BMRB: 5241

1H and 15N assignment and secondary structure of the double K18G/R82E mutant of Alicyclobacillus acidocaldarius thermostable thioredoxin

Authors

Leone, M., Di Lello, P., Pedone, E.MARIA., Bartolucci, S., Rossi, M., Di Blasio, B., Pedone, C., Saviano, M., Isernia, C., Fattorusso, R.

Assembly

Thioredoxin

Entity

1. Thioredoxin (polymer, Thiol state: all disulfide bound), 105 monomers, 11478.02 Da Detail

ATMTLTDANF QQAIQGDGPV LVDFWAAWCG PCRMMAPVLE EFAEAHADKV TVAKLNVDEN PETTSQFGIM SIPTLILFKG GEPVKQLIGY QPKEQLEAQL ADVLQ

Formula weight

11478.02 Da

Entity Connection

disulfide 1 Detail

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ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS29:SG	1:CYS32:SG

Source organism

Alicyclobacillus acidocaldarius subsp. acidocaldarius

Exptl. method

NMR

Refine. method

TORSION ANGLE DINAMICS AND RESTRAINED ENERGY MINIMIZATION

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 99.5 %, Completeness (bb): 99.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H	15N
All	99.5 % (731 of 735)	99.5 % (620 of 623)	99.1 % (111 of 112)
Backbone	99.4 % (306 of 308)	99.5 % (209 of 210)	99.0 % (97 of 98)
Sidechain	99.5 % (425 of 427)	99.5 % (411 of 413)	100.0 % (14 of 14)
Aromatic	100.0 % (45 of 45)	100.0 % (43 of 43)	100.0 % (2 of 2)
Methyl	100.0 % (65 of 65)	100.0 % (65 of 65)

1. Alicyclobacillus acidocaldarius thioredoxin

ATMTLTDANF QQAIQGDGPV LVDFWAAWCG PCRMMAPVLE EFAEAHADKV TVAKLNVDEN PETTSQFGIM SIPTLILFKG GEPVKQLIGY QPKEQLEAQL ADVLQ

Show sample condition

Sample

Temperature 298.0 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Alicyclobacillus acidocaldarius thioredoxin	[U-15N]		1.0 mM

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Calculated from 20 models in PDB: 1RQM, Strand ID: A Detail

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Release date

2004-09-09

Citation 1

Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: a molecular analysis of its reduced thermal stability
Leone, M., Di Lello, P., Ohlenschlager, O., Pedone, E.MARIA., Bartolucci, S., Rossi, M., Di Blasio, B., Pedone, C., Saviano, M., Isernia, C., Fattorusso, R.
Biochemistry (2004), 43, 6043-6058, PubMed 15147188 , DOI 10.1021/bi036261d , Abstract

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Citation 2

A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli
Pedone, E., Saviano, M., Rossi, M., Bartolucci, S.
Protein Eng. (2001), 14, 255-260, PubMed 11391017 , DOI: , Abstract

Citation 3

NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability
Nicastro, G., De Chiara, C., Pedone, E., Tato, M., Rossi, M., Bartolucci, S.
Eur. J. Biochem. (2000), 267, 403-413, PubMed 10632710 , DOI: , Abstract

Citation 4

Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling
Bartolucci, S., Guagliardi, A., Pedone, E., De Pascale, D., Cannio, R., Camardella, L., Rossi, M., Nicastro, G., de Chiara, C., Facci, P., Mascetti, G., Nicolini, C.
Biochem. J. (1997), 328 ( Pt 1), 277-285, PubMed 9359865 , DOI: , Abstract

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Entries sharing articles BMRB: 2, Swiss-Prot: 1 entries Detail

Related entities 1. Thioredoxin, : 1 : 4 : 252 entities Detail

Experiments performed 8 experiments Detail