data_16735 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR resonance assignment of the apo C-terminal polypeptide of the Anthrax Lethal Factor catalytic domain ; _BMRB_accession_number 16735 _BMRB_flat_file_name bmr16735.str _Entry_type original _Submission_date 2010-02-18 _Accession_date 2010-02-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Anthrax LF C-termoinal (106 a.a.) recombionant polypeptide expressed in E.coli studied through NMR spectroscopy' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dalkas Georgios A. . 2 Chasapis Christos T. . 3 Gkazonis Petros V. . 4 Bentrop Detlef . . 5 Spyroulias Georgios A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 88 "13C chemical shifts" 264 "15N chemical shifts" 88 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-08-19 update BMRB 'complete entry citation' 2010-05-18 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Purification and biophysical characterization of the core protease domain of anthrax lethal factor.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20438702 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gkazonis Petros V. . 2 Dalkas Georgios A. . 3 Chasapis Christos T. . 4 Vlamis-Gardikas Alexios . . 5 Bentrop Detlef . . 6 Spyroulias Georgios A. . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_name_full 'Biochemical and biophysical research communications' _Journal_volume 396 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 643 _Page_last 647 _Year 2010 _Details . loop_ _Keyword 'Bacillus Anrhacis' 'Lethal Factor Catalytic domain' 'NMR Spectroscopy' 'Overexpression in E. coli' 'Zinc Metalloprotease' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Anthrax Lethal Factor C-terminal' _Enzyme_commission_number 'EC 3.4.24.83' loop_ _Mol_system_component_name _Mol_label 'Anthrax Lethal Factor C-terminal' $Anthrax_LF_C-terminal stop_ _System_molecular_weight 12122.4 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Zinc metallopeptidase' stop_ _Database_query_date . _Details '106 residues C-terminal of the Anthrax lethal toxin endopeptidase component' save_ ######################## # Monomeric polymers # ######################## save_Anthrax_LF_C-terminal _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Anthrax_LF_C-terminal _Molecular_mass 12122.4 _Mol_thiol_state 'not present' loop_ _Biological_function 'Anthrax lethal toxin endopeptidase component' 'Zinc Metallopeptidase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; GSKGVELRNDSEGFIHEFGH AVDDYAGYLLDKNQSDLVTN SKKFIDIFKEEGSNLTSYGR TNEAEFFAEAFRLMHSTDHA ERLKVQKNAPKTFQFINDQI KFIINS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 LYS 4 GLY 5 VAL 6 GLU 7 LEU 8 ARG 9 ASN 10 ASP 11 SER 12 GLU 13 GLY 14 PHE 15 ILE 16 HIS 17 GLU 18 PHE 19 GLY 20 HIS 21 ALA 22 VAL 23 ASP 24 ASP 25 TYR 26 ALA 27 GLY 28 TYR 29 LEU 30 LEU 31 ASP 32 LYS 33 ASN 34 GLN 35 SER 36 ASP 37 LEU 38 VAL 39 THR 40 ASN 41 SER 42 LYS 43 LYS 44 PHE 45 ILE 46 ASP 47 ILE 48 PHE 49 LYS 50 GLU 51 GLU 52 GLY 53 