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Biological Magnetic Resonance Data Bank


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BMRB Entry 18465

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18465
MolProbity Validation Chart

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Title: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, ROSSMANN 3x1 FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR157   PubMed: 23135467

Deposition date: 2012-05-15 Original release date: 2012-06-11

Authors: Liu, Gaohua; Koga, Rie; Koga, Nobuyasu; Xiao, Rong; Pederson, Kari; Hamilton, Keith; Kohan, Eitan; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano; Northeast Structural Genomics Consortium, NESG

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:
OR157, polymer, 110 residues, 13065.128 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):
OR157: MGSKIIVIISSDDTTLEELA RKIKDEGLEVYILLKDKDEK RLEEKIQKLKSQGFEVRKVK DDDDIDKWIDKIKKERPQLE VRKVTDEDQAKQILEDLKKK GSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts483
15N chemical shifts105
1H chemical shifts800

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR1571

Entities:

Entity 1, OR157 110 residues - 13065.128 Da.

1   METGLYSERLYSILEILEVALILEILESER
2   SERASPASPTHRTHRLEUGLUGLULEUALA
3   ARGLYSILELYSASPGLUGLYLEUGLUVAL
4   TYRILELEULEULYSASPLYSASPGLULYS
5   ARGLEUGLUGLULYSILEGLNLYSLEULYS
6   SERGLNGLYPHEGLUVALARGLYSVALLYS
7   ASPASPASPASPILEASPLYSTRPILEASP
8   LYSILELYSLYSGLUARGPROGLNLEUGLU
9   VALARGLYSVALTHRASPGLUASPGLNALA
10   LYSGLNILELEUGLUASPLEULYSLYSLYS
11   GLYSERLEUGLUHISHISHISHISHISHIS

Samples:

sample_NC: OR157.004, [U-100% 13C; U-100% 15N], 1.035 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%

sample_NC5: OR157.006, [U-100% 13C; U-100% 15N], 0.805 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%

sample_NC5_RDC: OR157.006, [U-100% 13C; U-100% 15N], 0.805 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_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
2D 1H-15N HSQCsample_NC5_RDCisotropicsample_conditions_1
3D HBHA(CO)NHsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_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

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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