data_477 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411 ; _BMRB_accession_number 477 _BMRB_flat_file_name bmr477.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Mayo Kevin H. . 2 Burke Carl . . 3 Lindon J. N. . 4 Kloczewiak Marek A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 62 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' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Mayo, Kevin H., Burke, Carl, Lindon, J.N., Kloczewiak, Marek A., "1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411," Biochemistry 29, 3277-3286 (1990). ; _Citation_title ; 1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411 ; _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 Mayo Kevin H. . 2 Burke Carl . . 3 Lindon J. N. . 4 Kloczewiak Marek A. . 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 3277 _Page_last 3286 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_fibrinogen _Saveframe_category molecular_system _Mol_system_name fibrinogen _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label fibrinogen $fibrinogen stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_fibrinogen _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common fibrinogen _Name_variant 'gamma-chain C-terminal residues 400-411' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence HHLGGAKQAGDV loop_ _Residue_seq_code _Residue_label 1 HIS 2 HIS 3 LEU 4 GLY 5 GLY 6 ALA 7 LYS 8 GLN 9 ALA 10 GLY 11 ASP 12 VAL stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2003-06-19 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $fibrinogen human . . . Homo sapiens generic 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 $fibrinogen '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 3 . na temperature 303 . 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 TSP 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 fibrinogen _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 HIS H H 8.86 . 1 2 . 1 HIS HA H 4.77 . 1 3 . 1 HIS HB2 H 3.31 . 1 4 . 1 HIS HB3 H 3.31 . 1 5 . 1 HIS HD2 H 7.4 . 1 6 . 1 HIS HE1 H 8.75 . 1 7 . 2 HIS H H 8.83 . 1 8 . 2 HIS HA H 4.86 . 1 9 . 2 HIS HB2 H 3.25 . 1 10 . 2 HIS HB3 H 3.25 . 1 11 . 2 HIS HD2 H 7.45 . 1 12 . 2 HIS HE1 H 8.74 . 1 13 . 3 LEU H H 8.61 . 1 14 . 3 LEU HA H 4.72 . 1 15 . 3 LEU HB2 H 1.8 . 2 16 . 3 LEU HB3 H 1.74 . 2 17 . 3 LEU HG H 1.74 . 1 18 . 3 LEU HD1 H 1.05 . 2 19 . 3 LEU HD2 H .9 . 2 20 . 4 GLY H H 8.49 . 1 21 . 4 GLY HA2 H 4.1 . 1 22 . 4 GLY HA3 H 4.1 . 1 23 . 5 GLY H H 8.4 . 1 24 . 5 GLY HA2 H 4.12 . 1 25 . 5 GLY HA3 H 4.12 . 1 26 . 6 ALA H H 8.48 . 1 27 . 6 ALA HA H 4.45 . 1 28 . 6 ALA HB H 1.55 . 1 29 . 7 LYS H H 8.46 . 1 30 . 7 LYS HA H 4.43 . 1 31 . 7 LYS HB2 H 1.98 . 2 32 . 7 LYS HB3 H 1.92 . 2 33 . 7 LYS HG2 H 1.59 . 1 34 . 7 LYS HG3 H 1.59 . 1 35 . 7 LYS HD2 H 1.84 . 1 36 . 7 LYS HD3 H 1.84 . 1 37 . 7 LYS HE2 H 3.17 . 1 38 . 7 LYS HE3 H 3.17 . 1 39 . 7 LYS HZ H 7.71 . 1 40 . 8 GLN H H 8.45 . 1 41 . 8 GLN HA H 4.48 . 1 42 . 8 GLN HB2 H 2.25 . 2 43 . 8 GLN HB3 H 2.13 . 2 44 . 8 GLN HG2 H 2.49 . 1 45 . 8 GLN HG3 H 2.49 . 1 46 . 8 GLN HE21 H 7.65 . 2 47 . 8 GLN HE22 H 6.98 . 2 48 . 9 ALA H H 8.35 . 1 49 . 9 ALA HA H 4.47 . 1 50 . 9 ALA HB H 1.52 . 1 51 . 10 GLY H H 8.59 . 1 52 . 10 GLY HA2 H 4.12 . 1 53 . 10 GLY HA3 H 4.12 . 1 54 . 11 ASP H H 8.36 . 1 55 . 11 ASP HA H 4.91 . 1 56 . 11 ASP HB2 H 3.04 . 2 57 . 11 ASP HB3 H 2.94 . 2 58 . 12 VAL H H 8.09 . 1 59 . 12 VAL HA H 4.39 . 1 60 . 12 VAL HB H 2.06 . 1 61 . 12 VAL HG1 H 1.05 . 1 62 . 12 VAL HG2 H 1.05 . 1 stop_ save_