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 18561

Title: Solution NMR Structure DE NOVO DESIGNED PFK fold PROTEIN, Northeast Structural Genomics Consortium (NESG) Target OR250   PubMed: 23135467

Deposition date: 2012-06-30 Original release date: 2012-06-30

Authors: Liu, Gaohua; ., Koga; ., .; ., .; ., .; 7, .; Gregory, 8; Everett, John; ., Baker; T., .

Citation: Koga, Nobuyasu; ., Tatsumi-Koga; ., .; ., .; ., .; 18561, .; , 18561. "Principles for designing ideal protein structures"  Nature 491, 222-227 (2012).

Assembly members:
OR250, polymer, 112 residues, 12671.271 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
OR250: MGKVLLVISTDTNIISSVQE RAKHNYPGREIRTATSSQDI RDIIKSMKDNGKPLVVFVNG ASQNDVNEFQNEAKKEGVSY DVLKSTDPEELTQRVREFLK TAGSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts455
1091H chemical shifts

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR2501

Entities:

Entity 1, OR250 112 residues - 12671.271 Da.

1   MET.185615.VAL.1856111.
2   ASN.1856117.GLN.1856123.
3   ASN.1856129.ILE.1856135.
4   SER.1856141.ILE.1856147.
5   ASP.1856153.VAL.1856159.
6   ALA.1856165.ASN.1856171.
7   ALA.1856177.SER.1856183.
8   SER.1856189.LEU.1856195.
9   GLU.18561101.GLY.18561107.
10   HIS.18561

Samples:

sample_NC: OR250.001, [U-100% 13C; U-100% 15N], 0.784 mM; natural abundance; .; . %; . 18561

sample_NC5: OR250.003, [U-100% 13C; U-100% 15N], 0.854 mM; natural abundance; .; . %; . 18561

sample_conditions_1: pH: 6.5; 1: . 18561; .: K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available
not availablenot available$sample_conditions_1not available
not availablesample_conditions_1not availablespectrometer_1
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot available2not available

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen, structure solution, geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis, chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18161
2LND .
. Solution Nmr Structure De Novo Designed Pfk Fold Protein, Northeast Structural Genomics Consortium (nesg) Target Or250

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