SER 54 ASN 55 LEU 56 THR 57 SER 58 TYR 59 GLY 60 ARG 61 THR 62 ASN 63 GLU 64 ALA 65 GLU 66 PHE 67 PHE 68 ALA 69 GLU 70 ALA 71 PHE 72 ARG 73 LEU 74 MET 75 HIS 76 SER 77 THR 78 ASP 79 HIS 80 ALA 81 GLU 82 ARG 83 LEU 84 LYS 85 VAL 86 GLN 87 LYS 88 ASN 89 ALA 90 PRO 91 LYS 92 THR 93 PHE 94 GLN 95 PHE 96 ILE 97 ASN 98 ASP 99 GLN 100 ILE 101 LYS 102 PHE 103 ILE 104 ILE 105 ASN 106 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1J7N "Anthrax Toxin Lethal Factor" 99.06 776 100.00 100.00 7.09e-64 PDB 1JKY "Crystal Structure Of The Anthrax Lethal Factor (Lf): Wild- Type Lf Complexed With The N-Terminal Sequence Of Mapkk2" 99.06 776 100.00 100.00 7.09e-64 PDB 1PWP "Crystal Structure Of The Anthrax Lethal Factor Complexed With Small Molecule Inhibitor Nsc 12155" 99.06 776 100.00 100.00 7.09e-64 PDB 1PWQ "Crystal Structure Of Anthrax Lethal Factor Complexed With Thioacetyl-Tyr-Pro-Met-Amide, A Metal-Chelating Peptidyl Small Molecu" 99.06 776 100.00 100.00 7.09e-64 PDB 1PWU "Crystal Structure Of Anthrax Lethal Factor Complexed With (3-(n-hydroxycarboxamido)-2-isobutylpropanoyl-trp- Methylamide), A Kn" 99.06 776 99.05 99.05 8.69e-63 PDB 1PWV "Crystal Structure Of Anthrax Lethal Factor Wild-Type Protein Complexed With An Optimised Peptide Substrate." 99.06 776 100.00 100.00 7.09e-64 PDB 1PWW "Crystal Structure Of Anthrax Lethal Factor Active Site Mutant Protein Complexed With An Optimised Peptide Substrate In The Pres" 99.06 776 99.05 99.05 8.69e-63 PDB 1YQY "Structure Of B. Anthrax Lethal Factor In Complex With A Hydroxamate Inhibitor" 99.06 523 100.00 100.00 1.46e-65 PDB 1ZXV "X-Ray Crystal Structure Of The Anthrax Lethal Factor Bound To A Small Molecule Inhibitor, Bi-Mfm3, 3-{5-[5-(4-Chloro- Phenyl)-F" 99.06 776 100.00 100.00 7.09e-64 PDB 2L0R "Conformational Dynamics Of The Anthrax Lethal Factor Catalytic Center" 100.00 106 100.00 100.00 4.71e-70 PDB 4DV8 "Anthrax Lethal Factor Metalloproteinase In Complex With The Hydroxamic Acid Based Small Molecule Pt8421" 99.06 526 100.00 100.00 2.87e-65 PDB 4PKQ "Anthrax Toxin Lethal Factor With Bound Zinc" 99.06 519 100.00 100.00 1.09e-65 PDB 4PKR "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor 10" 99.06 519 100.00 100.00 1.09e-65 PDB 4PKS "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor 11" 99.06 519 100.00 100.00 1.09e-65 PDB 4PKT "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor 13" 99.06 519 100.00 100.00 1.09e-65 PDB 4PKU "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor 15" 99.06 519 100.00 100.00 1.09e-65 PDB 4PKV "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor 16" 99.06 519 100.00 100.00 1.09e-65 PDB 4PKW "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor Gm6001" 99.06 519 100.00 100.00 1.09e-65 PDB 4WF6 "Anthrax Toxin Lethal Factor With Bound Small Molecule Inhibitor Mk-31" 99.06 519 100.00 100.00 1.09e-65 PDB 4XM6 "Anthrax Toxin Lethal Factor With Ligand-induced Binding Pocket" 99.06 519 100.00 100.00 1.09e-65 PDB 4XM7 "Anthrax Toxin Lethal Factor