SHIFTS takes a protein structure in Brookhaven (PDB) format, and computes
proton chemical shifts from empirical formulas. It can also compute
N, Cα, Cβ and C' shifts in proteins, using a database based
on DFT calculations on peptides.
Note: The SHIFTS package used to include quantum calculations of
shifts. These have been separated into a separate package,
The basic ideas are presented in the
- K. Osapay and D.A. Case. A new analysis of proton chemical
shifts in proteins. J. Am. Chem. Soc.
113, 9436-9444 (1991).
- K. Osapay and D.A. Case. Analysis of proton chemical shifts in
regular secondary structure of proteins. J. Biomol. NMR
4, 215-230 (1994).
- D.F. Sitkoff and D.A. Case. Density functional calculations of proton
shifts in model peptide systems. J. Am. Chem. Soc. 119,
- D. Sitkoff and D.A. Case. Theories of chemical shift anisotropies in
proteins and nucleic acids. Prog. NMR Spectr. 32, 165-190 (1998).
- A. Dejaegere and D.A. Case. Density functional study of ribose and
deoxyribose chemical shifts. J. Phys. Chem. 102, 5280-5289 (1998).
- A.P. Dejaegere, R.A. Bryce and D.A. Case. An empirical analysis of
shifts in nucleic acids. In Modeling NMR Chemical Shifts, J.C.
Facelli and A.C. de Dios, eds. (Washington, American Chemical Society, 1999),
- X.P Xu and D.A. Case. Automated prediction of 15N,
13Cα, 13Cβ and 13C' chemical shifts in proteins
using a density functional database. J. Biomol. NMR. 21, 321-333
- X.P. Xu and D.A. Case. Probing multiple effects on 15N,
13Cα, 13Cβ and 13C' chemical shifts in peptides
using density functional theory. Biopolymers 65, 408-423 (2002).
- S. Moon and D.A. Case. A new model for chemical shifts of amide hydrogens
in proteins. J. Biomol. NMR 38, 139-150 (2007).
The latest version (5.6, June, 2018) can be obtained from:
Some version history:
- Version 4.1.2 is a minor bug-fix release compared to versions 4.1 and 4.1.1,
required primarily for some Linux machines and for compatibility with the
latest version of NAB. If you have version 4.1 or 4.1.1, and it passes the
test suite, you should not need to download the updated version.
- Version 4.2 adds a new model for estimating amide proton shifts in proteins.
It is described in paper 9, above.
- Version 4.3 just has a minor fix to the
lsq program, and updates the
- Version 5.0 is a major rewrite; it updates the empirical formulaas for
proton shifts in nucleic acids, and adds the afnmr capability, described in
papers 10-15 above. Version 5.0.1 contains minor tweaks and adds a
protein-DNA complex example.
- Version 5.1 is an update to coincide with AmberTools16.
- Version 5.2 fixes a bug in fragmentation that could sometimes leave out
carbonyl acceptors in proteins; adds better support for water and ligands, and
for choosing which residues to analyze.
- Version 5.3 slightly modifies the minimization procedure; uses residue
numbers from the input pdb file (rather than a sequential number starting at
- Version 5.4 mainly changes the default basis sets (to the pcSseg-n group
from Frank Jensen), and adds other, mostly minor, convenience features.
- Version 5.5 includes some code cleanup, and support for deMon version 5.
- Version 5.6 has fixes for AmberTools20, removes some remaining
remnants of afnmr.
You will need the AmberTools package (see
in order to compile SHIFTS.
Both AmberTools and SHIFTS are distributed under the GNU General Public License (GPL).
Updated on December 1, 2022. Comments to firstname.lastname@example.org