data_3MON
# 
_entry.id   3MON 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3MON         
WWPDB D_1000179058 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             1993-10-15 
_pdbx_database_PDB_obs_spr.pdb_id           3MON 
_pdbx_database_PDB_obs_spr.replace_pdb_id   1MON 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3MON 
_pdbx_database_status.recvd_initial_deposition_date   1992-08-26 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Jiang, F.'  1 
'Tong, L.'   2 
'Kim, S.-H.' 3 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Crystal structures of two intensely sweet proteins.'                         'Trends Biochem.Sci.' 13  13    15 1988 
TBSCDB NE 0968-0004 0946 ? 3072690 '10.1016/0968-0004(88)90011-4' 
1       'Crystal Structure of the Intensely Sweet Protein Monellin'                   Nature                328 739   ?  1987 
NATUAS UK 0028-0836 0006 ? ?       ?                              
2       'Crystal Structure of a Sweet Protein, Monellin, at 5.5-Angstroms Resolution' Biochemistry          22  5772  ?  1983 
BICHAW US 0006-2960 0033 ? ?       ?                              
3       'Preliminary Crystallographic Studies of a Sweet Protein, Monellin'           J.Biol.Chem.          256 12476 ?  1981 
JBCHA3 US 0021-9258 0071 ? ?       ?                              
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kim, S.H.'     1  
primary 'de Vos, A.'    2  
primary 'Ogata, C.'     3  
1       'Ogata, C.'     4  
1       'Hatada, M.'    5  
1       'Tomlinson, G.' 6  
1       'Shin, W.-C.'   7  
1       'Kim, S.-H.'    8  
2       'Tomlinson, G.' 9  
2       'Ogata, C.'     10 
2       'Shin, W.-C.'   11 
2       'Kim, S.-H.'    12 
3       'Tomlinson, G.' 13 
3       'Kim, S.-H.'    14 
# 
_cell.entry_id           3MON 
_cell.length_a           39.840 
_cell.length_b           87.200 
_cell.length_c           72.060 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        107.30 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         3MON 
_symmetry.space_group_name_H-M             'P 1 1 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man MONELLIN 5259.993 4 ? ? ? ? 
2 polymer man MONELLIN 5841.647 4 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no REIKGYEYQLYVYASDKLFRADISEDYKTRGRKLLRFNGPVPPP       REIKGYEYQLYVYASDKLFRADISEDYKTRGRKLLRFNGPVPPP       
A,C,E,G ? 
2 'polypeptide(L)' no no GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYENE GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYENE 
B,D,F,H ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  ARG n 
1 2  GLU n 
1 3  ILE n 
1 4  LYS n 
1 5  GLY n 
1 6  TYR n 
1 7  GLU n 
1 8  TYR n 
1 9  GLN n 
1 10 LEU n 
1 11 TYR n 
1 12 VAL n 
1 13 TYR n 
1 14 ALA n 
1 15 SER n 
1 16 ASP n 
1 17 LYS n 
1 18 LEU n 
1 19 PHE n 
1 20 ARG n 
1 21 ALA n 
1 22 ASP n 
1 23 ILE n 
1 24 SER n 
1 25 GLU n 
1 26 ASP n 
1 27 TYR n 
1 28 LYS n 
1 29 THR n 
1 30 ARG n 
1 31 GLY n 
1 32 ARG n 
1 33 LYS n 
1 34 LEU n 
1 35 LEU n 
1 36 ARG n 
1 37 PHE n 
1 38 ASN n 
1 39 GLY n 
1 40 PRO n 
1 41 VAL n 
1 42 PRO n 
1 43 PRO n 
1 44 PRO n 
2 1  GLY n 
2 2  GLU n 
2 3  TRP n 
2 4  GLU n 
2 5  ILE n 
2 6  ILE n 
2 7  ASP n 
2 8  ILE n 
2 9  GLY n 
2 10 PRO n 
2 11 PHE n 
2 12 THR n 
2 13 GLN n 
2 14 ASN n 
2 15 LEU n 
2 16 GLY n 
2 17 LYS n 
2 18 PHE n 
2 19 ALA n 
2 20 VAL n 
2 21 ASP n 
2 22 GLU n 
2 23 GLU n 
2 24 ASN n 
2 25 LYS n 
2 26 ILE n 
2 27 GLY n 
2 28 GLN n 
2 29 TYR n 
2 30 GLY n 
2 31 ARG n 
2 32 LEU n 
2 33 THR n 
2 34 PHE n 
2 35 ASN n 
2 36 LYS n 
2 37 VAL n 
2 38 ILE n 
2 39 ARG n 
2 40 PRO n 
2 41 CYS n 
2 42 MET n 
2 43 LYS n 
2 44 LYS n 
2 45 THR n 
2 46 ILE n 
2 47 TYR n 
2 48 GLU n 
2 49 ASN n 
2 50 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample ? ? ? 'serendipity berry' ? ? ? ? ? ? ? ? 'Dioscoreophyllum cumminsii' 3457 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? 'serendipity berry' ? ? ? ? ? ? ? ? 'Dioscoreophyllum cumminsii' 3457 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_db_isoform 
1 UNP MONA_DIOCU 1 P02881 1 FREIKGYEYQLYVYASDKLFRADISEDYKTRGRKLLRFNGPVPPP      ? 
2 UNP MONB_DIOCU 2 P02882 1 GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYEEN ? 
# 
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 3MON A 1 ? 44 ? P02881 2 ? 45 ? 2 45 
2 2 3MON B 1 ? 49 ? P02882 1 ? 50 ? 1 49 
3 1 3MON C 1 ? 44 ? P02881 2 ? 45 ? 2 45 
4 2 3MON D 1 ? 49 ? P02882 1 ? 50 ? 1 49 
5 1 3MON E 1 ? 44 ? P02881 2 ? 45 ? 2 45 
6 2 3MON F 1 ? 49 ? P02882 1 ? 50 ? 1 49 
7 1 3MON G 1 ? 44 ? P02881 2 ? 45 ? 2 45 
8 2 3MON H 1 ? 49 ? P02882 1 ? 50 ? 1 49 
# 
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 
2 3MON ? B ? ? UNP P02882 GLU 48 DELETION ? 1 
4 3MON ? D ? ? UNP P02882 GLU 48 DELETION ? 2 
6 3MON ? F ? ? UNP P02882 GLU 48 DELETION ? 3 
8 3MON ? H ? ? UNP P02882 GLU 48 DELETION ? 4 
# 
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  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3MON 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.69 
_exptl_crystal.density_percent_sol   54.27 
_exptl_crystal.description           ? 
# 
_refine.entry_id                                 3MON 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            2.8 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1930000 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  
;PLEASE NOTE THAT THE SPACE GROUP GROUP SETTING USED IN THIS
ENTRY IS THE FIRST SETTING (Z-AXIS UNIQUE).
;
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3136 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3136 
_refine_hist.d_res_high                       2.8 
_refine_hist.d_res_low                        . 
# 
_struct.entry_id                  3MON 
_struct.title                     'CRYSTAL STRUCTURES OF TWO INTENSELY SWEET PROTEINS' 
_struct.pdbx_descriptor           MONELLIN 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3MON 
_struct_keywords.pdbx_keywords   'SWEET-TASTING PROTEIN' 
_struct_keywords.text            'SWEET-TASTING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 1 ? 
F N N 2 ? 
G N N 1 ? 
H N N 2 ? 
# 
loop_
_struct_biol.id 
1 
2 
3 
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 HB PRO B 10 ? LYS B 25 ? PRO B 10 LYS B 25 1 ? 16 
HELX_P HELX_P2 HD PRO D 10 ? LYS D 25 ? PRO D 10 LYS D 25 1 ? 16 
HELX_P HELX_P3 HF PRO F 10 ? LYS F 25 ? PRO F 10 LYS F 25 1 ? 16 
HELX_P HELX_P4 HH PRO H 10 ? LYS H 25 ? PRO H 10 LYS H 25 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 39 A . ? GLY 40 A PRO 40 A ? PRO 41 A 1 -1.54 
2 ARG 39 B . ? ARG 39 B PRO 40 B ? PRO 40 B 1 -0.25 
3 GLY 39 C . ? GLY 40 C PRO 40 C ? PRO 41 C 1 -1.98 
4 ARG 39 D . ? ARG 39 D PRO 40 D ? PRO 40 D 1 -1.61 
5 GLY 39 E . ? GLY 40 E PRO 40 E ? PRO 41 E 1 0.77  
6 ARG 39 F . ? ARG 39 F PRO 40 F ? PRO 40 F 1 1.39  
7 GLY 39 G . ? GLY 40 G PRO 40 G ? PRO 41 G 1 -1.54 
8 ARG 39 H . ? ARG 39 H PRO 40 H ? PRO 40 H 1 -2.76 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AB1 ? 5 ? 
AB2 ? 5 ? 
CD1 ? 5 ? 
CD2 ? 5 ? 
EF1 ? 5 ? 
EF2 ? 5 ? 
GH1 ? 5 ? 
GH2 ? 5 ? 
# 
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 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
CD1 1 2 ? anti-parallel 
CD1 2 3 ? anti-parallel 
CD1 3 4 ? anti-parallel 
CD1 4 5 ? anti-parallel 
CD2 1 2 ? anti-parallel 
CD2 2 3 ? anti-parallel 
CD2 3 4 ? anti-parallel 
CD2 4 5 ? anti-parallel 
EF1 1 2 ? anti-parallel 
EF1 2 3 ? anti-parallel 
EF1 3 4 ? anti-parallel 
EF1 4 5 ? anti-parallel 
EF2 1 2 ? anti-parallel 
EF2 2 3 ? anti-parallel 
EF2 3 4 ? anti-parallel 
EF2 4 5 ? anti-parallel 
GH1 1 2 ? anti-parallel 
GH1 2 3 ? anti-parallel 
GH1 3 4 ? anti-parallel 
GH1 4 5 ? anti-parallel 
GH2 1 2 ? anti-parallel 
GH2 2 3 ? anti-parallel 
GH2 3 4 ? anti-parallel 
GH2 4 5 ? 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 
AB1 1 GLY B 1  ? ILE B 5  ? GLY B 1  ILE B 5  
AB1 2 ASN B 35 ? ILE B 38 ? ASN B 35 ILE B 38 
AB1 3 LYS A 4  ? ALA A 14 ? LYS A 5  ALA A 15 
AB1 4 LYS A 17 ? ASP A 26 ? LYS A 18 ASP A 27 
AB1 5 THR A 29 ? ASN A 38 ? THR A 30 ASN A 39 
AB2 1 GLY B 1  ? ILE B 5  ? GLY B 1  ILE B 5  
AB2 2 CYS B 41 ? TYR B 47 ? CYS B 41 TYR B 47 
AB2 3 LYS A 4  ? ALA A 14 ? LYS A 5  ALA A 15 
AB2 4 LYS A 17 ? ASP A 26 ? LYS A 18 ASP A 27 
AB2 5 THR A 29 ? ASN A 38 ? THR A 30 ASN A 39 
CD1 1 GLY D 1  ? ILE D 5  ? GLY D 1  ILE D 5  
CD1 2 ASN D 35 ? ILE D 38 ? ASN D 35 ILE D 38 
CD1 3 LYS C 4  ? ALA C 14 ? LYS C 5  ALA C 15 
CD1 4 LYS C 17 ? ASP C 26 ? LYS C 18 ASP C 27 
CD1 5 THR C 29 ? ASN C 38 ? THR C 30 ASN C 39 
CD2 1 GLY D 1  ? ILE D 5  ? GLY D 1  ILE D 5  
CD2 2 CYS D 41 ? TYR D 47 ? CYS D 41 TYR D 47 
CD2 3 LYS C 4  ? ALA C 14 ? LYS C 5  ALA C 15 
CD2 4 LYS C 17 ? ASP C 26 ? LYS C 18 ASP C 27 
CD2 5 THR C 29 ? ASN C 38 ? THR C 30 ASN C 39 
EF1 1 GLY F 1  ? ILE F 5  ? GLY F 1  ILE F 5  
EF1 2 ASN F 35 ? ILE F 38 ? ASN F 35 ILE F 38 
EF1 3 LYS E 4  ? ALA E 14 ? LYS E 5  ALA E 15 
EF1 4 LYS E 17 ? ASP E 26 ? LYS E 18 ASP E 27 
EF1 5 THR E 29 ? ASN E 38 ? THR E 30 ASN E 39 
EF2 1 GLY F 1  ? ILE F 5  ? GLY F 1  ILE F 5  
EF2 2 CYS F 41 ? TYR F 47 ? CYS F 41 TYR F 47 
EF2 3 LYS E 4  ? ALA E 14 ? LYS E 5  ALA E 15 
EF2 4 LYS E 17 ? ASP E 26 ? LYS E 18 ASP E 27 
EF2 5 THR E 29 ? ASN E 38 ? THR E 30 ASN E 39 
GH1 1 GLY H 1  ? ILE H 5  ? GLY H 1  ILE H 5  
GH1 2 ASN H 35 ? ILE H 38 ? ASN H 35 ILE H 38 
GH1 3 LYS G 4  ? ALA G 14 ? LYS G 5  ALA G 15 
GH1 4 LYS G 17 ? ASP G 26 ? LYS G 18 ASP G 27 
GH1 5 THR G 29 ? ASN G 38 ? THR G 30 ASN G 39 
GH2 1 GLY H 1  ? ILE H 5  ? GLY H 1  ILE H 5  
GH2 2 CYS H 41 ? TYR H 47 ? CYS H 41 TYR H 47 
GH2 3 LYS G 4  ? ALA G 14 ? LYS G 5  ALA G 15 
GH2 4 LYS G 17 ? ASP G 26 ? LYS G 18 ASP G 27 
GH2 5 THR G 29 ? ASN G 38 ? THR G 30 ASN G 39 
# 
_database_PDB_matrix.entry_id          3MON 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3MON 
_atom_sites.fract_transf_matrix[1][1]   0.025100 
_atom_sites.fract_transf_matrix[1][2]   0.007818 
_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]   0.012011 
_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]   0.013877 
_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_sites_footnote.id 
_atom_sites_footnote.text 
1 'CIS PROLINE - PRO A    41' 
2 'CIS PROLINE - PRO B    40' 
3 'CIS PROLINE - PRO C    41' 
4 'CIS PROLINE - PRO D    40' 
5 'CIS PROLINE - PRO E    41' 
6 'CIS PROLINE - PRO F    40' 
7 'CIS PROLINE - PRO G    41' 
8 'CIS PROLINE - PRO H    40' 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . ARG A 1 1  ? 26.033 10.028 35.555 1.00 78.14  ? 2  ARG A N   1 
ATOM 2    C CA  . ARG A 1 1  ? 25.254 9.312  34.549 1.00 82.71  ? 2  ARG A CA  1 
ATOM 3    C C   . ARG A 1 1  ? 23.757 9.413  34.820 1.00 84.18  ? 2  ARG A C   1 
ATOM 4    O O   . ARG A 1 1  ? 22.913 9.027  34.007 1.00 80.46  ? 2  ARG A O   1 
ATOM 5    C CB  . ARG A 1 1  ? 25.611 7.793  34.498 1.00 83.95  ? 2  ARG A CB  1 
ATOM 6    C CG  . ARG A 1 1  ? 25.473 6.814  35.716 1.00 78.41  ? 2  ARG A CG  1 
ATOM 7    C CD  . ARG A 1 1  ? 24.069 6.575  36.318 1.00 73.17  ? 2  ARG A CD  1 
ATOM 8    N NE  . ARG A 1 1  ? 23.179 5.905  35.384 1.00 73.31  ? 2  ARG A NE  1 
ATOM 9    C CZ  . ARG A 1 1  ? 21.971 5.429  35.738 1.00 69.05  ? 2  ARG A CZ  1 
ATOM 10   N NH1 . ARG A 1 1  ? 21.374 5.733  36.879 1.00 67.54  ? 2  ARG A NH1 1 
ATOM 11   N NH2 . ARG A 1 1  ? 21.293 4.684  34.878 1.00 67.87  ? 2  ARG A NH2 1 
ATOM 12   N N   . GLU A 1 2  ? 23.447 9.860  36.038 1.00 86.49  ? 3  GLU A N   1 
ATOM 13   C CA  . GLU A 1 2  ? 22.088 9.937  36.473 1.00 84.24  ? 3  GLU A CA  1 
ATOM 14   C C   . GLU A 1 2  ? 21.930 11.418 36.718 1.00 84.10  ? 3  GLU A C   1 
ATOM 15   O O   . GLU A 1 2  ? 22.923 12.121 37.012 1.00 86.06  ? 3  GLU A O   1 
ATOM 16   C CB  . GLU A 1 2  ? 21.979 9.119  37.731 1.00 82.37  ? 3  GLU A CB  1 
ATOM 17   C CG  . GLU A 1 2  ? 20.547 8.776  37.936 1.00 86.18  ? 3  GLU A CG  1 
ATOM 18   C CD  . GLU A 1 2  ? 20.183 8.214  39.310 1.00 89.44  ? 3  GLU A CD  1 
ATOM 19   O OE1 . GLU A 1 2  ? 21.067 8.090  40.183 1.00 92.71  ? 3  GLU A OE1 1 
ATOM 20   O OE2 . GLU A 1 2  ? 18.983 7.960  39.539 1.00 89.03  ? 3  GLU A OE2 1 
ATOM 21   N N   . ILE A 1 3  ? 20.741 11.942 36.481 1.00 82.47  ? 4  ILE A N   1 
ATOM 22   C CA  . ILE A 1 3  ? 20.449 13.344 36.673 1.00 83.29  ? 4  ILE A CA  1 
ATOM 23   C C   . ILE A 1 3  ? 20.430 13.529 38.188 1.00 81.12  ? 4  ILE A C   1 
ATOM 24   O O   . ILE A 1 3  ? 19.474 13.915 38.854 1.00 83.87  ? 4  ILE A O   1 
ATOM 25   C CB  . ILE A 1 3  ? 19.081 13.555 35.869 1.00 86.41  ? 4  ILE A CB  1 
ATOM 26   C CG1 . ILE A 1 3  ? 17.991 12.560 36.296 1.00 90.50  ? 4  ILE A CG1 1 
ATOM 27   C CG2 . ILE A 1 3  ? 19.407 13.459 34.371 1.00 84.10  ? 4  ILE A CG2 1 
ATOM 28   C CD1 . ILE A 1 3  ? 16.591 12.666 35.656 1.00 95.34  ? 4  ILE A CD1 1 
ATOM 29   N N   . LYS A 1 4  ? 21.604 13.408 38.789 1.00 74.65  ? 5  LYS A N   1 
ATOM 30   C CA  . LYS A 1 4  ? 21.771 13.198 40.185 1.00 72.29  ? 5  LYS A CA  1 
ATOM 31   C C   . LYS A 1 4  ? 23.274 13.102 40.187 1.00 66.82  ? 5  LYS A C   1 
ATOM 32   O O   . LYS A 1 4  ? 23.920 12.064 40.117 1.00 65.37  ? 5  LYS A O   1 
ATOM 33   C CB  . LYS A 1 4  ? 21.149 11.805 40.636 1.00 83.85  ? 5  LYS A CB  1 
ATOM 34   C CG  . LYS A 1 4  ? 19.697 11.272 40.911 1.00 90.87  ? 5  LYS A CG  1 
ATOM 35   C CD  . LYS A 1 4  ? 18.857 11.130 39.637 1.00 92.00  ? 5  LYS A CD  1 
ATOM 36   C CE  . LYS A 1 4  ? 17.411 10.697 39.843 1.00 89.96  ? 5  LYS A CE  1 
ATOM 37   N NZ  . LYS A 1 4  ? 16.845 11.366 41.020 1.00 94.63  ? 5  LYS A NZ  1 
ATOM 38   N N   . GLY A 1 5  ? 23.932 14.256 40.193 1.00 63.14  ? 6  GLY A N   1 
ATOM 39   C CA  . GLY A 1 5  ? 25.388 14.275 40.138 1.00 60.23  ? 6  GLY A CA  1 
ATOM 40   C C   . GLY A 1 5  ? 25.877 15.689 39.875 1.00 53.79  ? 6  GLY A C   1 
ATOM 41   O O   . GLY A 1 5  ? 25.328 16.670 40.396 1.00 55.08  ? 6  GLY A O   1 
ATOM 42   N N   . TYR A 1 6  ? 26.942 15.859 39.118 1.00 51.66  ? 7  TYR A N   1 
ATOM 43   C CA  . TYR A 1 6  ? 27.372 17.201 38.786 1.00 50.03  ? 7  TYR A CA  1 
ATOM 44   C C   . TYR A 1 6  ? 27.967 17.201 37.396 1.00 43.29  ? 7  TYR A C   1 
ATOM 45   O O   . TYR A 1 6  ? 28.019 16.183 36.708 1.00 34.58  ? 7  TYR A O   1 
ATOM 46   C CB  . TYR A 1 6  ? 28.430 17.753 39.779 1.00 49.86  ? 7  TYR A CB  1 
ATOM 47   C CG  . TYR A 1 6  ? 27.987 17.710 41.228 1.00 48.68  ? 7  TYR A CG  1 
ATOM 48   C CD1 . TYR A 1 6  ? 27.211 18.704 41.745 1.00 45.16  ? 7  TYR A CD1 1 
ATOM 49   C CD2 . TYR A 1 6  ? 28.352 16.627 41.996 1.00 51.38  ? 7  TYR A CD2 1 
ATOM 50   C CE1 . TYR A 1 6  ? 26.787 18.601 43.043 1.00 50.73  ? 7  TYR A CE1 1 
ATOM 51   C CE2 . TYR A 1 6  ? 27.937 16.523 43.295 1.00 53.07  ? 7  TYR A CE2 1 
ATOM 52   C CZ  . TYR A 1 6  ? 27.147 17.516 43.811 1.00 54.55  ? 7  TYR A CZ  1 
ATOM 53   O OH  . TYR A 1 6  ? 26.685 17.382 45.119 1.00 61.63  ? 7  TYR A OH  1 
ATOM 54   N N   . GLU A 1 7  ? 28.397 18.364 36.972 1.00 38.51  ? 8  GLU A N   1 
ATOM 55   C CA  . GLU A 1 7  ? 29.017 18.566 35.708 1.00 36.80  ? 8  GLU A CA  1 
ATOM 56   C C   . GLU A 1 7  ? 29.799 19.810 35.998 1.00 36.02  ? 8  GLU A C   1 
ATOM 57   O O   . GLU A 1 7  ? 29.307 20.713 36.647 1.00 41.87  ? 8  GLU A O   1 
ATOM 58   C CB  . GLU A 1 7  ? 27.976 18.813 34.633 1.00 39.17  ? 8  GLU A CB  1 
ATOM 59   C CG  . GLU A 1 7  ? 28.438 18.098 33.363 1.00 46.73  ? 8  GLU A CG  1 
ATOM 60   C CD  . GLU A 1 7  ? 27.619 18.302 32.090 1.00 49.41  ? 8  GLU A CD  1 
ATOM 61   O OE1 . GLU A 1 7  ? 26.483 17.778 32.006 1.00 50.84  ? 8  GLU A OE1 1 
ATOM 62   O OE2 . GLU A 1 7  ? 28.159 18.968 31.186 1.00 43.69  ? 8  GLU A OE2 1 
ATOM 63   N N   . TYR A 1 8  ? 31.027 19.868 35.578 1.00 37.04  ? 9  TYR A N   1 
ATOM 64   C CA  . TYR A 1 8  ? 31.912 20.974 35.818 1.00 39.82  ? 9  TYR A CA  1 
ATOM 65   C C   . TYR A 1 8  ? 32.341 21.458 34.456 1.00 39.73  ? 9  TYR A C   1 
ATOM 66   O O   . TYR A 1 8  ? 32.382 20.647 33.547 1.00 49.96  ? 9  TYR A O   1 
ATOM 67   C CB  . TYR A 1 8  ? 33.140 20.494 36.581 1.00 43.91  ? 9  TYR A CB  1 
ATOM 68   C CG  . TYR A 1 8  ? 32.852 19.834 37.938 1.00 47.82  ? 9  TYR A CG  1 
ATOM 69   C CD1 . TYR A 1 8  ? 32.369 18.546 37.987 1.00 45.07  ? 9  TYR A CD1 1 
ATOM 70   C CD2 . TYR A 1 8  ? 33.054 20.558 39.118 1.00 51.27  ? 9  TYR A CD2 1 
ATOM 71   C CE1 . TYR A 1 8  ? 32.078 17.986 39.203 1.00 45.06  ? 9  TYR A CE1 1 
ATOM 72   C CE2 . TYR A 1 8  ? 32.758 19.999 40.342 1.00 47.65  ? 9  TYR A CE2 1 
ATOM 73   C CZ  . TYR A 1 8  ? 32.274 18.714 40.355 1.00 46.16  ? 9  TYR A CZ  1 
ATOM 74   O OH  . TYR A 1 8  ? 31.998 18.127 41.556 1.00 43.00  ? 9  TYR A OH  1 
ATOM 75   N N   . GLN A 1 9  ? 32.588 22.712 34.183 1.00 35.43  ? 10 GLN A N   1 
ATOM 76   C CA  . GLN A 1 9  ? 33.217 23.082 32.926 1.00 33.82  ? 10 GLN A CA  1 
ATOM 77   C C   . GLN A 1 9  ? 34.556 23.642 33.384 1.00 36.40  ? 10 GLN A C   1 
ATOM 78   O O   . GLN A 1 9  ? 34.568 24.263 34.454 1.00 45.28  ? 10 GLN A O   1 
ATOM 79   C CB  . GLN A 1 9  ? 32.325 24.108 32.217 1.00 31.63  ? 10 GLN A CB  1 
ATOM 80   C CG  . GLN A 1 9  ? 31.257 23.371 31.407 1.00 38.21  ? 10 GLN A CG  1 
ATOM 81   C CD  . GLN A 1 9  ? 29.907 24.039 31.127 1.00 41.76  ? 10 GLN A CD  1 
ATOM 82   O OE1 . GLN A 1 9  ? 29.661 25.169 31.542 1.00 47.98  ? 10 GLN A OE1 1 
ATOM 83   N NE2 . GLN A 1 9  ? 28.960 23.376 30.450 1.00 37.72  ? 10 GLN A NE2 1 
ATOM 84   N N   . LEU A 1 10 ? 35.719 23.478 32.730 1.00 35.16  ? 11 LEU A N   1 
ATOM 85   C CA  . LEU A 1 10 ? 36.972 24.002 33.299 1.00 34.66  ? 11 LEU A CA  1 
ATOM 86   C C   . LEU A 1 10 ? 37.850 24.669 32.257 1.00 29.76  ? 11 LEU A C   1 
ATOM 87   O O   . LEU A 1 10 ? 37.803 24.336 31.070 1.00 27.78  ? 11 LEU A O   1 
ATOM 88   C CB  . LEU A 1 10 ? 37.861 22.886 33.962 1.00 41.77  ? 11 LEU A CB  1 
ATOM 89   C CG  . LEU A 1 10 ? 37.782 22.115 35.309 1.00 37.24  ? 11 LEU A CG  1 
ATOM 90   C CD1 . LEU A 1 10 ? 36.485 21.379 35.538 1.00 36.00  ? 11 LEU A CD1 1 
ATOM 91   C CD2 . LEU A 1 10 ? 38.895 21.094 35.253 1.00 32.03  ? 11 LEU A CD2 1 
ATOM 92   N N   . TYR A 1 11 ? 38.684 25.590 32.703 1.00 30.84  ? 12 TYR A N   1 
ATOM 93   C CA  . TYR A 1 11 ? 39.678 26.185 31.833 1.00 35.19  ? 12 TYR A CA  1 
ATOM 94   C C   . TYR A 1 11 ? 41.014 25.658 32.358 1.00 34.17  ? 12 TYR A C   1 
ATOM 95   O O   . TYR A 1 11 ? 41.445 26.139 33.430 1.00 35.37  ? 12 TYR A O   1 
ATOM 96   C CB  . TYR A 1 11 ? 39.628 27.748 31.924 1.00 38.29  ? 12 TYR A CB  1 
ATOM 97   C CG  . TYR A 1 11 ? 38.525 28.418 31.120 1.00 37.60  ? 12 TYR A CG  1 
ATOM 98   C CD1 . TYR A 1 11 ? 37.222 28.462 31.561 1.00 37.97  ? 12 TYR A CD1 1 
ATOM 99   C CD2 . TYR A 1 11 ? 38.817 28.868 29.858 1.00 38.59  ? 12 TYR A CD2 1 
ATOM 100  C CE1 . TYR A 1 11 ? 36.216 28.916 30.730 1.00 34.50  ? 12 TYR A CE1 1 
ATOM 101  C CE2 . TYR A 1 11 ? 37.818 29.331 29.032 1.00 31.42  ? 12 TYR A CE2 1 
ATOM 102  C CZ  . TYR A 1 11 ? 36.524 29.337 29.465 1.00 30.81  ? 12 TYR A CZ  1 
ATOM 103  O OH  . TYR A 1 11 ? 35.519 29.686 28.579 1.00 31.61  ? 12 TYR A OH  1 
ATOM 104  N N   . VAL A 1 12 ? 41.655 24.665 31.695 1.00 28.94  ? 13 VAL A N   1 
ATOM 105  C CA  . VAL A 1 12 ? 42.897 24.056 32.234 1.00 23.37  ? 13 VAL A CA  1 
ATOM 106  C C   . VAL A 1 12 ? 44.088 24.549 31.442 1.00 27.75  ? 13 VAL A C   1 
ATOM 107  O O   . VAL A 1 12 ? 43.996 24.695 30.221 1.00 32.05  ? 13 VAL A O   1 
ATOM 108  C CB  . VAL A 1 12 ? 42.947 22.444 32.161 1.00 19.14  ? 13 VAL A CB  1 
ATOM 109  C CG1 . VAL A 1 12 ? 44.046 21.926 33.121 1.00 5.48   ? 13 VAL A CG1 1 
ATOM 110  C CG2 . VAL A 1 12 ? 41.606 21.807 32.495 1.00 9.93   ? 13 VAL A CG2 1 
ATOM 111  N N   . TYR A 1 13 ? 45.159 24.901 32.121 1.00 35.80  ? 14 TYR A N   1 
ATOM 112  C CA  . TYR A 1 13 ? 46.418 25.196 31.468 1.00 51.11  ? 14 TYR A CA  1 
ATOM 113  C C   . TYR A 1 13 ? 47.252 23.930 31.489 1.00 47.42  ? 14 TYR A C   1 
ATOM 114  O O   . TYR A 1 13 ? 47.456 23.378 32.579 1.00 47.10  ? 14 TYR A O   1 
ATOM 115  C CB  . TYR A 1 13 ? 47.267 26.284 32.171 1.00 62.06  ? 14 TYR A CB  1 
ATOM 116  C CG  . TYR A 1 13 ? 47.146 27.655 31.520 1.00 72.85  ? 14 TYR A CG  1 
ATOM 117  C CD1 . TYR A 1 13 ? 47.882 27.981 30.391 1.00 73.96  ? 14 TYR A CD1 1 
ATOM 118  C CD2 . TYR A 1 13 ? 46.282 28.582 32.062 1.00 79.33  ? 14 TYR A CD2 1 
ATOM 119  C CE1 . TYR A 1 13 ? 47.743 29.223 29.794 1.00 77.85  ? 14 TYR A CE1 1 
ATOM 120  C CE2 . TYR A 1 13 ? 46.141 29.823 31.472 1.00 83.06  ? 14 TYR A CE2 1 
ATOM 121  C CZ  . TYR A 1 13 ? 46.872 30.147 30.341 1.00 82.44  ? 14 TYR A CZ  1 
ATOM 122  O OH  . TYR A 1 13 ? 46.721 31.410 29.773 1.00 83.17  ? 14 TYR A OH  1 
ATOM 123  N N   . ALA A 1 14 ? 47.670 23.463 30.314 1.00 37.98  ? 15 ALA A N   1 
ATOM 124  C CA  . ALA A 1 14 ? 48.509 22.309 30.204 1.00 33.51  ? 15 ALA A CA  1 
ATOM 125  C C   . ALA A 1 14 ? 49.497 22.589 29.140 1.00 31.91  ? 15 ALA A C   1 
ATOM 126  O O   . ALA A 1 14 ? 49.075 22.952 28.056 1.00 37.31  ? 15 ALA A O   1 
ATOM 127  C CB  . ALA A 1 14 ? 47.774 21.079 29.759 1.00 31.38  ? 15 ALA A CB  1 
ATOM 128  N N   . SER A 1 15 ? 50.772 22.472 29.439 1.00 31.51  ? 16 SER A N   1 
ATOM 129  C CA  . SER A 1 15 ? 51.832 22.709 28.492 1.00 40.04  ? 16 SER A CA  1 
ATOM 130  C C   . SER A 1 15 ? 51.722 24.090 27.855 1.00 40.53  ? 16 SER A C   1 
ATOM 131  O O   . SER A 1 15 ? 51.868 24.257 26.651 1.00 44.41  ? 16 SER A O   1 
ATOM 132  C CB  . SER A 1 15 ? 51.806 21.592 27.412 1.00 45.53  ? 16 SER A CB  1 
ATOM 133  O OG  . SER A 1 15 ? 51.746 20.261 27.942 1.00 46.18  ? 16 SER A OG  1 
ATOM 134  N N   . ASP A 1 16 ? 51.510 25.120 28.690 1.00 42.94  ? 17 ASP A N   1 
ATOM 135  C CA  . ASP A 1 16 ? 51.384 26.517 28.275 1.00 31.89  ? 17 ASP A CA  1 
ATOM 136  C C   . ASP A 1 16 ? 50.303 26.716 27.195 1.00 27.48  ? 17 ASP A C   1 
ATOM 137  O O   . ASP A 1 16 ? 50.423 27.540 26.296 1.00 27.77  ? 17 ASP A O   1 
ATOM 138  C CB  . ASP A 1 16 ? 52.748 26.990 27.774 1.00 40.85  ? 17 ASP A CB  1 
ATOM 139  C CG  . ASP A 1 16 ? 53.957 26.557 28.625 1.00 46.67  ? 17 ASP A CG  1 
ATOM 140  O OD1 . ASP A 1 16 ? 54.335 27.257 29.572 1.00 53.38  ? 17 ASP A OD1 1 
ATOM 141  O OD2 . ASP A 1 16 ? 54.541 25.517 28.321 1.00 45.97  ? 17 ASP A OD2 1 
ATOM 142  N N   . LYS A 1 17 ? 49.199 25.979 27.249 1.00 16.87  ? 18 LYS A N   1 
ATOM 143  C CA  . LYS A 1 17 ? 48.109 26.122 26.322 1.00 18.33  ? 18 LYS A CA  1 
ATOM 144  C C   . LYS A 1 17 ? 46.805 26.109 27.124 1.00 21.18  ? 18 LYS A C   1 
ATOM 145  O O   . LYS A 1 17 ? 46.745 25.532 28.202 1.00 23.58  ? 18 LYS A O   1 
ATOM 146  C CB  . LYS A 1 17 ? 48.146 24.965 25.352 1.00 24.84  ? 18 LYS A CB  1 
ATOM 147  C CG  . LYS A 1 17 ? 49.395 24.852 24.482 1.00 27.33  ? 18 LYS A CG  1 
ATOM 148  C CD  . LYS A 1 17 ? 49.142 23.804 23.369 1.00 35.59  ? 18 LYS A CD  1 
ATOM 149  C CE  . LYS A 1 17 ? 50.321 23.522 22.441 1.00 31.73  ? 18 LYS A CE  1 
ATOM 150  N NZ  . LYS A 1 17 ? 51.449 23.061 23.225 1.00 40.21  ? 18 LYS A NZ  1 
ATOM 151  N N   . LEU A 1 18 ? 45.702 26.687 26.666 1.00 24.91  ? 19 LEU A N   1 
ATOM 152  C CA  . LEU A 1 18 ? 44.490 26.841 27.467 1.00 23.55  ? 19 LEU A CA  1 
ATOM 153  C C   . LEU A 1 18 ? 43.455 25.947 26.882 1.00 21.85  ? 19 LEU A C   1 
ATOM 154  O O   . LEU A 1 18 ? 43.254 26.047 25.676 1.00 23.14  ? 19 LEU A O   1 
ATOM 155  C CB  . LEU A 1 18 ? 44.029 28.287 27.389 1.00 38.28  ? 19 LEU A CB  1 
ATOM 156  C CG  . LEU A 1 18 ? 42.886 28.880 28.234 1.00 45.66  ? 19 LEU A CG  1 
ATOM 157  C CD1 . LEU A 1 18 ? 42.463 28.044 29.437 1.00 50.25  ? 19 LEU A CD1 1 
ATOM 158  C CD2 . LEU A 1 18 ? 43.449 30.180 28.767 1.00 51.20  ? 19 LEU A CD2 1 
ATOM 159  N N   . PHE A 1 19 ? 42.758 25.146 27.675 1.00 27.76  ? 20 PHE A N   1 
ATOM 160  C CA  . PHE A 1 19 ? 41.843 24.125 27.167 1.00 25.54  ? 20 PHE A CA  1 
ATOM 161  C C   . PHE A 1 19 ? 40.494 24.160 27.866 1.00 24.61  ? 20 PHE A C   1 
ATOM 162  O O   . PHE A 1 19 ? 40.334 24.533 29.049 1.00 24.67  ? 20 PHE A O   1 
ATOM 163  C CB  . PHE A 1 19 ? 42.452 22.681 27.371 1.00 25.96  ? 20 PHE A CB  1 
ATOM 164  C CG  . PHE A 1 19 ? 43.689 22.308 26.577 1.00 15.81  ? 20 PHE A CG  1 
ATOM 165  C CD1 . PHE A 1 19 ? 43.525 21.802 25.286 1.00 13.67  ? 20 PHE A CD1 1 
ATOM 166  C CD2 . PHE A 1 19 ? 44.934 22.575 27.101 1.00 11.91  ? 20 PHE A CD2 1 
ATOM 167  C CE1 . PHE A 1 19 ? 44.616 21.581 24.492 1.00 5.93   ? 20 PHE A CE1 1 
ATOM 168  C CE2 . PHE A 1 19 ? 46.030 22.353 26.285 1.00 12.72  ? 20 PHE A CE2 1 
ATOM 169  C CZ  . PHE A 1 19 ? 45.870 21.862 24.987 1.00 14.21  ? 20 PHE A CZ  1 
ATOM 170  N N   . ARG A 1 20 ? 39.533 23.629 27.175 1.00 19.84  ? 21 ARG A N   1 
ATOM 171  C CA  . ARG A 1 20 ? 38.239 23.503 27.766 1.00 26.73  ? 21 ARG A CA  1 
ATOM 172  C C   . ARG A 1 20 ? 37.874 22.078 28.182 1.00 28.17  ? 21 ARG A C   1 
ATOM 173  O O   . ARG A 1 20 ? 37.910 21.165 27.361 1.00 33.18  ? 21 ARG A O   1 
ATOM 174  C CB  . ARG A 1 20 ? 37.295 24.099 26.760 1.00 27.60  ? 21 ARG A CB  1 
ATOM 175  C CG  . ARG A 1 20 ? 37.301 25.566 27.066 1.00 30.76  ? 21 ARG A CG  1 
ATOM 176  C CD  . ARG A 1 20 ? 36.489 25.740 28.352 1.00 34.61  ? 21 ARG A CD  1 
ATOM 177  N NE  . ARG A 1 20 ? 35.084 25.428 28.123 1.00 33.72  ? 21 ARG A NE  1 
ATOM 178  C CZ  . ARG A 1 20 ? 34.337 24.897 29.059 1.00 36.60  ? 21 ARG A CZ  1 
ATOM 179  N NH1 . ARG A 1 20 ? 34.804 24.686 30.266 1.00 42.33  ? 21 ARG A NH1 1 
ATOM 180  N NH2 . ARG A 1 20 ? 33.092 24.589 28.797 1.00 40.89  ? 21 ARG A NH2 1 
ATOM 181  N N   . ALA A 1 21 ? 37.507 21.837 29.442 1.00 26.29  ? 22 ALA A N   1 
ATOM 182  C CA  . ALA A 1 21 ? 37.199 20.504 29.892 1.00 16.35  ? 22 ALA A CA  1 
ATOM 183  C C   . ALA A 1 21 ? 35.928 20.380 30.667 1.00 22.43  ? 22 ALA A C   1 
ATOM 184  O O   . ALA A 1 21 ? 35.727 21.074 31.664 1.00 22.31  ? 22 ALA A O   1 
ATOM 185  C CB  . ALA A 1 21 ? 38.290 20.015 30.774 1.00 22.82  ? 22 ALA A CB  1 
ATOM 186  N N   . ASP A 1 22 ? 35.064 19.482 30.235 1.00 23.28  ? 23 ASP A N   1 
ATOM 187  C CA  . ASP A 1 22 ? 33.784 19.320 30.867 1.00 27.74  ? 23 ASP A CA  1 
ATOM 188  C C   . ASP A 1 22 ? 33.778 17.997 31.573 1.00 30.28  ? 23 ASP A C   1 
ATOM 189  O O   . ASP A 1 22 ? 33.894 16.998 30.880 1.00 42.28  ? 23 ASP A O   1 
ATOM 190  C CB  . ASP A 1 22 ? 32.703 19.325 29.832 1.00 33.69  ? 23 ASP A CB  1 
ATOM 191  C CG  . ASP A 1 22 ? 32.629 20.544 28.933 1.00 42.62  ? 23 ASP A CG  1 
ATOM 192  O OD1 . ASP A 1 22 ? 33.194 21.591 29.271 1.00 53.76  ? 23 ASP A OD1 1 
ATOM 193  O OD2 . ASP A 1 22 ? 31.993 20.455 27.883 1.00 42.69  ? 23 ASP A OD2 1 
ATOM 194  N N   . ILE A 1 23 ? 33.662 17.878 32.884 1.00 30.69  ? 24 ILE A N   1 
ATOM 195  C CA  . ILE A 1 23 ? 33.750 16.582 33.548 1.00 33.45  ? 24 ILE A CA  1 
ATOM 196  C C   . ILE A 1 23 ? 32.405 16.147 34.147 1.00 37.31  ? 24 ILE A C   1 
ATOM 197  O O   . ILE A 1 23 ? 31.572 17.006 34.428 1.00 36.63  ? 24 ILE A O   1 
ATOM 198  C CB  . ILE A 1 23 ? 34.891 16.727 34.604 1.00 35.48  ? 24 ILE A CB  1 
ATOM 199  C CG1 . ILE A 1 23 ? 36.139 17.097 33.787 1.00 30.10  ? 24 ILE A CG1 1 
ATOM 200  C CG2 . ILE A 1 23 ? 35.073 15.477 35.513 1.00 34.93  ? 24 ILE A CG2 1 
ATOM 201  C CD1 . ILE A 1 23 ? 37.431 17.155 34.579 1.00 28.37  ? 24 ILE A CD1 1 
ATOM 202  N N   . SER A 1 24 ? 32.059 14.859 34.261 1.00 40.36  ? 25 SER A N   1 
ATOM 203  C CA  . SER A 1 24 ? 30.861 14.522 35.010 1.00 43.11  ? 25 SER A CA  1 
ATOM 204  C C   . SER A 1 24 ? 31.221 13.830 36.340 1.00 40.86  ? 25 SER A C   1 
ATOM 205  O O   . SER A 1 24 ? 32.394 13.515 36.579 1.00 38.31  ? 25 SER A O   1 
ATOM 206  C CB  . SER A 1 24 ? 29.988 13.672 34.157 1.00 43.28  ? 25 SER A CB  1 
ATOM 207  O OG  . SER A 1 24 ? 30.494 12.368 34.035 1.00 53.54  ? 25 SER A OG  1 
ATOM 208  N N   . GLU A 1 25 ? 30.244 13.661 37.249 1.00 42.10  ? 26 GLU A N   1 
ATOM 209  C CA  . GLU A 1 25 ? 30.471 13.240 38.639 1.00 40.57  ? 26 GLU A CA  1 
ATOM 210  C C   . GLU A 1 25 ? 29.211 12.660 39.249 1.00 43.68  ? 26 GLU A C   1 
ATOM 211  O O   . GLU A 1 25 ? 28.354 13.452 39.651 1.00 42.02  ? 26 GLU A O   1 
ATOM 212  C CB  . GLU A 1 25 ? 30.835 14.403 39.504 1.00 34.39  ? 26 GLU A CB  1 
ATOM 213  C CG  . GLU A 1 25 ? 31.986 14.029 40.343 1.00 39.10  ? 26 GLU A CG  1 
ATOM 214  C CD  . GLU A 1 25 ? 32.107 14.847 41.602 1.00 39.76  ? 26 GLU A CD  1 
ATOM 215  O OE1 . GLU A 1 25 ? 31.094 14.816 42.313 1.00 46.56  ? 26 GLU A OE1 1 
ATOM 216  O OE2 . GLU A 1 25 ? 33.167 15.456 41.869 1.00 28.25  ? 26 GLU A OE2 1 
ATOM 217  N N   . ASP A 1 26 ? 29.056 11.315 39.319 1.00 49.83  ? 27 ASP A N   1 
ATOM 218  C CA  . ASP A 1 26 ? 27.848 10.692 39.866 1.00 51.82  ? 27 ASP A CA  1 
ATOM 219  C C   . ASP A 1 26 ? 27.744 10.936 41.359 1.00 48.70  ? 27 ASP A C   1 
ATOM 220  O O   . ASP A 1 26 ? 28.658 10.582 42.082 1.00 44.12  ? 27 ASP A O   1 
ATOM 221  C CB  . ASP A 1 26 ? 27.820 9.165  39.656 1.00 52.05  ? 27 ASP A CB  1 
ATOM 222  C CG  . ASP A 1 26 ? 26.482 8.461  40.003 1.00 54.51  ? 27 ASP A CG  1 
ATOM 223  O OD1 . ASP A 1 26 ? 25.762 8.817  40.942 1.00 55.37  ? 27 ASP A OD1 1 
ATOM 224  O OD2 . ASP A 1 26 ? 26.136 7.509  39.312 1.00 59.29  ? 27 ASP A OD2 1 
ATOM 225  N N   . TYR A 1 27 ? 26.577 11.376 41.808 1.00 55.26  ? 28 TYR A N   1 
ATOM 226  C CA  . TYR A 1 27 ? 26.332 11.702 43.200 1.00 65.07  ? 28 TYR A CA  1 
ATOM 227  C C   . TYR A 1 27 ? 26.574 10.520 44.128 1.00 67.41  ? 28 TYR A C   1 
ATOM 228  O O   . TYR A 1 27 ? 27.204 10.663 45.177 1.00 70.13  ? 28 TYR A O   1 
ATOM 229  C CB  . TYR A 1 27 ? 24.889 12.214 43.304 1.00 69.26  ? 28 TYR A CB  1 
ATOM 230  C CG  . TYR A 1 27 ? 24.471 12.793 44.650 1.00 73.85  ? 28 TYR A CG  1 
ATOM 231  C CD1 . TYR A 1 27 ? 24.841 14.063 45.039 1.00 73.99  ? 28 TYR A CD1 1 
ATOM 232  C CD2 . TYR A 1 27 ? 23.734 12.001 45.506 1.00 77.82  ? 28 TYR A CD2 1 
ATOM 233  C CE1 . TYR A 1 27 ? 24.471 14.530 46.291 1.00 75.76  ? 28 TYR A CE1 1 
ATOM 234  C CE2 . TYR A 1 27 ? 23.363 12.466 46.751 1.00 79.12  ? 28 TYR A CE2 1 
ATOM 235  C CZ  . TYR A 1 27 ? 23.732 13.728 47.142 1.00 75.74  ? 28 TYR A CZ  1 
ATOM 236  O OH  . TYR A 1 27 ? 23.352 14.160 48.400 1.00 74.12  ? 28 TYR A OH  1 
ATOM 237  N N   . LYS A 1 28 ? 26.069 9.342  43.768 1.00 67.02  ? 29 LYS A N   1 
ATOM 238  C CA  . LYS A 1 28 ? 26.331 8.151  44.575 1.00 68.17  ? 29 LYS A CA  1 
ATOM 239  C C   . LYS A 1 28 ? 27.741 7.557  44.451 1.00 63.65  ? 29 LYS A C   1 
ATOM 240  O O   . LYS A 1 28 ? 28.457 7.406  45.434 1.00 65.92  ? 29 LYS A O   1 
ATOM 241  C CB  . LYS A 1 28 ? 25.335 7.048  44.234 1.00 65.57  ? 29 LYS A CB  1 
ATOM 242  C CG  . LYS A 1 28 ? 23.989 7.564  44.582 1.00 70.81  ? 29 LYS A CG  1 
ATOM 243  C CD  . LYS A 1 28 ? 22.976 6.549  44.184 1.00 78.30  ? 29 LYS A CD  1 
ATOM 244  C CE  . LYS A 1 28 ? 21.640 7.264  44.401 1.00 83.09  ? 29 LYS A CE  1 
ATOM 245  N NZ  . LYS A 1 28 ? 20.604 6.740  43.533 1.00 86.42  ? 29 LYS A NZ  1 
ATOM 246  N N   . THR A 1 29 ? 28.236 7.236  43.265 1.00 55.90  ? 30 THR A N   1 
ATOM 247  C CA  . THR A 1 29 ? 29.454 6.474  43.247 1.00 51.56  ? 30 THR A CA  1 
ATOM 248  C C   . THR A 1 29 ? 30.731 7.321  43.381 1.00 49.81  ? 30 THR A C   1 
ATOM 249  O O   . THR A 1 29 ? 31.758 6.835  43.871 1.00 47.03  ? 30 THR A O   1 
ATOM 250  C CB  . THR A 1 29 ? 29.386 5.567  41.937 1.00 47.92  ? 30 THR A CB  1 
ATOM 251  O OG1 . THR A 1 29 ? 29.577 6.318  40.754 1.00 45.54  ? 30 THR A OG1 1 
ATOM 252  C CG2 . THR A 1 29 ? 28.011 4.856  41.868 1.00 43.51  ? 30 THR A CG2 1 
ATOM 253  N N   . ARG A 1 30 ? 30.618 8.617  43.044 1.00 51.59  ? 31 ARG A N   1 
ATOM 254  C CA  . ARG A 1 30 ? 31.709 9.594  42.852 1.00 54.13  ? 31 ARG A CA  1 
ATOM 255  C C   . ARG A 1 30 ? 32.459 9.313  41.566 1.00 53.96  ? 31 ARG A C   1 
ATOM 256  O O   . ARG A 1 30 ? 33.635 9.635  41.352 1.00 54.96  ? 31 ARG A O   1 
ATOM 257  C CB  . ARG A 1 30 ? 32.735 9.602  43.968 1.00 60.22  ? 31 ARG A CB  1 
ATOM 258  C CG  . ARG A 1 30 ? 32.036 9.943  45.241 1.00 67.60  ? 31 ARG A CG  1 
ATOM 259  C CD  . ARG A 1 30 ? 31.410 11.310 45.061 1.00 76.41  ? 31 ARG A CD  1 
ATOM 260  N NE  . ARG A 1 30 ? 31.289 11.966 46.341 1.00 82.48  ? 31 ARG A NE  1 
ATOM 261  C CZ  . ARG A 1 30 ? 32.363 12.223 47.115 1.00 86.71  ? 31 ARG A CZ  1 
ATOM 262  N NH1 . ARG A 1 30 ? 33.636 11.820 46.850 1.00 86.24  ? 31 ARG A NH1 1 
ATOM 263  N NH2 . ARG A 1 30 ? 32.073 12.892 48.224 1.00 89.83  ? 31 ARG A NH2 1 
ATOM 264  N N   . GLY A 1 31 ? 31.693 8.773  40.617 1.00 54.99  ? 32 GLY A N   1 
ATOM 265  C CA  . GLY A 1 31 ? 32.218 8.362  39.325 1.00 53.14  ? 32 GLY A CA  1 
ATOM 266  C C   . GLY A 1 31 ? 32.516 9.510  38.386 1.00 47.18  ? 32 GLY A C   1 
ATOM 267  O O   . GLY A 1 31 ? 31.610 10.022 37.719 1.00 46.18  ? 32 GLY A O   1 
ATOM 268  N N   . ARG A 1 32 ? 33.756 9.954  38.369 1.00 39.26  ? 33 ARG A N   1 
ATOM 269  C CA  . ARG A 1 32 ? 34.066 10.968 37.421 1.00 39.61  ? 33 ARG A CA  1 
ATOM 270  C C   . ARG A 1 32 ? 34.355 10.343 36.088 1.00 41.60  ? 33 ARG A C   1 
ATOM 271  O O   . ARG A 1 32 ? 34.949 9.269  36.041 1.00 43.58  ? 33 ARG A O   1 
ATOM 272  C CB  . ARG A 1 32 ? 35.241 11.740 37.899 1.00 37.99  ? 33 ARG A CB  1 
ATOM 273  C CG  . ARG A 1 32 ? 34.684 12.728 38.871 1.00 30.50  ? 33 ARG A CG  1 
ATOM 274  C CD  . ARG A 1 32 ? 35.864 13.258 39.566 1.00 29.64  ? 33 ARG A CD  1 
ATOM 275  N NE  . ARG A 1 32 ? 35.402 13.792 40.812 1.00 30.09  ? 33 ARG A NE  1 
ATOM 276  C CZ  . ARG A 1 32 ? 36.282 14.216 41.687 1.00 31.77  ? 33 ARG A CZ  1 
ATOM 277  N NH1 . ARG A 1 32 ? 37.583 14.222 41.423 1.00 30.63  ? 33 ARG A NH1 1 
ATOM 278  N NH2 . ARG A 1 32 ? 35.818 14.658 42.826 1.00 32.16  ? 33 ARG A NH2 1 
ATOM 279  N N   . LYS A 1 33 ? 33.928 11.016 35.025 1.00 45.49  ? 34 LYS A N   1 
ATOM 280  C CA  . LYS A 1 33 ? 34.157 10.628 33.642 1.00 43.28  ? 34 LYS A CA  1 
ATOM 281  C C   . LYS A 1 33 ? 34.590 11.882 32.840 1.00 43.31  ? 34 LYS A C   1 
ATOM 282  O O   . LYS A 1 33 ? 33.909 12.912 32.901 1.00 47.04  ? 34 LYS A O   1 
ATOM 283  C CB  . LYS A 1 33 ? 32.854 10.017 33.062 1.00 35.41  ? 34 LYS A CB  1 
ATOM 284  C CG  . LYS A 1 33 ? 33.202 9.714  31.629 1.00 41.07  ? 34 LYS A CG  1 
ATOM 285  C CD  . LYS A 1 33 ? 32.048 9.307  30.790 1.00 41.73  ? 34 LYS A CD  1 
ATOM 286  C CE  . LYS A 1 33 ? 32.456 9.303  29.311 1.00 41.82  ? 34 LYS A CE  1 
ATOM 287  N NZ  . LYS A 1 33 ? 31.183 9.263  28.644 1.00 56.80  ? 34 LYS A NZ  1 
ATOM 288  N N   . LEU A 1 34 ? 35.734 11.895 32.139 1.00 39.89  ? 35 LEU A N   1 
ATOM 289  C CA  . LEU A 1 34 ? 36.072 13.027 31.291 1.00 36.52  ? 35 LEU A CA  1 
ATOM 290  C C   . LEU A 1 34 ? 35.150 12.990 30.090 1.00 40.17  ? 35 LEU A C   1 
ATOM 291  O O   . LEU A 1 34 ? 35.005 11.910 29.513 1.00 46.07  ? 35 LEU A O   1 
ATOM 292  C CB  . LEU A 1 34 ? 37.467 12.965 30.759 1.00 29.46  ? 35 LEU A CB  1 
ATOM 293  C CG  . LEU A 1 34 ? 37.792 14.130 29.855 1.00 27.69  ? 35 LEU A CG  1 
ATOM 294  C CD1 . LEU A 1 34 ? 37.574 15.420 30.631 1.00 25.51  ? 35 LEU A CD1 1 
ATOM 295  C CD2 . LEU A 1 34 ? 39.216 13.999 29.325 1.00 31.21  ? 35 LEU A CD2 1 
ATOM 296  N N   . LEU A 1 35 ? 34.551 14.141 29.749 1.00 39.30  ? 36 LEU A N   1 
ATOM 297  C CA  . LEU A 1 35 ? 33.524 14.240 28.717 1.00 38.43  ? 36 LEU A CA  1 
ATOM 298  C C   . LEU A 1 35 ? 33.945 14.829 27.399 1.00 37.01  ? 36 LEU A C   1 
ATOM 299  O O   . LEU A 1 35 ? 33.652 14.292 26.330 1.00 43.80  ? 36 LEU A O   1 
ATOM 300  C CB  . LEU A 1 35 ? 32.355 15.083 29.189 1.00 36.43  ? 36 LEU A CB  1 
ATOM 301  C CG  . LEU A 1 35 ? 31.465 14.509 30.219 1.00 33.86  ? 36 LEU A CG  1 
ATOM 302  C CD1 . LEU A 1 35 ? 30.746 15.570 30.994 1.00 31.47  ? 36 LEU A CD1 1 
ATOM 303  C CD2 . LEU A 1 35 ? 30.559 13.562 29.476 1.00 34.77  ? 36 LEU A CD2 1 
ATOM 304  N N   . ARG A 1 36 ? 34.535 16.008 27.436 1.00 33.35  ? 37 ARG A N   1 
ATOM 305  C CA  . ARG A 1 36 ? 34.946 16.683 26.229 1.00 29.60  ? 37 ARG A CA  1 
ATOM 306  C C   . ARG A 1 36 ? 36.209 17.378 26.579 1.00 22.52  ? 37 ARG A C   1 
ATOM 307  O O   . ARG A 1 36 ? 36.309 17.890 27.684 1.00 27.80  ? 37 ARG A O   1 
ATOM 308  C CB  . ARG A 1 36 ? 33.923 17.735 25.778 1.00 33.38  ? 37 ARG A CB  1 
ATOM 309  C CG  . ARG A 1 36 ? 32.540 17.182 25.389 1.00 46.26  ? 37 ARG A CG  1 
ATOM 310  C CD  . ARG A 1 36 ? 31.479 17.989 26.125 1.00 49.10  ? 37 ARG A CD  1 
ATOM 311  N NE  . ARG A 1 36 ? 30.144 17.418 26.222 1.00 46.78  ? 37 ARG A NE  1 
ATOM 312  C CZ  . ARG A 1 36 ? 29.391 17.686 27.286 1.00 46.21  ? 37 ARG A CZ  1 
