BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15972

Title: 1H, 13C and 15N resonance assignments of the PDZ of MAST205 in complex with the C-terminal tail from the rabies virus glycoprotein   PubMed: 19636944

Authors: Wolff, Nicolas; Terrien, Elouan; Simenel, Catherine; Lafon, Monique; Delepierre, Muriel

Citation: Terrien, Elouan; Simenel, Catherine; Prehaud, Christophe; Buc, Henri; Delepierre, Muriel; Lafon, Monique; Wolff, Nicolas. "1H, 13C and 15N resonance assignments of the PDZ of microtubule-associated serine/threonine kinase 205 (MAST205) in complex with the C-terminal motif from the rabies virus glycoprotein"  Biomol. NMR Assignments 3, 45-48 (2009).

Assembly members:
Mast205, polymer, 96 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
Mast205: GGSMRPPIIIHRAGKKYGFT LRAIRVYMGDSDVYTVHHMV WHVEDGGPASEAGLRQGDLI THVNGEPVHGLVHTEVVELI LKSGNKVAISTTPLEN

Data sets:
Data typeCount
13C chemical shifts402
15N chemical shifts93
1H chemical shifts645

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 96 residues - Formula weight is not available

1   GLYGLYSERMETARGPROPROILEILEILE
2   HISARGALAGLYLYSLYSTYRGLYPHETHR
3   LEUARGALAILEARGVALTYRMETGLYASP
4   SERASPVALTYRTHRVALHISHISMETVAL
5   TRPHISVALGLUASPGLYGLYPROALASER
6   GLUALAGLYLEUARGGLNGLYASPLEUILE
7   THRHISVALASNGLYGLUPROVALHISGLY
8   LEUVALHISTHRGLUVALVALGLULEUILE
9   LEULYSSERGLYASNLYSVALALAILESER
10   THRTHRPROLEUGLUASN

Samples:

sample_1: Tris; NaCl, [U-100% 13C; U-100% 15N], 800 uM; Mast205 800 uM; H2O 88%; D2O 12%

sample_conditions_1: ionic strength: 150 M; pH: 7.5; 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 C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16967
PDB
DBJ BAA34527 BAB40778
EMBL CAD38775
GB AAH65499 EAX06948 EAX06949 EFB27522 EHB01606
REF NP_055927 XP_001105315 XP_002810932 XP_004025774 XP_004285802
SP Q6P0Q8