wwPDB validation report of PDB entry 1MNK

THE HEME IRON IN MOLECULE A IS COORDINATED TO HOH 105. THE HEME IRON IN MOLECULE B IS COORDINATED TO HOH 1.

MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH HIS 64 REPLACED BY VAL AND VAL 68 REPLACED BY THR (H64V,V68T)
INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN

MTRIX
THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
SECOND.

APPLIED TO TRANSFORMED TO
MTRIX CHAIN RESIDUES CHAIN RESIDUES RMSD
M1 A 1 - A 153 B 1 - B 153 0.719

The analyses of the Patterson function reveals a significant off-origin peak that is 100.00 % of the origin peak, indicating pseudo-translational symmetry. The chance of finding a peak of this or larger height by random in a structure without pseudo-translational symmetry is equal to 0.0000e+00. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.

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)