data_15731 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the folded domain of intermediate IIIb of Tick Carboxypeptidase Inhibitor ; _BMRB_accession_number 15731 _BMRB_flat_file_name bmr15731.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" 202 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-27 update BMRB 'update entity/assembly 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 'in preparation' _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 'Tick Carboxypeptidase Inhibitor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'intermediate IIIb' $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 IIIb' _Molecular_mass 4173.853 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 39 _Mol_residue_sequence ; LTGCKGKGGECNPLDRQCKE LQAESASCGKGQKCCVWLH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 37 LEU 2 38 THR 3 39 GLY 4 40 CYS 5 41 LYS 6 42 GLY 7 43 LYS 8 44 GLY 9 45 GLY 10 46 GLU 11 47 CYS 12 48 ASN 13 49 PRO 14 50 LEU 15 51 ASP 16 52 ARG 17 53 GLN 18 54 CYS 19 55 LYS 20 56 GLU 21 57 LEU 22 58 GLN 23 59 ALA 24 60 GLU 25 61 SER 26 62 ALA 27 63 SER 28 64 CYS 29 65 GLY 30 66 LYS 31 67 GLY 32 68 GLN 33 69 LYS 34 70 CYS 35 71 CYS 36 72 VAL 37 73 TRP 38 74 LEU 39 75 HIS 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 1.45e-17 BMRB 15729 TCI 100.00 75 100.00 100.00 1.45e-17 PDB 1ZLH "Crystal Structure Of The Tick Carboxypeptidase Inhibitor In Complex With Bovine Carboxypeptidase A" 100.00 75 100.00 100.00 1.45e-17 PDB 1ZLI "Crystal Structure Of The Tick Carboxypeptidase Inhibitor In Complex With Human Carboxypeptidase B" 100.00 75 100.00 100.00 1.45e-17 PDB 2JTO "Solution Structure Of Tick Carboxypeptidase Inhibitor" 100.00 75 100.00 100.00 1.45e-17 PDB 2K2X "Solution Structure Of Tick Carboxypeptidase Inhibitor At Ph 3.5" 100.00 75 100.00 100.00 1.45e-17 PDB 2K2Z "Solution Structure Of The Folded Domain Of Intermediate Iiib Of Tick Carboxypeptidase Inhibitor" 100.00 39 100.00 100.00 7.79e-18 PDB 3D4U "Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) In Complex With Tick-Derived Carboxypeptidase Inhibitor." 97.44 74 100.00 100.00 2.07e-16 PDB 3LMS "Structure Of Human Activated Thrombin-Activatable Fibrinolys Inhibitor, Tafia, In Complex With Tick-Derived Funnelin Inh Tci." 97.44 74 100.00 100.00 2.07e-16 PDB 3OSL "Structure Of Bovine Thrombin-Activatable Fibrinolysis Inhibitor In Complex With Tick Carboxypeptidase Inhibitor" 97.44 74 100.00 100.00 2.07e-16 GB AAW72225 "carboxypeptidase inhibitor precursor [Rhipicephalus bursa]" 100.00 97 100.00 100.00 3.23e-18 SP Q5EPH2 "RecName: Full=Carboxypeptidase inhibitor; AltName: Full=TCI; Flags: Precursor" 100.00 97 100.00 100.00 3.23e-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 Rhipicephalus 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 'intermediate IIIb' _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 37 1 LEU H H 7.874 . 