With Ligand-induced Binding Pocket" 99.06 519 100.00 100.00 1.09e-65 PDB 4XM8 "Anthrax Toxin Lethal Factor With Ligand-induced Binding Pocket" 99.06 519 100.00 100.00 1.09e-65 PDB 5D1S "Anthrax Toxin Lethal Factor With Hydroxamic Acid Inhibitor" 99.06 519 100.00 100.00 1.09e-65 PDB 5D1T "Anthrax Toxin Lethal Factor With Hydroxamic Acid Inhibitor" 99.06 519 100.00 100.00 1.09e-65 PDB 5D1U "Anthrax Toxin Lethal Factor With Hydroxamic Acid Inhibitor" 99.06 519 100.00 100.00 1.09e-65 DBJ BAR79124 "lethal factor (plasmid) [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 DBJ GAF01219 "calmodulin sensitive adenylate cyclase, edema factor, cya, plasmid pXO1, B. anthracis [Bacillus anthracis CZC5]" 99.06 809 100.00 100.00 6.78e-64 DBJ GAO62612 "lethal factor [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 DBJ GAO68443 "lethal factor [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 EMBL CAC93932 "Lef protein [Bacillus anthracis]" 99.06 781 100.00 100.00 7.75e-64 EMBL CAC93933 "Lef protein [Bacillus anthracis]" 99.06 781 100.00 100.00 7.75e-64 GB AAA22569 "lethal factor precursor [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 GB AAA79216 "lethal factor precursor [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 GB AAD32411 "pXO1-107 [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 GB AAM26117 "anthrax lethal factor endopeptidase [Bacillus anthracis str. A2012]" 99.06 809 100.00 100.00 6.78e-64 GB AAT28913 "anthrax lethal factor endopeptidase [Bacillus anthracis str. 'Ames Ancestor']" 99.06 809 100.00 100.00 6.78e-64 REF NP_052803 "pXO1-107 [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 REF WP_001022096 "Lethal factor [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 REF WP_001022097 "Lethal factor [Bacillus anthracis]" 99.06 809 100.00 100.00 6.78e-64 REF WP_001022099 "Lethal factor [Bacillus anthracis]" 99.06 809 99.05 99.05 9.17e-63 REF WP_001022100 "Lethal factor [Bacillus cereus]" 99.06 809 100.00 100.00 6.64e-64 SP P15917 "RecName: Full=Lethal factor; Short=LF; AltName: Full=Anthrax lethal toxin endopeptidase component; Flags: Precursor" 99.06 809 100.00 100.00 6.78e-64 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Anthrax_LF_C-terminal 'Bacillus Anthracis' 1392 Bacteria . Bacillus Anthracis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Anthrax_LF_C-terminal 'recombinant technology' . Escherichia coli BL21 pGEX-4T1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Anthrax_LF_C-terminal 0.6 mM '[U-98% 13C; U-98% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN+ _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'equipped with Cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HN(CO)CA' '3D HNCA' '3D HNCO' '3D HCACO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Anthrax Lethal Factor C-terminal' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 GLY H H 7.859 0.0015 1 2 1 1 GLY CA C 45.715 0.0015 1 3 1 1 GLY N N 106.813 0.0015 1 4 2 2 SER H H 8.182 0.0015 1 5 2 2 