data_5491 #Corrected using PDB structure: 1IYCA # #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 # 14 S HA 4.36 3.29 # 18 C HA 5.22 5.98 # 31 S HA 4.89 4.14 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 27 F CA 59.44 54.02 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 28 D H 7.84 4.00 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.02 0.54 N/A N/A N/A -0.35 # #bmr5491.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5491.str file): #HA CA CB CO N HN #N/A +0.54 N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.06 +/-0.35 N/A N/A N/A +/-0.18 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.662 0.943 N/A N/A N/A 0.570 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.185 1.036 N/A N/A N/A 0.489 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural basis for new pattern of the conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle, Oryctes rhinoceros ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Ishibashi Jun . . 3 Tomie Tetsuya . . 4 Yamakawa Minoru . . stop_ _BMRB_accession_number 5491 _BMRB_flat_file_name bmr5491.str _Entry_type new _Submission_date 2002-08-05 _Accession_date 2002-08-05 _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' 238 '13C chemical shifts' 36 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structural basis for new pattern of the conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle, Oryctes rhinoceros ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 12676931 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Ishibashi Jun . . 3 Tomie Tetsuya . . 4 Yamakawa Minoru . . stop_ _Journal_abbreviation "J. Biol. Chem." _Journal_volume 278 _Journal_issue ? _Page_first 22820 _Page_last 22827 _Year 2003 save_ ################################## # Molecular system description # ################################## save_system_scarabaecin _Saveframe_category molecular_system _Mol_system_name "scarabaecin monomer" _Abbreviation_common scarabaecin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "scarabaecin monomer" $scarabaecin stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all disulfide bound" loop_ _Biological_function "antifungal peptide" stop_ loop_ _Database_name _Database_accession_code PDB 1IYC stop_ save_ ######################## # Monomeric polymers # ######################## save_scarabaecin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common scarabaecin _Name_variant . _Abbreviation_common scarabaecin _Mol_thiol_state "all disulfide bound" ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; ELPKLPDDKVLIRSRSNCPK GKVWNGFDCKSPFAFS ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 LEU 3 PRO 4 LYS 5 LEU 6 PRO 7 ASP 8 ASP 9 LYS 10 VAL 11 LEU 12 ILE 13 ARG 14 SER 15 ARG 16 SER 