1PYN
DUAL-SITE POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR USING A LINKED FRAGMENT STRATEGY AND A MALONATE HEAD ON THE FIRST SITE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-05-09 |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 88.710, 88.710, 104.830 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.740 - 2.200 |
R-factor | 0.211 |
Rwork | 0.198 |
R-free | 0.22400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1TYR AND INITIAL INTERNAL REFINEMENT OF OTHER COMPLEXES. RESIDUE CYS215 LISTED IN REMARK 500 CORRESPONDS TO THE ACTIVE SITE CYS WHICH IS KNOWN TO BE IN A STRAINED CONFORMATION IN THIS CLASS OF ENZYMES. |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNX (2000) |
Refinement software | CNX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.057 | 0.338 |
Number of reflections | 25276 | |
<I/σ(I)> | 20.2 | 2.23 |
Completeness [%] | 94.0 | 73 |
Redundancy | 4.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.1 | 277 | Barford, D., (1994) J. Mol. Biol., 239, 726. * |