ATOM 313  N NH1 . ARG A 1 36 ? 29.861 18.371 28.325 1.00 41.81  ? 37 ARG A NH1 1 
ATOM 314  N NH2 . ARG A 1 36 ? 28.137 17.249 27.338 1.00 51.12  ? 37 ARG A NH2 1 
ATOM 315  N N   . PHE A 1 37 ? 37.180 17.366 25.719 1.00 21.20  ? 38 PHE A N   1 
ATOM 316  C CA  . PHE A 1 37 ? 38.365 18.142 25.973 1.00 23.62  ? 38 PHE A CA  1 
ATOM 317  C C   . PHE A 1 37 ? 38.732 18.684 24.613 1.00 35.47  ? 38 PHE A C   1 
ATOM 318  O O   . PHE A 1 37 ? 38.761 17.945 23.622 1.00 38.40  ? 38 PHE A O   1 
ATOM 319  C CB  . PHE A 1 37 ? 39.419 17.238 26.556 1.00 13.62  ? 38 PHE A CB  1 
ATOM 320  C CG  . PHE A 1 37 ? 40.712 17.845 27.064 1.00 6.23   ? 38 PHE A CG  1 
ATOM 321  C CD1 . PHE A 1 37 ? 41.654 18.347 26.191 1.00 3.01   ? 38 PHE A CD1 1 
ATOM 322  C CD2 . PHE A 1 37 ? 40.964 17.844 28.436 1.00 9.66   ? 38 PHE A CD2 1 
ATOM 323  C CE1 . PHE A 1 37 ? 42.857 18.835 26.706 1.00 2.65   ? 38 PHE A CE1 1 
ATOM 324  C CE2 . PHE A 1 37 ? 42.172 18.340 28.933 1.00 9.73   ? 38 PHE A CE2 1 
ATOM 325  C CZ  . PHE A 1 37 ? 43.125 18.839 28.068 1.00 5.30   ? 38 PHE A CZ  1 
ATOM 326  N N   . ASN A 1 38 ? 38.852 20.008 24.541 1.00 45.79  ? 39 ASN A N   1 
ATOM 327  C CA  . ASN A 1 38 ? 39.134 20.728 23.304 1.00 47.63  ? 39 ASN A CA  1 
ATOM 328  C C   . ASN A 1 38 ? 39.940 21.955 23.589 1.00 41.83  ? 39 ASN A C   1 
ATOM 329  O O   . ASN A 1 38 ? 39.757 22.600 24.613 1.00 42.68  ? 39 ASN A O   1 
ATOM 330  C CB  . ASN A 1 38 ? 37.921 21.252 22.596 1.00 56.74  ? 39 ASN A CB  1 
ATOM 331  C CG  . ASN A 1 38 ? 36.990 20.206 22.016 1.00 68.01  ? 39 ASN A CG  1 
ATOM 332  O OD1 . ASN A 1 38 ? 35.805 20.492 21.837 1.00 73.52  ? 39 ASN A OD1 1 
ATOM 333  N ND2 . ASN A 1 38 ? 37.401 18.993 21.651 1.00 68.69  ? 39 ASN A ND2 1 
ATOM 334  N N   . GLY A 1 39 ? 40.825 22.284 22.684 1.00 38.05  ? 40 GLY A N   1 
ATOM 335  C CA  . GLY A 1 39 ? 41.693 23.409 22.836 1.00 32.40  ? 40 GLY A CA  1 
ATOM 336  C C   . GLY A 1 39 ? 42.692 23.410 21.688 1.00 32.66  ? 40 GLY A C   1 
ATOM 337  O O   . GLY A 1 39 ? 42.624 22.492 20.843 1.00 28.11  ? 40 GLY A O   1 
ATOM 338  N N   . PRO A 1 40 ? 43.571 24.435 21.595 1.00 30.69  ? 41 PRO A N   1 
ATOM 339  C CA  . PRO A 1 40 ? 43.573 25.543 22.527 1.00 25.58  ? 41 PRO A CA  1 
ATOM 340  C C   . PRO A 1 40 ? 42.420 26.497 22.294 1.00 30.14  ? 41 PRO A C   1 
ATOM 341  O O   . PRO A 1 40 ? 41.739 26.481 21.256 1.00 30.68  ? 41 PRO A O   1 
ATOM 342  C CB  . PRO A 1 40 ? 44.898 26.214 22.365 1.00 26.34  ? 41 PRO A CB  1 
ATOM 343  C CG  . PRO A 1 40 ? 45.727 25.491 21.324 1.00 26.58  ? 41 PRO A CG  1 
ATOM 344  C CD  . PRO A 1 40 ? 44.809 24.383 20.812 1.00 28.74  ? 41 PRO A CD  1 
ATOM 345  N N   . VAL A 1 41 ? 42.098 27.236 23.341 1.00 30.88  ? 42 VAL A N   1 
ATOM 346  C CA  . VAL A 1 41 ? 41.081 28.264 23.243 1.00 32.55  ? 42 VAL A CA  1 
ATOM 347  C C   . VAL A 1 41 ? 41.681 29.673 23.561 1.00 40.74  ? 42 VAL A C   1 
ATOM 348  O O   . VAL A 1 41 ? 42.872 29.794 23.957 1.00 40.61  ? 42 VAL A O   1 
ATOM 349  C CB  . VAL A 1 41 ? 39.862 27.909 24.207 1.00 28.82  ? 42 VAL A CB  1 
ATOM 350  C CG1 . VAL A 1 41 ? 39.227 26.664 23.664 1.00 27.24  ? 42 VAL A CG1 1 
ATOM 351  C CG2 . VAL A 1 41 ? 40.221 27.693 25.645 1.00 23.03  ? 42 VAL A CG2 1 
ATOM 352  N N   . PRO A 1 42 ? 40.944 30.792 23.275 1.00 42.79  ? 43 PRO A N   1 
ATOM 353  C CA  . PRO A 1 42 ? 41.381 32.146 23.574 1.00 36.15  ? 43 PRO A CA  1 
ATOM 354  C C   . PRO A 1 42 ? 41.064 32.298 25.058 1.00 34.31  ? 43 PRO A C   1 
ATOM 355  O O   . PRO A 1 42 ? 40.092 31.665 25.520 1.00 33.52  ? 43 PRO A O   1 
ATOM 356  C CB  . PRO A 1 42 ? 40.535 33.017 22.694 1.00 34.44  ? 43 PRO A CB  1 
ATOM 357  C CG  . PRO A 1 42 ? 39.880 32.106 21.698 1.00 37.40  ? 43 PRO A CG  1 
ATOM 358  C CD  . PRO A 1 42 ? 39.666 30.878 22.554 1.00 36.62  ? 43 PRO A CD  1 
ATOM 359  N N   . PRO A 1 43 ? 41.857 33.037 25.854 1.00 34.69  ? 44 PRO A N   1 
ATOM 360  C CA  . PRO A 1 43 ? 41.608 33.258 27.289 1.00 36.12  ? 44 PRO A CA  1 
ATOM 361  C C   . PRO A 1 43 ? 40.356 34.061 27.489 1.00 44.72  ? 44 PRO A C   1 
ATOM 362  O O   . PRO A 1 43 ? 40.002 34.803 26.562 1.00 46.58  ? 44 PRO A O   1 
ATOM 363  C CB  . PRO A 1 43 ? 42.817 33.963 27.806 1.00 32.19  ? 44 PRO A CB  1 
ATOM 364  C CG  . PRO A 1 43 ? 43.307 34.658 26.563 1.00 33.44  ? 44 PRO A CG  1 
ATOM 365  C CD  . PRO A 1 43 ? 43.130 33.608 25.468 1.00 32.43  ? 44 PRO A CD  1 
ATOM 366  N N   . PRO A 1 44 ? 39.653 33.843 28.613 1.00 56.35  ? 45 PRO A N   1 
ATOM 367  C CA  . PRO A 1 44 ? 38.416 34.540 28.965 1.00 61.34  ? 45 PRO A CA  1 
ATOM 368  C C   . PRO A 1 44 ? 38.679 35.829 29.791 1.00 69.09  ? 45 PRO A C   1 
ATOM 369  O O   . PRO A 1 44 ? 39.819 36.329 29.828 1.00 70.39  ? 45 PRO A O   1 
ATOM 370  C CB  . PRO A 1 44 ? 37.645 33.428 29.680 1.00 59.45  ? 45 PRO A CB  1 
ATOM 371  C CG  . PRO A 1 44 ? 38.725 32.770 30.531 1.00 56.52  ? 45 PRO A CG  1 
ATOM 372  C CD  . PRO A 1 44 ? 39.972 32.832 29.631 1.00 54.32  ? 45 PRO A CD  1 
ATOM 373  O OXT . PRO A 1 44 ? 37.736 36.332 30.420 1.00 76.02  ? 45 PRO A OXT 1 
ATOM 374  N N   . GLY B 2 1  ? 20.556 22.236 35.537 1.00 56.35  ? 1  GLY B N   1 
ATOM 375  C CA  . GLY B 2 1  ? 19.576 22.377 36.598 1.00 57.88  ? 1  GLY B CA  1 
ATOM 376  C C   . GLY B 2 1  ? 20.071 23.654 37.235 1.00 51.42  ? 1  GLY B C   1 
ATOM 377  O O   . GLY B 2 1  ? 20.224 24.603 36.482 1.00 53.84  ? 1  GLY B O   1 
ATOM 378  N N   . GLU B 2 2  ? 20.404 23.676 38.521 1.00 47.93  ? 2  GLU B N   1 
ATOM 379  C CA  . GLU B 2 2  ? 21.063 24.810 39.145 1.00 46.48  ? 2  GLU B CA  1 
ATOM 380  C C   . GLU B 2 2  ? 22.394 25.012 38.415 1.00 42.89  ? 2  GLU B C   1 
ATOM 381  O O   . GLU B 2 2  ? 22.856 24.138 37.665 1.00 49.59  ? 2  GLU B O   1 
ATOM 382  C CB  . GLU B 2 2  ? 21.247 24.468 40.642 1.00 52.76  ? 2  GLU B CB  1 
ATOM 383  C CG  . GLU B 2 2  ? 20.882 25.575 41.622 1.00 63.45  ? 2  GLU B CG  1 
ATOM 384  C CD  . GLU B 2 2  ? 22.075 26.290 42.272 1.00 71.35  ? 2  GLU B CD  1 
ATOM 385  O OE1 . GLU B 2 2  ? 22.803 25.604 43.003 1.00 73.55  ? 2  GLU B OE1 1 
ATOM 386  O OE2 . GLU B 2 2  ? 22.267 27.507 42.066 1.00 70.86  ? 2  GLU B OE2 1 
ATOM 387  N N   . TRP B 2 3  ? 22.996 26.164 38.547 1.00 42.18  ? 3  TRP B N   1 
ATOM 388  C CA  . TRP B 2 3  ? 24.253 26.500 37.917 1.00 33.15  ? 3  TRP B CA  1 
ATOM 389  C C   . TRP B 2 3  ? 24.906 27.402 38.939 1.00 40.04  ? 3  TRP B C   1 
ATOM 390  O O   . TRP B 2 3  ? 24.184 28.148 39.607 1.00 52.04  ? 3  TRP B O   1 
ATOM 391  C CB  . TRP B 2 3  ? 23.981 27.269 36.640 1.00 32.44  ? 3  TRP B CB  1 
ATOM 392  C CG  . TRP B 2 3  ? 23.806 26.432 35.367 1.00 36.78  ? 3  TRP B CG  1 
ATOM 393  C CD1 . TRP B 2 3  ? 22.614 26.115 34.729 1.00 37.10  ? 3  TRP B CD1 1 
ATOM 394  C CD2 . TRP B 2 3  ? 24.873 25.925 34.702 1.00 35.35  ? 3  TRP B CD2 1 
ATOM 395  N NE1 . TRP B 2 3  ? 22.945 25.401 33.673 1.00 33.99  ? 3  TRP B NE1 1 
ATOM 396  C CE2 . TRP B 2 3  ? 24.292 25.289 33.630 1.00 34.74  ? 3  TRP B CE2 1 
ATOM 397  C CE3 . TRP B 2 3  ? 26.233 25.968 34.944 1.00 33.91  ? 3  TRP B CE3 1 
ATOM 398  C CZ2 . TRP B 2 3  ? 25.136 24.644 32.768 1.00 39.19  ? 3  TRP B CZ2 1 
ATOM 399  C CZ3 . TRP B 2 3  ? 27.070 25.343 34.069 1.00 36.66  ? 3  TRP B CZ3 1 
ATOM 400  C CH2 . TRP B 2 3  ? 26.513 24.682 32.988 1.00 42.47  ? 3  TRP B CH2 1 
ATOM 401  N N   . GLU B 2 4  ? 26.212 27.344 39.178 1.00 44.49  ? 4  GLU B N   1 
ATOM 402  C CA  . GLU B 2 4  ? 26.920 28.238 40.107 1.00 41.71  ? 4  GLU B CA  1 
ATOM 403  C C   . GLU B 2 4  ? 28.406 28.299 39.784 1.00 36.26  ? 4  GLU B C   1 
ATOM 404  O O   . GLU B 2 4  ? 28.934 27.513 38.994 1.00 39.56  ? 4  GLU B O   1 
ATOM 405  C CB  . GLU B 2 4  ? 26.754 27.790 41.543 1.00 48.06  ? 4  GLU B CB  1 
ATOM 406  C CG  . GLU B 2 4  ? 27.259 26.388 41.781 1.00 55.99  ? 4  GLU B CG  1 
ATOM 407  C CD  . GLU B 2 4  ? 27.024 25.942 43.206 1.00 58.50  ? 4  GLU B CD  1 
ATOM 408  O OE1 . GLU B 2 4  ? 27.767 26.400 44.078 1.00 55.21  ? 4  GLU B OE1 1 
ATOM 409  O OE2 . GLU B 2 4  ? 26.110 25.137 43.415 1.00 59.55  ? 4  GLU B OE2 1 
ATOM 410  N N   . ILE B 2 5  ? 29.071 29.328 40.237 1.00 32.80  ? 5  ILE B N   1 
ATOM 411  C CA  . ILE B 2 5  ? 30.484 29.488 39.970 1.00 31.56  ? 5  ILE B CA  1 
ATOM 412  C C   . ILE B 2 5  ? 31.130 28.858 41.181 1.00 34.17  ? 5  ILE B C   1 
ATOM 413  O O   . ILE B 2 5  ? 30.409 28.708 42.177 1.00 33.34  ? 5  ILE B O   1 
ATOM 414  C CB  . ILE B 2 5  ? 30.816 31.021 39.805 1.00 34.30  ? 5  ILE B CB  1 
ATOM 415  C CG1 . ILE B 2 5  ? 30.244 31.494 38.473 1.00 31.94  ? 5  ILE B CG1 1 
ATOM 416  C CG2 . ILE B 2 5  ? 32.334 31.297 39.885 1.00 35.93  ? 5  ILE B CG2 1 
ATOM 417  C CD1 . ILE B 2 5  ? 31.053 32.650 37.827 1.00 36.72  ? 5  ILE B CD1 1 
ATOM 418  N N   . ILE B 2 6  ? 32.385 28.390 41.097 1.00 39.23  ? 6  ILE B N   1 
ATOM 419  C CA  . ILE B 2 6  ? 33.113 27.809 42.233 1.00 42.24  ? 6  ILE B CA  1 
ATOM 420  C C   . ILE B 2 6  ? 34.531 28.341 42.159 1.00 42.47  ? 6  ILE B C   1 
ATOM 421  O O   . ILE B 2 6  ? 34.948 28.785 41.078 1.00 38.78  ? 6  ILE B O   1 
ATOM 422  C CB  . ILE B 2 6  ? 33.202 26.210 42.235 1.00 42.67  ? 6  ILE B CB  1 
ATOM 423  C CG1 . ILE B 2 6  ? 33.844 25.692 40.940 1.00 45.43  ? 6  ILE B CG1 1 
ATOM 424  C CG2 . ILE B 2 6  ? 31.820 25.600 42.428 1.00 34.94  ? 6  ILE B CG2 1 
ATOM 425  C CD1 . ILE B 2 6  ? 34.038 24.148 40.753 1.00 49.11  ? 6  ILE B CD1 1 
ATOM 426  N N   . ASP B 2 7  ? 35.257 28.236 43.281 1.00 44.26  ? 7  ASP B N   1 
ATOM 427  C CA  . ASP B 2 7  ? 36.613 28.768 43.445 1.00 51.05  ? 7  ASP B CA  1 
ATOM 428  C C   . ASP B 2 7  ? 37.715 27.757 43.144 1.00 49.07  ? 7  ASP B C   1 
ATOM 429  O O   . ASP B 2 7  ? 37.669 26.609 43.585 1.00 52.92  ? 7  ASP B O   1 
ATOM 430  C CB  . ASP B 2 7  ? 36.790 29.279 44.896 1.00 57.68  ? 7  ASP B CB  1 
ATOM 431  C CG  . ASP B 2 7  ? 38.041 30.099 45.274 1.00 68.22  ? 7  ASP B CG  1 
ATOM 432  O OD1 . ASP B 2 7  ? 38.584 30.860 44.457 1.00 73.17  ? 7  ASP B OD1 1 
ATOM 433  O OD2 . ASP B 2 7  ? 38.461 29.990 46.431 1.00 70.65  ? 7  ASP B OD2 1 
ATOM 434  N N   . ILE B 2 8  ? 38.764 28.217 42.481 1.00 42.62  ? 8  ILE B N   1 
ATOM 435  C CA  . ILE B 2 8  ? 39.898 27.408 42.127 1.00 37.78  ? 8  ILE B CA  1 
ATOM 436  C C   . ILE B 2 8  ? 40.823 26.990 43.282 1.00 47.09  ? 8  ILE B C   1 
ATOM 437  O O   . ILE B 2 8  ? 42.050 27.183 43.238 1.00 50.50  ? 8  ILE B O   1 
ATOM 438  C CB  . ILE B 2 8  ? 40.708 28.162 41.051 1.00 33.75  ? 8  ILE B CB  1 
ATOM 439  C CG1 . ILE B 2 8  ? 41.129 29.516 41.533 1.00 35.94  ? 8  ILE B CG1 1 
ATOM 440  C CG2 . ILE B 2 8  ? 39.861 28.338 39.831 1.00 31.44  ? 8  ILE B CG2 1 
ATOM 441  C CD1 . ILE B 2 8  ? 42.463 29.905 40.901 1.00 34.79  ? 8  ILE B CD1 1 
ATOM 442  N N   . GLY B 2 9  ? 40.306 26.357 44.336 1.00 54.61  ? 9  GLY B N   1 
ATOM 443  C CA  . GLY B 2 9  ? 41.154 25.817 45.395 1.00 55.41  ? 9  GLY B CA  1 
ATOM 444  C C   . GLY B 2 9  ? 41.669 24.434 45.013 1.00 58.72  ? 9  GLY B C   1 
ATOM 445  O O   . GLY B 2 9  ? 41.451 23.976 43.876 1.00 62.07  ? 9  GLY B O   1 
ATOM 446  N N   . PRO B 2 10 ? 42.338 23.663 45.885 1.00 59.95  ? 10 PRO B N   1 
ATOM 447  C CA  . PRO B 2 10 ? 42.825 22.313 45.513 1.00 56.24  ? 10 PRO B CA  1 
ATOM 448  C C   . PRO B 2 10 ? 41.716 21.302 45.115 1.00 47.96  ? 10 PRO B C   1 
ATOM 449  O O   . PRO B 2 10 ? 41.977 20.226 44.581 1.00 45.26  ? 10 PRO B O   1 
ATOM 450  C CB  . PRO B 2 10 ? 43.683 21.911 46.723 1.00 58.29  ? 10 PRO B CB  1 
ATOM 451  C CG  . PRO B 2 10 ? 43.218 22.819 47.864 1.00 60.21  ? 10 PRO B CG  1 
ATOM 452  C CD  . PRO B 2 10 ? 42.830 24.117 47.186 1.00 56.35  ? 10 PRO B CD  1 
ATOM 453  N N   . PHE B 2 11 ? 40.441 21.646 45.299 1.00 43.37  ? 11 PHE B N   1 
ATOM 454  C CA  . PHE B 2 11 ? 39.373 20.815 44.788 1.00 43.32  ? 11 PHE B CA  1 
ATOM 455  C C   . PHE B 2 11 ? 39.367 21.041 43.301 1.00 49.32  ? 11 PHE B C   1 
ATOM 456  O O   . PHE B 2 11 ? 39.484 20.070 42.551 1.00 59.01  ? 11 PHE B O   1 
ATOM 457  C CB  . PHE B 2 11 ? 37.993 21.192 45.299 1.00 34.54  ? 11 PHE B CB  1 
ATOM 458  C CG  . PHE B 2 11 ? 36.958 20.225 44.789 1.00 32.70  ? 11 PHE B CG  1 
ATOM 459  C CD1 . PHE B 2 11 ? 36.687 19.096 45.507 1.00 25.85  ? 11 PHE B CD1 1 
ATOM 460  C CD2 . PHE B 2 11 ? 36.294 20.470 43.602 1.00 36.29  ? 11 PHE B CD2 1 
ATOM 461  C CE1 . PHE B 2 11 ? 35.745 18.215 45.033 1.00 24.21  ? 11 PHE B CE1 1 
ATOM 462  C CE2 . PHE B 2 11 ? 35.348 19.564 43.145 1.00 33.25  ? 11 PHE B CE2 1 
ATOM 463  C CZ  . PHE B 2 11 ? 35.074 18.432 43.861 1.00 26.28  ? 11 PHE B CZ  1 
ATOM 464  N N   . THR B 2 12 ? 39.276 22.293 42.855 1.00 48.73  ? 12 THR B N   1 
ATOM 465  C CA  . THR B 2 12 ? 39.254 22.551 41.423 1.00 44.86  ? 12 THR B CA  1 
ATOM 466  C C   . THR B 2 12 ? 40.561 22.166 40.762 1.00 40.26  ? 12 THR B C   1 
ATOM 467  O O   . THR B 2 12 ? 40.517 21.594 39.680 1.00 34.17  ? 12 THR B O   1 
ATOM 468  C CB  . THR B 2 12 ? 38.920 24.019 41.207 1.00 45.28  ? 12 THR B CB  1 
ATOM 469  O OG1 . THR B 2 12 ? 37.932 24.340 42.192 1.00 52.45  ? 12 THR B OG1 1 
ATOM 470  C CG2 . THR B 2 12 ? 38.358 24.304 39.841 1.00 42.53  ? 12 THR B CG2 1 
ATOM 471  N N   . GLN B 2 13 ? 41.722 22.322 41.424 1.00 39.62  ? 13 GLN B N   1 
ATOM 472  C CA  . GLN B 2 13 ? 43.009 21.937 40.826 1.00 40.25  ? 13 GLN B CA  1 
ATOM 473  C C   . GLN B 2 13 ? 43.077 20.454 40.583 1.00 41.03  ? 13 GLN B C   1 
ATOM 474  O O   . GLN B 2 13 ? 43.759 20.028 39.654 1.00 45.04  ? 13 GLN B O   1 
ATOM 475  C CB  . GLN B 2 13 ? 44.206 22.265 41.695 1.00 39.78  ? 13 GLN B CB  1 
ATOM 476  C CG  . GLN B 2 13 ? 44.403 23.755 41.962 1.00 44.56  ? 13 GLN B CG  1 
ATOM 477  C CD  . GLN B 2 13 ? 44.446 24.635 40.709 1.00 44.99  ? 13 GLN B CD  1 
ATOM 478  O OE1 . GLN B 2 13 ? 45.267 24.465 39.797 1.00 45.87  ? 13 GLN B OE1 1 
ATOM 479  N NE2 . GLN B 2 13 ? 43.542 25.606 40.632 1.00 41.07  ? 13 GLN B NE2 1 
ATOM 480  N N   . ASN B 2 14 ? 42.381 19.675 41.414 1.00 40.84  ? 14 ASN B N   1 
ATOM 481  C CA  . ASN B 2 14 ? 42.251 18.242 41.202 1.00 42.49  ? 14 ASN B CA  1 
ATOM 482  C C   . ASN B 2 14 ? 41.515 17.870 39.940 1.00 36.82  ? 14 ASN B C   1 
ATOM 483  O O   . ASN B 2 14 ? 41.970 17.011 39.180 1.00 38.76  ? 14 ASN B O   1 
ATOM 484  C CB  . ASN B 2 14 ? 41.511 17.553 42.336 1.00 51.41  ? 14 ASN B CB  1 
ATOM 485  C CG  . ASN B 2 14 ? 42.438 16.660 43.141 1.00 58.54  ? 14 ASN B CG  1 
ATOM 486  O OD1 . ASN B 2 14 ? 43.685 16.825 43.178 1.00 61.32  ? 14 ASN B OD1 1 
ATOM 487  N ND2 . ASN B 2 14 ? 41.815 15.645 43.756 1.00 55.66  ? 14 ASN B ND2 1 
ATOM 488  N N   . LEU B 2 15 ? 40.369 18.481 39.658 1.00 33.48  ? 15 LEU B N   1 
ATOM 489  C CA  . LEU B 2 15 ? 39.665 18.190 38.421 1.00 29.32  ? 15 LEU B CA  1 
ATOM 490  C C   . LEU B 2 15 ? 40.511 18.679 37.266 1.00 31.55  ? 15 LEU B C   1 
ATOM 491  O O   . LEU B 2 15 ? 40.309 18.264 36.127 1.00 36.42  ? 15 LEU B O   1 
ATOM 492  C CB  . LEU B 2 15 ? 38.346 18.878 38.400 1.00 25.75  ? 15 LEU B CB  1 
ATOM 493  C CG  . LEU B 2 15 ? 37.396 18.380 39.438 1.00 25.29  ? 15 LEU B CG  1 
ATOM 494  C CD1 . LEU B 2 15 ? 36.777 19.555 40.109 1.00 34.33  ? 15 LEU B CD1 1 
ATOM 495  C CD2 . LEU B 2 15 ? 36.273 17.579 38.800 1.00 32.39  ? 15 LEU B CD2 1 
ATOM 496  N N   . GLY B 2 16 ? 41.475 19.569 37.520 1.00 30.15  ? 16 GLY B N   1 
ATOM 497  C CA  . GLY B 2 16 ? 42.421 19.921 36.485 1.00 35.00  ? 16 GLY B CA  1 
ATOM 498  C C   . GLY B 2 16 ? 43.239 18.694 36.094 1.00 38.08  ? 16 GLY B C   1 
ATOM 499  O O   . GLY B 2 16 ? 43.154 18.233 34.943 1.00 38.50  ? 16 GLY B O   1 
ATOM 500  N N   . LYS B 2 17 ? 43.998 18.152 37.077 1.00 40.36  ? 17 LYS B N   1 
ATOM 501  C CA  . LYS B 2 17 ? 44.854 16.962 36.927 1.00 36.84  ? 17 LYS B CA  1 
ATOM 502  C C   . LYS B 2 17 ? 44.128 15.782 36.309 1.00 34.89  ? 17 LYS B C   1 
ATOM 503  O O   . LYS B 2 17 ? 44.624 15.258 35.316 1.00 33.78  ? 17 LYS B O   1 
ATOM 504  C CB  . LYS B 2 17 ? 45.387 16.488 38.243 1.00 37.45  ? 17 LYS B CB  1 
ATOM 505  C CG  . LYS B 2 17 ? 46.367 17.490 38.727 1.00 47.99  ? 17 LYS B CG  1 
ATOM 506  C CD  . LYS B 2 17 ? 47.113 16.924 39.905 1.00 54.46  ? 17 LYS B CD  1 
ATOM 507  C CE  . LYS B 2 17 ? 48.307 17.849 40.197 1.00 54.79  ? 17 LYS B CE  1 
ATOM 508  N NZ  . LYS B 2 17 ? 47.991 18.815 41.229 1.00 52.95  ? 17 LYS B NZ  1 
ATOM 509  N N   . PHE B 2 18 ? 42.970 15.368 36.857 1.00 33.84  ? 18 PHE B N   1 
ATOM 510  C CA  . PHE B 2 18 ? 42.157 14.310 36.273 1.00 30.09  ? 18 PHE B CA  1 
ATOM 511  C C   . PHE B 2 18 ? 41.897 14.597 34.815 1.00 32.61  ? 18 PHE B C   1 
ATOM 512  O O   . PHE B 2 18 ? 42.096 13.661 34.048 1.00 40.35  ? 18 PHE B O   1 
ATOM 513  C CB  . PHE B 2 18 ? 40.793 14.158 36.943 1.00 23.95  ? 18 PHE B CB  1 
ATOM 514  C CG  . PHE B 2 18 ? 39.810 13.166 36.318 1.00 23.26  ? 18 PHE B CG  1 
ATOM 515  C CD1 . PHE B 2 18 ? 39.083 13.463 35.189 1.00 25.17  ? 18 PHE B CD1 1 
ATOM 516  C CD2 . PHE B 2 18 ? 39.572 11.957 36.927 1.00 27.47  ? 18 PHE B CD2 1 
ATOM 517  C CE1 . PHE B 2 18 ? 38.143 12.580 34.685 1.00 31.64  ? 18 PHE B CE1 1 
ATOM 518  C CE2 . PHE B 2 18 ? 38.629 11.071 36.430 1.00 26.58  ? 18 PHE B CE2 1 
ATOM 519  C CZ  . PHE B 2 18 ? 37.905 11.374 35.303 1.00 31.37  ? 18 PHE B CZ  1 
ATOM 520  N N   . ALA B 2 19 ? 41.499 15.806 34.390 1.00 32.17  ? 19 ALA B N   1 
ATOM 521  C CA  . ALA B 2 19 ? 41.156 16.024 32.996 1.00 31.06  ? 19 ALA B CA  1 
ATOM 522  C C   . ALA B 2 19 ? 42.342 15.783 32.117 1.00 28.96  ? 19 ALA B C   1 
ATOM 523  O O   . ALA B 2 19 ? 42.223 15.041 31.149 1.00 34.50  ? 19 ALA B O   1 
ATOM 524  C CB  . ALA B 2 19 ? 40.667 17.439 32.748 1.00 34.01  ? 19 ALA B CB  1 
ATOM 525  N N   . VAL B 2 20 ? 43.507 16.291 32.477 1.00 26.55  ? 20 VAL B N   1 
ATOM 526  C CA  . VAL B 2 20 ? 44.723 16.065 31.673 1.00 29.77  ? 20 VAL B CA  1 
ATOM 527  C C   . VAL B 2 20 ? 45.138 14.610 31.600 1.00 32.36  ? 20 VAL B C   1 
ATOM 528  O O   . VAL B 2 20 ? 45.372 14.135 30.499 1.00 34.80  ? 20 VAL B O   1 
ATOM 529  C CB  . VAL B 2 20 ? 45.910 16.803 32.218 1.00 26.67  ? 20 VAL B CB  1 
ATOM 530  C CG1 . VAL B 2 20 ? 47.112 16.451 31.444 1.00 25.75  ? 20 VAL B CG1 1 
ATOM 531  C CG2 . VAL B 2 20 ? 45.654 18.280 32.141 1.00 29.90  ? 20 VAL B CG2 1 
ATOM 532  N N   . ASP B 2 21 ? 45.290 13.912 32.739 1.00 40.59  ? 21 ASP B N   1 
ATOM 533  C CA  . ASP B 2 21 ? 45.638 12.487 32.794 1.00 41.76  ? 21 ASP B CA  1 
ATOM 534  C C   . ASP B 2 21 ? 44.706 11.655 31.914 1.00 50.39  ? 21 ASP B C   1 
ATOM 535  O O   . ASP B 2 21 ? 45.172 10.873 31.056 1.00 56.81  ? 21 ASP B O   1 
ATOM 536  C CB  . ASP B 2 21 ? 45.557 11.977 34.218 1.00 33.50  ? 21 ASP B CB  1 
ATOM 537  C CG  . ASP B 2 21 ? 46.680 12.528 35.093 1.00 42.21  ? 21 ASP B CG  1 
ATOM 538  O OD1 . ASP B 2 21 ? 47.676 13.042 34.561 1.00 41.99  ? 21 ASP B OD1 1 
ATOM 539  O OD2 . ASP B 2 21 ? 46.572 12.449 36.327 1.00 45.98  ? 21 ASP B OD2 1 
ATOM 540  N N   . GLU B 2 22 ? 43.396 11.888 32.047 1.00 46.03  ? 22 GLU B N   1 
ATOM 541  C CA  . GLU B 2 22 ? 42.423 11.248 31.193 1.00 43.67  ? 22 GLU B CA  1 
ATOM 542  C C   . GLU B 2 22 ? 42.566 11.576 29.720 1.00 45.66  ? 22 GLU B C   1 
ATOM 543  O O   . GLU B 2 22 ? 42.336 10.718 28.858 1.00 53.76  ? 22 GLU B O   1 
ATOM 544  C CB  . GLU B 2 22 ? 41.089 11.634 31.620 1.00 44.01  ? 22 GLU B CB  1 
ATOM 545  C CG  . GLU B 2 22 ? 40.841 10.693 32.752 1.00 48.54  ? 22 GLU B CG  1 
ATOM 546  C CD  . GLU B 2 22 ? 39.878 9.604  32.347 1.00 51.47  ? 22 GLU B CD  1 
ATOM 547  O OE1 . GLU B 2 22 ? 38.677 9.877  32.223 1.00 49.21  ? 22 GLU B OE1 1 
ATOM 548  O OE2 . GLU B 2 22 ? 40.354 8.490  32.165 1.00 52.28  ? 22 GLU B OE2 1 
ATOM 549  N N   . GLU B 2 23 ? 42.949 12.786 29.351 1.00 41.55  ? 23 GLU B N   1 
ATOM 550  C CA  . GLU B 2 23 ? 43.163 13.025 27.943 1.00 38.78  ? 23 GLU B CA  1 
ATOM 551  C C   . GLU B 2 23 ? 44.368 12.219 27.488 1.00 37.09  ? 23 GLU B C   1 
ATOM 552  O O   . GLU B 2 23 ? 44.302 11.617 26.416 1.00 31.04  ? 23 GLU B O   1 
ATOM 553  C CB  . GLU B 2 23 ? 43.428 14.516 27.646 1.00 39.94  ? 23 GLU B CB  1 
ATOM 554  C CG  . GLU B 2 23 ? 43.626 14.910 26.172 1.00 36.35  ? 23 GLU B CG  1 
ATOM 555  C CD  . GLU B 2 23 ? 42.540 14.461 25.184 1.00 37.37  ? 23 GLU B CD  1 
ATOM 556  O OE1 . GLU B 2 23 ? 41.439 14.130 25.648 1.00 33.61  ? 23 GLU B OE1 1 
ATOM 557  O OE2 . GLU B 2 23 ? 42.801 14.446 23.957 1.00 36.09  ? 23 GLU B OE2 1 
ATOM 558  N N   . ASN B 2 24 ? 45.419 12.131 28.310 1.00 31.57  ? 24 ASN B N   1 
ATOM 559  C CA  . ASN B 2 24 ? 46.663 11.534 27.897 1.00 29.61  ? 24 ASN B CA  1 
ATOM 560  C C   . ASN B 2 24 ? 46.615 10.064 27.526 1.00 32.09  ? 24 ASN B C   1 
ATOM 561  O O   . ASN B 2 24 ? 47.389 9.625  26.666 1.00 31.16  ? 24 ASN B O   1 
ATOM 562  C CB  . ASN B 2 24 ? 47.650 11.816 28.986 1.00 33.79  ? 24 ASN B CB  1 
ATOM 563  C CG  . ASN B 2 24 ? 48.294 13.215 28.889 1.00 38.56  ? 24 ASN B CG  1 
ATOM 564  O OD1 . ASN B 2 24 ? 48.473 13.785 27.809 1.00 45.06  ? 24 ASN B OD1 1 
ATOM 565  N ND2 . ASN B 2 24 ? 48.695 13.861 29.977 1.00 36.47  ? 24 ASN B ND2 1 
ATOM 566  N N   . LYS B 2 25 ? 45.638 9.323  28.049 1.00 35.97  ? 25 LYS B N   1 
ATOM 567  C CA  . LYS B 2 25 ? 45.344 7.954  27.625 1.00 38.62  ? 25 LYS B CA  1 
ATOM 568  C C   . LYS B 2 25 ? 44.663 7.865  26.246 1.00 42.17  ? 25 LYS B C   1 
ATOM 569  O O   . LYS B 2 25 ? 44.705 6.811  25.596 1.00 46.70  ? 25 LYS B O   1 
ATOM 570  C CB  . LYS B 2 25 ? 44.393 7.305  28.509 1.00 45.11  ? 25 LYS B CB  1 
ATOM 571  C CG  . LYS B 2 25 ? 44.602 7.299  29.980 1.00 54.84  ? 25 LYS B CG  1 
ATOM 572  C CD  . LYS B 2 25 ? 43.263 6.654  30.367 1.00 66.97  ? 25 LYS B CD  1 
ATOM 573  C CE  . LYS B 2 25 ? 43.158 6.476  31.865 1.00 76.12  ? 25 LYS B CE  1 
ATOM 574  N NZ  . LYS B 2 25 ? 41.963 5.722  32.203 1.00 82.20  ? 25 LYS B NZ  1 
ATOM 575  N N   . ILE B 2 26 ? 43.979 8.941  25.793 1.00 44.04  ? 26 ILE B N   1 
ATOM 576  C CA  . ILE B 2 26 ? 43.315 9.074  24.481 1.00 37.17  ? 26 ILE B CA  1 
ATOM 577  C C   . ILE B 2 26 ? 44.008 10.121 23.571 1.00 43.96  ? 26 ILE B C   1 
ATOM 578  O O   . ILE B 2 26 ? 43.557 10.462 22.491 1.00 38.35  ? 26 ILE B O   1 
ATOM 579  C CB  . ILE B 2 26 ? 41.909 9.505  24.725 1.00 33.86  ? 26 ILE B CB  1 
ATOM 580  C CG1 . ILE B 2 26 ? 41.336 8.993  26.087 1.00 37.25  ? 26 ILE B CG1 1 
ATOM 581  C CG2 . ILE B 2 26 ? 41.154 8.971  23.528 1.00 38.57  ? 26 ILE B CG2 1 
ATOM 582  C CD1 . ILE B 2 26 ? 40.147 9.716  26.761 1.00 28.67  ? 26 ILE B CD1 1 
ATOM 583  N N   . GLY B 2 27 ? 45.226 10.520 23.961 1.00 62.92  ? 27 GLY B N   1 
ATOM 584  C CA  . GLY B 2 27 ? 46.109 11.614 23.523 1.00 75.47  ? 27 GLY B CA  1 
ATOM 585  C C   . GLY B 2 27 ? 46.346 12.055 22.094 1.00 82.96  ? 27 GLY B C   1 
ATOM 586  O O   . GLY B 2 27 ? 47.456 12.287 21.595 1.00 83.05  ? 27 GLY B O   1 
ATOM 587  N N   . GLN B 2 28 ? 45.202 12.466 21.611 1.00 88.88  ? 28 GLN B N   1 
ATOM 588  C CA  . GLN B 2 28 ? 44.997 13.216 20.388 1.00 93.32  ? 28 GLN B CA  1 
ATOM 589  C C   . GLN B 2 28 ? 45.930 14.495 20.284 1.00 85.64  ? 28 GLN B C   1 
ATOM 590  O O   . GLN B 2 28 ? 46.206 14.981 19.188 1.00 76.93  ? 28 GLN B O   1 
ATOM 591  C CB  . GLN B 2 28 ? 43.485 13.433 20.581 1.00 99.54  ? 28 GLN B CB  1 
ATOM 592  C CG  . GLN B 2 28 ? 42.325 13.665 19.629 1.00 102.41 ? 28 GLN B CG  1 
ATOM 593  C CD  . GLN B 2 28 ? 41.490 12.408 19.455 1.00 103.42 ? 28 GLN B CD  1 
ATOM 594  O OE1 . GLN B 2 28 ? 40.576 12.062 20.212 1.00 103.55 ? 28 GLN B OE1 1 
ATOM 595  N NE2 . GLN B 2 28 ? 41.841 11.759 18.358 1.00 101.88 ? 28 GLN B NE2 1 
ATOM 596  N N   . TYR B 2 29 ? 46.263 15.137 21.437 1.00 83.94  ? 29 TYR B N   1 
ATOM 597  C CA  . TYR B 2 29 ? 47.147 16.333 21.573 1.00 80.60  ? 29 TYR B CA  1 
ATOM 598  C C   . TYR B 2 29 ? 48.615 15.870 21.766 1.00 73.99  ? 29 TYR B C   1 
ATOM 599  O O   . TYR B 2 29 ? 49.484 16.598 22.281 1.00 72.62  ? 29 TYR B O   1 
ATOM 600  C CB  . TYR B 2 29 ? 46.801 17.282 22.841 1.00 83.96  ? 29 TYR B CB  1 
ATOM 601  C CG  . TYR B 2 29 ? 45.485 18.060 22.807 1.00 84.33  ? 29 TYR B CG  1 
ATOM 602  C CD1 . TYR B 2 29 ? 45.430 19.216 22.032 1.00 82.27  ? 29 TYR B CD1 1 
ATOM 603  C CD2 . TYR B 2 29 ? 44.362 17.560 23.394 1.00 88.44  ? 29 TYR B CD2 1 
ATOM 604  C CE1 . TYR B 2 29 ? 44.231 19.831 21.811 1.00 86.69  ? 29 TYR B CE1 1 
ATOM 605  C CE2 . TYR B 2 29 ? 43.147 18.191 23.166 1.00 90.45  ? 29 TYR B CE2 1 
ATOM 606  C CZ  . TYR B 2 29 ? 43.088 19.305 22.362 1.00 90.37  ? 29 TYR B CZ  1 
ATOM 607  O OH  . TYR B 2 29 ? 41.869 19.837 22.003 1.00 94.55  ? 29 TYR B OH  1 
ATOM 608  N N   . GLY B 2 30 ? 48.979 14.642 21.381 1.00 60.55  ? 30 GLY B N   1 
ATOM 609  C CA  . GLY B 2 30 ? 50.285 14.155 21.748 1.00 55.21  ? 30 GLY B CA  1 
ATOM 610  C C   . GLY B 2 30 ? 50.203 13.654 23.183 1.00 55.51  ? 30 GLY B C   1 
ATOM 611  O O   . GLY B 2 30 ? 49.555 12.619 23.423 1.00 60.53  ? 30 GLY B O   1 
ATOM 612  N N   . ARG B 2 31 ? 50.841 14.380 24.113 1.00 46.85  ? 31 ARG B N   1 
ATOM 613  C CA  . ARG B 2 31 ? 50.843 14.095 25.560 1.00 45.66  ? 31 ARG B CA  1 
ATOM 614  C C   . ARG B 2 31 ? 51.102 15.453 26.207 1.00 45.23  ? 31 ARG B C   1 
ATOM 615  O O   . ARG B 2 31 ? 51.887 16.184 25.598 1.00 43.56  ? 31 ARG B O   1 
ATOM 616  C CB  . ARG B 2 31 ? 51.990 13.176 26.004 1.00 51.76  ? 31 ARG B CB  1 
ATOM 617  C CG  . ARG B 2 31 ? 52.306 12.981 27.532 1.00 51.54  ? 31 ARG B CG  1 
ATOM 618  C CD  . ARG B 2 31 ? 51.689 11.717 28.180 1.00 50.19  ? 31 ARG B CD  1 
ATOM 619  N NE  . ARG B 2 31 ? 52.132 10.564 27.407 1.00 49.84  ? 31 ARG B NE  1 
ATOM 620  C CZ  . ARG B 2 31 ? 51.531 9.377  27.399 1.00 50.38  ? 31 ARG B CZ  1 
ATOM 621  N NH1 . ARG B 2 31 ? 50.513 9.096  28.220 1.00 52.86  ? 31 ARG B NH1 1 
ATOM 622  N NH2 . ARG B 2 31 ? 52.019 8.444  26.581 1.00 44.19  ? 31 ARG B NH2 1 
ATOM 623  N N   . LEU B 2 32 ? 50.548 15.790 27.396 1.00 39.96  ? 32 LEU B N   1 
ATOM 624  C CA  . LEU B 2 32 ? 50.622 17.147 27.952 1.00 30.93  ? 32 LEU B CA  1 
ATOM 625  C C   . LEU B 2 32 ? 50.930 17.191 29.425 1.00 36.38  ? 32 LEU B C   1 
ATOM 626  O O   . LEU B 2 32 ? 50.324 16.414 30.174 1.00 39.94  ? 32 LEU B O   1 
ATOM 627  C CB  . LEU B 2 32 ? 49.321 17.916 27.861 1.00 17.10  ? 32 LEU B CB  1 
ATOM 628  C CG  . LEU B 2 32 ? 48.660 18.285 26.564 1.00 9.57   ? 32 LEU B CG  1 
ATOM 629  C CD1 . LEU B 2 32 ? 47.180 18.355 26.838 1.00 2.00   ? 32 LEU B CD1 1 
ATOM 630  C CD2 . LEU B 2 32 ? 49.299 19.511 25.965 1.00 2.00   ? 32 LEU B CD2 1 
ATOM 631  N N   . THR B 2 33 ? 51.745 18.177 29.811 1.00 36.01  ? 33 THR B N   1 
ATOM 632  C CA  . THR B 2 33 ? 52.008 18.477 31.220 1.00 39.35  ? 33 THR B CA  1 
ATOM 633  C C   . THR B 2 33 ? 51.012 19.488 31.801 1.00 37.30  ? 33 THR B C   1 
ATOM 634  O O   . THR B 2 33 ? 50.821 20.579 31.281 1.00 43.35  ? 33 THR B O   1 
ATOM 635  C CB  . THR B 2 33 ? 53.492 18.985 31.397 1.00 39.52  ? 33 THR B CB  1 
ATOM 636  O OG1 . THR B 2 33 ? 53.550 19.560 32.712 1.00 37.44  ? 33 THR B OG1 1 
ATOM 637  C CG2 . THR B 2 33 ? 53.985 19.877 30.259 1.00 37.96  ? 33 THR B CG2 1 
ATOM 638  N N   . PHE B 2 34 ? 50.262 19.125 32.831 1.00 36.89  ? 34 PHE B N   1 
ATOM 639  C CA  . PHE B 2 34 ? 49.327 20.024 33.491 1.00 39.52  ? 34 PHE B CA  1 
ATOM 640  C C   . PHE B 2 34 ? 50.148 21.142 34.045 1.00 44.64  ? 34 PHE B C   1 
ATOM 641  O O   . PHE B 2 34 ? 51.305 20.895 34.412 1.00 43.56  ? 34 PHE B O   1 
ATOM 642  C CB  . PHE B 2 34 ? 48.629 19.334 34.638 1.00 39.35  ? 34 PHE B CB  1 
ATOM 643  C CG  . PHE B 2 34 ? 47.789 20.114 35.639 1.00 36.53  ? 34 PHE B CG  1 
ATOM 644  C CD1 . PHE B 2 34 ? 48.366 20.697 36.758 1.00 40.59  ? 34 PHE B CD1 1 
ATOM 645  C CD2 . PHE B 2 34 ? 46.417 20.162 35.487 1.00 41.48  ? 34 PHE B CD2 1 
ATOM 646  C CE1 . PHE B 2 34 ? 47.576 21.328 37.717 1.00 41.83  ? 34 PHE B CE1 1 
ATOM 647  C CE2 . PHE B 2 34 ? 45.643 20.793 36.449 1.00 39.77  ? 34 PHE B CE2 1 
ATOM 648  C CZ  . PHE B 2 34 ? 46.206 21.371 37.567 1.00 40.63  ? 34 PHE B CZ  1 
ATOM 649  N N   . ASN B 2 35 ? 49.499 22.313 34.095 1.00 49.32  ? 35 ASN B N   1 
ATOM 650  C CA  . ASN B 2 35 ? 50.069 23.557 34.611 1.00 49.69  ? 35 ASN B CA  1 
ATOM 651  C C   . ASN B 2 35 ? 49.195 24.280 35.615 1.00 48.95  ? 35 ASN B C   1 
ATOM 652  O O   . ASN B 2 35 ? 49.756 24.558 36.664 1.00 47.87  ? 35 ASN B O   1 
ATOM 653  C CB  . ASN B 2 35 ? 50.380 24.503 33.488 1.00 50.10  ? 35 ASN B CB  1 
ATOM 654  C CG  . ASN B 2 35 ? 51.663 24.047 32.838 1.00 55.50  ? 35 ASN B CG  1 
ATOM 655  O OD1 . ASN B 2 35 ? 51.708 23.901 31.607 1.00 57.62  ? 35 ASN B OD1 1 
ATOM 656  N ND2 . ASN B 2 35 ? 52.702 23.843 33.660 1.00 52.51  ? 35 ASN B ND2 1 
ATOM 657  N N   . LYS B 2 36 ? 47.909 24.622 35.374 1.00 46.35  ? 36 LYS B N   1 
ATOM 658  C CA  . LYS B 2 36 ? 47.045 25.154 36.432 1.00 43.18  ? 36 LYS B CA  1 
ATOM 659  C C   . LYS B 2 36 ? 45.599 25.261 35.971 1.00 40.85  ? 36 LYS B C   1 
ATOM 660  O O   . LYS B 2 36 ? 45.387 25.030 34.789 1.00 40.78  ? 36 LYS B O   1 
ATOM 661  C CB  . LYS B 2 36 ? 47.466 26.538 36.877 1.00 46.12  ? 36 LYS B CB  1 
ATOM 662  C CG  . LYS B 2 36 ? 47.403 27.547 35.774 1.00 54.11  ? 36 LYS B CG  1 
ATOM 663  C CD  . LYS B 2 36 ? 47.336 28.880 36.452 1.00 62.70  ? 36 LYS B CD  1 
ATOM 664  C CE  . LYS B 2 36 ? 48.719 29.308 36.872 1.00 69.33  ? 36 LYS B CE  1 
ATOM 665  N NZ  . LYS B 2 36 ? 49.352 29.962 35.741 1.00 72.79  ? 36 LYS B NZ  1 
ATOM 666  N N   . VAL B 2 37 ? 44.616 25.515 36.860 1.00 40.52  ? 37 VAL B N   1 
ATOM 667  C CA  . VAL B 2 37 ? 43.206 25.777 36.529 1.00 37.52  ? 37 VAL B CA  1 
ATOM 668  C C   . VAL B 2 37 ? 43.028 27.267 36.715 1.00 42.40  ? 37 VAL B C   1 
ATOM 669  O O   . VAL B 2 37 ? 43.378 27.818 37.777 1.00 41.21  ? 37 VAL B O   1 
ATOM 670  C CB  . VAL B 2 37 ? 42.154 25.082 37.483 1.00 35.32  ? 37 VAL B CB  1 
ATOM 671  C CG1 . VAL B 2 37 ? 40.791 25.763 37.505 1.00 33.89  ? 37 VAL B CG1 1 
ATOM 672  C CG2 . VAL B 2 37 ? 41.787 23.747 36.912 1.00 32.98  ? 37 VAL B CG2 1 
ATOM 673  N N   . ILE B 2 38 ? 42.460 27.911 35.697 1.00 44.70  ? 38 ILE B N   1 
ATOM 674  C CA  . ILE B 2 38 ? 42.211 29.344 35.799 1.00 37.90  ? 38 ILE B CA  1 
ATOM 675  C C   . ILE B 2 38 ? 40.717 29.569 35.996 1.00 36.32  ? 38 ILE B C   1 
ATOM 676  O O   . ILE B 2 38 ? 39.946 28.598 35.812 1.00 37.62  ? 38 ILE B O   1 
ATOM 677  C CB  . ILE B 2 38 ? 42.733 30.072 34.522 1.00 34.33  ? 38 ILE B CB  1 
ATOM 678  C CG1 . ILE B 2 38 ? 42.160 29.616 33.226 1.00 28.41  ? 38 ILE B CG1 1 
ATOM 679  C CG2 . ILE B 2 38 ? 44.218 29.801 34.473 1.00 37.18  ? 38 ILE B CG2 1 
ATOM 680  C CD1 . ILE B 2 38 ? 42.703 30.542 32.142 1.00 25.14  ? 38 ILE B CD1 1 
ATOM 681  N N   . ARG B 2 39 ? 40.307 30.799 36.421 1.00 32.46  ? 39 ARG B N   1 
ATOM 682  C CA  . ARG B 2 39 ? 38.877 31.136 36.615 1.00 26.93  ? 39 ARG B CA  1 
ATOM 683  C C   . ARG B 2 39 ? 38.254 31.584 35.293 1.00 25.01  ? 39 ARG B C   1 
ATOM 684  O O   . ARG B 2 39 ? 38.956 32.100 34.420 1.00 25.07  ? 39 ARG B O   1 
ATOM 685  C CB  . ARG B 2 39 ? 38.678 32.270 37.590 1.00 31.13  ? 39 ARG B CB  1 
ATOM 686  C CG  . ARG B 2 39 ? 39.626 32.300 38.780 1.00 42.24  ? 39 ARG B CG  1 
ATOM 687  C CD  . ARG B 2 39 ? 39.504 33.640 39.549 1.00 49.52  ? 39 ARG B CD  1 
ATOM 688  N NE  . ARG B 2 39 ? 40.479 33.788 40.628 1.00 54.02  ? 39 ARG B NE  1 
ATOM 689  C CZ  . ARG B 2 39 ? 40.335 33.145 41.804 1.00 58.17  ? 39 ARG B CZ  1 
ATOM 690  N NH1 . ARG B 2 39 ? 39.283 32.363 42.080 1.00 56.85  ? 39 ARG B NH1 1 
ATOM 691  N NH2 . ARG B 2 39 ? 41.280 33.260 42.737 1.00 59.94  ? 39 ARG B NH2 1 
ATOM 692  N N   . PRO B 2 40 ? 36.972 31.435 35.030 1.00 23.07  ? 40 PRO B N   1 
ATOM 693  C CA  . PRO B 2 40 ? 35.969 30.848 35.891 1.00 33.92  ? 40 PRO B CA  1 
ATOM 694  C C   . PRO B 2 40 ? 35.749 29.290 35.815 1.00 37.82  ? 40 PRO B C   1 
ATOM 695  O O   . PRO B 2 40 ? 36.013 28.639 34.800 1.00 43.49  ? 40 PRO B O   1 
ATOM 696  C CB  . PRO B 2 40 ? 34.778 31.730 35.499 1.00 24.35  ? 40 PRO B CB  1 
ATOM 697  C CG  . PRO B 2 40 ? 34.874 31.745 34.011 1.00 17.16  ? 40 PRO B CG  1 
ATOM 698  C CD  . PRO B 2 40 ? 36.370 31.871 33.779 1.00 19.78  ? 40 PRO B CD  1 
ATOM 699  N N   . CYS B 2 41 ? 35.192 28.677 36.875 1.00 38.21  ? 41 CYS B N   1 
ATOM 700  C CA  . CYS B 2 41 ? 34.907 27.256 36.959 1.00 38.24  ? 41 CYS B CA  1 
ATOM 701  C C   . CYS B 2 41 ? 33.483 27.151 37.392 1.00 27.11  ? 41 CYS B C   1 
ATOM 702  O O   . CYS B 2 41 ? 33.057 27.476 38.485 1.00 24.61  ? 41 CYS B O   1 
ATOM 703  C CB  . CYS B 2 41 ? 35.837 26.567 37.999 1.00 47.16  ? 41 CYS B CB  1 
ATOM 704  S SG  . CYS B 2 41 ? 35.809 24.748 38.128 1.00 48.84  ? 41 CYS B SG  1 
ATOM 705  N N   . MET B 2 42 ? 32.776 26.640 36.487 1.00 20.41  ? 42 MET B N   1 
ATOM 706  C CA  . MET B 2 42 ? 31.352 26.551 36.530 1.00 34.51  ? 42 MET B CA  1 
ATOM 707  C C   . MET B 2 42 ? 30.887 25.209 37.178 1.00 37.46  ? 42 MET B C   1 
ATOM 708  O O   . MET B 2 42 ? 31.615 24.211 37.065 1.00 39.79  ? 42 MET B O   1 
ATOM 709  C CB  . MET B 2 42 ? 31.176 26.773 35.030 1.00 43.71  ? 42 MET B CB  1 
ATOM 710  C CG  . MET B 2 42 ? 29.965 27.278 34.285 1.00 49.17  ? 42 MET B CG  1 
ATOM 711  S SD  . MET B 2 42 ? 29.725 28.972 34.824 1.00 49.36  ? 42 MET B SD  1 
ATOM 712  C CE  . MET B 2 42 ? 28.040 28.769 35.335 1.00 50.46  ? 42 MET B CE  1 
ATOM 713  N N   . LYS B 2 43 ? 29.740 25.041 37.861 1.00 36.14  ? 43 LYS B N   1 
ATOM 714  C CA  . LYS B 2 43 ? 29.342 23.699 38.232 1.00 32.12  ? 43 LYS B CA  1 
ATOM 715  C C   . LYS B 2 43 ? 27.863 23.467 38.265 1.00 31.64  ? 43 LYS B C   1 
ATOM 716  O O   . LYS B 2 43 ? 27.137 24.025 39.075 1.00 40.09  ? 43 LYS B O   1 
ATOM 717  C CB  . LYS B 2 43 ? 29.988 23.368 39.571 1.00 37.16  ? 43 LYS B CB  1 
ATOM 718  C CG  . LYS B 2 43 ? 29.369 23.424 40.962 1.00 41.99  ? 43 LYS B CG  1 
ATOM 719  C CD  . LYS B 2 43 ? 29.342 21.995 41.534 1.00 45.62  ? 43 LYS B CD  1 
ATOM 720  C CE  . LYS B 2 43 ? 28.796 21.881 42.949 1.00 47.77  ? 43 LYS B CE  1 
ATOM 721  N NZ  . LYS B 2 43 ? 29.765 22.320 43.936 1.00 50.57  ? 43 LYS B NZ  1 
ATOM 722  N N   . LYS B 2 44 ? 27.373 22.683 37.326 1.00 36.04  ? 44 LYS B N   1 
ATOM 723  C CA  . LYS B 2 44 ? 25.962 22.310 37.220 1.00 41.00  ? 44 LYS B CA  1 
ATOM 724  C C   . LYS B 2 44 ? 25.643 21.143 38.171 1.00 44.00  ? 44 LYS B C   1 
ATOM 725  O O   . LYS B 2 44 ? 26.487 20.274 38.393 1.00 47.27  ? 44 LYS B O   1 
ATOM 726  C CB  . LYS B 2 44 ? 25.726 21.952 35.757 1.00 41.05  ? 44 LYS B CB  1 
ATOM 727  C CG  . LYS B 2 44 ? 24.372 21.451 35.281 1.00 50.13  ? 44 LYS B CG  1 
ATOM 728  C CD  . LYS B 2 44 ? 24.471 21.461 33.746 1.00 57.71  ? 44 LYS B CD  1 
ATOM 729  C CE  . LYS B 2 44 ? 23.767 20.348 32.960 1.00 63.75  ? 44 LYS B CE  1 
ATOM 730  N NZ  . LYS B 2 44 ? 22.330 20.519 32.908 1.00 63.59  ? 44 LYS B NZ  1 
ATOM 731  N N   . THR B 2 45 ? 24.470 21.102 38.785 1.00 41.66  ? 45 THR B N   1 
ATOM 732  C CA  . THR B 2 45 ? 24.069 20.008 39.655 1.00 39.63  ? 45 THR B CA  1 
ATOM 733  C C   . THR B 2 45 ? 22.796 19.533 39.025 1.00 38.86  ? 45 THR B C   1 
ATOM 734  O O   . THR B 2 45 ? 21.915 20.350 38.707 1.00 41.12  ? 45 THR B O   1 
ATOM 735  C CB  . THR B 2 45 ? 23.778 20.492 41.113 1.00 41.75  ? 45 THR B CB  1 
ATOM 736  O OG1 . THR B 2 45 ? 24.947 21.193 41.582 1.00 45.28  ? 45 THR B OG1 1 
ATOM 737  C CG2 . THR B 2 45 ? 23.444 19.341 42.060 1.00 35.89  ? 45 THR B CG2 1 
ATOM 738  N N   . ILE B 2 46 ? 22.665 18.260 38.750 1.00 36.98  ? 46 ILE B N   1 
ATOM 739  C CA  . ILE B 2 46 ? 21.462 17.876 38.060 1.00 44.24  ? 46 ILE B CA  1 
ATOM 740  C C   . ILE B 2 46 ? 20.559 17.261 39.095 1.00 51.90  ? 46 ILE B C   1 
ATOM 741  O O   . ILE B 2 46 ? 21.077 16.827 40.122 1.00 55.35  ? 46 ILE B O   1 
ATOM 742  C CB  . ILE B 2 46 ? 21.814 16.916 36.932 1.00 42.60  ? 46 ILE B CB  1 
ATOM 743  C CG1 . ILE B 2 46 ? 22.976 17.371 36.076 1.00 42.34  ? 46 ILE B CG1 1 
ATOM 744  C CG2 . ILE B 2 46 ? 20.636 16.924 36.003 1.00 45.62  ? 46 ILE B CG2 1 
ATOM 745  C CD1 . ILE B 2 46 ? 23.378 16.297 35.072 1.00 45.47  ? 46 ILE B CD1 1 
ATOM 746  N N   . TYR B 2 47 ? 19.240 17.312 38.894 1.00 60.47  ? 47 TYR B N   1 
ATOM 747  C CA  . TYR B 2 47 ? 18.228 16.761 39.819 1.00 62.45  ? 47 TYR B CA  1 
ATOM 748  C C   . TYR B 2 47 ? 17.333 15.789 39.002 1.00 66.39  ? 47 TYR B C   1 
ATOM 749  O O   . TYR B 2 47 ? 17.504 15.658 37.780 1.00 64.53  ? 47 TYR B O   1 
ATOM 750  C CB  . TYR B 2 47 ? 17.358 17.922 40.438 1.00 56.01  ? 47 TYR B CB  1 
ATOM 751  C CG  . TYR B 2 47 ? 18.138 19.015 41.179 1.00 54.76  ? 47 TYR B CG  1 
