BMRB Entry 4836

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4836

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Title:
Complete 1H, 13C and 15N Backbone Assignments for the Hepatitis A Virus 3C Protease
Deposition date:
2000-09-19
Original release date:
2003-01-13
Authors:
Bjorndahl, Trent; Watson, Scott; Slupsky, Carolyn; Spyracopoulos, Leo; Sykes, Brian; Wishart, David
Citation:

Citation: Bjorndahl, Trent; Watson, M.; Slupsky, Carolyn; Spyracopoulos, Leo; Sykes, Brian; Wishart, David. "Letter to the Editor: Complete 1H, 13C and 15N backbone assignments for the hepatitis A virus 3C protease"  J. Biomol. NMR 19, 187-188 (2001).

Assembly members:

Assembly members:
HAV3C, polymer, 217 residues, 23976.59 Da.

Natural source:

Natural source:   Common Name: Hepatitis A   Taxonomy ID: 39112   Superkingdom: Virus   Kingdom: Flaviviridae   Genus/species: Hepatitis not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHAV-3CEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HAV3C: STLEIAGLVRKNLVQFGVGE KNGSVRWVMNALGVKDDWLL VPSHAYKFEKDYEMMEFYFN RGGTYYSISAGNVVIQSLDV GFQDVVLMKVPTIPKFRDIT QHFIKKGDVPRALNRLATLV TTVNGTPMLISEGPLKMEEK ATYVHKKNDGTTVDLTVDQA WRGKGEGLPGMCGGALVSSN QSIQNAILGIHVAGGNSILV AKLVTQEMFQNIDKKIE

Data sets:
Data typeCount
1H chemical shifts414
13C chemical shifts615
15N chemical shifts206

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Hepatis A 3C Protease1

Entities:

Entity 1, Hepatis A 3C Protease 217 residues - 23976.59 Da.

1   SERTHRLEUGLUILEALAGLYLEUVALARG
2   LYSASNLEUVALGLNPHEGLYVALGLYGLU
3   LYSASNGLYSERVALARGTRPVALMETASN
4   ALALEUGLYVALLYSASPASPTRPLEULEU
5   VALPROSERHISALATYRLYSPHEGLULYS
6   ASPTYRGLUMETMETGLUPHETYRPHEASN
7   ARGGLYGLYTHRTYRTYRSERILESERALA
8   GLYASNVALVALILEGLNSERLEUASPVAL
9   GLYPHEGLNASPVALVALLEUMETLYSVAL
10   PROTHRILEPROLYSPHEARGASPILETHR
11   GLNHISPHEILELYSLYSGLYASPVALPRO
12   ARGALALEUASNARGLEUALATHRLEUVAL
13   THRTHRVALASNGLYTHRPROMETLEUILE
14   SERGLUGLYPROLEULYSMETGLUGLULYS
15   ALATHRTYRVALHISLYSLYSASNASPGLY
16   THRTHRVALASPLEUTHRVALASPGLNALA
17   TRPARGGLYLYSGLYGLUGLYLEUPROGLY
18   METCYSGLYGLYALALEUVALSERSERASN
19   GLNSERILEGLNASNALAILELEUGLYILE
20   HISVALALAGLYGLYASNSERILELEUVAL
21   ALALYSLEUVALTHRGLNGLUMETPHEGLN
22   ASNILEASPLYSLYSILEGLU

Samples:

sample_1: HAV3C, [U-15N], 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_2: HAV3C, [U-15N; U-13C], 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_3: HAV3C, [U-15N; U-13C; U-2H], 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_4: HAV3C, [98% 15N]-Gly, 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_5: HAV3C, [98% 15N]-Leu, 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_6: HAV3C, [98% 15N]-Ile, 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_7: HAV3C, [98% 15N]-Val, 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_8: HAV3C, [98% 15N]-Lys, 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_9: HAV3C, [98% 15N]-Ala, 1 mM; KH2PO4 20 mM; NaCl 100 mM

sample_10: HAV3C, [98% 15N]-Phe, 1 mM; KH2PO4 20 mM; NaCl 100 mM

conditions_1: pH: 5.4; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
HNCOnot availablenot availablenot available

Software:

NMR-PIPE - specta processing, peak picking, spectral analysis

PIPP - peak picking, spectral analysis

NMR spectrometers:

  • Varian Unity 500 MHz

Related Database Links:

BMRB 16837
PDB
DBJ BAA35102 BAA35103 BAA35104 BAA35105 BAA35106
EMBL CAA33491 CAA50195 CAA53024 CAA53025 CAA53026
GB AAA45465 AAA45466 AAA45467 AAA45468 AAA45469
PIR GNNYHB
REF NP_041007 NP_041008 NP_740558
SP A3FMB2 A5LGW7 P06441 P08617 P13901
AlphaFold A3FMB2 A5LGW7 P06441 P08617 P13901

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks