data_754 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-Specific 1H NMR Assignments and Secondary Structure of Porcine Motilin ; _BMRB_accession_number 754 _BMRB_flat_file_name bmr754.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Khan Nikhat . . 2 Graslund Astrid . . 3 Ehrenberg Anders . . 4 Shriver John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 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 ; Khan, Nikhat, Graslund, Astrid, Ehrenberg, Anders, Shriver, John, "Sequence-Specific 1H NMR Assignments and Secondary Structure of Porcine Motilin," Biochemistry 29, 5743-5751 (1990). ; _Citation_title 'Sequence-Specific 1H NMR Assignments and Secondary Structure of Porcine Motilin' _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 Khan Nikhat . . 2 Graslund Astrid . . 3 Ehrenberg Anders . . 4 Shriver John . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5743 _Page_last 5751 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_motilin _Saveframe_category molecular_system _Mol_system_name motilin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label motilin $motilin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_motilin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common motilin _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 22 _Mol_residue_sequence ; FVPIFTYGELQRMQEKERNK GQ ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 VAL 3 PRO 4 ILE 5 PHE 6 THR 7 TYR 8 GLY 9 GLU 10 LEU 11 GLN 12 ARG 13 MET 14 GLN 15 GLU 16 LYS 17 GLU 18 ARG 19 ASN 20 LYS 21 GLY 22 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 5454 motilin 100.00 22 100.00 100.00 4.75e-06 PDB 1LBJ "Nmr Solution Structure Of Motilin In Phospholipid Bicellar Solution" 100.00 22 100.00 100.00 4.75e-06 EMBL CAA33448 "motinlin [Homo sapiens]" 100.00 115 100.00 100.00 1.64e-06 EMBL CAA68690 "unnamed protein product [Homo sapiens]" 100.00 115 100.00 100.00 1.64e-06 GB AAA59860 "motilin [Homo sapiens]" 100.00 115 100.00 100.00 1.64e-06 GB AAH69675 "Motilin [Homo sapiens]" 100.00 115 100.00 100.00 1.57e-06 GB AAI12315 "Motilin [Homo sapiens]" 100.00 115 100.00 100.00 1.57e-06 GB AAI43982 "Unknown (protein for MGC:177516) [Homo sapiens]" 100.00 108 100.00 100.00 1.59e-06 GB AAY53628 "gastrin-related protein [Sus scrofa]" 100.00 52 100.00 100.00 3.37e-07 REF NP_001035198 "promotilin isoform 2 preproprotein [Homo sapiens]" 100.00 114 100.00 100.00 1.82e-06 REF NP_001171627 "promotilin isoform 3 preproprotein [Homo sapiens]" 100.00 108 100.00 100.00 1.69e-06 REF NP_002409 "promotilin isoform 1 preproprotein [Homo sapiens]" 100.00 115 100.00 100.00 1.64e-06 REF XP_002816813 "PREDICTED: promotilin