Table 3.
Measurement | Sample | Experiment(s)† | Time‡ (hrs.) |
Ref. |
---|---|---|---|---|
NOE-derived distance restraints |
Rhodobacter capsulatus ferrocytochrome c2 |
(4,3)-D 13C/15N-NOESY (4,3)-D 15N/15N-NOESY |
not given |
[119] |
Backbone assignment | residues 1-68 of merA from Ralstonia metallidurans CH34 |
(3,2)-D HNCA, HN(CO)CA, HN(CA)CB, HN(COCA)CB, HN(CA)HA, HN(COCA)HA |
14 | [50] |
Backbone assignment | 1.5 mM ubiquitin | (3,2)-D HNCA, HN(CO)CA (4,2)-D HACANH |
not given |
[55] |
Solid-state backbone assignment |
histidine | (3,2)-D MAS NCC | not given |
[128] |
Backbone assignment | 2 mM ubiquitin | (5,2)-D HACACONH | 2.3 | [52] |
Backbone assignments | 1.5 mM ubiquitin 1.1 mM 21 kDa bovine S100A1 |
(4,2)-D HNCACB and HN(CO)CACB, with Cα and Cβcoevolved as an MQ coherence producing only the DQ (Cα+Cβ) peak |
Not given |
[120] |
Backbone assignments | 1.5 mM ubiquitin | (3,2)-D HNCO, HNCA, HN(CO)CA, H(N)COCA; (4,2)-D HNCOCA (all MQ) |
not given |
[121] |
Backbone and sidechain assignments |
1.4 mM ubiquitin | (3,2)-D HNCO, HNCACB, HN(CO)CACB, HN(CA)CO, HNCA, HN(CO)CA, CBCANH, CBCA(CO)NH, C(CCO)NH, H(CCCO)NH |
18 | [129] |
Backbone and Cβ assignment | 2 mM ubiquitin, 1 mM TT212 |
(5,2)-D intra-HACACONN and HACACONH; (5,3)-D intra-<HACA,CO>NH and HACACONH; (4,3)-D intra-<CBCA,CO>NH and CBCACONH |
42.6, 62.6 |
[122] |
Backbone and sidechain assignments |
1 mM 17 kDa ER75, 1 mM 13 kDa PfR13, 2 mM ubiquitin |
(4,2)-D HCCH; (4,3)-D Cα/βCα(CO)NH, L- HN(CO)Cα/βCα, HNCα/βCα and L-HNCα/βCα; (5,3)-D Hα/βCα/βCα(CO)NH and HCCCH; (6,3)-D Hα/βCα/βCαCONH |
224, 32, 68.8 |
[124] |
Backbone and sidechain assignments [also reported structures using non-GFT time-shared NOESY] |
8 targets from the NESH consortium, at ~1 mM each |
(4,3)-D Hα/βCα/β(CO)NH and HCCH [plus previously published (4,3)-D Cα/βCα(CO)NH, L- HN(CO)Cα/βCα; and (5,2)-D HACACONH] |
26 to 214 |
[130] |
Structure determination: backbone assignments by previously published protocols; distance constraints from GFT NOESY |
1 mM 14 kDa YqfB | (4,3)-D [HCali/HN]- NOESY-[CHali/NH], which is a time-shared NOESY experiment detecting HCali HCali, HN HCali HCali HN and HN HN [assignment by previously published experiments] |
16.9+, 39 |
[125] |
Dynamics of aromatic rings | 21 kDa HR41, 13 kDa MAR11 |
(4,3)-D L-HCCH and L- TROSY-HCCH |
24, 0.42 |
[131] |
Backbone assignments | 0.8 mM 17 kDa yqbG, 13.5 kDa rps24e, 8 kDa protein Z-domain, ubiquitin, 13.5 kDa rps24e |
various combinations of (5,3)-D HN{NCO} {Cα/βCα}, intra-HN{<N,CO>} {Cα/βCα}, intra-HN{<N,CO>} {Cα/βHα}, {HαCα}{CON}NH HN{NCα}{Cα/βCα}, HN{N(CO)Cα}{Cα/βCα} and (6,3)-D {Hα/βCα/βCα}{CON}NH, with and without L-optimization and/or TROSY |
7 to 44 | [109] |
Residual dipolar couplings | 8 kDa protein Z- domain |
(6,2)-D (HA-CA-CO)-N- HN |
24 | [123] |
Sidechain assignments | Nck Sh3-1 | (4,3)-D HC(CO)NH- TOCSY, with nonuniform sampling and MaxEnt reconstruction in both the combined HC dimension and the conventional N dimension |
48 | [127] |
Membrane protein backbone And sidechain assignments |
Subunit c of F1F0 ATP synthase in micelles |
previously published (3,2)- D HNNCO; (4,3)-D L- HNCα/βCα, L-HN(CO)Cα/βCα HCCH; (4,2)-D HACA(CO)NH; (5,3)-D intra-HN{<N,CO>}{Cα/βCα} and {Cα/βCα}{CON}NH |
118 | [132] |
Scalar coupling constants | 9.5 kDa M-crystallin 16.2 kDa Eh-CaBP |
(3,2)-D quantitative-J HNHA, HNHB |
1.5 to 18 |
[133] |
Pseudocontact shifts | 8.5 kDa calbindin | previously published (3,2)- D HNCO, HN(CO)CA, HN(COCA)CB, HNHA |
7.5 | [134] |
NOE-derived distance restraints |
1.4 mM ubiquitin | (4,3)-D time-shared NOESY detecting HN CH and HN NH |
48 | [126] |
(n,m)-D indicates that n dimensions of correlations are collected with m independent evolution times. Underlining indicates coevolved nuclei; underlined nuclei grouped in {curly braces} indicate independen sets of coevolved nuclei. (Parentheses) indicate nuclei through which magnetization is passed, without evolving chemical shifts. <Angled brackets> indicate nuclei involved in bifurcated magnetization transfer. intra- indicates that only the intraresidue peaks are detected. [Square brackets] indicate time-shared evolution of two nuclei, with diagonal slashes separating the nuclei or sets of nuclei that evolve independently. L- indicates that longitudinal relaxation optimization is used. Hyphens between nuclei indicate that the coupling between the nuclei are evolved. The names for some experiments have been adjusted from the original publications to maintain consistency in nomenclature.
The measurement times represent the time reported for running the set of experiments on the sample, or a range of times for multiple samples. Where multiple individual times are listed on separate lines, they correspond to the samples listed in the sample column, and are in the same order. For the YqfB structure determination, a+b indicates a hours for the assignment experiments and b hours for the NOESY.