data_20092 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; To be advised ; _BMRB_accession_number 20092 _BMRB_flat_file_name bmr20092.str _Entry_type new _Submission_date 2009-08-13 _Accession_date 2009-08-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fairlie David P. . 2 Harrison Rosemary . . 3 Hoang Huy N. . 4 Ruiz-Gomez Gloria . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 81 "coupling constants" 14 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-03-17 update BMRB 'PDBj annotated the coordinate file, BMRB add residue NH2' 2010-10-13 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20543141 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Harrisona Rosemary S. . 2 Shepherda Nicholas E. . 3 Hoanga Huy N. . 4 Ruiz-Gomeza Gloria . . 5 Hilla Timothy A. . 6 Drivera Russell W. . 7 Desaib Vishal S. . 8 Youngb Paul R. . 9 Abbenantea Giovanni . . 10 Fairliea David P. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume 107 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11686 _Page_last 11691 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name csp _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label csp $csp stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_csp _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common csp _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence EXRLKKFFDKFILDRKKX loop_ _Residue_seq_code _Residue_label 1 GLU 2 NLE 3 ARG 4 LEU 5 LYS 6 LYS 7 PHE 8 PHE 9 ASP 10 LYS 11 PHE 12 ILE 13 LEU 14 ASP 15 ARG 16 LYS 17 LYS 18 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_NLE _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common NORLEUCINE _BMRB_code . _PDB_code NLE _Standard_residue_derivative . _Molecular_mass 131.173 _Mol_paramagnetic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 15:26:17 2009 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD CE ? ? SING CD HD2 ? ? SING CD HD3 ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Mar 17 11:42:19 2011 ; save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $csp 'Streptococcus pneumoniae CSP-1' 1313 Bacteria . Streptococcus pneumoniae 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 $csp 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $csp . mM 2 5 'natural abundance' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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 temperature 288 . K pH 4.1 . pH 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 H 1 'methyl protons' ppm 0 internal direct . . . 1.00000 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-1H NOESY' '2D 1H-1H TOCSY' '2D DQF-COSY' 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 csp _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 GLU HA H 4.07 0.0035 1 2 1 1 GLU HB2 H 2.51 0.0035 2 3 1 1 GLU HB3 H 2.13 0.0035 2 4 2 2 NLE H H 8.70 0.0035 1 5 2 2 NLE HA H 4.30 0.0035 1 6 2 2 NLE HB2 H 1.76 0.0035 1 7 2 2 NLE HB3 H 1.76 0.0035 1 8 3 3 ARG H H 8.65 0.0035 1 9 3 3 ARG HA H 4.23 0.0035 1 10 3 3 ARG HB2 H 1.79 0.0035 1 11 3 3 ARG HB3 