isoform X3 [Pongo abelii]" 100.00 108 100.00 100.00 1.33e-06 REF XP_002816814 "PREDICTED: promotilin isoform X1 [Pongo abelii]" 100.00 115 100.00 100.00 1.39e-06 SP P01307 "RecName: Full=Promotilin; Contains: RecName: Full=Motilin; Contains: RecName: Full=Motilin-associated peptide; Short=MAP; Flags" 100.00 119 100.00 100.00 1.14e-06 SP P12872 "RecName: Full=Promotilin; Contains: RecName: Full=Motilin; Contains: RecName: Full=Motilin-associated peptide; Short=MAP; Flags" 100.00 115 100.00 100.00 1.64e-06 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 $motilin pig 9823 Eukaryota Metazoa Sus scrofa generic blood 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 $motilin '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 3.9 . na temperature 294 . 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 DSS 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 motilin _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 PHE HA H 4.2 . 1 2 . 1 PHE HB2 H 3.19 . 2 3 . 1 PHE HB3 H 3.11 . 2 4 . 1 PHE HD1 H 7.245 . 1 5 . 1 PHE HD2 H 7.245 . 1 6 . 1 PHE HE1 H 7.36 . 1 7 . 1 PHE HE2 H 7.36 . 1 8 . 1 PHE HZ H 7.35 . 1 9 . 2 VAL H H 7.53 . 1 10 . 2 VAL HA H 4.35 . 1 11 . 2 VAL HB H 1.99 . 1 12 . 2 VAL HG1 H .87 . 1 13 . 2 VAL HG2 H .87 . 1 14 . 3 PRO HA H 4.365 . 1 15 . 3 PRO HB2 H 2.22 . 2 16 . 3 PRO HB3 H 1.85 . 2 17 . 3 PRO HG2 H 2.016 . 1 18 . 3 PRO HG3 H 2.016 . 1 19 . 3 PRO HD2 H 3.72 . 2 20 . 3 PRO HD3 H 3.55 . 2 21 . 4 ILE H H 7.09 . 1 22 . 4 ILE HA H 3.985 . 1 23 . 4 ILE HB H 1.79 . 1 24 . 4 ILE HG12 H 1.39 . 2 25 . 4 ILE HG13 H 1.15 . 2 26 . 4 ILE HG2 H .854 . 1 27 . 4 ILE HD1 H .835 . 1 28 . 5 PHE H H 7.84 . 1 29 . 5 PHE HA H 4.61 . 1 30 . 5 PHE HB2 H 3.28 . 2 31 . 5 PHE HB3 H 3.14 . 2 32 . 5 PHE HD1 H 7.21 . 1 33 . 5 PHE HD2 H 7.21 . 1 34 . 5 PHE HE1 H 7.34 . 1 35 . 5 PHE HE2 H 7.34 . 1 36 . 5 PHE HZ H 7.37 . 1 37 . 6 THR H H 7.84 . 1 38 . 6 THR HA H 4.13 . 1 39 . 6 THR HB H 4.24 . 1 40 . 6 THR HG2 H 1.265 . 1 41 . 7 TYR H H 7.94 . 1 42 . 7 TYR HA H 4.265 . 1 43 . 7 TYR HB2 H 3.145 . 1 44 . 7 TYR HB3 H 3.145 . 1 45 . 7 TYR HD1 H 7.12 . 1 46 . 7 TYR HD2 H 7.12 . 1 47 . 7 TYR HE1 H 6.8 . 1 48 . 7 TYR HE2 H 6.8 . 1 49 . 8 GLY H H 8.215 . 1 50 . 8 GLY HA2 H 3.91 . 2 51 . 8 GLY HA3 H 3.81 . 2 52 . 9 GLU H H 7.92 . 1 53 . 9 GLU HA H 4.18 . 1 54 . 9 GLU HB2 H 2.23 . 2 55 . 9 GLU HB3 H 2.15 . 2 56 . 9 GLU HG2 H 2.4 . 1 57 . 9 GLU HG3 H 2.4 . 1 58 . 10 LEU H H 8.22 . 1 59 . 10 LEU HA H 4.18 . 1 60 . 10 LEU HB2 H 1.85 . 2 61 . 10 LEU HB3 H 1.58 . 2 62 . 10 LEU HG H 1.74 . 1 63 . 10 LEU HD1 H .89 . 2 64 . 10 LEU HD2 H .88 . 2 65 . 11 GLN H H 8.17 . 1 66 . 11 GLN HA H 3.98 . 1 67 . 11 GLN HB2 H 2.12 . 