Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15821

Title: Structure of uncharacterized protein MJ1198 from Methanocaldococcus jannaschii. Northeast Structural Genomics Target MjR117B

Deposition date: 2008-06-24 Original release date: 2008-07-15

Authors: Rossi, Paolo; Maglaqui, Melissa; Foote, Erica; Hamilton, Keith; Ciccosanti, Coleen; Xiao, Rong; Nair, Rajesh; Swapna, G.V.T.; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Structure of uncharacterized protein MJ1198 from Methanocaldococcus jannaschii. Northeast Structural Genomics Target MjR117B"  .

Assembly members:
MjR117B, polymer, 74 residues, 8674.141 Da.

Natural source:   Common Name: not available   Taxonomy ID: 2190   Superkingdom: not available   Kingdom: Methanococcus   Genus/species: jannaschii not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21(DE3)+ Magic' . . . . . 'pET 21-23C

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts346
15N chemical shifts75
1H chemical shifts566

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, MJ1198 74 residues - 8674.141 Da.

N-term M is a cloning artifact and the C-term LE is part of the purification tag



sample_1: MjR117B, [U-100% 13C; U-100% 15N], 1.682 mM; ammonium acetate' 'natural abundance; .; . mM; . mM; . uM; .; . 15821; . 15821; . 15821

sample_2: MjR117B, [5% 13C; U-100% 15N], 1.226 mM; ammonium acetate' 'natural abundance; .; . mM; . mM; . uM; .; . 15821; . 15821; . 15821

sample_conditions_1: ionic strength: 0.1 M; pH: 4.5; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aliph)sample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D SIM 13C,15N NOESYsample_1isotropicsample_conditions_1
3D ARO 13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC Stereosample_2isotropicsample_conditions_1
2D HETNOEsample_2isotropicsample_conditions_1
pseudo 2D N15 T1sample_2isotropicsample_conditions_1
pseudo 2D N15 T2 (CPMG)sample_2isotropicsample_conditions_1
2D 1H-13C HSQC CT AROsample_1isotropicsample_conditions_1


CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

TOPSPIN v2.1, Bruker Biospin - collection

RPF(AutoStructure) v2.2.1, Huang, Tejero, Powers and Montelione - validation

PSVS v1.3, Bhattacharya and Montelione - validation

Molmol, Koradi, Billeter and Wuthrich - visualization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation

MolProbity, Richardson - validation

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

GB AAB99202 ACV24909 ADC69513 AIJ05492
REF WP_012980423 WP_015791645 WP_048201674
SP Q58598

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts