BMRB Entry 17725

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17725

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
KSR1(1-170)
Deposition date:
2011-06-21
Original release date:
2013-02-11
Authors:
Koveal, Dorothy; Page, Rebecca; Peti, Wolfgang
Citation:

Citation: Koveal, Dorothy; Schuh-Nuhfer, Natasha; Ritt, Daniel; Page, Rebecca; Morrison, Deborah; Peti, Wolfgang. "A CC-SAM, for coiled coil-sterile alpha motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane"  Sci. Signal 5, ra94-ra94 (2012).
PubMed: 23250398

Assembly members:

Assembly members:
KSR1_CA1-CA1a, polymer, 172 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KSR1_CA1-CA1a: GHMDRAALRAAAMGEKKEGG GGGAAADGGAGAAVSRALQQ CGQLQKLIDISIGSLRGLRT KCSVSNDLTQQEIRTLEAKL VKYICKQQQSKLSVTPSDRT AELNSYPRFSDWLYIFNVRP EVVQEIPQELTLDALLEMDE AKAKEMLRRWGASTEECSRL QQALTCLRKVTG

Data sets:
Data typeCount
13C chemical shifts649
15N chemical shifts156
1H chemical shifts533

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KSR1 CA1-CA1a domain1

Entities:

Entity 1, KSR1 CA1-CA1a domain 172 residues - Formula weight is not available

Residues G(-2) and H(-1) represent non-native residues that remain after cleavage of the N-terminal affinity tag.

1   GLYHISMETASPARGALAALALEUARGALA
2   ALAALAMETGLYGLULYSLYSGLUGLYGLY
3   GLYGLYGLYALAALAALAASPGLYGLYALA
4   GLYALAALAVALSERARGALALEUGLNGLN
5   CYSGLYGLNLEUGLNLYSLEUILEASPILE
6   SERILEGLYSERLEUARGGLYLEUARGTHR
7   LYSCYSSERVALSERASNASPLEUTHRGLN
8   GLNGLUILEARGTHRLEUGLUALALYSLEU
9   VALLYSTYRILECYSLYSGLNGLNGLNSER
10   LYSLEUSERVALTHRPROSERASPARGTHR
11   ALAGLULEUASNSERTYRPROARGPHESER
12   ASPTRPLEUTYRILEPHEASNVALARGPRO
13   GLUVALVALGLNGLUILEPROGLNGLULEU
14   THRLEUASPALALEULEUGLUMETASPGLU
15   ALALYSALALYSGLUMETLEUARGARGTRP
16   GLYALASERTHRGLUGLUCYSSERARGLEU
17   GLNGLNALALEUTHRCYSLEUARGLYSVAL
18   THRGLY

Samples:

sample_1: KSR1 CA1-CA1a, [U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_2: KSR1 CA1-CA1a, [U-99% 13C; U-99% 15N], 2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 17045 17724 18740
PDB
EMBL CAA57288
GB AAC52382 AAI68386 ABK42251
REF NP_038599 XP_006532397 XP_006532398 XP_006532399 XP_011247072
SP Q61097
AlphaFold Q61097

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