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 16575

Title: HUMAN NEDD4 3RD WW DOMAIN COMPLEX WITH EBOLA ZAIRE VIRUS MATRIX PROTEIN VP40 DERIVED PEPTIDE ILPTAPPEYMEA

Authors: Iglesias-Bexiga, Manuel; Luque, Irene; Macias, Maria; Blanco, Francisco; Cobos, Eva; Bonet, Roman

Citation: Iglesias-Bexiga, Manuel. "HUMAN NEDD4 3RD WW DOMAIN COMPLEX WITH EBOLA ZAIRE VIRUS MATRIX PROTEIN VP40 DERIVED PEPTIDE"  Not known ., .-..

Assembly members:
NEDD4-WW3, polymer, 49 residues, 4213.847 Da.
ILPTAPPEYMEA, polymer, 12 residues, 1008.108 Da.

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):
NEDD4-WW3: GAMGPSEIEQGFLPKGWEVR HAPNGRPFFIDHNTKTTTWE DPRLKIPAH
ILPTAPPEYMEA: ILPTAPPEYMEA

Data sets:
Data typeCount
15N chemical shifts45
1H chemical shifts398

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NEDD4-WW31
2ILPTAPPEYMEA2

Entities:

Entity 1, NEDD4-WW3 49 residues - 4213.847 Da.

Residues 1-4 represent a non-native cloning tag resulting from TEV cleavage

1   GLYALAMETGLYPROSERGLUILEGLUGLN
2   GLYPHELEUPROLYSGLYTRPGLUVALARG
3   HISALAPROASNGLYARGPROPHEPHEILE
4   ASPHISASNTHRLYSTHRTHRTHRTRPGLU
5   ASPPROARGLEULYSILEPROALAHIS

Entity 2, ILPTAPPEYMEA 12 residues - 1008.108 Da.

1   ILELEUPROTHRALAPROPROGLUTYRMET
2   GLUALA

Samples:

15nSAMPLE: PROTEIN, [U-100% 15N], 1 mM; PEPTIDE 10 mM; sodium phosphate 20 mM; sodium azide 0.02 v/v; H2O 90%; D2O 10%

15N13Csample: PROTEIN, [U-100% 13C; U-100% 15N], 0.5 mM; PEPTIDE 5 mM; sodium phosphate 20 mM; sodium azide 0.02 v/v; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.00; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15nSAMPLEisotropicsample_conditions_1
2D 1H-1H TOCSY15nSAMPLEisotropicsample_conditions_1
2D 1H-1H NOESY15nSAMPLEisotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16574 18971
PDB
REF XP_011758823 XP_012325247