data_249 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential 1H Assignment and Secondary Structure Determination of Salmon Calcitonin in Solution ; _BMRB_accession_number 249 _BMRB_flat_file_name bmr249.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _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 Motta Andrea . . 2 'Castiglione Morelli' Maria Antoinetta . 3 Goud Nagana . . 4 Temussi Piero Andrea . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 188 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 revision BMRB 'Complete natural source information' 2008-09-24 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Motta, Andrea, Castiglione Morelli, Maria Antoinetta, Goud, Nagana, Temussi, Piero Andrea, "Sequential 1H Assignment and Secondary Structure Determination of Salmon Calcitonin in Solution," Biochemistry 28, 7996-8002 (1989). ; _Citation_title ; Sequential 1H Assignment and Secondary Structure Determination of Salmon Calcitonin in Solution ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Motta Andrea . . 2 'Castiglione Morelli' Maria Antoinetta . 3 Goud Nagana . . 4 Temussi Piero Andrea . stop_ _Journal_abbreviation Biochemistry _Journal_volume 28 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7996 _Page_last 8002 _Year 1989 _Details . save_ ################################## # Molecular system description # ################################## save_system_calcitonin_C _Saveframe_category molecular_system _Mol_system_name 'calcitonin C' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'calcitonin C' $calcitonin_C stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_calcitonin_C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'calcitonin C' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; CSNLSTCVLGKLSQELHKLQ TYPRTNTGSGTX ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 SER 3 ASN 4 LEU 5 SER 6 THR 7 CYS 8 VAL 9 LEU 10 GLY 11 LYS 12 LEU 13 SER 14 GLN 15 GLU 16 LEU 17 HIS 18 LYS 19 LEU 20 GLN 21 THR 22 TYR 23 PRO 24 ARG 25 THR 26 ASN 27 THR 28 GLY 29 SER 30 GLY 31 THR 32 LPD stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1481 "calcitonin C" 96.88 32 100.00 100.00 5.24e-12 BMRB 1482 "calcitonin C" 96.88 32 100.00 100.00 5.24e-12 BMRB 1643 "calcitonin C" 96.88 32 100.00 100.00 5.24e-12 BMRB 2012 "calcitonin C" 96.88 32 100.00 100.00 5.24e-12 BMRB 2047 "calcitonin C" 96.88 32 100.00 100.00 5.24e-12 BMRB 2048 "calcitonin C" 96.88 32 100.00 100.00 5.24e-12 PDB 2GLH "Solution Conformation Of Salmon Calcitonin In Sodium Dodecyl Sulfate Micelles" 96.88 33 100.00 100.00 5.83e-12 DBJ BAA00281 "calcitonin I precursor SCT-Gly [synthetic construct]" 96.88 34 