data_15640 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris ; _BMRB_accession_number 15640 _BMRB_flat_file_name bmr15640.str _Entry_type original _Submission_date 2008-01-25 _Accession_date 2008-01-25 _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 Kumaki Yasuhiro . . 2 Kawano Keiichi . . 3 Hikichi Kunio . . 4 Matsumoto Takeshi . . 5 Matsushima Norio . . 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" 86 "coupling constants" 11 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-11-21 update BMRB 'Update residue sequence: ASP_ACE and GLY_NH2' 2009-02-05 update BMRB 'Update coupling constant table' 2008-05-28 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A circular loop of the sixteen-residue repeating unit in ice nucleation protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18361918 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumaki Yasuhiro . . 2 Kawano Keiichi . . 3 Hikichi Kunio . . 4 Matsumoto Takeshi . . 5 Matsushima Norio . . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume 371 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5 _Page_last 9 _Year 2008 _Details . loop_ _Keyword 'aromatic ring interaction' 'circular loop' 'ice nucleation protein' 'tandem repeat' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name monomerp _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'model peptide for INP' $model_peptide_for_INP 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_model_peptide_for_INP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common model_peptide_for_INP _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 19 _Mol_residue_sequence XDSSLTAGYGSTQTARKGX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 ACE 2 1 ASP 3 2 SER 4 3 SER 5 4 LEU 6 5 THR 7 6 ALA 8 7 GLY 9 8 TYR 10 9 GLY 11 10 SER 12 11 THR 13 12 GLN 14 13 THR 15 14 ALA 16 15 ARG 17 16 LYS 18 17 GLY 19 18 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 DBJ GAE51334 "ice nucleation protein [Xanthomonas arboricola pv. pruni str. MAFF 311562]" 89.47 1432 100.00 100.00 4.11e+00 DBJ GAE56226 "ice nucleation protein [Xanthomonas arboricola pv. pruni MAFF 301420]" 89.47 1432 100.00 100.00 4.11e+00 DBJ GAE61386 "ice nucleation protein, partial [Xanthomonas arboricola pv. pruni MAFF 301427]" 89.47 971 100.00 100.00 4.04e+00 EMBL CAA37140 "unnamed protein product [Xanthomonas campestris]" 89.47 1567 100.00 100.00 4.18e+00 EMBL CAP49871 "ice nucleation protein [Xanthomonas campestris pv. campestris]" 89.47 1360 100.00 100.00 4.09e+00 EMBL CCP40923 "Ice nucleation protein inaA [Xanthomonas translucens pv. translucens DSM 18974]" 89.47 1567 100.00 100.00 4.11e+00 EMBL CEM56732 "ice nucleation protein [Xanthomonas campestris pv. campestris]" 89.47 1333 100.00 100.00 4.08e+00 EMBL CTP83946 "Ice nucleation protein [Xanthomonas translucens pv. phlei]" 89.47 1468 100.00 100.00 4.04e+00 GB AAM39823 "ice nucleation protein [Xanthomonas campestris pv. campestris str. ATCC 33913]" 89.47 1333 100.00 