BMRB Entry 16387

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16387
MolProbity Validation Chart

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Title:
Solution NMR Structure of denovo designed ferrodoxin fold like protein, Northeast Structural Genomics Consortium Target Target OR15
Deposition date:
2009-06-30
Original release date:
2009-08-06
Authors:
Liu, G.; Koga, N.; Jiang, J.; Xiao, R.; Ciccosanti, C.; Locke, J; Everett, J.; Nair, R.; Acton, T; Rost, B; Baker, D; Montelione, G.
Citation:

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).
PubMed: 23135467

Assembly members:

Assembly members:
OR15, polymer, 85 residues, 10066.570 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR15: MEMDIRFRGDDLEAFEKALK EMIRQARKFAGTVTYTLDGN DLEIRITGVPEQVRKELAKE AERLAKEFNITVTYTIRLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts349
15N chemical shifts84
1H chemical shifts597

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1OR151

Entities:

Entity 1, OR15 85 residues - 10066.570 Da.

1   METGLUMETASPILEARGPHEARGGLYASP
2   ASPLEUGLUALAPHEGLULYSALALEULYS
3   GLUMETILEARGGLNALAARGLYSPHEALA
4   GLYTHRVALTHRTYRTHRLEUASPGLYASN
5   ASPLEUGLUILEARGILETHRGLYVALPRO
6   GLUGLNVALARGLYSGLULEUALALYSGLU
7   ALAGLUARGLEUALALYSGLUPHEASNILE
8   THRVALTHRTYRTHRILEARGLEUGLUHIS
9   HISHISHISHISHIS

Samples:

sample_1: OR15, [U-100% 13C; U-100% 15N], 0.47 mM

sample_conditions_1: pH: 6.5; pressure: 1.0 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D simutaneous 1H, 15N, 13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, refinement, structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, refinement

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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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