data_1204 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Features of the Protoporphyrin-Apomyoglobin Complex: A Proton NMR Spectroscopy Study ; _BMRB_accession_number 1204 _BMRB_flat_file_name bmr1204.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 Lecomte Juliette T.J. . 2 Cocco Melanie J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-17 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 ; Lecomte, Juliette T.J., Cocco, Melanie J., "Structural Features of the Protoporphyrin-Apomyoglobin Complex: A Proton NMR Spectroscopy Study," Biochemistry 29 (50), 11057-11067 (1990). ; _Citation_title ; Structural Features of the Protoporphyrin-Apomyoglobin Complex: A Proton NMR Spectroscopy Study ; _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 Lecomte Juliette T.J. . 2 Cocco Melanie J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue 50 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11057 _Page_last 11067 _Year 1990 _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 151 _Mol_residue_sequence ; XLXXXXWXXXXXXWXXVXXX XXXHXXXXLXXXFXXHXXXL XXFXXFXHXXXXXXMXXXXX XXXHXXTVLXAXXXXXXXXX XXXXXXXXLXXXXAXXHXIX XXYLXFXXXXXXXXLXXXHX XXFXXXXXXXMXXXXXXFXX XIXXXYXXXXY ; loop_ _Residue_seq_code _Residue_label 1 X 2 LEU 3 X 4 X 5 X 6 X 7 TRP 8 X 9 X 10 X 11 X 12 X 13 X 14 TRP 15 X 16 X 17 VAL 18 X 19 X 20 X 21 X 22 X 23 X 24 HIS 25 X 26 X 27 X 28 X 29 LEU 30 X 31 X 32 X 33 PHE 34 X 35 X 36 HIS 37 X 38 X 39 X 40 LEU 41 X 42 X 43 PHE 44 X 45 X 46 PHE 47 X 48 HIS 49 X 50 X 51 X 52 X 53 X 54 X 55 MET 56 X 57 X 58 X 59 X 60 X 61 X 62 X 63 X 64 HIS 65 X 66 X 67 THR 68 VAL 69 LEU 70 X 71 ALA 72 X 73 X 74 X 75 X 76 X 77 X 78 X 79 X 80 X 81 X 82 X 83 X 84 X 85 X 86 X 87 X 88 X 89 LEU 90 X 91 X 92 X 93 X 94 ALA 95 X 96 X 97 HIS 98 X 99 ILE 100 X 101 X 102 X 103 TYR 104 LEU 105 X 106 PHE 107 X 108 X 109 X 110 X 111 X 112 X 113 X 114 X 115 LEU 116 X 117 X 118 X 119 HIS 120 X 121 X 122 X 123 PHE 124 X 125 X 126 X 127 X 128 X 129 X 130 X 131 MET 132 X 133 X 134 X 135 X 136 X 137 X 138 PHE 139 X 140 X 141 X 142 ILE 143 X 144 X 145 X 146 TYR 147 X 148 X 149 X 150 X 151 TYR stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-03-03 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 elephant 9783 Eukaryota Metazoa Elephas maximus 'skeletal 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 5.7 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O/HDO H . . ppm 4.76 . . . . . $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 . 2 LEU HG H 1.13 . 1 2 . 2 LEU HD1 H .38 . 1 3 . 2 LEU HD2 H -.37 . 1 4 . 7 TRP HD1 H 6.95 . 1 5 . 7 TRP HE1 H 9.73 . 1 6 . 7 TRP HE3 H 7.45 . 1 7 . 7 TRP HZ2 H 7.16 . 1 8 . 7 TRP HZ3 H 7.07 . 1 9 . 7 TRP HH2 H 7.29 . 1 10 . 14 TRP HD1 H 6.99 . 1 11 . 14 TRP HE1 H 10.31 . 1 12 . 14 TRP HE3 H 7.13 . 1 13 . 14 TRP HZ2 H 7.49 . 1 14 . 14 TRP HZ3 H 6.71 . 