SER CA C 58.727 0.0015 1 6 2 2 SER CB C 63.845 0.0015 1 7 2 2 SER N N 115.491 0.0015 1 8 3 3 LYS H H 8.591 0.0015 1 9 3 3 LYS C C 177.024 0.0015 1 10 3 3 LYS CA C 56.464 0.0015 1 11 3 3 LYS CB C 32.857 0.0015 1 12 3 3 LYS N N 123.364 0.0015 1 13 4 4 GLY H H 8.460 0.0015 1 14 4 4 GLY C C 174.059 0.0015 1 15 4 4 GLY CA C 45.280 0.0015 1 16 4 4 GLY N N 110.289 0.0015 1 17 5 5 VAL H H 8.000 0.0015 1 18 5 5 VAL CA C 62.305 0.0015 1 19 5 5 VAL CB C 32.521 0.0015 1 20 5 5 VAL N N 119.230 0.0015 1 21 6 6 GLU H H 8.543 0.0015 1 22 6 6 GLU C C 176.103 0.0015 1 23 6 6 GLU CA C 56.322 0.0015 1 24 6 6 GLU CB C 30.178 0.0015 1 25 6 6 GLU N N 124.694 0.0015 1 26 7 7 LEU H H 8.299 0.0015 1 27 7 7 LEU C C 177.055 0.0015 1 28 7 7 LEU CA C 54.968 0.0015 1 29 7 7 LEU CB C 42.252 0.0015 1 30 7 7 LEU N N 124.049 0.0015 1 31 8 8 ARG H H 8.357 0.0015 1 32 8 8 ARG C C 175.903 0.0015 1 33 8 8 ARG CA C 55.894 0.0015 1 34 8 8 ARG CB C 31.112 0.0015 1 35 8 8 ARG N N 122.015 0.0015 1 36 9 9 ASN H H 8.530 0.0015 1 37 9 9 ASN C C 174.828 0.0015 1 38 9 9 ASN CA C 53.116 0.0015 1 39 9 9 ASN CB C 38.829 0.0015 1 40 9 9 ASN N N 120.379 0.0015 1 41 10 10 ASP H H 8.406 0.0015 1 42 10 10 ASP C C 176.564 0.0015 1 43 10 10 ASP CA C 54.470 0.0015 1 44 10 10 ASP CB C 40.977 0.0015 1 45 10 10 ASP N N 120.993 0.0015 1 46 11 11 SER H H 8.257 0.0015 1 47 11 11 SER C C 174.854 0.0015 1 48 11 11 SER CA C 58.993 0.0015 1 49 11 11 SER CB C 63.524 0.0015 1 50 11 11 SER N N 115.601 0.0015 1 51 12 12 GLU H H 8.364 0.0015 1 52 12 12 GLU C C 177.009 0.0015 1 53 12 12 GLU CA C 57.105 0.0015 1 54 12 12 GLU CB C 29.971 0.0015 1 55 12 12 GLU N N 122.107 0.0015 1 56 13 13 GLY H H 8.305 0.0015 1 57 13 13 GLY C C 173.875 0.0015 1 58 13 13 GLY CA C 45.387 0.0015 1 59 13 13 GLY N N 108.975 0.0015 1 60 14 14 PHE H H 8.011 0.0015 1 61 14 14 PHE C C 175.780 0.0015 1 62 14 14 PHE CA C 57.925 0.0015 1 63 14 14 PHE CB C 39.395 0.0015 1 64 14 14 PHE N N 120.101 0.0015 1 65 15 15 ILE H H 7.989 0.0015 1 66 15 15 ILE CA C 61.166 0.0015 1 67 15 15 ILE CB C 38.274 0.0015 1 68 15 15 ILE N N 122.198 0.0015 1 69 16 16 HIS H H 8.266 0.0015 1 70 16 16 HIS C C 174.950 0.0015 1 71 16 16 HIS CA C 56.001 0.0015 1 72 16 16 HIS CB C 30.173 0.0015 1 73 16 16 HIS N N 122.914 0.0015 1 74 17 17 GLU H H 8.296 0.0015 1 75 17 17 GLU C C 176.087 0.0015 1 76 17 17 GLU CA C 56.714 0.0015 1 77 17 17 GLU CB C 30.354 0.0015 1 78 17 17 GLU N N 122.086 0.0015 1 79 18 18 PHE H H 8.381 0.0015 1 80 18 18 PHE C C 176.379 0.0015 1 81 18 18 PHE CA C 57.960 0.0015 1 82 18 18 PHE CB C 39.299 0.0015 1 83 18 18 PHE N N 120.618 0.0015 1 84 19 19 GLY H H 8.330 0.0015 1 85 19 19 GLY C C 173.783 0.0015 1 86 19 19 GLY CA C 45.387 0.0015 1 87 19 19 GLY N N 109.928 0.0015 1 88 20 20 HIS H H 8.120 0.0015 1 89 20 20 HIS C C 174.490 0.0015 1 90 20 20 HIS CA C 55.574 0.0015 1 91 20 20 HIS CB C 29.947 0.0015 1 92 20 20 HIS N N 118.374 0.0015 1 93 21 21 ALA H H 8.391 0.0015 1 94 21 21 ALA C C 177.839 0.0015 1 95 21 21 ALA CA C 52.475 0.0015 1 96 21 21 ALA CB C 