data_4509 #Corrected using PDB structure: 1AB1_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 20 G HA 3.27 4.01 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.05 N/A N/A N/A N/A -0.07 # #bmr4509.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4509.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 N/A N/A N/A N/A +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.811 N/A N/A N/A N/A 0.777 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.170 N/A N/A N/A N/A 0.254 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Automated 2D NOESY Assignment and Structure Calculation of crambin(S22/I25) with Self-Correcting Distance Geometry Based NOAH/DIAMOND Programs ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Y. . . 2 Wu J. . . 3 Gorenstein D. . . 4 Braun W. . . stop_ _BMRB_accession_number 4509 _BMRB_flat_file_name bmr4509.str _Entry_type new _Submission_date 1999-10-08 _Accession_date 1999-12-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 206 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Automated 2D NOESY assignment and structure calculation of Crambin(S22/I25) with the self-correcting distance geometry based NOAH/DIAMOD programs ; _Citation_status published _Citation_type Journal _MEDLINE_UI_code 99106048 _PubMed_ID 9887292 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Y. . . 2 Wu J. . . 3 Gorenstein D. . . 4 Braun W. . . stop_ _Journal_abbreviation 'J. Magn. Reson.' _Journal_name_full . _Journal_volume 136 _Page_first 76 _Page_last 85 _Year 1999 loop_ _Keyword crambin "crambe abyssinica" "plant seed protein" stop_ save_ ################################## # Molecular system description # ################################## save_system-crambin _Saveframe_category molecular_system _Mol_system_name crambin _Abbreviation_common crambin loop_ _Mol_system_component_name _Mol_label crambin $crambin stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1AB1 "Si Form Crambin" . PDB 1CXR "A Chain A, Automated 2d Noesy Assignment And Structure Calculation Of Crambin(S22I25) WITH SELF-Correcting Distance Geometry Based NoahDIAMOD PROGRAMS" . stop_ save_ ######################## # Monomeric polymers # ######################## save_crambin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common crambin _Abbreviation_common crambin _Mol_thiol_state 'not reported' ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; TTCCPSIVARSNFNVCRLPG TSEAICATYTGCIIIPGATC PGDYAN ; loop_ _Residue_seq_code _Residue_label 1 THR 2 THR 3 CYS 4 CYS 5 PRO 6 SER 7 ILE 8 VAL 9 ALA 10 ARG 11 SER 12 ASN 13 PHE 14 ASN 15 VAL 16 CYS 17 ARG 18 LEU 19 PRO 20 GLY 21 THR 22 SER 23 GLU 24 ALA 25 ILE 26 CYS 27 ALA 28 THR 29 TYR 30 THR 31 GLY 32 CYS 33 ILE 34 ILE 35 ILE 36 PRO 37 GLY 38 ALA 39 THR 40 CYS 41 PRO 42 GLY 43 ASP 44 TYR 45 ALA 46 ASN stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1AB1 "Si Form Crambin" 100.00 46 100 100 6e-22 PDB 1CXR "A Chain A, Automated 2d Noesy Assignment AndStructure Calculation Of Crambin(S22I25) WITHSELF-Correcting Distance Geometry Based NoahDIAMODPROGRAMS" 100.00 46 100 100 2e-21 PDB 1CRN Crambin 100.00 46 98 98 2e-21 PIR KECX "crambin - Abyssinian crambe" 100.00 46 98 98 2e-21 PIR S52545 "thionin variant Thi2Ca1 - Abyssiniancrambe" 33.82 136 100 100 6e-22 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $crambin "Abyssinian crambe" 3271 Eukaryota Viridiplantae Crambe abyssinica 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 $crambin ? . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; (SER/ILE) ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $crambin 2.5 mM . acetone 75 % [U-2H] H2O 20 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_NOAH _Saveframe_category software _Name NOAH _Version 1.0 loop_ _Task "STRUCTURE SOLUTION" stop_ _Details "C.MUMENTHALER, Y.XU, W.BRAUN" save_ save_DIAMOD _Saveframe_category software _Name DIAMOD _Version 1.0 loop_ _Task "STRUCTURE SOLUTION" stop_ _Details "P. GUNTERT, W. BRAUN, K. WUTHRICH" save_ save_FANTOM _Saveframe_category software _Name FANTOM _Version 4.0 loop_ _Task REFINEMENT stop_ _Details "TH.SCHAUMANN, W.BRAUN, K.WUTHRICH, R.FRACZKIEWICZ" save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXRS _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 2D NOESY DQF-COSY 2D TOCSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 298 . K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _Saveframe_category chemical_shift_reference 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 _Indirect_shift_ratio_citation_label . H 1 . . . . . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name crambin loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 THR HA H 4.22 . . 2 1 THR HB H 4.12 . . 3 1 THR HG2 H 1.13 . . 4 2 THR H H 8.62 . . 5 2 THR HA H 5.22 . . 6 2 THR HB H 3.73 . . 7 2 THR HG2 H 0.87 . . 8 3 CYS H H 9.08 . . 9 3 CYS HA H 5.00 . . 10 3 CYS HB2 H 2.54 . . 11 3 CYS HB3 H 4.60 . . 12 4 CYS H H 9.04 . . 13 4 CYS HA H 5.43 . . 14 4 CYS HB2 H 2.90 . . 15 5 PRO HB2 H 2.02 . . 16 5 PRO HB3 H 1.93 . . 17 5 PRO HG2 H 2.89 . . 18 5 PRO HD2 H 4.00 . . 19 5 PRO HD3 H 3.79 . . 20 6 SER H H 7.00 . . 21 6 SER HA H 4.78 . . 22 6 SER HB2 H 4.03 . . 23 7 ILE H H 9.23 . . 24 7 ILE HA H 4.12 . . 25 7 ILE HB H 1.98 . . 26 7 ILE HG2 H 1.04 . . 27 7 ILE HG12 H 1.72 . . 28 7 ILE HG13 H 1.34 . . 29 7 ILE HD1 H 0.97 . . 30 8 VAL H H 7.68 . . 31 8 VAL HA H 3.77 . . 32 8 VAL HB H 2.04 . . 33 8 VAL HG1 H 1.08 . . 34 8 VAL HG2 H 0.99 . . 35 9 ALA H H 8.08 . . 36 9 ALA HA H 4.49 . . 37 9 ALA HB H 1.70 . . 38 10 ARG H H 7.79 . . 39 10 ARG HA H 4.61 . . 40 10 ARG HB2 H 2.03 . . 41 10 ARG HB3 H 1.71 . . 42 10 ARG HD2 H 3.43 . . 43 10 ARG HE H 9.69 . . 44 10 ARG HH11 H 6.64 . . 45 10 ARG HH12 H 6.64 . . 46 10 ARG HH21 H 7.06 . . 47 10 ARG HH22 H 7.06 . . 48 11 SER H H 8.41 . . 49 11 SER HA H 4.06 . . 50 11 SER HB2 H 4.09 . . 51 12 ASN H H 8.57 . . 52 12 ASN HA H 4.54 . . 53 12 ASN HB2 H 3.18 . . 54 12 ASN HB3 H 2.71 . . 55 12 ASN HD21 H 6.72 . . 56 12 ASN HD22 H 7.55 . . 57 13 PHE H H 9.30 . . 58 13 PHE HA H 3.96 . . 59 13 PHE HB2 H 3.83 . . 60 13 PHE HB3 H 3.56 . . 61 13 PHE HD1 H 7.22 . . 62 13 PHE HE1 H 7.46 . . 63 13 PHE HZ H 7.33 . . 64 14 ASN H H 8.75 . . 65 14 ASN HB2 H 2.77 . . 66 14 ASN HB3 H 3.31 . . 67 14 ASN HD21 H 7.06 . . 68 14 ASN HD22 H 7.82 . . 69 15 VAL H H 8.25 . . 70 15 VAL HA H 3.70 . . 71 15 VAL HB H 2.23 . . 72 15 VAL HG1 H 1.16 . . 73 15 VAL HG2 H 0.99 . . 74 16 CYS H H 9.30 . . 75 16 CYS HA H 3.82 . . 76 16 CYS HB2 H 2.60 . . 77 16 CYS HB3 H 2.46 . . 