H 1.79 0.0035 1 12 3 3 ARG HG2 H 1.63 0.0035 2 13 3 3 ARG HG3 H 1.48 0.0035 2 14 4 4 LEU H H 8.40 0.0035 1 15 4 4 LEU HA H 4.22 0.0035 1 16 4 4 LEU HB2 H 1.74 0.0035 1 17 4 4 LEU HB3 H 1.74 0.0035 1 18 4 4 LEU HD1 H 0.94 0.0035 2 19 4 4 LEU HD2 H 0.85 0.0035 2 20 4 4 LEU HG H 1.64 0.0035 1 21 5 5 LYS H H 7.98 0.0035 1 22 5 5 LYS HA H 4.21 0.0035 1 23 5 5 LYS HB2 H 1.83 0.0035 2 24 5 5 LYS HB3 H 1.68 0.0035 2 25 6 6 LYS H H 8.49 0.0035 1 26 6 6 LYS HA H 4.03 0.0035 1 27 6 6 LYS HB2 H 1.82 0.0035 2 28 6 6 LYS HB3 H 1.67 0.0035 2 29 7 7 PHE H H 7.52 0.0035 1 30 7 7 PHE HA H 4.34 0.0035 1 31 7 7 PHE HB2 H 3.19 0.0035 1 32 7 7 PHE HB3 H 3.19 0.0035 1 33 8 8 PHE H H 8.63 0.0035 1 34 8 8 PHE HA H 4.22 0.0035 1 35 8 8 PHE HB2 H 3.14 0.0035 1 36 8 8 PHE HB3 H 3.11 0.0035 1 37 9 9 ASP H H 9.07 0.0035 1 38 9 9 ASP HA H 4.55 0.0035 1 39 9 9 ASP HB2 H 2.73 0.0035 1 40 9 9 ASP HB3 H 2.73 0.0035 1 41 10 10 LYS H H 7.33 0.0035 1 42 10 10 LYS HA H 4.26 0.0035 1 43 10 10 LYS HB2 H 1.90 0.0035 1 44 10 10 LYS HB3 H 1.90 0.0035 1 45 10 10 LYS HG2 H 1.56 0.0035 2 46 10 10 LYS HG3 H 1.49 0.0035 2 47 11 11 PHE H H 7.83 0.0035 1 48 11 11 PHE HA H 4.12 0.0035 1 49 11 11 PHE HB2 H 3.18 0.0035 2 50 11 11 PHE HB3 H 2.99 0.0035 2 51 12 12 ILE H H 7.76 0.0035 1 52 12 12 ILE HA H 3.47 0.0035 1 53 12 12 ILE HB H 1.87 0.0035 1 54 12 12 ILE HD1 H 0.83 0.0035 1 55 13 13 LEU H H 7.70 0.0035 1 56 13 13 LEU HA H 4.03 0.0035 1 57 13 13 LEU HB2 H 1.68 0.0035 1 58 13 13 LEU HB3 H 1.68 0.0035 1 59 13 13 LEU HD1 H 0.89 0.0035 1 60 14 14 ASP H H 8.44 0.0035 1 61 14 14 ASP HA H 4.58 0.0035 1 62 14 14 ASP HB2 H 2.83 0.0035 2 63 14 14 ASP HB3 H 2.26 0.0035 2 64 15 15 ARG H H 7.48 0.0035 1 65 15 15 ARG HA H 4.04 0.0035 1 66 15 15 ARG HB2 H 1.66 0.0035 2 67 15 15 ARG HB3 H 1.51 0.0035 2 68 16 16 LYS H H 7.87 0.0035 1 69 16 16 LYS HA H 4.21 0.0035 1 70 16 16 LYS HB2 H 1.67 0.0035 1 71 16 16 LYS HB3 H 1.67 0.0035 1 72 16 16 LYS HG2 H 1.43 0.0035 2 73 16 16 LYS HG3 H 1.51 0.0035 2 74 17 17 LYS H H 8.09 0.0035 1 75 17 17 LYS HA H 4.19 0.0035 1 76 17 17 LYS HB2 H 1.85 0.0035 2 77 17 17 LYS HB3 H 1.68 0.0035 2 78 17 17 LYS HG2 H 1.51 0.0035 2 79 17 17 LYS HG3 H 1.44 0.0035 2 80 17 18 NH2 HN1 H 7.46 0.0035 9 81 17 18 NH2 HN2 H 7.20 0.0035 9 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_list_1 _Saveframe_category coupling_constants _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' '2D DQF-COSY' stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name csp _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 NLE H 2 NLE HA 5.7 . . . 2 3JHNHA 3 ARG H 3 ARG HA 4.9 . . . 3 3JHNHA 4 LEU H 4 LEU HA 6.3 . . . 4 3JHNHA 7 PHE H 7 PHE HA 5.3 . . . 5 3JHNHA 8 PHE H 8 PHE HA 6.0 . . . 6 3JHNHA 9 ASP H 9 ASP HA 5.5 . . . 7 3JHNHA 10 LYS H 10 LYS HA 7.1 . . . 8 3JHNHA 11 PHE H 11 PHE HA 4.3 . . . 9 3JHNHA 12 ILE H 12 ILE HA 5.5 . . . 10 3JHNHA 13 LEU H 13 LEU HA 5.0 . . . 11 3JHNHA 14 ASP H 14 ASP HA 6.7 . . . 12 3JHNHA 15 ARG H 15 ARG HA 5.6 . . . 13 3JHNHA 16 LYS H 16 LYS HA 4.1 . . . 14 3JHNHA 17 LYS H 17 LYS HA 5.6 . . . stop_ save_