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Found 1 Document (1.913 seconds)

BMRB: 7106

2JM5

NMR Assignment of human RGS18 (regulator of G-protein signalling)

Authors

Higman, V.A., Leidert, M., Elkins, J., Soundararajan, M., Brockmann, C., Schmieder, P., Sundstrom, M., Arrowsmith, C., Weigelt, J., Edwards, A., Diehl, A., Oschkinat, H., Ball, L.J.

Assembly

RGS18 monomer

Entity

1. RGS18 monomer (polymer, Thiol state: all free), 151 monomers, 17759.80 Da Detail

SMVSPEEAVK WGESFDKLLS HRDGLEAFTR FLKTEFSEEN IEFWIACEDF KKSKGPQQIH LKAKAIYEKF IQTDAPKEVN LDFHTKEVIT NSITQPTLHS FDAAQSRVYQ LMEQDSYTRF LKSDIYLDLM EGRPQRPTNL RRRSRSFTCN E

Formula weight

17759.8 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 89.4 %, Completeness: 84.0 %, Completeness (bb): 88.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	84.0 % (1549 of 1844)	83.0 % (804 of 969)	85.0 % (608 of 715)	85.6 % (137 of 160)
Backbone	88.4 % (790 of 894)	88.7 % (266 of 300)	87.8 % (394 of 449)	89.7 % (130 of 145)
Sidechain	80.9 % (888 of 1097)	80.4 % (538 of 669)	83.1 % (343 of 413)	46.7 % (7 of 15)
Aromatic	80.2 % (146 of 182)	85.7 % (78 of 91)	74.2 % (66 of 89)	100.0 % (2 of 2)
Methyl	92.6 % (126 of 136)	92.6 % (63 of 68)	92.6 % (63 of 68)

1. RGS18

SMVSPEEAVK WGESFDKLLS HRDGLEAFTR FLKTEFSEEN IEFWIACEDF KKSKGPQQIH LKAKAIYEKF IQTDAPKEVN LDFHTKEVIT NSITQPTLHS FDAAQSRVYQ LMEQDSYTRF LKSDIYLDLM EGRPQRPTNL RRRSRSFTCN E

Show sample condition

Sample #1

Temperature 297.0 (±0.2) K, pH 6.0 (±0.05), Details 15N labelled RGS18

#	Name	Isotope labeling	Concentration
1	RGS18	[U-95% 15N]	1.0 mM
2	Sodium Phosphate buffer		20 mM
3	sodium chloride		50 mM

Sample #2

Temperature 297.0 (±0.2) K, pH 6.0 (±0.05), Details 15N,13C labelled RGS18

#	Name	Isotope labeling	Concentration
4	RGS18	[U-95% 15N; U-95% 13C]	1.0 mM
5	Sodium Phosphate buffer		20 mM
6	sodium chloride		50 mM

Sample #3

Temperature 297.0 (±0.2) K, pH 6.0 (±0.05), Details 15N,13C labelled RGS18 in 100% D2O, made from freeze-dried sample2

#	Name	Isotope labeling	Concentration
7	RGS18	[U-95% 15N; U-95% 13C]	1.0 mM
8	Sodium Phosphate buffer		20 mM
9	sodium chloride		50 mM
10	D2O		100 %

LACS Plot; CA

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

Referencing offset: 0.69 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.69 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.15 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: -0.07 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2JM5, Strand ID: A Detail

Release date

2006-08-14

Citation 1

NMR assignment of human RGS18
Higman, V.A., Leidert, M., Diehl, A., Elkins, J., Soundararajan, M., Oschkinat, H., Ball, L.J.
J. Biomol. NMR (2006), 36 Suppl 1, 72-72, PubMed 16964532 , DOI 10.1007/s10858-006-9061-6 , Abstract

Show more 4 citaions

Citation 2

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

Citation 3

Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
Herrmann, T., Guntert, P., Wuthrich, K.
J. Mol. Biol. (2002), 319, 209-227, PubMed 12051947 , DOI: , Abstract

Citation 4

The CCPN data model for NMR spectroscopy: development of a software pipeline
Vranken, W.F., Boucher, W., Stevens, T.J., Fogh, R.H., Pajon, A., Llinas, M., Ulrich, E.L., Markley, J.L., Ionides, J., Laue, E.D.
Proteins (2005), 59, 687-696, PubMed 15815974 , DOI 10.1002/prot.20449 , Abstract

Citation 5

The Xplor-NIH NMR molecular structure determination package
Schwieters, C.D., Kuszewski, J.J., Tjandra, N., Clore, M.
J. Magn. Reson. (2003), 160, 65-73, PubMed 12565051 , DOI: , Abstract

Hide non-primary 4 citaions

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Found 1 Document (1.913 seconds)

BMRB: 7106

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 38 entries Detail

Related entities 1. RGS18 monomer, : 1 : 1 : 3 : 209 entities Detail

Interaction partners 1. RGS18 monomer, : 1 interactors Detail

Experiments performed 15 experiments Detail

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