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 10101

Title: Solution structure of four helical up-and-down bundle domain of the hypothetical rotein 2610208M17Rik similar to the protein FLJ12806

Authors: Li, H.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Shirouzu, M.; Terada, M.; Yabuki, T.; Aoki, M.; Seki, E.; Matsuda, T.; Hirota, H.; Yoshida, M.; Tanaka, A.; Osanai, T.; Arakawa, T.; Carninci, P.; Kawai, J.; Hayashizaki, Y.; Yokoyama, S.

Citation: Li, H.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Shirouzu, M.; Terada, M.; Yabuki, T.; Aoki, M.; Seki, E.; Matsuda, T.; Hirota, H.; Yoshida, M.; Tanaka, A.; Osanai, T.; Arakawa, T.; Carninci, P.; Kawai, J.; Hayashizaki, Y.; Yokoyama, S.. "Solution structure of four helical up-and-down bundle domain of the hypothetical protein 2610208M17Rik similar to the protein FLJ12806"  . ., .-..

Assembly members:
Four helical up-and-down bundle domain, polymer, 128 residues, Formula weight is not available

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
Four helical up-and-down bundle domain: GSSGSSGMSEVTRSLLQRWG ASLRRGADFDSWGQLVEAID EYQILARHLQKEAQAQHNNS EFTEEQKKTIGKIATCLELR SAALQSTQSQEEFKLEDLKK LEPILKNILTYNKEFPFDVQ PISGPSSG

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts126
1H chemical shifts860

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
12610208M17Rik protein1

Entities:

Entity 1, 2610208M17Rik protein 128 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETSERGLU
2   VALTHRARGSERLEULEUGLNARGTRPGLY
3   ALASERLEUARGARGGLYALAASPPHEASP
4   SERTRPGLYGLNLEUVALGLUALAILEASP
5   GLUTYRGLNILELEUALAARGHISLEUGLN
6   LYSGLUALAGLNALAGLNHISASNASNSER
7   GLUPHETHRGLUGLUGLNLYSLYSTHRILE
8   GLYLYSILEALATHRCYSLEUGLULEUARG
9   SERALAALALEUGLNSERTHRGLNSERGLN
10   GLUGLUPHELYSLEUGLUASPLEULYSLYS
11   LEUGLUPROILELEULYSASNILELEUTHR
12   TYRASNLYSGLUPHEPROPHEASPVALGLN
13   PROILESERGLYPROSERSERGLY

Samples:

sample_1: four helical up-and-down bundle domain, [U-13C; U-15N], 0.8 mM; d-Tris 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 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.811, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB14281 BAC38234 BAE00645 BAE25512 BAE29085
EMBL CAH56257 CAH91107
GB AAH15535 AAH57183 AAH66829 AAH67805 AAH86763
REF NP_001121072 NP_001125646 NP_001192563 NP_001270111 NP_073742
SP Q4R8C7 Q5RAV3 Q8C4Q6 Q96BJ3
TPG DAA21418