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Backbone 1HN and 15N Chemical Shift Assignments for Sac7d V30I
Authors
Clark, A.T., McCrary, B.S., Edmondson, S.P., Shriver, J.W.
Assembly
Sac7d V30I monomer
Entity
1. Sac7d V30I monomer (polymer, Thiol state: not present), 66 monomers, 7622.794 Da Detail

MVKVKFKYKG EEKEVDTSKI KKVWRVGKMI SFTYDDNGKT GRGAVSEKDA PKELLDMLAR AEREKK


Formula weight
7622.794 Da
Source organism
Sulfolobus acidocaldarius
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 97.0 %, Completeness: 31.7 %, Completeness (bb): 66.2 % Detail

Polymer type: polypeptide(L)

Total1H15N
All31.7 % (158 of 499)21.3 % (92 of 432)98.5 % (66 of 67)
Backbone66.2 % (133 of 201)50.7 % (69 of 136)98.5 % (64 of 65)
Sidechain 8.4 % (25 of 298) 7.8 % (23 of 296)100.0 % (2 of 2)
Aromatic20.0 % (5 of 25)16.7 % (4 of 24)100.0 % (1 of 1)
Methyl 6.9 % (2 of 29) 6.9 % (2 of 29)

1. Sac7d

MVKVKFKYKG EEKEVDTSKI KKVWRVGKMI SFTYDDNGKT GRGAVSEKDA PKELLDMLAR AEREKK

Sample

Temperature 303 (±1) K, pH 4.06 (±0.1)


#NameIsotope labelingTypeConcentration
1Sac7d[U-98% 15N]1.18 mM
2KCl0.3 M
3H2O90 %
4D2O10 %
5DSS100 uM

Protein Blocks Logo
Calculated from 1 models in PDB: 1SAP, Strand ID: A Detail


Release date
2003-10-05
Citation 1
Thermodynamics of Hydrophobic Core Packing in the Thermophile Proteins Sac7d and Sso7d
Clark, A.T., McCrary, B.S., Edmondson, S.P., Shriver, J.W.
J. Mol. Biol.
Citation 2
Binding of proteins to the minor groove of DNA: what are the structural and energetic determinants for kinking a basepair step?
Bosch, D., Campillo, M., Pardo, L.
J. Comput. Chem. (2003), 24, 682-691, PubMed 12666159 , DOI 10.1002/jcc.10200 ,
Citation 3
DNA bending, compaction and negative supercoiling by the architectural protein Sso7d of Sulfolobus solfataricus
Napoli, A., Zivanovic, Y., Bocs, C., Buhler, C., Rossi, M., Forterre, P., Ciaramella, M.
Nucleic Acids Res. (2002), 30, 2656-2662, PubMed 12060682 ,
Citation 4
DNA binding proteins Sac7d and Sso7d from Sulfolobus
Edmondson, S.P., Shriver, J.W.
Methods. Enzymol. (2001), 334, 129-145, PubMed 11398456 , DOI: ,
Citation 5
The acid-induced folded state of Sac7d is the native state
Bedell, J.L., McCrary, B.S., Edmondson, S.P., Shriver, J.W.
Protein Sci. (2000), 9, 1878-1888, PubMed 11106160 , DOI 10.1110/ps.9.10.1878 ,
Citation 6
Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs
Su, S., Gao, Y.G., Robinson, H., Liaw, Y.C., Edmondson, S.P., Shriver, J.W., Wang, A.H.
J. Mol. Biol. (2000), 303, 395-403, PubMed 11031116 , DOI 10.1006/jmbi.2000.4112 ,
Citation 7
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
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J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 ,
Citation 8
Effect of artificial periodicity in simulations of biomolecules under Ewald boundary conditions: a continuum electrostatics study
Hunenberger, P.H., McCammon, J.A.
Biophys. Chem. (1999), 78, 69-88, PubMed 10343384 , DOI: ,
Citation 9
Molecular dynamics simulations of the hyperthermophilic protein sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability
de Bakker, P.I., Hunenberger, P.H., McCammon, J.A.
J. Mol. Biol. (1999), 285, 1811-1830, PubMed 9917414 , DOI 10.1006/jmbi.1998.2397 ,
Citation 10
The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA
Gao, Y.G., Su, S.Y., Robinson, H., Padmanabhan, S., Lim, L., McCrary, B.S., Edmondson, S.P., Shriver, J.W., Wang, A.H.
Nat. Struct. Biol. (1998), 5, 782-786, PubMed 9731772 , DOI 10.1038/1822 ,
Citation 11
The hyperthermophile chromosomal protein Sac7d sharply kinks DNA
Robinson, H., Gao, Y.G., McCrary, B.S., Edmondson, S.P., Shriver, J.W., Wang, A.H.
Nature (1998), 392, 202-205, PubMed 9515968 , DOI 10.1038/32455 ,
Citation 12
Linkage of protonation and anion binding to the folding of Sac7d
McCrary, B.S., Bedell, J., Edmondson, S.P., Shriver, J.W.
J. Mol. Biol. (1998), 276, 203-224, PubMed 9514720 , DOI 10.1006/jmbi.1998.1500 ,
Citation 13
Overproduction of Sac7d and Sac7e reveals only Sac7e to be a DNA-binding protein with ribonuclease activity from the extremophilic archaeon Sulfolobus acidocaldarius
Kulms, D., Schafer, G., Hahn, U.
Biol. Chem. (1997), 378, 545-551, PubMed 9224936 , DOI: ,
Citation 14
Hyperthermophile protein folding thermodynamics: differential scanning calorimetry and chemical denaturation of Sac7d
McCrary, B.S., Edmondson, S.P., Shriver, J.W.
J. Mol. Biol. (1996), 264, 784-805, PubMed 8980686 , DOI 10.1006/jmbi.1996.0677 ,
Citation 15
Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: fluorescence and circular dichroism studies
McAfee, J.G., Edmondson, S.P., Zegar, I., Shriver, J.W.
Biochemistry (1996), 35, 4034-4045, PubMed 8672437 , DOI 10.1021/bi952555q ,
Citation 16
Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius
Edmondson, S.P., Qiu, L., Shriver, J.W.
Biochemistry (1995), 34, 13289-13304, PubMed 7577913 , DOI: ,
Citation 17
Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius
McAfee, J.G., Edmondson, S.P., Datta, P.K., Shriver, J.W., Gupta, R.
Biochemistry (1995), 34, 10063-10077, PubMed 7632679 , DOI: ,
Related entities 1. Sac7d V30I monomer, : 1 : 8 : 74 entities Detail
Experiments performed 3 experiments Detail
nullKeywords hyperthermophile, Sulfolobus, calorimetry, nuclear magnetic resonance