data_81 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR of a Peptic Peptide Spanning the Triprolyl Sequence in Myelin Basic Protein ; _BMRB_accession_number 81 _BMRB_flat_file_name bmr81.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 Nygaard Erik . . 2 Mendz George L. . 3 Moore Walter J. . 4 Martenson Russell E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 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 ; Nygaard, Erik, Mendz, George L., Moore, Walter J., Martenson, Russell E., "NMR of a Peptic Peptide Spanning the Triprolyl Sequence in Myelin Basic Protein," Biochemistry 23, 4003-4010 (1984). ; _Citation_title 'NMR of a Peptic Peptide Spanning the Triprolyl Sequence in Myelin Basic Protein' _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 Nygaard Erik . . 2 Mendz George L. . 3 Moore Walter J. . 4 Martenson Russell E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 23 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4003 _Page_last 4010 _Year 1984 _Details . save_ ################################## # Molecular system description # ################################## save_system_myelin_basic_protein _Saveframe_category molecular_system _Mol_system_name 'myelin basic protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'myelin basic protein' $myelin_basic_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_myelin_basic_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'myelin basic protein' _Name_variant 'residues 91-112' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 22 _Mol_residue_sequence ; FKNIVTPRXPPPSQGKGXGT VL ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 LYS 3 ASN 4 ILE 5 VAL 6 THR 7 PRO 8 ARG 9 X 10 PRO 11 PRO 12 PRO 13 SER 14 GLN 15 GLY 16 LYS 17 GLY 18 X 19 GLY 20 THR 21 VAL 22 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2005-12-09 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 $myelin_basic_protein 'domestic rabbit' 9986 Eukaryota Metazoa Oryctolagus cuniculus generic muscle 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 $myelin_basic_protein '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 4.71 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C . . ppm 0 . . . . . $entry_citation $entry_citation 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 'myelin basic protein' _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 4.28 . 1 2 . 1 PHE HB2 H 3.158 . 2 3 . 1 PHE HB3 H 3.281 . 2 4 . 1 PHE HD1 H 7.294 . 1 5 . 1 PHE HD2 H 7.294 . 1 6 . 1 PHE HE1 H 7.413 . 1 7 . 1 PHE HE2 H 7.413 . 1 8 . 1 PHE HZ H 7.413 . 1 9 . 2 LYS HA H 4.35 . 1 10 . 2 LYS HB2 H 1.779 . 2 11 . 2 LYS HB3 H 1.73 . 2 12 . 2 LYS HG2 H 1.398 . 2 13 . 2 LYS HG3 H 1.43 . 2 14 . 2 LYS HD2 H 1.712 . 1 15 . 2 LYS HD3 H 1.712 . 1 16 . 2 LYS HE2 H 3.016 . 1 17 . 2 LYS HE3 H 3.016 . 1 18 . 3 ASN HA H 4.693 . 1 19 . 3 ASN HB2 H 2.745 . 2 20 . 3 ASN HB3 H 2.842 . 2 21 . 4 ILE HA H 4.211 . 1 22 . 4 ILE HB H 1.864 . 1 23 . 4 ILE HG12 H 1.171 . 2 24 . 4 ILE HG13 H 1.464 . 2 25 . 4 ILE HG2 H .888 . 1 26 . 4 ILE HD1 H .855 . 1 27 . 5 VAL HA H 4.139 . 1 28 . 5 VAL HB H 2.121 . 1 29 . 5 VAL HG1 H .848 . 2 30 . 5 VAL HG2 H .906 . 2 31 . 6 THR HA H 4.581 . 1 32 . 6 THR HB H 4.111 . 1 33 . 6 THR HG2 H 1.253 . 1 34 . 7 PRO HA H 4.707 . 1 35 . 7 PRO HB2 H 1.926 . 2 36 . 7 PRO HB3 H 2.387 . 2 37 . 7 PRO HG2 H 2.06 . 1 38 . 7 PRO HG3 H 2.06 . 1 39 . 7 PRO HD2 H 3.649 . 2 40 . 7 PRO HD3 H 3.839 . 2 41 . 8 ARG HA H 4.35 . 1 42 . 8 ARG HB2 H 1.769 . 2 43 . 8 ARG HB3 H 1.91 . 2 44 . 8 ARG HG2 H 1.681 . 1 45 . 8 ARG HG3 H 1.681 . 1 46 . 8 ARG HD2 H 3.208 . 1 47 . 8 ARG HD3 H 3.208 . 1 48 . 10 PRO HA H 4.455 . 1 49 . 10 PRO HB2 H 1.978 . 2 50 . 10 PRO HB3 H 2.339 . 2 51 . 10 PRO HG2 H 2.06 . 1 52 . 10 PRO HG3 H 2.06 . 1 53 . 10 PRO HD2 H 3.912 . 2 54 . 10 PRO HD3 H 3.737 . 2 55 . 11 PRO HA H 4.386 . 1 56 . 11 PRO HB2 H 2.003 . 2 57 . 11 PRO HB3 H 2.158 . 2 58 . 11 PRO HG2 H 2.06 . 1 59 . 11 PRO HG3 H 2.06 . 1 60 . 11 PRO HD2 H 3.649 . 2 61 . 11 PRO HD3 H 3.737 . 2 62 . 12 PRO HA H 4.404 . 1 63 . 12 PRO HB2 H 1.978 . 2 64 . 12 PRO HB3 H 2.312 . 2 65 . 12 PRO HG2 H 2.06 . 1 66 . 12 PRO HG3 H 2.06 . 1 67 . 12 PRO HD2 H 3.839 . 2 68 . 12 PRO HD3 H 3.912 . 2 69 . 13 SER HA H 4.43 . 1 70 . 13 SER HB2 H 3.896 . 2 71 . 13 SER HB3 H 3.891 . 2 72 . 14 GLN HA H 4.412 . 1 73 . 14 GLN HB2 H 2.092 . 1 74 . 14 GLN HB3 H 2.092 . 1 75 . 14 GLN HG2 H 2.395 . 1 76 . 14 GLN HG3 H 2.395 . 1 77 . 15 GLY HA2 H 3.987 . 1 78 . 15 GLY HA3 H 3.987 . 1 79 . 16 LYS HA H 4.35 . 1 80 . 16 LYS HB2 H 1.73 . 2 81 . 16 LYS HB3 H 1.779 . 2 82 . 16 LYS HG2 H 1.398 . 2 83 . 16 LYS HG3 H 1.43 . 2 84 . 16 LYS HD2 H 1.712 . 1 85 . 16 LYS HD3 H 1.712 . 1 86 . 16 LYS HE2 H 2.995 . 1 87 . 17 GLY HA2 H 3.987 . 1 88 . 17 GLY HA3 H 3.987 . 1 89 . 19 GLY HA2 H 4.019 . 1 90 . 19 GLY HA3 H 4.019 . 1 91 . 20 THR HA H 4.342 . 1 92 . 20 THR HB H 4.166 . 1 93 . 20 THR HG2 H 1.184 . 1 94 . 21 VAL HA H 4.166 . 1 95 . 21 VAL HB H 2.052 . 1 96 . 21 VAL HG1 H .948 . 2 97 . 21 VAL HG2 H .954 . 2 98 . 22 LEU HA H 4.33 . 1 99 . 22 LEU HB2 H 1.684 . 1 100 . 22 LEU HB3 H 1.684 . 1 101 . 22 LEU HG H 1.638 . 1 102 . 22 LEU HD1 H .878 . 2 103 . 22 LEU HD2 H .934 . 2 stop_ save_