data_6386 #Corrected using PDB structure: 1Y1BA # #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 # 7 I HA 4.72 3.03 # 8 C HA 5.42 4.20 # 12 Y HA 4.78 3.79 # 42 L HA 4.18 4.91 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 12 Y H 8.69 6.47 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.09 N/A N/A N/A N/A -0.16 # #bmr6386.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6386.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 +/-0.12 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.529 N/A N/A N/A N/A 0.350 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.161 N/A N/A N/A N/A 0.398 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural and Functional Study of Anemonia Elastase Inhibitor, a "Non-classical" Kazal-type Inhibitor from Anemonia sulcata ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Kumazaki Takashi . . 3 Yoshizawa-Kumagaye Kumiko . . 4 Nishiuchi Yuji . . 5 Yoshida Takuya . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ _BMRB_accession_number 6386 _BMRB_flat_file_name bmr6386.str _Entry_type new _Submission_date 2004-11-15 _Accession_date 2004-11-15 _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' 267 stop_ loop_ _Related_BMRB_accession_number _Relationship 6387 "aei-analogue monomer" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structural and Functional Study of an Anemonia Elastase Inhibitor, a "Nonclassical" Kazal-Type Inhibitor from Anemonia sulcata. ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 16008348 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Kumazaki Takashi . . 3 Yoshizawa-Kumagaye Kumiko . . 4 Nishiuchi Yuji . . 5 Yoshida Takuya . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 44 _Journal_issue 28 _Page_first 9626 _Page_last 9636 _Year 2005 save_ ################################## # Molecular system description # ################################## save_system_aei _Saveframe_category molecular_system _Mol_system_name "aei monomer" _Abbreviation_common aei _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "aei monomer" $aei stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' save_ ######################## # Monomeric polymers # ######################## save_aei _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "anemonia elastase inhibitor" _Name_variant . _Abbreviation_common aei _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 48 _Mol_residue_sequence ; KPDCPLICTMQYDPVCGSDG ITYGNACMLLGASCRSDTPI ELVHKGRC ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 PRO 3 ASP 4 CYS 5 PRO 6 LEU 7 ILE 8 CYS 9 THR 10 MET 11 GLN 12 TYR 13 ASP 14 PRO 15 VAL 16 CYS 17 GLY 18 SER 19 ASP 20 GLY 21 ILE 22 THR 23 TYR 24 GLY 25 ASN 26 ALA 27 CYS 28 MET 29 LEU 30 LEU 31 GLY 32 ALA 33 SER 34 CYS 35 ARG 36 