Table 1.
Sample | Experiment | Scans | F3 | F2 | F1 |
---|---|---|---|---|---|
1H/15N HIV1-CA DM, 10% D2O | TROSY-15N HSQC | 16 | 2,048 | 200 | |
15N NOESY-HSQC, 125 ms mixing time | 24 | 2,048 | 40 | 128 | |
1H/15N HIV1-CA DM, 100% D2O | SOFAST15N HMQC | 8 | 2,048 | 128 | |
1H/13C/15N HIV1-CA DM, 10% D2O | TROSY-HNCA | 16 | 2,048 | 40 | 100 |
TROSY-HNCACB | 32 | 2,048 | 40 | 128 | |
TROSY-CBCA(CO)NH | 32 | 2,048 | 40 | 128 | |
TROSY-HNCO | 16 | 2,048 | 40 | 100 | |
1H/13C/15N HIV1-CA DM, 100% D2O | 13C HSQC | 16 | 2,048 | 256 | |
13C NOESY-HSQC, 175 mixing time | 24 | 2,048 | 64 | 128 | |
13C NOESY-HSQC, 250 mixing time | 24 | 2,048 | 64 | 128 | |
HCCH COSY | 24 | 2,048 | 64 | 128 | |
HCCH TOCSY | 24 | 2,048 | 64 | 128 | |
2H/13C/15N HIV1-CA DM, 10% D2O | TROSY-HNCACB | 32 | 2,048 | 40 | 128 |
2H/13C/15N HIV1-CA DM, 100% D2O | HCCH TOCSY | 32 | 2,048 | 64 | 128 |
The list of 3D-NMR and 2D-NMR experiments (at 600 MHz) that were utilized in the sequence-specific assignment of backbone and sidechain nuclei, as well as identification of structural constraints. Sample conditions were: protein concentration 1.2 mM, 303 K, 25 mM perdeuterated acetate (pH 5.5), 25 mM NaCl, 0.02% azide, and 0.1 mM AEBSF, 10 mM DTT. 15N-, 15N/13C- and 15N/13C/2H (70%)-labeled proteins were utilized as appropriate. DM refers to double mutant (W184A/M185A-CA)