96.23  ? 39  THR U CA  1 
ATOM   11364 C  C   . THR K  1 39  ? -19.631 -35.778 -2.448  0.75 97.11  ? 39  THR U C   1 
ATOM   11365 O  O   . THR K  1 39  ? -18.633 -35.701 -1.722  0.75 94.25  ? 39  THR U O   1 
ATOM   11366 C  CB  . THR K  1 39  ? -20.286 -33.988 -4.092  0.75 96.78  ? 39  THR U CB  1 
ATOM   11367 O  OG1 . THR K  1 39  ? -18.943 -33.507 -4.211  0.75 93.75  ? 39  THR U OG1 1 
ATOM   11368 C  CG2 . THR K  1 39  ? -21.252 -32.846 -4.374  0.75 96.54  ? 39  THR U CG2 1 
ATOM   11369 N  N   . GLU K  1 40  ? -20.001 -36.899 -3.066  0.75 101.29 ? 40  GLU U N   1 
ATOM   11370 C  CA  . GLU K  1 40  ? -19.286 -38.170 -2.888  0.75 102.88 ? 40  GLU U CA  1 
ATOM   11371 C  C   . GLU K  1 40  ? -17.898 -38.133 -3.530  0.75 101.53 ? 40  GLU U C   1 
ATOM   11372 O  O   . GLU K  1 40  ? -17.746 -37.648 -4.652  0.75 101.96 ? 40  GLU U O   1 
ATOM   11373 C  CB  . GLU K  1 40  ? -20.093 -39.329 -3.479  0.75 108.15 ? 40  GLU U CB  1 
ATOM   11374 N  N   . GLY K  1 41  ? -16.900 -38.649 -2.811  1.00 100.19 ? 41  GLY U N   1 
ATOM   11375 C  CA  . GLY K  1 41  ? -15.507 -38.673 -3.270  1.00 99.06  ? 41  GLY U CA  1 
ATOM   11376 C  C   . GLY K  1 41  ? -14.578 -37.827 -2.413  1.00 94.56  ? 41  GLY U C   1 
ATOM   11377 O  O   . GLY K  1 41  ? -14.930 -37.431 -1.299  1.00 92.43  ? 41  GLY U O   1 
ATOM   11378 N  N   . LEU K  1 42  ? -13.388 -37.557 -2.948  1.00 93.46  ? 42  LEU U N   1 
ATOM   11379 C  CA  . LEU K  1 42  ? -12.343 -36.810 -2.241  1.00 89.66  ? 42  LEU U CA  1 
ATOM   11380 C  C   . LEU K  1 42  ? -12.579 -35.301 -2.322  1.00 86.80  ? 42  LEU U C   1 
ATOM   11381 O  O   . LEU K  1 42  ? -13.145 -34.799 -3.297  1.00 87.82  ? 42  LEU U O   1 
ATOM   11382 C  CB  . LEU K  1 42  ? -10.960 -37.134 -2.818  1.00 90.09  ? 42  LEU U CB  1 
ATOM   11383 C  CG  . LEU K  1 42  ? -10.471 -38.584 -2.715  1.00 92.85  ? 42  LEU U CG  1 
ATOM   11384 C  CD1 . LEU K  1 42  ? -9.373  -38.865 -3.732  1.00 94.41  ? 42  LEU U CD1 1 
ATOM   11385 C  CD2 . LEU K  1 42  ? -9.987  -38.897 -1.306  1.00 91.07  ? 42  LEU U CD2 1 
ATOM   11386 N  N   . HIS K  1 43  ? -12.133 -34.596 -1.283  1.00 83.46  ? 43  HIS U N   1 
ATOM   11387 C  CA  . HIS K  1 43  ? -12.218 -33.137 -1.196  1.00 80.59  ? 43  HIS U CA  1 
ATOM   11388 C  C   . HIS K  1 43  ? -10.961 -32.600 -0.507  1.00 77.67  ? 43  HIS U C   1 
ATOM   11389 O  O   . HIS K  1 43  ? -10.586 -33.089 0.563   1.00 76.93  ? 43  HIS U O   1 
ATOM   11390 C  CB  . HIS K  1 43  ? -13.459 -32.729 -0.399  1.00 79.90  ? 43  HIS U CB  1 
ATOM   11391 C  CG  . HIS K  1 43  ? -14.751 -33.030 -1.093  1.00 82.79  ? 43  HIS U CG  1 
ATOM   11392 N  ND1 . HIS K  1 43  ? -15.364 -32.137 -1.944  1.00 82.99  ? 43  HIS U ND1 1 
ATOM   11393 C  CD2 . HIS K  1 43  ? -15.544 -34.128 -1.065  1.00 85.89  ? 43  HIS U CD2 1 
ATOM   11394 C  CE1 . HIS K  1 43  ? -16.483 -32.668 -2.402  1.00 86.06  ? 43  HIS U CE1 1 
ATOM   11395 N  NE2 . HIS K  1 43  ? -16.614 -33.877 -1.887  1.00 87.91  ? 43  HIS U NE2 1 
ATOM   11396 N  N   . GLY K  1 44  ? -10.318 -31.600 -1.114  1.00 76.32  ? 44  GLY U N   1 
ATOM   11397 C  CA  . GLY K  1 44  ? -9.073  -31.028 -0.581  1.00 73.92  ? 44  GLY U CA  1 
ATOM   11398 C  C   . GLY K  1 44  ? -9.251  -30.441 0.806   1.00 71.23  ? 44  GLY U C   1 
ATOM   11399 O  O   . GLY K  1 44  ? -10.289 -29.854 1.104   1.00 70.51  ? 44  GLY U O   1 
ATOM   11400 N  N   . PHE K  1 45  ? -8.230  -30.599 1.646   1.00 70.00  ? 45  PHE U N   1 
ATOM   11401 C  CA  . PHE K  1 45  ? -8.324  -30.286 3.072   1.00 67.98  ? 45  PHE U CA  1 
ATOM   11402 C  C   . PHE K  1 45  ? -7.029  -29.607 3.529   1.00 66.04  ? 45  PHE U C   1 
ATOM   11403 O  O   . PHE K  1 45  ? -5.985  -30.260 3.623   1.00 66.70  ? 45  PHE U O   1 
ATOM   11404 C  CB  . PHE K  1 45  ? -8.580  -31.585 3.838   1.00 69.42  ? 45  PHE U CB  1 
ATOM   11405 C  CG  . PHE K  1 45  ? -9.021  -31.389 5.259   1.00 68.04  ? 45  PHE U CG  1 
ATOM   11406 C  CD1 . PHE K  1 45  ? -10.186 -30.692 5.551   1.00 67.36  ? 45  PHE U CD1 1 
ATOM   11407 C  CD2 . PHE K  1 45  ? -8.298  -31.952 6.305   1.00 67.81  ? 45  PHE U CD2 1 
ATOM   11408 C  CE1 . PHE K  1 45  ? -10.603 -30.527 6.861   1.00 66.46  ? 45  PHE U CE1 1 
ATOM   11409 C  CE2 . PHE K  1 45  ? -8.711  -31.793 7.618   1.00 66.89  ? 45  PHE U CE2 1 
ATOM   11410 C  CZ  . PHE K  1 45  ? -9.867  -31.081 7.896   1.00 66.24  ? 45  PHE U CZ  1 
ATOM   11411 N  N   . HIS K  1 46  ? -7.097  -28.298 3.793   1.00 63.95  ? 46  HIS U N   1 
ATOM   11412 C  CA  . HIS K  1 46  ? -5.894  -27.461 3.952   1.00 62.48  ? 46  HIS U CA  1 
ATOM   11413 C  C   . HIS K  1 46  ? -5.979  -26.466 5.110   1.00 60.18  ? 46  HIS U C   1 
ATOM   11414 O  O   . HIS K  1 46  ? -7.053  -25.949 5.422   1.00 59.51  ? 46  HIS U O   1 
ATOM   11415 C  CB  . HIS K  1 46  ? -5.617  -26.683 2.658   1.00 62.87  ? 46  HIS U CB  1 
ATOM   11416 C  CG  . HIS K  1 46  ? -5.532  -27.548 1.441   1.00 65.38  ? 46  HIS U CG  1 
ATOM   11417 N  ND1 . HIS K  1 46  ? -6.328  -27.354 0.333   1.00 66.61  ? 46  HIS U ND1 1 
ATOM   11418 C  CD2 . HIS K  1 46  ? -4.768  -28.631 1.172   1.00 67.17  ? 46  HIS U CD2 1 
ATOM   11419 C  CE1 . HIS K  1 46  ? -6.044  -28.272 -0.574  1.00 69.03  ? 46  HIS U CE1 1 
ATOM   11420 N  NE2 . HIS K  1 46  ? -5.102  -29.061 -0.089  1.00 69.40  ? 46  HIS U NE2 1 
ATOM   11421 N  N   . VAL K  1 47  ? -4.832  -26.212 5.739   1.00 59.23  ? 47  VAL U N   1 
ATOM   11422 C  CA  . VAL K  1 47  ? -4.674  -25.088 6.644   1.00 57.30  ? 47  VAL U CA  1 
ATOM   11423 C  C   . VAL K  1 47  ? -4.114  -23.925 5.824   1.00 56.79  ? 47  VAL U C   1 
ATOM   11424 O  O   . VAL K  1 47  ? -2.981  -23.999 5.342   1.00 57.48  ? 47  VAL U O   1 
ATOM   11425 C  CB  . VAL K  1 47  ? -3.736  -25.408 7.826   1.00 56.94  ? 47  VAL U CB  1 
ATOM   11426 C  CG1 . VAL K  1 47  ? -3.616  -24.204 8.757   1.00 55.26  ? 47  VAL U CG1 1 
ATOM   11427 C  CG2 . VAL K  1 47  ? -4.235  -26.638 8.579   1.00 57.81  ? 47  VAL U CG2 1 
ATOM   11428 N  N   . HIS K  1 48  ? -4.924  -22.878 5.648   1.00 55.84  ? 48  HIS U N   1 
ATOM   11429 C  CA  . HIS K  1 48  ? -4.528  -21.678 4.902   1.00 55.51  ? 48  HIS U CA  1 
ATOM   11430 C  C   . HIS K  1 48  ? -3.952  -20.639 5.859   1.00 54.03  ? 48  HIS U C   1 
ATOM   11431 O  O   . HIS K  1 48  ? -4.291  -20.621 7.040   1.00 53.08  ? 48  HIS U O   1 
ATOM   11432 C  CB  . HIS K  1 48  ? -5.713  -21.096 4.112   1.00 55.71  ? 48  HIS U CB  1 
ATOM   11433 C  CG  . HIS K  1 48  ? -6.136  -21.936 2.941   1.00 57.51  ? 48  HIS U CG  1 
ATOM   11434 N  ND1 . HIS K  1 48  ? -6.259  -21.428 1.665   1.00 58.51  ? 48  HIS U ND1 1 
ATOM   11435 C  CD2 . HIS K  1 48  ? -6.458  -23.250 2.854   1.00 58.73  ? 48  HIS U CD2 1 
ATOM   11436 C  CE1 . HIS K  1 48  ? -6.646  -22.389 0.845   1.00 60.30  ? 48  HIS U CE1 1 
ATOM   11437 N  NE2 . HIS K  1 48  ? -6.777  -23.504 1.541   1.00 60.46  ? 48  HIS U NE2 1 
ATOM   11438 N  N   . GLU K  1 49  ? -3.105  -19.765 5.323   1.00 54.12  ? 49  GLU U N   1 
ATOM   11439 C  CA  . GLU K  1 49  ? -2.210  -18.931 6.130   1.00 53.39  ? 49  GLU U CA  1 
ATOM   11440 C  C   . GLU K  1 49  ? -2.910  -17.988 7.128   1.00 51.98  ? 49  GLU U C   1 
ATOM   11441 O  O   . GLU K  1 49  ? -2.453  -17.857 8.271   1.00 51.34  ? 49  GLU U O   1 
ATOM   11442 C  CB  . GLU K  1 49  ? -1.280  -18.122 5.216   1.00 54.29  ? 49  GLU U CB  1 
ATOM   11443 C  CG  . GLU K  1 49  ? -0.074  -17.522 5.924   1.00 54.29  ? 49  GLU U CG  1 
ATOM   11444 C  CD  . GLU K  1 49  ? 0.737   -16.586 5.042   1.00 55.47  ? 49  GLU U CD  1 
ATOM   11445 O  OE1 . GLU K  1 49  ? 0.610   -16.636 3.799   1.00 56.59  ? 49  GLU U OE1 1 
ATOM   11446 O  OE2 . GLU K  1 49  ? 1.514   -15.791 5.604   1.00 55.56  ? 49  GLU U OE2 1 
ATOM   11447 N  N   . PHE K  1 50  ? -4.000  -17.342 6.700   1.00 51.66  ? 50  PHE U N   1 
ATOM   11448 C  CA  . PHE K  1 50  ? -4.664  -16.317 7.516   1.00 50.67  ? 50  PHE U CA  1 
ATOM   11449 C  C   . PHE K  1 50  ? -6.003  -16.780 8.070   1.00 50.30  ? 50  PHE U C   1 
ATOM   11450 O  O   . PHE K  1 50  ? -6.781  -17.419 7.359   1.00 50.89  ? 50  PHE U O   1 
ATOM   11451 C  CB  . PHE K  1 50  ? -4.859  -15.033 6.706   1.00 50.89  ? 50  PHE U CB  1 
ATOM   11452 C  CG  . PHE K  1 50  ? -3.574  -14.432 6.221   1.00 51.56  ? 50  PHE U CG  1 
ATOM   11453 C  CD1 . PHE K  1 50  ? -2.596  -14.025 7.132   1.00 51.34  ? 50  PHE U CD1 1 
ATOM   11454 C  CD2 . PHE K  1 50  ? -3.325  -14.282 4.859   1.00 52.75  ? 50  PHE U CD2 1 
ATOM   11455 C  CE1 . PHE K  1 50  ? -1.398  -13.480 6.691   1.00 52.32  ? 50  PHE U CE1 1 
ATOM   11456 C  CE2 . PHE K  1 50  ? -2.129  -13.733 4.415   1.00 53.74  ? 50  PHE U CE2 1 
ATOM   11457 C  CZ  . PHE K  1 50  ? -1.166  -13.333 5.333   1.00 53.54  ? 50  PHE U CZ  1 
ATOM   11458 N  N   . GLY K  1 51  ? -6.256  -16.442 9.340   1.00 49.58  ? 51  GLY U N   1 
ATOM   11459 C  CA  . GLY K  1 51  ? -7.566  -16.600 9.981   1.00 49.46  ? 51  GLY U CA  1 
ATOM   11460 C  C   . GLY K  1 51  ? -8.439  -15.383 9.731   1.00 49.35  ? 51  GLY U C   1 
ATOM   11461 O  O   . GLY K  1 51  ? -8.909  -14.739 10.673  1.00 49.04  ? 51  GLY U O   1 
ATOM   11462 N  N   . ASP K  1 52  ? -8.657  -15.081 8.453   1.00 49.83  ? 52  ASP U N   1 
ATOM   11463 C  CA  . ASP K  1 52  ? -9.373  -13.888 8.017   1.00 49.99  ? 52  ASP U CA  1 
ATOM   11464 C  C   . ASP K  1 52  ? -10.618 -14.343 7.254   1.00 50.88  ? 52  ASP U C   1 
ATOM   11465 O  O   . ASP K  1 52  ? -10.507 -14.780 6.109   1.00 51.64  ? 52  ASP U O   1 
ATOM   11466 C  CB  . ASP K  1 52  ? -8.453  -13.030 7.131   1.00 50.18  ? 52  ASP U CB  1 
ATOM   11467 C  CG  . ASP K  1 52  ? -9.050  -11.661 6.782   1.00 50.45  ? 52  ASP U CG  1 
ATOM   11468 O  OD1 . ASP K  1 52  ? -10.292 -11.515 6.753   1.00 50.72  ? 52  ASP U OD1 1 
ATOM   11469 O  OD2 . ASP K  1 52  ? -8.261  -10.726 6.522   1.00 50.60  ? 52  ASP U OD2 1 
ATOM   11470 N  N   A ASN K  1 53  ? -11.780 -14.220 7.900   0.50 51.05  ? 53  ASN U N   1 
ATOM   11471 N  N   B ASN K  1 53  ? -11.783 -14.249 7.898   0.50 51.07  ? 53  ASN U N   1 
ATOM   11472 C  CA  A ASN K  1 53  ? -13.069 -14.646 7.348   0.50 52.22  ? 53  ASN U CA  1 
ATOM   11473 C  CA  B ASN K  1 53  ? -13.063 -14.644 7.297   0.50 52.26  ? 53  ASN U CA  1 
ATOM   11474 C  C   A ASN K  1 53  ? -13.963 -13.460 6.935   0.50 52.80  ? 53  ASN U C   1 
ATOM   11475 C  C   B ASN K  1 53  ? -13.963 -13.456 6.935   0.50 52.82  ? 53  ASN U C   1 
ATOM   11476 O  O   A ASN K  1 53  ? -15.187 -13.603 6.880   0.50 53.87  ? 53  ASN U O   1 
ATOM   11477 O  O   B ASN K  1 53  ? -15.189 -13.593 6.911   0.50 53.87  ? 53  ASN U O   1 
ATOM   11478 C  CB  A ASN K  1 53  ? -13.802 -15.497 8.391   0.50 52.53  ? 53  ASN U CB  1 
ATOM   11479 C  CB  B ASN K  1 53  ? -13.815 -15.583 8.240   0.50 52.68  ? 53  ASN U CB  1 
ATOM   11480 C  CG  A ASN K  1 53  ? -14.674 -16.576 7.771   0.50 53.98  ? 53  ASN U CG  1 
ATOM   11481 C  CG  B ASN K  1 53  ? -13.317 -17.013 8.159   0.50 52.97  ? 53  ASN U CG  1 
ATOM   11482 O  OD1 A ASN K  1 53  ? -14.188 -17.444 7.044   0.50 54.38  ? 53  ASN U OD1 1 
ATOM   11483 O  OD1 B ASN K  1 53  ? -12.209 -17.276 7.683   0.50 52.57  ? 53  ASN U OD1 1 
ATOM   11484 N  ND2 A ASN K  1 53  ? -15.966 -16.538 8.075   0.50 55.05  ? 53  ASN U ND2 1 
ATOM   11485 N  ND2 B ASN K  1 53  ? -14.139 -17.949 8.620   0.50 53.96  ? 53  ASN U ND2 1 
ATOM   11486 N  N   . THR K  1 54  ? -13.357 -12.306 6.639   1.00 52.41  ? 54  THR U N   1 
ATOM   11487 C  CA  . THR K  1 54  ? -14.105 -11.097 6.260   1.00 53.08  ? 54  THR U CA  1 
ATOM   11488 C  C   . THR K  1 54  ? -14.703 -11.190 4.855   1.00 54.47  ? 54  THR U C   1 
ATOM   11489 O  O   . THR K  1 54  ? -15.726 -10.569 4.586   1.00 55.48  ? 54  THR U O   1 
ATOM   11490 C  CB  . THR K  1 54  ? -13.221 -9.836  6.312   1.00 52.57  ? 54  THR U CB  1 
ATOM   11491 O  OG1 . THR K  1 54  ? -12.071 -10.026 5.479   1.00 52.51  ? 54  THR U OG1 1 
ATOM   11492 C  CG2 . THR K  1 54  ? -12.784 -9.535  7.749   1.00 51.59  ? 54  THR U CG2 1 
ATOM   11493 N  N   . ALA K  1 55  ? -14.043 -11.934 3.965   1.00 54.77  ? 55  ALA U N   1 
ATOM   11494 C  CA  . ALA K  1 55  ? -14.584 -12.262 2.636   1.00 56.39  ? 55  ALA U CA  1 
ATOM   11495 C  C   . ALA K  1 55  ? -14.740 -13.784 2.469   1.00 57.00  ? 55  ALA U C   1 
ATOM   11496 O  O   . ALA K  1 55  ? -14.457 -14.339 1.400   1.00 58.02  ? 55  ALA U O   1 
ATOM   11497 C  CB  . ALA K  1 55  ? -13.685 -11.686 1.549   1.00 56.83  ? 55  ALA U CB  1 
ATOM   11498 N  N   . GLY K  1 56  ? -15.206 -14.447 3.530   1.00 56.62  ? 56  GLY U N   1 
ATOM   11499 C  CA  . GLY K  1 56  ? -15.320 -15.911 3.560   1.00 57.29  ? 56  GLY U CA  1 
ATOM   11500 C  C   . GLY K  1 56  ? -13.963 -16.591 3.483   1.00 56.55  ? 56  GLY U C   1 
ATOM   11501 O  O   . GLY K  1 56  ? -12.982 -16.090 4.031   1.00 55.12  ? 56  GLY U O   1 
ATOM   11502 N  N   . ALA K  1 57  ? -13.914 -17.723 2.782   1.00 57.79  ? 57  ALA U N   1 
ATOM   11503 C  CA  . ALA K  1 57  ? -12.656 -18.427 2.499   1.00 57.65  ? 57  ALA U CA  1 
ATOM   11504 C  C   . ALA K  1 57  ? -11.682 -17.654 1.583   1.00 57.58  ? 57  ALA U C   1 
ATOM   11505 O  O   . ALA K  1 57  ? -10.479 -17.908 1.621   1.00 57.13  ? 57  ALA U O   1 
ATOM   11506 C  CB  . ALA K  1 57  ? -12.945 -19.802 1.910   1.00 59.43  ? 57  ALA U CB  1 
ATOM   11507 N  N   . THR K  1 58  ? -12.194 -16.720 0.777   1.00 58.30  ? 58  THR U N   1 
ATOM   11508 C  CA  . THR K  1 58  ? -11.367 -15.910 -0.140  1.00 58.66  ? 58  THR U CA  1 
ATOM   11509 C  C   . THR K  1 58  ? -10.287 -15.063 0.560   1.00 57.09  ? 58  THR U C   1 
ATOM   11510 O  O   . THR K  1 58  ? -9.234  -14.802 -0.025  1.00 57.49  ? 58  THR U O   1 
ATOM   11511 C  CB  . THR K  1 58  ? -12.250 -14.977 -1.003  1.00 59.90  ? 58  THR U CB  1 
ATOM   11512 O  OG1 . THR K  1 58  ? -13.386 -15.702 -1.483  1.00 61.43  ? 58  THR U OG1 1 
ATOM   11513 C  CG2 . THR K  1 58  ? -11.478 -14.409 -2.197  1.00 61.09  ? 58  THR U CG2 1 
ATOM   11514 N  N   . SER K  1 59  ? -10.549 -14.639 1.799   1.00 55.60  ? 59  SER U N   1 
ATOM   11515 C  CA  . SER K  1 59  ? -9.596  -13.823 2.565   1.00 54.32  ? 59  SER U CA  1 
ATOM   11516 C  C   . SER K  1 59  ? -8.615  -14.634 3.432   1.00 53.44  ? 59  SER U C   1 
ATOM   11517 O  O   . SER K  1 59  ? -7.695  -14.058 4.021   1.00 52.69  ? 59  SER U O   1 
ATOM   11518 C  CB  . SER K  1 59  ? -10.350 -12.787 3.413   1.00 53.55  ? 59  SER U CB  1 
ATOM   11519 O  OG  . SER K  1 59  ? -11.443 -13.362 4.105   1.00 53.40  ? 59  SER U OG  1 
ATOM   11520 N  N   . ALA K  1 60  ? -8.782  -15.958 3.481   1.00 53.77  ? 60  ALA U N   1 
ATOM   11521 C  CA  . ALA K  1 60  ? -7.869  -16.852 4.231   1.00 53.28  ? 60  ALA U CA  1 
ATOM   11522 C  C   . ALA K  1 60  ? -6.423  -16.935 3.700   1.00 53.74  ? 60  ALA U C   1 
ATOM   11523 O  O   . ALA K  1 60  ? -5.541  -17.428 4.410   1.00 53.32  ? 60  ALA U O   1 
ATOM   11524 C  CB  . ALA K  1 60  ? -8.459  -18.260 4.315   1.00 53.93  ? 60  ALA U CB  1 
ATOM   11525 N  N   . GLY K  1 61  ? -6.188  -16.486 2.463   1.00 54.87  ? 61  GLY U N   1 
ATOM   11526 C  CA  . GLY K  1 61  ? -4.853  -16.500 1.864   1.00 55.80  ? 61  GLY U CA  1 
ATOM   11527 C  C   . GLY K  1 61  ? -4.508  -17.867 1.288   1.00 57.06  ? 61  GLY U C   1 
ATOM   11528 O  O   . GLY K  1 61  ? -5.374  -18.740 1.206   1.00 57.40  ? 61  GLY U O   1 
ATOM   11529 N  N   . PRO K  1 62  ? -3.238  -18.070 0.888   1.00 58.08  ? 62  PRO U N   1 
ATOM   11530 C  CA  . PRO K  1 62  ? -2.803  -19.356 0.326   1.00 59.58  ? 62  PRO U CA  1 
ATOM   11531 C  C   . PRO K  1 62  ? -2.583  -20.410 1.417   1.00 58.86  ? 62  PRO U C   1 
ATOM   11532 O  O   . PRO K  1 62  ? -2.851  -20.144 2.593   1.00 57.22  ? 62  PRO U O   1 
ATOM   11533 C  CB  . PRO K  1 62  ? -1.488  -18.992 -0.371  1.00 61.03  ? 62  PRO U CB  1 
ATOM   11534 C  CG  . PRO K  1 62  ? -0.936  -17.876 0.457   1.00 59.81  ? 62  PRO U CG  1 
ATOM   11535 C  CD  . PRO K  1 62  ? -2.111  -17.126 1.027   1.00 58.11  ? 62  PRO U CD  1 
ATOM   11536 N  N   . HIS K  1 63  ? -2.104  -21.592 1.029   1.00 60.32  ? 63  HIS U N   1 
ATOM   11537 C  CA  . HIS K  1 63  ? -1.807  -22.668 1.987   1.00 60.06  ? 63  HIS U CA  1 
ATOM   11538 C  C   . HIS K  1 63  ? -0.720  -22.211 2.961   1.00 59.18  ? 63  HIS U C   1 
ATOM   11539 O  O   . HIS K  1 63  ? 0.220   -21.517 2.559   1.00 59.75  ? 63  HIS U O   1 
ATOM   11540 C  CB  . HIS K  1 63  ? -1.353  -23.953 1.272   1.00 62.20  ? 63  HIS U CB  1 
ATOM   11541 C  CG  . HIS K  1 63  ? -2.418  -24.604 0.442   1.00 63.43  ? 63  HIS U CG  1 
ATOM   11542 N  ND1 . HIS K  1 63  ? -2.135  -25.533 -0.535  1.00 65.82  ? 63  HIS U ND1 1 
ATOM   11543 C  CD2 . HIS K  1 63  ? -3.763  -24.449 0.433   1.00 62.91  ? 63  HIS U CD2 1 
ATOM   11544 C  CE1 . HIS K  1 63  ? -3.261  -25.931 -1.102  1.00 66.70  ? 63  HIS U CE1 1 
ATOM   11545 N  NE2 . HIS K  1 63  ? -4.263  -25.285 -0.536  1.00 64.97  ? 63  HIS U NE2 1 
ATOM   11546 N  N   . PHE K  1 64  ? -0.860  -22.585 4.235   1.00 58.07  ? 64  PHE U N   1 
ATOM   11547 C  CA  . PHE K  1 64  ? 0.119   -22.218 5.264   1.00 57.45  ? 64  PHE U CA  1 
ATOM   11548 C  C   . PHE K  1 64  ? 1.469   -22.877 4.933   1.00 59.21  ? 64  PHE U C   1 
ATOM   11549 O  O   . PHE K  1 64  ? 1.589   -24.112 4.903   1.00 60.23  ? 64  PHE U O   1 
ATOM   11550 C  CB  . PHE K  1 64  ? -0.387  -22.597 6.667   1.00 56.25  ? 64  PHE U CB  1 
ATOM   11551 C  CG  . PHE K  1 64  ? 0.579   -22.276 7.793   1.00 55.82  ? 64  PHE U CG  1 
ATOM   11552 C  CD1 . PHE K  1 64  ? 1.248   -21.046 7.854   1.00 55.51  ? 64  PHE U CD1 1 
ATOM   11553 C  CD2 . PHE K  1 64  ? 0.798   -23.200 8.817   1.00 55.99  ? 64  PHE U CD2 1 
ATOM   11554 C  CE1 . PHE K  1 64  ? 2.127   -20.762 8.894   1.00 55.43  ? 64  PHE U CE1 1 
ATOM   11555 C  CE2 . PHE K  1 64  ? 1.677   -22.919 9.859   1.00 55.86  ? 64  PHE U CE2 1 
ATOM   11556 C  CZ  . PHE K  1 64  ? 2.340   -21.697 9.900   1.00 55.59  ? 64  PHE U CZ  1 
ATOM   11557 N  N   . ASN K  1 65  ? 2.461   -22.027 4.662   1.00 59.80  ? 65  ASN U N   1 
ATOM   11558 C  CA  . ASN K  1 65  ? 3.740   -22.436 4.082   1.00 61.94  ? 65  ASN U CA  1 
ATOM   11559 C  C   . ASN K  1 65  ? 4.883   -21.576 4.663   1.00 62.15  ? 65  ASN U C   1 
ATOM   11560 O  O   . ASN K  1 65  ? 5.438   -20.716 3.968   1.00 63.13  ? 65  ASN U O   1 
ATOM   11561 C  CB  . ASN K  1 65  ? 3.657   -22.315 2.546   1.00 63.50  ? 65  ASN U CB  1 
ATOM   11562 C  CG  . ASN K  1 65  ? 4.890   -22.859 1.832   1.00 66.11  ? 65  ASN U CG  1 
ATOM   11563 O  OD1 . ASN K  1 65  ? 5.581   -23.754 2.329   1.00 66.94  ? 65  ASN U OD1 1 
ATOM   11564 N  ND2 . ASN K  1 65  ? 5.156   -22.330 0.641   1.00 67.68  ? 65  ASN U ND2 1 
ATOM   11565 N  N   . PRO K  1 66  ? 5.227   -21.794 5.951   1.00 61.51  ? 66  PRO U N   1 
ATOM   11566 C  CA  . PRO K  1 66  ? 6.301   -21.014 6.585   1.00 61.95  ? 66  PRO U CA  1 
ATOM   11567 C  C   . PRO K  1 66  ? 7.706   -21.364 6.075   1.00 64.52  ? 66  PRO U C   1 
ATOM   11568 O  O   . PRO K  1 66  ? 8.550   -20.474 5.966   1.00 65.54  ? 66  PRO U O   1 
ATOM   11569 C  CB  . PRO K  1 66  ? 6.151   -21.351 8.076   1.00 60.78  ? 66  PRO U CB  1 
ATOM   11570 C  CG  . PRO K  1 66  ? 5.512   -22.693 8.099   1.00 60.71  ? 66  PRO U CG  1 
ATOM   11571 C  CD  . PRO K  1 66  ? 4.599   -22.732 6.903   1.00 60.56  ? 66  PRO U CD  1 
ATOM   11572 N  N   . LEU K  1 67  ? 7.944   -22.638 5.760   1.00 65.81  ? 67  LEU U N   1 
ATOM   11573 C  CA  . LEU K  1 67  ? 9.234   -23.088 5.214   1.00 68.59  ? 67  LEU U CA  1 
ATOM   11574 C  C   . LEU K  1 67  ? 9.410   -22.839 3.702   1.00 70.36  ? 67  LEU U C   1 
ATOM   11575 O  O   . LEU K  1 67  ? 10.467  -23.160 3.153   1.00 72.99  ? 67  LEU U O   1 
ATOM   11576 C  CB  . LEU K  1 67  ? 9.455   -24.576 5.529   1.00 69.58  ? 67  LEU U CB  1 
ATOM   11577 C  CG  . LEU K  1 67  ? 9.423   -24.980 7.011   1.00 68.47  ? 67  LEU U CG  1 
ATOM   11578 C  CD1 . LEU K  1 67  ? 9.542   -26.492 7.148   1.00 69.73  ? 67  LEU U CD1 1 
ATOM   11579 C  CD2 . LEU K  1 67  ? 10.517  -24.284 7.809   1.00 69.15  ? 67  LEU U CD2 1 
ATOM   11580 N  N   . SER K  1 68  ? 8.384   -22.293 3.038   1.00 69.21  ? 68  SER U N   1 
ATOM   11581 C  CA  . SER K  1 68  ? 8.472   -21.833 1.640   1.00 70.90  ? 68  SER U CA  1 
ATOM   11582 C  C   . SER K  1 68  ? 8.746   -22.974 0.646   1.00 73.34  ? 68  SER U C   1 
ATOM   11583 O  O   . SER K  1 68  ? 9.617   -22.868 -0.226  1.00 76.01  ? 68  SER U O   1 
ATOM   11584 C  CB  . SER K  1 68  ? 9.512   -20.708 1.501   1.00 72.33  ? 68  SER U CB  1 
ATOM   11585 O  OG  . SER K  1 68  ? 9.314   -19.718 2.496   1.00 70.35  ? 68  SER U OG  1 
ATOM   11586 N  N   . ARG K  1 69  ? 7.984   -24.056 0.798   1.00 72.65  ? 69  ARG U N   1 
ATOM   11587 C  CA  . ARG K  1 69  ? 8.071   -25.240 -0.062  1.00 74.94  ? 69  ARG U CA  1 
ATOM   11588 C  C   . ARG K  1 69  ? 7.026   -25.185 -1.182  1.00 75.11  ? 69  ARG U C   1 
ATOM   11589 O  O   . ARG K  1 69  ? 6.244   -24.235 -1.270  1.00 73.44  ? 69  ARG U O   1 
ATOM   11590 C  CB  . ARG K  1 69  ? 7.837   -26.505 0.775   1.00 74.47  ? 69  ARG U CB  1 
ATOM   11591 C  CG  . ARG K  1 69  ? 8.696   -26.640 2.027   1.00 74.17  ? 69  ARG U CG  1 
ATOM   11592 C  CD  . ARG K  1 69  ? 10.170  -26.833 1.702   1.00 77.16  ? 69  ARG U CD  1 
ATOM   11593 N  NE  . ARG K  1 69  ? 10.973  -26.962 2.921   1.00 77.08  ? 69  ARG U NE  1 
ATOM   11594 C  CZ  . ARG K  1 69  ? 11.085  -28.066 3.670   1.00 77.40  ? 69  ARG U CZ  1 
ATOM   11595 N  NH1 . ARG K  1 69  ? 10.448  -29.199 3.353   1.00 77.86  ? 69  ARG U NH1 1 
ATOM   11596 N  NH2 . ARG K  1 69  ? 11.851  -28.037 4.760   1.00 77.50  ? 69  ARG U NH2 1 
ATOM   11597 N  N   . LYS K  1 70  ? 7.034   -26.207 -2.038  1.00 77.40  ? 70  LYS U N   1 
ATOM   11598 C  CA  . LYS K  1 70  ? 5.970   -26.439 -3.019  1.00 77.88  ? 70  LYS U CA  1 
ATOM   11599 C  C   . LYS K  1 70  ? 4.910   -27.393 -2.453  1.00 76.57  ? 70  LYS U C   1 
ATOM   11600 O  O   . LYS K  1 70  ? 5.163   -28.109 -1.480  1.00 76.02  ? 70  LYS U O   1 
ATOM   11601 C  CB  . LYS K  1 70  ? 6.556   -26.997 -4.319  1.00 81.58  ? 70  LYS U CB  1 
ATOM   11602 C  CG  . LYS K  1 70  ? 7.575   -26.071 -4.967  1.00 83.41  ? 70  LYS U CG  1 
ATOM   11603 C  CD  . LYS K  1 70  ? 7.860   -26.458 -6.408  1.00 87.13  ? 70  LYS U CD  1 
ATOM   11604 C  CE  . LYS K  1 70  ? 8.814   -25.471 -7.062  1.00 89.20  ? 70  LYS U CE  1 
ATOM   11605 N  NZ  . LYS K  1 70  ? 8.877   -25.655 -8.537  1.00 92.79  ? 70  LYS U NZ  1 
ATOM   11606 N  N   . HIS K  1 71  ? 3.727   -27.385 -3.068  1.00 76.34  ? 71  HIS U N   1 
ATOM   11607 C  CA  . HIS K  1 71  ? 2.579   -28.185 -2.613  1.00 75.37  ? 71  HIS U CA  1 
ATOM   11608 C  C   . HIS K  1 71  ? 2.817   -29.690 -2.792  1.00 77.74  ? 71  HIS U C   1 
ATOM   11609 O  O   . HIS K  1 71  ? 3.489   -30.116 -3.734  1.00 80.55  ? 71  HIS U O   1 
ATOM   11610 C  CB  . HIS K  1 71  ? 1.304   -27.761 -3.372  1.00 75.15  ? 71  HIS U CB  1 
ATOM   11611 C  CG  . HIS K  1 71  ? 0.083   -28.560 -3.027  1.00 74.69  ? 71  HIS U CG  1 
ATOM   11612 N  ND1 . HIS K  1 71  ? -0.728  -28.266 -1.952  1.00 72.10  ? 71  HIS U ND1 1 
ATOM   11613 C  CD2 . HIS K  1 71  ? -0.468  -29.642 -3.627  1.00 76.84  ? 71  HIS U CD2 1 
ATOM   11614 C  CE1 . HIS K  1 71  ? -1.722  -29.134 -1.902  1.00 72.71  ? 71  HIS U CE1 1 
ATOM   11615 N  NE2 . HIS K  1 71  ? -1.584  -29.983 -2.904  1.00 75.57  ? 71  HIS U NE2 1 
ATOM   11616 N  N   . GLY K  1 72  ? 2.259   -30.476 -1.874  1.00 76.80  ? 72  GLY U N   1 
ATOM   11617 C  CA  . GLY K  1 72  ? 2.220   -31.929 -2.001  1.00 79.10  ? 72  GLY U CA  1 
ATOM   11618 C  C   . GLY K  1 72  ? 1.106   -32.536 -1.169  1.00 77.97  ? 72  GLY U C   1 
ATOM   11619 O  O   . GLY K  1 72  ? 0.184   -31.832 -0.748  1.00 75.73  ? 72  GLY U O   1 
ATOM   11620 N  N   . GLY K  1 73  ? 1.190   -33.852 -0.966  1.00 79.88  ? 73  GLY U N   1 
ATOM   11621 C  CA  . GLY K  1 73  ? 0.359   -34.571 0.004   1.00 79.26  ? 73  GLY U CA  1 
ATOM   11622 C  C   . GLY K  1 73  ? 1.088   -34.651 1.340   1.00 77.97  ? 73  GLY U C   1 
ATOM   11623 O  O   . GLY K  1 73  ? 2.314   -34.501 1.379   1.00 78.40  ? 73  GLY U O   1 
ATOM   11624 N  N   . PRO K  1 74  ? 0.351   -34.912 2.444   1.00 76.73  ? 74  PRO U N   1 
ATOM   11625 C  CA  . PRO K  1 74  ? 0.931   -34.857 3.802   1.00 75.36  ? 74  PRO U CA  1 
ATOM   11626 C  C   . PRO K  1 74  ? 2.044   -35.887 4.081   1.00 77.49  ? 74  PRO U C   1 
ATOM   11627 O  O   . PRO K  1 74  ? 2.881   -35.654 4.957   1.00 76.71  ? 74  PRO U O   1 
ATOM   11628 C  CB  . PRO K  1 74  ? -0.277  -35.109 4.712   1.00 74.39  ? 74  PRO U CB  1 
ATOM   11629 C  CG  . PRO K  1 74  ? -1.206  -35.917 3.874   1.00 76.50  ? 74  PRO U CG  1 
ATOM   11630 C  CD  . PRO K  1 74  ? -1.033  -35.423 2.465   1.00 77.17  ? 74  PRO U CD  1 
ATOM   11631 N  N   . LYS K  1 75  ? 2.046   -36.998 3.343   1.00 80.34  ? 75  LYS U N   1 
ATOM   11632 C  CA  . LYS K  1 75  ? 3.098   -38.014 3.447   1.00 82.84  ? 75  LYS U CA  1 
ATOM   11633 C  C   . LYS K  1 75  ? 4.422   -37.567 2.815   1.00 83.70  ? 75  LYS U C   1 
ATOM   11634 O  O   . LYS K  1 75  ? 5.474   -38.106 3.157   1.00 85.22  ? 75  LYS U O   1 
ATOM   11635 C  CB  . LYS K  1 75  ? 2.644   -39.330 2.802   1.00 85.97  ? 75  LYS U CB  1 
ATOM   11636 C  CG  . LYS K  1 75  ? 1.376   -39.941 3.390   1.00 85.94  ? 75  LYS U CG  1 
ATOM   11637 C  CD  . LYS K  1 75  ? 1.558   -40.388 4.832   1.00 85.45  ? 75  LYS U CD  1 
ATOM   11638 C  CE  . LYS K  1 75  ? 0.283   -41.000 5.391   1.00 85.85  ? 75  LYS U CE  1 
ATOM   11639 N  NZ  . LYS K  1 75  ? -0.057  -42.308 4.763   1.00 89.45  ? 75  LYS U NZ  1 
ATOM   11640 N  N   . ASP K  1 76  ? 4.369   -36.590 1.907   1.00 82.98  ? 76  ASP U N   1 
ATOM   11641 C  CA  . ASP K  1 76  ? 5.568   -36.078 1.232   1.00 84.08  ? 76  ASP U CA  1 
ATOM   11642 C  C   . ASP K  1 76  ? 6.423   -35.202 2.155   1.00 82.27  ? 76  ASP U C   1 
ATOM   11643 O  O   . ASP K  1 76  ? 5.891   -34.491 3.018   1.00 79.43  ? 76  ASP U O   1 
ATOM   11644 C  CB  . ASP K  1 76  ? 5.191   -35.257 -0.011  1.00 84.05  ? 76  ASP U CB  1 
ATOM   11645 C  CG  . ASP K  1 76  ? 4.340   -36.035 -1.007  1.00 86.17  ? 76  ASP U CG  1 
ATOM   11646 O  OD1 . ASP K  1 76  ? 4.489   -37.272 -1.103  1.00 88.77  ? 76  ASP U OD1 1 
ATOM   11647 O  OD2 . ASP K  1 76  ? 3.522   -35.400 -1.703  1.00 85.47  ? 76  ASP U OD2 1 
ATOM   11648 N  N   . GLU K  1 77  ? 7.744   -35.263 1.961   1.00 84.18  ? 77  GLU U N   1 
ATOM   11649 C  CA  . GLU K  1 77  ? 8.691   -34.334 2.596   1.00 83.10  ? 77  GLU U CA  1 
ATOM   11650 C  C   . GLU K  1 77  ? 8.517   -32.932 2.001   1.00 81.54  ? 77  GLU U C   1 
ATOM   11651 O  O   . GLU K  1 77  ? 8.482   -31.939 2.733   1.00 79.14  ? 77  GLU U O   1 
ATOM   11652 C  CB  . GLU K  1 77  ? 10.140  -34.812 2.399   1.00 86.19  ? 77  GLU U CB  1 
ATOM   11653 C  CG  . GLU K  1 77  ? 11.197  -33.996 3.145   1.00 85.66  ? 77  GLU U CG  1 
ATOM   11654 C  CD  . GLU K  1 77  ? 12.627  -34.345 2.738   1.00 89.16  ? 77  GLU U CD  1 
ATOM   11655 O  OE1 . GLU K  1 77  ? 12.930  -35.544 2.515   1.00 91.83  ? 77  GLU U OE1 1 
ATOM   11656 O  OE2 . GLU K  1 77  ? 13.461  -33.413 2.648   1.00 89.49  ? 77  GLU U OE2 1 
ATOM   11657 N  N   . GLU K  1 78  ? 8.428   -32.872 0.672   1.00 83.18  ? 78  GLU U N   1 
ATOM   11658 C  CA  . GLU K  1 78  ? 8.145   -31.632 -0.048  1.00 82.14  ? 78  GLU U CA  1 
ATOM   11659 C  C   . GLU K  1 78  ? 6.642   -31.332 0.015   1.00 79.70  ? 78  GLU U C   1 
ATOM   11660 O  O   . GLU K  1 78  ? 5.846   -31.910 -0.734  1.00 80.70  ? 78  GLU U O   1 
ATOM   11661 C  CB  . GLU K  1 78  ? 8.631   -31.736 -1.503  1.00 85.29  ? 78  GLU U CB  1 
ATOM   11662 C  CG  . GLU K  1 78  ? 8.510   -30.458 -2.332  1.00 84.88  ? 78  GLU U CG  1 
ATOM   11663 C  CD  . GLU K  1 78  ? 9.315   -29.284 -1.787  1.00 83.80  ? 78  GLU U CD  1 
ATOM   11664 O  OE1 . GLU K  1 78  ? 10.296  -29.494 -1.039  1.00 84.39  ? 78  GLU U OE1 1 
ATOM   11665 O  OE2 . GLU K  1 78  ? 8.968   -28.133 -2.122  1.00 82.58  ? 78  GLU U OE2 1 
ATOM   11666 N  N   . ARG K  1 79  ? 6.274   -30.434 0.928   1.00 76.76  ? 79  ARG U N   1 
ATOM   11667 C  CA  . ARG K  1 79  ? 4.883   -30.033 1.141   1.00 74.40  ? 79  ARG U CA  1 
ATOM   11668 C  C   . ARG K  1 79  ? 4.818   -28.696 1.863   1.00 71.77  ? 79  ARG U C   1 
ATOM   11669 O  O   . ARG K  1 79  ? 5.793   -28.269 2.485   1.00 71.60  ? 79  ARG U O   1 
ATOM   11670 C  CB  . ARG K  1 79  ? 4.147   -31.081 1.986   1.00 73.94  ? 79  ARG U CB  1 
ATOM   11671 C  CG  . ARG K  1 79  ? 4.803   -31.373 3.334   1.00 73.34  ? 79  ARG U CG  1 
ATOM   11672 C  CD  . ARG K  1 79  ? 3.939   -32.252 4.226   1.00 72.81  ? 79  ARG U CD  1 
ATOM   11673 N  NE  . ARG K  1 79  ? 2.926   -31.487 4.955   1.00 70.14  ? 79  ARG U NE  1 
ATOM   11674 C  CZ  . ARG K  1 79  ? 2.154   -31.970 5.933   1.00 69.40  ? 79  ARG U CZ  1 
ATOM   11675 N  NH1 . ARG K  1 79  ? 2.250   -33.242 6.330   1.00 71.07  ? 79  ARG U NH1 1 
ATOM   11676 N  NH2 . ARG K  1 79  ? 1.267   -31.171 6.524   1.00 67.21  ? 79  ARG U NH2 1 
ATOM   11677 N  N   . HIS K  1 80  ? 3.656   -28.057 1.802   1.00 69.95  ? 80  HIS U N   1 
ATOM   11678 C  CA  . HIS K  1 80  ? 3.353   -26.931 2.686   1.00 67.36  ? 80  HIS U CA  1 
ATOM   11679 C  C   . HIS K  1 80  ? 2.960   -27.504 4.048   1.00 66.09  ? 80  HIS U C   1 
ATOM   11680 O  O   . HIS K  1 80  ? 2.435   -28.616 4.123   1.00 66.86  ? 80  HIS U O   1 
ATOM   11681 C  CB  . HIS K  1 80  ? 2.221   -26.079 2.117   1.00 66.19  ? 80  HIS U CB  1 
ATOM   11682 C  CG  . HIS K  1 80  ? 2.480   -25.586 0.731   1.00 67.74  ? 80  HIS U CG  1 
ATOM   11683 N  ND1 . HIS K  1 80  ? 1.477   -25.381 -0.190  1.00 68.01  ? 80  HIS U ND1 1 
ATOM   11684 C  CD2 . HIS K  1 80  ? 3.639   -25.289 0.097   1.00 69.47  ? 80  HIS U CD2 1 
ATOM   11685 C  CE1 . HIS K  1 80  ? 2.006   -24.952 -1.323  1.00 69.77  ? 80  HIS U CE1 1 
ATOM   11686 N  NE2 . HIS K  1 80  ? 3.316   -24.890 -1.176  1.00 70.70  ? 80  HIS U NE2 1 
ATOM   11687 N  N   . VAL K  1 81  ? 3.221   -26.758 5.120   1.00 64.46  ? 81  VAL U N   1 
ATOM   11688 C  CA  . VAL K  1 81  ? 2.812   -27.177 6.471   1.00 63.37  ? 81  VAL U CA  1 
ATOM   11689 C  C   . VAL K  1 81  ? 1.309   -27.499 6.511   1.00 62.59  ? 81  VAL U C   1 
ATOM   11690 O  O   . VAL K  1 81  ? 0.904   -28.542 7.043   1.00 63.14  ? 81  VAL U O   1 
ATOM   11691 C  CB  . VAL K  1 81  ? 3.198   -26.111 7.535   1.00 61.83  ? 81  VAL U CB  1 
ATOM   11692 C  CG1 . VAL K  1 81  ? 2.452   -26.311 8.854   1.00 60.56  ? 81  VAL U CG1 1 
ATOM   11693 C  CG2 . VAL K  1 81  ? 4.702   -26.147 7.776   1.00 63.12  ? 81  VAL U CG2 1 
ATOM   11694 N  N   . GLY K  1 82  ? 0.505   -26.623 5.909   1.00 61.64  ? 82  GLY U N   1 
ATOM   11695 C  CA  . GLY K  1 82  ? -0.942  -26.785 5.876   1.00 61.11  ? 82  GLY U CA  1 
ATOM   11696 C  C   . GLY K  1 82  ? -1.530  -27.908 5.032   1.00 62.93  ? 82  GLY U C   1 
ATOM   11697 O  O   . GLY K  1 82  ? -2.734  -28.151 5.119   1.00 62.83  ? 82  GLY U O   1 
ATOM   11698 N  N   . ASP K  1 83  ? -0.716  -28.587 4.217   1.00 64.86  ? 83  ASP U N   1 
ATOM   11699 C  CA  . ASP K  1 83  ? -1.197  -29.705 3.388   1.00 66.98  ? 83  ASP U CA  1 
ATOM   11700 C  C   . ASP K  1 83  ? -1.587  -30.910 4.246   1.00 67.64  ? 83  ASP U C   1 
ATOM   11701 O  O   . ASP K  1 83  ? -0.717  -31.625 4.742   1.00 68.48  ? 83  ASP U O   1 
ATOM   11702 C  CB  . ASP K  1 83  ? -0.134  -30.129 2.358   1.00 69.19  ? 83  ASP U CB  1 
ATOM   11703 C  CG  . ASP K  1 83  ? 0.104   -29.076 1.284   1.00 69.24  ? 83  ASP U CG  1 
ATOM   11704 O  OD1 . ASP K  1 83  ? -0.852  -28.371 0.892   1.00 68.34  ? 83  ASP U OD1 1 
ATOM   11705 O  OD2 . ASP K  1 83  ? 1.257   -28.956 0.817   1.00 70.37  ? 83  ASP U OD2 1 
ATOM   11706 N  N   . LEU K  1 84  ? -2.896  -31.113 4.422   1.00 67.46  ? 84  LEU U N   1 
ATOM   11707 C  CA  . LEU K  1 84  ? -3.439  -32.252 5.176   1.00 68.49  ? 84  LEU U CA  1 
ATOM   11708 C  C   . LEU K  1 84  ? -4.168  -33.262 4.276   1.00 71.02  ? 84  LEU U C   1 
ATOM   11709 O  O   . LEU K  1 84  ? -4.888  -34.131 4.778   1.00 72.16  ? 84  LEU U O   1 
ATOM   11710 C  CB  . LEU K  1 84  ? -4.368  -31.755 6.295   1.00 66.76  ? 84  LEU U CB  1 
ATOM   11711 C  CG  . LEU K  1 84  ? -3.741  -30.800 7.316   1.00 64.53  ? 84  LEU U CG  1 
ATOM   11712 C  CD1 . LEU K  1 84  ? -4.793  -30.268 8.276   1.00 63.19  ? 84  LEU U CD1 1 
ATOM   11713 C  CD2 . LEU K  1 84  ? -2.613  -31.478 8.081   1.00 65.14  ? 84  LEU U CD2 1 
ATOM   11714 N  N   . GLY K  1 85  ? -3.981  -33.146 2.957   1.00 72.18  ? 85  GLY U N   1 
ATOM   11715 C  CA  . GLY K  1 85  ? -4.417  -34.171 2.000   1.00 75.11  ? 85  GLY U CA  1 
ATOM   11716 C  C   . GLY K  1 85  ? -5.881  -34.106 1.597   1.00 75.69  ? 85  GLY U C   1 
ATOM   11717 O  O   . GLY K  1 85  ? -6.339  -33.084 1.066   1.00 74.62  ? 85  GLY U O   1 
ATOM   11718 N  N   . ASN K  1 86  ? -6.606  -35.202 1.848   1.00 77.65  ? 86  ASN U N   1 
ATOM   11719 C  CA  . ASN K  1 86  ? -8.011  -35.351 1.446   1.00 78.99  ? 86  ASN U CA  1 
ATOM   11720 C  C   . ASN K  1 86  ? -8.898  -35.904 2.567   1.00 79.30  ? 86  ASN U C   1 
ATOM   11721 O  O   . ASN K  1 86  ? -8.449  -36.697 3.401   1.00 79.80  ? 86  ASN U O   1 
ATOM   11722 C  CB  . ASN K  1 86  ? -8.114  -36.275 0.230   1.00 82.45  ? 86  ASN U CB  1 
ATOM   11723 C  CG  . ASN K  1 86  ? -7.609  -35.624 -1.038  1.00 82.65  ? 86  ASN U CG  1 
ATOM   11724 O  OD1 . ASN K  1 86  ? -8.150  -34.614 -1.484  1.00 81.54  ? 86  ASN U OD1 1 
ATOM   11725 N  ND2 . ASN K  1 86  ? -6.573  -36.202 -1.631  1.00 84.34  ? 86  ASN U ND2 1 
ATOM   11726 N  N   . VAL K  1 87  ? -10.162 -35.478 2.547   1.00 79.31  ? 87  VAL U N   1 
ATOM   11727 C  CA  . VAL K  1 87  ? -11.207 -35.965 3.456   1.00 80.21  ? 87  VAL U CA  1 
ATOM   11728 C  C   . VAL K  1 87  ? -12.292 -36.620 2.596   1.00 83.50  ? 87  VAL U C   1 
ATOM   11729 O  O   . VAL K  1 87  ? -12.930 -35.963 1.769   1.00 83.61  ? 87  VAL U O   1 
ATOM   11730 C  CB  . VAL K  1 87  ? -11.785 -34.854 4.390   1.00 77.56  ? 87  VAL U CB  1 
ATOM   11731 C  CG1 . VAL K  1 87  ? -10.712 -34.366 5.358   1.00 74.86  ? 87  VAL U CG1 1 
ATOM   11732 C  CG2 . VAL K  1 87  ? -12.393 -33.676 3.625   1.00 76.48  ? 87  VAL U CG2 1 
ATOM   11733 N  N   . THR K  1 88  ? -12.471 -37.927 2.776   1.00 86.42  ? 88  THR U N   1 
ATOM   11734 C  CA  . THR K  1 88  ? -13.342 -38.723 1.915   1.00 90.15  ? 88  THR U CA  1 
ATOM   11735 C  C   . THR K  1 88  ? -14.781 -38.707 2.427   1.00 91.30  ? 88  THR U C   1 
ATOM   11736 O  O   . THR K  1 88  ? -15.073 -39.266 3.487   1.00 91.99  ? 88  THR U O   1 
ATOM   11737 C  CB  . THR K  1 88  ? -12.836 -40.178 1.830   1.00 93.25  ? 88  THR U CB  1 
ATOM   11738 O  OG1 . THR K  1 88  ? -11.438 -40.170 1.518   1.00 92.16  ? 88  THR U OG1 1 
ATOM   11739 C  CG2 . THR K  1 88  ? -13.599 -40.978 0.764   1.00 97.42  ? 88  THR U CG2 1 
ATOM   11740 N  N   . ALA K  1 89  ? -15.667 -38.056 1.675   1.00 91.74  ? 89  ALA U N   1 
ATOM   11741 C  CA  . ALA K  1 89  ? -17.102 -38.078 1.963   1.00 93.57  ? 89  ALA U CA  1 
ATOM   11742 C  C   . ALA K  1 89  ? -17.693 -39.384 1.444   1.00 98.32  ? 89  ALA U C   1 
ATOM   11743 O  O   . ALA K  1 89  ? -17.451 -39.753 0.295   1.00 100.22 ? 89  ALA U O   1 
ATOM   11744 C  CB  . ALA K  1 89  ? -17.796 -36.890 1.318   1.00 92.52  ? 89  ALA U CB  1 
ATOM   11745 N  N   . ASP K  1 90  ? -18.456 -40.079 2.291   1.00 100.51 ? 90  ASP U N   1 
ATOM   11746 C  CA  . ASP K  1 90  ? -19.134 -41.335 1.904   1.00 105.50 ? 90  ASP U CA  1 
ATOM   11747 C  C   . ASP K  1 90  ? -20.376 -41.065 1.031   1.00 108.08 ? 90  ASP U C   1 
ATOM   11748 O  O   . ASP K  1 90  ? -20.676 -39.905 0.718   1.00 105.90 ? 90  ASP U O   1 
ATOM   11749 C  CB  . ASP K  1 90  ? -19.462 -42.206 3.144   1.00 107.29 ? 90  ASP U CB  1 
ATOM   11750 C  CG  . ASP K  1 90  ? -20.402 -41.524 4.145   1.00 106.32 ? 90  ASP U CG  1 
ATOM   11751 O  OD1 . ASP K  1 90  ? -21.452 -40.977 3.745   1.00 107.28 ? 90  ASP U OD1 1 
ATOM   11752 O  OD2 . ASP K  1 90  ? -20.086 -41.551 5.355   1.00 104.84 ? 90  ASP U OD2 1 
ATOM   11753 N  N   . LYS K  1 91  ? -21.079 -42.133 0.641   1.00 112.94 ? 91  LYS U N   1 
ATOM   11754 C  CA  . LYS K  1 91  ? -22.275 -42.052 -0.220  1.00 116.28 ? 91  LYS U CA  1 
ATOM   11755 C  C   . LYS K  1 91  ? -23.317 -40.998 0.191   1.00 115.14 ? 91  LYS U C   1 
ATOM   11756 O  O   . LYS K  1 91  ? -23.899 -40.339 -0.677  1.00 115.70 ? 91  LYS U O   1 
ATOM   11757 C  CB  . LYS K  1 91  ? -22.955 -43.424 -0.308  1.00 121.91 ? 91  LYS U CB  1 
ATOM   11758 N  N   . ASP K  1 92  ? -23.528 -40.829 1.500   1.00 113.72 ? 92  ASP U N   1 
ATOM   11759 C  CA  . ASP K  1 92  ? -24.519 -39.875 2.037   1.00 112.89 ? 92  ASP U CA  1 
ATOM   11760 C  C   . ASP K  1 92  ? -24.017 -38.424 2.174   1.00 107.73 ? 92  ASP U C   1 
ATOM   11761 O  O   . ASP K  1 92  ? -24.713 -37.585 2.751   1.00 106.65 ? 92  ASP U O   1 
ATOM   11762 C  CB  . ASP K  1 92  ? -25.042 -40.368 3.400   1.00 114.28 ? 92  ASP U CB  1 
ATOM   11763 C  CG  . ASP K  1 92  ? -25.728 -41.729 3.320   1.00 119.96 ? 92  ASP U CG  1 
ATOM   11764 O  OD1 . ASP K  1 92  ? -26.490 -41.974 2.360   1.00 123.51 ? 92  ASP U OD1 1 
ATOM   11765 O  OD2 . ASP K  1 92  ? -25.515 -42.554 4.232   1.00 121.16 ? 92  ASP U OD2 1 
ATOM   11766 N  N   . GLY K  1 93  ? -22.827 -38.124 1.652   1.00 104.87 ? 93  GLY U N   1 
ATOM   11767 C  CA  . GLY K  1 93  ? -22.273 -36.776 1.705   1.00 100.34 ? 93  GLY U CA  1 
ATOM   11768 C  C   . GLY K  1 93  ? -21.788 -36.373 3.085   1.00 97.09  ? 93  GLY U C   1 
ATOM   11769 O  O   . GLY K  1 93  ? -21.952 -35.220 3.490   1.00 94.48  ? 93  GLY U O   1 
ATOM   11770 N  N   . VAL K  1 94  ? -21.190 -37.329 3.799   1.00 97.58  ? 94  VAL U N   1 
ATOM   11771 C  CA  . VAL K  1 94  ? -20.648 -37.114 5.143   1.00 94.95  ? 94  VAL U CA  1 
ATOM   11772 C  C   . VAL K  1 94  ? -19.206 -37.625 5.158   1.00 93.48  ? 94  VAL U C   1 
ATOM   11773 O  O   . VAL K  1 94  ? -18.965 -38.795 4.851   1.00 96.18  ? 94  VAL U O   1 
ATOM   11774 C  CB  . VAL K  1 94  ? -21.467 -37.866 6.226   1.00 97.72  ? 94  VAL U CB  1 
ATOM   11775 C  CG1 . VAL K  1 94  ? -20.943 -37.541 7.625   1.00 95.11  ? 94  VAL U CG1 1 
ATOM   11776 C  CG2 . VAL K  1 94  ? -22.953 -37.533 6.123   1.00 100.13 ? 94  VAL U CG2 1 
ATOM   11777 N  N   . ALA K  1 95  ? -18.259 -36.751 5.508   1.00 89.50  ? 95  ALA U N   1 
ATOM   11778 C  CA  . ALA K  1 95  ? -16.835 -37.102 5.572   1.00 87.97  ? 95  ALA U CA  1 
ATOM   11779 C  C   . ALA K  1 95  ? -16.357 -37.181 7.020   1.00 86.46  ? 95  ALA U C   1 
ATOM   11780 O  O   . ALA K  1 95  ? -16.257 -36.155 7.697   1.00 83.64  ? 95  ALA U O   1 
ATOM   11781 C  CB  . ALA K  1 95  ? -16.007 -36.084 4.797   1.00 85.04  ? 95  ALA U CB  1 
ATOM   11782 N  N   . ASP K  1 96  ? -16.077 -38.398 7.487   1.00 88.62  ? 96  ASP U N   1 
ATOM   11783 C  CA  . ASP K  1 96  ? -15.506 -38.619 8.816   1.00 87.66  ? 96  ASP U CA  1 
ATOM   11784 C  C   . ASP K  1 96  ? -13.997 -38.405 8.742   1.00 85.12  ? 96  ASP U C   1 
ATOM   11785 O  O   . ASP K  1 96  ? -13.292 -39.161 8.067   1.00 86.39  ? 96  ASP U O   1 
ATOM   11786 C  CB  . ASP K  1 96  ? -15.810 -40.034 9.327   1.00 91.41  ? 96  ASP U CB  1 
ATOM   11787 C  CG  . ASP K  1 96  ? -17.294 -40.266 9.571   1.00 94.29  ? 96  ASP U CG  1 
ATOM   11788 O  OD1 . ASP K  1 96  ? -17.911 -39.490 10.329  1.00 93.13  ? 96  ASP U OD1 1 
ATOM   11789 O  OD2 . ASP K  1 96  ? -17.842 -41.237 9.011   1.00 98.02  ? 96  ASP U OD2 1 
ATOM   11790 N  N   . VAL K  1 97  ? -13.517 -37.366 9.426   1.00 81.81  ? 97  VAL U N   1 
ATOM   11791 C  CA  . VAL K  1 97  ? -12.089 -37.049 9.503   1.00 79.45  ? 97  VAL U CA  1 
ATOM   11792 C  C   . VAL K  1 97  ? -11.493 -37.801 10.705  1.00 80.11  ? 97  VAL U C   1 
ATOM   11793 O  O   . VAL K  1 97  ? -12.111 -37.858 11.773  1.00 80.62  ? 97  VAL U O   1 
ATOM   11794 C  CB  . VAL K  1 97  ? -11.855 -35.516 9.630   1.00 75.89  ? 97  VAL U CB  1 
ATOM   11795 C  CG1 . VAL K  1 97  ? -10.367 -35.180 9.604   1.00 73.87  ? 97  VAL U CG1 1 
ATOM   11796 C  CG2 . VAL K  1 97  ? -12.586 -34.767 8.517   1.00 75.56  ? 97  VAL U CG2 1 
ATOM   11797 N  N   . SER K  1 98  ? -10.314 -38.399 10.511  1.00 80.41  ? 98  SER U N   1 
ATOM   11798 C  CA  . SER K  1 98  ? -9.582  -39.090 11.586  1.00 81.08  ? 98  SER U CA  1 
ATOM   11799 C  C   . SER K  1 98  ? -8.104  -39.258 11.211  1.00 80.44  ? 98  SER U C   1 
ATOM   11800 O  O   . SER K  1 98  ? -7.600  -40.375 11.069  1.00 82.78  ? 98  SER U O   1 
ATOM   11801 C  CB  . SER K  1 98  ? -10.222 -40.447 11.907  1.00 84.83  ? 98  SER U CB  1 
ATOM   11802 O  OG  . SER K  1 98  ? -9.649  -41.001 13.078  1.00 85.51  ? 98  SER U OG  1 
ATOM   11803 N  N   . ILE K  1 99  ? -7.432  -38.120 11.064  1.00 77.48  ? 99  ILE U N   1 
ATOM   11804 C  CA  . ILE K  1 99  ? -6.041  -38.032 10.606  1.00 76.75  ? 99  ILE U CA  1 
ATOM   11805 C  C   . ILE K  1 99  ? -5.097  -37.941 11.813  1.00 75.81  ? 99  ILE U C   1 
ATOM   11806 O  O   . ILE K  1 99  ? -5.502  -37.524 12.902  1.00 74.87  ? 99  ILE U O   1 
ATOM   11807 C  CB  . ILE K  1 99  ? -5.841  -36.764 9.709   1.00 74.38  ? 99  ILE U CB  1 
ATOM   11808 C  CG1 . ILE K  1 99  ? -6.738  -36.804 8.459   1.00 75.46  ? 99  ILE U CG1 1 
ATOM   11809 C  CG2 . ILE K  1 99  ? -4.382  -36.588 9.281   1.00 73.83  ? 99  ILE U CG2 1 
ATOM   11810 C  CD1 . ILE K  1 99  ? -6.969  -35.440 7.827   1.00 73.17  ? 99  ILE U CD1 1 
ATOM   11811 N  N   . GLU K  1 100 ? -3.846  -38.354 11.613  1.00 76.37  ? 100 GLU U N   1 
ATOM   11812 C  CA  . GLU K  1 100 ? -2.728  -37.947 12.473  1.00 75.10  ? 100 GLU U CA  1 
ATOM   11813 C  C   . GLU K  1 100 ? -1.693  -37.224 11.599  1.00 73.79  ? 100 GLU U C   1 
ATOM   11814 O  O   . GLU K  1 100 ? -1.507  -37.584 10.430  1.00 74.95  ? 100 GLU U O   1 
ATOM   11815 C  CB  . GLU K  1 100 ? -2.099  -39.157 13.166  1.00 77.51  ? 100 GLU U CB  1 
ATOM   11816 C  CG  . GLU K  1 100 ? -1.290  -38.785 14.401  1.00 76.61  ? 100 GLU U CG  1 
ATOM   11817 C  CD  . GLU K  1 100 ? -0.477  -39.943 14.949  1.00 79.15  ? 100 GLU U CD  1 
ATOM   11818 O  OE1 . GLU K  1 100 ? 0.551   -40.292 14.329  1.00 80.10  ? 100 GLU U OE1 1 
ATOM   11819 O  OE2 . GLU K  1 100 ? -0.858  -40.494 16.004  1.00 80.41  ? 100 GLU U OE2 1 
ATOM   11820 N  N   . ASP K  1 101 ? -1.032  -36.209 12.157  1.00 71.65  ? 101 ASP U N   1 
ATOM   11821 C  CA  . ASP K  1 101 ? -0.027  -35.437 11.413  1.00 70.61  ? 101 ASP U CA  1 
ATOM   11822 C  C   . ASP K  1 101 ? 1.046   -34.870 12.345  1.00 69.66  ? 101 ASP U C   1 
ATOM   11823 O  O   . ASP K  1 101 ? 0.727   -34.376 13.423  1.00 68.48  ? 101 ASP U O   1 
ATOM   11824 C  CB  . ASP K  1 101 ? -0.702  -34.306 10.634  1.00 68.71  ? 101 ASP U CB  1 
ATOM   11825 C  CG  . ASP K  1 101 ? 0.134   -33.823 9.460   1.00 68.68  ? 101 ASP U CG  1 
ATOM   11826 O  OD1 . ASP K  1 101 ? -0.022  -34.381 8.348   1.00 70.20  ? 101 ASP U OD1 1 
ATOM   11827 O  OD2 . ASP K  1 101 ? 0.942   -32.886 9.646   1.00 67.37  ? 101 ASP U OD2 1 
ATOM   11828 N  N   . SER K  1 102 ? 2.308   -34.943 11.917  1.00 70.47  ? 102 SER U N   1 
ATOM   11829 C  CA  . SER K  1 102 ? 3.461   -34.523 12.730  1.00 70.22  ? 102 SER U CA  1 
ATOM   11830 C  C   . SER K  1 102 ? 4.178   -33.266 12.200  1.00 68.87  ? 102 SER U C   1 
ATOM   11831 O  O   . SER K  1 102 ? 5.227   -32.891 12.735  1.00 69.03  ? 102 SER U O   1 
ATOM   11832 C  CB  . SER K  1 102 ? 4.464   -35.674 12.832  1.00 72.85  ? 102 SER U CB  1 
ATOM   11833 O  OG  . SER K  1 102 ? 3.825   -36.871 13.243  1.00 74.46  ? 102 SER U OG  1 
ATOM   11834 N  N   . VAL K  1 103 ? 3.619   -32.628 11.165  1.00 67.81  ? 103 VAL U N   1 
ATOM   11835 C  CA  . VAL K  1 103 ? 4.185   -31.406 10.571  1.00 66.73  ? 103 VAL U CA  1 
ATOM   11836 C  C   . VAL K  1 103 ? 3.458   -30.177 11.118  1.00 64.27  ? 103 VAL U C   1 
ATOM   11837 O  O   . VAL K  1 103 ? 4.098   -29.206 11.542  1.00 63.44  ? 103 VAL U O   1 
ATOM   11838 C  CB  . VAL K  1 103 ? 4.101   -31.436 9.028   1.00 67.50  ? 103 VAL U CB  1 
ATOM   11839 C  CG1 . VAL K  1 103 ? 4.627   -30.133 8.423   1.00 66.62  ? 103 VAL U CG1 1 
ATOM   11840 C  CG2 . VAL K  1 103 ? 4.871   -32.637 8.479   1.00 70.23  ? 103 VAL U CG2 1 
ATOM   11841 N  N   . ILE K  1 104 ? 2.125   -30.218 11.081  1.00 63.39  ? 104 ILE U N   1 
ATOM   11842 C  CA  . ILE K  1 104 ? 1.295   -29.215 11.760  1.00 61.39  ? 104 ILE U CA  1 
ATOM   11843 C  C   . ILE K  1 104 ? 1.480   -29.297 13.275  1.00 61.27  ? 104 ILE U C   1 
ATOM   11844 O  O   . ILE K  1 104 ? 1.863   -30.345 13.805  1.00 62.76  ? 104 ILE U O   1 
ATOM   11845 C  CB  . ILE K  1 104 ? -0.214  -29.348 11.422  1.00 60.94  ? 104 ILE U CB  1 
ATOM   11846 C  CG1 . ILE K  1 104 ? -0.759  -30.755 11.746  1.00 62.57  ? 104 ILE U CG1 1 
ATOM   11847 C  CG2 . ILE K  1 104 ? -0.457  -28.996 9.959   1.00 60.95  ? 104 ILE U CG2 1 
ATOM   11848 C  CD1 . ILE K  1 104 ? -2.215  -30.773 12.155  1.00 62.18  ? 104 ILE U CD1 1 
ATOM   11849 N  N   . SER K  1 105 ? 1.207   -28.190 13.958  1.00 59.72  ? 105 SER U N   1 
ATOM   11850 C  CA  . SER K  1 105 ? 1.385   -28.111 15.409  1.00 59.73  ? 105 SER U CA  1 
ATOM   11851 C  C   . SER K  1 105 ? 0.361   -27.163 16.052  1.00 58.22  ? 105 SER U C   1 
ATOM   11852 O  O   . SER K  1 105 ? -0.201  -26.287 15.385  1.00 56.93  ? 105 SER U O   1 
ATOM   11853 C  CB  . SER K  1 105 ? 2.819   -27.666 15.729  1.00 60.17  ? 105 SER U CB  1 
ATOM   11854 O  OG  . SER K  1 105 ? 3.189   -28.010 17.051  1.00 61.02  ? 105 SER U OG  1 
ATOM   11855 N  N   . LEU K  1 106 ? 0.119   -27.378 17.346  1.00 58.59  ? 106 LEU U N   1 
ATOM   11856 C  CA  . LEU K  1 106 ? -0.702  -26.489 18.165  1.00 57.59  ? 106 LEU U CA  1 
ATOM   11857 C  C   . LEU K  1 106 ? 0.172   -25.518 18.972  1.00 57.28  ? 106 LEU U C   1 
ATOM   11858 O  O   . LEU K  1 106 ? -0.341  -24.804 19.838  1.00 56.84  ? 106 LEU U O   1 
ATOM   11859 C  CB  . LEU K  1 106 ? -1.622  -27.292 19.098  1.00 58.57  ? 106 LEU U CB  1 
ATOM   11860 C  CG  . LEU K  1 106 ? -2.376  -28.491 18.498  1.00 59.60  ? 106 LEU U CG  1 
ATOM   11861 C  CD1 . LEU K  1 106 ? -3.383  -29.032 19.504  1.00 60.70  ? 106 LEU U CD1 1 
ATOM   11862 C  CD2 . LEU K  1 106 ? -3.073  -28.142 17.186  1.00 58.69  ? 106 LEU U CD2 1 
ATOM   11863 N  N   . SER K  1 107 ? 1.478   -25.485 18.684  1.00 57.79  ? 107 SER U N   1 
ATOM   11864 C  CA  . SER K  1 107 ? 2.367   -24.457 19.226  1.00 57.71  ? 107 SER U CA  1 
ATOM   11865 C  C   . SER K  1 107 ? 3.617   -24.237 18.357  1.00 58.15  ? 107 SER U C   1 
ATOM   11866 O  O   . SER K  1 107 ? 3.879   -24.990 17.418  1.00 58.68  ? 107 SER U O   1 
ATOM   11867 C  CB  . SER K  1 107 ? 2.762   -24.814 20.665  1.00 59.00  ? 107 SER U CB  1 
ATOM   11868 O  OG  . SER K  1 107 ? 3.302   -26.120 20.741  1.00 60.58  ? 107 SER U OG  1 
ATOM   11869 N  N   . GLY K  1 108 ? 4.362   -23.178 18.668  1.00 58.19  ? 108 GLY U N   1 
ATOM   11870 C  CA  . GLY K  1 108 ? 5.636   -22.882 18.006  1.00 59.08  ? 108 GLY U CA  1 
ATOM   11871 C  C   . GLY K  1 108 ? 5.512   -22.340 16.590  1.00 58.34  ? 108 GLY U C   1 
ATOM   11872 O  O   . GLY K  1 108 ? 4.535   -21.659 16.256  1.00 56.90  ? 108 GLY U O   1 
ATOM   11873 N  N   . ASP K  1 109 ? 6.512   -22.651 15.763  1.00 59.59  ? 109 ASP U N   1 
ATOM   11874 C  CA  . ASP K  1 109 ? 6.622   -22.132 14.391  1.00 59.45  ? 109 ASP U CA  1 
ATOM   11875 C  C   . ASP K  1 109 ? 5.538   -22.655 13.448  1.00 58.55  ? 109 ASP U C   1 
ATOM   11876 O  O   . ASP K  1 109 ? 5.083   -21.923 12.564  1.00 57.82  ? 109 ASP U O   1 
ATOM   11877 C  CB  . ASP K  1 109 ? 7.998   -22.471 13.802  1.00 61.53  ? 109 ASP U CB  1 
ATOM   11878 N  N   . HIS K  1 110 ? 5.135   -23.914 13.636  1.00 58.86  ? 110 HIS U N   1 
ATOM   11879 C  CA  . HIS K  1 110 ? 4.116   -24.561 12.792  1.00 58.46  ? 110 HIS U CA  1 
ATOM   11880 C  C   . HIS K  1 110 ? 2.713   -24.545 13.432  1.00 57.08  ? 110 HIS U C   1 
ATOM   11881 O  O   . HIS K  1 110 ? 1.873   -25.400 13.119  1.00 57.22  ? 110 HIS U O   1 
ATOM   11882 C  CB  . HIS K  1 110 ? 4.557   -26.002 12.471  1.00 60.17  ? 110 HIS U CB  1 
ATOM   11883 C  CG  . HIS K  1 110 ? 5.730   -26.085 11.541  1.00 61.76  ? 110 HIS U CG  1 
ATOM   11884 N  ND1 . HIS K  1 110 ? 6.002   -27.208 10.790  1.00 63.41  ? 110 HIS U ND1 1 
ATOM   11885 C  CD2 . HIS K  1 110 ? 6.687   -25.179 11.222  1.00 62.25  ? 110 HIS U CD2 1 
ATOM   11886 C  CE1 . HIS K  1 110 ? 7.085   -26.996 10.063  1.00 64.85  ? 110 HIS U CE1 1 
ATOM   11887 N  NE2 . HIS K  1 110 ? 7.518   -25.772 10.306  1.00 64.19  ? 110 HIS U NE2 1 
ATOM   11888 N  N   . CYS K  1 111 ? 2.457   -23.564 14.306  1.00 56.02  ? 111 CYS U N   1 
ATOM   11889 C  CA  . CYS K  1 111 ? 1.174   -23.457 15.005  1.00 55.02  ? 111 CYS U CA  1 
ATOM   11890 C  C   . CYS K  1 111 ? 0.065   -23.097 14.024  1.00 54.07  ? 111 CYS U C   1 
ATOM   11891 O  O   . CYS K  1 111 ? 0.197   -22.126 13.280  1.00 53.50  ? 111 CYS U O   1 
ATOM   11892 C  CB  . CYS K  1 111 ? 1.224   -22.407 16.119  1.00 54.45  ? 111 CYS U CB  1 
ATOM   11893 S  SG  . CYS K  1 111 ? -0.263  -22.375 17.154  1.00 53.86  ? 111 CYS U SG  1 
ATOM   11894 N  N   . ILE K  1 112 ? -1.013  -23.882 14.031  1.00 54.15  ? 112 ILE U N   1 
ATOM   11895 C  CA  . ILE K  1 112 ? -2.149  -23.667 13.119  1.00 53.65  ? 112 ILE U CA  1 
ATOM   11896 C  C   . ILE K  1 112 ? -3.313  -22.890 13.752  1.00 52.71  ? 112 ILE U C   1 
ATOM   11897 O  O   . ILE K  1 112 ? -4.253  -22.511 13.050  1.00 52.36  ? 112 ILE U O   1 
ATOM   11898 C  CB  . ILE K  1 112 ? -2.667  -24.989 12.496  1.00 54.78  ? 112 ILE U CB  1 
ATOM   11899 C  CG1 . ILE K  1 112 ? -3.137  -25.991 13.565  1.00 55.58  ? 112 ILE U CG1 1 
ATOM   11900 C  CG2 . ILE K  1 112 ? -1.587  -25.603 11.609  1.00 55.85  ? 112 ILE U CG2 1 
ATOM   11901 C  CD1 . ILE K  1 112 ? -3.979  -27.118 13.012  1.00 56.81  ? 112 ILE U CD1 1 
ATOM   11902 N  N   . ILE K  1 113 ? -3.249  -22.654 15.063  1.00 52.55  ? 113 ILE U N   1 
ATOM   11903 C  CA  . ILE K  1 113 ? -4.307  -21.941 15.775  1.00 52.01  ? 113 ILE U CA  1 
ATOM   11904 C  C   . ILE K  1 113 ? -4.263  -20.477 15.331  1.00 50.98  ? 113 ILE U C   1 
ATOM   11905 O  O   . ILE K  1 113 ? -3.183  -19.885 15.213  1.00 50.80  ? 113 ILE U O   1 
ATOM   11906 C  CB  . ILE K  1 113 ? -4.155  -22.092 17.310  1.00 52.52  ? 113 ILE U CB  1 
ATOM   11907 C  CG1 . ILE K  1 113 ? -4.383  -23.555 17.720  1.00 53.81  ? 113 ILE U CG1 1 
ATOM   11908 C  CG2 . ILE K  1 113 ? -5.127  -21.184 18.056  1.00 52.17  ? 113 ILE U CG2 1 
ATOM   11909 C  CD1 . ILE K  1 113 ? -3.768  -23.922 19.052  1.00 54.69  ? 113 ILE U CD1 1 
ATOM   11910 N  N   . GLY K  1 114 ? -5.438  -19.916 15.051  1.00 50.57  ? 114 GLY U N   1 
ATOM   11911 C  CA  . GLY K  1 114 ? -5.554  -18.574 14.482  1.00 49.82  ? 114 GLY U CA  1 
ATOM   11912 C  C   . GLY K  1 114 ? -5.508  -18.519 12.964  1.00 49.78  ? 114 GLY U C   1 
ATOM   11913 O  O   . GLY K  1 114 ? -5.574  -17.428 12.390  1.00 49.33  ? 114 GLY U O   1 