19.234 0.0015 1 97 21 21 ALA N N 125.187 0.0015 1 98 22 22 VAL H H 8.141 0.0015 1 99 22 22 VAL C C 175.964 0.0015 1 100 22 22 VAL CA C 62.840 0.0015 1 101 22 22 VAL CB C 32.521 0.0015 1 102 22 22 VAL N N 118.709 0.0015 1 103 23 23 ASP H H 8.215 0.0015 1 104 23 23 ASP C C 176.170 0.0015 1 105 23 23 ASP CA C 54.602 0.0015 1 106 23 23 ASP CB C 40.977 0.0015 1 107 23 23 ASP N N 121.772 0.0015 1 108 24 24 ASP H H 8.065 0.0015 1 109 24 24 ASP C C 176.385 0.0015 1 110 24 24 ASP CA C 54.631 0.0015 1 111 24 24 ASP CB C 41.054 0.0015 1 112 24 24 ASP N N 119.928 0.0015 1 113 25 25 TYR H H 8.135 0.0015 1 114 25 25 TYR C C 176.094 0.0015 1 115 25 25 TYR CA C 58.517 0.0015 1 116 25 25 TYR CB C 38.164 0.0015 1 117 25 25 TYR N N 120.541 0.0015 1 118 26 26 ALA H H 8.023 0.0015 1 119 26 26 ALA C C 178.591 0.0015 1 120 26 26 ALA CA C 53.900 0.0015 1 121 26 26 ALA CB C 18.568 0.0015 1 122 26 26 ALA N N 124.148 0.0015 1 123 27 27 GLY H H 7.967 0.0015 1 124 27 27 GLY C C 174.505 0.0015 1 125 27 27 GLY CA C 45.850 0.0015 1 126 27 27 GLY N N 105.909 0.0015 1 127 28 28 TYR H H 7.668 0.0015 1 128 28 28 TYR C C 175.749 0.0015 1 129 28 28 TYR CA C 58.708 0.0015 1 130 28 28 TYR CB C 38.494 0.0015 1 131 28 28 TYR N N 119.851 0.0015 1 132 29 29 LEU H H 7.816 0.0015 1 133 29 29 LEU CA C 55.289 0.0015 1 134 29 29 LEU CB C 42.014 0.0015 1 135 29 29 LEU N N 120.875 0.0015 1 136 30 30 LEU H H 7.865 0.0015 1 137 30 30 LEU CA C 55.583 0.0015 1 138 30 30 LEU CB C 42.464 0.0015 1 139 30 30 LEU N N 121.666 0.0015 1 140 32 32 LYS C C 177.288 0.0015 1 141 32 32 LYS CA C 58.313 0.0015 1 142 32 32 LYS CB C 32.253 0.0015 1 143 33 33 ASN H H 8.325 0.0015 1 144 33 33 ASN CA C 55.090 0.0015 1 145 33 33 ASN CB C 38.053 0.0015 1 146 33 33 ASN N N 116.829 0.0015 1 147 34 34 GLN C C 177.379 0.0015 1 148 34 34 GLN CA C 57.497 0.0015 1 149 34 34 GLN CB C 29.099 0.0015 1 150 35 35 SER H H 8.328 0.0015 1 151 35 35 SER CA C 60.988 0.0015 1 152 35 35 SER CB C 62.558 0.0015 1 153 35 35 SER N N 114.919 0.0015 1 154 40 40 ASN C C 175.304 0.0015 1 155 40 40 ASN CA C 52.726 0.0015 1 156 40 40 ASN CB C 38.762 0.0015 1 157 41 41 SER H H 7.642 0.0015 1 158 41 41 SER CA C 58.037 0.0015 1 159 41 41 SER CB C 64.415 0.0015 1 160 41 41 SER N N 115.872 0.0015 1 161 46 46 ASP C C 179.798 0.0015 1 162 46 46 ASP CA C 57.462 0.0015 1 163 46 46 ASP CB C 39.836 0.0015 1 164 47 47 ILE H H 7.486 0.0015 1 165 47 47 ILE C C 177.531 0.0015 1 166 47 47 ILE CA C 65.938 0.0015 1 167 47 47 ILE CB C 37.769 0.0015 1 168 47 47 ILE N N 123.011 0.0015 1 169 48 48 PHE H H 8.820 0.0015 1 170 48 48 PHE C C 178.282 0.0015 1 171 48 48 PHE CA C 60.614 0.0015 1 172 48 48 PHE CB C 38.494 0.0015 1 173 48 48 PHE N N 122.251 0.0015 1 174 49 49 LYS H H 8.321 0.0015 1 175 49 49 LYS C C 177.301 0.0015 1 176 49 49 LYS CA C 59.565 0.0015 1 177 49 49 LYS CB C 32.106 0.0015 1 178 49 49 LYS N N 120.058 0.0015 1 179 50 50 GLU H H 7.160 0.0015 1 180 50 50 GLU C C 178.359 0.0015 1 181 50 50 GLU CA C 58.482 0.0015 1 182 50 50 GLU CB C 31.328 0.0015 1 183 