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 25149

Title: Isolated Ring domain   PubMed: 25306923

Deposition date: 2014-08-13 Original release date: 2014-10-27

Authors: Brown, Nicholas; Watson, Edmond; Weissman, Florian; Royappa, Grace; Schulman, Brenda; Jarvis, Marc; Vanderlinden, Ryan; Frye, Jeremiah; Qiao, Renping; Petzold, Georg; Peters, Jan-Michael; Stark, Holger

Citation: Brown, Nicholas; Watson, Edmond; Weissman, Florian; Royappa, Grace; Jarvis, Marc; Vanderlinden, Ryan; Frye, Jeremiah; Qiao, Renping; Petzold, Georg; Peters, Jan-Michael; Stark, Holger; Schulman, Brenda. "Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly"  Mol. Cell ., .-. (2014).

Assembly members:
entity_1, polymer, 70 residues, 8191.060 Da.
ZINC ION, non-polymer, 65.409 Da.

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

Entity Sequences (FASTA):
entity_1: GSVANDENCGICRMAFNGCC PDCKVPGDDCPLVWGQCSHC FHMHCILKWLHAQQVQQHCP MCRQEWKFKE

Data sets:
Data typeCount
1H chemical shifts469
13C chemical shifts292
15N chemical shifts76

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2Zinc Ion 12
3Zinc Ion 22
4Zinc Ion 32

Entities:

Entity 1, entity_1 70 residues - 8191.060 Da.

1   GLYSERVALALAASNASPGLUASNCYSGLY
2   ILECYSARGMETALAPHEASNGLYCYSCYS
3   PROASPCYSLYSVALPROGLYASPASPCYS
4   PROLEUVALTRPGLYGLNCYSSERHISCYS
5   PHEHISMETHISCYSILELEULYSTRPLEU
6   HISALAGLNGLNVALGLNGLNHISCYSPRO
7   METCYSARGGLNGLUTRPLYSPHELYSGLU

Entity 2, Zinc Ion 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm; ionic strength: 100 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

cyana v2.1, Guntert, Mumenthaler and Wuthrich - structure solution, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB22663 BAB22890 BAB22937 BAC32348 BAE22944
EMBL CAH92008
GB AAF65816 AAH23039 AAH66308 AAH95454 AAI02427
REF NP_001002245 NP_001002246 NP_001002247 NP_001002248 NP_001002249
SP Q3ZCF6 Q5R8A2 Q9CPX9 Q9NYG5
TPG DAA14168 DAA18262

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