1 2 37 1 LEU HA H 4.371 . 1 3 37 1 LEU HB2 H 1.753 . 2 4 37 1 LEU HB3 H 1.597 . 2 5 37 1 LEU HD1 H 0.839 . 2 6 37 1 LEU HD2 H 0.780 . 2 7 37 1 LEU HG H 1.484 . 1 8 38 2 THR H H 7.765 . 1 9 38 2 THR HA H 4.400 . 1 10 38 2 THR HB H 4.192 . 1 11 38 2 THR HG2 H 1.156 . 1 12 39 3 GLY H H 8.375 . 1 13 39 3 GLY HA2 H 3.928 . 2 14 39 3 GLY HA3 H 3.849 . 2 15 40 4 CYS H H 7.854 . 1 16 40 4 CYS HA H 3.860 . 1 17 40 4 CYS HB2 H 2.895 . 2 18 40 4 CYS HB3 H 2.577 . 2 19 41 5 LYS H H 8.333 . 1 20 41 5 LYS HA H 4.325 . 1 21 41 5 LYS HB2 H 1.751 . 2 22 41 5 LYS HB3 H 1.751 . 2 23 41 5 LYS HG2 H 1.476 . 2 24 41 5 LYS HG3 H 1.414 . 2 25 42 6 GLY H H 7.951 . 1 26 42 6 GLY HA2 H 3.822 . 2 27 42 6 GLY HA3 H 3.655 . 2 28 43 7 LYS H H 7.203 . 1 29 43 7 LYS HA H 4.409 . 1 30 43 7 LYS HB2 H 1.991 . 2 31 43 7 LYS HB3 H 1.519 . 2 32 43 7 LYS HG2 H 1.335 . 2 33 43 7 LYS HG3 H 1.335 . 2 34 44 8 GLY H H 7.781 . 1 35 44 8 GLY HA2 H 4.154 . 2 36 44 8 GLY HA3 H 3.775 . 2 37 45 9 GLY H H 7.961 . 1 38 45 9 GLY HA2 H 4.685 . 2 39 45 9 GLY HA3 H 3.187 . 2 40 46 10 GLU H H 8.906 . 1 41 46 10 GLU HA H 4.484 . 1 42 46 10 GLU HB2 H 1.805 . 2 43 46 10 GLU HB3 H 1.711 . 2 44 46 10 GLU HG2 H 2.145 . 2 45 46 10 GLU HG3 H 2.145 . 2 46 47 11 CYS H H 9.298 . 1 47 47 11 CYS HA H 5.275 . 1 48 47 11 CYS HB2 H 2.998 . 2 49 47 11 CYS HB3 H 2.741 . 2 50 48 12 ASN H H 9.673 . 1 51 48 12 ASN HA H 5.190 . 1 52 48 12 ASN HB2 H 2.501 . 2 53 48 12 ASN HB3 H 2.337 . 2 54 48 12 ASN HD21 H 7.432 . 2 55 48 12 ASN HD22 H 6.671 . 2 56 49 13 PRO HA H 4.628 . 1 57 49 13 PRO HB2 H 2.421 . 2 58 49 13 PRO HB3 H 2.421 . 2 59 49 13 PRO HD2 H 3.845 . 2 60 49 13 PRO HD3 H 3.523 . 2 61 49 13 PRO HG2 H 2.038 . 2 62 49 13 PRO HG3 H 2.038 . 2 63 50 14 LEU H H 7.345 . 1 64 50 14 LEU HA H 3.558 . 1 65 50 14 LEU HB2 H 1.519 . 2 66 50 14 LEU HB3 H 1.519 . 2 67 50 14 LEU HD1 H 0.804 . 2 68 50 14 LEU HD2 H 0.664 . 2 69 50 14 LEU HG H 1.400 . 1 70 51 15 ASP H H 8.066 . 1 71 51 15 ASP HA H 4.342 . 1 72 51 15 ASP HB2 H 2.810 . 2 73 51 15 ASP HB3 H 2.572 . 2 74 52 16 ARG H H 7.495 . 1 75 52 16 ARG HA H 4.121 . 1 76 52 16 ARG HB2 H 1.771 . 2 77 52 16 ARG HB3 H 1.674 . 2 78 52 16 ARG HD2 H 3.182 . 2 79 52 16 ARG HD3 H 3.223 . 2 80 52 16 ARG HE H 7.233 . 1 81 52 16 ARG HG2 H 1.555 . 2 82 52 16 ARG HG3 H 1.555 . 2 83 53 17 GLN H H 8.863 . 1 84 53 17 GLN HA H 4.397 . 1 85 53 17 GLN HB2 H 1.977 . 2 86 53 17 GLN HB3 H 1.977 . 2 87 53 17 GLN HG2 H 2.332 . 2 88 53 17 GLN HG3 H 2.271 . 2 89 54 18 CYS H H 8.008 . 1 90 54 18 CYS HA H 4.689 . 1 91 54 18 CYS HB2 H 3.122 . 2 92 54 18 CYS HB3 H 2.766 . 2 93 55 19 LYS H H 8.590 . 1 94 55 19 LYS HA H 4.223 . 1 95 55 19 LYS HB2 H 1.745 . 2 96 55 19 LYS HB3 H 1.582 . 2 97 55 19 LYS HG2 H 1.275 . 2 98 55 19 LYS HG3 H 1.144 . 2 99 56 20 GLU H H 8.429 . 1 100 56 20 GLU HA H 4.649 . 1 101 56 20 GLU HB2 H 1.794 . 2 102 56 20 GLU HG2 H 2.129 . 2 103 57 21 LEU H H 8.576 . 1 104 57 21 LEU HA H 4.507 . 