BMRB Entry 25640

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25640
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
STRUCTURE OF OXIDIZED HORSE HEART CYTOCHROME C ENCAPSULATED IN REVERSE MICELLES
Deposition date:
2015-05-27
Original release date:
2015-10-26
Authors:
O'Brien, Evan; Nucci, Nathaniel; Fuglestad, Brian; Tommos, Cecilia; Wand, A. Joshua
Citation:

Citation: O'Brien, Evan; Nucci, Nathaniel; Fuglestad, Brian; Tommos, Cecilia; Wand, A. Joshua. "Defining the Apoptotic Trigger: THE INTERACTION OF CYTOCHROME c AND CARDIOLIPIN"  J. Biol. Chem. 290, 30879-30887 (2015).
PubMed: 26487716

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 11744.722 Da.
WATER, water, 18.015 Da.

Natural source:

Natural source:   Common Name: odd-toed ungulates   Taxonomy ID: 9796   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Equus caballus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJRhrsN2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GDVEKGKKIFVQKCAQCXTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNEX

Data sets:
Data typeCount
13C chemical shifts396
15N chemical shifts103
1H chemical shifts697

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2water2

Entities:

Entity 1, entity_1 105 residues - 11744.722 Da.

Normal histidines are found at residues 26 and 33, while NE2 deprotonated histidine is present at residue 18 in order to coordinate the heme residue (HEC 105). Four waters (residues 200-203) are also present in the structure.

1   GLYASPVALGLULYSGLYLYSLYSILEPHE
2   VALGLNLYSCYSALAGLNCYSHSDTHRVAL
3   GLULYSGLYGLYLYSHISLYSTHRGLYPRO
4   ASNLEUHISGLYLEUPHEGLYARGLYSTHR
5   GLYGLNALAPROGLYPHETHRTYRTHRASP
6   ALAASNLYSASNLYSGLYILETHRTRPLYS
7   GLUGLUTHRLEUMETGLUTYRLEUGLUASN
8   PROLYSLYSTYRILEPROGLYTHRLYSMET
9   ILEPHEALAGLYILELYSLYSLYSTHRGLU
10   ARGGLUASPLEUILEALATYRLEULYSLYS
11   ALATHRASNGLUHEC

Entity 2, water - 18.015 Da.

1   HOH

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.15 mM; H2O 1.5 M; sodium phosphate 25 mM; 1-decanoyl-rac-glycerol 105 mM; lauryldimethylamine-N-oxide 45 mM; hexanol 8 mM; pentane, [U-99% 2H], 8.67 M

sample_2: entity_1, [U-100% 15N], 0.15 mM; H2O 1.5 M; sodium phosphate 25 mM; 1-decanoyl-rac-glycerol 105 mM; lauryldimethylamine-N-oxide 45 mM; hexanol 8 mM; pentane, [U-99% 2H], 8.67 M

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
4D 1H-15N-13C-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

Felix, Accelrys Software Inc. - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks