data_4645 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A Peptide Derived from the C-Terminal Part of a Plant Cysteine Protease Folds into a Stack of Two Beta-Hairpins, a Scaffold Present in the Emerging Family of Granulin-Like Growth Factors ; _BMRB_accession_number 4645 _BMRB_flat_file_name bmr4645.str _Entry_type original _Submission_date 2000-09-24 _Accession_date 2001-03-16 _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 Tolkatchev D. . . 2 Xu P. . . 3 Ni F. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 180 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-15 original BMRB . stop_ _Original_release_date 2001-03-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Peptide Derived from the C-Terminal Part of a Plant Cysteine Protease Folds into a Stack of Two Beta-Hairpins, a Scaffold Present in the Emerging Family of Granulin-Like Growth Factors ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11298924 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tolkatchev D. . . 2 Xu P. . . 3 Ni F. . . stop_ _Journal_abbreviation 'J. Pept. Res.' _Journal_volume 57 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 227 _Page_last 233 _Year 2001 _Details . loop_ _Keyword 'beta-hairpin stack fold' 'granulin/epithelin-like protein repeats' stop_ save_ ################################## # Molecular system description # ################################## save_system_ROB _Saveframe_category molecular_system _Mol_system_name 'ORYZAIN BETA CHAIN' _Abbreviation_common ROB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ORYZAIN BETA CHAIN' $ROB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ROB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ORYZAIN BETA CHAIN' _Abbreviation_common ROB _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; DHVCDDNFSCPAGSTCSSAF GFRNLSLVWGCSPVE ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 HIS 3 VAL 4 CYS 5 ASP 6 ASP 7 ASN 8 PHE 9 SER 10 CYS 11 PRO 12 ALA 13 GLY 14 SER 15 THR 16 CYS 17 SER 18 SER 19 ALA 20 PHE 21 GLY 22 PHE 23 ARG 24 ASN 25 LEU 26 SER 27 LEU 28 VAL 29 TRP 30 GLY 31 CYS 32 SER 33 PRO 34 VAL 35 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1FWO ; The Solution Structure Of A 35-Residue Fragment From The GranulinEPITHELIN-Like Subdomain Of Rice Oryzain Beta (Rob 382-416 (C398s,C399s,C407s,C413s)) ; 100.00 35 100.00 100.00 5.54e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ROB Rice 4530 Eukaryota Viridiplantae Oryza sativa 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 $ROB '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 $ROB 0.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ROB 0.5 mM . 