data_1100 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Proton Nuclear Magnetic Resonance Study of the Molecular and Electronic Structure of the Heme Cavity in Aplysia Cyanometmyoglobin ; _BMRB_accession_number 1100 _BMRB_flat_file_name bmr1100.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 Peyton David H. . 2 'La Mar' Gerd N. . 3 Pande Usha . . 4 Ascoli Franca . . 5 Smith Kevin M. . 6 Pandey Ravindra K. . 7 Parish Daniel W. . 8 Bolognesi Martino . . 9 Brunori Maurizio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 2 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-14 revision BMRB 'Complete natural source information' 2008-09-30 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 ; Peyton, David H., La Mar, Gerd N., Pande, Usha, Ascoli, Franca, Smith, Kevin M., Pandey, Ravindra K., Parish, Daniel W., Bolognesi, Martino, Brunori, Maurizio, "Proton Nuclear Magnetic Resonance Study of the Molecular and Electronic Structure of the Heme Cavity in Aplysia Cyanometmyoglobin," Biochemistry 28, 4880-4887 (1989). ; _Citation_title ; Proton Nuclear Magnetic Resonance Study of the Molecular and Electronic Structure of the Heme Cavity in Aplysia Cyanometmyoglobin ; _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 Peyton David H. . 2 'La Mar' Gerd N. . 3 Pande Usha . . 4 Ascoli Franca . . 5 Smith Kevin M. . 6 Pandey Ravindra K. . 7 Parish Daniel W. . 8 Bolognesi Martino . . 9 Brunori Maurizio . . 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 4880 _Page_last 4887 _Year 1989 _Details . save_ ################################## # Molecular system description # ################################## save_system_myoglobin _Saveframe_category molecular_system _Mol_system_name myoglobin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label myoglobin $myoglobin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_myoglobin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common myoglobin _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 144 _Mol_residue_sequence ; XLSAAEADLAGKSWAPVFAN KNANGADFLVALFEKFPDSA NFFADFKGKSVADIKASPKL RDVSSRIFTRLNEFVNDAAN AGKMSAMLSQFAKEHVGFGV GSAQFENVRSMFPGFVASVA APPAGADAWKLFGLIIDALK AAGK ; loop_ _Residue_seq_code _Residue_label 1 SAC 2 LEU 3 SER 4 ALA 5 ALA 6 GLU 7 ALA 8 ASP 9 LEU 10 ALA 11 GLY 12 LYS 13 SER 14 TRP 15 ALA 16 PRO 17 VAL 18 PHE 19 ALA 20 ASN 21 LYS 22 ASN 23 ALA 24 ASN 25 GLY 26 ALA 27 ASP 28 PHE 29 LEU 30 VAL 31 ALA 32 LEU 33 PHE 34 GLU 35 LYS 36 PHE 37 PRO 38 ASP 39 SER 40 ALA 41 ASN 42 PHE 43 PHE 44 ALA 45 ASP 46 PHE 47 LYS 48 GLY 49 LYS 50 SER 51 VAL 52 ALA 53 ASP 54 ILE 55 LYS 56 ALA 57 SER 58 PRO 59 LYS 60 LEU 61 ARG 62 ASP 63 VAL 64 SER 65 SER 66 ARG 67 ILE 68 PHE 69 THR 70 ARG 71 LEU 72 ASN 73 GLU 74 PHE 75 VAL 76 ASN 77 ASP 78 ALA 79 ALA 80 ASN 81 ALA 82 GLY 83 LYS 84 MET 85 SER 86 ALA 87 MET 88 LEU 89 SER 90 GLN 91 PHE 92 ALA 93 LYS 94 GLU 95 HIS 96 VAL 97 GLY 98 PHE 99 GLY 100 VAL 101 GLY 102 SER 103 ALA 104 GLN 105 PHE 106 GLU 107 ASN 108 VAL 109 ARG 110 SER 111 MET 112 PHE 113 PRO 114 GLY 115 PHE 116 VAL 117 ALA 118 SER 119 VAL 120 ALA 121 ALA 122 PRO 123 PRO 124 ALA 125 GLY 126 ALA 127 ASP 128 ALA 129 TRP 130 LYS 131 LEU 132 PHE 133 GLY 134 LEU 135 ILE 136 ILE 137 ASP 138 ALA 139 LEU 140 LYS 141 ALA 142 ALA 143 GLY 144 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-27 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 1099 myoglobin 99.31 144 100.00 100.00 7.36e-93 BMRB 2218 myoglobin 99.31 144 100.00 100.00 7.36e-93 PDB 1MBA "Aplysia Limacina Myoglobin. Crystallographic Analysis At 1.6 Angstroms Resolution" 100.00 147 97.22 97.92 2.46e-87 PDB 2FAL "X-Ray Crystal Structure Of Ferric Aplysia Limacina Myoglobin In Different Liganded States" 100.00 147 97.22 97.92 2.46e-87 PDB 2FAM "X-Ray Crystal Structure Of Ferric Aplysia Limacina Myoglobin In Different Liganded States" 100.69 147 97.24 97.93 5.70e-88 PDB 3MBA "Aplysia Limacina Myoglobin. Crystallographic Analysis At 1.6 Angstroms Resolution" 100.00 147 97.22 97.92 2.46e-87 PDB 4MBA "Aplysia Limacina Myoglobin. Crystallographic Analysis At 1.6 Angstroms Resolution" 100.00 147 97.22 97.92 2.46e-87 PDB 5MBA "Binding Mode Of Azide To Ferric Aplysia Limacina Myoglobin. Crystallographic Analysis At 1.9 Angstroms Resolution" 100.00 147 97.22 97.92 2.46e-87 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SAC _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-ACETYL-SERINE _BMRB_code SAC _PDB_code SAC _Standard_residue_derivative . _Molecular_mass 147.129 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1A C1A C . 0 . ? C2A C2A C . 0 . ? OAC OAC O . 0 . ? N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? OG OG O . 0 . ? H2A1 H2A1 H . 0 . ? H2A2 H2A2 H . 0 . ? H2A3 H2A3 H . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG HG 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 SING C1A C2A ? ? DOUB C1A OAC ? ? SING C1A N ? ? SING C2A H2A1 ? ? SING C2A H2A2 ? ? SING C2A H2A3 ? ? SING N CA ? ? SING N H ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG HG ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $myoglobin 'sea hare' 6502 Eukaryota Metazoa Aplysia limacina 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 $myoglobin '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 8.9 . n/a 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 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 myoglobin _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 . 95 HIS HD2 H 18.5 . 1 2 . 95 HIS HE2 H 14.4 . 1 stop_ save_