ATOM   11914 N  N   . ARG K  1 115 ? -5.396  -19.684 12.319  1.00 50.44  ? 115 ARG U N   1 
ATOM   11915 C  CA  . ARG K  1 115 ? -5.344  -19.798 10.858  1.00 50.86  ? 115 ARG U CA  1 
ATOM   11916 C  C   . ARG K  1 115 ? -6.602  -20.519 10.372  1.00 51.51  ? 115 ARG U C   1 
ATOM   11917 O  O   . ARG K  1 115 ? -7.426  -20.957 11.185  1.00 51.77  ? 115 ARG U O   1 
ATOM   11918 C  CB  . ARG K  1 115 ? -4.082  -20.554 10.428  1.00 51.55  ? 115 ARG U CB  1 
ATOM   11919 C  CG  . ARG K  1 115 ? -2.803  -19.979 11.012  1.00 51.32  ? 115 ARG U CG  1 
ATOM   11920 C  CD  . ARG K  1 115 ? -1.559  -20.613 10.415  1.00 52.31  ? 115 ARG U CD  1 
ATOM   11921 N  NE  . ARG K  1 115 ? -0.342  -20.085 11.033  1.00 52.42  ? 115 ARG U NE  1 
ATOM   11922 C  CZ  . ARG K  1 115 ? 0.197   -18.882 10.792  1.00 52.31  ? 115 ARG U CZ  1 
ATOM   11923 N  NH1 . ARG K  1 115 ? -0.351  -18.029 9.926   1.00 52.00  ? 115 ARG U NH1 1 
ATOM   11924 N  NH2 . ARG K  1 115 ? 1.316   -18.530 11.421  1.00 52.79  ? 115 ARG U NH2 1 
ATOM   11925 N  N   . THR K  1 116 ? -6.757  -20.639 9.058   1.00 52.10  ? 116 THR U N   1 
ATOM   11926 C  CA  . THR K  1 116 ? -8.007  -21.138 8.493   1.00 52.97  ? 116 THR U CA  1 
ATOM   11927 C  C   . THR K  1 116 ? -7.894  -22.582 7.990   1.00 54.39  ? 116 THR U C   1 
ATOM   11928 O  O   . THR K  1 116 ? -6.955  -22.928 7.274   1.00 54.84  ? 116 THR U O   1 
ATOM   11929 C  CB  . THR K  1 116 ? -8.487  -20.215 7.370   1.00 53.04  ? 116 THR U CB  1 
ATOM   11930 O  OG1 . THR K  1 116 ? -8.621  -18.893 7.890   1.00 51.94  ? 116 THR U OG1 1 
ATOM   11931 C  CG2 . THR K  1 116 ? -9.845  -20.660 6.811   1.00 54.20  ? 116 THR U CG2 1 
ATOM   11932 N  N   . LEU K  1 117 ? -8.861  -23.407 8.385   1.00 55.30  ? 117 LEU U N   1 
ATOM   11933 C  CA  . LEU K  1 117 ? -9.033  -24.749 7.840   1.00 57.08  ? 117 LEU U CA  1 
ATOM   11934 C  C   . LEU K  1 117 ? -10.056 -24.644 6.711   1.00 58.19  ? 117 LEU U C   1 
ATOM   11935 O  O   . LEU K  1 117 ? -11.180 -24.200 6.948   1.00 58.23  ? 117 LEU U O   1 
ATOM   11936 C  CB  . LEU K  1 117 ? -9.542  -25.696 8.928   1.00 57.84  ? 117 LEU U CB  1 
ATOM   11937 C  CG  . LEU K  1 117 ? -9.639  -27.186 8.592   1.00 59.90  ? 117 LEU U CG  1 
ATOM   11938 C  CD1 . LEU K  1 117 ? -8.269  -27.784 8.288   1.00 60.16  ? 117 LEU U CD1 1 
ATOM   11939 C  CD2 . LEU K  1 117 ? -10.311 -27.907 9.752   1.00 60.80  ? 117 LEU U CD2 1 
ATOM   11940 N  N   . VAL K  1 118 ? -9.662  -25.032 5.497   1.00 59.33  ? 118 VAL U N   1 
ATOM   11941 C  CA  . VAL K  1 118 ? -10.534 -24.970 4.316   1.00 60.74  ? 118 VAL U CA  1 
ATOM   11942 C  C   . VAL K  1 118 ? -10.798 -26.383 3.787   1.00 63.12  ? 118 VAL U C   1 
ATOM   11943 O  O   . VAL K  1 118 ? -9.878  -27.192 3.709   1.00 63.69  ? 118 VAL U O   1 
ATOM   11944 C  CB  . VAL K  1 118 ? -9.897  -24.116 3.191   1.00 60.52  ? 118 VAL U CB  1 
ATOM   11945 C  CG1 . VAL K  1 118 ? -10.783 -24.085 1.947   1.00 62.26  ? 118 VAL U CG1 1 
ATOM   11946 C  CG2 . VAL K  1 118 ? -9.627  -22.700 3.678   1.00 58.53  ? 118 VAL U CG2 1 
ATOM   11947 N  N   . VAL K  1 119 ? -12.053 -26.664 3.428   1.00 64.76  ? 119 VAL U N   1 
ATOM   11948 C  CA  . VAL K  1 119 ? -12.414 -27.892 2.692   1.00 67.53  ? 119 VAL U CA  1 
ATOM   11949 C  C   . VAL K  1 119 ? -12.834 -27.507 1.259   1.00 68.94  ? 119 VAL U C   1 
ATOM   11950 O  O   . VAL K  1 119 ? -13.528 -26.500 1.052   1.00 68.42  ? 119 VAL U O   1 
ATOM   11951 C  CB  . VAL K  1 119 ? -13.480 -28.759 3.427   1.00 69.04  ? 119 VAL U CB  1 
ATOM   11952 C  CG1 . VAL K  1 119 ? -14.801 -28.019 3.620   1.00 69.10  ? 119 VAL U CG1 1 
ATOM   11953 C  CG2 . VAL K  1 119 ? -13.701 -30.083 2.698   1.00 72.08  ? 119 VAL U CG2 1 
ATOM   11954 N  N   . HIS K  1 120 ? -12.402 -28.307 0.283   1.00 70.95  ? 120 HIS U N   1 
ATOM   11955 C  CA  . HIS K  1 120 ? -12.453 -27.919 -1.134  1.00 72.33  ? 120 HIS U CA  1 
ATOM   11956 C  C   . HIS K  1 120 ? -13.506 -28.678 -1.957  1.00 75.50  ? 120 HIS U C   1 
ATOM   11957 O  O   . HIS K  1 120 ? -14.118 -29.638 -1.481  1.00 76.93  ? 120 HIS U O   1 
ATOM   11958 C  CB  . HIS K  1 120 ? -11.061 -28.076 -1.764  1.00 72.51  ? 120 HIS U CB  1 
ATOM   11959 C  CG  . HIS K  1 120 ? -10.158 -26.901 -1.544  1.00 70.11  ? 120 HIS U CG  1 
ATOM   11960 N  ND1 . HIS K  1 120 ? -10.117 -25.822 -2.400  1.00 70.02  ? 120 HIS U ND1 1 
ATOM   11961 C  CD2 . HIS K  1 120 ? -9.252  -26.644 -0.571  1.00 68.01  ? 120 HIS U CD2 1 
ATOM   11962 C  CE1 . HIS K  1 120 ? -9.224  -24.951 -1.964  1.00 68.01  ? 120 HIS U CE1 1 
ATOM   11963 N  NE2 . HIS K  1 120 ? -8.687  -25.425 -0.854  1.00 66.74  ? 120 HIS U NE2 1 
ATOM   11964 N  N   . GLU K  1 121 ? -13.706 -28.218 -3.193  1.00 76.81  ? 121 GLU U N   1 
ATOM   11965 C  CA  . GLU K  1 121 ? -14.714 -28.767 -4.105  1.00 80.07  ? 121 GLU U CA  1 
ATOM   11966 C  C   . GLU K  1 121 ? -14.400 -30.195 -4.563  1.00 82.85  ? 121 GLU U C   1 
ATOM   11967 O  O   . GLU K  1 121 ? -15.288 -31.045 -4.590  1.00 85.31  ? 121 GLU U O   1 
ATOM   11968 C  CB  . GLU K  1 121 ? -14.863 -27.852 -5.331  1.00 80.90  ? 121 GLU U CB  1 
ATOM   11969 C  CG  . GLU K  1 121 ? -16.013 -28.205 -6.269  1.00 84.34  ? 121 GLU U CG  1 
ATOM   11970 C  CD  . GLU K  1 121 ? -16.125 -27.269 -7.463  1.00 85.31  ? 121 GLU U CD  1 
ATOM   11971 O  OE1 . GLU K  1 121 ? -15.217 -26.437 -7.682  1.00 83.60  ? 121 GLU U OE1 1 
ATOM   11972 O  OE2 . GLU K  1 121 ? -17.131 -27.372 -8.195  1.00 88.07  ? 121 GLU U OE2 1 
ATOM   11973 N  N   . LYS K  1 122 ? -13.142 -30.438 -4.928  1.00 82.71  ? 122 LYS U N   1 
ATOM   11974 C  CA  . LYS K  1 122 ? -12.718 -31.704 -5.533  1.00 85.64  ? 122 LYS U CA  1 
ATOM   11975 C  C   . LYS K  1 122 ? -11.407 -32.199 -4.914  1.00 84.39  ? 122 LYS U C   1 
ATOM   11976 O  O   . LYS K  1 122 ? -10.866 -31.567 -4.003  1.00 81.31  ? 122 LYS U O   1 
ATOM   11977 C  CB  . LYS K  1 122 ? -12.626 -31.555 -7.069  1.00 88.21  ? 122 LYS U CB  1 
ATOM   11978 C  CG  . LYS K  1 122 ? -11.901 -30.312 -7.571  1.00 86.53  ? 122 LYS U CG  1 
ATOM   11979 C  CD  . LYS K  1 122 ? -11.997 -30.180 -9.085  1.00 89.55  ? 122 LYS U CD  1 
ATOM   11980 C  CE  . LYS K  1 122 ? -11.551 -28.800 -9.553  1.00 88.09  ? 122 LYS U CE  1 
ATOM   11981 N  NZ  . LYS K  1 122 ? -11.801 -28.582 -11.003 1.00 91.22  ? 122 LYS U NZ  1 
ATOM   11982 N  N   . ALA K  1 123 ? -10.926 -33.345 -5.390  1.00 87.04  ? 123 ALA U N   1 
ATOM   11983 C  CA  . ALA K  1 123 ? -9.722  -33.983 -4.854  1.00 86.55  ? 123 ALA U CA  1 
ATOM   11984 C  C   . ALA K  1 123 ? -8.482  -33.091 -4.926  1.00 84.42  ? 123 ALA U C   1 
ATOM   11985 O  O   . ALA K  1 123 ? -8.278  -32.372 -5.904  1.00 84.85  ? 123 ALA U O   1 
ATOM   11986 C  CB  . ALA K  1 123 ? -9.450  -35.293 -5.585  1.00 90.33  ? 123 ALA U CB  1 
ATOM   11987 N  N   . ASP K  1 124 ? -7.680  -33.136 -3.864  1.00 82.35  ? 124 ASP U N   1 
ATOM   11988 C  CA  . ASP K  1 124 ? -6.315  -32.624 -3.875  1.00 81.13  ? 124 ASP U CA  1 
ATOM   11989 C  C   . ASP K  1 124 ? -5.472  -33.670 -4.606  1.00 84.15  ? 124 ASP U C   1 
ATOM   11990 O  O   . ASP K  1 124 ? -5.431  -34.832 -4.188  1.00 85.55  ? 124 ASP U O   1 
ATOM   11991 C  CB  . ASP K  1 124 ? -5.818  -32.431 -2.429  1.00 78.35  ? 124 ASP U CB  1 
ATOM   11992 C  CG  . ASP K  1 124 ? -4.417  -31.821 -2.342  1.00 77.15  ? 124 ASP U CG  1 
ATOM   11993 O  OD1 . ASP K  1 124 ? -3.931  -31.248 -3.340  1.00 77.93  ? 124 ASP U OD1 1 
ATOM   11994 O  OD2 . ASP K  1 124 ? -3.801  -31.912 -1.256  1.00 75.66  ? 124 ASP U OD2 1 
ATOM   11995 N  N   . ASP K  1 125 ? -4.816  -33.270 -5.697  1.00 85.43  ? 125 ASP U N   1 
ATOM   11996 C  CA  . ASP K  1 125 ? -3.983  -34.206 -6.484  1.00 88.70  ? 125 ASP U CA  1 
ATOM   11997 C  C   . ASP K  1 125 ? -2.633  -34.567 -5.825  1.00 88.24  ? 125 ASP U C   1 
ATOM   11998 O  O   . ASP K  1 125 ? -1.926  -35.448 -6.320  1.00 91.04  ? 125 ASP U O   1 
ATOM   11999 C  CB  . ASP K  1 125 ? -3.777  -33.708 -7.931  1.00 90.82  ? 125 ASP U CB  1 
ATOM   12000 C  CG  . ASP K  1 125 ? -3.076  -32.355 -8.015  1.00 88.80  ? 125 ASP U CG  1 
ATOM   12001 O  OD1 . ASP K  1 125 ? -2.376  -31.957 -7.062  1.00 86.29  ? 125 ASP U OD1 1 
ATOM   12002 O  OD2 . ASP K  1 125 ? -3.232  -31.684 -9.055  1.00 89.98  ? 125 ASP U OD2 1 
ATOM   12003 N  N   . LEU K  1 126 ? -2.285  -33.865 -4.739  1.00 84.98  ? 126 LEU U N   1 
ATOM   12004 C  CA  . LEU K  1 126 ? -1.105  -34.147 -3.904  1.00 84.31  ? 126 LEU U CA  1 
ATOM   12005 C  C   . LEU K  1 126 ? 0.208   -33.805 -4.623  1.00 85.62  ? 126 LEU U C   1 
ATOM   12006 O  O   . LEU K  1 126 ? 1.197   -34.538 -4.527  1.00 87.28  ? 126 LEU U O   1 
ATOM   12007 C  CB  . LEU K  1 126 ? -1.108  -35.601 -3.381  1.00 86.04  ? 126 LEU U CB  1 
ATOM   12008 C  CG  . LEU K  1 126 ? -2.396  -36.127 -2.725  1.00 85.60  ? 126 LEU U CG  1 
ATOM   12009 C  CD1 . LEU K  1 126 ? -2.338  -37.640 -2.555  1.00 88.38  ? 126 LEU U CD1 1 
ATOM   12010 C  CD2 . LEU K  1 126 ? -2.667  -35.448 -1.384  1.00 82.10  ? 126 LEU U CD2 1 
ATOM   12011 N  N   . GLY K  1 127 ? 0.199   -32.687 -5.350  1.00 85.15  ? 127 GLY U N   1 
ATOM   12012 C  CA  . GLY K  1 127 ? 1.377   -32.199 -6.067  1.00 86.54  ? 127 GLY U CA  1 
ATOM   12013 C  C   . GLY K  1 127 ? 1.780   -32.954 -7.328  1.00 90.65  ? 127 GLY U C   1 
ATOM   12014 O  O   . GLY K  1 127 ? 2.781   -32.595 -7.950  1.00 92.25  ? 127 GLY U O   1 
ATOM   12015 N  N   . LYS K  1 128 ? 1.003   -33.970 -7.721  1.00 92.67  ? 128 LYS U N   1 
ATOM   12016 C  CA  . LYS K  1 128 ? 1.338   -34.854 -8.847  1.00 96.95  ? 128 LYS U CA  1 
ATOM   12017 C  C   . LYS K  1 128 ? 0.366   -34.671 -10.020 1.00 98.79  ? 128 LYS U C   1 
ATOM   12018 O  O   . LYS K  1 128 ? 0.001   -35.640 -10.693 1.00 102.01 ? 128 LYS U O   1 
ATOM   12019 C  CB  . LYS K  1 128 ? 1.331   -36.312 -8.377  1.00 98.56  ? 128 LYS U CB  1 
ATOM   12020 N  N   . GLY K  1 129 ? -0.036  -33.423 -10.262 1.00 96.99  ? 129 GLY U N   1 
ATOM   12021 C  CA  . GLY K  1 129 ? -0.949  -33.072 -11.351 1.00 98.63  ? 129 GLY U CA  1 
ATOM   12022 C  C   . GLY K  1 129 ? -0.255  -32.795 -12.674 1.00 101.96 ? 129 GLY U C   1 
ATOM   12023 O  O   . GLY K  1 129 ? -0.888  -32.869 -13.728 1.00 104.57 ? 129 GLY U O   1 
ATOM   12024 N  N   . GLY K  1 130 ? 1.036   -32.458 -12.622 1.00 102.13 ? 130 GLY U N   1 
ATOM   12025 C  CA  . GLY K  1 130 ? 1.831   -32.195 -13.821 1.00 105.62 ? 130 GLY U CA  1 
ATOM   12026 C  C   . GLY K  1 130 ? 1.507   -30.857 -14.458 1.00 105.15 ? 130 GLY U C   1 
ATOM   12027 O  O   . GLY K  1 130 ? 1.337   -30.769 -15.675 1.00 108.40 ? 130 GLY U O   1 
ATOM   12028 N  N   . ASN K  1 131 ? 1.430   -29.817 -13.629 1.00 101.34 ? 131 ASN U N   1 
ATOM   12029 C  CA  . ASN K  1 131 ? 1.088   -28.465 -14.087 1.00 100.58 ? 131 ASN U CA  1 
ATOM   12030 C  C   . ASN K  1 131 ? 1.456   -27.398 -13.048 1.00 96.79  ? 131 ASN U C   1 
ATOM   12031 O  O   . ASN K  1 131 ? 1.786   -27.722 -11.901 1.00 94.45  ? 131 ASN U O   1 
ATOM   12032 C  CB  . ASN K  1 131 ? -0.406  -28.379 -14.455 1.00 100.38 ? 131 ASN U CB  1 
ATOM   12033 C  CG  . ASN K  1 131 ? -1.322  -28.896 -13.353 1.00 97.47  ? 131 ASN U CG  1 
ATOM   12034 O  OD1 . ASN K  1 131 ? -1.556  -28.218 -12.354 1.00 93.80  ? 131 ASN U OD1 1 
ATOM   12035 N  ND2 . ASN K  1 131 ? -1.863  -30.095 -13.546 1.00 99.39  ? 131 ASN U ND2 1 
ATOM   12036 N  N   . GLU K  1 132 ? 1.402   -26.134 -13.471 1.00 96.52  ? 132 GLU U N   1 
ATOM   12037 C  CA  . GLU K  1 132 ? 1.722   -24.981 -12.612 1.00 93.39  ? 132 GLU U CA  1 
ATOM   12038 C  C   . GLU K  1 132 ? 0.841   -24.915 -11.356 1.00 89.31  ? 132 GLU U C   1 
ATOM   12039 O  O   . GLU K  1 132 ? 1.340   -24.636 -10.259 1.00 86.79  ? 132 GLU U O   1 
ATOM   12040 C  CB  . GLU K  1 132 ? 1.613   -23.671 -13.425 1.00 94.31  ? 132 GLU U CB  1 
ATOM   12041 C  CG  . GLU K  1 132 ? 1.777   -22.359 -12.652 1.00 91.40  ? 132 GLU U CG  1 
ATOM   12042 C  CD  . GLU K  1 132 ? 3.058   -22.277 -11.833 1.00 90.60  ? 132 GLU U CD  1 
ATOM   12043 O  OE1 . GLU K  1 132 ? 4.100   -22.807 -12.281 1.00 93.38  ? 132 GLU U OE1 1 
ATOM   12044 O  OE2 . GLU K  1 132 ? 3.021   -21.669 -10.740 1.00 87.40  ? 132 GLU U OE2 1 
ATOM   12045 N  N   . GLU K  1 133 ? -0.455  -25.179 -11.523 1.00 89.00  ? 133 GLU U N   1 
ATOM   12046 C  CA  . GLU K  1 133 ? -1.430  -25.051 -10.432 1.00 85.59  ? 133 GLU U CA  1 
ATOM   12047 C  C   . GLU K  1 133 ? -1.392  -26.212 -9.425  1.00 84.47  ? 133 GLU U C   1 
ATOM   12048 O  O   . GLU K  1 133 ? -1.753  -26.023 -8.261  1.00 81.46  ? 133 GLU U O   1 
ATOM   12049 C  CB  . GLU K  1 133 ? -2.845  -24.864 -11.012 1.00 86.08  ? 133 GLU U CB  1 
ATOM   12050 C  CG  . GLU K  1 133 ? -3.947  -24.492 -10.015 1.00 82.91  ? 133 GLU U CG  1 
ATOM   12051 C  CD  . GLU K  1 133 ? -3.744  -23.150 -9.314  1.00 80.12  ? 133 GLU U CD  1 
ATOM   12052 O  OE1 . GLU K  1 133 ? -2.853  -22.367 -9.706  1.00 80.74  ? 133 GLU U OE1 1 
ATOM   12053 O  OE2 . GLU K  1 133 ? -4.498  -22.866 -8.360  1.00 77.53  ? 133 GLU U OE2 1 
ATOM   12054 N  N   . SER K  1 134 ? -0.952  -27.395 -9.859  1.00 87.09  ? 134 SER U N   1 
ATOM   12055 C  CA  . SER K  1 134 ? -0.808  -28.550 -8.959  1.00 86.52  ? 134 SER U CA  1 
ATOM   12056 C  C   . SER K  1 134 ? 0.265   -28.330 -7.886  1.00 84.54  ? 134 SER U C   1 
ATOM   12057 O  O   . SER K  1 134 ? 0.108   -28.783 -6.750  1.00 82.60  ? 134 SER U O   1 
ATOM   12058 C  CB  . SER K  1 134 ? -0.490  -29.821 -9.750  1.00 90.23  ? 134 SER U CB  1 
ATOM   12059 O  OG  . SER K  1 134 ? -0.332  -30.934 -8.885  1.00 89.90  ? 134 SER U OG  1 
ATOM   12060 N  N   . THR K  1 135 ? 1.340   -27.633 -8.254  1.00 85.34  ? 135 THR U N   1 
ATOM   12061 C  CA  . THR K  1 135 ? 2.441   -27.328 -7.332  1.00 83.95  ? 135 THR U CA  1 
ATOM   12062 C  C   . THR K  1 135 ? 2.163   -26.160 -6.366  1.00 80.45  ? 135 THR U C   1 
ATOM   12063 O  O   . THR K  1 135 ? 2.951   -25.942 -5.442  1.00 79.12  ? 135 THR U O   1 
ATOM   12064 C  CB  . THR K  1 135 ? 3.747   -27.037 -8.103  1.00 86.65  ? 135 THR U CB  1 
ATOM   12065 O  OG1 . THR K  1 135 ? 3.562   -25.905 -8.962  1.00 87.28  ? 135 THR U OG1 1 
ATOM   12066 C  CG2 . THR K  1 135 ? 4.165   -28.248 -8.941  1.00 90.35  ? 135 THR U CG2 1 
ATOM   12067 N  N   . LYS K  1 136 ? 1.068   -25.419 -6.576  1.00 79.23  ? 136 LYS U N   1 
ATOM   12068 C  CA  . LYS K  1 136 ? 0.626   -24.360 -5.646  1.00 76.05  ? 136 LYS U CA  1 
ATOM   12069 C  C   . LYS K  1 136 ? -0.561  -24.793 -4.773  1.00 73.95  ? 136 LYS U C   1 
ATOM   12070 O  O   . LYS K  1 136 ? -0.487  -24.717 -3.546  1.00 71.70  ? 136 LYS U O   1 
ATOM   12071 C  CB  . LYS K  1 136 ? 0.245   -23.082 -6.405  1.00 76.22  ? 136 LYS U CB  1 
ATOM   12072 C  CG  . LYS K  1 136 ? 1.423   -22.271 -6.936  1.00 77.72  ? 136 LYS U CG  1 
ATOM   12073 C  CD  . LYS K  1 136 ? 1.077   -20.790 -7.082  1.00 76.79  ? 136 LYS U CD  1 
ATOM   12074 C  CE  . LYS K  1 136 ? 0.034   -20.539 -8.165  1.00 78.07  ? 136 LYS U CE  1 
ATOM   12075 N  NZ  . LYS K  1 136 ? -0.498  -19.150 -8.103  1.00 76.81  ? 136 LYS U NZ  1 
ATOM   12076 N  N   . THR K  1 137 ? -1.651  -25.219 -5.416  1.00 74.96  ? 137 THR U N   1 
ATOM   12077 C  CA  . THR K  1 137 ? -2.915  -25.569 -4.732  1.00 73.50  ? 137 THR U CA  1 
ATOM   12078 C  C   . THR K  1 137 ? -3.333  -27.049 -4.810  1.00 75.13  ? 137 THR U C   1 
ATOM   12079 O  O   . THR K  1 137 ? -4.195  -27.493 -4.047  1.00 74.09  ? 137 THR U O   1 
ATOM   12080 C  CB  . THR K  1 137 ? -4.081  -24.730 -5.295  1.00 73.36  ? 137 THR U CB  1 
ATOM   12081 O  OG1 . THR K  1 137 ? -4.190  -24.951 -6.707  1.00 76.30  ? 137 THR U OG1 1 
ATOM   12082 C  CG2 . THR K  1 137 ? -3.864  -23.239 -5.018  1.00 71.52  ? 137 THR U CG2 1 
ATOM   12083 N  N   . GLY K  1 138 ? -2.743  -27.801 -5.734  1.00 77.93  ? 138 GLY U N   1 
ATOM   12084 C  CA  . GLY K  1 138 ? -3.132  -29.186 -5.965  1.00 80.07  ? 138 GLY U CA  1 
ATOM   12085 C  C   . GLY K  1 138 ? -4.450  -29.393 -6.708  1.00 81.56  ? 138 GLY U C   1 
ATOM   12086 O  O   . GLY K  1 138 ? -5.076  -30.448 -6.569  1.00 82.79  ? 138 GLY U O   1 
ATOM   12087 N  N   . ASN K  1 139 ? -4.869  -28.394 -7.493  1.00 81.70  ? 139 ASN U N   1 
ATOM   12088 C  CA  . ASN K  1 139 ? -6.069  -28.470 -8.354  1.00 83.53  ? 139 ASN U CA  1 
ATOM   12089 C  C   . ASN K  1 139 ? -7.375  -28.847 -7.623  1.00 82.62  ? 139 ASN U C   1 
ATOM   12090 O  O   . ASN K  1 139 ? -8.272  -29.456 -8.212  1.00 84.94  ? 139 ASN U O   1 
ATOM   12091 C  CB  . ASN K  1 139 ? -5.814  -29.431 -9.531  1.00 87.50  ? 139 ASN U CB  1 
ATOM   12092 C  CG  . ASN K  1 139 ? -4.599  -29.042 -10.357 1.00 88.96  ? 139 ASN U CG  1 
ATOM   12093 O  OD1 . ASN K  1 139 ? -4.209  -27.875 -10.405 1.00 87.57  ? 139 ASN U OD1 1 
ATOM   12094 N  ND2 . ASN K  1 139 ? -4.002  -30.022 -11.024 1.00 92.10  ? 139 ASN U ND2 1 
ATOM   12095 N  N   . ALA K  1 140 ? -7.490  -28.450 -6.354  1.00 79.50  ? 140 ALA U N   1 
ATOM   12096 C  CA  . ALA K  1 140 ? -8.627  -28.851 -5.514  1.00 78.75  ? 140 ALA U CA  1 
ATOM   12097 C  C   . ALA K  1 140 ? -9.924  -28.063 -5.770  1.00 78.59  ? 140 ALA U C   1 
ATOM   12098 O  O   . ALA K  1 140 ? -10.965 -28.414 -5.215  1.00 78.63  ? 140 ALA U O   1 
ATOM   12099 C  CB  . ALA K  1 140 ? -8.246  -28.779 -4.040  1.00 75.88  ? 140 ALA U CB  1 
ATOM   12100 N  N   . GLY K  1 141 ? -9.868  -27.011 -6.592  1.00 78.66  ? 141 GLY U N   1 
ATOM   12101 C  CA  . GLY K  1 141 ? -11.058 -26.225 -6.939  1.00 78.85  ? 141 GLY U CA  1 
ATOM   12102 C  C   . GLY K  1 141 ? -11.430 -25.205 -5.874  1.00 75.73  ? 141 GLY U C   1 
ATOM   12103 O  O   . GLY K  1 141 ? -10.578 -24.779 -5.085  1.00 73.36  ? 141 GLY U O   1 
ATOM   12104 N  N   . SER K  1 142 ? -12.709 -24.825 -5.849  1.00 76.01  ? 142 SER U N   1 
ATOM   12105 C  CA  . SER K  1 142 ? -13.202 -23.756 -4.968  1.00 73.53  ? 142 SER U CA  1 
ATOM   12106 C  C   . SER K  1 142 ? -13.165 -24.121 -3.484  1.00 71.41  ? 142 SER U C   1 
ATOM   12107 O  O   . SER K  1 142 ? -13.126 -25.297 -3.117  1.00 72.21  ? 142 SER U O   1 
ATOM   12108 C  CB  . SER K  1 142 ? -14.637 -23.365 -5.341  1.00 74.90  ? 142 SER U CB  1 
ATOM   12109 O  OG  . SER K  1 142 ? -14.709 -22.850 -6.658  1.00 76.82  ? 142 SER U OG  1 
ATOM   12110 N  N   . ARG K  1 143 ? -13.191 -23.088 -2.646  1.00 68.96  ? 143 ARG U N   1 
ATOM   12111 C  CA  . ARG K  1 143 ? -13.211 -23.241 -1.191  1.00 67.01  ? 143 ARG U CA  1 
ATOM   12112 C  C   . ARG K  1 143 ? -14.675 -23.316 -0.736  1.00 67.72  ? 143 ARG U C   1 
ATOM   12113 O  O   . ARG K  1 143 ? -15.361 -22.291 -0.646  1.00 67.15  ? 143 ARG U O   1 
ATOM   12114 C  CB  . ARG K  1 143 ? -12.463 -22.077 -0.528  1.00 64.40  ? 143 ARG U CB  1 
ATOM   12115 C  CG  . ARG K  1 143 ? -11.035 -21.902 -1.043  1.00 64.09  ? 143 ARG U CG  1 
ATOM   12116 C  CD  . ARG K  1 143 ? -10.321 -20.691 -0.456  1.00 61.93  ? 143 ARG U CD  1 
ATOM   12117 N  NE  . ARG K  1 143 ? -9.015  -20.483 -1.091  1.00 62.19  ? 143 ARG U NE  1 
ATOM   12118 C  CZ  . ARG K  1 143 ? -8.103  -19.581 -0.718  1.00 60.85  ? 143 ARG U CZ  1 
ATOM   12119 N  NH1 . ARG K  1 143 ? -8.313  -18.764 0.315   1.00 59.02  ? 143 ARG U NH1 1 
ATOM   12120 N  NH2 . ARG K  1 143 ? -6.955  -19.497 -1.384  1.00 61.65  ? 143 ARG U NH2 1 
ATOM   12121 N  N   . LEU K  1 144 ? -15.152 -24.537 -0.480  1.00 69.27  ? 144 LEU U N   1 
ATOM   12122 C  CA  . LEU K  1 144 ? -16.572 -24.779 -0.177  1.00 70.74  ? 144 LEU U CA  1 
ATOM   12123 C  C   . LEU K  1 144 ? -16.962 -24.321 1.226   1.00 68.99  ? 144 LEU U C   1 
ATOM   12124 O  O   . LEU K  1 144 ? -18.042 -23.761 1.409   1.00 69.48  ? 144 LEU U O   1 
ATOM   12125 C  CB  . LEU K  1 144 ? -16.943 -26.262 -0.348  1.00 73.36  ? 144 LEU U CB  1 
ATOM   12126 C  CG  . LEU K  1 144 ? -16.907 -26.898 -1.742  1.00 76.07  ? 144 LEU U CG  1 
ATOM   12127 C  CD1 . LEU K  1 144 ? -17.526 -28.286 -1.671  1.00 78.88  ? 144 LEU U CD1 1 
ATOM   12128 C  CD2 . LEU K  1 144 ? -17.632 -26.061 -2.787  1.00 77.30  ? 144 LEU U CD2 1 
ATOM   12129 N  N   . ALA K  1 145 ? -16.098 -24.578 2.207   1.00 67.24  ? 145 ALA U N   1 
ATOM   12130 C  CA  . ALA K  1 145 ? -16.331 -24.126 3.588   1.00 65.67  ? 145 ALA U CA  1 
ATOM   12131 C  C   . ALA K  1 145 ? -15.021 -23.863 4.329   1.00 63.28  ? 145 ALA U C   1 
ATOM   12132 O  O   . ALA K  1 145 ? -14.027 -24.568 4.123   1.00 63.29  ? 145 ALA U O   1 
ATOM   12133 C  CB  . ALA K  1 145 ? -17.170 -25.144 4.345   1.00 67.34  ? 145 ALA U CB  1 
ATOM   12134 N  N   . ALA K  1 146 ? -15.041 -22.849 5.194   1.00 61.51  ? 146 ALA U N   1 
ATOM   12135 C  CA  . ALA K  1 146 ? -13.860 -22.422 5.944   1.00 59.40  ? 146 ALA U CA  1 
ATOM   12136 C  C   . ALA K  1 146 ? -14.215 -21.955 7.355   1.00 58.40  ? 146 ALA U C   1 
ATOM   12137 O  O   . ALA K  1 146 ? -15.322 -21.466 7.608   1.00 58.93  ? 146 ALA U O   1 
ATOM   12138 C  CB  . ALA K  1 146 ? -13.136 -21.314 5.194   1.00 58.31  ? 146 ALA U CB  1 
ATOM   12139 N  N   . GLY K  1 147 ? -13.256 -22.109 8.265   1.00 57.19  ? 147 GLY U N   1 
ATOM   12140 C  CA  . GLY K  1 147 ? -13.397 -21.654 9.644   1.00 56.30  ? 147 GLY U CA  1 
ATOM   12141 C  C   . GLY K  1 147 ? -12.048 -21.382 10.279  1.00 54.75  ? 147 GLY U C   1 
ATOM   12142 O  O   . GLY K  1 147 ? -11.044 -21.975 9.887   1.00 54.66  ? 147 GLY U O   1 
ATOM   12143 N  N   . VAL K  1 148 ? -12.039 -20.483 11.263  1.00 53.77  ? 148 VAL U N   1 
ATOM   12144 C  CA  . VAL K  1 148 ? -10.822 -20.099 11.979  1.00 52.56  ? 148 VAL U CA  1 
ATOM   12145 C  C   . VAL K  1 148 ? -10.572 -21.113 13.103  1.00 53.08  ? 148 VAL U C   1 
ATOM   12146 O  O   . VAL K  1 148 ? -11.488 -21.432 13.868  1.00 53.95  ? 148 VAL U O   1 
ATOM   12147 C  CB  . VAL K  1 148 ? -10.933 -18.664 12.553  1.00 51.63  ? 148 VAL U CB  1 
ATOM   12148 C  CG1 . VAL K  1 148 ? -9.660  -18.277 13.309  1.00 50.76  ? 148 VAL U CG1 1 
ATOM   12149 C  CG2 . VAL K  1 148 ? -11.241 -17.661 11.442  1.00 51.35  ? 148 VAL U CG2 1 
ATOM   12150 N  N   . ILE K  1 149 ? -9.328  -21.593 13.196  1.00 52.79  ? 149 ILE U N   1 
ATOM   12151 C  CA  . ILE K  1 149 ? -8.923  -22.610 14.177  1.00 53.46  ? 149 ILE U CA  1 
ATOM   12152 C  C   . ILE K  1 149 ? -8.690  -21.940 15.536  1.00 52.98  ? 149 ILE U C   1 
ATOM   12153 O  O   . ILE K  1 149 ? -7.833  -21.065 15.649  1.00 51.99  ? 149 ILE U O   1 
ATOM   12154 C  CB  . ILE K  1 149 ? -7.626  -23.337 13.749  1.00 53.58  ? 149 ILE U CB  1 
ATOM   12155 C  CG1 . ILE K  1 149 ? -7.780  -23.967 12.355  1.00 54.32  ? 149 ILE U CG1 1 
ATOM   12156 C  CG2 . ILE K  1 149 ? -7.246  -24.422 14.762  1.00 54.54  ? 149 ILE U CG2 1 
ATOM   12157 C  CD1 . ILE K  1 149 ? -6.469  -24.157 11.624  1.00 54.27  ? 149 ILE U CD1 1 
ATOM   12158 N  N   . GLY K  1 150 ? -9.438  -22.363 16.557  1.00 53.96  ? 150 GLY U N   1 
ATOM   12159 C  CA  . GLY K  1 150 ? -9.371  -21.747 17.890  1.00 53.95  ? 150 GLY U CA  1 
ATOM   12160 C  C   . GLY K  1 150 ? -8.964  -22.715 18.987  1.00 55.09  ? 150 GLY U C   1 
ATOM   12161 O  O   . GLY K  1 150 ? -9.041  -23.924 18.801  1.00 56.16  ? 150 GLY U O   1 
ATOM   12162 N  N   . ILE K  1 151 ? -8.548  -22.168 20.132  1.00 55.12  ? 151 ILE U N   1 
ATOM   12163 C  CA  . ILE K  1 151 ? -8.169  -22.961 21.318  1.00 56.43  ? 151 ILE U CA  1 
ATOM   12164 C  C   . ILE K  1 151 ? -9.450  -23.512 21.948  1.00 58.10  ? 151 ILE U C   1 
ATOM   12165 O  O   . ILE K  1 151 ? -10.509 -22.903 21.830  1.00 58.15  ? 151 ILE U O   1 
ATOM   12166 C  CB  . ILE K  1 151 ? -7.387  -22.124 22.373  1.00 56.28  ? 151 ILE U CB  1 
ATOM   12167 C  CG1 . ILE K  1 151 ? -6.149  -21.453 21.755  1.00 54.96  ? 151 ILE U CG1 1 
ATOM   12168 C  CG2 . ILE K  1 151 ? -6.943  -22.996 23.545  1.00 57.87  ? 151 ILE U CG2 1 
ATOM   12169 C  CD1 . ILE K  1 151 ? -5.591  -20.303 22.571  1.00 54.79  ? 151 ILE U CD1 1 
ATOM   12170 N  N   . ALA K  1 152 ? -9.352  -24.669 22.594  1.00 59.75  ? 152 ALA U N   1 
ATOM   12171 C  CA  . ALA K  1 152 ? -10.500 -25.307 23.237  1.00 61.86  ? 152 ALA U CA  1 
ATOM   12172 C  C   . ALA K  1 152 ? -10.117 -25.813 24.615  1.00 63.55  ? 152 ALA U C   1 
ATOM   12173 O  O   . ALA K  1 152 ? -8.932  -25.957 24.913  1.00 63.22  ? 152 ALA U O   1 
ATOM   12174 C  CB  . ALA K  1 152 ? -10.996 -26.457 22.376  1.00 62.84  ? 152 ALA U CB  1 
ATOM   12175 N  N   . GLN K  1 153 ? -11.120 -26.073 25.453  1.00 65.64  ? 153 GLN U N   1 
ATOM   12176 C  CA  . GLN K  1 153 ? -10.895 -26.684 26.765  1.00 67.80  ? 153 GLN U CA  1 
ATOM   12177 C  C   . GLN K  1 153 ? -10.621 -28.166 26.589  1.00 69.30  ? 153 GLN U C   1 
ATOM   12178 O  O   . GLN K  1 153 ? -11.093 -28.775 25.628  1.00 69.44  ? 153 GLN U O   1 
ATOM   12179 C  CB  . GLN K  1 153 ? -12.102 -26.498 27.687  1.00 69.96  ? 153 GLN U CB  1 
ATOM   12180 C  CG  . GLN K  1 153 ? -11.816 -26.890 29.134  1.00 72.26  ? 153 GLN U CG  1 
ATOM   12181 C  CD  . GLN K  1 153 ? -12.877 -26.432 30.119  1.00 74.40  ? 153 GLN U CD  1 
ATOM   12182 O  OE1 . GLN K  1 153 ? -13.528 -25.407 29.925  1.00 73.60  ? 153 GLN U OE1 1 
ATOM   12183 N  NE2 . GLN K  1 153 ? -13.042 -27.190 31.200  1.00 77.39  ? 153 GLN U NE2 1 
ATOM   12184 O  OXT . GLN K  1 153 ? -9.941  -28.787 27.405  1.00 70.69  ? 153 GLN U OXT 1 
ATOM   12185 N  N   . THR L  1 2   ? 2.236   -7.003  13.551  1.00 56.64  ? 2   THR W N   1 
ATOM   12186 C  CA  . THR L  1 2   ? 1.233   -8.115  13.511  1.00 55.91  ? 2   THR W CA  1 
ATOM   12187 C  C   . THR L  1 2   ? -0.184  -7.566  13.451  1.00 54.15  ? 2   THR W C   1 
ATOM   12188 O  O   . THR L  1 2   ? -0.472  -6.511  14.024  1.00 52.69  ? 2   THR W O   1 
ATOM   12189 C  CB  . THR L  1 2   ? 1.320   -9.047  14.748  1.00 54.89  ? 2   THR W CB  1 
ATOM   12190 O  OG1 . THR L  1 2   ? 2.680   -9.174  15.170  1.00 56.05  ? 2   THR W OG1 1 
ATOM   12191 C  CG2 . THR L  1 2   ? 0.737   -10.441 14.427  1.00 55.55  ? 2   THR W CG2 1 
ATOM   12192 N  N   . LYS L  1 3   ? -1.048  -8.296  12.749  1.00 54.51  ? 3   LYS W N   1 
ATOM   12193 C  CA  . LYS L  1 3   ? -2.463  -7.978  12.631  1.00 53.19  ? 3   LYS W CA  1 
ATOM   12194 C  C   . LYS L  1 3   ? -3.308  -9.227  12.828  1.00 52.83  ? 3   LYS W C   1 
ATOM   12195 O  O   . LYS L  1 3   ? -2.868  -10.346 12.566  1.00 54.15  ? 3   LYS W O   1 
ATOM   12196 C  CB  . LYS L  1 3   ? -2.769  -7.373  11.254  1.00 54.70  ? 3   LYS W CB  1 
ATOM   12197 C  CG  . LYS L  1 3   ? -2.111  -6.025  11.015  1.00 55.19  ? 3   LYS W CG  1 
ATOM   12198 C  CD  . LYS L  1 3   ? -2.460  -5.447  9.652   1.00 56.91  ? 3   LYS W CD  1 
ATOM   12199 C  CE  . LYS L  1 3   ? -1.765  -4.111  9.439   1.00 57.70  ? 3   LYS W CE  1 
ATOM   12200 N  NZ  . LYS L  1 3   ? -1.937  -3.594  8.058   1.00 59.82  ? 3   LYS W NZ  1 
ATOM   12201 N  N   . ALA L  1 4   ? -4.535  -9.013  13.278  1.00 51.21  ? 4   ALA W N   1 
ATOM   12202 C  CA  . ALA L  1 4   ? -5.493  -10.090 13.472  1.00 51.14  ? 4   ALA W CA  1 
ATOM   12203 C  C   . ALA L  1 4   ? -6.896  -9.540  13.260  1.00 50.43  ? 4   ALA W C   1 
ATOM   12204 O  O   . ALA L  1 4   ? -7.099  -8.323  13.263  1.00 49.48  ? 4   ALA W O   1 
ATOM   12205 C  CB  . ALA L  1 4   ? -5.346  -10.684 14.869  1.00 49.84  ? 4   ALA W CB  1 
ATOM   12206 N  N   . VAL L  1 5   ? -7.855  -10.440 13.088  1.00 51.06  ? 5   VAL W N   1 
ATOM   12207 C  CA  . VAL L  1 5   ? -9.215  -10.049 12.744  1.00 51.00  ? 5   VAL W CA  1 
ATOM   12208 C  C   . VAL L  1 5   ? -10.221 -11.045 13.314  1.00 51.04  ? 5   VAL W C   1 
ATOM   12209 O  O   . VAL L  1 5   ? -9.898  -12.208 13.530  1.00 51.81  ? 5   VAL W O   1 
ATOM   12210 C  CB  . VAL L  1 5   ? -9.357  -9.902  11.200  1.00 53.03  ? 5   VAL W CB  1 
ATOM   12211 C  CG1 . VAL L  1 5   ? -9.331  -11.258 10.511  1.00 55.16  ? 5   VAL W CG1 1 
ATOM   12212 C  CG2 . VAL L  1 5   ? -10.603 -9.117  10.822  1.00 52.92  ? 5   VAL W CG2 1 
ATOM   12213 N  N   . CYS L  1 6   ? -11.437 -10.562 13.550  1.00 50.51  ? 6   CYS W N   1 
ATOM   12214 C  CA  . CYS L  1 6   ? -12.511 -11.347 14.152  1.00 50.71  ? 6   CYS W CA  1 
ATOM   12215 C  C   . CYS L  1 6   ? -13.850 -10.908 13.586  1.00 51.44  ? 6   CYS W C   1 
ATOM   12216 O  O   . CYS L  1 6   ? -14.218 -9.732  13.700  1.00 50.41  ? 6   CYS W O   1 
ATOM   12217 C  CB  . CYS L  1 6   ? -12.512 -11.130 15.665  1.00 48.71  ? 6   CYS W CB  1 
ATOM   12218 S  SG  . CYS L  1 6   ? -13.943 -11.820 16.527  1.00 48.86  ? 6   CYS W SG  1 
ATOM   12219 N  N   . VAL L  1 7   ? -14.569 -11.844 12.969  1.00 53.50  ? 7   VAL W N   1 
ATOM   12220 C  CA  . VAL L  1 7   ? -15.942 -11.600 12.535  1.00 54.50  ? 7   VAL W CA  1 
ATOM   12221 C  C   . VAL L  1 7   ? -16.872 -11.939 13.703  1.00 53.88  ? 7   VAL W C   1 
ATOM   12222 O  O   . VAL L  1 7   ? -16.971 -13.097 14.111  1.00 54.67  ? 7   VAL W O   1 
ATOM   12223 C  CB  . VAL L  1 7   ? -16.328 -12.434 11.294  1.00 57.33  ? 7   VAL W CB  1 
ATOM   12224 C  CG1 . VAL L  1 7   ? -17.737 -12.071 10.824  1.00 58.49  ? 7   VAL W CG1 1 
ATOM   12225 C  CG2 . VAL L  1 7   ? -15.318 -12.224 10.167  1.00 58.24  ? 7   VAL W CG2 1 
ATOM   12226 N  N   . LEU L  1 8   ? -17.530 -10.915 14.241  1.00 52.66  ? 8   LEU W N   1 
ATOM   12227 C  CA  . LEU L  1 8   ? -18.541 -11.089 15.284  1.00 52.36  ? 8   LEU W CA  1 
ATOM   12228 C  C   . LEU L  1 8   ? -19.883 -11.480 14.658  1.00 54.71  ? 8   LEU W C   1 
ATOM   12229 O  O   . LEU L  1 8   ? -20.383 -10.777 13.775  1.00 55.46  ? 8   LEU W O   1 
ATOM   12230 C  CB  . LEU L  1 8   ? -18.705 -9.804  16.106  1.00 50.31  ? 8   LEU W CB  1 
ATOM   12231 C  CG  . LEU L  1 8   ? -17.522 -9.424  16.997  1.00 48.16  ? 8   LEU W CG  1 
ATOM   12232 C  CD1 . LEU L  1 8   ? -17.603 -7.963  17.424  1.00 46.63  ? 8   LEU W CD1 1 
ATOM   12233 C  CD2 . LEU L  1 8   ? -17.458 -10.340 18.212  1.00 47.63  ? 8   LEU W CD2 1 
ATOM   12234 N  N   . LYS L  1 9   ? -20.431 -12.611 15.113  1.00 56.05  ? 9   LYS W N   1 
ATOM   12235 C  CA  . LYS L  1 9   ? -21.785 -13.065 14.763  1.00 58.51  ? 9   LYS W CA  1 
ATOM   12236 C  C   . LYS L  1 9   ? -22.454 -13.728 15.965  1.00 58.80  ? 9   LYS W C   1 
ATOM   12237 O  O   . LYS L  1 9   ? -21.783 -14.175 16.887  1.00 57.61  ? 9   LYS W O   1 
ATOM   12238 C  CB  . LYS L  1 9   ? -21.734 -14.091 13.625  1.00 61.20  ? 9   LYS W CB  1 
ATOM   12239 C  CG  . LYS L  1 9   ? -21.335 -13.535 12.268  1.00 61.83  ? 9   LYS W CG  1 
ATOM   12240 C  CD  . LYS L  1 9   ? -21.653 -14.528 11.154  1.00 65.03  ? 9   LYS W CD  1 
ATOM   12241 C  CE  . LYS L  1 9   ? -21.431 -13.926 9.777   1.00 65.96  ? 9   LYS W CE  1 
ATOM   12242 N  NZ  . LYS L  1 9   ? -21.904 -14.845 8.707   1.00 69.37  ? 9   LYS W NZ  1 
ATOM   12243 N  N   . GLY L  1 10  ? -23.779 -13.808 15.933  1.00 60.73  ? 10  GLY W N   1 
ATOM   12244 C  CA  . GLY L  1 10  ? -24.531 -14.584 16.919  1.00 61.86  ? 10  GLY W CA  1 
ATOM   12245 C  C   . GLY L  1 10  ? -25.971 -14.809 16.497  1.00 64.88  ? 10  GLY W C   1 
ATOM   12246 O  O   . GLY L  1 10  ? -26.282 -14.871 15.300  1.00 66.75  ? 10  GLY W O   1 
ATOM   12247 N  N   . ASP L  1 11  ? -26.844 -14.939 17.493  1.00 65.56  ? 11  ASP W N   1 
ATOM   12248 C  CA  . ASP L  1 11  ? -28.295 -14.984 17.282  1.00 68.39  ? 11  ASP W CA  1 
ATOM   12249 C  C   . ASP L  1 11  ? -28.818 -13.567 17.500  1.00 67.11  ? 11  ASP W C   1 
ATOM   12250 O  O   . ASP L  1 11  ? -28.321 -12.851 18.374  1.00 64.55  ? 11  ASP W O   1 
ATOM   12251 C  CB  . ASP L  1 11  ? -28.964 -15.951 18.265  1.00 70.14  ? 11  ASP W CB  1 
ATOM   12252 C  CG  . ASP L  1 11  ? -28.224 -17.268 18.389  1.00 70.92  ? 11  ASP W CG  1 
ATOM   12253 O  OD1 . ASP L  1 11  ? -27.706 -17.767 17.367  1.00 71.89  ? 11  ASP W OD1 1 
ATOM   12254 O  OD2 . ASP L  1 11  ? -28.151 -17.794 19.517  1.00 70.73  ? 11  ASP W OD2 1 
ATOM   12255 N  N   . GLY L  1 12  ? -29.817 -13.164 16.722  1.00 69.29  ? 12  GLY W N   1 
ATOM   12256 C  CA  . GLY L  1 12  ? -30.279 -11.773 16.730  1.00 68.37  ? 12  GLY W CA  1 
ATOM   12257 C  C   . GLY L  1 12  ? -29.394 -10.890 15.853  1.00 66.70  ? 12  GLY W C   1 
ATOM   12258 O  O   . GLY L  1 12  ? -28.509 -11.394 15.149  1.00 66.56  ? 12  GLY W O   1 
ATOM   12259 N  N   . PRO L  1 13  ? -29.607 -9.561  15.902  1.00 65.58  ? 13  PRO W N   1 
ATOM   12260 C  CA  . PRO L  1 13  ? -29.072 -8.663  14.874  1.00 64.93  ? 13  PRO W CA  1 
ATOM   12261 C  C   . PRO L  1 13  ? -27.592 -8.268  15.001  1.00 61.89  ? 13  PRO W C   1 
ATOM   12262 O  O   . PRO L  1 13  ? -27.053 -7.691  14.050  1.00 61.71  ? 13  PRO W O   1 
ATOM   12263 C  CB  . PRO L  1 13  ? -29.961 -7.425  15.021  1.00 65.31  ? 13  PRO W CB  1 
ATOM   12264 C  CG  . PRO L  1 13  ? -30.241 -7.377  16.485  1.00 64.12  ? 13  PRO W CG  1 
ATOM   12265 C  CD  . PRO L  1 13  ? -30.373 -8.814  16.920  1.00 65.17  ? 13  PRO W CD  1 
ATOM   12266 N  N   . VAL L  1 14  ? -26.938 -8.565  16.129  1.00 59.72  ? 14  VAL W N   1 
ATOM   12267 C  CA  . VAL L  1 14  ? -25.588 -8.039  16.368  1.00 56.95  ? 14  VAL W CA  1 
ATOM   12268 C  C   . VAL L  1 14  ? -24.542 -8.762  15.507  1.00 57.05  ? 14  VAL W C   1 
ATOM   12269 O  O   . VAL L  1 14  ? -24.400 -9.986  15.570  1.00 57.94  ? 14  VAL W O   1 
ATOM   12270 C  CB  . VAL L  1 14  ? -25.172 -8.056  17.862  1.00 54.75  ? 14  VAL W CB  1 
ATOM   12271 C  CG1 . VAL L  1 14  ? -23.838 -7.330  18.054  1.00 52.27  ? 14  VAL W CG1 1 
ATOM   12272 C  CG2 . VAL L  1 14  ? -26.252 -7.405  18.723  1.00 54.90  ? 14  VAL W CG2 1 
ATOM   12273 N  N   . GLN L  1 15  ? -23.834 -7.986  14.693  1.00 56.41  ? 15  GLN W N   1 
ATOM   12274 C  CA  . GLN L  1 15  ? -22.736 -8.498  13.875  1.00 56.52  ? 15  GLN W CA  1 
ATOM   12275 C  C   . GLN L  1 15  ? -21.691 -7.417  13.624  1.00 54.82  ? 15  GLN W C   1 
ATOM   12276 O  O   . GLN L  1 15  ? -21.980 -6.222  13.721  1.00 54.21  ? 15  GLN W O   1 
ATOM   12277 C  CB  . GLN L  1 15  ? -23.260 -9.042  12.536  1.00 59.40  ? 15  GLN W CB  1 
ATOM   12278 C  CG  . GLN L  1 15  ? -24.072 -8.055  11.686  1.00 60.83  ? 15  GLN W CG  1 
ATOM   12279 C  CD  . GLN L  1 15  ? -23.237 -7.159  10.773  1.00 60.56  ? 15  GLN W CD  1 
ATOM   12280 O  OE1 . GLN L  1 15  ? -22.068 -7.435  10.490  1.00 59.98  ? 15  GLN W OE1 1 
ATOM   12281 N  NE2 . GLN L  1 15  ? -23.848 -6.079  10.298  1.00 61.35  ? 15  GLN W NE2 1 
ATOM   12282 N  N   . GLY L  1 16  ? -20.479 -7.840  13.290  1.00 54.26  ? 16  GLY W N   1 
ATOM   12283 C  CA  . GLY L  1 16  ? -19.453 -6.889  12.881  1.00 53.23  ? 16  GLY W CA  1 
ATOM   12284 C  C   . GLY L  1 16  ? -18.090 -7.497  12.653  1.00 52.80  ? 16  GLY W C   1 
ATOM   12285 O  O   . GLY L  1 16  ? -17.885 -8.686  12.883  1.00 53.17  ? 16  GLY W O   1 
ATOM   12286 N  N   . ILE L  1 17  ? -17.171 -6.656  12.187  1.00 52.25  ? 17  ILE W N   1 
ATOM   12287 C  CA  . ILE L  1 17  ? -15.769 -7.019  11.989  1.00 51.90  ? 17  ILE W CA  1 
ATOM   12288 C  C   . ILE L  1 17  ? -14.925 -6.115  12.882  1.00 49.78  ? 17  ILE W C   1 
ATOM   12289 O  O   . ILE L  1 17  ? -15.103 -4.893  12.868  1.00 49.37  ? 17  ILE W O   1 
ATOM   12290 C  CB  . ILE L  1 17  ? -15.339 -6.840  10.513  1.00 53.76  ? 17  ILE W CB  1 
ATOM   12291 C  CG1 . ILE L  1 17  ? -16.178 -7.740  9.594   1.00 56.01  ? 17  ILE W CG1 1 
ATOM   12292 C  CG2 . ILE L  1 17  ? -13.846 -7.133  10.350  1.00 53.66  ? 17  ILE W CG2 1 
ATOM   12293 C  CD1 . ILE L  1 17  ? -16.224 -7.265  8.161   1.00 58.03  ? 17  ILE W CD1 1 
ATOM   12294 N  N   . ILE L  1 18  ? -14.034 -6.722  13.671  1.00 48.63  ? 18  ILE W N   1 
ATOM   12295 C  CA  . ILE L  1 18  ? -13.101 -5.991  14.514  1.00 46.88  ? 18  ILE W CA  1 
ATOM   12296 C  C   . ILE L  1 18  ? -11.671 -6.326  14.068  1.00 47.38  ? 18  ILE W C   1 
ATOM   12297 O  O   . ILE L  1 18  ? -11.317 -7.505  13.931  1.00 48.06  ? 18  ILE W O   1 
ATOM   12298 C  CB  . ILE L  1 18  ? -13.289 -6.349  16.012  1.00 45.24  ? 18  ILE W CB  1 
ATOM   12299 C  CG1 . ILE L  1 18  ? -14.736 -6.075  16.474  1.00 44.97  ? 18  ILE W CG1 1 
ATOM   12300 C  CG2 . ILE L  1 18  ? -12.273 -5.600  16.872  1.00 43.72  ? 18  ILE W CG2 1 
ATOM   12301 C  CD1 . ILE L  1 18  ? -15.161 -4.618  16.447  1.00 44.59  ? 18  ILE W CD1 1 
ATOM   12302 N  N   . ASN L  1 19  ? -10.871 -5.276  13.847  1.00 47.19  ? 19  ASN W N   1 
ATOM   12303 C  CA  . ASN L  1 19  ? -9.469  -5.382  13.402  1.00 47.91  ? 19  ASN W CA  1 
ATOM   12304 C  C   . ASN L  1 19  ? -8.530  -5.221  14.590  1.00 46.48  ? 19  ASN W C   1 
ATOM   12305 O  O   . ASN L  1 19  ? -8.794  -4.419  15.483  1.00 45.09  ? 19  ASN W O   1 
ATOM   12306 C  CB  . ASN L  1 19  ? -9.151  -4.290  12.374  1.00 49.06  ? 19  ASN W CB  1 
ATOM   12307 C  CG  . ASN L  1 19  ? -10.134 -4.272  11.227  1.00 50.54  ? 19  ASN W CG  1 
ATOM   12308 O  OD1 . ASN L  1 19  ? -10.113 -5.155  10.377  1.00 52.01  ? 19  ASN W OD1 1 
ATOM   12309 N  ND2 . ASN L  1 19  ? -11.015 -3.274  11.207  1.00 50.26  ? 19  ASN W ND2 1 
ATOM   12310 N  N   . PHE L  1 20  ? -7.440  -5.986  14.594  1.00 47.05  ? 20  PHE W N   1 
ATOM   12311 C  CA  . PHE L  1 20  ? -6.391  -5.872  15.601  1.00 46.14  ? 20  PHE W CA  1 
ATOM   12312 C  C   . PHE L  1 20  ? -5.067  -5.512  14.917  1.00 47.58  ? 20  PHE W C   1 
ATOM   12313 O  O   . PHE L  1 20  ? -4.749  -6.057  13.860  1.00 49.21  ? 20  PHE W O   1 
ATOM   12314 C  CB  . PHE L  1 20  ? -6.244  -7.181  16.360  1.00 45.82  ? 20  PHE W CB  1 
ATOM   12315 C  CG  . PHE L  1 20  ? -7.473  -7.591  17.131  1.00 44.67  ? 20  PHE W CG  1 
ATOM   12316 C  CD1 . PHE L  1 20  ? -7.656  -7.180  18.453  1.00 42.96  ? 20  PHE W CD1 1 
ATOM   12317 C  CD2 . PHE L  1 20  ? -8.434  -8.415  16.550  1.00 45.55  ? 20  PHE W CD2 1 
ATOM   12318 C  CE1 . PHE L  1 20  ? -8.782  -7.572  19.168  1.00 42.14  ? 20  PHE W CE1 1 
ATOM   12319 C  CE2 . PHE L  1 20  ? -9.555  -8.813  17.262  1.00 44.81  ? 20  PHE W CE2 1 
ATOM   12320 C  CZ  . PHE L  1 20  ? -9.734  -8.389  18.569  1.00 43.10  ? 20  PHE W CZ  1 
ATOM   12321 N  N   . GLU L  1 21  ? -4.310  -4.587  15.509  1.00 47.14  ? 21  GLU W N   1 
ATOM   12322 C  CA  . GLU L  1 21  ? -3.047  -4.122  14.906  1.00 48.85  ? 21  GLU W CA  1 
ATOM   12323 C  C   . GLU L  1 21  ? -1.994  -3.797  15.963  1.00 48.32  ? 21  GLU W C   1 
ATOM   12324 O  O   . GLU L  1 21  ? -2.170  -2.888  16.773  1.00 47.10  ? 21  GLU W O   1 
ATOM   12325 C  CB  . GLU L  1 21  ? -3.282  -2.904  13.996  1.00 49.87  ? 21  GLU W CB  1 
ATOM   12326 C  CG  . GLU L  1 21  ? -1.999  -2.358  13.369  1.00 51.91  ? 21  GLU W CG  1 
ATOM   12327 C  CD  . GLU L  1 21  ? -2.226  -1.462  12.160  1.00 53.63  ? 21  GLU W CD  1 
ATOM   12328 O  OE1 . GLU L  1 21  ? -3.347  -0.942  11.971  1.00 53.12  ? 21  GLU W OE1 1 
ATOM   12329 O  OE2 . GLU L  1 21  ? -1.258  -1.270  11.393  1.00 55.80  ? 21  GLU W OE2 1 
ATOM   12330 N  N   . GLN L  1 22  ? -0.895  -4.540  15.929  1.00 49.49  ? 22  GLN W N   1 
ATOM   12331 C  CA  . GLN L  1 22  ? 0.209   -4.337  16.852  1.00 49.53  ? 22  GLN W CA  1 
ATOM   12332 C  C   . GLN L  1 22  ? 1.481   -4.136  16.024  1.00 52.01  ? 22  GLN W C   1 
ATOM   12333 O  O   . GLN L  1 22  ? 2.047   -5.095  15.499  1.00 53.42  ? 22  GLN W O   1 
ATOM   12334 C  CB  . GLN L  1 22  ? 0.315   -5.537  17.799  1.00 48.74  ? 22  GLN W CB  1 
ATOM   12335 C  CG  . GLN L  1 22  ? 1.130   -5.279  19.050  1.00 48.21  ? 22  GLN W CG  1 
ATOM   12336 C  CD  . GLN L  1 22  ? 1.163   -6.472  19.992  1.00 47.61  ? 22  GLN W CD  1 
ATOM   12337 O  OE1 . GLN L  1 22  ? 0.758   -7.583  19.629  1.00 47.97  ? 22  GLN W OE1 1 
ATOM   12338 N  NE2 . GLN L  1 22  ? 1.633   -6.245  21.214  1.00 46.84  ? 22  GLN W NE2 1 
ATOM   12339 N  N   . LYS L  1 23  ? 1.894   -2.874  15.894  1.00 52.77  ? 23  LYS W N   1 
ATOM   12340 C  CA  . LYS L  1 23  ? 3.066   -2.497  15.093  1.00 55.46  ? 23  LYS W CA  1 
ATOM   12341 C  C   . LYS L  1 23  ? 4.375   -3.038  15.678  1.00 56.58  ? 23  LYS W C   1 
ATOM   12342 O  O   . LYS L  1 23  ? 5.218   -3.531  14.938  1.00 58.78  ? 23  LYS W O   1 
ATOM   12343 C  CB  . LYS L  1 23  ? 3.163   -0.970  14.948  1.00 56.11  ? 23  LYS W CB  1 
ATOM   12344 C  CG  A LYS L  1 23  ? 2.042   -0.341  14.141  0.50 55.86  ? 23  LYS W CG  1 
ATOM   12345 C  CD  A LYS L  1 23  ? 2.291   1.144   13.924  0.50 57.12  ? 23  LYS W CD  1 
ATOM   12346 C  CE  A LYS L  1 23  ? 1.078   1.823   13.310  0.50 56.76  ? 23  LYS W CE  1 
ATOM   12347 N  NZ  A LYS L  1 23  ? -0.125  1.636   14.164  0.50 54.01  ? 23  LYS W NZ  1 
ATOM   12348 N  N   . GLU L  1 24  ? 4.528   -2.936  16.999  1.00 55.25  ? 24  GLU W N   1 
ATOM   12349 C  CA  . GLU L  1 24  ? 5.701   -3.447  17.715  1.00 56.29  ? 24  GLU W CA  1 
ATOM   12350 C  C   . GLU L  1 24  ? 5.259   -4.507  18.722  1.00 54.57  ? 24  GLU W C   1 
ATOM   12351 O  O   . GLU L  1 24  ? 4.308   -4.273  19.472  1.00 52.27  ? 24  GLU W O   1 
ATOM   12352 C  CB  . GLU L  1 24  ? 6.402   -2.310  18.467  1.00 56.72  ? 24  GLU W CB  1 
ATOM   12353 C  CG  . GLU L  1 24  ? 6.727   -1.068  17.641  1.00 58.54  ? 24  GLU W CG  1 
ATOM   12354 C  CD  . GLU L  1 24  ? 7.800   -1.285  16.583  0.50 61.67  ? 24  GLU W CD  1 
ATOM   12355 O  OE1 . GLU L  1 24  ? 8.427   -2.366  16.536  0.50 62.59  ? 24  GLU W OE1 1 
ATOM   12356 O  OE2 . GLU L  1 24  ? 8.023   -0.350  15.789  0.50 63.43  ? 24  GLU W OE2 1 
ATOM   12357 N  N   . SER L  1 25  ? 5.962   -5.646  18.766  1.00 55.87  ? 25  SER W N   1 
ATOM   12358 C  CA  . SER L  1 25  ? 5.599   -6.778  19.655  1.00 54.67  ? 25  SER W CA  1 
ATOM   12359 C  C   . SER L  1 25  ? 5.430   -6.395  21.125  1.00 52.91  ? 25  SER W C   1 
ATOM   12360 O  O   . SER L  1 25  ? 4.556   -6.933  21.818  1.00 51.20  ? 25  SER W O   1 
ATOM   12361 C  CB  . SER L  1 25  ? 6.627   -7.911  19.541  1.00 56.84  ? 25  SER W CB  1 
ATOM   12362 O  OG  . SER L  1 25  ? 7.947   -7.435  19.748  1.00 58.68  ? 25  SER W OG  1 
ATOM   12363 N  N   . ASN L  1 26  ? 6.255   -5.460  21.595  1.00 53.60  ? 26  ASN W N   1 
ATOM   12364 C  CA  . ASN L  1 26  ? 6.169   -4.964  22.988  1.00 52.13  ? 26  ASN W CA  1 
ATOM   12365 C  C   . ASN L  1 26  ? 5.077   -3.906  23.248  1.00 50.01  ? 26  ASN W C   1 
ATOM   12366 O  O   . ASN L  1 26  ? 4.867   -3.520  24.400  1.00 48.87  ? 26  ASN W O   1 
ATOM   12367 C  CB  . ASN L  1 26  ? 7.534   -4.424  23.455  1.00 54.11  ? 26  ASN W CB  1 
ATOM   12368 C  CG  . ASN L  1 26  ? 8.087   -3.321  22.554  1.00 56.00  ? 26  ASN W CG  1 
ATOM   12369 O  OD1 . ASN L  1 26  ? 7.494   -2.977  21.526  1.00 56.06  ? 26  ASN W OD1 1 
ATOM   12370 N  ND2 . ASN L  1 26  ? 9.243   -2.780  22.926  1.00 57.92  ? 26  ASN W ND2 1 
ATOM   12371 N  N   . GLY L  1 27  ? 4.362   -3.476  22.206  1.00 49.67  ? 27  GLY W N   1 
ATOM   12372 C  CA  . GLY L  1 27  ? 3.574   -2.245  22.245  1.00 48.41  ? 27  GLY W CA  1 
ATOM   12373 C  C   . GLY L  1 27  ? 2.065   -2.424  22.202  1.00 46.23  ? 27  GLY W C   1 
ATOM   12374 O  O   . GLY L  1 27  ? 1.562   -3.555  22.176  1.00 45.60  ? 27  GLY W O   1 
ATOM   12375 N  N   . PRO L  1 28  ? 1.328   -1.297  22.180  1.00 45.30  ? 28  PRO W N   1 
ATOM   12376 C  CA  . PRO L  1 28  ? -0.139  -1.354  22.235  1.00 43.46  ? 28  PRO W CA  1 
ATOM   12377 C  C   . PRO L  1 28  ? -0.776  -2.044  21.032  1.00 43.68  ? 28  PRO W C   1 
ATOM   12378 O  O   . PRO L  1 28  ? -0.198  -2.055  19.946  1.00 45.35  ? 28  PRO W O   1 
ATOM   12379 C  CB  . PRO L  1 28  ? -0.564  0.125   22.304  1.00 43.32  ? 28  PRO W CB  1 
ATOM   12380 C  CG  . PRO L  1 28  ? 0.618   0.910   21.854  1.00 45.38  ? 28  PRO W CG  1 
ATOM   12381 C  CD  . PRO L  1 28  ? 1.835   0.090   22.154  1.00 46.30  ? 28  PRO W CD  1 
ATOM   12382 N  N   . VAL L  1 29  ? -1.948  -2.631  21.257  1.00 42.14  ? 29  VAL W N   1 
ATOM   12383 C  CA  . VAL L  1 29  ? -2.757  -3.237  20.206  1.00 42.38  ? 29  VAL W CA  1 
ATOM   12384 C  C   . VAL L  1 29  ? -3.911  -2.273  19.915  1.00 41.79  ? 29  VAL W C   1 
ATOM   12385 O  O   . VAL L  1 29  ? -4.702  -1.983  20.806  1.00 40.32  ? 29  VAL W O   1 
ATOM   12386 C  CB  . VAL L  1 29  ? -3.343  -4.589  20.659  1.00 41.55  ? 29  VAL W CB  1 
ATOM   12387 C  CG1 . VAL L  1 29  ? -4.185  -5.222  19.557  1.00 42.19  ? 29  VAL W CG1 1 
ATOM   12388 C  CG2 . VAL L  1 29  ? -2.234  -5.528  21.110  1.00 42.21  ? 29  VAL W CG2 1 
ATOM   12389 N  N   . LYS L  1 30  ? -3.995  -1.766  18.683  1.00 43.08  ? 30  LYS W N   1 
ATOM   12390 C  CA  . LYS L  1 30  ? -5.167  -0.996  18.253  1.00 42.93  ? 30  LYS W CA  1 
ATOM   12391 C  C   . LYS L  1 30  ? -6.304  -1.953  17.872  1.00 42.56  ? 30  LYS W C   1 
ATOM   12392 O  O   . LYS L  1 30  ? -6.087  -2.932  17.175  1.00 43.42  ? 30  LYS W O   1 
ATOM   12393 C  CB  . LYS L  1 30  ? -4.833  -0.058  17.091  1.00 44.75  ? 30  LYS W CB  1 
ATOM   12394 C  CG  . LYS L  1 30  ? -3.832  1.034   17.451  1.00 45.45  ? 30  LYS W CG  1 
ATOM   12395 C  CD  . LYS L  1 30  ? -3.915  2.219   16.492  1.00 47.14  ? 30  LYS W CD  1 
ATOM   12396 C  CE  . LYS L  1 30  ? -2.591  2.963   16.373  1.00 48.86  ? 30  LYS W CE  1 
ATOM   12397 N  NZ  . LYS L  1 30  ? -2.060  3.432   17.682  1.00 48.08  ? 30  LYS W NZ  1 
ATOM   12398 N  N   . VAL L  1 31  ? -7.504  -1.661  18.365  1.00 41.50  ? 31  VAL W N   1 
ATOM   12399 C  CA  . VAL L  1 31  ? -8.704  -2.455  18.098  1.00 41.40  ? 31  VAL W CA  1 
ATOM   12400 C  C   . VAL L  1 31  ? -9.739  -1.503  17.496  1.00 41.89  ? 31  VAL W C   1 
ATOM   12401 O  O   . VAL L  1 31  ? -10.099 -0.500  18.119  1.00 41.21  ? 31  VAL W O   1 
ATOM   12402 C  CB  . VAL L  1 31  ? -9.272  -3.097  19.381  1.00 39.93  ? 31  VAL W CB  1 
ATOM   12403 C  CG1 . VAL L  1 31  ? -10.378 -4.094  19.046  1.00 40.26  ? 31  VAL W CG1 1 
ATOM   12404 C  CG2 . VAL L  1 31  ? -8.169  -3.782  20.183  1.00 39.48  ? 31  VAL W CG2 1 
ATOM   12405 N  N   . TRP L  1 32  ? -10.199 -1.795  16.283  1.00 43.28  ? 32  TRP W N   1 
ATOM   12406 C  CA  . TRP L  1 32  ? -11.184 -0.927  15.622  1.00 44.10  ? 32  TRP W CA  1 
ATOM   12407 C  C   . TRP L  1 32  ? -12.095 -1.668  14.652  1.00 45.30  ? 32  TRP W C   1 
ATOM   12408 O  O   . TRP L  1 32  ? -11.720 -2.683  14.075  1.00 46.01  ? 32  TRP W O   1 
ATOM   12409 C  CB  . TRP L  1 32  ? -10.491 0.264   14.927  1.00 45.26  ? 32  TRP W CB  1 
ATOM   12410 C  CG  . TRP L  1 32  ? -9.647  -0.092  13.717  1.00 46.96  ? 32  TRP W CG  1 
ATOM   12411 C  CD1 . TRP L  1 32  ? -8.344  -0.524  13.714  1.00 47.26  ? 32  TRP W CD1 1 
ATOM   12412 C  CD2 . TRP L  1 32  ? -10.049 -0.031  12.346  1.00 48.83  ? 32  TRP W CD2 1 
ATOM   12413 N  NE1 . TRP L  1 32  ? -7.917  -0.737  12.422  1.00 49.18  ? 32  TRP W NE1 1 
ATOM   12414 C  CE2 . TRP L  1 32  ? -8.941  -0.443  11.563  1.00 50.16  ? 32  TRP W CE2 1 
ATOM   12415 C  CE3 . TRP L  1 32  ? -11.239 0.329   11.697  1.00 49.73  ? 32  TRP W CE3 1 
ATOM   12416 C  CZ2 . TRP L  1 32  ? -8.992  -0.508  10.166  1.00 52.28  ? 32  TRP W CZ2 1 
ATOM   12417 C  CZ3 . TRP L  1 32  ? -11.288 0.268   10.299  1.00 51.84  ? 32  TRP W CZ3 1 
ATOM   12418 C  CH2 . TRP L  1 32  ? -10.170 -0.147  9.553   1.00 53.06  ? 32  TRP W CH2 1 
ATOM   12419 N  N   . GLY L  1 33  ? -13.297 -1.128  14.482  1.00 45.82  ? 33  GLY W N   1 
ATOM   12420 C  CA  . GLY L  1 33  ? -14.282 -1.677  13.550  1.00 47.33  ? 33  GLY W CA  1 
ATOM   12421 C  C   . GLY L  1 33  ? -15.669 -1.123  13.796  1.00 47.56  ? 33  GLY W C   1 
ATOM   12422 O  O   . GLY L  1 33  ? -15.832 -0.137  14.524  1.00 46.74  ? 33  GLY W O   1 
ATOM   12423 N  N   . SER L  1 34  ? -16.665 -1.767  13.190  1.00 48.93  ? 34  SER W N   1 
ATOM   12424 C  CA  . SER L  1 34  ? -18.066 -1.349  13.303  1.00 49.59  ? 34  SER W CA  1 
ATOM   12425 C  C   . SER L  1 34  ? -18.970 -2.549  13.622  1.00 49.91  ? 34  SER W C   1 
ATOM   12426 O  O   . SER L  1 34  ? -19.138 -3.445  12.798  1.00 51.34  ? 34  SER W O   1 
ATOM   12427 C  CB  . SER L  1 34  ? -18.512 -0.660  12.013  1.00 51.69  ? 34  SER W CB  1 
ATOM   12428 O  OG  . SER L  1 34  ? -19.824 -0.130  12.133  1.00 52.46  ? 34  SER W OG  1 
ATOM   12429 N  N   . ILE L  1 35  ? -19.539 -2.553  14.826  1.00 48.83  ? 35  ILE W N   1 
ATOM   12430 C  CA  . ILE L  1 35  ? -20.518 -3.558  15.241  1.00 49.36  ? 35  ILE W CA  1 
ATOM   12431 C  C   . ILE L  1 35  ? -21.896 -2.949  15.012  1.00 50.76  ? 35  ILE W C   1 
ATOM   12432 O  O   . ILE L  1 35  ? -22.138 -1.815  15.416  1.00 50.33  ? 35  ILE W O   1 
ATOM   12433 C  CB  . ILE L  1 35  ? -20.376 -3.932  16.736  1.00 47.62  ? 35  ILE W CB  1 
ATOM   12434 C  CG1 . ILE L  1 35  ? -18.920 -4.290  17.079  1.00 46.18  ? 35  ILE W CG1 1 
ATOM   12435 C  CG2 . ILE L  1 35  ? -21.316 -5.092  17.086  1.00 48.55  ? 35  ILE W CG2 1 
ATOM   12436 C  CD1 . ILE L  1 35  ? -18.592 -4.223  18.555  1.00 44.34  ? 35  ILE W CD1 1 
ATOM   12437 N  N   . LYS L  1 36  ? -22.784 -3.701  14.366  1.00 52.69  ? 36  LYS W N   1 
ATOM   12438 C  CA  . LYS L  1 36  ? -24.160 -3.263  14.091  1.00 54.46  ? 36  LYS W CA  1 
ATOM   12439 C  C   . LYS L  1 36  ? -25.167 -4.104  14.862  1.00 54.98  ? 36  LYS W C   1 
ATOM   12440 O  O   . LYS L  1 36  ? -24.806 -5.116  15.449  1.00 54.18  ? 36  LYS W O   1 
ATOM   12441 C  CB  . LYS L  1 36  ? -24.436 -3.326  12.581  1.00 56.85  ? 36  LYS W CB  1 
ATOM   12442 C  CG  . LYS L  1 36  ? -23.907 -2.105  11.841  1.00 57.03  ? 36  LYS W CG  1 
ATOM   12443 C  CD  . LYS L  1 36  ? -23.077 -2.467  10.624  1.00 58.00  ? 36  LYS W CD  1 
ATOM   12444 C  CE  . LYS L  1 36  ? -22.367 -1.243  10.051  1.00 58.02  ? 36  LYS W CE  1 
ATOM   12445 N  NZ  . LYS L  1 36  ? -20.969 -1.563  9.653   1.00 57.38  ? 36  LYS W NZ  1 
ATOM   12446 N  N   . GLY L  1 37  ? -26.420 -3.649  14.870  1.00 56.50  ? 37  GLY W N   1 
ATOM   12447 C  CA  . GLY L  1 37  ? -27.527 -4.357  15.521  1.00 57.61  ? 37  GLY W CA  1 
ATOM   12448 C  C   . GLY L  1 37  ? -27.680 -4.136  17.022  1.00 56.01  ? 37  GLY W C   1 
ATOM   12449 O  O   . GLY L  1 37  ? -28.566 -4.737  17.635  1.00 57.04  ? 37  GLY W O   1 
ATOM   12450 N  N   . LEU L  1 38  ? -26.856 -3.265  17.611  1.00 53.72  ? 38  LEU W N   1 
ATOM   12451 C  CA  . LEU L  1 38  ? -26.837 -3.076  19.069  1.00 52.14  ? 38  LEU W CA  1 
ATOM   12452 C  C   . LEU L  1 38  ? -27.926 -2.108  19.520  1.00 53.06  ? 38  LEU W C   1 
ATOM   12453 O  O   . LEU L  1 38  ? -28.316 -1.223  18.766  1.00 54.29  ? 38  LEU W O   1 
ATOM   12454 C  CB  . LEU L  1 38  ? -25.472 -2.544  19.543  1.00 49.56  ? 38  LEU W CB  1 
ATOM   12455 C  CG  . LEU L  1 38  ? -24.293 -3.518  19.501  1.00 48.38  ? 38  LEU W CG  1 
ATOM   12456 C  CD1 . LEU L  1 38  ? -22.974 -2.759  19.578  1.00 46.54  ? 38  LEU W CD1 1 
ATOM   12457 C  CD2 . LEU L  1 38  ? -24.389 -4.548  20.619  1.00 47.82  ? 38  LEU W CD2 1 
ATOM   12458 N  N   . THR L  1 39  ? -28.402 -2.285  20.753  1.00 52.71  ? 39  THR W N   1 
ATOM   12459 C  CA  . THR L  1 39  ? -29.232 -1.273  21.422  1.00 53.19  ? 39  THR W CA  1 
ATOM   12460 C  C   . THR L  1 39  ? -28.341 -0.083  21.766  1.00 51.27  ? 39  THR W C   1 
ATOM   12461 O  O   . THR L  1 39  ? -27.164 -0.262  22.118  1.00 49.11  ? 39  THR W O   1 
ATOM   12462 C  CB  . THR L  1 39  ? -29.843 -1.777  22.748  1.00 53.24  ? 39  THR W CB  1 
ATOM   12463 O  OG1 . THR L  1 39  ? -28.792 -2.073  23.676  1.00 50.79  ? 39  THR W OG1 1 
ATOM   12464 C  CG2 . THR L  1 39  ? -30.692 -3.018  22.530  1.00 55.35  ? 39  THR W CG2 1 