1 105 57 21 LEU HB2 H 1.336 . 2 106 57 21 LEU HB3 H 1.128 . 2 107 57 21 LEU HD2 H 0.715 . 2 108 57 21 LEU HG H 1.424 . 1 109 58 22 GLN H H 8.047 . 1 110 58 22 GLN HA H 3.886 . 1 111 58 22 GLN HB2 H 1.891 . 2 112 58 22 GLN HB3 H 1.788 . 2 113 58 22 GLN HE21 H 6.748 . 2 114 58 22 GLN HE22 H 7.495 . 2 115 58 22 GLN HG2 H 2.312 . 2 116 58 22 GLN HG3 H 2.006 . 2 117 59 23 ALA H H 8.842 . 1 118 59 23 ALA HA H 4.104 . 1 119 59 23 ALA HB H 1.335 . 1 120 60 24 GLU H H 7.557 . 1 121 60 24 GLU HA H 4.883 . 1 122 60 24 GLU HB2 H 1.710 . 2 123 60 24 GLU HB3 H 2.039 . 2 124 61 25 SER H H 7.902 . 1 125 61 25 SER HA H 4.043 . 1 126 62 26 ALA H H 8.866 . 1 127 62 26 ALA HA H 4.123 . 1 128 62 26 ALA HB H 1.351 . 1 129 63 27 SER H H 7.726 . 1 130 63 27 SER HA H 4.250 . 1 131 63 27 SER HB2 H 4.054 . 2 132 63 27 SER HB3 H 4.111 . 2 133 64 28 CYS H H 7.655 . 1 134 64 28 CYS HA H 4.628 . 1 135 64 28 CYS HB2 H 2.966 . 2 136 64 28 CYS HB3 H 2.777 . 2 137 65 29 GLY H H 7.414 . 1 138 65 29 GLY HA2 H 4.137 . 2 139 65 29 GLY HA3 H 3.771 . 2 140 66 30 LYS H H 8.171 . 1 141 66 30 LYS HA H 3.992 . 1 142 66 30 LYS HB2 H 1.719 . 2 143 66 30 LYS HB3 H 1.670 . 2 144 66 30 LYS HD2 H 1.616 . 2 145 66 30 LYS HD3 H 1.616 . 2 146 66 30 LYS HE2 H 2.937 . 2 147 66 30 LYS HE3 H 2.937 . 2 148 66 30 LYS HG2 H 1.326 . 2 149 66 30 LYS HG3 H 1.413 . 2 150 67 31 GLY H H 9.212 . 1 151 67 31 GLY HA2 H 4.117 . 2 152 67 31 GLY HA3 H 3.607 . 2 153 68 32 GLN H H 7.730 . 1 154 68 32 GLN HA H 5.067 . 1 155 68 32 GLN HB2 H 1.812 . 2 156 68 32 GLN HB3 H 1.634 . 2 157 68 32 GLN HE21 H 7.164 . 2 158 68 32 GLN HE22 H 6.373 . 2 159 68 32 GLN HG2 H 2.060 . 2 160 68 32 GLN HG3 H 1.770 . 2 161 69 33 LYS H H 9.347 . 1 162 69 33 LYS HA H 4.584 . 1 163 69 33 LYS HD2 H 1.313 . 2 164 69 33 LYS HD3 H 1.313 . 2 165 69 33 LYS HE2 H 3.044 . 2 166 69 33 LYS HE3 H 2.811 . 2 167 69 33 LYS HG2 H 0.862 . 2 168 69 33 LYS HG3 H 1.028 . 2 169 69 33 LYS HZ H 7.349 . 3 170 70 34 CYS H H 9.016 . 1 171 70 34 CYS HA H 4.830 . 1 172 70 34 CYS HB2 H 3.173 . 2 173 70 34 CYS HB3 H 2.446 . 2 174 71 35 CYS H H 8.741 . 1 175 71 35 CYS HA H 5.030 . 1 176 71 35 CYS HB2 H 2.692 . 2 177 71 35 CYS HB3 H 2.473 . 2 178 72 36 VAL H H 8.489 . 1 179 72 36 VAL HA H 4.113 . 1 180 72 36 VAL HB H 1.825 . 1 181 72 36 VAL HG1 H 0.744 . 2 182 73 37 TRP H H 8.597 . 1 183 73 37 TRP HA H 4.768 . 1 184 73 37 TRP HB2 H 3.225 . 2 185 73 37 TRP HB3 H 2.908 . 2 186 73 37 TRP HD1 H 7.075 . 1 187 73 37 TRP HE1 H 9.938 . 1 188 73 37 TRP HE3 H 7.564 . 1 189 73 37 TRP HH2 H 7.046 . 1 190 73 37 TRP HZ2 H 7.249 . 1 191 73 37 TRP HZ3 H 6.999 . 1 192 74 38 LEU H H 8.190 . 1 193 74 38 LEU HA H 4.257 . 1 194 74 38 LEU HB2 H 1.503 . 2 195 74 38 LEU HB3 H 1.451 . 2 196 74 38 LEU HD1 H 0.813 . 2 197 74 38 LEU HD2 H 0.749 . 2 198 75 39 HIS H H 7.863 . 1 199 75 39 HIS HA H 4.296 . 1 200 75 39 HIS HB2 H 3.021 . 2 201 75 39 HIS HB3 H 2.925 . 2 202 75 39 HIS HD1 H 6.992 . 1 stop_ save_