SER 37 ASP 38 THR 39 PRO 40 ILE 41 GLU 42 LEU 43 VAL 44 HIS 45 LYS 46 GLY 47 ARG 48 CYS stop_ _Sequence_homology_query_date 2005-09-22 _Sequence_homology_query_revised_last_date 2005-09-15 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 1Y1B "A Chain A, Solution Structure Of AnemoniaElastase Inhibitor" 100.00 48 100 100 1e-23 PIR S00130 "elastase inhibitor - snake-locks sea anemone" 100.00 48 100 100 1e-23 SWISS-PROT P16895 "IELA_ANESU Elastase inhibitor" 100.00 48 100 100 1e-23 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _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 "aei monomer" 4 CYS SG "aei monomer" 34 CYS SG single disulfide "aei monomer" 8 CYS SG "aei monomer" 27 CYS SG single disulfide "aei monomer" 16 CYS SG "aei monomer" 48 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 $aei "Anemonia sulcata" 6108 Eukaryota Fungi Anemonia sulcata 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 $aei '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $aei . mM 3.0 3.5 . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr loop_ _Task processing stop_ save_ save_Sparky _Saveframe_category software _Name Sparky loop_ _Task "peak picking" "assignment" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-1H NOESY 1H-1H TOCSY 1H-1H DQFCOSY 1H-1H ECOSY 1H-1H ROESY 1H-15N HSQC ; 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 0.1 pH temperature 298 1 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 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 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 "aei 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 LYS HA H 4.35 . 1 2 1 LYS HB2 H 1.95 . 1 3 1 LYS HB3 H 1.95 . 1 4 1 LYS HG2 H 1.53 . 1 5 1 LYS HG3 H 1.53 . 1 6 1 LYS HD2 H 1.74 . 1 7 1 LYS HD3 H 1.74 . 1 8 1 LYS HE2 H 3.04 . 1 9 1 LYS HE3 H 3.04 . 1 10 1 LYS HZ H 7.53 . 1 11 2 PRO HA H 4.49 . 1 12 2 PRO HB2 H 1.90 . 2 13 2 PRO HB3 H 2.32 . 2 14 2 PRO HG2 H 2.01 . 1 15 2 PRO HG3 H 2.01 . 1 16 2 PRO HD2 H 3.60 . 2 17 2 PRO HD3 H 3.74 . 2 18 3 ASP H H 8.61 . 1 19 3 ASP HA H 4.67 . 1 20 3 ASP HB2 H 2.80 . 2 21 3 ASP HB3 H 2.91 . 2 22 4 CYS H H 8.39 . 1 23 4 CYS HA H 4.91 . 1 24 4 CYS HB2 H 2.82 . 1 25 4 CYS HB3 H 3.15 . 1 26 5 PRO HA H 4.44 . 1 27 5 PRO HB2 H 1.87 . 2 28 5 PRO HB3 H 2.26 . 2 29 5 PRO HG2 H 2.03 . 1 30 5 PRO HG3 H 2.03 . 1 31 5 PRO HD2 H 3.67 . 1 32 5 PRO HD3 H 3.67 . 1 33 6 LEU H H 8.74 . 1 34 6 LEU HA H 4.25 . 1 35 6 LEU HB2 H 1.71 . 1 36 6 LEU HB3 H 1.71 . 1 37 6 LEU HG H 1.63 . 1 38 6 LEU HD1 H 0.88 . 2 39 6 LEU HD2 H 0.95 . 2 40 7 ILE H H 7.55 . 1 41 7 ILE HA H 4.63 . 1 42 7 ILE HB H 1.69 . 1 43 7 ILE HG12 H 1.03 . 2 44 7 ILE HG13 H 1.41 . 2 45 7 ILE HG2 H 0.83 . 1 46 7 ILE HD1 H 0.80 . 1 47 8 CYS H H 8.45 . 1 48 8 CYS HA H 5.33 . 1 49 8 CYS HB2 H 2.63 . 