A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex
Protein Sci
Katoh et al. 12 (7): 1376.
Supplemental Research Data
Files in this Data Supplement:
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This file contains the following 4 tables:
Table S1. Backbone chemical shifts for the inactive protease, PRD25N.
Table S2. Backbone assignment of PRD25N bound to substrate C.
Table S3. 15N relaxation data of PRD25N.
Table S4. 15N relaxation data of PRD25N bound to substrate C.
