data_15730 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the folded domain of intermediate IIIa of Tick Carboxypeptidase Inhibitor ; _BMRB_accession_number 15730 _BMRB_flat_file_name bmr15730.str _Entry_type original _Submission_date 2008-04-15 _Accession_date 2008-04-15 _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 Pantoja David . . 2 Blanco Francisco . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-26 update BMRB 'update entity name' 2008-07-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18558717 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pantoja-Uceda David . . 2 Arolas 'Joan L.' . . 3 Garcia Pascal . . 4 Lopez-Hernandez Eva . . 5 Padro Daniel . . 6 Aviles 'Francesc X.' . . 7 Blanco Francisco . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 47 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7066 _Page_last 7078 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'intermediate IIIa of Tick Carboxypeptidase Inhibitor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'intermediate IIIa of Tick Carboxypeptidase Inhibitor' _Molecular_mass 4060.599 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 39 _Mol_residue_sequence ; NECVSKGFGCLPQSDCPQEA RLSYGGCSTVCCDLSKLTG ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 GLU 3 CYS 4 VAL 5 SER 6 LYS 7 GLY 8 PHE 9 GLY 10 CYS 11 LEU 12 PRO 13 GLN 14 SER 15 ASP 16 CYS 17 PRO 18 GLN 19 GLU 20 ALA 21 ARG 22 LEU 23 SER 24 TYR 25 GLY 26 GLY 27 CYS 28 SER 29 THR 30 VAL 31 CYS 32 CYS 33 ASP 34 LEU 35 SER 36 LYS 37 LEU 38 THR 39 GLY 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 BMRB 15372 TCI 100.00 75 100.00 100.00 9.41e-18 BMRB 15729 TCI 100.00 75 100.00 100.00 9.41e-18 PDB 1ZLH "Crystal Structure Of The Tick Carboxypeptidase Inhibitor In Complex With Bovine Carboxypeptidase A" 100.00 75 100.00 100.00 9.41e-18 PDB 1ZLI "Crystal Structure Of The Tick Carboxypeptidase Inhibitor In Complex With Human Carboxypeptidase B" 100.00 75 100.00 100.00 9.41e-18 PDB 2JTO "Solution Structure Of Tick Carboxypeptidase Inhibitor" 100.00 75 100.00 100.00 9.41e-18 PDB 2K2X "Solution Structure Of Tick Carboxypeptidase Inhibitor At Ph 3.5" 100.00 75 100.00 100.00 9.41e-18 PDB 2K2Y "Solution Structure Of The Folded Domain Of Intermediate Iiia Of Tick Carboxypeptidase Inhibitor" 100.00 39 100.00 100.00 3.58e-18 PDB 3D4U "Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) In Complex With Tick-Derived Carboxypeptidase Inhibitor." 100.00 74 100.00 100.00 9.70e-18 PDB 3LMS "Structure Of Human Activated Thrombin-Activatable Fibrinolys Inhibitor, Tafia, In Complex With Tick-Derived Funnelin Inh Tci." 100.00 74 100.00 100.00 9.70e-18 PDB 3OSL "Structure Of Bovine Thrombin-Activatable Fibrinolysis Inhibitor In Complex With Tick Carboxypeptidase Inhibitor" 100.00 74 100.00 100.00 9.70e-18 GB AAW72225 "carboxypeptidase inhibitor precursor [Rhipicephalus bursa]" 100.00 97 100.00 100.00 4.26e-18 SP Q5EPH2 "RecName: Full=Carboxypeptidase inhibitor; AltName: Full=TCI; Flags: Precursor" 100.00 97 100.00 100.00 4.26e-18 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity . 67831 Eukaryota Metazoa Rhipecphalus bursa 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 $entity 'recombinant technology' . Escherichia coli . pBAT-4-OmpA 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 $entity 1.00 mM 'natural abundance' D2O 5 % . H2O 95 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _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' . . M pH 3.5 . pH pressure 1 . atm temperature 298 . 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_ _Experiment_label '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 entity _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 1 ASN HA H 3.969 . 1 2 1 1 ASN HB2 H 3.092 . 2 3 1 1 ASN HB3 H 2.885 . 2 4 1 1 ASN HD21 H 7.636 . 2 5 1 1 ASN HD22 H 5.676 . 2 6 2 2 GLU H H 9.059 . 1 7 2 2 GLU HA H 3.857 . 1 8 2 2 GLU HB2 H 2.110 . 2 9 2 2 GLU HB3 H 1.976 . 2 10 2 2 GLU HG3 H 2.202 . 2 11 3 3 CYS H H 8.529 . 1 12 3 3 CYS HA H 3.928 . 1 13 3 3 CYS HB2 H 3.106 . 2 14 3 3 CYS HB3 H 2.966 . 2 15 4 4 VAL H H 7.279 . 1 16 4 4 VAL HA H 3.906 . 1 17 4 4 VAL HB H 1.627 . 1 18 4 4 VAL HG1 H 0.893 . 2 19 4 4 VAL HG2 H 0.945 . 2 20 5 5 SER H H 8.564 . 1 21 5 5 SER HA H 4.120 . 1 22 5 5 SER HB2 H 3.869 . 2 23 5 5 SER HB3 H 3.869 . 2 24 6 6 LYS H H 7.586 . 1 25 6 6 LYS HA H 4.023 . 1 26 6 6 LYS HB2 H 1.755 . 2 27 6 6 LYS HB3 H 1.614 . 2 28 6 6 LYS HG2 H 1.117 . 2 29 6 6 LYS HG3 H 0.769 . 2 30 7 7 GLY H H 7.705 . 1 31 7 7 GLY HA2 H 3.757 . 2 32 7 7 GLY HA3 H 3.487 . 2 33 8 8 PHE H H 7.576 . 1 34 8 8 PHE HA H 5.050 . 1 35 8 8 PHE HB2 H 3.525 . 2 36 8 8 PHE HB3 H 2.836 . 2 37 8 8 PHE HD1 H 7.123 . 3 38 8 8 PHE HD2 H 7.123 . 3 39 8 8 PHE HE1 H 7.210 . 3 40 8 8 PHE HE2 H 7.210 . 3 41 9 9 GLY H H 7.746 . 1 42 9 9 GLY HA2 H 4.505 . 2 43 9 9 GLY HA3 H 3.688 . 2 44 10 10 CYS H H 8.493 . 1 45 10 10 CYS HA H 5.537 . 1 46 10 10 CYS HB2 H 2.974 . 2 47 10 10 CYS HB3 H 2.571 . 2 48 11 11 LEU H H 9.177 . 1 49 11 11 LEU HA H 4.896 . 1 50 11 11 LEU HB2 H 1.194 . 2 51 11 11 LEU HB3 H 1.418 . 2 52 11 11 LEU HD1 H 0.806 . 2 53 11 11 LEU HD2 H 0.938 . 2 54 11 11 LEU HG H 1.510 . 1 55 12 12 PRO HA H 4.272 . 1 56 12 12 PRO HB2 H 2.340 . 2 57 12 12 PRO HD2 H 3.788 . 2 58 12 12 PRO HD3 H 3.512 . 2 59 12 12 PRO HG2 H 1.912 . 2 60 12 12 PRO HG3 H 2.019 . 2 61 13 13 GLN H H 9.280 . 1 62 13 13 GLN HA H 3.629 . 1 63 13 13 GLN HB2 H 1.989 . 2 64 13 13 GLN HB3 H 1.937 . 2 65 13 13 GLN HG2 H 2.351 . 2 66 13 13 GLN HG3 H 2.174 . 2 67 14 14 SER H H 8.203 . 1 68 14 14 SER HA H 3.947 . 1 69 14 14 SER HB2 H 3.816 . 2 70 14 14 SER HB3 H 3.720 . 2 71 15 15 ASP H H 7.721 . 1 72 15 15 ASP HA H 4.758 . 1 73 15 15 ASP HB2 H 2.916 . 2 74 15 15 ASP HB3 H 2.501 . 2 75 16 16 CYS H H 7.288 . 1 76 16 16 CYS HA H 5.089 . 1 77 16 16 CYS HB2 H 3.082 . 2 78 16 16 CYS HB3 H 2.224 . 2 79 17 17 PRO HA H 4.378 . 1 80 17 17 PRO HB2 H 2.348 . 2 81 17 17 PRO HB3 H 2.223 . 2 82 17 17 PRO HD2 H 3.772 . 2 83 17 17 PRO HD3 H 3.411 . 2 84 17 17 PRO HG2 H 1.866 . 2 85 17 17 PRO HG3 H 1.945 . 2 86 18 18 GLN H H 8.730 . 