'sodium acetate' 20 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ROB 0.5 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task refinement stop_ _Details Brunger save_ save_UXNMR _Saveframe_category software _Name UXNMR _Version 2.1 loop_ _Task processing stop_ _Details Bruker save_ save_PRONTO _Saveframe_category software _Name PRONTO _Version 19990105 loop_ _Task 'data analysis' stop_ _Details 'Kjaer, M., Andersen, K.V., Poulsen, F. M.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.0 . pH pressure 1 . atm temperature 288 . K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 . M pH 5.0 . pH pressure 1 . atm temperature 288 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_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 . ppm . . . . . . 1.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_2 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'ORYZAIN BETA CHAIN' _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 ASP HA H 4.15 . . 2 . 1 ASP HB2 H 2.64 . . 3 . 1 ASP HB3 H 2.64 . . 4 . 2 HIS H H 8.94 . . 5 . 2 HIS HA H 4.78 . . 6 . 2 HIS HB2 H 3.01 . . 7 . 2 HIS HB3 H 3.12 . . 8 . 2 HIS HD2 H 7.24 . . 9 . 2 HIS HE1 H 8.56 . . 10 . 3 VAL H H 8.48 . . 11 . 3 VAL HA H 3.94 . . 12 . 3 VAL HB H 1.93 . . 13 . 3 VAL HG1 H 0.78 . . 14 . 3 VAL HG2 H 0.86 . . 15 . 4 CYS H H 8.56 . . 16 . 4 CYS HA H 4.45 . . 17 . 4 CYS HB2 H 2.33 . . 18 . 4 CYS HB3 H 2.33 . . 19 . 5 ASP H H 8.23 . . 20 . 5 ASP HA H 4.41 . . 21 . 5 ASP HB2 H 2.81 . . 22 . 5 ASP HB3 H 2.92 . . 23 . 6 ASP H H 8.38 . . 24 . 6 ASP HA H 4.32 . . 25 . 6 ASP HB2 H 2.61 . . 26 . 6 ASP HB3 H 2.72 . . 27 . 7 ASN H H 8.53 . . 28 . 7 ASN HA H 4.75 . . 29 . 7 ASN HB2 H 2.76 . . 30 . 7 ASN HB3 H 2.76 . . 31 . 7 ASN HD21 H 6.96 . . 32 . 7 ASN HD22 H 7.76 . . 33 . 8 PHE H H 8.02 . . 34 . 8 PHE HA H 4.60 . . 35 . 8 PHE HB2 H 2.72 . . 36 . 8 PHE HB3 H 2.95 . . 37 . 8 PHE HD1 H 7.06 . . 38 . 8 PHE HD2 H 7.06 . . 39 . 8 PHE HE1 H 7.29 . . 40 . 8 PHE HE2 H 7.29 . . 41 . 9 SER H H 7.93 . . 42 . 9 SER HA H 4.84 . . 43 . 9 SER HB2 H 3.59 . . 44 . 9 SER HB3 H 3.67 . . 45 . 10 CYS H H 8.63 . . 46 . 10 CYS HA H 5.08 . . 47 . 10 CYS HB2 H 2.32 . . 48 . 10 CYS HB3 H 3.26 . . 49 . 11 PRO HA H 4.42 . . 50 . 11 PRO HB2 H 1.93 . . 51 . 11 PRO HB3 H 2.32 . . 52 . 11 PRO HG2 H 1.96 . . 53 . 11 PRO HG3 H 2.02 . . 54 . 11 PRO HD2 H 3.63 . . 55 . 11 PRO HD3 H 3.82 . . 56 . 12 ALA H H 8.49 . . 57 . 12 ALA HA H 4.11 . . 58 . 12 ALA HB H 1.38 . . 59 . 13 GLY H H 8.98 . . 60 . 13 GLY HA2 H 3.76 . . 61 . 13 GLY HA3 H 4.29 . . 62 . 14 SER H H 8.24 . . 63 . 14 SER HA H 5.14 . . 64 . 14 SER HB2 H 3.63 . . 65 . 14 SER HB3 H 3.74 . . 66 . 15 THR H H 8.99 . . 67 . 15 THR HA H 4.54 . . 68 . 15 THR HB H 3.99 . . 69 . 15 THR HG2 H 1.11 . . 70 . 16 CYS H H 8.71 . . 71 . 16 CYS HA H 5.14 . . 72 . 16 CYS HB2 H 3.03 . . 73 . 16 CYS HB3 H 3.11 . . 74 . 17 SER H H 9.27 . . 75 . 17 SER HA H 4.86 . . 76 . 17 SER HB2 H 3.73 . . 77 . 17 SER HB3 H 3.83 . . 78 . 18 SER H H 8.62 . . 