D-I-TASSER Q8TDX7-D1

D-I-TASSER results for Q8TDX7-D1

[Click result.zip to download all results on this page]

Input Sequence in FASTA format

>Q8TDX7 (113 residues)
MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPV
ALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL

Predicted Secondary Structure

Sequence	20 40 60 80 100 \| \| \| \| \| MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL
Prediction	CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHSSSSSSSSSCCCSSSSSSSSCCCCCSSSSSSSSHHHCCCHCHHHHHHHHHHHHHHCCCCCSCSSSSSSSSCCSSSSSSSC
Confidence	98666788998988777655567666888612058866753157638999999799969999999867704620799999999999978997130077699979999999829
	H:Helix; S:Strand; C:Coil

Predicted Solvent Accessibility

Sequence	20 40 60 80 100 \| \| \| \| \| MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL
Prediction	86657664674454655565545674545405405224404644203012031374443000020416616567236403400500562614100302320346630100047
	Values range from 0 (buried residue) to 8 (highly exposed residue)

Predicted Contact, Hydrogen and Distance Map Used in D-I-TASSER simulation

Contact Map

Distance Map

Hydrogen bond networks

D-I-TASSER simulation is guided by the consensus contact map (left figure), distance map (middle figure) and Hydrogen bond network (right figure) derived based on confidence scores of AttentionPotential. In the contact, distance map and hydrogen bond networks, the axes mark the residue index along the sequence. For the contact map, each dot represents a residue pair with predicted contact, while for the distance map and hydrogen bond network, a color scale represents a distance of 1-20+ angstroms or a angle of 0-180 degree.

Top 10 threading templates used by D-I-TASSER

Rank

PDB
hit

ID1

ID2

Cov

Norm.
Zscore

Download
alignment

                  20                  40                  60                  80                 100

                   |                   |                   |                   |                   |

SS
Seq

CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHSSSSSSSSSCCCSSSSSSSSCCCCCSSSSSSSSHHHCCCHCHHHHHHHHHHHHHHCCCCCSCSSSSSSSSCCSSSSSSSC
MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL

6pjxA

0.21

0.19

6.19

1.17

DEthreader

QDSQTELFCAQV----FWKLERQP----VTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTI

2wqmA1

0.99

0.81

22.56

2.00

SPARKS-K

-------------------KALRPDMGYNTLANFRIEKKIGRGS--EVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL

6vg3A1

0.24

0.18

5.53

0.34

MapAlign

-------------------------KMHFPRSSLQPITTLGKSEFGEVFLAKAQGAETLVLVKSLQ---SKDEQQQLDFRRELEMFGKLNHANVVRLLGLCREAEPHYMVLEY

6vg3A

0.24

0.18

5.53

0.20

CEthreader

-------------------------KMHFPRSSLQPITTLGKSEFGEVFLAKAQGLETLVLVKSLQ---SKDEQQQLDFRRELEMFGKLNHANVVRLLGLCREAEPHYMVLEY

2qg5A1

0.25

0.22

6.88

1.94

MUSTER

--------HHHHHSSGRENLYFQGSTKGDINQYYTLENTIGRGSWGEVKIAVQKGTRIRRAAKKIPKYFVED---VDRFKQEIEIMKSLDHPNIIRLYETFEDNTDIYLVMEL

3i7bA

0.26

0.19

6.01

0.65

HHsearch

----------------------------IFSDRYKGQRVLGKGSFGEVILCKDKITGQECAVKVISKRQVKQKTDKESLLREVQLLKQLDHPNIMKLYEFFEDKGYFYLVGEV

2wqmA1

1.00

0.81

22.80

1.66

FFAS-3D

-------------------KALRPDMGYNTLANFRIEKKIGRG--SEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL

2acxA

0.20

0.19

6.24

0.67

EigenThreader

DYHSLCERNTPDDKSHTGPDLIPEVPQPVTKNTFRQYRVLGG--FGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL

5de2A

0.99

0.82

23.05

1.60

CNFpred

-------------------KALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKFYASFIEDNELNIVLEL

2bcjA

0.21

0.19

6.19

1.17

DEthreader

KSEHVQLFYIEI----WKVELNIH----LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSCPFIVCMSYAFHTPDKLSFILDL

(a)	ID1 is the number of template residues identical to query divided by number of aligned residues.
(b)	ID2 is the number of template residues identical to query divided by query sequence length.
(c)	Cov is equal the number of aligned template residues divided by query sequence length.
(d)	Norm. Zscore is the normalized Z-score of the threading alignments. A Normalized Z-score >1 means a good alignment and is highlighted in bold.
(e)	Download alignment lists the threading program used to identify the template, and provide the 3D structure of aligned regions of threading templates (threading[1-10].pdb.gz).
(f)	Template residues identical to query sequence are highlighted in color.

