Statistics Summary Report for CSMP Center

Last updated: Feb 2 2012

• Target Status Statistics
• Table 1: Status Statistics for CSMP
• Table 2: Status Statistics for CSMP by Organisms
• Deposited Structure Statistics
• Table 3: PDB Status Statistics for Structures from CSMP
• Table 4: List of Structures Deposited by CSMP in the PDB
• Sequence Redundancy Statistics
• Table 5: Sequence Redundancy Statistics for CSMP by Experimental Status
• Table 6: Sequence Redundancy Statistics for Structures Released by CSMP in the PDB by Year

Target Status Statistics

Total number of targets deposited by CSMP to TargetDB: 1919

      View CSMP Target List

Table 1: Status Statistics for CSMP

Status	Total Number of Targets	(%) Relative to "Cloned" Targets	(%) Relative to "Expressed" Targets	(%) Relative to "Purified" Targets	(%) Relative to "Crystallized" Targets
Cloned	1911	100.0	-	-	-
Expressed	1183	61.9	100.0	-	-
Soluble	0	0.0	0.0	-	-
Purified	1103	57.7	93.2	100.0	-
Crystallized	42	2.2	3.6	3.8	100.0
Diffraction-quality Crystals	30	1.6	2.5	2.7	71.4
Diffraction	13	0.7	1.1	1.2	31.0
NMR Assigned	0	0.0	0.0	0.0	-
HSQC	0	0.0	0.0	0.0	-
Crystal Structure	13	0.7	1.1	1.2	31.0
NMR Structure	0	0.0	0.0	0.0	-
In PDB1	13	0.7	1.1	1.2	31
Work Stopped	0	-	-	-	-
Test Target	0	-	-	-	-
Other	0	-	-	-	-

Last updated: Feb 2 2012

Note 1:   Number of targets with status "in PDB" may not be equal to number of structures determined by a project. 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.

Table 2: Status Statistics for CSMP by Organism

These statistics are derived from mapping of target sequences to GenBank using >=98% sequence identity cut off.

Organism	Total Number1	Work Stopped	Cloned	Expressed	Purified	Crystallized	Crystal Structure	NMR Structure	In PDB
Viruses	1	0	1	1	1	0	0	0	0
Archaea	125	0	125	4	4	3	1	0	1
Bacteria	1198	0	1198	790	761	34	9	0	9
Prokaryota	1323	0	1323	794	765	37	10	0	10
Yeast	457	0	449	380	329	0	0	0	0
Plasmodium	2	0	2	1	1	1	1	0	1
Arabidopsis	1	0	1	0	0	0	0	0	0
Worm	1	0	1	0	0	0	0	0	0
Drosophila	4	0	4	0	0	0	0	0	0
Mouse	34	0	34	3	3	2	0	0	0
Human	112	0	112	6	6	4	2	0	2
Eukaryota	618	0	610	411	359	6	3	0	3
Uncultured or unidentified	15	0	15	13	13	0	0	0	0

Last updated: Feb 2 2012

Note 1:   Total counts in this table may differ from total number of targets and structures. A target is counted in different organism specifications if:
- a target is mapped to different organisms
- a target is a hybrid complex (for example:a complex of human and mouse polypeptides).

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Deposited Structure Statistics for CSMP Center

Number of Released X-Ray Structures: 9

Number of Released NMR Structures: 3

Total number of released structures from CSMP center in the PDB: 12

Table 3: PDB Status Statistics for Structures from CSMP

PDB Status	Number of Structures
Total Deposited	12
Released	12
In Process	0

Last updated: Feb 2 2012

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 CSMP

Total number of structures: 12

Structures of distinct targets: 121

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
3JZ3	structure of the cytoplasmic segment of histidine kinase qsec	4280C CSMP:4308C	2009-09-22	2010-07-21	REL	none
3C02	x-ray structure of the aquaglyceroporin from plasmodium falciparum	4279S	2008-01-18	2008-05-27	REL	none
3BHS	nitrosomonas europaea rh50 and mechanism of conduction by rhesus protein family of channels	2009	2007-11-29	2007-12-04	REL	none
2F2B	crystal structure of integral membrane protein aquaporin aqpm at 1.68a resolution	4278S	2005-11-15	2005-12-06	REL	none
3HD6	crystal structure of the human rhesus glycoprotein rhcg	1681S	2009-05-06	2009-09-01	REL	none
2O9D	crystal structure of aqpz mutant t183c.	2454S	2006-12-13	2007-02-13	REL	none
2KSF	backbone structure of the membrane domain of e. coli histidine kinase receptor kdpd, center for structures of membrane proteins (csmp) target 4312c	4312C	2010-01-03	2010-03-02	REL	none
2KSE	backbone structure of the membrane domain of e. coli histidine kinase receptor qsec, center for structures of membrane proteins (csmp) target 4311c	4311C	2010-01-02	2010-03-02	REL	none
3GD8	crystal structure of human aquaporin 4 at 1.8 and its mechanism of conductance	1070S	2009-02-23	2009-03-31	REL	none
3K1B	structure of ompf porin	4309C	2009-09-26	2010-04-14	REL	none
2KSD	backbone structure of the membrane domain of e. coli histidine kinase receptor arcb, center for structures of membrane proteins (csmp) target 4310c	4310C	2010-01-02	2010-03-02	REL	none
3K19	ompf porin	4307C	2009-09-26	2010-04-14	REL	none

Last updated: Feb 2 2012

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Sequence Redundancy Statistics

Table 5: Sequence Redundancy Statistics for CSMP 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	1808	1810	1115	1083	38	11	11
<98	1787	1766	1108	1077	37	11	11
<95	1742	1744	1107	1076	37	11	11
<90	1715	1717	1107	1076	37	11	11
<70	1636	1638	1084	1056	37	11	11
<50	1528	1531	1033	1012	37	11	11
<40	1360	1386	974	967	36	11	11
<30	920	992	777	820	30	8	8

Last updated: 12-01-10

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 CSMP 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
2005	1	0	0
2007	2	0	0
2008	1	0	0
2009	2	1	50
2010	6	3	50
Total	12	4	33

Last updated: 12-02-02

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.

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