ATOM 752  C CD1 . TYR B 2 47 ? 18.723 20.031 40.451 1.00 59.12  ? 47 TYR B CD1 1 
ATOM 753  C CD2 . TYR B 2 47 ? 18.330 18.988 42.552 1.00 52.54  ? 47 TYR B CD2 1 
ATOM 754  C CE1 . TYR B 2 47 ? 19.512 20.988 41.068 1.00 60.33  ? 47 TYR B CE1 1 
ATOM 755  C CE2 . TYR B 2 47 ? 19.118 19.946 43.185 1.00 56.77  ? 47 TYR B CE2 1 
ATOM 756  C CZ  . TYR B 2 47 ? 19.717 20.958 42.434 1.00 60.27  ? 47 TYR B CZ  1 
ATOM 757  O OH  . TYR B 2 47 ? 20.585 21.918 42.987 1.00 63.74  ? 47 TYR B OH  1 
ATOM 758  N N   . GLU B 2 48 ? 16.394 15.061 39.614 1.00 68.11  ? 48 GLU B N   1 
ATOM 759  C CA  . GLU B 2 48 ? 15.493 14.147 38.904 1.00 71.22  ? 48 GLU B CA  1 
ATOM 760  C C   . GLU B 2 48 ? 14.558 14.767 37.830 1.00 77.88  ? 48 GLU B C   1 
ATOM 761  O O   . GLU B 2 48 ? 13.327 14.787 37.977 1.00 81.94  ? 48 GLU B O   1 
ATOM 762  C CB  . GLU B 2 48 ? 14.642 13.434 39.940 1.00 68.43  ? 48 GLU B CB  1 
ATOM 763  C CG  . GLU B 2 48 ? 13.824 12.242 39.434 1.00 70.80  ? 48 GLU B CG  1 
ATOM 764  C CD  . GLU B 2 48 ? 12.467 12.067 40.141 1.00 73.73  ? 48 GLU B CD  1 
ATOM 765  O OE1 . GLU B 2 48 ? 12.415 11.550 41.271 1.00 72.04  ? 48 GLU B OE1 1 
ATOM 766  O OE2 . GLU B 2 48 ? 11.448 12.451 39.547 1.00 72.29  ? 48 GLU B OE2 1 
ATOM 767  N N   . ASN B 2 49 ? 15.037 15.349 36.732 1.00 81.02  ? 49 ASN B N   1 
ATOM 768  C CA  . ASN B 2 49 ? 14.200 15.777 35.616 1.00 82.19  ? 49 ASN B CA  1 
ATOM 769  C C   . ASN B 2 49 ? 15.165 16.036 34.476 1.00 87.20  ? 49 ASN B C   1 
ATOM 770  O O   . ASN B 2 49 ? 16.245 16.622 34.655 1.00 80.30  ? 49 ASN B O   1 
ATOM 771  C CB  . ASN B 2 49 ? 13.366 17.056 35.922 1.00 80.19  ? 49 ASN B CB  1 
ATOM 772  C CG  . ASN B 2 49 ? 14.045 18.284 36.537 1.00 82.69  ? 49 ASN B CG  1 
ATOM 773  O OD1 . ASN B 2 49 ? 15.267 18.356 36.682 1.00 86.73  ? 49 ASN B OD1 1 
ATOM 774  N ND2 . ASN B 2 49 ? 13.298 19.310 36.959 1.00 78.64  ? 49 ASN B ND2 1 
ATOM 775  N N   . GLU B 2 50 ? 14.780 15.429 33.342 1.00 97.69  ? 50 GLU B N   1 
ATOM 776  C CA  . GLU B 2 50 ? 15.547 15.391 32.097 1.00 104.60 ? 50 GLU B CA  1 
ATOM 777  C C   . GLU B 2 50 ? 14.619 15.715 30.914 1.00 105.64 ? 50 GLU B C   1 
ATOM 778  O O   . GLU B 2 50 ? 13.488 15.211 30.891 1.00 106.59 ? 50 GLU B O   1 
ATOM 779  C CB  . GLU B 2 50 ? 16.163 13.979 31.954 1.00 108.66 ? 50 GLU B CB  1 
ATOM 780  C CG  . GLU B 2 50 ? 16.931 13.615 30.669 1.00 113.19 ? 50 GLU B CG  1 
ATOM 781  C CD  . GLU B 2 50 ? 16.109 13.323 29.404 1.00 114.00 ? 50 GLU B CD  1 
ATOM 782  O OE1 . GLU B 2 50 ? 15.184 12.504 29.458 1.00 115.09 ? 50 GLU B OE1 1 
ATOM 783  O OE2 . GLU B 2 50 ? 16.400 13.936 28.370 1.00 111.91 ? 50 GLU B OE2 1 
ATOM 784  O OXT . GLU B 2 50 ? 15.030 16.481 30.034 1.00 104.97 ? 50 GLU B OXT 1 
ATOM 785  N N   . ARG C 1 1  ? 36.513 53.522 41.985 1.00 109.52 ? 2  ARG C N   1 
ATOM 786  C CA  . ARG C 1 1  ? 37.609 54.228 41.341 1.00 104.75 ? 2  ARG C CA  1 
ATOM 787  C C   . ARG C 1 1  ? 37.542 53.470 40.003 1.00 101.75 ? 2  ARG C C   1 
ATOM 788  O O   . ARG C 1 1  ? 36.398 53.444 39.527 1.00 101.12 ? 2  ARG C O   1 
ATOM 789  C CB  . ARG C 1 1  ? 38.854 54.018 42.264 1.00 107.17 ? 2  ARG C CB  1 
ATOM 790  C CG  . ARG C 1 1  ? 38.511 54.605 43.675 1.00 108.06 ? 2  ARG C CG  1 
ATOM 791  C CD  . ARG C 1 1  ? 39.465 54.391 44.845 1.00 109.88 ? 2  ARG C CD  1 
ATOM 792  N NE  . ARG C 1 1  ? 40.606 55.315 44.923 1.00 114.10 ? 2  ARG C NE  1 
ATOM 793  C CZ  . ARG C 1 1  ? 41.630 55.103 45.779 1.00 115.62 ? 2  ARG C CZ  1 
ATOM 794  N NH1 . ARG C 1 1  ? 41.629 54.059 46.626 1.00 116.82 ? 2  ARG C NH1 1 
ATOM 795  N NH2 . ARG C 1 1  ? 42.661 55.958 45.826 1.00 113.23 ? 2  ARG C NH2 1 
ATOM 796  N N   . GLU C 1 2  ? 38.541 52.754 39.442 1.00 95.91  ? 3  GLU C N   1 
ATOM 797  C CA  . GLU C 1 2  ? 38.368 52.205 38.085 1.00 88.10  ? 3  GLU C CA  1 
ATOM 798  C C   . GLU C 1 2  ? 37.727 50.835 37.923 1.00 78.03  ? 3  GLU C C   1 
ATOM 799  O O   . GLU C 1 2  ? 37.638 50.056 38.879 1.00 77.63  ? 3  GLU C O   1 
ATOM 800  C CB  . GLU C 1 2  ? 39.703 52.138 37.327 1.00 90.89  ? 3  GLU C CB  1 
ATOM 801  C CG  . GLU C 1 2  ? 40.160 53.524 36.906 1.00 94.85  ? 3  GLU C CG  1 
ATOM 802  C CD  . GLU C 1 2  ? 40.513 53.643 35.428 1.00 96.67  ? 3  GLU C CD  1 
ATOM 803  O OE1 . GLU C 1 2  ? 39.626 53.870 34.593 1.00 96.39  ? 3  GLU C OE1 1 
ATOM 804  O OE2 . GLU C 1 2  ? 41.697 53.507 35.119 1.00 98.80  ? 3  GLU C OE2 1 
ATOM 805  N N   . ILE C 1 3  ? 37.271 50.666 36.676 1.00 62.91  ? 4  ILE C N   1 
ATOM 806  C CA  . ILE C 1 3  ? 36.641 49.527 36.005 1.00 49.34  ? 4  ILE C CA  1 
ATOM 807  C C   . ILE C 1 3  ? 36.679 49.975 34.545 1.00 49.13  ? 4  ILE C C   1 
ATOM 808  O O   . ILE C 1 3  ? 36.624 51.181 34.322 1.00 54.31  ? 4  ILE C O   1 
ATOM 809  C CB  . ILE C 1 3  ? 35.141 49.316 36.413 1.00 40.26  ? 4  ILE C CB  1 
ATOM 810  C CG1 . ILE C 1 3  ? 35.006 48.889 37.855 1.00 32.65  ? 4  ILE C CG1 1 
ATOM 811  C CG2 . ILE C 1 3  ? 34.512 48.297 35.464 1.00 38.16  ? 4  ILE C CG2 1 
ATOM 812  C CD1 . ILE C 1 3  ? 33.660 48.311 38.269 1.00 38.63  ? 4  ILE C CD1 1 
ATOM 813  N N   . LYS C 1 4  ? 36.801 49.138 33.515 1.00 47.26  ? 5  LYS C N   1 
ATOM 814  C CA  . LYS C 1 4  ? 36.657 49.689 32.187 1.00 52.77  ? 5  LYS C CA  1 
ATOM 815  C C   . LYS C 1 4  ? 35.440 49.225 31.426 1.00 55.89  ? 5  LYS C C   1 
ATOM 816  O O   . LYS C 1 4  ? 34.970 49.957 30.547 1.00 59.84  ? 5  LYS C O   1 
ATOM 817  C CB  . LYS C 1 4  ? 37.882 49.420 31.349 1.00 59.47  ? 5  LYS C CB  1 
ATOM 818  C CG  . LYS C 1 4  ? 38.760 50.590 31.762 1.00 70.61  ? 5  LYS C CG  1 
ATOM 819  C CD  . LYS C 1 4  ? 39.950 50.950 30.862 1.00 78.84  ? 5  LYS C CD  1 
ATOM 820  C CE  . LYS C 1 4  ? 40.695 52.236 31.295 1.00 81.42  ? 5  LYS C CE  1 
ATOM 821  N NZ  . LYS C 1 4  ? 40.906 52.153 32.735 1.00 84.88  ? 5  LYS C NZ  1 
ATOM 822  N N   . GLY C 1 5  ? 34.830 48.076 31.731 1.00 57.31  ? 6  GLY C N   1 
ATOM 823  C CA  . GLY C 1 5  ? 33.669 47.633 30.967 1.00 55.08  ? 6  GLY C CA  1 
ATOM 824  C C   . GLY C 1 5  ? 33.067 46.344 31.511 1.00 58.46  ? 6  GLY C C   1 
ATOM 825  O O   . GLY C 1 5  ? 33.395 45.895 32.624 1.00 55.55  ? 6  GLY C O   1 
ATOM 826  N N   . TYR C 1 6  ? 32.147 45.775 30.739 1.00 60.51  ? 7  TYR C N   1 
ATOM 827  C CA  . TYR C 1 6  ? 31.504 44.510 31.068 1.00 59.46  ? 7  TYR C CA  1 
ATOM 828  C C   . TYR C 1 6  ? 31.483 43.687 29.791 1.00 57.51  ? 7  TYR C C   1 
ATOM 829  O O   . TYR C 1 6  ? 31.775 44.217 28.702 1.00 54.74  ? 7  TYR C O   1 
ATOM 830  C CB  . TYR C 1 6  ? 30.021 44.663 31.532 1.00 59.13  ? 7  TYR C CB  1 
ATOM 831  C CG  . TYR C 1 6  ? 29.865 45.683 32.624 1.00 61.35  ? 7  TYR C CG  1 
ATOM 832  C CD1 . TYR C 1 6  ? 30.318 45.404 33.891 1.00 60.88  ? 7  TYR C CD1 1 
ATOM 833  C CD2 . TYR C 1 6  ? 29.328 46.924 32.324 1.00 64.85  ? 7  TYR C CD2 1 
ATOM 834  C CE1 . TYR C 1 6  ? 30.238 46.389 34.857 1.00 66.09  ? 7  TYR C CE1 1 
ATOM 835  C CE2 . TYR C 1 6  ? 29.247 47.918 33.286 1.00 65.47  ? 7  TYR C CE2 1 
ATOM 836  C CZ  . TYR C 1 6  ? 29.707 47.631 34.545 1.00 66.85  ? 7  TYR C CZ  1 
ATOM 837  O OH  . TYR C 1 6  ? 29.628 48.588 35.523 1.00 66.68  ? 7  TYR C OH  1 
ATOM 838  N N   . GLU C 1 7  ? 31.121 42.413 29.953 1.00 56.18  ? 8  GLU C N   1 
ATOM 839  C CA  . GLU C 1 7  ? 30.911 41.489 28.870 1.00 50.40  ? 8  GLU C CA  1 
ATOM 840  C C   . GLU C 1 7  ? 29.742 40.639 29.264 1.00 51.72  ? 8  GLU C C   1 
ATOM 841  O O   . GLU C 1 7  ? 29.513 40.398 30.461 1.00 50.17  ? 8  GLU C O   1 
ATOM 842  C CB  . GLU C 1 7  ? 32.096 40.614 28.673 1.00 50.27  ? 8  GLU C CB  1 
ATOM 843  C CG  . GLU C 1 7  ? 32.443 40.752 27.204 1.00 51.14  ? 8  GLU C CG  1 
ATOM 844  C CD  . GLU C 1 7  ? 33.807 40.198 26.800 1.00 49.02  ? 8  GLU C CD  1 
ATOM 845  O OE1 . GLU C 1 7  ? 34.822 40.794 27.202 1.00 47.25  ? 8  GLU C OE1 1 
ATOM 846  O OE2 . GLU C 1 7  ? 33.827 39.194 26.074 1.00 39.87  ? 8  GLU C OE2 1 
ATOM 847  N N   . TYR C 1 8  ? 28.993 40.191 28.269 1.00 57.30  ? 9  TYR C N   1 
ATOM 848  C CA  . TYR C 1 8  ? 27.787 39.418 28.504 1.00 56.40  ? 9  TYR C CA  1 
ATOM 849  C C   . TYR C 1 8  ? 27.739 38.209 27.588 1.00 49.99  ? 9  TYR C C   1 
ATOM 850  O O   . TYR C 1 8  ? 27.799 38.328 26.359 1.00 39.71  ? 9  TYR C O   1 
ATOM 851  C CB  . TYR C 1 8  ? 26.530 40.251 28.248 1.00 58.90  ? 9  TYR C CB  1 
ATOM 852  C CG  . TYR C 1 8  ? 26.267 41.407 29.204 1.00 64.61  ? 9  TYR C CG  1 
ATOM 853  C CD1 . TYR C 1 8  ? 25.951 41.181 30.533 1.00 63.59  ? 9  TYR C CD1 1 
ATOM 854  C CD2 . TYR C 1 8  ? 26.337 42.702 28.717 1.00 67.53  ? 9  TYR C CD2 1 
ATOM 855  C CE1 . TYR C 1 8  ? 25.704 42.251 31.369 1.00 63.48  ? 9  TYR C CE1 1 
ATOM 856  C CE2 . TYR C 1 8  ? 26.090 43.774 29.550 1.00 66.78  ? 9  TYR C CE2 1 
ATOM 857  C CZ  . TYR C 1 8  ? 25.777 43.535 30.867 1.00 64.94  ? 9  TYR C CZ  1 
ATOM 858  O OH  . TYR C 1 8  ? 25.575 44.621 31.690 1.00 66.61  ? 9  TYR C OH  1 
ATOM 859  N N   . GLN C 1 9  ? 27.718 37.037 28.200 1.00 47.03  ? 10 GLN C N   1 
ATOM 860  C CA  . GLN C 1 9  ? 27.557 35.788 27.476 1.00 45.37  ? 10 GLN C CA  1 
ATOM 861  C C   . GLN C 1 9  ? 26.138 35.337 27.721 1.00 40.41  ? 10 GLN C C   1 
ATOM 862  O O   . GLN C 1 9  ? 25.753 35.291 28.880 1.00 37.67  ? 10 GLN C O   1 
ATOM 863  C CB  . GLN C 1 9  ? 28.590 34.831 28.017 1.00 45.81  ? 10 GLN C CB  1 
ATOM 864  C CG  . GLN C 1 9  ? 29.937 35.366 27.578 1.00 38.45  ? 10 GLN C CG  1 
ATOM 865  C CD  . GLN C 1 9  ? 31.136 34.679 28.147 1.00 42.91  ? 10 GLN C CD  1 
ATOM 866  O OE1 . GLN C 1 9  ? 31.087 33.807 29.006 1.00 43.43  ? 10 GLN C OE1 1 
ATOM 867  N NE2 . GLN C 1 9  ? 32.295 35.107 27.690 1.00 48.91  ? 10 GLN C NE2 1 
ATOM 868  N N   . LEU C 1 10 ? 25.344 35.085 26.692 1.00 46.06  ? 11 LEU C N   1 
ATOM 869  C CA  . LEU C 1 10 ? 23.909 34.827 26.828 1.00 55.22  ? 11 LEU C CA  1 
ATOM 870  C C   . LEU C 1 10 ? 23.467 33.668 25.932 1.00 58.10  ? 11 LEU C C   1 
ATOM 871  O O   . LEU C 1 10 ? 24.022 33.502 24.835 1.00 60.41  ? 11 LEU C O   1 
ATOM 872  C CB  . LEU C 1 10 ? 23.047 35.997 26.354 1.00 62.70  ? 11 LEU C CB  1 
ATOM 873  C CG  . LEU C 1 10 ? 22.815 37.430 26.832 1.00 65.98  ? 11 LEU C CG  1 
ATOM 874  C CD1 . LEU C 1 10 ? 24.067 38.171 27.206 1.00 66.91  ? 11 LEU C CD1 1 
ATOM 875  C CD2 . LEU C 1 10 ? 22.138 38.130 25.659 1.00 65.11  ? 11 LEU C CD2 1 
ATOM 876  N N   . TYR C 1 11 ? 22.459 32.888 26.322 1.00 56.54  ? 12 TYR C N   1 
ATOM 877  C CA  . TYR C 1 11 ? 21.914 31.866 25.451 1.00 54.46  ? 12 TYR C CA  1 
ATOM 878  C C   . TYR C 1 11 ? 20.575 32.432 25.048 1.00 55.60  ? 12 TYR C C   1 
ATOM 879  O O   . TYR C 1 11 ? 19.663 32.506 25.896 1.00 55.76  ? 12 TYR C O   1 
ATOM 880  C CB  . TYR C 1 11 ? 21.664 30.544 26.159 1.00 57.27  ? 12 TYR C CB  1 
ATOM 881  C CG  . TYR C 1 11 ? 22.872 29.656 26.408 1.00 60.19  ? 12 TYR C CG  1 
ATOM 882  C CD1 . TYR C 1 11 ? 23.368 28.800 25.435 1.00 58.02  ? 12 TYR C CD1 1 
ATOM 883  C CD2 . TYR C 1 11 ? 23.451 29.709 27.649 1.00 60.51  ? 12 TYR C CD2 1 
ATOM 884  C CE1 . TYR C 1 11 ? 24.452 28.005 25.690 1.00 57.92  ? 12 TYR C CE1 1 
ATOM 885  C CE2 . TYR C 1 11 ? 24.537 28.931 27.918 1.00 61.06  ? 12 TYR C CE2 1 
ATOM 886  C CZ  . TYR C 1 11 ? 25.007 28.093 26.944 1.00 62.23  ? 12 TYR C CZ  1 
ATOM 887  O OH  . TYR C 1 11 ? 26.108 27.350 27.263 1.00 71.15  ? 12 TYR C OH  1 
ATOM 888  N N   . VAL C 1 12 ? 20.502 32.896 23.796 1.00 54.53  ? 13 VAL C N   1 
ATOM 889  C CA  . VAL C 1 12 ? 19.315 33.546 23.290 1.00 52.94  ? 13 VAL C CA  1 
ATOM 890  C C   . VAL C 1 12 ? 18.543 32.686 22.334 1.00 52.43  ? 13 VAL C C   1 
ATOM 891  O O   . VAL C 1 12 ? 19.055 32.259 21.296 1.00 49.95  ? 13 VAL C O   1 
ATOM 892  C CB  . VAL C 1 12 ? 19.634 34.864 22.534 1.00 54.74  ? 13 VAL C CB  1 
ATOM 893  C CG1 . VAL C 1 12 ? 18.312 35.614 22.537 1.00 58.57  ? 13 VAL C CG1 1 
ATOM 894  C CG2 . VAL C 1 12 ? 20.733 35.733 23.140 1.00 51.48  ? 13 VAL C CG2 1 
ATOM 895  N N   . TYR C 1 13 ? 17.327 32.397 22.725 1.00 60.46  ? 14 TYR C N   1 
ATOM 896  C CA  . TYR C 1 13 ? 16.371 31.741 21.858 1.00 73.32  ? 14 TYR C CA  1 
ATOM 897  C C   . TYR C 1 13 ? 15.851 32.754 20.848 1.00 73.70  ? 14 TYR C C   1 
ATOM 898  O O   . TYR C 1 13 ? 15.321 33.805 21.235 1.00 72.33  ? 14 TYR C O   1 
ATOM 899  C CB  . TYR C 1 13 ? 15.156 31.154 22.652 1.00 82.01  ? 14 TYR C CB  1 
ATOM 900  C CG  . TYR C 1 13 ? 15.262 29.703 23.127 1.00 85.66  ? 14 TYR C CG  1 
ATOM 901  C CD1 . TYR C 1 13 ? 15.305 28.682 22.192 1.00 88.91  ? 14 TYR C CD1 1 
ATOM 902  C CD2 . TYR C 1 13 ? 15.340 29.406 24.474 1.00 87.40  ? 14 TYR C CD2 1 
ATOM 903  C CE1 . TYR C 1 13 ? 15.437 27.365 22.581 1.00 92.71  ? 14 TYR C CE1 1 
ATOM 904  C CE2 . TYR C 1 13 ? 15.471 28.089 24.877 1.00 92.46  ? 14 TYR C CE2 1 
ATOM 905  C CZ  . TYR C 1 13 ? 15.525 27.076 23.928 1.00 94.70  ? 14 TYR C CZ  1 
ATOM 906  O OH  . TYR C 1 13 ? 15.717 25.760 24.318 1.00 97.61  ? 14 TYR C OH  1 
ATOM 907  N N   . ALA C 1 14 ? 16.013 32.409 19.574 1.00 75.12  ? 15 ALA C N   1 
ATOM 908  C CA  . ALA C 1 14 ? 15.599 33.209 18.433 1.00 77.20  ? 15 ALA C CA  1 
ATOM 909  C C   . ALA C 1 14 ? 15.097 32.256 17.378 1.00 78.70  ? 15 ALA C C   1 
ATOM 910  O O   . ALA C 1 14 ? 15.788 31.287 17.085 1.00 81.44  ? 15 ALA C O   1 
ATOM 911  C CB  . ALA C 1 14 ? 16.739 33.954 17.778 1.00 74.65  ? 15 ALA C CB  1 
ATOM 912  N N   . SER C 1 15 ? 13.897 32.476 16.841 1.00 82.51  ? 16 SER C N   1 
ATOM 913  C CA  . SER C 1 15 ? 13.251 31.637 15.827 1.00 83.11  ? 16 SER C CA  1 
ATOM 914  C C   . SER C 1 15 ? 13.270 30.169 16.225 1.00 83.21  ? 16 SER C C   1 
ATOM 915  O O   . SER C 1 15 ? 13.464 29.254 15.416 1.00 83.05  ? 16 SER C O   1 
ATOM 916  C CB  . SER C 1 15 ? 13.927 31.822 14.454 1.00 84.07  ? 16 SER C CB  1 
ATOM 917  O OG  . SER C 1 15 ? 13.716 33.141 13.948 1.00 83.91  ? 16 SER C OG  1 
ATOM 918  N N   . ASP C 1 16 ? 13.030 29.992 17.535 1.00 77.88  ? 17 ASP C N   1 
ATOM 919  C CA  . ASP C 1 16 ? 12.982 28.700 18.196 1.00 74.10  ? 17 ASP C CA  1 
ATOM 920  C C   . ASP C 1 16 ? 14.291 27.909 18.181 1.00 70.52  ? 17 ASP C C   1 
ATOM 921  O O   . ASP C 1 16 ? 14.299 26.718 18.500 1.00 76.08  ? 17 ASP C O   1 
ATOM 922  C CB  . ASP C 1 16 ? 11.836 27.871 17.582 1.00 75.03  ? 17 ASP C CB  1 
ATOM 923  C CG  . ASP C 1 16 ? 10.476 28.501 17.882 1.00 79.07  ? 17 ASP C CG  1 
ATOM 924  O OD1 . ASP C 1 16 ? 9.919  28.196 18.942 1.00 82.05  ? 17 ASP C OD1 1 
ATOM 925  O OD2 . ASP C 1 16 ? 9.986  29.301 17.074 1.00 75.01  ? 17 ASP C OD2 1 
ATOM 926  N N   . LYS C 1 17 ? 15.426 28.564 17.922 1.00 61.40  ? 18 LYS C N   1 
ATOM 927  C CA  . LYS C 1 17 ? 16.721 27.914 17.997 1.00 51.50  ? 18 LYS C CA  1 
ATOM 928  C C   . LYS C 1 17 ? 17.413 28.532 19.174 1.00 49.29  ? 18 LYS C C   1 
ATOM 929  O O   . LYS C 1 17 ? 16.917 29.483 19.789 1.00 46.55  ? 18 LYS C O   1 
ATOM 930  C CB  . LYS C 1 17 ? 17.577 28.167 16.796 1.00 51.03  ? 18 LYS C CB  1 
ATOM 931  C CG  . LYS C 1 17 ? 16.874 27.562 15.624 1.00 56.62  ? 18 LYS C CG  1 
ATOM 932  C CD  . LYS C 1 17 ? 17.373 28.075 14.290 1.00 57.74  ? 18 LYS C CD  1 
ATOM 933  C CE  . LYS C 1 17 ? 16.354 27.661 13.215 1.00 58.03  ? 18 LYS C CE  1 
ATOM 934  N NZ  . LYS C 1 17 ? 15.103 28.389 13.369 1.00 56.97  ? 18 LYS C NZ  1 
ATOM 935  N N   . LEU C 1 18 ? 18.564 27.983 19.480 1.00 48.49  ? 19 LEU C N   1 
ATOM 936  C CA  . LEU C 1 18 ? 19.374 28.409 20.592 1.00 48.34  ? 19 LEU C CA  1 
ATOM 937  C C   . LEU C 1 18 ? 20.628 29.066 20.031 1.00 49.54  ? 19 LEU C C   1 
ATOM 938  O O   . LEU C 1 18 ? 21.300 28.450 19.188 1.00 48.76  ? 19 LEU C O   1 
ATOM 939  C CB  . LEU C 1 18 ? 19.718 27.167 21.432 1.00 40.89  ? 19 LEU C CB  1 
ATOM 940  C CG  . LEU C 1 18 ? 19.951 27.272 22.911 1.00 31.81  ? 19 LEU C CG  1 
ATOM 941  C CD1 . LEU C 1 18 ? 21.057 28.198 23.239 1.00 29.66  ? 19 LEU C CD1 1 
ATOM 942  C CD2 . LEU C 1 18 ? 18.725 27.836 23.521 1.00 31.06  ? 19 LEU C CD2 1 
ATOM 943  N N   . PHE C 1 19 ? 20.963 30.266 20.518 1.00 50.60  ? 20 PHE C N   1 
ATOM 944  C CA  . PHE C 1 19 ? 22.137 30.999 20.085 1.00 51.23  ? 20 PHE C CA  1 
ATOM 945  C C   . PHE C 1 19 ? 22.980 31.443 21.263 1.00 41.14  ? 20 PHE C C   1 
ATOM 946  O O   . PHE C 1 19 ? 22.488 31.650 22.368 1.00 35.43  ? 20 PHE C O   1 
ATOM 947  C CB  . PHE C 1 19 ? 21.691 32.227 19.277 1.00 56.15  ? 20 PHE C CB  1 
ATOM 948  C CG  . PHE C 1 19 ? 21.141 31.876 17.898 1.00 58.58  ? 20 PHE C CG  1 
ATOM 949  C CD1 . PHE C 1 19 ? 22.039 31.555 16.886 1.00 58.39  ? 20 PHE C CD1 1 
ATOM 950  C CD2 . PHE C 1 19 ? 19.773 31.838 17.675 1.00 58.83  ? 20 PHE C CD2 1 
ATOM 951  C CE1 . PHE C 1 19 ? 21.560 31.163 15.655 1.00 59.33  ? 20 PHE C CE1 1 
ATOM 952  C CE2 . PHE C 1 19 ? 19.311 31.441 16.432 1.00 60.83  ? 20 PHE C CE2 1 
ATOM 953  C CZ  . PHE C 1 19 ? 20.200 31.110 15.427 1.00 59.87  ? 20 PHE C CZ  1 
ATOM 954  N N   . ARG C 1 20 ? 24.265 31.587 21.059 1.00 40.15  ? 21 ARG C N   1 
ATOM 955  C CA  . ARG C 1 20 ? 25.148 32.075 22.101 1.00 45.25  ? 21 ARG C CA  1 
ATOM 956  C C   . ARG C 1 20 ? 25.491 33.474 21.656 1.00 43.85  ? 21 ARG C C   1 
ATOM 957  O O   . ARG C 1 20 ? 25.838 33.666 20.470 1.00 43.49  ? 21 ARG C O   1 
ATOM 958  C CB  . ARG C 1 20 ? 26.444 31.241 22.212 1.00 43.02  ? 21 ARG C CB  1 
ATOM 959  C CG  . ARG C 1 20 ? 26.405 30.011 23.128 1.00 43.20  ? 21 ARG C CG  1 
ATOM 960  C CD  . ARG C 1 20 ? 26.606 30.322 24.596 1.00 39.26  ? 21 ARG C CD  1 
ATOM 961  N NE  . ARG C 1 20 ? 27.930 30.843 24.787 1.00 48.91  ? 21 ARG C NE  1 
ATOM 962  C CZ  . ARG C 1 20 ? 28.170 32.138 25.031 1.00 51.61  ? 21 ARG C CZ  1 
ATOM 963  N NH1 . ARG C 1 20 ? 27.210 33.067 25.126 1.00 54.76  ? 21 ARG C NH1 1 
ATOM 964  N NH2 . ARG C 1 20 ? 29.435 32.494 25.177 1.00 49.18  ? 21 ARG C NH2 1 
ATOM 965  N N   . ALA C 1 21 ? 25.353 34.454 22.547 1.00 37.78  ? 22 ALA C N   1 
ATOM 966  C CA  . ALA C 1 21 ? 25.583 35.816 22.131 1.00 32.34  ? 22 ALA C CA  1 
ATOM 967  C C   . ALA C 1 21 ? 26.561 36.436 23.068 1.00 29.38  ? 22 ALA C C   1 
ATOM 968  O O   . ALA C 1 21 ? 26.460 36.192 24.273 1.00 31.40  ? 22 ALA C O   1 
ATOM 969  C CB  . ALA C 1 21 ? 24.287 36.591 22.174 1.00 36.04  ? 22 ALA C CB  1 
ATOM 970  N N   . ASP C 1 22 ? 27.530 37.137 22.515 1.00 28.07  ? 23 ASP C N   1 
ATOM 971  C CA  . ASP C 1 22 ? 28.503 37.775 23.343 1.00 39.59  ? 23 ASP C CA  1 
ATOM 972  C C   . ASP C 1 22 ? 28.382 39.242 23.063 1.00 44.45  ? 23 ASP C C   1 
ATOM 973  O O   . ASP C 1 22 ? 28.372 39.605 21.870 1.00 44.06  ? 23 ASP C O   1 
ATOM 974  C CB  . ASP C 1 22 ? 29.916 37.301 23.009 1.00 47.69  ? 23 ASP C CB  1 
ATOM 975  C CG  . ASP C 1 22 ? 30.310 35.896 23.481 1.00 52.99  ? 23 ASP C CG  1 
ATOM 976  O OD1 . ASP C 1 22 ? 29.616 35.338 24.334 1.00 55.38  ? 23 ASP C OD1 1 
ATOM 977  O OD2 . ASP C 1 22 ? 31.310 35.352 22.994 1.00 50.48  ? 23 ASP C OD2 1 
ATOM 978  N N   . ILE C 1 23 ? 28.218 40.029 24.148 1.00 47.30  ? 24 ILE C N   1 
ATOM 979  C CA  . ILE C 1 23 ? 28.013 41.486 24.142 1.00 44.44  ? 24 ILE C CA  1 
ATOM 980  C C   . ILE C 1 23 ? 29.028 42.210 25.029 1.00 44.84  ? 24 ILE C C   1 
ATOM 981  O O   . ILE C 1 23 ? 29.520 41.719 26.058 1.00 38.18  ? 24 ILE C O   1 
ATOM 982  C CB  . ILE C 1 23 ? 26.562 41.845 24.626 1.00 38.04  ? 24 ILE C CB  1 
ATOM 983  C CG1 . ILE C 1 23 ? 25.505 41.070 23.816 1.00 38.67  ? 24 ILE C CG1 1 
ATOM 984  C CG2 . ILE C 1 23 ? 26.317 43.326 24.409 1.00 33.39  ? 24 ILE C CG2 1 
ATOM 985  C CD1 . ILE C 1 23 ? 24.002 41.248 24.114 1.00 35.08  ? 24 ILE C CD1 1 
ATOM 986  N N   . SER C 1 24 ? 29.443 43.369 24.573 1.00 50.22  ? 25 SER C N   1 
ATOM 987  C CA  . SER C 1 24 ? 30.298 44.208 25.381 1.00 56.28  ? 25 SER C CA  1 
ATOM 988  C C   . SER C 1 24 ? 29.453 45.333 25.944 1.00 53.78  ? 25 SER C C   1 
ATOM 989  O O   . SER C 1 24 ? 28.312 45.526 25.520 1.00 51.68  ? 25 SER C O   1 
ATOM 990  C CB  . SER C 1 24 ? 31.403 44.787 24.512 1.00 61.58  ? 25 SER C CB  1 
ATOM 991  O OG  . SER C 1 24 ? 30.794 45.373 23.354 1.00 67.10  ? 25 SER C OG  1 
ATOM 992  N N   . GLU C 1 25 ? 30.012 46.104 26.861 1.00 53.85  ? 26 GLU C N   1 
ATOM 993  C CA  . GLU C 1 25 ? 29.363 47.306 27.312 1.00 52.53  ? 26 GLU C CA  1 
ATOM 994  C C   . GLU C 1 25 ? 30.398 48.273 27.903 1.00 49.41  ? 26 GLU C C   1 
ATOM 995  O O   . GLU C 1 25 ? 31.257 47.871 28.719 1.00 39.36  ? 26 GLU C O   1 
ATOM 996  C CB  . GLU C 1 25 ? 28.309 46.919 28.329 1.00 53.81  ? 26 GLU C CB  1 
ATOM 997  C CG  . GLU C 1 25 ? 27.243 47.970 28.455 1.00 52.81  ? 26 GLU C CG  1 
ATOM 998  C CD  . GLU C 1 25 ? 26.539 47.810 29.773 1.00 54.98  ? 26 GLU C CD  1 
ATOM 999  O OE1 . GLU C 1 25 ? 27.064 48.327 30.767 1.00 54.00  ? 26 GLU C OE1 1 
ATOM 1000 O OE2 . GLU C 1 25 ? 25.487 47.169 29.793 1.00 50.39  ? 26 GLU C OE2 1 
ATOM 1001 N N   . ASP C 1 26 ? 30.370 49.530 27.423 1.00 45.17  ? 27 ASP C N   1 
ATOM 1002 C CA  . ASP C 1 26 ? 31.256 50.509 27.999 1.00 47.17  ? 27 ASP C CA  1 
ATOM 1003 C C   . ASP C 1 26 ? 30.824 50.932 29.375 1.00 45.22  ? 27 ASP C C   1 
ATOM 1004 O O   . ASP C 1 26 ? 29.644 51.158 29.583 1.00 43.51  ? 27 ASP C O   1 
ATOM 1005 C CB  . ASP C 1 26 ? 31.344 51.801 27.272 1.00 44.49  ? 27 ASP C CB  1 
ATOM 1006 C CG  . ASP C 1 26 ? 32.741 52.360 27.526 1.00 47.06  ? 27 ASP C CG  1 
ATOM 1007 O OD1 . ASP C 1 26 ? 33.092 52.778 28.636 1.00 39.11  ? 27 ASP C OD1 1 
ATOM 1008 O OD2 . ASP C 1 26 ? 33.515 52.338 26.573 1.00 54.84  ? 27 ASP C OD2 1 
ATOM 1009 N N   . TYR C 1 27 ? 31.782 51.117 30.283 1.00 47.39  ? 28 TYR C N   1 
ATOM 1010 C CA  . TYR C 1 27 ? 31.477 51.585 31.616 1.00 53.00  ? 28 TYR C CA  1 
ATOM 1011 C C   . TYR C 1 27 ? 31.023 53.046 31.682 1.00 62.47  ? 28 TYR C C   1 
ATOM 1012 O O   . TYR C 1 27 ? 30.100 53.345 32.430 1.00 69.60  ? 28 TYR C O   1 
ATOM 1013 C CB  . TYR C 1 27 ? 32.678 51.428 32.505 1.00 47.37  ? 28 TYR C CB  1 
ATOM 1014 C CG  . TYR C 1 27 ? 32.318 51.676 33.961 1.00 48.31  ? 28 TYR C CG  1 
ATOM 1015 C CD1 . TYR C 1 27 ? 31.459 50.827 34.634 1.00 48.43  ? 28 TYR C CD1 1 
ATOM 1016 C CD2 . TYR C 1 27 ? 32.898 52.734 34.617 1.00 45.90  ? 28 TYR C CD2 1 
ATOM 1017 C CE1 . TYR C 1 27 ? 31.223 51.035 35.974 1.00 47.59  ? 28 TYR C CE1 1 
ATOM 1018 C CE2 . TYR C 1 27 ? 32.661 52.936 35.950 1.00 43.07  ? 28 TYR C CE2 1 
ATOM 1019 C CZ  . TYR C 1 27 ? 31.833 52.082 36.620 1.00 46.05  ? 28 TYR C CZ  1 
ATOM 1020 O OH  . TYR C 1 27 ? 31.673 52.241 37.980 1.00 49.85  ? 28 TYR C OH  1 
ATOM 1021 N N   . LYS C 1 28 ? 31.666 54.000 30.999 1.00 67.69  ? 29 LYS C N   1 
ATOM 1022 C CA  . LYS C 1 28 ? 31.182 55.392 31.037 1.00 69.13  ? 29 LYS C CA  1 
ATOM 1023 C C   . LYS C 1 28 ? 30.141 55.758 29.974 1.00 64.18  ? 29 LYS C C   1 
ATOM 1024 O O   . LYS C 1 28 ? 29.247 56.582 30.176 1.00 60.58  ? 29 LYS C O   1 
ATOM 1025 C CB  . LYS C 1 28 ? 32.326 56.350 30.876 1.00 76.85  ? 29 LYS C CB  1 
ATOM 1026 C CG  . LYS C 1 28 ? 33.461 56.087 31.832 1.00 83.95  ? 29 LYS C CG  1 
ATOM 1027 C CD  . LYS C 1 28 ? 34.626 56.810 31.198 1.00 88.91  ? 29 LYS C CD  1 
ATOM 1028 C CE  . LYS C 1 28 ? 35.893 56.697 32.022 1.00 92.14  ? 29 LYS C CE  1 
ATOM 1029 N NZ  . LYS C 1 28 ? 36.459 55.365 32.027 1.00 88.87  ? 29 LYS C NZ  1 
ATOM 1030 N N   . THR C 1 29 ? 30.263 55.196 28.782 1.00 60.03  ? 30 THR C N   1 
ATOM 1031 C CA  . THR C 1 29 ? 29.320 55.555 27.759 1.00 62.68  ? 30 THR C CA  1 
ATOM 1032 C C   . THR C 1 29 ? 28.159 54.581 27.674 1.00 63.53  ? 30 THR C C   1 
ATOM 1033 O O   . THR C 1 29 ? 27.195 54.822 26.942 1.00 67.53  ? 30 THR C O   1 
ATOM 1034 C CB  . THR C 1 29 ? 30.078 55.645 26.416 1.00 64.35  ? 30 THR C CB  1 
ATOM 1035 O OG1 . THR C 1 29 ? 30.404 54.326 25.965 1.00 61.87  ? 30 THR C OG1 1 
ATOM 1036 C CG2 . THR C 1 29 ? 31.347 56.513 26.589 1.00 66.35  ? 30 THR C CG2 1 
ATOM 1037 N N   . ARG C 1 30 ? 28.265 53.422 28.334 1.00 63.18  ? 31 ARG C N   1 
ATOM 1038 C CA  . ARG C 1 30 ? 27.250 52.372 28.286 1.00 60.99  ? 31 ARG C CA  1 
ATOM 1039 C C   . ARG C 1 30 ? 26.967 51.767 26.917 1.00 61.79  ? 31 ARG C C   1 
ATOM 1040 O O   . ARG C 1 30 ? 25.987 51.038 26.696 1.00 61.29  ? 31 ARG C O   1 
ATOM 1041 C CB  . ARG C 1 30 ? 25.982 52.910 28.862 1.00 61.03  ? 31 ARG C CB  1 
ATOM 1042 C CG  . ARG C 1 30 ? 26.131 53.066 30.330 1.00 54.06  ? 31 ARG C CG  1 
ATOM 1043 C CD  . ARG C 1 30 ? 25.005 52.161 30.483 1.00 53.73  ? 31 ARG C CD  1 
ATOM 1044 N NE  . ARG C 1 30 ? 24.714 52.037 31.863 1.00 54.78  ? 31 ARG C NE  1 
ATOM 1045 C CZ  . ARG C 1 30 ? 23.499 51.595 32.199 1.00 59.06  ? 31 ARG C CZ  1 
ATOM 1046 N NH1 . ARG C 1 30 ? 22.532 51.181 31.284 1.00 46.15  ? 31 ARG C NH1 1 
ATOM 1047 N NH2 . ARG C 1 30 ? 23.349 51.599 33.534 1.00 62.55  ? 31 ARG C NH2 1 
ATOM 1048 N N   . GLY C 1 31 ? 27.898 52.005 25.998 1.00 61.91  ? 32 GLY C N   1 
ATOM 1049 C CA  . GLY C 1 31 ? 27.798 51.503 24.631 1.00 61.90  ? 32 GLY C CA  1 
ATOM 1050 C C   . GLY C 1 31 ? 28.073 50.011 24.493 1.00 60.89  ? 32 GLY C C   1 
ATOM 1051 O O   . GLY C 1 31 ? 29.170 49.492 24.778 1.00 63.62  ? 32 GLY C O   1 
ATOM 1052 N N   . ARG C 1 32 ? 27.041 49.369 23.992 1.00 57.33  ? 33 ARG C N   1 
ATOM 1053 C CA  . ARG C 1 32 ? 26.982 47.936 23.845 1.00 56.27  ? 33 ARG C CA  1 
ATOM 1054 C C   . ARG C 1 32 ? 27.238 47.522 22.443 1.00 56.30  ? 33 ARG C C   1 
ATOM 1055 O O   . ARG C 1 32 ? 26.771 48.183 21.514 1.00 60.10  ? 33 ARG C O   1 
ATOM 1056 C CB  . ARG C 1 32 ? 25.638 47.433 24.193 1.00 58.70  ? 33 ARG C CB  1 
ATOM 1057 C CG  . ARG C 1 32 ? 25.238 47.805 25.589 1.00 56.04  ? 33 ARG C CG  1 
ATOM 1058 C CD  . ARG C 1 32 ? 23.982 47.084 25.824 1.00 44.16  ? 33 ARG C CD  1 
ATOM 1059 N NE  . ARG C 1 32 ? 23.909 47.037 27.241 1.00 45.30  ? 33 ARG C NE  1 
ATOM 1060 C CZ  . ARG C 1 32 ? 22.737 47.128 27.852 1.00 54.49  ? 33 ARG C CZ  1 
ATOM 1061 N NH1 . ARG C 1 32 ? 21.612 47.343 27.156 1.00 56.00  ? 33 ARG C NH1 1 
ATOM 1062 N NH2 . ARG C 1 32 ? 22.702 47.008 29.175 1.00 56.73  ? 33 ARG C NH2 1 
ATOM 1063 N N   . LYS C 1 33 ? 27.835 46.368 22.266 1.00 55.61  ? 34 LYS C N   1 
ATOM 1064 C CA  . LYS C 1 33 ? 28.218 45.976 20.927 1.00 57.49  ? 34 LYS C CA  1 
ATOM 1065 C C   . LYS C 1 33 ? 27.952 44.511 20.758 1.00 60.09  ? 34 LYS C C   1 
ATOM 1066 O O   . LYS C 1 33 ? 28.410 43.750 21.627 1.00 63.03  ? 34 LYS C O   1 
ATOM 1067 C CB  . LYS C 1 33 ? 29.701 46.289 20.756 1.00 55.64  ? 34 LYS C CB  1 
ATOM 1068 C CG  . LYS C 1 33 ? 30.395 45.944 19.459 1.00 59.43  ? 34 LYS C CG  1 
ATOM 1069 C CD  . LYS C 1 33 ? 31.887 46.214 19.663 1.00 62.62  ? 34 LYS C CD  1 
ATOM 1070 C CE  . LYS C 1 33 ? 32.560 45.894 18.326 1.00 65.16  ? 34 LYS C CE  1 
ATOM 1071 N NZ  . LYS C 1 33 ? 34.009 45.726 18.460 1.00 69.08  ? 34 LYS C NZ  1 
ATOM 1072 N N   . LEU C 1 34 ? 27.195 44.103 19.717 1.00 56.91  ? 35 LEU C N   1 
ATOM 1073 C CA  . LEU C 1 34 ? 27.106 42.667 19.431 1.00 49.25  ? 35 LEU C CA  1 
ATOM 1074 C C   . LEU C 1 34 ? 28.484 42.243 18.938 1.00 48.29  ? 35 LEU C C   1 
ATOM 1075 O O   . LEU C 1 34 ? 28.974 42.757 17.920 1.00 52.41  ? 35 LEU C O   1 
ATOM 1076 C CB  . LEU C 1 34 ? 26.127 42.302 18.340 1.00 43.18  ? 35 LEU C CB  1 
ATOM 1077 C CG  . LEU C 1 34 ? 26.004 40.795 18.106 1.00 44.40  ? 35 LEU C CG  1 
ATOM 1078 C CD1 . LEU C 1 34 ? 25.571 40.083 19.388 1.00 45.39  ? 35 LEU C CD1 1 
ATOM 1079 C CD2 . LEU C 1 34 ? 24.911 40.517 17.107 1.00 46.89  ? 35 LEU C CD2 1 
ATOM 1080 N N   . LEU C 1 35 ? 29.110 41.421 19.765 1.00 41.68  ? 36 LEU C N   1 
ATOM 1081 C CA  . LEU C 1 35 ? 30.449 40.970 19.535 1.00 41.60  ? 36 LEU C CA  1 
ATOM 1082 C C   . LEU C 1 35 ? 30.498 39.760 18.631 1.00 48.60  ? 36 LEU C C   1 
ATOM 1083 O O   . LEU C 1 35 ? 31.232 39.726 17.640 1.00 52.98  ? 36 LEU C O   1 
ATOM 1084 C CB  . LEU C 1 35 ? 31.057 40.618 20.834 1.00 33.21  ? 36 LEU C CB  1 
ATOM 1085 C CG  . LEU C 1 35 ? 31.683 41.678 21.597 1.00 32.56  ? 36 LEU C CG  1 
ATOM 1086 C CD1 . LEU C 1 35 ? 31.969 41.215 22.986 1.00 31.84  ? 36 LEU C CD1 1 
ATOM 1087 C CD2 . LEU C 1 35 ? 32.979 42.013 20.922 1.00 35.21  ? 36 LEU C CD2 1 
ATOM 1088 N N   . ARG C 1 36 ? 29.720 38.740 18.983 1.00 52.01  ? 37 ARG C N   1 
ATOM 1089 C CA  . ARG C 1 36 ? 29.786 37.427 18.361 1.00 52.87  ? 37 ARG C CA  1 
ATOM 1090 C C   . ARG C 1 36 ? 28.396 36.809 18.530 1.00 55.26  ? 37 ARG C C   1 
ATOM 1091 O O   . ARG C 1 36 ? 27.712 37.039 19.545 1.00 57.27  ? 37 ARG C O   1 
ATOM 1092 C CB  . ARG C 1 36 ? 30.853 36.567 19.101 1.00 53.92  ? 37 ARG C CB  1 
ATOM 1093 C CG  . ARG C 1 36 ? 32.322 37.112 19.286 1.00 50.82  ? 37 ARG C CG  1 
ATOM 1094 C CD  . ARG C 1 36 ? 32.850 36.728 20.677 1.00 51.04  ? 37 ARG C CD  1 
ATOM 1095 N NE  . ARG C 1 36 ? 34.051 37.403 21.169 1.00 44.30  ? 37 ARG C NE  1 
ATOM 1096 C CZ  . ARG C 1 36 ? 34.265 37.587 22.495 1.00 39.47  ? 37 ARG C CZ  1 
ATOM 1097 N NH1 . ARG C 1 36 ? 33.371 37.228 23.426 1.00 29.18  ? 37 ARG C NH1 1 
ATOM 1098 N NH2 . ARG C 1 36 ? 35.395 38.187 22.903 1.00 36.98  ? 37 ARG C NH2 1 
ATOM 1099 N N   . PHE C 1 37 ? 27.946 35.998 17.585 1.00 56.26  ? 38 PHE C N   1 
ATOM 1100 C CA  . PHE C 1 37 ? 26.611 35.411 17.633 1.00 53.81  ? 38 PHE C CA  1 
ATOM 1101 C C   . PHE C 1 37 ? 26.609 34.184 16.679 1.00 58.33  ? 38 PHE C C   1 
ATOM 1102 O O   . PHE C 1 37 ? 26.593 34.241 15.431 1.00 52.68  ? 38 PHE C O   1 
ATOM 1103 C CB  . PHE C 1 37 ? 25.610 36.530 17.224 1.00 46.09  ? 38 PHE C CB  1 
ATOM 1104 C CG  . PHE C 1 37 ? 24.167 36.078 17.285 1.00 39.87  ? 38 PHE C CG  1 
ATOM 1105 C CD1 . PHE C 1 37 ? 23.660 35.213 16.344 1.00 37.48  ? 38 PHE C CD1 1 
ATOM 1106 C CD2 . PHE C 1 37 ? 23.366 36.528 18.304 1.00 37.64  ? 38 PHE C CD2 1 
ATOM 1107 C CE1 . PHE C 1 37 ? 22.355 34.793 16.429 1.00 41.73  ? 38 PHE C CE1 1 
ATOM 1108 C CE2 . PHE C 1 37 ? 22.057 36.101 18.385 1.00 36.84  ? 38 PHE C CE2 1 
ATOM 1109 C CZ  . PHE C 1 37 ? 21.546 35.241 17.450 1.00 40.61  ? 38 PHE C CZ  1 
ATOM 1110 N N   . ASN C 1 38 ? 26.690 33.003 17.273 1.00 63.38  ? 39 ASN C N   1 
ATOM 1111 C CA  . ASN C 1 38 ? 26.817 31.765 16.526 1.00 62.37  ? 39 ASN C CA  1 
ATOM 1112 C C   . ASN C 1 38 ? 25.824 30.802 17.078 1.00 60.24  ? 39 ASN C C   1 
ATOM 1113 O O   . ASN C 1 38 ? 25.400 30.936 18.232 1.00 67.75  ? 39 ASN C O   1 
ATOM 1114 C CB  . ASN C 1 38 ? 28.202 31.157 16.677 1.00 66.24  ? 39 ASN C CB  1 
ATOM 1115 C CG  . ASN C 1 38 ? 29.309 32.007 16.058 1.00 71.12  ? 39 ASN C CG  1 
ATOM 1116 O OD1 . ASN C 1 38 ? 30.392 32.131 16.608 1.00 74.15  ? 39 ASN C OD1 1 
ATOM 1117 N ND2 . ASN C 1 38 ? 29.176 32.737 14.962 1.00 73.37  ? 39 ASN C ND2 1 
ATOM 1118 N N   . GLY C 1 39 ? 25.401 29.865 16.266 1.00 57.15  ? 40 GLY C N   1 
ATOM 1119 C CA  . GLY C 1 39 ? 24.494 28.844 16.723 1.00 52.75  ? 40 GLY C CA  1 
ATOM 1120 C C   . GLY C 1 39 ? 23.975 28.112 15.503 1.00 46.92  ? 40 GLY C C   1 
ATOM 1121 O O   . GLY C 1 39 ? 24.415 28.478 14.405 1.00 50.18  ? 40 GLY C O   1 
ATOM 1122 N N   . PRO C 1 40 ? 23.113 27.090 15.570 1.00 40.10  ? 41 PRO C N   1 
ATOM 1123 C CA  . PRO C 1 40 ? 22.597 26.524 16.792 1.00 36.42  ? 41 PRO C CA  1 
ATOM 1124 C C   . PRO C 1 40 ? 23.652 25.917 17.668 1.00 33.01  ? 41 PRO C C   1 
ATOM 1125 O O   . PRO C 1 40 ? 24.769 25.602 17.275 1.00 34.44  ? 41 PRO C O   1 
ATOM 1126 C CB  . PRO C 1 40 ? 21.552 25.521 16.354 1.00 43.29  ? 41 PRO C CB  1 
ATOM 1127 C CG  . PRO C 1 40 ? 21.728 25.381 14.859 1.00 45.27  ? 41 PRO C CG  1 
ATOM 1128 C CD  . PRO C 1 40 ? 22.170 26.792 14.498 1.00 41.91  ? 41 PRO C CD  1 
ATOM 1129 N N   . VAL C 1 41 ? 23.363 25.954 18.934 1.00 31.61  ? 42 VAL C N   1 
ATOM 1130 C CA  . VAL C 1 41 ? 24.220 25.333 19.893 1.00 33.58  ? 42 VAL C CA  1 
ATOM 1131 C C   . VAL C 1 41 ? 23.306 24.423 20.710 1.00 40.75  ? 42 VAL C C   1 
ATOM 1132 O O   . VAL C 1 41 ? 22.080 24.436 20.493 1.00 43.86  ? 42 VAL C O   1 
ATOM 1133 C CB  . VAL C 1 41 ? 24.917 26.411 20.744 1.00 34.42  ? 42 VAL C CB  1 
ATOM 1134 C CG1 . VAL C 1 41 ? 25.818 27.234 19.807 1.00 27.73  ? 42 VAL C CG1 1 
ATOM 1135 C CG2 . VAL C 1 41 ? 23.887 27.167 21.575 1.00 35.92  ? 42 VAL C CG2 1 
ATOM 1136 N N   . PRO C 1 42 ? 23.805 23.542 21.587 1.00 46.46  ? 43 PRO C N   1 
ATOM 1137 C CA  . PRO C 1 42 ? 22.922 22.661 22.338 1.00 48.57  ? 43 PRO C CA  1 
ATOM 1138 C C   . PRO C 1 42 ? 22.475 23.273 23.649 1.00 54.14  ? 43 PRO C C   1 
ATOM 1139 O O   . PRO C 1 42 ? 23.228 24.074 24.205 1.00 52.43  ? 43 PRO C O   1 
ATOM 1140 C CB  . PRO C 1 42 ? 23.765 21.417 22.471 1.00 51.88  ? 43 PRO C CB  1 
ATOM 1141 C CG  . PRO C 1 42 ? 24.931 21.567 21.486 1.00 48.93  ? 43 PRO C CG  1 
ATOM 1142 C CD  . PRO C 1 42 ? 25.187 23.041 21.634 1.00 44.01  ? 43 PRO C CD  1 
ATOM 1143 N N   . PRO C 1 43 ? 21.269 22.995 24.157 1.00 57.86  ? 44 PRO C N   1 
ATOM 1144 C CA  . PRO C 1 43 ? 20.759 23.506 25.442 1.00 60.36  ? 44 PRO C CA  1 
ATOM 1145 C C   . PRO C 1 43 ? 21.603 22.909 26.558 1.00 63.71  ? 44 PRO C C   1 
ATOM 1146 O O   . PRO C 1 43 ? 21.936 21.716 26.428 1.00 63.26  ? 44 PRO C O   1 
ATOM 1147 C CB  . PRO C 1 43 ? 19.360 23.036 25.532 1.00 61.65  ? 44 PRO C CB  1 
ATOM 1148 C CG  . PRO C 1 43 ? 19.440 21.733 24.742 1.00 64.14  ? 44 PRO C CG  1 
ATOM 1149 C CD  . PRO C 1 43 ? 20.275 22.148 23.522 1.00 62.37  ? 44 PRO C CD  1 
ATOM 1150 N N   . PRO C 1 44 ? 21.989 23.705 27.574 1.00 61.24  ? 45 PRO C N   1 
ATOM 1151 C CA  . PRO C 1 44 ? 22.807 23.236 28.684 1.00 56.71  ? 45 PRO C CA  1 
ATOM 1152 C C   . PRO C 1 44 ? 22.030 22.525 29.800 1.00 53.27  ? 45 PRO C C   1 
ATOM 1153 O O   . PRO C 1 44 ? 20.955 21.978 29.577 1.00 43.59  ? 45 PRO C O   1 
ATOM 1154 C CB  . PRO C 1 44 ? 23.549 24.523 29.078 1.00 54.06  ? 45 PRO C CB  1 
ATOM 1155 C CG  . PRO C 1 44 ? 22.507 25.592 28.887 1.00 59.41  ? 45 PRO C CG  1 
ATOM 1156 C CD  . PRO C 1 44 ? 21.842 25.162 27.586 1.00 60.50  ? 45 PRO C CD  1 
ATOM 1157 O OXT . PRO C 1 44 ? 22.521 22.503 30.919 1.00 60.98  ? 45 PRO C OXT 1 
ATOM 1158 N N   . GLY D 2 1  ? 37.703 39.708 34.089 1.00 64.83  ? 1  GLY D N   1 
ATOM 1159 C CA  . GLY D 2 1  ? 38.394 40.090 35.302 1.00 68.36  ? 1  GLY D CA  1 
ATOM 1160 C C   . GLY D 2 1  ? 37.592 39.331 36.338 1.00 68.47  ? 1  GLY D C   1 
ATOM 1161 O O   . GLY D 2 1  ? 37.724 38.112 36.383 1.00 70.11  ? 1  GLY D O   1 
ATOM 1162 N N   . GLU D 2 2  ? 36.732 39.988 37.127 1.00 67.01  ? 2  GLU D N   1 
ATOM 1163 C CA  . GLU D 2 2  ? 35.789 39.249 37.950 1.00 60.01  ? 2  GLU D CA  1 
ATOM 1164 C C   . GLU D 2 2  ? 34.776 38.744 36.940 1.00 52.81  ? 2  GLU D C   1 
ATOM 1165 O O   . GLU D 2 2  ? 34.718 39.273 35.811 1.00 50.29  ? 2  GLU D O   1 
ATOM 1166 C CB  . GLU D 2 2  ? 35.057 40.129 38.959 1.00 66.87  ? 2  GLU D CB  1 
ATOM 1167 C CG  . GLU D 2 2  ? 34.747 39.338 40.240 1.00 77.02  ? 2  GLU D CG  1 
ATOM 1168 C CD  . GLU D 2 2  ? 33.319 39.269 40.837 1.00 82.03  ? 2  GLU D CD  1 
ATOM 1169 O OE1 . GLU D 2 2  ? 32.367 39.859 40.292 1.00 80.53  ? 2  GLU D OE1 1 
ATOM 1170 O OE2 . GLU D 2 2  ? 33.168 38.592 41.872 1.00 84.15  ? 2  GLU D OE2 1 
ATOM 1171 N N   . TRP D 2 3  ? 34.084 37.678 37.300 1.00 43.49  ? 3  TRP D N   1 
ATOM 1172 C CA  . TRP D 2 3  ? 33.066 37.045 36.479 1.00 35.35  ? 3  TRP D CA  1 
ATOM 1173 C C   . TRP D 2 3  ? 31.985 36.732 37.468 1.00 38.51  ? 3  TRP D C   1 
ATOM 1174 O O   . TRP D 2 3  ? 32.355 36.504 38.628 1.00 39.16  ? 3  TRP D O   1 
ATOM 1175 C CB  . TRP D 2 3  ? 33.511 35.712 35.875 1.00 29.81  ? 3  TRP D CB  1 
ATOM 1176 C CG  . TRP D 2 3  ? 34.317 35.706 34.560 1.00 32.06  ? 3  TRP D CG  1 
ATOM 1177 C CD1 . TRP D 2 3  ? 35.703 35.904 34.491 1.00 32.32  ? 3  TRP D CD1 1 
ATOM 1178 C CD2 . TRP D 2 3  ? 33.759 35.534 33.310 1.00 25.49  ? 3  TRP D CD2 1 
ATOM 1179 N NE1 . TRP D 2 3  ? 35.996 35.863 33.195 1.00 35.50  ? 3  TRP D NE1 1 
ATOM 1180 C CE2 . TRP D 2 3  ? 34.860 35.641 32.481 1.00 28.80  ? 3  TRP D CE2 1 
ATOM 1181 C CE3 . TRP D 2 3  ? 32.526 35.300 32.746 1.00 26.18  ? 3  TRP D CE3 1 
ATOM 1182 C CZ2 . TRP D 2 3  ? 34.699 35.527 31.117 1.00 27.15  ? 3  TRP D CZ2 1 
ATOM 1183 C CZ3 . TRP D 2 3  ? 32.353 35.184 31.375 1.00 22.95  ? 3  TRP D CZ3 1 
ATOM 1184 C CH2 . TRP D 2 3  ? 33.443 35.312 30.558 1.00 26.64  ? 3  TRP D CH2 1 
ATOM 1185 N N   . GLU D 2 4  ? 30.686 36.782 37.092 1.00 46.06  ? 4  GLU D N   1 
ATOM 1186 C CA  . GLU D 2 4  ? 29.557 36.355 37.956 1.00 47.52  ? 4  GLU D CA  1 
ATOM 1187 C C   . GLU D 2 4  ? 28.277 36.031 37.180 1.00 48.26  ? 4  GLU D C   1 
ATOM 1188 O O   . GLU D 2 4  ? 28.117 36.429 36.022 1.00 47.23  ? 4  GLU D O   1 
ATOM 1189 C CB  . GLU D 2 4  ? 29.172 37.394 38.968 1.00 47.89  ? 4  GLU D CB  1 
ATOM 1190 C CG  . GLU D 2 4  ? 28.530 38.577 38.298 1.00 55.94  ? 4  GLU D CG  1 
