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 15522

Title: Solution structure of pUL89(580-600) from Human Cytomegalovirus at pH 6.8.

Deposition date: 2007-10-12 Original release date: 2007-10-17

Authors: Couvreux, Anthony; Champier, Gael; Marquant, Rodrigue; Hantz, Sebastien; Alain, Sophie; Morellet, Nelly; Bouaziz, Serge

Citation: Couvreux, Anthony; Champier, Gael; Marquant, Rodrigue; Hantz, Sebastien; Alain, Sophie; Morellet, Nelly; Bouaziz, Serge. "Solution structure of the small terminase subunit interaction domain of pUL89 within the Human Cytomegalovirus terminase complex."  Biochem. J. ., .-..

Assembly members:
pUL89(580-600), polymer, 21 residues, 2403.760 Da.

Natural source:   Common Name: Human herpesvirus 5   Taxonomy ID: 10359   Superkingdom: Viruses   Kingdom: not available   Genus/species: Cytomegalovirus Human herpesvirus 5

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
pUL89(580-600): GRDKALAVEQFISRFNSGYI K

Data sets:
Data typeCount
1H chemical shifts300

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 21 residues - 2403.760 Da.

1   GLYARGASPLYSALALEUALAVALGLUGLN
2   PHEILESERARGPHEASNSERGLYTYRILE
3   LYS

Samples:

sample: pUL89(580-600) 1.4 mM; TFE, [U-99% 2H], 30%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 280 K

sample_conditions_2: pH: 2.8; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsampleisotropicsample_conditions_1
2D 1H-1H NOESYsampleisotropicsample_conditions_1

Software:

FELIX v98.0, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16452
PDB
EMBL CAA35363
GB AAC40814 AAR31641 AAS48974 ABF47048 ABF47049
REF YP_081537
SP F5HCU8 P16732
TPG DAA00186