BMRB Entry 15932

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15932
MolProbity Validation Chart

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Title:
Solution Structure of the Catalytic Domain of Procaspase-8
Deposition date:
2008-08-28
Original release date:
2009-03-11
Authors:
Keller, Nadine; Zerbe, Oliver; Mares, Jiri; Gruetter, Markus
Citation:

Citation: Keller, Nadine; Mares, Jiri; Zerbe, Oliver; Gruetter, Markus. "Structural and Biochemical Studies on Procaspase-8: New Insights on Initiator Caspase Activation"  Structure 17, 438-448 (2009).
PubMed: 19278658

Assembly members:

Assembly members:
procaspase8, polymer, 266 residues, 24713.402 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: pQE-50

Entity Sequences (FASTA):

Entity Sequences (FASTA):
procaspase8: MRGSESQTLDKVYQMKSKPR GYCLIINNHNFAKAREKVPK LHSIRDRNGTHLDAGALTTT FEELHFEIKPHDDCTVEQIY EILKIYQLMDHSNMDCFICC ILSHGDKGIIYGTDGQEAPI YELTSQFTGLKCPSLAGKPK VFFIQAAQGDNYQKGIPVET DSEEQPYLEMDLSSPQTRYI PDEADFLLGMATVNNCVSYR NPAEGTWYIQSLCQSLRERC PRGDDILTILTEVNYEVSNK DDKKNMGKQMPQPTFTLRKK LVFPSD

Data sets:
Data typeCount
13C chemical shifts922
15N chemical shifts209
1H chemical shifts1346

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1procaspase81

Entities:

Entity 1, procaspase8 266 residues - 24713.402 Da.

1   METARGGLYSERGLUSERGLNTHRLEUASP
2   LYSVALTYRGLNMETLYSSERLYSPROARG
3   GLYTYRCYSLEUILEILEASNASNHISASN
4   PHEALALYSALAARGGLULYSVALPROLYS
5   LEUHISSERILEARGASPARGASNGLYTHR
6   HISLEUASPALAGLYALALEUTHRTHRTHR
7   PHEGLUGLULEUHISPHEGLUILELYSPRO
8   HISASPASPCYSTHRVALGLUGLNILETYR
9   GLUILELEULYSILETYRGLNLEUMETASP
10   HISSERASNMETASPCYSPHEILECYSCYS
11   ILELEUSERHISGLYASPLYSGLYILEILE
12   TYRGLYTHRASPGLYGLNGLUALAPROILE
13   TYRGLULEUTHRSERGLNPHETHRGLYLEU
14   LYSCYSPROSERLEUALAGLYLYSPROLYS
15   VALPHEPHEILEGLNALAALAGLNGLYASP
16   ASNTYRGLNLYSGLYILEPROVALGLUTHR
17   ASPSERGLUGLUGLNPROTYRLEUGLUMET
18   ASPLEUSERSERPROGLNTHRARGTYRILE
19   PROASPGLUALAASPPHELEULEUGLYMET
20   ALATHRVALASNASNCYSVALSERTYRARG
21   ASNPROALAGLUGLYTHRTRPTYRILEGLN
22   SERLEUCYSGLNSERLEUARGGLUARGCYS
23   PROARGGLYASPASPILELEUTHRILELEU
24   THRGLUVALASNTYRGLUVALSERASNLYS
25   ASPASPLYSLYSASNMETGLYLYSGLNMET
26   PROGLNPROTHRPHETHRLEUARGLYSLYS
27   LEUVALPHEPROSERASP

Samples:

sample_1: procaspase8, [U-99% 13C; U-99% 15N], 0.8 mM; DTT 10 mM; sodium chloride 100 mM; TRIS, [U-2H], 20 mM; H2O 90%; D2O 10%

sample_2: procaspase8, [U-100% 13C; U-100% 15N; 80% 2H], 0.8 mM; DTT 10 mM; sodium chloride 100 mM; TRIS, [U-2H], 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 8.0; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HN(CO)CGsample_2isotropicsample_conditions_1
3D HNCGsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
HN(CACO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v6.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - geometry optimization

CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution

XEASY v1.55, Bartels et al. - chemical shift assignment

CARA, Keller, W thrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB32555 BAG70096 BAG70228
EMBL CAA66853 CAA66854 CAA66855
GB AAB70913 AAC50602 AAC50645 AAD24962 AAL87628
REF NP_001073593 NP_001073594 NP_001125222 NP_001219 NP_203519
SP Q14790
AlphaFold Q14790

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