BMRB Entry 27234

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27234

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

Title:
Solution chemical shifts CAMSAP3 CKK domain
Deposition date:
2017-08-24
Original release date:
2017-09-25
Authors:
Atherton, Joseph; Jiang, Kai; Marcel, Stangier; Luo, Yanzhang; Hua, Sasha; Houben, Klaartje; van Hooff, Jolien; Joseph, Agnel-Praveen; Scarabelli, Guido; Grant, Barry; Roberts, Anthony; Topf, Maya; Steinmetz, Michel; Baldus, Marc; Moores, Carolyn; Akhmanova, Anna
Citation:

Citation: Atherton, Joseph; Jiang, Kai; Stangier, Marcel; Luo, Yanzhang; Hua, Sasha; Houben, Klaartje; van Hooff, Jolien; Joseph, Agnel-Praveen; Scarabelli, Guido; Grant, Barry; Roberts, Anthony; Topf, Maya; Steinmetz, Michel; Baldus, Marc; Moores, Carolyn; Akhmanova, Anna. "A structural model for microtubule minus-end recognition and protection by CAMSAP proteins."  Nat. Struct. Mol. Biol. 24, 931-943 (2017).
PubMed: 28991265

Assembly members:

Assembly members:
CAMSAP3_CKK, polymer, 175 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CAMSAP3_CKK: MGSSHHHHHHSSGLVPRGSH MASMTGGQQMGRGSGPRLYK EPSAKSNKFIIHNALSHCCL AGKVNEPQKNRILEEIEKSK ANHFLILFRDSSCQFRALYT LSGETEELSRLAGYGPRTVT PAMVEGIYKYNSDRKRFTQI PAKTMSMSVDAFTIQGHLWQ SKKPTTPKKGGGTPK

Data sets:
Data typeCount
13C chemical shifts520
15N chemical shifts124
1H chemical shifts750

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CAMSAP3 CKK domain1

Entities:

Entity 1, CAMSAP3 CKK domain 175 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERMETTHRGLYGLYGLNGLNMET
4   GLYARGGLYSERGLYPROARGLEUTYRLYS
5   GLUPROSERALALYSSERASNLYSPHEILE
6   ILEHISASNALALEUSERHISCYSCYSLEU
7   ALAGLYLYSVALASNGLUPROGLNLYSASN
8   ARGILELEUGLUGLUILEGLULYSSERLYS
9   ALAASNHISPHELEUILELEUPHEARGASP
10   SERSERCYSGLNPHEARGALALEUTYRTHR
11   LEUSERGLYGLUTHRGLUGLULEUSERARG
12   LEUALAGLYTYRGLYPROARGTHRVALTHR
13   PROALAMETVALGLUGLYILETYRLYSTYR
14   ASNSERASPARGLYSARGPHETHRGLNILE
15   PROALALYSTHRMETSERMETSERVALASP
16   ALAPHETHRILEGLNGLYHISLEUTRPGLN
17   SERLYSLYSPROTHRTHRPROLYSLYSGLY
18   GLYGLYTHRPROLYS

Samples:

sample_1: CAMSAP3 CKK, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 40 mM; DTT 1 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 190 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

Uniprot U5LHW9
AlphaFold U5LK79

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