1 87 18 18 GLN HA H 3.438 . 1 88 18 18 GLN HB2 H 1.924 . 2 89 18 18 GLN HB3 H 1.860 . 2 90 18 18 GLN HG2 H 2.292 . 2 91 18 18 GLN HG3 H 2.039 . 2 92 19 19 GLU H H 9.154 . 1 93 19 19 GLU HA H 4.099 . 1 94 19 19 GLU HB2 H 2.002 . 2 95 19 19 GLU HG2 H 2.285 . 2 96 20 20 ALA H H 8.185 . 1 97 20 20 ALA HA H 4.405 . 1 98 20 20 ALA HB H 1.395 . 1 99 21 21 ARG H H 7.038 . 1 100 21 21 ARG HA H 4.475 . 1 101 21 21 ARG HB2 H 1.714 . 2 102 21 21 ARG HB3 H 1.714 . 2 103 21 21 ARG HD2 H 3.140 . 2 104 21 21 ARG HD3 H 2.953 . 2 105 21 21 ARG HE H 6.891 . 1 106 21 21 ARG HG2 H 1.842 . 2 107 21 21 ARG HG3 H 1.400 . 2 108 22 22 LEU H H 8.400 . 1 109 22 22 LEU HA H 4.506 . 1 110 22 22 LEU HB2 H 0.915 . 2 111 22 22 LEU HB3 H 0.915 . 2 112 22 22 LEU HD1 H 0.456 . 2 113 22 22 LEU HD2 H -0.099 . 2 114 22 22 LEU HG H 1.169 . 1 115 23 23 SER H H 8.250 . 1 116 23 23 SER HA H 4.229 . 1 117 23 23 SER HB2 H 3.677 . 2 118 23 23 SER HB3 H 3.622 . 2 119 24 24 TYR H H 5.971 . 1 120 24 24 TYR HA H 4.468 . 1 121 24 24 TYR HB2 H 2.945 . 2 122 24 24 TYR HB3 H 2.887 . 2 123 24 24 TYR HD1 H 7.056 . 3 124 24 24 TYR HD2 H 7.056 . 3 125 24 24 TYR HE1 H 6.812 . 3 126 24 24 TYR HE2 H 6.812 . 3 127 25 25 GLY H H 8.867 . 1 128 25 25 GLY HA2 H 4.320 . 2 129 25 25 GLY HA3 H 3.881 . 2 130 26 26 GLY H H 8.066 . 1 131 26 26 GLY HA2 H 4.692 . 2 132 26 26 GLY HA3 H 3.455 . 2 133 27 27 CYS H H 8.929 . 1 134 27 27 CYS HA H 4.944 . 1 135 27 27 CYS HB2 H 2.660 . 2 136 27 27 CYS HB3 H 2.575 . 2 137 28 28 SER H H 9.181 . 1 138 28 28 SER HA H 4.433 . 1 139 28 28 SER HB2 H 3.851 . 2 140 28 28 SER HB3 H 3.907 . 2 141 29 29 THR H H 6.811 . 1 142 29 29 THR HA H 4.284 . 1 143 29 29 THR HB H 4.441 . 1 144 29 29 THR HG2 H 1.054 . 1 145 30 30 VAL H H 8.340 . 1 146 30 30 VAL HA H 4.444 . 1 147 30 30 VAL HB H 2.100 . 1 148 30 30 VAL HG1 H 0.954 . 2 149 30 30 VAL HG2 H 0.854 . 2 150 31 31 CYS H H 8.636 . 1 151 31 31 CYS HA H 4.955 . 1 152 31 31 CYS HB2 H 2.978 . 2 153 31 31 CYS HB3 H 2.849 . 2 154 32 32 CYS H H 9.685 . 1 155 32 32 CYS HA H 5.068 . 1 156 32 32 CYS HB2 H 3.010 . 2 157 32 32 CYS HB3 H 2.473 . 2 158 33 33 ASP H H 9.246 . 1 159 33 33 ASP HA H 4.846 . 1 160 33 33 ASP HB2 H 2.879 . 2 161 33 33 ASP HB3 H 2.149 . 2 162 34 34 LEU H H 7.981 . 1 163 34 34 LEU HA H 3.916 . 1 164 34 34 LEU HB2 H 1.872 . 2 165 34 34 LEU HB3 H 1.593 . 2 166 34 34 LEU HD1 H 0.887 . 2 167 34 34 LEU HD2 H 0.777 . 2 168 34 34 LEU HG H 1.773 . 1 169 35 35 SER H H 8.426 . 1 170 35 35 SER HA H 4.296 . 1 171 35 35 SER HB2 H 3.979 . 2 172 36 36 LYS H H 7.591 . 1 173 36 36 LYS HA H 4.294 . 1 174 36 36 LYS HB2 H 1.706 . 2 175 36 36 LYS HB3 H 1.942 . 2 176 36 36 LYS HG2 H 1.268 . 2 177 36 36 LYS HG3 H 1.395 . 2 178 37 37 LEU H H 7.356 . 1 179 37 37 LEU HA H 4.286 . 1 180 37 37 LEU HB2 H 1.745 . 2 181 37 37 LEU HB3 H 1.698 . 2 182 37 37 LEU HD1 H 0.904 . 2 183 37 37 LEU HD2 H 0.785 . 2 184 37 37 LEU HG H 1.594 . 1 185 38 38 THR H H 7.898 . 1 186 38 38 THR HA H 4.223 . 1 187 38 38 THR HB H 4.207 . 1 188 38 38 THR HG2 H 1.152 . 1 189 39 39 GLY H H 8.286 . 1 190 39 39 GLY HA2 H 3.930 . 2 stop_ save_