ATOM   12465 N  N   . GLU L  1 40  ? -28.901 1.121   21.679  1.00 52.18  ? 40  GLU W N   1 
ATOM   12466 C  CA  . GLU L  1 40  ? -28.170 2.334   22.056  1.00 50.83  ? 40  GLU W CA  1 
ATOM   12467 C  C   . GLU L  1 40  ? -27.594 2.192   23.475  1.00 48.71  ? 40  GLU W C   1 
ATOM   12468 O  O   . GLU L  1 40  ? -28.243 1.627   24.361  1.00 48.90  ? 40  GLU W O   1 
ATOM   12469 C  CB  . GLU L  1 40  ? -29.091 3.557   21.977  1.00 52.62  ? 40  GLU W CB  1 
ATOM   12470 C  CG  . GLU L  1 40  ? -28.385 4.902   22.102  1.00 51.93  ? 40  GLU W CG  1 
ATOM   12471 C  CD  . GLU L  1 40  ? -29.346 6.089   22.085  1.00 54.09  ? 40  GLU W CD  1 
ATOM   12472 O  OE1 . GLU L  1 40  ? -30.586 5.896   22.031  1.00 56.04  ? 40  GLU W OE1 1 
ATOM   12473 O  OE2 . GLU L  1 40  ? -28.847 7.233   22.131  1.00 54.02  ? 40  GLU W OE2 1 
ATOM   12474 N  N   . GLY L  1 41  ? -26.369 2.677   23.669  1.00 46.88  ? 41  GLY W N   1 
ATOM   12475 C  CA  . GLY L  1 41  ? -25.724 2.680   24.989  1.00 44.99  ? 41  GLY W CA  1 
ATOM   12476 C  C   . GLY L  1 41  ? -24.567 1.707   25.139  1.00 43.22  ? 41  GLY W C   1 
ATOM   12477 O  O   . GLY L  1 41  ? -23.961 1.281   24.145  1.00 43.18  ? 41  GLY W O   1 
ATOM   12478 N  N   . LEU L  1 42  ? -24.269 1.351   26.394  1.00 41.93  ? 42  LEU W N   1 
ATOM   12479 C  CA  . LEU L  1 42  ? -23.037 0.625   26.746  1.00 40.20  ? 42  LEU W CA  1 
ATOM   12480 C  C   . LEU L  1 42  ? -23.159 -0.893  26.645  1.00 40.38  ? 42  LEU W C   1 
ATOM   12481 O  O   . LEU L  1 42  ? -24.140 -1.471  27.094  1.00 41.23  ? 42  LEU W O   1 
ATOM   12482 C  CB  . LEU L  1 42  ? -22.591 0.992   28.169  1.00 38.98  ? 42  LEU W CB  1 
ATOM   12483 C  CG  . LEU L  1 42  ? -21.971 2.379   28.359  1.00 38.49  ? 42  LEU W CG  1 
ATOM   12484 C  CD1 . LEU L  1 42  ? -21.971 2.758   29.833  1.00 37.90  ? 42  LEU W CD1 1 
ATOM   12485 C  CD2 . LEU L  1 42  ? -20.549 2.425   27.816  1.00 37.55  ? 42  LEU W CD2 1 
ATOM   12486 N  N   . HIS L  1 43  ? -22.127 -1.534  26.093  1.00 39.69  ? 43  HIS W N   1 
ATOM   12487 C  CA  . HIS L  1 43  ? -22.095 -2.993  25.950  1.00 40.11  ? 43  HIS W CA  1 
ATOM   12488 C  C   . HIS L  1 43  ? -20.744 -3.570  26.327  1.00 38.72  ? 43  HIS W C   1 
ATOM   12489 O  O   . HIS L  1 43  ? -19.721 -3.131  25.804  1.00 37.98  ? 43  HIS W O   1 
ATOM   12490 C  CB  . HIS L  1 43  ? -22.412 -3.372  24.507  1.00 41.55  ? 43  HIS W CB  1 
ATOM   12491 C  CG  . HIS L  1 43  ? -23.808 -3.032  24.103  1.00 43.33  ? 43  HIS W CG  1 
ATOM   12492 N  ND1 . HIS L  1 43  ? -24.879 -3.851  24.384  1.00 44.78  ? 43  HIS W ND1 1 
ATOM   12493 C  CD2 . HIS L  1 43  ? -24.316 -1.945  23.475  1.00 44.15  ? 43  HIS W CD2 1 
ATOM   12494 C  CE1 . HIS L  1 43  ? -25.983 -3.297  23.919  1.00 46.41  ? 43  HIS W CE1 1 
ATOM   12495 N  NE2 . HIS L  1 43  ? -25.671 -2.139  23.364  1.00 46.03  ? 43  HIS W NE2 1 
ATOM   12496 N  N   . GLY L  1 44  ? -20.752 -4.567  27.210  1.00 38.68  ? 44  GLY W N   1 
ATOM   12497 C  CA  . GLY L  1 44  ? -19.530 -5.265  27.621  1.00 37.83  ? 44  GLY W CA  1 
ATOM   12498 C  C   . GLY L  1 44  ? -18.830 -5.872  26.415  1.00 38.33  ? 44  GLY W C   1 
ATOM   12499 O  O   . GLY L  1 44  ? -19.480 -6.270  25.449  1.00 39.74  ? 44  GLY W O   1 
ATOM   12500 N  N   . PHE L  1 45  ? -17.508 -5.914  26.474  1.00 37.47  ? 45  PHE W N   1 
ATOM   12501 C  CA  . PHE L  1 45  ? -16.664 -6.239  25.332  1.00 37.92  ? 45  PHE W CA  1 
ATOM   12502 C  C   . PHE L  1 45  ? -15.440 -6.965  25.878  1.00 37.35  ? 45  PHE W C   1 
ATOM   12503 O  O   . PHE L  1 45  ? -14.535 -6.338  26.405  1.00 36.30  ? 45  PHE W O   1 
ATOM   12504 C  CB  . PHE L  1 45  ? -16.274 -4.933  24.630  1.00 37.61  ? 45  PHE W CB  1 
ATOM   12505 C  CG  . PHE L  1 45  ? -15.636 -5.104  23.275  1.00 38.44  ? 45  PHE W CG  1 
ATOM   12506 C  CD1 . PHE L  1 45  ? -16.271 -5.826  22.264  1.00 39.94  ? 45  PHE W CD1 1 
ATOM   12507 C  CD2 . PHE L  1 45  ? -14.436 -4.459  22.979  1.00 38.04  ? 45  PHE W CD2 1 
ATOM   12508 C  CE1 . PHE L  1 45  ? -15.698 -5.941  21.005  1.00 40.82  ? 45  PHE W CE1 1 
ATOM   12509 C  CE2 . PHE L  1 45  ? -13.854 -4.577  21.722  1.00 38.99  ? 45  PHE W CE2 1 
ATOM   12510 C  CZ  . PHE L  1 45  ? -14.492 -5.310  20.733  1.00 40.35  ? 45  PHE W CZ  1 
ATOM   12511 N  N   . HIS L  1 46  ? -15.441 -8.291  25.779  1.00 38.34  ? 46  HIS W N   1 
ATOM   12512 C  CA  . HIS L  1 46  ? -14.419 -9.127  26.425  1.00 38.12  ? 46  HIS W CA  1 
ATOM   12513 C  C   . HIS L  1 46  ? -13.756 -10.094 25.449  1.00 39.30  ? 46  HIS W C   1 
ATOM   12514 O  O   . HIS L  1 46  ? -14.356 -10.492 24.453  1.00 40.52  ? 46  HIS W O   1 
ATOM   12515 C  CB  . HIS L  1 46  ? -15.034 -9.944  27.570  1.00 38.46  ? 46  HIS W CB  1 
ATOM   12516 C  CG  . HIS L  1 46  ? -15.818 -9.128  28.550  1.00 37.65  ? 46  HIS W CG  1 
ATOM   12517 N  ND1 . HIS L  1 46  ? -17.052 -9.518  29.023  1.00 38.52  ? 46  HIS W ND1 1 
ATOM   12518 C  CD2 . HIS L  1 46  ? -15.549 -7.936  29.136  1.00 36.30  ? 46  HIS W CD2 1 
ATOM   12519 C  CE1 . HIS L  1 46  ? -17.505 -8.607  29.866  1.00 37.69  ? 46  HIS W CE1 1 
ATOM   12520 N  NE2 . HIS L  1 46  ? -16.614 -7.635  29.949  1.00 36.31  ? 46  HIS W NE2 1 
ATOM   12521 N  N   . VAL L  1 47  ? -12.509 -10.459 25.745  1.00 39.05  ? 47  VAL W N   1 
ATOM   12522 C  CA  . VAL L  1 47  ? -11.896 -11.633 25.153  1.00 40.40  ? 47  VAL W CA  1 
ATOM   12523 C  C   . VAL L  1 47  ? -12.119 -12.765 26.152  1.00 41.06  ? 47  VAL W C   1 
ATOM   12524 O  O   . VAL L  1 47  ? -11.619 -12.707 27.281  1.00 40.20  ? 47  VAL W O   1 
ATOM   12525 C  CB  . VAL L  1 47  ? -10.398 -11.435 24.871  1.00 40.22  ? 47  VAL W CB  1 
ATOM   12526 C  CG1 . VAL L  1 47  ? -9.782  -12.704 24.286  1.00 41.95  ? 47  VAL W CG1 1 
ATOM   12527 C  CG2 . VAL L  1 47  ? -10.187 -10.247 23.940  1.00 39.79  ? 47  VAL W CG2 1 
ATOM   12528 N  N   . HIS L  1 48  ? -12.894 -13.770 25.749  1.00 42.73  ? 48  HIS W N   1 
ATOM   12529 C  CA  . HIS L  1 48  ? -13.102 -14.970 26.561  1.00 43.96  ? 48  HIS W CA  1 
ATOM   12530 C  C   . HIS L  1 48  ? -12.030 -16.013 26.217  1.00 45.42  ? 48  HIS W C   1 
ATOM   12531 O  O   . HIS L  1 48  ? -11.400 -15.936 25.156  1.00 45.82  ? 48  HIS W O   1 
ATOM   12532 C  CB  . HIS L  1 48  ? -14.512 -15.533 26.370  1.00 45.41  ? 48  HIS W CB  1 
ATOM   12533 C  CG  . HIS L  1 48  ? -15.579 -14.714 27.027  1.00 44.40  ? 48  HIS W CG  1 
ATOM   12534 N  ND1 . HIS L  1 48  ? -16.398 -15.215 28.017  1.00 45.11  ? 48  HIS W ND1 1 
ATOM   12535 C  CD2 . HIS L  1 48  ? -15.954 -13.426 26.846  1.00 42.96  ? 48  HIS W CD2 1 
ATOM   12536 C  CE1 . HIS L  1 48  ? -17.234 -14.272 28.412  1.00 44.15  ? 48  HIS W CE1 1 
ATOM   12537 N  NE2 . HIS L  1 48  ? -16.984 -13.176 27.721  1.00 42.83  ? 48  HIS W NE2 1 
ATOM   12538 N  N   . GLU L  1 49  ? -11.850 -16.983 27.112  1.00 46.43  ? 49  GLU W N   1 
ATOM   12539 C  CA  . GLU L  1 49  ? -10.650 -17.841 27.138  1.00 47.66  ? 49  GLU W CA  1 
ATOM   12540 C  C   . GLU L  1 49  ? -10.409 -18.673 25.868  1.00 49.77  ? 49  GLU W C   1 
ATOM   12541 O  O   . GLU L  1 49  ? -9.313  -18.652 25.294  1.00 49.98  ? 49  GLU W O   1 
ATOM   12542 C  CB  . GLU L  1 49  ? -10.695 -18.763 28.366  1.00 48.68  ? 49  GLU W CB  1 
ATOM   12543 C  CG  . GLU L  1 49  ? -9.397  -19.527 28.636  1.00 49.83  ? 49  GLU W CG  1 
ATOM   12544 C  CD  . GLU L  1 49  ? -9.398  -20.292 29.954  1.00 50.76  ? 49  GLU W CD  1 
ATOM   12545 O  OE1 . GLU L  1 49  ? -10.062 -19.854 30.915  1.00 49.75  ? 49  GLU W OE1 1 
ATOM   12546 O  OE2 . GLU L  1 49  ? -8.713  -21.336 30.034  1.00 52.77  ? 49  GLU W OE2 1 
ATOM   12547 N  N   . PHE L  1 50  ? -11.438 -19.391 25.435  1.00 51.53  ? 50  PHE W N   1 
ATOM   12548 C  CA  . PHE L  1 50  ? -11.317 -20.352 24.339  1.00 53.98  ? 50  PHE W CA  1 
ATOM   12549 C  C   . PHE L  1 50  ? -11.789 -19.762 23.005  1.00 53.96  ? 50  PHE W C   1 
ATOM   12550 O  O   . PHE L  1 50  ? -12.652 -18.882 22.974  1.00 52.62  ? 50  PHE W O   1 
ATOM   12551 C  CB  . PHE L  1 50  ? -12.118 -21.616 24.680  1.00 56.47  ? 50  PHE W CB  1 
ATOM   12552 C  CG  . PHE L  1 50  ? -11.803 -22.184 26.043  1.00 56.74  ? 50  PHE W CG  1 
ATOM   12553 C  CD1 . PHE L  1 50  ? -10.548 -22.730 26.311  1.00 57.43  ? 50  PHE W CD1 1 
ATOM   12554 C  CD2 . PHE L  1 50  ? -12.756 -22.177 27.062  1.00 56.54  ? 50  PHE W CD2 1 
ATOM   12555 C  CE1 . PHE L  1 50  ? -10.250 -23.252 27.566  1.00 57.88  ? 50  PHE W CE1 1 
ATOM   12556 C  CE2 . PHE L  1 50  ? -12.464 -22.701 28.316  1.00 56.97  ? 50  PHE W CE2 1 
ATOM   12557 C  CZ  . PHE L  1 50  ? -11.208 -23.235 28.570  1.00 57.62  ? 50  PHE W CZ  1 
ATOM   12558 N  N   . GLY L  1 51  ? -11.211 -20.253 21.908  1.00 55.61  ? 51  GLY W N   1 
ATOM   12559 C  CA  . GLY L  1 51  ? -11.736 -20.003 20.559  1.00 56.48  ? 51  GLY W CA  1 
ATOM   12560 C  C   . GLY L  1 51  ? -12.742 -21.055 20.123  1.00 59.24  ? 51  GLY W C   1 
ATOM   12561 O  O   . GLY L  1 51  ? -12.692 -21.523 18.985  1.00 61.21  ? 51  GLY W O   1 
ATOM   12562 N  N   . ASP L  1 52  ? -13.659 -21.410 21.026  1.00 59.62  ? 52  ASP W N   1 
ATOM   12563 C  CA  . ASP L  1 52  ? -14.618 -22.488 20.820  1.00 62.56  ? 52  ASP W CA  1 
ATOM   12564 C  C   . ASP L  1 52  ? -15.969 -21.855 20.469  1.00 62.44  ? 52  ASP W C   1 
ATOM   12565 O  O   . ASP L  1 52  ? -16.649 -21.303 21.340  1.00 61.06  ? 52  ASP W O   1 
ATOM   12566 C  CB  . ASP L  1 52  ? -14.713 -23.334 22.092  1.00 63.44  ? 52  ASP W CB  1 
ATOM   12567 C  CG  . ASP L  1 52  ? -15.489 -24.626 21.896  1.00 67.08  ? 52  ASP W CG  1 
ATOM   12568 O  OD1 . ASP L  1 52  ? -16.153 -24.810 20.851  1.00 68.81  ? 52  ASP W OD1 1 
ATOM   12569 O  OD2 . ASP L  1 52  ? -15.433 -25.470 22.814  1.00 68.48  ? 52  ASP W OD2 1 
ATOM   12570 N  N   . ASN L  1 53  ? -16.330 -21.922 19.186  1.00 64.03  ? 53  ASN W N   1 
ATOM   12571 C  CA  . ASN L  1 53  ? -17.589 -21.364 18.672  1.00 64.39  ? 53  ASN W CA  1 
ATOM   12572 C  C   . ASN L  1 53  ? -18.572 -22.481 18.252  1.00 68.03  ? 53  ASN W C   1 
ATOM   12573 O  O   . ASN L  1 53  ? -19.360 -22.299 17.316  1.00 69.32  ? 53  ASN W O   1 
ATOM   12574 C  CB  . ASN L  1 53  ? -17.281 -20.414 17.494  1.00 63.45  ? 53  ASN W CB  1 
ATOM   12575 C  CG  . ASN L  1 53  ? -18.349 -19.346 17.284  1.00 62.53  ? 53  ASN W CG  1 
ATOM   12576 O  OD1 . ASN L  1 53  ? -18.978 -19.293 16.232  1.00 64.15  ? 53  ASN W OD1 1 
ATOM   12577 N  ND2 . ASN L  1 53  ? -18.541 -18.481 18.279  1.00 60.19  ? 53  ASN W ND2 1 
ATOM   12578 N  N   . THR L  1 54  ? -18.531 -23.621 18.953  1.00 69.90  ? 54  THR W N   1 
ATOM   12579 C  CA  . THR L  1 54  ? -19.418 -24.762 18.668  1.00 73.74  ? 54  THR W CA  1 
ATOM   12580 C  C   . THR L  1 54  ? -20.799 -24.503 19.257  1.00 74.14  ? 54  THR W C   1 
ATOM   12581 O  O   . THR L  1 54  ? -21.806 -24.600 18.551  1.00 76.26  ? 54  THR W O   1 
ATOM   12582 C  CB  . THR L  1 54  ? -18.875 -26.090 19.241  1.00 75.96  ? 54  THR W CB  1 
ATOM   12583 O  OG1 . THR L  1 54  ? -18.580 -25.933 20.636  1.00 74.08  ? 54  THR W OG1 1 
ATOM   12584 C  CG2 . THR L  1 54  ? -17.621 -26.531 18.494  1.00 76.56  ? 54  THR W CG2 1 
ATOM   12585 N  N   . ALA L  1 55  ? -20.829 -24.177 20.550  1.00 72.31  ? 55  ALA W N   1 
ATOM   12586 C  CA  . ALA L  1 55  ? -22.042 -23.717 21.230  1.00 72.21  ? 55  ALA W CA  1 
ATOM   12587 C  C   . ALA L  1 55  ? -22.040 -22.183 21.305  1.00 68.67  ? 55  ALA W C   1 
ATOM   12588 O  O   . ALA L  1 55  ? -22.194 -21.597 22.385  1.00 66.78  ? 55  ALA W O   1 
ATOM   12589 C  CB  . ALA L  1 55  ? -22.143 -24.338 22.619  1.00 72.81  ? 55  ALA W CB  1 
ATOM   12590 N  N   . GLY L  1 56  ? -21.866 -21.550 20.141  1.00 68.05  ? 56  GLY W N   1 
ATOM   12591 C  CA  . GLY L  1 56  ? -21.844 -20.094 20.007  1.00 65.16  ? 56  GLY W CA  1 
ATOM   12592 C  C   . GLY L  1 56  ? -20.813 -19.404 20.880  1.00 61.88  ? 56  GLY W C   1 
ATOM   12593 O  O   . GLY L  1 56  ? -19.687 -19.881 21.031  1.00 61.51  ? 56  GLY W O   1 
ATOM   12594 N  N   . ALA L  1 57  ? -21.212 -18.280 21.466  1.00 59.74  ? 57  ALA W N   1 
ATOM   12595 C  CA  . ALA L  1 57  ? -20.382 -17.569 22.431  1.00 56.79  ? 57  ALA W CA  1 
ATOM   12596 C  C   . ALA L  1 57  ? -20.295 -18.274 23.803  1.00 56.96  ? 57  ALA W C   1 
ATOM   12597 O  O   . ALA L  1 57  ? -19.378 -17.986 24.574  1.00 54.97  ? 57  ALA W O   1 
ATOM   12598 C  CB  . ALA L  1 57  ? -20.883 -16.142 22.597  1.00 54.82  ? 57  ALA W CB  1 
ATOM   12599 N  N   . THR L  1 58  ? -21.228 -19.183 24.104  1.00 59.47  ? 58  THR W N   1 
ATOM   12600 C  CA  . THR L  1 58  ? -21.263 -19.878 25.405  1.00 60.08  ? 58  THR W CA  1 
ATOM   12601 C  C   . THR L  1 58  ? -20.044 -20.776 25.657  1.00 60.39  ? 58  THR W C   1 
ATOM   12602 O  O   . THR L  1 58  ? -19.506 -20.787 26.768  1.00 59.31  ? 58  THR W O   1 
ATOM   12603 C  CB  . THR L  1 58  ? -22.531 -20.750 25.548  1.00 63.35  ? 58  THR W CB  1 
ATOM   12604 O  OG1 . THR L  1 58  ? -23.654 -20.063 24.982  1.00 63.78  ? 58  THR W OG1 1 
ATOM   12605 C  CG2 . THR L  1 58  ? -22.812 -21.080 27.022  1.00 63.67  ? 58  THR W CG2 1 
ATOM   12606 N  N   . SER L  1 59  ? -19.610 -21.512 24.629  1.00 62.06  ? 59  SER W N   1 
ATOM   12607 C  CA  . SER L  1 59  ? -18.470 -22.442 24.763  1.00 62.87  ? 59  SER W CA  1 
ATOM   12608 C  C   . SER L  1 59  ? -17.087 -21.772 24.870  1.00 60.14  ? 59  SER W C   1 
ATOM   12609 O  O   . SER L  1 59  ? -16.094 -22.460 25.124  1.00 60.77  ? 59  SER W O   1 
ATOM   12610 C  CB  . SER L  1 59  ? -18.464 -23.479 23.632  1.00 65.90  ? 59  SER W CB  1 
ATOM   12611 O  OG  . SER L  1 59  ? -18.561 -22.878 22.355  1.00 65.54  ? 59  SER W OG  1 
ATOM   12612 N  N   . ALA L  1 60  ? -17.022 -20.447 24.707  1.00 57.37  ? 60  ALA W N   1 
ATOM   12613 C  CA  . ALA L  1 60  ? -15.763 -19.703 24.817  1.00 54.87  ? 60  ALA W CA  1 
ATOM   12614 C  C   . ALA L  1 60  ? -15.176 -19.586 26.244  1.00 53.38  ? 60  ALA W C   1 
ATOM   12615 O  O   . ALA L  1 60  ? -14.055 -19.099 26.390  1.00 51.79  ? 60  ALA W O   1 
ATOM   12616 C  CB  . ALA L  1 60  ? -15.922 -18.316 24.196  1.00 52.83  ? 60  ALA W CB  1 
ATOM   12617 N  N   . GLY L  1 61  ? -15.912 -20.016 27.276  1.00 54.01  ? 61  GLY W N   1 
ATOM   12618 C  CA  . GLY L  1 61  ? -15.398 -20.048 28.642  1.00 53.04  ? 61  GLY W CA  1 
ATOM   12619 C  C   . GLY L  1 61  ? -15.523 -18.708 29.350  1.00 50.24  ? 61  GLY W C   1 
ATOM   12620 O  O   . GLY L  1 61  ? -16.273 -17.841 28.895  1.00 49.37  ? 61  GLY W O   1 
ATOM   12621 N  N   . PRO L  1 62  ? -14.789 -18.521 30.471  1.00 48.95  ? 62  PRO W N   1 
ATOM   12622 C  CA  . PRO L  1 62  ? -14.811 -17.244 31.183  1.00 46.44  ? 62  PRO W CA  1 
ATOM   12623 C  C   . PRO L  1 62  ? -13.914 -16.222 30.501  1.00 44.46  ? 62  PRO W C   1 
ATOM   12624 O  O   . PRO L  1 62  ? -13.380 -16.488 29.416  1.00 44.99  ? 62  PRO W O   1 
ATOM   12625 C  CB  . PRO L  1 62  ? -14.266 -17.613 32.562  1.00 46.49  ? 62  PRO W CB  1 
ATOM   12626 C  CG  . PRO L  1 62  ? -13.283 -18.692 32.270  1.00 48.01  ? 62  PRO W CG  1 
ATOM   12627 C  CD  . PRO L  1 62  ? -13.875 -19.479 31.126  1.00 50.03  ? 62  PRO W CD  1 
ATOM   12628 N  N   . HIS L  1 63  ? -13.756 -15.059 31.130  1.00 42.36  ? 63  HIS W N   1 
ATOM   12629 C  CA  . HIS L  1 63  ? -12.828 -14.053 30.633  1.00 40.71  ? 63  HIS W CA  1 
ATOM   12630 C  C   . HIS L  1 63  ? -11.419 -14.633 30.658  1.00 40.94  ? 63  HIS W C   1 
ATOM   12631 O  O   . HIS L  1 63  ? -11.032 -15.284 31.634  1.00 41.47  ? 63  HIS W O   1 
ATOM   12632 C  CB  . HIS L  1 63  ? -12.876 -12.771 31.470  1.00 38.94  ? 63  HIS W CB  1 
ATOM   12633 C  CG  . HIS L  1 63  ? -14.218 -12.112 31.492  1.00 38.74  ? 63  HIS W CG  1 
ATOM   12634 N  ND1 . HIS L  1 63  ? -14.499 -11.025 32.288  1.00 37.55  ? 63  HIS W ND1 1 
ATOM   12635 C  CD2 . HIS L  1 63  ? -15.371 -12.410 30.844  1.00 39.90  ? 63  HIS W CD2 1 
ATOM   12636 C  CE1 . HIS L  1 63  ? -15.758 -10.666 32.112  1.00 37.81  ? 63  HIS W CE1 1 
ATOM   12637 N  NE2 . HIS L  1 63  ? -16.311 -11.494 31.246  1.00 39.27  ? 63  HIS W NE2 1 
ATOM   12638 N  N   . PHE L  1 64  ? -10.680 -14.423 29.572  1.00 40.73  ? 64  PHE W N   1 
ATOM   12639 C  CA  . PHE L  1 64  ? -9.302  -14.885 29.463  1.00 41.20  ? 64  PHE W CA  1 
ATOM   12640 C  C   . PHE L  1 64  ? -8.471  -14.253 30.588  1.00 39.89  ? 64  PHE W C   1 
ATOM   12641 O  O   . PHE L  1 64  ? -8.268  -13.039 30.605  1.00 38.37  ? 64  PHE W O   1 
ATOM   12642 C  CB  . PHE L  1 64  ? -8.739  -14.527 28.086  1.00 41.31  ? 64  PHE W CB  1 
ATOM   12643 C  CG  . PHE L  1 64  ? -7.306  -14.927 27.879  1.00 42.09  ? 64  PHE W CG  1 
ATOM   12644 C  CD1 . PHE L  1 64  ? -6.853  -16.190 28.246  1.00 43.73  ? 64  PHE W CD1 1 
ATOM   12645 C  CD2 . PHE L  1 64  ? -6.410  -14.043 27.289  1.00 41.49  ? 64  PHE W CD2 1 
ATOM   12646 C  CE1 . PHE L  1 64  ? -5.534  -16.550 28.043  1.00 44.73  ? 64  PHE W CE1 1 
ATOM   12647 C  CE2 . PHE L  1 64  ? -5.087  -14.403 27.081  1.00 42.51  ? 64  PHE W CE2 1 
ATOM   12648 C  CZ  . PHE L  1 64  ? -4.649  -15.657 27.458  1.00 44.11  ? 64  PHE W CZ  1 
ATOM   12649 N  N   . ASN L  1 65  ? -8.027  -15.098 31.520  1.00 40.66  ? 65  ASN W N   1 
ATOM   12650 C  CA  . ASN L  1 65  ? -7.448  -14.665 32.794  1.00 39.78  ? 65  ASN W CA  1 
ATOM   12651 C  C   . ASN L  1 65  ? -6.235  -15.528 33.180  1.00 41.09  ? 65  ASN W C   1 
ATOM   12652 O  O   . ASN L  1 65  ? -6.280  -16.235 34.187  1.00 41.91  ? 65  ASN W O   1 
ATOM   12653 C  CB  . ASN L  1 65  ? -8.532  -14.737 33.892  1.00 39.49  ? 65  ASN W CB  1 
ATOM   12654 C  CG  . ASN L  1 65  ? -8.073  -14.159 35.228  1.00 38.60  ? 65  ASN W CG  1 
ATOM   12655 O  OD1 . ASN L  1 65  ? -7.138  -13.354 35.293  1.00 37.70  ? 65  ASN W OD1 1 
ATOM   12656 N  ND2 . ASN L  1 65  ? -8.754  -14.544 36.294  1.00 38.93  ? 65  ASN W ND2 1 
ATOM   12657 N  N   . PRO L  1 66  ? -5.147  -15.469 32.385  1.00 41.49  ? 66  PRO W N   1 
ATOM   12658 C  CA  . PRO L  1 66  ? -3.949  -16.272 32.691  1.00 43.08  ? 66  PRO W CA  1 
ATOM   12659 C  C   . PRO L  1 66  ? -3.196  -15.837 33.959  1.00 42.60  ? 66  PRO W C   1 
ATOM   12660 O  O   . PRO L  1 66  ? -2.463  -16.641 34.522  1.00 44.08  ? 66  PRO W O   1 
ATOM   12661 C  CB  . PRO L  1 66  ? -3.070  -16.084 31.448  1.00 43.59  ? 66  PRO W CB  1 
ATOM   12662 C  CG  . PRO L  1 66  ? -3.468  -14.757 30.911  1.00 41.79  ? 66  PRO W CG  1 
ATOM   12663 C  CD  . PRO L  1 66  ? -4.938  -14.609 31.206  1.00 40.78  ? 66  PRO W CD  1 
ATOM   12664 N  N   . LEU L  1 67  ? -3.385  -14.590 34.404  1.00 40.79  ? 67  LEU W N   1 
ATOM   12665 C  CA  . LEU L  1 67  ? -2.784  -14.101 35.653  1.00 40.45  ? 67  LEU W CA  1 
ATOM   12666 C  C   . LEU L  1 67  ? -3.685  -14.251 36.891  1.00 40.05  ? 67  LEU W C   1 
ATOM   12667 O  O   . LEU L  1 67  ? -3.326  -13.776 37.965  1.00 39.69  ? 67  LEU W O   1 
ATOM   12668 C  CB  . LEU L  1 67  ? -2.344  -12.640 35.491  1.00 39.11  ? 67  LEU W CB  1 
ATOM   12669 C  CG  . LEU L  1 67  ? -1.216  -12.385 34.485  1.00 39.84  ? 67  LEU W CG  1 
ATOM   12670 C  CD1 . LEU L  1 67  ? -1.008  -10.888 34.302  1.00 38.65  ? 67  LEU W CD1 1 
ATOM   12671 C  CD2 . LEU L  1 67  ? 0.084   -13.055 34.919  1.00 41.60  ? 67  LEU W CD2 1 
ATOM   12672 N  N   . SER L  1 68  ? -4.839  -14.910 36.745  1.00 40.36  ? 68  SER W N   1 
ATOM   12673 C  CA  . SER L  1 68  ? -5.762  -15.177 37.861  1.00 40.40  ? 68  SER W CA  1 
ATOM   12674 C  C   . SER L  1 68  ? -6.029  -13.952 38.745  1.00 38.73  ? 68  SER W C   1 
ATOM   12675 O  O   . SER L  1 68  ? -5.837  -13.999 39.964  1.00 39.02  ? 68  SER W O   1 
ATOM   12676 C  CB  . SER L  1 68  ? -5.258  -16.352 38.705  1.00 42.38  ? 68  SER W CB  1 
ATOM   12677 O  OG  . SER L  1 68  ? -5.074  -17.510 37.907  1.00 44.21  ? 68  SER W OG  1 
ATOM   12678 N  N   . ARG L  1 69  ? -6.429  -12.860 38.095  1.00 37.15  ? 69  ARG W N   1 
ATOM   12679 C  CA  A ARG L  1 69  ? -6.791  -11.613 38.766  0.50 35.74  ? 69  ARG W CA  1 
ATOM   12680 C  CA  B ARG L  1 69  ? -6.799  -11.618 38.771  0.50 35.71  ? 69  ARG W CA  1 
ATOM   12681 C  C   . ARG L  1 69  ? -8.310  -11.523 38.897  1.00 35.33  ? 69  ARG W C   1 
ATOM   12682 O  O   . ARG L  1 69  ? -9.050  -12.367 38.366  1.00 36.07  ? 69  ARG W O   1 
ATOM   12683 C  CB  A ARG L  1 69  ? -6.295  -10.402 37.962  0.50 34.70  ? 69  ARG W CB  1 
ATOM   12684 C  CB  B ARG L  1 69  ? -6.309  -10.406 37.977  0.50 34.63  ? 69  ARG W CB  1 
ATOM   12685 C  CG  A ARG L  1 69  ? -4.823  -10.405 37.571  0.50 35.32  ? 69  ARG W CG  1 
ATOM   12686 C  CG  B ARG L  1 69  ? -4.830  -10.403 37.662  0.50 35.20  ? 69  ARG W CG  1 
ATOM   12687 C  CD  A ARG L  1 69  ? -3.950  -9.592  38.512  0.50 35.15  ? 69  ARG W CD  1 
ATOM   12688 C  CD  B ARG L  1 69  ? -3.986  -10.633 38.898  0.50 35.89  ? 69  ARG W CD  1 
ATOM   12689 N  NE  A ARG L  1 69  ? -2.556  -9.628  38.076  0.50 36.06  ? 69  ARG W NE  1 
ATOM   12690 N  NE  B ARG L  1 69  ? -2.576  -10.623 38.537  0.50 36.72  ? 69  ARG W NE  1 
ATOM   12691 C  CZ  A ARG L  1 69  ? -1.845  -8.568  37.700  0.50 35.83  ? 69  ARG W CZ  1 
ATOM   12692 C  CZ  B ARG L  1 69  ? -1.595  -11.053 39.316  0.50 37.86  ? 69  ARG W CZ  1 
ATOM   12693 N  NH1 A ARG L  1 69  ? -2.376  -7.357  37.728  0.50 34.71  ? 69  ARG W NH1 1 
ATOM   12694 N  NH1 B ARG L  1 69  ? -1.862  -11.541 40.516  0.50 38.29  ? 69  ARG W NH1 1 
ATOM   12695 N  NH2 A ARG L  1 69  ? -0.582  -8.722  37.320  0.50 36.99  ? 69  ARG W NH2 1 
ATOM   12696 N  NH2 B ARG L  1 69  ? -0.346  -11.002 38.880  0.50 38.81  ? 69  ARG W NH2 1 
ATOM   12697 N  N   . LYS L  1 70  ? -8.759  -10.488 39.598  1.00 34.29  ? 70  LYS W N   1 
ATOM   12698 C  CA  . LYS L  1 70  ? -10.168 -10.139 39.651  1.00 33.92  ? 70  LYS W CA  1 
ATOM   12699 C  C   . LYS L  1 70  ? -10.530 -9.327  38.399  1.00 32.97  ? 70  LYS W C   1 
ATOM   12700 O  O   . LYS L  1 70  ? -9.657  -8.737  37.736  1.00 32.40  ? 70  LYS W O   1 
ATOM   12701 C  CB  . LYS L  1 70  ? -10.482 -9.354  40.933  1.00 33.54  ? 70  LYS W CB  1 
ATOM   12702 C  CG  . LYS L  1 70  ? -10.274 -10.173 42.210  1.00 34.68  ? 70  LYS W CG  1 
ATOM   12703 C  CD  . LYS L  1 70  ? -10.795 -9.459  43.457  1.00 34.53  ? 70  LYS W CD  1 
ATOM   12704 C  CE  . LYS L  1 70  ? -10.439 -10.244 44.724  1.00 35.80  ? 70  LYS W CE  1 
ATOM   12705 N  NZ  . LYS L  1 70  ? -11.031 -9.666  45.962  0.50 35.90  ? 70  LYS W NZ  1 
ATOM   12706 N  N   . HIS L  1 71  ? -11.823 -9.317  38.078  1.00 32.98  ? 71  HIS W N   1 
ATOM   12707 C  CA  . HIS L  1 71  ? -12.352 -8.558  36.949  1.00 32.34  ? 71  HIS W CA  1 
ATOM   12708 C  C   . HIS L  1 71  ? -12.212 -7.052  37.189  1.00 31.16  ? 71  HIS W C   1 
ATOM   12709 O  O   . HIS L  1 71  ? -12.491 -6.561  38.292  1.00 30.86  ? 71  HIS W O   1 
ATOM   12710 C  CB  . HIS L  1 71  ? -13.829 -8.903  36.719  1.00 33.07  ? 71  HIS W CB  1 
ATOM   12711 C  CG  . HIS L  1 71  ? -14.464 -8.140  35.601  1.00 32.77  ? 71  HIS W CG  1 
ATOM   12712 N  ND1 . HIS L  1 71  ? -14.299 -8.481  34.277  1.00 33.14  ? 71  HIS W ND1 1 
ATOM   12713 C  CD2 . HIS L  1 71  ? -15.252 -7.041  35.611  1.00 32.32  ? 71  HIS W CD2 1 
ATOM   12714 C  CE1 . HIS L  1 71  ? -14.976 -7.633  33.521  1.00 32.92  ? 71  HIS W CE1 1 
ATOM   12715 N  NE2 . HIS L  1 71  ? -15.556 -6.746  34.307  1.00 32.43  ? 71  HIS W NE2 1 
ATOM   12716 N  N   . GLY L  1 72  ? -11.794 -6.336  36.143  1.00 30.63  ? 72  GLY W N   1 
ATOM   12717 C  CA  . GLY L  1 72  ? -11.703 -4.878  36.167  1.00 29.91  ? 72  GLY W CA  1 
ATOM   12718 C  C   . GLY L  1 72  ? -12.050 -4.274  34.822  1.00 29.87  ? 72  GLY W C   1 
ATOM   12719 O  O   . GLY L  1 72  ? -12.487 -4.975  33.907  1.00 30.34  ? 72  GLY W O   1 
ATOM   12720 N  N   . GLY L  1 73  ? -11.887 -2.960  34.722  1.00 29.51  ? 73  GLY W N   1 
ATOM   12721 C  CA  . GLY L  1 73  ? -11.921 -2.268  33.447  1.00 29.69  ? 73  GLY W CA  1 
ATOM   12722 C  C   . GLY L  1 73  ? -10.535 -2.327  32.813  1.00 29.85  ? 73  GLY W C   1 
ATOM   12723 O  O   . GLY L  1 73  ? -9.558  -2.671  33.490  1.00 29.78  ? 73  GLY W O   1 
ATOM   12724 N  N   . PRO L  1 74  ? -10.430 -1.986  31.511  1.00 30.29  ? 74  PRO W N   1 
ATOM   12725 C  CA  . PRO L  1 74  ? -9.125  -2.045  30.828  1.00 30.75  ? 74  PRO W CA  1 
ATOM   12726 C  C   . PRO L  1 74  ? -8.058  -1.117  31.402  1.00 30.82  ? 74  PRO W C   1 
ATOM   12727 O  O   . PRO L  1 74  ? -6.882  -1.444  31.337  1.00 31.29  ? 74  PRO W O   1 
ATOM   12728 C  CB  . PRO L  1 74  ? -9.455  -1.665  29.373  1.00 31.28  ? 74  PRO W CB  1 
ATOM   12729 C  CG  . PRO L  1 74  ? -10.776 -0.980  29.436  1.00 31.11  ? 74  PRO W CG  1 
ATOM   12730 C  CD  . PRO L  1 74  ? -11.509 -1.604  30.589  1.00 30.59  ? 74  PRO W CD  1 
ATOM   12731 N  N   . LYS L  1 75  ? -8.462  0.013   31.974  1.00 30.71  ? 75  LYS W N   1 
ATOM   12732 C  CA  . LYS L  1 75  ? -7.522  0.944   32.596  1.00 31.10  ? 75  LYS W CA  1 
ATOM   12733 C  C   . LYS L  1 75  ? -6.949  0.471   33.948  1.00 30.85  ? 75  LYS W C   1 
ATOM   12734 O  O   . LYS L  1 75  ? -5.986  1.056   34.427  1.00 31.29  ? 75  LYS W O   1 
ATOM   12735 C  CB  . LYS L  1 75  ? -8.177  2.312   32.794  1.00 31.32  ? 75  LYS W CB  1 
ATOM   12736 C  CG  . LYS L  1 75  ? -8.659  2.974   31.506  1.00 31.98  ? 75  LYS W CG  1 
ATOM   12737 C  CD  . LYS L  1 75  ? -9.521  4.193   31.791  1.00 32.33  ? 75  LYS W CD  1 
ATOM   12738 C  CE  . LYS L  1 75  ? -8.704  5.384   32.266  1.00 33.19  ? 75  LYS W CE  1 
ATOM   12739 N  NZ  . LYS L  1 75  ? -9.584  6.478   32.761  1.00 33.64  ? 75  LYS W NZ  1 
ATOM   12740 N  N   . ASP L  1 76  ? -7.539  -0.555  34.568  1.00 30.37  ? 76  ASP W N   1 
ATOM   12741 C  CA  . ASP L  1 76  ? -7.069  -1.044  35.877  1.00 30.34  ? 76  ASP W CA  1 
ATOM   12742 C  C   . ASP L  1 76  ? -5.891  -2.003  35.758  1.00 30.81  ? 76  ASP W C   1 
ATOM   12743 O  O   . ASP L  1 76  ? -5.818  -2.797  34.822  1.00 31.02  ? 76  ASP W O   1 
ATOM   12744 C  CB  . ASP L  1 76  ? -8.188  -1.796  36.608  1.00 29.98  ? 76  ASP W CB  1 
ATOM   12745 C  CG  . ASP L  1 76  ? -9.379  -0.929  36.916  1.00 29.77  ? 76  ASP W CG  1 
ATOM   12746 O  OD1 . ASP L  1 76  ? -9.198  0.206   37.388  1.00 29.93  ? 76  ASP W OD1 1 
ATOM   12747 O  OD2 . ASP L  1 76  ? -10.514 -1.396  36.704  1.00 29.81  ? 76  ASP W OD2 1 
ATOM   12748 N  N   . GLU L  1 77  ? -5.001  -1.954  36.744  1.00 31.18  ? 77  GLU W N   1 
ATOM   12749 C  CA  . GLU L  1 77  ? -3.938  -2.953  36.919  1.00 31.84  ? 77  GLU W CA  1 
ATOM   12750 C  C   . GLU L  1 77  ? -4.561  -4.305  37.303  1.00 31.65  ? 77  GLU W C   1 
ATOM   12751 O  O   . GLU L  1 77  ? -4.191  -5.348  36.764  1.00 32.19  ? 77  GLU W O   1 
ATOM   12752 C  CB  . GLU L  1 77  ? -2.962  -2.476  38.000  1.00 32.50  ? 77  GLU W CB  1 
ATOM   12753 C  CG  . GLU L  1 77  ? -1.729  -3.348  38.196  1.00 33.63  ? 77  GLU W CG  1 
ATOM   12754 C  CD  . GLU L  1 77  ? -0.660  -2.675  39.040  0.50 34.58  ? 77  GLU W CD  1 
ATOM   12755 O  OE1 . GLU L  1 77  ? -1.005  -2.030  40.053  0.50 34.35  ? 77  GLU W OE1 1 
ATOM   12756 O  OE2 . GLU L  1 77  ? 0.531   -2.794  38.694  0.50 35.80  ? 77  GLU W OE2 1 
ATOM   12757 N  N   . GLU L  1 78  ? -5.518  -4.269  38.230  1.00 31.05  ? 78  GLU W N   1 
ATOM   12758 C  CA  . GLU L  1 78  ? -6.292  -5.449  38.607  1.00 31.11  ? 78  GLU W CA  1 
ATOM   12759 C  C   . GLU L  1 78  ? -7.396  -5.666  37.566  1.00 30.71  ? 78  GLU W C   1 
ATOM   12760 O  O   . GLU L  1 78  ? -8.434  -5.003  37.600  1.00 30.16  ? 78  GLU W O   1 
ATOM   12761 C  CB  . GLU L  1 78  ? -6.894  -5.280  40.015  1.00 31.00  ? 78  GLU W CB  1 
ATOM   12762 C  CG  . GLU L  1 78  ? -7.531  -6.541  40.592  1.00 31.54  ? 78  GLU W CG  1 
ATOM   12763 C  CD  . GLU L  1 78  ? -6.531  -7.654  40.875  1.00 32.58  ? 78  GLU W CD  1 
ATOM   12764 O  OE1 . GLU L  1 78  ? -5.306  -7.391  40.920  1.00 33.04  ? 78  GLU W OE1 1 
ATOM   12765 O  OE2 . GLU L  1 78  ? -6.962  -8.810  41.064  1.00 33.29  ? 78  GLU W OE2 1 
ATOM   12766 N  N   . ARG L  1 79  ? -7.135  -6.585  36.642  1.00 31.16  ? 79  ARG W N   1 
ATOM   12767 C  CA  . ARG L  1 79  ? -8.037  -6.898  35.543  1.00 31.12  ? 79  ARG W CA  1 
ATOM   12768 C  C   . ARG L  1 79  ? -7.673  -8.242  34.959  1.00 32.11  ? 79  ARG W C   1 
ATOM   12769 O  O   . ARG L  1 79  ? -6.532  -8.686  35.083  1.00 32.71  ? 79  ARG W O   1 
ATOM   12770 C  CB  . ARG L  1 79  ? -7.931  -5.844  34.433  1.00 30.74  ? 79  ARG W CB  1 
ATOM   12771 C  CG  . ARG L  1 79  ? -6.539  -5.710  33.812  1.00 31.21  ? 79  ARG W CG  1 
ATOM   12772 C  CD  . ARG L  1 79  ? -6.549  -4.828  32.573  1.00 31.18  ? 79  ARG W CD  1 
ATOM   12773 N  NE  . ARG L  1 79  ? -6.848  -5.584  31.353  1.00 31.70  ? 79  ARG W NE  1 
ATOM   12774 C  CZ  . ARG L  1 79  ? -6.821  -5.077  30.121  1.00 31.99  ? 79  ARG W CZ  1 
ATOM   12775 N  NH1 . ARG L  1 79  ? -6.511  -3.797  29.909  1.00 31.84  ? 79  ARG W NH1 1 
ATOM   12776 N  NH2 . ARG L  1 79  ? -7.099  -5.861  29.086  1.00 32.66  ? 79  ARG W NH2 1 
ATOM   12777 N  N   . HIS L  1 80  ? -8.637  -8.875  34.298  1.00 32.50  ? 80  HIS W N   1 
ATOM   12778 C  CA  . HIS L  1 80  ? -8.343  -10.016 33.423  1.00 33.66  ? 80  HIS W CA  1 
ATOM   12779 C  C   . HIS L  1 80  ? -7.677  -9.480  32.157  1.00 33.66  ? 80  HIS W C   1 
ATOM   12780 O  O   . HIS L  1 80  ? -7.890  -8.324  31.784  1.00 32.82  ? 80  HIS W O   1 
ATOM   12781 C  CB  . HIS L  1 80  ? -9.613  -10.790 33.057  1.00 34.34  ? 80  HIS W CB  1 
ATOM   12782 C  CG  . HIS L  1 80  ? -10.394 -11.266 34.239  1.00 34.62  ? 80  HIS W CG  1 
ATOM   12783 N  ND1 . HIS L  1 80  ? -11.768 -11.335 34.251  1.00 34.88  ? 80  HIS W ND1 1 
ATOM   12784 C  CD2 . HIS L  1 80  ? -9.988  -11.671 35.466  1.00 34.90  ? 80  HIS W CD2 1 
ATOM   12785 C  CE1 . HIS L  1 80  ? -12.173 -11.793 35.423  1.00 35.36  ? 80  HIS W CE1 1 
ATOM   12786 N  NE2 . HIS L  1 80  ? -11.112 -12.005 36.179  1.00 35.33  ? 80  HIS W NE2 1 
ATOM   12787 N  N   . VAL L  1 81  ? -6.874  -10.314 31.500  1.00 34.78  ? 81  VAL W N   1 
ATOM   12788 C  CA  . VAL L  1 81  ? -6.278  -9.945  30.208  1.00 35.17  ? 81  VAL W CA  1 
ATOM   12789 C  C   . VAL L  1 81  ? -7.380  -9.556  29.213  1.00 34.96  ? 81  VAL W C   1 
ATOM   12790 O  O   . VAL L  1 81  ? -7.281  -8.529  28.536  1.00 34.57  ? 81  VAL W O   1 
ATOM   12791 C  CB  . VAL L  1 81  ? -5.362  -11.067 29.651  1.00 36.74  ? 81  VAL W CB  1 
ATOM   12792 C  CG1 . VAL L  1 81  ? -4.975  -10.828 28.194  1.00 37.40  ? 81  VAL W CG1 1 
ATOM   12793 C  CG2 . VAL L  1 81  ? -4.099  -11.167 30.491  1.00 37.13  ? 81  VAL W CG2 1 
ATOM   12794 N  N   . GLY L  1 82  ? -8.450  -10.341 29.173  1.00 35.43  ? 82  GLY W N   1 
ATOM   12795 C  CA  . GLY L  1 82  ? -9.561  -10.072 28.273  1.00 35.56  ? 82  GLY W CA  1 
ATOM   12796 C  C   . GLY L  1 82  ? -10.532 -8.945  28.614  1.00 34.50  ? 82  GLY W C   1 
ATOM   12797 O  O   . GLY L  1 82  ? -11.513 -8.779  27.898  1.00 34.82  ? 82  GLY W O   1 
ATOM   12798 N  N   . ASP L  1 83  ? -10.289 -8.181  29.678  1.00 33.51  ? 83  ASP W N   1 
ATOM   12799 C  CA  . ASP L  1 83  ? -11.206 -7.108  30.093  1.00 32.76  ? 83  ASP W CA  1 
ATOM   12800 C  C   . ASP L  1 83  ? -11.023 -5.847  29.238  1.00 32.50  ? 83  ASP W C   1 
ATOM   12801 O  O   . ASP L  1 83  ? -10.258 -4.949  29.590  1.00 32.01  ? 83  ASP W O   1 
ATOM   12802 C  CB  . ASP L  1 83  ? -11.028 -6.768  31.586  1.00 32.01  ? 83  ASP W CB  1 
ATOM   12803 C  CG  . ASP L  1 83  ? -11.566 -7.854  32.532  1.00 32.47  ? 83  ASP W CG  1 
ATOM   12804 O  OD1 . ASP L  1 83  ? -12.326 -8.769  32.128  1.00 33.39  ? 83  ASP W OD1 1 
ATOM   12805 O  OD2 . ASP L  1 83  ? -11.215 -7.797  33.728  1.00 32.08  ? 83  ASP W OD2 1 
ATOM   12806 N  N   . LEU L  1 84  ? -11.735 -5.773  28.116  1.00 33.12  ? 84  LEU W N   1 
ATOM   12807 C  CA  . LEU L  1 84  ? -11.646 -4.600  27.234  1.00 33.19  ? 84  LEU W CA  1 
ATOM   12808 C  C   . LEU L  1 84  ? -12.709 -3.523  27.529  1.00 32.83  ? 84  LEU W C   1 
ATOM   12809 O  O   . LEU L  1 84  ? -12.766 -2.515  26.827  1.00 33.08  ? 84  LEU W O   1 
ATOM   12810 C  CB  . LEU L  1 84  ? -11.674 -5.027  25.756  1.00 34.29  ? 84  LEU W CB  1 
ATOM   12811 C  CG  . LEU L  1 84  ? -10.558 -5.980  25.305  1.00 34.98  ? 84  LEU W CG  1 
ATOM   12812 C  CD1 . LEU L  1 84  ? -10.801 -6.478  23.883  1.00 36.27  ? 84  LEU W CD1 1 
ATOM   12813 C  CD2 . LEU L  1 84  ? -9.200  -5.305  25.399  1.00 34.79  ? 84  LEU W CD2 1 
ATOM   12814 N  N   . GLY L  1 85  ? -13.530 -3.728  28.566  1.00 32.47  ? 85  GLY W N   1 
ATOM   12815 C  CA  . GLY L  1 85  ? -14.469 -2.712  29.035  1.00 32.22  ? 85  GLY W CA  1 
ATOM   12816 C  C   . GLY L  1 85  ? -15.771 -2.706  28.259  1.00 33.05  ? 85  GLY W C   1 
ATOM   12817 O  O   . GLY L  1 85  ? -16.371 -3.762  28.023  1.00 33.69  ? 85  GLY W O   1 
ATOM   12818 N  N   . ASN L  1 86  ? -16.204 -1.509  27.871  1.00 33.22  ? 86  ASN W N   1 
ATOM   12819 C  CA  . ASN L  1 86  ? -17.432 -1.328  27.117  1.00 34.26  ? 86  ASN W CA  1 
ATOM   12820 C  C   . ASN L  1 86  ? -17.175 -0.738  25.744  1.00 34.95  ? 86  ASN W C   1 
ATOM   12821 O  O   . ASN L  1 86  ? -16.187 -0.036  25.528  1.00 34.68  ? 86  ASN W O   1 
ATOM   12822 C  CB  . ASN L  1 86  ? -18.382 -0.395  27.869  1.00 34.34  ? 86  ASN W CB  1 
ATOM   12823 C  CG  . ASN L  1 86  ? -18.934 -1.025  29.121  1.00 34.09  ? 86  ASN W CG  1 
ATOM   12824 O  OD1 . ASN L  1 86  ? -19.570 -2.076  29.062  1.00 34.70  ? 86  ASN W OD1 1 
ATOM   12825 N  ND2 . ASN L  1 86  ? -18.697 -0.387  30.267  1.00 33.38  ? 86  ASN W ND2 1 
ATOM   12826 N  N   . VAL L  1 87  ? -18.102 -1.021  24.842  1.00 36.15  ? 87  VAL W N   1 
ATOM   12827 C  CA  . VAL L  1 87  ? -18.220 -0.330  23.552  1.00 37.19  ? 87  VAL W CA  1 
ATOM   12828 C  C   . VAL L  1 87  ? -19.562 0.395   23.566  1.00 38.16  ? 87  VAL W C   1 
ATOM   12829 O  O   . VAL L  1 87  ? -20.516 -0.103  24.171  1.00 38.44  ? 87  VAL W O   1 
ATOM   12830 C  CB  . VAL L  1 87  ? -18.120 -1.303  22.354  1.00 38.12  ? 87  VAL W CB  1 
ATOM   12831 C  CG1 . VAL L  1 87  ? -16.720 -1.888  22.287  1.00 37.45  ? 87  VAL W CG1 1 
ATOM   12832 C  CG2 . VAL L  1 87  ? -19.163 -2.419  22.418  1.00 38.90  ? 87  VAL W CG2 1 
ATOM   12833 N  N   . THR L  1 88  ? -19.629 1.558   22.906  1.00 38.90  ? 88  THR W N   1 
ATOM   12834 C  CA  . THR L  1 88  ? -20.828 2.413   22.884  1.00 40.03  ? 88  THR W CA  1 
ATOM   12835 C  C   . THR L  1 88  ? -21.484 2.409   21.497  1.00 41.83  ? 88  THR W C   1 
ATOM   12836 O  O   . THR L  1 88  ? -20.864 2.829   20.512  1.00 42.33  ? 88  THR W O   1 
ATOM   12837 C  CB  . THR L  1 88  ? -20.470 3.866   23.271  1.00 39.92  ? 88  THR W CB  1 
ATOM   12838 O  OG1 . THR L  1 88  ? -20.011 3.903   24.627  1.00 38.49  ? 88  THR W OG1 1 
ATOM   12839 C  CG2 . THR L  1 88  ? -21.676 4.829   23.119  1.00 41.48  ? 88  THR W CG2 1 
ATOM   12840 N  N   . ALA L  1 89  ? -22.732 1.931   21.443  1.00 42.95  ? 89  ALA W N   1 
ATOM   12841 C  CA  . ALA L  1 89  ? -23.568 1.983   20.247  1.00 45.02  ? 89  ALA W CA  1 
ATOM   12842 C  C   . ALA L  1 89  ? -24.354 3.300   20.198  1.00 46.31  ? 89  ALA W C   1 
ATOM   12843 O  O   . ALA L  1 89  ? -24.954 3.706   21.202  1.00 46.19  ? 89  ALA W O   1 
ATOM   12844 C  CB  . ALA L  1 89  ? -24.537 0.810   20.240  1.00 45.97  ? 89  ALA W CB  1 
ATOM   12845 N  N   . ASP L  1 90  ? -24.350 3.953   19.034  1.00 47.76  ? 90  ASP W N   1 
ATOM   12846 C  CA  . ASP L  1 90  ? -25.114 5.190   18.814  1.00 49.49  ? 90  ASP W CA  1 
ATOM   12847 C  C   . ASP L  1 90  ? -26.616 4.902   18.657  1.00 51.42  ? 90  ASP W C   1 
ATOM   12848 O  O   . ASP L  1 90  ? -27.041 3.744   18.745  1.00 51.37  ? 90  ASP W O   1 
ATOM   12849 C  CB  . ASP L  1 90  ? -24.548 6.012   17.622  1.00 50.63  ? 90  ASP W CB  1 
ATOM   12850 C  CG  . ASP L  1 90  ? -24.676 5.312   16.256  1.00 51.97  ? 90  ASP W CG  1 
ATOM   12851 O  OD1 . ASP L  1 90  ? -25.468 4.360   16.080  1.00 52.66  ? 90  ASP W OD1 1 
ATOM   12852 O  OD2 . ASP L  1 90  ? -23.960 5.746   15.332  1.00 52.57  ? 90  ASP W OD2 1 
ATOM   12853 N  N   . LYS L  1 91  ? -27.405 5.956   18.435  1.00 53.34  ? 91  LYS W N   1 
ATOM   12854 C  CA  . LYS L  1 91  ? -28.862 5.839   18.225  1.00 55.68  ? 91  LYS W CA  1 
ATOM   12855 C  C   . LYS L  1 91  ? -29.279 4.923   17.055  1.00 57.22  ? 91  LYS W C   1 
ATOM   12856 O  O   . LYS L  1 91  ? -30.375 4.353   17.071  1.00 58.77  ? 91  LYS W O   1 
ATOM   12857 C  CB  . LYS L  1 91  ? -29.490 7.231   18.039  1.00 57.75  ? 91  LYS W CB  1 
ATOM   12858 C  CG  . LYS L  1 91  ? -29.100 7.928   16.743  1.00 59.15  ? 91  LYS W CG  1 
ATOM   12859 C  CD  . LYS L  1 91  ? -29.412 9.411   16.779  1.00 60.84  ? 91  LYS W CD  1 
ATOM   12860 C  CE  . LYS L  1 91  ? -28.967 10.076  15.487  1.00 62.40  ? 91  LYS W CE  1 
ATOM   12861 N  NZ  . LYS L  1 91  ? -29.523 11.446  15.343  1.00 64.87  ? 91  LYS W NZ  1 
ATOM   12862 N  N   . ASP L  1 92  ? -28.410 4.798   16.048  1.00 57.03  ? 92  ASP W N   1 
ATOM   12863 C  CA  . ASP L  1 92  ? -28.622 3.866   14.928  1.00 58.39  ? 92  ASP W CA  1 
ATOM   12864 C  C   . ASP L  1 92  ? -28.123 2.443   15.216  1.00 56.87  ? 92  ASP W C   1 
ATOM   12865 O  O   . ASP L  1 92  ? -28.169 1.591   14.328  1.00 57.85  ? 92  ASP W O   1 
ATOM   12866 C  CB  . ASP L  1 92  ? -27.945 4.401   13.661  1.00 59.25  ? 92  ASP W CB  1 
ATOM   12867 C  CG  . ASP L  1 92  ? -28.420 5.793   13.292  1.00 61.17  ? 92  ASP W CG  1 
ATOM   12868 O  OD1 . ASP L  1 92  ? -29.649 6.006   13.220  1.00 63.28  ? 92  ASP W OD1 1 
ATOM   12869 O  OD2 . ASP L  1 92  ? -27.562 6.675   13.083  1.00 60.82  ? 92  ASP W OD2 1 
ATOM   12870 N  N   . GLY L  1 93  ? -27.644 2.194   16.438  1.00 54.65  ? 93  GLY W N   1 
ATOM   12871 C  CA  . GLY L  1 93  ? -27.220 0.866   16.867  1.00 53.41  ? 93  GLY W CA  1 
ATOM   12872 C  C   . GLY L  1 93  ? -25.861 0.411   16.372  1.00 52.12  ? 93  GLY W C   1 
ATOM   12873 O  O   . GLY L  1 93  ? -25.601 -0.788  16.325  1.00 51.83  ? 93  GLY W O   1 
ATOM   12874 N  N   . VAL L  1 94  ? -24.999 1.369   16.023  1.00 51.59  ? 94  VAL W N   1 
ATOM   12875 C  CA  . VAL L  1 94  ? -23.657 1.100   15.500  1.00 50.67  ? 94  VAL W CA  1 
ATOM   12876 C  C   . VAL L  1 94  ? -22.611 1.496   16.544  1.00 48.40  ? 94  VAL W C   1 
ATOM   12877 O  O   . VAL L  1 94  ? -22.626 2.629   17.034  1.00 48.07  ? 94  VAL W O   1 
ATOM   12878 C  CB  . VAL L  1 94  ? -23.376 1.896   14.199  1.00 52.18  ? 94  VAL W CB  1 
ATOM   12879 C  CG1 . VAL L  1 94  ? -21.939 1.670   13.719  1.00 51.37  ? 94  VAL W CG1 1 
ATOM   12880 C  CG2 . VAL L  1 94  ? -24.369 1.515   13.111  1.00 54.67  ? 94  VAL W CG2 1 
ATOM   12881 N  N   . ALA L  1 95  ? -21.710 0.564   16.867  1.00 47.09  ? 95  ALA W N   1 
ATOM   12882 C  CA  . ALA L  1 95  ? -20.546 0.851   17.689  1.00 45.25  ? 95  ALA W CA  1 
ATOM   12883 C  C   . ALA L  1 95  ? -19.307 0.955   16.803  1.00 45.42  ? 95  ALA W C   1 
ATOM   12884 O  O   . ALA L  1 95  ? -18.751 -0.061  16.397  1.00 45.38  ? 95  ALA W O   1 
ATOM   12885 C  CB  . ALA L  1 95  ? -20.358 -0.230  18.743  1.00 43.88  ? 95  ALA W CB  1 
ATOM   12886 N  N   . ASP L  1 96  ? -18.891 2.186   16.500  1.00 45.91  ? 96  ASP W N   1 
ATOM   12887 C  CA  . ASP L  1 96  ? -17.633 2.432   15.772  1.00 46.25  ? 96  ASP W CA  1 
ATOM   12888 C  C   . ASP L  1 96  ? -16.461 2.324   16.733  1.00 44.56  ? 96  ASP W C   1 
ATOM   12889 O  O   . ASP L  1 96  ? -15.966 3.330   17.231  1.00 44.15  ? 96  ASP W O   1 
ATOM   12890 C  CB  . ASP L  1 96  ? -17.627 3.806   15.102  1.00 47.71  ? 96  ASP W CB  1 
ATOM   12891 C  CG  . ASP L  1 96  ? -18.598 3.894   13.952  1.00 49.78  ? 96  ASP W CG  1 
ATOM   12892 O  OD1 . ASP L  1 96  ? -18.541 3.014   13.067  1.00 50.62  ? 96  ASP W OD1 1 
ATOM   12893 O  OD2 . ASP L  1 96  ? -19.402 4.843   13.932  1.00 50.77  ? 96  ASP W OD2 1 
ATOM   12894 N  N   . VAL L  1 97  ? -16.000 1.092   16.931  1.00 43.92  ? 97  VAL W N   1 
ATOM   12895 C  CA  . VAL L  1 97  ? -15.057 0.738   18.003  1.00 42.39  ? 97  VAL W CA  1 
ATOM   12896 C  C   . VAL L  1 97  ? -13.669 1.372   17.781  1.00 42.65  ? 97  VAL W C   1 
ATOM   12897 O  O   . VAL L  1 97  ? -13.167 1.410   16.662  1.00 43.81  ? 97  VAL W O   1 
ATOM   12898 C  CB  . VAL L  1 97  ? -14.951 -0.801  18.146  1.00 41.97  ? 97  VAL W CB  1 
ATOM   12899 C  CG1 . VAL L  1 97  ? -13.976 -1.185  19.258  1.00 40.52  ? 97  VAL W CG1 1 
ATOM   12900 C  CG2 . VAL L  1 97  ? -16.333 -1.418  18.405  1.00 42.17  ? 97  VAL W CG2 1 
ATOM   12901 N  N   . SER L  1 98  ? -13.067 1.888   18.853  1.00 41.80  ? 98  SER W N   1 
ATOM   12902 C  CA  . SER L  1 98  ? -11.725 2.486   18.775  1.00 42.26  ? 98  SER W CA  1 
ATOM   12903 C  C   . SER L  1 98  ? -11.051 2.371   20.127  1.00 41.02  ? 98  SER W C   1 
ATOM   12904 O  O   . SER L  1 98  ? -11.183 3.256   20.986  1.00 40.61  ? 98  SER W O   1 
ATOM   12905 C  CB  . SER L  1 98  ? -11.785 3.947   18.320  1.00 43.50  ? 98  SER W CB  1 
ATOM   12906 O  OG  . SER L  1 98  ? -10.484 4.508   18.226  1.00 44.10  ? 98  SER W OG  1 
ATOM   12907 N  N   . ILE L  1 99  ? -10.354 1.251   20.309  1.00 40.66  ? 99  ILE W N   1 
ATOM   12908 C  CA  . ILE L  1 99  ? -9.716  0.905   21.572  1.00 39.58  ? 99  ILE W CA  1 
ATOM   12909 C  C   . ILE L  1 99  ? -8.230  0.675   21.307  1.00 40.30  ? 99  ILE W C   1 
ATOM   12910 O  O   . ILE L  1 99  ? -7.856  0.154   20.259  1.00 41.33  ? 99  ILE W O   1 
ATOM   12911 C  CB  . ILE L  1 99  ? -10.395 -0.341  22.198  1.00 38.64  ? 99  ILE W CB  1 
ATOM   12912 C  CG1 . ILE L  1 99  ? -11.778 0.037   22.742  1.00 38.10  ? 99  ILE W CG1 1 
ATOM   12913 C  CG2 . ILE L  1 99  ? -9.544  -0.959  23.308  1.00 37.78  ? 99  ILE W CG2 1 
ATOM   12914 C  CD1 . ILE L  1 99  ? -12.735 -1.131  22.852  1.00 37.96  ? 99  ILE W CD1 1 
ATOM   12915 N  N   . GLU L  1 100 ? -7.399  1.120   22.247  1.00 40.06  ? 100 GLU W N   1 
ATOM   12916 C  CA  . GLU L  1 100 ? -5.968  0.836   22.259  1.00 40.78  ? 100 GLU W CA  1 
ATOM   12917 C  C   . GLU L  1 100 ? -5.650  0.235   23.626  1.00 39.57  ? 100 GLU W C   1 
ATOM   12918 O  O   . GLU L  1 100 ? -5.896  0.875   24.653  1.00 38.70  ? 100 GLU W O   1 
ATOM   12919 C  CB  . GLU L  1 100 ? -5.172  2.120   22.018  1.00 42.16  ? 100 GLU W CB  1 
ATOM   12920 C  CG  . GLU L  1 100 ? -3.675  1.905   21.822  1.00 43.47  ? 100 GLU W CG  1 
ATOM   12921 C  CD  . GLU L  1 100 ? -3.005  3.083   21.131  1.00 45.49  ? 100 GLU W CD  1 
ATOM   12922 O  OE1 . GLU L  1 100 ? -3.473  3.483   20.036  1.00 46.63  ? 100 GLU W OE1 1 
ATOM   12923 O  OE2 . GLU L  1 100 ? -2.011  3.613   21.678  1.00 46.28  ? 100 GLU W OE2 1 
ATOM   12924 N  N   . ASP L  1 101 ? -5.129  -0.996  23.633  1.00 39.58  ? 101 ASP W N   1 
ATOM   12925 C  CA  . ASP L  1 101 ? -4.890  -1.741  24.873  1.00 38.61  ? 101 ASP W CA  1 
ATOM   12926 C  C   . ASP L  1 101 ? -3.499  -2.342  24.869  1.00 39.38  ? 101 ASP W C   1 
ATOM   12927 O  O   . ASP L  1 101 ? -3.107  -2.983  23.892  1.00 40.49  ? 101 ASP W O   1 
ATOM   12928 C  CB  . ASP L  1 101 ? -5.923  -2.858  25.046  1.00 37.94  ? 101 ASP W CB  1 
ATOM   12929 C  CG  . ASP L  1 101 ? -5.976  -3.383  26.484  1.00 37.12  ? 101 ASP W CG  1 
ATOM   12930 O  OD1 . ASP L  1 101 ? -6.387  -2.607  27.386  1.00 36.22  ? 101 ASP W OD1 1 
ATOM   12931 O  OD2 . ASP L  1 101 ? -5.585  -4.559  26.720  1.00 37.40  ? 101 ASP W OD2 1 
ATOM   12932 N  N   . SER L  1 102 ? -2.769  -2.145  25.966  1.00 38.98  ? 102 SER W N   1 
ATOM   12933 C  CA  . SER L  1 102 ? -1.408  -2.662  26.111  1.00 39.91  ? 102 SER W CA  1 
ATOM   12934 C  C   . SER L  1 102 ? -1.299  -3.998  26.871  1.00 39.42  ? 102 SER W C   1 
ATOM   12935 O  O   . SER L  1 102 ? -0.185  -4.469  27.097  1.00 40.35  ? 102 SER W O   1 
ATOM   12936 C  CB  . SER L  1 102 ? -0.528  -1.601  26.781  1.00 40.45  ? 102 SER W CB  1 
ATOM   12937 O  OG  . SER L  1 102 ? -0.395  -0.470  25.932  1.00 41.48  ? 102 SER W OG  1 
ATOM   12938 N  N   . VAL L  1 103 ? -2.425  -4.613  27.252  1.00 38.10  ? 103 VAL W N   1 
ATOM   12939 C  CA  . VAL L  1 103 ? -2.407  -5.859  28.039  1.00 37.82  ? 103 VAL W CA  1 
ATOM   12940 C  C   . VAL L  1 103 ? -2.690  -7.069  27.161  1.00 38.42  ? 103 VAL W C   1 
ATOM   12941 O  O   . VAL L  1 103 ? -1.996  -8.084  27.271  1.00 39.35  ? 103 VAL W O   1 
ATOM   12942 C  CB  . VAL L  1 103 ? -3.382  -5.794  29.239  1.00 36.42  ? 103 VAL W CB  1 
ATOM   12943 C  CG1 . VAL L  1 103 ? -3.539  -7.154  29.912  1.00 36.55  ? 103 VAL W CG1 1 
ATOM   12944 C  CG2 . VAL L  1 103 ? -2.885  -4.760  30.241  1.00 36.00  ? 103 VAL W CG2 1 
ATOM   12945 N  N   . ILE L  1 104 ? -3.712  -6.984  26.311  1.00 38.01  ? 104 ILE W N   1 
ATOM   12946 C  CA  . ILE L  1 104 ? -3.863  -7.978  25.239  1.00 39.04  ? 104 ILE W CA  1 
ATOM   12947 C  C   . ILE L  1 104 ? -2.682  -7.884  24.278  1.00 40.38  ? 104 ILE W C   1 
ATOM   12948 O  O   . ILE L  1 104 ? -2.010  -6.849  24.187  1.00 40.45  ? 104 ILE W O   1 
ATOM   12949 C  CB  . ILE L  1 104 ? -5.188  -7.873  24.446  1.00 38.82  ? 104 ILE W CB  1 
ATOM   12950 C  CG1 . ILE L  1 104 ? -5.378  -6.482  23.814  1.00 38.51  ? 104 ILE W CG1 1 
ATOM   12951 C  CG2 . ILE L  1 104 ? -6.363  -8.238  25.340  1.00 37.88  ? 104 ILE W CG2 1 
ATOM   12952 C  CD1 . ILE L  1 104 ? -6.378  -6.466  22.674  1.00 38.96  ? 104 ILE W CD1 1 
ATOM   12953 N  N   . SER L  1 105 ? -2.422  -8.982  23.583  1.00 41.64  ? 105 SER W N   1 
ATOM   12954 C  CA  . SER L  1 105 ? -1.323  -9.042  22.630  1.00 43.25  ? 105 SER W CA  1 
ATOM   12955 C  C   . SER L  1 105 ? -1.684  -9.881  21.424  1.00 44.49  ? 105 SER W C   1 
ATOM   12956 O  O   . SER L  1 105 ? -2.641  -10.658 21.457  1.00 44.23  ? 105 SER W O   1 
ATOM   12957 C  CB  . SER L  1 105 ? -0.083  -9.629  23.301  1.00 44.18  ? 105 SER W CB  1 
ATOM   12958 O  OG  . SER L  1 105 ? 1.048   -9.509  22.458  1.00 45.93  ? 105 SER W OG  1 
ATOM   12959 N  N   . LEU L  1 106 ? -0.899  -9.706  20.361  1.00 46.01  ? 106 LEU W N   1 
ATOM   12960 C  CA  . LEU L  1 106 ? -0.950  -10.574 19.192  1.00 47.75  ? 106 LEU W CA  1 
ATOM   12961 C  C   . LEU L  1 106 ? 0.170   -11.635 19.191  1.00 49.68  ? 106 LEU W C   1 
ATOM   12962 O  O   . LEU L  1 106 ? 0.332   -12.361 18.208  1.00 51.49  ? 106 LEU W O   1 
ATOM   12963 C  CB  . LEU L  1 106 ? -0.926  -9.723  17.918  1.00 48.53  ? 106 LEU W CB  1 
ATOM   12964 C  CG  . LEU L  1 106 ? -2.022  -8.646  17.851  1.00 47.00  ? 106 LEU W CG  1 
ATOM   12965 C  CD1 . LEU L  1 106 ? -1.960  -7.870  16.540  1.00 48.15  ? 106 LEU W CD1 1 
ATOM   12966 C  CD2 . LEU L  1 106 ? -3.407  -9.259  18.053  1.00 46.11  ? 106 LEU W CD2 1 
ATOM   12967 N  N   . SER L  1 107 ? 0.925   -11.728 20.292  1.00 49.46  ? 107 SER W N   1 
ATOM   12968 C  CA  . SER L  1 107 ? 1.848   -12.849 20.533  1.00 51.27  ? 107 SER W CA  1 
ATOM   12969 C  C   . SER L  1 107 ? 2.177   -13.014 22.031  1.00 50.49  ? 107 SER W C   1 
ATOM   12970 O  O   . SER L  1 107 ? 1.924   -12.111 22.846  1.00 48.61  ? 107 SER W O   1 
ATOM   12971 C  CB  . SER L  1 107 ? 3.130   -12.661 19.732  1.00 53.39  ? 107 SER W CB  1 
ATOM   12972 O  OG  . SER L  1 107 ? 3.766   -11.447 20.080  1.00 52.86  ? 107 SER W OG  1 
ATOM   12973 N  N   . GLY L  1 108 ? 2.724   -14.182 22.376  1.00 52.11  ? 108 GLY W N   1 
ATOM   12974 C  CA  . GLY L  1 108 ? 3.125   -14.503 23.756  1.00 51.90  ? 108 GLY W CA  1 
ATOM   12975 C  C   . GLY L  1 108 ? 2.023   -15.081 24.640  1.00 50.71  ? 108 GLY W C   1 
ATOM   12976 O  O   . GLY L  1 108 ? 1.034   -15.620 24.145  1.00 50.74  ? 108 GLY W O   1 
ATOM   12977 N  N   . ASP L  1 109 ? 2.205   -14.970 25.955  1.00 49.96  ? 109 ASP W N   1 
ATOM   12978 C  CA  . ASP L  1 109 ? 1.278   -15.552 26.943  1.00 49.16  ? 109 ASP W CA  1 
ATOM   12979 C  C   . ASP L  1 109 ? -0.086  -14.873 26.937  1.00 47.09  ? 109 ASP W C   1 
ATOM   12980 O  O   . ASP L  1 109 ? -1.106  -15.519 27.185  1.00 46.88  ? 109 ASP W O   1 
ATOM   12981 C  CB  . ASP L  1 109 ? 1.842   -15.435 28.365  1.00 48.83  ? 109 ASP W CB  1 
ATOM   12982 C  CG  . ASP L  1 109 ? 3.127   -16.209 28.565  1.00 51.14  ? 109 ASP W CG  1 
ATOM   12983 O  OD1 . ASP L  1 109 ? 3.327   -17.255 27.917  1.00 53.12  ? 109 ASP W OD1 1 
ATOM   12984 O  OD2 . ASP L  1 109 ? 3.945   -15.766 29.399  1.00 51.21  ? 109 ASP W OD2 1 
ATOM   12985 N  N   . HIS L  1 110 ? -0.092  -13.568 26.667  1.00 45.85  ? 110 HIS W N   1 
ATOM   12986 C  CA  . HIS L  1 110 ? -1.329  -12.790 26.580  1.00 44.13  ? 110 HIS W CA  1 
ATOM   12987 C  C   . HIS L  1 110 ? -1.839  -12.689 25.131  1.00 44.60  ? 110 HIS W C   1 
ATOM   12988 O  O   . HIS L  1 110 ? -2.568  -11.742 24.797  1.00 43.40  ? 110 HIS W O   1 
ATOM   12989 C  CB  . HIS L  1 110 ? -1.104  -11.380 27.142  1.00 42.69  ? 110 HIS W CB  1 
ATOM   12990 C  CG  . HIS L  1 110 ? -0.689  -11.344 28.580  1.00 42.29  ? 110 HIS W CG  1 
ATOM   12991 N  ND1 . HIS L  1 110 ? -0.697  -10.178 29.314  1.00 41.07  ? 110 HIS W ND1 1 
ATOM   12992 C  CD2 . HIS L  1 110 ? -0.274  -12.317 29.425  1.00 43.17  ? 110 HIS W CD2 1 
ATOM   12993 C  CE1 . HIS L  1 110 ? -0.283  -10.432 30.543  1.00 41.12  ? 110 HIS W CE1 1 
ATOM   12994 N  NE2 . HIS L  1 110 ? -0.023  -11.723 30.636  1.00 42.38  ? 110 HIS W NE2 1 
ATOM   12995 N  N   . CYS L  1 111 ? -1.472  -13.647 24.272  1.00 46.52  ? 111 CYS W N   1 
ATOM   12996 C  CA  . CYS L  1 111 ? -1.926  -13.635 22.880  1.00 47.26  ? 111 CYS W CA  1 
ATOM   12997 C  C   . CYS L  1 111 ? -3.402  -13.988 22.836  1.00 46.67  ? 111 CYS W C   1 
ATOM   12998 O  O   . CYS L  1 111 ? -3.817  -14.981 23.435  1.00 47.18  ? 111 CYS W O   1 
ATOM   12999 C  CB  . CYS L  1 111 ? -1.135  -14.610 21.999  1.00 49.75  ? 111 CYS W CB  1 
ATOM   13000 S  SG  . CYS L  1 111 ? -1.557  -14.470 20.241  1.00 50.91  ? 111 CYS W SG  1 
ATOM   13001 N  N   . ILE L  1 112 ? -4.181  -13.162 22.139  1.00 45.83  ? 112 ILE W N   1 
ATOM   13002 C  CA  . ILE L  1 112 ? -5.629  -13.370 22.014  1.00 45.47  ? 112 ILE W CA  1 
ATOM   13003 C  C   . ILE L  1 112 ? -6.040  -14.034 20.697  1.00 47.18  ? 112 ILE W C   1 
ATOM   13004 O  O   . ILE L  1 112 ? -7.221  -14.334 20.507  1.00 47.40  ? 112 ILE W O   1 
ATOM   13005 C  CB  . ILE L  1 112 ? -6.439  -12.059 22.213  1.00 43.65  ? 112 ILE W CB  1 
ATOM   13006 C  CG1 . ILE L  1 112 ? -6.047  -10.977 21.194  1.00 43.70  ? 112 ILE W CG1 1 
ATOM   13007 C  CG2 . ILE L  1 112 ? -6.259  -11.542 23.637  1.00 42.08  ? 112 ILE W CG2 1 
ATOM   13008 C  CD1 . ILE L  1 112 ? -7.041  -9.836  21.113  1.00 42.49  ? 112 ILE W CD1 1 
ATOM   13009 N  N   . ILE L  1 113 ? -5.083  -14.236 19.789  1.00 48.55  ? 113 ILE W N   1 
ATOM   13010 C  CA  . ILE L  1 113 ? -5.328  -14.995 18.558  1.00 50.53  ? 113 ILE W CA  1 
ATOM   13011 C  C   . ILE L  1 113 ? -5.635  -16.448 18.943  1.00 51.87  ? 113 ILE W C   1 
ATOM   13012 O  O   . ILE L  1 113 ? -4.962  -17.028 19.792  1.00 52.12  ? 113 ILE W O   1 
ATOM   13013 C  CB  . ILE L  1 113 ? -4.126  -14.905 17.581  1.00 52.04  ? 113 ILE W CB  1 
ATOM   13014 C  CG1 . ILE L  1 113 ? -4.036  -13.485 16.996  1.00 51.12  ? 113 ILE W CG1 1 
ATOM   13015 C  CG2 . ILE L  1 113 ? -4.241  -15.931 16.462  1.00 54.51  ? 113 ILE W CG2 1 
ATOM   13016 C  CD1 . ILE L  1 113 ? -2.712  -13.148 16.341  1.00 52.37  ? 113 ILE W CD1 1 
ATOM   13017 N  N   . GLY L  1 114 ? -6.674  -17.003 18.328  1.00 52.87  ? 114 GLY W N   1 
ATOM   13018 C  CA  . GLY L  1 114 ? -7.183  -18.320 18.686  1.00 54.37  ? 114 GLY W CA  1 
ATOM   13019 C  C   . GLY L  1 114 ? -8.220  -18.310 19.792  1.00 53.05  ? 114 GLY W C   1 
ATOM   13020 O  O   . GLY L  1 114 ? -8.716  -19.362 20.161  1.00 54.41  ? 114 GLY W O   1 
ATOM   13021 N  N   . ARG L  1 115 ? -8.549  -17.127 20.314  1.00 50.68  ? 115 ARG W N   1 
ATOM   13022 C  CA  . ARG L  1 115 ? -9.516  -16.968 21.400  1.00 49.44  ? 115 ARG W CA  1 
ATOM   13023 C  C   . ARG L  1 115 ? -10.743 -16.228 20.863  1.00 48.91  ? 115 ARG W C   1 
ATOM   13024 O  O   . ARG L  1 115 ? -10.809 -15.937 19.664  1.00 49.57  ? 115 ARG W O   1 
ATOM   13025 C  CB  . ARG L  1 115 ? -8.869  -16.215 22.567  1.00 47.37  ? 115 ARG W CB  1 
ATOM   13026 C  CG  . ARG L  1 115 ? -7.540  -16.813 23.007  1.00 48.01  ? 115 ARG W CG  1 
ATOM   13027 C  CD  . ARG L  1 115 ? -7.075  -16.277 24.351  1.00 46.30  ? 115 ARG W CD  1 
ATOM   13028 N  NE  . ARG L  1 115 ? -5.773  -16.841 24.712  1.00 47.19  ? 115 ARG W NE  1 
ATOM   13029 C  CZ  . ARG L  1 115 ? -5.567  -18.043 25.264  1.00 48.72  ? 115 ARG W CZ  1 
ATOM   13030 N  NH1 . ARG L  1 115 ? -6.583  -18.854 25.573  1.00 49.53  ? 115 ARG W NH1 1 
ATOM   13031 N  NH2 . ARG L  1 115 ? -4.317  -18.429 25.541  1.00 49.60  ? 115 ARG W NH2 1 
ATOM   13032 N  N   . THR L  1 116 ? -11.704 -15.927 21.740  1.00 47.92  ? 116 THR W N   1 
ATOM   13033 C  CA  . THR L  1 116 ? -12.992 -15.369 21.324  1.00 47.84  ? 116 THR W CA  1 
ATOM   13034 C  C   . THR L  1 116 ? -13.212 -13.948 21.832  1.00 45.59  ? 116 THR W C   1 
ATOM   13035 O  O   . THR L  1 116 ? -13.108 -13.686 23.030  1.00 44.27  ? 116 THR W O   1 
ATOM   13036 C  CB  . THR L  1 116 ? -14.159 -16.262 21.793  1.00 49.23  ? 116 THR W CB  1 
ATOM   13037 O  OG1 . THR L  1 116 ? -13.988 -17.581 21.265  1.00 51.65  ? 116 THR W OG1 1 
ATOM   13038 C  CG2 . THR L  1 116 ? -15.503 -15.719 21.298  1.00 49.54  ? 116 THR W CG2 1 
ATOM   13039 N  N   . LEU L  1 117 ? -13.530 -13.047 20.903  1.00 45.36  ? 117 LEU W N   1 
ATOM   13040 C  CA  . LEU L  1 117 ? -13.980 -11.701 21.223  1.00 43.76  ? 117 LEU W CA  1 
ATOM   13041 C  C   . LEU L  1 117 ? -15.487 -11.772 21.378  1.00 44.34  ? 117 LEU W C   1 
ATOM   13042 O  O   . LEU L  1 117 ? -16.155 -12.364 20.540  1.00 46.09  ? 117 LEU W O   1 
ATOM   13043 C  CB  . LEU L  1 117 ? -13.629 -10.735 20.087  1.00 43.73  ? 117 LEU W CB  1 
ATOM   13044 C  CG  . LEU L  1 117 ? -14.018 -9.268  20.291  1.00 42.39  ? 117 LEU W CG  1 
ATOM   13045 C  CD1 . LEU L  1 117 ? -13.261 -8.675  21.471  1.00 40.62  ? 117 LEU W CD1 1 
ATOM   13046 C  CD2 . LEU L  1 117 ? -13.762 -8.483  19.016  1.00 42.96  ? 117 LEU W CD2 1 
ATOM   13047 N  N   . VAL L  1 118 ? -16.017 -11.161 22.432  1.00 43.12  ? 118 VAL W N   1 
ATOM   13048 C  CA  . VAL L  1 118 ? -17.448 -11.261 22.761  1.00 43.89  ? 118 VAL W CA  1 
ATOM   13049 C  C   . VAL L  1 118 ? -18.017 -9.883  23.079  1.00 42.73  ? 118 VAL W C   1 
ATOM   13050 O  O   . VAL L  1 118 ? -17.437 -9.150  23.880  1.00 41.05  ? 118 VAL W O   1 
ATOM   13051 C  CB  . VAL L  1 118 ? -17.690 -12.195 23.968  1.00 44.16  ? 118 VAL W CB  1 
ATOM   13052 C  CG1 . VAL L  1 118 ? -19.171 -12.239 24.344  1.00 45.15  ? 118 VAL W CG1 1 
ATOM   13053 C  CG2 . VAL L  1 118 ? -17.180 -13.590 23.664  1.00 45.72  ? 118 VAL W CG2 1 
ATOM   13054 N  N   . VAL L  1 119 ? -19.150 -9.545  22.455  1.00 43.85  ? 119 VAL W N   1 
ATOM   13055 C  CA  . VAL L  1 119 ? -19.903 -8.333  22.817  1.00 43.21  ? 119 VAL W CA  1 
ATOM   13056 C  C   . VAL L  1 119 ? -21.159 -8.738  23.603  1.00 44.16  ? 119 VAL W C   1 
ATOM   13057 O  O   . VAL L  1 119 ? -21.817 -9.718  23.278  1.00 45.98  ? 119 VAL W O   1 
ATOM   13058 C  CB  . VAL L  1 119 ? -20.211 -7.419  21.599  1.00 43.81  ? 119 VAL W CB  1 
ATOM   13059 C  CG1 . VAL L  1 119 ? -21.182 -8.065  20.614  1.00 46.07  ? 119 VAL W CG1 1 
ATOM   13060 C  CG2 . VAL L  1 119 ? -20.750 -6.071  22.070  1.00 43.05  ? 119 VAL W CG2 1 
ATOM   13061 N  N   . HIS L  1 120 ? -21.462 -7.966  24.642  1.00 43.17  ? 120 HIS W N   1 
ATOM   13062 C  CA  . HIS L  1 120 ? -22.433 -8.342  25.673  1.00 43.85  ? 120 HIS W CA  1 
ATOM   13063 C  C   . HIS L  1 120 ? -23.698 -7.487  25.616  1.00 44.66  ? 120 HIS W C   1 
ATOM   13064 O  O   . HIS L  1 120 ? -23.757 -6.464  24.920  1.00 44.47  ? 120 HIS W O   1 
ATOM   13065 C  CB  . HIS L  1 120 ? -21.791 -8.218  27.065  1.00 42.34  ? 120 HIS W CB  1 
ATOM   13066 C  CG  . HIS L  1 120 ? -21.086 -9.456  27.530  1.00 42.51  ? 120 HIS W CG  1 
ATOM   13067 N  ND1 . HIS L  1 120 ? -21.669 -10.366 28.386  1.00 43.67  ? 120 HIS W ND1 1 
ATOM   13068 C  CD2 . HIS L  1 120 ? -19.839 -9.921  27.279  1.00 41.91  ? 120 HIS W CD2 1 
ATOM   13069 C  CE1 . HIS L  1 120 ? -20.815 -11.345 28.634  1.00 43.72  ? 120 HIS W CE1 1 
ATOM   13070 N  NE2 . HIS L  1 120 ? -19.698 -11.099 27.974  1.00 42.67  ? 120 HIS W NE2 1 
ATOM   13071 N  N   . GLU L  1 121 ? -24.694 -7.930  26.379  1.00 45.71  ? 121 GLU W N   1 
ATOM   13072 C  CA  . GLU L  1 121 ? -26.026 -7.344  26.412  1.00 47.02  ? 121 GLU W CA  1 
ATOM   13073 C  C   . GLU L  1 121 ? -26.052 -5.893  26.894  1.00 45.63  ? 121 GLU W C   1 
ATOM   13074 O  O   . GLU L  1 121 ? -26.674 -5.036  26.262  1.00 46.32  ? 121 GLU W O   1 
ATOM   13075 C  CB  . GLU L  1 121 ? -26.900 -8.194  27.338  1.00 48.61  ? 121 GLU W CB  1 
ATOM   13076 C  CG  . GLU L  1 121 ? -28.381 -7.865  27.331  1.00 50.77  ? 121 GLU W CG  1 
ATOM   13077 C  CD  . GLU L  1 121 ? -29.120 -8.481  28.507  1.00 52.08  ? 121 GLU W CD  1 
ATOM   13078 O  OE1 . GLU L  1 121 ? -28.533 -9.320  29.230  1.00 51.60  ? 121 GLU W OE1 1 
ATOM   13079 O  OE2 . GLU L  1 121 ? -30.295 -8.115  28.709  1.00 53.85  ? 121 GLU W OE2 1 
ATOM   13080 N  N   . LYS L  1 122 ? -25.383 -5.647  28.020  1.00 43.80  ? 122 LYS W N   1 
ATOM   13081 C  CA  . LYS L  1 122 ? -25.458 -4.373  28.732  1.00 42.72  ? 122 LYS W CA  1 
ATOM   13082 C  C   . LYS L  1 122 ? -24.082 -3.991  29.314  1.00 40.33  ? 122 LYS W C   1 
ATOM   13083 O  O   . LYS L  1 122 ? -23.058 -4.593  28.955  1.00 39.53  ? 122 LYS W O   1 
ATOM   13084 C  CB  . LYS L  1 122 ? -26.558 -4.463  29.804  1.00 43.93  ? 122 LYS W CB  1 
ATOM   13085 C  CG  . LYS L  1 122 ? -26.330 -5.518  30.864  1.00 43.86  ? 122 LYS W CG  1 
ATOM   13086 C  CD  . LYS L  1 122 ? -27.563 -5.709  31.733  1.00 45.65  ? 122 LYS W CD  1 
ATOM   13087 C  CE  . LYS L  1 122 ? -27.179 -6.346  33.062  1.00 45.23  ? 122 LYS W CE  1 
ATOM   13088 N  NZ  . LYS L  1 122 ? -28.348 -6.834  33.841  1.00 47.43  ? 122 LYS W NZ  1 
ATOM   13089 N  N   . ALA L  1 123 ? -24.053 -2.975  30.175  1.00 39.32  ? 123 ALA W N   1 
ATOM   13090 C  CA  . ALA L  1 123 ? -22.800 -2.399  30.647  1.00 37.34  ? 123 ALA W CA  1 
ATOM   13091 C  C   . ALA L  1 123 ? -21.989 -3.340  31.540  1.00 36.29  ? 123 ALA W C   1 
ATOM   13092 O  O   . ALA L  1 123 ? -22.528 -3.994  32.430  1.00 36.81  ? 123 ALA W O   1 
ATOM   13093 C  CB  . ALA L  1 123 ? -23.073 -1.096  31.388  1.00 37.12  ? 123 ALA W CB  1 
ATOM   13094 N  N   . ASP L  1 124 ? -20.685 -3.393  31.271  1.00 34.95  ? 124 ASP W N   1 
ATOM   13095 C  CA  . ASP L  1 124 ? -19.705 -3.920  32.205  1.00 33.87  ? 124 ASP W CA  1 
ATOM   13096 C  C   . ASP L  1 124 ? -19.556 -2.862  33.298  1.00 32.99  ? 124 ASP W C   1 
ATOM   13097 O  O   . ASP L  1 124 ? -19.255 -1.706  32.989  1.00 32.57  ? 124 ASP W O   1 
ATOM   13098 C  CB  . ASP L  1 124 ? -18.380 -4.150  31.471  1.00 33.13  ? 124 ASP W CB  1 
ATOM   13099 C  CG  . ASP L  1 124 ? -17.363 -4.930  32.285  1.00 32.55  ? 124 ASP W CG  1 
ATOM   13100 O  OD1 . ASP L  1 124 ? -17.380 -4.877  33.536  1.00 32.17  ? 124 ASP W OD1 1 
ATOM   13101 O  OD2 . ASP L  1 124 ? -16.513 -5.588  31.645  1.00 32.56  ? 124 ASP W OD2 1 
ATOM   13102 N  N   . ASP L  1 125 ? -19.789 -3.242  34.557  1.00 32.93  ? 125 ASP W N   1 
ATOM   13103 C  CA  . ASP L  1 125 ? -19.594 -2.315  35.684  1.00 32.31  ? 125 ASP W CA  1 
ATOM   13104 C  C   . ASP L  1 125 ? -18.110 -2.128  36.105  1.00 31.12  ? 125 ASP W C   1 
ATOM   13105 O  O   . ASP L  1 125 ? -17.827 -1.397  37.050  1.00 30.75  ? 125 ASP W O   1 
ATOM   13106 C  CB  . ASP L  1 125 ? -20.488 -2.691  36.888  1.00 33.08  ? 125 ASP W CB  1 
ATOM   13107 C  CG  . ASP L  1 125 ? -19.992 -3.911  37.682  1.00 33.07  ? 125 ASP W CG  1 
ATOM   13108 O  OD1 . ASP L  1 125 ? -18.834 -4.373  37.507  1.00 32.23  ? 125 ASP W OD1 1 
ATOM   13109 O  OD2 . ASP L  1 125 ? -20.793 -4.403  38.514  1.00 34.03  ? 125 ASP W OD2 1 
ATOM   13110 N  N   . LEU L  1 126 ? -17.194 -2.831  35.430  1.00 30.78  ? 126 LEU W N   1 
ATOM   13111 C  CA  . LEU L  1 126 ? -15.743 -2.616  35.537  1.00 29.97  ? 126 LEU W CA  1 
ATOM   13112 C  C   . LEU L  1 126 ? -15.194 -2.938  36.933  1.00 29.78  ? 126 LEU W C   1 
ATOM   13113 O  O   . LEU L  1 126 ? -14.199 -2.348  37.370  1.00 29.28  ? 126 LEU W O   1 
ATOM   13114 C  CB  . LEU L  1 126 ? -15.370 -1.186  35.104  1.00 29.62  ? 126 LEU W CB  1 
ATOM   13115 C  CG  . LEU L  1 126 ? -16.036 -0.653  33.821  1.00 30.10  ? 126 LEU W CG  1 
ATOM   13116 C  CD1 . LEU L  1 126 ? -15.568 0.759   33.503  1.00 30.02  ? 126 LEU W CD1 1 
ATOM   13117 C  CD2 . LEU L  1 126 ? -15.800 -1.576  32.636  1.00 30.33  ? 126 LEU W CD2 1 
ATOM   13118 N  N   . GLY L  1 127 ? -15.841 -3.890  37.612  1.00 30.40  ? 127 GLY W N   1 
ATOM   13119 C  CA  . GLY L  1 127 ? -15.462 -4.299  38.957  1.00 30.52  ? 127 GLY W CA  1 
ATOM   13120 C  C   . GLY L  1 127 ? -15.919 -3.397  40.093  1.00 30.60  ? 127 GLY W C   1 
ATOM   13121 O  O   . GLY L  1 127 ? -15.510 -3.607  41.224  1.00 30.66  ? 127 GLY W O   1 
ATOM   13122 N  N   . LYS L  1 128 ? -16.790 -2.428  39.818  1.00 30.82  ? 128 LYS W N   1 
ATOM   13123 C  CA  . LYS L  1 128 ? -17.136 -1.404  40.803  1.00 31.10  ? 128 LYS W CA  1 
ATOM   13124 C  C   . LYS L  1 128 ? -18.556 -1.525  41.380  1.00 32.20  ? 128 LYS W C   1 
ATOM   13125 O  O   . LYS L  1 128 ? -19.051 -0.577  41.992  1.00 32.58  ? 128 LYS W O   1 
ATOM   13126 C  CB  . LYS L  1 128 ? -16.928 -0.021  40.181  1.00 30.86  ? 128 LYS W CB  1 
ATOM   13127 C  CG  . LYS L  1 128 ? -15.480 0.237   39.803  1.00 30.20  ? 128 LYS W CG  1 
ATOM   13128 C  CD  . LYS L  1 128 ? -15.319 1.478   38.949  1.00 30.29  ? 128 LYS W CD  1 
ATOM   13129 C  CE  . LYS L  1 128 ? -15.268 2.740   39.784  1.00 30.70  ? 128 LYS W CE  1 
ATOM   13130 N  NZ  . LYS L  1 128 ? -14.995 3.915   38.920  1.00 31.02  ? 128 LYS W NZ  1 
ATOM   13131 N  N   . GLY L  1 129 ? -19.177 -2.695  41.214  1.00 32.97  ? 129 GLY W N   1 
ATOM   13132 C  CA  . GLY L  1 129 ? -20.563 -2.935  41.627  1.00 34.39  ? 129 GLY W CA  1 
ATOM   13133 C  C   . GLY L  1 129 ? -20.772 -3.315  43.085  1.00 35.24  ? 129 GLY W C   1 
ATOM   13134 O  O   . GLY L  1 129 ? -21.906 -3.259  43.583  1.00 36.49  ? 129 GLY W O   1 
ATOM   13135 N  N   . GLY L  1 130 ? -19.695 -3.712  43.768  1.00 34.75  ? 130 GLY W N   1 
ATOM   13136 C  CA  . GLY L  1 130 ? -19.747 -4.040  45.189  1.00 35.62  ? 130 GLY W CA  1 
ATOM   13137 C  C   . GLY L  1 130 ? -20.399 -5.369  45.529  1.00 37.24  ? 130 GLY W C   1 
ATOM   13138 O  O   . GLY L  1 130 ? -20.893 -5.545  46.646  1.00 38.38  ? 130 GLY W O   1 
ATOM   13139 N  N   . ASN L  1 131 ? -20.407 -6.297  44.572  1.00 37.59  ? 131 ASN W N   1 
ATOM   13140 C  CA  . ASN L  1 131 ? -20.834 -7.679  44.817  1.00 39.39  ? 131 ASN W CA  1 
ATOM   13141 C  C   . ASN L  1 131 ? -19.836 -8.660  44.208  1.00 39.18  ? 131 ASN W C   1 
ATOM   13142 O  O   . ASN L  1 131 ? -18.941 -8.259  43.458  1.00 37.68  ? 131 ASN W O   1 
ATOM   13143 C  CB  . ASN L  1 131 ? -22.267 -7.938  44.309  1.00 40.95  ? 131 ASN W CB  1 
ATOM   13144 C  CG  . ASN L  1 131 ? -22.459 -7.620  42.835  1.00 40.28  ? 131 ASN W CG  1 
ATOM   13145 O  OD1 . ASN L  1 131 ? -21.568 -7.797  42.012  1.00 39.15  ? 131 ASN W OD1 1 
ATOM   13146 N  ND2 . ASN L  1 131 ? -23.651 -7.174  42.495  1.00 41.26  ? 131 ASN W ND2 1 
ATOM   13147 N  N   . GLU L  1 132 ? -19.996 -9.941  44.536  1.00 41.03  ? 132 GLU W N   1 
ATOM   13148 C  CA  . GLU L  1 132 ? -19.071 -10.979 44.070  1.00 41.28  ? 132 GLU W CA  1 
ATOM   13149 C  C   . GLU L  1 132 ? -19.052 -11.080 42.550  1.00 40.85  ? 132 GLU W C   1 
ATOM   13150 O  O   . GLU L  1 132 ? -17.994 -11.271 41.960  1.00 40.04  ? 132 GLU W O   1 
ATOM   13151 C  CB  . GLU L  1 132 ? -19.412 -12.344 44.679  1.00 43.66  ? 132 GLU W CB  1 
ATOM   13152 C  CG  . GLU L  1 132 ? -18.307 -13.376 44.491  1.00 44.04  ? 132 GLU W CG  1 
ATOM   13153 C  CD  . GLU L  1 132 ? -18.633 -14.721 45.118  1.00 46.69  ? 132 GLU W CD  1 
ATOM   13154 O  OE1 . GLU L  1 132 ? -19.699 -15.298 44.801  1.00 48.52  ? 132 GLU W OE1 1 
ATOM   13155 O  OE2 . GLU L  1 132 ? -17.810 -15.211 45.922  1.00 47.26  ? 132 GLU W OE2 1 
ATOM   13156 N  N   . GLU L  1 133 ? -20.218 -10.926 41.927  1.00 41.62  ? 133 GLU W N   1 
ATOM   13157 C  CA  . GLU L  1 133 ? -20.340 -11.033 40.480  1.00 41.52  ? 133 GLU W CA  1 
ATOM   13158 C  C   . GLU L  1 133 ? -19.575 -9.937  39.730  1.00 39.35  ? 133 GLU W C   1 
ATOM   13159 O  O   . GLU L  1 133 ? -19.041 -10.184 38.651  1.00 38.87  ? 133 GLU W O   1 
ATOM   13160 C  CB  . GLU L  1 133 ? -21.819 -11.009 40.080  1.00 43.13  ? 133 GLU W CB  1 
ATOM   13161 C  CG  . GLU L  1 133 ? -22.110 -11.473 38.660  1.00 43.89  ? 133 GLU W CG  1 
ATOM   13162 C  CD  . GLU L  1 133 ? -21.670 -12.901 38.387  1.00 45.27  ? 133 GLU W CD  1 
ATOM   13163 O  OE1 . GLU L  1 133 ? -21.716 -13.741 39.311  1.00 46.74  ? 133 GLU W OE1 1 
ATOM   13164 O  OE2 . GLU L  1 133 ? -21.272 -13.184 37.241  1.00 45.20  ? 133 GLU W OE2 1 
ATOM   13165 N  N   . SER L  1 134 ? -19.525 -8.735  40.303  1.00 38.18  ? 134 SER W N   1 
ATOM   13166 C  CA  . SER L  1 134 ? -18.799 -7.612  39.706  1.00 36.45  ? 134 SER W CA  1 
ATOM   13167 C  C   . SER L  1 134 ? -17.316 -7.930  39.478  1.00 35.61  ? 134 SER W C   1 
ATOM   13168 O  O   . SER L  1 134 ? -16.763 -7.594  38.428  1.00 34.75  ? 134 SER W O   1 
ATOM   13169 C  CB  . SER L  1 134 ? -18.932 -6.367  40.583  1.00 35.75  ? 134 SER W CB  1 
ATOM   13170 O  OG  . SER L  1 134 ? -18.353 -5.236  39.969  1.00 34.40  ? 134 SER W OG  1 
ATOM   13171 N  N   . THR L  1 135 ? -16.705 -8.604  40.455  1.00 36.04  ? 135 THR W N   1 
ATOM   13172 C  CA  . THR L  1 135 ? -15.287 -8.972  40.405  1.00 35.67  ? 135 THR W CA  1 
ATOM   13173 C  C   . THR L  1 135 ? -14.994 -10.268 39.630  1.00 36.65  ? 135 THR W C   1 
ATOM   13174 O  O   . THR L  1 135 ? -13.836 -10.685 39.571  1.00 36.54  ? 135 THR W O   1 
ATOM   13175 C  CB  . THR L  1 135 ? -14.698 -9.105  41.831  1.00 35.93  ? 135 THR W CB  1 
ATOM   13176 O  OG1 . THR L  1 135 ? -15.345 -10.175 42.529  1.00 37.56  ? 135 THR W OG1 1 
ATOM   13177 C  CG2 . THR L  1 135 ? -14.877 -7.810  42.608  1.00 35.19  ? 135 THR W CG2 1 
ATOM   13178 N  N   . LYS L  1 136 ? -16.023 -10.889 39.046  1.00 37.82  ? 136 LYS W N   1 
ATOM   13179 C  CA  . LYS L  1 136 ? -15.889 -12.061 38.177  1.00 39.06  ? 136 LYS W CA  1 
ATOM   13180 C  C   . LYS L  1 136 ? -16.250 -11.743 36.718  1.00 38.85  ? 136 LYS W C   1 
ATOM   13181 O  O   . LYS L  1 136 ? -15.472 -12.020 35.813  1.00 38.72  ? 136 LYS W O   1 
ATOM   13182 C  CB  . LYS L  1 136 ? -16.794 -13.189 38.681  1.00 41.23  ? 136 LYS W CB  1 
ATOM   13183 C  CG  . LYS L  1 136 ? -16.313 -13.846 39.962  1.00 42.09  ? 136 LYS W CG  1 
ATOM   13184 C  CD  . LYS L  1 136 ? -17.379 -14.752 40.562  1.00 44.37  ? 136 LYS W CD  1 
ATOM   13185 C  CE  . LYS L  1 136 ? -16.777 -15.844 41.431  1.00 45.91  ? 136 LYS W CE  1 
ATOM   13186 N  NZ  . LYS L  1 136 ? -15.866 -15.312 42.488  1.00 44.82  ? 136 LYS W NZ  1 
ATOM   13187 N  N   . THR L  1 137 ? -17.447 -11.196 36.496  1.00 39.07  ? 137 THR W N   1 
ATOM   13188 C  CA  . THR L  1 137 ? -17.946 -10.899 35.140  1.00 39.16  ? 137 THR W CA  1 
ATOM   13189 C  C   . THR L  1 137 ? -18.223 -9.423  34.851  1.00 37.83  ? 137 THR W C   1 
ATOM   13190 O  O   . THR L  1 137 ? -18.303 -9.033  33.692  1.00 37.70  ? 137 THR W O   1 
ATOM   13191 C  CB  . THR L  1 137 ? -19.252 -11.664 34.854  1.00 41.23  ? 137 THR W CB  1 
ATOM   13192 O  OG1 . THR L  1 137 ? -20.289 -11.192 35.727  1.00 41.67  ? 137 THR W OG1 1 
ATOM   13193 C  CG2 . THR L  1 137 ? -19.052 -13.174 35.030  1.00 42.95  ? 137 THR W CG2 1 
ATOM   13194 N  N   . GLY L  1 138 ? -18.389 -8.612  35.889  1.00 37.08  ? 138 GLY W N   1 
ATOM   13195 C  CA  . GLY L  1 138 ? -18.784 -7.219  35.727  1.00 36.24  ? 138 GLY W CA  1 
ATOM   13196 C  C   . GLY L  1 138 ? -20.272 -7.007  35.467  1.00 37.35  ? 138 GLY W C   1 
ATOM   13197 O  O   . GLY L  1 138 ? -20.669 -5.915  35.068  1.00 36.91  ? 138 GLY W O   1 
ATOM   13198 N  N   . ASN L  1 139 ? -21.085 -8.037  35.714  1.00 38.98  ? 139 ASN W N   1 
ATOM   13199 C  CA  . ASN L  1 139 ? -22.549 -7.979  35.549  1.00 40.58  ? 139 ASN W CA  1 
ATOM   13200 C  C   . ASN L  1 139 ? -22.997 -7.467  34.177  1.00 40.79  ? 139 ASN W C   1 
ATOM   13201 O  O   . ASN L  1 139 ? -23.887 -6.618  34.093  1.00 41.34  ? 139 ASN W O   1 
ATOM   13202 C  CB  . ASN L  1 139 ? -23.165 -7.122  36.669  1.00 40.60  ? 139 ASN W CB  1 
ATOM   13203 C  CG  . ASN L  1 139 ? -22.912 -7.697  38.039  1.00 40.82  ? 139 ASN W CG  1 
ATOM   13204 O  OD1 . ASN L  1 139 ? -23.414 -8.765  38.358  1.00 42.49  ? 139 ASN W OD1 1 
ATOM   13205 N  ND2 . ASN L  1 139 ? -22.128 -6.999  38.855  1.00 39.42  ? 139 ASN W ND2 1 
ATOM   13206 N  N   . ALA L  1 140 ? -22.386 -7.993  33.116  1.00 40.68  ? 140 ALA W N   1 
ATOM   13207 C  CA  . ALA L  1 140 ? -22.601 -7.499  31.746  1.00 40.88  ? 140 ALA W CA  1 
ATOM   13208 C  C   . ALA L  1 140 ? -23.750 -8.161  30.967  1.00 43.12  ? 140 ALA W C   1 
ATOM   13209 O  O   . ALA L  1 140 ? -23.980 -7.816  29.796  1.00 43.54  ? 140 ALA W O   1 
ATOM   13210 C  CB  . ALA L  1 140 ? -21.312 -7.602  30.944  1.00 39.79  ? 140 ALA W CB  1 
ATOM   13211 N  N   . GLY L  1 141 ? -24.461 -9.097  31.592  1.00 44.74  ? 141 GLY W N   1 
ATOM   13212 C  CA  . GLY L  1 141 ? -25.561 -9.788  30.936  1.00 47.22  ? 141 GLY W CA  1 
ATOM   13213 C  C   . GLY L  1 141 ? -25.090 -10.829 29.936  1.00 48.06  ? 141 GLY W C   1 
ATOM   13214 O  O   . GLY L  1 141 ? -23.943 -11.294 29.993  1.00 47.05  ? 141 GLY W O   1 
ATOM   13215 N  N   . SER L  1 142 ? -25.985 -11.173 29.010  1.00 50.12  ? 142 SER W N   1 
ATOM   13216 C  CA  . SER L  1 142 ? -25.794 -12.280 28.076  1.00 51.61  ? 142 SER W CA  1 
ATOM   13217 C  C   . SER L  1 142 ? -24.829 -11.928 26.947  1.00 50.34  ? 142 SER W C   1 
ATOM   13218 O  O   . SER L  1 142 ? -24.483 -10.758 26.748  1.00 48.54  ? 142 SER W O   1 
ATOM   13219 C  CB  . SER L  1 142 ? -27.147 -12.690 27.471  1.00 54.58  ? 142 SER W CB  1 
ATOM   13220 O  OG  . SER L  1 142 ? -28.118 -12.960 28.480  1.00 56.13  ? 142 SER W OG  1 
ATOM   13221 N  N   . ARG L  1 143 ? -24.426 -12.958 26.201  1.00 51.56  ? 143 ARG W N   1 
ATOM   13222 C  CA  . ARG L  1 143 ? -23.451 -12.836 25.108  1.00 50.78  ? 143 ARG W CA  1 
ATOM   13223 C  C   . ARG L  1 143 ? -24.175 -12.751 23.760  1.00 52.54  ? 143 ARG W C   1 
ATOM   13224 O  O   . ARG L  1 143 ? -24.701 -13.749 23.254  1.00 55.00  ? 143 ARG W O   1 
ATOM   13225 C  CB  . ARG L  1 143 ? -22.479 -14.026 25.127  1.00 51.16  ? 143 ARG W CB  1 
ATOM   13226 C  CG  . ARG L  1 143 ? -21.717 -14.177 26.441  1.00 49.74  ? 143 ARG W CG  1 
ATOM   13227 C  CD  . ARG L  1 143 ? -20.835 -15.418 26.475  1.00 50.60  ? 143 ARG W CD  1 
ATOM   13228 N  NE  . ARG L  1 143 ? -20.392 -15.733 27.838  1.00 49.98  ? 143 ARG W NE  1 
ATOM   13229 C  CZ  . ARG L  1 143 ? -19.521 -16.690 28.170  1.00 50.50  ? 143 ARG W CZ  1 
ATOM   13230 N  NH1 . ARG L  1 143 ? -18.948 -17.460 27.247  1.00 51.66  ? 143 ARG W NH1 1 
ATOM   13231 N  NH2 . ARG L  1 143 ? -19.209 -16.873 29.452  1.00 50.03  ? 143 ARG W NH2 1 
ATOM   13232 N  N   . LEU L  1 144 ? -24.180 -11.558 23.170  1.00 51.52  ? 144 LEU W N   1 
ATOM   13233 C  CA  . LEU L  1 144 ? -24.966 -11.299 21.958  1.00 53.20  ? 144 LEU W CA  1 
ATOM   13234 C  C   . LEU L  1 144 ? -24.278 -11.808 20.692  1.00 53.88  ? 144 LEU W C   1 
ATOM   13235 O  O   . LEU L  1 144 ? -24.930 -12.377 19.823  1.00 56.20  ? 144 LEU W O   1 
ATOM   13236 C  CB  . LEU L  1 144 ? -25.263 -9.803  21.813  1.00 52.14  ? 144 LEU W CB  1 
ATOM   13237 C  CG  . LEU L  1 144 ? -25.868 -9.074  23.020  1.00 51.41  ? 144 LEU W CG  1 
ATOM   13238 C  CD1 . LEU L  1 144 ? -25.998 -7.587  22.696  1.00 50.56  ? 144 LEU W CD1 1 
ATOM   13239 C  CD2 . LEU L  1 144 ? -27.210 -9.682  23.432  1.00 53.74  ? 144 LEU W CD2 1 
ATOM   13240 N  N   . ALA L  1 145 ? -22.970 -11.578 20.575  1.00 52.03  ? 145 ALA W N   1 
ATOM   13241 C  CA  . ALA L  1 145 ? -22.218 -11.992 19.382  1.00 52.70  ? 145 ALA W CA  1 
ATOM   13242 C  C   . ALA L  1 145 ? -20.765 -12.294 19.701  1.00 51.20  ? 145 ALA W C   1 
ATOM   13243 O  O   . ALA L  1 145 ? -20.225 -11.834 20.713  1.00 49.17  ? 145 ALA W O   1 
ATOM   13244 C  CB  . ALA L  1 145 ? -22.306 -10.927 18.298  1.00 52.68  ? 145 ALA W CB  1 
ATOM   13245 N  N   . ALA L  1 146 ? -20.142 -13.069 18.817  1.00 52.39  ? 146 ALA W N   1 
ATOM   13246 C  CA  . ALA L  1 146 ? -18.793 -13.566 19.040  1.00 51.59  ? 146 ALA W CA  1 
ATOM   13247 C  C   . ALA L  1 146 ? -18.121 -14.041 17.758  1.00 52.93  ? 146 ALA W C   1 
ATOM   13248 O  O   . ALA L  1 146 ? -18.785 -14.345 16.755  1.00 55.00  ? 146 ALA W O   1 
ATOM   13249 C  CB  . ALA L  1 146 ? -18.817 -14.696 20.066  1.00 52.19  ? 146 ALA W CB  1 
ATOM   13250 N  N   . GLY L  1 147 ? -16.793 -14.088 17.806  1.00 51.93  ? 147 GLY W N   1 
ATOM   13251 C  CA  . GLY L  1 147 ? -15.995 -14.667 16.738  1.00 53.33  ? 147 GLY W CA  1 
ATOM   13252 C  C   . GLY L  1 147 ? -14.649 -15.113 17.253  1.00 52.64  ? 147 GLY W C   1 
ATOM   13253 O  O   . GLY L  1 147 ? -14.132 -14.537 18.217  1.00 50.63  ? 147 GLY W O   1 
ATOM   13254 N  N   . VAL L  1 148 ? -14.078 -16.138 16.624  1.00 54.45  ? 148 VAL W N   1 
ATOM   13255 C  CA  . VAL L  1 148 ? -12.728 -16.564 16.971  1.00 54.18  ? 148 VAL W CA  1 
ATOM   13256 C  C   . VAL L  1 148 ? -11.753 -15.596 16.293  1.00 53.26  ? 148 VAL W C   1 
ATOM   13257 O  O   . VAL L  1 148 ? -11.891 -15.301 15.101  1.00 54.26  ? 148 VAL W O   1 
ATOM   13258 C  CB  . VAL L  1 148 ? -12.429 -18.011 16.545  1.00 56.82  ? 148 VAL W CB  1 
ATOM   13259 C  CG1 . VAL L  1 148 ? -11.018 -18.401 16.987  1.00 56.68  ? 148 VAL W CG1 1 
ATOM   13260 C  CG2 . VAL L  1 148 ? -13.458 -18.970 17.139  1.00 58.15  ? 148 VAL W CG2 1 
ATOM   13261 N  N   . ILE L  1 149 ? -10.784 -15.101 17.058  1.00 51.55  ? 149 ILE W N   1 
ATOM   13262 C  CA  . ILE L  1 149 ? -9.799  -14.139 16.550  1.00 50.83  ? 149 ILE W CA  1 
ATOM   13263 C  C   . ILE L  1 149 ? -8.705  -14.871 15.766  1.00 52.69  ? 149 ILE W C   1 
ATOM   13264 O  O   . ILE L  1 149 ? -7.995  -15.708 16.330  1.00 53.19  ? 149 ILE W O   1 
ATOM   13265 C  CB  . ILE L  1 149 ? -9.163  -13.326 17.693  1.00 48.65  ? 149 ILE W CB  1 
ATOM   13266 C  CG1 . ILE L  1 149 ? -10.237 -12.526 18.446  1.00 46.96  ? 149 ILE W CG1 1 
ATOM   13267 C  CG2 . ILE L  1 149 ? -8.089  -12.379 17.156  1.00 48.39  ? 149 ILE W CG2 1 
ATOM   13268 C  CD1 . ILE L  1 149 ? -9.867  -12.206 19.880  1.00 45.20  ? 149 ILE W CD1 1 
ATOM   13269 N  N   . GLY L  1 150 ? -8.573  -14.545 14.476  1.00 53.85  ? 150 GLY W N   1 
ATOM   13270 C  CA  . GLY L  1 150 ? -7.585  -15.171 13.592  1.00 55.93  ? 150 GLY W CA  1 
ATOM   13271 C  C   . GLY L  1 150 ? -6.539  -14.190 13.086  1.00 55.72  ? 150 GLY W C   1 
ATOM   13272 O  O   . GLY L  1 150 ? -6.713  -12.969 13.183  1.00 54.15  ? 150 GLY W O   1 
ATOM   13273 N  N   . ILE L  1 151 ? -5.458  -14.740 12.532  1.00 57.57  ? 151 ILE W N   1 
ATOM   13274 C  CA  . ILE L  1 151 ? -4.321  -13.956 12.028  1.00 57.96  ? 151 ILE W CA  1 
ATOM   13275 C  C   . ILE L  1 151 ? -4.697  -13.332 10.683  1.00 59.06  ? 151 ILE W C   1 
ATOM   13276 O  O   . ILE L  1 151 ? -5.410  -13.943 9.886   1.00 60.47  ? 151 ILE W O   1 
ATOM   13277 C  CB  . ILE L  1 151 ? -3.042  -14.819 11.816  1.00 60.01  ? 151 ILE W CB  1 
ATOM   13278 C  CG1 . ILE L  1 151 ? -2.648  -15.582 13.087  1.00 59.44  ? 151 ILE W CG1 1 
ATOM   13279 C  CG2 . ILE L  1 151 ? -1.867  -13.946 11.368  1.00 60.53  ? 151 ILE W CG2 1 
ATOM   13280 C  CD1 . ILE L  1 151 ? -1.731  -16.760 12.831  1.00 61.98  ? 151 ILE W CD1 1 
ATOM   13281 N  N   . ALA L  1 152 ? -4.189  -12.123 10.442  1.00 58.64  ? 152 ALA W N   1 
ATOM   13282 C  CA  . ALA L  1 152 ? -4.475  -11.356 9.224   1.00 59.78  ? 152 ALA W CA  1 
ATOM   13283 C  C   . ALA L  1 152 ? -3.201  -10.799 8.577   1.00 61.26  ? 152 ALA W C   1 
ATOM   13284 O  O   . ALA L  1 152 ? -2.150  -10.696 9.219   1.00 60.95  ? 152 ALA W O   1 
ATOM   13285 C  CB  . ALA L  1 152 ? -5.436  -10.223 9.549   1.00 57.88  ? 152 ALA W CB  1 
ATOM   13286 N  N   . GLN L  1 153 ? -3.317  -10.436 7.302   1.00 63.13  ? 153 GLN W N   1 
ATOM   13287 C  CA  . GLN L  1 153 ? -2.211  -9.869  6.530   1.00 64.96  ? 153 GLN W CA  1 
ATOM   13288 C  C   . GLN L  1 153 ? -2.053  -8.378  6.825   1.00 63.81  ? 153 GLN W C   1 
ATOM   13289 O  O   . GLN L  1 153 ? -3.045  -7.646  6.943   1.00 62.54  ? 153 GLN W O   1 
ATOM   13290 C  CB  . GLN L  1 153 ? -2.451  -10.078 5.038   1.00 67.60  ? 153 GLN W CB  1 
ATOM   13291 C  CG  . GLN L  1 153 ? -1.189  -9.984  4.189   1.00 70.23  ? 153 GLN W CG  1 
ATOM   13292 C  CD  . GLN L  1 153 ? -1.445  -10.255 2.719   1.00 73.02  ? 153 GLN W CD  1 
ATOM   13293 O  OE1 . GLN L  1 153 ? -2.541  -10.009 2.205   1.00 72.98  ? 153 GLN W OE1 1 
ATOM   13294 N  NE2 . GLN L  1 153 ? -0.428  -10.762 2.029   1.00 75.70  ? 153 GLN W NE2 1 
HETATM 13295 ZN ZN  . ZN  M  2 .   ? 21.558  41.324  6.345   1.00 25.35  ? 201 ZN  A ZN  1 
HETATM 13296 S  S   A SO4 N  3 .   ? 29.782  36.467  6.418   0.75 42.80  ? 202 SO4 A S   1 
HETATM 13297 O  O1  A SO4 N  3 .   ? 30.263  37.294  5.290   0.75 42.00  ? 202 SO4 A O1  1 
HETATM 13298 O  O2  A SO4 N  3 .   ? 29.677  35.062  5.963   0.75 41.25  ? 202 SO4 A O2  1 
HETATM 13299 O  O3  A SO4 N  3 .   ? 28.457  36.942  6.885   0.75 41.44  ? 202 SO4 A O3  1 
HETATM 13300 O  O4  A SO4 N  3 .   ? 30.733  36.577  7.546   0.75 41.68  ? 202 SO4 A O4  1 
HETATM 13301 ZN ZN  . ZN  O  2 .   ? 16.704  21.881  40.461  1.00 25.49  ? 201 ZN  F ZN  1 
HETATM 13302 S  S   A SO4 P  3 .   ? 24.635  26.874  42.875  0.75 44.62  ? 202 SO4 F S   1 
HETATM 13303 O  O1  A SO4 P  3 .   ? 25.483  26.479  41.731  0.75 43.36  ? 202 SO4 F O1  1 
HETATM 13304 O  O2  A SO4 P  3 .   ? 23.211  26.805  42.483  0.75 45.60  ? 202 SO4 F O2  1 
HETATM 13305 O  O3  A SO4 P  3 .   ? 24.874  25.961  44.013  0.75 44.81  ? 202 SO4 F O3  1 
HETATM 13306 O  O4  A SO4 P  3 .   ? 24.946  28.260  43.277  0.75 45.16  ? 202 SO4 F O4  1 
HETATM 13307 S  S   A SO4 Q  3 .   ? 13.795  6.293   43.393  0.75 60.08  ? 203 SO4 F S   1 
HETATM 13308 O  O1  A SO4 Q  3 .   ? 15.250  6.470   43.187  0.75 58.59  ? 203 SO4 F O1  1 
HETATM 13309 O  O2  A SO4 Q  3 .   ? 13.098  6.422   42.094  0.75 58.06  ? 203 SO4 F O2  1 
HETATM 13310 O  O3  A SO4 Q  3 .   ? 13.536  4.951   43.964  0.75 56.13  ? 203 SO4 F O3  1 
HETATM 13311 O  O4  A SO4 Q  3 .   ? 13.309  7.342   44.321  0.75 57.33  ? 203 SO4 F O4  1 
HETATM 13312 ZN ZN  . ZN  R  2 .   ? -10.233 55.483  26.627  1.00 28.47  ? 201 ZN  D ZN  1 
HETATM 13313 S  S   . SO4 S  3 .   ? -18.849 54.248  30.159  1.00 50.06  ? 202 SO4 D S   1 
HETATM 13314 O  O1  . SO4 S  3 .   ? -17.467 53.955  29.716  1.00 49.93  ? 202 SO4 D O1  1 
HETATM 13315 O  O2  . SO4 S  3 .   ? -19.791 53.382  29.416  1.00 49.35  ? 202 SO4 D O2  1 
HETATM 13316 O  O3  . SO4 S  3 .   ? -18.977 53.969  31.607  1.00 49.70  ? 202 SO4 D O3  1 
HETATM 13317 O  O4  . SO4 S  3 .   ? -19.170 55.667  29.883  1.00 48.62  ? 202 SO4 D O4  1 
HETATM 13318 ZN ZN  . ZN  T  2 .   ? -11.925 16.207  25.294  1.00 23.87  ? 201 ZN  G ZN  1 
HETATM 13319 S  S   . SO4 U  3 .   ? -19.332 18.015  19.784  1.00 54.46  ? 202 SO4 G S   1 
HETATM 13320 O  O1  . SO4 U  3 .   ? -19.030 18.334  18.371  1.00 53.24  ? 202 SO4 G O1  1 
HETATM 13321 O  O2  . SO4 U  3 .   ? -19.697 16.582  19.872  1.00 53.39  ? 202 SO4 G O2  1 
HETATM 13322 O  O3  . SO4 U  3 .   ? -20.459 18.859  20.239  1.00 53.24  ? 202 SO4 G O3  1 
HETATM 13323 O  O4  . SO4 U  3 .   ? -18.161 18.288  20.655  1.00 52.91  ? 202 SO4 G O4  1 
HETATM 13324 ZN ZN  . ZN  V  2 .   ? 16.512  -43.436 32.728  1.00 39.82  ? 201 ZN  I ZN  1 
HETATM 13325 S  S   . SO4 W  3 .   ? 22.684  -42.430 39.592  1.00 63.62  ? 202 SO4 I S   1 
HETATM 13326 O  O1  . SO4 W  3 .   ? 22.923  -43.862 39.301  1.00 60.85  ? 202 SO4 I O1  1 
HETATM 13327 O  O2  . SO4 W  3 .   ? 21.611  -41.929 38.701  1.00 62.35  ? 202 SO4 I O2  1 
HETATM 13328 O  O3  . SO4 W  3 .   ? 23.930  -41.663 39.362  1.00 61.21  ? 202 SO4 I O3  1 
HETATM 13329 O  O4  . SO4 W  3 .   ? 22.282  -42.263 41.009  1.00 62.48  ? 202 SO4 I O4  1 
HETATM 13330 ZN ZN  . ZN  X  2 .   ? 19.394  -4.061  32.297  1.00 33.07  ? 201 ZN  K ZN  1 
HETATM 13331 S  S   . SO4 Y  3 .   ? 28.135  -6.076  30.401  1.00 79.44  ? 202 SO4 K S   1 
HETATM 13332 O  O1  . SO4 Y  3 .   ? 28.846  -5.804  29.132  1.00 78.39  ? 202 SO4 K O1  1 
HETATM 13333 O  O2  . SO4 Y  3 .   ? 26.772  -6.579  30.103  1.00 77.74  ? 202 SO4 K O2  1 
HETATM 13334 O  O3  . SO4 Y  3 .   ? 28.883  -7.090  31.173  1.00 78.84  ? 202 SO4 K O3  1 
HETATM 13335 O  O4  . SO4 Y  3 .   ? 28.049  -4.836  31.205  1.00 77.72  ? 202 SO4 K O4  1 
HETATM 13336 ZN ZN  . ZN  Z  2 .   ? 13.403  1.539   58.353  1.00 25.73  ? 201 ZN  M ZN  1 
HETATM 13337 S  S   A SO4 AA 3 .   ? 20.847  -0.944  63.965  0.75 50.49  ? 202 SO4 M S   1 
HETATM 13338 O  O1  A SO4 AA 3 .   ? 21.560  -1.706  62.914  0.75 49.50  ? 202 SO4 M O1  1 
HETATM 13339 O  O2  A SO4 AA 3 .   ? 19.574  -0.411  63.420  0.75 50.35  ? 202 SO4 M O2  1 
HETATM 13340 O  O3  A SO4 AA 3 .   ? 20.568  -1.844  65.108  0.75 50.37  ? 202 SO4 M O3  1 
HETATM 13341 O  O4  A SO4 AA 3 .   ? 21.696  0.179   64.421  0.75 50.48  ? 202 SO4 M O4  1 
HETATM 13342 ZN ZN  . ZN  BA 2 .   ? 3.101   21.663  90.833  1.00 64.93  ? 201 ZN  O ZN  1 
HETATM 13343 ZN ZN  . ZN  CA 2 .   ? -17.427 10.226  51.410  1.00 26.89  ? 201 ZN  Q ZN  1 
HETATM 13344 S  S   A SO4 DA 3 .   ? -26.655 12.782  53.513  0.75 54.14  ? 202 SO4 Q S   1 
HETATM 13345 O  O1  A SO4 DA 3 .   ? -26.525 13.657  52.326  0.75 52.78  ? 202 SO4 Q O1  1 
HETATM 13346 O  O2  A SO4 DA 3 .   ? -27.783 11.842  53.325  0.75 52.59  ? 202 SO4 Q O2  1 
HETATM 13347 O  O3  A SO4 DA 3 .   ? -25.403 12.008  53.704  0.75 53.28  ? 202 SO4 Q O3  1 
HETATM 13348 O  O4  A SO4 DA 3 .   ? -26.923 13.623  54.701  0.75 54.68  ? 202 SO4 Q O4  1 
HETATM 13349 S  S   A SO4 EA 3 .   ? -11.621 5.098   37.507  0.75 52.39  ? 203 SO4 Q S   1 
HETATM 13350 O  O1  A SO4 EA 3 .   ? -10.496 5.024   36.549  0.75 50.30  ? 203 SO4 Q O1  1 
HETATM 13351 O  O2  A SO4 EA 3 .   ? -12.898 5.146   36.762  0.75 52.09  ? 203 SO4 Q O2  1 
HETATM 13352 O  O3  A SO4 EA 3 .   ? -11.627 3.901   38.383  0.75 49.25  ? 203 SO4 Q O3  1 
HETATM 13353 O  O4  A SO4 EA 3 .   ? -11.480 6.323   38.327  0.75 50.67  ? 203 SO4 Q O4  1 
HETATM 13354 ZN ZN  . ZN  FA 2 .   ? -22.066 -8.200  85.786  0.80 37.80  ? 201 ZN  S ZN  1 
HETATM 13355 S  S   . SO4 GA 3 .   ? -29.073 -11.977 81.025  0.75 57.97  ? 202 SO4 S S   1 
HETATM 13356 O  O1  . SO4 GA 3 .   ? -28.447 -13.074 80.257  0.75 57.41  ? 202 SO4 S O1  1 
HETATM 13357 O  O2  . SO4 GA 3 .   ? -30.183 -11.388 80.239  0.75 56.55  ? 202 SO4 S O2  1 
HETATM 13358 O  O3  . SO4 GA 3 .   ? -29.614 -12.519 82.292  0.75 58.20  ? 202 SO4 S O3  1 
HETATM 13359 O  O4  . SO4 GA 3 .   ? -28.059 -10.938 81.328  0.75 56.68  ? 202 SO4 S O4  1 
HETATM 13360 ZN ZN  . ZN  HA 2 .   ? -0.253  -26.770 -0.339  0.70 48.85  ? 201 ZN  U ZN  1 
HETATM 13361 S  S   . SO4 IA 3 .   ? -7.078  -22.219 -3.770  0.50 48.10  ? 202 SO4 U S   1 
HETATM 13362 O  O1  . SO4 IA 3 .   ? -7.174  -23.033 -5.003  0.50 47.84  ? 202 SO4 U O1  1 
HETATM 13363 O  O2  . SO4 IA 3 .   ? -6.174  -21.070 -4.002  0.50 47.48  ? 202 SO4 U O2  1 
HETATM 13364 O  O3  . SO4 IA 3 .   ? -6.548  -23.053 -2.667  0.50 46.80  ? 202 SO4 U O3  1 
HETATM 13365 O  O4  . SO4 IA 3 .   ? -8.426  -21.723 -3.416  0.50 47.84  ? 202 SO4 U O4  1 
HETATM 13366 ZN ZN  . ZN  JA 2 .   ? -13.169 -9.884  33.350  1.00 31.21  ? 201 ZN  W ZN  1 
HETATM 13367 S  S   . SO4 KA 3 .   ? -20.825 -14.126 31.512  1.00 79.64  ? 202 SO4 W S   1 
HETATM 13368 O  O1  . SO4 KA 3 .   ? -19.538 -13.471 31.165  1.00 74.81  ? 202 SO4 W O1  1 
HETATM 13369 O  O2  . SO4 KA 3 .   ? -21.368 -14.821 30.322  1.00 77.70  ? 202 SO4 W O2  1 
HETATM 13370 O  O3  . SO4 KA 3 .   ? -20.626 -15.114 32.597  1.00 75.55  ? 202 SO4 W O3  1 
HETATM 13371 O  O4  . SO4 KA 3 .   ? -21.788 -13.094 31.963  1.00 80.85  ? 202 SO4 W O4  1 
HETATM 13372 O  O   . HOH LA 4 .   ? 28.677  37.064  -7.312  1.00 39.21  ? 301 HOH A O   1 
HETATM 13373 O  O   . HOH LA 4 .   ? 29.608  56.724  13.040  1.00 41.00  ? 302 HOH A O   1 
HETATM 13374 O  O   . HOH LA 4 .   ? 30.249  34.595  24.341  1.00 37.39  ? 303 HOH A O   1 
HETATM 13375 O  O   . HOH LA 4 .   ? 27.605  39.326  7.889   1.00 36.36  ? 304 HOH A O   1 
HETATM 13376 O  O   . HOH LA 4 .   ? 25.090  33.102  -3.660  1.00 45.83  ? 305 HOH A O   1 
HETATM 13377 O  O   . HOH LA 4 .   ? 12.560  33.679  16.220  1.00 30.81  ? 306 HOH A O   1 
HETATM 13378 O  O   . HOH LA 4 .   ? 22.407  50.721  14.073  1.00 34.59  ? 307 HOH A O   1 
HETATM 13379 O  O   . HOH LA 4 .   ? 33.267  35.929  7.267   1.00 51.16  ? 308 HOH A O   1 
HETATM 13380 O  O   . HOH LA 4 .   ? 18.144  46.616  1.007   1.00 31.45  ? 309 HOH A O   1 
HETATM 13381 O  O   . HOH LA 4 .   ? 6.956   40.158  20.147  1.00 28.15  ? 310 HOH A O   1 
HETATM 13382 O  O   . HOH LA 4 .   ? 24.105  47.375  -3.953  1.00 38.71  ? 311 HOH A O   1 
HETATM 13383 O  O   . HOH LA 4 .   ? 3.144   47.904  17.476  1.00 33.07  ? 312 HOH A O   1 
HETATM 13384 O  O   . HOH LA 4 .   ? 30.707  39.747  6.200   1.00 48.09  ? 313 HOH A O   1 
HETATM 13385 O  O   . HOH LA 4 .   ? 17.228  50.271  14.338  1.00 31.03  ? 314 HOH A O   1 
HETATM 13386 O  O   . HOH LA 4 .   ? 13.010  49.032  8.413   1.00 44.79  ? 315 HOH A O   1 
HETATM 13387 O  O   . HOH LA 4 .   ? 26.160  22.015  15.364  1.00 42.04  ? 316 HOH A O   1 
HETATM 13388 O  O   . HOH LA 4 .   ? 38.751  45.298  11.889  1.00 36.95  ? 317 HOH A O   1 
HETATM 13389 O  O   . HOH LA 4 .   ? 24.349  51.865  15.457  1.00 37.09  ? 318 HOH A O   1 
HETATM 13390 O  O   . HOH LA 4 .   ? 20.552  44.537  -0.877  1.00 32.99  ? 319 HOH A O   1 
HETATM 13391 O  O   . HOH LA 4 .   ? 2.463   41.071  21.053  1.00 27.30  ? 320 HOH A O   1 
HETATM 13392 O  O   . HOH LA 4 .   ? 26.122  35.463  25.397  1.00 20.93  ? 321 HOH A O   1 
HETATM 13393 O  O   . HOH LA 4 .   ? 27.331  53.464  14.133  1.00 41.37  ? 322 HOH A O   1 
HETATM 13394 O  O   . HOH LA 4 .   ? 31.310  33.598  22.063  1.00 48.12  ? 323 HOH A O   1 
HETATM 13395 O  O   . HOH LA 4 .   ? 35.863  49.991  9.544   1.00 48.75  ? 324 HOH A O   1 
HETATM 13396 O  O   . HOH LA 4 .   ? 29.066  31.137  7.968   1.00 36.31  ? 325 HOH A O   1 
HETATM 13397 O  O   . HOH LA 4 .   ? 32.720  47.418  3.730   1.00 41.51  ? 326 HOH A O   1 
HETATM 13398 O  O   . HOH LA 4 .   ? 19.898  29.279  6.621   1.00 47.47  ? 327 HOH A O   1 
HETATM 13399 O  O   . HOH LA 4 .   ? 36.983  55.239  24.924  1.00 47.44  ? 328 HOH A O   1 
HETATM 13400 O  O   . HOH LA 4 .   ? 1.733   43.736  23.875  1.00 33.69  ? 329 HOH A O   1 
HETATM 13401 O  O   . HOH LA 4 .   ? 23.308  37.083  5.190   1.00 22.04  ? 330 HOH A O   1 
HETATM 13402 O  O   . HOH LA 4 .   ? 13.790  38.989  7.238   1.00 23.60  ? 331 HOH A O   1 
HETATM 13403 O  O   . HOH LA 4 .   ? 23.572  24.888  13.393  1.00 33.76  ? 332 HOH A O   1 
HETATM 13404 O  O   . HOH LA 4 .   ? 8.697   40.663  24.064  1.00 31.41  ? 333 HOH A O   1 
HETATM 13405 O  O   . HOH LA 4 .   ? 8.215   42.614  26.207  1.00 33.06  ? 334 HOH A O   1 
HETATM 13406 O  O   . HOH LA 4 .   ? 16.483  28.513  7.509   1.00 59.13  ? 335 HOH A O   1 
HETATM 13407 O  O   . HOH LA 4 .   ? 37.619  38.050  22.362  1.00 44.44  ? 336 HOH A O   1 
HETATM 13408 O  O   . HOH LA 4 .   ? 38.116  39.664  5.315   1.00 44.22  ? 337 HOH A O   1 
HETATM 13409 O  O   . HOH LA 4 .   ? 12.840  51.843  2.958   1.00 50.18  ? 338 HOH A O   1 
HETATM 13410 O  O   . HOH LA 4 .   ? 16.663  33.362  8.937   1.00 35.99  ? 339 HOH A O   1 
HETATM 13411 O  O   . HOH LA 4 .   ? 26.203  35.579  6.214   1.00 38.01  ? 340 HOH A O   1 
HETATM 13412 O  O   . HOH LA 4 .   ? 24.084  55.106  18.992  1.00 58.16  ? 341 HOH A O   1 
HETATM 13413 O  O   . HOH LA 4 .   ? 37.554  36.269  16.349  1.00 39.79  ? 342 HOH A O   1 
HETATM 13414 O  O   . HOH LA 4 .   ? 24.943  26.204  11.460  1.00 38.84  ? 343 HOH A O   1 
HETATM 13415 O  O   . HOH LA 4 .   ? 38.458  49.842  10.391  1.00 49.67  ? 344 HOH A O   1 
HETATM 13416 O  O   . HOH LA 4 .   ? 7.556   46.792  16.265  1.00 32.96  ? 345 HOH A O   1 
HETATM 13417 O  O   . HOH LA 4 .   ? 12.791  41.331  7.092   1.00 25.77  ? 346 HOH A O   1 
HETATM 13418 O  O   . HOH LA 4 .   ? 20.191  52.294  4.749   1.00 58.71  ? 347 HOH A O   1 
HETATM 13419 O  O   . HOH LA 4 .   ? 12.573  51.494  16.814  1.00 38.45  ? 348 HOH A O   1 
HETATM 13420 O  O   . HOH LA 4 .   ? 40.037  48.730  22.785  1.00 36.70  ? 349 HOH A O   1 
HETATM 13421 O  O   . HOH LA 4 .   ? 35.464  34.849  15.316  1.00 50.06  ? 350 HOH A O   1 
HETATM 13422 O  O   . HOH LA 4 .   ? 34.438  53.635  9.315   1.00 45.42  ? 351 HOH A O   1 
HETATM 13423 O  O   . HOH LA 4 .   ? 20.719  38.771  -4.117  1.00 52.05  ? 352 HOH A O   1 
HETATM 13424 O  O   . HOH LA 4 .   ? 23.212  49.089  31.535  1.00 55.81  ? 353 HOH A O   1 
HETATM 13425 O  O   . HOH LA 4 .   ? 26.139  27.459  20.724  1.00 22.53  ? 354 HOH A O   1 
HETATM 13426 O  O   . HOH LA 4 .   ? 20.714  42.723  29.730  1.00 34.90  ? 355 HOH A O   1 
HETATM 13427 O  O   . HOH LA 4 .   ? 22.534  46.273  8.367   1.00 30.08  ? 356 HOH A O   1 
HETATM 13428 O  O   . HOH LA 4 .   ? 24.717  43.186  31.491  1.00 39.31  ? 357 HOH A O   1 
HETATM 13429 O  O   . HOH LA 4 .   ? 9.922   45.293  17.805  1.00 30.46  ? 358 HOH A O   1 
HETATM 13430 O  O   . HOH LA 4 .   ? 26.027  52.931  8.978   1.00 32.71  ? 359 HOH A O   1 
HETATM 13431 O  O   . HOH LA 4 .   ? 19.920  38.295  1.256   1.00 35.65  ? 360 HOH A O   1 
HETATM 13432 O  O   . HOH LA 4 .   ? 6.876   46.140  31.030  1.00 46.03  ? 361 HOH A O   1 
HETATM 13433 O  O   . HOH LA 4 .   ? 38.259  39.105  18.494  1.00 35.73  ? 362 HOH A O   1 
HETATM 13434 O  O   . HOH LA 4 .   ? 7.958   38.999  16.345  1.00 37.54  ? 363 HOH A O   1 
HETATM 13435 O  O   . HOH LA 4 .   ? 28.162  52.009  5.062   1.00 44.36  ? 364 HOH A O   1 
HETATM 13436 O  O   . HOH LA 4 .   ? 8.933   47.988  23.879  1.00 42.08  ? 365 HOH A O   1 
HETATM 13437 O  O   . HOH LA 4 .   ? 8.138   36.774  10.231  1.00 53.79  ? 366 HOH A O   1 
HETATM 13438 O  O   . HOH LA 4 .   ? 18.684  44.196  29.440  1.00 41.00  ? 367 HOH A O   1 
HETATM 13439 O  O   . HOH LA 4 .   ? 36.805  32.146  19.904  1.00 57.98  ? 368 HOH A O   1 
HETATM 13440 O  O   . HOH LA 4 .   ? 2.564   35.070  14.944  1.00 35.19  ? 369 HOH A O   1 
HETATM 13441 O  O   . HOH LA 4 .   ? 13.427  38.880  31.000  1.00 38.29  ? 370 HOH A O   1 
HETATM 13442 O  O   . HOH LA 4 .   ? 28.419  52.080  -2.438  1.00 56.86  ? 371 HOH A O   1 
HETATM 13443 O  O   . HOH LA 4 .   ? 28.114  46.661  28.247  1.00 41.76  ? 372 HOH A O   1 
HETATM 13444 O  O   . HOH LA 4 .   ? 27.666  31.392  17.348  1.00 38.85  ? 373 HOH A O   1 
HETATM 13445 O  O   . HOH LA 4 .   ? 13.427  49.719  13.381  1.00 38.16  ? 374 HOH A O   1 
HETATM 13446 O  O   . HOH LA 4 .   ? 16.008  29.491  12.275  1.00 36.42  ? 375 HOH A O   1 
HETATM 13447 O  O   . HOH LA 4 .   ? 23.757  51.627  11.846  1.00 46.62  ? 376 HOH A O   1 
HETATM 13448 O  O   . HOH LA 4 .   ? 22.321  36.370  -4.505  1.00 49.47  ? 377 HOH A O   1 
HETATM 13449 O  O   . HOH LA 4 .   ? 15.195  32.608  4.982   1.00 56.72  ? 378 HOH A O   1 
HETATM 13450 O  O   . HOH LA 4 .   ? 27.411  32.632  23.851  1.00 23.89  ? 379 HOH A O   1 
HETATM 13451 O  O   . HOH LA 4 .   ? 34.735  35.242  9.751   1.00 34.97  ? 380 HOH A O   1 
HETATM 13452 O  O   . HOH LA 4 .   ? 19.665  35.353  5.246   1.00 44.35  ? 381 HOH A O   1 
HETATM 13453 O  O   . HOH LA 4 .   ? 19.792  48.663  0.404   1.00 44.78  ? 382 HOH A O   1 
HETATM 13454 O  O   . HOH LA 4 .   ? 19.761  52.124  7.606   1.00 31.29  ? 383 HOH A O   1 
HETATM 13455 O  O   . HOH LA 4 .   ? 18.738  53.279  16.562  1.00 43.92  ? 384 HOH A O   1 
HETATM 13456 O  O   . HOH LA 4 .   ? 29.981  39.705  -4.391  1.00 36.96  ? 385 HOH A O   1 
HETATM 13457 O  O   . HOH LA 4 .   ? 32.863  33.564  18.540  1.00 43.61  ? 386 HOH A O   1 
HETATM 13458 O  O   . HOH LA 4 .   ? 14.397  49.477  1.075   1.00 39.69  ? 387 HOH A O   1 
HETATM 13459 O  O   . HOH LA 4 .   ? 26.541  46.267  30.206  1.00 38.03  ? 388 HOH A O   1 
HETATM 13460 O  O   . HOH LA 4 .   ? 14.009  36.890  38.571  1.00 46.29  ? 389 HOH A O   1 
HETATM 13461 O  O   . HOH LA 4 .   ? 38.614  45.587  14.618  1.00 31.25  ? 390 HOH A O   1 
HETATM 13462 O  O   . HOH LA 4 .   ? 35.060  49.916  6.576   1.00 47.46  ? 391 HOH A O   1 
HETATM 13463 O  O   . HOH LA 4 .   ? 44.904  36.369  18.927  1.00 52.33  ? 392 HOH A O   1 
HETATM 13464 O  O   . HOH LA 4 .   ? 34.232  31.488  20.151  1.00 52.13  ? 393 HOH A O   1 
HETATM 13465 O  O   . HOH LA 4 .   ? 27.791  52.897  17.964  1.00 36.32  ? 394 HOH A O   1 
HETATM 13466 O  O   . HOH LA 4 .   ? 29.345  39.596  -6.903  1.00 30.52  ? 395 HOH A O   1 
HETATM 13467 O  O   . HOH LA 4 .   ? 26.183  52.445  25.776  1.00 57.23  ? 396 HOH A O   1 
HETATM 13468 O  O   . HOH LA 4 .   ? 3.663   49.076  22.430  1.00 52.77  ? 397 HOH A O   1 
HETATM 13469 O  O   . HOH LA 4 .   ? 40.646  44.115  16.051  1.00 35.34  ? 398 HOH A O   1 
HETATM 13470 O  O   . HOH LA 4 .   ? 41.872  59.483  15.720  1.00 55.23  ? 399 HOH A O   1 
HETATM 13471 O  O   . HOH LA 4 .   ? 25.143  52.284  18.307  1.00 42.89  ? 400 HOH A O   1 
HETATM 13472 O  O   . HOH LA 4 .   ? 11.965  48.997  25.333  1.00 52.52  ? 401 HOH A O   1 
HETATM 13473 O  O   . HOH LA 4 .   ? 13.742  29.317  13.501  1.00 42.73  ? 402 HOH A O   1 
HETATM 13474 O  O   . HOH LA 4 .   ? 44.180  53.770  22.716  1.00 46.88  ? 403 HOH A O   1 
HETATM 13475 O  O   . HOH LA 4 .   ? 7.817   33.732  22.213  1.00 47.26  ? 404 HOH A O   1 
HETATM 13476 O  O   . HOH LA 4 .   ? 16.281  35.949  0.893   1.00 49.45  ? 405 HOH A O   1 
HETATM 13477 O  O   . HOH LA 4 .   ? 7.149   48.933  17.858  1.00 45.11  ? 406 HOH A O   1 
HETATM 13478 O  O   . HOH LA 4 .   ? 19.729  48.589  -2.276  1.00 55.51  ? 407 HOH A O   1 
HETATM 13479 O  O   . HOH LA 4 .   ? 31.297  32.648  7.706   1.00 40.26  ? 408 HOH A O   1 
HETATM 13480 O  O   . HOH LA 4 .   ? 22.460  57.022  19.970  1.00 60.89  ? 409 HOH A O   1 
HETATM 13481 O  O   . HOH LA 4 .   ? 21.260  52.424  29.575  1.00 57.87  ? 410 HOH A O   1 
HETATM 13482 O  O   . HOH LA 4 .   ? 40.831  46.286  27.725  1.00 67.03  ? 411 HOH A O   1 
HETATM 13483 O  O   . HOH LA 4 .   ? 26.998  50.920  27.897  1.00 48.89  ? 412 HOH A O   1 
HETATM 13484 O  O   . HOH LA 4 .   ? 24.224  45.922  -8.429  1.00 54.23  ? 413 HOH A O   1 
HETATM 13485 O  O   . HOH LA 4 .   ? 26.700  31.519  6.756   1.00 43.17  ? 414 HOH A O   1 
HETATM 13486 O  O   . HOH LA 4 .   ? 36.743  59.495  18.984  1.00 45.26  ? 415 HOH A O   1 
HETATM 13487 O  O   . HOH LA 4 .   ? 33.705  45.536  26.892  1.00 47.44  ? 416 HOH A O   1 
HETATM 13488 O  O   . HOH LA 4 .   ? 33.132  40.496  27.414  1.00 48.79  ? 417 HOH A O   1 
HETATM 13489 O  O   . HOH LA 4 .   ? 26.160  27.622  9.157   1.00 52.59  ? 418 HOH A O   1 
HETATM 13490 O  O   . HOH LA 4 .   ? 11.298  43.292  8.142   1.00 49.53  ? 419 HOH A O   1 
HETATM 13491 O  O   . HOH LA 4 .   ? 34.541  37.925  4.788   1.00 54.40  ? 420 HOH A O   1 
HETATM 13492 O  O   . HOH LA 4 .   ? 16.024  52.292  12.379  1.00 49.16  ? 421 HOH A O   1 
HETATM 13493 O  O   . HOH LA 4 .   ? 14.415  32.091  9.745   1.00 48.12  ? 422 HOH A O   1 
HETATM 13494 O  O   . HOH LA 4 .   ? 28.218  33.893  25.943  1.00 41.79  ? 423 HOH A O   1 
HETATM 13495 O  O   . HOH LA 4 .   ? 34.095  57.962  16.375  1.00 54.98  ? 424 HOH A O   1 
HETATM 13496 O  O   . HOH LA 4 .   ? 24.898  29.919  5.574   1.00 54.10  ? 425 HOH A O   1 
HETATM 13497 O  O   . HOH LA 4 .   ? 27.034  53.834  6.621   1.00 52.98  ? 426 HOH A O   1 
HETATM 13498 O  O   . HOH LA 4 .   ? 19.914  35.187  39.744  1.00 49.60  ? 427 HOH A O   1 
HETATM 13499 O  O   . HOH LA 4 .   ? 4.101   37.009  23.266  1.00 52.19  ? 428 HOH A O   1 
HETATM 13500 O  O   . HOH LA 4 .   ? 19.708  51.381  14.095  1.00 33.39  ? 429 HOH A O   1 
HETATM 13501 O  O   . HOH LA 4 .   ? 21.617  53.223  9.218   1.00 45.23  ? 430 HOH A O   1 
HETATM 13502 O  O   . HOH LA 4 .   ? 9.112   43.837  9.720   1.00 41.11  ? 431 HOH A O   1 
HETATM 13503 O  O   . HOH LA 4 .   ? 15.709  56.648  5.888   1.00 62.72  ? 432 HOH A O   1 
HETATM 13504 O  O   . HOH LA 4 .   ? 29.757  51.452  -0.158  1.00 48.90  ? 433 HOH A O   1 
HETATM 13505 O  O   . HOH LA 4 .   ? 5.844   51.633  21.635  1.00 57.56  ? 434 HOH A O   1 
HETATM 13506 O  O   . HOH LA 4 .   ? 11.505  34.563  26.964  1.00 49.64  ? 435 HOH A O   1 
HETATM 13507 O  O   . HOH LA 4 .   ? 26.886  44.522  32.372  1.00 55.40  ? 436 HOH A O   1 
HETATM 13508 O  O   . HOH LA 4 .   ? 27.529  27.334  4.193   1.00 58.62  ? 437 HOH A O   1 
HETATM 13509 O  O   . HOH MA 4 .   ? 14.855  11.998  43.465  1.00 32.92  ? 301 HOH F O   1 
HETATM 13510 O  O   . HOH MA 4 .   ? 22.667  20.455  17.738  1.00 30.08  ? 302 HOH F O   1 
HETATM 13511 O  O   . HOH MA 4 .   ? 6.462   22.583  45.600  1.00 40.51  ? 303 HOH F O   1 
HETATM 13512 O  O   . HOH MA 4 .   ? 14.884  12.717  31.663  1.00 29.66  ? 304 HOH F O   1 
HETATM 13513 O  O   . HOH MA 4 .   ? 35.139  23.988  42.045  1.00 41.59  ? 305 HOH F O   1 
HETATM 13514 O  O   . HOH MA 4 .   ? 34.946  26.778  35.631  1.00 31.32  ? 306 HOH F O   1 
HETATM 13515 O  O   . HOH MA 4 .   ? 15.828  15.867  50.999  1.00 26.22  ? 307 HOH F O   1 
HETATM 13516 O  O   . HOH MA 4 .   ? 36.461  8.152   26.793  1.00 41.99  ? 308 HOH F O   1 
HETATM 13517 O  O   . HOH MA 4 .   ? 40.090  20.375  28.550  1.00 22.56  ? 309 HOH F O   1 
HETATM 13518 O  O   . HOH MA 4 .   ? 2.475   26.348  31.106  1.00 44.37  ? 310 HOH F O   1 
HETATM 13519 O  O   . HOH MA 4 .   ? 6.369   22.075  24.485  1.00 30.37  ? 311 HOH F O   1 
HETATM 13520 O  O   . HOH MA 4 .   ? 41.053  29.245  32.305  1.00 30.47  ? 312 HOH F O   1 
HETATM 13521 O  O   . HOH MA 4 .   ? 23.021  21.992  12.842  1.00 49.53  ? 313 HOH F O   1 
HETATM 13522 O  O   . HOH MA 4 .   ? 26.452  15.741  46.216  1.00 37.56  ? 314 HOH F O   1 
HETATM 13523 O  O   . HOH MA 4 .   ? 20.509  12.234  34.088  1.00 27.41  ? 315 HOH F O   1 
HETATM 13524 O  O   . HOH MA 4 .   ? 25.086  23.384  43.392  1.00 39.27  ? 316 HOH F O   1 
HETATM 13525 O  O   . HOH MA 4 .   ? 21.417  36.999  36.395  1.00 34.39  ? 317 HOH F O   1 
HETATM 13526 O  O   . HOH MA 4 .   ? 34.666  17.630  39.904  1.00 26.05  ? 318 HOH F O   1 
HETATM 13527 O  O   . HOH MA 4 .   ? 20.527  10.795  45.640  1.00 41.47  ? 319 HOH F O   1 
HETATM 13528 O  O   . HOH MA 4 .   ? 23.425  15.188  49.753  1.00 40.52  ? 320 HOH F O   1 
HETATM 13529 O  O   . HOH MA 4 .   ? 8.954   18.273  25.781  1.00 34.35  ? 321 HOH F O   1 
HETATM 13530 O  O   . HOH MA 4 .   ? 29.855  28.917  25.709  1.00 30.60  ? 322 HOH F O   1 
HETATM 13531 O  O   . HOH MA 4 .   ? 36.599  25.231  30.064  1.00 21.86  ? 323 HOH F O   1 
HETATM 13532 O  O   . HOH MA 4 .   ? 15.115  33.994  39.518  1.00 43.96  ? 324 HOH F O   1 
HETATM 13533 O  O   . HOH MA 4 .   ? 11.238  11.407  28.310  1.00 42.98  ? 325 HOH F O   1 
HETATM 13534 O  O   . HOH MA 4 .   ? 17.987  25.927  42.058  1.00 26.18  ? 326 HOH F O   1 
HETATM 13535 O  O   . HOH MA 4 .   ? 26.839  6.540   36.886  1.00 31.22  ? 327 HOH F O   1 
HETATM 13536 O  O   . HOH MA 4 .   ? 39.989  27.122  37.422  1.00 40.70  ? 328 HOH F O   1 
HETATM 13537 O  O   . HOH MA 4 .   ? 11.131  26.541  18.847  1.00 39.14  ? 329 HOH F O   1 
HETATM 13538 O  O   . HOH MA 4 .   ? 26.456  27.817  23.349  1.00 19.31  ? 330 HOH F O   1 
HETATM 13539 O  O   . HOH MA 4 .   ? 19.593  10.001  50.291  1.00 31.38  ? 331 HOH F O   1 
HETATM 13540 O  O   . HOH MA 4 .   ? 26.219  30.430  42.302  1.00 39.46  ? 332 HOH F O   1 
HETATM 13541 O  O   . HOH MA 4 .   ? 10.667  29.058  28.602  1.00 34.00  ? 333 HOH F O   1 
HETATM 13542 O  O   . HOH MA 4 .   ? 34.789  15.186  24.356  1.00 47.91  ? 334 HOH F O   1 
HETATM 13543 O  O   . HOH MA 4 .   ? 9.510   24.239  37.360  1.00 26.16  ? 335 HOH F O   1 
HETATM 13544 O  O   . HOH MA 4 .   ? 26.750  10.917  23.620  1.00 36.33  ? 336 HOH F O   1 
HETATM 13545 O  O   . HOH MA 4 .   ? 26.946  39.910  35.817  1.00 43.49  ? 337 HOH F O   1 
HETATM 13546 O  O   . HOH MA 4 .   ? 23.193  22.456  41.545  1.00 35.87  ? 338 HOH F O   1 
HETATM 13547 O  O   . HOH MA 4 .   ? 36.922  19.319  36.000  1.00 27.99  ? 339 HOH F O   1 
HETATM 13548 O  O   . HOH MA 4 .   ? 25.090  26.698  46.620  1.00 53.33  ? 340 HOH F O   1 
HETATM 13549 O  O   . HOH MA 4 .   ? 20.396  38.136  34.184  1.00 32.16  ? 341 HOH F O   1 
HETATM 13550 O  O   . HOH MA 4 .   ? 18.311  16.998  38.779  1.00 22.99  ? 342 HOH F O   1 
HETATM 13551 O  O   . HOH MA 4 .   ? 0.195   13.383  19.681  1.00 43.40  ? 343 HOH F O   1 
HETATM 13552 O  O   . HOH MA 4 .   ? 18.909  26.793  7.196   1.00 52.99  ? 344 HOH F O   1 
HETATM 13553 O  O   B HOH MA 4 .   ? 14.963  6.453   40.508  1.00 38.29  ? 345 HOH F O   1 
HETATM 13554 O  O   . HOH MA 4 .   ? 36.396  25.352  25.107  1.00 45.35  ? 346 HOH F O   1 
HETATM 13555 O  O   . HOH MA 4 .   ? 31.210  13.431  41.738  1.00 46.09  ? 347 HOH F O   1 
HETATM 13556 O  O   . HOH MA 4 .   ? 24.993  35.867  28.035  1.00 22.67  ? 348 HOH F O   1 
HETATM 13557 O  O   . HOH MA 4 .   ? 20.608  27.123  41.741  1.00 39.27  ? 349 HOH F O   1 
HETATM 13558 O  O   . HOH MA 4 .   ? 11.582  15.941  44.513  1.00 37.74  ? 350 HOH F O   1 
HETATM 13559 O  O   . HOH MA 4 .   ? 2.646   31.042  26.790  1.00 44.22  ? 351 HOH F O   1 
HETATM 13560 O  O   . HOH MA 4 .   ? 26.752  20.121  17.321  1.00 31.47  ? 352 HOH F O   1 
HETATM 13561 O  O   . HOH MA 4 .   ? 25.524  14.094  16.864  1.00 54.37  ? 353 HOH F O   1 
HETATM 13562 O  O   . HOH MA 4 .   ? 39.146  14.465  30.070  1.00 24.83  ? 354 HOH F O   1 
HETATM 13563 O  O   . HOH MA 4 .   ? 12.876  29.786  36.676  1.00 38.00  ? 355 HOH F O   1 
HETATM 13564 O  O   . HOH MA 4 .   ? 30.577  34.328  27.061  1.00 48.99  ? 356 HOH F O   1 
HETATM 13565 O  O   . HOH MA 4 .   ? 13.922  6.793   47.239  1.00 44.56  ? 357 HOH F O   1 
