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

Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Kohan, Eitan; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation: Koga, Nobuyasu; Tatsumi-Koga, Rie; Liu, Gaohua; Xiao, Rong; Acton, Thomas; Montelione, Gaetano; Baker, David. "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   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts455
15N chemical shifts109
1H chemical shifts748

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   METGLYLYSVALLEULEUVALILESERTHR
2   ASPTHRASNILEILESERSERVALGLNGLU
3   ARGALALYSHISASNTYRPROGLYARGGLU
4   ILEARGTHRALATHRSERSERGLNASPILE
5   ARGASPILEILELYSSERMETLYSASPASN
6   GLYLYSPROLEUVALVALPHEVALASNGLY
7   ALASERGLNASNASPVALASNGLUPHEGLN
8   ASNGLUALALYSLYSGLUGLYVALSERTYR
9   ASPVALLEULYSSERTHRASPPROGLUGLU
10   LEUTHRGLNARGVALARGGLUPHELEULYS
11   THRALAGLYSERLEUGLUHISHISHISHIS
12   HISHIS

Samples:

sample_NC: OR250.001, [U-100% 13C; U-100% 15N], 0.784 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

sample_NC5: OR250.003, [U-100% 13C; U-100% 15N], 0.854 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1

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
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