BMRB

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

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"  Not known ., .-..

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

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

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

Entity Sequences (FASTA):
MjR117B: MDVEPGKFYKGVVTRIEKYG AFINLNEQVRGLLRPRDMIS LRLENLNVGDEIIVQAIDVR PEKREIDFKYIPLE

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

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MJ11981

Entities:

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

1   METASPVALGLUPROGLYLYSPHETYRLYS
2   GLYVALVALTHRARGILEGLULYSTYRGLY
3   ALAPHEILEASNLEUASNGLUGLNVALARG
4   GLYLEULEUARGPROARGASPMETILESER
5   LEUARGLEUGLUASNLEUASNVALGLYASP
6   GLUILEILEVALGLNALAILEASPVALARG
7   PROGLULYSARGGLUILEASPPHELYSTYR
8   ILEPROLEUGLU

Samples:

sample_1: MjR117B, [U-100% 13C; U-100% 15N], 1.682 mM; ammonium acetate 20 mM; sodium chloride 100 mM; sodium azide 0.02 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: MjR117B, [5% 13C; U-100% 15N], 1.226 mM; ammonium acetate 20 mM; sodium chloride 100 mM; sodium azide 0.02 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%

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

Experiments:

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

Software:

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:

PDB
GB AAB99202 ACV24909 ADC69513 AIJ05492
REF WP_012980423 WP_015791645 WP_048201674
SP Q58598