wwPDB validation report of PDB entry 1CB6

Lactoferrin,Growth-inhibiting protein 12,Talalactoferrin

THERE IS A TWO FOLD INTERNAL SEQUENCE HOMOLOGY (~40% IDENTITY).

THE SEQUENCE USED IN THE X-RAY STRUCTURE FOR RESIDUES
1001-1005 (GRRRS) IS AT VARIANCE WITH
THE MOST RECENT SEQUENCE (SWS P02788, TRFL_H: GRRRRS).
IN THIS REGION ELECTRON DENSITY IS POORLY DEFINED AND
THE DIFFERENCE IS OF LITTLE STRUCTURAL CONSEQUENCE.

THE AMINO ACID SEQUENCE GIVEN IN ENTRY 1LFH REQUIRED
CORRECTIONS AT RESIDUE 13 (GLN), 24 (ARG), 28 (LYS),
200 (ARG), 512(GLN)

ANISOTROPIC SCALING APPLIED BY THE METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56. PROLSQ WAS USED FOR INITIAL REFINEMENTS. SHELXL97 WAS USED FOR FINAL REFINEMENTS.

THERE IS POOR DENSITY FOR RESIDUES 1-3. DENSITY FOR RESIDUES 418 - 424 IS POORLY DEFINED.

MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228

STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.

CHLORIDE ION LOCATED NEAR CARBONATE SITE IN CLOSED C LOBE, FORMING HYDROGEN BONDS WITH THR461_OG1, ARG465_NE, ARG465_NH2, GLY468_N AND TYR528_OH

CHLORIDE ION LOCATED NEAR CARBONATE SITE IN OPEN N LOBE, FORMING HYDROGEN BONDS WITH THR117_OG1, ARG121_NE, ALA123_N AND TYR192_OH

The largest off-origin peak in the Patterson function is 6.38% 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)