1 68 . 11 GLN HB3 H 2.12 . 1 69 . 11 GLN HG2 H 2.28 . 2 70 . 11 GLN HG3 H 2.23 . 2 71 . 11 GLN HE21 H 6.565 . 2 72 . 11 GLN HE22 H 6.46 . 2 73 . 12 ARG H H 7.95 . 1 74 . 12 ARG HA H 4.09 . 1 75 . 12 ARG HB2 H 2.06 . 2 76 . 12 ARG HB3 H 1.97 . 2 77 . 12 ARG HG2 H 1.89 . 2 78 . 12 ARG HG3 H 1.66 . 2 79 . 12 ARG HD2 H 3.245 . 1 80 . 12 ARG HD3 H 3.245 . 1 81 . 12 ARG HE H 7.27 . 1 82 . 12 ARG HH11 H 6.635 . 1 83 . 12 ARG HH12 H 6.635 . 1 84 . 12 ARG HH21 H 6.635 . 1 85 . 12 ARG HH22 H 6.635 . 1 86 . 13 MET H H 8.39 . 1 87 . 13 MET HA H 4.18 . 1 88 . 13 MET HB2 H 2.34 . 2 89 . 13 MET HB3 H 2.24 . 2 90 . 13 MET HG2 H 2.74 . 2 91 . 13 MET HG3 H 2.61 . 2 92 . 13 MET HE H 2.06 . 1 93 . 14 GLN H H 8.34 . 1 94 . 14 GLN HA H 4.05 . 1 95 . 14 GLN HB2 H 2.235 . 2 96 . 14 GLN HB3 H 2.18 . 2 97 . 14 GLN HG2 H 2.6 . 2 98 . 14 GLN HG3 H 2.355 . 2 99 . 14 GLN HE21 H 6.73 . 2 100 . 14 GLN HE22 H 6.47 . 2 101 . 15 GLU H H 8.07 . 1 102 . 15 GLU HA H 4.07 . 1 103 . 15 GLU HB2 H 2.225 . 2 104 . 15 GLU HB3 H 2.19 . 2 105 . 15 GLU HG2 H 2.495 . 2 106 . 15 GLU HG3 H 2.43 . 2 107 . 16 LYS H H 8.085 . 1 108 . 16 LYS HA H 4.135 . 1 109 . 16 LYS HB2 H 2.045 . 1 110 . 16 LYS HB3 H 2.045 . 1 111 . 16 LYS HG2 H 1.61 . 2 112 . 16 LYS HG3 H 1.53 . 2 113 . 16 LYS HD2 H 1.745 . 1 114 . 16 LYS HD3 H 1.745 . 1 115 . 16 LYS HE2 H 3.03 . 1 116 . 16 LYS HE3 H 3.03 . 1 117 . 17 GLU H H 8.16 . 1 118 . 17 GLU HA H 4.165 . 1 119 . 17 GLU HB2 H 2.19 . 2 120 . 17 GLU HB3 H 2.09 . 2 121 . 17 GLU HG2 H 2.46 . 1 122 . 17 GLU HG3 H 2.46 . 1 123 . 18 ARG H H 8.06 . 1 124 . 18 ARG HA H 4.22 . 1 125 . 18 ARG HB2 H 1.97 . 1 126 . 18 ARG HB3 H 1.97 . 1 127 . 18 ARG HG2 H 1.84 . 2 128 . 18 ARG HG3 H 1.74 . 2 129 . 18 ARG HD2 H 3.255 . 1 130 . 18 ARG HD3 H 3.255 . 1 131 . 18 ARG HE H 7.36 . 1 132 . 18 ARG HH11 H 6.67 . 1 133 . 18 ARG HH12 H 6.67 . 1 134 . 18 ARG HH21 H 6.67 . 1 135 . 18 ARG HH22 H 6.67 . 1 136 . 19 ASN H H 7.99 . 1 137 . 19 ASN HA H 4.76 . 1 138 . 19 ASN HB2 H 2.95 . 2 139 . 19 ASN HB3 H 2.83 . 2 140 . 19 ASN HD21 H 7.61 . 2 141 . 19 ASN HD22 H 6.84 . 2 142 . 20 LYS H H 8.01 . 1 143 . 20 LYS HA H 4.3 . 1 144 . 20 LYS HB2 H 1.96 . 1 145 . 20 LYS HB3 H 1.96 . 1 146 . 20 LYS HG2 H 1.55 . 1 147 . 20 LYS HG3 H 1.55 . 1 148 . 20 LYS HD2 H 1.76 . 1 149 . 20 LYS HD3 H 1.76 . 1 150 . 20 LYS HE2 H 3.08 . 1 151 . 20 LYS HE3 H 3.08 . 1 152 . 21 GLY H H 8.43 . 1 153 . 21 GLY HA2 H 4.05 . 2 154 . 21 GLY HA3 H 3.94 . 2 155 . 22 GLN H H 7.8 . 1 156 . 22 GLN HA H 4.275 . 1 157 . 22 GLN HB2 H 2.235 . 2 158 . 22 GLN HB3 H 2.02 . 2 159 . 22 GLN HG2 H 2.37 . 1 160 . 22 GLN HG3 H 2.37 . 1 161 . 22 GLN HE21 H 7.79 . 2 162 . 22 GLN HE22 H 6.63 . 2 stop_ save_