BMRB Entry 17724

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17724

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Title:
Micelle-bound KSR1 CA1CA1a
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, polymer, 149 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: pJexpress411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KSR1: GHMDGGAGAAVSRALQQCGQ LQKLIDISIGSLRGLRTKCS VSNDLTQQEIRTLEAKLVKY ICKQQQSKLSVTPSDRTAEL NSYPRFSDWLYIFNVRPEVV QEIPQELTLDALLEMDEAKA KEMLRRWGASTEECSRLQQA LTCLRKVTG

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts136
1H chemical shifts136

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1KSR1 CA1-CA1a domain1

Entities:

Entity 1, KSR1 CA1-CA1a domain 149 residues - Formula weight is not available

Residues G(-2), H(-1) and M(0) represent non-native residues that remain after cleavage of the N-terminal affinity tag.

1   GLYHISMETASPGLYGLYALAGLYALAALA
2   VALSERARGALALEUGLNGLNCYSGLYGLN
3   LEUGLNLYSLEUILEASPILESERILEGLY
4   SERLEUARGGLYLEUARGTHRLYSCYSSER
5   VALSERASNASPLEUTHRGLNGLNGLUILE
6   ARGTHRLEUGLUALALYSLEUVALLYSTYR
7   ILECYSLYSGLNGLNGLNSERLYSLEUSER
8   VALTHRPROSERASPARGTHRALAGLULEU
9   ASNSERTYRPROARGPHESERASPTRPLEU
10   TYRILEPHEASNVALARGPROGLUVALVAL
11   GLNGLUILEPROGLNGLULEUTHRLEUASP
12   ALALEULEUGLUMETASPGLUALALYSALA
13   LYSGLUMETLEUARGARGTRPGLYALASER
14   THRGLUGLUCYSSERARGLEUGLNGLNALA
15   LEUTHRCYSLEUARGLYSVALTHRGLY

Samples:

sample_1: KSR1 CA1-CA1a, [U-13C; U-15N; U-2H], 0.55 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM; SDS 82 mM; H2O 90%; D2O 10%

sample_2: KSR1 CA1-CA1a, [U-15N; U-2H], 0.55 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM; SDS 82 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17045 17725 18740
PDB
EMBL CAA57288
GB AAC52382 AAI68386 ABK42251
REF NP_038599 XP_006246986 XP_006246988 XP_006246989 XP_006532397
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