BMRB Entry 16263

Title:
Backbone and sidechain 1H, 15N and 13C assignments of the NLRP7 Pyrin domain   PubMed: 19888692
Deposition date:
2009-04-24
Original release date:
2009-07-23
Authors:
Pinheiro, Anderson; Ehart, Angela; Ebner, Nina; Schwarzenbacher, Robert; Peti, Wolfgang
Citation:

Citation: de Sa Pinheiro, Anderson; Ehart, Angela; Ebner, Nina; Proell, Martina; Schwarzenbacher, Robert; Peti, Wolfgang. "Backbone and sidechain (1)H, (15)N and (13)C assignments of the NLRP7 pyrin domain."  Biomol. NMR Assignments 3, 207-209 (2009).

Assembly members:

Assembly members:
NLRP7_Pyd, polymer, 106 residues, Formula weight is not available

Natural source:

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

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

Experimental source:

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

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

Data sets:
Data typeCount
13C chemical shifts417
15N chemical shifts101
1H chemical shifts713

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit_11

Entities:

Entity 1, subunit_1 106 residues - Formula weight is not available

Residues 1 and 2 (GH) are part of the protease cleavage site used to cleave off the solubility tag used in the expression of this protein. Residues 101-106 comprise a His6-tag used for purification.

1   GLYHISMETTHRSERPROGLNLEUGLUTRP
2   THRLEUGLNTHRLEULEUGLUGLNLEUASN
3   GLUASPGLULEULYSSERPHELYSSERLEU
4   LEUTRPALAPHEPROLEUGLUASPVALLEU
5   GLNLYSTHRPROTRPSERGLUVALGLUGLU
6   ALAASPGLYLYSLYSLEUALAGLUILELEU
7   VALASNTHRSERSERGLUASNTRPILEARG
8   ASNALATHRVALASNILELEUGLUGLUMET
9   ASNLEUTHRGLULEUCYSLYSMETALALYS
10   ALAGLUMETMETGLUASPGLYGLNLEUGLU
11   HISHISHISHISHISHIS

Samples:

sample_1: NLRP7 Pyd, [U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.25 mM; H2O 90%; D2O 10%

sample_2: NLRP7 Pyd, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.25 mM; H2O 90%; D2O 10%

sample_3: NLRP7 Pyd 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.25 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_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 HNCACOsample_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 TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D DQF-COSYsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance II 500 MHz

Related Database Links:

PDB
DBJ BAG63894
GB AAI09125 AAI09126 AAL69963 AAO18158 AIC57936
REF NP_001120727 NP_631915 NP_996611 XP_004061498 XP_006723138
SP Q8WX94
TPG DAA01246
AlphaFold Q8WX94

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