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 16389

Title: Solution NMR structure of protein of unknown function (NP_247299.1) from Methanococcus jannaschii   PubMed: 20944234

Deposition date: 2009-06-30 Original release date: 2011-05-19

Authors: Jaudzems, Kristaps; Mohanty, Biswaranjan; Geralt, Michael; Serrano, Pedro; Wilson, Ian; Wuthrich, Kurt

Citation: Jaudzems, Kristaps; Geralt, Michael; Serrano, Pedro; Mohanty, Biswaranjan; Horst, Reto; Pedrini, Bill; Elsliger, Marc Andre; Wilson, Ian; Wuthrich, Kurt. "NMR structure of the protein NP_247299.1: comparison with the crystal structure."  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1367-1380 (2010).

Assembly members:
NP_247299.1, polymer, 106 residues, 12109.914 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

Entity Sequences (FASTA):
NP_247299.1: GHMINMKVAISMDVDKISNS FEDCKYFLIVRIDDNEVKST KVIFNDESGKKSIVKENVNA IICKNISEENYKKFSKKIEI YHAEGDDVDKNISLFIEGEL SKISNP

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts113
1H chemical shifts781

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_247299.11

Entities:

Entity 1, NP_247299.1 106 residues - 12109.914 Da.

1   GLYHISMETILEASNMETLYSVALALAILE
2   SERMETASPVALASPLYSILESERASNSER
3   PHEGLUASPCYSLYSTYRPHELEUILEVAL
4   ARGILEASPASPASNGLUVALLYSSERTHR
5   LYSVALILEPHEASNASPGLUSERGLYLYS
6   LYSSERILEVALLYSGLUASNVALASNALA
7   ILEILECYSLYSASNILESERGLUGLUASN
8   TYRLYSLYSPHESERLYSLYSILEGLUILE
9   TYRHISALAGLUGLYASPASPVALASPLYS
10   ASNILESERLEUPHEILEGLUGLYGLULEU
11   SERLYSILESERASNPRO

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 0.9 mM; sodium phosphate' 'natural abundance; natural abundance; .; .; .

sample_conditions_1: ionic strength: 0.029 M; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D [15N,1H]-HSQCsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
3D 15N-RESOLVED [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13C(aliphatic)-RESOLVED [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13C(aromatic)-RESOLVED [1H,1H]-NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, P.GUNTERT ET AL. - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

Molmol, Koradi, Billeter and Wuthrich - data analysis

UNIO v1.0.2, T. Herrmann, F. Fiorito, J. Volk - chemical shift assignment, peak picking, structure solution

CARA v1.8.4, Keller - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAB98315
SP Q57773

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