HETATM 13566 O  O   . HOH MA 4 .   ? 36.400  19.314  43.412  1.00 41.00  ? 358 HOH F O   1 
HETATM 13567 O  O   . HOH MA 4 .   ? 13.572  25.201  44.642  1.00 32.22  ? 359 HOH F O   1 
HETATM 13568 O  O   . HOH MA 4 .   ? 5.141   19.972  16.923  1.00 42.89  ? 360 HOH F O   1 
HETATM 13569 O  O   . HOH MA 4 .   ? 9.411   20.435  17.793  1.00 41.32  ? 361 HOH F O   1 
HETATM 13570 O  O   . HOH MA 4 .   ? 23.297  41.171  32.590  1.00 53.12  ? 362 HOH F O   1 
HETATM 13571 O  O   . HOH MA 4 .   ? 3.544   23.676  32.388  1.00 57.18  ? 363 HOH F O   1 
HETATM 13572 O  O   . HOH MA 4 .   ? 8.476   21.737  37.179  1.00 27.32  ? 364 HOH F O   1 
HETATM 13573 O  O   . HOH MA 4 .   ? 6.728   23.973  26.753  1.00 22.48  ? 365 HOH F O   1 
HETATM 13574 O  O   . HOH MA 4 .   ? 9.720   14.895  20.383  1.00 29.55  ? 366 HOH F O   1 
HETATM 13575 O  O   . HOH MA 4 .   ? 9.970   30.130  40.201  1.00 54.85  ? 367 HOH F O   1 
HETATM 13576 O  O   . HOH MA 4 .   ? 29.985  8.797   29.698  1.00 33.19  ? 368 HOH F O   1 
HETATM 13577 O  O   . HOH MA 4 .   ? 34.057  24.138  24.913  1.00 30.06  ? 369 HOH F O   1 
HETATM 13578 O  O   . HOH MA 4 .   ? 8.452   14.766  35.874  1.00 39.98  ? 370 HOH F O   1 
HETATM 13579 O  O   . HOH MA 4 .   ? 13.192  30.282  26.619  1.00 36.97  ? 371 HOH F O   1 
HETATM 13580 O  O   . HOH MA 4 .   ? 31.813  30.315  34.510  1.00 40.99  ? 372 HOH F O   1 
HETATM 13581 O  O   . HOH MA 4 .   ? 16.039  22.077  12.534  1.00 54.95  ? 373 HOH F O   1 
HETATM 13582 O  O   . HOH MA 4 .   ? 29.956  27.927  41.027  1.00 29.06  ? 374 HOH F O   1 
HETATM 13583 O  O   . HOH MA 4 .   ? 20.996  23.249  53.452  1.00 49.19  ? 375 HOH F O   1 
HETATM 13584 O  O   . HOH MA 4 .   ? 29.497  16.635  21.421  1.00 34.21  ? 376 HOH F O   1 
HETATM 13585 O  O   . HOH MA 4 .   ? 25.677  31.764  31.789  1.00 41.22  ? 377 HOH F O   1 
HETATM 13586 O  O   . HOH MA 4 .   ? 7.755   13.778  43.054  1.00 34.30  ? 378 HOH F O   1 
HETATM 13587 O  O   . HOH MA 4 .   ? 9.230   10.035  42.360  1.00 51.23  ? 379 HOH F O   1 
HETATM 13588 O  O   . HOH MA 4 .   ? 17.102  10.053  30.017  1.00 38.28  ? 380 HOH F O   1 
HETATM 13589 O  O   . HOH MA 4 .   ? 7.545   17.163  36.619  1.00 42.88  ? 381 HOH F O   1 
HETATM 13590 O  O   . HOH MA 4 .   ? 13.494  13.881  45.571  1.00 31.95  ? 382 HOH F O   1 
HETATM 13591 O  O   . HOH MA 4 .   ? 35.913  23.787  34.028  1.00 25.70  ? 383 HOH F O   1 
HETATM 13592 O  O   . HOH MA 4 .   ? 33.891  26.922  20.832  1.00 54.18  ? 384 HOH F O   1 
HETATM 13593 O  O   . HOH MA 4 .   ? 8.144   30.071  31.567  1.00 39.49  ? 385 HOH F O   1 
HETATM 13594 O  O   . HOH MA 4 .   ? 30.193  9.703   41.443  1.00 32.86  ? 386 HOH F O   1 
HETATM 13595 O  O   . HOH MA 4 .   ? 32.565  6.356   35.706  1.00 42.23  ? 387 HOH F O   1 
HETATM 13596 O  O   . HOH MA 4 .   ? 15.879  24.148  14.843  1.00 33.00  ? 388 HOH F O   1 
HETATM 13597 O  O   B HOH MA 4 .   ? 22.790  24.910  41.042  0.50 22.29  ? 389 HOH F O   1 
HETATM 13598 O  O   . HOH MA 4 .   ? 32.231  7.590   28.372  1.00 37.69  ? 390 HOH F O   1 
HETATM 13599 O  O   . HOH MA 4 .   ? 30.197  29.978  28.106  1.00 39.34  ? 391 HOH F O   1 
HETATM 13600 O  O   . HOH MA 4 .   ? 12.843  33.698  33.111  1.00 35.21  ? 392 HOH F O   1 
HETATM 13601 O  O   . HOH MA 4 .   ? 35.120  17.760  37.241  1.00 23.08  ? 393 HOH F O   1 
HETATM 13602 O  O   . HOH MA 4 .   ? 27.378  30.300  25.213  1.00 29.02  ? 394 HOH F O   1 
HETATM 13603 O  O   . HOH MA 4 .   ? 7.861   28.715  21.445  1.00 42.82  ? 395 HOH F O   1 
HETATM 13604 O  O   . HOH MA 4 .   ? 26.656  22.203  46.834  1.00 47.19  ? 396 HOH F O   1 
HETATM 13605 O  O   . HOH MA 4 .   ? 38.942  29.681  30.328  1.00 44.97  ? 397 HOH F O   1 
HETATM 13606 O  O   . HOH MA 4 .   ? 12.784  14.439  48.089  1.00 39.72  ? 398 HOH F O   1 
HETATM 13607 O  O   . HOH MA 4 .   ? 4.906   24.140  22.928  1.00 44.06  ? 399 HOH F O   1 
HETATM 13608 O  O   . HOH MA 4 .   ? 4.788   17.344  41.965  1.00 51.46  ? 400 HOH F O   1 
HETATM 13609 O  O   . HOH MA 4 .   ? 16.553  10.724  51.908  1.00 34.93  ? 401 HOH F O   1 
HETATM 13610 O  O   . HOH MA 4 .   ? 35.526  4.185   33.134  1.00 39.07  ? 402 HOH F O   1 
HETATM 13611 O  O   . HOH MA 4 .   ? 8.638   30.801  25.293  1.00 48.27  ? 403 HOH F O   1 
HETATM 13612 O  O   . HOH MA 4 .   ? 11.179  33.780  31.114  1.00 36.28  ? 404 HOH F O   1 
HETATM 13613 O  O   . HOH MA 4 .   ? 12.885  13.996  19.820  1.00 30.86  ? 405 HOH F O   1 
HETATM 13614 O  O   . HOH MA 4 .   ? 15.484  11.078  38.759  1.00 28.81  ? 406 HOH F O   1 
HETATM 13615 O  O   . HOH MA 4 .   ? 29.864  13.389  44.042  1.00 35.99  ? 407 HOH F O   1 
HETATM 13616 O  O   . HOH MA 4 .   ? 34.024  8.335   41.029  1.00 55.35  ? 408 HOH F O   1 
HETATM 13617 O  O   . HOH MA 4 .   ? 11.030  12.811  31.529  1.00 39.18  ? 409 HOH F O   1 
HETATM 13618 O  O   . HOH MA 4 .   ? 37.307  16.722  21.298  1.00 55.79  ? 410 HOH F O   1 
HETATM 13619 O  O   . HOH MA 4 .   ? 39.709  14.984  32.578  1.00 40.32  ? 411 HOH F O   1 
HETATM 13620 O  O   . HOH MA 4 .   ? 40.601  23.618  23.486  1.00 55.62  ? 412 HOH F O   1 
HETATM 13621 O  O   . HOH MA 4 .   ? 21.726  31.590  41.483  1.00 38.63  ? 413 HOH F O   1 
HETATM 13622 O  O   . HOH MA 4 .   ? 5.922   30.679  25.594  1.00 55.26  ? 414 HOH F O   1 
HETATM 13623 O  O   . HOH MA 4 .   ? 9.987   27.368  44.483  1.00 61.12  ? 415 HOH F O   1 
HETATM 13624 O  O   . HOH MA 4 .   ? 6.580   19.257  26.852  1.00 45.78  ? 416 HOH F O   1 
HETATM 13625 O  O   . HOH MA 4 .   ? 35.212  30.532  28.987  1.00 49.95  ? 417 HOH F O   1 
HETATM 13626 O  O   . HOH MA 4 .   ? 33.789  22.326  23.005  1.00 43.67  ? 418 HOH F O   1 
HETATM 13627 O  O   . HOH MA 4 .   ? 36.824  25.833  37.707  1.00 41.26  ? 419 HOH F O   1 
HETATM 13628 O  O   . HOH MA 4 .   ? 28.973  25.593  45.579  1.00 56.40  ? 420 HOH F O   1 
HETATM 13629 O  O   . HOH MA 4 .   ? 16.184  26.753  12.620  1.00 54.51  ? 421 HOH F O   1 
HETATM 13630 O  O   . HOH MA 4 .   ? 43.014  5.298   32.393  1.00 62.24  ? 422 HOH F O   1 
HETATM 13631 O  O   . HOH MA 4 .   ? 19.369  6.298   45.864  1.00 53.84  ? 423 HOH F O   1 
HETATM 13632 O  O   . HOH MA 4 .   ? 10.811  30.880  35.266  1.00 42.08  ? 424 HOH F O   1 
HETATM 13633 O  O   . HOH MA 4 .   ? 42.673  13.018  31.057  1.00 52.27  ? 425 HOH F O   1 
HETATM 13634 O  O   . HOH MA 4 .   ? 5.336   14.574  43.832  1.00 45.14  ? 426 HOH F O   1 
HETATM 13635 O  O   . HOH MA 4 .   ? 43.120  22.674  26.482  1.00 42.24  ? 427 HOH F O   1 
HETATM 13636 O  O   . HOH MA 4 .   ? 37.054  26.178  27.554  1.00 33.16  ? 428 HOH F O   1 
HETATM 13637 O  O   . HOH MA 4 .   ? 40.477  18.124  27.193  1.00 31.33  ? 429 HOH F O   1 
HETATM 13638 O  O   . HOH MA 4 .   ? 40.596  14.826  23.549  1.00 58.80  ? 430 HOH F O   1 
HETATM 13639 O  O   . HOH MA 4 .   ? 33.471  36.523  35.903  1.00 59.58  ? 431 HOH F O   1 
HETATM 13640 O  O   . HOH MA 4 .   ? 7.344   19.781  35.828  1.00 40.93  ? 432 HOH F O   1 
HETATM 13641 O  O   . HOH MA 4 .   ? 36.632  22.488  36.234  1.00 32.16  ? 433 HOH F O   1 
HETATM 13642 O  O   . HOH MA 4 .   ? 11.237  32.038  26.435  1.00 39.63  ? 434 HOH F O   1 
HETATM 13643 O  O   . HOH MA 4 .   ? 9.354   8.067   44.217  1.00 46.02  ? 435 HOH F O   1 
HETATM 13644 O  O   . HOH MA 4 .   ? 13.121  12.806  50.185  1.00 39.27  ? 436 HOH F O   1 
HETATM 13645 O  O   . HOH MA 4 .   ? 23.634  20.994  15.281  1.00 45.73  ? 437 HOH F O   1 
HETATM 13646 O  O   . HOH MA 4 .   ? 28.735  14.403  46.269  1.00 48.01  ? 438 HOH F O   1 
HETATM 13647 O  O   . HOH MA 4 .   ? 17.719  8.557   23.812  1.00 54.08  ? 439 HOH F O   1 
HETATM 13648 O  O   . HOH MA 4 .   ? 35.272  20.230  22.849  1.00 49.00  ? 440 HOH F O   1 
HETATM 13649 O  O   . HOH MA 4 .   ? 2.934   24.033  29.849  1.00 49.99  ? 441 HOH F O   1 
HETATM 13650 O  O   . HOH MA 4 .   ? 40.312  15.409  27.883  1.00 28.38  ? 442 HOH F O   1 
HETATM 13651 O  O   . HOH MA 4 .   ? 14.496  13.869  52.253  1.00 31.09  ? 443 HOH F O   1 
HETATM 13652 O  O   . HOH MA 4 .   ? 5.623   19.551  33.691  1.00 44.34  ? 444 HOH F O   1 
HETATM 13653 O  O   . HOH MA 4 .   ? 20.601  11.188  18.224  1.00 55.24  ? 445 HOH F O   1 
HETATM 13654 O  O   . HOH MA 4 .   ? 24.849  10.579  44.766  1.00 50.75  ? 446 HOH F O   1 
HETATM 13655 O  O   . HOH MA 4 .   ? 33.403  31.747  26.838  1.00 56.38  ? 447 HOH F O   1 
HETATM 13656 O  O   . HOH MA 4 .   ? 37.180  13.703  24.221  1.00 44.29  ? 448 HOH F O   1 
HETATM 13657 O  O   . HOH MA 4 .   ? 12.789  28.721  18.341  1.00 49.76  ? 449 HOH F O   1 
HETATM 13658 O  O   . HOH MA 4 .   ? 43.089  18.733  25.987  1.00 40.55  ? 450 HOH F O   1 
HETATM 13659 O  O   . HOH MA 4 .   ? 39.386  13.999  25.797  1.00 33.62  ? 451 HOH F O   1 
HETATM 13660 O  O   . HOH MA 4 .   ? 43.152  28.462  39.637  1.00 45.77  ? 452 HOH F O   1 
HETATM 13661 O  O   . HOH MA 4 .   ? 3.497   9.313   22.027  1.00 58.21  ? 453 HOH F O   1 
HETATM 13662 O  O   . HOH MA 4 .   ? 34.460  3.261   22.842  1.00 56.29  ? 454 HOH F O   1 
HETATM 13663 O  O   . HOH MA 4 .   ? 20.194  32.468  46.015  1.00 55.11  ? 455 HOH F O   1 
HETATM 13664 O  O   . HOH MA 4 .   ? 16.547  9.118   9.142   1.00 52.97  ? 456 HOH F O   1 
HETATM 13665 O  O   . HOH NA 4 .   ? -18.757 42.015  28.667  1.00 44.20  ? 301 HOH D O   1 
HETATM 13666 O  O   . HOH NA 4 .   ? -7.539  40.200  8.642   1.00 49.08  ? 302 HOH D O   1 
HETATM 13667 O  O   . HOH NA 4 .   ? -1.169  60.658  31.669  1.00 48.75  ? 303 HOH D O   1 
HETATM 13668 O  O   . HOH NA 4 .   ? 0.242   38.277  18.317  1.00 30.88  ? 304 HOH D O   1 
HETATM 13669 O  O   . HOH NA 4 .   ? 6.580   42.504  28.355  1.00 43.64  ? 305 HOH D O   1 
HETATM 13670 O  O   . HOH NA 4 .   ? -16.649 54.005  27.229  1.00 36.48  ? 306 HOH D O   1 
HETATM 13671 O  O   . HOH NA 4 .   ? -5.241  35.802  6.523   1.00 51.28  ? 307 HOH D O   1 
HETATM 13672 O  O   . HOH NA 4 .   ? -4.850  51.535  34.640  1.00 45.28  ? 308 HOH D O   1 
HETATM 13673 O  O   . HOH NA 4 .   ? -31.429 44.262  15.158  1.00 39.80  ? 309 HOH D O   1 
HETATM 13674 O  O   . HOH NA 4 .   ? -15.173 53.627  31.011  1.00 39.35  ? 310 HOH D O   1 
HETATM 13675 O  O   . HOH NA 4 .   ? -10.646 54.034  14.534  1.00 37.14  ? 311 HOH D O   1 
HETATM 13676 O  O   . HOH NA 4 .   ? -1.756  53.487  26.476  1.00 30.19  ? 312 HOH D O   1 
HETATM 13677 O  O   . HOH NA 4 .   ? 1.559   60.825  25.953  1.00 45.83  ? 313 HOH D O   1 
HETATM 13678 O  O   . HOH NA 4 .   ? -2.220  35.043  21.460  1.00 38.95  ? 314 HOH D O   1 
HETATM 13679 O  O   . HOH NA 4 .   ? -15.962 36.178  11.252  1.00 39.04  ? 315 HOH D O   1 
HETATM 13680 O  O   . HOH NA 4 .   ? -16.216 43.986  36.342  1.00 39.44  ? 316 HOH D O   1 
HETATM 13681 O  O   . HOH NA 4 .   ? -15.155 41.523  36.550  1.00 31.44  ? 317 HOH D O   1 
HETATM 13682 O  O   . HOH NA 4 .   ? -18.003 65.781  24.456  1.00 42.68  ? 318 HOH D O   1 
HETATM 13683 O  O   . HOH NA 4 .   ? -12.732 53.600  12.837  1.00 40.21  ? 319 HOH D O   1 
HETATM 13684 O  O   . HOH NA 4 .   ? -27.937 47.514  24.950  1.00 35.79  ? 320 HOH D O   1 
HETATM 13685 O  O   . HOH NA 4 .   ? -5.770  52.833  14.982  1.00 33.48  ? 321 HOH D O   1 
HETATM 13686 O  O   . HOH NA 4 .   ? -11.984 36.451  12.912  1.00 33.10  ? 322 HOH D O   1 
HETATM 13687 O  O   . HOH NA 4 .   ? -10.854 56.599  21.397  1.00 27.57  ? 323 HOH D O   1 
HETATM 13688 O  O   . HOH NA 4 .   ? 6.827   42.842  12.614  1.00 43.11  ? 324 HOH D O   1 
HETATM 13689 O  O   . HOH NA 4 .   ? -23.570 59.906  16.873  1.00 42.94  ? 325 HOH D O   1 
HETATM 13690 O  O   . HOH NA 4 .   ? -1.407  50.293  12.901  1.00 40.79  ? 326 HOH D O   1 
HETATM 13691 O  O   . HOH NA 4 .   ? 1.081   42.265  12.420  1.00 27.28  ? 327 HOH D O   1 
HETATM 13692 O  O   . HOH NA 4 .   ? -22.777 40.011  24.421  1.00 37.96  ? 328 HOH D O   1 
HETATM 13693 O  O   . HOH NA 4 .   ? -17.759 37.264  21.156  1.00 24.25  ? 329 HOH D O   1 
HETATM 13694 O  O   . HOH NA 4 .   ? -25.644 37.526  32.530  1.00 48.65  ? 330 HOH D O   1 
HETATM 13695 O  O   . HOH NA 4 .   ? -7.820  46.603  8.609   1.00 38.21  ? 331 HOH D O   1 
HETATM 13696 O  O   . HOH NA 4 .   ? -18.254 37.246  30.476  1.00 25.23  ? 332 HOH D O   1 
HETATM 13697 O  O   . HOH NA 4 .   ? 2.799   54.759  31.786  1.00 42.79  ? 333 HOH D O   1 
HETATM 13698 O  O   . HOH NA 4 .   ? -20.869 51.889  6.562   1.00 51.88  ? 334 HOH D O   1 
HETATM 13699 O  O   . HOH NA 4 .   ? -0.685  56.081  19.642  1.00 52.34  ? 335 HOH D O   1 
HETATM 13700 O  O   . HOH NA 4 .   ? -2.974  52.198  28.501  1.00 25.42  ? 336 HOH D O   1 
HETATM 13701 O  O   . HOH NA 4 .   ? -5.544  62.224  25.122  1.00 39.61  ? 337 HOH D O   1 
HETATM 13702 O  O   . HOH NA 4 .   ? -8.234  57.744  31.992  1.00 30.39  ? 338 HOH D O   1 
HETATM 13703 O  O   . HOH NA 4 .   ? -10.447 67.498  27.170  1.00 42.35  ? 339 HOH D O   1 
HETATM 13704 O  O   . HOH NA 4 .   ? -9.860  48.755  36.797  1.00 43.14  ? 340 HOH D O   1 
HETATM 13705 O  O   . HOH NA 4 .   ? -19.442 64.849  30.752  1.00 37.50  ? 341 HOH D O   1 
HETATM 13706 O  O   . HOH NA 4 .   ? -6.774  48.450  32.167  1.00 36.93  ? 342 HOH D O   1 
HETATM 13707 O  O   . HOH NA 4 .   ? -22.010 61.637  14.128  1.00 42.01  ? 343 HOH D O   1 
HETATM 13708 O  O   . HOH NA 4 .   ? 0.341   45.956  17.569  1.00 28.05  ? 344 HOH D O   1 
HETATM 13709 O  O   . HOH NA 4 .   ? -17.123 38.836  9.775   1.00 46.46  ? 345 HOH D O   1 
HETATM 13710 O  O   . HOH NA 4 .   ? -4.290  40.479  5.506   1.00 46.17  ? 346 HOH D O   1 
HETATM 13711 O  O   . HOH NA 4 .   ? 0.326   53.946  24.861  1.00 50.48  ? 347 HOH D O   1 
HETATM 13712 O  O   . HOH NA 4 .   ? -27.796 40.605  8.849   1.00 49.23  ? 348 HOH D O   1 
HETATM 13713 O  O   . HOH NA 4 .   ? -21.210 59.595  27.969  1.00 41.50  ? 349 HOH D O   1 
HETATM 13714 O  O   . HOH NA 4 .   ? -3.450  41.988  28.263  1.00 38.52  ? 350 HOH D O   1 
HETATM 13715 O  O   . HOH NA 4 .   ? -27.442 55.835  19.430  1.00 37.45  ? 351 HOH D O   1 
HETATM 13716 O  O   . HOH NA 4 .   ? -7.173  59.639  16.777  1.00 34.66  ? 352 HOH D O   1 
HETATM 13717 O  O   . HOH NA 4 .   ? -28.358 43.224  20.226  1.00 42.49  ? 353 HOH D O   1 
HETATM 13718 O  O   . HOH NA 4 .   ? 2.388   35.327  10.164  1.00 49.75  ? 354 HOH D O   1 
HETATM 13719 O  O   . HOH NA 4 .   ? -31.835 51.199  14.825  1.00 45.48  ? 355 HOH D O   1 
HETATM 13720 O  O   . HOH NA 4 .   ? 0.539   51.846  34.437  1.00 46.97  ? 356 HOH D O   1 
HETATM 13721 O  O   . HOH NA 4 .   ? -8.174  63.487  27.399  1.00 46.59  ? 357 HOH D O   1 
HETATM 13722 O  O   . HOH NA 4 .   ? -8.084  53.913  33.449  1.00 38.91  ? 358 HOH D O   1 
HETATM 13723 O  O   . HOH NA 4 .   ? -5.444  32.672  16.282  1.00 25.10  ? 359 HOH D O   1 
HETATM 13724 O  O   . HOH NA 4 .   ? -6.854  43.554  33.703  1.00 36.36  ? 360 HOH D O   1 
HETATM 13725 O  O   . HOH NA 4 .   ? -12.347 54.481  31.020  1.00 31.70  ? 361 HOH D O   1 
HETATM 13726 O  O   . HOH NA 4 .   ? -1.785  52.616  15.968  1.00 42.61  ? 362 HOH D O   1 
HETATM 13727 O  O   . HOH NA 4 .   ? -19.196 37.424  24.055  1.00 29.75  ? 363 HOH D O   1 
HETATM 13728 O  O   . HOH NA 4 .   ? 2.661   50.713  20.172  1.00 48.71  ? 364 HOH D O   1 
HETATM 13729 O  O   . HOH NA 4 .   ? -9.180  38.502  9.816   1.00 42.59  ? 365 HOH D O   1 
HETATM 13730 O  O   . HOH NA 4 .   ? -0.336  62.837  20.218  1.00 51.22  ? 366 HOH D O   1 
HETATM 13731 O  O   . HOH NA 4 .   ? -22.517 61.943  27.448  1.00 63.41  ? 367 HOH D O   1 
HETATM 13732 O  O   . HOH NA 4 .   ? 1.563   47.705  29.163  1.00 46.43  ? 368 HOH D O   1 
HETATM 13733 O  O   . HOH NA 4 .   ? -6.757  52.590  10.838  1.00 35.63  ? 369 HOH D O   1 
HETATM 13734 O  O   . HOH NA 4 .   ? -16.339 52.977  10.560  1.00 41.35  ? 370 HOH D O   1 
HETATM 13735 O  O   . HOH NA 4 .   ? -0.003  55.621  22.243  1.00 50.37  ? 371 HOH D O   1 
HETATM 13736 O  O   . HOH NA 4 .   ? -24.332 51.752  29.447  1.00 35.18  ? 372 HOH D O   1 
HETATM 13737 O  O   . HOH NA 4 .   ? -13.338 59.977  15.138  1.00 41.78  ? 373 HOH D O   1 
HETATM 13738 O  O   . HOH NA 4 .   ? -28.234 46.756  21.018  1.00 37.89  ? 374 HOH D O   1 
HETATM 13739 O  O   . HOH NA 4 .   ? -18.617 41.063  10.055  1.00 45.62  ? 375 HOH D O   1 
HETATM 13740 O  O   . HOH NA 4 .   ? -17.478 58.163  36.687  1.00 50.96  ? 376 HOH D O   1 
HETATM 13741 O  O   . HOH NA 4 .   ? -17.364 65.478  32.939  1.00 38.50  ? 377 HOH D O   1 
HETATM 13742 O  O   . HOH NA 4 .   ? -1.754  42.093  10.724  1.00 39.06  ? 378 HOH D O   1 
HETATM 13743 O  O   . HOH NA 4 .   ? -22.475 62.013  18.436  1.00 51.74  ? 379 HOH D O   1 
HETATM 13744 O  O   . HOH NA 4 .   ? 0.296   40.455  30.813  1.00 80.36  ? 380 HOH D O   1 
HETATM 13745 O  O   . HOH NA 4 .   ? -8.756  53.124  9.154   1.00 51.26  ? 381 HOH D O   1 
HETATM 13746 O  O   . HOH NA 4 .   ? -30.442 56.819  11.855  1.00 49.92  ? 382 HOH D O   1 
HETATM 13747 O  O   . HOH NA 4 .   ? -9.077  57.065  36.497  1.00 54.94  ? 383 HOH D O   1 
HETATM 13748 O  O   . HOH NA 4 .   ? -25.641 46.704  26.439  1.00 54.03  ? 384 HOH D O   1 
HETATM 13749 O  O   . HOH NA 4 .   ? -22.842 50.488  31.219  1.00 50.53  ? 385 HOH D O   1 
HETATM 13750 O  O   . HOH NA 4 .   ? -25.610 40.996  27.288  1.00 53.71  ? 386 HOH D O   1 
HETATM 13751 O  O   . HOH NA 4 .   ? -11.282 56.854  14.905  1.00 45.78  ? 387 HOH D O   1 
HETATM 13752 O  O   . HOH NA 4 .   ? -30.600 59.534  9.888   1.00 52.32  ? 388 HOH D O   1 
HETATM 13753 O  O   . HOH NA 4 .   ? -1.674  63.076  22.585  1.00 50.11  ? 389 HOH D O   1 
HETATM 13754 O  O   . HOH NA 4 .   ? -24.148 39.805  15.541  1.00 49.78  ? 390 HOH D O   1 
HETATM 13755 O  O   . HOH NA 4 .   ? -30.302 48.782  10.940  1.00 43.98  ? 391 HOH D O   1 
HETATM 13756 O  O   . HOH NA 4 .   ? -13.627 51.925  10.551  1.00 46.43  ? 392 HOH D O   1 
HETATM 13757 O  O   . HOH NA 4 .   ? -27.585 53.564  17.976  1.00 40.00  ? 393 HOH D O   1 
HETATM 13758 O  O   . HOH NA 4 .   ? 3.325   47.459  14.883  1.00 44.78  ? 394 HOH D O   1 
HETATM 13759 O  O   B HOH NA 4 .   ? -11.445 68.645  36.868  0.50 38.22  ? 395 HOH D O   1 
HETATM 13760 O  O   . HOH NA 4 .   ? -29.569 51.695  18.467  1.00 40.93  ? 396 HOH D O   1 
HETATM 13761 O  O   . HOH NA 4 .   ? -4.944  56.089  34.623  1.00 47.42  ? 397 HOH D O   1 
HETATM 13762 O  O   . HOH NA 4 .   ? -24.731 56.959  3.827   1.00 49.88  ? 398 HOH D O   1 
HETATM 13763 O  O   . HOH NA 4 .   ? -12.183 23.652  10.779  1.00 58.49  ? 399 HOH D O   1 
HETATM 13764 O  O   . HOH NA 4 .   ? -16.647 51.036  34.486  1.00 46.86  ? 400 HOH D O   1 
HETATM 13765 O  O   . HOH NA 4 .   ? -29.012 49.284  20.696  1.00 42.66  ? 401 HOH D O   1 
HETATM 13766 O  O   . HOH NA 4 .   ? -20.452 49.066  36.854  1.00 55.60  ? 402 HOH D O   1 
HETATM 13767 O  O   . HOH NA 4 .   ? -29.084 40.629  20.457  1.00 38.66  ? 403 HOH D O   1 
HETATM 13768 O  O   . HOH NA 4 .   ? 5.306   46.940  12.602  1.00 54.22  ? 404 HOH D O   1 
HETATM 13769 O  O   . HOH NA 4 .   ? -10.932 64.459  35.559  1.00 42.42  ? 405 HOH D O   1 
HETATM 13770 O  O   . HOH NA 4 .   ? -24.826 60.632  28.008  1.00 51.03  ? 406 HOH D O   1 
HETATM 13771 O  O   . HOH NA 4 .   ? 1.922   31.237  9.974   1.00 52.98  ? 407 HOH D O   1 
HETATM 13772 O  O   . HOH NA 4 .   ? 4.079   35.803  20.825  1.00 46.36  ? 408 HOH D O   1 
HETATM 13773 O  O   . HOH NA 4 .   ? -4.139  38.903  29.564  1.00 53.13  ? 409 HOH D O   1 
HETATM 13774 O  O   . HOH NA 4 .   ? -27.712 59.614  20.487  1.00 50.29  ? 410 HOH D O   1 
HETATM 13775 O  O   . HOH NA 4 .   ? -31.444 50.858  12.205  1.00 54.80  ? 411 HOH D O   1 
HETATM 13776 O  O   . HOH NA 4 .   ? -24.541 40.584  12.929  1.00 60.61  ? 412 HOH D O   1 
HETATM 13777 O  O   . HOH NA 4 .   ? -33.724 41.655  15.494  1.00 44.74  ? 413 HOH D O   1 
HETATM 13778 O  O   . HOH NA 4 .   ? -5.987  49.399  35.928  1.00 55.34  ? 414 HOH D O   1 
HETATM 13779 O  O   . HOH NA 4 .   ? -14.189 25.518  13.601  1.00 55.71  ? 415 HOH D O   1 
HETATM 13780 O  O   . HOH NA 4 .   ? -7.922  53.766  13.820  1.00 38.50  ? 416 HOH D O   1 
HETATM 13781 O  O   . HOH NA 4 .   ? -10.106 56.027  33.025  1.00 46.34  ? 417 HOH D O   1 
HETATM 13782 O  O   . HOH NA 4 .   ? -31.206 45.324  12.358  1.00 46.99  ? 418 HOH D O   1 
HETATM 13783 O  O   . HOH NA 4 .   ? -5.672  28.394  14.639  1.00 43.77  ? 419 HOH D O   1 
HETATM 13784 O  O   . HOH NA 4 .   ? 0.088   42.946  9.002   1.00 45.84  ? 420 HOH D O   1 
HETATM 13785 O  O   . HOH NA 4 .   ? -9.037  59.495  14.896  1.00 44.62  ? 421 HOH D O   1 
HETATM 13786 O  O   . HOH NA 4 .   ? -15.530 54.511  6.268   1.00 61.63  ? 422 HOH D O   1 
HETATM 13787 O  O   . HOH NA 4 .   ? -26.391 44.527  7.671   1.00 57.10  ? 423 HOH D O   1 
HETATM 13788 O  O   . HOH NA 4 .   ? 2.468   48.287  36.492  1.00 57.74  ? 424 HOH D O   1 
HETATM 13789 O  O   . HOH NA 4 .   ? -18.602 54.509  1.457   1.00 54.12  ? 425 HOH D O   1 
HETATM 13790 O  O   . HOH OA 4 .   ? -30.004 29.928  27.258  1.00 40.83  ? 301 HOH G O   1 
HETATM 13791 O  O   . HOH OA 4 .   ? -27.920 26.975  43.528  1.00 45.29  ? 302 HOH G O   1 
HETATM 13792 O  O   . HOH OA 4 .   ? -35.313 19.126  37.123  1.00 31.22  ? 303 HOH G O   1 
HETATM 13793 O  O   . HOH OA 4 .   ? 3.756   23.958  27.322  1.00 48.88  ? 304 HOH G O   1 
HETATM 13794 O  O   . HOH OA 4 .   ? -10.039 18.521  37.875  1.00 33.20  ? 305 HOH G O   1 
HETATM 13795 O  O   . HOH OA 4 .   ? -6.227  20.466  40.758  1.00 39.91  ? 306 HOH G O   1 
HETATM 13796 O  O   . HOH OA 4 .   ? -8.025  9.050   28.353  1.00 34.67  ? 307 HOH G O   1 
HETATM 13797 O  O   . HOH OA 4 .   ? -22.421 34.227  26.526  1.00 32.95  ? 308 HOH G O   1 
HETATM 13798 O  O   . HOH OA 4 .   ? -11.662 8.422   32.424  1.00 29.61  ? 309 HOH G O   1 
HETATM 13799 O  O   . HOH OA 4 .   ? -32.231 21.586  29.088  1.00 21.02  ? 310 HOH G O   1 
HETATM 13800 O  O   . HOH OA 4 .   ? -18.786 35.140  28.842  1.00 21.03  ? 311 HOH G O   1 
HETATM 13801 O  O   . HOH OA 4 .   ? -15.805 9.960   16.068  1.00 53.84  ? 312 HOH G O   1 
HETATM 13802 O  O   . HOH OA 4 .   ? -12.801 4.197   25.188  1.00 23.31  ? 313 HOH G O   1 
HETATM 13803 O  O   . HOH OA 4 .   ? -4.097  20.012  18.738  1.00 43.58  ? 314 HOH G O   1 
HETATM 13804 O  O   . HOH OA 4 .   ? 0.128   28.265  34.332  1.00 37.34  ? 315 HOH G O   1 
HETATM 13805 O  O   . HOH OA 4 .   ? -19.405 36.278  38.518  1.00 39.99  ? 316 HOH G O   1 
HETATM 13806 O  O   . HOH OA 4 .   ? -3.420  17.469  27.446  1.00 21.23  ? 317 HOH G O   1 
HETATM 13807 O  O   . HOH OA 4 .   ? -16.031 16.962  36.616  1.00 25.61  ? 318 HOH G O   1 
HETATM 13808 O  O   . HOH OA 4 .   ? -32.847 13.648  33.720  1.00 44.55  ? 319 HOH G O   1 
HETATM 13809 O  O   . HOH OA 4 .   ? -27.495 21.523  43.325  1.00 26.57  ? 320 HOH G O   1 
HETATM 13810 O  O   . HOH OA 4 .   ? -12.757 30.441  14.615  1.00 29.45  ? 321 HOH G O   1 
HETATM 13811 O  O   . HOH OA 4 .   ? -27.237 12.944  31.548  1.00 40.45  ? 322 HOH G O   1 
HETATM 13812 O  O   . HOH OA 4 .   ? -22.910 31.422  39.154  1.00 34.79  ? 323 HOH G O   1 
HETATM 13813 O  O   . HOH OA 4 .   ? -37.992 22.065  40.701  1.00 35.90  ? 324 HOH G O   1 
HETATM 13814 O  O   . HOH OA 4 .   ? -15.315 35.264  38.150  1.00 38.63  ? 325 HOH G O   1 
HETATM 13815 O  O   . HOH OA 4 .   ? -10.114 8.102   25.157  1.00 47.89  ? 326 HOH G O   1 
HETATM 13816 O  O   . HOH OA 4 .   ? -36.861 23.346  38.380  1.00 32.00  ? 327 HOH G O   1 
HETATM 13817 O  O   . HOH OA 4 .   ? 1.408   14.462  24.242  1.00 43.82  ? 328 HOH G O   1 
HETATM 13818 O  O   . HOH OA 4 .   ? -2.916  25.367  36.190  1.00 41.18  ? 329 HOH G O   1 
HETATM 13819 O  O   . HOH OA 4 .   ? -13.864 15.324  30.189  1.00 21.81  ? 330 HOH G O   1 
HETATM 13820 O  O   . HOH OA 4 .   ? -3.735  29.046  25.619  1.00 29.36  ? 331 HOH G O   1 
HETATM 13821 O  O   . HOH OA 4 .   ? -31.809 23.610  43.363  1.00 38.10  ? 332 HOH G O   1 
HETATM 13822 O  O   . HOH OA 4 .   ? -24.494 28.734  22.761  1.00 42.42  ? 333 HOH G O   1 
HETATM 13823 O  O   . HOH OA 4 .   ? -3.370  35.828  32.750  1.00 45.07  ? 334 HOH G O   1 
HETATM 13824 O  O   . HOH OA 4 .   ? 2.267   31.902  33.247  1.00 50.59  ? 335 HOH G O   1 
HETATM 13825 O  O   . HOH OA 4 .   ? -17.446 6.689   32.023  1.00 38.21  ? 336 HOH G O   1 
HETATM 13826 O  O   . HOH OA 4 .   ? -34.374 30.760  21.933  1.00 53.19  ? 337 HOH G O   1 
HETATM 13827 O  O   . HOH OA 4 .   ? -26.830 11.422  34.793  1.00 29.89  ? 338 HOH G O   1 
HETATM 13828 O  O   . HOH OA 4 .   ? -6.606  22.938  20.768  1.00 36.29  ? 339 HOH G O   1 
HETATM 13829 O  O   . HOH OA 4 .   ? -2.244  9.945   22.370  1.00 46.95  ? 340 HOH G O   1 
HETATM 13830 O  O   . HOH OA 4 .   ? -14.112 28.111  14.299  1.00 35.49  ? 341 HOH G O   1 
HETATM 13831 O  O   . HOH OA 4 .   ? -23.377 12.881  39.798  1.00 22.67  ? 342 HOH G O   1 
HETATM 13832 O  O   . HOH OA 4 .   ? -23.551 34.846  16.767  1.00 48.82  ? 343 HOH G O   1 
HETATM 13833 O  O   . HOH OA 4 .   ? -20.181 4.451   17.997  1.00 34.19  ? 344 HOH G O   1 
HETATM 13834 O  O   . HOH OA 4 .   ? -30.093 17.327  27.995  1.00 28.68  ? 345 HOH G O   1 
HETATM 13835 O  O   . HOH OA 4 .   ? -8.961  13.526  20.504  1.00 34.79  ? 346 HOH G O   1 
HETATM 13836 O  O   . HOH OA 4 .   ? -28.857 25.800  22.857  1.00 40.54  ? 347 HOH G O   1 
HETATM 13837 O  O   . HOH OA 4 .   ? -18.699 30.313  21.224  1.00 44.06  ? 348 HOH G O   1 
HETATM 13838 O  O   . HOH OA 4 .   ? -23.031 9.653   27.280  1.00 36.03  ? 349 HOH G O   1 
HETATM 13839 O  O   . HOH OA 4 .   ? -19.368 31.271  11.564  1.00 53.30  ? 350 HOH G O   1 
HETATM 13840 O  O   . HOH OA 4 .   ? -33.277 24.950  36.588  1.00 20.63  ? 351 HOH G O   1 
HETATM 13841 O  O   . HOH OA 4 .   ? -30.002 25.827  26.180  1.00 34.91  ? 352 HOH G O   1 
HETATM 13842 O  O   . HOH OA 4 .   ? -16.650 25.419  44.634  1.00 43.78  ? 353 HOH G O   1 
HETATM 13843 O  O   . HOH OA 4 .   ? -7.998  38.617  36.885  1.00 30.18  ? 354 HOH G O   1 
HETATM 13844 O  O   . HOH OA 4 .   ? -3.851  8.662   34.151  1.00 44.93  ? 355 HOH G O   1 
HETATM 13845 O  O   . HOH OA 4 .   ? -25.192 27.789  20.364  1.00 38.89  ? 356 HOH G O   1 
HETATM 13846 O  O   . HOH OA 4 .   ? -16.924 35.137  19.457  1.00 25.40  ? 357 HOH G O   1 
HETATM 13847 O  O   . HOH OA 4 .   ? -34.688 17.218  35.046  1.00 25.67  ? 358 HOH G O   1 
HETATM 13848 O  O   . HOH OA 4 .   ? -17.090 2.101   30.136  1.00 32.41  ? 359 HOH G O   1 
HETATM 13849 O  O   . HOH OA 4 .   ? -3.692  28.444  42.155  1.00 35.69  ? 360 HOH G O   1 
HETATM 13850 O  O   . HOH OA 4 .   ? -4.097  18.816  25.263  1.00 24.78  ? 361 HOH G O   1 
HETATM 13851 O  O   . HOH OA 4 .   ? -18.210 16.783  24.009  1.00 45.24  ? 362 HOH G O   1 
HETATM 13852 O  O   . HOH OA 4 .   ? -12.883 17.325  20.823  1.00 31.00  ? 363 HOH G O   1 
HETATM 13853 O  O   . HOH OA 4 .   ? -38.167 19.447  40.517  1.00 37.21  ? 364 HOH G O   1 
HETATM 13854 O  O   . HOH OA 4 .   ? -29.647 14.015  32.231  1.00 53.10  ? 365 HOH G O   1 
HETATM 13855 O  O   . HOH OA 4 .   ? -4.202  15.375  34.189  1.00 44.89  ? 366 HOH G O   1 
HETATM 13856 O  O   . HOH OA 4 .   ? -30.240 19.556  29.739  1.00 20.94  ? 367 HOH G O   1 
HETATM 13857 O  O   . HOH OA 4 .   ? -24.809 26.732  14.454  1.00 56.35  ? 368 HOH G O   1 
HETATM 13858 O  O   . HOH OA 4 .   ? -10.282 7.208   29.816  1.00 43.35  ? 369 HOH G O   1 
HETATM 13859 O  O   . HOH OA 4 .   ? -20.742 26.802  43.054  1.00 49.57  ? 370 HOH G O   1 
HETATM 13860 O  O   . HOH OA 4 .   ? -0.167  27.083  31.034  1.00 27.68  ? 371 HOH G O   1 
HETATM 13861 O  O   . HOH OA 4 .   ? -5.815  27.640  19.417  1.00 36.86  ? 372 HOH G O   1 
HETATM 13862 O  O   . HOH OA 4 .   ? -26.131 10.983  30.069  1.00 39.54  ? 373 HOH G O   1 
HETATM 13863 O  O   . HOH OA 4 .   ? -22.470 22.210  17.606  1.00 47.52  ? 374 HOH G O   1 
HETATM 13864 O  O   . HOH OA 4 .   ? -22.282 12.692  21.233  1.00 39.48  ? 375 HOH G O   1 
HETATM 13865 O  O   . HOH OA 4 .   ? -12.812 11.208  42.402  1.00 31.68  ? 376 HOH G O   1 
HETATM 13866 O  O   . HOH OA 4 .   ? -11.713 11.903  35.461  1.00 31.77  ? 377 HOH G O   1 
HETATM 13867 O  O   . HOH OA 4 .   ? -4.275  8.320   31.416  1.00 32.80  ? 378 HOH G O   1 
HETATM 13868 O  O   . HOH OA 4 .   ? -24.396 20.983  19.085  1.00 30.89  ? 379 HOH G O   1 
HETATM 13869 O  O   . HOH OA 4 .   ? -0.054  34.330  29.626  1.00 43.30  ? 380 HOH G O   1 
HETATM 13870 O  O   . HOH OA 4 .   ? -21.508 33.101  40.622  1.00 42.91  ? 381 HOH G O   1 
HETATM 13871 O  O   . HOH OA 4 .   ? -14.316 0.879   28.881  1.00 32.52  ? 382 HOH G O   1 
HETATM 13872 O  O   . HOH OA 4 .   ? -28.863 14.613  40.335  1.00 32.71  ? 383 HOH G O   1 
HETATM 13873 O  O   . HOH OA 4 .   ? -19.545 35.172  25.501  1.00 42.36  ? 384 HOH G O   1 
HETATM 13874 O  O   . HOH OA 4 .   ? -12.647 18.782  40.657  1.00 38.46  ? 385 HOH G O   1 
HETATM 13875 O  O   . HOH OA 4 .   ? -33.558 12.397  35.972  1.00 48.44  ? 386 HOH G O   1 
HETATM 13876 O  O   . HOH OA 4 .   ? -12.184 1.956   35.105  1.00 39.64  ? 387 HOH G O   1 
HETATM 13877 O  O   . HOH OA 4 .   ? -17.937 6.597   17.357  1.00 30.94  ? 388 HOH G O   1 
HETATM 13878 O  O   . HOH OA 4 .   ? -5.998  18.231  37.690  1.00 39.48  ? 389 HOH G O   1 
HETATM 13879 O  O   . HOH OA 4 .   ? -6.834  29.042  43.019  1.00 43.23  ? 390 HOH G O   1 
HETATM 13880 O  O   . HOH OA 4 .   ? -14.070 21.099  44.232  1.00 50.50  ? 391 HOH G O   1 
HETATM 13881 O  O   . HOH OA 4 .   ? -3.390  12.641  36.154  1.00 47.10  ? 392 HOH G O   1 
HETATM 13882 O  O   . HOH OA 4 .   ? -31.441 16.362  43.770  1.00 36.05  ? 393 HOH G O   1 
HETATM 13883 O  O   . HOH OA 4 .   ? -25.655 31.926  37.869  1.00 43.68  ? 394 HOH G O   1 
HETATM 13884 O  O   . HOH OA 4 .   ? -37.560 20.749  38.231  1.00 107.80 ? 395 HOH G O   1 
HETATM 13885 O  O   . HOH OA 4 .   ? -33.656 34.611  34.374  1.00 74.82  ? 396 HOH G O   1 
HETATM 13886 O  O   . HOH OA 4 .   ? -15.832 20.751  16.472  1.00 35.22  ? 397 HOH G O   1 
HETATM 13887 O  O   . HOH OA 4 .   ? -9.675  5.125   28.374  1.00 41.51  ? 398 HOH G O   1 
HETATM 13888 O  O   . HOH OA 4 .   ? -14.424 25.340  43.119  1.00 48.64  ? 399 HOH G O   1 
HETATM 13889 O  O   . HOH OA 4 .   ? -5.129  15.057  18.754  1.00 51.93  ? 400 HOH G O   1 
HETATM 13890 O  O   . HOH OA 4 .   ? -0.867  23.902  33.114  1.00 44.74  ? 401 HOH G O   1 
HETATM 13891 O  O   . HOH OA 4 .   ? -27.963 32.609  23.230  1.00 52.66  ? 402 HOH G O   1 
HETATM 13892 O  O   . HOH OA 4 .   ? -26.596 33.463  32.028  1.00 48.05  ? 403 HOH G O   1 
HETATM 13893 O  O   . HOH OA 4 .   ? 4.111   29.421  44.163  1.00 49.97  ? 404 HOH G O   1 
HETATM 13894 O  O   . HOH OA 4 .   ? -24.522 16.187  18.841  1.00 56.05  ? 405 HOH G O   1 
HETATM 13895 O  O   . HOH OA 4 .   ? -20.561 7.506   17.684  1.00 37.59  ? 406 HOH G O   1 
HETATM 13896 O  O   . HOH OA 4 .   ? -38.392 18.717  48.096  1.00 54.84  ? 407 HOH G O   1 
HETATM 13897 O  O   . HOH OA 4 .   ? -4.331  24.423  20.524  1.00 36.16  ? 408 HOH G O   1 
HETATM 13898 O  O   . HOH OA 4 .   ? -3.515  5.926   26.076  1.00 65.11  ? 409 HOH G O   1 
HETATM 13899 O  O   . HOH OA 4 .   ? -2.209  17.638  29.739  1.00 46.30  ? 410 HOH G O   1 
HETATM 13900 O  O   . HOH OA 4 .   ? -21.478 8.227   29.628  1.00 37.35  ? 411 HOH G O   1 
HETATM 13901 O  O   . HOH OA 4 .   ? -26.251 30.323  15.117  1.00 49.04  ? 412 HOH G O   1 
HETATM 13902 O  O   . HOH OA 4 .   ? -3.791  32.156  24.206  1.00 43.87  ? 413 HOH G O   1 
HETATM 13903 O  O   . HOH OA 4 .   ? -12.784 22.698  45.993  1.00 54.63  ? 414 HOH G O   1 
HETATM 13904 O  O   . HOH OA 4 .   ? -16.009 37.714  38.830  1.00 43.49  ? 415 HOH G O   1 
HETATM 13905 O  O   . HOH OA 4 .   ? -31.642 15.092  27.830  1.00 34.61  ? 416 HOH G O   1 
HETATM 13906 O  O   . HOH OA 4 .   ? -28.645 32.022  35.653  1.00 48.52  ? 417 HOH G O   1 
HETATM 13907 O  O   . HOH OA 4 .   ? -28.440 12.315  39.084  1.00 52.11  ? 418 HOH G O   1 
HETATM 13908 O  O   . HOH OA 4 .   ? -18.623 9.252   35.220  1.00 41.83  ? 419 HOH G O   1 
HETATM 13909 O  O   . HOH OA 4 .   ? -10.639 2.712   28.544  1.00 33.81  ? 420 HOH G O   1 
HETATM 13910 O  O   . HOH OA 4 .   ? 2.716   21.548  30.899  1.00 66.65  ? 421 HOH G O   1 
HETATM 13911 O  O   . HOH OA 4 .   ? -23.526 26.559  12.088  1.00 59.35  ? 422 HOH G O   1 
HETATM 13912 O  O   . HOH OA 4 .   ? -28.888 29.356  38.905  1.00 47.91  ? 423 HOH G O   1 
HETATM 13913 O  O   . HOH OA 4 .   ? -11.499 1.943   26.110  1.00 35.80  ? 424 HOH G O   1 
HETATM 13914 O  O   . HOH OA 4 .   ? -12.517 2.089   30.506  1.00 32.09  ? 425 HOH G O   1 
HETATM 13915 O  O   . HOH OA 4 .   ? -21.206 5.962   28.657  1.00 32.17  ? 426 HOH G O   1 
HETATM 13916 O  O   . HOH OA 4 .   ? -29.177 18.169  17.958  1.00 61.92  ? 427 HOH G O   1 
HETATM 13917 O  O   . HOH OA 4 .   ? -25.836 18.138  17.467  1.00 62.36  ? 428 HOH G O   1 
HETATM 13918 O  O   . HOH PA 4 .   ? 4.897   -27.495 19.069  1.00 39.98  ? 301 HOH I O   1 
HETATM 13919 O  O   . HOH PA 4 .   ? 8.439   -28.440 21.873  1.00 39.85  ? 302 HOH I O   1 
HETATM 13920 O  O   . HOH PA 4 .   ? 17.686  -20.443 21.521  1.00 51.74  ? 303 HOH I O   1 
HETATM 13921 O  O   . HOH PA 4 .   ? 16.847  -29.435 43.861  1.00 32.67  ? 304 HOH I O   1 
HETATM 13922 O  O   . HOH PA 4 .   ? 35.194  -44.285 33.763  1.00 48.25  ? 305 HOH I O   1 
HETATM 13923 O  O   . HOH PA 4 .   ? 17.890  -31.936 44.121  1.00 47.16  ? 306 HOH I O   1 
HETATM 13924 O  O   . HOH PA 4 .   ? 10.704  -31.637 37.525  1.00 47.46  ? 307 HOH I O   1 
HETATM 13925 O  O   . HOH PA 4 .   ? 22.665  -52.938 40.439  1.00 46.13  ? 308 HOH I O   1 
HETATM 13926 O  O   . HOH PA 4 .   ? 18.579  -46.181 44.323  1.00 58.07  ? 309 HOH I O   1 
HETATM 13927 O  O   . HOH PA 4 .   ? 12.381  -45.659 36.660  1.00 40.84  ? 310 HOH I O   1 
HETATM 13928 O  O   . HOH PA 4 .   ? 26.572  -51.222 33.770  1.00 55.12  ? 311 HOH I O   1 
HETATM 13929 O  O   . HOH PA 4 .   ? 28.101  -39.951 41.153  1.00 44.66  ? 312 HOH I O   1 
HETATM 13930 O  O   . HOH PA 4 .   ? 22.435  -25.281 39.737  1.00 29.56  ? 313 HOH I O   1 
HETATM 13931 O  O   . HOH PA 4 .   ? 12.354  -36.186 41.922  1.00 40.21  ? 314 HOH I O   1 
HETATM 13932 O  O   . HOH PA 4 .   ? 19.059  -41.754 39.661  1.00 55.40  ? 315 HOH I O   1 
HETATM 13933 O  O   . HOH PA 4 .   ? 10.301  -50.556 25.194  1.00 61.13  ? 316 HOH I O   1 
HETATM 13934 O  O   . HOH PA 4 .   ? 10.724  -35.225 16.284  1.00 60.33  ? 317 HOH I O   1 
HETATM 13935 O  O   . HOH PA 4 .   ? 30.145  -29.109 39.028  1.00 61.07  ? 318 HOH I O   1 
HETATM 13936 O  O   . HOH PA 4 .   ? 15.684  -37.332 13.688  1.00 44.00  ? 319 HOH I O   1 
HETATM 13937 O  O   . HOH PA 4 .   ? 26.010  -25.493 34.353  1.00 54.29  ? 320 HOH I O   1 
HETATM 13938 O  O   . HOH PA 4 .   ? 26.194  -25.158 31.462  1.00 38.85  ? 321 HOH I O   1 
HETATM 13939 O  O   . HOH PA 4 .   ? 23.684  -30.433 38.385  1.00 44.37  ? 322 HOH I O   1 
HETATM 13940 O  O   . HOH PA 4 .   ? 29.972  -36.542 41.089  1.00 56.25  ? 323 HOH I O   1 
HETATM 13941 O  O   . HOH PA 4 .   ? 8.285   -24.172 26.730  1.00 49.47  ? 324 HOH I O   1 
HETATM 13942 O  O   . HOH PA 4 .   ? 16.552  -42.436 37.798  1.00 43.47  ? 325 HOH I O   1 
HETATM 13943 O  O   . HOH PA 4 .   ? 18.153  -47.751 22.617  1.00 41.13  ? 326 HOH I O   1 
HETATM 13944 O  O   . HOH PA 4 .   ? 19.544  -53.444 41.706  1.00 41.00  ? 327 HOH I O   1 
HETATM 13945 O  O   . HOH PA 4 .   ? 21.466  -50.083 44.403  1.00 50.02  ? 328 HOH I O   1 
HETATM 13946 O  O   . HOH PA 4 .   ? 41.462  -42.745 29.729  1.00 63.48  ? 329 HOH I O   1 
HETATM 13947 O  O   . HOH PA 4 .   ? 4.924   -26.435 29.008  1.00 60.21  ? 330 HOH I O   1 
HETATM 13948 O  O   . HOH PA 4 .   ? 19.272  -40.785 14.921  1.00 57.19  ? 331 HOH I O   1 
HETATM 13949 O  O   . HOH PA 4 .   ? 8.104   -37.894 16.658  1.00 52.55  ? 332 HOH I O   1 
HETATM 13950 O  O   . HOH PA 4 .   ? 37.315  -36.782 42.516  1.00 53.34  ? 333 HOH I O   1 
HETATM 13951 O  O   . HOH PA 4 .   ? 25.596  -18.168 17.475  1.00 47.08  ? 334 HOH I O   1 
HETATM 13952 O  O   . HOH PA 4 .   ? 42.459  -45.238 29.235  1.00 67.28  ? 335 HOH I O   1 
HETATM 13953 O  O   . HOH PA 4 .   ? 24.846  -47.900 16.262  1.00 56.70  ? 336 HOH I O   1 
HETATM 13954 O  O   . HOH PA 4 .   ? 40.690  -26.550 24.491  1.00 59.86  ? 337 HOH I O   1 
HETATM 13955 O  O   . HOH PA 4 .   ? -2.952  -45.983 34.069  1.00 57.15  ? 338 HOH I O   1 
HETATM 13956 O  O   . HOH QA 4 .   ? 25.628  -6.113  32.496  1.00 45.89  ? 301 HOH K O   1 
HETATM 13957 O  O   . HOH QA 4 .   ? 7.539   -8.383  44.109  1.00 37.27  ? 302 HOH K O   1 
HETATM 13958 O  O   . HOH QA 4 .   ? 20.314  8.086   32.723  1.00 26.19  ? 303 HOH K O   1 
HETATM 13959 O  O   . HOH QA 4 .   ? 35.984  -10.152 44.292  1.00 35.72  ? 304 HOH K O   1 
HETATM 13960 O  O   . HOH QA 4 .   ? 28.367  2.348   39.008  1.00 45.29  ? 305 HOH K O   1 
HETATM 13961 O  O   . HOH QA 4 .   ? 10.844  -5.346  30.628  1.00 30.60  ? 306 HOH K O   1 
HETATM 13962 O  O   . HOH QA 4 .   ? 12.448  -6.591  28.887  1.00 30.00  ? 307 HOH K O   1 
HETATM 13963 O  O   . HOH QA 4 .   ? 35.463  -13.937 37.116  1.00 42.73  ? 308 HOH K O   1 
HETATM 13964 O  O   . HOH QA 4 .   ? 12.454  -6.430  42.759  1.00 34.58  ? 309 HOH K O   1 
HETATM 13965 O  O   . HOH QA 4 .   ? 30.994  -1.431  44.214  1.00 46.43  ? 310 HOH K O   1 
HETATM 13966 O  O   . HOH QA 4 .   ? 20.113  -24.317 47.546  1.00 36.58  ? 311 HOH K O   1 
HETATM 13967 O  O   . HOH QA 4 .   ? 23.666  -23.284 38.431  1.00 31.83  ? 312 HOH K O   1 
HETATM 13968 O  O   . HOH QA 4 .   ? 25.931  -23.378 29.288  1.00 49.79  ? 313 HOH K O   1 
HETATM 13969 O  O   . HOH QA 4 .   ? 16.215  3.634   38.574  1.00 32.56  ? 314 HOH K O   1 
HETATM 13970 O  O   . HOH QA 4 .   ? 17.057  -6.293  50.077  1.00 31.45  ? 315 HOH K O   1 
HETATM 13971 O  O   . HOH QA 4 .   ? 18.326  -5.155  44.276  1.00 24.37  ? 316 HOH K O   1 
HETATM 13972 O  O   . HOH QA 4 .   ? 25.993  -15.632 55.385  1.00 52.23  ? 317 HOH K O   1 
HETATM 13973 O  O   . HOH QA 4 .   ? 6.157   -15.116 32.366  1.00 33.60  ? 318 HOH K O   1 
HETATM 13974 O  O   . HOH QA 4 .   ? 30.781  -20.917 51.618  1.00 58.74  ? 319 HOH K O   1 
HETATM 13975 O  O   . HOH QA 4 .   ? 19.106  -3.351  37.570  1.00 25.39  ? 320 HOH K O   1 
HETATM 13976 O  O   . HOH QA 4 .   ? 6.442   -13.006 38.450  1.00 37.35  ? 321 HOH K O   1 
HETATM 13977 O  O   . HOH QA 4 .   ? 10.424  -26.434 40.932  1.00 41.90  ? 322 HOH K O   1 
HETATM 13978 O  O   . HOH QA 4 .   ? 18.240  -5.404  24.781  1.00 48.27  ? 323 HOH K O   1 
HETATM 13979 O  O   . HOH QA 4 .   ? 8.586   -3.301  34.375  1.00 35.08  ? 324 HOH K O   1 
HETATM 13980 O  O   . HOH QA 4 .   ? 21.246  -21.303 49.887  1.00 40.79  ? 325 HOH K O   1 
HETATM 13981 O  O   . HOH QA 4 .   ? 25.739  -9.794  55.314  1.00 37.39  ? 326 HOH K O   1 
HETATM 13982 O  O   . HOH QA 4 .   ? 27.140  -18.097 31.354  1.00 44.02  ? 327 HOH K O   1 
HETATM 13983 O  O   . HOH QA 4 .   ? 6.262   -10.886 34.493  1.00 48.17  ? 328 HOH K O   1 
HETATM 13984 O  O   . HOH QA 4 .   ? 33.758  -13.219 51.376  1.00 42.69  ? 329 HOH K O   1 
HETATM 13985 O  O   . HOH QA 4 .   ? 14.395  3.325   33.910  1.00 33.41  ? 330 HOH K O   1 
HETATM 13986 O  O   . HOH QA 4 .   ? 20.162  11.141  36.694  1.00 36.79  ? 331 HOH K O   1 
HETATM 13987 O  O   . HOH QA 4 .   ? 23.266  -19.535 49.567  1.00 34.68  ? 332 HOH K O   1 
HETATM 13988 O  O   . HOH QA 4 .   ? 23.174  2.846   42.256  1.00 40.50  ? 333 HOH K O   1 
HETATM 13989 O  O   . HOH QA 4 .   ? 29.129  0.471   47.334  1.00 37.47  ? 334 HOH K O   1 
HETATM 13990 O  O   . HOH QA 4 .   ? 15.146  -10.330 54.367  1.00 40.35  ? 335 HOH K O   1 
HETATM 13991 O  O   . HOH QA 4 .   ? 28.741  -17.877 50.994  1.00 57.16  ? 336 HOH K O   1 
HETATM 13992 O  O   . HOH QA 4 .   ? 18.485  -1.502  26.734  1.00 42.83  ? 337 HOH K O   1 
HETATM 13993 O  O   . HOH QA 4 .   ? 37.573  -10.254 47.268  1.00 48.24  ? 338 HOH K O   1 
HETATM 13994 O  O   . HOH QA 4 .   ? 40.174  -19.488 40.627  1.00 63.94  ? 339 HOH K O   1 
HETATM 13995 O  O   . HOH QA 4 .   ? 18.391  -13.602 52.646  1.00 46.20  ? 340 HOH K O   1 
HETATM 13996 O  O   . HOH QA 4 .   ? 22.031  9.991   39.042  1.00 35.54  ? 341 HOH K O   1 
HETATM 13997 O  O   . HOH QA 4 .   ? 15.995  4.747   35.769  1.00 36.20  ? 342 HOH K O   1 
HETATM 13998 O  O   . HOH QA 4 .   ? -2.746  -18.918 41.197  1.00 46.15  ? 343 HOH K O   1 
HETATM 13999 O  O   . HOH QA 4 .   ? 8.486   -3.011  37.560  1.00 47.04  ? 344 HOH K O   1 
HETATM 14000 O  O   . HOH QA 4 .   ? 4.511   -16.247 43.965  1.00 36.58  ? 345 HOH K O   1 
HETATM 14001 O  O   . HOH QA 4 .   ? 8.382   3.413   37.239  1.00 36.23  ? 346 HOH K O   1 
HETATM 14002 O  O   . HOH QA 4 .   ? 22.226  -5.139  28.420  1.00 40.20  ? 347 HOH K O   1 
HETATM 14003 O  O   . HOH QA 4 .   ? 13.566  -6.782  46.450  1.00 27.60  ? 348 HOH K O   1 
HETATM 14004 O  O   . HOH QA 4 .   ? 15.022  0.067   41.509  1.00 25.84  ? 349 HOH K O   1 
HETATM 14005 O  O   . HOH QA 4 .   ? 8.850   -6.183  41.420  1.00 40.28  ? 350 HOH K O   1 
HETATM 14006 O  O   . HOH QA 4 .   ? 10.166  3.856   34.901  1.00 34.67  ? 351 HOH K O   1 
HETATM 14007 O  O   . HOH QA 4 .   ? 19.122  8.145   43.854  1.00 52.15  ? 352 HOH K O   1 
HETATM 14008 O  O   . HOH QA 4 .   ? 29.437  -5.116  57.605  1.00 43.33  ? 353 HOH K O   1 
HETATM 14009 O  O   . HOH QA 4 .   ? 16.316  6.955   34.215  1.00 40.61  ? 354 HOH K O   1 
HETATM 14010 O  O   A HOH QA 4 .   ? 11.458  -11.102 50.851  0.50 29.74  ? 355 HOH K O   1 
HETATM 14011 O  O   . HOH QA 4 .   ? 3.955   -17.976 24.606  1.00 47.11  ? 356 HOH K O   1 
HETATM 14012 O  O   . HOH QA 4 .   ? 33.814  -14.577 35.038  1.00 58.71  ? 357 HOH K O   1 
HETATM 14013 O  O   . HOH QA 4 .   ? 32.061  -4.832  31.432  1.00 58.78  ? 358 HOH K O   1 
HETATM 14014 O  O   . HOH QA 4 .   ? 14.961  -16.864 24.200  1.00 48.37  ? 359 HOH K O   1 
HETATM 14015 O  O   . HOH QA 4 .   ? 15.203  10.069  41.654  1.00 45.17  ? 360 HOH K O   1 
HETATM 14016 O  O   . HOH QA 4 .   ? 36.270  -9.029  51.171  1.00 40.69  ? 361 HOH K O   1 
HETATM 14017 O  O   . HOH QA 4 .   ? 31.014  5.199   32.195  1.00 43.18  ? 362 HOH K O   1 
HETATM 14018 O  O   . HOH QA 4 .   ? 28.513  5.840   28.078  1.00 38.92  ? 363 HOH K O   1 
HETATM 14019 O  O   . HOH QA 4 .   ? 41.018  -16.652 42.819  1.00 50.60  ? 364 HOH K O   1 
HETATM 14020 O  O   . HOH QA 4 .   ? 2.394   -18.573 32.848  1.00 57.07  ? 365 HOH K O   1 
HETATM 14021 O  O   . HOH QA 4 .   ? 4.084   -11.831 30.448  1.00 55.15  ? 366 HOH K O   1 
HETATM 14022 O  O   . HOH QA 4 .   ? 33.279  -2.548  45.047  1.00 52.47  ? 367 HOH K O   1 
HETATM 14023 O  O   . HOH QA 4 .   ? 33.213  -15.422 53.905  1.00 58.51  ? 368 HOH K O   1 
HETATM 14024 O  O   . HOH QA 4 .   ? 16.608  -25.309 48.852  1.00 56.27  ? 369 HOH K O   1 
HETATM 14025 O  O   . HOH QA 4 .   ? 38.408  -20.086 44.197  1.00 54.06  ? 370 HOH K O   1 
HETATM 14026 O  O   . HOH QA 4 .   ? 6.471   -6.592  32.684  1.00 44.37  ? 371 HOH K O   1 
HETATM 14027 O  O   . HOH QA 4 .   ? 9.315   -0.136  47.176  1.00 43.73  ? 372 HOH K O   1 
HETATM 14028 O  O   . HOH QA 4 .   ? 18.808  10.284  33.275  1.00 32.36  ? 373 HOH K O   1 
HETATM 14029 O  O   . HOH QA 4 .   ? 16.846  9.430   34.937  1.00 40.56  ? 374 HOH K O   1 
HETATM 14030 O  O   . HOH QA 4 .   ? 17.575  10.046  37.414  1.00 28.84  ? 375 HOH K O   1 
HETATM 14031 O  O   . HOH QA 4 .   ? 17.613  -15.994 20.183  1.00 52.09  ? 376 HOH K O   1 
HETATM 14032 O  O   . HOH QA 4 .   ? 37.065  -22.834 50.185  1.00 56.54  ? 377 HOH K O   1 
HETATM 14033 O  O   . HOH QA 4 .   ? 11.212  -23.247 29.912  1.00 63.82  ? 378 HOH K O   1 
HETATM 14034 O  O   . HOH QA 4 .   ? 33.848  -0.124  21.041  1.00 63.14  ? 379 HOH K O   1 
HETATM 14035 O  O   . HOH QA 4 .   ? 33.251  -27.509 54.128  1.00 61.98  ? 380 HOH K O   1 
HETATM 14036 O  O   . HOH RA 4 .   ? 19.817  -13.408 54.768  1.00 45.23  ? 301 HOH M O   1 
HETATM 14037 O  O   . HOH RA 4 .   ? 31.690  11.477  63.668  1.00 40.62  ? 302 HOH M O   1 
HETATM 14038 O  O   . HOH RA 4 .   ? 0.691   2.882   66.361  1.00 44.68  ? 303 HOH M O   1 
HETATM 14039 O  O   . HOH RA 4 .   ? 16.806  -4.225  48.436  1.00 25.96  ? 304 HOH M O   1 
HETATM 14040 O  O   . HOH RA 4 .   ? 14.006  3.828   47.863  1.00 29.11  ? 305 HOH M O   1 
HETATM 14041 O  O   . HOH RA 4 .   ? 21.440  5.959   49.811  1.00 34.78  ? 306 HOH M O   1 
HETATM 14042 O  O   . HOH RA 4 .   ? 12.305  -0.541  76.071  1.00 46.46  ? 307 HOH M O   1 
HETATM 14043 O  O   . HOH RA 4 .   ? 14.918  5.827   55.377  1.00 26.25  ? 308 HOH M O   1 
HETATM 14044 O  O   . HOH RA 4 .   ? 15.904  12.427  54.022  1.00 30.19  ? 309 HOH M O   1 
HETATM 14045 O  O   . HOH RA 4 .   ? 15.142  18.086  52.293  1.00 36.58  ? 310 HOH M O   1 
HETATM 14046 O  O   . HOH RA 4 .   ? 9.823   13.042  53.724  1.00 32.64  ? 311 HOH M O   1 
HETATM 14047 O  O   . HOH RA 4 .   ? 14.012  -1.768  74.327  1.00 44.25  ? 312 HOH M O   1 
HETATM 14048 O  O   . HOH RA 4 .   ? 25.294  2.278   53.472  1.00 39.14  ? 313 HOH M O   1 
HETATM 14049 O  O   . HOH RA 4 .   ? 4.675   2.040   57.134  1.00 27.71  ? 314 HOH M O   1 
HETATM 14050 O  O   . HOH RA 4 .   ? 0.653   8.901   59.039  1.00 49.22  ? 315 HOH M O   1 
HETATM 14051 O  O   . HOH RA 4 .   ? 24.895  -8.581  52.959  1.00 38.37  ? 316 HOH M O   1 
HETATM 14052 O  O   . HOH RA 4 .   ? 23.673  -0.954  50.366  1.00 27.76  ? 317 HOH M O   1 
HETATM 14053 O  O   . HOH RA 4 .   ? 5.679   0.344   70.374  1.00 45.65  ? 318 HOH M O   1 
HETATM 14054 O  O   . HOH RA 4 .   ? 0.468   -1.962  55.803  1.00 49.20  ? 319 HOH M O   1 
HETATM 14055 O  O   . HOH RA 4 .   ? -4.072  6.628   68.297  1.00 48.71  ? 320 HOH M O   1 
HETATM 14056 O  O   . HOH RA 4 .   ? 10.947  -0.072  49.980  1.00 38.20  ? 321 HOH M O   1 
HETATM 14057 O  O   . HOH RA 4 .   ? 6.182   -6.026  53.494  1.00 46.91  ? 322 HOH M O   1 
HETATM 14058 O  O   . HOH RA 4 .   ? 25.167  22.329  56.384  1.00 43.57  ? 323 HOH M O   1 
HETATM 14059 O  O   . HOH RA 4 .   ? 30.318  8.215   60.652  1.00 34.54  ? 324 HOH M O   1 
HETATM 14060 O  O   . HOH RA 4 .   ? 2.575   6.258   68.007  1.00 30.90  ? 325 HOH M O   1 
HETATM 14061 O  O   . HOH RA 4 .   ? -0.975  9.243   63.235  1.00 25.46  ? 326 HOH M O   1 
HETATM 14062 O  O   . HOH RA 4 .   ? 19.984  3.883   47.500  1.00 42.94  ? 327 HOH M O   1 
HETATM 14063 O  O   . HOH RA 4 .   ? 1.275   13.437  59.389  1.00 40.60  ? 328 HOH M O   1 
HETATM 14064 O  O   . HOH RA 4 .   ? 15.722  15.129  73.722  1.00 42.22  ? 329 HOH M O   1 
HETATM 14065 O  O   . HOH RA 4 .   ? 11.661  -4.439  58.074  1.00 33.88  ? 330 HOH M O   1 
HETATM 14066 O  O   . HOH RA 4 .   ? 5.236   1.007   59.533  1.00 23.49  ? 331 HOH M O   1 
HETATM 14067 O  O   . HOH RA 4 .   ? 15.571  -9.126  62.299  1.00 50.78  ? 332 HOH M O   1 
HETATM 14068 O  O   . HOH RA 4 .   ? 0.923   19.989  59.185  1.00 38.19  ? 333 HOH M O   1 
HETATM 14069 O  O   . HOH RA 4 .   ? 15.778  3.425   41.253  1.00 44.94  ? 334 HOH M O   1 
HETATM 14070 O  O   . HOH RA 4 .   ? 27.817  10.310  51.479  1.00 36.31  ? 335 HOH M O   1 
HETATM 14071 O  O   . HOH RA 4 .   ? 7.402   -0.397  65.597  1.00 36.65  ? 336 HOH M O   1 
HETATM 14072 O  O   . HOH RA 4 .   ? 14.786  6.687   78.058  1.00 36.87  ? 337 HOH M O   1 
HETATM 14073 O  O   . HOH RA 4 .   ? 33.924  15.728  61.369  1.00 56.47  ? 338 HOH M O   1 
HETATM 14074 O  O   . HOH RA 4 .   ? 6.002   12.155  53.181  1.00 38.04  ? 339 HOH M O   1 
HETATM 14075 O  O   . HOH RA 4 .   ? 28.630  16.757  51.927  1.00 47.74  ? 340 HOH M O   1 
HETATM 14076 O  O   . HOH RA 4 .   ? 28.065  10.853  69.531  1.00 53.41  ? 341 HOH M O   1 
HETATM 14077 O  O   . HOH RA 4 .   ? 7.240   1.443   47.716  1.00 36.40  ? 342 HOH M O   1 
HETATM 14078 O  O   . HOH RA 4 .   ? 20.959  0.022   44.771  1.00 27.98  ? 343 HOH M O   1 
HETATM 14079 O  O   . HOH RA 4 .   ? 0.532   -5.034  58.458  1.00 52.83  ? 344 HOH M O   1 
HETATM 14080 O  O   . HOH RA 4 .   ? 14.587  -1.779  61.634  1.00 27.71  ? 345 HOH M O   1 
HETATM 14081 O  O   . HOH RA 4 .   ? 11.709  16.273  52.892  1.00 35.96  ? 346 HOH M O   1 
HETATM 14082 O  O   . HOH RA 4 .   ? 0.849   10.358  54.276  1.00 61.72  ? 347 HOH M O   1 
HETATM 14083 O  O   . HOH RA 4 .   ? 12.681  -6.638  48.946  1.00 45.92  ? 348 HOH M O   1 
HETATM 14084 O  O   . HOH RA 4 .   ? 24.992  0.943   67.164  1.00 42.91  ? 349 HOH M O   1 
HETATM 14085 O  O   . HOH RA 4 .   ? 18.513  -2.524  43.830  1.00 30.51  ? 350 HOH M O   1 
HETATM 14086 O  O   . HOH RA 4 .   ? 13.210  0.748   48.345  1.00 34.72  ? 351 HOH M O   1 
HETATM 14087 O  O   . HOH RA 4 .   ? 5.520   15.685  53.371  1.00 44.51  ? 352 HOH M O   1 
HETATM 14088 O  O   . HOH RA 4 .   ? 5.608   7.601   51.717  1.00 41.61  ? 353 HOH M O   1 
HETATM 14089 O  O   . HOH RA 4 .   ? -2.645  10.451  69.743  1.00 44.91  ? 354 HOH M O   1 
HETATM 14090 O  O   . HOH RA 4 .   ? 30.025  10.590  61.731  1.00 41.96  ? 355 HOH M O   1 
HETATM 14091 O  O   . HOH RA 4 .   ? 34.289  16.520  57.934  1.00 58.08  ? 356 HOH M O   1 
HETATM 14092 O  O   . HOH RA 4 .   ? 33.889  14.897  64.178  1.00 51.12  ? 357 HOH M O   1 
HETATM 14093 O  O   . HOH RA 4 .   ? 6.221   4.052   46.208  1.00 37.26  ? 358 HOH M O   1 
HETATM 14094 O  O   . HOH RA 4 .   ? 22.370  -8.576  54.983  1.00 28.75  ? 359 HOH M O   1 
HETATM 14095 O  O   . HOH RA 4 .   ? 21.237  -14.498 57.220  1.00 56.64  ? 360 HOH M O   1 
HETATM 14096 O  O   . HOH RA 4 .   ? 13.032  8.068   49.550  1.00 25.59  ? 361 HOH M O   1 
HETATM 14097 O  O   . HOH RA 4 .   ? 10.116  -4.029  62.335  1.00 40.19  ? 362 HOH M O   1 
HETATM 14098 O  O   . HOH RA 4 .   ? 27.998  5.924   53.534  1.00 48.27  ? 363 HOH M O   1 
HETATM 14099 O  O   . HOH RA 4 .   ? 22.151  -10.619 56.842  1.00 41.57  ? 364 HOH M O   1 
HETATM 14100 O  O   . HOH RA 4 .   ? 23.866  -1.737  59.146  1.00 48.68  ? 365 HOH M O   1 
HETATM 14101 O  O   . HOH RA 4 .   ? -0.150  24.311  70.217  1.00 70.73  ? 366 HOH M O   1 
HETATM 14102 O  O   . HOH RA 4 .   ? 13.206  -1.863  47.469  1.00 30.07  ? 367 HOH M O   1 
HETATM 14103 O  O   . HOH RA 4 .   ? 34.883  13.984  57.420  1.00 48.27  ? 368 HOH M O   1 
HETATM 14104 O  O   . HOH RA 4 .   ? 16.699  12.566  75.403  1.00 42.63  ? 369 HOH M O   1 
HETATM 14105 O  O   . HOH RA 4 .   ? 24.673  2.981   77.486  1.00 52.30  ? 370 HOH M O   1 
HETATM 14106 O  O   . HOH RA 4 .   ? 22.739  -0.034  68.758  1.00 47.46  ? 371 HOH M O   1 
HETATM 14107 O  O   . HOH RA 4 .   ? 4.043   4.854   53.821  1.00 40.54  ? 372 HOH M O   1 
HETATM 14108 O  O   . HOH RA 4 .   ? 4.563   7.864   49.138  1.00 62.87  ? 373 HOH M O   1 
HETATM 14109 O  O   . HOH RA 4 .   ? 16.968  -3.118  67.923  1.00 44.35  ? 374 HOH M O   1 
HETATM 14110 O  O   . HOH RA 4 .   ? 7.734   -6.529  59.403  1.00 52.04  ? 375 HOH M O   1 
HETATM 14111 O  O   . HOH RA 4 .   ? -4.531  11.443  64.684  1.00 56.98  ? 376 HOH M O   1 
HETATM 14112 O  O   . HOH RA 4 .   ? 24.771  -7.310  56.167  1.00 38.19  ? 377 HOH M O   1 
HETATM 14113 O  O   . HOH RA 4 .   ? 10.281  12.341  51.078  1.00 43.47  ? 378 HOH M O   1 
HETATM 14114 O  O   . HOH RA 4 .   ? -0.449  11.337  59.410  1.00 51.24  ? 379 HOH M O   1 
HETATM 14115 O  O   . HOH RA 4 .   ? 38.096  24.900  53.357  1.00 50.88  ? 380 HOH M O   1 