50 50 GLU N N 117.170 0.0015 1 184 51 51 GLU H H 8.744 0.0015 1 185 51 51 GLU C C 177.163 0.0015 1 186 51 51 GLU CA C 56.717 0.0015 1 187 51 51 GLU CB C 31.476 0.0015 1 188 51 51 GLU N N 116.027 0.0015 1 189 52 52 GLY H H 7.735 0.0015 1 190 52 52 GLY C C 174.413 0.0015 1 191 52 52 GLY CA C 46.705 0.0015 1 192 52 52 GLY N N 106.370 0.0015 1 193 53 53 SER H H 8.022 0.0015 1 194 53 53 SER C C 176.087 0.0015 1 195 53 53 SER CA C 57.946 0.0015 1 196 53 53 SER CB C 63.256 0.0015 1 197 53 53 SER N N 114.182 0.0015 1 198 54 54 ASN H H 8.212 0.0015 1 199 54 54 ASN CA C 54.470 0.0015 1 200 54 54 ASN CB C 38.225 0.0015 1 201 54 54 ASN N N 118.332 0.0015 1 202 55 55 LEU H H 8.522 0.0015 1 203 55 55 LEU C C 176.057 0.0015 1 204 55 55 LEU CA C 54.327 0.0015 1 205 55 55 LEU CB C 42.252 0.0015 1 206 55 55 LEU N N 118.216 0.0015 1 207 56 56 THR H H 7.546 0.0015 1 208 56 56 THR C C 175.027 0.0015 1 209 56 56 THR CA C 60.489 0.0015 1 210 56 56 THR CB C 70.771 0.0015 1 211 56 56 THR N N 111.305 0.0015 1 212 57 57 SER C C 175.084 0.0015 1 213 57 57 SER CA C 59.634 0.0015 1 214 57 57 SER CB C 62.987 0.0015 1 215 58 58 TYR H H 7.882 0.0015 1 216 58 58 TYR C C 176.195 0.0015 1 217 58 58 TYR CA C 57.925 0.0015 1 218 58 58 TYR CB C 38.427 0.0015 1 219 58 58 TYR N N 120.229 0.0015 1 220 59 59 GLY H H 8.049 0.0015 1 221 59 59 GLY C C 172.800 0.0015 1 222 59 59 GLY CA C 45.245 0.0015 1 223 59 59 GLY N N 109.115 0.0015 1 224 60 60 ARG H H 7.886 0.0015 1 225 60 60 ARG C C 176.948 0.0015 1 226 60 60 ARG CA C 56.144 0.0015 1 227 60 60 ARG CB C 30.844 0.0015 1 228 60 60 ARG N N 118.466 0.0015 1 229 61 61 THR H H 8.463 0.0015 1 230 61 61 THR C C 174.182 0.0015 1 231 61 61 THR CA C 61.949 0.0015 1 232 61 61 THR CB C 69.863 0.0015 1 233 61 61 THR N N 115.187 0.0015 1 234 62 62 ASN H H 8.452 0.0015 1 235 62 62 ASN C C 173.584 0.0015 1 236 62 62 ASN CA C 52.475 0.0015 1 237 62 62 ASN CB C 40.104 0.0015 1 238 62 62 ASN N N 117.325 0.0015 1 239 63 63 GLU H H 10.030 0.0015 1 240 63 63 GLU C C 177.531 0.0015 1 241 63 63 GLU CA C 61.433 0.0015 1 242 63 63 GLU CB C 28.814 0.0015 1 243 63 63 GLU N N 120.688 0.0015 1 244 64 64 ALA H H 8.122 0.0015 1 245 64 64 ALA C C 181.096 0.0015 1 246 64 64 ALA CA C 55.574 0.0015 1 247 64 64 ALA CB C 18.228 0.0015 1 248 64 64 ALA N N 121.540 0.0015 1 249 65 65 GLU H H 8.463 0.0015 1 250 65 65 GLU C C 179.436 0.0015 1 251 65 65 GLU CA C 58.922 0.0015 1 252 65 65 GLU CB C 29.367 0.0015 1 253 65 65 GLU N N 119.884 0.0015 1 254 66 66 PHE H H 8.790 0.0015 1 255 66 66 PHE C C 176.517 0.0015 1 256 66 66 PHE CA C 61.878 0.0015 1 257 66 66 PHE CB C 40.438 0.0015 1 258 66 66 PHE N N 122.392 0.0015 1 259 67 67 PHE H H 8.665 0.0015 1 260 67 67 PHE C C 176.354 0.0015 1 261 67 67 PHE CA C 62.056 0.0015 1 262 67 67 PHE CB C 39.272 0.0015 1 263 67 67 PHE N N 118.354 0.0015 1 264 68 68 ALA H H 8.012 0.0015 1 265 68 68 ALA C C 180.312 0.0015 1 266 68 68 ALA CA C 55.289 0.0015 1 267 68 68 ALA CB C 17.959 0.0015 1 268 68 68 ALA N N 118.563 0.0015 1 269 69 69 GLU H H 