BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 18539

Click here to enlarge.

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/BMR18539
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: NMR structure of Carcinoscorpius rotundicauda thioredoxin related protein 16 and its role in regulating transcription factor NF-kB activity   PubMed: 22763700

Deposition date: 2012-06-21 Original release date: 2012-07-09

Authors: Pankaj, Giri; Fan, Jing-Song; Swaminathan, Kunchithapadam; Sivaraman, J.

Citation: Giri, Pankaj; Fan, Jing-Song; Kumaraswamy, Shanmugam; Ding, Jeak; Sethi, Gautam; Swaminathan, Kunchithapadam; Sivaraman, J.. "NMR structure of Carcinoscorpius rotundicauda thioredoxin related protein 16 and its role in regulating transcription factor NF-kB activity"  J. Biol. Chem. 287, 29417-29428 (2012).

Assembly members:
protein_16, polymer, 143 residues, 16062.451 Da.

Natural source:   Common Name: Southeast Asian horsehoe crab   Taxonomy ID: 6848   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Carcinoscorpius rotundicauda

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

Entity Sequences (FASTA):
protein_16: MEFIQGIKLVKKNRCEVNAN EALKDKDIIGFYFSAHWCPP CRGFTPILADMYSELVDDSA PFEIIFVSSDRSEDDMFQYM MESHGDWLAIPYRSGPASNV TAKYGITGIPALVIVKKDGT LISMNGRGEVQSLGPRAFQN WAR

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts133
1H chemical shifts884

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein_161

Entities:

Entity 1, protein_16 143 residues - 16062.451 Da.

1   METGLUPHEILEGLNGLYILELYSLEUVAL
2   LYSLYSASNARGCYSGLUVALASNALAASN
3   GLUALALEULYSASPLYSASPILEILEGLY
4   PHETYRPHESERALAHISTRPCYSPROPRO
5   CYSARGGLYPHETHRPROILELEUALAASP
6   METTYRSERGLULEUVALASPASPSERALA
7   PROPHEGLUILEILEPHEVALSERSERASP
8   ARGSERGLUASPASPMETPHEGLNTYRMET
9   METGLUSERHISGLYASPTRPLEUALAILE
10   PROTYRARGSERGLYPROALASERASNVAL
11   THRALALYSTYRGLYILETHRGLYILEPRO
12   ALALEUVALILEVALLYSLYSASPGLYTHR
13   LEUILESERMETASNGLYARGGLYGLUVAL
14   GLNSERLEUGLYPROARGALAPHEGLNASN
15   TRPALAARG

Samples:

sample_1: sodium chloride 100 mM; DTT 5 mM; EDTA 1 mM; glycerol 5%; H2O 95%; D2O, [U-2H], 5%; protein_16, [U-100% 13C; U-100% 15N], 1.0 mM

sample_2: sodium chloride 100 mM; DTT 5 mM; EDTA 1 mM; glycerol 5%; H2O 95%; D2O, [U-2H], 5%; protein_16, [U-100% 13C; U-100% 15N], 1.0 mM

sample_3: sodium chloride 100 mM; DTT 5 mM; EDTA 1 mM; Pf1 phage 8 mg/mL; H2O 95%; D2O, [U-2H], 5%; protein_16, [U-100% 13C; U-100% 15N], 1.0 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB ABF22607

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