BMRB Entry 18912

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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/BMR18912
MolProbity Validation Chart

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Title:
The membran-proximal domain of ADAM17
Deposition date:
2012-12-20
Original release date:
2013-04-08
Authors:
Dusterhoft, Stefan; Jung, Sascha; Hung, Chien-Wen; Thoely, Andreas; Sonnichsen, Frank; Grotzinger, Joachim; Lorenzen, Inken
Citation:

Citation: Dusterhoft, Stefan; Jung, Sascha; Hung, Chien-Wen; Thoely, Andreas; Sonnichsen, Frank. "The membrane-proximal domain of ADAM17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase"  J. Am. Chem. Soc. ., .-. (2013).
PubMed: 23521534

Assembly members:

Assembly members:
entity, polymer, 62 residues, 7013.041 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: FCEREQQLESCACNETDNSC KVCCRDLSGRCVPYVDAEQK NLFLRKGKPCTVGFCDMNGK CE

Data sets:
Data typeCount
13C chemical shifts8
15N chemical shifts63
1H chemical shifts338

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ADAM171

Entities:

Entity 1, ADAM17 62 residues - 7013.041 Da.

1   PHECYSGLUARGGLUGLNGLNLEUGLUSER
2   CYSALACYSASNGLUTHRASPASNSERCYS
3   LYSVALCYSCYSARGASPLEUSERGLYARG
4   CYSVALPROTYRVALASPALAGLUGLNLYS
5   ASNLEUPHELEUARGLYSGLYLYSPROCYS
6   THRVALGLYPHECYSASPMETASNGLYLYS
7   CYSGLU

Samples:

sample_1: ADAM17, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - data analysis, processing, processing

NMR spectrometers:

  • Bruker Bruker Avance 600 600 MHz

Related Database Links:

PDB
GB AAB51514 AAB51586 AAB53014 AAC39721 AAI36784
REF NP_001295481 NP_003174 XP_002758088 XP_002799185 XP_002812349
SP P78536
AlphaFold P78536

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