8.201 0.0015 1 270 69 69 GLU C C 177.854 0.0015 1 271 69 69 GLU CA C 58.245 0.0015 1 272 69 69 GLU CB C 29.099 0.0015 1 273 69 69 GLU N N 120.308 0.0015 1 274 70 70 ALA H H 8.472 0.0015 1 275 70 70 ALA C C 178.899 0.0015 1 276 70 70 ALA CA C 55.431 0.0015 1 277 70 70 ALA CB C 17.825 0.0015 1 278 70 70 ALA N N 121.580 0.0015 1 279 71 71 PHE H H 8.662 0.0015 1 280 71 71 PHE C C 178.346 0.0015 1 281 71 71 PHE CA C 62.555 0.0015 1 282 71 71 PHE CB C 39.366 0.0015 1 283 71 71 PHE N N 117.264 0.0015 1 284 72 72 ARG H H 8.341 0.0015 1 285 72 72 ARG C C 180.005 0.0015 1 286 72 72 ARG CA C 59.634 0.0015 1 287 72 72 ARG CB C 30.131 0.0015 1 288 72 72 ARG N N 120.993 0.0015 1 289 73 73 LEU H H 8.400 0.0015 1 290 73 73 LEU C C 178.848 0.0015 1 291 73 73 LEU CA C 58.028 0.0015 1 292 73 73 LEU CB C 42.144 0.0015 1 293 73 73 LEU N N 120.319 0.0015 1 294 74 74 MET H H 8.122 0.0015 1 295 74 74 MET C C 176.461 0.0015 1 296 74 74 MET CA C 58.889 0.0015 1 297 74 74 MET CB C 33.796 0.0015 1 298 74 74 MET N N 113.853 0.0015 1 299 75 75 HIS H H 7.184 0.0015 1 300 75 75 HIS C C 173.401 0.0015 1 301 75 75 HIS CA C 56.429 0.0015 1 302 75 75 HIS CB C 28.294 0.0015 1 303 75 75 HIS N N 114.291 0.0015 1 304 76 76 SER H H 7.174 0.0015 1 305 76 76 SER C C 175.864 0.0015 1 306 76 76 SER CA C 57.699 0.0015 1 307 76 76 SER CB C 63.994 0.0015 1 308 76 76 SER N N 115.777 0.0015 1 309 77 77 THR H H 8.463 0.0015 1 310 77 77 THR C C 174.395 0.0015 1 311 77 77 THR CA C 63.410 0.0015 1 312 77 77 THR CB C 68.850 0.0015 1 313 77 77 THR N N 115.840 0.0015 1 314 78 78 ASP H H 8.679 0.0015 1 315 78 78 ASP C C 176.966 0.0015 1 316 78 78 ASP CA C 53.046 0.0015 1 317 78 78 ASP CB C 41.312 0.0015 1 318 78 78 ASP N N 123.182 0.0015 1 319 79 79 HIS H H 9.013 0.0015 1 320 79 79 HIS C C 176.614 0.0015 1 321 79 79 HIS CA C 59.353 0.0015 1 322 79 79 HIS CB C 29.703 0.0015 1 323 79 79 HIS N N 126.994 0.0015 1 324 80 80 ALA H H 8.341 0.0015 1 325 80 80 ALA C C 181.465 0.0015 1 326 80 80 ALA CA C 54.933 0.0015 1 327 80 80 ALA CB C 18.094 0.0015 1 328 80 80 ALA N N 120.165 0.0015 1 329 81 81 GLU H H 7.666 0.0015 1 330 81 81 GLU C C 177.425 0.0015 1 331 81 81 GLU CA C 59.741 0.0015 1 332 81 81 GLU CB C 28.965 0.0015 1 333 81 81 GLU N N 118.820 0.0015 1 334 82 82 ARG H H 7.052 0.0015 1 335 82 82 ARG C C 179.430 0.0015 1 336 82 82 ARG CA C 59.705 0.0015 1 337 82 82 ARG CB C 29.582 0.0015 1 338 82 82 ARG N N 118.403 0.0015 1 339 83 83 LEU H H 7.734 0.0015 1 340 83 83 LEU C C 178.451 0.0015 1 341 83 83 LEU CA C 56.892 0.0015 1 342 83 83 LEU CB C 41.648 0.0015 1 343 83 83 LEU N N 118.034 0.0015 1 344 84 84 LYS H H 7.536 0.0015 1 345 84 84 LYS C C 178.879 0.0015 1 346 84 84 LYS CA C 59.777 0.0015 1 347 84 84 LYS CB C 32.119 0.0015 1 348 84 84 LYS N N 119.218 0.0015 1 349 85 85 VAL H H 7.304 0.0015 1 350 85 85 VAL C C 175.864 0.0015 1 351 85 85 VAL CA C 65.689 0.0015 1 352 85 85 VAL CB C 31.356 0.0015 1 353 85 85 VAL N N 116.850 0.0015 1 354 86 86 GLN H H 7.093 0.0015 1 355 86 86 GLN C C 176.951 0.0015 1 356 