1 50 8 CYS HB3 H 3.32 . 1 51 9 THR H H 8.34 . 1 52 9 THR HA H 4.62 . 1 53 9 THR HB H 4.49 . 1 54 9 THR HG2 H 1.30 . 1 55 10 MET H H 7.94 . 1 56 10 MET HA H 4.72 . 1 57 10 MET HB2 H 1.79 . 2 58 10 MET HB3 H 2.48 . 2 59 10 MET HG2 H 2.24 . 1 60 10 MET HG3 H 2.27 . 1 61 10 MET HE H 2.07 . 1 62 11 GLN H H 7.95 . 1 63 11 GLN HA H 4.13 . 1 64 11 GLN HB2 H 2.05 . 1 65 11 GLN HB3 H 2.05 . 1 66 11 GLN HG2 H 2.95 . 2 67 11 GLN HG3 H 3.09 . 2 68 11 GLN HE21 H 7.61 . 2 69 11 GLN HE22 H 6.96 . 2 70 12 TYR H H 8.85 . 1 71 12 TYR HA H 4.69 . 1 72 12 TYR HB2 H 3.09 . 1 73 12 TYR HB3 H 2.95 . 1 74 12 TYR HD1 H 7.24 . 1 75 12 TYR HD2 H 7.24 . 1 76 12 TYR HE1 H 6.83 . 1 77 12 TYR HE2 H 6.83 . 1 78 13 ASP H H 8.74 . 1 79 13 ASP HA H 4.81 . 1 80 13 ASP HB2 H 2.65 . 1 81 13 ASP HB3 H 2.79 . 1 82 14 PRO HA H 4.51 . 1 83 14 PRO HB2 H 1.36 . 2 84 14 PRO HB3 H 1.79 . 2 85 14 PRO HG2 H 1.67 . 2 86 14 PRO HG3 H 1.80 . 2 87 14 PRO HD2 H 3.40 . 1 88 14 PRO HD3 H 3.40 . 1 89 15 VAL H H 8.34 . 1 90 15 VAL HA H 4.68 . 1 91 15 VAL HB H 1.93 . 1 92 15 VAL HG1 H 0.65 . 2 93 15 VAL HG2 H 0.96 . 2 94 16 CYS H H 8.38 . 1 95 16 CYS HA H 5.14 . 1 96 16 CYS HB2 H 1.37 . 1 97 16 CYS HB3 H 2.41 . 1 98 17 GLY H H 9.18 . 1 99 17 GLY HA2 H 4.02 . 2 100 17 GLY HA3 H 5.20 . 2 101 18 SER H H 9.24 . 1 102 18 SER HA H 4.09 . 1 103 18 SER HB2 H 3.77 . 2 104 18 SER HB3 H 4.26 . 2 105 19 ASP H H 8.52 . 1 106 19 ASP HA H 4.61 . 1 107 19 ASP HB2 H 2.81 . 2 108 19 ASP HB3 H 3.14 . 2 109 20 GLY H H 8.38 . 1 110 20 GLY HA2 H 3.79 . 2 111 20 GLY HA3 H 4.10 . 2 112 21 ILE H H 7.47 . 1 113 21 ILE HA H 3.95 . 1 114 21 ILE HB H 1.92 . 1 115 21 ILE HG12 H 0.91 . 2 116 21 ILE HG13 H 1.21 . 2 117 21 ILE HG2 H 0.06 . 1 118 21 ILE HD1 H 0.70 . 1 119 22 THR H H 8.05 . 1 120 22 THR HA H 4.86 . 1 121 22 THR HB H 4.02 . 1 122 22 THR HG2 H 1.14 . 1 123 23 TYR H H 9.26 . 1 124 23 TYR HA H 4.52 . 1 125 23 TYR HB2 H 2.52 . 1 126 23 TYR HB3 H 2.91 . 1 127 23 TYR HD1 H 7.28 . 1 128 23 TYR HD2 H 7.28 . 1 129 23 TYR HE1 H 6.90 . 1 130 23 TYR HE2 H 6.90 . 1 131 24 GLY H H 9.05 . 1 132 24 GLY HA2 H 3.69 . 2 133 24 GLY HA3 H 4.01 . 2 134 25 ASN H H 7.29 . 1 135 25 ASN HA H 4.85 . 1 136 25 ASN HB2 H 3.14 . 2 137 25 ASN HB3 H 3.62 . 2 138 25 ASN HD21 H 6.95 . 2 139 25 ASN HD22 H 7.94 . 2 140 26 ALA H H 9.07 . 1 141 26 ALA HA H 3.93 . 1 142 26 ALA HB H 1.46 . 1 143 27 CYS H H 8.19 . 1 144 27 CYS HA H 4.26 . 1 145 27 CYS HB2 H 3.50 . 1 146 27 CYS HB3 H 3.02 . 1 147 28 MET H H 8.28 . 1 148 28 MET HA H 4.09 . 1 149 28 MET HB2 H 2.28 . 2 150 28 MET HB3 H 2.32 . 2 151 28 MET HG2 H 2.61 . 2 152 28 MET HG3 H 2.86 . 2 153 28 MET HE H 2.25 . 1 154 29 LEU H H 7.33 . 1 155 29 LEU HA H 2.81 . 1 156 29 LEU HB2 H 1.04 . 2 157 29 LEU HB3 H 1.62 . 2 158 29 LEU HG H 1.05 . 1 159 29 LEU HD1 H 0.60 . 