BMRB Entry 18137

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18137

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Title:
NMR assignment of the monomeric DUF59 domain of human Fam96a
Deposition date:
2011-12-12
Original release date:
2012-01-09
Authors:
Mas, Caroline; Chen, Kai-En; Brereton, Ian; Martin, Jennifer; Hill, Justine
Citation:

Citation: Mas, Caroline; Chen, Kai-En; Brereton, Ian; Martin, Jennifer; Hill, Justine. "Backbone resonance assignments of the monomeric DUF59 domain of human Fam96a."  Biomol. NMR Assignments 7, 117-120 (2013).
PubMed: 22618863

Assembly members:

Assembly members:
Fam96a, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMCSG7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fam96a: SNARIMEEKALEVYDLIRTI RDPEKPNTLEELEVVSESCV EVQEINEEEYLVIIRFTPTV PHCSLATLIGLCLRVKLQRC LPFKHKLEIYISEGTHSTEE DINKQINDKERVAAAMENPN LREIVEQCVL

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts105
1H chemical shifts103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fam96a1

Entities:

Entity 1, Fam96a 130 residues - Formula weight is not available

1   SERASNALAARGILEMETGLUGLULYSALA
2   LEUGLUVALTYRASPLEUILEARGTHRILE
3   ARGASPPROGLULYSPROASNTHRLEUGLU
4   GLULEUGLUVALVALSERGLUSERCYSVAL
5   GLUVALGLNGLUILEASNGLUGLUGLUTYR
6   LEUVALILEILEARGPHETHRPROTHRVAL
7   PROHISCYSSERLEUALATHRLEUILEGLY
8   LEUCYSLEUARGVALLYSLEUGLNARGCYS
9   LEUPROPHELYSHISLYSLEUGLUILETYR
10   ILESERGLUGLYTHRHISSERTHRGLUGLU
11   ASPILEASNLYSGLNILEASNASPLYSGLU
12   ARGVALALAALAALAMETGLUASNPROASN
13   LEUARGGLUILEVALGLUGLNCYSVALLEU

Samples:

sample_1: Fam96a, [U-100% 13C; U-100% 15N], 0.8 mM; Hepes buffer 25 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CC-TOCSY-CONHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

CCcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP Q9H5X1
BMRB 18548
PDB
DBJ BAB15496 BAG35105 BAH14131
GB AAH08865 AAI02257 AAI51429 ABQ82139 AIC57308
REF NP_001014812 NP_001030282 NP_001092912 NP_001276037 NP_115607
SP Q3T0U7 Q9H5X1
TPG DAA25322
AlphaFold B7Z8Z5 Q3T0U7 Q9H5X1

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