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 16574

Title: HUMAN NEDD4 3RD WW DOMAIN COMPLEX WITH THE HUMAN T-CELL LEUKEMIA VIRUS 1 GAG-PRO POLIPROTEIN DERIVED PEPTIDE SDPQIPPPYVEP

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

Citation: Iglesias-Bexiga, Manuel; Luque, Irene; Macias, Maria Jesus. "HUMAN NEDD4 3RD WW DOMAIN COMPLEX WITH HUMAN T-CELL LEUKEMIA VIRUS GAP-PRO POLIPROTEIN DERIVED PEPTIDE"  Not known ., .-..

Assembly members:
PROTEIN, polymer, 49 residues, 4100.688 Da.
PEPTIDE, polymer, 12 residues, 1039.193 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):
PROTEIN: GAMGPSEIEQGFLPKGWEVR HAPNGRPFFIDHNTKTTTWE DPRLKIPAH
PEPTIDE: SDPQIPPPYVEP

Data sets:
Data typeCount
13C chemical shifts122
15N chemical shifts46
1H chemical shifts399

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NEDD4 3RD WW1
2T-CELL LEUKEMIA VIRUS2

Entities:

Entity 1, NEDD4 3RD WW 49 residues - 4100.688 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, T-CELL LEUKEMIA VIRUS 12 residues - 1039.193 Da.

1   SERASPPROGLNILEPROPROPROTYRVAL
2   GLUPRO

Samples:

15Nsample: PROTEIN, [U-100% 15N], 1 mM; PEPTIDE 3 mM; sodium phosphate 20 mM; sodium azide 0.02 v/v; H2O 90%; D2O 10%

15N13Csample: PROTEIN, [U-100% 13C; U-100% 15N], 1 mM; PEPTIDE 3 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
3D CBCA(CO)NH15N13Csampleisotropicsample_conditions_1
3D HNCACB15N13Csampleisotropicsample_conditions_1
3D HCCH-TOCSY15N13Csampleisotropicsample_conditions_1
3D 1H-15N NOESY15Nsampleisotropicsample_conditions_1
3D 1H-13C NOESY15N13Csampleisotropicsample_conditions_1
3D 1H-15N TOCSY15Nsampleisotropicsample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - processing

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16575 18971
PDB
REF XP_011758823 XP_012325247