78 17 ARG H H 7.72 . . 79 17 ARG HA H 4.06 . . 80 17 ARG HB2 H 1.85 . . 81 17 ARG HB3 H 1.70 . . 82 17 ARG HG2 H 1.27 . . 83 17 ARG HG3 H 1.27 . . 84 17 ARG HD2 H 3.25 . . 85 17 ARG HD3 H 2.60 . . 86 17 ARG HE H 7.42 . . 87 18 LEU H H 7.64 . . 88 18 LEU HA H 4.21 . . 89 18 LEU HB2 H 2.08 . . 90 18 LEU HB3 H 1.64 . . 91 18 LEU HD1 H 1.01 . . 92 18 LEU HD2 H 0.93 . . 93 19 PRO HD2 H 4.07 . . 94 19 PRO HD3 H 3.96 . . 95 20 GLY H H 8.20 . . 96 20 GLY HA2 H 3.49 . . 97 20 GLY HA3 H 3.17 . . 98 21 THR H H 6.93 . . 99 21 THR HA H 4.03 . . 100 21 THR HB H 3.86 . . 101 21 THR HG2 H 1.34 . . 102 22 SER H H 8.20 . . 103 22 SER HA H 4.06 . . 104 22 SER HB2 H 3.54 . . 105 23 GLU H H 9.69 . . 106 23 GLU HA H 3.42 . . 107 23 GLU HB2 H 2.02 . . 108 23 GLU HB3 H 1.77 . . 109 23 GLU HG2 H 2.89 . . 110 23 GLU HG3 H 2.88 . . 111 24 ALA H H 8.60 . . 112 24 ALA HA H 4.10 . . 113 24 ALA HB H 1.47 . . 114 25 ILE H H 7.44 . . 115 25 ILE HA H 3.79 . . 116 25 ILE HB H 2.05 . . 117 25 ILE HG2 H 0.82 . . 118 25 ILE HG12 H 1.18 . . 119 25 ILE HG13 H 1.10 . . 120 26 CYS H H 8.33 . . 121 26 CYS HA H 4.67 . . 122 26 CYS HB2 H 2.77 . . 123 26 CYS HB3 H 2.49 . . 124 27 ALA H H 9.43 . . 125 27 ALA HA H 4.11 . . 126 27 ALA HB H 1.56 . . 127 28 THR H H 7.68 . . 128 28 THR HA H 3.99 . . 129 28 THR HG2 H 1.13 . . 130 29 TYR H H 7.92 . . 131 29 TYR HA H 4.43 . . 132 29 TYR HB2 H 3.24 . . 133 29 TYR HB3 H 3.05 . . 134 29 TYR HD1 H 7.25 . . 135 29 TYR HE1 H 6.76 . . 136 30 THR H H 7.59 . . 137 30 THR HA H 4.64 . . 138 30 THR HB H 4.74 . . 139 30 THR HG2 H 1.43 . . 140 31 GLY H H 8.04 . . 141 31 GLY HA2 H 3.96 . . 142 31 GLY HA3 H 3.56 . . 143 32 CYS H H 7.76 . . 144 32 CYS HA H 5.19 . . 145 32 CYS HB2 H 2.87 . . 146 32 CYS HB3 H 2.50 . . 147 33 ILE H H 9.05 . . 148 33 ILE HA H 4.77 . . 149 33 ILE HB H 1.62 . . 150 33 ILE HG2 H 0.61 . . 151 33 ILE HG12 H 1.09 . . 152 33 ILE HG13 H 0.82 . . 153 33 ILE HD1 H 0.16 . . 154 34 ILE H H 8.16 . . 155 34 ILE HA H 4.74 . . 156 34 ILE HB H 1.64 . . 157 34 ILE HG2 H 0.78 . . 158 34 ILE HG12 H 1.37 . . 159 34 ILE HG13 H 1.10 . . 160 35 ILE H H 8.49 . . 161 35 ILE HA H 5.00 . . 162 35 ILE HB H 2.04 . . 163 35 ILE HG2 H 0.82 . . 164 35 ILE HG12 H 1.47 . . 165 35 ILE HG13 H 0.96 . . 166 35 ILE HD1 H 0.77 . . 167 36 PRO HA H 4.60 . . 168 36 PRO HD2 H 3.79 . . 169 37 GLY H H 7.96 . . 170 37 GLY HA2 H 4.08 . . 171 38 ALA H H 8.47 . . 172 38 ALA HB H 1.45 . . 173 39 THR H H 7.72 . . 174 39 THR HA H 4.55 . . 175 39 THR HB H 3.96 . . 176 39 THR HG2 H 1.19 . . 177 40 CYS H H 8.76 . . 178 40 CYS HA H 4.88 . . 179 40 CYS HB2 H 2.63 . . 180 40 CYS HB3 H 3.45 . . 181 41 PRO HA H 4.61 . . 182 41 PRO HB2 H 2.42 . . 183 41 PRO HB3 H 2.23 . . 184 41 PRO HD2 H 3.81 . . 185 41 PRO HD3 H 3.68 . . 186 42 GLY H H 8.84 . . 187 42 GLY HA2 H 3.85 . . 188 43 ASP H H 8.39 . . 189 43 ASP HA H 4.68 . . 190 43 ASP HB2 H 3.04 . . 191 43 ASP HB3 H 2.85 . . 192 44 TYR H H 8.11 . . 193 44 TYR HA H 4.47 . . 194 44 TYR HB2 H 2.41 . . 195 44 TYR HB3 H 2.95 . . 196 44 TYR HD1 H 6.83 . . 197 44 TYR HE1 H 6.92 . . 198 45 ALA H H 7.67 . . 199 45 ALA HA H 4.49 . . 200 45 ALA HB H 1.37 . . 201 46 ASN H H 8.08 . . 202 46 ASN HA H 4.68 . . 203 46 ASN HB2 H 2.55 . . 204 46 ASN HB3 H 1.91 . . 205 46 ASN HD21 H 6.70 . . 206 46 ASN HD22 H 6.99 . . stop_ save_