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 18933

Title: ASFV Pol X structure   PubMed: 24617852

Deposition date: 2013-01-03 Original release date: 2014-03-31

Authors: Wu, Wen-Jin; Su, Mei-I; Tsai, Ming-Daw

Citation: Wu, Wen-Jin; Su, Mei-I; Wu, Jian-Li; Kumar, Sandeep; Lim, Liang-Hin; Wang, Chun-Wei Eric; Nelissen, Frank; Chen, Ming-Chuan Chad; Doreleijers, Jurgen; Wijmenga, Sybren; Tsai, Ming-Daw. "How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation."  J. Am. Chem. Soc. 136, 4927-4937 (2014).

Assembly members:
entity, polymer, 174 residues, 20351.670 Da.

Natural source:   Common Name: African Swine Fever Virus   Taxonomy ID: 10497   Superkingdom: Viruses   Kingdom: not available   Genus/species: Asfivirus African Swine Fever Virus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-17b

Entity Sequences (FASTA):
entity: MLTLIQGKKIVNHLRSRLAF EYNGQLIKILSKNIVAVGSL RREEKMLNDVDLLIIVPEKK LLKHVLPNIRIKGLSFSVKV CGERKCVLFIEWEKKTYQLD LFTALAEEKPYAIFHFTGPV SYLIRIRAALKKKNYKLNQY GLFKNQTLVPLKITTEKELI KELGFTYRIPKKRL

Data sets:
Data typeCount
13C chemical shifts430
15N chemical shifts154
1H chemical shifts154

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ASFV Pol X1

Entities:

Entity 1, ASFV Pol X 174 residues - 20351.670 Da.

1   METLEUTHRLEUILEGLNGLYLYSLYSILE
2   VALASNHISLEUARGSERARGLEUALAPHE
3   GLUTYRASNGLYGLNLEUILELYSILELEU
4   SERLYSASNILEVALALAVALGLYSERLEU
5   ARGARGGLUGLULYSMETLEUASNASPVAL
6   ASPLEULEUILEILEVALPROGLULYSLYS
7   LEULEULYSHISVALLEUPROASNILEARG
8   ILELYSGLYLEUSERPHESERVALLYSVAL
9   CYSGLYGLUARGLYSCYSVALLEUPHEILE
10   GLUTRPGLULYSLYSTHRTYRGLNLEUASP
11   LEUPHETHRALALEUALAGLUGLULYSPRO
12   TYRALAILEPHEHISPHETHRGLYPROVAL
13   SERTYRLEUILEARGILEARGALAALALEU
14   LYSLYSLYSASNTYRLYSLEUASNGLNTYR
15   GLYLEUPHELYSASNGLNTHRLEUVALPRO
16   LEULYSILETHRTHRGLULYSGLULEUILE
17   LYSGLULEUGLYPHETHRTYRARGILEPRO
18   LYSLYSARGLEU

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N; U-80% 2H], 1.0 mM; DTT, [U-2H], 10 mM; potassium chloride 50 mM; borate 50 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 1.0 mM; DTT, [U-2H], 10 mM; potassium chloride 50 mM; borate 50 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

HADDOCK, Dr. Alexandre Bonvin - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18934 18935
PDB
EMBL CAN10196 CAN10446 CBH29197
GB AAA65326 AIY22288 AIY22446 AKO62778
PRF 2113434DC
REF NP_042790
SP P0C984 P42494

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