17 ASN 18 CYS 19 PRO 20 LYS 21 GLY 22 LYS 23 VAL 24 TRP 25 ASN 26 GLY 27 PHE 28 ASP 29 CYS 30 LYS 31 SER 32 PRO 33 PHE 34 ALA 35 PHE 36 SER stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-04-29 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 1IYC "A Chain A, Solution Structure Of AntifungalPeptide, Scarabaecin" 100.00 36 100 100 3e-15 DBJ BAC54897.1 "scarabaecin [Oryctes rhinoceros]" 54.55 66 100 100 3e-15 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "scarabaecin monomer" 18 CYS SG "scarabaecin monomer" 29 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $scarabaecin "rhinoceros beetle" 72550 Eukaryota Metazoa Oryctes rhinoceros 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 $scarabaecin 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $scarabaecin 3 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task "acquisition" "processing" stop_ save_ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task processing stop_ save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.1 loop_ _Task "peak assignment" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-1H TOCSY 1H-1H DQF-COSY 1H-1H NOESY 1H-1H E.COSY 1H-1H ROESY ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.4 0.01 n/a temperature 298 0.01 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "scarabaecin monomer" 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 GLU HA H 4.09 . 1 2 1 GLU HB2 H 2.16 . 1 3 1 GLU HB3 H 2.16 . 1 4 1 GLU HG2 H 2.54 . 1 5 1 GLU HG3 H 2.54 . 1 6 1 GLU CA C 55.74 . 1 7 2 LEU H H 8.74 . 1 8 2 LEU HA H 4.43 . 1 9 2 LEU HB2 H 1.61 . 1 10 2 LEU HB3 H 1.61 . 1 11 2 LEU HG H 1.71 . 1 12 2 LEU HD1 H 0.93 . 2 13 2 LEU HD2 H 0.98 . 2 14 2 LEU CA C 54.04 . 1 15 3 PRO HA H 4.43 . 1 16 3 PRO HB2 H 1.86 . 2 17 3 PRO HB3 H 2.29 . 2 18 3 PRO HG2 H 2.03 . 1 19 3 PRO HG3 H 2.03 . 1 20 3 PRO HD2 H 3.66 . 2 21 3 PRO HD3 H 3.86 . 2 22 3 PRO CA C 63.84 . 1 23 4 LYS H H 8.35 . 1 24 4 LYS HA H 4.30 . 1 25 4 LYS HB2 H 1.78 . 1 26 4 LYS HB3 H 1.78 . 1 27 4 LYS HG2 H 1.44 . 1 28 4 LYS HG3 H 1.44 . 1 29 4 LYS HD2 H 1.69 . 1 30 4 LYS HD3 H 1.69 . 1 31 4 LYS HE2 H 3.08 . 1 32 4 LYS HE3 H 3.08 . 1 33 4 LYS HZ H 7.54 . 1 34 4 LYS CA C 56.84 . 1 35 5 LEU H H 8.30 . 1 36 5 LEU HA H 4.64 . 1 37 5 LEU HB2 H 1.61 . 1 38 5 LEU HB3 H 1.61 . 1 39 5 LEU HG H 1.54 . 1 40 5 LEU HD1 H 0.92 . 2 41 5 LEU HD2 H 0.94 . 2 42 5 LEU CA C 53.84 . 1 43 6 PRO HA H 4.40 . 1 44 6 PRO HB2 H 1.89 . 2 45 6 PRO HB3 H 2.28 . 2 46 6 PRO HG2 H 2.03 . 1 47 6 PRO HG3 H 2.03 . 1 48 6 PRO HD2 H 3.65 . 2 49 6 PRO HD3 H 3.84 . 2 50 6 PRO CA C 63.94 . 1 51 7 ASP H H 8.51 . 1 52 7 ASP HA H 4.67 . 1 53 7 ASP HB2 H 2.86 . 2 54 7 ASP HB3 H 2.90 . 2 55 7 ASP CA C 53.74 . 1 56 8 ASP H H 8.40 . 1 57 8 ASP HA H 4.69 . 1 58 8 ASP HB2 H 2.90 . 1 59 8 ASP HB3 H 2.90 . 1 60 8 ASP CA C 53.84 . 1 61 9 LYS H H 8.16 . 1 62 9 LYS HA H 4.29 . 1 63 9 LYS HB2 H 1.78 . 1 64 9 LYS HB3 H 1.78 . 1 65 9 LYS HG2 H 1.42 . 1 66 9 LYS HG3 H 1.42 . 1 67 9 LYS HD2 H 1.68 . 1 68 9 LYS HD3 H 1.68 . 1 69 9 LYS HE2 H 3.00 . 1 70 9 LYS HE3 H 3.00 . 1 71 9 LYS HZ H 7.54 . 1 72 9 LYS CA C 57.44 . 1 73 10 VAL H H 7.97 . 1 74 10 VAL HA H 4.03 . 1 75 10 VAL HB H 2.03 . 1 76 10 VAL HG1 H 0.90 . 2 77 10 VAL HG2 H 0.93 . 2 78 10 VAL CA C 63.34 . 1 79 11 LEU H H 8.26 . 1 80 11 LEU HA H 4.37 . 1 81 11 LEU HB2 H 1.60 . 1 82 11 LEU HB3 H 1.60 . 1 83 11 LEU HG H 1.56 . 1 84 11 LEU HD1 H 0.84 . 2 85 11 LEU HD2 H 0.90 . 2 86 11 LEU CA C 55.84 . 1 87 12 ILE H H 8.16 . 1 88 12 ILE HA H 4.11 . 1 89 12 ILE HB H 1.84 . 1 90 12 ILE HG12 H 1.18 . 1 91 12 ILE HG13 H 1.18 . 1 92 12 ILE HG2 H 0.88 . 1 93 12 ILE HD1 H 0.84 . 1 94 12 ILE CA C 61.94 . 1 95 13 ARG H H 8.42 . 1 96 13 ARG HA H 4.35 . 1 97 13 ARG HB2 H 1.75 . 2 98 13 ARG HB3 H 1.84 . 2 99 13 ARG HG2 H 1.62 . 1 100 13 ARG HG3 H 1.62 . 1 101 13 ARG HD2 H 3.16 . 1 102 13 ARG HD3 H 3.16 . 1 103 13 ARG HE H 7.18 . 1 104 13 ARG CA C 56.84 . 1 105 14 SER H H 8.26 . 1 106 14 SER HA H 4.34 . 1 107 14 SER HB2 H 3.78 . 2 108 14 SER HB3 H 3.82 . 2 109 14 SER CA C 59.04 . 1 110 15 ARG H H 8.21 . 1 111 15 ARG HA H 4.06 . 1 112 15 ARG HB2 H 1.54 . 2 113 15 ARG HB3 H 1.65 . 2 114 15 ARG HG2 H 1.45 . 1 115 15 ARG HG3 H 1.45 . 1 116 15 ARG HD2 H 3.04 . 1 117 15 ARG HD3 H 3.04 . 1 118 15 ARG HE H 7.08 . 1 119 15 ARG CA C 57.14 . 1 120 16 SER H H 7.63 . 1 121 16 SER HA H 3.93 . 1 122 16 SER HB2 H 3.24 . 2 123 16 SER HB3 H 3.31 . 2 124 16 SER CA C 58.54 . 1 125 17 ASN H H 8.07 . 1 126 17 ASN HA H 4.60 . 1 127 17 ASN HB2 H 2.51 . 1 128 17 ASN HB3 H 2.58 . 1 129 17 ASN HD21 H 6.67 . 2 130 17 ASN HD22 H 7.20 . 2 131 17 ASN CA C 53.84 . 1 132 18 CYS H H 8.34 . 1 133 18 CYS HA H 5.20 . 1 134 18 CYS HB2 H 2.69 . 1 135 18 CYS HB3 H 2.88 . 1 136 18 CYS CA C 52.94 . 1 137 19 PRO HA H 4.49 . 1 138 19 PRO HB2 H 1.82 . 2 139 19 PRO HB3 H 2.36 . 2 140 19 PRO HG2 H 1.93 . 2 141 19 PRO HG3 H 2.07 . 2 142 19 PRO HD2 H 3.35 . 2 143 19 PRO HD3 H 3.98 . 2 144 19 PRO CA C 63.14 . 1 145 20 LYS H H 8.34 . 1 146 20 LYS HA H 4.05 . 1 147 20 LYS HB2 H 1.78 . 1 148 20 LYS HB3 H 1.78 . 1 149 20 LYS HG2 H 1.44 . 1 150 20 LYS HG3 H 1.44 . 1 151 20 LYS HD2 H 1.73 . 1 152 20 LYS HD3 H 1.73 . 1 153 20 LYS HE2 H 2.98 . 1 154 20 LYS HE3 H 2.98 . 1 155 20 LYS HZ H 7.54 . 1 156 20 LYS CA C 59.04 . 1 157 21 GLY H H 8.87 . 1 158 21 GLY HA2 H 3.66 . 2 159 21 GLY HA3 H 4.31 . 2 160 21 GLY CA C 45.84 . 1 161 22 LYS H H 8.08 . 1 162 22 LYS HA H 4.78 . 1 163 22 LYS HB2 H 1.77 . 1 164 22 LYS HB3 H 1.77 . 1 165 22 LYS HG2 H 1.15 . 1 166 22 LYS HG3 H 1.15 . 1 167 22 LYS HD2 H 1.40 . 