86 86 GLN CA C 59.456 0.0015 1 357 86 86 GLN CB C 28.185 0.0015 1 358 86 86 GLN N N 118.628 0.0015 1 359 87 87 LYS H H 7.995 0.0015 1 360 87 87 LYS C C 178.129 0.0015 1 361 87 87 LYS CA C 57.746 0.0015 1 362 87 87 LYS CB C 32.924 0.0015 1 363 87 87 LYS N N 113.309 0.0015 1 364 88 88 ASN H H 8.044 0.0015 1 365 88 88 ASN C C 174.564 0.0015 1 366 88 88 ASN CA C 54.461 0.0015 1 367 88 88 ASN CB C 39.232 0.0015 1 368 88 88 ASN N N 114.516 0.0015 1 369 89 89 ALA H H 8.468 0.0015 1 370 89 89 ALA C C 171.763 0.0015 1 371 89 89 ALA CA C 50.338 0.0015 1 372 89 89 ALA CB C 18.362 0.0015 1 373 89 89 ALA N N 123.978 0.0015 1 374 90 90 PRO CA C 65.486 0.0015 1 375 90 90 PRO CB C 31.752 0.0015 1 376 91 91 LYS H H 11.170 0.0015 1 377 91 91 LYS C C 180.800 0.0015 1 378 91 91 LYS CA C 60.525 0.0015 1 379 91 91 LYS CB C 32.561 0.0015 1 380 91 91 LYS N N 124.683 0.0015 1 381 92 92 THR H H 9.947 0.0015 1 382 92 92 THR CA C 67.290 0.0015 1 383 92 92 THR CB C 69.071 0.0015 1 384 92 92 THR N N 125.754 0.0015 1 385 93 93 PHE H H 8.954 0.0015 1 386 93 93 PHE C C 176.840 0.0015 1 387 93 93 PHE CA C 61.201 0.0015 1 388 93 93 PHE CB C 39.970 0.0015 1 389 93 93 PHE N N 122.064 0.0015 1 390 94 94 GLN H H 8.070 0.0015 1 391 94 94 GLN C C 177.255 0.0015 1 392 94 94 GLN CA C 58.601 0.0015 1 393 94 94 GLN CB C 28.763 0.0015 1 394 94 94 GLN N N 117.107 0.0015 1 395 95 95 PHE H H 8.557 0.0015 1 396 95 95 PHE C C 178.161 0.0015 1 397 95 95 PHE CA C 61.736 0.0015 1 398 95 95 PHE CB C 40.028 0.0015 1 399 95 95 PHE N N 120.073 0.0015 1 400 96 96 ILE H H 8.929 0.0015 1 401 96 96 ILE C C 177.624 0.0015 1 402 96 96 ILE CA C 66.793 0.0015 1 403 96 96 ILE CB C 36.682 0.0015 1 404 96 96 ILE N N 119.055 0.0015 1 405 97 97 ASN H H 7.877 0.0015 1 406 97 97 ASN C C 177.885 0.0015 1 407 97 97 ASN CA C 56.286 0.0015 1 408 97 97 ASN CB C 37.638 0.0015 1 409 97 97 ASN N N 117.544 0.0015 1 410 98 98 ASP H H 8.437 0.0015 1 411 98 98 ASP C C 178.177 0.0015 1 412 98 98 ASP CA C 56.785 0.0015 1 413 98 98 ASP CB C 40.373 0.0015 1 414 98 98 ASP N N 119.189 0.0015 1 415 99 99 GLN H H 7.963 0.0015 1 416 99 99 GLN C C 177.916 0.0015 1 417 99 99 GLN CA C 56.911 0.0015 1 418 99 99 GLN CB C 28.800 0.0015 1 419 99 99 GLN N N 117.840 0.0015 1 420 100 100 ILE H H 7.899 0.0015 1 421 100 100 ILE CA C 63.725 0.0015 1 422 100 100 ILE CB C 39.745 0.0015 1 423 100 100 ILE N N 119.221 0.0015 1 424 102 102 PHE C C 176.630 0.0015 1 425 102 102 PHE CA C 58.798 0.0015 1 426 102 102 PHE CB C 39.045 0.0015 1 427 103 103 ILE H H 7.869 0.0015 1 428 103 103 ILE C C 176.825 0.0015 1 429 103 103 ILE CA C 62.626 0.0015 1 430 103 103 ILE CB C 32.620 0.0015 1 431 103 103 ILE N N 119.540 0.0015 1 432 105 105 ASN H H 8.037 0.0015 1 433 105 105 ASN CA C 53.330 0.0015 1 434 105 105 ASN CB C 38.963 0.0015 1 435 105 105 ASN N N 120.826 0.0015 1 436 106 106 SER H H 7.723 0.0015 1 437 106 106 SER C C 178.591 0.0015 1 438 106 106 SER CA C 60.168 0.0015 1 439 106 106 SER CB C 64.799 0.0015 1 440 106 106 SER N N 121.544 0.0015 1 stop_ save_