BMRB Entry 19205

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19205
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution NMR Structure of Engineered Cystine Knot Protein 2.5D
Deposition date:
2013-04-30
Original release date:
2014-05-05
Authors:
Cochran, Frank; Das, Rhiju
Citation:

Citation: Kryshtafovych, Andriy; Moult, John; Bales, Patrick; Bazan, J. Fernando; Biasini, Marco; Burgin, Alex; Chen, Chen; Cochran, Frank; Craig, Timothy; Das, Rhiju; Fass, Deborah; Garcia-Doval, Carmela; Herzberg, Osnat; Lorimer, Donald; Luecke, Hartmut; Ma, Xiaolei; Nelson, Daniel; van Raaij, Mark; Rohwer, Forest; Segall, Anca; Seguritan, Victor; Zeth, Kornelius; Schwede, Torsten. "Challenging the state of the art in protein structure prediction: Highlights of experimental target structures for the 10th Critical Assessment of Techniques for Protein Structure Prediction Experiment CASP10"  Proteins 82, 26-42 (2014).
PubMed: 24318984

Assembly members:

Assembly members:
entity, polymer, 33 residues, 3250.559 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: pET-32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GCPQGRGDWAPTSCSQDSDC LAGCVCGPNGFCG

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts33
1H chemical shifts174

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Engineered Cystine Knot Protein 2.5D1

Entities:

Entity 1, Engineered Cystine Knot Protein 2.5D 33 residues - 3250.559 Da.

1   GLYCYSPROGLNGLYARGGLYASPTRPALA
2   PROTHRSERCYSSERGLNASPSERASPCYS
3   LEUALAGLYCYSVALCYSGLYPROASNGLY
4   PHECYSGLY

Samples:

sample_1: 2.5D, [U-13C; U-15N], 300 uM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
ghnco_LRAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian VNS 600 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks