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BMRB: 5701

1R6E

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic GEF domain of Salmonella SopE2

Authors

Williams, C.

Assembly

SopE2 momomer

Entity

1. SopE2 momomer (polymer, Thiol state: all free), 172 monomers, 18565.15 Da Detail

GNASEGRAVL TSKTVKDFML QKLNSLDIKG NASKDPAYAR QTCEAILSAV YSNNKDQCCK LLISKGVSIT PFLKEIGEAA QNAGLPGEIK NGVFTPGGAG ANPFVVPLIA SASIKYPHMF INHNQQVSFK AYAEKIVMKE VTPLFNKGTM PTPQQFQLTI ENIANKYLQN AS

Formula weight

18565.15 Da

Source organism

Salmonella enterica

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.3 %, Completeness: 84.8 %, Completeness (bb): 95.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	84.8 % (1691 of 1995)	82.1 % (853 of 1039)	88.1 % (678 of 770)	86.0 % (160 of 186)
Backbone	95.4 % (965 of 1012)	95.1 % (329 of 346)	96.4 % (486 of 504)	92.6 % (150 of 162)
Sidechain	76.9 % (879 of 1143)	75.6 % (524 of 693)	81.0 % (345 of 426)	41.7 % (10 of 24)
Aromatic	32.8 % (42 of 128)	51.6 % (33 of 64)	14.1 % (9 of 64)
Methyl	91.8 % (178 of 194)	91.8 % (89 of 97)	91.8 % (89 of 97)

1. Salmonella SopE2

GNASEGRAVL TSKTVKDFML QKLNSLDIKG NASKDPAYAR QTCEAILSAV YSNNKDQCCK LLISKGVSIT PFLKEIGEAA QNAGLPGEIK NGVFTPGGAG ANPFVVPLIA SASIKYPHMF INHNQQVSFK AYAEKIVMKE VTPLFNKGTM PTPQQFQLTI ENIANKYLQN AS

Show sample condition

Sample

Temperature 298 (±1) K, pH 7.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	Salmonella SopE2	[U-95% 13C; U-90% 15N]		0.5 ~ 1.0 mM

LACS Plot; CA

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

Referencing offset: -0.97 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.97 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: -0.9 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 1 models in PDB: 1R9K, Strand ID: A Detail

Release date

2003-06-11

Citation 1

Assignment of the 1H, 13C and 15N resonances of the catalytic domain of guanine nucleotide exchange factor SopE2 from Salmonella dublin
Williams, C., Galyov, E.E., Bagby, S.
J. Biomol. NMR (2003), 26, 379-380, PubMed 12815267 , Abstract

Show more 2 citaions

Citation 2

Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells
Bakshi, C.S., Singh, V.P., Wood, M.W., Jones, P.W., Wallis, T.S., Galyov, E.E.
J. Bacteriol. (2000), 182, 2341-2344, PubMed 10735884 , DOI: , Abstract

Citation 3

SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell
Friebel, A., Ilchmann, H., Aepfelbacher, M., Ehrbar, K., Machleidt, W., Hardt, W.D.
J. Biol. Chem. (2001), 276, 34035-34040, PubMed 11440999 , DOI 10.1074/jbc.M100609200 , Abstract

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Entries sharing articles Swiss-Prot: 2 entries Detail

  Swiss-Prot: Q7CQD4 released on 2005-03-15
    Title SOPE2_SALTY Entity Guanine nucleotide exchange factor sopE2
  Swiss-Prot: O52623 released on 2005-03-01
    Title SOPE_SALTM Entity Guanine nucleotide exchange factor SopE

Related entities 1. SopE2 momomer, : 1 : 2 : 15 entities Detail

Interaction partners 1. SopE2 momomer, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 20 experiments Detail

1 1H-15N HSQC