ATOM 1191 C CD  . GLU D 2 4  ? 28.255 39.628 39.314 1.00 62.84  ? 4  GLU D CD  1 
ATOM 1192 O OE1 . GLU D 2 4  ? 29.186 40.378 39.625 1.00 71.46  ? 4  GLU D OE1 1 
ATOM 1193 O OE2 . GLU D 2 4  ? 27.123 39.654 39.789 1.00 63.07  ? 4  GLU D OE2 1 
ATOM 1194 N N   . ILE D 2 5  ? 27.340 35.336 37.814 1.00 48.07  ? 5  ILE D N   1 
ATOM 1195 C CA  . ILE D 2 5  ? 26.142 34.874 37.131 1.00 54.27  ? 5  ILE D CA  1 
ATOM 1196 C C   . ILE D 2 5  ? 25.027 35.865 37.362 1.00 56.13  ? 5  ILE D C   1 
ATOM 1197 O O   . ILE D 2 5  ? 24.639 36.104 38.521 1.00 54.96  ? 5  ILE D O   1 
ATOM 1198 C CB  . ILE D 2 5  ? 25.671 33.453 37.653 1.00 58.70  ? 5  ILE D CB  1 
ATOM 1199 C CG1 . ILE D 2 5  ? 26.670 32.378 37.247 1.00 60.62  ? 5  ILE D CG1 1 
ATOM 1200 C CG2 . ILE D 2 5  ? 24.310 33.063 37.043 1.00 57.84  ? 5  ILE D CG2 1 
ATOM 1201 C CD1 . ILE D 2 5  ? 26.324 31.036 37.925 1.00 57.55  ? 5  ILE D CD1 1 
ATOM 1202 N N   . ILE D 2 6  ? 24.509 36.420 36.266 1.00 55.28  ? 6  ILE D N   1 
ATOM 1203 C CA  . ILE D 2 6  ? 23.407 37.325 36.434 1.00 56.20  ? 6  ILE D CA  1 
ATOM 1204 C C   . ILE D 2 6  ? 22.089 36.636 36.143 1.00 59.51  ? 6  ILE D C   1 
ATOM 1205 O O   . ILE D 2 6  ? 22.020 35.710 35.316 1.00 64.21  ? 6  ILE D O   1 
ATOM 1206 C CB  . ILE D 2 6  ? 23.540 38.588 35.549 1.00 56.17  ? 6  ILE D CB  1 
ATOM 1207 C CG1 . ILE D 2 6  ? 23.550 38.332 34.050 1.00 54.81  ? 6  ILE D CG1 1 
ATOM 1208 C CG2 . ILE D 2 6  ? 24.771 39.299 36.136 1.00 52.04  ? 6  ILE D CG2 1 
ATOM 1209 C CD1 . ILE D 2 6  ? 23.130 39.588 33.246 1.00 43.57  ? 6  ILE D CD1 1 
ATOM 1210 N N   . ASP D 2 7  ? 21.062 37.115 36.869 1.00 60.67  ? 7  ASP D N   1 
ATOM 1211 C CA  . ASP D 2 7  ? 19.726 36.566 36.867 1.00 58.25  ? 7  ASP D CA  1 
ATOM 1212 C C   . ASP D 2 7  ? 19.013 36.906 35.575 1.00 59.87  ? 7  ASP D C   1 
ATOM 1213 O O   . ASP D 2 7  ? 19.342 37.908 34.935 1.00 63.22  ? 7  ASP D O   1 
ATOM 1214 C CB  . ASP D 2 7  ? 18.972 37.122 38.063 1.00 59.57  ? 7  ASP D CB  1 
ATOM 1215 C CG  . ASP D 2 7  ? 17.639 36.419 38.332 1.00 66.57  ? 7  ASP D CG  1 
ATOM 1216 O OD1 . ASP D 2 7  ? 17.541 35.193 38.225 1.00 70.44  ? 7  ASP D OD1 1 
ATOM 1217 O OD2 . ASP D 2 7  ? 16.670 37.101 38.652 1.00 69.32  ? 7  ASP D OD2 1 
ATOM 1218 N N   . ILE D 2 8  ? 18.055 36.086 35.143 1.00 58.94  ? 8  ILE D N   1 
ATOM 1219 C CA  . ILE D 2 8  ? 17.352 36.357 33.904 1.00 60.02  ? 8  ILE D CA  1 
ATOM 1220 C C   . ILE D 2 8  ? 16.160 37.281 34.090 1.00 66.82  ? 8  ILE D C   1 
ATOM 1221 O O   . ILE D 2 8  ? 15.040 37.044 33.622 1.00 63.93  ? 8  ILE D O   1 
ATOM 1222 C CB  . ILE D 2 8  ? 16.859 35.073 33.204 1.00 57.15  ? 8  ILE D CB  1 
ATOM 1223 C CG1 . ILE D 2 8  ? 16.193 34.085 34.128 1.00 53.65  ? 8  ILE D CG1 1 
ATOM 1224 C CG2 . ILE D 2 8  ? 18.072 34.505 32.515 1.00 57.17  ? 8  ILE D CG2 1 
ATOM 1225 C CD1 . ILE D 2 8  ? 15.502 33.021 33.284 1.00 54.98  ? 8  ILE D CD1 1 
ATOM 1226 N N   . GLY D 2 9  ? 16.458 38.422 34.721 1.00 72.58  ? 9  GLY D N   1 
ATOM 1227 C CA  . GLY D 2 9  ? 15.499 39.494 34.883 1.00 70.80  ? 9  GLY D CA  1 
ATOM 1228 C C   . GLY D 2 9  ? 15.305 40.190 33.530 1.00 68.70  ? 9  GLY D C   1 
ATOM 1229 O O   . GLY D 2 9  ? 15.998 39.920 32.533 1.00 67.95  ? 9  GLY D O   1 
ATOM 1230 N N   . PRO D 2 10 ? 14.433 41.190 33.463 1.00 63.69  ? 10 PRO D N   1 
ATOM 1231 C CA  . PRO D 2 10 ? 14.144 41.910 32.243 1.00 53.45  ? 10 PRO D CA  1 
ATOM 1232 C C   . PRO D 2 10 ? 15.354 42.708 31.818 1.00 44.55  ? 10 PRO D C   1 
ATOM 1233 O O   . PRO D 2 10 ? 15.456 43.018 30.634 1.00 40.62  ? 10 PRO D O   1 
ATOM 1234 C CB  . PRO D 2 10 ? 12.962 42.704 32.623 1.00 59.55  ? 10 PRO D CB  1 
ATOM 1235 C CG  . PRO D 2 10 ? 13.388 43.171 34.004 1.00 61.24  ? 10 PRO D CG  1 
ATOM 1236 C CD  . PRO D 2 10 ? 13.918 41.903 34.626 1.00 61.95  ? 10 PRO D CD  1 
ATOM 1237 N N   . PHE D 2 11 ? 16.292 43.014 32.732 1.00 37.77  ? 11 PHE D N   1 
ATOM 1238 C CA  . PHE D 2 11 ? 17.557 43.561 32.258 1.00 47.12  ? 11 PHE D CA  1 
ATOM 1239 C C   . PHE D 2 11 ? 18.214 42.535 31.299 1.00 51.10  ? 11 PHE D C   1 
ATOM 1240 O O   . PHE D 2 11 ? 18.544 42.928 30.163 1.00 54.74  ? 11 PHE D O   1 
ATOM 1241 C CB  . PHE D 2 11 ? 18.534 43.867 33.427 1.00 46.69  ? 11 PHE D CB  1 
ATOM 1242 C CG  . PHE D 2 11 ? 19.960 44.342 33.082 1.00 45.36  ? 11 PHE D CG  1 
ATOM 1243 C CD1 . PHE D 2 11 ? 20.286 44.740 31.796 1.00 43.17  ? 11 PHE D CD1 1 
ATOM 1244 C CD2 . PHE D 2 11 ? 20.909 44.401 34.082 1.00 43.26  ? 11 PHE D CD2 1 
ATOM 1245 C CE1 . PHE D 2 11 ? 21.532 45.178 31.504 1.00 42.81  ? 11 PHE D CE1 1 
ATOM 1246 C CE2 . PHE D 2 11 ? 22.165 44.853 33.775 1.00 40.64  ? 11 PHE D CE2 1 
ATOM 1247 C CZ  . PHE D 2 11 ? 22.471 45.241 32.501 1.00 43.35  ? 11 PHE D CZ  1 
ATOM 1248 N N   . THR D 2 12 ? 18.359 41.240 31.700 1.00 49.45  ? 12 THR D N   1 
ATOM 1249 C CA  . THR D 2 12 ? 18.980 40.197 30.872 1.00 34.82  ? 12 THR D CA  1 
ATOM 1250 C C   . THR D 2 12 ? 18.177 39.905 29.597 1.00 34.41  ? 12 THR D C   1 
ATOM 1251 O O   . THR D 2 12 ? 18.723 39.610 28.524 1.00 35.00  ? 12 THR D O   1 
ATOM 1252 C CB  . THR D 2 12 ? 19.130 39.030 31.811 1.00 28.07  ? 12 THR D CB  1 
ATOM 1253 O OG1 . THR D 2 12 ? 20.098 39.450 32.764 1.00 22.58  ? 12 THR D OG1 1 
ATOM 1254 C CG2 . THR D 2 12 ? 19.598 37.786 31.169 1.00 32.87  ? 12 THR D CG2 1 
ATOM 1255 N N   . GLN D 2 13 ? 16.869 40.116 29.634 1.00 34.00  ? 13 GLN D N   1 
ATOM 1256 C CA  . GLN D 2 13 ? 16.068 40.020 28.440 1.00 41.90  ? 13 GLN D CA  1 
ATOM 1257 C C   . GLN D 2 13 ? 16.325 41.156 27.461 1.00 45.94  ? 13 GLN D C   1 
ATOM 1258 O O   . GLN D 2 13 ? 16.222 40.973 26.251 1.00 47.64  ? 13 GLN D O   1 
ATOM 1259 C CB  . GLN D 2 13 ? 14.635 40.018 28.817 1.00 46.89  ? 13 GLN D CB  1 
ATOM 1260 C CG  . GLN D 2 13 ? 14.363 38.829 29.747 1.00 56.63  ? 13 GLN D CG  1 
ATOM 1261 C CD  . GLN D 2 13 ? 14.585 37.402 29.220 1.00 59.00  ? 13 GLN D CD  1 
ATOM 1262 O OE1 . GLN D 2 13 ? 14.336 37.064 28.063 1.00 59.99  ? 13 GLN D OE1 1 
ATOM 1263 N NE2 . GLN D 2 13 ? 15.050 36.499 30.080 1.00 63.06  ? 13 GLN D NE2 1 
ATOM 1264 N N   . ASN D 2 14 ? 16.685 42.344 27.935 1.00 50.80  ? 14 ASN D N   1 
ATOM 1265 C CA  . ASN D 2 14 ? 16.977 43.501 27.078 1.00 55.32  ? 14 ASN D CA  1 
ATOM 1266 C C   . ASN D 2 14 ? 18.176 43.290 26.160 1.00 53.10  ? 14 ASN D C   1 
ATOM 1267 O O   . ASN D 2 14 ? 18.193 43.656 24.981 1.00 54.12  ? 14 ASN D O   1 
ATOM 1268 C CB  . ASN D 2 14 ? 17.221 44.764 27.961 1.00 61.42  ? 14 ASN D CB  1 
ATOM 1269 C CG  . ASN D 2 14 ? 15.982 45.604 28.355 1.00 65.57  ? 14 ASN D CG  1 
ATOM 1270 O OD1 . ASN D 2 14 ? 14.814 45.328 28.087 1.00 67.17  ? 14 ASN D OD1 1 
ATOM 1271 N ND2 . ASN D 2 14 ? 16.117 46.706 29.065 1.00 71.37  ? 14 ASN D ND2 1 
ATOM 1272 N N   . LEU D 2 15 ? 19.218 42.710 26.731 1.00 50.58  ? 15 LEU D N   1 
ATOM 1273 C CA  . LEU D 2 15 ? 20.431 42.317 26.040 1.00 45.10  ? 15 LEU D CA  1 
ATOM 1274 C C   . LEU D 2 15 ? 20.118 41.250 24.971 1.00 48.57  ? 15 LEU D C   1 
ATOM 1275 O O   . LEU D 2 15 ? 20.767 41.167 23.923 1.00 43.34  ? 15 LEU D O   1 
ATOM 1276 C CB  . LEU D 2 15 ? 21.381 41.760 27.078 1.00 42.83  ? 15 LEU D CB  1 
ATOM 1277 C CG  . LEU D 2 15 ? 22.088 42.567 28.128 1.00 38.12  ? 15 LEU D CG  1 
ATOM 1278 C CD1 . LEU D 2 15 ? 22.630 41.687 29.236 1.00 36.79  ? 15 LEU D CD1 1 
ATOM 1279 C CD2 . LEU D 2 15 ? 23.215 43.286 27.440 1.00 39.61  ? 15 LEU D CD2 1 
ATOM 1280 N N   . GLY D 2 16 ? 19.155 40.355 25.261 1.00 53.15  ? 16 GLY D N   1 
ATOM 1281 C CA  . GLY D 2 16 ? 18.682 39.354 24.331 1.00 48.84  ? 16 GLY D CA  1 
ATOM 1282 C C   . GLY D 2 16 ? 18.121 40.084 23.140 1.00 54.23  ? 16 GLY D C   1 
ATOM 1283 O O   . GLY D 2 16 ? 18.619 39.851 22.035 1.00 64.99  ? 16 GLY D O   1 
ATOM 1284 N N   . LYS D 2 17 ? 17.135 40.992 23.350 1.00 52.91  ? 17 LYS D N   1 
ATOM 1285 C CA  . LYS D 2 17 ? 16.549 41.834 22.284 1.00 44.17  ? 17 LYS D CA  1 
ATOM 1286 C C   . LYS D 2 17 ? 17.599 42.566 21.443 1.00 34.17  ? 17 LYS D C   1 
ATOM 1287 O O   . LYS D 2 17 ? 17.671 42.354 20.243 1.00 25.33  ? 17 LYS D O   1 
ATOM 1288 C CB  . LYS D 2 17 ? 15.618 42.867 22.887 1.00 47.99  ? 17 LYS D CB  1 
ATOM 1289 C CG  . LYS D 2 17 ? 14.325 42.217 23.324 1.00 52.14  ? 17 LYS D CG  1 
ATOM 1290 C CD  . LYS D 2 17 ? 13.207 43.240 23.223 1.00 56.85  ? 17 LYS D CD  1 
ATOM 1291 C CE  . LYS D 2 17 ? 11.787 42.664 23.420 1.00 57.32  ? 17 LYS D CE  1 
ATOM 1292 N NZ  . LYS D 2 17 ? 11.508 42.296 24.798 1.00 58.75  ? 17 LYS D NZ  1 
ATOM 1293 N N   . PHE D 2 18 ? 18.460 43.393 22.036 1.00 34.12  ? 18 PHE D N   1 
ATOM 1294 C CA  . PHE D 2 18 ? 19.566 44.030 21.335 1.00 37.44  ? 18 PHE D CA  1 
ATOM 1295 C C   . PHE D 2 18 ? 20.345 43.033 20.460 1.00 52.28  ? 18 PHE D C   1 
ATOM 1296 O O   . PHE D 2 18 ? 20.387 43.210 19.231 1.00 63.51  ? 18 PHE D O   1 
ATOM 1297 C CB  . PHE D 2 18 ? 20.494 44.663 22.348 1.00 26.08  ? 18 PHE D CB  1 
ATOM 1298 C CG  . PHE D 2 18 ? 21.797 45.173 21.780 1.00 29.81  ? 18 PHE D CG  1 
ATOM 1299 C CD1 . PHE D 2 18 ? 21.821 46.184 20.860 1.00 29.15  ? 18 PHE D CD1 1 
ATOM 1300 C CD2 . PHE D 2 18 ? 22.980 44.622 22.207 1.00 35.52  ? 18 PHE D CD2 1 
ATOM 1301 C CE1 . PHE D 2 18 ? 23.038 46.631 20.386 1.00 29.76  ? 18 PHE D CE1 1 
ATOM 1302 C CE2 . PHE D 2 18 ? 24.196 45.080 21.720 1.00 38.67  ? 18 PHE D CE2 1 
ATOM 1303 C CZ  . PHE D 2 18 ? 24.232 46.095 20.801 1.00 32.72  ? 18 PHE D CZ  1 
ATOM 1304 N N   . ALA D 2 19 ? 20.897 41.946 21.030 1.00 57.35  ? 19 ALA D N   1 
ATOM 1305 C CA  . ALA D 2 19 ? 21.680 40.948 20.300 1.00 52.76  ? 19 ALA D CA  1 
ATOM 1306 C C   . ALA D 2 19 ? 21.049 40.513 18.998 1.00 48.50  ? 19 ALA D C   1 
ATOM 1307 O O   . ALA D 2 19 ? 21.643 40.674 17.935 1.00 43.98  ? 19 ALA D O   1 
ATOM 1308 C CB  . ALA D 2 19 ? 21.865 39.679 21.121 1.00 55.03  ? 19 ALA D CB  1 
ATOM 1309 N N   . VAL D 2 20 ? 19.801 40.069 19.079 1.00 46.75  ? 20 VAL D N   1 
ATOM 1310 C CA  . VAL D 2 20 ? 19.114 39.528 17.937 1.00 47.83  ? 20 VAL D CA  1 
ATOM 1311 C C   . VAL D 2 20 ? 18.859 40.641 16.929 1.00 54.55  ? 20 VAL D C   1 
ATOM 1312 O O   . VAL D 2 20 ? 19.095 40.481 15.724 1.00 57.03  ? 20 VAL D O   1 
ATOM 1313 C CB  . VAL D 2 20 ? 17.844 38.862 18.481 1.00 46.24  ? 20 VAL D CB  1 
ATOM 1314 C CG1 . VAL D 2 20 ? 16.995 38.280 17.371 1.00 49.75  ? 20 VAL D CG1 1 
ATOM 1315 C CG2 . VAL D 2 20 ? 18.245 37.687 19.363 1.00 42.11  ? 20 VAL D CG2 1 
ATOM 1316 N N   . ASP D 2 21 ? 18.489 41.836 17.381 1.00 59.36  ? 21 ASP D N   1 
ATOM 1317 C CA  . ASP D 2 21 ? 18.228 42.967 16.490 1.00 58.28  ? 21 ASP D CA  1 
ATOM 1318 C C   . ASP D 2 21 ? 19.473 43.384 15.738 1.00 60.68  ? 21 ASP D C   1 
ATOM 1319 O O   . ASP D 2 21 ? 19.395 43.751 14.559 1.00 67.03  ? 21 ASP D O   1 
ATOM 1320 C CB  . ASP D 2 21 ? 17.747 44.186 17.251 1.00 55.64  ? 21 ASP D CB  1 
ATOM 1321 C CG  . ASP D 2 21 ? 16.295 44.190 17.708 1.00 56.89  ? 21 ASP D CG  1 
ATOM 1322 O OD1 . ASP D 2 21 ? 15.452 43.501 17.101 1.00 57.31  ? 21 ASP D OD1 1 
ATOM 1323 O OD2 . ASP D 2 21 ? 16.029 44.919 18.672 1.00 54.77  ? 21 ASP D OD2 1 
ATOM 1324 N N   . GLU D 2 22 ? 20.625 43.291 16.396 1.00 57.17  ? 22 GLU D N   1 
ATOM 1325 C CA  . GLU D 2 22 ? 21.891 43.665 15.787 1.00 58.74  ? 22 GLU D CA  1 
ATOM 1326 C C   . GLU D 2 22 ? 22.394 42.641 14.790 1.00 57.82  ? 22 GLU D C   1 
ATOM 1327 O O   . GLU D 2 22 ? 23.073 42.945 13.801 1.00 54.54  ? 22 GLU D O   1 
ATOM 1328 C CB  . GLU D 2 22 ? 22.881 43.851 16.879 1.00 63.49  ? 22 GLU D CB  1 
ATOM 1329 C CG  . GLU D 2 22 ? 22.792 45.280 17.371 1.00 66.15  ? 22 GLU D CG  1 
ATOM 1330 C CD  . GLU D 2 22 ? 23.968 46.099 16.872 1.00 66.52  ? 22 GLU D CD  1 
ATOM 1331 O OE1 . GLU D 2 22 ? 25.075 46.034 17.441 1.00 64.58  ? 22 GLU D OE1 1 
ATOM 1332 O OE2 . GLU D 2 22 ? 23.744 46.801 15.893 1.00 65.73  ? 22 GLU D OE2 1 
ATOM 1333 N N   . GLU D 2 23 ? 22.039 41.387 15.072 1.00 58.53  ? 23 GLU D N   1 
ATOM 1334 C CA  . GLU D 2 23 ? 22.351 40.294 14.198 1.00 51.10  ? 23 GLU D CA  1 
ATOM 1335 C C   . GLU D 2 23 ? 21.517 40.479 12.958 1.00 47.85  ? 23 GLU D C   1 
ATOM 1336 O O   . GLU D 2 23 ? 22.070 40.530 11.865 1.00 39.12  ? 23 GLU D O   1 
ATOM 1337 C CB  . GLU D 2 23 ? 22.024 38.951 14.875 1.00 45.99  ? 23 GLU D CB  1 
ATOM 1338 C CG  . GLU D 2 23 ? 22.254 37.716 13.973 1.00 45.84  ? 23 GLU D CG  1 
ATOM 1339 C CD  . GLU D 2 23 ? 23.542 37.635 13.118 1.00 45.11  ? 23 GLU D CD  1 
ATOM 1340 O OE1 . GLU D 2 23 ? 24.665 37.888 13.584 1.00 43.61  ? 23 GLU D OE1 1 
ATOM 1341 O OE2 . GLU D 2 23 ? 23.409 37.326 11.938 1.00 47.64  ? 23 GLU D OE2 1 
ATOM 1342 N N   . ASN D 2 24 ? 20.207 40.652 13.128 1.00 49.20  ? 24 ASN D N   1 
ATOM 1343 C CA  . ASN D 2 24 ? 19.282 40.783 12.006 1.00 54.63  ? 24 ASN D CA  1 
ATOM 1344 C C   . ASN D 2 24 ? 19.702 41.871 11.004 1.00 62.38  ? 24 ASN D C   1 
ATOM 1345 O O   . ASN D 2 24 ? 19.405 41.794 9.807  1.00 67.82  ? 24 ASN D O   1 
ATOM 1346 C CB  . ASN D 2 24 ? 17.896 41.103 12.520 1.00 50.09  ? 24 ASN D CB  1 
ATOM 1347 C CG  . ASN D 2 24 ? 17.007 39.928 12.837 1.00 42.02  ? 24 ASN D CG  1 
ATOM 1348 O OD1 . ASN D 2 24 ? 16.839 39.017 12.060 1.00 38.52  ? 24 ASN D OD1 1 
ATOM 1349 N ND2 . ASN D 2 24 ? 16.330 39.887 13.962 1.00 42.93  ? 24 ASN D ND2 1 
ATOM 1350 N N   . LYS D 2 25 ? 20.424 42.907 11.453 1.00 67.24  ? 25 LYS D N   1 
ATOM 1351 C CA  . LYS D 2 25 ? 21.000 43.872 10.539 1.00 72.13  ? 25 LYS D CA  1 
ATOM 1352 C C   . LYS D 2 25 ? 22.005 43.147 9.641  1.00 79.10  ? 25 LYS D C   1 
ATOM 1353 O O   . LYS D 2 25 ? 22.022 43.290 8.421  1.00 85.57  ? 25 LYS D O   1 
ATOM 1354 C CB  . LYS D 2 25 ? 21.767 44.940 11.257 1.00 74.09  ? 25 LYS D CB  1 
ATOM 1355 C CG  . LYS D 2 25 ? 21.039 45.851 12.212 1.00 76.43  ? 25 LYS D CG  1 
ATOM 1356 C CD  . LYS D 2 25 ? 22.151 46.823 12.554 1.00 77.88  ? 25 LYS D CD  1 
ATOM 1357 C CE  . LYS D 2 25 ? 21.642 47.852 13.516 1.00 82.50  ? 25 LYS D CE  1 
ATOM 1358 N NZ  . LYS D 2 25 ? 22.729 48.751 13.873 1.00 86.89  ? 25 LYS D NZ  1 
ATOM 1359 N N   . ILE D 2 26 ? 22.855 42.330 10.273 1.00 80.18  ? 26 ILE D N   1 
ATOM 1360 C CA  . ILE D 2 26 ? 23.891 41.569 9.588  1.00 76.85  ? 26 ILE D CA  1 
ATOM 1361 C C   . ILE D 2 26 ? 23.286 40.424 8.784  1.00 76.39  ? 26 ILE D C   1 
ATOM 1362 O O   . ILE D 2 26 ? 23.919 39.984 7.835  1.00 76.07  ? 26 ILE D O   1 
ATOM 1363 C CB  . ILE D 2 26 ? 24.893 40.951 10.603 1.00 79.30  ? 26 ILE D CB  1 
ATOM 1364 C CG1 . ILE D 2 26 ? 25.242 41.873 11.769 1.00 77.29  ? 26 ILE D CG1 1 
ATOM 1365 C CG2 . ILE D 2 26 ? 26.166 40.679 9.833  1.00 82.09  ? 26 ILE D CG2 1 
ATOM 1366 C CD1 . ILE D 2 26 ? 26.019 41.158 12.871 1.00 80.31  ? 26 ILE D CD1 1 
ATOM 1367 N N   . GLY D 2 27 ? 22.125 39.871 9.151  1.00 78.76  ? 27 GLY D N   1 
ATOM 1368 C CA  . GLY D 2 27 ? 21.439 38.847 8.360  1.00 87.70  ? 27 GLY D CA  1 
ATOM 1369 C C   . GLY D 2 27 ? 22.058 37.448 8.112  1.00 92.71  ? 27 GLY D C   1 
ATOM 1370 O O   . GLY D 2 27 ? 21.495 36.678 7.323  1.00 95.56  ? 27 GLY D O   1 
ATOM 1371 N N   . GLN D 2 28 ? 23.176 37.030 8.744  1.00 91.42  ? 28 GLN D N   1 
ATOM 1372 C CA  . GLN D 2 28 ? 23.747 35.673 8.615  1.00 86.01  ? 28 GLN D CA  1 
ATOM 1373 C C   . GLN D 2 28 ? 22.729 34.532 8.566  1.00 77.33  ? 28 GLN D C   1 
ATOM 1374 O O   . GLN D 2 28 ? 22.766 33.657 7.717  1.00 74.48  ? 28 GLN D O   1 
ATOM 1375 C CB  . GLN D 2 28 ? 24.696 35.425 9.794  1.00 92.51  ? 28 GLN D CB  1 
ATOM 1376 C CG  . GLN D 2 28 ? 26.128 35.085 9.480  1.00 102.72 ? 28 GLN D CG  1 
ATOM 1377 C CD  . GLN D 2 28 ? 26.777 36.179 8.644  1.00 110.84 ? 28 GLN D CD  1 
ATOM 1378 O OE1 . GLN D 2 28 ? 27.188 37.217 9.158  1.00 113.98 ? 28 GLN D OE1 1 
ATOM 1379 N NE2 . GLN D 2 28 ? 26.862 36.016 7.330  1.00 114.61 ? 28 GLN D NE2 1 
ATOM 1380 N N   . TYR D 2 29 ? 21.777 34.582 9.479  1.00 73.92  ? 29 TYR D N   1 
ATOM 1381 C CA  . TYR D 2 29 ? 20.803 33.520 9.685  1.00 74.49  ? 29 TYR D CA  1 
ATOM 1382 C C   . TYR D 2 29 ? 19.439 33.870 9.102  1.00 70.17  ? 29 TYR D C   1 
ATOM 1383 O O   . TYR D 2 29 ? 18.389 33.251 9.398  1.00 64.78  ? 29 TYR D O   1 
ATOM 1384 C CB  . TYR D 2 29 ? 20.694 33.241 11.219 1.00 77.55  ? 29 TYR D CB  1 
ATOM 1385 C CG  . TYR D 2 29 ? 22.014 32.747 11.804 1.00 79.76  ? 29 TYR D CG  1 
ATOM 1386 C CD1 . TYR D 2 29 ? 22.342 31.414 11.740 1.00 80.11  ? 29 TYR D CD1 1 
ATOM 1387 C CD2 . TYR D 2 29 ? 22.905 33.656 12.342 1.00 81.00  ? 29 TYR D CD2 1 
ATOM 1388 C CE1 . TYR D 2 29 ? 23.584 30.989 12.181 1.00 85.07  ? 29 TYR D CE1 1 
ATOM 1389 C CE2 . TYR D 2 29 ? 24.139 33.231 12.777 1.00 83.79  ? 29 TYR D CE2 1 
ATOM 1390 C CZ  . TYR D 2 29 ? 24.479 31.901 12.697 1.00 84.42  ? 29 TYR D CZ  1 
ATOM 1391 O OH  . TYR D 2 29 ? 25.742 31.500 13.114 1.00 86.76  ? 29 TYR D OH  1 
ATOM 1392 N N   . GLY D 2 30 ? 19.467 34.820 8.172  1.00 67.11  ? 30 GLY D N   1 
ATOM 1393 C CA  . GLY D 2 30 ? 18.221 35.376 7.714  1.00 65.20  ? 30 GLY D CA  1 
ATOM 1394 C C   . GLY D 2 30 ? 17.702 36.281 8.820  1.00 62.75  ? 30 GLY D C   1 
ATOM 1395 O O   . GLY D 2 30 ? 18.482 36.953 9.493  1.00 64.19  ? 30 GLY D O   1 
ATOM 1396 N N   . ARG D 2 31 ? 16.405 36.245 9.039  1.00 63.68  ? 31 ARG D N   1 
ATOM 1397 C CA  . ARG D 2 31 ? 15.756 37.160 9.954  1.00 67.43  ? 31 ARG D CA  1 
ATOM 1398 C C   . ARG D 2 31 ? 15.403 36.325 11.154 1.00 71.13  ? 31 ARG D C   1 
ATOM 1399 O O   . ARG D 2 31 ? 15.315 35.097 11.015 1.00 77.40  ? 31 ARG D O   1 
ATOM 1400 C CB  . ARG D 2 31 ? 14.481 37.747 9.305  1.00 69.35  ? 31 ARG D CB  1 
ATOM 1401 C CG  . ARG D 2 31 ? 13.688 38.873 10.033 1.00 69.39  ? 31 ARG D CG  1 
ATOM 1402 C CD  . ARG D 2 31 ? 14.332 40.270 10.007 1.00 68.97  ? 31 ARG D CD  1 
ATOM 1403 N NE  . ARG D 2 31 ? 14.533 40.732 8.637  1.00 64.38  ? 31 ARG D NE  1 
ATOM 1404 C CZ  . ARG D 2 31 ? 15.511 41.574 8.319  1.00 62.10  ? 31 ARG D CZ  1 
ATOM 1405 N NH1 . ARG D 2 31 ? 16.306 42.163 9.227  1.00 55.63  ? 31 ARG D NH1 1 
ATOM 1406 N NH2 . ARG D 2 31 ? 15.649 41.859 7.032  1.00 61.61  ? 31 ARG D NH2 1 
ATOM 1407 N N   . LEU D 2 32 ? 15.200 36.917 12.328 1.00 70.60  ? 32 LEU D N   1 
ATOM 1408 C CA  . LEU D 2 32 ? 14.865 36.138 13.512 1.00 71.78  ? 32 LEU D CA  1 
ATOM 1409 C C   . LEU D 2 32 ? 13.833 36.829 14.389 1.00 72.80  ? 32 LEU D C   1 
ATOM 1410 O O   . LEU D 2 32 ? 13.858 38.060 14.524 1.00 77.95  ? 32 LEU D O   1 
ATOM 1411 C CB  . LEU D 2 32 ? 16.133 35.881 14.340 1.00 68.58  ? 32 LEU D CB  1 
ATOM 1412 C CG  . LEU D 2 32 ? 17.282 35.123 13.670 1.00 69.51  ? 32 LEU D CG  1 
ATOM 1413 C CD1 . LEU D 2 32 ? 18.588 35.496 14.341 1.00 68.14  ? 32 LEU D CD1 1 
ATOM 1414 C CD2 . LEU D 2 32 ? 16.969 33.626 13.667 1.00 67.51  ? 32 LEU D CD2 1 
ATOM 1415 N N   . THR D 2 33 ? 12.903 36.059 14.961 1.00 70.76  ? 33 THR D N   1 
ATOM 1416 C CA  . THR D 2 33 ? 11.977 36.582 15.959 1.00 62.95  ? 33 THR D CA  1 
ATOM 1417 C C   . THR D 2 33 ? 12.723 36.276 17.250 1.00 61.43  ? 33 THR D C   1 
ATOM 1418 O O   . THR D 2 33 ? 13.270 35.178 17.421 1.00 65.50  ? 33 THR D O   1 
ATOM 1419 C CB  . THR D 2 33 ? 10.587 35.835 15.870 1.00 60.61  ? 33 THR D CB  1 
ATOM 1420 O OG1 . THR D 2 33 ? 9.690  36.673 16.573 1.00 56.56  ? 33 THR D OG1 1 
ATOM 1421 C CG2 . THR D 2 33 ? 10.525 34.414 16.455 1.00 58.10  ? 33 THR D CG2 1 
ATOM 1422 N N   . PHE D 2 34 ? 12.970 37.261 18.093 1.00 57.45  ? 34 PHE D N   1 
ATOM 1423 C CA  . PHE D 2 34 ? 13.565 36.951 19.385 1.00 55.46  ? 34 PHE D CA  1 
ATOM 1424 C C   . PHE D 2 34 ? 12.541 36.142 20.189 1.00 51.82  ? 34 PHE D C   1 
ATOM 1425 O O   . PHE D 2 34 ? 11.378 36.057 19.793 1.00 47.72  ? 34 PHE D O   1 
ATOM 1426 C CB  . PHE D 2 34 ? 13.929 38.266 20.097 1.00 55.15  ? 34 PHE D CB  1 
ATOM 1427 C CG  . PHE D 2 34 ? 14.114 38.250 21.614 1.00 53.79  ? 34 PHE D CG  1 
ATOM 1428 C CD1 . PHE D 2 34 ? 13.026 38.479 22.424 1.00 52.27  ? 34 PHE D CD1 1 
ATOM 1429 C CD2 . PHE D 2 34 ? 15.353 38.039 22.173 1.00 54.78  ? 34 PHE D CD2 1 
ATOM 1430 C CE1 . PHE D 2 34 ? 13.182 38.499 23.786 1.00 56.18  ? 34 PHE D CE1 1 
ATOM 1431 C CE2 . PHE D 2 34 ? 15.497 38.062 23.545 1.00 54.90  ? 34 PHE D CE2 1 
ATOM 1432 C CZ  . PHE D 2 34 ? 14.413 38.291 24.354 1.00 55.19  ? 34 PHE D CZ  1 
ATOM 1433 N N   . ASN D 2 35 ? 12.959 35.483 21.262 1.00 48.28  ? 35 ASN D N   1 
ATOM 1434 C CA  . ASN D 2 35 ? 12.031 34.816 22.125 1.00 49.59  ? 35 ASN D CA  1 
ATOM 1435 C C   . ASN D 2 35 ? 12.582 34.901 23.516 1.00 48.88  ? 35 ASN D C   1 
ATOM 1436 O O   . ASN D 2 35 ? 12.136 35.784 24.248 1.00 56.96  ? 35 ASN D O   1 
ATOM 1437 C CB  . ASN D 2 35 ? 11.814 33.342 21.725 1.00 55.16  ? 35 ASN D CB  1 
ATOM 1438 C CG  . ASN D 2 35 ? 10.844 33.255 20.548 1.00 58.19  ? 35 ASN D CG  1 
ATOM 1439 O OD1 . ASN D 2 35 ? 11.232 33.069 19.385 1.00 59.88  ? 35 ASN D OD1 1 
ATOM 1440 N ND2 . ASN D 2 35 ? 9.546  33.417 20.790 1.00 60.36  ? 35 ASN D ND2 1 
ATOM 1441 N N   . LYS D 2 36 ? 13.593 34.135 23.930 1.00 43.91  ? 36 LYS D N   1 
ATOM 1442 C CA  . LYS D 2 36 ? 13.952 34.235 25.331 1.00 37.28  ? 36 LYS D CA  1 
ATOM 1443 C C   . LYS D 2 36 ? 15.426 34.026 25.614 1.00 30.38  ? 36 LYS D C   1 
ATOM 1444 O O   . LYS D 2 36 ? 16.190 33.599 24.746 1.00 20.33  ? 36 LYS D O   1 
ATOM 1445 C CB  . LYS D 2 36 ? 13.042 33.245 26.099 1.00 35.43  ? 36 LYS D CB  1 
ATOM 1446 C CG  . LYS D 2 36 ? 13.576 31.990 26.741 1.00 37.52  ? 36 LYS D CG  1 
ATOM 1447 C CD  . LYS D 2 36 ? 12.769 31.708 28.021 1.00 45.17  ? 36 LYS D CD  1 
ATOM 1448 C CE  . LYS D 2 36 ? 11.249 31.408 27.907 1.00 46.58  ? 36 LYS D CE  1 
ATOM 1449 N NZ  . LYS D 2 36 ? 10.936 30.209 27.159 1.00 46.94  ? 36 LYS D NZ  1 
ATOM 1450 N N   . VAL D 2 37 ? 15.834 34.527 26.763 1.00 26.69  ? 37 VAL D N   1 
ATOM 1451 C CA  . VAL D 2 37 ? 17.147 34.274 27.280 1.00 30.94  ? 37 VAL D CA  1 
ATOM 1452 C C   . VAL D 2 37 ? 16.917 33.279 28.404 1.00 41.11  ? 37 VAL D C   1 
ATOM 1453 O O   . VAL D 2 37 ? 15.957 33.409 29.179 1.00 40.91  ? 37 VAL D O   1 
ATOM 1454 C CB  . VAL D 2 37 ? 17.794 35.562 27.824 1.00 21.76  ? 37 VAL D CB  1 
ATOM 1455 C CG1 . VAL D 2 37 ? 19.080 35.310 28.599 1.00 11.42  ? 37 VAL D CG1 1 
ATOM 1456 C CG2 . VAL D 2 37 ? 18.142 36.415 26.607 1.00 23.65  ? 37 VAL D CG2 1 
ATOM 1457 N N   . ILE D 2 38 ? 17.796 32.280 28.466 1.00 44.99  ? 38 ILE D N   1 
ATOM 1458 C CA  . ILE D 2 38 ? 17.729 31.245 29.473 1.00 42.81  ? 38 ILE D CA  1 
ATOM 1459 C C   . ILE D 2 38 ? 19.077 31.278 30.200 1.00 46.55  ? 38 ILE D C   1 
ATOM 1460 O O   . ILE D 2 38 ? 20.080 31.709 29.584 1.00 48.82  ? 38 ILE D O   1 
ATOM 1461 C CB  . ILE D 2 38 ? 17.511 29.764 28.877 1.00 38.31  ? 38 ILE D CB  1 
ATOM 1462 C CG1 . ILE D 2 38 ? 18.679 29.313 27.994 1.00 24.86  ? 38 ILE D CG1 1 
ATOM 1463 C CG2 . ILE D 2 38 ? 16.140 29.737 28.189 1.00 39.71  ? 38 ILE D CG2 1 
ATOM 1464 C CD1 . ILE D 2 38 ? 18.358 29.227 26.506 1.00 22.92  ? 38 ILE D CD1 1 
ATOM 1465 N N   . ARG D 2 39 ? 19.032 30.777 31.466 1.00 42.42  ? 39 ARG D N   1 
ATOM 1466 C CA  . ARG D 2 39 ? 20.164 30.650 32.359 1.00 33.57  ? 39 ARG D CA  1 
ATOM 1467 C C   . ARG D 2 39 ? 21.229 29.704 31.768 1.00 40.51  ? 39 ARG D C   1 
ATOM 1468 O O   . ARG D 2 39 ? 20.948 28.840 30.927 1.00 45.52  ? 39 ARG D O   1 
ATOM 1469 C CB  . ARG D 2 39 ? 19.697 30.105 33.701 1.00 39.73  ? 39 ARG D CB  1 
ATOM 1470 C CG  . ARG D 2 39 ? 18.362 30.610 34.254 1.00 53.25  ? 39 ARG D CG  1 
ATOM 1471 C CD  . ARG D 2 39 ? 17.961 30.053 35.663 1.00 58.35  ? 39 ARG D CD  1 
ATOM 1472 N NE  . ARG D 2 39 ? 16.584 30.427 36.050 1.00 58.23  ? 39 ARG D NE  1 
ATOM 1473 C CZ  . ARG D 2 39 ? 16.266 31.467 36.853 1.00 55.54  ? 39 ARG D CZ  1 
ATOM 1474 N NH1 . ARG D 2 39 ? 17.193 32.237 37.441 1.00 50.06  ? 39 ARG D NH1 1 
ATOM 1475 N NH2 . ARG D 2 39 ? 14.971 31.737 37.056 1.00 53.82  ? 39 ARG D NH2 1 
ATOM 1476 N N   . PRO D 2 40 ? 22.502 29.803 32.142 1.00 40.05  ? 40 PRO D N   1 
ATOM 1477 C CA  . PRO D 2 40 ? 22.973 30.795 33.074 1.00 42.25  ? 40 PRO D CA  1 
ATOM 1478 C C   . PRO D 2 40 ? 23.247 32.101 32.285 1.00 40.50  ? 40 PRO D C   1 
ATOM 1479 O O   . PRO D 2 40 ? 23.330 32.053 31.034 1.00 33.28  ? 40 PRO D O   1 
ATOM 1480 C CB  . PRO D 2 40 ? 24.164 30.027 33.697 1.00 39.06  ? 40 PRO D CB  1 
ATOM 1481 C CG  . PRO D 2 40 ? 24.778 29.332 32.523 1.00 37.17  ? 40 PRO D CG  1 
ATOM 1482 C CD  . PRO D 2 40 ? 23.544 28.828 31.811 1.00 38.59  ? 40 PRO D CD  1 
ATOM 1483 N N   . CYS D 2 41 ? 23.227 33.285 32.931 1.00 33.62  ? 41 CYS D N   1 
ATOM 1484 C CA  . CYS D 2 41 ? 23.760 34.377 32.157 1.00 34.36  ? 41 CYS D CA  1 
ATOM 1485 C C   . CYS D 2 41 ? 25.065 34.719 32.845 1.00 25.82  ? 41 CYS D C   1 
ATOM 1486 O O   . CYS D 2 41 ? 25.193 34.584 34.065 1.00 24.29  ? 41 CYS D O   1 
ATOM 1487 C CB  . CYS D 2 41 ? 22.764 35.545 32.131 1.00 39.84  ? 41 CYS D CB  1 
ATOM 1488 S SG  . CYS D 2 41 ? 23.092 36.871 30.917 1.00 34.27  ? 41 CYS D SG  1 
ATOM 1489 N N   . MET D 2 42 ? 26.038 35.202 32.111 1.00 26.13  ? 42 MET D N   1 
ATOM 1490 C CA  . MET D 2 42 ? 27.357 35.358 32.653 1.00 34.90  ? 42 MET D CA  1 
ATOM 1491 C C   . MET D 2 42 ? 27.862 36.767 32.311 1.00 38.32  ? 42 MET D C   1 
ATOM 1492 O O   . MET D 2 42 ? 27.844 37.195 31.144 1.00 38.09  ? 42 MET D O   1 
ATOM 1493 C CB  . MET D 2 42 ? 28.057 34.190 31.999 1.00 44.25  ? 42 MET D CB  1 
ATOM 1494 C CG  . MET D 2 42 ? 29.475 33.760 32.288 1.00 48.89  ? 42 MET D CG  1 
ATOM 1495 S SD  . MET D 2 42 ? 29.575 32.639 33.692 1.00 53.26  ? 42 MET D SD  1 
ATOM 1496 C CE  . MET D 2 42 ? 30.949 33.350 34.563 1.00 41.83  ? 42 MET D CE  1 
ATOM 1497 N N   . LYS D 2 43 ? 28.249 37.521 33.331 1.00 37.79  ? 43 LYS D N   1 
ATOM 1498 C CA  . LYS D 2 43 ? 28.707 38.869 33.149 1.00 39.32  ? 43 LYS D CA  1 
ATOM 1499 C C   . LYS D 2 43 ? 30.103 38.966 33.734 1.00 41.93  ? 43 LYS D C   1 
ATOM 1500 O O   . LYS D 2 43 ? 30.361 38.530 34.865 1.00 41.38  ? 43 LYS D O   1 
ATOM 1501 C CB  . LYS D 2 43 ? 27.688 39.816 33.836 1.00 41.86  ? 43 LYS D CB  1 
ATOM 1502 C CG  . LYS D 2 43 ? 27.977 40.660 35.113 1.00 44.93  ? 43 LYS D CG  1 
ATOM 1503 C CD  . LYS D 2 43 ? 28.237 42.143 34.827 1.00 49.71  ? 43 LYS D CD  1 
ATOM 1504 C CE  . LYS D 2 43 ? 28.211 43.003 36.075 1.00 51.10  ? 43 LYS D CE  1 
ATOM 1505 N NZ  . LYS D 2 43 ? 26.845 43.105 36.587 1.00 60.07  ? 43 LYS D NZ  1 
ATOM 1506 N N   . LYS D 2 44 ? 31.028 39.455 32.925 1.00 42.81  ? 44 LYS D N   1 
ATOM 1507 C CA  . LYS D 2 44 ? 32.408 39.609 33.327 1.00 44.02  ? 44 LYS D CA  1 
ATOM 1508 C C   . LYS D 2 44 ? 32.648 41.072 33.376 1.00 45.75  ? 44 LYS D C   1 
ATOM 1509 O O   . LYS D 2 44 ? 32.206 41.757 32.456 1.00 52.28  ? 44 LYS D O   1 
ATOM 1510 C CB  . LYS D 2 44 ? 33.386 39.045 32.299 1.00 48.29  ? 44 LYS D CB  1 
ATOM 1511 C CG  . LYS D 2 44 ? 34.892 39.290 32.534 1.00 46.76  ? 44 LYS D CG  1 
ATOM 1512 C CD  . LYS D 2 44 ? 35.660 38.634 31.418 1.00 46.36  ? 44 LYS D CD  1 
ATOM 1513 C CE  . LYS D 2 44 ? 36.561 39.471 30.567 1.00 45.13  ? 44 LYS D CE  1 
ATOM 1514 N NZ  . LYS D 2 44 ? 37.868 39.514 31.165 1.00 40.44  ? 44 LYS D NZ  1 
ATOM 1515 N N   . THR D 2 45 ? 33.376 41.528 34.375 1.00 51.46  ? 45 THR D N   1 
ATOM 1516 C CA  . THR D 2 45 ? 33.738 42.934 34.510 1.00 53.35  ? 45 THR D CA  1 
ATOM 1517 C C   . THR D 2 45 ? 35.240 43.103 34.179 1.00 53.81  ? 45 THR D C   1 
ATOM 1518 O O   . THR D 2 45 ? 36.119 42.331 34.632 1.00 50.78  ? 45 THR D O   1 
ATOM 1519 C CB  . THR D 2 45 ? 33.377 43.372 35.969 1.00 54.78  ? 45 THR D CB  1 
ATOM 1520 O OG1 . THR D 2 45 ? 32.037 42.951 36.325 1.00 54.02  ? 45 THR D OG1 1 
ATOM 1521 C CG2 . THR D 2 45 ? 33.508 44.877 36.063 1.00 50.86  ? 45 THR D CG2 1 
ATOM 1522 N N   . ILE D 2 46 ? 35.563 44.080 33.339 1.00 52.47  ? 46 ILE D N   1 
ATOM 1523 C CA  . ILE D 2 46 ? 36.914 44.259 32.837 1.00 52.64  ? 46 ILE D CA  1 
ATOM 1524 C C   . ILE D 2 46 ? 37.590 45.361 33.606 1.00 55.12  ? 46 ILE D C   1 
ATOM 1525 O O   . ILE D 2 46 ? 36.847 46.237 34.029 1.00 57.19  ? 46 ILE D O   1 
ATOM 1526 C CB  . ILE D 2 46 ? 36.779 44.571 31.352 1.00 51.70  ? 46 ILE D CB  1 
ATOM 1527 C CG1 . ILE D 2 46 ? 36.137 43.347 30.726 1.00 50.01  ? 46 ILE D CG1 1 
ATOM 1528 C CG2 . ILE D 2 46 ? 38.109 44.975 30.735 1.00 53.81  ? 46 ILE D CG2 1 
ATOM 1529 C CD1 . ILE D 2 46 ? 36.443 42.990 29.255 1.00 55.77  ? 46 ILE D CD1 1 
ATOM 1530 N N   . TYR D 2 47 ? 38.926 45.424 33.773 1.00 60.53  ? 47 TYR D N   1 
ATOM 1531 C CA  . TYR D 2 47 ? 39.480 46.447 34.656 1.00 65.06  ? 47 TYR D CA  1 
ATOM 1532 C C   . TYR D 2 47 ? 40.630 47.413 34.262 1.00 74.22  ? 47 TYR D C   1 
ATOM 1533 O O   . TYR D 2 47 ? 40.592 48.530 34.802 1.00 79.95  ? 47 TYR D O   1 
ATOM 1534 C CB  . TYR D 2 47 ? 39.854 45.749 35.988 1.00 58.58  ? 47 TYR D CB  1 
ATOM 1535 C CG  . TYR D 2 47 ? 38.728 45.724 37.036 1.00 55.52  ? 47 TYR D CG  1 
ATOM 1536 C CD1 . TYR D 2 47 ? 37.460 45.315 36.689 1.00 51.94  ? 47 TYR D CD1 1 
ATOM 1537 C CD2 . TYR D 2 47 ? 38.941 46.123 38.351 1.00 57.53  ? 47 TYR D CD2 1 
ATOM 1538 C CE1 . TYR D 2 47 ? 36.412 45.318 37.578 1.00 49.83  ? 47 TYR D CE1 1 
ATOM 1539 C CE2 . TYR D 2 47 ? 37.878 46.128 39.258 1.00 56.75  ? 47 TYR D CE2 1 
ATOM 1540 C CZ  . TYR D 2 47 ? 36.612 45.711 38.864 1.00 51.28  ? 47 TYR D CZ  1 
ATOM 1541 O OH  . TYR D 2 47 ? 35.519 45.712 39.720 1.00 52.35  ? 47 TYR D OH  1 
ATOM 1542 N N   . GLU D 2 48 ? 41.614 47.189 33.361 1.00 80.58  ? 48 GLU D N   1 
ATOM 1543 C CA  . GLU D 2 48 ? 42.706 48.177 33.235 1.00 89.32  ? 48 GLU D CA  1 
ATOM 1544 C C   . GLU D 2 48 ? 43.449 47.952 31.939 1.00 91.81  ? 48 GLU D C   1 
ATOM 1545 O O   . GLU D 2 48 ? 44.571 47.449 31.875 1.00 92.71  ? 48 GLU D O   1 
ATOM 1546 C CB  . GLU D 2 48 ? 43.705 48.061 34.431 1.00 92.95  ? 48 GLU D CB  1 
ATOM 1547 C CG  . GLU D 2 48 ? 44.299 49.376 34.984 1.00 96.51  ? 48 GLU D CG  1 
ATOM 1548 C CD  . GLU D 2 48 ? 45.489 49.998 34.251 1.00 100.59 ? 48 GLU D CD  1 
ATOM 1549 O OE1 . GLU D 2 48 ? 45.431 50.203 33.033 1.00 103.59 ? 48 GLU D OE1 1 
ATOM 1550 O OE2 . GLU D 2 48 ? 46.482 50.294 34.919 1.00 101.02 ? 48 GLU D OE2 1 
ATOM 1551 N N   . ASN D 2 49 ? 42.807 48.375 30.877 1.00 95.56  ? 49 ASN D N   1 
ATOM 1552 C CA  . ASN D 2 49 ? 43.267 48.032 29.547 1.00 100.33 ? 49 ASN D CA  1 
ATOM 1553 C C   . ASN D 2 49 ? 44.258 49.009 28.948 1.00 99.29  ? 49 ASN D C   1 
ATOM 1554 O O   . ASN D 2 49 ? 44.798 49.876 29.648 1.00 95.92  ? 49 ASN D O   1 
ATOM 1555 C CB  . ASN D 2 49 ? 42.011 47.897 28.674 1.00 107.11 ? 49 ASN D CB  1 
ATOM 1556 C CG  . ASN D 2 49 ? 41.048 46.806 29.160 1.00 111.89 ? 49 ASN D CG  1 
ATOM 1557 O OD1 . ASN D 2 49 ? 40.799 46.595 30.365 1.00 111.97 ? 49 ASN D OD1 1 
ATOM 1558 N ND2 . ASN D 2 49 ? 40.466 46.074 28.214 1.00 113.78 ? 49 ASN D ND2 1 
ATOM 1559 N N   . GLU D 2 50 ? 44.577 48.745 27.680 1.00 100.30 ? 50 GLU D N   1 
ATOM 1560 C CA  . GLU D 2 50 ? 45.268 49.689 26.822 1.00 103.73 ? 50 GLU D CA  1 
ATOM 1561 C C   . GLU D 2 50 ? 44.348 49.940 25.597 1.00 105.43 ? 50 GLU D C   1 
ATOM 1562 O O   . GLU D 2 50 ? 43.213 49.437 25.596 1.00 106.71 ? 50 GLU D O   1 
ATOM 1563 C CB  . GLU D 2 50 ? 46.626 49.141 26.335 1.00 100.70 ? 50 GLU D CB  1 
ATOM 1564 C CG  . GLU D 2 50 ? 47.658 48.861 27.405 1.00 98.64  ? 50 GLU D CG  1 
ATOM 1565 C CD  . GLU D 2 50 ? 47.358 47.563 28.101 1.00 98.65  ? 50 GLU D CD  1 
ATOM 1566 O OE1 . GLU D 2 50 ? 47.337 46.536 27.429 1.00 97.97  ? 50 GLU D OE1 1 
ATOM 1567 O OE2 . GLU D 2 50 ? 47.117 47.591 29.303 1.00 102.27 ? 50 GLU D OE2 1 
ATOM 1568 O OXT . GLU D 2 50 ? 44.746 50.641 24.659 1.00 106.80 ? 50 GLU D OXT 1 
ATOM 1569 N N   . ARG E 1 1  ? -0.521 74.397 55.404 1.00 96.63  ? 2  ARG E N   1 
ATOM 1570 C CA  . ARG E 1 1  ? -1.574 73.401 55.678 1.00 96.15  ? 2  ARG E CA  1 
ATOM 1571 C C   . ARG E 1 1  ? -2.261 73.107 54.351 1.00 89.81  ? 2  ARG E C   1 
ATOM 1572 O O   . ARG E 1 1  ? -2.801 72.023 54.166 1.00 88.18  ? 2  ARG E O   1 
ATOM 1573 C CB  . ARG E 1 1  ? -2.708 73.880 56.643 1.00 98.31  ? 2  ARG E CB  1 
ATOM 1574 C CG  . ARG E 1 1  ? -3.457 72.881 57.535 1.00 97.52  ? 2  ARG E CG  1 
ATOM 1575 C CD  . ARG E 1 1  ? -3.003 72.945 59.011 1.00 103.21 ? 2  ARG E CD  1 
ATOM 1576 N NE  . ARG E 1 1  ? -3.460 74.135 59.730 1.00 105.39 ? 2  ARG E NE  1 
ATOM 1577 C CZ  . ARG E 1 1  ? -3.521 74.258 61.084 1.00 107.81 ? 2  ARG E CZ  1 
ATOM 1578 N NH1 . ARG E 1 1  ? -3.182 73.306 61.968 1.00 109.16 ? 2  ARG E NH1 1 
ATOM 1579 N NH2 . ARG E 1 1  ? -3.900 75.420 61.629 1.00 106.57 ? 2  ARG E NH2 1 
ATOM 1580 N N   . GLU E 1 2  ? -2.323 74.086 53.442 1.00 82.63  ? 3  GLU E N   1 
ATOM 1581 C CA  . GLU E 1 2  ? -2.846 73.829 52.137 1.00 73.82  ? 3  GLU E CA  1 
ATOM 1582 C C   . GLU E 1 2  ? -1.631 74.033 51.274 1.00 68.52  ? 3  GLU E C   1 
ATOM 1583 O O   . GLU E 1 2  ? -1.327 75.154 50.879 1.00 73.85  ? 3  GLU E O   1 
ATOM 1584 C CB  . GLU E 1 2  ? -3.989 74.805 51.871 1.00 75.03  ? 3  GLU E CB  1 
ATOM 1585 C CG  . GLU E 1 2  ? -5.125 74.416 52.842 1.00 80.16  ? 3  GLU E CG  1 
ATOM 1586 C CD  . GLU E 1 2  ? -6.569 74.820 52.523 1.00 83.56  ? 3  GLU E CD  1 
ATOM 1587 O OE1 . GLU E 1 2  ? -6.929 75.957 52.832 1.00 87.60  ? 3  GLU E OE1 1 
ATOM 1588 O OE2 . GLU E 1 2  ? -7.342 74.002 52.000 1.00 81.66  ? 3  GLU E OE2 1 
ATOM 1589 N N   . ILE E 1 3  ? -0.791 73.001 51.427 1.00 60.98  ? 4  ILE E N   1 
ATOM 1590 C CA  . ILE E 1 3  ? 0.361  72.661 50.589 1.00 47.45  ? 4  ILE E CA  1 
ATOM 1591 C C   . ILE E 1 3  ? 0.110  71.145 50.461 1.00 44.58  ? 4  ILE E C   1 
ATOM 1592 O O   . ILE E 1 3  ? -0.226 70.551 51.504 1.00 43.42  ? 4  ILE E O   1 
ATOM 1593 C CB  . ILE E 1 3  ? 1.786  72.752 51.200 1.00 38.66  ? 4  ILE E CB  1 
ATOM 1594 C CG1 . ILE E 1 3  ? 2.224  74.088 51.727 1.00 41.11  ? 4  ILE E CG1 1 
ATOM 1595 C CG2 . ILE E 1 3  ? 2.706  72.400 50.029 1.00 35.37  ? 4  ILE E CG2 1 
ATOM 1596 C CD1 . ILE E 1 3  ? 3.759  74.216 51.938 1.00 30.62  ? 4  ILE E CD1 1 
ATOM 1597 N N   . LYS E 1 4  ? 0.160  70.578 49.236 1.00 37.28  ? 5  LYS E N   1 
ATOM 1598 C CA  . LYS E 1 4  ? -0.030 69.173 49.064 1.00 35.86  ? 5  LYS E CA  1 
ATOM 1599 C C   . LYS E 1 4  ? 1.278  68.354 49.027 1.00 34.77  ? 5  LYS E C   1 
ATOM 1600 O O   . LYS E 1 4  ? 1.344  67.345 49.736 1.00 38.03  ? 5  LYS E O   1 
ATOM 1601 C CB  . LYS E 1 4  ? -0.907 69.022 47.839 1.00 40.05  ? 5  LYS E CB  1 
ATOM 1602 C CG  . LYS E 1 4  ? -2.324 69.198 48.394 1.00 48.25  ? 5  LYS E CG  1 
ATOM 1603 C CD  . LYS E 1 4  ? -3.535 68.732 47.562 1.00 53.67  ? 5  LYS E CD  1 
ATOM 1604 C CE  . LYS E 1 4  ? -4.855 68.744 48.358 1.00 55.89  ? 5  LYS E CE  1 
ATOM 1605 N NZ  . LYS E 1 4  ? -5.111 70.051 48.965 1.00 61.88  ? 5  LYS E NZ  1 
ATOM 1606 N N   . GLY E 1 5  ? 2.374  68.723 48.366 1.00 25.25  ? 6  GLY E N   1 
ATOM 1607 C CA  . GLY E 1 5  ? 3.601  67.957 48.423 1.00 25.36  ? 6  GLY E CA  1 
ATOM 1608 C C   . GLY E 1 5  ? 4.780  68.725 47.787 1.00 31.29  ? 6  GLY E C   1 
ATOM 1609 O O   . GLY E 1 5  ? 4.687  69.955 47.621 1.00 29.07  ? 6  GLY E O   1 
ATOM 1610 N N   . TYR E 1 6  ? 5.907  68.037 47.474 1.00 25.48  ? 7  TYR E N   1 
ATOM 1611 C CA  . TYR E 1 6  ? 7.017  68.598 46.711 1.00 22.80  ? 7  TYR E CA  1 
ATOM 1612 C C   . TYR E 1 6  ? 7.394  67.727 45.501 1.00 23.80  ? 7  TYR E C   1 
ATOM 1613 O O   . TYR E 1 6  ? 6.799  66.669 45.221 1.00 17.12  ? 7  TYR E O   1 
ATOM 1614 C CB  . TYR E 1 6  ? 8.246  68.758 47.559 1.00 26.62  ? 7  TYR E CB  1 
ATOM 1615 C CG  . TYR E 1 6  ? 7.868  69.584 48.753 1.00 36.34  ? 7  TYR E CG  1 
ATOM 1616 C CD1 . TYR E 1 6  ? 7.841  70.963 48.718 1.00 35.45  ? 7  TYR E CD1 1 
ATOM 1617 C CD2 . TYR E 1 6  ? 7.454  68.909 49.874 1.00 43.41  ? 7  TYR E CD2 1 
ATOM 1618 C CE1 . TYR E 1 6  ? 7.374  71.662 49.815 1.00 32.14  ? 7  TYR E CE1 1 
ATOM 1619 C CE2 . TYR E 1 6  ? 6.982  69.608 50.968 1.00 41.66  ? 7  TYR E CE2 1 
ATOM 1620 C CZ  . TYR E 1 6  ? 6.945  70.974 50.927 1.00 33.27  ? 7  TYR E CZ  1 
ATOM 1621 O OH  . TYR E 1 6  ? 6.427  71.619 52.027 1.00 38.08  ? 7  TYR E OH  1 
ATOM 1622 N N   . GLU E 1 7  ? 8.319  68.235 44.701 1.00 17.37  ? 8  GLU E N   1 
ATOM 1623 C CA  . GLU E 1 7  ? 8.895  67.525 43.597 1.00 25.19  ? 8  GLU E CA  1 
ATOM 1624 C C   . GLU E 1 7  ? 10.337 67.963 43.459 1.00 35.29  ? 8  GLU E C   1 
ATOM 1625 O O   . GLU E 1 7  ? 10.739 69.112 43.737 1.00 36.87  ? 8  GLU E O   1 
ATOM 1626 C CB  . GLU E 1 7  ? 8.200  67.787 42.301 1.00 26.54  ? 8  GLU E CB  1 
ATOM 1627 C CG  . GLU E 1 7  ? 7.274  66.602 42.234 1.00 39.86  ? 8  GLU E CG  1 
ATOM 1628 C CD  . GLU E 1 7  ? 6.625  66.309 40.885 1.00 46.60  ? 8  GLU E CD  1 
ATOM 1629 O OE1 . GLU E 1 7  ? 7.342  66.351 39.876 1.00 52.65  ? 8  GLU E OE1 1 
