BMRB Entry 18558

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18558
MolProbity Validation Chart

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Title:
Solution NMR Structure de novo designed rossmann 2x2 fold protein, Northeast Structural Genomics Consortium (NESG) Target OR16
Deposition date:
2012-06-29
Original release date:
2012-07-31
Authors:
Liu, Gaohua; Koga, Rie; Koga, Nobuyasu; Xiao, Rong; Pederson, Kari; Hamilton, Keith; Ciccosanti, Colleen; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano
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:
OR16, polymer, 110 residues, 13078.123 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: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR16: MLLYVLIISNDKKLIEEARK MAEKANLELRTVKTEDELKK YLEEFRKESQNIKVLILVSN DEELDKAKELAQKMEIDVRT RKVTSPDEAKRWIKEFSEEG GSLEHHHHHH

Data typeCount
residual dipolar couplings170

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1OR161

Entities:

Entity 1, OR16 110 residues - 13078.123 Da.

1   METLEULEUTYRVALLEUILEILESERASN
2   ASPLYSLYSLEUILEGLUGLUALAARGLYS
3   METALAGLULYSALAASNLEUGLULEUARG
4   THRVALLYSTHRGLUASPGLULEULYSLYS
5   TYRLEUGLUGLUPHEARGLYSGLUSERGLN
6   ASNILELYSVALLEUILELEUVALSERASN
7   ASPGLUGLULEUASPLYSALALYSGLULEU
8   ALAGLNLYSMETGLUILEASPVALARGTHR
9   ARGLYSVALTHRSERPROASPGLUALALYS
10   ARGTRPILELYSGLUPHESERGLUGLUGLY
11   GLYSERLEUGLUHISHISHISHISHISHIS

Samples:

sample_NC: OR16.004, [U-100% 13C; U-100% 15N], 1.073 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_NC5: OR16.006, [U-100% 13C; U-100% 15N], 0.867 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_NC5_RDC: OR16.013, [U-100% 13C; U-100% 15N], 0.859 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

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 C(CO)NHsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5_RDCisotropicsample_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

PALES, PALES (Zweckstetter, 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:

BMRB 16562
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