HETATM 14116 O  O   . HOH RA 4 .   ? 14.631  -2.607  45.206  1.00 29.14  ? 381 HOH M O   1 
HETATM 14117 O  O   . HOH RA 4 .   ? 2.362   1.036   67.475  1.00 47.68  ? 382 HOH M O   1 
HETATM 14118 O  O   . HOH RA 4 .   ? 16.271  -0.878  43.794  1.00 29.46  ? 383 HOH M O   1 
HETATM 14119 O  O   . HOH RA 4 .   ? 15.981  -4.906  45.668  1.00 28.03  ? 384 HOH M O   1 
HETATM 14120 O  O   . HOH RA 4 .   ? 14.550  10.240  49.933  1.00 31.48  ? 385 HOH M O   1 
HETATM 14121 O  O   . HOH RA 4 .   ? 3.844   -4.301  65.863  1.00 61.04  ? 386 HOH M O   1 
HETATM 14122 O  O   . HOH RA 4 .   ? 17.604  25.263  69.316  1.00 48.10  ? 387 HOH M O   1 
HETATM 14123 O  O   . HOH RA 4 .   ? 10.873  26.429  66.838  1.00 58.39  ? 388 HOH M O   1 
HETATM 14124 O  O   . HOH RA 4 .   ? 31.439  9.286   65.168  1.00 47.38  ? 389 HOH M O   1 
HETATM 14125 O  O   . HOH RA 4 .   ? 33.883  23.506  48.719  1.00 50.25  ? 390 HOH M O   1 
HETATM 14126 O  O   . HOH RA 4 .   ? 14.216  -6.397  66.019  1.00 52.78  ? 391 HOH M O   1 
HETATM 14127 O  O   . HOH SA 4 .   ? 10.595  0.844   81.994  1.00 49.83  ? 301 HOH O O   1 
HETATM 14128 O  O   . HOH SA 4 .   ? -1.225  6.102   95.912  1.00 55.35  ? 302 HOH O O   1 
HETATM 14129 O  O   . HOH SA 4 .   ? -5.310  7.563   79.790  1.00 41.16  ? 303 HOH O O   1 
HETATM 14130 O  O   . HOH SA 4 .   ? -3.430  20.289  86.364  1.00 39.53  ? 304 HOH O O   1 
HETATM 14131 O  O   . HOH SA 4 .   ? -9.869  24.777  92.193  1.00 56.46  ? 305 HOH O O   1 
HETATM 14132 O  O   . HOH SA 4 .   ? -3.601  0.872   85.535  1.00 46.15  ? 306 HOH O O   1 
HETATM 14133 O  O   . HOH SA 4 .   ? 5.059   11.093  96.734  1.00 61.01  ? 307 HOH O O   1 
HETATM 14134 O  O   . HOH SA 4 .   ? 14.219  18.438  79.570  1.00 50.40  ? 308 HOH O O   1 
HETATM 14135 O  O   . HOH SA 4 .   ? 14.850  9.326   79.279  1.00 36.48  ? 309 HOH O O   1 
HETATM 14136 O  O   . HOH SA 4 .   ? -2.610  1.710   79.458  1.00 45.46  ? 310 HOH O O   1 
HETATM 14137 O  O   . HOH SA 4 .   ? 4.536   0.223   76.060  1.00 44.83  ? 311 HOH O O   1 
HETATM 14138 O  O   . HOH SA 4 .   ? 22.174  19.198  82.438  1.00 70.24  ? 312 HOH O O   1 
HETATM 14139 O  O   . HOH SA 4 .   ? 19.713  19.828  83.398  1.00 54.86  ? 313 HOH O O   1 
HETATM 14140 O  O   . HOH SA 4 .   ? 15.448  0.202   86.254  1.00 62.45  ? 314 HOH O O   1 
HETATM 14141 O  O   . HOH SA 4 .   ? 9.814   23.872  89.886  1.00 52.00  ? 315 HOH O O   1 
HETATM 14142 O  O   . HOH SA 4 .   ? 21.783  16.392  95.850  1.00 47.64  ? 316 HOH O O   1 
HETATM 14143 O  O   . HOH SA 4 .   ? 8.854   27.693  83.668  1.00 58.50  ? 317 HOH O O   1 
HETATM 14144 O  O   . HOH SA 4 .   ? 0.093   19.901  75.423  1.00 52.56  ? 318 HOH O O   1 
HETATM 14145 O  O   . HOH SA 4 .   ? -8.305  14.105  96.011  1.00 59.62  ? 319 HOH O O   1 
HETATM 14146 O  O   . HOH SA 4 .   ? -11.696 17.400  87.089  1.00 51.92  ? 320 HOH O O   1 
HETATM 14147 O  O   . HOH SA 4 .   ? 10.909  26.274  89.288  1.00 48.38  ? 321 HOH O O   1 
HETATM 14148 O  O   . HOH SA 4 .   ? 6.326   30.859  88.241  1.00 55.97  ? 322 HOH O O   1 
HETATM 14149 O  O   . HOH SA 4 .   ? 5.541   -3.527  88.904  1.00 57.85  ? 323 HOH O O   1 
HETATM 14150 O  O   . HOH SA 4 .   ? 20.712  3.194   92.668  1.00 58.93  ? 324 HOH O O   1 
HETATM 14151 O  O   . HOH SA 4 .   ? 0.757   10.486  73.345  1.00 51.59  ? 325 HOH O O   1 
HETATM 14152 O  O   . HOH SA 4 .   ? 8.832   -6.771  86.069  1.00 64.61  ? 326 HOH O O   1 
HETATM 14153 O  O   . HOH SA 4 .   ? 16.323  -9.131  68.968  1.00 64.01  ? 327 HOH O O   1 
HETATM 14154 O  O   . HOH TA 4 .   ? -26.133 -2.360  64.519  1.00 36.51  ? 301 HOH Q O   1 
HETATM 14155 O  O   . HOH TA 4 .   ? -13.656 7.968   41.725  1.00 34.92  ? 302 HOH Q O   1 
HETATM 14156 O  O   . HOH TA 4 .   ? -16.277 16.116  40.920  1.00 21.73  ? 303 HOH Q O   1 
HETATM 14157 O  O   . HOH TA 4 .   ? -24.991 22.633  46.356  1.00 40.91  ? 304 HOH Q O   1 
HETATM 14158 O  O   . HOH TA 4 .   ? -26.230 9.748   42.050  1.00 32.92  ? 305 HOH Q O   1 
HETATM 14159 O  O   . HOH TA 4 .   ? -5.651  -0.022  61.323  1.00 44.48  ? 306 HOH Q O   1 
HETATM 14160 O  O   . HOH TA 4 .   ? -9.115  9.370   54.014  1.00 26.16  ? 307 HOH Q O   1 
HETATM 14161 O  O   . HOH TA 4 .   ? -16.967 -6.477  44.833  1.00 40.98  ? 308 HOH Q O   1 
HETATM 14162 O  O   . HOH TA 4 .   ? -3.320  8.107   61.771  1.00 58.47  ? 309 HOH Q O   1 
HETATM 14163 O  O   . HOH TA 4 .   ? -35.781 2.030   54.576  1.00 42.41  ? 310 HOH Q O   1 
HETATM 14164 O  O   . HOH TA 4 .   ? -11.615 11.913  45.015  1.00 34.19  ? 311 HOH Q O   1 
HETATM 14165 O  O   . HOH TA 4 .   ? -7.505  -4.701  63.606  1.00 57.51  ? 312 HOH Q O   1 
HETATM 14166 O  O   . HOH TA 4 .   ? -36.430 0.982   48.472  1.00 34.95  ? 313 HOH Q O   1 
HETATM 14167 O  O   . HOH TA 4 .   ? -12.874 18.652  43.292  1.00 45.72  ? 314 HOH Q O   1 
HETATM 14168 O  O   . HOH TA 4 .   ? -7.246  4.727   49.010  1.00 46.88  ? 315 HOH Q O   1 
HETATM 14169 O  O   . HOH TA 4 .   ? -19.242 25.632  44.640  1.00 60.69  ? 316 HOH Q O   1 
HETATM 14170 O  O   . HOH TA 4 .   ? -24.591 14.250  65.288  1.00 41.15  ? 317 HOH Q O   1 
HETATM 14171 O  O   . HOH TA 4 .   ? -33.782 4.154   46.074  1.00 29.22  ? 318 HOH Q O   1 
HETATM 14172 O  O   . HOH TA 4 .   ? -35.145 5.093   56.479  1.00 46.52  ? 319 HOH Q O   1 
HETATM 14173 O  O   . HOH TA 4 .   ? -14.514 14.768  45.233  1.00 46.65  ? 320 HOH Q O   1 
HETATM 14174 O  O   . HOH TA 4 .   ? -23.491 20.616  50.111  1.00 56.91  ? 321 HOH Q O   1 
HETATM 14175 O  O   . HOH TA 4 .   ? -7.146  -1.780  57.161  1.00 38.40  ? 322 HOH Q O   1 
HETATM 14176 O  O   . HOH TA 4 .   ? -21.143 5.746   40.110  1.00 37.21  ? 323 HOH Q O   1 
HETATM 14177 O  O   . HOH TA 4 .   ? -12.540 -1.200  48.671  1.00 34.51  ? 324 HOH Q O   1 
HETATM 14178 O  O   . HOH TA 4 .   ? -17.506 5.985   47.961  1.00 22.14  ? 325 HOH Q O   1 
HETATM 14179 O  O   . HOH TA 4 .   ? -23.468 -2.721  39.138  1.00 35.63  ? 326 HOH Q O   1 
HETATM 14180 O  O   . HOH TA 4 .   ? -7.250  10.371  44.523  1.00 31.22  ? 327 HOH Q O   1 
HETATM 14181 O  O   . HOH TA 4 .   ? -18.125 -0.688  46.261  1.00 31.05  ? 328 HOH Q O   1 
HETATM 14182 O  O   . HOH TA 4 .   ? -18.868 7.936   38.923  1.00 33.39  ? 329 HOH Q O   1 
HETATM 14183 O  O   . HOH TA 4 .   ? -21.911 -10.892 46.272  1.00 42.29  ? 330 HOH Q O   1 
HETATM 14184 O  O   . HOH TA 4 .   ? -9.544  8.916   64.151  1.00 44.54  ? 331 HOH Q O   1 
HETATM 14185 O  O   . HOH TA 4 .   ? -8.203  -11.756 54.201  1.00 59.05  ? 332 HOH Q O   1 
HETATM 14186 O  O   . HOH TA 4 .   ? -35.933 -7.034  48.426  1.00 42.76  ? 333 HOH Q O   1 
HETATM 14187 O  O   . HOH TA 4 .   ? -30.753 2.797   62.758  1.00 43.23  ? 334 HOH Q O   1 
HETATM 14188 O  O   . HOH TA 4 .   ? -33.018 6.673   59.701  1.00 50.04  ? 335 HOH Q O   1 
HETATM 14189 O  O   . HOH TA 4 .   ? -17.184 18.188  42.355  1.00 36.90  ? 336 HOH Q O   1 
HETATM 14190 O  O   . HOH TA 4 .   ? -20.092 -10.143 61.839  1.00 48.62  ? 337 HOH Q O   1 
HETATM 14191 O  O   . HOH TA 4 .   ? -22.507 -11.435 49.878  1.00 44.93  ? 338 HOH Q O   1 
HETATM 14192 O  O   . HOH TA 4 .   ? -18.585 11.860  35.956  1.00 29.50  ? 339 HOH Q O   1 
HETATM 14193 O  O   . HOH TA 4 .   ? -26.985 6.014   68.914  1.00 45.67  ? 340 HOH Q O   1 
HETATM 14194 O  O   . HOH TA 4 .   ? -19.836 13.629  53.946  1.00 29.38  ? 341 HOH Q O   1 
HETATM 14195 O  O   . HOH TA 4 .   ? -29.420 4.229   41.601  1.00 52.23  ? 342 HOH Q O   1 
HETATM 14196 O  O   . HOH TA 4 .   ? -23.651 9.881   50.907  1.00 37.41  ? 343 HOH Q O   1 
HETATM 14197 O  O   . HOH TA 4 .   ? -25.733 20.481  41.646  1.00 22.75  ? 344 HOH Q O   1 
HETATM 14198 O  O   . HOH TA 4 .   ? -10.538 10.600  55.976  1.00 30.01  ? 345 HOH Q O   1 
HETATM 14199 O  O   . HOH TA 4 .   ? -22.142 -14.981 56.228  1.00 60.78  ? 346 HOH Q O   1 
HETATM 14200 O  O   . HOH TA 4 .   ? -15.775 16.253  51.990  1.00 39.52  ? 347 HOH Q O   1 
HETATM 14201 O  O   . HOH TA 4 .   ? -6.474  2.450   61.726  1.00 27.26  ? 348 HOH Q O   1 
HETATM 14202 O  O   . HOH TA 4 .   ? -15.999 14.453  36.033  1.00 25.56  ? 349 HOH Q O   1 
HETATM 14203 O  O   . HOH TA 4 .   ? -23.874 -5.319  46.151  1.00 41.48  ? 350 HOH Q O   1 
HETATM 14204 O  O   . HOH TA 4 .   ? -6.496  -8.486  57.037  1.00 44.33  ? 351 HOH Q O   1 
HETATM 14205 O  O   . HOH TA 4 .   ? -24.115 20.296  44.595  1.00 27.62  ? 352 HOH Q O   1 
HETATM 14206 O  O   . HOH TA 4 .   ? -34.064 1.764   47.375  1.00 29.17  ? 353 HOH Q O   1 
HETATM 14207 O  O   . HOH TA 4 .   ? -13.856 -4.467  46.892  1.00 36.41  ? 354 HOH Q O   1 
HETATM 14208 O  O   . HOH TA 4 .   ? -22.719 12.746  54.600  1.00 45.72  ? 355 HOH Q O   1 
HETATM 14209 O  O   . HOH TA 4 .   ? -7.712  2.236   48.119  1.00 46.98  ? 356 HOH Q O   1 
HETATM 14210 O  O   . HOH TA 4 .   ? -31.640 11.242  54.589  1.00 37.77  ? 357 HOH Q O   1 
HETATM 14211 O  O   . HOH TA 4 .   ? -27.784 2.150   38.890  1.00 39.67  ? 358 HOH Q O   1 
HETATM 14212 O  O   . HOH TA 4 .   ? -13.398 3.735   43.367  1.00 24.63  ? 359 HOH Q O   1 
HETATM 14213 O  O   . HOH TA 4 .   ? -36.520 -1.996  41.234  1.00 34.28  ? 360 HOH Q O   1 
HETATM 14214 O  O   . HOH TA 4 .   ? -35.524 7.380   61.415  1.00 48.11  ? 361 HOH Q O   1 
HETATM 14215 O  O   . HOH TA 4 .   ? -13.381 -11.371 66.974  1.00 49.54  ? 362 HOH Q O   1 
HETATM 14216 O  O   . HOH TA 4 .   ? -27.817 -0.345  65.233  1.00 55.11  ? 363 HOH Q O   1 
HETATM 14217 O  O   . HOH TA 4 .   ? -8.651  0.001   49.629  1.00 43.28  ? 364 HOH Q O   1 
HETATM 14218 O  O   . HOH TA 4 .   ? -13.559 3.644   67.261  1.00 52.86  ? 365 HOH Q O   1 
HETATM 14219 O  O   . HOH TA 4 .   ? -12.582 13.800  41.632  1.00 39.69  ? 366 HOH Q O   1 
HETATM 14220 O  O   . HOH TA 4 .   ? -26.606 19.085  44.588  1.00 26.76  ? 367 HOH Q O   1 
HETATM 14221 O  O   . HOH TA 4 .   ? -24.962 14.855  58.621  1.00 49.42  ? 368 HOH Q O   1 
HETATM 14222 O  O   . HOH TA 4 .   ? -12.008 8.970   35.067  1.00 42.11  ? 369 HOH Q O   1 
HETATM 14223 O  O   . HOH TA 4 .   ? -38.702 -5.293  51.790  1.00 40.07  ? 370 HOH Q O   1 
HETATM 14224 O  O   . HOH TA 4 .   ? -21.719 -18.007 71.108  1.00 61.57  ? 371 HOH Q O   1 
HETATM 14225 O  O   . HOH TA 4 .   ? -32.078 5.131   42.548  1.00 51.58  ? 372 HOH Q O   1 
HETATM 14226 O  O   . HOH TA 4 .   ? -21.003 -13.487 66.360  1.00 45.55  ? 373 HOH Q O   1 
HETATM 14227 O  O   . HOH TA 4 .   ? -31.939 -13.095 49.124  1.00 49.86  ? 374 HOH Q O   1 
HETATM 14228 O  O   . HOH TA 4 .   ? -35.149 12.182  62.566  1.00 60.14  ? 375 HOH Q O   1 
HETATM 14229 O  O   . HOH TA 4 .   ? -36.178 -0.838  37.934  1.00 54.65  ? 376 HOH Q O   1 
HETATM 14230 O  O   . HOH TA 4 .   ? -5.629  3.449   46.971  1.00 52.44  ? 377 HOH Q O   1 
HETATM 14231 O  O   . HOH TA 4 .   ? -5.638  0.253   57.936  1.00 50.40  ? 378 HOH Q O   1 
HETATM 14232 O  O   . HOH TA 4 .   ? -36.061 9.648   62.836  1.00 50.15  ? 379 HOH Q O   1 
HETATM 14233 O  O   . HOH TA 4 .   ? -24.582 -14.873 48.562  1.00 55.36  ? 380 HOH Q O   1 
HETATM 14234 O  O   . HOH TA 4 .   ? -3.559  5.714   60.644  1.00 43.41  ? 381 HOH Q O   1 
HETATM 14235 O  O   . HOH TA 4 .   ? -38.534 0.397   46.743  1.00 56.21  ? 382 HOH Q O   1 
HETATM 14236 O  O   . HOH TA 4 .   ? -7.749  7.826   38.758  1.00 42.60  ? 383 HOH Q O   1 
HETATM 14237 O  O   . HOH TA 4 .   ? -7.587  3.647   40.417  1.00 48.28  ? 384 HOH Q O   1 
HETATM 14238 O  O   . HOH TA 4 .   ? -14.658 16.783  38.902  1.00 23.34  ? 385 HOH Q O   1 
HETATM 14239 O  O   . HOH TA 4 .   ? -6.979  10.611  62.977  1.00 50.47  ? 386 HOH Q O   1 
HETATM 14240 O  O   . HOH TA 4 .   ? -38.800 -1.627  44.991  1.00 48.75  ? 387 HOH Q O   1 
HETATM 14241 O  O   . HOH TA 4 .   ? -19.247 3.320   39.409  1.00 44.92  ? 388 HOH Q O   1 
HETATM 14242 O  O   . HOH TA 4 .   ? -7.440  7.357   53.334  1.00 40.71  ? 389 HOH Q O   1 
HETATM 14243 O  O   . HOH TA 4 .   ? -12.845 14.547  38.953  1.00 31.37  ? 390 HOH Q O   1 
HETATM 14244 O  O   . HOH TA 4 .   ? -13.779 12.920  37.036  1.00 28.98  ? 391 HOH Q O   1 
HETATM 14245 O  O   . HOH TA 4 .   ? -12.679 1.552   68.747  1.00 54.82  ? 392 HOH Q O   1 
HETATM 14246 O  O   . HOH TA 4 .   ? -39.347 0.036   62.467  1.00 49.64  ? 393 HOH Q O   1 
HETATM 14247 O  O   . HOH TA 4 .   ? -8.797  -8.451  69.642  1.00 50.72  ? 394 HOH Q O   1 
HETATM 14248 O  O   . HOH TA 4 .   ? -26.036 0.755   37.071  1.00 48.54  ? 395 HOH Q O   1 
HETATM 14249 O  O   . HOH TA 4 .   ? -9.082  -1.122  45.424  1.00 46.57  ? 396 HOH Q O   1 
HETATM 14250 O  O   . HOH TA 4 .   ? -36.816 3.235   49.824  1.00 38.94  ? 397 HOH Q O   1 
HETATM 14251 O  O   . HOH TA 4 .   ? -2.232  -10.921 64.767  1.00 58.40  ? 398 HOH Q O   1 
HETATM 14252 O  O   . HOH TA 4 .   ? -2.597  16.170  50.961  1.00 51.76  ? 399 HOH Q O   1 
HETATM 14253 O  O   . HOH TA 4 .   ? -13.373 -18.013 67.048  1.00 58.48  ? 400 HOH Q O   1 
HETATM 14254 O  O   . HOH TA 4 .   ? -36.271 5.403   48.346  1.00 48.76  ? 401 HOH Q O   1 
HETATM 14255 O  O   . HOH TA 4 .   ? -31.037 8.420   40.274  1.00 51.02  ? 402 HOH Q O   1 
HETATM 14256 O  O   . HOH TA 4 .   ? -10.628 -15.519 69.361  1.00 53.04  ? 403 HOH Q O   1 
HETATM 14257 O  O   . HOH UA 4 .   ? -22.292 -12.009 83.561  1.00 34.26  ? 301 HOH S O   1 
HETATM 14258 O  O   . HOH UA 4 .   ? -14.247 -12.314 80.028  1.00 43.78  ? 302 HOH S O   1 
HETATM 14259 O  O   . HOH UA 4 .   ? -12.874 -1.997  75.399  1.00 47.00  ? 303 HOH S O   1 
HETATM 14260 O  O   . HOH UA 4 .   ? -23.065 -12.707 69.801  1.00 49.22  ? 304 HOH S O   1 
HETATM 14261 O  O   . HOH UA 4 .   ? -24.381 -4.257  88.710  1.00 45.20  ? 305 HOH S O   1 
HETATM 14262 O  O   . HOH UA 4 .   ? -14.227 -7.048  84.222  1.00 33.93  ? 306 HOH S O   1 
HETATM 14263 O  O   . HOH UA 4 .   ? -9.298  5.739   78.762  1.00 44.32  ? 307 HOH S O   1 
HETATM 14264 O  O   . HOH UA 4 .   ? -24.119 -12.362 64.681  1.00 55.43  ? 308 HOH S O   1 
HETATM 14265 O  O   . HOH UA 4 .   ? -38.911 0.177   72.712  1.00 49.49  ? 309 HOH S O   1 
HETATM 14266 O  O   . HOH UA 4 .   ? -11.778 8.739   77.074  1.00 43.67  ? 310 HOH S O   1 
HETATM 14267 O  O   . HOH UA 4 .   ? -28.082 4.749   88.882  1.00 40.73  ? 311 HOH S O   1 
HETATM 14268 O  O   . HOH UA 4 .   ? -19.001 -8.861  93.587  1.00 37.24  ? 312 HOH S O   1 
HETATM 14269 O  O   . HOH UA 4 .   ? -39.299 -3.069  75.709  1.00 54.77  ? 313 HOH S O   1 
HETATM 14270 O  O   . HOH UA 4 .   ? -13.239 5.962   84.055  1.00 35.56  ? 314 HOH S O   1 
HETATM 14271 O  O   . HOH UA 4 .   ? -22.247 -0.467  94.301  1.00 45.53  ? 315 HOH S O   1 
HETATM 14272 O  O   . HOH UA 4 .   ? -15.100 -7.939  73.135  1.00 43.94  ? 316 HOH S O   1 
HETATM 14273 O  O   . HOH UA 4 .   ? -21.079 4.082   88.822  1.00 42.83  ? 317 HOH S O   1 
HETATM 14274 O  O   . HOH UA 4 .   ? -41.945 -2.378  80.470  1.00 50.25  ? 318 HOH S O   1 
HETATM 14275 O  O   . HOH UA 4 .   ? -12.066 -7.446  93.219  1.00 48.89  ? 319 HOH S O   1 
HETATM 14276 O  O   . HOH UA 4 .   ? -42.153 -5.177  86.962  1.00 50.67  ? 320 HOH S O   1 
HETATM 14277 O  O   . HOH UA 4 .   ? -5.599  11.286  80.592  1.00 43.10  ? 321 HOH S O   1 
HETATM 14278 O  O   . HOH UA 4 .   ? -27.544 3.518   69.745  1.00 31.31  ? 322 HOH S O   1 
HETATM 14279 O  O   . HOH UA 4 .   ? -27.664 -13.722 75.698  1.00 59.40  ? 323 HOH S O   1 
HETATM 14280 O  O   . HOH UA 4 .   ? -15.176 -13.509 82.218  1.00 50.92  ? 324 HOH S O   1 
HETATM 14281 O  O   . HOH UA 4 .   ? -37.944 -4.343  89.581  1.00 51.04  ? 325 HOH S O   1 
HETATM 14282 O  O   . HOH UA 4 .   ? -27.922 -3.293  70.517  1.00 56.71  ? 326 HOH S O   1 
HETATM 14283 O  O   . HOH UA 4 .   ? -16.968 12.598  71.334  1.00 46.15  ? 327 HOH S O   1 
HETATM 14284 O  O   . HOH UA 4 .   ? -24.497 -13.656 96.035  1.00 53.64  ? 328 HOH S O   1 
HETATM 14285 O  O   . HOH UA 4 .   ? -14.707 -0.587  73.048  1.00 40.63  ? 329 HOH S O   1 
HETATM 14286 O  O   . HOH UA 4 .   ? -28.238 0.630   68.525  1.00 42.22  ? 330 HOH S O   1 
HETATM 14287 O  O   . HOH UA 4 .   ? -8.272  3.660   72.838  1.00 52.84  ? 331 HOH S O   1 
HETATM 14288 O  O   . HOH UA 4 .   ? -32.014 -13.119 85.279  1.00 50.71  ? 332 HOH S O   1 
HETATM 14289 O  O   . HOH UA 4 .   ? -45.424 1.575   87.221  1.00 51.81  ? 333 HOH S O   1 
HETATM 14290 O  O   . HOH UA 4 .   ? -23.298 6.847   90.285  1.00 40.65  ? 334 HOH S O   1 
HETATM 14291 O  O   . HOH UA 4 .   ? -33.851 -11.349 77.099  1.00 54.07  ? 335 HOH S O   1 
HETATM 14292 O  O   . HOH UA 4 .   ? -28.552 -14.312 70.106  1.00 48.87  ? 336 HOH S O   1 
HETATM 14293 O  O   . HOH UA 4 .   ? -14.947 -14.837 85.638  1.00 47.84  ? 337 HOH S O   1 
HETATM 14294 O  O   . HOH UA 4 .   ? -40.497 -4.079  88.806  1.00 53.32  ? 338 HOH S O   1 
HETATM 14295 O  O   . HOH UA 4 .   ? -12.633 4.140   71.938  1.00 56.73  ? 339 HOH S O   1 
HETATM 14296 O  O   . HOH UA 4 .   ? -15.783 -6.209  96.482  1.00 47.15  ? 340 HOH S O   1 
HETATM 14297 O  O   . HOH UA 4 .   ? -34.099 -5.502  72.225  1.00 51.01  ? 341 HOH S O   1 
HETATM 14298 O  O   . HOH UA 4 .   ? -30.086 -13.015 76.607  1.00 51.78  ? 342 HOH S O   1 
HETATM 14299 O  O   . HOH UA 4 .   ? -26.056 -23.020 90.259  1.00 52.86  ? 343 HOH S O   1 
HETATM 14300 O  O   . HOH UA 4 .   ? -24.438 -12.036 81.677  1.00 48.77  ? 344 HOH S O   1 
HETATM 14301 O  O   . HOH UA 4 .   ? -40.485 -7.196  75.569  1.00 52.78  ? 345 HOH S O   1 
HETATM 14302 O  O   . HOH UA 4 .   ? -33.992 -13.335 69.513  1.00 52.13  ? 346 HOH S O   1 
HETATM 14303 O  O   . HOH UA 4 .   ? -34.921 -2.852  68.812  1.00 52.43  ? 347 HOH S O   1 
HETATM 14304 O  O   . HOH UA 4 .   ? -41.911 -7.754  85.780  1.00 54.42  ? 348 HOH S O   1 
HETATM 14305 O  O   . HOH UA 4 .   ? -25.254 -14.005 68.871  1.00 63.07  ? 349 HOH S O   1 
HETATM 14306 O  O   . HOH UA 4 .   ? -26.478 0.201   92.420  1.00 51.32  ? 350 HOH S O   1 
HETATM 14307 O  O   . HOH UA 4 .   ? -33.714 -14.013 80.632  1.00 60.87  ? 351 HOH S O   1 
HETATM 14308 O  O   . HOH UA 4 .   ? -6.892  6.091   74.029  1.00 58.29  ? 352 HOH S O   1 
HETATM 14309 O  O   . HOH UA 4 .   ? -33.591 -14.231 83.398  1.00 54.32  ? 353 HOH S O   1 
HETATM 14310 O  O   . HOH UA 4 .   ? -22.665 -14.869 74.649  1.00 50.32  ? 354 HOH S O   1 
HETATM 14311 O  O   . HOH UA 4 .   ? -13.465 -9.694  71.709  1.00 63.31  ? 355 HOH S O   1 
HETATM 14312 O  O   . HOH UA 4 .   ? -30.863 -15.807 70.467  1.00 58.49  ? 356 HOH S O   1 
HETATM 14313 O  O   . HOH UA 4 .   ? -20.666 -15.510 76.371  1.00 55.56  ? 357 HOH S O   1 
HETATM 14314 O  O   . HOH UA 4 .   ? -12.489 -13.217 75.233  1.00 53.09  ? 358 HOH S O   1 
HETATM 14315 O  O   . HOH UA 4 .   ? -20.663 -22.763 82.931  1.00 62.27  ? 359 HOH S O   1 
HETATM 14316 O  O   . HOH UA 4 .   ? -32.511 -10.989 59.935  1.00 57.86  ? 360 HOH S O   1 
HETATM 14317 O  O   . HOH UA 4 .   ? -19.617 -24.655 92.763  1.00 54.78  ? 361 HOH S O   1 
HETATM 14318 O  O   . HOH UA 4 .   ? -45.262 -4.301  82.142  1.00 59.76  ? 362 HOH S O   1 
HETATM 14319 O  O   . HOH UA 4 .   ? -24.765 -17.181 74.937  1.00 47.73  ? 363 HOH S O   1 
HETATM 14320 O  O   . HOH UA 4 .   ? -45.844 -8.074  77.136  1.00 62.08  ? 364 HOH S O   1 
HETATM 14321 O  O   . HOH VA 4 .   ? 1.759   -27.897 21.694  1.00 38.64  ? 301 HOH U O   1 
HETATM 14322 O  O   . HOH VA 4 .   ? -13.987 -22.102 14.385  1.00 45.64  ? 302 HOH U O   1 
HETATM 14323 O  O   . HOH VA 4 .   ? -2.957  -31.217 1.146   1.00 56.76  ? 303 HOH U O   1 
HETATM 14324 O  O   . HOH VA 4 .   ? -11.846 -8.298  3.473   1.00 40.67  ? 304 HOH U O   1 
HETATM 14325 O  O   . HOH VA 4 .   ? -26.239 -45.036 4.881   1.00 58.18  ? 305 HOH U O   1 
HETATM 14326 O  O   . HOH VA 4 .   ? -17.751 -14.393 7.071   1.00 51.02  ? 306 HOH U O   1 
HETATM 14327 O  O   . HOH VA 4 .   ? 6.084   -24.893 4.754   1.00 40.53  ? 307 HOH U O   1 
HETATM 14328 O  O   . HOH VA 4 .   ? -24.464 -35.113 4.556   1.00 59.12  ? 308 HOH U O   1 
HETATM 14329 O  O   . HOH VA 4 .   ? 0.734   -29.921 23.154  1.00 50.17  ? 309 HOH U O   1 
HETATM 14330 O  O   . HOH VA 4 .   ? -11.286 -29.665 20.473  1.00 41.36  ? 310 HOH U O   1 
HETATM 14331 O  O   . HOH VA 4 .   ? 7.783   -37.172 4.375   1.00 62.12  ? 311 HOH U O   1 
HETATM 14332 O  O   . HOH VA 4 .   ? -11.378 -39.011 5.183   1.00 47.46  ? 312 HOH U O   1 
HETATM 14333 O  O   . HOH VA 4 .   ? -16.096 -19.312 5.472   1.00 47.49  ? 313 HOH U O   1 
HETATM 14334 O  O   . HOH VA 4 .   ? 4.077   -21.505 21.043  1.00 54.58  ? 314 HOH U O   1 
HETATM 14335 O  O   . HOH VA 4 .   ? -15.199 -38.882 13.227  1.00 61.38  ? 315 HOH U O   1 
HETATM 14336 O  O   . HOH VA 4 .   ? -21.467 -43.916 6.434   1.00 49.26  ? 316 HOH U O   1 
HETATM 14337 O  O   . HOH VA 4 .   ? -5.311  -41.829 22.206  1.00 55.66  ? 317 HOH U O   1 
HETATM 14338 O  O   . HOH VA 4 .   ? -17.006 -32.665 16.593  1.00 49.01  ? 318 HOH U O   1 
HETATM 14339 O  O   . HOH VA 4 .   ? -20.835 -27.247 11.424  1.00 53.77  ? 319 HOH U O   1 
HETATM 14340 O  O   . HOH VA 4 .   ? -16.009 -19.497 1.016   1.00 58.23  ? 320 HOH U O   1 
HETATM 14341 O  O   . HOH VA 4 .   ? -12.911 -40.097 14.058  1.00 53.81  ? 321 HOH U O   1 
HETATM 14342 O  O   . HOH VA 4 .   ? -26.822 -43.554 7.188   1.00 59.04  ? 322 HOH U O   1 
HETATM 14343 O  O   . HOH VA 4 .   ? -3.454  -36.410 -12.017 1.00 61.93  ? 323 HOH U O   1 
HETATM 14344 O  O   . HOH VA 4 .   ? -18.628 -17.471 4.431   1.00 58.84  ? 324 HOH U O   1 
HETATM 14345 O  O   . HOH VA 4 .   ? -16.705 -37.199 15.213  1.00 57.01  ? 325 HOH U O   1 
HETATM 14346 O  O   . HOH VA 4 .   ? 5.568   -24.780 23.590  1.00 61.08  ? 326 HOH U O   1 
HETATM 14347 O  O   . HOH VA 4 .   ? -9.717  -17.390 -3.384  1.00 61.65  ? 327 HOH U O   1 
HETATM 14348 O  O   . HOH VA 4 .   ? -14.809 -33.204 21.113  1.00 42.92  ? 328 HOH U O   1 
HETATM 14349 O  O   . HOH VA 4 .   ? -7.804  -39.864 26.535  1.00 60.05  ? 329 HOH U O   1 
HETATM 14350 O  O   . HOH VA 4 .   ? -22.447 -40.449 9.656   1.00 62.94  ? 330 HOH U O   1 
HETATM 14351 O  O   . HOH VA 4 .   ? -22.364 -32.049 11.589  1.00 64.32  ? 331 HOH U O   1 
HETATM 14352 O  O   . HOH VA 4 .   ? -2.956  -38.500 4.431   1.00 47.71  ? 332 HOH U O   1 
HETATM 14353 O  O   . HOH VA 4 .   ? -1.639  -44.761 19.379  1.00 60.88  ? 333 HOH U O   1 
HETATM 14354 O  O   . HOH VA 4 .   ? -17.355 -47.386 -0.690  1.00 47.04  ? 334 HOH U O   1 
HETATM 14355 O  O   . HOH VA 4 .   ? -31.476 -35.105 -1.380  1.00 49.71  ? 335 HOH U O   1 
HETATM 14356 O  O   . HOH VA 4 .   ? -8.213  -43.233 30.773  1.00 51.41  ? 336 HOH U O   1 
HETATM 14357 O  O   . HOH WA 4 .   ? -29.341 -5.788  19.746  1.00 36.01  ? 301 HOH W O   1 
HETATM 14358 O  O   . HOH WA 4 .   ? -12.671 -0.133  37.140  1.00 33.27  ? 302 HOH W O   1 
HETATM 14359 O  O   . HOH WA 4 .   ? -25.771 -11.369 13.816  1.00 49.33  ? 303 HOH W O   1 
HETATM 14360 O  O   . HOH WA 4 .   ? -4.376  -9.749  34.012  1.00 30.14  ? 304 HOH W O   1 
HETATM 14361 O  O   . HOH WA 4 .   ? -20.303 6.065   26.099  1.00 29.15  ? 305 HOH W O   1 
HETATM 14362 O  O   . HOH WA 4 .   ? -3.384  -17.112 21.946  1.00 51.83  ? 306 HOH W O   1 
HETATM 14363 O  O   . HOH WA 4 .   ? -26.774 -10.890 17.511  1.00 34.06  ? 307 HOH W O   1 
HETATM 14364 O  O   . HOH WA 4 .   ? -2.453  -17.375 37.532  1.00 47.27  ? 308 HOH W O   1 
HETATM 14365 O  O   . HOH WA 4 .   ? -16.916 -4.196  43.394  1.00 25.66  ? 309 HOH W O   1 
HETATM 14366 O  O   . HOH WA 4 .   ? 3.666   -14.192 31.515  1.00 46.47  ? 310 HOH W O   1 
HETATM 14367 O  O   . HOH WA 4 .   ? -7.624  -17.701 31.182  1.00 43.31  ? 311 HOH W O   1 
HETATM 14368 O  O   . HOH WA 4 .   ? -5.631  -11.067 6.156   1.00 34.10  ? 312 HOH W O   1 
HETATM 14369 O  O   . HOH WA 4 .   ? -16.853 -26.567 24.777  1.00 47.16  ? 313 HOH W O   1 
HETATM 14370 O  O   . HOH WA 4 .   ? -19.525 2.020   41.626  1.00 37.60  ? 314 HOH W O   1 
HETATM 14371 O  O   . HOH WA 4 .   ? -18.501 1.138   36.564  1.00 37.18  ? 315 HOH W O   1 
HETATM 14372 O  O   . HOH WA 4 .   ? -10.155 -3.772  39.269  1.00 34.01  ? 316 HOH W O   1 
HETATM 14373 O  O   . HOH WA 4 .   ? -0.082  -10.129 11.025  1.00 33.70  ? 317 HOH W O   1 
HETATM 14374 O  O   . HOH WA 4 .   ? 1.887   -11.576 25.493  1.00 38.07  ? 318 HOH W O   1 
HETATM 14375 O  O   . HOH WA 4 .   ? -30.352 -0.538  17.129  1.00 55.25  ? 319 HOH W O   1 
HETATM 14376 O  O   . HOH WA 4 .   ? -19.644 0.823   33.861  1.00 41.42  ? 320 HOH W O   1 
HETATM 14377 O  O   . HOH WA 4 .   ? -16.528 -18.664 20.080  1.00 45.69  ? 321 HOH W O   1 
HETATM 14378 O  O   . HOH WA 4 .   ? 6.079   -8.693  23.203  1.00 48.05  ? 322 HOH W O   1 
HETATM 14379 O  O   . HOH WA 4 .   ? -20.838 -16.421 18.073  1.00 46.54  ? 323 HOH W O   1 
HETATM 14380 O  O   . HOH WA 4 .   ? 0.913   -5.043  24.353  1.00 40.22  ? 324 HOH W O   1 
HETATM 14381 O  O   . HOH WA 4 .   ? -16.260 6.035   37.774  1.00 53.75  ? 325 HOH W O   1 
HETATM 14382 O  O   . HOH WA 4 .   ? -14.858 -14.148 34.229  1.00 41.18  ? 326 HOH W O   1 
HETATM 14383 O  O   . HOH WA 4 .   ? -17.637 -22.378 27.977  1.00 58.78  ? 327 HOH W O   1 
HETATM 14384 O  O   . HOH WA 4 .   ? -12.128 -13.027 38.526  1.00 39.28  ? 328 HOH W O   1 
HETATM 14385 O  O   . HOH WA 4 .   ? -25.587 2.798   28.337  1.00 35.67  ? 329 HOH W O   1 
HETATM 14386 O  O   B HOH WA 4 .   ? -11.594 5.755   34.510  0.50 29.67  ? 330 HOH W O   1 
HETATM 14387 O  O   . HOH WA 4 .   ? -15.387 -16.668 14.241  1.00 33.89  ? 331 HOH W O   1 
HETATM 14388 O  O   . HOH WA 4 .   ? -5.255  -12.205 33.611  1.00 28.48  ? 332 HOH W O   1 
HETATM 14389 O  O   . HOH WA 4 .   ? -24.358 -3.561  34.471  1.00 47.05  ? 333 HOH W O   1 
HETATM 14390 O  O   . HOH WA 4 .   ? 3.946   -6.646  16.823  1.00 47.78  ? 334 HOH W O   1 
HETATM 14391 O  O   . HOH WA 4 .   ? 0.400   -7.615  29.204  1.00 44.38  ? 335 HOH W O   1 
HETATM 14392 O  O   . HOH WA 4 .   ? -27.797 -4.829  21.741  1.00 42.16  ? 336 HOH W O   1 
HETATM 14393 O  O   . HOH WA 4 .   ? -20.392 -27.358 22.229  1.00 51.19  ? 337 HOH W O   1 
HETATM 14394 O  O   . HOH WA 4 .   ? -12.408 -1.923  39.504  1.00 32.50  ? 338 HOH W O   1 
HETATM 14395 O  O   . HOH WA 4 .   ? -13.372 0.191   26.310  1.00 29.01  ? 339 HOH W O   1 
HETATM 14396 O  O   . HOH WA 4 .   ? -13.733 -4.852  31.375  1.00 25.63  ? 340 HOH W O   1 
HETATM 14397 O  O   . HOH WA 4 .   ? -4.342  -0.889  28.313  1.00 42.77  ? 341 HOH W O   1 
HETATM 14398 O  O   . HOH WA 4 .   ? -8.379  4.554   20.126  1.00 44.21  ? 342 HOH W O   1 
HETATM 14399 O  O   . HOH WA 4 .   ? -6.340  -1.968  39.796  1.00 31.40  ? 343 HOH W O   1 
HETATM 14400 O  O   . HOH WA 4 .   ? -26.391 8.644   18.918  1.00 46.39  ? 344 HOH W O   1 
HETATM 14401 O  O   . HOH WA 4 .   ? -30.356 -3.480  25.704  1.00 42.74  ? 345 HOH W O   1 
HETATM 14402 O  O   . HOH WA 4 .   ? -19.835 -10.412 31.603  1.00 49.38  ? 346 HOH W O   1 
HETATM 14403 O  O   . HOH WA 4 .   ? -0.241  -0.621  17.034  1.00 39.41  ? 347 HOH W O   1 
HETATM 14404 O  O   . HOH WA 4 .   ? -11.196 0.995   32.759  1.00 25.62  ? 348 HOH W O   1 
HETATM 14405 O  O   . HOH WA 4 .   ? -17.734 1.131   44.120  1.00 32.36  ? 349 HOH W O   1 
HETATM 14406 O  O   . HOH WA 4 .   ? -26.341 -1.068  30.736  1.00 40.46  ? 350 HOH W O   1 
HETATM 14407 O  O   . HOH WA 4 .   ? -3.304  -5.263  33.840  1.00 44.04  ? 351 HOH W O   1 
HETATM 14408 O  O   . HOH WA 4 .   ? -8.864  2.510   24.543  1.00 38.52  ? 352 HOH W O   1 
HETATM 14409 O  O   . HOH WA 4 .   ? -24.650 -18.093 17.466  1.00 58.19  ? 353 HOH W O   1 
HETATM 14410 O  O   . HOH WA 4 .   ? -11.158 -16.384 35.706  1.00 47.93  ? 354 HOH W O   1 
HETATM 14411 O  O   . HOH WA 4 .   ? -31.181 -17.336 20.073  1.00 61.71  ? 355 HOH W O   1 
HETATM 14412 O  O   . HOH WA 4 .   ? -13.316 5.339   41.148  1.00 38.14  ? 356 HOH W O   1 
HETATM 14413 O  O   . HOH WA 4 .   ? -12.713 -2.412  42.099  1.00 39.93  ? 357 HOH W O   1 
HETATM 14414 O  O   . HOH WA 4 .   ? -17.674 7.631   14.532  1.00 45.23  ? 358 HOH W O   1 
HETATM 14415 O  O   . HOH WA 4 .   ? -9.180  -15.509 39.711  1.00 53.79  ? 359 HOH W O   1 
HETATM 14416 O  O   . HOH WA 4 .   ? 0.508   -5.157  36.159  1.00 59.67  ? 360 HOH W O   1 
HETATM 14417 O  O   . HOH WA 4 .   ? -25.275 -19.986 19.339  1.00 58.93  ? 361 HOH W O   1 
HETATM 14418 O  O   . HOH WA 4 .   ? -14.714 -9.517  46.420  1.00 51.24  ? 362 HOH W O   1 
HETATM 14419 O  O   . HOH WA 4 .   ? 2.750   -6.561  25.926  1.00 58.53  ? 363 HOH W O   1 
HETATM 14420 O  O   . HOH WA 4 .   ? -4.992  -18.894 30.654  1.00 75.45  ? 364 HOH W O   1 
HETATM 14421 O  O   . HOH WA 4 .   ? -21.301 -13.469 47.985  1.00 56.19  ? 365 HOH W O   1 
HETATM 14422 O  O   B HOH WA 4 .   ? -7.464  4.538   35.885  0.75 42.28  ? 366 HOH W O   1 
HETATM 14423 O  O   . HOH WA 4 .   ? -33.782 -13.576 15.563  1.00 64.52  ? 367 HOH W O   1 
HETATM 14424 O  O   . HOH WA 4 .   ? -20.677 1.531   37.936  1.00 40.88  ? 368 HOH W O   1 
HETATM 14425 O  O   . HOH WA 4 .   ? -13.918 -0.753  43.898  1.00 35.56  ? 369 HOH W O   1 
HETATM 14426 O  O   . HOH WA 4 .   ? -22.013 -4.791  6.668   1.00 51.89  ? 370 HOH W O   1 
HETATM 14427 O  O   . HOH WA 4 .   ? -2.699  -7.848  33.310  1.00 36.05  ? 371 HOH W O   1 
HETATM 14428 O  O   . HOH WA 4 .   ? -32.629 -9.513  19.071  1.00 47.78  ? 372 HOH W O   1 
HETATM 14429 O  O   . HOH WA 4 .   ? -15.980 -1.869  45.347  1.00 34.53  ? 373 HOH W O   1 
HETATM 14430 O  O   . HOH WA 4 .   ? -12.114 -22.513 33.853  1.00 53.62  ? 374 HOH W O   1 
HETATM 14431 O  O   . HOH WA 4 .   ? -15.214 1.497   43.044  1.00 31.97  ? 375 HOH W O   1 
HETATM 14432 O  O   . HOH WA 4 .   ? -22.945 -0.349  37.473  1.00 45.18  ? 376 HOH W O   1 
HETATM 14433 O  O   . HOH WA 4 .   ? -33.224 -4.219  20.526  1.00 54.57  ? 377 HOH W O   1 
HETATM 14434 O  O   . HOH WA 4 .   ? -34.053 -1.664  21.569  1.00 57.82  ? 378 HOH W O   1 
HETATM 14435 O  O   . HOH WA 4 .   ? -34.898 -0.891  16.994  1.00 60.10  ? 379 HOH W 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   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA F . n 
B 1 2   THR 2   2   2   THR THR F . n 
B 1 3   LYS 3   3   3   LYS LYS F . n 
B 1 4   ALA 4   4   4   ALA ALA F . n 
B 1 5   VAL 5   5   5   VAL VAL F . n 
B 1 6   CYS 6   6   6   CYS CYS F . n 
B 1 7   VAL 7   7   7   VAL VAL F . n 
B 1 8   LEU 8   8   8   LEU LEU F . n 
B 1 9   LYS 9   9   9   LYS LYS F . n 
B 1 10  GLY 10  10  10  GLY GLY F . n 
B 1 11  ASP 11  11  11  ASP ASP F . n 
B 1 12  GLY 12  12  12  GLY GLY F . n 
B 1 13  PRO 13  13  13  PRO PRO F . n 
B 1 14  VAL 14  14  14  VAL VAL F . n 
B 1 15  GLN 15  15  15  GLN GLN F . n 
B 1 16  GLY 16  16  16  GLY GLY F . n 
B 1 17  ILE 17  17  17  ILE ILE F . n 
B 1 18  ILE 18  18  18  ILE ILE F . n 
B 1 19  ASN 19  19  19  ASN ASN F . n 
B 1 20  PHE 20  20  20  PHE PHE F . n 
B 1 21  GLU 21  21  21  GLU GLU F . n 
B 1 22  GLN 22  22  22  GLN GLN F . n 
B 1 23  LYS 23  23  23  LYS LYS F . n 
B 1 24  GLU 24  24  24  GLU GLU F . n 
B 1 25  SER 25  25  25  SER SER F . n 
B 1 26  ASN 26  26  26  ASN ASN F . n 
B 1 27  GLY 27  27  27  GLY GLY F . n 
B 1 28  PRO 28  28  28  PRO PRO F . n 
B 1 29  VAL 29  29  29  VAL VAL F . n 
B 1 30  LYS 30  30  30  LYS LYS F . n 
B 1 31  VAL 31  31  31  VAL VAL F . n 
B 1 32  TRP 32  32  32  TRP TRP F . n 
B 1 33  GLY 33  33  33  GLY GLY F . n 
B 1 34  SER 34  34  34  SER SER F . n 
B 1 35  ILE 35  35  35  ILE ILE F . n 
B 1 36  LYS 36  36  36  LYS LYS F . n 
B 1 37  GLY 37  37  37  GLY GLY F . n 
B 1 38  LEU 38  38  38  LEU LEU F . n 
B 1 39  THR 39  39  39  THR THR F . n 
B 1 40  GLU 40  40  40  GLU GLU F . n 
B 1 41  GLY 41  41  41  GLY GLY F . n 
B 1 42  LEU 42  42  42  LEU LEU F . n 
B 1 43  HIS 43  43  43  HIS HIS F . n 
B 1 44  GLY 44  44  44  GLY GLY F . n 
B 1 45  PHE 45  45  45  PHE PHE F . n 
B 1 46  HIS 46  46  46  HIS HIS F . n 
B 1 47  VAL 47  47  47  VAL VAL F . n 
B 1 48  HIS 48  48  48  HIS HIS F . n 
B 1 49  GLU 49  49  49  GLU GLU F . n 
B 1 50  PHE 50  50  50  PHE PHE F . n 
B 1 51  GLY 51  51  51  GLY GLY F . n 
B 1 52  ASP 52  52  52  ASP ASP F . n 
B 1 53  ASN 53  53  53  ASN ASN F . n 
B 1 54  THR 54  54  54  THR THR F . n 
B 1 55  ALA 55  55  55  ALA ALA F . n 
B 1 56  GLY 56  56  56  GLY GLY F . n 
B 1 57  ALA 57  57  57  ALA ALA F . n 
B 1 58  THR 58  58  58  THR THR F . n 
B 1 59  SER 59  59  59  SER SER F . n 
B 1 60  ALA 60  60  60  ALA ALA F . n 
B 1 61  GLY 61  61  61  GLY GLY F . n 
B 1 62  PRO 62  62  62  PRO PRO F . n 
B 1 63  HIS 63  63  63  HIS HIS F . n 
B 1 64  PHE 64  64  64  PHE PHE F . n 
B 1 65  ASN 65  65  65  ASN ASN F . n 
B 1 66  PRO 66  66  66  PRO PRO F . n 
B 1 67  LEU 67  67  67  LEU LEU F . n 
B 1 68  SER 68  68  68  SER SER F . n 
B 1 69  ARG 69  69  69  ARG ARG F . n 
B 1 70  LYS 70  70  70  LYS LYS F . n 
B 1 71  HIS 71  71  71  HIS HIS F . n 
B 1 72  GLY 72  72  72  GLY GLY F . n 
B 1 73  GLY 73  73  73  GLY GLY F . n 
B 1 74  PRO 74  74  74  PRO PRO F . n 
B 1 75  LYS 75  75  75  LYS LYS F . n 
B 1 76  ASP 76  76  76  ASP ASP F . n 
B 1 77  GLU 77  77  77  GLU GLU F . n 
B 1 78  GLU 78  78  78  GLU GLU F . n 
B 1 79  ARG 79  79  79  ARG ARG F . n 
B 1 80  HIS 80  80  80  HIS HIS F . n 
B 1 81  VAL 81  81  81  VAL VAL F . n 
B 1 82  GLY 82  82  82  GLY GLY F . n 
B 1 83  ASP 83  83  83  ASP ASP F . n 
B 1 84  LEU 84  84  84  LEU LEU F . n 
B 1 85  GLY 85  85  85  GLY GLY F . n 
B 1 86  ASN 86  86  86  ASN ASN F . n 
B 1 87  VAL 87  87  87  VAL VAL F . n 
B 1 88  THR 88  88  88  THR THR F . n 
B 1 89  ALA 89  89  89  ALA ALA F . n 
B 1 90  ASP 90  90  90  ASP ASP F . n 
B 1 91  LYS 91  91  91  LYS LYS F . n 
B 1 92  ASP 92  92  92  ASP ASP F . n 
B 1 93  GLY 93  93  93  GLY GLY F . n 
B 1 94  VAL 94  94  94  VAL VAL F . n 
B 1 95  ALA 95  95  95  ALA ALA F . n 
B 1 96  ASP 96  96  96  ASP ASP F . n 
B 1 97  VAL 97  97  97  VAL VAL F . n 
B 1 98  SER 98  98  98  SER SER F . n 
B 1 99  ILE 99  99  99  ILE ILE F . n 
B 1 100 GLU 100 100 100 GLU GLU F . n 
B 1 101 ASP 101 101 101 ASP ASP F . n 
B 1 102 SER 102 102 102 SER SER F . n 
B 1 103 VAL 103 103 103 VAL VAL F . n 
B 1 104 ILE 104 104 104 ILE ILE F . n 
B 1 105 SER 105 105 105 SER SER F . n 
B 1 106 LEU 106 106 106 LEU LEU F . n 
B 1 107 SER 107 107 107 SER SER F . n 
B 1 108 GLY 108 108 108 GLY GLY F . n 
B 1 109 ASP 109 109 109 ASP ASP F . n 
B 1 110 HIS 110 110 110 HIS HIS F . n 
B 1 111 CYS 111 111 111 CYS CYS F . n 
B 1 112 ILE 112 112 112 ILE ILE F . n 
B 1 113 ILE 113 113 113 ILE ILE F . n 
B 1 114 GLY 114 114 114 GLY GLY F . n 
B 1 115 ARG 115 115 115 ARG ARG F . n 
B 1 116 THR 116 116 116 THR THR F . n 
B 1 117 LEU 117 117 117 LEU LEU F . n 
B 1 118 VAL 118 118 118 VAL VAL F . n 
B 1 119 VAL 119 119 119 VAL VAL F . n 
B 1 120 HIS 120 120 120 HIS HIS F . n 
B 1 121 GLU 121 121 121 GLU GLU F . n 
B 1 122 LYS 122 122 122 LYS LYS F . n 
B 1 123 ALA 123 123 123 ALA ALA F . n 
B 1 124 ASP 124 124 124 ASP ASP F . n 
B 1 125 ASP 125 125 125 ASP ASP F . n 
B 1 126 LEU 126 126 126 LEU LEU F . n 
B 1 127 GLY 127 127 127 GLY GLY F . n 
B 1 128 LYS 128 128 128 LYS LYS F . n 
B 1 129 GLY 129 129 129 GLY GLY F . n 
B 1 130 GLY 130 130 130 GLY GLY F . n 
B 1 131 ASN 131 131 131 ASN ASN F . n 
B 1 132 GLU 132 132 132 GLU GLU F . n 
B 1 133 GLU 133 133 133 GLU GLU F . n 
B 1 134 SER 134 134 134 SER SER F . n 
B 1 135 THR 135 135 135 THR THR F . n 
B 1 136 LYS 136 136 136 LYS LYS F . n 
B 1 137 THR 137 137 137 THR THR F . n 
B 1 138 GLY 138 138 138 GLY GLY F . n 
B 1 139 ASN 139 139 139 ASN ASN F . n 
B 1 140 ALA 140 140 140 ALA ALA F . n 
B 1 141 GLY 141 141 141 GLY GLY F . n 
B 1 142 SER 142 142 142 SER SER F . n 
B 1 143 ARG 143 143 143 ARG ARG F . n 
B 1 144 LEU 144 144 144 LEU LEU F . n 
B 1 145 ALA 145 145 145 ALA ALA F . n 
B 1 146 ALA 146 146 146 ALA ALA F . n 
B 1 147 GLY 147 147 147 GLY GLY F . n 
B 1 148 VAL 148 148 148 VAL VAL F . n 
B 1 149 ILE 149 149 149 ILE ILE F . n 
B 1 150 GLY 150 150 150 GLY GLY F . n 
B 1 151 ILE 151 151 151 ILE ILE F . n 
B 1 152 ALA 152 152 152 ALA ALA F . n 
B 1 153 GLN 153 153 153 GLN GLN F . n 
C 1 1   ALA 1   1   1   ALA ALA D . n 
C 1 2   THR 2   2   2   THR THR D . n 
C 1 3   LYS 3   3   3   LYS LYS D . n 
C 1 4   ALA 4   4   4   ALA ALA D . n 
C 1 5   VAL 5   5   5   VAL VAL D . n 
C 1 6   CYS 6   6   6   CYS CYS D . n 
C 1 7   VAL 7   7   7   VAL VAL D . n 
C 1 8   LEU 8   8   8   LEU LEU D . n 
C 1 9   LYS 9   9   9   LYS LYS D . n 
C 1 10  GLY 10  10  10  GLY GLY D . n 
C 1 11  ASP 11  11  11  ASP ASP D . n 
C 1 12  GLY 12  12  12  GLY GLY D . n 
C 1 13  PRO 13  13  13  PRO PRO D . n 
C 1 14  VAL 14  14  14  VAL VAL D . n 
C 1 15  GLN 15  15  15  GLN GLN D . n 
C 1 16  GLY 16  16  16  GLY GLY D . n 
C 1 17  ILE 17  17  17  ILE ILE D . n 
C 1 18  ILE 18  18  18  ILE ILE D . n 
C 1 19  ASN 19  19  19  ASN ASN D . n 
C 1 20  PHE 20  20  20  PHE PHE D . n 
C 1 21  GLU 21  21  21  GLU GLU D . n 
C 1 22  GLN 22  22  22  GLN GLN D . n 
C 1 23  LYS 23  23  23  LYS LYS D . n 
C 1 24  GLU 24  24  24  GLU GLU D . n 
C 1 25  SER 25  25  25  SER SER D . n 
C 1 26  ASN 26  26  26  ASN ASN D . n 
C 1 27  GLY 27  27  27  GLY GLY D . n 
C 1 28  PRO 28  28  28  PRO PRO D . n 
C 1 29  VAL 29  29  29  VAL VAL D . n 
C 1 30  LYS 30  30  30  LYS LYS D . n 
C 1 31  VAL 31  31  31  VAL VAL D . n 
C 1 32  TRP 32  32  32  TRP TRP D . n 
C 1 33  GLY 33  33  33  GLY GLY D . n 
C 1 34  SER 34  34  34  SER SER D . n 
C 1 35  ILE 35  35  35  ILE ILE D . n 
C 1 36  LYS 36  36  36  LYS LYS D . n 
C 1 37  GLY 37  37  37  GLY GLY D . n 
C 1 38  LEU 38  38  38  LEU LEU D . n 
C 1 39  THR 39  39  39  THR THR D . n 
C 1 40  GLU 40  40  40  GLU GLU D . n 
C 1 41  GLY 41  41  41  GLY GLY D . n 
C 1 42  LEU 42  42  42  LEU LEU D . n 
C 1 43  HIS 43  43  43  HIS HIS D . n 
C 1 44  GLY 44  44  44  GLY GLY D . n 
C 1 45  PHE 45  45  45  PHE PHE D . n 
C 1 46  HIS 46  46  46  HIS HIS D . n 
C 1 47  VAL 47  47  47  VAL VAL D . n 
C 1 48  HIS 48  48  48  HIS HIS D . n 
C 1 49  GLU 49  49  49  GLU GLU D . n 
C 1 50  PHE 50  50  50  PHE PHE D . n 
C 1 51  GLY 51  51  51  GLY GLY D . n 
C 1 52  ASP 52  52  52  ASP ASP D . n 
C 1 53  ASN 53  53  53  ASN ASN D . n 
C 1 54  THR 54  54  54  THR THR D . n 
C 1 55  ALA 55  55  55  ALA ALA D . n 
C 1 56  GLY 56  56  56  GLY GLY D . n 
C 1 57  ALA 57  57  57  ALA ALA D . n 
C 1 58  THR 58  58  58  THR THR D . n 
C 1 59  SER 59  59  59  SER SER D . n 
C 1 60  ALA 60  60  60  ALA ALA D . n 
C 1 61  GLY 61  61  61  GLY GLY D . n 
C 1 62  PRO 62  62  62  PRO PRO D . n 
C 1 63  HIS 63  63  63  HIS HIS D . n 
C 1 64  PHE 64  64  64  PHE PHE D . n 
C 1 65  ASN 65  65  65  ASN ASN D . n 
C 1 66  PRO 66  66  66  PRO PRO D . n 
C 1 67  LEU 67  67  67  LEU LEU D . n 
C 1 68  SER 68  68  68  SER SER D . n 
C 1 69  ARG 69  69  69  ARG ARG D . n 
C 1 70  LYS 70  70  70  LYS LYS D . n 
C 1 71  HIS 71  71  71  HIS HIS D . n 
C 1 72  GLY 72  72  72  GLY GLY D . n 
C 1 73  GLY 73  73  73  GLY GLY D . n 
C 1 74  PRO 74  74  74  PRO PRO D . n 
C 1 75  LYS 75  75  75  LYS LYS D . n 
C 1 76  ASP 76  76  76  ASP ASP D . n 
C 1 77  GLU 77  77  77  GLU GLU D . n 
C 1 78  GLU 78  78  78  GLU GLU D . n 
C 1 79  ARG 79  79  79  ARG ARG D . n 
C 1 80  HIS 80  80  80  HIS HIS D . n 
C 1 81  VAL 81  81  81  VAL VAL D . n 
C 1 82  GLY 82  82  82  GLY GLY D . n 
C 1 83  ASP 83  83  83  ASP ASP D . n 
C 1 84  LEU 84  84  84  LEU LEU D . n 
C 1 85  GLY 85  85  85  GLY GLY D . n 
C 1 86  ASN 86  86  86  ASN ASN D . n 
C 1 87  VAL 87  87  87  VAL VAL D . n 
C 1 88  THR 88  88  88  THR THR D . n 
C 1 89  ALA 89  89  89  ALA ALA D . n 
C 1 90  ASP 90  90  90  ASP ASP D . n 
C 1 91  LYS 91  91  91  LYS LYS D . n 
C 1 92  ASP 92  92  92  ASP ASP D . n 
C 1 93  GLY 93  93  93  GLY GLY D . n 
C 1 94  VAL 94  94  94  VAL VAL D . n 
C 1 95  ALA 95  95  95  ALA ALA D . n 
C 1 96  ASP 96  96  96  ASP ASP D . n 
C 1 97  VAL 97  97  97  VAL VAL D . n 
C 1 98  SER 98  98  98  SER SER D . n 
C 1 99  ILE 99  99  99  ILE ILE D . n 
C 1 100 GLU 100 100 100 GLU GLU D . n 
C 1 101 ASP 101 101 101 ASP ASP D . n 
C 1 102 SER 102 102 102 SER SER D . n 
C 1 103 VAL 103 103 103 VAL VAL D . n 
C 1 104 ILE 104 104 104 ILE ILE D . n 
C 1 105 SER 105 105 105 SER SER D . n 
C 1 106 LEU 106 106 106 LEU LEU D . n 
C 1 107 SER 107 107 107 SER SER D . n 
C 1 108 GLY 108 108 108 GLY GLY D . n 
C 1 109 ASP 109 109 109 ASP ASP D . n 
C 1 110 HIS 110 110 110 HIS HIS D . n 
C 1 111 CYS 111 111 111 CYS CYS D . n 
C 1 112 ILE 112 112 112 ILE ILE D . n 
C 1 113 ILE 113 113 113 ILE ILE D . n 
C 1 114 GLY 114 114 114 GLY GLY D . n 
C 1 115 ARG 115 115 115 ARG ARG D . n 
C 1 116 THR 116 116 116 THR THR D . n 
C 1 117 LEU 117 117 117 LEU LEU D . n 
C 1 118 VAL 118 118 118 VAL VAL D . n 
C 1 119 VAL 119 119 119 VAL VAL D . n 
C 1 120 HIS 120 120 120 HIS HIS D . n 
C 1 121 GLU 121 121 121 GLU GLU D . n 
C 1 122 LYS 122 122 122 LYS LYS D . n 
C 1 123 ALA 123 123 123 ALA ALA D . n 
C 1 124 ASP 124 124 124 ASP ASP D . n 
C 1 125 ASP 125 125 125 ASP ASP D . n 
C 1 126 LEU 126 126 126 LEU LEU D . n 
C 1 127 GLY 127 127 127 GLY GLY D . n 
C 1 128 LYS 128 128 128 LYS LYS D . n 
C 1 129 GLY 129 129 129 GLY GLY D . n 
C 1 130 GLY 130 130 130 GLY GLY D . n 
C 1 131 ASN 131 131 131 ASN ASN D . n 
C 1 132 GLU 132 132 132 GLU GLU D . n 
C 1 133 GLU 133 133 133 GLU GLU D . n 
C 1 134 SER 134 134 134 SER SER D . n 
C 1 135 THR 135 135 135 THR THR D . n 
C 1 136 LYS 136 136 136 LYS LYS D . n 
C 1 137 THR 137 137 137 THR THR D . n 
C 1 138 GLY 138 138 138 GLY GLY D . n 
C 1 139 ASN 139 139 139 ASN ASN D . n 
C 1 140 ALA 140 140 140 ALA ALA D . n 
C 1 141 GLY 141 141 141 GLY GLY D . n 
C 1 142 SER 142 142 142 SER SER D . n 
C 1 143 ARG 143 143 143 ARG ARG D . n 
C 1 144 LEU 144 144 144 LEU LEU D . n 
C 1 145 ALA 145 145 145 ALA ALA D . n 
C 1 146 ALA 146 146 146 ALA ALA D . n 
C 1 147 GLY 147 147 147 GLY GLY D . n 
C 1 148 VAL 148 148 148 VAL VAL D . n 
C 1 149 ILE 149 149 149 ILE ILE D . n 
C 1 150 GLY 150 150 150 GLY GLY D . n 
C 1 151 ILE 151 151 151 ILE ILE D . n 
C 1 152 ALA 152 152 152 ALA ALA D . n 
C 1 153 GLN 153 153 153 GLN GLN D . n 
D 1 1   ALA 1   1   1   ALA ALA G . n 
D 1 2   THR 2   2   2   THR THR G . n 
D 1 3   LYS 3   3   3   LYS LYS G . n 
D 1 4   ALA 4   4   4   ALA ALA G . n 
D 1 5   VAL 5   5   5   VAL VAL G . n 
D 1 6   CYS 6   6   6   CYS CYS G . n 
D 1 7   VAL 7   7   7   VAL VAL G . n 
D 1 8   LEU 8   8   8   LEU LEU G . n 
D 1 9   LYS 9   9   9   LYS LYS G . n 
D 1 10  GLY 10  10  10  GLY GLY G . n 
D 1 11  ASP 11  11  11  ASP ASP G . n 
D 1 12  GLY 12  12  12  GLY GLY G . n 
D 1 13  PRO 13  13  13  PRO PRO G . n 
D 1 14  VAL 14  14  14  VAL VAL G . n 
D 1 15  GLN 15  15  15  GLN GLN G . n 
D 1 16  GLY 16  16  16  GLY GLY G . n 
D 1 17  ILE 17  17  17  ILE ILE G . n 
D 1 18  ILE 18  18  18  ILE ILE G . n 
D 1 19  ASN 19  19  19  ASN ASN G . n 
D 1 20  PHE 20  20  20  PHE PHE G . n 
D 1 21  GLU 21  21  21  GLU GLU G . n 
D 1 22  GLN 22  22  22  GLN GLN G . n 
D 1 23  LYS 23  23  23  LYS LYS G . n 
D 1 24  GLU 24  24  24  GLU GLU G . n 
D 1 25  SER 25  25  25  SER SER G . n 
D 1 26  ASN 26  26  26  ASN ASN G . n 
D 1 27  GLY 27  27  27  GLY GLY G . n 
D 1 28  PRO 28  28  28  PRO PRO G . n 
D 1 29  VAL 29  29  29  VAL VAL G . n 
D 1 30  LYS 30  30  30  LYS LYS G . n 
D 1 31  VAL 31  31  31  VAL VAL G . n 
D 1 32  TRP 32  32  32  TRP TRP G . n 
D 1 33  GLY 33  33  33  GLY GLY G . n 
D 1 34  SER 34  34  34  SER SER G . n 
D 1 35  ILE 35  35  35  ILE ILE G . n 
D 1 36  LYS 36  36  36  LYS LYS G . n 
D 1 37  GLY 37  37  37  GLY GLY G . n 
D 1 38  LEU 38  38  38  LEU LEU G . n 
D 1 39  THR 39  39  39  THR THR G . n 
D 1 40  GLU 40  40  40  GLU GLU G . n 
D 1 41  GLY 41  41  41  GLY GLY G . n 
D 1 42  LEU 42  42  42  LEU LEU G . n 
D 1 43  HIS 43  43  43  HIS HIS G . n 
D 1 44  GLY 44  44  44  GLY GLY G . n 
D 1 45  PHE 45  45  45  PHE PHE G . n 
D 1 46  HIS 46  46  46  HIS HIS G . n 
D 1 47  VAL 47  47  47  VAL VAL G . n 
D 1 48  HIS 48  48  48  HIS HIS G . n 
D 1 49  GLU 49  49  49  GLU GLU G . n 
D 1 50  PHE 50  50  50  PHE PHE G . n 
D 1 51  GLY 51  51  51  GLY GLY G . n 
D 1 52  ASP 52  52  52  ASP ASP G . n 
D 1 53  ASN 53  53  53  ASN ASN G . n 
D 1 54  THR 54  54  54  THR THR G . n 
D 1 55  ALA 55  55  55  ALA ALA G . n 
D 1 56  GLY 56  56  56  GLY GLY G . n 
D 1 57  ALA 57  57  57  ALA ALA G . n 
D 1 58  THR 58  58  58  THR THR G . n 
D 1 59  SER 59  59  59  SER SER G . n 
D 1 60  ALA 60  60  60  ALA ALA G . n 
D 1 61  GLY 61  61  61  GLY GLY G . n 
D 1 62  PRO 62  62  62  PRO PRO G . n 
D 1 63  HIS 63  63  63  HIS HIS G . n 
D 1 64  PHE 64  64  64  PHE PHE G . n 
D 1 65  ASN 65  65  65  ASN ASN G . n 
D 1 66  PRO 66  66  66  PRO PRO G . n 
D 1 67  LEU 67  67  67  LEU LEU G . n 
D 1 68  SER 68  68  68  SER SER G . n 
D 1 69  ARG 69  69  69  ARG ARG G . n 
D 1 70  LYS 70  70  70  LYS LYS G . n 
D 1 71  HIS 71  71  71  HIS HIS G . n 
D 1 72  GLY 72  72  72  GLY GLY G . n 
D 1 73  GLY 73  73  73  GLY GLY G . n 
D 1 74  PRO 74  74  74  PRO PRO G . n 
D 1 75  LYS 75  75  75  LYS LYS G . n 
D 1 76  ASP 76  76  76  ASP ASP G . n 
D 1 77  GLU 77  77  77  GLU GLU G . n 
D 1 78  GLU 78  78  78  GLU GLU G . n 
D 1 79  ARG 79  79  79  ARG ARG G . n 
D 1 80  HIS 80  80  80  HIS HIS G . n 
D 1 81  VAL 81  81  81  VAL VAL G . n 
D 1 82  GLY 82  82  82  GLY GLY G . n 
D 1 83  ASP 83  83  83  ASP ASP G . n 
D 1 84  LEU 84  84  84  LEU LEU G . n 
D 1 85  GLY 85  85  85  GLY GLY G . n 
D 1 86  ASN 86  86  86  ASN ASN G . n 
D 1 87  VAL 87  87  87  VAL VAL G . n 
D 1 88  THR 88  88  88  THR THR G . n 
D 1 89  ALA 89  89  89  ALA ALA G . n 
D 1 90  ASP 90  90  90  ASP ASP G . n 
D 1 91  LYS 91  91  91  LYS LYS G . n 
D 1 92  ASP 92  92  92  ASP ASP G . n 
D 1 93  GLY 93  93  93  GLY GLY G . n 
D 1 94  VAL 94  94  94  VAL VAL G . n 
D 1 95  ALA 95  95  95  ALA ALA G . n 
D 1 96  ASP 96  96  96  ASP ASP G . n 
D 1 97  VAL 97  97  97  VAL VAL G . n 
D 1 98  SER 98  98  98  SER SER G . n 
D 1 99  ILE 99  99  99  ILE ILE G . n 
D 1 100 GLU 100 100 100 GLU GLU G . n 
D 1 101 ASP 101 101 101 ASP ASP G . n 
D 1 102 SER 102 102 102 SER SER G . n 
D 1 103 VAL 103 103 103 VAL VAL G . n 
D 1 104 ILE 104 104 104 ILE ILE G . n 
D 1 105 SER 105 105 105 SER SER G . n 
D 1 106 LEU 106 106 106 LEU LEU G . n 
D 1 107 SER 107 107 107 SER SER G . n 
D 1 108 GLY 108 108 108 GLY GLY G . n 
D 1 109 ASP 109 109 109 ASP ASP G . n 
D 1 110 HIS 110 110 110 HIS HIS G . n 
D 1 111 CYS 111 111 111 CYS CYS G . n 
D 1 112 ILE 112 112 112 ILE ILE G . n 
D 1 113 ILE 113 113 113 ILE ILE G . n 
D 1 114 GLY 114 114 114 GLY GLY G . n 
D 1 115 ARG 115 115 115 ARG ARG G . n 
D 1 116 THR 116 116 116 THR THR G . n 
D 1 117 LEU 117 117 117 LEU LEU G . n 
D 1 118 VAL 118 118 118 VAL VAL G . n 
D 1 119 VAL 119 119 119 VAL VAL G . n 
D 1 120 HIS 120 120 120 HIS HIS G . n 
D 1 121 GLU 121 121 121 GLU GLU G . n 
D 1 122 LYS 122 122 122 LYS LYS G . n 
D 1 123 ALA 123 123 123 ALA ALA G . n 
D 1 124 ASP 124 124 124 ASP ASP G . n 
D 1 125 ASP 125 125 125 ASP ASP G . n 
D 1 126 LEU 126 126 126 LEU LEU G . n 
D 1 127 GLY 127 127 127 GLY GLY G . n 
D 1 128 LYS 128 128 128 LYS LYS G . n 
D 1 129 GLY 129 129 129 GLY GLY G . n 
D 1 130 GLY 130 130 130 GLY GLY G . n 
D 1 131 ASN 131 131 131 ASN ASN G . n 
D 1 132 GLU 132 132 132 GLU GLU G . n 
D 1 133 GLU 133 133 133 GLU GLU G . n 
D 1 134 SER 134 134 134 SER SER G . n 
D 1 135 THR 135 135 135 THR THR G . n 
D 1 136 LYS 136 136 136 LYS LYS G . n 
D 1 137 THR 137 137 137 THR THR G . n 
D 1 138 GLY 138 138 138 GLY GLY G . n 
D 1 139 ASN 139 139 139 ASN ASN G . n 
D 1 140 ALA 140 140 140 ALA ALA G . n 
D 1 141 GLY 141 141 141 GLY GLY G . n 
D 1 142 SER 142 142 142 SER SER G . n 
D 1 143 ARG 143 143 143 ARG ARG G . n 
D 1 144 LEU 144 144 144 LEU LEU G . n 
D 1 145 ALA 145 145 145 ALA ALA G . n 
D 1 146 ALA 146 146 146 ALA ALA G . n 
D 1 147 GLY 147 147 147 GLY GLY G . n 
D 1 148 VAL 148 148 148 VAL VAL G . n 
D 1 149 ILE 149 149 149 ILE ILE G . n 
D 1 150 GLY 150 150 150 GLY GLY G . n 
D 1 151 ILE 151 151 151 ILE ILE G . n 
D 1 152 ALA 152 152 152 ALA ALA G . n 
D 1 153 GLN 153 153 153 GLN GLN G . n 
E 1 1   ALA 1   1   1   ALA ALA I . n 
E 1 2   THR 2   2   2   THR THR I . n 
E 1 3   LYS 3   3   3   LYS LYS I . n 
E 1 4   ALA 4   4   4   ALA ALA I . n 
E 1 5   VAL 5   5   5   VAL VAL I . n 
E 1 6   CYS 6   6   6   CYS CYS I . n 
E 1 7   VAL 7   7   7   VAL VAL I . n 
E 1 8   LEU 8   8   8   LEU LEU I . n 
E 1 9   LYS 9   9   9   LYS LYS I . n 
E 1 10  GLY 10  10  10  GLY GLY I . n 
E 1 11  ASP 11  11  11  ASP ASP I . n 
E 1 12  GLY 12  12  12  GLY GLY I . n 
E 1 13  PRO 13  13  13  PRO PRO I . n 
E 1 14  VAL 14  14  14  VAL VAL I . n 
E 1 15  GLN 15  15  15  GLN GLN I . n 
E 1 16  GLY 16  16  16  GLY GLY I . n 
E 1 17  ILE 17  17  17  ILE ILE I . n 
E 1 18  ILE 18  18  18  ILE ILE I . n 
E 1 19  ASN 19  19  19  ASN ASN I . n 
E 1 20  PHE 20  20  20  PHE PHE I . n 
E 1 21  GLU 21  21  21  GLU GLU I . n 
E 1 22  GLN 22  22  22  GLN GLN I . n 
E 1 23  LYS 23  23  23  LYS LYS I . n 
E 1 24  GLU 24  24  24  GLU GLU I . n 
E 1 25  SER 25  25  25  SER SER I . n 
E 1 26  ASN 26  26  26  ASN ASN I . n 
E 1 27  GLY 27  27  27  GLY GLY I . n 
E 1 28  PRO 28  28  28  PRO PRO I . n 
E 1 29  VAL 29  29  29  VAL VAL I . n 
E 1 30  LYS 30  30  30  LYS LYS I . n 
E 1 31  VAL 31  31  31  VAL VAL I . n 
E 1 32  TRP 32  32  32  TRP TRP I . n 
E 1 33  GLY 33  33  33  GLY GLY I . n 
E 1 34  SER 34  34  34  SER SER I . n 
E 1 35  ILE 35  35  35  ILE ILE I . n 
E 1 36  LYS 36  36  36  LYS LYS I . n 
E 1 37  GLY 37  37  37  GLY GLY I . n 
E 1 38  LEU 38  38  38  LEU LEU I . n 
E 1 39  THR 39  39  39  THR THR I . n 
E 1 40  GLU 40  40  40  GLU GLU I . n 
E 1 41  GLY 41  41  41  GLY GLY I . n 
E 1 42  LEU 42  42  42  LEU LEU I . n 
E 1 43  HIS 43  43  43  HIS HIS I . n 
E 1 44  GLY 44  44  44  GLY GLY I . n 
E 1 45  PHE 45  45  45  PHE PHE I . n 
E 1 46  HIS 46  46  46  HIS HIS I . n 
E 1 47  VAL 47  47  47  VAL VAL I . n 
E 1 48  HIS 48  48  48  HIS HIS I . n 
E 1 49  GLU 49  49  49  GLU GLU I . n 
E 1 50  PHE 50  50  50  PHE PHE I . n 
E 1 51  GLY 51  51  51  GLY GLY I . n 
E 1 52  ASP 52  52  52  ASP ASP I . n 
E 1 53  ASN 53  53  53  ASN ASN I . n 
E 1 54  THR 54  54  54  THR THR I . n 
E 1 55  ALA 55  55  55  ALA ALA I . n 
E 1 56  GLY 56  56  56  GLY GLY I . n 
E 1 57  ALA 57  57  57  ALA ALA I . n 
E 1 58  THR 58  58  58  THR THR I . n 
E 1 59  SER 59  59  59  SER SER I . n 
E 1 60  ALA 60  60  60  ALA ALA I . n 
E 1 61  GLY 61  61  61  GLY GLY I . n 
E 1 62  PRO 62  62  62  PRO PRO I . n 
E 1 63  HIS 63  63  63  HIS HIS I . n 
E 1 64  PHE 64  64  64  PHE PHE I . n 
E 1 65  ASN 65  65  65  ASN ASN I . n 
E 1 66  PRO 66  66  66  PRO PRO I . n 
E 1 67  LEU 67  67  67  LEU LEU I . n 
E 1 68  SER 68  68  68  SER SER I . n 
E 1 69  ARG 69  69  69  ARG ARG I . n 
E 1 70  LYS 70  70  70  LYS LYS I . n 
E 1 71  HIS 71  71  71  HIS HIS I . n 
E 1 72  GLY 72  72  72  GLY GLY I . n 
E 1 73  GLY 73  73  73  GLY GLY I . n 
E 1 74  PRO 74  74  74  PRO PRO I . n 
E 1 75  LYS 75  75  75  LYS LYS I . n 
E 1 76  ASP 76  76  76  ASP ASP I . n 
E 1 77  GLU 77  77  77  GLU GLU I . n 
E 1 78  GLU 78  78  78  GLU GLU I . n 
E 1 79  ARG 79  79  79  ARG ARG I . n 
E 1 80  HIS 80  80  80  HIS HIS I . n 
E 1 81  VAL 81  81  81  VAL VAL I . n 
E 1 82  GLY 82  82  82  GLY GLY I . n 
E 1 83  ASP 83  83  83  ASP ASP I . n 