2 168 22 LYS HD3 H 1.51 . 2 169 22 LYS HE2 H 2.92 . 1 170 22 LYS HE3 H 2.92 . 1 171 22 LYS HZ H 7.60 . 1 172 22 LYS CA C 55.44 . 1 173 23 VAL H H 8.92 . 1 174 23 VAL HA H 4.54 . 1 175 23 VAL HB H 2.02 . 1 176 23 VAL HG1 H 0.84 . 2 177 23 VAL HG2 H 0.90 . 2 178 23 VAL CA C 61.14 . 1 179 24 TRP H H 8.93 . 1 180 24 TRP HA H 5.13 . 1 181 24 TRP HB2 H 3.23 . 1 182 24 TRP HB3 H 3.33 . 1 183 24 TRP HD1 H 7.17 . 1 184 24 TRP HE1 H 10.26 . 1 185 24 TRP HE3 H 7.40 . 1 186 24 TRP HZ2 H 7.21 . 1 187 24 TRP HZ3 H 6.97 . 1 188 24 TRP HH2 H 7.01 . 1 189 24 TRP CA C 57.74 . 1 190 25 ASN H H 8.08 . 1 191 25 ASN HA H 4.81 . 1 192 25 ASN HB2 H 2.57 . 2 193 25 ASN HB3 H 3.25 . 2 194 25 ASN HD21 H 6.83 . 2 195 25 ASN HD22 H 7.58 . 2 196 25 ASN CA C 52.34 . 1 197 26 GLY H H 8.07 . 1 198 26 GLY HA2 H 3.13 . 2 199 26 GLY HA3 H 4.04 . 2 200 26 GLY CA C 46.04 . 1 201 27 PHE H H 7.55 . 1 202 27 PHE HA H 4.30 . 1 203 27 PHE HB2 H 2.70 . 2 204 27 PHE HB3 H 2.93 . 2 205 27 PHE HD1 H 7.02 . 1 206 27 PHE HD2 H 7.02 . 1 207 27 PHE HE1 H 7.28 . 1 208 27 PHE HE2 H 7.28 . 1 209 27 PHE HZ H 7.26 . 1 210 27 PHE CA C 59.44 . 1 211 28 ASP H H 8.19 . 1 212 28 ASP HA H 4.73 . 1 213 28 ASP HB2 H 2.69 . 2 214 28 ASP HB3 H 2.78 . 2 215 28 ASP CA C 53.14 . 1 216 29 CYS H H 8.65 . 1 217 29 CYS HA H 5.23 . 1 218 29 CYS HB2 H 3.14 . 1 219 29 CYS HB3 H 2.71 . 1 220 29 CYS CA C 55.54 . 1 221 30 LYS H H 9.07 . 1 222 30 LYS HA H 4.71 . 1 223 30 LYS HB2 H 1.71 . 1 224 30 LYS HB3 H 1.71 . 1 225 30 LYS HG2 H 1.36 . 2 226 30 LYS HG3 H 1.64 . 2 227 30 LYS HD2 H 1.84 . 1 228 30 LYS HD3 H 1.84 . 1 229 30 LYS HE2 H 2.94 . 1 230 30 LYS HE3 H 2.94 . 1 231 30 LYS HZ H 7.51 . 1 232 30 LYS CA C 55.24 . 1 233 31 SER H H 8.90 . 1 234 31 SER HA H 4.87 . 1 235 31 SER HB2 H 3.87 . 2 236 31 SER HB3 H 3.90 . 2 237 31 SER CA C 57.94 . 1 238 32 PRO HA H 4.34 . 1 239 32 PRO HB2 H 1.72 . 2 240 32 PRO HB3 H 2.12 . 2 241 32 PRO HG2 H 1.78 . 2 242 32 PRO HG3 H 1.89 . 2 243 32 PRO HD2 H 3.79 . 2 244 32 PRO HD3 H 3.91 . 2 245 32 PRO CA C 64.24 . 1 246 33 PHE H H 7.97 . 1 247 33 PHE HA H 4.56 . 1 248 33 PHE HB2 H 2.92 . 1 249 33 PHE HB3 H 3.08 . 1 250 33 PHE HD1 H 7.20 . 1 251 33 PHE HD2 H 7.20 . 1 252 33 PHE HE1 H 7.32 . 1 253 33 PHE HE2 H 7.32 . 1 254 33 PHE HZ H 7.31 . 1 255 33 PHE CA C 58.24 . 1 256 34 ALA H H 7.98 . 1 257 34 ALA HA H 4.29 . 1 258 34 ALA HB H 1.27 . 1 259 34 ALA CA C 52.94 . 1 260 35 PHE H H 8.04 . 1 261 35 PHE HA H 4.63 . 1 262 35 PHE HB2 H 3.04 . 1 263 35 PHE HB3 H 3.17 . 1 264 35 PHE HD1 H 7.36 . 1 265 35 PHE HD2 H 7.36 . 1 266 35 PHE HE1 H 7.28 . 1 267 35 PHE HE2 H 7.28 . 1 268 35 PHE HZ H 7.35 . 1 269 35 PHE CA C 58.34 . 1 270 36 SER H H 8.22 . 1 271 36 SER HA H 4.46 . 1 272 36 SER HB2 H 3.84 . 2 273 36 SER HB3 H 3.92 . 2 274 36 SER CA C 58.64 . 1 stop_ save_