B

• Best buffer protonation Thermodynamic parameters of buffer protonation
• Best compound protonation pK_a Arithmetic averages of compound pK_a values that fulfill the defined threshold of reliability.
• Best compound protonation ΔH_a Arithmetic averages of compound ΔH_a values that fulfill the defined threshold of reliability.
• Best protein protonation pK_a Arithmetic averages of protein pK_a values that fulfill the defined threshold of reliability.
• Best protein protonation ΔH_a Arithmetic averages of protein ΔH_a values that fulfill the defined threshold of reliability.
• Buffers Buffer composition

C

• Compound batches Properties of synthesized chemical compound batches
• Compounds Compound (ligand) properties
• Crystal structures X-ray crystallographic structures of protein-ligand complexes

D

• Devices Instruments used for measurements

F

• FTSA experiments Fluorescent thermal shift assay (FTSA, TSA, DSF, ThermoFluor, TF) experimental data

I

• Intrinsic parameters The thermodynamic parameters of protein-ligand interaction, corrected to account for linked protonation reactions.
• ITC experiments Isothermal titration calorimetry (ITC) experimental data

K

• K_b,int Intrinsic binding constants (calculated from FTSA and protonation data)

• K_d,int Intrinsic dissociation constants (calculated from FTSA and protonation data)
• K_d,obs Observed dissociation constants (from FTSA experiments data)

P

• Protein batches Purified protein batches
• Proteins Protein properties and origins
• Publications The list contains publications used as PLBD data sources

R

• Revisions Data revisions of Protein-Ligand Binding Database

S

• SFA experiments Experimental data of stopped-flow assay (SFA) of enzyme inhibition
• SPR experiments Experimental data of surface plasmon resonance

V

• Versions Versions of Protein-Ligand Binding Database schema

Δ

• ΔG_b,int The intrinsic Gibbs energy changes upon binding (calculated from FTSA and protonation data)
• ΔG_b,obs The observed Gibbs energy changes upon binding (from FTSA experiments)
• ΔH_b,int The intrinsic binding enthalpy changes (calculated from ITC and protonation data)