ATOM 1630 O OE2 . GLU E 1 7  ? 5.414  66.036 40.855 1.00 42.15  ? 8  GLU E OE2 1 
ATOM 1631 N N   . TYR E 1 8  ? 11.164 66.983 43.160 1.00 37.58  ? 9  TYR E N   1 
ATOM 1632 C CA  . TYR E 1 8  ? 12.568 67.241 43.075 1.00 32.78  ? 9  TYR E CA  1 
ATOM 1633 C C   . TYR E 1 8  ? 12.943 66.737 41.693 1.00 34.22  ? 9  TYR E C   1 
ATOM 1634 O O   . TYR E 1 8  ? 12.351 65.792 41.169 1.00 32.11  ? 9  TYR E O   1 
ATOM 1635 C CB  . TYR E 1 8  ? 13.269 66.494 44.252 1.00 32.56  ? 9  TYR E CB  1 
ATOM 1636 C CG  . TYR E 1 8  ? 12.804 66.932 45.654 1.00 32.94  ? 9  TYR E CG  1 
ATOM 1637 C CD1 . TYR E 1 8  ? 13.371 68.059 46.253 1.00 34.03  ? 9  TYR E CD1 1 
ATOM 1638 C CD2 . TYR E 1 8  ? 11.735 66.280 46.278 1.00 28.69  ? 9  TYR E CD2 1 
ATOM 1639 C CE1 . TYR E 1 8  ? 12.860 68.541 47.453 1.00 35.30  ? 9  TYR E CE1 1 
ATOM 1640 C CE2 . TYR E 1 8  ? 11.218 66.756 47.477 1.00 29.88  ? 9  TYR E CE2 1 
ATOM 1641 C CZ  . TYR E 1 8  ? 11.780 67.895 48.062 1.00 34.79  ? 9  TYR E CZ  1 
ATOM 1642 O OH  . TYR E 1 8  ? 11.246 68.426 49.234 1.00 27.86  ? 9  TYR E OH  1 
ATOM 1643 N N   . GLN E 1 9  ? 13.815 67.476 41.034 1.00 33.98  ? 10 GLN E N   1 
ATOM 1644 C CA  . GLN E 1 9  ? 14.348 67.143 39.745 1.00 31.26  ? 10 GLN E CA  1 
ATOM 1645 C C   . GLN E 1 9  ? 15.834 67.239 39.969 1.00 32.45  ? 10 GLN E C   1 
ATOM 1646 O O   . GLN E 1 9  ? 16.287 68.347 40.291 1.00 32.84  ? 10 GLN E O   1 
ATOM 1647 C CB  . GLN E 1 9  ? 13.948 68.153 38.700 1.00 32.28  ? 10 GLN E CB  1 
ATOM 1648 C CG  . GLN E 1 9  ? 12.440 68.298 38.590 1.00 38.14  ? 10 GLN E CG  1 
ATOM 1649 C CD  . GLN E 1 9  ? 11.921 68.815 37.249 1.00 44.29  ? 10 GLN E CD  1 
ATOM 1650 O OE1 . GLN E 1 9  ? 12.623 69.397 36.401 1.00 39.51  ? 10 GLN E OE1 1 
ATOM 1651 N NE2 . GLN E 1 9  ? 10.615 68.586 37.069 1.00 44.57  ? 10 GLN E NE2 1 
ATOM 1652 N N   . LEU E 1 10 ? 16.579 66.118 39.878 1.00 34.80  ? 11 LEU E N   1 
ATOM 1653 C CA  . LEU E 1 10 ? 17.996 66.098 40.227 1.00 31.86  ? 11 LEU E CA  1 
ATOM 1654 C C   . LEU E 1 10 ? 18.865 65.529 39.131 1.00 27.83  ? 11 LEU E C   1 
ATOM 1655 O O   . LEU E 1 10 ? 18.408 64.786 38.254 1.00 27.26  ? 11 LEU E O   1 
ATOM 1656 C CB  . LEU E 1 10 ? 18.338 65.203 41.429 1.00 37.77  ? 11 LEU E CB  1 
ATOM 1657 C CG  . LEU E 1 10 ? 17.889 65.139 42.891 1.00 36.60  ? 11 LEU E CG  1 
ATOM 1658 C CD1 . LEU E 1 10 ? 16.391 65.141 43.004 1.00 33.69  ? 11 LEU E CD1 1 
ATOM 1659 C CD2 . LEU E 1 10 ? 18.421 63.847 43.491 1.00 34.46  ? 11 LEU E CD2 1 
ATOM 1660 N N   . TYR E 1 11 ? 20.152 65.770 39.313 1.00 26.08  ? 12 TYR E N   1 
ATOM 1661 C CA  . TYR E 1 11 ? 21.222 65.203 38.515 1.00 30.63  ? 12 TYR E CA  1 
ATOM 1662 C C   . TYR E 1 11 ? 22.080 64.342 39.438 1.00 31.24  ? 12 TYR E C   1 
ATOM 1663 O O   . TYR E 1 11 ? 23.038 64.886 40.021 1.00 35.02  ? 12 TYR E O   1 
ATOM 1664 C CB  . TYR E 1 11 ? 22.107 66.291 37.957 1.00 37.09  ? 12 TYR E CB  1 
ATOM 1665 C CG  . TYR E 1 11 ? 21.457 67.034 36.844 1.00 46.32  ? 12 TYR E CG  1 
ATOM 1666 C CD1 . TYR E 1 11 ? 21.285 66.398 35.643 1.00 52.03  ? 12 TYR E CD1 1 
ATOM 1667 C CD2 . TYR E 1 11 ? 21.052 68.324 37.023 1.00 50.64  ? 12 TYR E CD2 1 
ATOM 1668 C CE1 . TYR E 1 11 ? 20.710 67.053 34.585 1.00 57.95  ? 12 TYR E CE1 1 
ATOM 1669 C CE2 . TYR E 1 11 ? 20.464 68.986 35.965 1.00 57.90  ? 12 TYR E CE2 1 
ATOM 1670 C CZ  . TYR E 1 11 ? 20.296 68.349 34.750 1.00 58.96  ? 12 TYR E CZ  1 
ATOM 1671 O OH  . TYR E 1 11 ? 19.665 68.983 33.689 1.00 64.64  ? 12 TYR E OH  1 
ATOM 1672 N N   . VAL E 1 12 ? 21.770 63.039 39.623 1.00 29.15  ? 13 VAL E N   1 
ATOM 1673 C CA  . VAL E 1 12 ? 22.543 62.129 40.516 1.00 24.59  ? 13 VAL E CA  1 
ATOM 1674 C C   . VAL E 1 12 ? 23.643 61.431 39.739 1.00 31.24  ? 13 VAL E C   1 
ATOM 1675 O O   . VAL E 1 12 ? 23.355 60.791 38.718 1.00 35.91  ? 13 VAL E O   1 
ATOM 1676 C CB  . VAL E 1 12 ? 21.800 60.910 41.104 1.00 19.66  ? 13 VAL E CB  1 
ATOM 1677 C CG1 . VAL E 1 12 ? 22.738 60.458 42.214 1.00 5.22   ? 13 VAL E CG1 1 
ATOM 1678 C CG2 . VAL E 1 12 ? 20.318 61.150 41.475 1.00 16.05  ? 13 VAL E CG2 1 
ATOM 1679 N N   . TYR E 1 13 ? 24.879 61.589 40.184 1.00 37.94  ? 14 TYR E N   1 
ATOM 1680 C CA  . TYR E 1 13 ? 25.992 60.755 39.751 1.00 44.58  ? 14 TYR E CA  1 
ATOM 1681 C C   . TYR E 1 13 ? 25.835 59.396 40.459 1.00 52.11  ? 14 TYR E C   1 
ATOM 1682 O O   . TYR E 1 13 ? 25.818 59.308 41.710 1.00 50.32  ? 14 TYR E O   1 
ATOM 1683 C CB  . TYR E 1 13 ? 27.343 61.343 40.157 1.00 37.66  ? 14 TYR E CB  1 
ATOM 1684 C CG  . TYR E 1 13 ? 27.934 62.237 39.100 1.00 35.92  ? 14 TYR E CG  1 
ATOM 1685 C CD1 . TYR E 1 13 ? 28.047 61.776 37.800 1.00 40.72  ? 14 TYR E CD1 1 
ATOM 1686 C CD2 . TYR E 1 13 ? 28.423 63.468 39.453 1.00 35.94  ? 14 TYR E CD2 1 
ATOM 1687 C CE1 . TYR E 1 13 ? 28.662 62.544 36.834 1.00 41.54  ? 14 TYR E CE1 1 
ATOM 1688 C CE2 . TYR E 1 13 ? 29.043 64.253 38.500 1.00 40.30  ? 14 TYR E CE2 1 
ATOM 1689 C CZ  . TYR E 1 13 ? 29.159 63.781 37.197 1.00 42.44  ? 14 TYR E CZ  1 
ATOM 1690 O OH  . TYR E 1 13 ? 29.810 64.543 36.244 1.00 44.38  ? 14 TYR E OH  1 
ATOM 1691 N N   . ALA E 1 14 ? 25.631 58.361 39.641 1.00 54.16  ? 15 ALA E N   1 
ATOM 1692 C CA  . ALA E 1 14 ? 25.443 56.973 40.044 1.00 50.13  ? 15 ALA E CA  1 
ATOM 1693 C C   . ALA E 1 14 ? 26.415 56.259 39.142 1.00 52.32  ? 15 ALA E C   1 
ATOM 1694 O O   . ALA E 1 14 ? 26.450 56.566 37.942 1.00 44.35  ? 15 ALA E O   1 
ATOM 1695 C CB  . ALA E 1 14 ? 24.054 56.438 39.717 1.00 38.88  ? 15 ALA E CB  1 
ATOM 1696 N N   . SER E 1 15 ? 27.283 55.440 39.757 1.00 54.53  ? 16 SER E N   1 
ATOM 1697 C CA  . SER E 1 15 ? 28.312 54.626 39.101 1.00 50.53  ? 16 SER E CA  1 
ATOM 1698 C C   . SER E 1 15 ? 29.087 55.373 38.028 1.00 50.69  ? 16 SER E C   1 
ATOM 1699 O O   . SER E 1 15 ? 29.447 54.798 36.999 1.00 47.38  ? 16 SER E O   1 
ATOM 1700 C CB  . SER E 1 15 ? 27.709 53.352 38.459 1.00 49.28  ? 16 SER E CB  1 
ATOM 1701 O OG  . SER E 1 15 ? 26.966 52.530 39.362 1.00 49.23  ? 16 SER E OG  1 
ATOM 1702 N N   . ASP E 1 16 ? 29.409 56.636 38.350 1.00 48.88  ? 17 ASP E N   1 
ATOM 1703 C CA  . ASP E 1 16 ? 30.187 57.525 37.508 1.00 47.69  ? 17 ASP E CA  1 
ATOM 1704 C C   . ASP E 1 16 ? 29.493 57.889 36.196 1.00 48.93  ? 17 ASP E C   1 
ATOM 1705 O O   . ASP E 1 16 ? 30.070 58.271 35.176 1.00 46.34  ? 17 ASP E O   1 
ATOM 1706 C CB  . ASP E 1 16 ? 31.553 56.864 37.286 1.00 50.05  ? 17 ASP E CB  1 
ATOM 1707 C CG  . ASP E 1 16 ? 32.263 56.542 38.603 1.00 54.39  ? 17 ASP E CG  1 
ATOM 1708 O OD1 . ASP E 1 16 ? 31.664 55.910 39.492 1.00 50.76  ? 17 ASP E OD1 1 
ATOM 1709 O OD2 . ASP E 1 16 ? 33.427 56.941 38.736 1.00 57.47  ? 17 ASP E OD2 1 
ATOM 1710 N N   . LYS E 1 17 ? 28.173 57.878 36.252 1.00 53.91  ? 18 LYS E N   1 
ATOM 1711 C CA  . LYS E 1 17 ? 27.343 58.287 35.144 1.00 55.77  ? 18 LYS E CA  1 
ATOM 1712 C C   . LYS E 1 17 ? 26.380 59.322 35.696 1.00 59.06  ? 18 LYS E C   1 
ATOM 1713 O O   . LYS E 1 17 ? 25.976 59.284 36.867 1.00 61.05  ? 18 LYS E O   1 
ATOM 1714 C CB  . LYS E 1 17 ? 26.540 57.142 34.608 1.00 51.51  ? 18 LYS E CB  1 
ATOM 1715 C CG  . LYS E 1 17 ? 27.349 56.127 33.872 1.00 47.72  ? 18 LYS E CG  1 
ATOM 1716 C CD  . LYS E 1 17 ? 26.386 54.978 33.725 1.00 45.04  ? 18 LYS E CD  1 
ATOM 1717 C CE  . LYS E 1 17 ? 27.215 53.793 33.536 1.00 37.27  ? 18 LYS E CE  1 
ATOM 1718 N NZ  . LYS E 1 17 ? 28.051 53.643 34.715 1.00 43.05  ? 18 LYS E NZ  1 
ATOM 1719 N N   . LEU E 1 18 ? 26.049 60.297 34.858 1.00 59.94  ? 19 LEU E N   1 
ATOM 1720 C CA  . LEU E 1 18 ? 25.138 61.343 35.235 1.00 54.26  ? 19 LEU E CA  1 
ATOM 1721 C C   . LEU E 1 18 ? 23.748 60.799 35.009 1.00 50.07  ? 19 LEU E C   1 
ATOM 1722 O O   . LEU E 1 18 ? 23.453 60.313 33.905 1.00 41.19  ? 19 LEU E O   1 
ATOM 1723 C CB  . LEU E 1 18 ? 25.383 62.554 34.353 1.00 59.36  ? 19 LEU E CB  1 
ATOM 1724 C CG  . LEU E 1 18 ? 25.050 63.964 34.816 1.00 61.63  ? 19 LEU E CG  1 
ATOM 1725 C CD1 . LEU E 1 18 ? 24.480 64.011 36.223 1.00 66.68  ? 19 LEU E CD1 1 
ATOM 1726 C CD2 . LEU E 1 18 ? 26.361 64.717 34.892 1.00 66.90  ? 19 LEU E CD2 1 
ATOM 1727 N N   . PHE E 1 19 ? 22.902 60.879 36.022 1.00 46.49  ? 20 PHE E N   1 
ATOM 1728 C CA  . PHE E 1 19 ? 21.540 60.449 35.882 1.00 42.79  ? 20 PHE E CA  1 
ATOM 1729 C C   . PHE E 1 19 ? 20.540 61.539 36.230 1.00 37.69  ? 20 PHE E C   1 
ATOM 1730 O O   . PHE E 1 19 ? 20.840 62.476 36.972 1.00 42.01  ? 20 PHE E O   1 
ATOM 1731 C CB  . PHE E 1 19 ? 21.371 59.218 36.756 1.00 48.65  ? 20 PHE E CB  1 
ATOM 1732 C CG  . PHE E 1 19 ? 21.814 57.997 35.968 1.00 52.79  ? 20 PHE E CG  1 
ATOM 1733 C CD1 . PHE E 1 19 ? 21.059 57.535 34.895 1.00 51.74  ? 20 PHE E CD1 1 
ATOM 1734 C CD2 . PHE E 1 19 ? 22.982 57.371 36.306 1.00 53.94  ? 20 PHE E CD2 1 
ATOM 1735 C CE1 . PHE E 1 19 ? 21.465 56.454 34.149 1.00 49.39  ? 20 PHE E CE1 1 
ATOM 1736 C CE2 . PHE E 1 19 ? 23.381 56.286 35.552 1.00 55.54  ? 20 PHE E CE2 1 
ATOM 1737 C CZ  . PHE E 1 19 ? 22.633 55.827 34.481 1.00 52.49  ? 20 PHE E CZ  1 
ATOM 1738 N N   . ARG E 1 20 ? 19.329 61.470 35.714 1.00 29.49  ? 21 ARG E N   1 
ATOM 1739 C CA  . ARG E 1 20 ? 18.337 62.425 36.068 1.00 25.66  ? 21 ARG E CA  1 
ATOM 1740 C C   . ARG E 1 20 ? 17.196 61.762 36.848 1.00 23.25  ? 21 ARG E C   1 
ATOM 1741 O O   . ARG E 1 20 ? 16.424 60.919 36.368 1.00 13.70  ? 21 ARG E O   1 
ATOM 1742 C CB  . ARG E 1 20 ? 17.897 63.081 34.744 1.00 34.04  ? 21 ARG E CB  1 
ATOM 1743 C CG  . ARG E 1 20 ? 18.356 64.522 34.341 1.00 33.75  ? 21 ARG E CG  1 
ATOM 1744 C CD  . ARG E 1 20 ? 17.655 65.679 35.141 1.00 36.28  ? 21 ARG E CD  1 
ATOM 1745 N NE  . ARG E 1 20 ? 16.237 65.921 34.830 1.00 33.02  ? 21 ARG E NE  1 
ATOM 1746 C CZ  . ARG E 1 20 ? 15.265 65.910 35.756 1.00 26.02  ? 21 ARG E CZ  1 
ATOM 1747 N NH1 . ARG E 1 20 ? 15.520 65.648 37.023 1.00 21.46  ? 21 ARG E NH1 1 
ATOM 1748 N NH2 . ARG E 1 20 ? 14.001 66.120 35.411 1.00 20.27  ? 21 ARG E NH2 1 
ATOM 1749 N N   . ALA E 1 21 ? 17.023 62.163 38.087 1.00 18.95  ? 22 ALA E N   1 
ATOM 1750 C CA  . ALA E 1 21 ? 16.009 61.550 38.896 1.00 21.41  ? 22 ALA E CA  1 
ATOM 1751 C C   . ALA E 1 21 ? 14.890 62.534 39.165 1.00 31.27  ? 22 ALA E C   1 
ATOM 1752 O O   . ALA E 1 21 ? 15.200 63.731 39.269 1.00 40.85  ? 22 ALA E O   1 
ATOM 1753 C CB  . ALA E 1 21 ? 16.615 61.120 40.215 1.00 25.42  ? 22 ALA E CB  1 
ATOM 1754 N N   . ASP E 1 22 ? 13.627 62.065 39.285 1.00 23.31  ? 23 ASP E N   1 
ATOM 1755 C CA  . ASP E 1 22 ? 12.468 62.858 39.629 1.00 17.31  ? 23 ASP E CA  1 
ATOM 1756 C C   . ASP E 1 22 ? 11.712 62.218 40.790 1.00 24.48  ? 23 ASP E C   1 
ATOM 1757 O O   . ASP E 1 22 ? 10.966 61.245 40.617 1.00 24.58  ? 23 ASP E O   1 
ATOM 1758 C CB  . ASP E 1 22 ? 11.537 62.979 38.435 1.00 19.70  ? 23 ASP E CB  1 
ATOM 1759 C CG  . ASP E 1 22 ? 11.924 63.985 37.339 1.00 28.83  ? 23 ASP E CG  1 
ATOM 1760 O OD1 . ASP E 1 22 ? 13.047 64.511 37.342 1.00 24.09  ? 23 ASP E OD1 1 
ATOM 1761 O OD2 . ASP E 1 22 ? 11.094 64.267 36.466 1.00 30.62  ? 23 ASP E OD2 1 
ATOM 1762 N N   . ILE E 1 23 ? 11.862 62.789 41.991 1.00 27.13  ? 24 ILE E N   1 
ATOM 1763 C CA  . ILE E 1 23 ? 11.348 62.257 43.263 1.00 25.31  ? 24 ILE E CA  1 
ATOM 1764 C C   . ILE E 1 23 ? 10.164 63.094 43.771 1.00 27.44  ? 24 ILE E C   1 
ATOM 1765 O O   . ILE E 1 23 ? 10.375 64.302 43.903 1.00 31.85  ? 24 ILE E O   1 
ATOM 1766 C CB  . ILE E 1 23 ? 12.480 62.306 44.311 1.00 20.92  ? 24 ILE E CB  1 
ATOM 1767 C CG1 . ILE E 1 23 ? 13.656 61.499 43.814 1.00 23.54  ? 24 ILE E CG1 1 
ATOM 1768 C CG2 . ILE E 1 23 ? 11.968 61.844 45.654 1.00 19.30  ? 24 ILE E CG2 1 
ATOM 1769 C CD1 . ILE E 1 23 ? 15.002 62.225 44.046 1.00 15.74  ? 24 ILE E CD1 1 
ATOM 1770 N N   . SER E 1 24 ? 8.968  62.545 43.992 1.00 20.08  ? 25 SER E N   1 
ATOM 1771 C CA  . SER E 1 24 ? 7.902  63.254 44.636 1.00 31.81  ? 25 SER E CA  1 
ATOM 1772 C C   . SER E 1 24 ? 8.005  63.013 46.165 1.00 39.95  ? 25 SER E C   1 
ATOM 1773 O O   . SER E 1 24 ? 8.808  62.174 46.589 1.00 45.87  ? 25 SER E O   1 
ATOM 1774 C CB  . SER E 1 24 ? 6.596  62.746 44.074 1.00 31.96  ? 25 SER E CB  1 
ATOM 1775 O OG  . SER E 1 24 ? 6.588  61.327 44.214 1.00 40.40  ? 25 SER E OG  1 
ATOM 1776 N N   . GLU E 1 25 ? 7.208  63.705 47.013 1.00 38.28  ? 26 GLU E N   1 
ATOM 1777 C CA  . GLU E 1 25 ? 7.255  63.655 48.479 1.00 28.07  ? 26 GLU E CA  1 
ATOM 1778 C C   . GLU E 1 25 ? 5.900  64.174 49.088 1.00 30.36  ? 26 GLU E C   1 
ATOM 1779 O O   . GLU E 1 25 ? 5.337  65.170 48.643 1.00 33.02  ? 26 GLU E O   1 
ATOM 1780 C CB  . GLU E 1 25 ? 8.478  64.502 48.880 1.00 14.98  ? 26 GLU E CB  1 
ATOM 1781 C CG  . GLU E 1 25 ? 8.533  64.739 50.366 1.00 31.08  ? 26 GLU E CG  1 
ATOM 1782 C CD  . GLU E 1 25 ? 9.793  65.404 50.934 1.00 42.93  ? 26 GLU E CD  1 
ATOM 1783 O OE1 . GLU E 1 25 ? 10.906 64.990 50.617 1.00 47.77  ? 26 GLU E OE1 1 
ATOM 1784 O OE2 . GLU E 1 25 ? 9.674  66.340 51.734 1.00 51.74  ? 26 GLU E OE2 1 
ATOM 1785 N N   . ASP E 1 26 ? 5.249  63.540 50.056 1.00 27.79  ? 27 ASP E N   1 
ATOM 1786 C CA  . ASP E 1 26 ? 3.994  64.056 50.594 1.00 30.18  ? 27 ASP E CA  1 
ATOM 1787 C C   . ASP E 1 26 ? 4.193  65.222 51.585 1.00 36.18  ? 27 ASP E C   1 
ATOM 1788 O O   . ASP E 1 26 ? 5.208  65.259 52.282 1.00 37.49  ? 27 ASP E O   1 
ATOM 1789 C CB  . ASP E 1 26 ? 3.263  62.942 51.301 1.00 32.07  ? 27 ASP E CB  1 
ATOM 1790 C CG  . ASP E 1 26 ? 1.752  63.137 51.439 1.00 40.32  ? 27 ASP E CG  1 
ATOM 1791 O OD1 . ASP E 1 26 ? 1.019  62.750 50.531 1.00 50.58  ? 27 ASP E OD1 1 
ATOM 1792 O OD2 . ASP E 1 26 ? 1.269  63.621 52.462 1.00 40.50  ? 27 ASP E OD2 1 
ATOM 1793 N N   . TYR E 1 27 ? 3.237  66.181 51.696 1.00 37.08  ? 28 TYR E N   1 
ATOM 1794 C CA  . TYR E 1 27 ? 3.278  67.234 52.719 1.00 34.58  ? 28 TYR E CA  1 
ATOM 1795 C C   . TYR E 1 27 ? 3.016  66.735 54.142 1.00 33.07  ? 28 TYR E C   1 
ATOM 1796 O O   . TYR E 1 27 ? 3.798  67.020 55.054 1.00 30.39  ? 28 TYR E O   1 
ATOM 1797 C CB  . TYR E 1 27 ? 2.243  68.330 52.509 1.00 28.76  ? 28 TYR E CB  1 
ATOM 1798 C CG  . TYR E 1 27 ? 2.491  69.546 53.429 1.00 25.10  ? 28 TYR E CG  1 
ATOM 1799 C CD1 . TYR E 1 27 ? 3.685  70.266 53.290 1.00 19.37  ? 28 TYR E CD1 1 
ATOM 1800 C CD2 . TYR E 1 27 ? 1.558  69.889 54.410 1.00 23.88  ? 28 TYR E CD2 1 
ATOM 1801 C CE1 . TYR E 1 27 ? 3.959  71.325 54.130 1.00 16.29  ? 28 TYR E CE1 1 
ATOM 1802 C CE2 . TYR E 1 27 ? 1.831  70.956 55.257 1.00 16.47  ? 28 TYR E CE2 1 
ATOM 1803 C CZ  . TYR E 1 27 ? 3.028  71.646 55.103 1.00 17.85  ? 28 TYR E CZ  1 
ATOM 1804 O OH  . TYR E 1 27 ? 3.290  72.690 55.964 1.00 25.24  ? 28 TYR E OH  1 
ATOM 1805 N N   . LYS E 1 28 ? 1.863  66.102 54.353 1.00 30.77  ? 29 LYS E N   1 
ATOM 1806 C CA  . LYS E 1 28 ? 1.526  65.514 55.635 1.00 34.96  ? 29 LYS E CA  1 
ATOM 1807 C C   . LYS E 1 28 ? 2.272  64.231 56.045 1.00 37.31  ? 29 LYS E C   1 
ATOM 1808 O O   . LYS E 1 28 ? 2.747  64.119 57.170 1.00 33.57  ? 29 LYS E O   1 
ATOM 1809 C CB  . LYS E 1 28 ? 0.092  65.236 55.627 1.00 37.96  ? 29 LYS E CB  1 
ATOM 1810 C CG  . LYS E 1 28 ? -0.709 66.475 55.369 1.00 41.79  ? 29 LYS E CG  1 
ATOM 1811 C CD  . LYS E 1 28 ? -2.093 65.925 55.052 1.00 46.47  ? 29 LYS E CD  1 
ATOM 1812 C CE  . LYS E 1 28 ? -3.136 67.010 54.783 1.00 50.42  ? 29 LYS E CE  1 
ATOM 1813 N NZ  . LYS E 1 28 ? -2.863 67.699 53.535 1.00 52.33  ? 29 LYS E NZ  1 
ATOM 1814 N N   . THR E 1 29 ? 2.415  63.246 55.155 1.00 39.87  ? 30 THR E N   1 
ATOM 1815 C CA  . THR E 1 29 ? 3.023  61.979 55.500 1.00 44.63  ? 30 THR E CA  1 
ATOM 1816 C C   . THR E 1 29 ? 4.468  61.824 55.093 1.00 48.44  ? 30 THR E C   1 
ATOM 1817 O O   . THR E 1 29 ? 5.058  60.788 55.373 1.00 58.07  ? 30 THR E O   1 
ATOM 1818 C CB  . THR E 1 29 ? 2.239  60.806 54.854 1.00 47.49  ? 30 THR E CB  1 
ATOM 1819 O OG1 . THR E 1 29 ? 1.911  61.278 53.563 1.00 50.78  ? 30 THR E OG1 1 
ATOM 1820 C CG2 . THR E 1 29 ? 0.956  60.380 55.544 1.00 50.07  ? 30 THR E CG2 1 
ATOM 1821 N N   . ARG E 1 30 ? 5.078  62.753 54.380 1.00 49.72  ? 31 ARG E N   1 
ATOM 1822 C CA  . ARG E 1 30 ? 6.438  62.565 53.825 1.00 51.52  ? 31 ARG E CA  1 
ATOM 1823 C C   . ARG E 1 30 ? 6.737  61.271 53.046 1.00 42.16  ? 31 ARG E C   1 
ATOM 1824 O O   . ARG E 1 30 ? 7.888  60.856 52.826 1.00 36.95  ? 31 ARG E O   1 
ATOM 1825 C CB  . ARG E 1 30 ? 7.493  62.711 54.920 1.00 56.93  ? 31 ARG E CB  1 
ATOM 1826 C CG  . ARG E 1 30 ? 7.853  64.139 55.094 1.00 74.90  ? 31 ARG E CG  1 
ATOM 1827 C CD  . ARG E 1 30 ? 8.830  64.937 54.254 1.00 89.78  ? 31 ARG E CD  1 
ATOM 1828 N NE  . ARG E 1 30 ? 9.025  66.013 55.180 1.00 98.54  ? 31 ARG E NE  1 
ATOM 1829 C CZ  . ARG E 1 30 ? 10.200 66.200 55.793 1.00 109.06 ? 31 ARG E CZ  1 
ATOM 1830 N NH1 . ARG E 1 30 ? 11.418 65.719 55.397 1.00 112.49 ? 31 ARG E NH1 1 
ATOM 1831 N NH2 . ARG E 1 30 ? 10.147 67.001 56.879 1.00 112.58 ? 31 ARG E NH2 1 
ATOM 1832 N N   . GLY E 1 31 ? 5.672  60.692 52.501 1.00 36.10  ? 32 GLY E N   1 
ATOM 1833 C CA  . GLY E 1 31 ? 5.799  59.506 51.683 1.00 39.16  ? 32 GLY E CA  1 
ATOM 1834 C C   . GLY E 1 31 ? 6.485  59.906 50.401 1.00 39.14  ? 32 GLY E C   1 
ATOM 1835 O O   . GLY E 1 31 ? 5.829  60.536 49.564 1.00 39.23  ? 32 GLY E O   1 
ATOM 1836 N N   . ARG E 1 32 ? 7.806  59.684 50.294 1.00 40.37  ? 33 ARG E N   1 
ATOM 1837 C CA  . ARG E 1 32 ? 8.511  60.001 49.038 1.00 40.24  ? 33 ARG E CA  1 
ATOM 1838 C C   . ARG E 1 32 ? 8.221  58.943 47.936 1.00 43.45  ? 33 ARG E C   1 
ATOM 1839 O O   . ARG E 1 32 ? 7.521  57.954 48.246 1.00 44.93  ? 33 ARG E O   1 
ATOM 1840 C CB  . ARG E 1 32 ? 10.008 60.062 49.246 1.00 32.32  ? 33 ARG E CB  1 
ATOM 1841 C CG  . ARG E 1 32 ? 10.515 60.584 50.569 1.00 35.93  ? 33 ARG E CG  1 
ATOM 1842 C CD  . ARG E 1 32 ? 11.981 60.782 50.331 1.00 36.96  ? 33 ARG E CD  1 
ATOM 1843 N NE  . ARG E 1 32 ? 12.259 62.198 50.260 1.00 39.62  ? 33 ARG E NE  1 
ATOM 1844 C CZ  . ARG E 1 32 ? 13.292 62.675 50.920 1.00 45.09  ? 33 ARG E CZ  1 
ATOM 1845 N NH1 . ARG E 1 32 ? 14.164 61.883 51.491 1.00 50.21  ? 33 ARG E NH1 1 
ATOM 1846 N NH2 . ARG E 1 32 ? 13.520 63.969 50.981 1.00 46.87  ? 33 ARG E NH2 1 
ATOM 1847 N N   . LYS E 1 33 ? 8.730  59.077 46.677 1.00 41.53  ? 34 LYS E N   1 
ATOM 1848 C CA  . LYS E 1 33 ? 8.410  58.129 45.610 1.00 43.17  ? 34 LYS E CA  1 
ATOM 1849 C C   . LYS E 1 33 ? 9.278  58.308 44.375 1.00 42.34  ? 34 LYS E C   1 
ATOM 1850 O O   . LYS E 1 33 ? 9.078  59.310 43.707 1.00 53.70  ? 34 LYS E O   1 
ATOM 1851 C CB  . LYS E 1 33 ? 6.918  58.293 45.228 1.00 42.21  ? 34 LYS E CB  1 
ATOM 1852 C CG  . LYS E 1 33 ? 6.529  57.491 44.003 1.00 49.96  ? 34 LYS E CG  1 
ATOM 1853 C CD  . LYS E 1 33 ? 5.040  57.348 43.723 1.00 53.62  ? 34 LYS E CD  1 
ATOM 1854 C CE  . LYS E 1 33 ? 4.975  56.785 42.286 1.00 55.69  ? 34 LYS E CE  1 
ATOM 1855 N NZ  . LYS E 1 33 ? 3.801  57.205 41.526 1.00 52.68  ? 34 LYS E NZ  1 
ATOM 1856 N N   . LEU E 1 34 ? 10.203 57.432 43.971 1.00 35.42  ? 35 LEU E N   1 
ATOM 1857 C CA  . LEU E 1 34 ? 10.993 57.713 42.765 1.00 34.82  ? 35 LEU E CA  1 
ATOM 1858 C C   . LEU E 1 34 ? 10.073 57.614 41.569 1.00 42.59  ? 35 LEU E C   1 
ATOM 1859 O O   . LEU E 1 34 ? 9.437  56.550 41.479 1.00 49.40  ? 35 LEU E O   1 
ATOM 1860 C CB  . LEU E 1 34 ? 12.130 56.717 42.484 1.00 29.41  ? 35 LEU E CB  1 
ATOM 1861 C CG  . LEU E 1 34 ? 12.879 56.889 41.137 1.00 26.20  ? 35 LEU E CG  1 
ATOM 1862 C CD1 . LEU E 1 34 ? 14.068 57.800 41.300 1.00 26.24  ? 35 LEU E CD1 1 
ATOM 1863 C CD2 . LEU E 1 34 ? 13.387 55.559 40.643 1.00 27.07  ? 35 LEU E CD2 1 
ATOM 1864 N N   . LEU E 1 35 ? 9.988  58.691 40.736 1.00 39.53  ? 36 LEU E N   1 
ATOM 1865 C CA  . LEU E 1 35 ? 9.165  58.682 39.518 1.00 37.22  ? 36 LEU E CA  1 
ATOM 1866 C C   . LEU E 1 35 ? 9.925  58.485 38.215 1.00 38.29  ? 36 LEU E C   1 
ATOM 1867 O O   . LEU E 1 35 ? 9.449  57.840 37.278 1.00 42.41  ? 36 LEU E O   1 
ATOM 1868 C CB  . LEU E 1 35 ? 8.374  59.961 39.384 1.00 32.39  ? 36 LEU E CB  1 
ATOM 1869 C CG  . LEU E 1 35 ? 7.421  60.258 40.532 1.00 31.39  ? 36 LEU E CG  1 
ATOM 1870 C CD1 . LEU E 1 35 ? 7.020  61.698 40.426 1.00 37.26  ? 36 LEU E CD1 1 
ATOM 1871 C CD2 . LEU E 1 35 ? 6.198  59.384 40.479 1.00 30.63  ? 36 LEU E CD2 1 
ATOM 1872 N N   . ARG E 1 36 ? 11.126 58.996 38.054 1.00 38.46  ? 37 ARG E N   1 
ATOM 1873 C CA  . ARG E 1 36 ? 11.805 58.822 36.774 1.00 41.11  ? 37 ARG E CA  1 
ATOM 1874 C C   . ARG E 1 36 ? 13.276 58.761 37.095 1.00 38.34  ? 37 ARG E C   1 
ATOM 1875 O O   . ARG E 1 36 ? 13.762 59.468 37.989 1.00 41.80  ? 37 ARG E O   1 
ATOM 1876 C CB  . ARG E 1 36 ? 11.527 60.032 35.764 1.00 52.97  ? 37 ARG E CB  1 
ATOM 1877 C CG  . ARG E 1 36 ? 10.088 60.261 35.196 1.00 61.37  ? 37 ARG E CG  1 
ATOM 1878 C CD  . ARG E 1 36 ? 9.588  61.646 35.612 1.00 70.49  ? 37 ARG E CD  1 
ATOM 1879 N NE  . ARG E 1 36 ? 8.148  61.927 35.652 1.00 79.53  ? 37 ARG E NE  1 
ATOM 1880 C CZ  . ARG E 1 36 ? 7.677  62.993 36.348 1.00 87.90  ? 37 ARG E CZ  1 
ATOM 1881 N NH1 . ARG E 1 36 ? 8.486  63.760 37.079 1.00 91.73  ? 37 ARG E NH1 1 
ATOM 1882 N NH2 . ARG E 1 36 ? 6.376  63.320 36.387 1.00 93.49  ? 37 ARG E NH2 1 
ATOM 1883 N N   . PHE E 1 37 ? 13.968 57.847 36.470 1.00 33.41  ? 38 PHE E N   1 
ATOM 1884 C CA  . PHE E 1 37 ? 15.394 57.770 36.622 1.00 37.73  ? 38 PHE E CA  1 
ATOM 1885 C C   . PHE E 1 37 ? 15.763 57.429 35.191 1.00 38.91  ? 38 PHE E C   1 
ATOM 1886 O O   . PHE E 1 37 ? 15.297 56.431 34.652 1.00 40.74  ? 38 PHE E O   1 
ATOM 1887 C CB  . PHE E 1 37 ? 15.713 56.678 37.654 1.00 35.31  ? 38 PHE E CB  1 
ATOM 1888 C CG  . PHE E 1 37 ? 17.119 56.770 38.249 1.00 40.97  ? 38 PHE E CG  1 
ATOM 1889 C CD1 . PHE E 1 37 ? 18.196 56.181 37.604 1.00 42.50  ? 38 PHE E CD1 1 
ATOM 1890 C CD2 . PHE E 1 37 ? 17.347 57.467 39.425 1.00 39.93  ? 38 PHE E CD2 1 
ATOM 1891 C CE1 . PHE E 1 37 ? 19.475 56.285 38.153 1.00 46.44  ? 38 PHE E CE1 1 
ATOM 1892 C CE2 . PHE E 1 37 ? 18.637 57.564 39.959 1.00 42.72  ? 38 PHE E CE2 1 
ATOM 1893 C CZ  . PHE E 1 37 ? 19.717 56.984 39.327 1.00 42.93  ? 38 PHE E CZ  1 
ATOM 1894 N N   . ASN E 1 38 ? 16.426 58.314 34.476 1.00 39.01  ? 39 ASN E N   1 
ATOM 1895 C CA  . ASN E 1 38 ? 16.668 58.105 33.072 1.00 42.10  ? 39 ASN E CA  1 
ATOM 1896 C C   . ASN E 1 38 ? 18.032 58.589 32.754 1.00 44.80  ? 39 ASN E C   1 
ATOM 1897 O O   . ASN E 1 38 ? 18.523 59.480 33.453 1.00 48.34  ? 39 ASN E O   1 
ATOM 1898 C CB  . ASN E 1 38 ? 15.725 58.894 32.235 1.00 54.44  ? 39 ASN E CB  1 
ATOM 1899 C CG  . ASN E 1 38 ? 14.314 58.323 32.221 1.00 70.66  ? 39 ASN E CG  1 
ATOM 1900 O OD1 . ASN E 1 38 ? 13.318 59.057 32.203 1.00 73.64  ? 39 ASN E OD1 1 
ATOM 1901 N ND2 . ASN E 1 38 ? 14.128 57.002 32.277 1.00 75.46  ? 39 ASN E ND2 1 
ATOM 1902 N N   . GLY E 1 39 ? 18.674 58.063 31.719 1.00 46.64  ? 40 GLY E N   1 
ATOM 1903 C CA  . GLY E 1 39 ? 20.013 58.547 31.358 1.00 49.24  ? 40 GLY E CA  1 
ATOM 1904 C C   . GLY E 1 39 ? 21.003 57.439 30.956 1.00 46.40  ? 40 GLY E C   1 
ATOM 1905 O O   . GLY E 1 39 ? 20.534 56.325 30.711 1.00 57.62  ? 40 GLY E O   1 
ATOM 1906 N N   . PRO E 1 40 ? 22.322 57.566 30.932 1.00 36.28  ? 41 PRO E N   1 
ATOM 1907 C CA  . PRO E 1 40 ? 23.027 58.765 31.297 1.00 46.87  ? 41 PRO E CA  1 
ATOM 1908 C C   . PRO E 1 40 ? 22.733 59.971 30.380 1.00 52.89  ? 41 PRO E C   1 
ATOM 1909 O O   . PRO E 1 40 ? 22.439 59.823 29.182 1.00 56.16  ? 41 PRO E O   1 
ATOM 1910 C CB  . PRO E 1 40 ? 24.489 58.287 31.335 1.00 41.32  ? 41 PRO E CB  1 
ATOM 1911 C CG  . PRO E 1 40 ? 24.574 57.251 30.263 1.00 37.70  ? 41 PRO E CG  1 
ATOM 1912 C CD  . PRO E 1 40 ? 23.212 56.600 30.324 1.00 35.65  ? 41 PRO E CD  1 
ATOM 1913 N N   . VAL E 1 41 ? 22.696 61.172 30.977 1.00 50.00  ? 42 VAL E N   1 
ATOM 1914 C CA  . VAL E 1 41 ? 22.398 62.412 30.256 1.00 42.29  ? 42 VAL E CA  1 
ATOM 1915 C C   . VAL E 1 41 ? 23.687 63.250 30.213 1.00 40.13  ? 42 VAL E C   1 
ATOM 1916 O O   . VAL E 1 41 ? 24.710 62.865 30.831 1.00 39.40  ? 42 VAL E O   1 
ATOM 1917 C CB  . VAL E 1 41 ? 21.225 63.136 30.986 1.00 42.29  ? 42 VAL E CB  1 
ATOM 1918 C CG1 . VAL E 1 41 ? 20.026 62.185 31.077 1.00 38.30  ? 42 VAL E CG1 1 
ATOM 1919 C CG2 . VAL E 1 41 ? 21.655 63.601 32.385 1.00 45.63  ? 42 VAL E CG2 1 
ATOM 1920 N N   . PRO E 1 42 ? 23.767 64.343 29.441 1.00 33.64  ? 43 PRO E N   1 
ATOM 1921 C CA  . PRO E 1 42 ? 24.967 65.171 29.376 1.00 27.84  ? 43 PRO E CA  1 
ATOM 1922 C C   . PRO E 1 42 ? 24.996 65.991 30.644 1.00 27.37  ? 43 PRO E C   1 
ATOM 1923 O O   . PRO E 1 42 ? 23.938 66.223 31.245 1.00 29.20  ? 43 PRO E O   1 
ATOM 1924 C CB  . PRO E 1 42 ? 24.802 65.996 28.136 1.00 30.09  ? 43 PRO E CB  1 
ATOM 1925 C CG  . PRO E 1 42 ? 23.730 65.290 27.352 1.00 33.99  ? 43 PRO E CG  1 
ATOM 1926 C CD  . PRO E 1 42 ? 22.801 64.777 28.447 1.00 34.52  ? 43 PRO E CD  1 
ATOM 1927 N N   . PRO E 1 43 ? 26.149 66.438 31.126 1.00 29.64  ? 44 PRO E N   1 
ATOM 1928 C CA  . PRO E 1 43 ? 26.199 67.224 32.341 1.00 34.24  ? 44 PRO E CA  1 
ATOM 1929 C C   . PRO E 1 43 ? 25.564 68.584 32.056 1.00 45.66  ? 44 PRO E C   1 
ATOM 1930 O O   . PRO E 1 43 ? 25.349 68.908 30.874 1.00 49.33  ? 44 PRO E O   1 
ATOM 1931 C CB  . PRO E 1 43 ? 27.690 67.223 32.660 1.00 35.94  ? 44 PRO E CB  1 
ATOM 1932 C CG  . PRO E 1 43 ? 28.362 67.251 31.323 1.00 27.57  ? 44 PRO E CG  1 
ATOM 1933 C CD  . PRO E 1 43 ? 27.418 66.498 30.403 1.00 25.62  ? 44 PRO E CD  1 
ATOM 1934 N N   . PRO E 1 44 ? 25.131 69.335 33.065 1.00 48.96  ? 45 PRO E N   1 
ATOM 1935 C CA  . PRO E 1 44 ? 24.561 70.637 32.846 1.00 49.85  ? 45 PRO E CA  1 
ATOM 1936 C C   . PRO E 1 44 ? 25.619 71.749 32.949 1.00 54.72  ? 45 PRO E C   1 
ATOM 1937 O O   . PRO E 1 44 ? 26.755 71.488 33.367 1.00 55.84  ? 45 PRO E O   1 
ATOM 1938 C CB  . PRO E 1 44 ? 23.465 70.619 33.866 1.00 48.27  ? 45 PRO E CB  1 
ATOM 1939 C CG  . PRO E 1 44 ? 24.110 70.024 35.067 1.00 46.83  ? 45 PRO E CG  1 
ATOM 1940 C CD  . PRO E 1 44 ? 24.830 68.869 34.411 1.00 50.81  ? 45 PRO E CD  1 
ATOM 1941 O OXT . PRO E 1 44 ? 25.320 72.866 32.529 1.00 60.41  ? 45 PRO E OXT 1 
ATOM 1942 N N   . GLY F 2 1  ? 3.803  74.440 40.888 1.00 57.89  ? 1  GLY F N   1 
ATOM 1943 C CA  . GLY F 2 1  ? 3.308  75.775 41.101 1.00 53.74  ? 1  GLY F CA  1 
ATOM 1944 C C   . GLY F 2 1  ? 4.580  76.585 41.228 1.00 52.21  ? 1  GLY F C   1 
ATOM 1945 O O   . GLY F 2 1  ? 5.300  76.766 40.247 1.00 50.11  ? 1  GLY F O   1 
ATOM 1946 N N   . GLU F 2 2  ? 4.911  77.010 42.440 1.00 52.15  ? 2  GLU F N   1 
ATOM 1947 C CA  . GLU F 2 2  ? 6.172  77.691 42.652 1.00 50.79  ? 2  GLU F CA  1 
ATOM 1948 C C   . GLU F 2 2  ? 7.264  76.646 42.393 1.00 39.10  ? 2  GLU F C   1 
ATOM 1949 O O   . GLU F 2 2  ? 7.039  75.461 42.580 1.00 31.52  ? 2  GLU F O   1 
ATOM 1950 C CB  . GLU F 2 2  ? 6.187  78.261 44.119 1.00 54.87  ? 2  GLU F CB  1 
ATOM 1951 C CG  . GLU F 2 2  ? 6.938  79.603 44.276 1.00 61.27  ? 2  GLU F CG  1 
ATOM 1952 C CD  . GLU F 2 2  ? 8.089  79.724 45.302 1.00 68.26  ? 2  GLU F CD  1 
ATOM 1953 O OE1 . GLU F 2 2  ? 8.505  78.724 45.910 1.00 71.33  ? 2  GLU F OE1 1 
ATOM 1954 O OE2 . GLU F 2 2  ? 8.583  80.845 45.502 1.00 70.14  ? 2  GLU F OE2 1 
ATOM 1955 N N   . TRP F 2 3  ? 8.374  77.069 41.869 1.00 35.23  ? 3  TRP F N   1 
ATOM 1956 C CA  . TRP F 2 3  ? 9.498  76.246 41.511 1.00 40.46  ? 3  TRP F CA  1 
ATOM 1957 C C   . TRP F 2 3  ? 10.737 76.928 42.062 1.00 41.12  ? 3  TRP F C   1 
ATOM 1958 O O   . TRP F 2 3  ? 10.853 78.133 41.858 1.00 45.65  ? 3  TRP F O   1 
ATOM 1959 C CB  . TRP F 2 3  ? 9.640  76.184 40.003 1.00 49.93  ? 3  TRP F CB  1 
ATOM 1960 C CG  . TRP F 2 3  ? 8.863  75.139 39.188 1.00 58.51  ? 3  TRP F CG  1 
ATOM 1961 C CD1 . TRP F 2 3  ? 7.628  75.341 38.613 1.00 57.70  ? 3  TRP F CD1 1 
ATOM 1962 C CD2 . TRP F 2 3  ? 9.378  73.899 38.911 1.00 61.93  ? 3  TRP F CD2 1 
ATOM 1963 N NE1 . TRP F 2 3  ? 7.370  74.215 37.984 1.00 59.20  ? 3  TRP F NE1 1 
ATOM 1964 C CE2 . TRP F 2 3  ? 8.375  73.340 38.137 1.00 61.62  ? 3  TRP F CE2 1 
ATOM 1965 C CE3 . TRP F 2 3  ? 10.528 73.216 39.251 1.00 61.47  ? 3  TRP F CE3 1 
ATOM 1966 C CZ2 . TRP F 2 3  ? 8.528  72.063 37.658 1.00 62.74  ? 3  TRP F CZ2 1 
ATOM 1967 C CZ3 . TRP F 2 3  ? 10.672 71.948 38.754 1.00 63.24  ? 3  TRP F CZ3 1 
ATOM 1968 C CH2 . TRP F 2 3  ? 9.669  71.374 37.990 1.00 63.44  ? 3  TRP F CH2 1 
ATOM 1969 N N   . GLU F 2 4  ? 11.697 76.281 42.720 1.00 43.66  ? 4  GLU F N   1 
ATOM 1970 C CA  . GLU F 2 4  ? 12.880 76.971 43.231 1.00 46.28  ? 4  GLU F CA  1 
ATOM 1971 C C   . GLU F 2 4  ? 14.121 76.107 43.330 1.00 43.44  ? 4  GLU F C   1 
ATOM 1972 O O   . GLU F 2 4  ? 14.064 74.922 43.661 1.00 48.45  ? 4  GLU F O   1 
ATOM 1973 C CB  . GLU F 2 4  ? 12.644 77.567 44.633 1.00 46.62  ? 4  GLU F CB  1 
ATOM 1974 C CG  . GLU F 2 4  ? 12.132 76.554 45.627 1.00 52.80  ? 4  GLU F CG  1 
ATOM 1975 C CD  . GLU F 2 4  ? 12.080 77.025 47.060 1.00 55.48  ? 4  GLU F CD  1 
ATOM 1976 O OE1 . GLU F 2 4  ? 13.137 77.312 47.638 1.00 57.10  ? 4  GLU F OE1 1 
ATOM 1977 O OE2 . GLU F 2 4  ? 10.966 77.080 47.581 1.00 58.72  ? 4  GLU F OE2 1 
ATOM 1978 N N   . ILE F 2 5  ? 15.251 76.737 43.089 1.00 34.90  ? 5  ILE F N   1 
ATOM 1979 C CA  . ILE F 2 5  ? 16.523 76.098 43.166 1.00 29.49  ? 5  ILE F CA  1 
ATOM 1980 C C   . ILE F 2 5  ? 16.931 75.879 44.613 1.00 31.55  ? 5  ILE F C   1 
ATOM 1981 O O   . ILE F 2 5  ? 17.156 76.836 45.336 1.00 36.53  ? 5  ILE F O   1 
ATOM 1982 C CB  . ILE F 2 5  ? 17.472 77.011 42.353 1.00 27.68  ? 5  ILE F CB  1 
ATOM 1983 C CG1 . ILE F 2 5  ? 17.038 76.837 40.897 1.00 25.95  ? 5  ILE F CG1 1 
ATOM 1984 C CG2 . ILE F 2 5  ? 18.969 76.681 42.496 1.00 21.75  ? 5  ILE F CG2 1 
ATOM 1985 C CD1 . ILE F 2 5  ? 17.945 77.690 40.011 1.00 33.44  ? 5  ILE F CD1 1 
ATOM 1986 N N   . ILE F 2 6  ? 17.000 74.628 45.069 1.00 37.97  ? 6  ILE F N   1 
ATOM 1987 C CA  . ILE F 2 6  ? 17.442 74.305 46.423 1.00 34.94  ? 6  ILE F CA  1 
ATOM 1988 C C   . ILE F 2 6  ? 18.874 73.860 46.325 1.00 35.97  ? 6  ILE F C   1 
ATOM 1989 O O   . ILE F 2 6  ? 19.341 73.474 45.254 1.00 36.28  ? 6  ILE F O   1 
ATOM 1990 C CB  . ILE F 2 6  ? 16.655 73.146 47.115 1.00 35.98  ? 6  ILE F CB  1 
ATOM 1991 C CG1 . ILE F 2 6  ? 16.839 71.778 46.461 1.00 33.96  ? 6  ILE F CG1 1 
ATOM 1992 C CG2 . ILE F 2 6  ? 15.202 73.589 47.121 1.00 40.71  ? 6  ILE F CG2 1 
ATOM 1993 C CD1 . ILE F 2 6  ? 16.060 70.671 47.215 1.00 37.34  ? 6  ILE F CD1 1 
ATOM 1994 N N   . ASP F 2 7  ? 19.526 73.814 47.468 1.00 42.68  ? 7  ASP F N   1 
ATOM 1995 C CA  . ASP F 2 7  ? 20.950 73.587 47.563 1.00 49.62  ? 7  ASP F CA  1 
ATOM 1996 C C   . ASP F 2 7  ? 21.331 72.125 47.762 1.00 49.48  ? 7  ASP F C   1 
ATOM 1997 O O   . ASP F 2 7  ? 20.629 71.398 48.456 1.00 48.44  ? 7  ASP F O   1 
ATOM 1998 C CB  . ASP F 2 7  ? 21.440 74.463 48.722 1.00 57.47  ? 7  ASP F CB  1 
ATOM 1999 C CG  . ASP F 2 7  ? 22.950 74.630 48.882 1.00 63.22  ? 7  ASP F CG  1 
ATOM 2000 O OD1 . ASP F 2 7  ? 23.703 74.576 47.897 1.00 67.16  ? 7  ASP F OD1 1 
ATOM 2001 O OD2 . ASP F 2 7  ? 23.371 74.828 50.024 1.00 66.93  ? 7  ASP F OD2 1 
ATOM 2002 N N   . ILE F 2 8  ? 22.486 71.739 47.197 1.00 48.64  ? 8  ILE F N   1 
ATOM 2003 C CA  . ILE F 2 8  ? 23.087 70.422 47.332 1.00 44.17  ? 8  ILE F CA  1 
ATOM 2004 C C   . ILE F 2 8  ? 23.715 70.256 48.698 1.00 47.77  ? 8  ILE F C   1 
ATOM 2005 O O   . ILE F 2 8  ? 24.914 70.116 48.897 1.00 47.60  ? 8  ILE F O   1 
ATOM 2006 C CB  . ILE F 2 8  ? 24.180 70.172 46.291 1.00 35.60  ? 8  ILE F CB  1 
ATOM 2007 C CG1 . ILE F 2 8  ? 25.226 71.263 46.242 1.00 32.17  ? 8  ILE F CG1 1 
ATOM 2008 C CG2 . ILE F 2 8  ? 23.464 70.041 44.983 1.00 37.46  ? 8  ILE F CG2 1 
ATOM 2009 C CD1 . ILE F 2 8  ? 26.450 70.822 45.441 1.00 34.48  ? 8  ILE F CD1 1 
ATOM 2010 N N   . GLY F 2 9  ? 22.909 70.297 49.722 1.00 51.42  ? 9  GLY F N   1 
ATOM 2011 C CA  . GLY F 2 9  ? 23.422 70.048 51.054 1.00 53.40  ? 9  GLY F CA  1 
ATOM 2012 C C   . GLY F 2 9  ? 23.045 68.633 51.414 1.00 50.93  ? 9  GLY F C   1 
ATOM 2013 O O   . GLY F 2 9  ? 22.341 67.984 50.639 1.00 50.14  ? 9  GLY F O   1 
ATOM 2014 N N   . PRO F 2 10 ? 23.347 68.133 52.602 1.00 50.56  ? 10 PRO F N   1 
ATOM 2015 C CA  . PRO F 2 10 ? 23.027 66.781 53.011 1.00 51.56  ? 10 PRO F CA  1 
ATOM 2016 C C   . PRO F 2 10 ? 21.613 66.337 52.647 1.00 53.64  ? 10 PRO F C   1 
ATOM 2017 O O   . PRO F 2 10 ? 21.447 65.208 52.188 1.00 62.30  ? 10 PRO F O   1 
ATOM 2018 C CB  . PRO F 2 10 ? 23.304 66.761 54.505 1.00 50.69  ? 10 PRO F CB  1 
ATOM 2019 C CG  . PRO F 2 10 ? 23.266 68.200 54.925 1.00 51.99  ? 10 PRO F CG  1 
ATOM 2020 C CD  . PRO F 2 10 ? 23.837 68.927 53.723 1.00 53.37  ? 10 PRO F CD  1 
ATOM 2021 N N   . PHE F 2 11 ? 20.629 67.246 52.630 1.00 49.94  ? 11 PHE F N   1 
ATOM 2022 C CA  . PHE F 2 11 ? 19.245 66.854 52.357 1.00 44.38  ? 11 PHE F CA  1 
ATOM 2023 C C   . PHE F 2 11 ? 19.089 66.506 50.941 1.00 37.12  ? 11 PHE F C   1 
ATOM 2024 O O   . PHE F 2 11 ? 18.222 65.688 50.637 1.00 41.07  ? 11 PHE F O   1 
ATOM 2025 C CB  . PHE F 2 11 ? 18.218 67.942 52.627 1.00 42.05  ? 11 PHE F CB  1 
ATOM 2026 C CG  . PHE F 2 11 ? 16.766 67.612 52.326 1.00 39.00  ? 11 PHE F CG  1 
ATOM 2027 C CD1 . PHE F 2 11 ? 16.021 66.925 53.246 1.00 33.43  ? 11 PHE F CD1 1 
ATOM 2028 C CD2 . PHE F 2 11 ? 16.201 68.077 51.146 1.00 40.31  ? 11 PHE F CD2 1 
ATOM 2029 C CE1 . PHE F 2 11 ? 14.693 66.698 53.008 1.00 28.23  ? 11 PHE F CE1 1 
ATOM 2030 C CE2 . PHE F 2 11 ? 14.871 67.838 50.916 1.00 35.60  ? 11 PHE F CE2 1 
ATOM 2031 C CZ  . PHE F 2 11 ? 14.118 67.149 51.848 1.00 35.49  ? 11 PHE F CZ  1 
ATOM 2032 N N   . THR F 2 12 ? 19.870 67.145 50.114 1.00 33.52  ? 12 THR F N   1 
ATOM 2033 C CA  . THR F 2 12 ? 19.784 66.761 48.738 1.00 45.91  ? 12 THR F CA  1 
ATOM 2034 C C   . THR F 2 12 ? 20.573 65.481 48.512 1.00 45.26  ? 12 THR F C   1 
ATOM 2035 O O   . THR F 2 12 ? 20.167 64.680 47.667 1.00 47.63  ? 12 THR F O   1 
ATOM 2036 C CB  . THR F 2 12 ? 20.271 67.937 47.919 1.00 47.17  ? 12 THR F CB  1 
ATOM 2037 O OG1 . THR F 2 12 ? 19.372 68.946 48.380 1.00 52.95  ? 12 THR F OG1 1 
ATOM 2038 C CG2 . THR F 2 12 ? 20.245 67.804 46.400 1.00 45.67  ? 12 THR F CG2 1 
ATOM 2039 N N   . GLN F 2 13 ? 21.615 65.213 49.313 1.00 40.09  ? 13 GLN F N   1 
ATOM 2040 C CA  . GLN F 2 13 ? 22.375 63.989 49.149 1.00 34.36  ? 13 GLN F CA  1 
ATOM 2041 C C   . GLN F 2 13 ? 21.462 62.843 49.472 1.00 32.22  ? 13 GLN F C   1 
ATOM 2042 O O   . GLN F 2 13 ? 21.271 61.971 48.625 1.00 37.55  ? 13 GLN F O   1 
ATOM 2043 C CB  . GLN F 2 13 ? 23.565 64.012 50.053 1.00 37.22  ? 13 GLN F CB  1 
ATOM 2044 C CG  . GLN F 2 13 ? 24.464 65.214 49.725 1.00 46.35  ? 13 GLN F CG  1 
ATOM 2045 C CD  . GLN F 2 13 ? 24.848 65.379 48.253 1.00 51.20  ? 13 GLN F CD  1 
ATOM 2046 O OE1 . GLN F 2 13 ? 24.926 64.406 47.498 1.00 59.89  ? 13 GLN F OE1 1 
ATOM 2047 N NE2 . GLN F 2 13 ? 25.133 66.575 47.723 1.00 56.91  ? 13 GLN F NE2 1 
ATOM 2048 N N   . ASN F 2 14 ? 20.777 62.870 50.609 1.00 31.97  ? 14 ASN F N   1 
ATOM 2049 C CA  . ASN F 2 14 ? 19.800 61.821 50.971 1.00 38.78  ? 14 ASN F CA  1 
ATOM 2050 C C   . ASN F 2 14 ? 18.826 61.509 49.870 1.00 38.93  ? 14 ASN F C   1 
ATOM 2051 O O   . ASN F 2 14 ? 18.537 60.348 49.597 1.00 39.63  ? 14 ASN F O   1 
ATOM 2052 C CB  . ASN F 2 14 ? 18.850 62.140 52.142 1.00 41.88  ? 14 ASN F CB  1 
ATOM 2053 C CG  . ASN F 2 14 ? 19.514 62.096 53.513 1.00 51.33  ? 14 ASN F CG  1 
ATOM 2054 O OD1 . ASN F 2 14 ? 20.677 61.704 53.692 1.00 56.28  ? 14 ASN F OD1 1 
ATOM 2055 N ND2 . ASN F 2 14 ? 18.770 62.522 54.532 1.00 53.88  ? 14 ASN F ND2 1 
ATOM 2056 N N   . LEU F 2 15 ? 18.294 62.550 49.245 1.00 40.07  ? 15 LEU F N   1 
ATOM 2057 C CA  . LEU F 2 15 ? 17.329 62.357 48.198 1.00 33.96  ? 15 LEU F CA  1 
ATOM 2058 C C   . LEU F 2 15 ? 17.897 61.527 47.091 1.00 34.70  ? 15 LEU F C   1 
ATOM 2059 O O   . LEU F 2 15 ? 17.251 60.573 46.691 1.00 37.83  ? 15 LEU F O   1 
ATOM 2060 C CB  . LEU F 2 15 ? 16.891 63.704 47.717 1.00 32.03  ? 15 LEU F CB  1 
ATOM 2061 C CG  . LEU F 2 15 ? 15.722 64.247 48.516 1.00 28.42  ? 15 LEU F CG  1 
ATOM 2062 C CD1 . LEU F 2 15 ? 15.782 65.685 48.351 1.00 37.28  ? 15 LEU F CD1 1 
ATOM 2063 C CD2 . LEU F 2 15 ? 14.363 63.845 47.995 1.00 20.21  ? 15 LEU F CD2 1 
ATOM 2064 N N   . GLY F 2 16 ? 19.138 61.777 46.693 1.00 41.46  ? 16 GLY F N   1 
ATOM 2065 C CA  . GLY F 2 16 ? 19.853 61.015 45.678 1.00 39.62  ? 16 GLY F CA  1 
ATOM 2066 C C   . GLY F 2 16 ? 20.036 59.603 46.208 1.00 44.19  ? 16 GLY F C   1 
ATOM 2067 O O   . GLY F 2 16 ? 19.762 58.671 45.457 1.00 47.76  ? 16 GLY F O   1 
