wwPDB validation report of PDB entry 1FWB

THIS MODEL IS THAT OF THE C319A MUTANT (PH=6.5) AT 2.0
ANGSTROMS. THE ACTIVE SITE IS NEARLY IDENTICAL TO
THAT OF THE HOLOENZYME (PDB ENTRY 1KAU).
THREE NONIDENTICAL CHAINS, GAMMA (A), BETA (B), AND ALPHA
(C) FORM ONE (ABC)-UNIT. THE ASYMMETRIC UNIT CONTAINS ONE
(ABC)-UNIT.
RESIDUES 312 - 336 IN CHAIN C, THE MOBILE ACTIVE SITE FLAP,
ARE MORE WELL ORDERED THAN IN THE HOLOENZYME (1KAU).
THREE WATERS, 500, 501, AND 502 ARE LIGATED TO THE ACTIVE
SITE NICKEL IONS. THEY MUST BE PARTIALLY OCCUPIED DUE TO
CLOSE OXYGEN-OXYGEN DISTANCES BETWEEN THEM.

ALL NON-BONDED INTERACTIONS WERE REMOVED BETWEEN THE
ACTIVE SITE NICKEL IONS AND NICKEL-BOUND WATERS
500, 501, 502.
THE OCCUPANCIES FOR ACTIVE SITE WATERS HOH 500 - HOH 502
WERE REFINED WITH A FIXED B-FACTOR OF 20 ANGSTROMS**2.
THE REFINED OCCUPANCIES FOR THESE WATERS SUGGEST NEARLY
FULL OCCUPANCY FOR EACH OF THEM, ALTHOUGH THEY ARE
POSITIONED TOO CLOSE (~ 2.0 ANGSTROMS APART) FOR
SIMULTANEOUS OCCUPANCY.

THE OCCUPANCIES FOR ACTIVE SITE WATERS HOH 500 - HOH 502
WERE REFINED WITH A FIXED B-FACTOR OF 20 ANGSTROMS**2.
THE REFINED OCCUPANCIES FOR THESE WATERS SUGGEST NEARLY
FULL OCCUPANCY FOR EACH OF THEM, ALTHOUGH THEY ARE
POSITIONED TOO CLOSE (~ 2.0 ANGSTROMS APART) FOR
SIMULTANEOUS OCCUPANCY.

KLEBSIELLA AEROGENES UREASE, C319A VARIANT AT PH 6.5

The largest off-origin peak in the Patterson function is 2.65% of the height of the origin peak. No significant pseudotranslation is detected.

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures

20191225.v01 (using entries in the PDB archive December 25th 2019)