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. Author manuscript; available in PMC: 2013 Jan 1.
Published in final edited form as: Biomol NMR Assign. 2011 Sep 20;6(2):131–134. doi: 10.1007/s12104-011-9340-3

Table 1.

Summary of 2D/3D-NMR measurements

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)