data_2218
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR Study of the Molecular and Electronic Structure of the Heme Cavity of
Aplysia Metmyoglobin. Resonance Assignments Based on Isotope Labeling and Proton
Nuclear Overhauser Effect Measurements
;
_BMRB_accession_number 2218
_BMRB_flat_file_name bmr2218.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 Pande Usha . .
2 'La Mar' Gerd N. .
3 Lecomte Juliette T.J. .
4 Ascoli Franca . .
5 Brunori Maurizio . .
6 Smith Kevin M. .
7 Pandey Ravindra K. .
8 Parish Daniel W. .
9 Thanabal V. . .
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
2010-06-16 revision BMRB 'Complete natural source information'
2008-10-01 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
;
Pande, Usha, La Mar, Gerd N., Lecomte, Juliette T.J., Ascoli, Franca,
Brunori, Maurizio, Smith, Kevin M., Pandey, Ravindra K., Parish, Daniel W.,
Thanabal, V.,
"NMR Study of the Molecular and Electronic Structure of the Heme Cavity
of Aplysia Metmyoglobin. Resonance Assignments Based on Isotope Labeling
and Proton Nuclear Overhauser Effect Measurements,"
Biochemistry 25, 5638-5646 (1986).
;
_Citation_title
;
NMR Study of the Molecular and Electronic Structure of the Heme Cavity of
Aplysia Metmyoglobin. Resonance Assignments Based on Isotope Labeling and Proton
Nuclear Overhauser Effect Measurements
;
_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 Pande Usha . .
2 'La Mar' Gerd N. .
3 Lecomte Juliette T.J. .
4 Ascoli Franca . .
5 Brunori Maurizio . .
6 Smith Kevin M. .
7 Pandey Ravindra K. .
8 Parish Daniel W. .
9 Thanabal V. . .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 25
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 5638
_Page_last 5646
_Year 1986
_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 2014-10-26
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 1100 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 5.9 . 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 . 63 VAL HG1 H -27.2 . 1
2 . 63 VAL HG2 H -27.2 . 1
stop_
save_