E 1 84  LEU 84  84  84  LEU LEU I . n 
E 1 85  GLY 85  85  85  GLY GLY I . n 
E 1 86  ASN 86  86  86  ASN ASN I . n 
E 1 87  VAL 87  87  87  VAL VAL I . n 
E 1 88  THR 88  88  88  THR THR I . n 
E 1 89  ALA 89  89  89  ALA ALA I . n 
E 1 90  ASP 90  90  90  ASP ASP I . n 
E 1 91  LYS 91  91  91  LYS LYS I . n 
E 1 92  ASP 92  92  92  ASP ASP I . n 
E 1 93  GLY 93  93  93  GLY GLY I . n 
E 1 94  VAL 94  94  94  VAL VAL I . n 
E 1 95  ALA 95  95  95  ALA ALA I . n 
E 1 96  ASP 96  96  96  ASP ASP I . n 
E 1 97  VAL 97  97  97  VAL VAL I . n 
E 1 98  SER 98  98  98  SER SER I . n 
E 1 99  ILE 99  99  99  ILE ILE I . n 
E 1 100 GLU 100 100 100 GLU GLU I . n 
E 1 101 ASP 101 101 101 ASP ASP I . n 
E 1 102 SER 102 102 102 SER SER I . n 
E 1 103 VAL 103 103 103 VAL VAL I . n 
E 1 104 ILE 104 104 104 ILE ILE I . n 
E 1 105 SER 105 105 105 SER SER I . n 
E 1 106 LEU 106 106 106 LEU LEU I . n 
E 1 107 SER 107 107 107 SER SER I . n 
E 1 108 GLY 108 108 108 GLY GLY I . n 
E 1 109 ASP 109 109 109 ASP ASP I . n 
E 1 110 HIS 110 110 110 HIS HIS I . n 
E 1 111 CYS 111 111 111 CYS CYS I . n 
E 1 112 ILE 112 112 112 ILE ILE I . n 
E 1 113 ILE 113 113 113 ILE ILE I . n 
E 1 114 GLY 114 114 114 GLY GLY I . n 
E 1 115 ARG 115 115 115 ARG ARG I . n 
E 1 116 THR 116 116 116 THR THR I . n 
E 1 117 LEU 117 117 117 LEU LEU I . n 
E 1 118 VAL 118 118 118 VAL VAL I . n 
E 1 119 VAL 119 119 119 VAL VAL I . n 
E 1 120 HIS 120 120 120 HIS HIS I . n 
E 1 121 GLU 121 121 121 GLU GLU I . n 
E 1 122 LYS 122 122 122 LYS LYS I . n 
E 1 123 ALA 123 123 123 ALA ALA I . n 
E 1 124 ASP 124 124 124 ASP ASP I . n 
E 1 125 ASP 125 125 125 ASP ASP I . n 
E 1 126 LEU 126 126 126 LEU LEU I . n 
E 1 127 GLY 127 127 127 GLY GLY I . n 
E 1 128 LYS 128 128 128 LYS LYS I . n 
E 1 129 GLY 129 129 129 GLY GLY I . n 
E 1 130 GLY 130 130 130 GLY GLY I . n 
E 1 131 ASN 131 131 131 ASN ASN I . n 
E 1 132 GLU 132 132 132 GLU GLU I . n 
E 1 133 GLU 133 133 133 GLU GLU I . n 
E 1 134 SER 134 134 134 SER SER I . n 
E 1 135 THR 135 135 135 THR THR I . n 
E 1 136 LYS 136 136 136 LYS LYS I . n 
E 1 137 THR 137 137 137 THR THR I . n 
E 1 138 GLY 138 138 138 GLY GLY I . n 
E 1 139 ASN 139 139 139 ASN ASN I . n 
E 1 140 ALA 140 140 140 ALA ALA I . n 
E 1 141 GLY 141 141 141 GLY GLY I . n 
E 1 142 SER 142 142 142 SER SER I . n 
E 1 143 ARG 143 143 143 ARG ARG I . n 
E 1 144 LEU 144 144 144 LEU LEU I . n 
E 1 145 ALA 145 145 145 ALA ALA I . n 
E 1 146 ALA 146 146 146 ALA ALA I . n 
E 1 147 GLY 147 147 147 GLY GLY I . n 
E 1 148 VAL 148 148 148 VAL VAL I . n 
E 1 149 ILE 149 149 149 ILE ILE I . n 
E 1 150 GLY 150 150 150 GLY GLY I . n 
E 1 151 ILE 151 151 151 ILE ILE I . n 
E 1 152 ALA 152 152 152 ALA ALA I . n 
E 1 153 GLN 153 153 153 GLN GLN I . n 
F 1 1   ALA 1   1   1   ALA ALA K . n 
F 1 2   THR 2   2   2   THR THR K . n 
F 1 3   LYS 3   3   3   LYS LYS K . n 
F 1 4   ALA 4   4   4   ALA ALA K . n 
F 1 5   VAL 5   5   5   VAL VAL K . n 
F 1 6   CYS 6   6   6   CYS CYS K . n 
F 1 7   VAL 7   7   7   VAL VAL K . n 
F 1 8   LEU 8   8   8   LEU LEU K . n 
F 1 9   LYS 9   9   9   LYS LYS K . n 
F 1 10  GLY 10  10  10  GLY GLY K . n 
F 1 11  ASP 11  11  11  ASP ASP K . n 
F 1 12  GLY 12  12  12  GLY GLY K . n 
F 1 13  PRO 13  13  13  PRO PRO K . n 
F 1 14  VAL 14  14  14  VAL VAL K . n 
F 1 15  GLN 15  15  15  GLN GLN K . n 
F 1 16  GLY 16  16  16  GLY GLY K . n 
F 1 17  ILE 17  17  17  ILE ILE K . n 
F 1 18  ILE 18  18  18  ILE ILE K . n 
F 1 19  ASN 19  19  19  ASN ASN K . n 
F 1 20  PHE 20  20  20  PHE PHE K . n 
F 1 21  GLU 21  21  21  GLU GLU K . n 
F 1 22  GLN 22  22  22  GLN GLN K . n 
F 1 23  LYS 23  23  23  LYS LYS K . n 
F 1 24  GLU 24  24  24  GLU GLU K . n 
F 1 25  SER 25  25  25  SER SER K . n 
F 1 26  ASN 26  26  26  ASN ASN K . n 
F 1 27  GLY 27  27  27  GLY GLY K . n 
F 1 28  PRO 28  28  28  PRO PRO K . n 
F 1 29  VAL 29  29  29  VAL VAL K . n 
F 1 30  LYS 30  30  30  LYS LYS K . n 
F 1 31  VAL 31  31  31  VAL VAL K . n 
F 1 32  TRP 32  32  32  TRP TRP K . n 
F 1 33  GLY 33  33  33  GLY GLY K . n 
F 1 34  SER 34  34  34  SER SER K . n 
F 1 35  ILE 35  35  35  ILE ILE K . n 
F 1 36  LYS 36  36  36  LYS LYS K . n 
F 1 37  GLY 37  37  37  GLY GLY K . n 
F 1 38  LEU 38  38  38  LEU LEU K . n 
F 1 39  THR 39  39  39  THR THR K . n 
F 1 40  GLU 40  40  40  GLU GLU K . n 
F 1 41  GLY 41  41  41  GLY GLY K . n 
F 1 42  LEU 42  42  42  LEU LEU K . n 
F 1 43  HIS 43  43  43  HIS HIS K . n 
F 1 44  GLY 44  44  44  GLY GLY K . n 
F 1 45  PHE 45  45  45  PHE PHE K . n 
F 1 46  HIS 46  46  46  HIS HIS K . n 
F 1 47  VAL 47  47  47  VAL VAL K . n 
F 1 48  HIS 48  48  48  HIS HIS K . n 
F 1 49  GLU 49  49  49  GLU GLU K . n 
F 1 50  PHE 50  50  50  PHE PHE K . n 
F 1 51  GLY 51  51  51  GLY GLY K . n 
F 1 52  ASP 52  52  52  ASP ASP K . n 
F 1 53  ASN 53  53  53  ASN ASN K . n 
F 1 54  THR 54  54  54  THR THR K . n 
F 1 55  ALA 55  55  55  ALA ALA K . n 
F 1 56  GLY 56  56  56  GLY GLY K . n 
F 1 57  ALA 57  57  57  ALA ALA K . n 
F 1 58  THR 58  58  58  THR THR K . n 
F 1 59  SER 59  59  59  SER SER K . n 
F 1 60  ALA 60  60  60  ALA ALA K . n 
F 1 61  GLY 61  61  61  GLY GLY K . n 
F 1 62  PRO 62  62  62  PRO PRO K . n 
F 1 63  HIS 63  63  63  HIS HIS K . n 
F 1 64  PHE 64  64  64  PHE PHE K . n 
F 1 65  ASN 65  65  65  ASN ASN K . n 
F 1 66  PRO 66  66  66  PRO PRO K . n 
F 1 67  LEU 67  67  67  LEU LEU K . n 
F 1 68  SER 68  68  68  SER SER K . n 
F 1 69  ARG 69  69  69  ARG ARG K . n 
F 1 70  LYS 70  70  70  LYS LYS K . n 
F 1 71  HIS 71  71  71  HIS HIS K . n 
F 1 72  GLY 72  72  72  GLY GLY K . n 
F 1 73  GLY 73  73  73  GLY GLY K . n 
F 1 74  PRO 74  74  74  PRO PRO K . n 
F 1 75  LYS 75  75  75  LYS LYS K . n 
F 1 76  ASP 76  76  76  ASP ASP K . n 
F 1 77  GLU 77  77  77  GLU GLU K . n 
F 1 78  GLU 78  78  78  GLU GLU K . n 
F 1 79  ARG 79  79  79  ARG ARG K . n 
F 1 80  HIS 80  80  80  HIS HIS K . n 
F 1 81  VAL 81  81  81  VAL VAL K . n 
F 1 82  GLY 82  82  82  GLY GLY K . n 
F 1 83  ASP 83  83  83  ASP ASP K . n 
F 1 84  LEU 84  84  84  LEU LEU K . n 
F 1 85  GLY 85  85  85  GLY GLY K . n 
F 1 86  ASN 86  86  86  ASN ASN K . n 
F 1 87  VAL 87  87  87  VAL VAL K . n 
F 1 88  THR 88  88  88  THR THR K . n 
F 1 89  ALA 89  89  89  ALA ALA K . n 
F 1 90  ASP 90  90  90  ASP ASP K . n 
F 1 91  LYS 91  91  91  LYS LYS K . n 
F 1 92  ASP 92  92  92  ASP ASP K . n 
F 1 93  GLY 93  93  93  GLY GLY K . n 
F 1 94  VAL 94  94  94  VAL VAL K . n 
F 1 95  ALA 95  95  95  ALA ALA K . n 
F 1 96  ASP 96  96  96  ASP ASP K . n 
F 1 97  VAL 97  97  97  VAL VAL K . n 
F 1 98  SER 98  98  98  SER SER K . n 
F 1 99  ILE 99  99  99  ILE ILE K . n 
F 1 100 GLU 100 100 100 GLU GLU K . n 
F 1 101 ASP 101 101 101 ASP ASP K . n 
F 1 102 SER 102 102 102 SER SER K . n 
F 1 103 VAL 103 103 103 VAL VAL K . n 
F 1 104 ILE 104 104 104 ILE ILE K . n 
F 1 105 SER 105 105 105 SER SER K . n 
F 1 106 LEU 106 106 106 LEU LEU K . n 
F 1 107 SER 107 107 107 SER SER K . n 
F 1 108 GLY 108 108 108 GLY GLY K . n 
F 1 109 ASP 109 109 109 ASP ASP K . n 
F 1 110 HIS 110 110 110 HIS HIS K . n 
F 1 111 CYS 111 111 111 CYS CYS K . n 
F 1 112 ILE 112 112 112 ILE ILE K . n 
F 1 113 ILE 113 113 113 ILE ILE K . n 
F 1 114 GLY 114 114 114 GLY GLY K . n 
F 1 115 ARG 115 115 115 ARG ARG K . n 
F 1 116 THR 116 116 116 THR THR K . n 
F 1 117 LEU 117 117 117 LEU LEU K . n 
F 1 118 VAL 118 118 118 VAL VAL K . n 
F 1 119 VAL 119 119 119 VAL VAL K . n 
F 1 120 HIS 120 120 120 HIS HIS K . n 
F 1 121 GLU 121 121 121 GLU GLU K . n 
F 1 122 LYS 122 122 122 LYS LYS K . n 
F 1 123 ALA 123 123 123 ALA ALA K . n 
F 1 124 ASP 124 124 124 ASP ASP K . n 
F 1 125 ASP 125 125 125 ASP ASP K . n 
F 1 126 LEU 126 126 126 LEU LEU K . n 
F 1 127 GLY 127 127 127 GLY GLY K . n 
F 1 128 LYS 128 128 128 LYS LYS K . n 
F 1 129 GLY 129 129 129 GLY GLY K . n 
F 1 130 GLY 130 130 130 GLY GLY K . n 
F 1 131 ASN 131 131 131 ASN ASN K . n 
F 1 132 GLU 132 132 132 GLU GLU K . n 
F 1 133 GLU 133 133 133 GLU GLU K . n 
F 1 134 SER 134 134 134 SER SER K . n 
F 1 135 THR 135 135 135 THR THR K . n 
F 1 136 LYS 136 136 136 LYS LYS K . n 
F 1 137 THR 137 137 137 THR THR K . n 
F 1 138 GLY 138 138 138 GLY GLY K . n 
F 1 139 ASN 139 139 139 ASN ASN K . n 
F 1 140 ALA 140 140 140 ALA ALA K . n 
F 1 141 GLY 141 141 141 GLY GLY K . n 
F 1 142 SER 142 142 142 SER SER K . n 
F 1 143 ARG 143 143 143 ARG ARG K . n 
F 1 144 LEU 144 144 144 LEU LEU K . n 
F 1 145 ALA 145 145 145 ALA ALA K . n 
F 1 146 ALA 146 146 146 ALA ALA K . n 
F 1 147 GLY 147 147 147 GLY GLY K . n 
F 1 148 VAL 148 148 148 VAL VAL K . n 
F 1 149 ILE 149 149 149 ILE ILE K . n 
F 1 150 GLY 150 150 150 GLY GLY K . n 
F 1 151 ILE 151 151 151 ILE ILE K . n 
F 1 152 ALA 152 152 152 ALA ALA K . n 
F 1 153 GLN 153 153 153 GLN GLN K . n 
G 1 1   ALA 1   1   1   ALA ALA M . n 
G 1 2   THR 2   2   2   THR THR M . n 
G 1 3   LYS 3   3   3   LYS LYS M . n 
G 1 4   ALA 4   4   4   ALA ALA M . n 
G 1 5   VAL 5   5   5   VAL VAL M . n 
G 1 6   CYS 6   6   6   CYS CYS M . n 
G 1 7   VAL 7   7   7   VAL VAL M . n 
G 1 8   LEU 8   8   8   LEU LEU M . n 
G 1 9   LYS 9   9   9   LYS LYS M . n 
G 1 10  GLY 10  10  10  GLY GLY M . n 
G 1 11  ASP 11  11  11  ASP ASP M . n 
G 1 12  GLY 12  12  12  GLY GLY M . n 
G 1 13  PRO 13  13  13  PRO PRO M . n 
G 1 14  VAL 14  14  14  VAL VAL M . n 
G 1 15  GLN 15  15  15  GLN GLN M . n 
G 1 16  GLY 16  16  16  GLY GLY M . n 
G 1 17  ILE 17  17  17  ILE ILE M . n 
G 1 18  ILE 18  18  18  ILE ILE M . n 
G 1 19  ASN 19  19  19  ASN ASN M . n 
G 1 20  PHE 20  20  20  PHE PHE M . n 
G 1 21  GLU 21  21  21  GLU GLU M . n 
G 1 22  GLN 22  22  22  GLN GLN M . n 
G 1 23  LYS 23  23  23  LYS LYS M . n 
G 1 24  GLU 24  24  24  GLU GLU M . n 
G 1 25  SER 25  25  25  SER SER M . n 
G 1 26  ASN 26  26  26  ASN ASN M . n 
G 1 27  GLY 27  27  27  GLY GLY M . n 
G 1 28  PRO 28  28  28  PRO PRO M . n 
G 1 29  VAL 29  29  29  VAL VAL M . n 
G 1 30  LYS 30  30  30  LYS LYS M . n 
G 1 31  VAL 31  31  31  VAL VAL M . n 
G 1 32  TRP 32  32  32  TRP TRP M . n 
G 1 33  GLY 33  33  33  GLY GLY M . n 
G 1 34  SER 34  34  34  SER SER M . n 
G 1 35  ILE 35  35  35  ILE ILE M . n 
G 1 36  LYS 36  36  36  LYS LYS M . n 
G 1 37  GLY 37  37  37  GLY GLY M . n 
G 1 38  LEU 38  38  38  LEU LEU M . n 
G 1 39  THR 39  39  39  THR THR M . n 
G 1 40  GLU 40  40  40  GLU GLU M . n 
G 1 41  GLY 41  41  41  GLY GLY M . n 
G 1 42  LEU 42  42  42  LEU LEU M . n 
G 1 43  HIS 43  43  43  HIS HIS M . n 
G 1 44  GLY 44  44  44  GLY GLY M . n 
G 1 45  PHE 45  45  45  PHE PHE M . n 
G 1 46  HIS 46  46  46  HIS HIS M . n 
G 1 47  VAL 47  47  47  VAL VAL M . n 
G 1 48  HIS 48  48  48  HIS HIS M . n 
G 1 49  GLU 49  49  49  GLU GLU M . n 
G 1 50  PHE 50  50  50  PHE PHE M . n 
G 1 51  GLY 51  51  51  GLY GLY M . n 
G 1 52  ASP 52  52  52  ASP ASP M . n 
G 1 53  ASN 53  53  53  ASN ASN M . n 
G 1 54  THR 54  54  54  THR THR M . n 
G 1 55  ALA 55  55  55  ALA ALA M . n 
G 1 56  GLY 56  56  56  GLY GLY M . n 
G 1 57  ALA 57  57  57  ALA ALA M . n 
G 1 58  THR 58  58  58  THR THR M . n 
G 1 59  SER 59  59  59  SER SER M . n 
G 1 60  ALA 60  60  60  ALA ALA M . n 
G 1 61  GLY 61  61  61  GLY GLY M . n 
G 1 62  PRO 62  62  62  PRO PRO M . n 
G 1 63  HIS 63  63  63  HIS HIS M . n 
G 1 64  PHE 64  64  64  PHE PHE M . n 
G 1 65  ASN 65  65  65  ASN ASN M . n 
G 1 66  PRO 66  66  66  PRO PRO M . n 
G 1 67  LEU 67  67  67  LEU LEU M . n 
G 1 68  SER 68  68  68  SER SER M . n 
G 1 69  ARG 69  69  69  ARG ARG M . n 
G 1 70  LYS 70  70  70  LYS LYS M . n 
G 1 71  HIS 71  71  71  HIS HIS M . n 
G 1 72  GLY 72  72  72  GLY GLY M . n 
G 1 73  GLY 73  73  73  GLY GLY M . n 
G 1 74  PRO 74  74  74  PRO PRO M . n 
G 1 75  LYS 75  75  75  LYS LYS M . n 
G 1 76  ASP 76  76  76  ASP ASP M . n 
G 1 77  GLU 77  77  77  GLU GLU M . n 
G 1 78  GLU 78  78  78  GLU GLU M . n 
G 1 79  ARG 79  79  79  ARG ARG M . n 
G 1 80  HIS 80  80  80  HIS HIS M . n 
G 1 81  VAL 81  81  81  VAL VAL M . n 
G 1 82  GLY 82  82  82  GLY GLY M . n 
G 1 83  ASP 83  83  83  ASP ASP M . n 
G 1 84  LEU 84  84  84  LEU LEU M . n 
G 1 85  GLY 85  85  85  GLY GLY M . n 
G 1 86  ASN 86  86  86  ASN ASN M . n 
G 1 87  VAL 87  87  87  VAL VAL M . n 
G 1 88  THR 88  88  88  THR THR M . n 
G 1 89  ALA 89  89  89  ALA ALA M . n 
G 1 90  ASP 90  90  90  ASP ASP M . n 
G 1 91  LYS 91  91  91  LYS LYS M . n 
G 1 92  ASP 92  92  92  ASP ASP M . n 
G 1 93  GLY 93  93  93  GLY GLY M . n 
G 1 94  VAL 94  94  94  VAL VAL M . n 
G 1 95  ALA 95  95  95  ALA ALA M . n 
G 1 96  ASP 96  96  96  ASP ASP M . n 
G 1 97  VAL 97  97  97  VAL VAL M . n 
G 1 98  SER 98  98  98  SER SER M . n 
G 1 99  ILE 99  99  99  ILE ILE M . n 
G 1 100 GLU 100 100 100 GLU GLU M . n 
G 1 101 ASP 101 101 101 ASP ASP M . n 
G 1 102 SER 102 102 102 SER SER M . n 
G 1 103 VAL 103 103 103 VAL VAL M . n 
G 1 104 ILE 104 104 104 ILE ILE M . n 
G 1 105 SER 105 105 105 SER SER M . n 
G 1 106 LEU 106 106 106 LEU LEU M . n 
G 1 107 SER 107 107 107 SER SER M . n 
G 1 108 GLY 108 108 108 GLY GLY M . n 
G 1 109 ASP 109 109 109 ASP ASP M . n 
G 1 110 HIS 110 110 110 HIS HIS M . n 
G 1 111 CYS 111 111 111 CYS CYS M . n 
G 1 112 ILE 112 112 112 ILE ILE M . n 
G 1 113 ILE 113 113 113 ILE ILE M . n 
G 1 114 GLY 114 114 114 GLY GLY M . n 
G 1 115 ARG 115 115 115 ARG ARG M . n 
G 1 116 THR 116 116 116 THR THR M . n 
G 1 117 LEU 117 117 117 LEU LEU M . n 
G 1 118 VAL 118 118 118 VAL VAL M . n 
G 1 119 VAL 119 119 119 VAL VAL M . n 
G 1 120 HIS 120 120 120 HIS HIS M . n 
G 1 121 GLU 121 121 121 GLU GLU M . n 
G 1 122 LYS 122 122 122 LYS LYS M . n 
G 1 123 ALA 123 123 123 ALA ALA M . n 
G 1 124 ASP 124 124 124 ASP ASP M . n 
G 1 125 ASP 125 125 125 ASP ASP M . n 
G 1 126 LEU 126 126 126 LEU LEU M . n 
G 1 127 GLY 127 127 127 GLY GLY M . n 
G 1 128 LYS 128 128 128 LYS LYS M . n 
G 1 129 GLY 129 129 129 GLY GLY M . n 
G 1 130 GLY 130 130 130 GLY GLY M . n 
G 1 131 ASN 131 131 131 ASN ASN M . n 
G 1 132 GLU 132 132 132 GLU GLU M . n 
G 1 133 GLU 133 133 133 GLU GLU M . n 
G 1 134 SER 134 134 134 SER SER M . n 
G 1 135 THR 135 135 135 THR THR M . n 
G 1 136 LYS 136 136 136 LYS LYS M . n 
G 1 137 THR 137 137 137 THR THR M . n 
G 1 138 GLY 138 138 138 GLY GLY M . n 
G 1 139 ASN 139 139 139 ASN ASN M . n 
G 1 140 ALA 140 140 140 ALA ALA M . n 
G 1 141 GLY 141 141 141 GLY GLY M . n 
G 1 142 SER 142 142 142 SER SER M . n 
G 1 143 ARG 143 143 143 ARG ARG M . n 
G 1 144 LEU 144 144 144 LEU LEU M . n 
G 1 145 ALA 145 145 145 ALA ALA M . n 
G 1 146 ALA 146 146 146 ALA ALA M . n 
G 1 147 GLY 147 147 147 GLY GLY M . n 
G 1 148 VAL 148 148 148 VAL VAL M . n 
G 1 149 ILE 149 149 149 ILE ILE M . n 
G 1 150 GLY 150 150 150 GLY GLY M . n 
G 1 151 ILE 151 151 151 ILE ILE M . n 
G 1 152 ALA 152 152 152 ALA ALA M . n 
G 1 153 GLN 153 153 153 GLN GLN M . n 
H 1 1   ALA 1   1   1   ALA ALA O . n 
H 1 2   THR 2   2   2   THR THR O . n 
H 1 3   LYS 3   3   3   LYS LYS O . n 
H 1 4   ALA 4   4   4   ALA ALA O . n 
H 1 5   VAL 5   5   5   VAL VAL O . n 
H 1 6   CYS 6   6   6   CYS CYS O . n 
H 1 7   VAL 7   7   7   VAL VAL O . n 
H 1 8   LEU 8   8   8   LEU LEU O . n 
H 1 9   LYS 9   9   9   LYS LYS O . n 
H 1 10  GLY 10  10  10  GLY GLY O . n 
H 1 11  ASP 11  11  11  ASP ASP O . n 
H 1 12  GLY 12  12  12  GLY GLY O . n 
H 1 13  PRO 13  13  13  PRO PRO O . n 
H 1 14  VAL 14  14  14  VAL VAL O . n 
H 1 15  GLN 15  15  15  GLN GLN O . n 
H 1 16  GLY 16  16  16  GLY GLY O . n 
H 1 17  ILE 17  17  17  ILE ILE O . n 
H 1 18  ILE 18  18  18  ILE ILE O . n 
H 1 19  ASN 19  19  19  ASN ASN O . n 
H 1 20  PHE 20  20  20  PHE PHE O . n 
H 1 21  GLU 21  21  21  GLU GLU O . n 
H 1 22  GLN 22  22  22  GLN GLN O . n 
H 1 23  LYS 23  23  23  LYS LYS O . n 
H 1 24  GLU 24  24  24  GLU GLU O . n 
H 1 25  SER 25  25  25  SER SER O . n 
H 1 26  ASN 26  26  26  ASN ASN O . n 
H 1 27  GLY 27  27  27  GLY GLY O . n 
H 1 28  PRO 28  28  28  PRO PRO O . n 
H 1 29  VAL 29  29  29  VAL VAL O . n 
H 1 30  LYS 30  30  30  LYS LYS O . n 
H 1 31  VAL 31  31  31  VAL VAL O . n 
H 1 32  TRP 32  32  32  TRP TRP O . n 
H 1 33  GLY 33  33  33  GLY GLY O . n 
H 1 34  SER 34  34  34  SER SER O . n 
H 1 35  ILE 35  35  35  ILE ILE O . n 
H 1 36  LYS 36  36  36  LYS LYS O . n 
H 1 37  GLY 37  37  37  GLY GLY O . n 
H 1 38  LEU 38  38  38  LEU LEU O . n 
H 1 39  THR 39  39  39  THR THR O . n 
H 1 40  GLU 40  40  40  GLU GLU O . n 
H 1 41  GLY 41  41  41  GLY GLY O . n 
H 1 42  LEU 42  42  42  LEU LEU O . n 
H 1 43  HIS 43  43  43  HIS HIS O . n 
H 1 44  GLY 44  44  44  GLY GLY O . n 
H 1 45  PHE 45  45  45  PHE PHE O . n 
H 1 46  HIS 46  46  46  HIS HIS O . n 
H 1 47  VAL 47  47  47  VAL VAL O . n 
H 1 48  HIS 48  48  48  HIS HIS O . n 
H 1 49  GLU 49  49  49  GLU GLU O . n 
H 1 50  PHE 50  50  50  PHE PHE O . n 
H 1 51  GLY 51  51  51  GLY GLY O . n 
H 1 52  ASP 52  52  52  ASP ASP O . n 
H 1 53  ASN 53  53  53  ASN ASN O . n 
H 1 54  THR 54  54  54  THR THR O . n 
H 1 55  ALA 55  55  55  ALA ALA O . n 
H 1 56  GLY 56  56  56  GLY GLY O . n 
H 1 57  ALA 57  57  57  ALA ALA O . n 
H 1 58  THR 58  58  58  THR THR O . n 
H 1 59  SER 59  59  59  SER SER O . n 
H 1 60  ALA 60  60  60  ALA ALA O . n 
H 1 61  GLY 61  61  61  GLY GLY O . n 
H 1 62  PRO 62  62  62  PRO PRO O . n 
H 1 63  HIS 63  63  63  HIS HIS O . n 
H 1 64  PHE 64  64  64  PHE PHE O . n 
H 1 65  ASN 65  65  65  ASN ASN O . n 
H 1 66  PRO 66  66  66  PRO PRO O . n 
H 1 67  LEU 67  67  67  LEU LEU O . n 
H 1 68  SER 68  68  68  SER SER O . n 
H 1 69  ARG 69  69  69  ARG ARG O . n 
H 1 70  LYS 70  70  70  LYS LYS O . n 
H 1 71  HIS 71  71  71  HIS HIS O . n 
H 1 72  GLY 72  72  72  GLY GLY O . n 
H 1 73  GLY 73  73  73  GLY GLY O . n 
H 1 74  PRO 74  74  74  PRO PRO O . n 
H 1 75  LYS 75  75  75  LYS LYS O . n 
H 1 76  ASP 76  76  76  ASP ASP O . n 
H 1 77  GLU 77  77  77  GLU GLU O . n 
H 1 78  GLU 78  78  78  GLU GLU O . n 
H 1 79  ARG 79  79  79  ARG ARG O . n 
H 1 80  HIS 80  80  80  HIS HIS O . n 
H 1 81  VAL 81  81  81  VAL VAL O . n 
H 1 82  GLY 82  82  82  GLY GLY O . n 
H 1 83  ASP 83  83  83  ASP ASP O . n 
H 1 84  LEU 84  84  84  LEU LEU O . n 
H 1 85  GLY 85  85  85  GLY GLY O . n 
H 1 86  ASN 86  86  86  ASN ASN O . n 
H 1 87  VAL 87  87  87  VAL VAL O . n 
H 1 88  THR 88  88  88  THR THR O . n 
H 1 89  ALA 89  89  89  ALA ALA O . n 
H 1 90  ASP 90  90  90  ASP ASP O . n 
H 1 91  LYS 91  91  91  LYS LYS O . n 
H 1 92  ASP 92  92  92  ASP ASP O . n 
H 1 93  GLY 93  93  93  GLY GLY O . n 
H 1 94  VAL 94  94  94  VAL VAL O . n 
H 1 95  ALA 95  95  95  ALA ALA O . n 
H 1 96  ASP 96  96  96  ASP ASP O . n 
H 1 97  VAL 97  97  97  VAL VAL O . n 
H 1 98  SER 98  98  98  SER SER O . n 
H 1 99  ILE 99  99  99  ILE ILE O . n 
H 1 100 GLU 100 100 100 GLU GLU O . n 
H 1 101 ASP 101 101 101 ASP ASP O . n 
H 1 102 SER 102 102 102 SER SER O . n 
H 1 103 VAL 103 103 103 VAL VAL O . n 
H 1 104 ILE 104 104 104 ILE ILE O . n 
H 1 105 SER 105 105 105 SER SER O . n 
H 1 106 LEU 106 106 106 LEU LEU O . n 
H 1 107 SER 107 107 107 SER SER O . n 
H 1 108 GLY 108 108 108 GLY GLY O . n 
H 1 109 ASP 109 109 109 ASP ASP O . n 
H 1 110 HIS 110 110 110 HIS HIS O . n 
H 1 111 CYS 111 111 111 CYS CYS O . n 
H 1 112 ILE 112 112 112 ILE ILE O . n 
H 1 113 ILE 113 113 113 ILE ILE O . n 
H 1 114 GLY 114 114 114 GLY GLY O . n 
H 1 115 ARG 115 115 115 ARG ARG O . n 
H 1 116 THR 116 116 116 THR THR O . n 
H 1 117 LEU 117 117 117 LEU LEU O . n 
H 1 118 VAL 118 118 118 VAL VAL O . n 
H 1 119 VAL 119 119 119 VAL VAL O . n 
H 1 120 HIS 120 120 120 HIS HIS O . n 
H 1 121 GLU 121 121 121 GLU GLU O . n 
H 1 122 LYS 122 122 122 LYS LYS O . n 
H 1 123 ALA 123 123 123 ALA ALA O . n 
H 1 124 ASP 124 124 124 ASP ASP O . n 
H 1 125 ASP 125 125 125 ASP ASP O . n 
H 1 126 LEU 126 126 126 LEU LEU O . n 
H 1 127 GLY 127 127 127 GLY GLY O . n 
H 1 128 LYS 128 128 128 LYS LYS O . n 
H 1 129 GLY 129 129 129 GLY GLY O . n 
H 1 130 GLY 130 130 130 GLY GLY O . n 
H 1 131 ASN 131 131 131 ASN ASN O . n 
H 1 132 GLU 132 132 132 GLU GLU O . n 
H 1 133 GLU 133 133 133 GLU GLU O . n 
H 1 134 SER 134 134 134 SER SER O . n 
H 1 135 THR 135 135 135 THR THR O . n 
H 1 136 LYS 136 136 136 LYS LYS O . n 
H 1 137 THR 137 137 137 THR THR O . n 
H 1 138 GLY 138 138 138 GLY GLY O . n 
H 1 139 ASN 139 139 139 ASN ASN O . n 
H 1 140 ALA 140 140 140 ALA ALA O . n 
H 1 141 GLY 141 141 141 GLY GLY O . n 
H 1 142 SER 142 142 142 SER SER O . n 
H 1 143 ARG 143 143 143 ARG ARG O . n 
H 1 144 LEU 144 144 144 LEU LEU O . n 
H 1 145 ALA 145 145 145 ALA ALA O . n 
H 1 146 ALA 146 146 146 ALA ALA O . n 
H 1 147 GLY 147 147 147 GLY GLY O . n 
H 1 148 VAL 148 148 148 VAL VAL O . n 
H 1 149 ILE 149 149 149 ILE ILE O . n 
H 1 150 GLY 150 150 150 GLY GLY O . n 
H 1 151 ILE 151 151 151 ILE ILE O . n 
H 1 152 ALA 152 152 152 ALA ALA O . n 
H 1 153 GLN 153 153 153 GLN GLN O . n 
I 1 1   ALA 1   1   1   ALA ALA Q . n 
I 1 2   THR 2   2   2   THR THR Q . n 
I 1 3   LYS 3   3   3   LYS LYS Q . n 
I 1 4   ALA 4   4   4   ALA ALA Q . n 
I 1 5   VAL 5   5   5   VAL VAL Q . n 
I 1 6   CYS 6   6   6   CYS CYS Q . n 
I 1 7   VAL 7   7   7   VAL VAL Q . n 
I 1 8   LEU 8   8   8   LEU LEU Q . n 
I 1 9   LYS 9   9   9   LYS LYS Q . n 
I 1 10  GLY 10  10  10  GLY GLY Q . n 
I 1 11  ASP 11  11  11  ASP ASP Q . n 
I 1 12  GLY 12  12  12  GLY GLY Q . n 
I 1 13  PRO 13  13  13  PRO PRO Q . n 
I 1 14  VAL 14  14  14  VAL VAL Q . n 
I 1 15  GLN 15  15  15  GLN GLN Q . n 
I 1 16  GLY 16  16  16  GLY GLY Q . n 
I 1 17  ILE 17  17  17  ILE ILE Q . n 
I 1 18  ILE 18  18  18  ILE ILE Q . n 
I 1 19  ASN 19  19  19  ASN ASN Q . n 
I 1 20  PHE 20  20  20  PHE PHE Q . n 
I 1 21  GLU 21  21  21  GLU GLU Q . n 
I 1 22  GLN 22  22  22  GLN GLN Q . n 
I 1 23  LYS 23  23  23  LYS LYS Q . n 
I 1 24  GLU 24  24  24  GLU GLU Q . n 
I 1 25  SER 25  25  25  SER SER Q . n 
I 1 26  ASN 26  26  26  ASN ASN Q . n 
I 1 27  GLY 27  27  27  GLY GLY Q . n 
I 1 28  PRO 28  28  28  PRO PRO Q . n 
I 1 29  VAL 29  29  29  VAL VAL Q . n 
I 1 30  LYS 30  30  30  LYS LYS Q . n 
I 1 31  VAL 31  31  31  VAL VAL Q . n 
I 1 32  TRP 32  32  32  TRP TRP Q . n 
I 1 33  GLY 33  33  33  GLY GLY Q . n 
I 1 34  SER 34  34  34  SER SER Q . n 
I 1 35  ILE 35  35  35  ILE ILE Q . n 
I 1 36  LYS 36  36  36  LYS LYS Q . n 
I 1 37  GLY 37  37  37  GLY GLY Q . n 
I 1 38  LEU 38  38  38  LEU LEU Q . n 
I 1 39  THR 39  39  39  THR THR Q . n 
I 1 40  GLU 40  40  40  GLU GLU Q . n 
I 1 41  GLY 41  41  41  GLY GLY Q . n 
I 1 42  LEU 42  42  42  LEU LEU Q . n 
I 1 43  HIS 43  43  43  HIS HIS Q . n 
I 1 44  GLY 44  44  44  GLY GLY Q . n 
I 1 45  PHE 45  45  45  PHE PHE Q . n 
I 1 46  HIS 46  46  46  HIS HIS Q . n 
I 1 47  VAL 47  47  47  VAL VAL Q . n 
I 1 48  HIS 48  48  48  HIS HIS Q . n 
I 1 49  GLU 49  49  49  GLU GLU Q . n 
I 1 50  PHE 50  50  50  PHE PHE Q . n 
I 1 51  GLY 51  51  51  GLY GLY Q . n 
I 1 52  ASP 52  52  52  ASP ASP Q . n 
I 1 53  ASN 53  53  53  ASN ASN Q . n 
I 1 54  THR 54  54  54  THR THR Q . n 
I 1 55  ALA 55  55  55  ALA ALA Q . n 
I 1 56  GLY 56  56  56  GLY GLY Q . n 
I 1 57  ALA 57  57  57  ALA ALA Q . n 
I 1 58  THR 58  58  58  THR THR Q . n 
I 1 59  SER 59  59  59  SER SER Q . n 
I 1 60  ALA 60  60  60  ALA ALA Q . n 
I 1 61  GLY 61  61  61  GLY GLY Q . n 
I 1 62  PRO 62  62  62  PRO PRO Q . n 
I 1 63  HIS 63  63  63  HIS HIS Q . n 
I 1 64  PHE 64  64  64  PHE PHE Q . n 
I 1 65  ASN 65  65  65  ASN ASN Q . n 
I 1 66  PRO 66  66  66  PRO PRO Q . n 
I 1 67  LEU 67  67  67  LEU LEU Q . n 
I 1 68  SER 68  68  68  SER SER Q . n 
I 1 69  ARG 69  69  69  ARG ARG Q . n 
I 1 70  LYS 70  70  70  LYS LYS Q . n 
I 1 71  HIS 71  71  71  HIS HIS Q . n 
I 1 72  GLY 72  72  72  GLY GLY Q . n 
I 1 73  GLY 73  73  73  GLY GLY Q . n 
I 1 74  PRO 74  74  74  PRO PRO Q . n 
I 1 75  LYS 75  75  75  LYS LYS Q . n 
I 1 76  ASP 76  76  76  ASP ASP Q . n 
I 1 77  GLU 77  77  77  GLU GLU Q . n 
I 1 78  GLU 78  78  78  GLU GLU Q . n 
I 1 79  ARG 79  79  79  ARG ARG Q . n 
I 1 80  HIS 80  80  80  HIS HIS Q . n 
I 1 81  VAL 81  81  81  VAL VAL Q . n 
I 1 82  GLY 82  82  82  GLY GLY Q . n 
I 1 83  ASP 83  83  83  ASP ASP Q . n 
I 1 84  LEU 84  84  84  LEU LEU Q . n 
I 1 85  GLY 85  85  85  GLY GLY Q . n 
I 1 86  ASN 86  86  86  ASN ASN Q . n 
I 1 87  VAL 87  87  87  VAL VAL Q . n 
I 1 88  THR 88  88  88  THR THR Q . n 
I 1 89  ALA 89  89  89  ALA ALA Q . n 
I 1 90  ASP 90  90  90  ASP ASP Q . n 
I 1 91  LYS 91  91  91  LYS LYS Q . n 
I 1 92  ASP 92  92  92  ASP ASP Q . n 
I 1 93  GLY 93  93  93  GLY GLY Q . n 
I 1 94  VAL 94  94  94  VAL VAL Q . n 
I 1 95  ALA 95  95  95  ALA ALA Q . n 
I 1 96  ASP 96  96  96  ASP ASP Q . n 
I 1 97  VAL 97  97  97  VAL VAL Q . n 
I 1 98  SER 98  98  98  SER SER Q . n 
I 1 99  ILE 99  99  99  ILE ILE Q . n 
I 1 100 GLU 100 100 100 GLU GLU Q . n 
I 1 101 ASP 101 101 101 ASP ASP Q . n 
I 1 102 SER 102 102 102 SER SER Q . n 
I 1 103 VAL 103 103 103 VAL VAL Q . n 
I 1 104 ILE 104 104 104 ILE ILE Q . n 
I 1 105 SER 105 105 105 SER SER Q . n 
I 1 106 LEU 106 106 106 LEU LEU Q . n 
I 1 107 SER 107 107 107 SER SER Q . n 
I 1 108 GLY 108 108 108 GLY GLY Q . n 
I 1 109 ASP 109 109 109 ASP ASP Q . n 
I 1 110 HIS 110 110 110 HIS HIS Q . n 
I 1 111 CYS 111 111 111 CYS CYS Q . n 
I 1 112 ILE 112 112 112 ILE ILE Q . n 
I 1 113 ILE 113 113 113 ILE ILE Q . n 
I 1 114 GLY 114 114 114 GLY GLY Q . n 
I 1 115 ARG 115 115 115 ARG ARG Q . n 
I 1 116 THR 116 116 116 THR THR Q . n 
I 1 117 LEU 117 117 117 LEU LEU Q . n 
I 1 118 VAL 118 118 118 VAL VAL Q . n 
I 1 119 VAL 119 119 119 VAL VAL Q . n 
I 1 120 HIS 120 120 120 HIS HIS Q . n 
I 1 121 GLU 121 121 121 GLU GLU Q . n 
I 1 122 LYS 122 122 122 LYS LYS Q . n 
I 1 123 ALA 123 123 123 ALA ALA Q . n 
I 1 124 ASP 124 124 124 ASP ASP Q . n 
I 1 125 ASP 125 125 125 ASP ASP Q . n 
I 1 126 LEU 126 126 126 LEU LEU Q . n 
I 1 127 GLY 127 127 127 GLY GLY Q . n 
I 1 128 LYS 128 128 128 LYS LYS Q . n 
I 1 129 GLY 129 129 129 GLY GLY Q . n 
I 1 130 GLY 130 130 130 GLY GLY Q . n 
I 1 131 ASN 131 131 131 ASN ASN Q . n 
I 1 132 GLU 132 132 132 GLU GLU Q . n 
I 1 133 GLU 133 133 133 GLU GLU Q . n 
I 1 134 SER 134 134 134 SER SER Q . n 
I 1 135 THR 135 135 135 THR THR Q . n 
I 1 136 LYS 136 136 136 LYS LYS Q . n 
I 1 137 THR 137 137 137 THR THR Q . n 
I 1 138 GLY 138 138 138 GLY GLY Q . n 
I 1 139 ASN 139 139 139 ASN ASN Q . n 
I 1 140 ALA 140 140 140 ALA ALA Q . n 
I 1 141 GLY 141 141 141 GLY GLY Q . n 
I 1 142 SER 142 142 142 SER SER Q . n 
I 1 143 ARG 143 143 143 ARG ARG Q . n 
I 1 144 LEU 144 144 144 LEU LEU Q . n 
I 1 145 ALA 145 145 145 ALA ALA Q . n 
I 1 146 ALA 146 146 146 ALA ALA Q . n 
I 1 147 GLY 147 147 147 GLY GLY Q . n 
I 1 148 VAL 148 148 148 VAL VAL Q . n 
I 1 149 ILE 149 149 149 ILE ILE Q . n 
I 1 150 GLY 150 150 150 GLY GLY Q . n 
I 1 151 ILE 151 151 151 ILE ILE Q . n 
I 1 152 ALA 152 152 152 ALA ALA Q . n 
I 1 153 GLN 153 153 153 GLN GLN Q . n 
J 1 1   ALA 1   1   1   ALA ALA S . n 
J 1 2   THR 2   2   2   THR THR S . n 
J 1 3   LYS 3   3   3   LYS LYS S . n 
J 1 4   ALA 4   4   4   ALA ALA S . n 
J 1 5   VAL 5   5   5   VAL VAL S . n 
J 1 6   CYS 6   6   6   CYS CYS S . n 
J 1 7   VAL 7   7   7   VAL VAL S . n 
J 1 8   LEU 8   8   8   LEU LEU S . n 
J 1 9   LYS 9   9   9   LYS LYS S . n 
J 1 10  GLY 10  10  10  GLY GLY S . n 
J 1 11  ASP 11  11  11  ASP ASP S . n 
J 1 12  GLY 12  12  12  GLY GLY S . n 
J 1 13  PRO 13  13  13  PRO PRO S . n 
J 1 14  VAL 14  14  14  VAL VAL S . n 
J 1 15  GLN 15  15  15  GLN GLN S . n 
J 1 16  GLY 16  16  16  GLY GLY S . n 
J 1 17  ILE 17  17  17  ILE ILE S . n 
J 1 18  ILE 18  18  18  ILE ILE S . n 
J 1 19  ASN 19  19  19  ASN ASN S . n 
J 1 20  PHE 20  20  20  PHE PHE S . n 
J 1 21  GLU 21  21  21  GLU GLU S . n 
J 1 22  GLN 22  22  22  GLN GLN S . n 
J 1 23  LYS 23  23  23  LYS LYS S . n 
J 1 24  GLU 24  24  24  GLU GLU S . n 
J 1 25  SER 25  25  25  SER SER S . n 
J 1 26  ASN 26  26  26  ASN ASN S . n 
J 1 27  GLY 27  27  27  GLY GLY S . n 
J 1 28  PRO 28  28  28  PRO PRO S . n 
J 1 29  VAL 29  29  29  VAL VAL S . n 
J 1 30  LYS 30  30  30  LYS LYS S . n 
J 1 31  VAL 31  31  31  VAL VAL S . n 
J 1 32  TRP 32  32  32  TRP TRP S . n 
J 1 33  GLY 33  33  33  GLY GLY S . n 
J 1 34  SER 34  34  34  SER SER S . n 
J 1 35  ILE 35  35  35  ILE ILE S . n 
J 1 36  LYS 36  36  36  LYS LYS S . n 
J 1 37  GLY 37  37  37  GLY GLY S . n 
J 1 38  LEU 38  38  38  LEU LEU S . n 
J 1 39  THR 39  39  39  THR THR S . n 
J 1 40  GLU 40  40  40  GLU GLU S . n 
J 1 41  GLY 41  41  41  GLY GLY S . n 
J 1 42  LEU 42  42  42  LEU LEU S . n 
J 1 43  HIS 43  43  43  HIS HIS S . n 
J 1 44  GLY 44  44  44  GLY GLY S . n 
J 1 45  PHE 45  45  45  PHE PHE S . n 
J 1 46  HIS 46  46  46  HIS HIS S . n 
J 1 47  VAL 47  47  47  VAL VAL S . n 
J 1 48  HIS 48  48  48  HIS HIS S . n 
J 1 49  GLU 49  49  49  GLU GLU S . n 
J 1 50  PHE 50  50  50  PHE PHE S . n 
J 1 51  GLY 51  51  51  GLY GLY S . n 
J 1 52  ASP 52  52  52  ASP ASP S . n 
J 1 53  ASN 53  53  53  ASN ASN S . n 
J 1 54  THR 54  54  54  THR THR S . n 
J 1 55  ALA 55  55  55  ALA ALA S . n 
J 1 56  GLY 56  56  56  GLY GLY S . n 
J 1 57  ALA 57  57  57  ALA ALA S . n 
J 1 58  THR 58  58  58  THR THR S . n 
J 1 59  SER 59  59  59  SER SER S . n 
J 1 60  ALA 60  60  60  ALA ALA S . n 
J 1 61  GLY 61  61  61  GLY GLY S . n 
J 1 62  PRO 62  62  62  PRO PRO S . n 
J 1 63  HIS 63  63  63  HIS HIS S . n 
J 1 64  PHE 64  64  64  PHE PHE S . n 
J 1 65  ASN 65  65  65  ASN ASN S . n 
J 1 66  PRO 66  66  66  PRO PRO S . n 
J 1 67  LEU 67  67  67  LEU LEU S . n 
J 1 68  SER 68  68  68  SER SER S . n 
J 1 69  ARG 69  69  69  ARG ARG S . n 
J 1 70  LYS 70  70  70  LYS LYS S . n 
J 1 71  HIS 71  71  71  HIS HIS S . n 
J 1 72  GLY 72  72  72  GLY GLY S . n 
J 1 73  GLY 73  73  73  GLY GLY S . n 
J 1 74  PRO 74  74  74  PRO PRO S . n 
J 1 75  LYS 75  75  75  LYS LYS S . n 
J 1 76  ASP 76  76  76  ASP ASP S . n 
J 1 77  GLU 77  77  77  GLU GLU S . n 
J 1 78  GLU 78  78  78  GLU GLU S . n 
J 1 79  ARG 79  79  79  ARG ARG S . n 
J 1 80  HIS 80  80  80  HIS HIS S . n 
J 1 81  VAL 81  81  81  VAL VAL S . n 
J 1 82  GLY 82  82  82  GLY GLY S . n 
J 1 83  ASP 83  83  83  ASP ASP S . n 
J 1 84  LEU 84  84  84  LEU LEU S . n 
J 1 85  GLY 85  85  85  GLY GLY S . n 
J 1 86  ASN 86  86  86  ASN ASN S . n 
J 1 87  VAL 87  87  87  VAL VAL S . n 
J 1 88  THR 88  88  88  THR THR S . n 
J 1 89  ALA 89  89  89  ALA ALA S . n 
J 1 90  ASP 90  90  90  ASP ASP S . n 
J 1 91  LYS 91  91  91  LYS LYS S . n 
J 1 92  ASP 92  92  92  ASP ASP S . n 
J 1 93  GLY 93  93  93  GLY GLY S . n 
J 1 94  VAL 94  94  94  VAL VAL S . n 
J 1 95  ALA 95  95  95  ALA ALA S . n 
J 1 96  ASP 96  96  96  ASP ASP S . n 
J 1 97  VAL 97  97  97  VAL VAL S . n 
J 1 98  SER 98  98  98  SER SER S . n 
J 1 99  ILE 99  99  99  ILE ILE S . n 
J 1 100 GLU 100 100 100 GLU GLU S . n 
J 1 101 ASP 101 101 101 ASP ASP S . n 
J 1 102 SER 102 102 102 SER SER S . n 
J 1 103 VAL 103 103 103 VAL VAL S . n 
J 1 104 ILE 104 104 104 ILE ILE S . n 
J 1 105 SER 105 105 105 SER SER S . n 
J 1 106 LEU 106 106 106 LEU LEU S . n 
J 1 107 SER 107 107 107 SER SER S . n 
J 1 108 GLY 108 108 108 GLY GLY S . n 
J 1 109 ASP 109 109 109 ASP ASP S . n 
J 1 110 HIS 110 110 110 HIS HIS S . n 
J 1 111 CYS 111 111 111 CYS CYS S . n 
J 1 112 ILE 112 112 112 ILE ILE S . n 
J 1 113 ILE 113 113 113 ILE ILE S . n 
J 1 114 GLY 114 114 114 GLY GLY S . n 
J 1 115 ARG 115 115 115 ARG ARG S . n 
J 1 116 THR 116 116 116 THR THR S . n 
J 1 117 LEU 117 117 117 LEU LEU S . n 
J 1 118 VAL 118 118 118 VAL VAL S . n 
J 1 119 VAL 119 119 119 VAL VAL S . n 
J 1 120 HIS 120 120 120 HIS HIS S . n 
J 1 121 GLU 121 121 121 GLU GLU S . n 
J 1 122 LYS 122 122 122 LYS LYS S . n 
J 1 123 ALA 123 123 123 ALA ALA S . n 
J 1 124 ASP 124 124 124 ASP ASP S . n 
J 1 125 ASP 125 125 125 ASP ASP S . n 
J 1 126 LEU 126 126 126 LEU LEU S . n 
J 1 127 GLY 127 127 127 GLY GLY S . n 
J 1 128 LYS 128 128 128 LYS LYS S . n 
J 1 129 GLY 129 129 129 GLY GLY S . n 
J 1 130 GLY 130 130 130 GLY GLY S . n 
J 1 131 ASN 131 131 131 ASN ASN S . n 
J 1 132 GLU 132 132 132 GLU GLU S . n 
J 1 133 GLU 133 133 133 GLU GLU S . n 
J 1 134 SER 134 134 134 SER SER S . n 
J 1 135 THR 135 135 135 THR THR S . n 
J 1 136 LYS 136 136 136 LYS LYS S . n 
J 1 137 THR 137 137 137 THR THR S . n 
J 1 138 GLY 138 138 138 GLY GLY S . n 
J 1 139 ASN 139 139 139 ASN ASN S . n 
J 1 140 ALA 140 140 140 ALA ALA S . n 
J 1 141 GLY 141 141 141 GLY GLY S . n 
J 1 142 SER 142 142 142 SER SER S . n 
J 1 143 ARG 143 143 143 ARG ARG S . n 
J 1 144 LEU 144 144 144 LEU LEU S . n 
J 1 145 ALA 145 145 145 ALA ALA S . n 
J 1 146 ALA 146 146 146 ALA ALA S . n 
J 1 147 GLY 147 147 147 GLY GLY S . n 
J 1 148 VAL 148 148 148 VAL VAL S . n 
J 1 149 ILE 149 149 149 ILE ILE S . n 
J 1 150 GLY 150 150 150 GLY GLY S . n 
J 1 151 ILE 151 151 151 ILE ILE S . n 
J 1 152 ALA 152 152 152 ALA ALA S . n 
J 1 153 GLN 153 153 153 GLN GLN S . n 
K 1 1   ALA 1   1   1   ALA ALA U . n 
K 1 2   THR 2   2   2   THR THR U . n 
K 1 3   LYS 3   3   3   LYS LYS U . n 
K 1 4   ALA 4   4   4   ALA ALA U . n 
K 1 5   VAL 5   5   5   VAL VAL U . n 
K 1 6   CYS 6   6   6   CYS CYS U . n 
K 1 7   VAL 7   7   7   VAL VAL U . n 
K 1 8   LEU 8   8   8   LEU LEU U . n 
K 1 9   LYS 9   9   9   LYS LYS U . n 
K 1 10  GLY 10  10  10  GLY GLY U . n 
K 1 11  ASP 11  11  11  ASP ASP U . n 
K 1 12  GLY 12  12  12  GLY GLY U . n 
K 1 13  PRO 13  13  13  PRO PRO U . n 
K 1 14  VAL 14  14  14  VAL VAL U . n 
K 1 15  GLN 15  15  15  GLN GLN U . n 
K 1 16  GLY 16  16  16  GLY GLY U . n 
K 1 17  ILE 17  17  17  ILE ILE U . n 
K 1 18  ILE 18  18  18  ILE ILE U . n 
K 1 19  ASN 19  19  19  ASN ASN U . n 
K 1 20  PHE 20  20  20  PHE PHE U . n 
K 1 21  GLU 21  21  21  GLU GLU U . n 
K 1 22  GLN 22  22  22  GLN GLN U . n 
K 1 23  LYS 23  23  23  LYS LYS U . n 
K 1 24  GLU 24  24  24  GLU GLU U . n 
K 1 25  SER 25  25  25  SER SER U . n 
K 1 26  ASN 26  26  26  ASN ASN U . n 
K 1 27  GLY 27  27  27  GLY GLY U . n 
K 1 28  PRO 28  28  28  PRO PRO U . n 
K 1 29  VAL 29  29  29  VAL VAL U . n 
K 1 30  LYS 30  30  30  LYS LYS U . n 
K 1 31  VAL 31  31  31  VAL VAL U . n 
K 1 32  TRP 32  32  32  TRP TRP U . n 
K 1 33  GLY 33  33  33  GLY GLY U . n 
K 1 34  SER 34  34  34  SER SER U . n 
K 1 35  ILE 35  35  35  ILE ILE U . n 
K 1 36  LYS 36  36  36  LYS LYS U . n 
K 1 37  GLY 37  37  37  GLY GLY U . n 
K 1 38  LEU 38  38  38  LEU LEU U . n 
K 1 39  THR 39  39  39  THR THR U . n 
K 1 40  GLU 40  40  40  GLU GLU U . n 
K 1 41  GLY 41  41  41  GLY GLY U . n 
K 1 42  LEU 42  42  42  LEU LEU U . n 
K 1 43  HIS 43  43  43  HIS HIS U . n 
K 1 44  GLY 44  44  44  GLY GLY U . n 
K 1 45  PHE 45  45  45  PHE PHE U . n 
K 1 46  HIS 46  46  46  HIS HIS U . n 
K 1 47  VAL 47  47  47  VAL VAL U . n 
K 1 48  HIS 48  48  48  HIS HIS U . n 
K 1 49  GLU 49  49  49  GLU GLU U . n 
K 1 50  PHE 50  50  50  PHE PHE U . n 
K 1 51  GLY 51  51  51  GLY GLY U . n 
K 1 52  ASP 52  52  52  ASP ASP U . n 
K 1 53  ASN 53  53  53  ASN ASN U . n 
K 1 54  THR 54  54  54  THR THR U . n 
K 1 55  ALA 55  55  55  ALA ALA U . n 
K 1 56  GLY 56  56  56  GLY GLY U . n 
K 1 57  ALA 57  57  57  ALA ALA U . n 
K 1 58  THR 58  58  58  THR THR U . n 
K 1 59  SER 59  59  59  SER SER U . n 
K 1 60  ALA 60  60  60  ALA ALA U . n 
K 1 61  GLY 61  61  61  GLY GLY U . n 
K 1 62  PRO 62  62  62  PRO PRO U . n 
K 1 63  HIS 63  63  63  HIS HIS U . n 
K 1 64  PHE 64  64  64  PHE PHE U . n 
K 1 65  ASN 65  65  65  ASN ASN U . n 
K 1 66  PRO 66  66  66  PRO PRO U . n 
K 1 67  LEU 67  67  67  LEU LEU U . n 
K 1 68  SER 68  68  68  SER SER U . n 
K 1 69  ARG 69  69  69  ARG ARG U . n 
K 1 70  LYS 70  70  70  LYS LYS U . n 
K 1 71  HIS 71  71  71  HIS HIS U . n 
K 1 72  GLY 72  72  72  GLY GLY U . n 
K 1 73  GLY 73  73  73  GLY GLY U . n 
K 1 74  PRO 74  74  74  PRO PRO U . n 
K 1 75  LYS 75  75  75  LYS LYS U . n 
K 1 76  ASP 76  76  76  ASP ASP U . n 
K 1 77  GLU 77  77  77  GLU GLU U . n 
K 1 78  GLU 78  78  78  GLU GLU U . n 
K 1 79  ARG 79  79  79  ARG ARG U . n 
K 1 80  HIS 80  80  80  HIS HIS U . n 
K 1 81  VAL 81  81  81  VAL VAL U . n 
K 1 82  GLY 82  82  82  GLY GLY U . n 
K 1 83  ASP 83  83  83  ASP ASP U . n 
K 1 84  LEU 84  84  84  LEU LEU U . n 
K 1 85  GLY 85  85  85  GLY GLY U . n 
K 1 86  ASN 86  86  86  ASN ASN U . n 
K 1 87  VAL 87  87  87  VAL VAL U . n 
K 1 88  THR 88  88  88  THR THR U . n 
K 1 89  ALA 89  89  89  ALA ALA U . n 
K 1 90  ASP 90  90  90  ASP ASP U . n 
K 1 91  LYS 91  91  91  LYS LYS U . n 
K 1 92  ASP 92  92  92  ASP ASP U . n 
K 1 93  GLY 93  93  93  GLY GLY U . n 
K 1 94  VAL 94  94  94  VAL VAL U . n 
K 1 95  ALA 95  95  95  ALA ALA U . n 
K 1 96  ASP 96  96  96  ASP ASP U . n 
K 1 97  VAL 97  97  97  VAL VAL U . n 
K 1 98  SER 98  98  98  SER SER U . n 
K 1 99  ILE 99  99  99  ILE ILE U . n 
K 1 100 GLU 100 100 100 GLU GLU U . n 
K 1 101 ASP 101 101 101 ASP ASP U . n 
K 1 102 SER 102 102 102 SER SER U . n 
K 1 103 VAL 103 103 103 VAL VAL U . n 
K 1 104 ILE 104 104 104 ILE ILE U . n 
K 1 105 SER 105 105 105 SER SER U . n 
K 1 106 LEU 106 106 106 LEU LEU U . n 
K 1 107 SER 107 107 107 SER SER U . n 
K 1 108 GLY 108 108 108 GLY GLY U . n 
K 1 109 ASP 109 109 109 ASP ASP U . n 
K 1 110 HIS 110 110 110 HIS HIS U . n 
K 1 111 CYS 111 111 111 CYS CYS U . n 
K 1 112 ILE 112 112 112 ILE ILE U . n 
K 1 113 ILE 113 113 113 ILE ILE U . n 
K 1 114 GLY 114 114 114 GLY GLY U . n 
K 1 115 ARG 115 115 115 ARG ARG U . n 
K 1 116 THR 116 116 116 THR THR U . n 
K 1 117 LEU 117 117 117 LEU LEU U . n 
K 1 118 VAL 118 118 118 VAL VAL U . n 
K 1 119 VAL 119 119 119 VAL VAL U . n 
K 1 120 HIS 120 120 120 HIS HIS U . n 
K 1 121 GLU 121 121 121 GLU GLU U . n 
K 1 122 LYS 122 122 122 LYS LYS U . n 
K 1 123 ALA 123 123 123 ALA ALA U . n 
K 1 124 ASP 124 124 124 ASP ASP U . n 
K 1 125 ASP 125 125 125 ASP ASP U . n 
K 1 126 LEU 126 126 126 LEU LEU U . n 
K 1 127 GLY 127 127 127 GLY GLY U . n 
K 1 128 LYS 128 128 128 LYS LYS U . n 
K 1 129 GLY 129 129 129 GLY GLY U . n 
K 1 130 GLY 130 130 130 GLY GLY U . n 
K 1 131 ASN 131 131 131 ASN ASN U . n 
K 1 132 GLU 132 132 132 GLU GLU U . n 
K 1 133 GLU 133 133 133 GLU GLU U . n 
K 1 134 SER 134 134 134 SER SER U . n 
K 1 135 THR 135 135 135 THR THR U . n 
K 1 136 LYS 136 136 136 LYS LYS U . n 
K 1 137 THR 137 137 137 THR THR U . n 
K 1 138 GLY 138 138 138 GLY GLY U . n 
K 1 139 ASN 139 139 139 ASN ASN U . n 
K 1 140 ALA 140 140 140 ALA ALA U . n 
K 1 141 GLY 141 141 141 GLY GLY U . n 
K 1 142 SER 142 142 142 SER SER U . n 
K 1 143 ARG 143 143 143 ARG ARG U . n 
K 1 144 LEU 144 144 144 LEU LEU U . n 
K 1 145 ALA 145 145 145 ALA ALA U . n 
K 1 146 ALA 146 146 146 ALA ALA U . n 
K 1 147 GLY 147 147 147 GLY GLY U . n 
K 1 148 VAL 148 148 148 VAL VAL U . n 
K 1 149 ILE 149 149 149 ILE ILE U . n 
K 1 150 GLY 150 150 150 GLY GLY U . n 
K 1 151 ILE 151 151 151 ILE ILE U . n 
K 1 152 ALA 152 152 152 ALA ALA U . n 
K 1 153 GLN 153 153 153 GLN GLN U . n 
L 1 1   ALA 1   1   ?   ?   ?   W . n 
L 1 2   THR 2   2   2   THR THR W . n 
L 1 3   LYS 3   3   3   LYS LYS W . n 
L 1 4   ALA 4   4   4   ALA ALA W . n 
L 1 5   VAL 5   5   5   VAL VAL W . n 
L 1 6   CYS 6   6   6   CYS CYS W . n 
L 1 7   VAL 7   7   7   VAL VAL W . n 
L 1 8   LEU 8   8   8   LEU LEU W . n 
L 1 9   LYS 9   9   9   LYS LYS W . n 
L 1 10  GLY 10  10  10  GLY GLY W . n 
L 1 11  ASP 11  11  11  ASP ASP W . n 
L 1 12  GLY 12  12  12  GLY GLY W . n 
L 1 13  PRO 13  13  13  PRO PRO W . n 
L 1 14  VAL 14  14  14  VAL VAL W . n 
L 1 15  GLN 15  15  15  GLN GLN W . n 
L 1 16  GLY 16  16  16  GLY GLY W . n 
L 1 17  ILE 17  17  17  ILE ILE W . n 
L 1 18  ILE 18  18  18  ILE ILE W . n 
L 1 19  ASN 19  19  19  ASN ASN W . n 
L 1 20  PHE 20  20  20  PHE PHE W . n 
L 1 21  GLU 21  21  21  GLU GLU W . n 
L 1 22  GLN 22  22  22  GLN GLN W . n 
L 1 23  LYS 23  23  23  LYS LYS W . n 
L 1 24  GLU 24  24  24  GLU GLU W . n 
L 1 25  SER 25  25  25  SER SER W . n 
L 1 26  ASN 26  26  26  ASN ASN W . n 
L 1 27  GLY 27  27  27  GLY GLY W . n 
L 1 28  PRO 28  28  28  PRO PRO W . n 
L 1 29  VAL 29  29  29  VAL VAL W . n 
L 1 30  LYS 30  30  30  LYS LYS W . n 
L 1 31  VAL 31  31  31  VAL VAL W . n 
L 1 32  TRP 32  32  32  TRP TRP W . n 
L 1 33  GLY 33  33  33  GLY GLY W . n 
L 1 34  SER 34  34  34  SER SER W . n 
L 1 35  ILE 35  35  35  ILE ILE W . n 
L 1 36  LYS 36  36  36  LYS LYS W . n 
L 1 37  GLY 37  37  37  GLY GLY W . n 
L 1 38  LEU 38  38  38  LEU LEU W . n 
L 1 39  THR 39  39  39  THR THR W . n 
L 1 40  GLU 40  40  40  GLU GLU W . n 
L 1 41  GLY 41  41  41  GLY GLY W . n 
L 1 42  LEU 42  42  42  LEU LEU W . n 
L 1 43  HIS 43  43  43  HIS HIS W . n 
L 1 44  GLY 44  44  44  GLY GLY W . n 
L 1 45  PHE 45  45  45  PHE PHE W . n 
L 1 46  HIS 46  46  46  HIS HIS W . n 
L 1 47  VAL 47  47  47  VAL VAL W . n 
L 1 48  HIS 48  48  48  HIS HIS W . n 
L 1 49  GLU 49  49  49  GLU GLU W . n 
L 1 50  PHE 50  50  50  PHE PHE W . n 
L 1 51  GLY 51  51  51  GLY GLY W . n 
L 1 52  ASP 52  52  52  ASP ASP W . n 
L 1 53  ASN 53  53  53  ASN ASN W . n 
L 1 54  THR 54  54  54  THR THR W . n 
L 1 55  ALA 55  55  55  ALA ALA W . n 
L 1 56  GLY 56  56  56  GLY GLY W . n 
L 1 57  ALA 57  57  57  ALA ALA W . n 
L 1 58  THR 58  58  58  THR THR W . n 
L 1 59  SER 59  59  59  SER SER W . n 
L 1 60  ALA 60  60  60  ALA ALA W . n 
L 1 61  GLY 61  61  61  GLY GLY W . n 
L 1 62  PRO 62  62  62  PRO PRO W . n 
L 1 63  HIS 63  63  63  HIS HIS W . n 
L 1 64  PHE 64  64  64  PHE PHE W . n 
L 1 65  ASN 65  65  65  ASN ASN W . n 
L 1 66  PRO 66  66  66  PRO PRO W . n 
L 1 67  LEU 67  67  67  LEU LEU W . n 
L 1 68  SER 68  68  68  SER SER W . n 
L 1 69  ARG 69  69  69  ARG ARG W . n 
L 1 70  LYS 70  70  70  LYS LYS W . n 
L 1 71  HIS 71  71  71  HIS HIS W . n 
L 1 72  GLY 72  72  72  GLY GLY W . n 
L 1 73  GLY 73  73  73  GLY GLY W . n 
L 1 74  PRO 74  74  74  PRO PRO W . n 
L 1 75  LYS 75  75  75  LYS LYS W . n 
L 1 76  ASP 76  76  76  ASP ASP W . n 
L 1 77  GLU 77  77  77  GLU GLU W . n 
L 1 78  GLU 78  78  78  GLU GLU W . n 
L 1 79  ARG 79  79  79  ARG ARG W . n 
L 1 80  HIS 80  80  80  HIS HIS W . n 
L 1 81  VAL 81  81  81  VAL VAL W . n 
L 1 82  GLY 82  82  82  GLY GLY W . n 
L 1 83  ASP 83  83  83  ASP ASP W . n 
L 1 84  LEU 84  84  84  LEU LEU W . n 
L 1 85  GLY 85  85  85  GLY GLY W . n 
L 1 86  ASN 86  86  86  ASN ASN W . n 
L 1 87  VAL 87  87  87  VAL VAL W . n 
L 1 88  THR 88  88  88  THR THR W . n 
L 1 89  ALA 89  89  89  ALA ALA W . n 
L 1 90  ASP 90  90  90  ASP ASP W . n 
L 1 91  LYS 91  91  91  LYS LYS W . n 
L 1 92  ASP 92  92  92  ASP ASP W . n 
L 1 93  GLY 93  93  93  GLY GLY W . n 
L 1 94  VAL 94  94  94  VAL VAL W . n 
L 1 95  ALA 95  95  95  ALA ALA W . n 
L 1 96  ASP 96  96  96  ASP ASP W . n 
L 1 97  VAL 97  97  97  VAL VAL W . n 
L 1 98  SER 98  98  98  SER SER W . n 
L 1 99  ILE 99  99  99  ILE ILE W . n 
L 1 100 GLU 100 100 100 GLU GLU W . n 
L 1 101 ASP 101 101 101 ASP ASP W . n 
L 1 102 SER 102 102 102 SER SER W . n 
L 1 103 VAL 103 103 103 VAL VAL W . n 
L 1 104 ILE 104 104 104 ILE ILE W . n 
L 1 105 SER 105 105 105 SER SER W . n 
L 1 106 LEU 106 106 106 LEU LEU W . n 
L 1 107 SER 107 107 107 SER SER W . n 
L 1 108 GLY 108 108 108 GLY GLY W . n 
L 1 109 ASP 109 109 109 ASP ASP W . n 
L 1 110 HIS 110 110 110 HIS HIS W . n 
L 1 111 CYS 111 111 111 CYS CYS W . n 
L 1 112 ILE 112 112 112 ILE ILE W . n 
L 1 113 ILE 113 113 113 ILE ILE W . n 
L 1 114 GLY 114 114 114 GLY GLY W . n 
L 1 115 ARG 115 115 115 ARG ARG W . n 
L 1 116 THR 116 116 116 THR THR W . n 
L 1 117 LEU 117 117 117 LEU LEU W . n 
L 1 118 VAL 118 118 118 VAL VAL W . n 
L 1 119 VAL 119 119 119 VAL VAL W . n 
L 1 120 HIS 120 120 120 HIS HIS W . n 
L 1 121 GLU 121 121 121 GLU GLU W . n 
L 1 122 LYS 122 122 122 LYS LYS W . n 
L 1 123 ALA 123 123 123 ALA ALA W . n 
L 1 124 ASP 124 124 124 ASP ASP W . n 
L 1 125 ASP 125 125 125 ASP ASP W . n 
L 1 126 LEU 126 126 126 LEU LEU W . n 
L 1 127 GLY 127 127 127 GLY GLY W . n 
L 1 128 LYS 128 128 128 LYS LYS W . n 
L 1 129 GLY 129 129 129 GLY GLY W . n 
L 1 130 GLY 130 130 130 GLY GLY W . n 
L 1 131 ASN 131 131 131 ASN ASN W . n 
L 1 132 GLU 132 132 132 GLU GLU W . n 
L 1 133 GLU 133 133 133 GLU GLU W . n 
L 1 134 SER 134 134 134 SER SER W . n 
L 1 135 THR 135 135 135 THR THR W . n 
L 1 136 LYS 136 136 136 LYS LYS W . n 
L 1 137 THR 137 137 137 THR THR W . n 
L 1 138 GLY 138 138 138 GLY GLY W . n 
L 1 139 ASN 139 139 139 ASN ASN W . n 
L 1 140 ALA 140 140 140 ALA ALA W . n 
L 1 141 GLY 141 141 141 GLY GLY W . n 
L 1 142 SER 142 142 142 SER SER W . n 
L 1 143 ARG 143 143 143 ARG ARG W . n 
L 1 144 LEU 144 144 144 LEU LEU W . n 
L 1 145 ALA 145 145 145 ALA ALA W . n 
L 1 146 ALA 146 146 146 ALA ALA W . n 
L 1 147 GLY 147 147 147 GLY GLY W . n 
L 1 148 VAL 148 148 148 VAL VAL W . n 
L 1 149 ILE 149 149 149 ILE ILE W . n 
L 1 150 GLY 150 150 150 GLY GLY W . n 
L 1 151 ILE 151 151 151 ILE ILE W . n 
L 1 152 ALA 152 152 152 ALA ALA W . n 
L 1 153 GLN 153 153 153 GLN GLN W . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  2 ZN  1   201 155  ZN  ZN  A . 
N  3 SO4 1   202 156  SO4 SO4 A . 
O  2 ZN  1   201 155  ZN  ZN  F . 
P  3 SO4 1   202 156  SO4 SO4 F . 
Q  3 SO4 1   203 1    SO4 SO4 F . 
R  2 ZN  1   201 155  ZN  ZN  D . 
S  3 SO4 1   202 156  SO4 SO4 D . 
T  2 ZN  1   201 155  ZN  ZN  G . 
U  3 SO4 1   202 156  SO4 SO4 G . 
V  2 ZN  1   201 155  ZN  ZN  I . 
W  3 SO4 1   202 156  SO4 SO4 I . 
X  2 ZN  1   201 155  ZN  ZN  K . 
Y  3 SO4 1   202 156  SO4 SO4 K . 
Z  2 ZN  1   201 155  ZN  ZN  M . 
AA 3 SO4 1   202 156  SO4 SO4 M . 
BA 2 ZN  1   201 155  ZN  ZN  O . 
CA 2 ZN  1   201 155  ZN  ZN  Q . 
DA 3 SO4 1   202 156  SO4 SO4 Q . 
EA 3 SO4 1   203 2    SO4 SO4 Q . 
FA 2 ZN  1   201 155  ZN  ZN  S . 
GA 3 SO4 1   202 156  SO4 SO4 S . 
HA 2 ZN  1   201 155  ZN  ZN  U . 
IA 3 SO4 1   202 156  SO4 SO4 U . 
JA 2 ZN  1   201 155  ZN  ZN  W . 
KA 3 SO4 1   202 1    SO4 SO4 W . 
LA 4 HOH 1   301 536  HOH HOH A . 
LA 4 HOH 2   302 910  HOH HOH A . 
LA 4 HOH 3   303 1123 HOH HOH A . 
LA 4 HOH 4   304 1114 HOH HOH A . 
LA 4 HOH 5   305 168  HOH HOH A . 
LA 4 HOH 6   306 142  HOH HOH A . 
LA 4 HOH 7   307 152  HOH HOH A . 
LA 4 HOH 8   308 1226 HOH HOH A . 
LA 4 HOH 9   309 942  HOH HOH A . 
LA 4 HOH 10  310 471  HOH HOH A . 
LA 4 HOH 11  311 291  HOH HOH A . 
LA 4 HOH 12  312 30   HOH HOH A . 
LA 4 HOH 13  313 1227 HOH HOH A . 
LA 4 HOH 14  314 276  HOH HOH A . 
LA 4 HOH 15  315 1121 HOH HOH A . 
LA 4 HOH 16  316 1000 HOH HOH A . 
LA 4 HOH 17  317 191  HOH HOH A . 
LA 4 HOH 18  318 949  HOH HOH A . 
LA 4 HOH 19  319 1020 HOH HOH A . 
LA 4 HOH 20  320 525  HOH HOH A . 
LA 4 HOH 21  321 647  HOH HOH A . 
LA 4 HOH 22  322 164  HOH HOH A . 
LA 4 HOH 23  323 33   HOH HOH A . 
LA 4 HOH 24  324 11   HOH HOH A . 
LA 4 HOH 25  325 1169 HOH HOH A . 
LA 4 HOH 26  326 498  HOH HOH A . 
LA 4 HOH 27  327 475  HOH HOH A . 
LA 4 HOH 28  328 447  HOH HOH A . 
LA 4 HOH 29  329 494  HOH HOH A . 
LA 4 HOH 30  330 382  HOH HOH A . 
LA 4 HOH 31  331 596  HOH HOH A . 
LA 4 HOH 32  332 22   HOH HOH A . 
LA 4 HOH 33  333 38   HOH HOH A . 
LA 4 HOH 34  334 309  HOH HOH A . 
LA 4 HOH 35  335 922  HOH HOH A . 
LA 4 HOH 36  336 410  HOH HOH A . 
LA 4 HOH 37  337 1077 HOH HOH A . 
LA 4 HOH 38  338 167  HOH HOH A . 
LA 4 HOH 39  339 161  HOH HOH A . 
LA 4 HOH 40  340 600  HOH HOH A . 
LA 4 HOH 41  341 709  HOH HOH A . 
LA 4 HOH 42  342 437  HOH HOH A . 
LA 4 HOH 43  343 701  HOH HOH A . 
LA 4 HOH 44  344 1098 HOH HOH A . 
LA 4 HOH 45  345 807  HOH HOH A . 
LA 4 HOH 46  346 561  HOH HOH A . 
LA 4 HOH 47  347 937  HOH HOH A . 
LA 4 HOH 48  348 224  HOH HOH A . 
LA 4 HOH 49  349 228  HOH HOH A . 
LA 4 HOH 50  350 814  HOH HOH A . 
LA 4 HOH 51  351 1180 HOH HOH A . 
LA 4 HOH 52  352 1143 HOH HOH A . 
LA 4 HOH 53  353 146  HOH HOH A . 
LA 4 HOH 54  354 655  HOH HOH A . 
LA 4 HOH 55  355 879  HOH HOH A . 
LA 4 HOH 56  356 240  HOH HOH A . 
LA 4 HOH 57  357 907  HOH HOH A . 
LA 4 HOH 58  358 508  HOH HOH A . 
LA 4 HOH 59  359 283  HOH HOH A . 
LA 4 HOH 60  360 255  HOH HOH A . 
LA 4 HOH 61  361 868  HOH HOH A . 
LA 4 HOH 62  362 338  HOH HOH A . 
LA 4 HOH 63  363 278  HOH HOH A . 
LA 4 HOH 64  364 1249 HOH HOH A . 
LA 4 HOH 65  365 37   HOH HOH A . 
LA 4 HOH 66  366 404  HOH HOH A . 
LA 4 HOH 67  367 213  HOH HOH A . 
LA 4 HOH 68  368 1233 HOH HOH A . 
LA 4 HOH 69  369 37   HOH HOH A . 
LA 4 HOH 70  370 426  HOH HOH A . 
LA 4 HOH 71  371 559  HOH HOH A . 
LA 4 HOH 72  372 15   HOH HOH A . 
LA 4 HOH 73  373 98   HOH HOH A . 
LA 4 HOH 74  374 10   HOH HOH A . 
LA 4 HOH 75  375 24   HOH HOH A . 
LA 4 HOH 76  376 420  HOH HOH A . 
LA 4 HOH 77  377 849  HOH HOH A . 
LA 4 HOH 78  378 1162 HOH HOH A . 
LA 4 HOH 79  379 72   HOH HOH A . 
LA 4 HOH 80  380 166  HOH HOH A . 
LA 4 HOH 81  381 813  HOH HOH A . 
LA 4 HOH 82  382 1144 HOH HOH A . 
LA 4 HOH 83  383 227  HOH HOH A . 
LA 4 HOH 84  384 533  HOH HOH A . 
LA 4 HOH 85  385 321  HOH HOH A . 
LA 4 HOH 86  386 293  HOH HOH A . 
LA 4 HOH 87  387 44   HOH HOH A . 
LA 4 HOH 88  388 900  HOH HOH A . 
LA 4 HOH 89  389 833  HOH HOH A . 
LA 4 HOH 90  390 81   HOH HOH A . 
LA 4 HOH 91  391 682  HOH HOH A . 
LA 4 HOH 92  392 549  HOH HOH A . 
LA 4 HOH 93  393 18   HOH HOH A . 
LA 4 HOH 94  394 505  HOH HOH A . 
LA 4 HOH 95  395 108  HOH HOH A . 
LA 4 HOH 96  396 356  HOH HOH A . 
LA 4 HOH 97  397 685  HOH HOH A . 
LA 4 HOH 98  398 398  HOH HOH A . 
LA 4 HOH 99  399 582  HOH HOH A . 
LA 4 HOH 100 400 488  HOH HOH A . 
LA 4 HOH 101 401 158  HOH HOH A . 
LA 4 HOH 102 402 678  HOH HOH A . 
LA 4 HOH 103 403 924  HOH HOH A . 
LA 4 HOH 104 404 1137 HOH HOH A . 
LA 4 HOH 105 405 67   HOH HOH A . 
LA 4 HOH 106 406 325  HOH HOH A . 
LA 4 HOH 107 407 408  HOH HOH A . 
LA 4 HOH 108 408 1183 HOH HOH A . 
LA 4 HOH 109 409 717  HOH HOH A . 
LA 4 HOH 110 410 335  HOH HOH A . 
LA 4 HOH 111 411 264  HOH HOH A . 
LA 4 HOH 112 412 251  HOH HOH A . 
LA 4 HOH 113 413 614  HOH HOH A . 
LA 4 HOH 114 414 1139 HOH HOH A . 
LA 4 HOH 115 415 863  HOH HOH A . 
LA 4 HOH 116 416 61   HOH HOH A . 
LA 4 HOH 117 417 694  HOH HOH A . 
LA 4 HOH 118 418 21   HOH HOH A . 
LA 4 HOH 119 419 1187 HOH HOH A . 
LA 4 HOH 120 420 238  HOH HOH A . 
LA 4 HOH 121 421 667  HOH HOH A . 
LA 4 HOH 122 422 1099 HOH HOH A . 
LA 4 HOH 123 423 995  HOH HOH A . 
LA 4 HOH 124 424 1253 HOH HOH A . 
LA 4 HOH 125 425 1161 HOH HOH A . 
LA 4 HOH 126 426 927  HOH HOH A . 
LA 4 HOH 127 427 405  HOH HOH A . 
LA 4 HOH 128 428 370  HOH HOH A . 
LA 4 HOH 129 429 799  HOH HOH A . 
LA 4 HOH 130 430 984  HOH HOH A . 
LA 4 HOH 131 431 1242 HOH HOH A . 
LA 4 HOH 132 432 1024 HOH HOH A . 
LA 4 HOH 133 433 627  HOH HOH A . 
LA 4 HOH 134 434 703  HOH HOH A . 
LA 4 HOH 135 435 1059 HOH HOH A . 
LA 4 HOH 136 436 269  HOH HOH A . 
LA 4 HOH 137 437 311  HOH HOH A . 
MA 4 HOH 1   301 89   HOH HOH F . 
MA 4 HOH 2   302 481  HOH HOH F . 
MA 4 HOH 3   303 1108 HOH HOH F . 
MA 4 HOH 4   304 124  HOH HOH F . 
MA 4 HOH 5   305 871  HOH HOH F . 
MA 4 HOH 6   306 169  HOH HOH F . 
MA 4 HOH 7   307 375  HOH HOH F . 
MA 4 HOH 8   308 490  HOH HOH F . 
MA 4 HOH 9   309 642  HOH HOH F . 
MA 4 HOH 10  310 126  HOH HOH F . 
MA 4 HOH 11  311 376  HOH HOH F . 
MA 4 HOH 12  312 708  HOH HOH F . 