ATOM 2068 N N   . LYS F 2 17 ? 20.434 59.384 47.488 1.00 45.64  ? 17 LYS F N   1 
ATOM 2069 C CA  . LYS F 2 17 ? 20.560 58.030 48.063 1.00 39.88  ? 17 LYS F CA  1 
ATOM 2070 C C   . LYS F 2 17 ? 19.299 57.260 47.900 1.00 31.14  ? 17 LYS F C   1 
ATOM 2071 O O   . LYS F 2 17 ? 19.414 56.179 47.348 1.00 39.59  ? 17 LYS F O   1 
ATOM 2072 C CB  . LYS F 2 17 ? 20.854 57.969 49.541 1.00 47.92  ? 17 LYS F CB  1 
ATOM 2073 C CG  . LYS F 2 17 ? 22.348 58.142 49.752 1.00 60.78  ? 17 LYS F CG  1 
ATOM 2074 C CD  . LYS F 2 17 ? 22.701 57.925 51.225 1.00 69.99  ? 17 LYS F CD  1 
ATOM 2075 C CE  . LYS F 2 17 ? 24.199 58.147 51.547 1.00 74.91  ? 17 LYS F CE  1 
ATOM 2076 N NZ  . LYS F 2 17 ? 24.523 59.538 51.852 1.00 74.82  ? 17 LYS F NZ  1 
ATOM 2077 N N   . PHE F 2 18 ? 18.126 57.777 48.264 1.00 27.16  ? 18 PHE F N   1 
ATOM 2078 C CA  . PHE F 2 18 ? 16.852 57.119 47.998 1.00 23.94  ? 18 PHE F CA  1 
ATOM 2079 C C   . PHE F 2 18 ? 16.685 56.895 46.513 1.00 28.66  ? 18 PHE F C   1 
ATOM 2080 O O   . PHE F 2 18 ? 16.248 55.810 46.169 1.00 39.11  ? 18 PHE F O   1 
ATOM 2081 C CB  . PHE F 2 18 ? 15.694 57.970 48.474 1.00 17.62  ? 18 PHE F CB  1 
ATOM 2082 C CG  . PHE F 2 18 ? 14.245 57.689 48.069 1.00 7.12   ? 18 PHE F CG  1 
ATOM 2083 C CD1 . PHE F 2 18 ? 13.754 58.053 46.858 1.00 6.04   ? 18 PHE F CD1 1 
ATOM 2084 C CD2 . PHE F 2 18 ? 13.395 57.103 48.978 1.00 4.36   ? 18 PHE F CD2 1 
ATOM 2085 C CE1 . PHE F 2 18 ? 12.402 57.859 46.581 1.00 9.24   ? 18 PHE F CE1 1 
ATOM 2086 C CE2 . PHE F 2 18 ? 12.063 56.921 48.710 1.00 2.00   ? 18 PHE F CE2 1 
ATOM 2087 C CZ  . PHE F 2 18 ? 11.556 57.285 47.485 1.00 3.60   ? 18 PHE F CZ  1 
ATOM 2088 N N   . ALA F 2 19 ? 17.005 57.822 45.623 1.00 27.43  ? 19 ALA F N   1 
ATOM 2089 C CA  . ALA F 2 19 ? 16.803 57.601 44.207 1.00 27.06  ? 19 ALA F CA  1 
ATOM 2090 C C   . ALA F 2 19 ? 17.508 56.366 43.675 1.00 29.39  ? 19 ALA F C   1 
ATOM 2091 O O   . ALA F 2 19 ? 16.881 55.463 43.112 1.00 26.79  ? 19 ALA F O   1 
ATOM 2092 C CB  . ALA F 2 19 ? 17.304 58.794 43.451 1.00 33.06  ? 19 ALA F CB  1 
ATOM 2093 N N   . VAL F 2 20 ? 18.820 56.311 43.907 1.00 31.67  ? 20 VAL F N   1 
ATOM 2094 C CA  . VAL F 2 20 ? 19.658 55.177 43.550 1.00 34.87  ? 20 VAL F CA  1 
ATOM 2095 C C   . VAL F 2 20 ? 19.141 53.874 44.184 1.00 38.11  ? 20 VAL F C   1 
ATOM 2096 O O   . VAL F 2 20 ? 18.807 52.938 43.458 1.00 38.10  ? 20 VAL F O   1 
ATOM 2097 C CB  . VAL F 2 20 ? 21.096 55.455 44.002 1.00 33.62  ? 20 VAL F CB  1 
ATOM 2098 C CG1 . VAL F 2 20 ? 21.974 54.238 43.767 1.00 34.45  ? 20 VAL F CG1 1 
ATOM 2099 C CG2 . VAL F 2 20 ? 21.647 56.626 43.202 1.00 29.66  ? 20 VAL F CG2 1 
ATOM 2100 N N   . ASP F 2 21 ? 19.010 53.765 45.507 1.00 40.95  ? 21 ASP F N   1 
ATOM 2101 C CA  . ASP F 2 21 ? 18.540 52.532 46.139 1.00 50.44  ? 21 ASP F CA  1 
ATOM 2102 C C   . ASP F 2 21 ? 17.178 52.090 45.586 1.00 48.03  ? 21 ASP F C   1 
ATOM 2103 O O   . ASP F 2 21 ? 16.995 50.903 45.286 1.00 50.46  ? 21 ASP F O   1 
ATOM 2104 C CB  . ASP F 2 21 ? 18.460 52.721 47.686 1.00 56.71  ? 21 ASP F CB  1 
ATOM 2105 C CG  . ASP F 2 21 ? 19.769 53.093 48.435 1.00 62.35  ? 21 ASP F CG  1 
ATOM 2106 O OD1 . ASP F 2 21 ? 20.845 53.186 47.821 1.00 58.25  ? 21 ASP F OD1 1 
ATOM 2107 O OD2 . ASP F 2 21 ? 19.708 53.310 49.657 1.00 63.20  ? 21 ASP F OD2 1 
ATOM 2108 N N   . GLU F 2 22 ? 16.234 53.001 45.321 1.00 43.33  ? 22 GLU F N   1 
ATOM 2109 C CA  . GLU F 2 22 ? 14.961 52.562 44.739 1.00 41.35  ? 22 GLU F CA  1 
ATOM 2110 C C   . GLU F 2 22 ? 15.120 52.160 43.285 1.00 41.32  ? 22 GLU F C   1 
ATOM 2111 O O   . GLU F 2 22 ? 14.321 51.354 42.778 1.00 43.06  ? 22 GLU F O   1 
ATOM 2112 C CB  . GLU F 2 22 ? 13.896 53.632 44.813 1.00 29.90  ? 22 GLU F CB  1 
ATOM 2113 C CG  . GLU F 2 22 ? 13.333 53.576 46.188 1.00 28.02  ? 22 GLU F CG  1 
ATOM 2114 C CD  . GLU F 2 22 ? 11.861 53.265 46.078 1.00 38.43  ? 22 GLU F CD  1 
ATOM 2115 O OE1 . GLU F 2 22 ? 11.173 53.996 45.375 1.00 53.41  ? 22 GLU F OE1 1 
ATOM 2116 O OE2 . GLU F 2 22 ? 11.350 52.311 46.670 1.00 41.44  ? 22 GLU F OE2 1 
ATOM 2117 N N   . GLU F 2 23 ? 16.144 52.684 42.584 1.00 42.64  ? 23 GLU F N   1 
ATOM 2118 C CA  . GLU F 2 23 ? 16.348 52.216 41.226 1.00 42.77  ? 23 GLU F CA  1 
ATOM 2119 C C   . GLU F 2 23 ? 16.916 50.825 41.364 1.00 45.24  ? 23 GLU F C   1 
ATOM 2120 O O   . GLU F 2 23 ? 16.401 49.933 40.692 1.00 47.01  ? 23 GLU F O   1 
ATOM 2121 C CB  . GLU F 2 23 ? 17.313 53.090 40.381 1.00 38.16  ? 23 GLU F CB  1 
ATOM 2122 C CG  . GLU F 2 23 ? 17.422 52.661 38.887 1.00 41.10  ? 23 GLU F CG  1 
ATOM 2123 C CD  . GLU F 2 23 ? 16.179 52.407 37.979 1.00 45.61  ? 23 GLU F CD  1 
ATOM 2124 O OE1 . GLU F 2 23 ? 15.015 52.457 38.398 1.00 48.69  ? 23 GLU F OE1 1 
ATOM 2125 O OE2 . GLU F 2 23 ? 16.371 52.128 36.791 1.00 40.10  ? 23 GLU F OE2 1 
ATOM 2126 N N   . ASN F 2 24 ? 17.822 50.571 42.315 1.00 42.95  ? 24 ASN F N   1 
ATOM 2127 C CA  . ASN F 2 24 ? 18.372 49.234 42.512 1.00 42.96  ? 24 ASN F CA  1 
ATOM 2128 C C   . ASN F 2 24 ? 17.291 48.175 42.681 1.00 47.90  ? 24 ASN F C   1 
ATOM 2129 O O   . ASN F 2 24 ? 17.463 47.006 42.322 1.00 57.05  ? 24 ASN F O   1 
ATOM 2130 C CB  . ASN F 2 24 ? 19.278 49.150 43.743 1.00 36.87  ? 24 ASN F CB  1 
ATOM 2131 C CG  . ASN F 2 24 ? 20.698 49.595 43.460 1.00 38.28  ? 24 ASN F CG  1 
ATOM 2132 O OD1 . ASN F 2 24 ? 21.124 49.591 42.300 1.00 41.97  ? 24 ASN F OD1 1 
ATOM 2133 N ND2 . ASN F 2 24 ? 21.541 49.966 44.423 1.00 33.88  ? 24 ASN F ND2 1 
ATOM 2134 N N   . LYS F 2 25 ? 16.128 48.566 43.161 1.00 45.14  ? 25 LYS F N   1 
ATOM 2135 C CA  . LYS F 2 25 ? 15.079 47.616 43.335 1.00 44.34  ? 25 LYS F CA  1 
ATOM 2136 C C   . LYS F 2 25 ? 14.485 47.226 41.988 1.00 47.45  ? 25 LYS F C   1 
ATOM 2137 O O   . LYS F 2 25 ? 13.889 46.176 41.866 1.00 52.92  ? 25 LYS F O   1 
ATOM 2138 C CB  . LYS F 2 25 ? 14.024 48.235 44.246 1.00 43.80  ? 25 LYS F CB  1 
ATOM 2139 C CG  . LYS F 2 25 ? 14.442 48.742 45.637 1.00 44.71  ? 25 LYS F CG  1 
ATOM 2140 C CD  . LYS F 2 25 ? 13.141 48.770 46.453 1.00 50.11  ? 25 LYS F CD  1 
ATOM 2141 C CE  . LYS F 2 25 ? 13.132 49.317 47.896 1.00 50.60  ? 25 LYS F CE  1 
ATOM 2142 N NZ  . LYS F 2 25 ? 11.731 49.547 48.251 1.00 54.26  ? 25 LYS F NZ  1 
ATOM 2143 N N   . ILE F 2 26 ? 14.549 48.071 40.963 1.00 51.37  ? 26 ILE F N   1 
ATOM 2144 C CA  . ILE F 2 26 ? 13.889 47.859 39.648 1.00 50.40  ? 26 ILE F CA  1 
ATOM 2145 C C   . ILE F 2 26 ? 14.864 47.279 38.637 1.00 48.51  ? 26 ILE F C   1 
ATOM 2146 O O   . ILE F 2 26 ? 14.506 46.629 37.666 1.00 47.19  ? 26 ILE F O   1 
ATOM 2147 C CB  . ILE F 2 26 ? 13.329 49.261 39.170 1.00 49.50  ? 26 ILE F CB  1 
ATOM 2148 C CG1 . ILE F 2 26 ? 12.329 49.757 40.241 1.00 56.71  ? 26 ILE F CG1 1 
ATOM 2149 C CG2 . ILE F 2 26 ? 12.552 49.195 37.883 1.00 47.20  ? 26 ILE F CG2 1 
ATOM 2150 C CD1 . ILE F 2 26 ? 12.124 51.277 40.442 1.00 59.25  ? 26 ILE F CD1 1 
ATOM 2151 N N   . GLY F 2 27 ? 16.132 47.603 38.812 1.00 49.73  ? 27 GLY F N   1 
ATOM 2152 C CA  . GLY F 2 27 ? 17.222 47.044 38.047 1.00 49.63  ? 27 GLY F CA  1 
ATOM 2153 C C   . GLY F 2 27 ? 17.401 47.375 36.580 1.00 48.66  ? 27 GLY F C   1 
ATOM 2154 O O   . GLY F 2 27 ? 18.315 46.821 35.969 1.00 49.68  ? 27 GLY F O   1 
ATOM 2155 N N   . GLN F 2 28 ? 16.647 48.285 35.984 1.00 46.23  ? 28 GLN F N   1 
ATOM 2156 C CA  . GLN F 2 28 ? 16.854 48.695 34.587 1.00 46.91  ? 28 GLN F CA  1 
ATOM 2157 C C   . GLN F 2 28 ? 18.302 49.045 34.232 1.00 41.28  ? 28 GLN F C   1 
ATOM 2158 O O   . GLN F 2 28 ? 18.656 49.138 33.066 1.00 40.92  ? 28 GLN F O   1 
ATOM 2159 C CB  . GLN F 2 28 ? 16.043 49.957 34.210 1.00 59.32  ? 28 GLN F CB  1 
ATOM 2160 C CG  . GLN F 2 28 ? 15.069 49.919 33.033 1.00 64.48  ? 28 GLN F CG  1 
ATOM 2161 C CD  . GLN F 2 28 ? 13.770 49.240 33.450 1.00 72.74  ? 28 GLN F CD  1 
ATOM 2162 O OE1 . GLN F 2 28 ? 13.107 49.752 34.347 1.00 74.08  ? 28 GLN F OE1 1 
ATOM 2163 N NE2 . GLN F 2 28 ? 13.356 48.094 32.902 1.00 74.85  ? 28 GLN F NE2 1 
ATOM 2164 N N   . TYR F 2 29 ? 19.143 49.347 35.206 1.00 38.84  ? 29 TYR F N   1 
ATOM 2165 C CA  . TYR F 2 29 ? 20.500 49.770 34.964 1.00 36.06  ? 29 TYR F CA  1 
ATOM 2166 C C   . TYR F 2 29 ? 21.407 48.822 35.737 1.00 40.27  ? 29 TYR F C   1 
ATOM 2167 O O   . TYR F 2 29 ? 22.551 49.167 36.043 1.00 43.88  ? 29 TYR F O   1 
ATOM 2168 C CB  . TYR F 2 29 ? 20.619 51.261 35.443 1.00 44.85  ? 29 TYR F CB  1 
ATOM 2169 C CG  . TYR F 2 29 ? 19.850 52.302 34.603 1.00 44.95  ? 29 TYR F CG  1 
ATOM 2170 C CD1 . TYR F 2 29 ? 18.513 52.606 34.856 1.00 41.30  ? 29 TYR F CD1 1 
ATOM 2171 C CD2 . TYR F 2 29 ? 20.467 52.882 33.503 1.00 44.34  ? 29 TYR F CD2 1 
ATOM 2172 C CE1 . TYR F 2 29 ? 17.811 53.415 33.971 1.00 39.43  ? 29 TYR F CE1 1 
ATOM 2173 C CE2 . TYR F 2 29 ? 19.767 53.688 32.626 1.00 33.77  ? 29 TYR F CE2 1 
ATOM 2174 C CZ  . TYR F 2 29 ? 18.448 53.935 32.854 1.00 33.95  ? 29 TYR F CZ  1 
ATOM 2175 O OH  . TYR F 2 29 ? 17.774 54.654 31.909 1.00 21.74  ? 29 TYR F OH  1 
ATOM 2176 N N   . GLY F 2 30 ? 20.929 47.603 36.061 1.00 38.10  ? 30 GLY F N   1 
ATOM 2177 C CA  . GLY F 2 30 ? 21.678 46.665 36.891 1.00 37.31  ? 30 GLY F CA  1 
ATOM 2178 C C   . GLY F 2 30 ? 21.710 46.961 38.405 1.00 42.95  ? 30 GLY F C   1 
ATOM 2179 O O   . GLY F 2 30 ? 20.720 46.717 39.115 1.00 47.69  ? 30 GLY F O   1 
ATOM 2180 N N   . ARG F 2 31 ? 22.851 47.430 38.930 1.00 41.67  ? 31 ARG F N   1 
ATOM 2181 C CA  . ARG F 2 31 ? 23.028 47.732 40.352 1.00 46.74  ? 31 ARG F CA  1 
ATOM 2182 C C   . ARG F 2 31 ? 23.952 48.924 40.366 1.00 49.39  ? 31 ARG F C   1 
ATOM 2183 O O   . ARG F 2 31 ? 24.971 48.944 39.656 1.00 47.17  ? 31 ARG F O   1 
ATOM 2184 C CB  . ARG F 2 31 ? 23.702 46.574 41.154 1.00 53.52  ? 31 ARG F CB  1 
ATOM 2185 C CG  . ARG F 2 31 ? 23.993 46.713 42.686 1.00 64.02  ? 31 ARG F CG  1 
ATOM 2186 C CD  . ARG F 2 31 ? 22.861 46.491 43.719 1.00 76.39  ? 31 ARG F CD  1 
ATOM 2187 N NE  . ARG F 2 31 ? 22.162 45.254 43.393 1.00 89.66  ? 31 ARG F NE  1 
ATOM 2188 C CZ  . ARG F 2 31 ? 20.848 45.017 43.578 1.00 97.83  ? 31 ARG F CZ  1 
ATOM 2189 N NH1 . ARG F 2 31 ? 19.981 45.841 44.182 1.00 101.64 ? 31 ARG F NH1 1 
ATOM 2190 N NH2 . ARG F 2 31 ? 20.388 43.837 43.147 1.00 103.49 ? 31 ARG F NH2 1 
ATOM 2191 N N   . LEU F 2 32 ? 23.605 49.933 41.158 1.00 49.05  ? 32 LEU F N   1 
ATOM 2192 C CA  . LEU F 2 32 ? 24.358 51.174 41.164 1.00 46.09  ? 32 LEU F CA  1 
ATOM 2193 C C   . LEU F 2 32 ? 24.843 51.654 42.514 1.00 43.85  ? 32 LEU F C   1 
ATOM 2194 O O   . LEU F 2 32 ? 24.195 51.536 43.563 1.00 40.15  ? 32 LEU F O   1 
ATOM 2195 C CB  . LEU F 2 32 ? 23.522 52.270 40.545 1.00 41.65  ? 32 LEU F CB  1 
ATOM 2196 C CG  . LEU F 2 32 ? 23.086 52.042 39.128 1.00 35.52  ? 32 LEU F CG  1 
ATOM 2197 C CD1 . LEU F 2 32 ? 21.602 52.296 39.153 1.00 29.86  ? 32 LEU F CD1 1 
ATOM 2198 C CD2 . LEU F 2 32 ? 23.919 52.845 38.115 1.00 34.32  ? 32 LEU F CD2 1 
ATOM 2199 N N   . THR F 2 33 ? 26.041 52.195 42.460 1.00 40.95  ? 33 THR F N   1 
ATOM 2200 C CA  . THR F 2 33 ? 26.640 52.747 43.636 1.00 46.48  ? 33 THR F CA  1 
ATOM 2201 C C   . THR F 2 33 ? 26.452 54.241 43.515 1.00 52.24  ? 33 THR F C   1 
ATOM 2202 O O   . THR F 2 33 ? 26.726 54.840 42.466 1.00 54.34  ? 33 THR F O   1 
ATOM 2203 C CB  . THR F 2 33 ? 28.130 52.299 43.689 1.00 47.69  ? 33 THR F CB  1 
ATOM 2204 O OG1 . THR F 2 33 ? 28.534 52.738 44.953 1.00 48.33  ? 33 THR F OG1 1 
ATOM 2205 C CG2 . THR F 2 33 ? 29.097 52.848 42.652 1.00 52.20  ? 33 THR F CG2 1 
ATOM 2206 N N   . PHE F 2 34 ? 25.847 54.796 44.562 1.00 51.76  ? 34 PHE F N   1 
ATOM 2207 C CA  . PHE F 2 34 ? 25.593 56.222 44.688 1.00 51.50  ? 34 PHE F CA  1 
ATOM 2208 C C   . PHE F 2 34 ? 26.888 57.000 44.700 1.00 47.87  ? 34 PHE F C   1 
ATOM 2209 O O   . PHE F 2 34 ? 27.836 56.614 45.383 1.00 47.37  ? 34 PHE F O   1 
ATOM 2210 C CB  . PHE F 2 34 ? 24.825 56.517 45.999 1.00 59.39  ? 34 PHE F CB  1 
ATOM 2211 C CG  . PHE F 2 34 ? 24.609 57.977 46.411 1.00 61.43  ? 34 PHE F CG  1 
ATOM 2212 C CD1 . PHE F 2 34 ? 23.657 58.759 45.789 1.00 65.22  ? 34 PHE F CD1 1 
ATOM 2213 C CD2 . PHE F 2 34 ? 25.365 58.510 47.422 1.00 62.96  ? 34 PHE F CD2 1 
ATOM 2214 C CE1 . PHE F 2 34 ? 23.468 60.064 46.184 1.00 65.49  ? 34 PHE F CE1 1 
ATOM 2215 C CE2 . PHE F 2 34 ? 25.167 59.818 47.807 1.00 65.37  ? 34 PHE F CE2 1 
ATOM 2216 C CZ  . PHE F 2 34 ? 24.222 60.600 47.195 1.00 64.27  ? 34 PHE F CZ  1 
ATOM 2217 N N   . ASN F 2 35 ? 26.937 58.075 43.934 1.00 45.81  ? 35 ASN F N   1 
ATOM 2218 C CA  . ASN F 2 35 ? 28.082 58.924 44.019 1.00 48.27  ? 35 ASN F CA  1 
ATOM 2219 C C   . ASN F 2 35 ? 27.759 60.328 44.509 1.00 51.22  ? 35 ASN F C   1 
ATOM 2220 O O   . ASN F 2 35 ? 28.066 60.611 45.677 1.00 46.38  ? 35 ASN F O   1 
ATOM 2221 C CB  . ASN F 2 35 ? 28.747 58.926 42.681 1.00 51.75  ? 35 ASN F CB  1 
ATOM 2222 C CG  . ASN F 2 35 ? 29.548 57.653 42.546 1.00 55.77  ? 35 ASN F CG  1 
ATOM 2223 O OD1 . ASN F 2 35 ? 29.382 56.876 41.597 1.00 60.63  ? 35 ASN F OD1 1 
ATOM 2224 N ND2 . ASN F 2 35 ? 30.446 57.437 43.500 1.00 59.79  ? 35 ASN F ND2 1 
ATOM 2225 N N   . LYS F 2 36 ? 27.154 61.244 43.733 1.00 53.63  ? 36 LYS F N   1 
ATOM 2226 C CA  . LYS F 2 36 ? 26.841 62.557 44.301 1.00 52.04  ? 36 LYS F CA  1 
ATOM 2227 C C   . LYS F 2 36 ? 25.705 63.282 43.592 1.00 48.91  ? 36 LYS F C   1 
ATOM 2228 O O   . LYS F 2 36 ? 25.403 62.989 42.425 1.00 41.04  ? 36 LYS F O   1 
ATOM 2229 C CB  . LYS F 2 36 ? 28.084 63.446 44.281 1.00 57.36  ? 36 LYS F CB  1 
ATOM 2230 C CG  . LYS F 2 36 ? 28.602 63.850 42.917 1.00 68.29  ? 36 LYS F CG  1 
ATOM 2231 C CD  . LYS F 2 36 ? 29.284 65.208 43.029 1.00 74.95  ? 36 LYS F CD  1 
ATOM 2232 C CE  . LYS F 2 36 ? 30.657 65.050 43.647 1.00 78.54  ? 36 LYS F CE  1 
ATOM 2233 N NZ  . LYS F 2 36 ? 31.577 64.548 42.644 1.00 80.55  ? 36 LYS F NZ  1 
ATOM 2234 N N   . VAL F 2 37 ? 24.978 64.171 44.286 1.00 45.67  ? 37 VAL F N   1 
ATOM 2235 C CA  . VAL F 2 37 ? 24.031 65.028 43.561 1.00 37.08  ? 37 VAL F CA  1 
ATOM 2236 C C   . VAL F 2 37 ? 24.823 66.275 43.235 1.00 37.89  ? 37 VAL F C   1 
ATOM 2237 O O   . VAL F 2 37 ? 25.578 66.745 44.094 1.00 40.81  ? 37 VAL F O   1 
ATOM 2238 C CB  . VAL F 2 37 ? 22.783 65.434 44.396 1.00 29.09  ? 37 VAL F CB  1 
ATOM 2239 C CG1 . VAL F 2 37 ? 22.000 66.501 43.647 1.00 31.58  ? 37 VAL F CG1 1 
ATOM 2240 C CG2 . VAL F 2 37 ? 21.799 64.289 44.533 1.00 20.96  ? 37 VAL F CG2 1 
ATOM 2241 N N   . ILE F 2 38 ? 24.730 66.734 41.986 1.00 40.60  ? 38 ILE F N   1 
ATOM 2242 C CA  . ILE F 2 38 ? 25.328 68.011 41.540 1.00 34.30  ? 38 ILE F CA  1 
ATOM 2243 C C   . ILE F 2 38 ? 24.241 69.079 41.355 1.00 33.84  ? 38 ILE F C   1 
ATOM 2244 O O   . ILE F 2 38 ? 23.035 68.828 41.492 1.00 35.51  ? 38 ILE F O   1 
ATOM 2245 C CB  . ILE F 2 38 ? 26.114 67.847 40.176 1.00 24.18  ? 38 ILE F CB  1 
ATOM 2246 C CG1 . ILE F 2 38 ? 25.351 67.071 39.116 1.00 22.58  ? 38 ILE F CG1 1 
ATOM 2247 C CG2 . ILE F 2 38 ? 27.386 67.092 40.487 1.00 24.53  ? 38 ILE F CG2 1 
ATOM 2248 C CD1 . ILE F 2 38 ? 26.131 66.957 37.780 1.00 20.68  ? 38 ILE F CD1 1 
ATOM 2249 N N   . ARG F 2 39 ? 24.661 70.306 41.073 1.00 39.90  ? 39 ARG F N   1 
ATOM 2250 C CA  . ARG F 2 39 ? 23.759 71.428 40.788 1.00 43.31  ? 39 ARG F CA  1 
ATOM 2251 C C   . ARG F 2 39 ? 23.388 71.435 39.296 1.00 37.31  ? 39 ARG F C   1 
ATOM 2252 O O   . ARG F 2 39 ? 24.279 71.172 38.472 1.00 35.59  ? 39 ARG F O   1 
ATOM 2253 C CB  . ARG F 2 39 ? 24.455 72.749 41.126 1.00 44.06  ? 39 ARG F CB  1 
ATOM 2254 C CG  . ARG F 2 39 ? 25.036 72.856 42.516 1.00 48.48  ? 39 ARG F CG  1 
ATOM 2255 C CD  . ARG F 2 39 ? 26.078 73.979 42.491 1.00 55.30  ? 39 ARG F CD  1 
ATOM 2256 N NE  . ARG F 2 39 ? 27.030 73.886 43.590 1.00 59.87  ? 39 ARG F NE  1 
ATOM 2257 C CZ  . ARG F 2 39 ? 26.673 74.122 44.857 1.00 66.10  ? 39 ARG F CZ  1 
ATOM 2258 N NH1 . ARG F 2 39 ? 25.425 74.484 45.229 1.00 62.25  ? 39 ARG F NH1 1 
ATOM 2259 N NH2 . ARG F 2 39 ? 27.617 73.960 45.780 1.00 68.81  ? 39 ARG F NH2 1 
ATOM 2260 N N   . PRO F 2 40 ? 22.167 71.826 38.881 1.00 34.39  ? 40 PRO F N   1 
ATOM 2261 C CA  . PRO F 2 40 ? 21.081 72.302 39.713 1.00 34.41  ? 40 PRO F CA  1 
ATOM 2262 C C   . PRO F 2 40 ? 20.132 71.290 40.348 1.00 36.98  ? 40 PRO F C   1 
ATOM 2263 O O   . PRO F 2 40 ? 19.734 70.326 39.706 1.00 41.88  ? 40 PRO F O   1 
ATOM 2264 C CB  . PRO F 2 40 ? 20.347 73.277 38.802 1.00 34.31  ? 40 PRO F CB  1 
ATOM 2265 C CG  . PRO F 2 40 ? 20.397 72.553 37.469 1.00 30.15  ? 40 PRO F CG  1 
ATOM 2266 C CD  . PRO F 2 40 ? 21.839 72.100 37.468 1.00 31.42  ? 40 PRO F CD  1 
ATOM 2267 N N   . CYS F 2 41 ? 19.671 71.581 41.568 1.00 40.53  ? 41 CYS F N   1 
ATOM 2268 C CA  . CYS F 2 41 ? 18.600 70.818 42.213 1.00 37.34  ? 41 CYS F CA  1 
ATOM 2269 C C   . CYS F 2 41 ? 17.388 71.765 42.259 1.00 32.13  ? 41 CYS F C   1 
ATOM 2270 O O   . CYS F 2 41 ? 17.533 72.928 42.627 1.00 23.49  ? 41 CYS F O   1 
ATOM 2271 C CB  . CYS F 2 41 ? 19.028 70.422 43.621 1.00 38.27  ? 41 CYS F CB  1 
ATOM 2272 S SG  . CYS F 2 41 ? 17.873 69.258 44.377 1.00 41.19  ? 41 CYS F SG  1 
ATOM 2273 N N   . MET F 2 42 ? 16.181 71.305 41.972 1.00 26.49  ? 42 MET F N   1 
ATOM 2274 C CA  . MET F 2 42 ? 15.056 72.153 41.797 1.00 23.61  ? 42 MET F CA  1 
ATOM 2275 C C   . MET F 2 42 ? 13.891 71.524 42.530 1.00 32.59  ? 42 MET F C   1 
ATOM 2276 O O   . MET F 2 42 ? 13.653 70.325 42.299 1.00 35.99  ? 42 MET F O   1 
ATOM 2277 C CB  . MET F 2 42 ? 14.790 72.220 40.319 1.00 26.62  ? 42 MET F CB  1 
ATOM 2278 C CG  . MET F 2 42 ? 14.028 73.406 39.743 1.00 36.43  ? 42 MET F CG  1 
ATOM 2279 S SD  . MET F 2 42 ? 15.172 74.456 38.802 1.00 47.07  ? 42 MET F SD  1 
ATOM 2280 C CE  . MET F 2 42 ? 14.103 75.073 37.533 1.00 39.75  ? 42 MET F CE  1 
ATOM 2281 N N   . LYS F 2 43 ? 13.148 72.285 43.374 1.00 38.19  ? 43 LYS F N   1 
ATOM 2282 C CA  . LYS F 2 43 ? 11.993 71.781 44.120 1.00 32.93  ? 43 LYS F CA  1 
ATOM 2283 C C   . LYS F 2 43 ? 10.775 72.467 43.621 1.00 25.92  ? 43 LYS F C   1 
ATOM 2284 O O   . LYS F 2 43 ? 10.883 73.626 43.293 1.00 25.05  ? 43 LYS F O   1 
ATOM 2285 C CB  . LYS F 2 43 ? 12.145 72.038 45.624 1.00 32.62  ? 43 LYS F CB  1 
ATOM 2286 C CG  . LYS F 2 43 ? 11.416 73.109 46.469 1.00 27.89  ? 43 LYS F CG  1 
ATOM 2287 C CD  . LYS F 2 43 ? 10.801 72.434 47.716 1.00 18.30  ? 43 LYS F CD  1 
ATOM 2288 C CE  . LYS F 2 43 ? 10.436 73.374 48.822 1.00 11.78  ? 43 LYS F CE  1 
ATOM 2289 N NZ  . LYS F 2 43 ? 11.605 74.074 49.332 1.00 22.61  ? 43 LYS F NZ  1 
ATOM 2290 N N   . LYS F 2 44 ? 9.661  71.781 43.524 1.00 28.80  ? 44 LYS F N   1 
ATOM 2291 C CA  . LYS F 2 44 ? 8.427  72.327 42.991 1.00 32.93  ? 44 LYS F CA  1 
ATOM 2292 C C   . LYS F 2 44 ? 7.369  72.116 44.038 1.00 40.54  ? 44 LYS F C   1 
ATOM 2293 O O   . LYS F 2 44 ? 7.113  70.953 44.387 1.00 44.82  ? 44 LYS F O   1 
ATOM 2294 C CB  . LYS F 2 44 ? 7.958  71.619 41.690 1.00 32.44  ? 44 LYS F CB  1 
ATOM 2295 C CG  . LYS F 2 44 ? 6.534  72.010 41.229 1.00 31.50  ? 44 LYS F CG  1 
ATOM 2296 C CD  . LYS F 2 44 ? 6.210  71.530 39.836 1.00 32.04  ? 44 LYS F CD  1 
ATOM 2297 C CE  . LYS F 2 44 ? 4.911  70.762 39.778 1.00 39.30  ? 44 LYS F CE  1 
ATOM 2298 N NZ  . LYS F 2 44 ? 3.972  71.336 38.831 1.00 38.94  ? 44 LYS F NZ  1 
ATOM 2299 N N   . THR F 2 45 ? 6.760  73.200 44.544 1.00 41.19  ? 45 THR F N   1 
ATOM 2300 C CA  . THR F 2 45 ? 5.757  73.042 45.562 1.00 32.34  ? 45 THR F CA  1 
ATOM 2301 C C   . THR F 2 45 ? 4.417  72.967 44.858 1.00 32.16  ? 45 THR F C   1 
ATOM 2302 O O   . THR F 2 45 ? 4.155  73.641 43.827 1.00 32.44  ? 45 THR F O   1 
ATOM 2303 C CB  . THR F 2 45 ? 5.875  74.210 46.527 1.00 38.01  ? 45 THR F CB  1 
ATOM 2304 O OG1 . THR F 2 45 ? 7.240  74.308 46.943 1.00 33.48  ? 45 THR F OG1 1 
ATOM 2305 C CG2 . THR F 2 45 ? 5.020  73.995 47.776 1.00 41.14  ? 45 THR F CG2 1 
ATOM 2306 N N   . ILE F 2 46 ? 3.642  71.996 45.333 1.00 26.98  ? 46 ILE F N   1 
ATOM 2307 C CA  . ILE F 2 46 ? 2.346  71.717 44.800 1.00 29.37  ? 46 ILE F CA  1 
ATOM 2308 C C   . ILE F 2 46 ? 1.317  72.106 45.874 1.00 42.15  ? 46 ILE F C   1 
ATOM 2309 O O   . ILE F 2 46 ? 1.426  71.630 47.008 1.00 48.87  ? 46 ILE F O   1 
ATOM 2310 C CB  . ILE F 2 46 ? 2.307  70.227 44.481 1.00 32.82  ? 46 ILE F CB  1 
ATOM 2311 C CG1 . ILE F 2 46 ? 3.382  69.844 43.469 1.00 38.81  ? 46 ILE F CG1 1 
ATOM 2312 C CG2 . ILE F 2 46 ? 0.915  69.888 44.010 1.00 33.70  ? 46 ILE F CG2 1 
ATOM 2313 C CD1 . ILE F 2 46 ? 3.130  68.472 42.757 1.00 37.90  ? 46 ILE F CD1 1 
ATOM 2314 N N   . TYR F 2 47 ? 0.298  72.955 45.600 1.00 46.53  ? 47 TYR F N   1 
ATOM 2315 C CA  . TYR F 2 47 ? -0.690 73.393 46.605 1.00 42.61  ? 47 TYR F CA  1 
ATOM 2316 C C   . TYR F 2 47 ? -2.017 72.682 46.428 1.00 50.65  ? 47 TYR F C   1 
ATOM 2317 O O   . TYR F 2 47 ? -2.831 72.472 47.337 1.00 45.78  ? 47 TYR F O   1 
ATOM 2318 C CB  . TYR F 2 47 ? -0.870 74.881 46.484 1.00 30.27  ? 47 TYR F CB  1 
ATOM 2319 C CG  . TYR F 2 47 ? 0.404  75.604 46.906 1.00 26.83  ? 47 TYR F CG  1 
ATOM 2320 C CD1 . TYR F 2 47 ? 0.651  75.744 48.249 1.00 25.92  ? 47 TYR F CD1 1 
ATOM 2321 C CD2 . TYR F 2 47 ? 1.332  76.062 45.984 1.00 25.46  ? 47 TYR F CD2 1 
ATOM 2322 C CE1 . TYR F 2 47 ? 1.801  76.332 48.678 1.00 20.66  ? 47 TYR F CE1 1 
ATOM 2323 C CE2 . TYR F 2 47 ? 2.505  76.648 46.413 1.00 22.22  ? 47 TYR F CE2 1 
ATOM 2324 C CZ  . TYR F 2 47 ? 2.703  76.766 47.762 1.00 22.62  ? 47 TYR F CZ  1 
ATOM 2325 O OH  . TYR F 2 47 ? 3.839  77.356 48.251 1.00 36.06  ? 47 TYR F OH  1 
ATOM 2326 N N   . GLU F 2 48 ? -2.216 72.323 45.177 1.00 64.31  ? 48 GLU F N   1 
ATOM 2327 C CA  . GLU F 2 48 ? -3.344 71.551 44.723 1.00 79.56  ? 48 GLU F CA  1 
ATOM 2328 C C   . GLU F 2 48 ? -2.867 71.148 43.314 1.00 87.84  ? 48 GLU F C   1 
ATOM 2329 O O   . GLU F 2 48 ? -2.296 71.965 42.570 1.00 89.00  ? 48 GLU F O   1 
ATOM 2330 C CB  . GLU F 2 48 ? -4.583 72.460 44.715 1.00 82.20  ? 48 GLU F CB  1 
ATOM 2331 C CG  . GLU F 2 48 ? -5.890 71.817 45.187 1.00 85.00  ? 48 GLU F CG  1 
ATOM 2332 C CD  . GLU F 2 48 ? -7.005 71.772 44.131 1.00 89.21  ? 48 GLU F CD  1 
ATOM 2333 O OE1 . GLU F 2 48 ? -6.990 72.595 43.197 1.00 89.11  ? 48 GLU F OE1 1 
ATOM 2334 O OE2 . GLU F 2 48 ? -7.889 70.907 44.254 1.00 90.73  ? 48 GLU F OE2 1 
ATOM 2335 N N   . ASN F 2 49 ? -2.850 69.842 43.033 1.00 95.21  ? 49 ASN F N   1 
ATOM 2336 C CA  . ASN F 2 49 ? -2.512 69.314 41.720 1.00 101.00 ? 49 ASN F CA  1 
ATOM 2337 C C   . ASN F 2 49 ? -3.890 68.843 41.256 1.00 103.83 ? 49 ASN F C   1 
ATOM 2338 O O   . ASN F 2 49 ? -4.726 68.462 42.088 1.00 98.98  ? 49 ASN F O   1 
ATOM 2339 C CB  . ASN F 2 49 ? -1.445 68.190 41.919 1.00 105.07 ? 49 ASN F CB  1 
ATOM 2340 C CG  . ASN F 2 49 ? -1.325 66.992 40.958 1.00 109.42 ? 49 ASN F CG  1 
ATOM 2341 O OD1 . ASN F 2 49 ? -1.895 65.929 41.183 1.00 111.53 ? 49 ASN F OD1 1 
ATOM 2342 N ND2 . ASN F 2 49 ? -0.490 66.927 39.932 1.00 111.35 ? 49 ASN F ND2 1 
ATOM 2343 N N   . GLU F 2 50 ? -4.119 69.139 39.981 1.00 109.64 ? 50 GLU F N   1 
ATOM 2344 C CA  . GLU F 2 50 ? -5.348 68.909 39.227 1.00 114.45 ? 50 GLU F CA  1 
ATOM 2345 C C   . GLU F 2 50 ? -5.539 67.413 38.840 1.00 117.77 ? 50 GLU F C   1 
ATOM 2346 O O   . GLU F 2 50 ? -6.615 67.050 38.349 1.00 120.73 ? 50 GLU F O   1 
ATOM 2347 C CB  . GLU F 2 50 ? -5.199 69.896 38.026 1.00 113.60 ? 50 GLU F CB  1 
ATOM 2348 C CG  . GLU F 2 50 ? -6.136 69.960 36.799 1.00 112.22 ? 50 GLU F CG  1 
ATOM 2349 C CD  . GLU F 2 50 ? -5.451 70.470 35.519 1.00 109.42 ? 50 GLU F CD  1 
ATOM 2350 O OE1 . GLU F 2 50 ? -4.381 69.966 35.161 1.00 110.73 ? 50 GLU F OE1 1 
ATOM 2351 O OE2 . GLU F 2 50 ? -5.991 71.360 34.863 1.00 105.85 ? 50 GLU F OE2 1 
ATOM 2352 O OXT . GLU F 2 50 ? -4.613 66.613 39.031 1.00 118.80 ? 50 GLU F OXT 1 
ATOM 2353 N N   . ARG G 1 1  ? 33.957 87.950 27.617 1.00 62.90  ? 2  ARG G N   1 
ATOM 2354 C CA  . ARG G 1 1  ? 35.226 88.368 28.169 1.00 66.31  ? 2  ARG G CA  1 
ATOM 2355 C C   . ARG G 1 1  ? 35.342 87.996 29.628 1.00 67.93  ? 2  ARG G C   1 
ATOM 2356 O O   . ARG G 1 1  ? 36.290 87.301 29.959 1.00 66.12  ? 2  ARG G O   1 
ATOM 2357 C CB  . ARG G 1 1  ? 35.456 89.870 28.123 1.00 65.03  ? 2  ARG G CB  1 
ATOM 2358 C CG  . ARG G 1 1  ? 35.915 90.387 26.796 1.00 63.93  ? 2  ARG G CG  1 
ATOM 2359 C CD  . ARG G 1 1  ? 37.336 90.003 26.451 1.00 60.66  ? 2  ARG G CD  1 
ATOM 2360 N NE  . ARG G 1 1  ? 38.144 91.166 26.715 1.00 70.45  ? 2  ARG G NE  1 
ATOM 2361 C CZ  . ARG G 1 1  ? 38.518 92.012 25.745 1.00 74.54  ? 2  ARG G CZ  1 
ATOM 2362 N NH1 . ARG G 1 1  ? 38.211 91.768 24.452 1.00 73.51  ? 2  ARG G NH1 1 
ATOM 2363 N NH2 . ARG G 1 1  ? 39.228 93.107 26.107 1.00 72.44  ? 2  ARG G NH2 1 
ATOM 2364 N N   . GLU G 1 2  ? 34.350 88.377 30.445 1.00 62.33  ? 3  GLU G N   1 
ATOM 2365 C CA  . GLU G 1 2  ? 34.445 88.251 31.891 1.00 53.37  ? 3  GLU G CA  1 
ATOM 2366 C C   . GLU G 1 2  ? 33.243 87.437 32.302 1.00 42.70  ? 3  GLU G C   1 
ATOM 2367 O O   . GLU G 1 2  ? 33.262 86.663 33.237 1.00 34.18  ? 3  GLU G O   1 
ATOM 2368 C CB  . GLU G 1 2  ? 34.478 89.678 32.545 1.00 59.37  ? 3  GLU G CB  1 
ATOM 2369 C CG  . GLU G 1 2  ? 33.259 90.620 32.686 1.00 63.63  ? 3  GLU G CG  1 
ATOM 2370 C CD  . GLU G 1 2  ? 32.729 91.286 31.416 1.00 63.97  ? 3  GLU G CD  1 
ATOM 2371 O OE1 . GLU G 1 2  ? 33.295 92.292 30.983 1.00 66.75  ? 3  GLU G OE1 1 
ATOM 2372 O OE2 . GLU G 1 2  ? 31.744 90.805 30.866 1.00 57.60  ? 3  GLU G OE2 1 
ATOM 2373 N N   . ILE G 1 3  ? 32.124 87.719 31.667 1.00 39.55  ? 4  ILE G N   1 
ATOM 2374 C CA  . ILE G 1 3  ? 31.076 86.730 31.491 1.00 41.05  ? 4  ILE G CA  1 
ATOM 2375 C C   . ILE G 1 3  ? 31.550 86.237 30.088 1.00 45.22  ? 4  ILE G C   1 
ATOM 2376 O O   . ILE G 1 3  ? 32.237 86.989 29.337 1.00 49.76  ? 4  ILE G O   1 
ATOM 2377 C CB  . ILE G 1 3  ? 29.599 87.361 31.360 1.00 39.41  ? 4  ILE G CB  1 
ATOM 2378 C CG1 . ILE G 1 3  ? 29.157 88.214 32.539 1.00 32.96  ? 4  ILE G CG1 1 
ATOM 2379 C CG2 . ILE G 1 3  ? 28.597 86.219 31.249 1.00 37.80  ? 4  ILE G CG2 1 
ATOM 2380 C CD1 . ILE G 1 3  ? 28.878 87.517 33.862 1.00 25.25  ? 4  ILE G CD1 1 
ATOM 2381 N N   . LYS G 1 4  ? 31.339 84.969 29.705 1.00 39.34  ? 5  LYS G N   1 
ATOM 2382 C CA  . LYS G 1 4  ? 31.630 84.663 28.341 1.00 33.84  ? 5  LYS G CA  1 
ATOM 2383 C C   . LYS G 1 4  ? 30.334 84.374 27.631 1.00 31.08  ? 5  LYS G C   1 
ATOM 2384 O O   . LYS G 1 4  ? 30.197 84.863 26.487 1.00 28.69  ? 5  LYS G O   1 
ATOM 2385 C CB  . LYS G 1 4  ? 32.624 83.481 28.237 1.00 43.59  ? 5  LYS G CB  1 
ATOM 2386 C CG  . LYS G 1 4  ? 34.012 84.113 27.934 1.00 53.21  ? 5  LYS G CG  1 
ATOM 2387 C CD  . LYS G 1 4  ? 35.293 83.288 27.615 1.00 59.22  ? 5  LYS G CD  1 
ATOM 2388 C CE  . LYS G 1 4  ? 36.581 84.157 27.428 1.00 57.82  ? 5  LYS G CE  1 
ATOM 2389 N NZ  . LYS G 1 4  ? 36.966 84.913 28.597 1.00 55.62  ? 5  LYS G NZ  1 
ATOM 2390 N N   . GLY G 1 5  ? 29.334 83.786 28.285 1.00 21.83  ? 6  GLY G N   1 
ATOM 2391 C CA  . GLY G 1 5  ? 28.090 83.484 27.586 1.00 14.72  ? 6  GLY G CA  1 
ATOM 2392 C C   . GLY G 1 5  ? 27.040 82.972 28.537 1.00 14.59  ? 6  GLY G C   1 
ATOM 2393 O O   . GLY G 1 5  ? 27.324 82.998 29.731 1.00 21.84  ? 6  GLY G O   1 
ATOM 2394 N N   . TYR G 1 6  ? 25.853 82.566 28.070 1.00 23.38  ? 7  TYR G N   1 
ATOM 2395 C CA  . TYR G 1 6  ? 24.737 82.068 28.904 1.00 33.66  ? 7  TYR G CA  1 
ATOM 2396 C C   . TYR G 1 6  ? 24.137 80.871 28.186 1.00 36.09  ? 7  TYR G C   1 
ATOM 2397 O O   . TYR G 1 6  ? 24.358 80.752 26.963 1.00 34.31  ? 7  TYR G O   1 
ATOM 2398 C CB  . TYR G 1 6  ? 23.478 83.003 29.076 1.00 34.37  ? 7  TYR G CB  1 
ATOM 2399 C CG  . TYR G 1 6  ? 23.823 84.444 29.316 1.00 36.16  ? 7  TYR G CG  1 
ATOM 2400 C CD1 . TYR G 1 6  ? 24.108 85.302 28.271 1.00 31.62  ? 7  TYR G CD1 1 
ATOM 2401 C CD2 . TYR G 1 6  ? 23.993 84.827 30.617 1.00 41.26  ? 7  TYR G CD2 1 
ATOM 2402 C CE1 . TYR G 1 6  ? 24.610 86.554 28.557 1.00 34.51  ? 7  TYR G CE1 1 
ATOM 2403 C CE2 . TYR G 1 6  ? 24.481 86.078 30.901 1.00 39.34  ? 7  TYR G CE2 1 
ATOM 2404 C CZ  . TYR G 1 6  ? 24.795 86.928 29.878 1.00 37.80  ? 7  TYR G CZ  1 
ATOM 2405 O OH  . TYR G 1 6  ? 25.345 88.152 30.209 1.00 40.26  ? 7  TYR G OH  1 
ATOM 2406 N N   . GLU G 1 7  ? 23.339 80.059 28.904 1.00 35.43  ? 8  GLU G N   1 
ATOM 2407 C CA  . GLU G 1 7  ? 22.651 78.924 28.303 1.00 33.69  ? 8  GLU G CA  1 
ATOM 2408 C C   . GLU G 1 7  ? 21.265 78.793 28.898 1.00 32.21  ? 8  GLU G C   1 
ATOM 2409 O O   . GLU G 1 7  ? 21.072 79.044 30.089 1.00 40.04  ? 8  GLU G O   1 
ATOM 2410 C CB  . GLU G 1 7  ? 23.410 77.660 28.566 1.00 36.36  ? 8  GLU G CB  1 
ATOM 2411 C CG  . GLU G 1 7  ? 23.782 77.041 27.241 1.00 36.30  ? 8  GLU G CG  1 
ATOM 2412 C CD  . GLU G 1 7  ? 24.715 75.900 27.493 1.00 43.69  ? 8  GLU G CD  1 
ATOM 2413 O OE1 . GLU G 1 7  ? 24.224 74.830 27.886 1.00 44.15  ? 8  GLU G OE1 1 
ATOM 2414 O OE2 . GLU G 1 7  ? 25.924 76.124 27.320 1.00 48.19  ? 8  GLU G OE2 1 
ATOM 2415 N N   . TYR G 1 8  ? 20.282 78.380 28.130 1.00 30.10  ? 9  TYR G N   1 
ATOM 2416 C CA  . TYR G 1 8  ? 18.909 78.383 28.576 1.00 36.94  ? 9  TYR G CA  1 
ATOM 2417 C C   . TYR G 1 8  ? 18.354 76.971 28.531 1.00 41.26  ? 9  TYR G C   1 
ATOM 2418 O O   . TYR G 1 8  ? 18.398 76.335 27.476 1.00 48.45  ? 9  TYR G O   1 
ATOM 2419 C CB  . TYR G 1 8  ? 18.106 79.299 27.644 1.00 38.04  ? 9  TYR G CB  1 
ATOM 2420 C CG  . TYR G 1 8  ? 18.686 80.690 27.429 1.00 45.68  ? 9  TYR G CG  1 
ATOM 2421 C CD1 . TYR G 1 8  ? 18.370 81.669 28.356 1.00 47.09  ? 9  TYR G CD1 1 
ATOM 2422 C CD2 . TYR G 1 8  ? 19.545 80.963 26.362 1.00 44.13  ? 9  TYR G CD2 1 
ATOM 2423 C CE1 . TYR G 1 8  ? 18.902 82.930 28.215 1.00 51.50  ? 9  TYR G CE1 1 
ATOM 2424 C CE2 . TYR G 1 8  ? 20.092 82.227 26.214 1.00 48.77  ? 9  TYR G CE2 1 
ATOM 2425 C CZ  . TYR G 1 8  ? 19.750 83.200 27.149 1.00 53.29  ? 9  TYR G CZ  1 
ATOM 2426 O OH  . TYR G 1 8  ? 20.216 84.499 27.025 1.00 54.88  ? 9  TYR G OH  1 
ATOM 2427 N N   . GLN G 1 9  ? 17.874 76.395 29.605 1.00 37.55  ? 10 GLN G N   1 
ATOM 2428 C CA  . GLN G 1 9  ? 17.239 75.118 29.464 1.00 40.52  ? 10 GLN G CA  1 
ATOM 2429 C C   . GLN G 1 9  ? 15.770 75.490 29.348 1.00 42.53  ? 10 GLN G C   1 
ATOM 2430 O O   . GLN G 1 9  ? 15.233 76.024 30.325 1.00 52.57  ? 10 GLN G O   1 
ATOM 2431 C CB  . GLN G 1 9  ? 17.588 74.257 30.707 1.00 44.29  ? 10 GLN G CB  1 
ATOM 2432 C CG  . GLN G 1 9  ? 18.947 73.518 30.493 1.00 48.86  ? 10 GLN G CG  1 
ATOM 2433 C CD  . GLN G 1 9  ? 19.748 72.891 31.654 1.00 51.21  ? 10 GLN G CD  1 
ATOM 2434 O OE1 . GLN G 1 9  ? 19.295 72.459 32.720 1.00 46.12  ? 10 GLN G OE1 1 
ATOM 2435 N NE2 . GLN G 1 9  ? 21.058 72.880 31.436 1.00 51.89  ? 10 GLN G NE2 1 
ATOM 2436 N N   . LEU G 1 10 ? 15.127 75.317 28.186 1.00 34.17  ? 11 LEU G N   1 
ATOM 2437 C CA  . LEU G 1 10 ? 13.711 75.648 27.956 1.00 33.09  ? 11 LEU G CA  1 
ATOM 2438 C C   . LEU G 1 10 ? 12.754 74.476 27.728 1.00 33.80  ? 11 LEU G C   1 
ATOM 2439 O O   . LEU G 1 10 ? 13.155 73.492 27.099 1.00 37.92  ? 11 LEU G O   1 
ATOM 2440 C CB  . LEU G 1 10 ? 13.436 76.468 26.691 1.00 27.13  ? 11 LEU G CB  1 
ATOM 2441 C CG  . LEU G 1 10 ? 13.834 77.861 26.436 1.00 18.20  ? 11 LEU G CG  1 
ATOM 2442 C CD1 . LEU G 1 10 ? 15.285 77.973 26.228 1.00 13.12  ? 11 LEU G CD1 1 
ATOM 2443 C CD2 . LEU G 1 10 ? 13.201 78.272 25.156 1.00 21.28  ? 11 LEU G CD2 1 
ATOM 2444 N N   . TYR G 1 11 ? 11.465 74.536 28.096 1.00 34.43  ? 12 TYR G N   1 
ATOM 2445 C CA  . TYR G 1 11 ? 10.523 73.525 27.592 1.00 35.88  ? 12 TYR G CA  1 
ATOM 2446 C C   . TYR G 1 11 ? 9.632  74.132 26.513 1.00 39.79  ? 12 TYR G C   1 
ATOM 2447 O O   . TYR G 1 11 ? 8.727  74.952 26.760 1.00 32.17  ? 12 TYR G O   1 
ATOM 2448 C CB  . TYR G 1 11 ? 9.585  73.025 28.624 1.00 37.28  ? 12 TYR G CB  1 
ATOM 2449 C CG  . TYR G 1 11 ? 10.187 72.182 29.708 1.00 38.53  ? 12 TYR G CG  1 
ATOM 2450 C CD1 . TYR G 1 11 ? 11.126 72.685 30.567 1.00 42.28  ? 12 TYR G CD1 1 
ATOM 2451 C CD2 . TYR G 1 11 ? 9.717  70.910 29.840 1.00 38.07  ? 12 TYR G CD2 1 
ATOM 2452 C CE1 . TYR G 1 11 ? 11.592 71.885 31.582 1.00 47.21  ? 12 TYR G CE1 1 
ATOM 2453 C CE2 . TYR G 1 11 ? 10.178 70.114 30.848 1.00 45.18  ? 12 TYR G CE2 1 
ATOM 2454 C CZ  . TYR G 1 11 ? 11.115 70.602 31.712 1.00 48.21  ? 12 TYR G CZ  1 
ATOM 2455 O OH  . TYR G 1 11 ? 11.604 69.760 32.689 1.00 52.54  ? 12 TYR G OH  1 
ATOM 2456 N N   . VAL G 1 12 ? 9.877  73.785 25.258 1.00 46.04  ? 13 VAL G N   1 
ATOM 2457 C CA  . VAL G 1 12 ? 9.073  74.385 24.194 1.00 48.91  ? 13 VAL G CA  1 
ATOM 2458 C C   . VAL G 1 12 ? 7.892  73.493 23.804 1.00 52.94  ? 13 VAL G C   1 
ATOM 2459 O O   . VAL G 1 12 ? 8.062  72.295 23.553 1.00 52.94  ? 13 VAL G O   1 
ATOM 2460 C CB  . VAL G 1 12 ? 9.955  74.662 22.939 1.00 42.10  ? 13 VAL G CB  1 
ATOM 2461 C CG1 . VAL G 1 12 ? 9.044  75.434 21.947 1.00 42.80  ? 13 VAL G CG1 1 
ATOM 2462 C CG2 . VAL G 1 12 ? 11.245 75.423 23.282 1.00 26.15  ? 13 VAL G CG2 1 
ATOM 2463 N N   . TYR G 1 13 ? 6.667  74.010 23.870 1.00 60.02  ? 14 TYR G N   1 
ATOM 2464 C CA  . TYR G 1 13 ? 5.537  73.329 23.254 1.00 63.01  ? 14 TYR G CA  1 
ATOM 2465 C C   . TYR G 1 13 ? 5.603  73.683 21.774 1.00 63.88  ? 14 TYR G C   1 
ATOM 2466 O O   . TYR G 1 13 ? 5.700  74.872 21.413 1.00 69.59  ? 14 TYR G O   1 
ATOM 2467 C CB  . TYR G 1 13 ? 4.165  73.820 23.705 1.00 66.06  ? 14 TYR G CB  1 
ATOM 2468 C CG  . TYR G 1 13 ? 3.562  73.074 24.865 1.00 74.06  ? 14 TYR G CG  1 
ATOM 2469 C CD1 . TYR G 1 13 ? 3.023  71.824 24.656 1.00 76.08  ? 14 TYR G CD1 1 
ATOM 2470 C CD2 . TYR G 1 13 ? 3.569  73.650 26.121 1.00 78.13  ? 14 TYR G CD2 1 
ATOM 2471 C CE1 . TYR G 1 13 ? 2.488  71.133 25.720 1.00 81.99  ? 14 TYR G CE1 1 
ATOM 2472 C CE2 . TYR G 1 13 ? 3.030  72.961 27.187 1.00 82.75  ? 14 TYR G CE2 1 
ATOM 2473 C CZ  . TYR G 1 13 ? 2.496  71.704 26.981 1.00 84.62  ? 14 TYR G CZ  1 
ATOM 2474 O OH  . TYR G 1 13 ? 1.964  71.001 28.052 1.00 87.12  ? 14 TYR G OH  1 
ATOM 2475 N N   . ALA G 1 14 ? 5.594  72.688 20.905 1.00 59.40  ? 15 ALA G N   1 
ATOM 2476 C CA  . ALA G 1 14 ? 5.540  72.902 19.475 1.00 53.68  ? 15 ALA G CA  1 
ATOM 2477 C C   . ALA G 1 14 ? 4.735  71.733 18.976 1.00 52.06  ? 15 ALA G C   1 
ATOM 2478 O O   . ALA G 1 14 ? 4.873  70.633 19.513 1.00 51.20  ? 15 ALA G O   1 
ATOM 2479 C CB  . ALA G 1 14 ? 6.925  72.845 18.853 1.00 53.80  ? 15 ALA G CB  1 
ATOM 2480 N N   . SER G 1 15 ? 3.834  71.970 18.035 1.00 50.69  ? 16 SER G N   1 
ATOM 2481 C CA  . SER G 1 15 ? 2.965  70.951 17.474 1.00 50.43  ? 16 SER G CA  1 
ATOM 2482 C C   . SER G 1 15 ? 2.364  70.061 18.539 1.00 52.54  ? 16 SER G C   1 
ATOM 2483 O O   . SER G 1 15 ? 2.347  68.835 18.436 1.00 51.91  ? 16 SER G O   1 
ATOM 2484 C CB  . SER G 1 15 ? 3.745  70.125 16.458 1.00 45.81  ? 16 SER G CB  1 
ATOM 2485 O OG  . SER G 1 15 ? 3.985  70.947 15.320 1.00 49.08  ? 16 SER G OG  1 
ATOM 2486 N N   . ASP G 1 16 ? 1.881  70.727 19.589 1.00 49.88  ? 17 ASP G N   1 
ATOM 2487 C CA  . ASP G 1 16 ? 1.217  70.054 20.688 1.00 56.68  ? 17 ASP G CA  1 
ATOM 2488 C C   . ASP G 1 16 ? 1.998  68.894 21.337 1.00 59.63  ? 17 ASP G C   1 
ATOM 2489 O O   . ASP G 1 16 ? 1.424  67.867 21.735 1.00 55.86  ? 17 ASP G O   1 
ATOM 2490 C CB  . ASP G 1 16 ? -0.135 69.570 20.184 1.00 55.55  ? 17 ASP G CB  1 
ATOM 2491 C CG  . ASP G 1 16 ? -0.916 70.718 19.589 1.00 57.50  ? 17 ASP G CG  1 
ATOM 2492 O OD1 . ASP G 1 16 ? -0.665 71.089 18.441 1.00 59.00  ? 17 ASP G OD1 1 
ATOM 2493 O OD2 . ASP G 1 16 ? -1.773 71.241 20.286 1.00 60.48  ? 17 ASP G OD2 1 
ATOM 2494 N N   . LYS G 1 17 ? 3.324  69.065 21.498 1.00 61.99  ? 18 LYS G N   1 
ATOM 2495 C CA  . LYS G 1 17 ? 4.172  68.089 22.192 1.00 61.61  ? 18 LYS G CA  1 
ATOM 2496 C C   . LYS G 1 17 ? 5.185  68.827 23.040 1.00 56.96  ? 18 LYS G C   1 
ATOM 2497 O O   . LYS G 1 17 ? 5.697  69.861 22.616 1.00 54.99  ? 18 LYS G O   1 
ATOM 2498 C CB  . LYS G 1 17 ? 4.965  67.231 21.231 1.00 65.09  ? 18 LYS G CB  1 
ATOM 2499 C CG  . LYS G 1 17 ? 4.154  66.336 20.324 1.00 67.46  ? 18 LYS G CG  1 
ATOM 2500 C CD  . LYS G 1 17 ? 5.032  66.123 19.109 1.00 69.53  ? 18 LYS G CD  1 
ATOM 2501 C CE  . LYS G 1 17 ? 4.199  65.599 17.973 1.00 74.23  ? 18 LYS G CE  1 
ATOM 2502 N NZ  . LYS G 1 17 ? 3.190  66.576 17.600 1.00 78.23  ? 18 LYS G NZ  1 
ATOM 2503 N N   . LEU G 1 18 ? 5.501  68.348 24.230 1.00 53.70  ? 19 LEU G N   1 
ATOM 2504 C CA  . LEU G 1 18 ? 6.477  69.050 25.050 1.00 55.12  ? 19 LEU G CA  1 
ATOM 2505 C C   . LEU G 1 18 ? 7.914  68.673 24.698 1.00 52.08  ? 19 LEU G C   1 
ATOM 2506 O O   . LEU G 1 18 ? 8.296  67.514 24.792 1.00 50.30  ? 19 LEU G O   1 