100.00 4.08e+00 GB AAY47600 "ice nucleation protein [Xanthomonas campestris pv. campestris str. 8004]" 89.47 1333 100.00 100.00 4.08e+00 GB AEL08859 "ice-nucleation proteins octamer repeat protein [Xanthomonas campestris pv. raphani 756C]" 89.47 1429 100.00 100.00 4.27e+00 GB AKC80693 "Ice nucleation protein [Xanthomonas campestris]" 89.47 1448 100.00 100.00 4.08e+00 GB AKK68120 "Ice nucleation protein [Xanthomonas translucens pv. undulosa]" 89.47 1567 100.00 100.00 4.18e+00 PIR S11672 "ice nucleation protein - Xanthomonas campestris" 89.47 1567 100.00 100.00 4.18e+00 REF NP_635899 "ice nucleation protein [Xanthomonas campestris pv. campestris str. ATCC 33913]" 89.47 1333 100.00 100.00 4.08e+00 REF WP_002804985 "ice nucleation protein [Xanthomonas fragariae]" 89.47 1226 100.00 100.00 4.05e+00 REF WP_003478675 "Ice nucleation protein [Xanthomonas translucens]" 89.47 1567 100.00 100.00 4.11e+00 REF WP_006450271 "Ice nucleation protein, partial [Xanthomonas gardneri]" 89.47 1073 100.00 100.00 3.84e+00 REF WP_011035756 "ice nucleation protein [Xanthomonas campestris]" 89.47 1333 100.00 100.00 4.08e+00 SP P18127 "RecName: Full=Ice nucleation protein" 89.47 1567 100.00 100.00 4.18e+00 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYL GROUP' _BMRB_code ACE _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'AMINO GROUP' _BMRB_code NH2 _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 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 HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $model_peptide_for_INP 'Xanthomonas campestris' 339 Bacteria . Xanthomonas campestris 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 $model_peptide_for_INP 'chemical synthesis' . . . . . 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 $model_peptide_for_INP 3 mM 'natural abundance' DSS 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_DELTA _Saveframe_category software _Name Delta _Version 4.3.2 loop_ _Vendor _Address _Electronic_address JEOL . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer JEOL _Model ALPHA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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' 0 . M pH 4.4 . pH pressure 1 . atm temperature 278 . 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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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_ _Software_label $DELTA stop_ loop_ _Experiment_label '2D DQF-COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' 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 'model peptide for INP' _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 2 ASP H H 8.39 0.02 1 2 1 2 ASP HA H 4.62 0.02 1 3 1 2 ASP HB2 H 2.65 0.02 2 4 1 2 ASP HB3 H 2.73 0.02 2 5 2 3 SER H H 8.65 0.02 1 6 2 3 SER HA H 4.44 0.02 1 7 2 3 SER HB2 H 3.88 0.02 2 8 2 3 SER HB3 H 3.95 0.02 2 9 3 4 SER H H 8.58 0.02 1 10 3 4 SER HA H 4.31 0.02 1 11 3 4 SER HB2 H 3.87 0.02 2 12 3 4 SER HB3 H 3.90 0.02 2 13 4 5 LEU H H 8.16 0.02 1 14 4 5 LEU HA H 4.38 0.02 1 15 4 5 LEU HB2 H 1.70 0.02 4 16 4 5 LEU HB3 H 1.70 0.02 4 17 4 5 LEU HD1 H 0.84 0.02 2 18 4 5 LEU HD2 H 0.93 0.02 2 19 4 5 LEU HG H 1.62 0.02 4 20 5 6 THR H H 8.02 0.02 1 21 5 6 THR HA H 4.27 0.02 1 22 5 6 THR HB H 4.27 0.02 1 23 5 6 THR HG2 H 1.20 0.02 1 24 6 7 ALA H H 8.30 0.02 1 25 6 7 ALA HA H 4.29 0.02 1 26 6 7 ALA HB H 1.38 0.02 1 27 7 8 GLY H H 8.64 0.02 1 28 7 8 GLY HA2 H 3.88 0.02 2 29 7 8 GLY HA3 H 3.94 0.02 2 30 8 9 TYR H H 8.20 0.02 1 31 8 9 TYR HA H 4.50 0.02 1 32 8 9 TYR HB2 H 3.01 0.02 2 33 8 9 TYR HB3 H 3.06 0.02 2 34 8 9 TYR HD1 H 7.11 0.02 1 35 8 9 TYR HD2 H 7.11 0.02 1 36 8 9 TYR HE1 H 6.82 0.02 1 37 8 9 TYR HE2 H 6.82 0.02 1 38 9 10 GLY H H 8.54 0.02 1 39 9 10 GLY HA2 H 3.84 0.02 2 40 9 10 GLY HA3 H 3.95 0.02 2 41 10 11 SER H H 8.29 0.02 1 42 10 11 SER HA H 4.51 0.02 1 43 10 11 SER HB2 H 3.88 0.02 2 44 10 11 SER HB3 H 3.93 0.02 2 45 11 12 THR H H 8.34 0.02 1 46 11 12 THR HA H 4.36 0.02 1 47 11 12 THR HB H 4.28 0.02 1 48 11 12 THR HG2 H 1.22 0.02 1 49 12 13 GLN H H 8.49 0.02 1 50 12 13 GLN HA H 4.37 0.02 1 51 12 13 GLN HB2 H 1.99 0.02 2 52 12 13 GLN HB3 H 2.10 0.02 2 53 12 13 GLN HE21 H 7.60 0.02 1 54 12 13 GLN HE22 H 7.60 0.02 1 55 12 13 GLN HG2 H 2.15 0.02 1 56 12 13 GLN HG3 H 2.15 0.02 1 57 13 14 THR H H 8.24 0.02 1 58 13 14 THR HA H 4.25 0.02 1 59 13 14 THR HB H 4.28 0.02 1 60 13 14 THR HG2 H 1.21 0.02 1 61 14 15 ALA H H 8.40 0.02 1 62 14 15 ALA HA H 4.29 0.02 1 63 14 15 ALA HB H 1.37 0.02 1 64 15 16 ARG H H 8.42 0.02 1 65 15 16 ARG HA H 4.29 0.02 1 66 15 16 ARG HB2 H 1.76 0.02 2 67 15 16 ARG HB3 H 1.82 0.02 2 68 15 16 ARG HD2 H 3.19 0.02 1 69 15 16 ARG HD3 H 3.19 0.02 1 70 15 16 ARG HE H 7.21 0.02 1 71 15 16 ARG HG2 H 1.63 0.02 1 72 15 16 ARG HG3 H 1.63 0.02 1 73 16 17 LYS H H 8.58 0.02 1 74 16 17 LYS HA H 4.31 0.02 1 75 16 17 LYS HB2 H 1.78 0.02 2 76 16 17 LYS HB3 H 1.84 0.02 2 77 16 17 LYS HD2 H 1.68 0.02 1 78 16 17 LYS HD3 H 1.68 0.02 1 79 16 17 LYS HE2 H 2.99 0.02 1 80 16 17 LYS HE3 H 2.99 0.02 1 81 16 17 LYS HG2 H 1.45 0.02 1 82 16 17 LYS HG3 H 1.45 0.02 1 83 16 17 LYS HZ H 7.60 0.02 1 84 17 18 GLY H H 8.42 0.02 1 85 17 18 GLY HA2 H 3.87 0.02 2 86 17 18 GLY HA3 H 3.91 0.02 2 stop_ loop_ _Atom_shift_assign_ID_ambiguity 15 '16,19' stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_list_1 _Saveframe_category coupling_constants _Details . loop_ _Software_label $DELTA stop_ loop_ _Experiment_label '2D DQF-COSY' stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'model peptide for INP' _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 ASP H 2 ASP HA 5.1 . . 1.5 2 3JHNHA 3 SER H 3 SER HA 5.9 . . 1.5 3 3JHNHA 4 SER H 4 SER HA 6.5 . . 1.5 4 3JHNHA 5 LEU H 5 LEU HA 7.8 . . 1.5 5 3JHNHA 6 THR H 6 THR HA 6.9 . . 1.5 6 3JHNHA 9 TYR H 9 TYR HA 6.9 . . 1.5 7 3JHNHA 11 SER H 11 SER HA 6.9 . . 1.5 8 3JHNHA 12 THR H 12 THR HA 7.6 . . 1.5 9 3JHNHA 13 GLN H 13 GLN HA 6.9 . . 1.5 10 3JHNHA 14 THR H 14 THR HA 5.9 . . 1.5 11 3JHNHA 17 LYS H 17 LYS HA 5.1 . . 1.5 stop_ save_