BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18380

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments and Complete 15N Relaxation Analysis of the Soluble C-terminal Domain of CcmE Heme Chaperone from Desulfovibrio vulgaris, dvCcmE(44-137). Northeast Structural Genomics Target DvR115.   PubMed: 22497251

Authors: Aramini, James; Hamilton, Keith; Rossi, Paolo; Wang, Huang; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano

Citation: Aramini, James; Hamilton, Keith; Rossi, Paolo; Ertekin, Asli; Lee, Hsiau-Wei; Lemak, Alexander; Wang, Huang; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano. "Solution NMR structure, backbone dynamics, and heme-binding properties of a novel cytochrome c maturation protein CcmE from Desulfovibrio vulgaris."  Biochemistry 51, 3705-3707 (2012).

Assembly members:
dvCcmE', polymer, 97 residues, Formula weight is not available

Natural source:   Common Name: d-proteobacteria   Taxonomy ID: 881   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Desulfovibrio vulgaris

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

Entity Sequences (FASTA):
dvCcmE': SHMATPQDKLHTVRLFGTVA ADGLTMLDGAPGVRFRLEDK DNTSKTVWVLYKGAVPDTFK PGVEVIIEGGLAPGEDTFKA RTLMTKCPSKYQKENRG

Data sets:
Data typeCount
13C chemical shifts270
15N chemical shifts93
1H chemical shifts304
heteronuclear NOE values82
T1 relaxation values82
T2 relaxation values82

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1dvCcmE'1

Entities:

Entity 1, dvCcmE' 97 residues - Formula weight is not available

N-terminal SHM remain after TEV cleavage

1   SERHISMETALATHRPROGLNASPLYSLEU
2   HISTHRVALARGLEUPHEGLYTHRVALALA
3   ALAASPGLYLEUTHRMETLEUASPGLYALA
4   PROGLYVALARGPHEARGLEUGLUASPLYS
5   ASPASNTHRSERLYSTHRVALTRPVALLEU
6   TYRLYSGLYALAVALPROASPTHRPHELYS
7   PROGLYVALGLUVALILEILEGLUGLYGLY
8   LEUALAPROGLYGLUASPTHRPHELYSALA
9   ARGTHRLEUMETTHRLYSCYSPROSERLYS
10   TYRGLNLYSGLUASNARGGLY

Samples:

DvR115.012: dvCcmE', [U-100% 13C; U-100% 15N], 1.06 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCDvR115.012isotropicsample_conditions_1
3D HNCODvR115.012isotropicsample_conditions_1
3D HN(CA)CODvR115.012isotropicsample_conditions_1
3D HNCADvR115.012isotropicsample_conditions_1
3D HN(CO)CADvR115.012isotropicsample_conditions_1
3D CBCA(CO)NHDvR115.012isotropicsample_conditions_1
3D HNCACBDvR115.012isotropicsample_conditions_1
3D HCCH-TOCSYDvR115.012isotropicsample_conditions_1
3D HCCH-COSYDvR115.012isotropicsample_conditions_1
3D CCH-TOCSYDvR115.012isotropicsample_conditions_1
2D 1H-15N hetNOEDvR115.012isotropicsample_conditions_1
2D 1H-15N T1 seriesDvR115.012isotropicsample_conditions_1
2D 1H-15N T2 seriesDvR115.012isotropicsample_conditions_1
3D HNHADvR115.012isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticDvR115.012isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - NMR data collection

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3, Goddard - data analysis, peak picking

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GB AAS95531 ABM28958 ADP86134
REF WP_010938350 WP_011792563 YP_010272