BMRB Entry 17045

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17045
MolProbity Validation Chart

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Title:
KSR1 CA1 domain
Deposition date:
2010-07-06
Original release date:
2010-09-08
Authors:
Koveal, Dorothy; Pinheiro, Anderson; Peti, Wolfgang; Page, Rebecca
Citation:

Citation: Koveal, Dorothy; Pinheiro, Anderson; Peti, Wolfgang; Page, Rebecca. "Backbone and side chain (1)H, (15)N and (13)C assignments of the KSR1 CA1 domain."  Biomol. NMR Assignments 5, 39-41 (2011).
PubMed: 20737253

Assembly members:

Assembly members:
KSR1_CA1, 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_CA1: GHMDGGAGAAVSRALQQCGQ LQKLIDISIGSLRGLRTKCS VSNDLTQQEIRTLEAKLVKY ICKQQQSKLSVTPSDRTAEL NSYPRFSDWLYIFNVRPEVV QEIPQELTLDALLEMDEAKA KEMLRRWGASTEECSRLQQA LTCLRKVTG

Data sets:
Data typeCount
13C chemical shifts621
15N chemical shifts159
1H chemical shifts1067

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1KSR1 CA1 monomer1

Entities:

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

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, [U-99% 13C; U-99% 15N], 2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_2: KSR1 CA1 2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_3: KSR1 CA1, [U-99% 15N], 2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17724 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