data_2948 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model ; _BMRB_accession_number 2948 _BMRB_flat_file_name bmr2948.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 Paolillo Livio . . 2 Simonetti Mario . . 3 Brakch Noureddine . . 4 D'Auria Gabriella . . 5 Saviano Michele . . 6 Dettin Monica . . 7 Rholam Mohamed . . 8 Scatturin A. . . 9 'Di Bello' C. . . 10 Cohen Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Paolillo, Livio, Simonetti, Mario, Brakch, Noureddine, D'Auria, Gabriella, Saviano, Michele, Dettin, Monica, Rholam, Mohamed, Scatturin, A., Di Bello, C., Cohen, Paul, "Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model," EMBO J. 11 (7), 2399-2405 (1992). ; _Citation_title ; Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model ; _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 Paolillo Livio . . 2 Simonetti Mario . . 3 Brakch Noureddine . . 4 D'Auria Gabriella . . 5 Saviano Michele . . 6 Dettin Monica . . 7 Rholam Mohamed . . 8 Scatturin A. . . 9 'Di Bello' C. . . 10 Cohen Paul . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 11 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2399 _Page_last 2405 _Year 1992 _Details . save_ ################################## # Molecular system description # ################################## save_system_ocytocin _Saveframe_category molecular_system _Mol_system_name ocytocin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ocytocin $ocytocin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ocytocin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ocytocin _Name_variant 'peptide 7Pro-XXXIII' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 14 _Mol_residue_sequence PLGGKRAVLDLDVR loop_ _Residue_seq_code _Residue_label 1 PRO 2 LEU 3 GLY 4 GLY 5 LYS 6 ARG 7 ALA 8 VAL 9 LEU 10 ASP 11 LEU 12 ASP 13 VAL 14 ARG stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2005-11-22 save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $ocytocin '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_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.7 . na temperature 298 . 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 TMS H . . ppm 0 . . . . . 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 ocytocin _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 PRO HB2 H 2.35 . 2 2 . 1 PRO HB3 H 1.93 . 2 3 . 1 PRO HG2 H 1.93 . 1 4 . 1 PRO HG3 H 1.93 . 1 5 . 1 PRO HD2 H 3.27 . 1 6 . 1 PRO HD3 H 3.27 . 1 7 . 2 LEU H H 8.87 . 1 8 . 2 LEU HA H 4.32 . 1 9 . 2 LEU HB2 H 1.55 . 1 10 . 2 LEU HB3 H 1.55 . 1 11 . 2 LEU HG H 1.56 . 1 12 . 2 LEU HD1 H .9 . 1 13 . 2 LEU HD2 H .9 . 1 14 . 3 GLY H H 8.44 . 1 15 . 3 GLY HA2 H 3.82 . 1 16 . 3 GLY HA3 H 3.82 . 1 17 . 4 GLY H H 8.17 . 1 18 . 4 GLY HA2 H 3.83 . 1 19 . 4 GLY HA3 H 3.83 . 1 20 . 5 LYS H H 8.15 . 1 21 . 5 LYS HA H 4.21 . 1 22 . 5 LYS HB2 H 1.71 . 1 23 . 5 LYS HB3 H 1.71 . 1 24 . 5 LYS HG2 H 1.35 . 1 25 . 5 LYS HG3 H 1.35 . 1 26 . 5 LYS HD2 H 1.58 . 1 27 . 5 LYS HD3 H 1.58 . 1 28 . 5 LYS HE2 H 2.83 . 1 29 . 5 LYS HE3 H 2.83 . 1 30 . 5 LYS HZ H 7.75 . 1 31 . 6 ARG H H 8.18 . 1 32 . 6 ARG HA H 4.21 . 1 33 . 6 ARG HB2 H 1.74 . 1 34 . 6 ARG HB3 H 1.74 . 1 35 . 6 ARG HG2 H 1.59 . 1 36 . 6 ARG HG3 H 1.59 . 1 37 . 6 ARG HD2 H 3.12 . 1 38 . 6 ARG HD3 H 3.12 . 1 39 . 6 ARG HE H 7.54 . 1 40 . 7 ALA H H 8.14 . 1 41 . 7 ALA HA H 4.21 . 1 42 . 7 ALA HB H 1.26 . 1 43 . 8 VAL H H 7.87 . 1 44 . 8 VAL HA H 4.04 . 1 45 . 8 VAL HB H 2 . 1 46 . 8 VAL HG1 H .86 . 1 47 . 8 VAL HG2 H .86 . 1 48 . 9 LEU H H 8.03 . 1 49 . 9 LEU HA H 4.3 . 1 50 . 9 LEU HB2 H 1.49 . 1 51 . 9 LEU HB3 H 1.49 . 1 52 . 9 LEU HG H 1.49 . 1 53 . 9 LEU HD1 H .85 . 1 54 . 9 LEU HD2 H .85 . 1 55 . 10 ASP H H 8.3 . 1 56 . 10 ASP HA H 4.55 . 1 57 . 10 ASP HB2 H 2.8 . 2 58 . 10 ASP HB3 H 2.61 . 2 59 . 11 LEU H H 7.93 . 1 60 . 11 LEU HA H 4.22 . 1 61 . 11 LEU HB2 H 1.5 . 1 62 . 11 LEU HB3 H 1.5 . 1 63 . 11 LEU HG H 1.5 . 1 64 . 11 LEU HD1 H .85 . 1 65 . 11 LEU HD2 H .85 . 1 66 . 12 ASP H H 8.25 . 1 67 . 12 ASP HA H 4.59 . 1 68 . 12 ASP HB2 H 2.82 . 2 69 . 12 ASP HB3 H 2.62 . 2 70 . 13 VAL H H 7.62 . 1 71 . 13 VAL HA H 4.09 . 1 72 . 13 VAL HB H 2.06 . 1 73 . 13 VAL HG1 H .85 . 1 74 . 13 VAL HG2 H .85 . 1 75 . 14 ARG H H 8.06 . 1 76 . 14 ARG HA H 4.18 . 1 77 . 14 ARG HB2 H 1.76 . 1 78 . 14 ARG HB3 H 1.76 . 1 79 . 14 ARG HG2 H 1.57 . 1 80 . 14 ARG HG3 H 1.57 . 1 81 . 14 ARG HD2 H 3.12 . 1 82 . 14 ARG HD3 H 3.12 . 1 83 . 14 ARG HE H 7.46 . 1 stop_ save_