Statistics Summary Report for BIGS Center | Last updated: Jul 2 2008 |
Target Status Statistics
Total number of targets deposited by BIGS to TargetDB: 297 View BIGS Target List
Table 1: Status Statistics for BIGS
| Status | Total Number of Targets | (%) Relative to "Cloned" Targets | (%) Relative to "Expressed" Targets | (%) Relative to "Purified" Targets | (%) Relative to "Crystallized" Targets |
| Cloned | 251 | 100.0 | - | - | - |
| Expressed | 223 | 88.8 | 100.0 | - | - |
| Soluble | 151 | 60.2 | 67.7 | - | - |
| Purified | 110 | 43.8 | 49.3 | 100.0 | - |
| Crystallized | 28 | 11.2 | 12.6 | 25.5 | 100.0 |
| Diffraction-quality Crystals | 21 | 8.4 | 9.4 | 19.1 | 75.0 |
| Diffraction | 19 | 7.6 | 8.5 | 17.3 | 67.9 |
| NMR Assigned | 0 | 0.0 | 0.0 | 0.0 | - |
| HSQC | 0 | 0.0 | 0.0 | 0.0 | - |
| Crystal Structure | 17 | 6.8 | 7.6 | 15.5 | 60.7 |
| NMR Structure | 0 | 0.0 | 0.0 | 0.0 | - |
| In PDB1 | 9 | 3.6 | 4.0 | 8.2 | 32 |
| Work Stopped | 3 | - | - | - | - |
| Test Target | 1 | - | - | - | - |
| Other | 0 | - | - | - | - |
Table 2: Status Statistics for BIGS by Organism
| Organism | Total Number1 | Work Stopped | Cloned | Expressed | Purified | Crystallized | Crystal Structure | NMR Structure | In PDB2 |
| Bacteria | 186 | 3 | 167 | 146 | 74 | 18 | 11 | 0 | 8 |
| Total Prokaryotes | 186 | 3 | 167 | 146 | 74 | 18 | 11 | 0 | 8 |
| Yeast | 57 | 0 | 53 | 52 | 23 | 5 | 2 | 0 | 0 |
| Other Eukaryotes | 54 | 0 | 31 | 25 | 13 | 5 | 4 | 0 | 1 |
| Total Eukaryotes | 111 | 0 | 84 | 77 | 36 | 10 | 6 | 0 | 1 |
| Total | 297 | 3 | 251 | 223 | 110 | 28 | 17 | 0 | 9 |
Last updated: Jul 2 2008
Note 1:
Total counts in this table may differ from total number of targets. If targtet
is a hybrid complex
(for example:a complex of human and mouse polypeptides)
it is counted in different organism classifications.
Note 2:
Number of targets with status "in PDB". A target may reference several
PDB IDs (example: structure of the same polypeptides with different ligands).
Multiple targets in TargetDB may identify the same PDB structure when a stucture
is a result of collaboration between different centers and each center includes
the target on its target list.
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Deposited Structure Statistics for BIGS Center
Number of Released X-Ray Structures: 8
Number of Released NMR Structures: 0
Total number of released structures from BIGS center in the PDB: 8
Table 3: PDB Status Statistics for Structures from BIGS
| PDB Status | Number of Structures |
| Total Deposited | 9 |
| Released | 8 |
| Release on Publication | 0 |
| Release on Certain Date | 0 |
| In Process | 1 |
| Last updated: Jul 2 2008 |
| Note 1: "Total Deposited" are all structures in the PDB including structures released to the public and structures that are in the process to be released("Released on Publication" , "Released on Certain Date", etc.). |
Table 4: List of Structures Deposited in the PDB by BIGS
Total number of structures: 9
Structures of distinct targets: 91
1
A target may reference several PDB IDs
(example: structure of the same polypeptides with different ligands).
In this case only one structure is counted to compute number of structures of
distinct targets
Related PDB_ID(s): PDB_ID(s) associated with the same target in targetDB
| PDB_ID | Title | Target_id | Deposition Date | Released Date | PDB Status | Related PDB_ID in TargetDB |
| ND_1 | Experimental status "in PDB", PDB ID is not provided | Pf-cal:CA1462 | - | - | - | none |
| 1UUF | crystal structure of a zinc-type alcohol dehydrogenase-like protein yahk | ASG-yahK | 2003-12-18 | 2004-01-29 | REL | none |
| 1OG6 | ydhf, an aldo-keto reductase from e.coli complexed with nadph | ASG-ydhF | 2003-04-24 | 2003-05-29 | REL | none |
| 1J2R | crystal structure of escherichia coli gene product yecd at 1.3 a resolution | ASG-yecD | 2003-01-09 | 2004-01-27 | REL | none |
| 1OKJ | mad crystal structure of the unknown function e. coli yeaz protein | IGS-yeaZ | 2003-07-26 | 2004-09-16 | REL | none |
| 1GPQ | structure of ivy complexed with its target, hewl | ORPH-ykfE | 2001-11-08 | 2003-03-11 | REL | none |
| 1OI4 | cristal structure of yhbo from escherichia coli | ASG-yhbO | 2003-06-06 | 2003-07-03 | REL | none |
| 1UQW | crystal structure of ylib protein from escherichia coi | ASG-yliB | 2003-10-22 | 2003-11-19 | REL | none |
| 1MZR | structure of dkga from e.coli at 2.13 a resolution solved by molecular replacement | ASG-yqhE | 2002-10-09 | 2003-10-28 | REL | none |
Note 1: Last updated: Jul 2 2008
back to topSequence Redundancy Statistics
Table 5: Sequence Redundancy Statistics for BIGS by Experimental Status
| Sequence Identity(%) | Novel Targets
Status: Selected |
Novel Targets Status: Cloned |
Novel Targets Status: Expressed |
Novel Targets Status: Purified |
Novel Targets Status: Crystallized |
Novel Targets Status: Crystal Structure | Novel Targets Status: in PDB |
| <100 | 297 | 251 | 223 | 110 | 28 | 17 | 9 |
| <90 | 296 | 250 | 222 | 110 | 28 | 17 | 9 |
| <70 | 289 | 249 | 221 | 110 | 28 | 17 | 9 |
| <50 | 282 | 245 | 218 | 110 | 28 | 17 | 9 |
| <30 | 219 | 206 | 187 | 98 | 27 | 17 | 9 |
| Last updated: 08-04-08 |
| Sequence redundancy is calculated by clustering analysis using BLASTClust program with similarity threshold set to percent of sequence identity. Please view detailed explanation of sequence redundancy calculations and BLASTClust threshold settings. Sequence redundancy calculations are based on comparison to all protein sequences in TargetDB which are in the same experimental status category and at least 20 amino acids long |
Table 6:Sequence Redundancy Statistics for Structures Released by BIGS by Year
| Year | Released Structures | Number of Released Structures <30% Identity at Time of Release | Percent(%) of Released Structures <30% Identity(%) at Time of Release |
| 2003 | 5 | 3 | 60 |
| 2004 | 3 | 2 | 67 |
| Total | 8 | 5 | 63 |
| Last updated:08-07-02 |
| Sequence redundancy is calculated by clustering analysis using BLASTClust program with similarity threshold set to percent of sequence identity. Please view detailed explanation of sequence redundancy calculations and BLASTClust threshold settings. Sequence redundancy calculations are based on comparison to all protein sequences in the PDB which are at least 20 amino acids long |