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 11247

Title: Solution structure of the FHA domain of human ubiquitin ligase protein RNF8

Deposition date: 2010-07-23 Original release date: 2011-08-03

Authors: Hayashi, F.; Nagashima, T.; Yokoyama, S.

Citation: Hayashi, F.; Nagashima, T.; Yokoyama, S.. "Solution structure of the FHA domain of human ubiquitin ligase protein RNF8"  . ., .-..

Assembly members:
FHA domain, polymer, 145 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
FHA domain: GSSGSSGVTGDRAGGRSWCL RRVGMSAGWLLLEDGCEVTV GRGFGVTYQLVSKICPLMIS RNHCVLKQNPEGQWTIMDNK SLNGVWLNRARLEPLRVYSI HQGDYIQLGVPLENKENAEY EYEVTEEDWETIYPCLSPKS GPSSG

Data sets:
Data typeCount
13C chemical shifts608
15N chemical shifts147
1H chemical shifts973

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FHA domain1

Entities:

Entity 1, FHA domain 145 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALTHRGLY
2   ASPARGALAGLYGLYARGSERTRPCYSLEU
3   ARGARGVALGLYMETSERALAGLYTRPLEU
4   LEULEUGLUASPGLYCYSGLUVALTHRVAL
5   GLYARGGLYPHEGLYVALTHRTYRGLNLEU
6   VALSERLYSILECYSPROLEUMETILESER
7   ARGASNHISCYSVALLEULYSGLNASNPRO
8   GLUGLYGLNTRPTHRILEMETASPASNLYS
9   SERLEUASNGLYVALTRPLEUASNARGALA
10   ARGLEUGLUPROLEUARGVALTYRSERILE
11   HISGLNGLYASPTYRILEGLNLEUGLYVAL
12   PROLEUGLUASNLYSGLUASNALAGLUTYR
13   GLUTYRGLUVALTHRGLUGLUASPTRPGLU
14   THRILETYRPROCYSLEUSERPROLYSSER
15   GLYPROSERSERGLY

Samples:

sample_1: FHA domain, [U-13C; U-15N], 1.1 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9297, Kobayashi, N. - data analysis

CYANA v2.0, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAA31621 BAA33557 BAD96485 BAE87261 BAG09793
EMBL CAH93334
GB AAH07517 AAP36114 AAP36421 AAQ14887 AAX29228
REF NP_001126963 NP_001252758 NP_001267209 NP_001274572 NP_003949
SP O76064 Q5R4I2

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