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 16357

Title: Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5

Deposition date: 2009-06-17 Original release date: 2009-07-07

Authors: Swapna, G.V.T.; Gunsalus, K.; Huang, Y.; Xiao, R.; Everett, J.; Acton, T.; Montelione, G.; NESG, NESG

Citation: Swapna, S.; Gunsalus, X.; Huang, L.; Xiao, G.; Everett, K.; Acton, A.; Montelione, G.. "Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5"  To be Published ., .-..

Assembly members:
TR5, polymer, 106 residues, 11927.964 Da.

Natural source:   Common Name: Methanothermobacter thermoautotrophicum   Taxonomy ID: 145262   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanothermobacter thermoautotrophicum

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

Entity Sequences (FASTA):
TR5: MVGRRPGGGLKDTKPVVVRL YPDEIEALKSRVPANTSMSA YIRRIILNHLEDEMVGRRPG GGLKDTKPVVVRLYPDEIEA LKSRVPANTSMSAYIRRIIL NHLEDE

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts100
1H chemical shifts750

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TR51

Entities:

Entity 1, TR5 106 residues - 11927.964 Da.

Chain B of the dimer has been numbered from 201-253 with the first residue M at 201.

1   METVALGLYARGARGPROGLYGLYGLYLEU
2   LYSASPTHRLYSPROVALVALVALARGLEU
3   TYRPROASPGLUILEGLUALALEULYSSER
4   ARGVALPROALAASNTHRSERMETSERALA
5   TYRILEARGARGILEILELEUASNHISLEU
6   GLUASPGLUMETVALGLYARGARGPROGLY
7   GLYGLYLEULYSASPTHRLYSPROVALVAL
8   VALARGLEUTYRPROASPGLUILEGLUALA
9   LEULYSSERARGVALPROALAASNTHRSER
10   METSERALATYRILEARGARGILEILELEU
11   ASNHISLEUGLUASPGLU

Samples:

sample_1: TR5-1, [U-100% 13C; U-100% 15N], 0.4 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%

sample_2: TR5-2, [U-10% 13C; U-100% 15N], 0.95 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%

sample_3: TR5-3, [U-10% 13C; U-100% 15N] + unlabeled TR5 protein, 0.4 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_3: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D- X-filtered NOESYsample_3isotropicsample_conditions_3
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
2D HNOEsample_2isotropicsample_conditions_2

Software:

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian Unity 500 MHz

Related Database Links:

PDB
DBJ BAM69652
GB AAB84973

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