100.00 100.00 5.35e-12 DBJ BAC57416 "salmon calcitonin-Ia precursor [Oncorhynchus mykiss]" 96.88 136 100.00 100.00 3.04e-12 DBJ BAC57417 "salmon calcitonin-Ib precursor [Oncorhynchus mykiss]" 96.88 136 100.00 100.00 2.98e-12 EMBL CAA54988 "calcitonin [Oncorhynchus gorbuscha]" 96.88 56 100.00 100.00 3.69e-12 EMBL CAA68734 "unnamed protein product [Oncorhynchus keta]" 96.88 136 100.00 100.00 3.04e-12 EMBL CDQ71353 "unnamed protein product [Oncorhynchus mykiss]" 96.88 136 100.00 100.00 2.98e-12 EMBL CDQ78480 "unnamed protein product [Oncorhynchus mykiss]" 96.88 136 100.00 100.00 3.04e-12 GB AAB22592 "calcitonin, partial [Oncorhynchus sp.]" 96.88 62 100.00 100.00 3.45e-12 GB AAD14151 "calcitonin I, partial [Oncorhynchus gorbuscha]" 96.88 59 100.00 100.00 3.51e-12 GB AAD14152 "calcitonin I, partial [Oncorhynchus gorbuscha]" 96.88 59 100.00 100.00 3.51e-12 GB AAL99993 "calcitonin [Oncorhynchus gorbuscha]" 96.88 32 100.00 100.00 5.77e-12 GB AAL99995 "calcitonin [Oncorhynchus sp. FY-02]" 96.88 32 100.00 100.00 5.77e-12 PIR TCON "calcitonin 1 precursor - salmon" 96.88 136 100.00 100.00 3.04e-12 REF NP_001117685 "salmon calcitonin-Ib precursor [Oncorhynchus mykiss]" 96.88 136 100.00 100.00 2.98e-12 REF NP_001118059 "salmon calcitonin-Ia precursor [Oncorhynchus mykiss]" 96.88 136 100.00 100.00 3.04e-12 REF NP_001135058 "Calcitonin-1 precursor [Salmo salar]" 96.88 143 100.00 100.00 4.14e-12 REF XP_010888827 "PREDICTED: calcitonin-1 [Esox lucius]" 96.88 140 100.00 100.00 3.05e-12 REF XP_013982623 "PREDICTED: calcitonin-1 isoform X1 [Salmo salar]" 96.88 136 100.00 100.00 3.04e-12 SP P01263 "RecName: Full=Calcitonin-1; Flags: Precursor" 96.88 136 100.00 100.00 3.04e-12 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_LPD _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common L-PROLINAMIDE _BMRB_code LPD _PDB_code LPD _Standard_residue_derivative . _Molecular_mass 114.146 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons O O O . 0 . ? C C C . 0 . ? N2 N2 N . 0 . ? CA CA C . 0 . ? N N N . 0 . ? CD CD C . 0 . ? CG CG C . 0 . ? CB CB C . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? HA HA H . 0 . ? H H H . 0 . ? HD3 HD3 H . 0 . ? HD2 HD2 H . 0 . ? HG3 HG3 H . 0 . ? HG2 HG2 H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB O C ? ? SING C N2 ? ? SING C CA ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING CA N ? ? SING CA CB ? ? SING CA HA ? ? SING N CD ? ? SING N H ? ? SING CD CG ? ? SING CD HD3 ? ? SING CD HD2 ? ? SING CG CB ? ? SING CG HG3 ? ? SING CG HG2 ? ? SING CB HB2 ? ? SING CB HB3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Tissue $calcitonin_C salmon 8025 Eukaryota Metazoa Oncorhynchus sp. generic 'ultimobrancial body' 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 $calcitonin_C 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . n/a temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TMS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'calcitonin C' _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 CYS HA H 4.11 . 