BMRB Entry 11159

Title:
Solution structure of the Ring finger of human Retinoblastoma-binding protein 6
Deposition date:
2010-04-15
Original release date:
2011-05-05
Authors:
Abe, H.; Miyamoto, K.; Tochio, N.; Tomizawa, T.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Abe, H.; Miyamoto, K.; Tochio, N.; Tomizawa, T.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the Ring finger of human Retinoblastoma-binding protein 6"  .

Assembly members:

Assembly members:
UNP residues 249-309, C3HC4 domain, polymer, 74 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P060731-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UNP residues 249-309, C3HC4 domain: GSSGSSGEDDPIPDELLCLI CKDIMTDAVVIPCCGNSYCD ECIRTALLESDEHTCPTCHQ NDVSPDALSGPSSG

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts63
1H chemical shifts429

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UNP residues 249-309, C3HC4 domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, UNP residues 249-309, C3HC4 domain 74 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUASPASP
2   PROILEPROASPGLULEULEUCYSLEUILE
3   CYSLYSASPILEMETTHRASPALAVALVAL
4   ILEPROCYSCYSGLYASNSERTYRCYSASP
5   GLUCYSILEARGTHRALALEULEUGLUSER
6   ASPGLUHISTHRCYSPROTHRCYSHISGLN
7   ASNASPVALSERPROASPALALEUSERGLY
8   PROSERSERGLY

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: UNP residues 249-309, C3HC4 domain, [U-13C; U-15N], 1.18 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.05 mM; IDA 1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

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

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9747, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 17466 17772
PDB
DBJ BAC77636 BAC77637 BAG64162
EMBL CAA59445
GB AAB49620 AAC72432 AAH63524 AAI72357 AAL05625
REF NP_001291483 NP_008841 NP_035377 NP_061173 XP_001076339
SP P97868 Q7Z6E9
TPG DAA15466
AlphaFold P97868 Q7Z6E9

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