ATOM 2507 C CB  . LEU G 1 18 ? 6.204  68.754 26.541 1.00 55.61  ? 19 LEU G CB  1 
ATOM 2508 C CG  . LEU G 1 18 ? 6.347  69.860 27.616 1.00 53.22  ? 19 LEU G CG  1 
ATOM 2509 C CD1 . LEU G 1 18 ? 6.536  71.260 27.017 1.00 51.04  ? 19 LEU G CD1 1 
ATOM 2510 C CD2 . LEU G 1 18 ? 5.079  69.845 28.434 1.00 51.12  ? 19 LEU G CD2 1 
ATOM 2511 N N   . PHE G 1 19 ? 8.735  69.610 24.270 1.00 50.67  ? 20 PHE G N   1 
ATOM 2512 C CA  . PHE G 1 19 ? 10.129 69.335 23.974 1.00 48.98  ? 20 PHE G CA  1 
ATOM 2513 C C   . PHE G 1 19 ? 11.043 69.907 25.058 1.00 45.01  ? 20 PHE G C   1 
ATOM 2514 O O   . PHE G 1 19 ? 10.605 70.421 26.094 1.00 49.09  ? 20 PHE G O   1 
ATOM 2515 C CB  . PHE G 1 19 ? 10.507 69.951 22.625 1.00 51.81  ? 20 PHE G CB  1 
ATOM 2516 C CG  . PHE G 1 19 ? 9.839  69.246 21.468 1.00 59.81  ? 20 PHE G CG  1 
ATOM 2517 C CD1 . PHE G 1 19 ? 8.552  69.603 21.109 1.00 61.60  ? 20 PHE G CD1 1 
ATOM 2518 C CD2 . PHE G 1 19 ? 10.515 68.258 20.765 1.00 65.36  ? 20 PHE G CD2 1 
ATOM 2519 C CE1 . PHE G 1 19 ? 7.918  68.942 20.068 1.00 64.44  ? 20 PHE G CE1 1 
ATOM 2520 C CE2 . PHE G 1 19 ? 9.875  67.599 19.722 1.00 67.81  ? 20 PHE G CE2 1 
ATOM 2521 C CZ  . PHE G 1 19 ? 8.579  67.953 19.361 1.00 65.86  ? 20 PHE G CZ  1 
ATOM 2522 N N   . ARG G 1 20 ? 12.343 69.845 24.857 1.00 35.91  ? 21 ARG G N   1 
ATOM 2523 C CA  . ARG G 1 20 ? 13.307 70.430 25.753 1.00 34.99  ? 21 ARG G CA  1 
ATOM 2524 C C   . ARG G 1 20 ? 14.329 71.006 24.836 1.00 35.12  ? 21 ARG G C   1 
ATOM 2525 O O   . ARG G 1 20 ? 14.851 70.231 24.022 1.00 39.84  ? 21 ARG G O   1 
ATOM 2526 C CB  . ARG G 1 20 ? 13.988 69.408 26.586 1.00 34.92  ? 21 ARG G CB  1 
ATOM 2527 C CG  . ARG G 1 20 ? 13.201 69.074 27.811 1.00 38.85  ? 21 ARG G CG  1 
ATOM 2528 C CD  . ARG G 1 20 ? 13.655 69.995 28.923 1.00 42.38  ? 21 ARG G CD  1 
ATOM 2529 N NE  . ARG G 1 20 ? 15.070 69.845 29.246 1.00 37.26  ? 21 ARG G NE  1 
ATOM 2530 C CZ  . ARG G 1 20 ? 15.934 70.825 28.990 1.00 36.44  ? 21 ARG G CZ  1 
ATOM 2531 N NH1 . ARG G 1 20 ? 15.559 71.934 28.368 1.00 34.00  ? 21 ARG G NH1 1 
ATOM 2532 N NH2 . ARG G 1 20 ? 17.217 70.678 29.301 1.00 36.42  ? 21 ARG G NH2 1 
ATOM 2533 N N   . ALA G 1 21 ? 14.592 72.308 24.893 1.00 32.82  ? 22 ALA G N   1 
ATOM 2534 C CA  . ALA G 1 21 ? 15.602 72.876 24.026 1.00 25.84  ? 22 ALA G CA  1 
ATOM 2535 C C   . ALA G 1 21 ? 16.599 73.515 24.931 1.00 22.22  ? 22 ALA G C   1 
ATOM 2536 O O   . ALA G 1 21 ? 16.263 73.906 26.036 1.00 30.72  ? 22 ALA G O   1 
ATOM 2537 C CB  . ALA G 1 21 ? 15.042 73.929 23.073 1.00 19.44  ? 22 ALA G CB  1 
ATOM 2538 N N   . ASP G 1 22 ? 17.845 73.457 24.553 1.00 21.68  ? 23 ASP G N   1 
ATOM 2539 C CA  . ASP G 1 22 ? 18.902 74.056 25.297 1.00 31.02  ? 23 ASP G CA  1 
ATOM 2540 C C   . ASP G 1 22 ? 19.527 75.024 24.301 1.00 32.90  ? 23 ASP G C   1 
ATOM 2541 O O   . ASP G 1 22 ? 19.873 74.600 23.180 1.00 31.40  ? 23 ASP G O   1 
ATOM 2542 C CB  . ASP G 1 22 ? 19.874 72.936 25.755 1.00 40.63  ? 23 ASP G CB  1 
ATOM 2543 C CG  . ASP G 1 22 ? 19.390 71.984 26.879 1.00 42.59  ? 23 ASP G CG  1 
ATOM 2544 O OD1 . ASP G 1 22 ? 18.204 71.673 26.949 1.00 38.35  ? 23 ASP G OD1 1 
ATOM 2545 O OD2 . ASP G 1 22 ? 20.202 71.566 27.709 1.00 41.93  ? 23 ASP G OD2 1 
ATOM 2546 N N   . ILE G 1 23 ? 19.585 76.333 24.616 1.00 30.94  ? 24 ILE G N   1 
ATOM 2547 C CA  . ILE G 1 23 ? 20.114 77.324 23.671 1.00 28.39  ? 24 ILE G CA  1 
ATOM 2548 C C   . ILE G 1 23 ? 21.404 77.951 24.148 1.00 26.34  ? 24 ILE G C   1 
ATOM 2549 O O   . ILE G 1 23 ? 21.620 78.066 25.345 1.00 27.32  ? 24 ILE G O   1 
ATOM 2550 C CB  . ILE G 1 23 ? 18.975 78.339 23.451 1.00 28.23  ? 24 ILE G CB  1 
ATOM 2551 C CG1 . ILE G 1 23 ? 18.131 77.609 22.448 1.00 34.72  ? 24 ILE G CG1 1 
ATOM 2552 C CG2 . ILE G 1 23 ? 19.336 79.700 22.887 1.00 24.24  ? 24 ILE G CG2 1 
ATOM 2553 C CD1 . ILE G 1 23 ? 16.692 78.044 22.259 1.00 39.36  ? 24 ILE G CD1 1 
ATOM 2554 N N   . SER G 1 24 ? 22.348 78.268 23.293 1.00 32.82  ? 25 SER G N   1 
ATOM 2555 C CA  . SER G 1 24 ? 23.533 78.964 23.759 1.00 38.79  ? 25 SER G CA  1 
ATOM 2556 C C   . SER G 1 24 ? 23.416 80.421 23.340 1.00 42.46  ? 25 SER G C   1 
ATOM 2557 O O   . SER G 1 24 ? 22.534 80.746 22.529 1.00 47.05  ? 25 SER G O   1 
ATOM 2558 C CB  . SER G 1 24 ? 24.764 78.294 23.160 1.00 42.36  ? 25 SER G CB  1 
ATOM 2559 O OG  . SER G 1 24 ? 24.605 77.866 21.813 1.00 46.29  ? 25 SER G OG  1 
ATOM 2560 N N   . GLU G 1 25 ? 24.214 81.331 23.887 1.00 43.24  ? 26 GLU G N   1 
ATOM 2561 C CA  . GLU G 1 25 ? 24.119 82.741 23.513 1.00 44.62  ? 26 GLU G CA  1 
ATOM 2562 C C   . GLU G 1 25 ? 25.362 83.458 23.986 1.00 41.78  ? 26 GLU G C   1 
ATOM 2563 O O   . GLU G 1 25 ? 25.580 83.574 25.199 1.00 40.26  ? 26 GLU G O   1 
ATOM 2564 C CB  . GLU G 1 25 ? 22.937 83.422 24.163 1.00 45.90  ? 26 GLU G CB  1 
ATOM 2565 C CG  . GLU G 1 25 ? 22.893 84.877 23.771 1.00 45.10  ? 26 GLU G CG  1 
ATOM 2566 C CD  . GLU G 1 25 ? 21.905 85.611 24.634 1.00 43.90  ? 26 GLU G CD  1 
ATOM 2567 O OE1 . GLU G 1 25 ? 20.724 85.632 24.302 1.00 41.06  ? 26 GLU G OE1 1 
ATOM 2568 O OE2 . GLU G 1 25 ? 22.339 86.154 25.642 1.00 46.87  ? 26 GLU G OE2 1 
ATOM 2569 N N   . ASP G 1 26 ? 26.181 83.906 23.042 1.00 40.49  ? 27 ASP G N   1 
ATOM 2570 C CA  . ASP G 1 26 ? 27.424 84.544 23.380 1.00 43.47  ? 27 ASP G CA  1 
ATOM 2571 C C   . ASP G 1 26 ? 27.156 85.923 23.953 1.00 44.00  ? 27 ASP G C   1 
ATOM 2572 O O   . ASP G 1 26 ? 26.330 86.628 23.410 1.00 49.22  ? 27 ASP G O   1 
ATOM 2573 C CB  . ASP G 1 26 ? 28.253 84.649 22.139 1.00 49.36  ? 27 ASP G CB  1 
ATOM 2574 C CG  . ASP G 1 26 ? 29.749 84.902 22.346 1.00 60.80  ? 27 ASP G CG  1 
ATOM 2575 O OD1 . ASP G 1 26 ? 30.167 85.841 23.039 1.00 63.88  ? 27 ASP G OD1 1 
ATOM 2576 O OD2 . ASP G 1 26 ? 30.521 84.137 21.765 1.00 70.14  ? 27 ASP G OD2 1 
ATOM 2577 N N   . TYR G 1 27 ? 27.896 86.334 24.975 1.00 48.67  ? 28 TYR G N   1 
ATOM 2578 C CA  . TYR G 1 27 ? 27.805 87.631 25.645 1.00 50.53  ? 28 TYR G CA  1 
ATOM 2579 C C   . TYR G 1 27 ? 28.319 88.793 24.787 1.00 53.46  ? 28 TYR G C   1 
ATOM 2580 O O   . TYR G 1 27 ? 27.775 89.898 24.792 1.00 56.71  ? 28 TYR G O   1 
ATOM 2581 C CB  . TYR G 1 27 ? 28.619 87.589 26.934 1.00 47.80  ? 28 TYR G CB  1 
ATOM 2582 C CG  . TYR G 1 27 ? 28.704 88.888 27.703 1.00 44.13  ? 28 TYR G CG  1 
ATOM 2583 C CD1 . TYR G 1 27 ? 27.601 89.267 28.412 1.00 43.40  ? 28 TYR G CD1 1 
ATOM 2584 C CD2 . TYR G 1 27 ? 29.841 89.677 27.684 1.00 45.05  ? 28 TYR G CD2 1 
ATOM 2585 C CE1 . TYR G 1 27 ? 27.608 90.451 29.106 1.00 47.96  ? 28 TYR G CE1 1 
ATOM 2586 C CE2 . TYR G 1 27 ? 29.854 90.877 28.373 1.00 48.48  ? 28 TYR G CE2 1 
ATOM 2587 C CZ  . TYR G 1 27 ? 28.724 91.253 29.080 1.00 47.21  ? 28 TYR G CZ  1 
ATOM 2588 O OH  . TYR G 1 27 ? 28.670 92.422 29.812 1.00 40.93  ? 28 TYR G OH  1 
ATOM 2589 N N   . LYS G 1 28 ? 29.459 88.608 24.122 1.00 53.86  ? 29 LYS G N   1 
ATOM 2590 C CA  . LYS G 1 28 ? 29.990 89.654 23.274 1.00 52.27  ? 29 LYS G CA  1 
ATOM 2591 C C   . LYS G 1 28 ? 29.096 89.887 22.086 1.00 59.98  ? 29 LYS G C   1 
ATOM 2592 O O   . LYS G 1 28 ? 28.486 90.930 21.827 1.00 62.21  ? 29 LYS G O   1 
ATOM 2593 C CB  . LYS G 1 28 ? 31.333 89.367 22.597 1.00 51.09  ? 29 LYS G CB  1 
ATOM 2594 C CG  . LYS G 1 28 ? 32.596 89.282 23.338 1.00 51.48  ? 29 LYS G CG  1 
ATOM 2595 C CD  . LYS G 1 28 ? 33.754 89.996 22.633 1.00 52.92  ? 29 LYS G CD  1 
ATOM 2596 C CE  . LYS G 1 28 ? 34.966 90.043 23.566 1.00 53.06  ? 29 LYS G CE  1 
ATOM 2597 N NZ  . LYS G 1 28 ? 35.018 88.865 24.429 1.00 55.78  ? 29 LYS G NZ  1 
ATOM 2598 N N   . THR G 1 29 ? 29.091 88.849 21.270 1.00 63.67  ? 30 THR G N   1 
ATOM 2599 C CA  . THR G 1 29 ? 28.623 88.950 19.930 1.00 61.58  ? 30 THR G CA  1 
ATOM 2600 C C   . THR G 1 29 ? 27.140 88.916 19.810 1.00 63.80  ? 30 THR G C   1 
ATOM 2601 O O   . THR G 1 29 ? 26.672 89.707 18.990 1.00 66.77  ? 30 THR G O   1 
ATOM 2602 C CB  . THR G 1 29 ? 29.374 87.871 19.175 1.00 62.98  ? 30 THR G CB  1 
ATOM 2603 O OG1 . THR G 1 29 ? 29.986 86.897 20.016 1.00 65.02  ? 30 THR G OG1 1 
ATOM 2604 C CG2 . THR G 1 29 ? 30.529 88.574 18.495 1.00 67.50  ? 30 THR G CG2 1 
ATOM 2605 N N   . ARG G 1 30 ? 26.518 88.215 20.770 1.00 60.18  ? 31 ARG G N   1 
ATOM 2606 C CA  . ARG G 1 30 ? 25.082 87.977 20.920 1.00 56.47  ? 31 ARG G CA  1 
ATOM 2607 C C   . ARG G 1 30 ? 24.536 86.876 20.044 1.00 58.44  ? 31 ARG G C   1 
ATOM 2608 O O   . ARG G 1 30 ? 23.321 86.716 19.891 1.00 63.21  ? 31 ARG G O   1 
ATOM 2609 C CB  . ARG G 1 30 ? 24.237 89.190 20.629 1.00 53.55  ? 31 ARG G CB  1 
ATOM 2610 C CG  . ARG G 1 30 ? 24.693 90.192 21.624 1.00 51.56  ? 31 ARG G CG  1 
ATOM 2611 C CD  . ARG G 1 30 ? 23.598 91.121 21.775 1.00 54.62  ? 31 ARG G CD  1 
ATOM 2612 N NE  . ARG G 1 30 ? 22.824 90.660 22.901 1.00 54.98  ? 31 ARG G NE  1 
ATOM 2613 C CZ  . ARG G 1 30 ? 21.939 91.442 23.494 1.00 52.24  ? 31 ARG G CZ  1 
ATOM 2614 N NH1 . ARG G 1 30 ? 22.133 92.726 23.267 1.00 48.11  ? 31 ARG G NH1 1 
ATOM 2615 N NH2 . ARG G 1 30 ? 21.068 91.169 24.468 1.00 44.86  ? 31 ARG G NH2 1 
ATOM 2616 N N   . GLY G 1 31 ? 25.438 86.062 19.495 1.00 58.04  ? 32 GLY G N   1 
ATOM 2617 C CA  . GLY G 1 31 ? 25.060 84.957 18.616 1.00 53.08  ? 32 GLY G CA  1 
ATOM 2618 C C   . GLY G 1 31 ? 24.389 83.846 19.414 1.00 45.13  ? 32 GLY G C   1 
ATOM 2619 O O   . GLY G 1 31 ? 24.859 83.542 20.520 1.00 45.73  ? 32 GLY G O   1 
ATOM 2620 N N   . ARG G 1 32 ? 23.329 83.251 18.879 1.00 38.35  ? 33 ARG G N   1 
ATOM 2621 C CA  . ARG G 1 32 ? 22.618 82.197 19.565 1.00 41.22  ? 33 ARG G CA  1 
ATOM 2622 C C   . ARG G 1 32 ? 22.642 80.917 18.714 1.00 43.77  ? 33 ARG G C   1 
ATOM 2623 O O   . ARG G 1 32 ? 22.431 81.014 17.505 1.00 46.83  ? 33 ARG G O   1 
ATOM 2624 C CB  . ARG G 1 32 ? 21.211 82.624 19.782 1.00 45.43  ? 33 ARG G CB  1 
ATOM 2625 C CG  . ARG G 1 32 ? 21.003 84.006 20.330 1.00 51.19  ? 33 ARG G CG  1 
ATOM 2626 C CD  . ARG G 1 32 ? 19.508 84.167 20.371 1.00 57.40  ? 33 ARG G CD  1 
ATOM 2627 N NE  . ARG G 1 32 ? 19.105 84.270 21.773 1.00 62.90  ? 33 ARG G NE  1 
ATOM 2628 C CZ  . ARG G 1 32 ? 18.575 85.353 22.300 1.00 62.80  ? 33 ARG G CZ  1 
ATOM 2629 N NH1 . ARG G 1 32 ? 18.425 86.428 21.592 1.00 67.68  ? 33 ARG G NH1 1 
ATOM 2630 N NH2 . ARG G 1 32 ? 18.175 85.382 23.541 1.00 62.83  ? 33 ARG G NH2 1 
ATOM 2631 N N   . LYS G 1 33 ? 22.812 79.701 19.275 1.00 44.32  ? 34 LYS G N   1 
ATOM 2632 C CA  . LYS G 1 33 ? 22.986 78.447 18.533 1.00 40.61  ? 34 LYS G CA  1 
ATOM 2633 C C   . LYS G 1 33 ? 22.189 77.294 19.178 1.00 32.46  ? 34 LYS G C   1 
ATOM 2634 O O   . LYS G 1 33 ? 22.334 77.062 20.377 1.00 28.26  ? 34 LYS G O   1 
ATOM 2635 C CB  . LYS G 1 33 ? 24.504 78.215 18.537 1.00 50.24  ? 34 LYS G CB  1 
ATOM 2636 C CG  . LYS G 1 33 ? 25.046 77.001 17.799 1.00 61.41  ? 34 LYS G CG  1 
ATOM 2637 C CD  . LYS G 1 33 ? 26.286 76.444 18.511 1.00 66.75  ? 34 LYS G CD  1 
ATOM 2638 C CE  . LYS G 1 33 ? 26.367 74.969 18.133 1.00 71.08  ? 34 LYS G CE  1 
ATOM 2639 N NZ  . LYS G 1 33 ? 27.373 74.261 18.907 1.00 72.29  ? 34 LYS G NZ  1 
ATOM 2640 N N   . LEU G 1 34 ? 21.320 76.541 18.476 1.00 29.54  ? 35 LEU G N   1 
ATOM 2641 C CA  . LEU G 1 34 ? 20.539 75.445 19.116 1.00 29.23  ? 35 LEU G CA  1 
ATOM 2642 C C   . LEU G 1 34 ? 21.400 74.245 19.486 1.00 34.05  ? 35 LEU G C   1 
ATOM 2643 O O   . LEU G 1 34 ? 21.898 73.585 18.574 1.00 42.17  ? 35 LEU G O   1 
ATOM 2644 C CB  . LEU G 1 34 ? 19.410 74.916 18.208 1.00 17.46  ? 35 LEU G CB  1 
ATOM 2645 C CG  . LEU G 1 34 ? 18.496 73.775 18.656 1.00 17.31  ? 35 LEU G CG  1 
ATOM 2646 C CD1 . LEU G 1 34 ? 17.745 74.093 19.939 1.00 16.70  ? 35 LEU G CD1 1 
ATOM 2647 C CD2 . LEU G 1 34 ? 17.423 73.571 17.601 1.00 16.65  ? 35 LEU G CD2 1 
ATOM 2648 N N   . LEU G 1 35 ? 21.554 73.940 20.780 1.00 37.05  ? 36 LEU G N   1 
ATOM 2649 C CA  . LEU G 1 35 ? 22.379 72.833 21.212 1.00 30.88  ? 36 LEU G CA  1 
ATOM 2650 C C   . LEU G 1 35 ? 21.665 71.519 21.269 1.00 36.37  ? 36 LEU G C   1 
ATOM 2651 O O   . LEU G 1 35 ? 22.363 70.580 20.908 1.00 48.44  ? 36 LEU G O   1 
ATOM 2652 C CB  . LEU G 1 35 ? 22.967 73.011 22.576 1.00 21.84  ? 36 LEU G CB  1 
ATOM 2653 C CG  . LEU G 1 35 ? 23.843 74.196 22.560 1.00 22.77  ? 36 LEU G CG  1 
ATOM 2654 C CD1 . LEU G 1 35 ? 24.402 74.367 23.948 1.00 22.53  ? 36 LEU G CD1 1 
ATOM 2655 C CD2 . LEU G 1 35 ? 24.888 74.065 21.475 1.00 21.86  ? 36 LEU G CD2 1 
ATOM 2656 N N   . ARG G 1 36 ? 20.399 71.327 21.688 1.00 26.84  ? 37 ARG G N   1 
ATOM 2657 C CA  . ARG G 1 36 ? 19.813 69.973 21.736 1.00 30.97  ? 37 ARG G CA  1 
ATOM 2658 C C   . ARG G 1 36 ? 18.301 70.112 21.660 1.00 31.78  ? 37 ARG G C   1 
ATOM 2659 O O   . ARG G 1 36 ? 17.755 70.979 22.320 1.00 38.92  ? 37 ARG G O   1 
ATOM 2660 C CB  . ARG G 1 36 ? 20.140 69.199 23.063 1.00 29.58  ? 37 ARG G CB  1 
ATOM 2661 C CG  . ARG G 1 36 ? 21.608 69.062 23.442 1.00 33.50  ? 37 ARG G CG  1 
ATOM 2662 C CD  . ARG G 1 36 ? 21.893 69.307 24.896 1.00 41.40  ? 37 ARG G CD  1 
ATOM 2663 N NE  . ARG G 1 36 ? 23.304 69.604 25.148 1.00 51.13  ? 37 ARG G NE  1 
ATOM 2664 C CZ  . ARG G 1 36 ? 23.670 70.576 26.006 1.00 55.01  ? 37 ARG G CZ  1 
ATOM 2665 N NH1 . ARG G 1 36 ? 22.780 71.406 26.555 1.00 55.44  ? 37 ARG G NH1 1 
ATOM 2666 N NH2 . ARG G 1 36 ? 24.961 70.767 26.310 1.00 56.60  ? 37 ARG G NH2 1 
ATOM 2667 N N   . PHE G 1 37 ? 17.552 69.336 20.913 1.00 36.41  ? 38 PHE G N   1 
ATOM 2668 C CA  . PHE G 1 37 ? 16.114 69.521 20.835 1.00 37.34  ? 38 PHE G CA  1 
ATOM 2669 C C   . PHE G 1 37 ? 15.574 68.113 20.926 1.00 39.37  ? 38 PHE G C   1 
ATOM 2670 O O   . PHE G 1 37 ? 15.650 67.313 19.986 1.00 43.45  ? 38 PHE G O   1 
ATOM 2671 C CB  . PHE G 1 37 ? 15.784 70.188 19.493 1.00 38.92  ? 38 PHE G CB  1 
ATOM 2672 C CG  . PHE G 1 37 ? 14.381 70.763 19.391 1.00 42.95  ? 38 PHE G CG  1 
ATOM 2673 C CD1 . PHE G 1 37 ? 13.277 69.962 19.214 1.00 45.00  ? 38 PHE G CD1 1 
ATOM 2674 C CD2 . PHE G 1 37 ? 14.208 72.125 19.504 1.00 45.75  ? 38 PHE G CD2 1 
ATOM 2675 C CE1 . PHE G 1 37 ? 12.019 70.531 19.154 1.00 46.09  ? 38 PHE G CE1 1 
ATOM 2676 C CE2 . PHE G 1 37 ? 12.946 72.677 19.445 1.00 43.85  ? 38 PHE G CE2 1 
ATOM 2677 C CZ  . PHE G 1 37 ? 11.840 71.882 19.270 1.00 44.85  ? 38 PHE G CZ  1 
ATOM 2678 N N   . ASN G 1 38 ? 15.150 67.701 22.089 1.00 37.33  ? 39 ASN G N   1 
ATOM 2679 C CA  . ASN G 1 38 ? 14.741 66.329 22.202 1.00 35.92  ? 39 ASN G CA  1 
ATOM 2680 C C   . ASN G 1 38 ? 13.334 66.280 22.581 1.00 37.31  ? 39 ASN G C   1 
ATOM 2681 O O   . ASN G 1 38 ? 12.696 67.304 22.744 1.00 45.98  ? 39 ASN G O   1 
ATOM 2682 C CB  . ASN G 1 38 ? 15.547 65.640 23.248 1.00 38.53  ? 39 ASN G CB  1 
ATOM 2683 C CG  . ASN G 1 38 ? 17.020 65.609 22.872 1.00 45.74  ? 39 ASN G CG  1 
ATOM 2684 O OD1 . ASN G 1 38 ? 17.878 65.862 23.705 1.00 49.12  ? 39 ASN G OD1 1 
ATOM 2685 N ND2 . ASN G 1 38 ? 17.444 65.381 21.632 1.00 47.76  ? 39 ASN G ND2 1 
ATOM 2686 N N   . GLY G 1 39 ? 12.808 65.096 22.642 1.00 44.01  ? 40 GLY G N   1 
ATOM 2687 C CA  . GLY G 1 39 ? 11.502 64.904 23.238 1.00 40.47  ? 40 GLY G CA  1 
ATOM 2688 C C   . GLY G 1 39 ? 10.633 64.106 22.284 1.00 37.33  ? 40 GLY G C   1 
ATOM 2689 O O   . GLY G 1 39 ? 11.221 63.471 21.411 1.00 42.15  ? 40 GLY G O   1 
ATOM 2690 N N   . PRO G 1 40 ? 9.316  64.031 22.344 1.00 35.89  ? 41 PRO G N   1 
ATOM 2691 C CA  . PRO G 1 40 ? 8.507  64.677 23.353 1.00 44.57  ? 41 PRO G CA  1 
ATOM 2692 C C   . PRO G 1 40 ? 8.875  64.150 24.759 1.00 50.93  ? 41 PRO G C   1 
ATOM 2693 O O   . PRO G 1 40 ? 9.414  63.038 24.861 1.00 54.77  ? 41 PRO G O   1 
ATOM 2694 C CB  . PRO G 1 40 ? 7.105  64.382 22.899 1.00 41.80  ? 41 PRO G CB  1 
ATOM 2695 C CG  . PRO G 1 40 ? 7.292  63.139 22.055 1.00 41.15  ? 41 PRO G CG  1 
ATOM 2696 C CD  . PRO G 1 40 ? 8.486  63.562 21.260 1.00 34.49  ? 41 PRO G CD  1 
ATOM 2697 N N   . VAL G 1 41 ? 8.769  65.009 25.798 1.00 47.51  ? 42 VAL G N   1 
ATOM 2698 C CA  . VAL G 1 41 ? 9.151  64.689 27.166 1.00 38.16  ? 42 VAL G CA  1 
ATOM 2699 C C   . VAL G 1 41 ? 7.941  64.853 28.070 1.00 39.41  ? 42 VAL G C   1 
ATOM 2700 O O   . VAL G 1 41 ? 6.942  65.489 27.671 1.00 39.23  ? 42 VAL G O   1 
ATOM 2701 C CB  . VAL G 1 41 ? 10.283 65.602 27.673 1.00 33.90  ? 42 VAL G CB  1 
ATOM 2702 C CG1 . VAL G 1 41 ? 11.548 65.290 26.890 1.00 31.25  ? 42 VAL G CG1 1 
ATOM 2703 C CG2 . VAL G 1 41 ? 9.878  67.073 27.552 1.00 35.87  ? 42 VAL G CG2 1 
ATOM 2704 N N   . PRO G 1 42 ? 7.934  64.194 29.242 1.00 38.01  ? 43 PRO G N   1 
ATOM 2705 C CA  . PRO G 1 42 ? 6.794  64.336 30.134 1.00 40.03  ? 43 PRO G CA  1 
ATOM 2706 C C   . PRO G 1 42 ? 6.758  65.773 30.748 1.00 41.48  ? 43 PRO G C   1 
ATOM 2707 O O   . PRO G 1 42 ? 7.802  66.410 30.973 1.00 37.26  ? 43 PRO G O   1 
ATOM 2708 C CB  . PRO G 1 42 ? 7.033  63.103 31.077 1.00 38.14  ? 43 PRO G CB  1 
ATOM 2709 C CG  . PRO G 1 42 ? 8.523  62.770 31.130 1.00 29.69  ? 43 PRO G CG  1 
ATOM 2710 C CD  . PRO G 1 42 ? 8.887  63.133 29.679 1.00 35.60  ? 43 PRO G CD  1 
ATOM 2711 N N   . PRO G 1 43 ? 5.590  66.405 30.952 1.00 44.60  ? 44 PRO G N   1 
ATOM 2712 C CA  . PRO G 1 43 ? 5.471  67.730 31.532 1.00 46.05  ? 44 PRO G CA  1 
ATOM 2713 C C   . PRO G 1 43 ? 5.964  67.652 32.965 1.00 44.36  ? 44 PRO G C   1 
ATOM 2714 O O   . PRO G 1 43 ? 5.892  66.533 33.520 1.00 41.95  ? 44 PRO G O   1 
ATOM 2715 C CB  . PRO G 1 43 ? 3.980  68.085 31.398 1.00 44.42  ? 44 PRO G CB  1 
ATOM 2716 C CG  . PRO G 1 43 ? 3.329  66.785 31.592 1.00 42.98  ? 44 PRO G CG  1 
ATOM 2717 C CD  . PRO G 1 43 ? 4.251  65.894 30.720 1.00 48.08  ? 44 PRO G CD  1 
ATOM 2718 N N   . PRO G 1 44 ? 6.461  68.800 33.500 1.00 43.34  ? 45 PRO G N   1 
ATOM 2719 C CA  . PRO G 1 44 ? 6.986  68.948 34.828 1.00 43.31  ? 45 PRO G CA  1 
ATOM 2720 C C   . PRO G 1 44 ? 5.916  69.284 35.878 1.00 48.56  ? 45 PRO G C   1 
ATOM 2721 O O   . PRO G 1 44 ? 4.721  68.989 35.667 1.00 47.05  ? 45 PRO G O   1 
ATOM 2722 C CB  . PRO G 1 44 ? 8.080  69.995 34.592 1.00 39.59  ? 45 PRO G CB  1 
ATOM 2723 C CG  . PRO G 1 44 ? 7.446  70.944 33.634 1.00 43.80  ? 45 PRO G CG  1 
ATOM 2724 C CD  . PRO G 1 44 ? 6.366  70.150 32.929 1.00 43.95  ? 45 PRO G CD  1 
ATOM 2725 O OXT . PRO G 1 44 ? 6.315  69.802 36.930 1.00 51.54  ? 45 PRO G OXT 1 
ATOM 2726 N N   . GLY H 2 1  ? 28.021 78.261 35.801 1.00 53.98  ? 1  GLY H N   1 
ATOM 2727 C CA  . GLY H 2 1  ? 28.609 78.985 36.901 1.00 59.77  ? 1  GLY H CA  1 
ATOM 2728 C C   . GLY H 2 1  ? 27.369 79.100 37.759 1.00 63.13  ? 1  GLY H C   1 
ATOM 2729 O O   . GLY H 2 1  ? 26.913 78.034 38.178 1.00 65.41  ? 1  GLY H O   1 
ATOM 2730 N N   . GLU H 2 2  ? 26.771 80.297 37.909 1.00 60.72  ? 2  GLU H N   1 
ATOM 2731 C CA  . GLU H 2 2  ? 25.530 80.469 38.662 1.00 52.27  ? 2  GLU H CA  1 
ATOM 2732 C C   . GLU H 2 2  ? 24.424 80.083 37.685 1.00 43.30  ? 2  GLU H C   1 
ATOM 2733 O O   . GLU H 2 2  ? 24.615 80.038 36.458 1.00 39.88  ? 2  GLU H O   1 
ATOM 2734 C CB  . GLU H 2 2  ? 25.355 81.941 39.123 1.00 60.60  ? 2  GLU H CB  1 
ATOM 2735 C CG  . GLU H 2 2  ? 24.199 82.239 40.121 1.00 70.91  ? 2  GLU H CG  1 
ATOM 2736 C CD  . GLU H 2 2  ? 23.215 83.429 39.853 1.00 76.70  ? 2  GLU H CD  1 
ATOM 2737 O OE1 . GLU H 2 2  ? 23.563 84.417 39.180 1.00 79.73  ? 2  GLU H OE1 1 
ATOM 2738 O OE2 . GLU H 2 2  ? 22.068 83.371 40.333 1.00 76.53  ? 2  GLU H OE2 1 
ATOM 2739 N N   . TRP H 2 3  ? 23.317 79.686 38.251 1.00 35.44  ? 3  TRP H N   1 
ATOM 2740 C CA  . TRP H 2 3  ? 22.166 79.212 37.529 1.00 39.40  ? 3  TRP H CA  1 
ATOM 2741 C C   . TRP H 2 3  ? 21.023 79.936 38.210 1.00 40.95  ? 3  TRP H C   1 
ATOM 2742 O O   . TRP H 2 3  ? 21.170 80.364 39.369 1.00 40.98  ? 3  TRP H O   1 
ATOM 2743 C CB  . TRP H 2 3  ? 21.933 77.682 37.700 1.00 44.46  ? 3  TRP H CB  1 
ATOM 2744 C CG  . TRP H 2 3  ? 22.715 76.635 36.878 1.00 44.77  ? 3  TRP H CG  1 
ATOM 2745 C CD1 . TRP H 2 3  ? 24.016 76.211 37.111 1.00 43.48  ? 3  TRP H CD1 1 
ATOM 2746 C CD2 . TRP H 2 3  ? 22.167 76.007 35.809 1.00 42.94  ? 3  TRP H CD2 1 
ATOM 2747 N NE1 . TRP H 2 3  ? 24.268 75.319 36.180 1.00 41.34  ? 3  TRP H NE1 1 
ATOM 2748 C CE2 . TRP H 2 3  ? 23.197 75.174 35.397 1.00 39.83  ? 3  TRP H CE2 1 
ATOM 2749 C CE3 . TRP H 2 3  ? 20.948 76.037 35.182 1.00 43.29  ? 3  TRP H CE3 1 
ATOM 2750 C CZ2 . TRP H 2 3  ? 23.022 74.364 34.314 1.00 39.80  ? 3  TRP H CZ2 1 
ATOM 2751 C CZ3 . TRP H 2 3  ? 20.781 75.217 34.079 1.00 44.58  ? 3  TRP H CZ3 1 
ATOM 2752 C CH2 . TRP H 2 3  ? 21.804 74.375 33.675 1.00 40.56  ? 3  TRP H CH2 1 
ATOM 2753 N N   . GLU H 2 4  ? 19.882 80.090 37.539 1.00 42.44  ? 4  GLU H N   1 
ATOM 2754 C CA  . GLU H 2 4  ? 18.774 80.826 38.110 1.00 44.48  ? 4  GLU H CA  1 
ATOM 2755 C C   . GLU H 2 4  ? 17.588 80.633 37.219 1.00 40.63  ? 4  GLU H C   1 
ATOM 2756 O O   . GLU H 2 4  ? 17.817 80.439 36.019 1.00 46.56  ? 4  GLU H O   1 
ATOM 2757 C CB  . GLU H 2 4  ? 19.110 82.303 38.170 1.00 53.92  ? 4  GLU H CB  1 
ATOM 2758 C CG  . GLU H 2 4  ? 19.764 82.813 36.875 1.00 60.04  ? 4  GLU H CG  1 
ATOM 2759 C CD  . GLU H 2 4  ? 20.108 84.285 36.911 1.00 62.78  ? 4  GLU H CD  1 
ATOM 2760 O OE1 . GLU H 2 4  ? 19.149 85.077 36.869 1.00 62.46  ? 4  GLU H OE1 1 
ATOM 2761 O OE2 . GLU H 2 4  ? 21.314 84.593 36.968 1.00 62.61  ? 4  GLU H OE2 1 
ATOM 2762 N N   . ILE H 2 5  ? 16.360 80.714 37.760 1.00 35.65  ? 5  ILE H N   1 
ATOM 2763 C CA  . ILE H 2 5  ? 15.139 80.494 36.970 1.00 30.35  ? 5  ILE H CA  1 
ATOM 2764 C C   . ILE H 2 5  ? 14.688 81.768 36.264 1.00 32.89  ? 5  ILE H C   1 
ATOM 2765 O O   . ILE H 2 5  ? 14.730 82.859 36.844 1.00 41.04  ? 5  ILE H O   1 
ATOM 2766 C CB  . ILE H 2 5  ? 14.040 80.047 37.877 1.00 28.76  ? 5  ILE H CB  1 
ATOM 2767 C CG1 . ILE H 2 5  ? 14.479 78.806 38.624 1.00 27.13  ? 5  ILE H CG1 1 
ATOM 2768 C CG2 . ILE H 2 5  ? 12.750 79.888 37.045 1.00 28.91  ? 5  ILE H CG2 1 
ATOM 2769 C CD1 . ILE H 2 5  ? 13.332 78.081 39.381 1.00 29.26  ? 5  ILE H CD1 1 
ATOM 2770 N N   . ILE H 2 6  ? 14.252 81.729 35.020 1.00 27.86  ? 6  ILE H N   1 
ATOM 2771 C CA  . ILE H 2 6  ? 13.856 82.976 34.441 1.00 24.93  ? 6  ILE H CA  1 
ATOM 2772 C C   . ILE H 2 6  ? 12.396 82.891 34.058 1.00 36.29  ? 6  ILE H C   1 
ATOM 2773 O O   . ILE H 2 6  ? 11.860 81.801 33.815 1.00 43.51  ? 6  ILE H O   1 
ATOM 2774 C CB  . ILE H 2 6  ? 14.794 83.327 33.248 1.00 18.43  ? 6  ILE H CB  1 
ATOM 2775 C CG1 . ILE H 2 6  ? 14.615 82.462 32.052 1.00 13.74  ? 6  ILE H CG1 1 
ATOM 2776 C CG2 . ILE H 2 6  ? 16.237 83.288 33.799 1.00 6.58   ? 6  ILE H CG2 1 
ATOM 2777 C CD1 . ILE H 2 6  ? 15.441 83.113 30.882 1.00 21.16  ? 6  ILE H CD1 1 
ATOM 2778 N N   . ASP H 2 7  ? 11.706 84.031 34.045 1.00 42.37  ? 7  ASP H N   1 
ATOM 2779 C CA  . ASP H 2 7  ? 10.266 84.043 33.847 1.00 48.47  ? 7  ASP H CA  1 
ATOM 2780 C C   . ASP H 2 7  ? 9.908  84.200 32.391 1.00 50.93  ? 7  ASP H C   1 
ATOM 2781 O O   . ASP H 2 7  ? 10.470 85.071 31.740 1.00 53.08  ? 7  ASP H O   1 
ATOM 2782 C CB  . ASP H 2 7  ? 9.638  85.184 34.647 1.00 49.97  ? 7  ASP H CB  1 
ATOM 2783 C CG  . ASP H 2 7  ? 8.211  85.461 34.232 1.00 55.78  ? 7  ASP H CG  1 
ATOM 2784 O OD1 . ASP H 2 7  ? 7.330  84.650 34.524 1.00 60.90  ? 7  ASP H OD1 1 
ATOM 2785 O OD2 . ASP H 2 7  ? 8.005  86.461 33.552 1.00 64.09  ? 7  ASP H OD2 1 
ATOM 2786 N N   . ILE H 2 8  ? 8.818  83.537 32.022 1.00 53.40  ? 8  ILE H N   1 
ATOM 2787 C CA  . ILE H 2 8  ? 8.313  83.421 30.663 1.00 57.43  ? 8  ILE H CA  1 
ATOM 2788 C C   . ILE H 2 8  ? 7.820  84.662 29.907 1.00 56.65  ? 8  ILE H C   1 
ATOM 2789 O O   . ILE H 2 8  ? 6.890  84.576 29.089 1.00 56.78  ? 8  ILE H O   1 
ATOM 2790 C CB  . ILE H 2 8  ? 7.169  82.328 30.631 1.00 58.69  ? 8  ILE H CB  1 
ATOM 2791 C CG1 . ILE H 2 8  ? 6.007  82.641 31.562 1.00 53.26  ? 8  ILE H CG1 1 
ATOM 2792 C CG2 . ILE H 2 8  ? 7.839  80.985 30.951 1.00 60.87  ? 8  ILE H CG2 1 
ATOM 2793 C CD1 . ILE H 2 8  ? 4.949  81.534 31.510 1.00 52.63  ? 8  ILE H CD1 1 
ATOM 2794 N N   . GLY H 2 9  ? 8.506  85.794 30.032 1.00 54.57  ? 9  GLY H N   1 
ATOM 2795 C CA  . GLY H 2 9  ? 8.128  86.996 29.322 1.00 53.36  ? 9  GLY H CA  1 
ATOM 2796 C C   . GLY H 2 9  ? 8.397  86.815 27.838 1.00 52.93  ? 9  GLY H C   1 
ATOM 2797 O O   . GLY H 2 9  ? 8.979  85.819 27.410 1.00 49.74  ? 9  GLY H O   1 
ATOM 2798 N N   . PRO H 2 10 ? 8.055  87.754 26.966 1.00 58.00  ? 10 PRO H N   1 
ATOM 2799 C CA  . PRO H 2 10 ? 8.277  87.668 25.529 1.00 55.46  ? 10 PRO H CA  1 
ATOM 2800 C C   . PRO H 2 10 ? 9.692  87.287 25.131 1.00 47.61  ? 10 PRO H C   1 
ATOM 2801 O O   . PRO H 2 10 ? 9.853  86.530 24.183 1.00 52.89  ? 10 PRO H O   1 
ATOM 2802 C CB  . PRO H 2 10 ? 7.843  89.021 25.017 1.00 56.26  ? 10 PRO H CB  1 
ATOM 2803 C CG  . PRO H 2 10 ? 7.915  89.908 26.233 1.00 57.35  ? 10 PRO H CG  1 
ATOM 2804 C CD  . PRO H 2 10 ? 7.337  88.977 27.281 1.00 57.56  ? 10 PRO H CD  1 
ATOM 2805 N N   . PHE H 2 11 ? 10.723 87.674 25.876 1.00 38.08  ? 11 PHE H N   1 
ATOM 2806 C CA  . PHE H 2 11 ? 12.089 87.272 25.530 1.00 38.85  ? 11 PHE H CA  1 
ATOM 2807 C C   . PHE H 2 11 ? 12.300 85.748 25.400 1.00 47.59  ? 11 PHE H C   1 
ATOM 2808 O O   . PHE H 2 11 ? 12.921 85.257 24.441 1.00 49.95  ? 11 PHE H O   1 
ATOM 2809 C CB  . PHE H 2 11 ? 12.953 87.769 26.567 1.00 29.21  ? 11 PHE H CB  1 
ATOM 2810 C CG  . PHE H 2 11 ? 14.402 87.488 26.369 1.00 29.30  ? 11 PHE H CG  1 
ATOM 2811 C CD1 . PHE H 2 11 ? 15.054 87.900 25.227 1.00 31.45  ? 11 PHE H CD1 1 
ATOM 2812 C CD2 . PHE H 2 11 ? 15.085 86.940 27.439 1.00 32.70  ? 11 PHE H CD2 1 
ATOM 2813 C CE1 . PHE H 2 11 ? 16.431 87.755 25.175 1.00 38.45  ? 11 PHE H CE1 1 
ATOM 2814 C CE2 . PHE H 2 11 ? 16.457 86.805 27.370 1.00 33.47  ? 11 PHE H CE2 1 
ATOM 2815 C CZ  . PHE H 2 11 ? 17.142 87.220 26.242 1.00 34.30  ? 11 PHE H CZ  1 
ATOM 2816 N N   . THR H 2 12 ? 11.790 85.022 26.415 1.00 49.42  ? 12 THR H N   1 
ATOM 2817 C CA  . THR H 2 12 ? 11.734 83.561 26.477 1.00 47.03  ? 12 THR H CA  1 
ATOM 2818 C C   . THR H 2 12 ? 10.821 83.006 25.359 1.00 49.98  ? 12 THR H C   1 
ATOM 2819 O O   . THR H 2 12 ? 11.049 81.912 24.826 1.00 53.38  ? 12 THR H O   1 
ATOM 2820 C CB  . THR H 2 12 ? 11.239 83.247 27.908 1.00 43.72  ? 12 THR H CB  1 
ATOM 2821 O OG1 . THR H 2 12 ? 12.331 83.611 28.745 1.00 42.44  ? 12 THR H OG1 1 
ATOM 2822 C CG2 . THR H 2 12 ? 10.752 81.841 28.119 1.00 40.04  ? 12 THR H CG2 1 
ATOM 2823 N N   . GLN H 2 13 ? 9.806  83.770 24.938 1.00 48.45  ? 13 GLN H N   1 
ATOM 2824 C CA  . GLN H 2 13 ? 8.918  83.346 23.868 1.00 43.97  ? 13 GLN H CA  1 
ATOM 2825 C C   . GLN H 2 13 ? 9.658  83.400 22.557 1.00 41.81  ? 13 GLN H C   1 
ATOM 2826 O O   . GLN H 2 13 ? 9.582  82.450 21.785 1.00 41.50  ? 13 GLN H O   1 
ATOM 2827 C CB  . GLN H 2 13 ? 7.689  84.240 23.807 1.00 41.54  ? 13 GLN H CB  1 
ATOM 2828 C CG  . GLN H 2 13 ? 6.965  84.168 25.139 1.00 41.65  ? 13 GLN H CG  1 
ATOM 2829 C CD  . GLN H 2 13 ? 6.528  82.754 25.502 1.00 44.37  ? 13 GLN H CD  1 
ATOM 2830 O OE1 . GLN H 2 13 ? 6.219  81.964 24.601 1.00 47.22  ? 13 GLN H OE1 1 
ATOM 2831 N NE2 . GLN H 2 13 ? 6.476  82.376 26.790 1.00 42.26  ? 13 GLN H NE2 1 
ATOM 2832 N N   . ASN H 2 14 ? 10.460 84.426 22.316 1.00 38.92  ? 14 ASN H N   1 
ATOM 2833 C CA  . ASN H 2 14 ? 11.270 84.445 21.111 1.00 43.81  ? 14 ASN H CA  1 
ATOM 2834 C C   . ASN H 2 14 ? 12.306 83.326 21.139 1.00 44.33  ? 14 ASN H C   1 
ATOM 2835 O O   . ASN H 2 14 ? 12.479 82.681 20.103 1.00 43.56  ? 14 ASN H O   1 
ATOM 2836 C CB  . ASN H 2 14 ? 12.063 85.689 20.948 1.00 56.46  ? 14 ASN H CB  1 
ATOM 2837 C CG  . ASN H 2 14 ? 11.290 86.919 20.520 1.00 65.73  ? 14 ASN H CG  1 
ATOM 2838 O OD1 . ASN H 2 14 ? 10.078 86.942 20.251 1.00 65.49  ? 14 ASN H OD1 1 
ATOM 2839 N ND2 . ASN H 2 14 ? 12.111 87.978 20.487 1.00 74.79  ? 14 ASN H ND2 1 
ATOM 2840 N N   . LEU H 2 15 ? 13.012 83.058 22.270 1.00 40.40  ? 15 LEU H N   1 
ATOM 2841 C CA  . LEU H 2 15 ? 13.935 81.916 22.376 1.00 33.74  ? 15 LEU H CA  1 
ATOM 2842 C C   . LEU H 2 15 ? 13.291 80.609 21.938 1.00 35.80  ? 15 LEU H C   1 
ATOM 2843 O O   . LEU H 2 15 ? 13.935 79.833 21.233 1.00 32.09  ? 15 LEU H O   1 
ATOM 2844 C CB  . LEU H 2 15 ? 14.416 81.760 23.802 1.00 30.97  ? 15 LEU H CB  1 
ATOM 2845 C CG  . LEU H 2 15 ? 15.457 82.782 24.094 1.00 36.23  ? 15 LEU H CG  1 
ATOM 2846 C CD1 . LEU H 2 15 ? 15.847 82.789 25.545 1.00 35.89  ? 15 LEU H CD1 1 
ATOM 2847 C CD2 . LEU H 2 15 ? 16.643 82.458 23.233 1.00 35.96  ? 15 LEU H CD2 1 
ATOM 2848 N N   . GLY H 2 16 ? 12.017 80.396 22.303 1.00 32.43  ? 16 GLY H N   1 
ATOM 2849 C CA  . GLY H 2 16 ? 11.245 79.276 21.829 1.00 35.66  ? 16 GLY H CA  1 
ATOM 2850 C C   . GLY H 2 16 ? 11.024 79.292 20.321 1.00 41.05  ? 16 GLY H C   1 
ATOM 2851 O O   . GLY H 2 16 ? 10.998 78.209 19.741 1.00 44.84  ? 16 GLY H O   1 
ATOM 2852 N N   . LYS H 2 17 ? 10.834 80.454 19.653 1.00 48.29  ? 17 LYS H N   1 
ATOM 2853 C CA  . LYS H 2 17 ? 10.664 80.548 18.191 1.00 52.72  ? 17 LYS H CA  1 
ATOM 2854 C C   . LYS H 2 17 ? 11.943 80.126 17.516 1.00 52.82  ? 17 LYS H C   1 
ATOM 2855 O O   . LYS H 2 17 ? 11.934 79.189 16.720 1.00 57.29  ? 17 LYS H O   1 
ATOM 2856 C CB  . LYS H 2 17 ? 10.381 81.959 17.647 1.00 60.36  ? 17 LYS H CB  1 
ATOM 2857 C CG  . LYS H 2 17 ? 8.924  82.385 17.787 1.00 70.20  ? 17 LYS H CG  1 
ATOM 2858 C CD  . LYS H 2 17 ? 8.553  83.610 16.922 1.00 75.62  ? 17 LYS H CD  1 
ATOM 2859 C CE  . LYS H 2 17 ? 7.060  84.014 16.987 1.00 74.47  ? 17 LYS H CE  1 
ATOM 2860 N NZ  . LYS H 2 17 ? 6.708  84.569 18.282 1.00 75.71  ? 17 LYS H NZ  1 
ATOM 2861 N N   . PHE H 2 18 ? 13.058 80.778 17.840 1.00 49.26  ? 18 PHE H N   1 
ATOM 2862 C CA  . PHE H 2 18 ? 14.390 80.393 17.374 1.00 48.02  ? 18 PHE H CA  1 
ATOM 2863 C C   . PHE H 2 18 ? 14.533 78.870 17.499 1.00 43.91  ? 18 PHE H C   1 
ATOM 2864 O O   . PHE H 2 18 ? 14.651 78.220 16.469 1.00 44.34  ? 18 PHE H O   1 
ATOM 2865 C CB  . PHE H 2 18 ? 15.429 81.094 18.244 1.00 46.72  ? 18 PHE H CB  1 
ATOM 2866 C CG  . PHE H 2 18 ? 16.895 80.829 17.954 1.00 43.99  ? 18 PHE H CG  1 
ATOM 2867 C CD1 . PHE H 2 18 ? 17.470 81.327 16.800 1.00 39.38  ? 18 PHE H CD1 1 
ATOM 2868 C CD2 . PHE H 2 18 ? 17.657 80.144 18.877 1.00 41.39  ? 18 PHE H CD2 1 
ATOM 2869 C CE1 . PHE H 2 18 ? 18.820 81.155 16.561 1.00 30.90  ? 18 PHE H CE1 1 
ATOM 2870 C CE2 . PHE H 2 18 ? 18.997 79.979 18.618 1.00 39.13  ? 18 PHE H CE2 1 
ATOM 2871 C CZ  . PHE H 2 18 ? 19.574 80.484 17.471 1.00 32.43  ? 18 PHE H CZ  1 
ATOM 2872 N N   . ALA H 2 19 ? 14.389 78.295 18.701 1.00 33.12  ? 19 ALA H N   1 
ATOM 2873 C CA  . ALA H 2 19 ? 14.427 76.871 18.894 1.00 29.55  ? 19 ALA H CA  1 
ATOM 2874 C C   . ALA H 2 19 ? 13.626 76.060 17.871 1.00 32.38  ? 19 ALA H C   1 
ATOM 2875 O O   . ALA H 2 19 ? 14.210 75.183 17.211 1.00 30.63  ? 19 ALA H O   1 
ATOM 2876 C CB  . ALA H 2 19 ? 13.925 76.576 20.276 1.00 30.28  ? 19 ALA H CB  1 
ATOM 2877 N N   . VAL H 2 20 ? 12.342 76.389 17.621 1.00 34.78  ? 20 VAL H N   1 
ATOM 2878 C CA  . VAL H 2 20 ? 11.523 75.664 16.635 1.00 30.86  ? 20 VAL H CA  1 
ATOM 2879 C C   . VAL H 2 20 ? 12.019 75.888 15.208 1.00 37.45  ? 20 VAL H C   1 
ATOM 2880 O O   . VAL H 2 20 ? 12.088 74.970 14.398 1.00 38.08  ? 20 VAL H O   1 
ATOM 2881 C CB  . VAL H 2 20 ? 10.111 76.120 16.684 1.00 23.52  ? 20 VAL H CB  1 
ATOM 2882 C CG1 . VAL H 2 20 ? 9.294  75.152 15.928 1.00 31.98  ? 20 VAL H CG1 1 
ATOM 2883 C CG2 . VAL H 2 20 ? 9.566  76.097 18.055 1.00 24.70  ? 20 VAL H CG2 1 
ATOM 2884 N N   . ASP H 2 21 ? 12.415 77.110 14.863 1.00 45.23  ? 21 ASP H N   1 
ATOM 2885 C CA  . ASP H 2 21 ? 12.887 77.440 13.527 1.00 48.98  ? 21 ASP H CA  1 
ATOM 2886 C C   . ASP H 2 21 ? 14.250 76.804 13.265 1.00 47.99  ? 21 ASP H C   1 
ATOM 2887 O O   . ASP H 2 21 ? 14.446 76.247 12.190 1.00 56.75  ? 21 ASP H O   1 
ATOM 2888 C CB  . ASP H 2 21 ? 12.996 78.977 13.332 1.00 55.43  ? 21 ASP H CB  1 
ATOM 2889 C CG  . ASP H 2 21 ? 11.755 79.898 13.557 1.00 60.47  ? 21 ASP H CG  1 
ATOM 2890 O OD1 . ASP H 2 21 ? 10.585 79.533 13.358 1.00 57.59  ? 21 ASP H OD1 1 
ATOM 2891 O OD2 . ASP H 2 21 ? 11.987 81.040 13.955 1.00 64.43  ? 21 ASP H OD2 1 
ATOM 2892 N N   . GLU H 2 22 ? 15.208 76.789 14.192 1.00 44.98  ? 22 GLU H N   1 
ATOM 2893 C CA  . GLU H 2 22 ? 16.488 76.108 14.006 1.00 42.62  ? 22 GLU H CA  1 
ATOM 2894 C C   . GLU H 2 22 ? 16.313 74.586 13.953 1.00 50.73  ? 22 GLU H C   1 
ATOM 2895 O O   . GLU H 2 22 ? 17.003 73.895 13.179 1.00 49.04  ? 22 GLU H O   1 
ATOM 2896 C CB  . GLU H 2 22 ? 17.396 76.442 15.127 1.00 37.44  ? 22 GLU H CB  1 
ATOM 2897 C CG  . GLU H 2 22 ? 18.056 77.745 14.902 1.00 40.83  ? 22 GLU H CG  1 
ATOM 2898 C CD  . GLU H 2 22 ? 19.289 77.618 14.029 1.00 46.22  ? 22 GLU H CD  1 
ATOM 2899 O OE1 . GLU H 2 22 ? 20.287 77.109 14.548 1.00 48.76  ? 22 GLU H OE1 1 
ATOM 2900 O OE2 . GLU H 2 22 ? 19.266 78.040 12.858 1.00 48.28  ? 22 GLU H OE2 1 
ATOM 2901 N N   . GLU H 2 23 ? 15.374 74.016 14.737 1.00 53.82  ? 23 GLU H N   1 
ATOM 2902 C CA  . GLU H 2 23 ? 15.151 72.601 14.610 1.00 55.73  ? 23 GLU H CA  1 
ATOM 2903 C C   . GLU H 2 23 ? 14.503 72.378 13.270 1.00 56.93  ? 23 GLU H C   1 
ATOM 2904 O O   . GLU H 2 23 ? 14.871 71.411 12.621 1.00 65.98  ? 23 GLU H O   1 
ATOM 2905 C CB  . GLU H 2 23 ? 14.246 72.005 15.713 1.00 60.18  ? 23 GLU H CB  1 
ATOM 2906 C CG  . GLU H 2 23 ? 14.055 70.448 15.654 1.00 62.77  ? 23 GLU H CG  1 
ATOM 2907 C CD  . GLU H 2 23 ? 15.295 69.515 15.570 1.00 64.96  ? 23 GLU H CD  1 
ATOM 2908 O OE1 . GLU H 2 23 ? 16.362 69.801 16.114 1.00 65.20  ? 23 GLU H OE1 1 
ATOM 2909 O OE2 . GLU H 2 23 ? 15.200 68.462 14.951 1.00 63.12  ? 23 GLU H OE2 1 
ATOM 2910 N N   . ASN H 2 24 ? 13.652 73.263 12.770 1.00 53.55  ? 24 ASN H N   1 
ATOM 2911 C CA  . ASN H 2 24 ? 13.086 73.094 11.447 1.00 49.64  ? 24 ASN H CA  1 
ATOM 2912 C C   . ASN H 2 24 ? 14.120 73.063 10.348 1.00 44.12  ? 24 ASN H C   1 
ATOM 2913 O O   . ASN H 2 24 ? 13.836 72.536 9.290  1.00 49.50  ? 24 ASN H O   1 
ATOM 2914 C CB  . ASN H 2 24 ? 12.101 74.198 11.138 1.00 57.32  ? 24 ASN H CB  1 
ATOM 2915 C CG  . ASN H 2 24 ? 10.710 73.891 11.664 1.00 63.36  ? 24 ASN H CG  1 
ATOM 2916 O OD1 . ASN H 2 24 ? 10.275 72.741 11.739 1.00 70.72  ? 24 ASN H OD1 1 
ATOM 2917 N ND2 . ASN H 2 24 ? 9.908  74.863 12.064 1.00 67.54  ? 24 ASN H ND2 1 
ATOM 2918 N N   . LYS H 2 25 ? 15.323 73.587 10.493 1.00 41.33  ? 25 LYS H N   1 
ATOM 2919 C CA  . LYS H 2 25 ? 16.324 73.355 9.469  1.00 53.11  ? 25 LYS H CA  1 
ATOM 2920 C C   . LYS H 2 25 ? 16.921 71.909 9.550  1.00 60.96  ? 25 LYS H C   1 
ATOM 2921 O O   . LYS H 2 25 ? 17.493 71.384 8.574  1.00 63.41  ? 25 LYS H O   1 
ATOM 2922 C CB  . LYS H 2 25 ? 17.421 74.358 9.634  1.00 57.71  ? 25 LYS H CB  1 
ATOM 2923 C CG  . LYS H 2 25 ? 17.074 75.823 9.507  1.00 65.99  ? 25 LYS H CG  1 
ATOM 2924 C CD  . LYS H 2 25 ? 18.386 76.508 9.896  1.00 69.99  ? 25 LYS H CD  1 
ATOM 2925 C CE  . LYS H 2 25 ? 18.445 77.997 9.655  1.00 70.07  ? 25 LYS H CE  1 
ATOM 2926 N NZ  . LYS H 2 25 ? 19.808 78.392 9.908  1.00 69.10  ? 25 LYS H NZ  1 
ATOM 2927 N N   . ILE H 2 26 ? 16.865 71.222 10.712 1.00 58.48  ? 26 ILE H N   1 
ATOM 2928 C CA  . ILE H 2 26 ? 17.357 69.844 10.861 1.00 54.60  ? 26 ILE H CA  1 
ATOM 2929 C C   . ILE H 2 26 ? 16.317 68.768 10.559 1.00 47.99  ? 26 ILE H C   1 
ATOM 2930 O O   . ILE H 2 26 ? 16.592 67.608 10.788 1.00 52.50  ? 26 ILE H O   1 
ATOM 2931 C CB  . ILE H 2 26 ? 17.903 69.523 12.291 1.00 60.37  ? 26 ILE H CB  1 
ATOM 2932 C CG1 . ILE H 2 26 ? 18.271 70.710 13.146 1.00 63.28  ? 26 ILE H CG1 1 
ATOM 2933 C CG2 . ILE H 2 26 ? 19.124 68.642 12.040 1.00 62.73  ? 26 ILE H CG2 1 
ATOM 2934 C CD1 . ILE H 2 26 ? 19.270 70.468 14.317 1.00 63.21  ? 26 ILE H CD1 1 
ATOM 2935 N N   . GLY H 2 27 ? 15.071 69.013 10.211 1.00 48.14  ? 27 GLY H N   1 
ATOM 2936 C CA  . GLY H 2 27 ? 14.062 67.969 9.930  1.00 47.57  ? 27 GLY H CA  1 
ATOM 2937 C C   . GLY H 2 27 ? 13.885 66.701 10.811 1.00 49.01  ? 27 GLY H C   1 
ATOM 2938 O O   . GLY H 2 27 ? 12.996 65.881 10.559 1.00 43.29  ? 27 GLY H O   1 
ATOM 2939 N N   . GLN H 2 28 ? 14.623 66.515 11.909 1.00 48.28  ? 28 GLN H N   1 
ATOM 2940 C CA  . GLN H 2 28 ? 14.598 65.305 12.730 1.00 51.07  ? 28 GLN H CA  1 
ATOM 2941 C C   . GLN H 2 28 ? 13.208 64.871 13.175 1.00 52.75  ? 28 GLN H C   1 
ATOM 2942 O O   . GLN H 2 28 ? 12.991 63.696 13.475 1.00 53.65  ? 28 GLN H O   1 
ATOM 2943 C CB  . GLN H 2 28 ? 15.484 65.506 13.982 1.00 50.15  ? 28 GLN H CB  1 
ATOM 2944 C CG  . GLN H 2 28 ? 16.248 64.278 14.471 1.00 56.66  ? 28 GLN H CG  1 
ATOM 2945 C CD  . GLN H 2 28 ? 17.460 63.914 13.613 1.00 63.27  ? 28 GLN H CD  1 