1 2 . 1 CYS HB2 H 3.01 . 2 3 . 1 CYS HB3 H 3.3 . 2 4 . 2 SER H H 7.91 . 1 5 . 2 SER HA H 4.13 . 1 6 . 2 SER HB2 H 3.62 . 2 7 . 2 SER HB3 H 3.69 . 2 8 . 2 SER HG H 5.29 . 1 9 . 3 ASN H H 7.61 . 1 10 . 3 ASN HA H 4.43 . 1 11 . 3 ASN HB2 H 2.62 . 2 12 . 3 ASN HB3 H 2.73 . 2 13 . 3 ASN HD21 H 6.98 . 2 14 . 3 ASN HD22 H 7.18 . 2 15 . 4 LEU H H 8.25 . 1 16 . 4 LEU HA H 4.3 . 1 17 . 4 LEU HB2 H 1.46 . 1 18 . 4 LEU HB3 H 1.46 . 1 19 . 4 LEU HG H 1.6 . 1 20 . 4 LEU HD1 H .81 . 2 21 . 4 LEU HD2 H .85 . 2 22 . 5 SER H H 7.76 . 1 23 . 5 SER HA H 4.28 . 1 24 . 5 SER HB2 H 3.58 . 1 25 . 5 SER HB3 H 3.58 . 1 26 . 5 SER HG H 4.98 . 1 27 . 6 THR H H 7.6 . 1 28 . 6 THR HA H 4.18 . 1 29 . 6 THR HB H 3.9 . 1 30 . 6 THR HG1 H 4.9 . 1 31 . 6 THR HG2 H .96 . 1 32 . 7 CYS H H 7.91 . 1 33 . 7 CYS HA H 4.5 . 1 34 . 7 CYS HB2 H 3.05 . 2 35 . 7 CYS HB3 H 3.21 . 2 36 . 8 VAL H H 7.72 . 1 37 . 8 VAL HA H 4.06 . 1 38 . 8 VAL HB H 1.99 . 1 39 . 8 VAL HG1 H .83 . 1 40 . 8 VAL HG2 H .83 . 1 41 . 9 LEU H H 8 . 1 42 . 9 LEU HA H 4.22 . 1 43 . 9 LEU HB2 H 1.48 . 1 44 . 9 LEU HB3 H 1.48 . 1 45 . 9 LEU HG H 1.6 . 1 46 . 9 LEU HD1 H .81 . 2 47 . 9 LEU HD2 H .85 . 2 48 . 10 GLY H H 8.06 . 1 49 . 10 GLY HA2 H 3.63 . 2 50 . 10 GLY HA3 H 3.79 . 2 51 . 11 LYS H H 8.08 . 1 52 . 11 LYS HA H 4.35 . 1 53 . 11 LYS HB2 H 1.52 . 1 54 . 11 LYS HB3 H 1.52 . 1 55 . 11 LYS HG2 H 1.28 . 1 56 . 11 LYS HG3 H 1.28 . 1 57 . 11 LYS HD2 H 1.48 . 1 58 . 11 LYS HD3 H 1.48 . 1 59 . 11 LYS HE2 H 2.74 . 1 60 . 11 LYS HE3 H 2.74 . 1 61 . 11 LYS HZ H 7.64 . 1 62 . 12 LEU H H 7.74 . 1 63 . 12 LEU HA H 4.09 . 1 64 . 12 LEU HB2 H 1.48 . 1 65 . 12 LEU HB3 H 1.48 . 1 66 . 12 LEU HG H 1.6 . 1 67 . 12 LEU HD1 H .81 . 2 68 . 12 LEU HD2 H .85 . 2 69 . 13 SER H H 8.89 . 1 70 . 13 SER HA H 4.34 . 1 71 . 13 SER HB2 H 3.62 . 2 72 . 13 SER HB3 H 3.76 . 2 73 . 14 GLN H H 7.88 . 1 74 . 14 GLN HA H 4.21 . 1 75 . 14 GLN HB2 H 1.78 . 2 76 . 14 GLN HB3 H 1.88 . 2 77 . 14 GLN HG2 H 1.99 . 2 78 . 14 GLN HG3 H 2.07 . 2 79 . 14 GLN HE21 H 6.82 . 2 80 . 14 GLN HE22 H 7.27 . 2 81 . 15 GLU H H 8.16 . 1 82 . 15 GLU HA H 4.13 . 1 83 . 15 GLU HB2 H 1.79 . 2 84 . 15 GLU HB3 H 1.91 . 2 85 . 15 GLU HG2 H 2.14 . 1 86 . 15 GLU HG3 H 2.14 . 1 87 . 16 LEU H H 7.49 . 1 88 . 16 LEU HA H 4.11 . 1 89 . 16 LEU HB2 H 1.56 . 1 90 . 16 LEU HB3 H 1.56 . 1 91 . 16 LEU HG H 1.55 . 