Top 1 final models from D-I-TASSER

Click to view	Rank^a	Download	Estimated TM-score^b
	1	model1.pdb.gz	0.7277

(a)

D-I-TASSER simulations generate a large ensemble of structural conformations, i.e. decoys. These decoys are clustered by SPICKER based on pairwise structure similarity to report up to five final models from the five largest clusters. Models are ranked in descending order of cluster size. If the simulations converge well, it is possible to have less than 5 models generated, which is usually an indication of good model quality.

(b)

The model confidence is quantitatified by estimated TM-score (eTM-score), calculated based on significance of threading template alignments, contact map satisfaction rate, mean absolute error between distance of model and distance of AttentionPotential, and convergence of D-I-TASSER simulations. eTM-score is typically in the range of [0, 1], with higher eTM-score signifies higher model confidence.

Proteins with similar structure

Top 10 structural analogs in PDB (as identified by TM-align)

Rank	PDB Hit	TM-score	RMSD^a	IDEN^a	Cov.	Download Alignment
1	2acxA2	0.75	2.21	0.195	0.858	model1_2acxA2.pdb.gz
2	3cokA1	0.74	2.04	0.261	0.814	model1_3cokA1.pdb.gz
3	4yhjA	0.73	2.54	0.195	0.867	model1_4yhjA.pdb.gz
4	4tnbA	0.73	2.28	0.177	0.858	model1_4tnbA.pdb.gz
5	3c4wB	0.73	2.76	0.168	0.885	model1_3c4wB.pdb.gz
6	6c0tA	0.72	3.02	0.146	0.894	model1_6c0tA.pdb.gz
7	2bcjA	0.72	2.69	0.186	0.850	model1_2bcjA.pdb.gz
8	4fr4A2	0.72	1.90	0.202	0.788	model1_4fr4A2.pdb.gz
9	2owbA1	0.72	1.97	0.188	0.788	model1_2owbA1.pdb.gz
10	5ig1A1	0.71	1.68	0.202	0.788	model1_5ig1A1.pdb.gz

(a)	Query structure is shown in cartoon, while the structural analog is displayed using backbone trace.
(b)	Ranking of proteins is based on TM-score of the structural alignment between the query structure and known structures in the PDB library.
(c)	RMSD^a is the RMSD between residues that are structurally aligned by TM-align.
(d)	IDEN^a is the percentage sequence identity in the structurally aligned region.
(e)	Cov. represents the coverage of the alignment by TM-align and is equal to the number of structurally aligned residues divided by length of the query protein.

Predicted Gene Ontology (GO) Terms

Molecular Function (MF)

GO term	Cscore^GO	Name
GO:0003824	0.98	catalytic activity
GO:0004672	0.97	protein kinase activity
GO:0004674	0.90	protein serine/threonine kinase activity

Download full result of the above consensus prediction.

Click the graph to show a high resolution version.

(a)

Cscore^GO is the confidence score of predicted GO terms. Cscore^GO values range in between [0-1]; where a higher value indicates a better confidence in predicting the function using the template.

(b)

The graph shows the predicted terms within the Gene Ontology hierachy for Molecular Function. Confidently predicted terms are color coded by Cscore^GO:

[0.4,0.5)

[0.5,0.6)

[0.6,0.7)

[0.7,0.8)

[0.8,0.9)

[0.9,1.0]

Biological Process (BP)

GO term	Cscore^GO	Name
GO:0009987	0.94	cellular process
GO:0065007	0.83	biological regulation
GO:0050789	0.83	regulation of biological process
GO:0050794	0.82	regulation of cellular process
GO:0071704	0.80	organic substance metabolic process
GO:0044238	0.79	primary metabolic process
GO:0044237	0.79	cellular metabolic process
GO:0043170	0.78	macromolecule metabolic process
GO:0044260	0.77	cellular macromolecule metabolic process
GO:0019538	0.73	protein metabolic process
GO:0016310	0.72	phosphorylation
GO:0006464	0.72	cellular protein modification process
GO:0006468	0.71	protein phosphorylation
GO:0007165	0.57	signal transduction
GO:0044699	0.53	single-organism process

Download full result of the above consensus prediction.

Click the graph to show a high resolution version.

(a)

Cscore^GO is the confidence score of predicted GO terms. Cscore^GO values range in between [0-1]; where a higher value indicates a better confidence in predicting the function using the template.

(b)

The graph shows the predicted terms within the Gene Ontology hierachy for Biological Process. Confidently predicted terms are color coded by Cscore^GO:

[0.4,0.5)

[0.5,0.6)

[0.6,0.7)

[0.7,0.8)

[0.8,0.9)

[0.9,1.0]

Cellular Component (CC)

GO term	Cscore^GO	Name
GO:0044464	1.00	cell part
GO:0044424	0.95	intracellular part
GO:0043226	0.63	organelle
GO:0043229	0.61	intracellular organelle
GO:0005737	0.60	cytoplasm
GO:0043227	0.54	membrane-bounded organelle
GO:0043231	0.52	intracellular membrane-bounded organelle

Download full result of the above consensus prediction.

Click the graph to show a high resolution version.

(a)

Cscore^GO is the confidence score of predicted GO terms. Cscore^GO values range in between [0-1]; where a higher value indicates a better confidence in predicting the function using the template.

(b)

The graph shows the predicted terms within the Gene Ontology hierachy for Cellular Component. Confidently predicted terms are color coded by Cscore^GO:

[0.4,0.5)

[0.5,0.6)

[0.6,0.7)

[0.7,0.8)

[0.8,0.9)

[0.9,1.0]

Predicted Enzyme Commission (EC) Numbers

Top 5 enzyme homologs in PDB

Rank	Cscore^EC	PDB Hit	TM-score	RMSD^a	IDEN^a	Cov.	EC Number	Predicted Active Site Residues
1	0.060	2bfyB	0.699	1.80	0.242	0.779	2.7.11.1	39,87
2	0.060	3db8A	0.715	1.99	0.200	0.788	2.7.11.21	NA
3	0.060	3d5uA	0.714	2.00	0.198	0.788	2.7.11.21	43
4	0.060	2w4kA	0.686	2.23	0.236	0.779	2.7.11.1	NA
5	0.060	2v7oA	0.710	2.18	0.200	0.788	2.7.11.17	NA

	Click on the radio buttons to visualize predicted active site residues.
(a)	Cscore^EC is the confidence score for the Enzyme Commission (EC) number prediction. Cscore^EC values range in between [0-1]; where a higher score indicates a more reliable EC number prediction.
(b)	TM-score is a measure of global structural similarity between query and template protein.
(c)	RMSD^a is the RMSD between residues that are structurally aligned by TM-align.
(d)	IDEN^a is the percentage sequence identity in the structurally aligned region.
(e)	Cov. represents the coverage of global structural alignment and is equal to the number of structurally aligned residues divided by length of the query protein.

Predicted Ligand Binding Sites

Template proteins with similar binding site:

Rank	Cscore^LB	PDB Hit	TM-score	RMSD^a	IDEN^a	Cov.	BS-score	Lig. Name	Download Complex	Predicted binding site residues
1	0.16	3e8cA	0.716	2.46	0.202	0.832	0.69	G96	complex1.pdb.gz	40,43,45,46,47,48,61,63,65,82,86,95,109,111,112
2	0.14	3nx8A	0.712	2.63	0.202	0.841	0.46	IPH	complex2.pdb.gz	41,42,43,48
3	0.13	3pvuA	0.722	2.37	0.177	0.832	0.43	QRW	complex3.pdb.gz	41,43,45,46,48,63,65
4	0.05	1xh9A	0.724	2.45	0.200	0.841	1.19	BU3	complex4.pdb.gz	45,46,47,64,66,69,106
5	0.04	3mvjA	0.719	2.45	0.202	0.832	0.58	III	complex5.pdb.gz	41,46,47,63

	Click on the radio buttons to visualize predicted binding site and residues.
(a)	Cscore^LB is the confidence score of predicted binding site. Cscore^LB values range in between [0-1]; where a higher score indicates a more reliable ligand-binding site prediction.
(b)	BS-score is a measure of local similarity (sequence & structure) between template binding site and predicted binding site in the query structure. Based on large scale benchmarking analysis, we have observed that a BS-score >1 reflects a significant local match between the predicted and template binding site.
(c)	TM-score is a measure of global structural similarity between query and template protein.
(d)	RMSD^a the RMSD between residues that are structurally aligned by TM-align.
(e)	IDEN^a is the percentage sequence identity in the structurally aligned region.
(f)	Cov. represents the coverage of global structural alignment and is equal to the number of structurally aligned residues divided by length of the query protein.

[Click result.zip to download all results on this page]

References:
1.	Wei Zheng, Chengxin Zhang, Yang Li, Robin Pearce, Eric W. Bell, Yang Zhang. Folding non-homology proteins by coupling deep-learning contact maps with I-TASSER assembly simulations. In preparation, 2020.