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 6297

Title: Solution structure of the RWD domain of the mouse GCN2 protein   PubMed: 15273307

Deposition date: 2004-08-26 Original release date: 2005-01-24

Authors: Nameki, Nobukazu; Yoneyama, Misao; Koshiba, Seizo; Tochio, Naoya; Inoue, Makoto; Seki, Eiko; Matsuda, Takayoshi; Tomo, Yasuko; Harada, Takushi; Saito, Kohei; Kobayashi, Naohiro; Yabuki, Takashi; Aoki, Masaaki; Nunokawa, Emi; Matsuda, Natsuko; Sakagami, Noriko; Terada, Takaho; Shirouzu, Mikako; Yoshida, Mayumi; Hirota, Hiroshi; Osanai, Takashi; Tanaka, Akiko; Arakawa, Takahiro; Carninci, Piero; Kawai, Jun; Hayashizaki, Yoshihide; Kinoshita, Kengo; Guntert, Peter; Kigawa, Takanori; Yokoyama, Shigeyuki

Citation: Nameki, Nobukazu; Yoneyama, Misao; Koshiba, Seizo; Tochio, Naoya; Inoue, Makoto; Seki, Eiko; Matsuda, Takayoshi; Tomo, Yasuko; Harada, Takushi; Saito, Kohei; Kobayashi, Naohiro; Yabuki, Takashi; Aoki, Masaaki; Nunokawa, Emi; Matsuda, Natsuko; Sakagami, Noriko; Terada, Takaho; Shirouzu, Mikako; Yoshida, Mayumi; Hirota, Hiroshi; Osanai, Takashi; Tanaka, Akiko; Arakawa, Takahiro; Carninci, Piero; Kawai, Jun; Hayashizaki, Yoshihide; Kinoshita, Kengo; Guntert, Peter; Kigawa, Takanori; Yokoyama, Shigeyuki. "Solution structure of the RWD domain of the mouse GCN2 protein"  Protein Sci. 13, 2089-2100 (2004).

Assembly members:
RWD domain, polymer, 137 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   Host organism: Escherichia coli   Vector: P021021-28

Entity Sequences (FASTA):
RWD domain: GSSGSSGMESYSQRQDHELQ ALEAIYGSDFQDLRPDARGR VREPPEINLVLYPQGLAGEE VYVQVELRVKCPPTYPDVVP EIDLKNAKGLSNESVNLLKS HLEELAKKQCGEVMIFELAH HVQSFLSEHNKSGPSSG

Data sets:
Data typeCount
13C chemical shifts575
15N chemical shifts134
1H chemical shifts933

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GCN2, RWD_domain1

Entities:

Entity 1, GCN2, RWD_domain 137 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETGLUSER
2   TYRSERGLNARGGLNASPHISGLULEUGLN
3   ALALEUGLUALAILETYRGLYSERASPPHE
4   GLNASPLEUARGPROASPALAARGGLYARG
5   VALARGGLUPROPROGLUILEASNLEUVAL
6   LEUTYRPROGLNGLYLEUALAGLYGLUGLU
7   VALTYRVALGLNVALGLULEUARGVALLYS
8   CYSPROPROTHRTYRPROASPVALVALPRO
9   GLUILEASPLEULYSASNALALYSGLYLEU
10   SERASNGLUSERVALASNLEULEULYSSER
11   HISLEUGLUGLULEUALALYSLYSGLNCYS
12   GLYGLUVALMETILEPHEGLULEUALAHIS
13   HISVALGLNSERPHELEUSERGLUHISASN
14   LYSSERGLYPROSERSERGLY

Samples:

sample_1: RWD domain, [U-15N; U-13C], 1.0 mM; dTris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; D20 10%; H20 90%

sample_conditions: ionic strength: 120 mM; pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N HSQCsample_1not availablesample_conditions
1H13C HSQCsample_1not availablesample_conditions
HNCOsample_1not availablesample_conditions
HNCACOsample_1not availablesample_conditions
HNCAsample_1not availablesample_conditions
HNCACAsample_1not availablesample_conditions
HNCACBsample_1not availablesample_conditions
CBCACONHsample_1not availablesample_conditions
HAHBNHsample_1not availablesample_conditions
CCCONNHsample_1not availablesample_conditions
HCCCONNHsample_1not availablesample_conditions
HCCHCOSYsample_1not availablesample_conditions
HCCHTOCSYsample_1not availablesample_conditions
15N NOESYsample_1not availablesample_conditions
13C NOESYsample_1not availablesample_conditions

Software:

NMRPipe v20020425 - processing

NMR spectrometers:

  • Bruker AVANCE 700 MHz
  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB28984
REF NP_038747 XP_006499687

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