1 92 . 16 LEU HD1 H .82 . 2 93 . 16 LEU HD2 H .88 . 2 94 . 17 HIS H H 7.82 . 1 95 . 17 HIS HA H 4.48 . 1 96 . 17 HIS HB2 H 3.03 . 2 97 . 17 HIS HB3 H 3.2 . 2 98 . 17 HIS HD2 H 7.35 . 1 99 . 17 HIS HE1 H 8.35 . 1 100 . 17 HIS HE2 H 14.11 . 1 101 . 18 LYS H H 7.95 . 1 102 . 18 LYS HA H 4.18 . 1 103 . 18 LYS HB2 H 1.52 . 1 104 . 18 LYS HB3 H 1.52 . 1 105 . 18 LYS HG2 H 1.28 . 1 106 . 18 LYS HG3 H 1.28 . 1 107 . 18 LYS HD2 H 1.31 . 1 108 . 18 LYS HD3 H 1.31 . 1 109 . 18 LYS HE2 H 2.74 . 1 110 . 18 LYS HE3 H 2.74 . 1 111 . 18 LYS HZ H 7.64 . 1 112 . 19 LEU H H 7.89 . 1 113 . 19 LEU HA H 4.2 . 1 114 . 19 LEU HB2 H 1.52 . 1 115 . 19 LEU HB3 H 1.52 . 1 116 . 19 LEU HG H 1.48 . 1 117 . 19 LEU HD1 H .81 . 2 118 . 19 LEU HD2 H .85 . 2 119 . 20 GLN H H 8 . 1 120 . 20 GLN HA H 4.22 . 1 121 . 20 GLN HB2 H 1.88 . 2 122 . 20 GLN HB3 H 1.78 . 2 123 . 20 GLN HG2 H 1.99 . 2 124 . 20 GLN HG3 H 2.07 . 2 125 . 20 GLN HE21 H 6.82 . 2 126 . 20 GLN HE22 H 7.27 . 2 127 . 21 THR H H 8.03 . 1 128 . 21 THR HA H 4.27 . 1 129 . 21 THR HB H 3.98 . 1 130 . 21 THR HG1 H 4.95 . 1 131 . 21 THR HG2 H 1.02 . 1 132 . 22 TYR H H 7.94 . 1 133 . 22 TYR HA H 4.58 . 1 134 . 22 TYR HB2 H 2.65 . 2 135 . 22 TYR HB3 H 2.86 . 2 136 . 22 TYR HD1 H 7.07 . 1 137 . 22 TYR HD2 H 7.07 . 1 138 . 22 TYR HE1 H 6.63 . 1 139 . 22 TYR HE2 H 6.63 . 1 140 . 22 TYR HH H 9.21 . 1 141 . 23 PRO HA H 4.34 . 1 142 . 23 PRO HB2 H 2.07 . 2 143 . 23 PRO HB3 H 2.02 . 2 144 . 23 PRO HG2 H 1.73 . 2 145 . 23 PRO HG3 H 1.86 . 2 146 . 23 PRO HD2 H 3.57 . 2 147 . 23 PRO HD3 H 3.75 . 2 148 . 24 ARG H H 7.96 . 1 149 . 24 ARG HA H 4.28 . 1 150 . 24 ARG HB2 H 1.53 . 1 151 . 24 ARG HB3 H 1.53 . 1 152 . 24 ARG HG2 H 1.52 . 1 153 . 24 ARG HG3 H 1.52 . 1 154 . 24 ARG HD2 H 3.11 . 1 155 . 24 ARG HD3 H 3.11 . 1 156 . 24 ARG HE H 7.45 . 1 157 . 25 THR H H 8.03 . 1 158 . 25 THR HA H 4.27 . 1 159 . 25 THR HB H 4.13 . 1 160 . 25 THR HG1 H 4.94 . 1 161 . 25 THR HG2 H 1.02 . 1 162 . 26 ASN H H 8.14 . 1 163 . 26 ASN HA H 4.64 . 1 164 . 26 ASN HB2 H 2.45 . 2 165 . 26 ASN HB3 H 2.59 . 2 166 . 26 ASN HD21 H 7.02 . 2 167 . 26 ASN HD22 H 7.49 . 2 168 . 27 THR H H 7.74 . 1 169 . 27 THR HA H 4.13 . 1 170 . 27 THR HB H 4.04 . 1 171 . 27 THR HG1 H 4.93 . 1 172 . 27 THR HG2 H 1.04 . 1 173 . 28 GLY H H 8.09 . 1 174 . 28 GLY HA2 H 3.6 . 2 175 . 28 GLY HA3 H 3.76 . 2 176 . 29 SER H H 7.95 . 1 177 . 29 SER HA H 4.28 . 1 178 . 29 SER HB2 H 3.58 . 1 179 . 29 SER HB3 H 3.58 . 1 180 . 29 SER HG H 4.98 . 1 181 . 30 GLY H H 8.17 . 1 182 . 30 GLY HA2 H 3.62 . 2 183 . 30 GLY HA3 H 3.71 . 2 184 . 31 THR H H 7.9 . 1 185 . 31 THR HA H 4.49 . 1 186 . 31 THR HB H 3.87 . 1 187 . 31 THR HG1 H 4.94 . 1 188 . 31 THR HG2 H 1.1 . 1 stop_ save_