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 19397

Title: Backbone 1H and 15N Chemical Shift Assignments for the first domain of FAT10

Deposition date: 2013-07-30 Original release date: 2014-08-25

Authors: Wang, Wei; Lim, Liangzhong; Qin, Haina

Citation: Wang, Wei; Lim, Liangzhong; Qin, Haina; Song, Jianxing. "Structure of FAT10 first domain"  Not known ., .-..

Assembly members:
FAT10, polymer, 75 residues, 8676.306 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):
FAT10: LCVHVRSEEWDLMTFDANPY DSVLKIKEHVRSKTKVPVQD QVLLLGSKILKPRRSLSSYG IDKEKTIHLTLKVVK

Data sets:
Data typeCount
15N chemical shifts52
1H chemical shifts296

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FAT101

Entities:

Entity 1, FAT10 75 residues - 8676.306 Da.

1   LEUCYSVALHISVALARGSERGLUGLUTRP
2   ASPLEUMETTHRPHEASPALAASNPROTYR
3   ASPSERVALLEULYSILELYSGLUHISVAL
4   ARGSERLYSTHRLYSVALPROVALGLNASP
5   GLNVALLEULEULEUGLYSERLYSILELEU
6   LYSPROARGARGSERLEUSERSERTYRGLY
7   ILEASPLYSGLULYSTHRILEHISLEUTHR
8   LEULYSVALVALLYS

Samples:

sample_1: sodium phosphate 0.01 mM; DTT 0.01 mM; FAT10, [U-100% 15N], 0.4 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

TOPSPIN, Bruker Biospin - collection

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAG34855
EMBL CAA21458 CAA73200
GB AAD52982 AAH12472 ABM85550 AIC55799 EAX03201
REF NP_006389 XP_004043579
SP O15205

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