ATOM 2946 O OE1 . GLN H 2 28 ? 18.483 64.589 13.710 1.00 62.28  ? 28 GLN H OE1 1 
ATOM 2947 N NE2 . GLN H 2 28 ? 17.506 62.877 12.771 1.00 61.78  ? 28 GLN H NE2 1 
ATOM 2948 N N   . TYR H 2 29 ? 12.277 65.827 13.261 1.00 55.81  ? 29 TYR H N   1 
ATOM 2949 C CA  . TYR H 2 29 ? 10.933 65.572 13.732 1.00 57.42  ? 29 TYR H CA  1 
ATOM 2950 C C   . TYR H 2 29 ? 9.949  66.066 12.678 1.00 60.90  ? 29 TYR H C   1 
ATOM 2951 O O   . TYR H 2 29 ? 8.793  66.392 12.980 1.00 63.08  ? 29 TYR H O   1 
ATOM 2952 C CB  . TYR H 2 29 ? 10.702 66.313 15.102 1.00 57.05  ? 29 TYR H CB  1 
ATOM 2953 C CG  . TYR H 2 29 ? 11.588 65.889 16.299 1.00 55.20  ? 29 TYR H CG  1 
ATOM 2954 C CD1 . TYR H 2 29 ? 12.823 66.489 16.503 1.00 50.09  ? 29 TYR H CD1 1 
ATOM 2955 C CD2 . TYR H 2 29 ? 11.154 64.937 17.197 1.00 52.62  ? 29 TYR H CD2 1 
ATOM 2956 C CE1 . TYR H 2 29 ? 13.613 66.118 17.563 1.00 49.61  ? 29 TYR H CE1 1 
ATOM 2957 C CE2 . TYR H 2 29 ? 11.944 64.561 18.257 1.00 49.62  ? 29 TYR H CE2 1 
ATOM 2958 C CZ  . TYR H 2 29 ? 13.171 65.147 18.426 1.00 49.17  ? 29 TYR H CZ  1 
ATOM 2959 O OH  . TYR H 2 29 ? 13.937 64.772 19.517 1.00 46.53  ? 29 TYR H OH  1 
ATOM 2960 N N   . GLY H 2 30 ? 10.357 66.099 11.408 1.00 63.86  ? 30 GLY H N   1 
ATOM 2961 C CA  . GLY H 2 30 ? 9.486  66.642 10.386 1.00 67.84  ? 30 GLY H CA  1 
ATOM 2962 C C   . GLY H 2 30 ? 9.460  68.155 10.529 1.00 70.32  ? 30 GLY H C   1 
ATOM 2963 O O   . GLY H 2 30 ? 10.510 68.755 10.791 1.00 72.38  ? 30 GLY H O   1 
ATOM 2964 N N   . ARG H 2 31 ? 8.281  68.759 10.406 1.00 72.78  ? 31 ARG H N   1 
ATOM 2965 C CA  . ARG H 2 31 ? 8.155  70.205 10.449 1.00 71.32  ? 31 ARG H CA  1 
ATOM 2966 C C   . ARG H 2 31 ? 7.256  70.570 11.619 1.00 70.40  ? 31 ARG H C   1 
ATOM 2967 O O   . ARG H 2 31 ? 6.200  69.946 11.769 1.00 75.04  ? 31 ARG H O   1 
ATOM 2968 C CB  . ARG H 2 31 ? 7.535  70.713 9.158  1.00 70.58  ? 31 ARG H CB  1 
ATOM 2969 C CG  . ARG H 2 31 ? 7.675  72.229 9.039  1.00 72.19  ? 31 ARG H CG  1 
ATOM 2970 C CD  . ARG H 2 31 ? 9.152  72.522 8.814  1.00 73.97  ? 31 ARG H CD  1 
ATOM 2971 N NE  . ARG H 2 31 ? 9.538  72.168 7.462  1.00 78.46  ? 31 ARG H NE  1 
ATOM 2972 C CZ  . ARG H 2 31 ? 10.707 72.539 6.919  1.00 81.86  ? 31 ARG H CZ  1 
ATOM 2973 N NH1 . ARG H 2 31 ? 11.612 73.258 7.580  1.00 80.02  ? 31 ARG H NH1 1 
ATOM 2974 N NH2 . ARG H 2 31 ? 10.925 72.214 5.646  1.00 84.71  ? 31 ARG H NH2 1 
ATOM 2975 N N   . LEU H 2 32 ? 7.604  71.566 12.439 1.00 64.35  ? 32 LEU H N   1 
ATOM 2976 C CA  . LEU H 2 32 ? 6.801  71.890 13.611 1.00 54.90  ? 32 LEU H CA  1 
ATOM 2977 C C   . LEU H 2 32 ? 6.264  73.319 13.600 1.00 55.63  ? 32 LEU H C   1 
ATOM 2978 O O   . LEU H 2 32 ? 6.910  74.239 13.071 1.00 53.35  ? 32 LEU H O   1 
ATOM 2979 C CB  . LEU H 2 32 ? 7.645  71.676 14.861 1.00 47.27  ? 32 LEU H CB  1 
ATOM 2980 C CG  . LEU H 2 32 ? 8.346  70.351 15.106 1.00 43.17  ? 32 LEU H CG  1 
ATOM 2981 C CD1 . LEU H 2 32 ? 9.463  70.576 16.106 1.00 43.11  ? 32 LEU H CD1 1 
ATOM 2982 C CD2 . LEU H 2 32 ? 7.384  69.307 15.626 1.00 39.54  ? 32 LEU H CD2 1 
ATOM 2983 N N   . THR H 2 33 ? 5.070  73.518 14.168 1.00 57.27  ? 33 THR H N   1 
ATOM 2984 C CA  . THR H 2 33 ? 4.511  74.859 14.337 1.00 63.64  ? 33 THR H CA  1 
ATOM 2985 C C   . THR H 2 33 ? 4.573  75.253 15.821 1.00 62.15  ? 33 THR H C   1 
ATOM 2986 O O   . THR H 2 33 ? 4.255  74.467 16.726 1.00 58.98  ? 33 THR H O   1 
ATOM 2987 C CB  . THR H 2 33 ? 3.045  74.934 13.834 1.00 66.00  ? 33 THR H CB  1 
ATOM 2988 O OG1 . THR H 2 33 ? 2.652  76.284 14.072 1.00 64.54  ? 33 THR H OG1 1 
ATOM 2989 C CG2 . THR H 2 33 ? 2.076  73.966 14.505 1.00 69.82  ? 33 THR H CG2 1 
ATOM 2990 N N   . PHE H 2 34 ? 5.020  76.489 16.044 1.00 61.06  ? 34 PHE H N   1 
ATOM 2991 C CA  . PHE H 2 34 ? 5.326  77.045 17.357 1.00 55.98  ? 34 PHE H CA  1 
ATOM 2992 C C   . PHE H 2 34 ? 4.092  77.216 18.202 1.00 57.42  ? 34 PHE H C   1 
ATOM 2993 O O   . PHE H 2 34 ? 3.067  77.634 17.670 1.00 62.87  ? 34 PHE H O   1 
ATOM 2994 C CB  . PHE H 2 34 ? 6.009  78.391 17.174 1.00 46.58  ? 34 PHE H CB  1 
ATOM 2995 C CG  . PHE H 2 34 ? 6.305  79.117 18.465 1.00 42.77  ? 34 PHE H CG  1 
ATOM 2996 C CD1 . PHE H 2 34 ? 7.435  78.819 19.177 1.00 42.02  ? 34 PHE H CD1 1 
ATOM 2997 C CD2 . PHE H 2 34 ? 5.432  80.070 18.937 1.00 44.58  ? 34 PHE H CD2 1 
ATOM 2998 C CE1 . PHE H 2 34 ? 7.686  79.472 20.364 1.00 43.48  ? 34 PHE H CE1 1 
ATOM 2999 C CE2 . PHE H 2 34 ? 5.695  80.717 20.129 1.00 45.44  ? 34 PHE H CE2 1 
ATOM 3000 C CZ  . PHE H 2 34 ? 6.824  80.421 20.849 1.00 42.14  ? 34 PHE H CZ  1 
ATOM 3001 N N   . ASN H 2 35 ? 4.184  76.884 19.488 1.00 57.48  ? 35 ASN H N   1 
ATOM 3002 C CA  . ASN H 2 35 ? 3.088  77.149 20.391 1.00 61.81  ? 35 ASN H CA  1 
ATOM 3003 C C   . ASN H 2 35 ? 3.450  78.020 21.574 1.00 66.58  ? 35 ASN H C   1 
ATOM 3004 O O   . ASN H 2 35 ? 3.011  79.170 21.595 1.00 68.61  ? 35 ASN H O   1 
ATOM 3005 C CB  . ASN H 2 35 ? 2.486  75.868 20.915 1.00 60.82  ? 35 ASN H CB  1 
ATOM 3006 C CG  . ASN H 2 35 ? 1.555  75.256 19.891 1.00 65.26  ? 35 ASN H CG  1 
ATOM 3007 O OD1 . ASN H 2 35 ? 1.539  74.028 19.775 1.00 70.16  ? 35 ASN H OD1 1 
ATOM 3008 N ND2 . ASN H 2 35 ? 0.759  76.021 19.127 1.00 66.50  ? 35 ASN H ND2 1 
ATOM 3009 N N   . LYS H 2 36 ? 4.246  77.566 22.555 1.00 70.04  ? 36 LYS H N   1 
ATOM 3010 C CA  . LYS H 2 36 ? 4.547  78.384 23.730 1.00 68.95  ? 36 LYS H CA  1 
ATOM 3011 C C   . LYS H 2 36 ? 5.609  77.805 24.671 1.00 64.93  ? 36 LYS H C   1 
ATOM 3012 O O   . LYS H 2 36 ? 5.728  76.580 24.824 1.00 65.51  ? 36 LYS H O   1 
ATOM 3013 C CB  . LYS H 2 36 ? 3.284  78.618 24.579 1.00 70.28  ? 36 LYS H CB  1 
ATOM 3014 C CG  . LYS H 2 36 ? 2.706  77.421 25.313 1.00 70.48  ? 36 LYS H CG  1 
ATOM 3015 C CD  . LYS H 2 36 ? 2.096  77.990 26.585 1.00 74.44  ? 36 LYS H CD  1 
ATOM 3016 C CE  . LYS H 2 36 ? 0.595  78.239 26.533 1.00 74.74  ? 36 LYS H CE  1 
ATOM 3017 N NZ  . LYS H 2 36 ? -0.101 76.969 26.515 1.00 72.68  ? 36 LYS H NZ  1 
ATOM 3018 N N   . VAL H 2 37 ? 6.380  78.672 25.331 1.00 55.48  ? 37 VAL H N   1 
ATOM 3019 C CA  . VAL H 2 37 ? 7.323  78.211 26.328 1.00 47.86  ? 37 VAL H CA  1 
ATOM 3020 C C   . VAL H 2 37 ? 6.631  78.345 27.667 1.00 43.46  ? 37 VAL H C   1 
ATOM 3021 O O   . VAL H 2 37 ? 5.907  79.313 27.909 1.00 44.51  ? 37 VAL H O   1 
ATOM 3022 C CB  . VAL H 2 37 ? 8.591  79.042 26.324 1.00 48.62  ? 37 VAL H CB  1 
ATOM 3023 C CG1 . VAL H 2 37 ? 9.639  78.522 27.301 1.00 50.17  ? 37 VAL H CG1 1 
ATOM 3024 C CG2 . VAL H 2 37 ? 9.212  78.912 24.960 1.00 53.14  ? 37 VAL H CG2 1 
ATOM 3025 N N   . ILE H 2 38 ? 6.851  77.343 28.509 1.00 39.73  ? 38 ILE H N   1 
ATOM 3026 C CA  . ILE H 2 38 ? 6.187  77.162 29.775 1.00 35.45  ? 38 ILE H CA  1 
ATOM 3027 C C   . ILE H 2 38 ? 7.187  77.069 30.866 1.00 28.74  ? 38 ILE H C   1 
ATOM 3028 O O   . ILE H 2 38 ? 8.325  76.760 30.595 1.00 23.55  ? 38 ILE H O   1 
ATOM 3029 C CB  . ILE H 2 38 ? 5.329  75.848 29.860 1.00 37.61  ? 38 ILE H CB  1 
ATOM 3030 C CG1 . ILE H 2 38 ? 6.121  74.575 29.524 1.00 29.47  ? 38 ILE H CG1 1 
ATOM 3031 C CG2 . ILE H 2 38 ? 4.129  76.047 28.926 1.00 43.12  ? 38 ILE H CG2 1 
ATOM 3032 C CD1 . ILE H 2 38 ? 5.232  73.342 29.824 1.00 21.84  ? 38 ILE H CD1 1 
ATOM 3033 N N   . ARG H 2 39 ? 6.725  77.299 32.080 1.00 33.64  ? 39 ARG H N   1 
ATOM 3034 C CA  . ARG H 2 39 ? 7.571  77.270 33.255 1.00 42.13  ? 39 ARG H CA  1 
ATOM 3035 C C   . ARG H 2 39 ? 8.010  75.827 33.463 1.00 37.85  ? 39 ARG H C   1 
ATOM 3036 O O   . ARG H 2 39 ? 7.215  74.940 33.199 1.00 42.12  ? 39 ARG H O   1 
ATOM 3037 C CB  . ARG H 2 39 ? 6.814  77.723 34.490 1.00 42.79  ? 39 ARG H CB  1 
ATOM 3038 C CG  . ARG H 2 39 ? 5.891  78.893 34.243 1.00 56.26  ? 39 ARG H CG  1 
ATOM 3039 C CD  . ARG H 2 39 ? 5.041  79.414 35.445 1.00 63.63  ? 39 ARG H CD  1 
ATOM 3040 N NE  . ARG H 2 39 ? 4.243  80.588 35.065 1.00 63.79  ? 39 ARG H NE  1 
ATOM 3041 C CZ  . ARG H 2 39 ? 4.763  81.824 35.006 1.00 61.31  ? 39 ARG H CZ  1 
ATOM 3042 N NH1 . ARG H 2 39 ? 6.043  82.128 35.261 1.00 57.18  ? 39 ARG H NH1 1 
ATOM 3043 N NH2 . ARG H 2 39 ? 3.966  82.793 34.603 1.00 64.28  ? 39 ARG H NH2 1 
ATOM 3044 N N   . PRO H 2 40 ? 9.200  75.500 33.931 1.00 35.24  ? 40 PRO H N   1 
ATOM 3045 C CA  . PRO H 2 40 ? 10.218 76.479 34.235 1.00 34.01  ? 40 PRO H CA  1 
ATOM 3046 C C   . PRO H 2 40 ? 11.100 76.755 33.031 1.00 35.35  ? 40 PRO H C   1 
ATOM 3047 O O   . PRO H 2 40 ? 10.935 76.171 31.962 1.00 40.92  ? 40 PRO H O   1 
ATOM 3048 C CB  . PRO H 2 40 ? 10.909 75.860 35.434 1.00 31.96  ? 40 PRO H CB  1 
ATOM 3049 C CG  . PRO H 2 40 ? 10.848 74.374 35.181 1.00 36.52  ? 40 PRO H CG  1 
ATOM 3050 C CD  . PRO H 2 40 ? 9.441  74.244 34.643 1.00 36.36  ? 40 PRO H CD  1 
ATOM 3051 N N   . CYS H 2 41 ? 11.986 77.730 33.139 1.00 33.27  ? 41 CYS H N   1 
ATOM 3052 C CA  . CYS H 2 41 ? 12.968 78.084 32.126 1.00 27.55  ? 41 CYS H CA  1 
ATOM 3053 C C   . CYS H 2 41 ? 14.117 78.436 33.067 1.00 29.83  ? 41 CYS H C   1 
ATOM 3054 O O   . CYS H 2 41 ? 13.939 78.900 34.199 1.00 32.38  ? 41 CYS H O   1 
ATOM 3055 C CB  . CYS H 2 41 ? 12.460 79.278 31.239 1.00 23.14  ? 41 CYS H CB  1 
ATOM 3056 S SG  . CYS H 2 41 ? 13.678 80.141 30.179 1.00 52.31  ? 41 CYS H SG  1 
ATOM 3057 N N   . MET H 2 42 ? 15.346 78.189 32.683 1.00 31.02  ? 42 MET H N   1 
ATOM 3058 C CA  . MET H 2 42 ? 16.457 78.181 33.605 1.00 24.52  ? 42 MET H CA  1 
ATOM 3059 C C   . MET H 2 42 ? 17.622 78.782 32.803 1.00 29.75  ? 42 MET H C   1 
ATOM 3060 O O   . MET H 2 42 ? 17.851 78.319 31.660 1.00 26.62  ? 42 MET H O   1 
ATOM 3061 C CB  . MET H 2 42 ? 16.441 76.680 33.879 1.00 32.65  ? 42 MET H CB  1 
ATOM 3062 C CG  . MET H 2 42 ? 17.402 75.932 34.739 1.00 31.29  ? 42 MET H CG  1 
ATOM 3063 S SD  . MET H 2 42 ? 16.573 75.919 36.318 1.00 34.88  ? 42 MET H SD  1 
ATOM 3064 C CE  . MET H 2 42 ? 18.061 75.880 37.272 1.00 35.58  ? 42 MET H CE  1 
ATOM 3065 N N   . LYS H 2 43 ? 18.322 79.817 33.279 1.00 27.17  ? 43 LYS H N   1 
ATOM 3066 C CA  . LYS H 2 43 ? 19.427 80.335 32.511 1.00 36.11  ? 43 LYS H CA  1 
ATOM 3067 C C   . LYS H 2 43 ? 20.667 80.262 33.361 1.00 42.06  ? 43 LYS H C   1 
ATOM 3068 O O   . LYS H 2 43 ? 20.648 80.644 34.539 1.00 46.78  ? 43 LYS H O   1 
ATOM 3069 C CB  . LYS H 2 43 ? 19.138 81.787 32.064 1.00 40.55  ? 43 LYS H CB  1 
ATOM 3070 C CG  . LYS H 2 43 ? 19.805 83.077 32.654 1.00 45.86  ? 43 LYS H CG  1 
ATOM 3071 C CD  . LYS H 2 43 ? 20.768 83.901 31.736 1.00 38.84  ? 43 LYS H CD  1 
ATOM 3072 C CE  . LYS H 2 43 ? 21.149 85.259 32.349 1.00 35.75  ? 43 LYS H CE  1 
ATOM 3073 N NZ  . LYS H 2 43 ? 19.998 86.124 32.512 1.00 35.97  ? 43 LYS H NZ  1 
ATOM 3074 N N   . LYS H 2 44 ? 21.728 79.722 32.774 1.00 43.95  ? 44 LYS H N   1 
ATOM 3075 C CA  . LYS H 2 44 ? 23.031 79.541 33.404 1.00 45.28  ? 44 LYS H CA  1 
ATOM 3076 C C   . LYS H 2 44 ? 24.043 80.522 32.803 1.00 47.26  ? 44 LYS H C   1 
ATOM 3077 O O   . LYS H 2 44 ? 24.000 80.791 31.585 1.00 38.99  ? 44 LYS H O   1 
ATOM 3078 C CB  . LYS H 2 44 ? 23.503 78.091 33.171 1.00 49.92  ? 44 LYS H CB  1 
ATOM 3079 C CG  . LYS H 2 44 ? 24.990 77.652 33.344 1.00 53.50  ? 44 LYS H CG  1 
ATOM 3080 C CD  . LYS H 2 44 ? 25.166 76.338 32.595 1.00 53.19  ? 44 LYS H CD  1 
ATOM 3081 C CE  . LYS H 2 44 ? 26.567 76.032 32.126 1.00 56.29  ? 44 LYS H CE  1 
ATOM 3082 N NZ  . LYS H 2 44 ? 27.491 75.587 33.147 1.00 61.43  ? 44 LYS H NZ  1 
ATOM 3083 N N   . THR H 2 45 ? 24.923 81.047 33.679 1.00 47.60  ? 45 THR H N   1 
ATOM 3084 C CA  . THR H 2 45 ? 26.012 81.956 33.324 1.00 45.79  ? 45 THR H CA  1 
ATOM 3085 C C   . THR H 2 45 ? 27.350 81.221 33.423 1.00 43.90  ? 45 THR H C   1 
ATOM 3086 O O   . THR H 2 45 ? 27.617 80.420 34.348 1.00 43.17  ? 45 THR H O   1 
ATOM 3087 C CB  . THR H 2 45 ? 26.110 83.199 34.279 1.00 48.36  ? 45 THR H CB  1 
ATOM 3088 O OG1 . THR H 2 45 ? 24.784 83.585 34.646 1.00 48.24  ? 45 THR H OG1 1 
ATOM 3089 C CG2 . THR H 2 45 ? 26.848 84.366 33.624 1.00 40.01  ? 45 THR H CG2 1 
ATOM 3090 N N   . ILE H 2 46 ? 28.196 81.515 32.450 1.00 39.07  ? 46 ILE H N   1 
ATOM 3091 C CA  . ILE H 2 46 ? 29.528 80.968 32.290 1.00 41.01  ? 46 ILE H CA  1 
ATOM 3092 C C   . ILE H 2 46 ? 30.486 82.171 32.316 1.00 49.55  ? 46 ILE H C   1 
ATOM 3093 O O   . ILE H 2 46 ? 30.409 83.027 31.423 1.00 55.25  ? 46 ILE H O   1 
ATOM 3094 C CB  . ILE H 2 46 ? 29.481 80.195 30.939 1.00 34.29  ? 46 ILE H CB  1 
ATOM 3095 C CG1 . ILE H 2 46 ? 28.586 78.980 31.112 1.00 28.24  ? 46 ILE H CG1 1 
ATOM 3096 C CG2 . ILE H 2 46 ? 30.867 79.794 30.481 1.00 33.51  ? 46 ILE H CG2 1 
ATOM 3097 C CD1 . ILE H 2 46 ? 28.277 78.320 29.781 1.00 27.59  ? 46 ILE H CD1 1 
ATOM 3098 N N   . TYR H 2 47 ? 31.385 82.296 33.294 1.00 48.25  ? 47 TYR H N   1 
ATOM 3099 C CA  . TYR H 2 47 ? 32.215 83.484 33.442 1.00 48.90  ? 47 TYR H CA  1 
ATOM 3100 C C   . TYR H 2 47 ? 33.608 83.185 32.886 1.00 55.30  ? 47 TYR H C   1 
ATOM 3101 O O   . TYR H 2 47 ? 34.041 82.055 32.932 1.00 54.72  ? 47 TYR H O   1 
ATOM 3102 C CB  . TYR H 2 47 ? 32.342 83.864 34.923 1.00 44.92  ? 47 TYR H CB  1 
ATOM 3103 C CG  . TYR H 2 47 ? 31.066 83.910 35.759 1.00 48.25  ? 47 TYR H CG  1 
ATOM 3104 C CD1 . TYR H 2 47 ? 30.130 82.888 35.743 1.00 53.33  ? 47 TYR H CD1 1 
ATOM 3105 C CD2 . TYR H 2 47 ? 30.831 85.010 36.550 1.00 52.20  ? 47 TYR H CD2 1 
ATOM 3106 C CE1 . TYR H 2 47 ? 28.978 82.969 36.491 1.00 54.81  ? 47 TYR H CE1 1 
ATOM 3107 C CE2 . TYR H 2 47 ? 29.677 85.100 37.301 1.00 51.84  ? 47 TYR H CE2 1 
ATOM 3108 C CZ  . TYR H 2 47 ? 28.761 84.080 37.265 1.00 54.70  ? 47 TYR H CZ  1 
ATOM 3109 O OH  . TYR H 2 47 ? 27.608 84.150 38.018 1.00 60.24  ? 47 TYR H OH  1 
ATOM 3110 N N   . GLU H 2 48 ? 34.333 84.165 32.359 1.00 68.48  ? 48 GLU H N   1 
ATOM 3111 C CA  . GLU H 2 48 ? 35.681 84.061 31.785 1.00 73.81  ? 48 GLU H CA  1 
ATOM 3112 C C   . GLU H 2 48 ? 36.504 82.893 32.235 1.00 73.40  ? 48 GLU H C   1 
ATOM 3113 O O   . GLU H 2 48 ? 36.975 82.842 33.373 1.00 60.92  ? 48 GLU H O   1 
ATOM 3114 C CB  . GLU H 2 48 ? 36.483 85.338 32.093 1.00 83.89  ? 48 GLU H CB  1 
ATOM 3115 C CG  . GLU H 2 48 ? 37.982 85.305 31.771 1.00 93.35  ? 48 GLU H CG  1 
ATOM 3116 C CD  . GLU H 2 48 ? 38.853 86.568 31.843 1.00 96.78  ? 48 GLU H CD  1 
ATOM 3117 O OE1 . GLU H 2 48 ? 38.896 87.296 30.850 1.00 99.97  ? 48 GLU H OE1 1 
ATOM 3118 O OE2 . GLU H 2 48 ? 39.534 86.792 32.854 1.00 99.39  ? 48 GLU H OE2 1 
ATOM 3119 N N   . ASN H 2 49 ? 36.591 81.942 31.318 1.00 86.05  ? 49 ASN H N   1 
ATOM 3120 C CA  . ASN H 2 49 ? 37.408 80.772 31.583 1.00 96.55  ? 49 ASN H CA  1 
ATOM 3121 C C   . ASN H 2 49 ? 38.788 81.085 31.059 1.00 94.38  ? 49 ASN H C   1 
ATOM 3122 O O   . ASN H 2 49 ? 39.083 80.807 29.892 1.00 92.32  ? 49 ASN H O   1 
ATOM 3123 C CB  . ASN H 2 49 ? 36.833 79.512 30.886 1.00 105.21 ? 49 ASN H CB  1 
ATOM 3124 C CG  . ASN H 2 49 ? 35.553 78.890 31.490 1.00 113.13 ? 49 ASN H CG  1 
ATOM 3125 O OD1 . ASN H 2 49 ? 35.062 79.190 32.584 1.00 116.79 ? 49 ASN H OD1 1 
ATOM 3126 N ND2 . ASN H 2 49 ? 34.935 77.941 30.798 1.00 114.11 ? 49 ASN H ND2 1 
ATOM 3127 N N   . GLU H 2 50 ? 39.503 81.825 31.909 1.00 94.16  ? 50 GLU H N   1 
ATOM 3128 C CA  . GLU H 2 50 ? 40.883 82.284 31.788 1.00 96.85  ? 50 GLU H CA  1 
ATOM 3129 C C   . GLU H 2 50 ? 41.078 83.339 32.894 1.00 96.00  ? 50 GLU H C   1 
ATOM 3130 O O   . GLU H 2 50 ? 41.881 84.271 32.770 1.00 93.41  ? 50 GLU H O   1 
ATOM 3131 C CB  . GLU H 2 50 ? 41.212 82.922 30.385 1.00 97.97  ? 50 GLU H CB  1 
ATOM 3132 C CG  . GLU H 2 50 ? 40.418 84.149 29.989 1.00 96.12  ? 50 GLU H CG  1 
ATOM 3133 C CD  . GLU H 2 50 ? 40.988 85.149 28.998 1.00 96.10  ? 50 GLU H CD  1 
ATOM 3134 O OE1 . GLU H 2 50 ? 42.211 85.332 28.937 1.00 95.46  ? 50 GLU H OE1 1 
ATOM 3135 O OE2 . GLU H 2 50 ? 40.165 85.757 28.303 1.00 95.97  ? 50 GLU H OE2 1 
ATOM 3136 O OXT . GLU H 2 50 ? 40.410 83.198 33.920 1.00 96.49  ? 50 GLU H OXT 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  ARG 1  2  2  ARG ARG A . n 
A 1 2  GLU 2  3  3  GLU GLU A . n 
A 1 3  ILE 3  4  4  ILE ILE A . n 
A 1 4  LYS 4  5  5  LYS LYS A . n 
A 1 5  GLY 5  6  6  GLY GLY A . n 
A 1 6  TYR 6  7  7  TYR TYR A . n 
A 1 7  GLU 7  8  8  GLU GLU A . n 
A 1 8  TYR 8  9  9  TYR TYR A . n 
A 1 9  GLN 9  10 10 GLN GLN A . n 
A 1 10 LEU 10 11 11 LEU LEU A . n 
A 1 11 TYR 11 12 12 TYR TYR A . n 
A 1 12 VAL 12 13 13 VAL VAL A . n 
A 1 13 TYR 13 14 14 TYR TYR A . n 
A 1 14 ALA 14 15 15 ALA ALA A . n 
A 1 15 SER 15 16 16 SER SER A . n 
A 1 16 ASP 16 17 17 ASP ASP A . n 
A 1 17 LYS 17 18 18 LYS LYS A . n 
A 1 18 LEU 18 19 19 LEU LEU A . n 
A 1 19 PHE 19 20 20 PHE PHE A . n 
A 1 20 ARG 20 21 21 ARG ARG A . n 
A 1 21 ALA 21 22 22 ALA ALA A . n 
A 1 22 ASP 22 23 23 ASP ASP A . n 
A 1 23 ILE 23 24 24 ILE ILE A . n 
A 1 24 SER 24 25 25 SER SER A . n 
A 1 25 GLU 25 26 26 GLU GLU A . n 
A 1 26 ASP 26 27 27 ASP ASP A . n 
A 1 27 TYR 27 28 28 TYR TYR A . n 
A 1 28 LYS 28 29 29 LYS LYS A . n 
A 1 29 THR 29 30 30 THR THR A . n 
A 1 30 ARG 30 31 31 ARG ARG A . n 
A 1 31 GLY 31 32 32 GLY GLY A . n 
A 1 32 ARG 32 33 33 ARG ARG A . n 
A 1 33 LYS 33 34 34 LYS LYS A . n 
A 1 34 LEU 34 35 35 LEU LEU A . n 
A 1 35 LEU 35 36 36 LEU LEU A . n 
A 1 36 ARG 36 37 37 ARG ARG A . n 
A 1 37 PHE 37 38 38 PHE PHE A . n 
A 1 38 ASN 38 39 39 ASN ASN A . n 
A 1 39 GLY 39 40 40 GLY GLY A . n 
A 1 40 PRO 40 41 41 PRO PRO A . n 
A 1 41 VAL 41 42 42 VAL VAL A . n 
A 1 42 PRO 42 43 43 PRO PRO A . n 
A 1 43 PRO 43 44 44 PRO PRO A . n 
A 1 44 PRO 44 45 45 PRO PRO A . n 
B 2 1  GLY 1  1  1  GLY GLY B . n 
B 2 2  GLU 2  2  2  GLU GLU B . n 
B 2 3  TRP 3  3  3  TRP TRP B . n 
B 2 4  GLU 4  4  4  GLU GLU B . n 
B 2 5  ILE 5  5  5  ILE ILE B . n 
B 2 6  ILE 6  6  6  ILE ILE B . n 
B 2 7  ASP 7  7  7  ASP ASP B . n 
B 2 8  ILE 8  8  8  ILE ILE B . n 
B 2 9  GLY 9  9  9  GLY GLY B . n 
B 2 10 PRO 10 10 10 PRO PRO B . n 
B 2 11 PHE 11 11 11 PHE PHE B . n 
B 2 12 THR 12 12 12 THR THR B . n 
B 2 13 GLN 13 13 13 GLN GLN B . n 
B 2 14 ASN 14 14 14 ASN ASN B . n 
B 2 15 LEU 15 15 15 LEU LEU B . n 
B 2 16 GLY 16 16 16 GLY GLY B . n 
B 2 17 LYS 17 17 17 LYS LYS B . n 
B 2 18 PHE 18 18 18 PHE PHE B . n 
B 2 19 ALA 19 19 19 ALA ALA B . n 
B 2 20 VAL 20 20 20 VAL VAL B . n 
B 2 21 ASP 21 21 21 ASP ASP B . n 
B 2 22 GLU 22 22 22 GLU GLU B . n 
B 2 23 GLU 23 23 23 GLU GLU B . n 
B 2 24 ASN 24 24 24 ASN ASN B . n 
B 2 25 LYS 25 25 25 LYS LYS B . n 
B 2 26 ILE 26 26 26 ILE ILE B . n 
B 2 27 GLY 27 27 27 GLY GLY B . n 
B 2 28 GLN 28 28 28 GLN GLN B . n 
B 2 29 TYR 29 29 29 TYR TYR B . n 
B 2 30 GLY 30 30 30 GLY GLY B . n 
B 2 31 ARG 31 31 31 ARG ARG B . n 
B 2 32 LEU 32 32 32 LEU LEU B . n 
B 2 33 THR 33 33 33 THR THR B . n 
B 2 34 PHE 34 34 34 PHE PHE B . n 
B 2 35 ASN 35 35 35 ASN ASN B . n 
B 2 36 LYS 36 36 36 LYS LYS B . n 
B 2 37 VAL 37 37 37 VAL VAL B . n 
B 2 38 ILE 38 38 38 ILE ILE B . n 
B 2 39 ARG 39 39 39 ARG ARG B . n 
B 2 40 PRO 40 40 40 PRO PRO B . n 
B 2 41 CYS 41 41 41 CYS CYS B . n 
B 2 42 MET 42 42 42 MET MET B . n 
B 2 43 LYS 43 43 43 LYS LYS B . n 
B 2 44 LYS 44 44 44 LYS LYS B . n 
B 2 45 THR 45 45 45 THR THR B . n 
B 2 46 ILE 46 46 46 ILE ILE B . n 
B 2 47 TYR 47 47 47 TYR TYR B . n 
B 2 48 GLU 48 48 48 GLU GLU B . n 
B 2 49 ASN 49 49 49 ASN ASN B . n 
B 2 50 GLU 50 50 50 GLU GLU B . n 
C 1 1  ARG 1  2  2  ARG ARG C . n 
C 1 2  GLU 2  3  3  GLU GLU C . n 
C 1 3  ILE 3  4  4  ILE ILE C . n 
C 1 4  LYS 4  5  5  LYS LYS C . n 
C 1 5  GLY 5  6  6  GLY GLY C . n 
C 1 6  TYR 6  7  7  TYR TYR C . n 
C 1 7  GLU 7  8  8  GLU GLU C . n 
C 1 8  TYR 8  9  9  TYR TYR C . n 
C 1 9  GLN 9  10 10 GLN GLN C . n 
C 1 10 LEU 10 11 11 LEU LEU C . n 
C 1 11 TYR 11 12 12 TYR TYR C . n 
C 1 12 VAL 12 13 13 VAL VAL C . n 
C 1 13 TYR 13 14 14 TYR TYR C . n 
C 1 14 ALA 14 15 15 ALA ALA C . n 
C 1 15 SER 15 16 16 SER SER C . n 
C 1 16 ASP 16 17 17 ASP ASP C . n 
C 1 17 LYS 17 18 18 LYS LYS C . n 
C 1 18 LEU 18 19 19 LEU LEU C . n 
C 1 19 PHE 19 20 20 PHE PHE C . n 
C 1 20 ARG 20 21 21 ARG ARG C . n 
C 1 21 ALA 21 22 22 ALA ALA C . n 
C 1 22 ASP 22 23 23 ASP ASP C . n 
C 1 23 ILE 23 24 24 ILE ILE C . n 
C 1 24 SER 24 25 25 SER SER C . n 
C 1 25 GLU 25 26 26 GLU GLU C . n 
C 1 26 ASP 26 27 27 ASP ASP C . n 
C 1 27 TYR 27 28 28 TYR TYR C . n 
C 1 28 LYS 28 29 29 LYS LYS C . n 
C 1 29 THR 29 30 30 THR THR C . n 
C 1 30 ARG 30 31 31 ARG ARG C . n 
C 1 31 GLY 31 32 32 GLY GLY C . n 
C 1 32 ARG 32 33 33 ARG ARG C . n 
C 1 33 LYS 33 34 34 LYS LYS C . n 
C 1 34 LEU 34 35 35 LEU LEU C . n 
C 1 35 LEU 35 36 36 LEU LEU C . n 
C 1 36 ARG 36 37 37 ARG ARG C . n 
C 1 37 PHE 37 38 38 PHE PHE C . n 
C 1 38 ASN 38 39 39 ASN ASN C . n 
C 1 39 GLY 39 40 40 GLY GLY C . n 
C 1 40 PRO 40 41 41 PRO PRO C . n 
C 1 41 VAL 41 42 42 VAL VAL C . n 
C 1 42 PRO 42 43 43 PRO PRO C . n 
C 1 43 PRO 43 44 44 PRO PRO C . n 
C 1 44 PRO 44 45 45 PRO PRO C . n 
D 2 1  GLY 1  1  1  GLY GLY D . n 
D 2 2  GLU 2  2  2  GLU GLU D . n 
D 2 3  TRP 3  3  3  TRP TRP D . n 
D 2 4  GLU 4  4  4  GLU GLU D . n 
D 2 5  ILE 5  5  5  ILE ILE D . n 
D 2 6  ILE 6  6  6  ILE ILE D . n 
D 2 7  ASP 7  7  7  ASP ASP D . n 
D 2 8  ILE 8  8  8  ILE ILE D . n 
D 2 9  GLY 9  9  9  GLY GLY D . n 
D 2 10 PRO 10 10 10 PRO PRO D . n 
D 2 11 PHE 11 11 11 PHE PHE D . n 
D 2 12 THR 12 12 12 THR THR D . n 
D 2 13 GLN 13 13 13 GLN GLN D . n 
D 2 14 ASN 14 14 14 ASN ASN D . n 
D 2 15 LEU 15 15 15 LEU LEU D . n 
D 2 16 GLY 16 16 16 GLY GLY D . n 
D 2 17 LYS 17 17 17 LYS LYS D . n 
D 2 18 PHE 18 18 18 PHE PHE D . n 
D 2 19 ALA 19 19 19 ALA ALA D . n 
D 2 20 VAL 20 20 20 VAL VAL D . n 
D 2 21 ASP 21 21 21 ASP ASP D . n 
D 2 22 GLU 22 22 22 GLU GLU D . n 
D 2 23 GLU 23 23 23 GLU GLU D . n 
D 2 24 ASN 24 24 24 ASN ASN D . n 
D 2 25 LYS 25 25 25 LYS LYS D . n 
D 2 26 ILE 26 26 26 ILE ILE D . n 
D 2 27 GLY 27 27 27 GLY GLY D . n 
D 2 28 GLN 28 28 28 GLN GLN D . n 
D 2 29 TYR 29 29 29 TYR TYR D . n 
D 2 30 GLY 30 30 30 GLY GLY D . n 
D 2 31 ARG 31 31 31 ARG ARG D . n 
D 2 32 LEU 32 32 32 LEU LEU D . n 
D 2 33 THR 33 33 33 THR THR D . n 
D 2 34 PHE 34 34 34 PHE PHE D . n 
D 2 35 ASN 35 35 35 ASN ASN D . n 
D 2 36 LYS 36 36 36 LYS LYS D . n 
D 2 37 VAL 37 37 37 VAL VAL D . n 
D 2 38 ILE 38 38 38 ILE ILE D . n 
D 2 39 ARG 39 39 39 ARG ARG D . n 
D 2 40 PRO 40 40 40 PRO PRO D . n 
D 2 41 CYS 41 41 41 CYS CYS D . n 
D 2 42 MET 42 42 42 MET MET D . n 
D 2 43 LYS 43 43 43 LYS LYS D . n 
D 2 44 LYS 44 44 44 LYS LYS D . n 
D 2 45 THR 45 45 45 THR THR D . n 
D 2 46 ILE 46 46 46 ILE ILE D . n 
D 2 47 TYR 47 47 47 TYR TYR D . n 
D 2 48 GLU 48 48 48 GLU GLU D . n 
D 2 49 ASN 49 49 49 ASN ASN D . n 
D 2 50 GLU 50 50 50 GLU GLU D . n 
E 1 1  ARG 1  2  2  ARG ARG E . n 
E 1 2  GLU 2  3  3  GLU GLU E . n 
E 1 3  ILE 3  4  4  ILE ILE E . n 
E 1 4  LYS 4  5  5  LYS LYS E . n 
E 1 5  GLY 5  6  6  GLY GLY E . n 
E 1 6  TYR 6  7  7  TYR TYR E . n 
E 1 7  GLU 7  8  8  GLU GLU E . n 
E 1 8  TYR 8  9  9  TYR TYR E . n 
E 1 9  GLN 9  10 10 GLN GLN E . n 
E 1 10 LEU 10 11 11 LEU LEU E . n 
E 1 11 TYR 11 12 12 TYR TYR E . n 
E 1 12 VAL 12 13 13 VAL VAL E . n 
E 1 13 TYR 13 14 14 TYR TYR E . n 
E 1 14 ALA 14 15 15 ALA ALA E . n 
E 1 15 SER 15 16 16 SER SER E . n 
E 1 16 ASP 16 17 17 ASP ASP E . n 
E 1 17 LYS 17 18 18 LYS LYS E . n 
E 1 18 LEU 18 19 19 LEU LEU E . n 
E 1 19 PHE 19 20 20 PHE PHE E . n 
E 1 20 ARG 20 21 21 ARG ARG E . n 
E 1 21 ALA 21 22 22 ALA ALA E . n 
E 1 22 ASP 22 23 23 ASP ASP E . n 
E 1 23 ILE 23 24 24 ILE ILE E . n 
E 1 24 SER 24 25 25 SER SER E . n 
E 1 25 GLU 25 26 26 GLU GLU E . n 
E 1 26 ASP 26 27 27 ASP ASP E . n 
E 1 27 TYR 27 28 28 TYR TYR E . n 
E 1 28 LYS 28 29 29 LYS LYS E . n 
E 1 29 THR 29 30 30 THR THR E . n 
E 1 30 ARG 30 31 31 ARG ARG E . n 
E 1 31 GLY 31 32 32 GLY GLY E . n 
E 1 32 ARG 32 33 33 ARG ARG E . n 
E 1 33 LYS 33 34 34 LYS LYS E . n 
E 1 34 LEU 34 35 35 LEU LEU E . n 
E 1 35 LEU 35 36 36 LEU LEU E . n 
E 1 36 ARG 36 37 37 ARG ARG E . n 
E 1 37 PHE 37 38 38 PHE PHE E . n 
E 1 38 ASN 38 39 39 ASN ASN E . n 
E 1 39 GLY 39 40 40 GLY GLY E . n 
E 1 40 PRO 40 41 41 PRO PRO E . n 
E 1 41 VAL 41 42 42 VAL VAL E . n 
E 1 42 PRO 42 43 43 PRO PRO E . n 
E 1 43 PRO 43 44 44 PRO PRO E . n 
E 1 44 PRO 44 45 45 PRO PRO E . n 
F 2 1  GLY 1  1  1  GLY GLY F . n 
F 2 2  GLU 2  2  2  GLU GLU F . n 
F 2 3  TRP 3  3  3  TRP TRP F . n 
F 2 4  GLU 4  4  4  GLU GLU F . n 
F 2 5  ILE 5  5  5  ILE ILE F . n 
F 2 6  ILE 6  6  6  ILE ILE F . n 
F 2 7  ASP 7  7  7  ASP ASP F . n 
F 2 8  ILE 8  8  8  ILE ILE F . n 
F 2 9  GLY 9  9  9  GLY GLY F . n 
F 2 10 PRO 10 10 10 PRO PRO F . n 
F 2 11 PHE 11 11 11 PHE PHE F . n 
F 2 12 THR 12 12 12 THR THR F . n 
F 2 13 GLN 13 13 13 GLN GLN F . n 
F 2 14 ASN 14 14 14 ASN ASN F . n 
F 2 15 LEU 15 15 15 LEU LEU F . n 
F 2 16 GLY 16 16 16 GLY GLY F . n 
F 2 17 LYS 17 17 17 LYS LYS F . n 
F 2 18 PHE 18 18 18 PHE PHE F . n 
F 2 19 ALA 19 19 19 ALA ALA F . n 
F 2 20 VAL 20 20 20 VAL VAL F . n 
F 2 21 ASP 21 21 21 ASP ASP F . n 
F 2 22 GLU 22 22 22 GLU GLU F . n 
F 2 23 GLU 23 23 23 GLU GLU F . n 
F 2 24 ASN 24 24 24 ASN ASN F . n 
F 2 25 LYS 25 25 25 LYS LYS F . n 
F 2 26 ILE 26 26 26 ILE ILE F . n 
F 2 27 GLY 27 27 27 GLY GLY F . n 
F 2 28 GLN 28 28 28 GLN GLN F . n 
F 2 29 TYR 29 29 29 TYR TYR F . n 
F 2 30 GLY 30 30 30 GLY GLY F . n 
F 2 31 ARG 31 31 31 ARG ARG F . n 
F 2 32 LEU 32 32 32 LEU LEU F . n 
F 2 33 THR 33 33 33 THR THR F . n 
F 2 34 PHE 34 34 34 PHE PHE F . n 
F 2 35 ASN 35 35 35 ASN ASN F . n 
F 2 36 LYS 36 36 36 LYS LYS F . n 
F 2 37 VAL 37 37 37 VAL VAL F . n 
F 2 38 ILE 38 38 38 ILE ILE F . n 
F 2 39 ARG 39 39 39 ARG ARG F . n 
F 2 40 PRO 40 40 40 PRO PRO F . n 
F 2 41 CYS 41 41 41 CYS CYS F . n 
F 2 42 MET 42 42 42 MET MET F . n 
F 2 43 LYS 43 43 43 LYS LYS F . n 
F 2 44 LYS 44 44 44 LYS LYS F . n 
F 2 45 THR 45 45 45 THR THR F . n 
F 2 46 ILE 46 46 46 ILE ILE F . n 
F 2 47 TYR 47 47 47 TYR TYR F . n 
F 2 48 GLU 48 48 48 GLU GLU F . n 
F 2 49 ASN 49 49 49 ASN ASN F . n 
F 2 50 GLU 50 50 50 GLU GLU F . n 
G 1 1  ARG 1  2  2  ARG ARG G . n 
G 1 2  GLU 2  3  3  GLU GLU G . n 
G 1 3  ILE 3  4  4  ILE ILE G . n 
G 1 4  LYS 4  5  5  LYS LYS G . n 
G 1 5  GLY 5  6  6  GLY GLY G . n 
G 1 6  TYR 6  7  7  TYR TYR G . n 
G 1 7  GLU 7  8  8  GLU GLU G . n 
G 1 8  TYR 8  9  9  TYR TYR G . n 
G 1 9  GLN 9  10 10 GLN GLN G . n 
G 1 10 LEU 10 11 11 LEU LEU G . n 
G 1 11 TYR 11 12 12 TYR TYR G . n 
G 1 12 VAL 12 13 13 VAL VAL G . n 
G 1 13 TYR 13 14 14 TYR TYR G . n 
G 1 14 ALA 14 15 15 ALA ALA G . n 
G 1 15 SER 15 16 16 SER SER G . n 
G 1 16 ASP 16 17 17 ASP ASP G . n 
G 1 17 LYS 17 18 18 LYS LYS G . n 
G 1 18 LEU 18 19 19 LEU LEU G . n 
G 1 19 PHE 19 20 20 PHE PHE G . n 
G 1 20 ARG 20 21 21 ARG ARG G . n 
G 1 21 ALA 21 22 22 ALA ALA G . n 
G 1 22 ASP 22 23 23 ASP ASP G . n 
G 1 23 ILE 23 24 24 ILE ILE G . n 
G 1 24 SER 24 25 25 SER SER G . n 
G 1 25 GLU 25 26 26 GLU GLU G . n 
G 1 26 ASP 26 27 27 ASP ASP G . n 
G 1 27 TYR 27 28 28 TYR TYR G . n 
G 1 28 LYS 28 29 29 LYS LYS G . n 
G 1 29 THR 29 30 30 THR THR G . n 
G 1 30 ARG 30 31 31 ARG ARG G . n 
G 1 31 GLY 31 32 32 GLY GLY G . n 
G 1 32 ARG 32 33 33 ARG ARG G . n 
G 1 33 LYS 33 34 34 LYS LYS G . n 
G 1 34 LEU 34 35 35 LEU LEU G . n 
G 1 35 LEU 35 36 36 LEU LEU G . n 
G 1 36 ARG 36 37 37 ARG ARG G . n 
G 1 37 PHE 37 38 38 PHE PHE G . n 
G 1 38 ASN 38 39 39 ASN ASN G . n 
G 1 39 GLY 39 40 40 GLY GLY G . n 
G 1 40 PRO 40 41 41 PRO PRO G . n 
G 1 41 VAL 41 42 42 VAL VAL G . n 
G 1 42 PRO 42 43 43 PRO PRO G . n 
G 1 43 PRO 43 44 44 PRO PRO G . n 
G 1 44 PRO 44 45 45 PRO PRO G . n 
H 2 1  GLY 1  1  1  GLY GLY H . n 
H 2 2  GLU 2  2  2  GLU GLU H . n 
H 2 3  TRP 3  3  3  TRP TRP H . n 
H 2 4  GLU 4  4  4  GLU GLU H . n 
H 2 5  ILE 5  5  5  ILE ILE H . n 
H 2 6  ILE 6  6  6  ILE ILE H . n 
H 2 7  ASP 7  7  7  ASP ASP H . n 
H 2 8  ILE 8  8  8  ILE ILE H . n 
H 2 9  GLY 9  9  9  GLY GLY H . n 
H 2 10 PRO 10 10 10 PRO PRO H . n 
H 2 11 PHE 11 11 11 PHE PHE H . n 
H 2 12 THR 12 12 12 THR THR H . n 
H 2 13 GLN 13 13 13 GLN GLN H . n 
H 2 14 ASN 14 14 14 ASN ASN H . n 
H 2 15 LEU 15 15 15 LEU LEU H . n 
H 2 16 GLY 16 16 16 GLY GLY H . n 
H 2 17 LYS 17 17 17 LYS LYS H . n 
H 2 18 PHE 18 18 18 PHE PHE H . n 
H 2 19 ALA 19 19 19 ALA ALA H . n 
H 2 20 VAL 20 20 20 VAL VAL H . n 
H 2 21 ASP 21 21 21 ASP ASP H . n 
H 2 22 GLU 22 22 22 GLU GLU H . n 
H 2 23 GLU 23 23 23 GLU GLU H . n 
H 2 24 ASN 24 24 24 ASN ASN H . n 
H 2 25 LYS 25 25 25 LYS LYS H . n 
H 2 26 ILE 26 26 26 ILE ILE H . n 
H 2 27 GLY 27 27 27 GLY GLY H . n 
H 2 28 GLN 28 28 28 GLN GLN H . n 
H 2 29 TYR 29 29 29 TYR TYR H . n 
H 2 30 GLY 30 30 30 GLY GLY H . n 
H 2 31 ARG 31 31 31 ARG ARG H . n 
H 2 32 LEU 32 32 32 LEU LEU H . n 
H 2 33 THR 33 33 33 THR THR H . n 
H 2 34 PHE 34 34 34 PHE PHE H . n 
H 2 35 ASN 35 35 35 ASN ASN H . n 
H 2 36 LYS 36 36 36 LYS LYS H . n 
H 2 37 VAL 37 37 37 VAL VAL H . n 
H 2 38 ILE 38 38 38 ILE ILE H . n 
H 2 39 ARG 39 39 39 ARG ARG H . n 
H 2 40 PRO 40 40 40 PRO PRO H . n 
H 2 41 CYS 41 41 41 CYS CYS H . n 
H 2 42 MET 42 42 42 MET MET H . n 
H 2 43 LYS 43 43 43 LYS LYS H . n 
H 2 44 LYS 44 44 44 LYS LYS H . n 
H 2 45 THR 45 45 45 THR THR H . n 
H 2 46 ILE 46 46 46 ILE ILE H . n 
H 2 47 TYR 47 47 47 TYR TYR H . n 
H 2 48 GLU 48 48 48 GLU GLU H . n 
H 2 49 ASN 49 49 49 ASN ASN H . n 
H 2 50 GLU 50 50 50 GLU GLU H . n 
# 
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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B 
2 1 C,D 
3 1 E,F 
4 1 G,H 
# 
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)' 2550 ? 
1 MORE         -21  ? 
1 'SSA (A^2)'  6020 ? 
2 'ABSA (A^2)' 2460 ? 
2 MORE         -20  ? 
2 'SSA (A^2)'  6080 ? 
3 'ABSA (A^2)' 2490 ? 
3 MORE         -21  ? 
3 'SSA (A^2)'  6070 ? 
4 'ABSA (A^2)' 2560 ? 
4 MORE         -20  ? 
4 'SSA (A^2)'  5870 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 1993-10-31 
2 'Structure model' 1 1 2008-03-25 
3 'Structure model' 1 2 2011-07-13 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
_software.name             X-PLOR 
_software.classification   refinement 
_software.version          . 
_software.citation_id      ? 
_software.pdbx_ordinal     1 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;SHEET
EACH MOLECULE CONTAINS A SHEET CONSISTING OF STRANDS FROM
BOTH CHAINS.  ONE OF THE STRANDS CONTAINS A BULGE AND THIS
IS REPRESENTED BY PRESENTING THE SHEET TWICE EACH WITH
PART OF THAT STRAND.
;
# 
_pdbx_entry_details.entry_id             3MON 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;SEQUENCE ADVISORY NOTICE:
     DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.

     SWISS-PROT ENTRY NAME: MONB_DIOCU MONELLIN

     SWISS-PROT RESIDUE      PDB SEQRES
       NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE
       GLU    49             ASN     B    49
       ASN    50             GLU     B    50
       GLU    49             ASN     D    49
       ASN    50             GLU     D    50
       GLU    49             ASN     F    49
       ASN    50             GLU     F    50
       GLU    49             ASN     H    49
       ASN    50             GLU     H    50
;
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 NE  A ARG 2  ? ? CZ  A ARG 2  ? ? NH1 A ARG 2  ? ? 123.41 120.30 3.11   0.50 N 
2  1 CA  A LYS 5  ? ? CB  A LYS 5  ? ? CG  A LYS 5  ? ? 135.08 113.40 21.68  2.20 N 
3  1 CA  A LEU 11 ? ? CB  A LEU 11 ? ? CG  A LEU 11 ? ? 133.51 115.30 18.21  2.30 N 
4  1 NE  A ARG 31 ? ? CZ  A ARG 31 ? ? NH1 A ARG 31 ? ? 125.21 120.30 4.91   0.50 N 
5  1 NE  A ARG 31 ? ? CZ  A ARG 31 ? ? NH2 A ARG 31 ? ? 113.68 120.30 -6.62  0.50 N 
6  1 NE  A ARG 33 ? ? CZ  A ARG 33 ? ? NH2 A ARG 33 ? ? 116.91 120.30 -3.39  0.50 N 
7  1 CD1 B TRP 3  ? ? CG  B TRP 3  ? ? CD2 B TRP 3  ? ? 111.40 106.30 5.10   0.80 N 
8  1 N   B GLN 28 ? ? CA  B GLN 28 ? ? CB  B GLN 28 ? ? 96.09  110.60 -14.51 1.80 N 
9  1 CA  B GLN 28 ? ? CB  B GLN 28 ? ? CG  B GLN 28 ? ? 133.88 113.40 20.48  2.20 N 
10 1 CG1 B VAL 37 ? ? CB  B VAL 37 ? ? CG2 B VAL 37 ? ? 100.64 110.90 -10.26 1.60 N 
11 1 N   B MET 42 ? ? CA  B MET 42 ? ? CB  B MET 42 ? ? 94.38  110.60 -16.22 1.80 N 
12 1 CA  B MET 42 ? ? CB  B MET 42 ? ? CG  B MET 42 ? ? 128.78 113.30 15.48  1.70 N 
13 1 CA  B LYS 43 ? ? CB  B LYS 43 ? ? CG  B LYS 43 ? ? 128.49 113.40 15.09  2.20 N 
14 1 CA  C LEU 11 ? ? CB  C LEU 11 ? ? CG  C LEU 11 ? ? 134.93 115.30 19.63  2.30 N 
15 1 NE  C ARG 21 ? ? CZ  C ARG 21 ? ? NH1 C ARG 21 ? ? 123.72 120.30 3.42   0.50 N 
16 1 NE  C ARG 21 ? ? CZ  C ARG 21 ? ? NH2 C ARG 21 ? ? 116.86 120.30 -3.44  0.50 N 
17 1 CB  C ARG 31 ? ? CG  C ARG 31 ? ? CD  C ARG 31 ? ? 87.76  111.60 -23.84 2.60 N 
18 1 NE  C ARG 31 ? ? CZ  C ARG 31 ? ? NH1 C ARG 31 ? ? 124.34 120.30 4.04   0.50 N 
19 1 NE  C ARG 31 ? ? CZ  C ARG 31 ? ? NH2 C ARG 31 ? ? 110.52 120.30 -9.78  0.50 N 
20 1 CD1 D TRP 3  ? ? CG  D TRP 3  ? ? CD2 D TRP 3  ? ? 111.90 106.30 5.60   0.80 N 
21 1 CE2 D TRP 3  ? ? CD2 D TRP 3  ? ? CG  D TRP 3  ? ? 102.21 107.30 -5.09  0.80 N 
22 1 NE  D ARG 31 ? ? CZ  D ARG 31 ? ? NH1 D ARG 31 ? ? 123.48 120.30 3.18   0.50 N 
23 1 NE  D ARG 31 ? ? CZ  D ARG 31 ? ? NH2 D ARG 31 ? ? 116.43 120.30 -3.87  0.50 N 
24 1 CA  D MET 42 ? ? CB  D MET 42 ? ? CG  D MET 42 ? ? 124.93 113.30 11.63  1.70 N 
25 1 NE  E ARG 2  ? ? CZ  E ARG 2  ? ? NH1 E ARG 2  ? ? 125.43 120.30 5.13   0.50 N 
26 1 CB  E TYR 7  ? ? CG  E TYR 7  ? ? CD2 E TYR 7  ? ? 117.08 121.00 -3.92  0.60 N 
27 1 CA  E LEU 11 ? ? CB  E LEU 11 ? ? CG  E LEU 11 ? ? 134.91 115.30 19.61  2.30 N 
28 1 CG  E ARG 31 ? ? CD  E ARG 31 ? ? NE  E ARG 31 ? ? 97.18  111.80 -14.62 2.10 N 
29 1 NE  E ARG 31 ? ? CZ  E ARG 31 ? ? NH1 E ARG 31 ? ? 126.86 120.30 6.56   0.50 N 
30 1 NE  E ARG 31 ? ? CZ  E ARG 31 ? ? NH2 E ARG 31 ? ? 114.63 120.30 -5.67  0.50 N 
31 1 CD1 F TRP 3  ? ? CG  F TRP 3  ? ? CD2 F TRP 3  ? ? 112.65 106.30 6.35   0.80 N 
32 1 CE2 F TRP 3  ? ? CD2 F TRP 3  ? ? CG  F TRP 3  ? ? 101.89 107.30 -5.41  0.80 N 
33 1 NE  F ARG 31 ? ? CZ  F ARG 31 ? ? NH1 F ARG 31 ? ? 125.77 120.30 5.47   0.50 N 
34 1 NE  F ARG 31 ? ? CZ  F ARG 31 ? ? NH2 F ARG 31 ? ? 116.49 120.30 -3.81  0.50 N 
35 1 NE  F ARG 39 ? ? CZ  F ARG 39 ? ? NH1 F ARG 39 ? ? 123.68 120.30 3.38   0.50 N 
36 1 NE  F ARG 39 ? ? CZ  F ARG 39 ? ? NH2 F ARG 39 ? ? 116.52 120.30 -3.78  0.50 N 
37 1 CA  F LYS 43 ? ? CB  F LYS 43 ? ? CG  F LYS 43 ? ? 127.24 113.40 13.84  2.20 N 
38 1 CB  G TYR 7  ? ? CG  G TYR 7  ? ? CD2 G TYR 7  ? ? 116.73 121.00 -4.27  0.60 N 
39 1 CB  G TYR 12 ? ? CG  G TYR 12 ? ? CD2 G TYR 12 ? ? 117.16 121.00 -3.84  0.60 N 
40 1 CB  G TYR 28 ? ? CG  G TYR 28 ? ? CD1 G TYR 28 ? ? 117.22 121.00 -3.78  0.60 N 
41 1 NE  G ARG 31 ? ? CZ  G ARG 31 ? ? NH1 G ARG 31 ? ? 113.61 120.30 -6.69  0.50 N 
42 1 NE  G ARG 31 ? ? CZ  G ARG 31 ? ? NH2 G ARG 31 ? ? 130.04 120.30 9.74   0.50 N 
43 1 N   H GLY 1  ? ? CA  H GLY 1  ? ? C   H GLY 1  ? ? 97.85  113.10 -15.25 2.50 N 
44 1 CD1 H TRP 3  ? ? CG  H TRP 3  ? ? CD2 H TRP 3  ? ? 111.70 106.30 5.40   0.80 N 
45 1 CE2 H TRP 3  ? ? CD2 H TRP 3  ? ? CG  H TRP 3  ? ? 102.25 107.30 -5.05  0.80 N 
46 1 NE  H ARG 39 ? ? CZ  H ARG 39 ? ? NH1 H ARG 39 ? ? 124.79 120.30 4.49   0.50 N 
47 1 NE  H ARG 39 ? ? CZ  H ARG 39 ? ? NH2 H ARG 39 ? ? 117.15 120.30 -3.15  0.50 N 
48 1 N   H MET 42 ? ? CA  H MET 42 ? ? CB  H MET 42 ? ? 96.43  110.60 -14.17 1.80 N 
49 1 CA  H MET 42 ? ? CB  H MET 42 ? ? CG  H MET 42 ? ? 126.18 113.30 12.88  1.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 5  ? ? 177.95  82.14  
2  1 ARG A 31 ? ? 72.55   30.71  
3  1 ASN B 35 ? ? -130.44 -53.91 
4  1 GLU B 48 ? ? -60.92  63.71  
5  1 PHE C 38 ? ? -160.91 102.70 
6  1 ASN D 35 ? ? -146.94 -76.11 
7  1 GLU D 48 ? ? -163.64 75.61  
8  1 GLU E 3  ? ? -114.38 73.37  
9  1 ARG E 31 ? ? 49.37   24.89  
10 1 LYS E 34 ? ? -169.12 111.07 
11 1 GLN F 28 ? ? -49.01  -19.93 
12 1 ASN F 35 ? ? -117.01 -74.70 
13 1 GLU G 26 ? ? -164.58 112.42 
14 1 ARG G 31 ? ? 80.35   15.20  
15 1 ILE H 8  ? ? -64.62  40.43  
16 1 ASN H 35 ? ? -122.27 -69.78 
17 1 LYS H 36 ? ? -172.43 148.29 
18 1 GLU H 48 ? ? -22.30  104.74 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             GLU 
_pdbx_validate_main_chain_plane.auth_asym_id             E 
_pdbx_validate_main_chain_plane.auth_seq_id              3 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.83 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR A 12 ? ? 0.073 'SIDE CHAIN' 
2 1 TYR B 29 ? ? 0.092 'SIDE CHAIN' 
3 1 ARG E 31 ? ? 0.087 'SIDE CHAIN' 
4 1 TYR F 29 ? ? 0.072 'SIDE CHAIN' 
5 1 TYR G 7  ? ? 0.064 'SIDE CHAIN' 
# 
