BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 6638

Title: 1H, 15N, and 13C assignments of N-terminal domain of Epstein-Barr Virus Latent Membrane Protein 2A   PubMed: 15802216

Deposition date: 2005-05-18 Original release date: 2006-08-11

Authors: Seo, Min-Duk; Park, Sung-Jean; Lee, Bong-Jin

Citation: Park, Sung-Jean; Seo, Min-Duk; Lee, S.; Ikeda, M.; Longnecker, R.; Lee, Bong-Jin. "Expression and characterization of N-terminal domain of Epstein-Barr Virus latent membrane protein 2A in Escherichia coli"  Protein Expr. Purf. 41, 9-17 (2005).

Assembly members:
lmp2a NTD, polymer, 122 residues, Formula weight is not available

Natural source:   Common Name: Epstein Barr Virus   Taxonomy ID: 10298   Superkingdom: Viruses   Kingdom: Not applicable   Genus/species: Simplexvirus Human herpesvirus 1

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
lmp2a NTD: GRAMGSLEMVPMGAGPPSPG GDPDGYDGGNNSQYPSASGS SGNTPTPPNDEERESNEEPP PPYEDPYWGNGDRHSDYQPL GTQDQSLYLGLQHDGNDGLP PPPYSPRDDSSQHIYEEAGR GS

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts101
1H chemical shifts437

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lmp2a NTD1

Entities:

Entity 1, lmp2a NTD 122 residues - Formula weight is not available

1   GLYARGALAMETGLYSERLEUGLUMETVAL
2   PROMETGLYALAGLYPROPROSERPROGLY
3   GLYASPPROASPGLYTYRASPGLYGLYASN
4   ASNSERGLNTYRPROSERALASERGLYSER
5   SERGLYASNTHRPROTHRPROPROASNASP
6   GLUGLUARGGLUSERASNGLUGLUPROPRO
7   PROPROTYRGLUASPPROTYRTRPGLYASN
8   GLYASPARGHISSERASPTYRGLNPROLEU
9   GLYTHRGLNASPGLNSERLEUTYRLEUGLY
10   LEUGLNHISASPGLYASNASPGLYLEUPRO
11   PROPROPROTYRSERPROARGASPASPSER
12   SERGLNHISILETYRGLUGLUALAGLYARG
13   GLYSER

Samples:

sample_1: lmp2a NTD, [U-13C; U-15N], 0.5 mM; Na phosphate 50 mM; NaCl 100 mM; EDTA 1 mM

conditions_1: ionic strength: 0.1 M; pH: 6.0; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
HNCAsample_1not availableconditions_1
HNCOCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCACONHnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCACOnot availablenot availablenot available
HBHACONHnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available
15N-TOCSYnot availablenot availablenot available

Software:

NMRPipe -

NMR spectrometers:

  • Bruker Avance DMX 600 MHz

Related Database Links:

DBJ BAF80317 BAF80319 BAF80320 BAF80321
EMBL CAA57360 CAA57363 CAA57365 CAA57366 CAA57369
GB AAA45887 AAS64577 ABB89217 ADK56647 ADK56649
REF YP_001129436 YP_401631
SP P0C729 P13285 Q1HVJ2

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts