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. *