wwPDB validation report of PDB entry 2KJ1

Structures were calculated using the program XPLOR-NIH (Schwieters et al., 2002). The secondary structure of the monomer was first calculated from random coil using intra-subunit NOEs, backbone dihedral restraints derived from chemical shifts (TALOS) (Cornilescu et al., 1999), and side chain χ1 restraints. A total of 20 monomer structures were calculated using a standard high-temperature simulated annealing (SA) protocol in which the bath temperature was cooled from 1000 to 200 K. To obtain an initial set of tetramer structures, four copies of the lowest-energy monomer structure calculated above were used. The same SA run was performed in the presence of inter-subunit NOEs and all other intra-subunit restraints. For each experimental inter-subunit NOE between two adjacent subunits, four identical distance restraints were assigned respectively to all pairs of neighboring subunits to satisfy the condition of C4 rotational symmetry. During the annealing run, the bath was cooled from 1000 to 200 K with a temperature step of 20 K. A total of 100 tetramer structures were calculated. For BM2(1-33), 15 low energy structures were selected as the structural ensemble.

cytoplasmic domain structure of BM2 proton channel from influenza B virus

geometric validation package for ligand chemistry in protein x-ray structures
assessment of nmr assigned chemical shifts
geometric validation of nmr ensemble structure
20191225.v01 (using entries in the PDB archive December 25th 2019)
domain identification of nmr ensemble structure
classification of nmr ensemble structure
nmr chemical shift validation and reference correction
random coil index prediction from nmr chemical shifts