BMRB Entry 17305

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17305
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Three-dimensional structure of the N-terminal effector PYRIN domain of NLRP12
Deposition date:
2010-11-17
Original release date:
2011-12-02
Authors:
Pinheiro, Anderson; Peti, Wolfgang
Citation:

Citation: Pinheiro, Anderson; Eibl, Clarissa; Ekman-Vural, Zeynep; Schwarzenbacher, Robert; Peti, Wolfgang. "Three-dimensional structure of the effector PYRIN domain of NLRP12"  J. Mol. Biol. 413, 790-803 (2011).
PubMed: 21978668

Assembly members:

Assembly members:
NLRP12_PYD, polymer, 102 residues, 11722.509 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHis parallel STOP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NLRP12_PYD: GHMLRTAGRDGLCRLSTYLE ELEAVELKKFKLYLGTATEL GEGKIPWGSMEKAGPLEMAQ LLITHFGPEEAWRLALSTFE RINRKDLWERGQREDLVRDT VE

Data sets:
Data typeCount
13C chemical shifts402
15N chemical shifts101
1H chemical shifts698

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NLRP12 PYD monomer1

Entities:

Entity 1, NLRP12 PYD monomer 102 residues - 11722.509 Da.

Residues GLY1, HIS2, VAL101 and GLU102 were introduced by cloning and are not part of the protein sequence.

1   GLYHISMETLEUARGTHRALAGLYARGASP
2   GLYLEUCYSARGLEUSERTHRTYRLEUGLU
3   GLULEUGLUALAVALGLULEULYSLYSPHE
4   LYSLEUTYRLEUGLYTHRALATHRGLULEU
5   GLYGLUGLYLYSILEPROTRPGLYSERMET
6   GLULYSALAGLYPROLEUGLUMETALAGLN
7   LEULEUILETHRHISPHEGLYPROGLUGLU
8   ALATRPARGLEUALALEUSERTHRPHEGLU
9   ARGILEASNARGLYSASPLEUTRPGLUARG
10   GLYGLNARGGLUASPLEUVALARGASPTHR
11   VALGLU

Samples:

sample_1: NLRP12 PYD, [U-99% 15N], 600 uM; sodium phosphate 20 mM; sodium chloride 500 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_2: NLRP12 PYD, [U-99% 13C; U-99% 15N], 600 uM; sodium phosphate 20 mM; sodium chloride 500 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_3: NLRP12 PYD 600 uM; sodium phosphate 20 mM; sodium chloride 500 mM; TCEP 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H COSYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAF83461 BAG53059
GB AAH28069 AAM18227 AAM75142 AAM75143 AAM75144
REF NP_001264055 NP_001264058 NP_653288 XP_003830191 XP_003830193
SP P59046
AlphaFold P59046

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