BMRB: 5596

Solution Structure of the hypothetical protein yggU from E. coli. Northeast Structural Genomics Consortium Target ER14.

Authors

Aramini, J.M., Xiao, R., Huang, Y.J., Acton, T.B., Wu, M.J., Mills, J.L., Tejero, R.T., Szyperski, T., Montelione, G.T.

Assembly

yggu

Entity

1. yggu (polymer, Thiol state: not present), 108 monomers, 11882.56 Da Detail

MDGVMSAVTV NDDGLVLRLY IQPKASRDSI VGLHGDEVKV AITAPPVDGQ ANSHLVKFLG KQFRVAKSQV VIEKGELGRH KQIKIINPQQ IPPEVAALIN LEHHHHHH

Formula weight

11882.56 Da

Source organism

Escherichia coli

Exptl. method

NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete

Sequence coverage: 95.4 %, Completeness: 92.3 %, Completeness (bb): 93.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	92.3 % (1159 of 1256)	91.6 % (598 of 653)	92.7 % (454 of 490)	94.7 % (107 of 113)
Backbone	93.4 % (594 of 636)	92.2 % (201 of 218)	94.0 % (297 of 316)	94.1 % (96 of 102)
Sidechain	91.5 % (659 of 720)	91.3 % (397 of 435)	91.6 % (251 of 274)	100.0 % (11 of 11)
Aromatic	56.3 % (36 of 64)	56.3 % (18 of 32)	56.3 % (18 of 32)
Methyl	100.0 % (144 of 144)	100.0 % (72 of 72)	100.0 % (72 of 72)

1. yggu ecoli

MDGVMSAVTV NDDGLVLRLY IQPKASRDSI VGLHGDEVKV AITAPPVDGQ ANSHLVKFLG KQFRVAKSQV VIEKGELGRH KQIKIINPQQ IPPEVAALIN LEHHHHHH

Show sample condition

Sample

Temperature 293 (±0.1) K, pH 6.5 (±0.05), Details Two identical samples were run at two different sites

#	Name	Isotope labeling	Type	Concentration
1	yggu_ecoli	[U-100% 13C; U-100% 15N]		1.0 mM
2	MES			20 mM
3	NaCL			50 mM
4	DTT			5 mM
5	D2O			5 %

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LACS Plot; CA

Referencing offset: -0.17 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; CB

Referencing offset: -0.17 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; HA

Referencing offset: -0.07 ppm, Outliers: 3 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; CO

Referencing offset: 0.3 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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Protein Blocks Logo

Calculated from 10 models in PDB: 1N91, Strand ID: A Detail

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Coupling constant

27 J values in 1 lists
Temperature 293 (±0.1) K, pH 6.5 (±0.05) Detail

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Temperature 293 (±0.1) K, pH 6.5 (±0.05)

List #1 ER14_JNH_1

Release date

2003-09-04

Citation 1

Resonance assignments for the hypothetical protein yggU from Escherichia coli
Aramini, J.M., Mills, J.L., Xiao, R., Acton, T.B., Wu, M.J., Szyperski, T., Montelione, G.T.
J. Biomol. NMR (2003), 27, 285-286, PubMed 12975589 , DOI: , Abstract

Show more 5 citaions

Citation 2

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment
Szyperski, T., Yeh, D.C., Sukumaran, D.K., Moseley, H.N., Montelione, G.T.
Proc. Natl. Acad. Sci. U. S. A. (2002), 99, 8009-8014, PubMed 12060747 , DOI 10.1073/pnas.122224599 , Abstract

Citation 3

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Citation 4

Automated analysis of protein NMR assignments using methods from artificial intelligence
Zimmerman, D.E., Kulikowski, C.A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R., Montelione, G.T.
J. Mol. Biol. (1997), 269, 592-610, PubMed 9217263 , Abstract

Citation 5

Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., Bax, A.
J. Biomol. NMR (1999), 13, 289-302, PubMed 10212987 , Abstract

Citation 6

Torsion angle dynamics for NMR structure calculation with the new program DYANA
Guntert, P., Mumenthaler, C., Wuthrich, K.
J. Mol. Biol. (1997), 273, 283-298, PubMed 9367762 , DOI 10.1006/jmbi.1997.1284 , Abstract

Hide non-primary 5 citaions

Related entities 1. yggu, : 1 : 1 : 1 : 72 entities Detail

Interaction partners 1. yggu, : 3 interactors Detail

Experiments performed 39 experiments Detail