79 . 18 SER HA H 4.48 . . 80 . 18 SER HB2 H 2.73 . . 81 . 18 SER HB3 H 3.24 . . 82 . 19 ALA H H 8.13 . . 83 . 19 ALA HA H 4.27 . . 84 . 19 ALA HB H 1.18 . . 85 . 20 PHE H H 8.28 . . 86 . 20 PHE HA H 4.60 . . 87 . 20 PHE HB2 H 2.89 . . 88 . 20 PHE HB3 H 3.11 . . 89 . 20 PHE HD1 H 7.14 . . 90 . 20 PHE HD2 H 7.14 . . 91 . 20 PHE HE1 H 7.27 . . 92 . 20 PHE HE2 H 7.27 . . 93 . 21 GLY H H 8.32 . . 94 . 21 GLY HA2 H 3.81 . . 95 . 21 GLY HA3 H 3.92 . . 96 . 22 PHE H H 8.25 . . 97 . 22 PHE HA H 4.53 . . 98 . 22 PHE HB2 H 3.06 . . 99 . 22 PHE HB3 H 3.06 . . 100 . 22 PHE HD1 H 7.24 . . 101 . 22 PHE HD2 H 7.24 . . 102 . 22 PHE HE1 H 7.35 . . 103 . 22 PHE HE2 H 7.35 . . 104 . 23 ARG H H 8.55 . . 105 . 23 ARG HA H 4.02 . . 106 . 23 ARG HB2 H 1.58 . . 107 . 23 ARG HB3 H 1.77 . . 108 . 23 ARG HG2 H 1.15 . . 109 . 23 ARG HG3 H 1.28 . . 110 . 23 ARG HD2 H 3.02 . . 111 . 23 ARG HD3 H 3.02 . . 112 . 23 ARG HE H 7.09 . . 113 . 24 ASN H H 8.43 . . 114 . 24 ASN HA H 4.46 . . 115 . 24 ASN HB2 H 2.77 . . 116 . 24 ASN HB3 H 2.77 . . 117 . 24 ASN HD21 H 6.83 . . 118 . 24 ASN HD22 H 7.49 . . 119 . 25 LEU H H 8.17 . . 120 . 25 LEU HA H 4.24 . . 121 . 25 LEU HB2 H 1.61 . . 122 . 25 LEU HB3 H 1.61 . . 123 . 25 LEU HG H 1.80 . . 124 . 25 LEU HD1 H 0.82 . . 125 . 25 LEU HD2 H 0.90 . . 126 . 26 SER H H 8.01 . . 127 . 26 SER HA H 4.51 . . 128 . 26 SER HB2 H 3.81 . . 129 . 26 SER HB3 H 3.84 . . 130 . 27 LEU H H 8.31 . . 131 . 27 LEU HA H 4.29 . . 132 . 27 LEU HB2 H 1.15 . . 133 . 27 LEU HB3 H 1.51 . . 134 . 27 LEU HG H 1.37 . . 135 . 27 LEU HD1 H 0.51 . . 136 . 27 LEU HD2 H 0.67 . . 137 . 28 VAL H H 8.26 . . 138 . 28 VAL HA H 4.11 . . 139 . 28 VAL HB H 1.83 . . 140 . 28 VAL HG1 H 0.76 . . 141 . 28 VAL HG2 H 0.76 . . 142 . 29 TRP H H 8.13 . . 143 . 29 TRP HA H 4.86 . . 144 . 29 TRP HB2 H 2.50 . . 145 . 29 TRP HB3 H 2.99 . . 146 . 29 TRP HD1 H 7.04 . . 147 . 29 TRP HE1 H 7.50 . . 148 . 29 TRP HE3 H 10.09 . . 149 . 29 TRP HZ2 H 7.41 . . 150 . 29 TRP HZ3 H 6.94 . . 151 . 29 TRP HH2 H 7.17 . . 152 . 30 GLY H H 8.73 . . 153 . 30 GLY HA2 H 3.81 . . 154 . 30 GLY HA3 H 4.32 . . 155 . 31 CYS H H 8.50 . . 156 . 31 CYS HA H 5.57 . . 157 . 31 CYS HB2 H 2.81 . . 158 . 31 CYS HB3 H 3.09 . . 159 . 32 SER H H 9.31 . . 160 . 32 SER HA H 4.95 . . 161 . 32 SER HB2 H 3.83 . . 162 . 32 SER HB3 H 3.89 . . 163 . 33 PRO HA H 4.63 . . 164 . 33 PRO HB2 H 1.94 . . 165 . 33 PRO HB3 H 2.33 . . 166 . 33 PRO HG2 H 2.02 . . 167 . 33 PRO HG3 H 2.11 . . 168 . 33 PRO HD2 H 3.75 . . 169 . 33 PRO HD3 H 3.89 . . 170 . 34 VAL H H 8.25 . . 171 . 34 VAL HA H 4.05 . . 172 . 34 VAL HB H 2.00 . . 173 . 34 VAL HG1 H 0.88 . . 174 . 34 VAL HG2 H 0.91 . . 175 . 35 GLU H H 8.14 . . 176 . 35 GLU HA H 4.17 . . 177 . 35 GLU HB2 H 1.90 . . 178 . 35 GLU HB3 H 2.06 . . 179 . 35 GLU HG2 H 2.26 . . 180 . 35 GLU HG3 H 2.26 . . stop_ save_