1 15 . 14 TRP HH2 H 6.92 . 1 16 . 17 VAL HA H 1.5 . 1 17 . 17 VAL HB H .83 . 1 18 . 17 VAL HG1 H -.47 . 1 19 . 17 VAL HG2 H -.13 . 1 20 . 24 HIS HD2 H 6.28 . 1 21 . 24 HIS HE1 H 7.85 . 1 22 . 29 LEU HB2 H .39 . 1 23 . 29 LEU HB3 H .39 . 1 24 . 29 LEU HG H 1.01 . 1 25 . 29 LEU HD1 H -.15 . 1 26 . 29 LEU HD2 H -.41 . 1 27 . 33 PHE HD1 H 7.14 . 1 28 . 33 PHE HD2 H 7.14 . 1 29 . 33 PHE HE1 H 6.67 . 1 30 . 33 PHE HE2 H 6.67 . 1 31 . 33 PHE HZ H 5.77 . 1 32 . 36 HIS HD2 H 7.18 . 1 33 . 36 HIS HE1 H 8.17 . 1 34 . 40 LEU HG H 1.28 . 1 35 . 40 LEU HD1 H .34 . 1 36 . 40 LEU HD2 H .28 . 1 37 . 43 PHE HD1 H 7.15 . 1 38 . 43 PHE HD2 H 7.15 . 1 39 . 43 PHE HE1 H 6.22 . 1 40 . 43 PHE HE2 H 6.22 . 1 41 . 43 PHE HZ H 5.16 . 1 42 . 46 PHE HA H 5.12 . 1 43 . 46 PHE HD1 H 6.68 . 1 44 . 46 PHE HD2 H 6.68 . 1 45 . 46 PHE HE1 H 6.49 . 1 46 . 46 PHE HE2 H 6.49 . 1 47 . 46 PHE HZ H 6.29 . 1 48 . 48 HIS HD2 H 7.12 . 1 49 . 48 HIS HE1 H 8.2 . 1 50 . 55 MET HE H 1.78 . 1 51 . 64 HIS HD2 H 4.95 . 1 52 . 67 THR HA H 3.61 . 1 53 . 67 THR HB H 3.35 . 1 54 . 67 THR HG2 H .82 . 1 55 . 68 VAL HA H 2.19 . 1 56 . 68 VAL HB H .4 . 1 57 . 68 VAL HG1 H -.93 . 1 58 . 68 VAL HG2 H -3.67 . 1 59 . 69 LEU HG H 1.69 . 1 60 . 69 LEU HD1 H .58 . 1 61 . 69 LEU HD2 H .72 . 1 62 . 71 ALA HA H 4.68 . 1 63 . 71 ALA HB H 2.54 . 1 64 . 89 LEU HA H 3.6 . 1 65 . 89 LEU HB2 H 1.42 . 1 66 . 89 LEU HB3 H 1.42 . 1 67 . 89 LEU HG H .24 . 1 68 . 89 LEU HD1 H -.72 . 1 69 . 89 LEU HD2 H .65 . 1 70 . 94 ALA HA H 3.03 . 1 71 . 94 ALA HB H .85 . 1 72 . 97 HIS HE1 H 8.61 . 1 73 . 99 ILE HA H 3.98 . 1 74 . 99 ILE HB H .56 . 1 75 . 99 ILE HG12 H .32 . 2 76 . 99 ILE HG13 H .44 . 2 77 . 99 ILE HG2 H .12 . 1 78 . 99 ILE HD1 H -2.7 . 1 79 . 104 LEU HA H 5.02 . 1 80 . 104 LEU HB2 H 2.38 . 2 81 . 104 LEU HB3 H 2.82 . 2 82 . 104 LEU HG H 1.83 . 1 83 . 104 LEU HD1 H 1.12 . 1 84 . 104 LEU HD2 H .63 . 1 85 . 106 PHE HD1 H 6.84 . 1 86 . 106 PHE HD2 H 6.84 . 1 87 . 106 PHE HE1 H 7.42 . 1 88 . 106 PHE HE2 H 7.42 . 1 89 . 106 PHE HZ H 7.42 . 1 90 . 115 LEU HG H 1.75 . 1 91 . 115 LEU HD1 H .68 . 1 92 . 115 LEU HD2 H .51 . 1 93 . 119 HIS HD2 H 6.77 . 1 94 . 119 HIS HE1 H 8.41 . 1 95 . 123 PHE HD1 H 7.11 . 1 96 . 123 PHE HD2 H 7.11 . 1 97 . 123 PHE HE1 H 7.38 . 1 98 . 123 PHE HE2 H 7.38 . 1 99 . 123 PHE HZ H 7.21 . 1 100 . 131 MET HE H 2.25 . 1 101 . 138 PHE HD1 H 7.15 . 1 102 . 138 PHE HD2 H 7.15 . 1 103 . 138 PHE HE1 H 7.18 . 1 104 . 138 PHE HE2 H 7.18 . 1 105 . 138 PHE HZ H 7.06 . 1 106 . 142 ILE HB H 1.2 . 1 107 . 142 ILE HG12 H .54 . 2 108 . 142 ILE HG13 H .73 . 2 109 . 142 ILE HG2 H -.18 . 1 110 . 142 ILE HD1 H -.06 . 1 111 . 146 TYR HD1 H 6.57 . 1 112 . 146 TYR HD2 H 6.57 . 1 113 . 146 TYR HE1 H 6.44 . 1 114 . 146 TYR HE2 H 6.44 . 1 115 . 151 TYR HD1 H 6.19 . 1 116 . 151 TYR HD2 H 6.19 . 1 117 . 151 TYR HE1 H 6.09 . 1 118 . 151 TYR HE2 H 6.09 . 1 stop_ save_