1H, 13C, and 15N Chemical Shift Assignments and coupling constants for the HRDC
domain from S. cerevisiae Sgs1 RecQ helicase

A Chain A, Nmr Structure Of The Hrdc Domain From Saccharomyces Cerevisiae Recq Helicase

The ratio used to calculate the 13C and 15N chemical shift is based on the 1H
chemical shift of the H2O signal at 295K.

The 3D structure of the HRDC domain and implications for the Werner and Bloom
syndrome proteins.

Nilges, M. and O' Donoghue, S. (1998) Prog. NMR Spectroscopy 32, 107-139.
Progress in Nuclear Magnetic Resonance Spectroscopy
Ambiguous NOEs and automated NOE assignment

A new software suite, called Crystallography & NMR System (CNS), has been
developed for macromolecular structure determination by X-ray crystallography
or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to
existing structure-determination programs, the architecture of CNS is highly
flexible, allowing for extension to other structure-determination methods, such
as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical
structure: a high-level hypertext markup language (HTML) user interface,
task-oriented user input files, module files, a symbolic
structure-determination language (CNS language), and low-level source code.
Each layer is accessible to the user. The novice user may just use the HTML
interface, while the more advanced user may use any of the other layers. The
source code will be distributed, thus source-code modification is possible. The
CNS language is sufficiently powerful and flexible that many new algorithms can
be easily implemented in the CNS language without changes to the source code.
The CNS language allows the user to perform operations on data structures, such
as structure factors, electron-density maps, and atomic properties. The power
of the CNS language has been demonstrated by the implementation of a
comprehensive set of crystallographic procedures for phasing, density
modification and refinement. User-friendly task-oriented input files are
available for nearly all aspects of macromolecular structure determination by
X-ray crystallography and solution NMR.

A. T. Brunger, P. D. Adams, G. M. Clore, W. L. Delano, P. Gros, R. W.
Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, M. Nilges, N. S. Pannu, R. J.
Read, L. M. Rice, T. Simonson, G. L. Warren

Acta crystallographica. Section D, Biological crystallography
Crystallography & NMR system: A new software suite for macromolecular structure determination.

Refinement of the protein backbone angle y in NMR structure
calculations. R Sprangers, MJ Bottomley, JP Linge, J Schultz, M Nilges
and M Sattler. Journal of Biomolecular NMR (2000) 16, 47-58.

Refinement of the protein backbone angle psi in NMR structure calculations.

Linge, J.P. and Nilges, M. (1999) Journal of Biomolecular NMR, 13, 51-59.
Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation.

Assigning Ambiguous NOEs with ARIA. JP Linge, S O'Donoghue and M Nilges.
Methods in Enzymology (2001)

Automated assignment of ambiguous nuclear overhauser effects with ARIA.

Nmr Structure Of The Hrdc Domain From Saccharomyces Cerevisiae Recq Helicase

K7_Sgs1p [Saccharomyces cerevisiae Kyokai no. 7]

bps. 390..881 = homology to E.coli recQ; bps. 414..430 = ATP binding site [Saccharomyces cerevisiae]

Sgs1p [Saccharomyces cerevisiae YJM1078]

ATP-dependent DNA helicase SGS1 [Saccharomyces cerevisiae S288c]

RecName: Full=ATP-dependent helicase SGS1; AltName: Full=Helicase TPS1

TPA: ATP-dependent DNA helicase SGS1 [Saccharomyces cerevisiae S288c]

1. We also submit cross correlated relaxation rates in Hz and H/D-isotope shift
effects on the C-alpha chemical shifts (values in ppb). psi refinement: The
structures have been directly refined against cross-correlated relaxation rates
(C-alpha-H-alpha dipole, CO CSA) and the three-bond H/D isotope effect on the
C-alpha chemical shift, see reference 3.

2. Due to the use of floating chirality assignment some atom names for
diastereotopic methylene protons or methyl groups might be reversed
compared to the restraint files!

The structures have been directly refined against cross-correlated relaxation

rates (C-alpha-H-alpha dipole, CO CSA) and the three-bond H/D isotope effect on

the C-alpha chemical shift. Pulse sequences and experimental details are

ARIA (AMBIGUOUS RESTRAINTS IN ITERATIVE ASSIGNMENTS) AMBIGUOUS DISTANCE RESTRAINTS SIMULATED ANNEALING WITH TORSION ANGLE DYNAMICS

Starting with an almost complete list of chemical shifts, some few assigned NOEs and otherwise uninterpreted NOE peak lists, the program ARIA (Ambiguous Restraints in Iterative Assignment) calibrates NOEs, merges the obtained ambiguous distance restraints from different NOE spectra and assigns the NOE peaks in an iterative manner.