2 160 29 LEU HD2 H 0.63 . 2 161 30 LEU H H 8.00 . 1 162 30 LEU HA H 4.00 . 1 163 30 LEU HB2 H 1.90 . 1 164 30 LEU HB3 H 1.90 . 1 165 30 LEU HG H 1.75 . 1 166 30 LEU HD1 H 0.95 . 1 167 30 LEU HD2 H 0.95 . 1 168 31 GLY H H 8.79 . 1 169 31 GLY HA2 H 3.66 . 2 170 31 GLY HA3 H 3.87 . 2 171 32 ALA H H 7.74 . 1 172 32 ALA HA H 4.18 . 1 173 32 ALA HB H 1.49 . 1 174 33 SER H H 8.70 . 1 175 33 SER HA H 3.98 . 1 176 33 SER HB2 H 4.03 . 2 177 33 SER HB3 H 4.10 . 2 178 34 CYS H H 8.22 . 1 179 34 CYS HA H 4.48 . 1 180 34 CYS HB2 H 3.41 . 2 181 34 CYS HB3 H 3.53 . 2 182 35 ARG H H 7.28 . 1 183 35 ARG HA H 4.44 . 1 184 35 ARG HB2 H 1.86 . 2 185 35 ARG HB3 H 2.04 . 2 186 35 ARG HG2 H 1.63 . 2 187 35 ARG HG3 H 1.72 . 2 188 35 ARG HD2 H 3.01 . 2 189 35 ARG HD3 H 3.27 . 2 190 35 ARG HE H 7.20 . 1 191 36 SER H H 7.38 . 1 192 36 SER HA H 4.58 . 1 193 36 SER HB2 H 3.91 . 1 194 36 SER HB3 H 3.97 . 1 195 37 ASP H H 8.82 . 1 196 37 ASP HA H 4.58 . 1 197 37 ASP HB2 H 2.94 . 2 198 37 ASP HB3 H 3.02 . 2 199 38 THR H H 7.81 . 1 200 38 THR HA H 4.75 . 1 201 38 THR HB H 4.04 . 1 202 38 THR HG2 H 1.20 . 1 203 39 PRO HA H 4.34 . 1 204 39 PRO HB2 H 1.78 . 2 205 39 PRO HB3 H 2.15 . 2 206 39 PRO HG2 H 1.93 . 2 207 39 PRO HG3 H 2.03 . 2 208 39 PRO HD2 H 3.66 . 2 209 39 PRO HD3 H 3.83 . 2 210 40 ILE H H 8.11 . 1 211 40 ILE HA H 3.91 . 1 212 40 ILE HB H 1.32 . 1 213 40 ILE HG12 H 1.65 . 1 214 40 ILE HG13 H 1.65 . 1 215 40 ILE HG2 H 0.86 . 1 216 40 ILE HD1 H 0.80 . 1 217 41 GLU H H 8.57 . 1 218 41 GLU HA H 4.57 . 1 219 41 GLU HB2 H 1.77 . 1 220 41 GLU HB3 H 1.77 . 1 221 41 GLU HG2 H 2.05 . 2 222 41 GLU HG3 H 2.36 . 2 223 42 LEU H H 8.78 . 1 224 42 LEU HA H 4.09 . 1 225 42 LEU HB2 H 1.85 . 1 226 42 LEU HB3 H 1.50 . 1 227 42 LEU HG H 1.31 . 1 228 42 LEU HD1 H 0.65 . 2 229 42 LEU HD2 H 0.88 . 2 230 43 VAL H H 8.90 . 1 231 43 VAL HA H 4.07 . 1 232 43 VAL HB H 1.74 . 1 233 43 VAL HG1 H 0.86 . 2 234 43 VAL HG2 H 1.01 . 2 235 44 HIS H H 7.01 . 1 236 44 HIS HA H 4.82 . 1 237 44 HIS HB2 H 3.31 . 2 238 44 HIS HB3 H 3.73 . 2 239 44 HIS HD2 H 8.76 . 1 240 44 HIS HE1 H 7.26 . 1 241 45 LYS H H 9.28 . 1 242 45 LYS HA H 4.35 . 1 243 45 LYS HB2 H 1.92 . 2 244 45 LYS HB3 H 2.03 . 2 245 45 LYS HG2 H 1.48 . 2 246 45 LYS HG3 H 1.62 . 2 247 45 LYS HD2 H 1.74 . 1 248 45 LYS HD3 H 1.74 . 1 249 45 LYS HE2 H 3.01 . 1 250 45 LYS HE3 H 3.01 . 1 251 45 LYS HZ H 7.57 . 1 252 46 GLY H H 8.65 . 1 253 46 GLY HA2 H 3.52 . 2 254 46 GLY HA3 H 4.55 . 2 255 47 ARG H H 7.94 . 1 256 47 ARG HA H 4.14 . 1 257 47 ARG HB2 H 1.80 . 2 258 47 ARG HB3 H 1.84 . 2 259 47 ARG HG2 H 1.70 . 1 260 47 ARG HG3 H 1.70 . 1 261 47 ARG HD2 H 3.26 . 1 262 47 ARG HD3 H 3.26 . 1 263 47 ARG HE H 7.24 . 1 264 48 CYS H H 8.33 . 1 265 48 CYS HA H 4.46 . 1 266 48 CYS HB2 H 2.62 . 1 267 48 CYS HB3 H 3.24 . 1 stop_ save_