RELAXFIT
A program for extracting relaxation rates (e.g. R₁ or R₂) from fitting experimental data to an exponentially decaying function.
Reference: Fushman et al., J. Mol. Biol. 266 (1997) 173.

DYNAMICS
A program for model-free analysis of ¹⁵N relaxation data.
Features isotropic, axially-symmetric and fully anisotropic models for the overall tumbling of the molecule, and monomer-dimer equilibration. Allows input of site-specific ¹⁵N CSA values or their determination, together with model-free parameters, when relaxation data at multiple fields are available.
References: Fushman et al., J. Mol. Biol. 266 (1997) 173; J.B.Hall & D.Fushman, J. Biomol. NMR (2003) 27, 261; J.B.Hall & D.Fushman, J. Amer. Chem. Soc. (2006) 128, 7855-7870; D.Fushman, "Determining protein dynamics from 15N relaxation data by using DYNAMICS", in Protein NMR Techniques, Third Edition, Eds. A. Shekhtman, D. S. Burz, Methods in Molecular Biology, 2012, Volume 831, 485-511, Springer Science, DOI: 10.1007/978-1-61779-480-3_24.

ROTDIF
A program for determining the overall rotational diffusion tensor of a molecule from spin-relaxation data.
Features isotropic, axially-symmetric, and fully anisotropic models for the overall motion.
Reference: Fushman et al., Biochemistry 38 (1999) 10225-10230; Varadan et al., JMB 324 (2002) 637; Walker et al. J. Magn. Reson. (2004) 168, 336; Fushman et al, Progress NMR Spectroscopy, (2004) 44, 189.

ROTDIF 3
A redesigned version of the program ROTDIF for determining the overall rotational diffusion tensor of a molecule from spin-relaxation data.
This version is written in Java and features a Graphical User Interface. Allows analysis of ¹⁵N and ¹³C relaxation data, separately or together, at a single or multiple fields, for proteins and/or nucleic acids. Also estimates model-free parameters. Features isotropic, axially-symmetric, and fully anisotropic models for the overall motion. The program also includes modules for prediction of the rotational diffusion tensor from atom coordinates using ellipsoid model (ELM), and for diffusion-tensor-based rigid-body docking of macromolecules (ELMDOCK).
Reference: K.Berlin, A.Longhini, T.K.Dayie, D.Fushman, J Biomol NMR (2013), 57, 333-352.

SES
A program for recovering a representative conformational ensemble of a macromolecule from (underdetermined) experimental data using sparce-ensemble selection (SES) combined with multi-orthogonal matching pursuit (Multi-OMP). Currently features analysis of residual dipolar coupling (RDC) data.
Reference: Berlin et al., JACS 135 (2013) 16595.

ALTENS
A program for determining the alignment tensor of a molecule from residual dipolar coupling (RDC) data, using singular value decomposition.
Reference: Varadan et al., JMB 324 (2002) 637; Fushman et al, Progress NMR Spectroscopy, (2004) 44, 189.

SLFIT
A program for determining the location of a paramagnetic center from analysis of Paramagnetic Relaxation Enhancement (PRE) data.
References: (1) Ryabov Ya. & Fushman D., Proteins, 63, pp.787-796 (2006). (2) D'Onofrio et al., Chemistry 18, 9919-9928 (2012).

PATI
A program for predicting the alignment tensor of a molecule and the residual dipolar couplings (RDCs) under steric alignment caused by planar objects, and for determining the alignment tensor from experimental RDC data using singular value decomposition.
Features isotropic, axially-symmetric, and fully anisotropic models for the overall motion. The program also includes a module for alignment-tensor-based rigid-body orientation and docking of macromolecules (PATIDOCK)
Reference: K.Berlin, D.P.O’Leary, D.Fushman, J. Magn. Reson (2009) 201, 25-33.

ETAFIT
A program for the determination of the magnitude and orientation of the ¹⁵N chemical shift anisotropy from the field dependence of the ratio, h /R₂, of the CSA/dipolar cross-correlation term h and the ¹⁵N transverse relaxation rate R₂. Requires relaxation data measured at 2 or more fields.
Reference: Fushman et al., J. Amer. Chem. Soc. 120 (1998) 10947-10952.

PICK
A program for automatic peak picking in a 2D spectrum given a reference peak list.
Features reading-in spectra produced with TopSpin and full peak-list export/importability with CARA.