MA 4 HOH 13  313 400  HOH HOH F . 
MA 4 HOH 14  314 237  HOH HOH F . 
MA 4 HOH 15  315 752  HOH HOH F . 
MA 4 HOH 16  316 843  HOH HOH F . 
MA 4 HOH 17  317 686  HOH HOH F . 
MA 4 HOH 18  318 796  HOH HOH F . 
MA 4 HOH 19  319 379  HOH HOH F . 
MA 4 HOH 20  320 887  HOH HOH F . 
MA 4 HOH 21  321 891  HOH HOH F . 
MA 4 HOH 22  322 756  HOH HOH F . 
MA 4 HOH 23  323 159  HOH HOH F . 
MA 4 HOH 24  324 496  HOH HOH F . 
MA 4 HOH 25  325 21   HOH HOH F . 
MA 4 HOH 26  326 200  HOH HOH F . 
MA 4 HOH 27  327 100  HOH HOH F . 
MA 4 HOH 28  328 529  HOH HOH F . 
MA 4 HOH 29  329 946  HOH HOH F . 
MA 4 HOH 30  330 643  HOH HOH F . 
MA 4 HOH 31  331 105  HOH HOH F . 
MA 4 HOH 32  332 1194 HOH HOH F . 
MA 4 HOH 33  333 20   HOH HOH F . 
MA 4 HOH 34  334 797  HOH HOH F . 
MA 4 HOH 35  335 140  HOH HOH F . 
MA 4 HOH 36  336 172  HOH HOH F . 
MA 4 HOH 37  337 1005 HOH HOH F . 
MA 4 HOH 38  338 744  HOH HOH F . 
MA 4 HOH 39  339 111  HOH HOH F . 
MA 4 HOH 40  340 890  HOH HOH F . 
MA 4 HOH 41  341 570  HOH HOH F . 
MA 4 HOH 42  342 374  HOH HOH F . 
MA 4 HOH 43  343 899  HOH HOH F . 
MA 4 HOH 44  344 970  HOH HOH F . 
MA 4 HOH 45  345 1219 HOH HOH F . 
MA 4 HOH 46  346 997  HOH HOH F . 
MA 4 HOH 47  347 366  HOH HOH F . 
MA 4 HOH 48  348 5    HOH HOH F . 
MA 4 HOH 49  349 681  HOH HOH F . 
MA 4 HOH 50  350 527  HOH HOH F . 
MA 4 HOH 51  351 275  HOH HOH F . 
MA 4 HOH 52  352 229  HOH HOH F . 
MA 4 HOH 53  353 1204 HOH HOH F . 
MA 4 HOH 54  354 6    HOH HOH F . 
MA 4 HOH 55  355 64   HOH HOH F . 
MA 4 HOH 56  356 1174 HOH HOH F . 
MA 4 HOH 57  357 1197 HOH HOH F . 
MA 4 HOH 58  358 673  HOH HOH F . 
MA 4 HOH 59  359 340  HOH HOH F . 
MA 4 HOH 60  360 451  HOH HOH F . 
MA 4 HOH 61  361 860  HOH HOH F . 
MA 4 HOH 62  362 788  HOH HOH F . 
MA 4 HOH 63  363 296  HOH HOH F . 
MA 4 HOH 64  364 25   HOH HOH F . 
MA 4 HOH 65  365 210  HOH HOH F . 
MA 4 HOH 66  366 121  HOH HOH F . 
MA 4 HOH 67  367 1256 HOH HOH F . 
MA 4 HOH 68  368 280  HOH HOH F . 
MA 4 HOH 69  369 185  HOH HOH F . 
MA 4 HOH 70  370 107  HOH HOH F . 
MA 4 HOH 71  371 774  HOH HOH F . 
MA 4 HOH 72  372 497  HOH HOH F . 
MA 4 HOH 73  373 573  HOH HOH F . 
MA 4 HOH 74  374 187  HOH HOH F . 
MA 4 HOH 75  375 993  HOH HOH F . 
MA 4 HOH 76  376 409  HOH HOH F . 
MA 4 HOH 77  377 760  HOH HOH F . 
MA 4 HOH 78  378 68   HOH HOH F . 
MA 4 HOH 79  379 181  HOH HOH F . 
MA 4 HOH 80  380 518  HOH HOH F . 
MA 4 HOH 81  381 940  HOH HOH F . 
MA 4 HOH 82  382 495  HOH HOH F . 
MA 4 HOH 83  383 63   HOH HOH F . 
MA 4 HOH 84  384 243  HOH HOH F . 
MA 4 HOH 85  385 1152 HOH HOH F . 
MA 4 HOH 86  386 128  HOH HOH F . 
MA 4 HOH 87  387 427  HOH HOH F . 
MA 4 HOH 88  388 120  HOH HOH F . 
MA 4 HOH 89  389 1221 HOH HOH F . 
MA 4 HOH 90  390 34   HOH HOH F . 
MA 4 HOH 91  391 635  HOH HOH F . 
MA 4 HOH 92  392 649  HOH HOH F . 
MA 4 HOH 93  393 94   HOH HOH F . 
MA 4 HOH 94  394 644  HOH HOH F . 
MA 4 HOH 95  395 419  HOH HOH F . 
MA 4 HOH 96  396 1125 HOH HOH F . 
MA 4 HOH 97  397 415  HOH HOH F . 
MA 4 HOH 98  398 892  HOH HOH F . 
MA 4 HOH 99  399 477  HOH HOH F . 
MA 4 HOH 100 400 515  HOH HOH F . 
MA 4 HOH 101 401 380  HOH HOH F . 
MA 4 HOH 102 402 162  HOH HOH F . 
MA 4 HOH 103 403 205  HOH HOH F . 
MA 4 HOH 104 404 16   HOH HOH F . 
MA 4 HOH 105 405 42   HOH HOH F . 
MA 4 HOH 106 406 271  HOH HOH F . 
MA 4 HOH 107 407 787  HOH HOH F . 
MA 4 HOH 108 408 916  HOH HOH F . 
MA 4 HOH 109 409 39   HOH HOH F . 
MA 4 HOH 110 410 1254 HOH HOH F . 
MA 4 HOH 111 411 721  HOH HOH F . 
MA 4 HOH 112 412 401  HOH HOH F . 
MA 4 HOH 113 413 482  HOH HOH F . 
MA 4 HOH 114 414 248  HOH HOH F . 
MA 4 HOH 115 415 412  HOH HOH F . 
MA 4 HOH 116 416 118  HOH HOH F . 
MA 4 HOH 117 417 877  HOH HOH F . 
MA 4 HOH 118 418 781  HOH HOH F . 
MA 4 HOH 119 419 811  HOH HOH F . 
MA 4 HOH 120 420 556  HOH HOH F . 
MA 4 HOH 121 421 988  HOH HOH F . 
MA 4 HOH 122 422 662  HOH HOH F . 
MA 4 HOH 123 423 786  HOH HOH F . 
MA 4 HOH 124 424 610  HOH HOH F . 
MA 4 HOH 125 425 1069 HOH HOH F . 
MA 4 HOH 126 426 588  HOH HOH F . 
MA 4 HOH 127 427 136  HOH HOH F . 
MA 4 HOH 128 428 463  HOH HOH F . 
MA 4 HOH 129 429 648  HOH HOH F . 
MA 4 HOH 130 430 76   HOH HOH F . 
MA 4 HOH 131 431 1063 HOH HOH F . 
MA 4 HOH 132 432 654  HOH HOH F . 
MA 4 HOH 133 433 903  HOH HOH F . 
MA 4 HOH 134 434 1132 HOH HOH F . 
MA 4 HOH 135 435 1250 HOH HOH F . 
MA 4 HOH 136 436 893  HOH HOH F . 
MA 4 HOH 137 437 862  HOH HOH F . 
MA 4 HOH 138 438 1237 HOH HOH F . 
MA 4 HOH 139 439 1028 HOH HOH F . 
MA 4 HOH 140 440 270  HOH HOH F . 
MA 4 HOH 141 441 1203 HOH HOH F . 
MA 4 HOH 142 442 657  HOH HOH F . 
MA 4 HOH 143 443 889  HOH HOH F . 
MA 4 HOH 144 444 290  HOH HOH F . 
MA 4 HOH 145 445 1110 HOH HOH F . 
MA 4 HOH 146 446 1147 HOH HOH F . 
MA 4 HOH 147 447 1017 HOH HOH F . 
MA 4 HOH 148 448 1181 HOH HOH F . 
MA 4 HOH 149 449 95   HOH HOH F . 
MA 4 HOH 150 450 589  HOH HOH F . 
MA 4 HOH 151 451 664  HOH HOH F . 
MA 4 HOH 152 452 934  HOH HOH F . 
MA 4 HOH 153 453 352  HOH HOH F . 
MA 4 HOH 154 454 345  HOH HOH F . 
MA 4 HOH 155 455 262  HOH HOH F . 
MA 4 HOH 156 456 747  HOH HOH F . 
NA 4 HOH 1   301 674  HOH HOH D . 
NA 4 HOH 2   302 1    HOH HOH D . 
NA 4 HOH 3   303 878  HOH HOH D . 
NA 4 HOH 4   304 102  HOH HOH D . 
NA 4 HOH 5   305 204  HOH HOH D . 
NA 4 HOH 6   306 953  HOH HOH D . 
NA 4 HOH 7   307 1211 HOH HOH D . 
NA 4 HOH 8   308 944  HOH HOH D . 
NA 4 HOH 9   309 1107 HOH HOH D . 
NA 4 HOH 10  310 1235 HOH HOH D . 
NA 4 HOH 11  311 252  HOH HOH D . 
NA 4 HOH 12  312 149  HOH HOH D . 
NA 4 HOH 13  313 925  HOH HOH D . 
NA 4 HOH 14  314 53   HOH HOH D . 
NA 4 HOH 15  315 1013 HOH HOH D . 
NA 4 HOH 16  316 661  HOH HOH D . 
NA 4 HOH 17  317 504  HOH HOH D . 
NA 4 HOH 18  318 150  HOH HOH D . 
NA 4 HOH 19  319 1043 HOH HOH D . 
NA 4 HOH 20  320 1164 HOH HOH D . 
NA 4 HOH 21  321 957  HOH HOH D . 
NA 4 HOH 22  322 492  HOH HOH D . 
NA 4 HOH 23  323 759  HOH HOH D . 
NA 4 HOH 24  324 1118 HOH HOH D . 
NA 4 HOH 25  325 173  HOH HOH D . 
NA 4 HOH 26  326 1038 HOH HOH D . 
NA 4 HOH 27  327 51   HOH HOH D . 
NA 4 HOH 28  328 217  HOH HOH D . 
NA 4 HOH 29  329 122  HOH HOH D . 
NA 4 HOH 30  330 304  HOH HOH D . 
NA 4 HOH 31  331 433  HOH HOH D . 
NA 4 HOH 32  332 704  HOH HOH D . 
NA 4 HOH 33  333 241  HOH HOH D . 
NA 4 HOH 34  334 928  HOH HOH D . 
NA 4 HOH 35  335 845  HOH HOH D . 
NA 4 HOH 36  336 474  HOH HOH D . 
NA 4 HOH 37  337 1122 HOH HOH D . 
NA 4 HOH 38  338 885  HOH HOH D . 
NA 4 HOH 39  339 1071 HOH HOH D . 
NA 4 HOH 40  340 918  HOH HOH D . 
NA 4 HOH 41  341 1178 HOH HOH D . 
NA 4 HOH 42  342 873  HOH HOH D . 
NA 4 HOH 43  343 281  HOH HOH D . 
NA 4 HOH 44  344 84   HOH HOH D . 
NA 4 HOH 45  345 670  HOH HOH D . 
NA 4 HOH 46  346 990  HOH HOH D . 
NA 4 HOH 47  347 1179 HOH HOH D . 
NA 4 HOH 48  348 931  HOH HOH D . 
NA 4 HOH 49  349 277  HOH HOH D . 
NA 4 HOH 50  350 209  HOH HOH D . 
NA 4 HOH 51  351 948  HOH HOH D . 
NA 4 HOH 52  352 116  HOH HOH D . 
NA 4 HOH 53  353 314  HOH HOH D . 
NA 4 HOH 54  354 546  HOH HOH D . 
NA 4 HOH 55  355 778  HOH HOH D . 
NA 4 HOH 56  356 802  HOH HOH D . 
NA 4 HOH 57  357 36   HOH HOH D . 
NA 4 HOH 58  358 1201 HOH HOH D . 
NA 4 HOH 59  359 28   HOH HOH D . 
NA 4 HOH 60  360 123  HOH HOH D . 
NA 4 HOH 61  361 523  HOH HOH D . 
NA 4 HOH 62  362 93   HOH HOH D . 
NA 4 HOH 63  363 52   HOH HOH D . 
NA 4 HOH 64  364 288  HOH HOH D . 
NA 4 HOH 65  365 1171 HOH HOH D . 
NA 4 HOH 66  366 92   HOH HOH D . 
NA 4 HOH 67  367 371  HOH HOH D . 
NA 4 HOH 68  368 803  HOH HOH D . 
NA 4 HOH 69  369 537  HOH HOH D . 
NA 4 HOH 70  370 576  HOH HOH D . 
NA 4 HOH 71  371 783  HOH HOH D . 
NA 4 HOH 72  372 65   HOH HOH D . 
NA 4 HOH 73  373 1084 HOH HOH D . 
NA 4 HOH 74  374 1166 HOH HOH D . 
NA 4 HOH 75  375 82   HOH HOH D . 
NA 4 HOH 76  376 46   HOH HOH D . 
NA 4 HOH 77  377 399  HOH HOH D . 
NA 4 HOH 78  378 285  HOH HOH D . 
NA 4 HOH 79  379 1243 HOH HOH D . 
NA 4 HOH 80  380 443  HOH HOH D . 
NA 4 HOH 81  381 952  HOH HOH D . 
NA 4 HOH 82  382 798  HOH HOH D . 
NA 4 HOH 83  383 73   HOH HOH D . 
NA 4 HOH 84  384 659  HOH HOH D . 
NA 4 HOH 85  385 567  HOH HOH D . 
NA 4 HOH 86  386 1150 HOH HOH D . 
NA 4 HOH 87  387 980  HOH HOH D . 
NA 4 HOH 88  388 791  HOH HOH D . 
NA 4 HOH 89  389 823  HOH HOH D . 
NA 4 HOH 90  390 33   HOH HOH D . 
NA 4 HOH 91  391 222  HOH HOH D . 
NA 4 HOH 92  392 795  HOH HOH D . 
NA 4 HOH 93  393 289  HOH HOH D . 
NA 4 HOH 94  394 1234 HOH HOH D . 
NA 4 HOH 95  395 599  HOH HOH D . 
NA 4 HOH 96  396 473  HOH HOH D . 
NA 4 HOH 97  397 156  HOH HOH D . 
NA 4 HOH 98  398 160  HOH HOH D . 
NA 4 HOH 99  399 725  HOH HOH D . 
NA 4 HOH 100 400 683  HOH HOH D . 
NA 4 HOH 101 401 775  HOH HOH D . 
NA 4 HOH 102 402 865  HOH HOH D . 
NA 4 HOH 103 403 785  HOH HOH D . 
NA 4 HOH 104 404 975  HOH HOH D . 
NA 4 HOH 105 405 208  HOH HOH D . 
NA 4 HOH 106 406 909  HOH HOH D . 
NA 4 HOH 107 407 974  HOH HOH D . 
NA 4 HOH 108 408 127  HOH HOH D . 
NA 4 HOH 109 409 933  HOH HOH D . 
NA 4 HOH 110 410 1267 HOH HOH D . 
NA 4 HOH 111 411 939  HOH HOH D . 
NA 4 HOH 112 412 656  HOH HOH D . 
NA 4 HOH 113 413 23   HOH HOH D . 
NA 4 HOH 114 414 430  HOH HOH D . 
NA 4 HOH 115 415 651  HOH HOH D . 
NA 4 HOH 116 416 886  HOH HOH D . 
NA 4 HOH 117 417 826  HOH HOH D . 
NA 4 HOH 118 418 784  HOH HOH D . 
NA 4 HOH 119 419 1195 HOH HOH D . 
NA 4 HOH 120 420 1124 HOH HOH D . 
NA 4 HOH 121 421 857  HOH HOH D . 
NA 4 HOH 122 422 829  HOH HOH D . 
NA 4 HOH 123 423 932  HOH HOH D . 
NA 4 HOH 124 424 1269 HOH HOH D . 
NA 4 HOH 125 425 724  HOH HOH D . 
OA 4 HOH 1   301 853  HOH HOH G . 
OA 4 HOH 2   302 896  HOH HOH G . 
OA 4 HOH 3   303 794  HOH HOH G . 
OA 4 HOH 4   304 608  HOH HOH G . 
OA 4 HOH 5   305 1100 HOH HOH G . 
OA 4 HOH 6   306 723  HOH HOH G . 
OA 4 HOH 7   307 436  HOH HOH G . 
OA 4 HOH 8   308 465  HOH HOH G . 
OA 4 HOH 9   309 502  HOH HOH G . 
OA 4 HOH 10  310 645  HOH HOH G . 
OA 4 HOH 11  311 15   HOH HOH G . 
OA 4 HOH 12  312 31   HOH HOH G . 
OA 4 HOH 13  313 119  HOH HOH G . 
OA 4 HOH 14  314 808  HOH HOH G . 
OA 4 HOH 15  315 854  HOH HOH G . 
OA 4 HOH 16  316 1213 HOH HOH G . 
OA 4 HOH 17  317 9    HOH HOH G . 
OA 4 HOH 18  318 43   HOH HOH G . 
OA 4 HOH 19  319 668  HOH HOH G . 
OA 4 HOH 20  320 764  HOH HOH G . 
OA 4 HOH 21  321 260  HOH HOH G . 
OA 4 HOH 22  322 431  HOH HOH G . 
OA 4 HOH 23  323 790  HOH HOH G . 
OA 4 HOH 24  324 772  HOH HOH G . 
OA 4 HOH 25  325 740  HOH HOH G . 
OA 4 HOH 26  326 1057 HOH HOH G . 
OA 4 HOH 27  327 29   HOH HOH G . 
OA 4 HOH 28  328 831  HOH HOH G . 
OA 4 HOH 29  329 233  HOH HOH G . 
OA 4 HOH 30  330 859  HOH HOH G . 
OA 4 HOH 31  331 478  HOH HOH G . 
OA 4 HOH 32  332 520  HOH HOH G . 
OA 4 HOH 33  333 501  HOH HOH G . 
OA 4 HOH 34  334 800  HOH HOH G . 
OA 4 HOH 35  335 1087 HOH HOH G . 
OA 4 HOH 36  336 583  HOH HOH G . 
OA 4 HOH 37  337 1062 HOH HOH G . 
OA 4 HOH 38  338 822  HOH HOH G . 
OA 4 HOH 39  339 301  HOH HOH G . 
OA 4 HOH 40  340 1065 HOH HOH G . 
OA 4 HOH 41  341 12   HOH HOH G . 
OA 4 HOH 42  342 106  HOH HOH G . 
OA 4 HOH 43  343 148  HOH HOH G . 
OA 4 HOH 44  344 994  HOH HOH G . 
OA 4 HOH 45  345 653  HOH HOH G . 
OA 4 HOH 46  346 566  HOH HOH G . 
OA 4 HOH 47  347 998  HOH HOH G . 
OA 4 HOH 48  348 77   HOH HOH G . 
OA 4 HOH 49  349 522  HOH HOH G . 
OA 4 HOH 50  350 622  HOH HOH G . 
OA 4 HOH 51  351 36   HOH HOH G . 
OA 4 HOH 52  352 388  HOH HOH G . 
OA 4 HOH 53  353 737  HOH HOH G . 
OA 4 HOH 54  354 702  HOH HOH G . 
OA 4 HOH 55  355 1209 HOH HOH G . 
OA 4 HOH 56  356 361  HOH HOH G . 
OA 4 HOH 57  357 78   HOH HOH G . 
OA 4 HOH 58  358 195  HOH HOH G . 
OA 4 HOH 59  359 397  HOH HOH G . 
OA 4 HOH 60  360 1032 HOH HOH G . 
OA 4 HOH 61  361 710  HOH HOH G . 
OA 4 HOH 62  362 12   HOH HOH G . 
OA 4 HOH 63  363 194  HOH HOH G . 
OA 4 HOH 64  364 1102 HOH HOH G . 
OA 4 HOH 65  365 1210 HOH HOH G . 
OA 4 HOH 66  366 542  HOH HOH G . 
OA 4 HOH 67  367 13   HOH HOH G . 
OA 4 HOH 68  368 629  HOH HOH G . 
OA 4 HOH 69  369 514  HOH HOH G . 
OA 4 HOH 70  370 357  HOH HOH G . 
OA 4 HOH 71  371 131  HOH HOH G . 
OA 4 HOH 72  372 129  HOH HOH G . 
OA 4 HOH 73  373 1202 HOH HOH G . 
OA 4 HOH 74  374 316  HOH HOH G . 
OA 4 HOH 75  375 201  HOH HOH G . 
OA 4 HOH 76  376 483  HOH HOH G . 
OA 4 HOH 77  377 470  HOH HOH G . 
OA 4 HOH 78  378 54   HOH HOH G . 
OA 4 HOH 79  379 59   HOH HOH G . 
OA 4 HOH 80  380 619  HOH HOH G . 
OA 4 HOH 81  381 74   HOH HOH G . 
OA 4 HOH 82  382 675  HOH HOH G . 
OA 4 HOH 83  383 45   HOH HOH G . 
OA 4 HOH 84  384 25   HOH HOH G . 
OA 4 HOH 85  385 115  HOH HOH G . 
OA 4 HOH 86  386 7    HOH HOH G . 
OA 4 HOH 87  387 677  HOH HOH G . 
OA 4 HOH 88  388 769  HOH HOH G . 
OA 4 HOH 89  389 90   HOH HOH G . 
OA 4 HOH 90  390 114  HOH HOH G . 
OA 4 HOH 91  391 1239 HOH HOH G . 
OA 4 HOH 92  392 441  HOH HOH G . 
OA 4 HOH 93  393 20   HOH HOH G . 
OA 4 HOH 94  394 310  HOH HOH G . 
OA 4 HOH 95  395 18   HOH HOH G . 
OA 4 HOH 96  396 544  HOH HOH G . 
OA 4 HOH 97  397 49   HOH HOH G . 
OA 4 HOH 98  398 137  HOH HOH G . 
OA 4 HOH 99  399 178  HOH HOH G . 
OA 4 HOH 100 400 324  HOH HOH G . 
OA 4 HOH 101 401 87   HOH HOH G . 
OA 4 HOH 102 402 373  HOH HOH G . 
OA 4 HOH 103 403 817  HOH HOH G . 
OA 4 HOH 104 404 560  HOH HOH G . 
OA 4 HOH 105 405 319  HOH HOH G . 
OA 4 HOH 106 406 117  HOH HOH G . 
OA 4 HOH 107 407 1115 HOH HOH G . 
OA 4 HOH 108 408 888  HOH HOH G . 
OA 4 HOH 109 409 669  HOH HOH G . 
OA 4 HOH 110 410 712  HOH HOH G . 
OA 4 HOH 111 411 825  HOH HOH G . 
OA 4 HOH 112 412 257  HOH HOH G . 
OA 4 HOH 113 413 165  HOH HOH G . 
OA 4 HOH 114 414 986  HOH HOH G . 
OA 4 HOH 115 415 965  HOH HOH G . 
OA 4 HOH 116 416 351  HOH HOH G . 
OA 4 HOH 117 417 901  HOH HOH G . 
OA 4 HOH 118 418 660  HOH HOH G . 
OA 4 HOH 119 419 1138 HOH HOH G . 
OA 4 HOH 120 420 1131 HOH HOH G . 
OA 4 HOH 121 421 1044 HOH HOH G . 
OA 4 HOH 122 422 368  HOH HOH G . 
OA 4 HOH 123 423 1019 HOH HOH G . 
OA 4 HOH 124 424 880  HOH HOH G . 
OA 4 HOH 125 425 58   HOH HOH G . 
OA 4 HOH 126 426 8    HOH HOH G . 
OA 4 HOH 127 427 1060 HOH HOH G . 
OA 4 HOH 128 428 1041 HOH HOH G . 
PA 4 HOH 1   301 48   HOH HOH I . 
PA 4 HOH 2   302 47   HOH HOH I . 
PA 4 HOH 3   303 284  HOH HOH I . 
PA 4 HOH 4   304 805  HOH HOH I . 
PA 4 HOH 5   305 554  HOH HOH I . 
PA 4 HOH 6   306 905  HOH HOH I . 
PA 4 HOH 7   307 239  HOH HOH I . 
PA 4 HOH 8   308 553  HOH HOH I . 
PA 4 HOH 9   309 244  HOH HOH I . 
PA 4 HOH 10  310 22   HOH HOH I . 
PA 4 HOH 11  311 1245 HOH HOH I . 
PA 4 HOH 12  312 1014 HOH HOH I . 
PA 4 HOH 13  313 32   HOH HOH I . 
PA 4 HOH 14  314 334  HOH HOH I . 
PA 4 HOH 15  315 603  HOH HOH I . 
PA 4 HOH 16  316 666  HOH HOH I . 
PA 4 HOH 17  317 1236 HOH HOH I . 
PA 4 HOH 18  318 842  HOH HOH I . 
PA 4 HOH 19  319 1120 HOH HOH I . 
PA 4 HOH 20  320 1157 HOH HOH I . 
PA 4 HOH 21  321 834  HOH HOH I . 
PA 4 HOH 22  322 1096 HOH HOH I . 
PA 4 HOH 23  323 1205 HOH HOH I . 
PA 4 HOH 24  324 1128 HOH HOH I . 
PA 4 HOH 25  325 1241 HOH HOH I . 
PA 4 HOH 26  326 700  HOH HOH I . 
PA 4 HOH 27  327 874  HOH HOH I . 
PA 4 HOH 28  328 628  HOH HOH I . 
PA 4 HOH 29  329 585  HOH HOH I . 
PA 4 HOH 30  330 1088 HOH HOH I . 
PA 4 HOH 31  331 1127 HOH HOH I . 
PA 4 HOH 32  332 1208 HOH HOH I . 
PA 4 HOH 33  333 1031 HOH HOH I . 
PA 4 HOH 34  334 738  HOH HOH I . 
PA 4 HOH 35  335 982  HOH HOH I . 
PA 4 HOH 36  336 594  HOH HOH I . 
PA 4 HOH 37  337 196  HOH HOH I . 
PA 4 HOH 38  338 706  HOH HOH I . 
QA 4 HOH 1   301 1220 HOH HOH K . 
QA 4 HOH 2   302 595  HOH HOH K . 
QA 4 HOH 3   303 232  HOH HOH K . 
QA 4 HOH 4   304 272  HOH HOH K . 
QA 4 HOH 5   305 1175 HOH HOH K . 
QA 4 HOH 6   306 144  HOH HOH K . 
QA 4 HOH 7   307 236  HOH HOH K . 
QA 4 HOH 8   308 317  HOH HOH K . 
QA 4 HOH 9   309 617  HOH HOH K . 
QA 4 HOH 10  310 1160 HOH HOH K . 
QA 4 HOH 11  311 104  HOH HOH K . 
QA 4 HOH 12  312 718  HOH HOH K . 
QA 4 HOH 13  313 1218 HOH HOH K . 
QA 4 HOH 14  314 757  HOH HOH K . 
QA 4 HOH 15  315 861  HOH HOH K . 
QA 4 HOH 16  316 531  HOH HOH K . 
QA 4 HOH 17  317 714  HOH HOH K . 
QA 4 HOH 18  318 282  HOH HOH K . 
QA 4 HOH 19  319 312  HOH HOH K . 
QA 4 HOH 20  320 258  HOH HOH K . 
QA 4 HOH 21  321 326  HOH HOH K . 
QA 4 HOH 22  322 580  HOH HOH K . 
QA 4 HOH 23  323 882  HOH HOH K . 
QA 4 HOH 24  324 1051 HOH HOH K . 
QA 4 HOH 25  325 1155 HOH HOH K . 
QA 4 HOH 26  326 1116 HOH HOH K . 
QA 4 HOH 27  327 42   HOH HOH K . 
QA 4 HOH 28  328 453  HOH HOH K . 
QA 4 HOH 29  329 1232 HOH HOH K . 
QA 4 HOH 30  330 383  HOH HOH K . 
QA 4 HOH 31  331 303  HOH HOH K . 
QA 4 HOH 32  332 322  HOH HOH K . 
QA 4 HOH 33  333 512  HOH HOH K . 
QA 4 HOH 34  334 897  HOH HOH K . 
QA 4 HOH 35  335 855  HOH HOH K . 
QA 4 HOH 36  336 883  HOH HOH K . 
QA 4 HOH 37  337 801  HOH HOH K . 
QA 4 HOH 38  338 141  HOH HOH K . 
QA 4 HOH 39  339 1049 HOH HOH K . 
QA 4 HOH 40  340 27   HOH HOH K . 
QA 4 HOH 41  341 138  HOH HOH K . 
QA 4 HOH 42  342 279  HOH HOH K . 
QA 4 HOH 43  343 265  HOH HOH K . 
QA 4 HOH 44  344 612  HOH HOH K . 
QA 4 HOH 45  345 1061 HOH HOH K . 
QA 4 HOH 46  346 182  HOH HOH K . 
QA 4 HOH 47  347 591  HOH HOH K . 
QA 4 HOH 48  348 385  HOH HOH K . 
QA 4 HOH 49  349 83   HOH HOH K . 
QA 4 HOH 50  350 320  HOH HOH K . 
QA 4 HOH 51  351 534  HOH HOH K . 
QA 4 HOH 52  352 130  HOH HOH K . 
QA 4 HOH 53  353 384  HOH HOH K . 
QA 4 HOH 54  354 1103 HOH HOH K . 
QA 4 HOH 55  355 1251 HOH HOH K . 
QA 4 HOH 56  356 692  HOH HOH K . 
QA 4 HOH 57  357 976  HOH HOH K . 
QA 4 HOH 58  358 528  HOH HOH K . 
QA 4 HOH 59  359 308  HOH HOH K . 
QA 4 HOH 60  360 705  HOH HOH K . 
QA 4 HOH 61  361 1097 HOH HOH K . 
QA 4 HOH 62  362 300  HOH HOH K . 
QA 4 HOH 63  363 584  HOH HOH K . 
QA 4 HOH 64  364 810  HOH HOH K . 
QA 4 HOH 65  365 713  HOH HOH K . 
QA 4 HOH 66  366 448  HOH HOH K . 
QA 4 HOH 67  367 507  HOH HOH K . 
QA 4 HOH 68  368 134  HOH HOH K . 
QA 4 HOH 69  369 777  HOH HOH K . 
QA 4 HOH 70  370 295  HOH HOH K . 
QA 4 HOH 71  371 1182 HOH HOH K . 
QA 4 HOH 72  372 733  HOH HOH K . 
QA 4 HOH 73  373 215  HOH HOH K . 
QA 4 HOH 74  374 884  HOH HOH K . 
QA 4 HOH 75  375 26   HOH HOH K . 
QA 4 HOH 76  376 1008 HOH HOH K . 
QA 4 HOH 77  377 341  HOH HOH K . 
QA 4 HOH 78  378 689  HOH HOH K . 
QA 4 HOH 79  379 517  HOH HOH K . 
QA 4 HOH 80  380 715  HOH HOH K . 
RA 4 HOH 1   301 19   HOH HOH M . 
RA 4 HOH 2   302 445  HOH HOH M . 
RA 4 HOH 3   303 1133 HOH HOH M . 
RA 4 HOH 4   304 763  HOH HOH M . 
RA 4 HOH 5   305 389  HOH HOH M . 
RA 4 HOH 6   306 818  HOH HOH M . 
RA 4 HOH 7   307 821  HOH HOH M . 
RA 4 HOH 8   308 377  HOH HOH M . 
RA 4 HOH 9   309 767  HOH HOH M . 
RA 4 HOH 10  310 1129 HOH HOH M . 
RA 4 HOH 11  311 945  HOH HOH M . 
RA 4 HOH 12  312 1230 HOH HOH M . 
RA 4 HOH 13  313 964  HOH HOH M . 
RA 4 HOH 14  314 297  HOH HOH M . 
RA 4 HOH 15  315 1009 HOH HOH M . 
RA 4 HOH 16  316 1053 HOH HOH M . 
RA 4 HOH 17  317 779  HOH HOH M . 
RA 4 HOH 18  318 840  HOH HOH M . 
RA 4 HOH 19  319 632  HOH HOH M . 
RA 4 HOH 20  320 302  HOH HOH M . 
RA 4 HOH 21  321 153  HOH HOH M . 
RA 4 HOH 22  322 999  HOH HOH M . 
RA 4 HOH 23  323 1136 HOH HOH M . 
RA 4 HOH 24  324 56   HOH HOH M . 
RA 4 HOH 25  325 348  HOH HOH M . 
RA 4 HOH 26  326 103  HOH HOH M . 
RA 4 HOH 27  327 225  HOH HOH M . 
RA 4 HOH 28  328 866  HOH HOH M . 
RA 4 HOH 29  329 1119 HOH HOH M . 
RA 4 HOH 30  330 346  HOH HOH M . 
RA 4 HOH 31  331 192  HOH HOH M . 
RA 4 HOH 32  332 459  HOH HOH M . 
RA 4 HOH 33  333 479  HOH HOH M . 
RA 4 HOH 34  334 616  HOH HOH M . 
RA 4 HOH 35  335 395  HOH HOH M . 
RA 4 HOH 36  336 245  HOH HOH M . 
RA 4 HOH 37  337 230  HOH HOH M . 
RA 4 HOH 38  338 349  HOH HOH M . 
RA 4 HOH 39  339 198  HOH HOH M . 
RA 4 HOH 40  340 1012 HOH HOH M . 
RA 4 HOH 41  341 32   HOH HOH M . 
RA 4 HOH 42  342 663  HOH HOH M . 
RA 4 HOH 43  343 221  HOH HOH M . 
RA 4 HOH 44  344 782  HOH HOH M . 
RA 4 HOH 45  345 396  HOH HOH M . 
RA 4 HOH 46  346 393  HOH HOH M . 
RA 4 HOH 47  347 586  HOH HOH M . 
RA 4 HOH 48  348 171  HOH HOH M . 
RA 4 HOH 49  349 870  HOH HOH M . 
RA 4 HOH 50  350 378  HOH HOH M . 
RA 4 HOH 51  351 719  HOH HOH M . 
RA 4 HOH 52  352 472  HOH HOH M . 
RA 4 HOH 53  353 511  HOH HOH M . 
RA 4 HOH 54  354 1113 HOH HOH M . 
RA 4 HOH 55  355 658  HOH HOH M . 
RA 4 HOH 56  356 620  HOH HOH M . 
RA 4 HOH 57  357 1167 HOH HOH M . 
RA 4 HOH 58  358 62   HOH HOH M . 
RA 4 HOH 59  359 274  HOH HOH M . 
RA 4 HOH 60  360 423  HOH HOH M . 
RA 4 HOH 61  361 183  HOH HOH M . 
RA 4 HOH 62  362 902  HOH HOH M . 
RA 4 HOH 63  363 819  HOH HOH M . 
RA 4 HOH 64  364 487  HOH HOH M . 
RA 4 HOH 65  365 538  HOH HOH M . 
RA 4 HOH 66  366 202  HOH HOH M . 
RA 4 HOH 67  367 254  HOH HOH M . 
RA 4 HOH 68  368 1010 HOH HOH M . 
RA 4 HOH 69  369 411  HOH HOH M . 
RA 4 HOH 70  370 1068 HOH HOH M . 
RA 4 HOH 71  371 958  HOH HOH M . 
RA 4 HOH 72  372 88   HOH HOH M . 
RA 4 HOH 73  373 989  HOH HOH M . 
RA 4 HOH 74  374 362  HOH HOH M . 
RA 4 HOH 75  375 804  HOH HOH M . 
RA 4 HOH 76  376 286  HOH HOH M . 
RA 4 HOH 77  377 1165 HOH HOH M . 
RA 4 HOH 78  378 337  HOH HOH M . 
RA 4 HOH 79  379 841  HOH HOH M . 
RA 4 HOH 80  380 1173 HOH HOH M . 
RA 4 HOH 81  381 157  HOH HOH M . 
RA 4 HOH 82  382 1083 HOH HOH M . 
RA 4 HOH 83  383 306  HOH HOH M . 
RA 4 HOH 84  384 676  HOH HOH M . 
RA 4 HOH 85  385 387  HOH HOH M . 
RA 4 HOH 86  386 1090 HOH HOH M . 
RA 4 HOH 87  387 318  HOH HOH M . 
RA 4 HOH 88  388 449  HOH HOH M . 
RA 4 HOH 89  389 1002 HOH HOH M . 
RA 4 HOH 90  390 962  HOH HOH M . 
RA 4 HOH 91  391 267  HOH HOH M . 
SA 4 HOH 1   301 1078 HOH HOH O . 
SA 4 HOH 2   302 1216 HOH HOH O . 
SA 4 HOH 3   303 971  HOH HOH O . 
SA 4 HOH 4   304 180  HOH HOH O . 
SA 4 HOH 5   305 1212 HOH HOH O . 
SA 4 HOH 6   306 1154 HOH HOH O . 
SA 4 HOH 7   307 837  HOH HOH O . 
SA 4 HOH 8   308 45   HOH HOH O . 
SA 4 HOH 9   309 421  HOH HOH O . 
SA 4 HOH 10  310 1142 HOH HOH O . 
SA 4 HOH 11  311 1198 HOH HOH O . 
SA 4 HOH 12  312 323  HOH HOH O . 
SA 4 HOH 13  313 462  HOH HOH O . 
SA 4 HOH 14  314 1050 HOH HOH O . 
SA 4 HOH 15  315 513  HOH HOH O . 
SA 4 HOH 16  316 1045 HOH HOH O . 
SA 4 HOH 17  317 422  HOH HOH O . 
SA 4 HOH 18  318 524  HOH HOH O . 
SA 4 HOH 19  319 830  HOH HOH O . 
SA 4 HOH 20  320 1112 HOH HOH O . 
SA 4 HOH 21  321 793  HOH HOH O . 
SA 4 HOH 22  322 485  HOH HOH O . 
SA 4 HOH 23  323 552  HOH HOH O . 
SA 4 HOH 24  324 510  HOH HOH O . 
SA 4 HOH 25  325 1117 HOH HOH O . 
SA 4 HOH 26  326 339  HOH HOH O . 
SA 4 HOH 27  327 1268 HOH HOH O . 
TA 4 HOH 1   301 417  HOH HOH Q . 
TA 4 HOH 2   302 163  HOH HOH Q . 
TA 4 HOH 3   303 133  HOH HOH Q . 
TA 4 HOH 4   304 1246 HOH HOH Q . 
TA 4 HOH 5   305 852  HOH HOH Q . 
TA 4 HOH 6   306 904  HOH HOH Q . 
TA 4 HOH 7   307 4    HOH HOH Q . 
TA 4 HOH 8   308 1240 HOH HOH Q . 
TA 4 HOH 9   309 369  HOH HOH Q . 
TA 4 HOH 10  310 966  HOH HOH Q . 
TA 4 HOH 11  311 809  HOH HOH Q . 
TA 4 HOH 12  312 539  HOH HOH Q . 
TA 4 HOH 13  313 75   HOH HOH Q . 
TA 4 HOH 14  314 968  HOH HOH Q . 
TA 4 HOH 15  315 1168 HOH HOH Q . 
TA 4 HOH 16  316 27   HOH HOH Q . 
TA 4 HOH 17  317 418  HOH HOH Q . 
TA 4 HOH 18  318 858  HOH HOH Q . 
TA 4 HOH 19  319 35   HOH HOH Q . 
TA 4 HOH 20  320 29   HOH HOH Q . 
TA 4 HOH 21  321 1021 HOH HOH Q . 
TA 4 HOH 22  322 1109 HOH HOH Q . 
TA 4 HOH 23  323 881  HOH HOH Q . 
TA 4 HOH 24  324 299  HOH HOH Q . 
TA 4 HOH 25  325 333  HOH HOH Q . 
TA 4 HOH 26  326 699  HOH HOH Q . 
TA 4 HOH 27  327 484  HOH HOH Q . 
TA 4 HOH 28  328 992  HOH HOH Q . 
TA 4 HOH 29  329 776  HOH HOH Q . 
TA 4 HOH 30  330 1034 HOH HOH Q . 
TA 4 HOH 31  331 1177 HOH HOH Q . 
TA 4 HOH 32  332 961  HOH HOH Q . 
TA 4 HOH 33  333 1200 HOH HOH Q . 
TA 4 HOH 34  334 1126 HOH HOH Q . 
TA 4 HOH 35  335 530  HOH HOH Q . 
TA 4 HOH 36  336 16   HOH HOH Q . 
TA 4 HOH 37  337 722  HOH HOH Q . 
TA 4 HOH 38  338 189  HOH HOH Q . 
TA 4 HOH 39  339 750  HOH HOH Q . 
TA 4 HOH 40  340 6    HOH HOH Q . 
TA 4 HOH 41  341 828  HOH HOH Q . 
TA 4 HOH 42  342 996  HOH HOH Q . 
TA 4 HOH 43  343 851  HOH HOH Q . 
TA 4 HOH 44  344 216  HOH HOH Q . 
TA 4 HOH 45  345 696  HOH HOH Q . 
TA 4 HOH 46  346 263  HOH HOH Q . 
TA 4 HOH 47  347 1067 HOH HOH Q . 
TA 4 HOH 48  348 287  HOH HOH Q . 
TA 4 HOH 49  349 698  HOH HOH Q . 
TA 4 HOH 50  350 1015 HOH HOH Q . 
TA 4 HOH 51  351 955  HOH HOH Q . 
TA 4 HOH 52  352 547  HOH HOH Q . 
TA 4 HOH 53  353 476  HOH HOH Q . 
TA 4 HOH 54  354 911  HOH HOH Q . 
TA 4 HOH 55  355 836  HOH HOH Q . 
TA 4 HOH 56  356 23   HOH HOH Q . 
TA 4 HOH 57  357 154  HOH HOH Q . 
TA 4 HOH 58  358 80   HOH HOH Q . 
TA 4 HOH 59  359 96   HOH HOH Q . 
TA 4 HOH 60  360 773  HOH HOH Q . 
TA 4 HOH 61  361 1247 HOH HOH Q . 
TA 4 HOH 62  362 743  HOH HOH Q . 
TA 4 HOH 63  363 1196 HOH HOH Q . 
TA 4 HOH 64  364 693  HOH HOH Q . 
TA 4 HOH 65  365 1056 HOH HOH Q . 
TA 4 HOH 66  366 390  HOH HOH Q . 
TA 4 HOH 67  367 226  HOH HOH Q . 
TA 4 HOH 68  368 1228 HOH HOH Q . 
TA 4 HOH 69  369 155  HOH HOH Q . 
TA 4 HOH 70  370 47   HOH HOH Q . 
TA 4 HOH 71  371 1072 HOH HOH Q . 
TA 4 HOH 72  372 450  HOH HOH Q . 
TA 4 HOH 73  373 850  HOH HOH Q . 
TA 4 HOH 74  374 956  HOH HOH Q . 
TA 4 HOH 75  375 605  HOH HOH Q . 
TA 4 HOH 76  376 894  HOH HOH Q . 
TA 4 HOH 77  377 1158 HOH HOH Q . 
TA 4 HOH 78  378 79   HOH HOH Q . 
TA 4 HOH 79  379 439  HOH HOH Q . 
TA 4 HOH 80  380 199  HOH HOH Q . 
TA 4 HOH 81  381 363  HOH HOH Q . 
TA 4 HOH 82  382 1089 HOH HOH Q . 
TA 4 HOH 83  383 1036 HOH HOH Q . 
TA 4 HOH 84  384 434  HOH HOH Q . 
TA 4 HOH 85  385 695  HOH HOH Q . 
TA 4 HOH 86  386 1093 HOH HOH Q . 
TA 4 HOH 87  387 876  HOH HOH Q . 
TA 4 HOH 88  388 1176 HOH HOH Q . 
TA 4 HOH 89  389 665  HOH HOH Q . 
TA 4 HOH 90  390 328  HOH HOH Q . 
TA 4 HOH 91  391 220  HOH HOH Q . 
TA 4 HOH 92  392 1105 HOH HOH Q . 
TA 4 HOH 93  393 1022 HOH HOH Q . 
TA 4 HOH 94  394 707  HOH HOH Q . 
TA 4 HOH 95  395 908  HOH HOH Q . 
TA 4 HOH 96  396 292  HOH HOH Q . 
TA 4 HOH 97  397 824  HOH HOH Q . 
TA 4 HOH 98  398 1244 HOH HOH Q . 
TA 4 HOH 99  399 981  HOH HOH Q . 
TA 4 HOH 100 400 978  HOH HOH Q . 
TA 4 HOH 101 401 872  HOH HOH Q . 
TA 4 HOH 102 402 506  HOH HOH Q . 
TA 4 HOH 103 403 1091 HOH HOH Q . 
UA 4 HOH 1   301 812  HOH HOH S . 
UA 4 HOH 2   302 125  HOH HOH S . 
UA 4 HOH 3   303 438  HOH HOH S . 
UA 4 HOH 4   304 541  HOH HOH S . 
UA 4 HOH 5   305 761  HOH HOH S . 
UA 4 HOH 6   306 770  HOH HOH S . 
UA 4 HOH 7   307 1007 HOH HOH S . 
UA 4 HOH 8   308 17   HOH HOH S . 
UA 4 HOH 9   309 1159 HOH HOH S . 
UA 4 HOH 10  310 143  HOH HOH S . 
UA 4 HOH 11  311 1079 HOH HOH S . 
UA 4 HOH 12  312 86   HOH HOH S . 
UA 4 HOH 13  313 261  HOH HOH S . 
UA 4 HOH 14  314 827  HOH HOH S . 
UA 4 HOH 15  315 392  HOH HOH S . 
UA 4 HOH 16  316 273  HOH HOH S . 
UA 4 HOH 17  317 816  HOH HOH S . 
UA 4 HOH 18  318 413  HOH HOH S . 
UA 4 HOH 19  319 1231 HOH HOH S . 
UA 4 HOH 20  320 684  HOH HOH S . 
UA 4 HOH 21  321 1134 HOH HOH S . 
UA 4 HOH 22  322 214  HOH HOH S . 
UA 4 HOH 23  323 749  HOH HOH S . 
UA 4 HOH 24  324 679  HOH HOH S . 
UA 4 HOH 25  325 1149 HOH HOH S . 
UA 4 HOH 26  326 969  HOH HOH S . 
UA 4 HOH 27  327 266  HOH HOH S . 
UA 4 HOH 28  328 1156 HOH HOH S . 
UA 4 HOH 29  329 820  HOH HOH S . 
UA 4 HOH 30  330 1188 HOH HOH S . 
UA 4 HOH 31  331 1135 HOH HOH S . 
UA 4 HOH 32  332 838  HOH HOH S . 
UA 4 HOH 33  333 1104 HOH HOH S . 
UA 4 HOH 34  334 1172 HOH HOH S . 
UA 4 HOH 35  335 331  HOH HOH S . 
UA 4 HOH 36  336 751  HOH HOH S . 
UA 4 HOH 37  337 151  HOH HOH S . 
UA 4 HOH 38  338 639  HOH HOH S . 
UA 4 HOH 39  339 242  HOH HOH S . 
UA 4 HOH 40  340 1191 HOH HOH S . 
UA 4 HOH 41  341 1042 HOH HOH S . 
UA 4 HOH 42  342 1146 HOH HOH S . 
UA 4 HOH 43  343 602  HOH HOH S . 
UA 4 HOH 44  344 13   HOH HOH S . 
UA 4 HOH 45  345 1064 HOH HOH S . 
UA 4 HOH 46  346 1026 HOH HOH S . 
UA 4 HOH 47  347 1248 HOH HOH S . 
UA 4 HOH 48  348 1111 HOH HOH S . 
UA 4 HOH 49  349 1255 HOH HOH S . 
UA 4 HOH 50  350 57   HOH HOH S . 
UA 4 HOH 51  351 923  HOH HOH S . 
UA 4 HOH 52  352 646  HOH HOH S . 
UA 4 HOH 53  353 1184 HOH HOH S . 
UA 4 HOH 54  354 113  HOH HOH S . 
UA 4 HOH 55  355 402  HOH HOH S . 
UA 4 HOH 56  356 548  HOH HOH S . 
UA 4 HOH 57  357 14   HOH HOH S . 
UA 4 HOH 58  358 1092 HOH HOH S . 
UA 4 HOH 59  359 355  HOH HOH S . 
UA 4 HOH 60  360 746  HOH HOH S . 
UA 4 HOH 61  361 611  HOH HOH S . 
UA 4 HOH 62  362 455  HOH HOH S . 
UA 4 HOH 63  363 1094 HOH HOH S . 
UA 4 HOH 64  364 467  HOH HOH S . 
VA 4 HOH 1   301 30   HOH HOH U . 
VA 4 HOH 2   302 690  HOH HOH U . 
VA 4 HOH 3   303 41   HOH HOH U . 
VA 4 HOH 4   304 69   HOH HOH U . 
VA 4 HOH 5   305 1222 HOH HOH U . 
VA 4 HOH 6   306 175  HOH HOH U . 
VA 4 HOH 7   307 457  HOH HOH U . 
VA 4 HOH 8   308 464  HOH HOH U . 
VA 4 HOH 9   309 1080 HOH HOH U . 
VA 4 HOH 10  310 109  HOH HOH U . 
VA 4 HOH 11  311 727  HOH HOH U . 
VA 4 HOH 12  312 950  HOH HOH U . 
VA 4 HOH 13  313 135  HOH HOH U . 
VA 4 HOH 14  314 480  HOH HOH U . 
VA 4 HOH 15  315 446  HOH HOH U . 
VA 4 HOH 16  316 1224 HOH HOH U . 
VA 4 HOH 17  317 416  HOH HOH U . 
VA 4 HOH 18  318 101  HOH HOH U . 
VA 4 HOH 19  319 1027 HOH HOH U . 
VA 4 HOH 20  320 60   HOH HOH U . 
VA 4 HOH 21  321 1207 HOH HOH U . 
VA 4 HOH 22  322 1223 HOH HOH U . 
VA 4 HOH 23  323 1025 HOH HOH U . 
VA 4 HOH 24  324 789  HOH HOH U . 
VA 4 HOH 25  325 1076 HOH HOH U . 
VA 4 HOH 26  326 41   HOH HOH U . 
VA 4 HOH 27  327 936  HOH HOH U . 
VA 4 HOH 28  328 66   HOH HOH U . 
VA 4 HOH 29  329 305  HOH HOH U . 
VA 4 HOH 30  330 458  HOH HOH U . 
VA 4 HOH 31  331 174  HOH HOH U . 
VA 4 HOH 32  332 832  HOH HOH U . 
VA 4 HOH 33  333 1085 HOH HOH U . 
VA 4 HOH 34  334 516  HOH HOH U . 
VA 4 HOH 35  335 359  HOH HOH U . 
VA 4 HOH 36  336 442  HOH HOH U . 
WA 4 HOH 1   301 792  HOH HOH W . 
WA 4 HOH 2   302 766  HOH HOH W . 
WA 4 HOH 3   303 1186 HOH HOH W . 
WA 4 HOH 4   304 671  HOH HOH W . 
WA 4 HOH 5   305 558  HOH HOH W . 
WA 4 HOH 6   306 758  HOH HOH W . 
WA 4 HOH 7   307 48   HOH HOH W . 
WA 4 HOH 8   308 729  HOH HOH W . 
WA 4 HOH 9   309 190  HOH HOH W . 
WA 4 HOH 10  310 1192 HOH HOH W . 
WA 4 HOH 11  311 615  HOH HOH W . 
WA 4 HOH 12  312 731  HOH HOH W . 
WA 4 HOH 13  313 406  HOH HOH W . 
WA 4 HOH 14  314 839  HOH HOH W . 
WA 4 HOH 15  315 947  HOH HOH W . 
WA 4 HOH 16  316 921  HOH HOH W . 
WA 4 HOH 17  317 231  HOH HOH W . 
WA 4 HOH 18  318 85   HOH HOH W . 
WA 4 HOH 19  319 730  HOH HOH W . 
WA 4 HOH 20  320 864  HOH HOH W . 
WA 4 HOH 21  321 4    HOH HOH W . 
WA 4 HOH 22  322 835  HOH HOH W . 
WA 4 HOH 23  323 869  HOH HOH W . 
WA 4 HOH 24  324 1106 HOH HOH W . 
WA 4 HOH 25  325 983  HOH HOH W . 
WA 4 HOH 26  326 1018 HOH HOH W . 
WA 4 HOH 27  327 435  HOH HOH W . 
WA 4 HOH 28  328 941  HOH HOH W . 
WA 4 HOH 29  329 1039 HOH HOH W . 
WA 4 HOH 30  330 2    HOH HOH W . 
WA 4 HOH 31  331 342  HOH HOH W . 
WA 4 HOH 32  332 218  HOH HOH W . 
WA 4 HOH 33  333 360  HOH HOH W . 
WA 4 HOH 34  334 593  HOH HOH W . 
WA 4 HOH 35  335 491  HOH HOH W . 
WA 4 HOH 36  336 31   HOH HOH W . 
WA 4 HOH 37  337 55   HOH HOH W . 
WA 4 HOH 38  338 550  HOH HOH W . 
WA 4 HOH 39  339 50   HOH HOH W . 
WA 4 HOH 40  340 753  HOH HOH W . 
WA 4 HOH 41  341 97   HOH HOH W . 
WA 4 HOH 42  342 489  HOH HOH W . 
WA 4 HOH 43  343 563  HOH HOH W . 
WA 4 HOH 44  344 543  HOH HOH W . 
WA 4 HOH 45  345 1199 HOH HOH W . 
WA 4 HOH 46  346 1054 HOH HOH W . 
WA 4 HOH 47  347 742  HOH HOH W . 
WA 4 HOH 48  348 207  HOH HOH W . 
WA 4 HOH 49  349 40   HOH HOH W . 
WA 4 HOH 50  350 110  HOH HOH W . 
WA 4 HOH 51  351 930  HOH HOH W . 
WA 4 HOH 52  352 350  HOH HOH W . 
WA 4 HOH 53  353 637  HOH HOH W . 
WA 4 HOH 54  354 1189 HOH HOH W . 
WA 4 HOH 55  355 979  HOH HOH W . 
WA 4 HOH 56  356 1003 HOH HOH W . 
WA 4 HOH 57  357 621  HOH HOH W . 
WA 4 HOH 58  358 1101 HOH HOH W . 
WA 4 HOH 59  359 354  HOH HOH W . 
WA 4 HOH 60  360 650  HOH HOH W . 
WA 4 HOH 61  361 587  HOH HOH W . 
WA 4 HOH 62  362 145  HOH HOH W . 
WA 4 HOH 63  363 219  HOH HOH W . 
WA 4 HOH 64  364 867  HOH HOH W . 
WA 4 HOH 65  365 748  HOH HOH W . 
WA 4 HOH 66  366 170  HOH HOH W . 
WA 4 HOH 67  367 1086 HOH HOH W . 
WA 4 HOH 68  368 917  HOH HOH W . 
WA 4 HOH 69  369 847  HOH HOH W . 
WA 4 HOH 70  370 1151 HOH HOH W . 
WA 4 HOH 71  371 381  HOH HOH W . 
WA 4 HOH 72  372 253  HOH HOH W . 
WA 4 HOH 73  373 1006 HOH HOH W . 
WA 4 HOH 74  374 1148 HOH HOH W . 
WA 4 HOH 75  375 806  HOH HOH W . 
WA 4 HOH 76  376 444  HOH HOH W . 
WA 4 HOH 77  377 726  HOH HOH W . 
WA 4 HOH 78  378 8    HOH HOH W . 
WA 4 HOH 79  379 358  HOH HOH W . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
6 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,M,N,O,P,Q,LA,MA      
2 1 C,D,R,S,T,U,NA,OA        
3 1 E,F,V,W,X,Y,PA,QA        
4 1 G,H,Z,AA,BA,RA,SA        
5 1 I,J,CA,DA,EA,FA,GA,TA,UA 
6 1 K,L,HA,IA,JA,KA,VA,WA    
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1810  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  13990 ? 
2 'ABSA (A^2)' 1830  ? 
2 MORE         -42   ? 
2 'SSA (A^2)'  14190 ? 
3 'ABSA (A^2)' 1830  ? 
3 MORE         -44   ? 
3 'SSA (A^2)'  14030 ? 
4 'ABSA (A^2)' 1750  ? 
4 MORE         -34   ? 
4 'SSA (A^2)'  14080 ? 
5 'ABSA (A^2)' 1920  ? 
5 MORE         -50   ? 
5 'SSA (A^2)'  13910 ? 
6 'ABSA (A^2)' 1790  ? 
6 MORE         -45   ? 
6 'SSA (A^2)'  13800 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 106.6 ? 
2  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 109.0 ? 
3  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 124.8 ? 
4  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 102.2 ? 
5  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 93.2  ? 
6  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 118.1 ? 
7  ND1 ? B HIS 63 ? F HIS 63 ? 1_555 ZN ? O  ZN . ? F ZN 201 ? 1_555 ND1 ? B HIS 71 ? F HIS 71 ? 1_555 105.0 ? 
8  ND1 ? B HIS 63 ? F HIS 63 ? 1_555 ZN ? O  ZN . ? F ZN 201 ? 1_555 ND1 ? B HIS 80 ? F HIS 80 ? 1_555 110.8 ? 
9  ND1 ? B HIS 71 ? F HIS 71 ? 1_555 ZN ? O  ZN . ? F ZN 201 ? 1_555 ND1 ? B HIS 80 ? F HIS 80 ? 1_555 124.8 ? 
10 ND1 ? B HIS 63 ? F HIS 63 ? 1_555 ZN ? O  ZN . ? F ZN 201 ? 1_555 OD1 ? B ASP 83 ? F ASP 83 ? 1_555 104.6 ? 
11 ND1 ? B HIS 71 ? F HIS 71 ? 1_555 ZN ? O  ZN . ? F ZN 201 ? 1_555 OD1 ? B ASP 83 ? F ASP 83 ? 1_555 90.1  ? 
12 ND1 ? B HIS 80 ? F HIS 80 ? 1_555 ZN ? O  ZN . ? F ZN 201 ? 1_555 OD1 ? B ASP 83 ? F ASP 83 ? 1_555 118.4 ? 
13 ND1 ? C HIS 63 ? D HIS 63 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 ND1 ? C HIS 71 ? D HIS 71 ? 1_555 105.1 ? 
14 ND1 ? C HIS 63 ? D HIS 63 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 ND1 ? C HIS 80 ? D HIS 80 ? 1_555 108.3 ? 
15 ND1 ? C HIS 71 ? D HIS 71 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 ND1 ? C HIS 80 ? D HIS 80 ? 1_555 125.3 ? 
16 ND1 ? C HIS 63 ? D HIS 63 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 OD1 ? C ASP 83 ? D ASP 83 ? 1_555 109.4 ? 
17 ND1 ? C HIS 71 ? D HIS 71 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 OD1 ? C ASP 83 ? D ASP 83 ? 1_555 89.7  ? 
18 ND1 ? C HIS 80 ? D HIS 80 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 OD1 ? C ASP 83 ? D ASP 83 ? 1_555 117.2 ? 
19 ND1 ? D HIS 63 ? G HIS 63 ? 1_555 ZN ? T  ZN . ? G ZN 201 ? 1_555 ND1 ? D HIS 71 ? G HIS 71 ? 1_555 106.1 ? 
20 ND1 ? D HIS 63 ? G HIS 63 ? 1_555 ZN ? T  ZN . ? G ZN 201 ? 1_555 ND1 ? D HIS 80 ? G HIS 80 ? 1_555 108.2 ? 
21 ND1 ? D HIS 71 ? G HIS 71 ? 1_555 ZN ? T  ZN . ? G ZN 201 ? 1_555 ND1 ? D HIS 80 ? G HIS 80 ? 1_555 121.2 ? 
22 ND1 ? D HIS 63 ? G HIS 63 ? 1_555 ZN ? T  ZN . ? G ZN 201 ? 1_555 OD1 ? D ASP 83 ? G ASP 83 ? 1_555 106.6 ? 
23 ND1 ? D HIS 71 ? G HIS 71 ? 1_555 ZN ? T  ZN . ? G ZN 201 ? 1_555 OD1 ? D ASP 83 ? G ASP 83 ? 1_555 95.0  ? 
24 ND1 ? D HIS 80 ? G HIS 80 ? 1_555 ZN ? T  ZN . ? G ZN 201 ? 1_555 OD1 ? D ASP 83 ? G ASP 83 ? 1_555 118.1 ? 
25 ND1 ? E HIS 63 ? I HIS 63 ? 1_555 ZN ? V  ZN . ? I ZN 201 ? 1_555 ND1 ? E HIS 71 ? I HIS 71 ? 1_555 102.1 ? 
26 ND1 ? E HIS 63 ? I HIS 63 ? 1_555 ZN ? V  ZN . ? I ZN 201 ? 1_555 ND1 ? E HIS 80 ? I HIS 80 ? 1_555 112.1 ? 
27 ND1 ? E HIS 71 ? I HIS 71 ? 1_555 ZN ? V  ZN . ? I ZN 201 ? 1_555 ND1 ? E HIS 80 ? I HIS 80 ? 1_555 122.7 ? 
28 ND1 ? E HIS 63 ? I HIS 63 ? 1_555 ZN ? V  ZN . ? I ZN 201 ? 1_555 OD1 ? E ASP 83 ? I ASP 83 ? 1_555 104.5 ? 
29 ND1 ? E HIS 71 ? I HIS 71 ? 1_555 ZN ? V  ZN . ? I ZN 201 ? 1_555 OD1 ? E ASP 83 ? I ASP 83 ? 1_555 88.1  ? 
30 ND1 ? E HIS 80 ? I HIS 80 ? 1_555 ZN ? V  ZN . ? I ZN 201 ? 1_555 OD1 ? E ASP 83 ? I ASP 83 ? 1_555 123.3 ? 
31 ND1 ? F HIS 63 ? K HIS 63 ? 1_555 ZN ? X  ZN . ? K ZN 201 ? 1_555 ND1 ? F HIS 71 ? K HIS 71 ? 1_555 102.9 ? 
32 ND1 ? F HIS 63 ? K HIS 63 ? 1_555 ZN ? X  ZN . ? K ZN 201 ? 1_555 ND1 ? F HIS 80 ? K HIS 80 ? 1_555 109.0 ? 
33 ND1 ? F HIS 71 ? K HIS 71 ? 1_555 ZN ? X  ZN . ? K ZN 201 ? 1_555 ND1 ? F HIS 80 ? K HIS 80 ? 1_555 131.1 ? 
34 ND1 ? F HIS 63 ? K HIS 63 ? 1_555 ZN ? X  ZN . ? K ZN 201 ? 1_555 OD1 ? F ASP 83 ? K ASP 83 ? 1_555 106.3 ? 
35 ND1 ? F HIS 71 ? K HIS 71 ? 1_555 ZN ? X  ZN . ? K ZN 201 ? 1_555 OD1 ? F ASP 83 ? K ASP 83 ? 1_555 99.8  ? 
36 ND1 ? F HIS 80 ? K HIS 80 ? 1_555 ZN ? X  ZN . ? K ZN 201 ? 1_555 OD1 ? F ASP 83 ? K ASP 83 ? 1_555 105.6 ? 
37 ND1 ? G HIS 63 ? M HIS 63 ? 1_555 ZN ? Z  ZN . ? M ZN 201 ? 1_555 ND1 ? G HIS 71 ? M HIS 71 ? 1_555 105.6 ? 
38 ND1 ? G HIS 63 ? M HIS 63 ? 1_555 ZN ? Z  ZN . ? M ZN 201 ? 1_555 ND1 ? G HIS 80 ? M HIS 80 ? 1_555 109.6 ? 
39 ND1 ? G HIS 71 ? M HIS 71 ? 1_555 ZN ? Z  ZN . ? M ZN 201 ? 1_555 ND1 ? G HIS 80 ? M HIS 80 ? 1_555 120.5 ? 
40 ND1 ? G HIS 63 ? M HIS 63 ? 1_555 ZN ? Z  ZN . ? M ZN 201 ? 1_555 OD1 ? G ASP 83 ? M ASP 83 ? 1_555 100.1 ? 
41 ND1 ? G HIS 71 ? M HIS 71 ? 1_555 ZN ? Z  ZN . ? M ZN 201 ? 1_555 OD1 ? G ASP 83 ? M ASP 83 ? 1_555 97.0  ? 
42 ND1 ? G HIS 80 ? M HIS 80 ? 1_555 ZN ? Z  ZN . ? M ZN 201 ? 1_555 OD1 ? G ASP 83 ? M ASP 83 ? 1_555 121.3 ? 
43 ND1 ? H HIS 63 ? O HIS 63 ? 1_555 ZN ? BA ZN . ? O ZN 201 ? 1_555 ND1 ? H HIS 71 ? O HIS 71 ? 1_555 96.2  ? 
44 ND1 ? H HIS 63 ? O HIS 63 ? 1_555 ZN ? BA ZN . ? O ZN 201 ? 1_555 ND1 ? H HIS 80 ? O HIS 80 ? 1_555 118.5 ? 
45 ND1 ? H HIS 71 ? O HIS 71 ? 1_555 ZN ? BA ZN . ? O ZN 201 ? 1_555 ND1 ? H HIS 80 ? O HIS 80 ? 1_555 124.5 ? 
46 ND1 ? H HIS 63 ? O HIS 63 ? 1_555 ZN ? BA ZN . ? O ZN 201 ? 1_555 OD1 ? H ASP 83 ? O ASP 83 ? 1_555 97.3  ? 
47 ND1 ? H HIS 71 ? O HIS 71 ? 1_555 ZN ? BA ZN . ? O ZN 201 ? 1_555 OD1 ? H ASP 83 ? O ASP 83 ? 1_555 86.8  ? 
48 ND1 ? H HIS 80 ? O HIS 80 ? 1_555 ZN ? BA ZN . ? O ZN 201 ? 1_555 OD1 ? H ASP 83 ? O ASP 83 ? 1_555 125.6 ? 
49 ND1 ? I HIS 63 ? Q HIS 63 ? 1_555 ZN ? CA ZN . ? Q ZN 201 ? 1_555 ND1 ? I HIS 71 ? Q HIS 71 ? 1_555 106.7 ? 
50 ND1 ? I HIS 63 ? Q HIS 63 ? 1_555 ZN ? CA ZN . ? Q ZN 201 ? 1_555 ND1 ? I HIS 80 ? Q HIS 80 ? 1_555 109.8 ? 
51 ND1 ? I HIS 71 ? Q HIS 71 ? 1_555 ZN ? CA ZN . ? Q ZN 201 ? 1_555 ND1 ? I HIS 80 ? Q HIS 80 ? 1_555 121.3 ? 
52 ND1 ? I HIS 63 ? Q HIS 63 ? 1_555 ZN ? CA ZN . ? Q ZN 201 ? 1_555 OD1 ? I ASP 83 ? Q ASP 83 ? 1_555 101.8 ? 
53 ND1 ? I HIS 71 ? Q HIS 71 ? 1_555 ZN ? CA ZN . ? Q ZN 201 ? 1_555 OD1 ? I ASP 83 ? Q ASP 83 ? 1_555 94.5  ? 
54 ND1 ? I HIS 80 ? Q HIS 80 ? 1_555 ZN ? CA ZN . ? Q ZN 201 ? 1_555 OD1 ? I ASP 83 ? Q ASP 83 ? 1_555 120.1 ? 
55 ND1 ? J HIS 63 ? S HIS 63 ? 1_555 ZN ? FA ZN . ? S ZN 201 ? 1_555 ND1 ? J HIS 71 ? S HIS 71 ? 1_555 100.5 ? 
56 ND1 ? J HIS 63 ? S HIS 63 ? 1_555 ZN ? FA ZN . ? S ZN 201 ? 1_555 ND1 ? J HIS 80 ? S HIS 80 ? 1_555 113.0 ? 
57 ND1 ? J HIS 71 ? S HIS 71 ? 1_555 ZN ? FA ZN . ? S ZN 201 ? 1_555 ND1 ? J HIS 80 ? S HIS 80 ? 1_555 123.9 ? 
58 ND1 ? J HIS 63 ? S HIS 63 ? 1_555 ZN ? FA ZN . ? S ZN 201 ? 1_555 OD1 ? J ASP 83 ? S ASP 83 ? 1_555 96.4  ? 
59 ND1 ? J HIS 71 ? S HIS 71 ? 1_555 ZN ? FA ZN . ? S ZN 201 ? 1_555 OD1 ? J ASP 83 ? S ASP 83 ? 1_555 92.9  ? 
60 ND1 ? J HIS 80 ? S HIS 80 ? 1_555 ZN ? FA ZN . ? S ZN 201 ? 1_555 OD1 ? J ASP 83 ? S ASP 83 ? 1_555 124.5 ? 
61 ND1 ? K HIS 63 ? U HIS 63 ? 1_555 ZN ? HA ZN . ? U ZN 201 ? 1_555 ND1 ? K HIS 71 ? U HIS 71 ? 1_555 97.2  ? 
62 ND1 ? K HIS 63 ? U HIS 63 ? 1_555 ZN ? HA ZN . ? U ZN 201 ? 1_555 ND1 ? K HIS 80 ? U HIS 80 ? 1_555 108.2 ? 
63 ND1 ? K HIS 71 ? U HIS 71 ? 1_555 ZN ? HA ZN . ? U ZN 201 ? 1_555 ND1 ? K HIS 80 ? U HIS 80 ? 1_555 128.9 ? 
64 ND1 ? K HIS 63 ? U HIS 63 ? 1_555 ZN ? HA ZN . ? U ZN 201 ? 1_555 OD1 ? K ASP 83 ? U ASP 83 ? 1_555 103.3 ? 
65 ND1 ? K HIS 71 ? U HIS 71 ? 1_555 ZN ? HA ZN . ? U ZN 201 ? 1_555 OD1 ? K ASP 83 ? U ASP 83 ? 1_555 81.6  ? 
66 ND1 ? K HIS 80 ? U HIS 80 ? 1_555 ZN ? HA ZN . ? U ZN 201 ? 1_555 OD1 ? K ASP 83 ? U ASP 83 ? 1_555 131.1 ? 
67 ND1 ? L HIS 63 ? W HIS 63 ? 1_555 ZN ? JA ZN . ? W ZN 201 ? 1_555 ND1 ? L HIS 71 ? W HIS 71 ? 1_555 105.1 ? 
68 ND1 ? L HIS 63 ? W HIS 63 ? 1_555 ZN ? JA ZN . ? W ZN 201 ? 1_555 ND1 ? L HIS 80 ? W HIS 80 ? 1_555 104.9 ? 
69 ND1 ? L HIS 71 ? W HIS 71 ? 1_555 ZN ? JA ZN . ? W ZN 201 ? 1_555 ND1 ? L HIS 80 ? W HIS 80 ? 1_555 128.5 ? 
70 ND1 ? L HIS 63 ? W HIS 63 ? 1_555 ZN ? JA ZN . ? W ZN 201 ? 1_555 OD1 ? L ASP 83 ? W ASP 83 ? 1_555 106.7 ? 
71 ND1 ? L HIS 71 ? W HIS 71 ? 1_555 ZN ? JA ZN . ? W ZN 201 ? 1_555 OD1 ? L ASP 83 ? W ASP 83 ? 1_555 98.0  ? 
72 ND1 ? L HIS 80 ? W HIS 80 ? 1_555 ZN ? JA ZN . ? W ZN 201 ? 1_555 OD1 ? L ASP 83 ? W ASP 83 ? 1_555 112.0 ? 
# 
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 2019-01-30 
2 'Structure model' 1 1 2019-06-19 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation           
2 2 'Structure model' citation_author    
3 2 'Structure model' pdbx_database_proc 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_citation_author.identifier_ORCID' 
13 2 'Structure model' '_citation_author.name'             
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 23.6078  42.5184  15.4422 0.1765 0.2059 0.2909 -0.0102 -0.0371 0.0228  1.8412 2.4714 3.3766 
0.3680  -0.3997 -1.3378 0.0234  0.0025  0.1588  0.0584  -0.0839 -0.0380 -0.3328 0.1076  0.0604  
'X-RAY DIFFRACTION' 2  ? refined -13.1199 48.9770  20.6001 0.1941 0.2344 0.3487 0.0114  -0.0245 -0.0166 1.6548 3.5759 2.1987 
-0.0742 -0.2430 0.4257  0.0026  -0.0502 0.2090  -0.4540 -0.0044 0.1513  -0.2034 -0.0583 0.0018  
'X-RAY DIFFRACTION' 3  ? refined 21.2758  20.6026  32.3746 0.0020 0.2490 0.2987 0.0027  0.0000  0.0502  2.1982 2.1807 3.0071 
-0.3428 -0.0559 -0.9793 0.0432  -0.1396 -0.1123 -0.0070 -0.0330 0.0591  0.0416  -0.0767 -0.0103 
'X-RAY DIFFRACTION' 4  ? refined -15.6033 23.0586  30.4817 0.0093 0.3564 0.2477 0.0410  -0.0031 0.0468  2.0934 2.8868 1.5803 
0.3003  -0.7052 -0.2007 -0.0274 -0.2898 0.1163  -0.0884 0.0339  -0.0895 0.0516  0.1682  -0.0065 
'X-RAY DIFFRACTION' 5  ? refined 21.9944  -37.0682 28.6700 0.5961 0.3855 0.4701 0.2293  0.0943  0.0542  1.3115 4.7566 3.0518 
-0.2424 -0.1800 0.3796  0.3587  0.2742  -0.1369 -0.8609 -0.3260 -0.5610 -0.0943 0.0227  -0.0328 
'X-RAY DIFFRACTION' 6  ? refined 20.4239  -11.1513 38.5848 0.2526 0.3388 0.3295 0.0982  0.1022  0.1640  2.0596 4.6455 1.7000 
-0.1883 0.8318  -0.5855 0.3387  -0.0790 -0.0714 -0.6053 -0.4572 -0.5753 0.3118  0.0810  0.1186  
'X-RAY DIFFRACTION' 7  ? refined 14.9167  9.9617   62.1134 0.1855 0.4539 0.2713 -0.0327 -0.0632 0.0540  2.1501 3.1592 3.5294 
-0.0948 -0.6658 0.7656  0.0576  -0.3305 0.2121  0.3098  -0.0616 -0.2382 -0.2938 0.0142  0.0040  
'X-RAY DIFFRACTION' 8  ? refined 7.8361   13.4612  88.6088 0.6623 1.0555 0.2712 -0.0407 -0.1058 -0.0441 2.8382 3.3102 2.4563 
0.1132  -0.4105 0.4241  0.0549  -0.8669 0.2345  0.7333  -0.1186 -0.1643 -0.2265 -0.0980 0.0637  
'X-RAY DIFFRACTION' 9  ? refined -20.5521 2.0853   54.0808 0.1294 0.5777 0.2279 0.0121  0.0333  0.0849  4.5271 2.7787 2.9865 
0.2021  0.7908  -1.0242 0.0862  -0.9438 -0.3185 0.1759  -0.0319 0.0967  0.1993  -0.2644 -0.0544 
'X-RAY DIFFRACTION' 10 ? refined -25.2558 -0.4199  81.4884 0.4372 0.5933 0.3934 -0.0285 0.0738  0.0250  2.7111 2.2810 5.2207 
-0.2763 0.2392  -0.2994 0.0062  -0.2932 -0.0314 0.1115  -0.0214 0.1873  0.1448  -0.5369 0.0152  
'X-RAY DIFFRACTION' 11 ? refined -6.6190  -28.3876 6.5199  0.8194 0.5530 0.6931 0.0380  -0.0856 -0.1293 2.3083 3.7155 3.0850 
-1.2888 0.6847  -0.1706 0.1001  0.4387  -0.6309 -0.3381 -0.0524 0.1690  0.8363  -0.0886 -0.0477 
'X-RAY DIFFRACTION' 12 ? refined -13.4209 -7.9372  24.0597 0.3755 0.4328 0.3581 0.1131  -0.0905 -0.0127 1.9598 1.5738 4.3138 
-0.8226 0.1880  0.3311  0.2728  0.4525  -0.2604 -0.3438 -0.2392 0.1552  0.4735  -0.1404 -0.0336 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  A 1 ? ? A 153 ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  D 1 ? ? D 153 ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  F 1 ? ? F 153 ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  G 1 ? ? G 153 ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  I 1 ? ? I 153 ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  K 1 ? ? K 153 ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  M 1 ? ? M 153 ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  O 1 ? ? O 153 ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  Q 1 ? ? Q 153 ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 S 1 ? ? S 153 ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 U 1 ? ? U 153 ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 W 2 ? ? W 153 ? ? ? ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0189 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER D 98  ? ? -153.27 89.88  
2  1 ASN G 65  ? ? -147.60 59.58  
3  1 SER I 98  ? ? -152.35 89.23  
4  1 ALA M 55  ? ? -112.90 53.47  
5  1 ALA O 55  ? ? -108.58 46.51  
6  1 ALA Q 55  ? ? -112.44 54.86  
7  1 ALA S 55  ? ? -114.17 52.06  
8  1 ASN S 65  ? ? -151.82 67.46  
9  1 SER S 98  ? ? -158.77 88.08  
10 1 LYS S 136 ? ? -108.02 -60.85 
11 1 SER U 98  ? ? -161.07 63.51  
12 1 LEU U 126 ? ? 70.49   39.90  
13 1 ALA W 55  ? ? -97.90  53.32  
14 1 SER W 98  ? ? -153.12 89.41  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 437 ? 6.97 . 
2  1 O ? F HOH 453 ? 6.33 . 
3  1 O ? F HOH 454 ? 6.53 . 
4  1 O ? F HOH 455 ? 6.76 . 
5  1 O ? F HOH 456 ? 7.89 . 
6  1 O ? D HOH 425 ? 6.78 . 
7  1 O ? I HOH 338 ? 8.09 . 
8  1 O ? K HOH 379 ? 8.70 . 
9  1 O ? K HOH 380 ? 9.26 . 
10 1 O ? O HOH 327 ? 7.45 . 
11 1 O ? S HOH 363 ? 5.90 . 
12 1 O ? S HOH 364 ? 6.87 . 
13 1 O ? U HOH 334 ? 6.58 . 
14 1 O ? U HOH 335 ? 8.30 . 
15 1 O ? U HOH 336 ? 8.63 . 
16 1 O ? W HOH 379 ? 6.82 . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 I GLU 24  ? CG  ? E GLU 24  CG  
2  1 Y 1 I GLU 24  ? CD  ? E GLU 24  CD  
3  1 Y 1 I GLU 24  ? OE1 ? E GLU 24  OE1 
4  1 Y 1 I GLU 24  ? OE2 ? E GLU 24  OE2 
5  1 Y 1 O LYS 122 ? CG  ? H LYS 122 CG  
6  1 Y 1 O LYS 122 ? CD  ? H LYS 122 CD  
7  1 Y 1 O LYS 122 ? CE  ? H LYS 122 CE  
8  1 Y 1 O LYS 122 ? NZ  ? H LYS 122 NZ  
9  1 Y 1 O LEU 144 ? CG  ? H LEU 144 CG  
10 1 Y 1 O LEU 144 ? CD1 ? H LEU 144 CD1 
11 1 Y 1 O LEU 144 ? CD2 ? H LEU 144 CD2 
12 1 Y 1 S LYS 91  ? CG  ? J LYS 91  CG  
13 1 Y 1 S LYS 91  ? CD  ? J LYS 91  CD  
14 1 Y 1 S LYS 91  ? CE  ? J LYS 91  CE  
15 1 Y 1 S LYS 91  ? NZ  ? J LYS 91  NZ  
16 1 Y 1 U GLU 40  ? CG  ? K GLU 40  CG  
17 1 Y 1 U GLU 40  ? CD  ? K GLU 40  CD  
18 1 Y 1 U GLU 40  ? OE1 ? K GLU 40  OE1 
19 1 Y 1 U GLU 40  ? OE2 ? K GLU 40  OE2 
20 1 Y 1 U LYS 91  ? CG  ? K LYS 91  CG  
21 1 Y 1 U LYS 91  ? CD  ? K LYS 91  CD  
22 1 Y 1 U LYS 91  ? CE  ? K LYS 91  CE  
23 1 Y 1 U LYS 91  ? NZ  ? K LYS 91  NZ  
24 1 Y 1 U ASP 109 ? CG  ? K ASP 109 CG  
25 1 Y 1 U ASP 109 ? OD1 ? K ASP 109 OD1 
26 1 Y 1 U ASP 109 ? OD2 ? K ASP 109 OD2 
27 1 Y 1 U LYS 128 ? CG  ? K LYS 128 CG  
28 1 Y 1 U LYS 128 ? CD  ? K LYS 128 CD  
29 1 Y 1 U LYS 128 ? CE  ? K LYS 128 CE  
30 1 Y 1 U LYS 128 ? NZ  ? K LYS 128 NZ  
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     W 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     ALA 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    L 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    ALA 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Motor Neurone Disease Association'                                    'United Kingdom' Hasnain/Apr15/833-791 1 
'Medical Research Council (United Kingdom)'                            'United Kingdom' MRF-060-0002-RG-HASNA 2 
'Sao Paulo Research Fundation'                                         Brazil           2015/00062-1          3 
'Sao Paulo Research Fundation'                                         Brazil           2016/24686-7          4 
'National Council for Scientific and Technological Development'        Brazil           407438/2013-0         5 
'National Council for Scientific and Technological Development (CNPq)' Brazil           407438/2013-0         6 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'    ZN  
3 'SULFATE ION' SO4 
4 water         HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
