RCSB - Contents

Contents

The PDB database is updated weekly (UTC+0 Wednesday). Likewise, the PDB Holdings List is also updated weekly. As of 4 September 2012 (2012 -09-04), the breakdown of current holdings is as follows:

Experimental
Method
Proteins Nucleic Acids Protein/Nucleic Acid
complexes
Other Total
X-ray diffraction 69232 1390 3506 3 74131
NMR 8381 1005 190 7 9583
Electron microscopy 311 22 120 0 453
Hybrid 45 3 2 1 51
Other 141 4 5 13 163
Total: 78110 2424 3823 24 84381
63,555 structures in the PDB have a structure factor file.
6,890 structures have an NMR restraint file.
650 structures in the PDB have a chemical shifts file.

These data show that most structures are determined by X-ray diffraction, but about 15% of structures are now determined by protein NMR. When using X-ray diffraction, approximations of the coordinates of the atoms of the protein are obtained, whereas estimations of the distances between pairs of atoms of the protein are found through NMR experiments. Therefore, the final conformation of the protein is obtained, in the latter case, by solving a distance geometry problem. A few proteins are determined by cryo-electron microscopy. (Clicking on the numbers in the original table will bring up examples of structures determined by that method.)

The significance of the structure factor files, mentioned above, is that, for PDB structures determined by X-ray diffraction that have a structure file, the electron density map may be viewed. The data of such structures is stored on the "electron density server", where the electron maps can be viewed.

In the past, the number of structures in the PDB has grown at an approximately exponential rate. However, since 2007, the rate of accumulation of new proteins appears to have plateaued:

Year # added
2007 7263
2008 7073
2009 7448
2010 7971
2011 8120

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