D-I-TASSER P50336-D2

D-I-TASSER results for P50336-D2

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

Input Sequence in FASTA format

>P50336 (116 residues)
PTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCR
GVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERW

Predicted Secondary Structure

Sequence	20 40 60 80 100 \| \| \| \| \| PTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERW
Prediction	CCCHHHHHHCCCCCCHHHHHHHHHCHCCCCCCCCCCCHHHHHHHHHCHHHHHHHHHHHHCHCCCCCHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHCCCCCCCHHHHHHHHHCC
Confidence	98878876427765568999997512369999999899999999829999999999998110169988810999999999999993859999999721158998614567765139
	H:Helix; S:Strand; C:Coil

Predicted Solvent Accessibility

Sequence	20 40 60 80 100 \| \| \| \| \| PTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERW
Prediction	87424432463423445213200431144476653220140034313550052003010100102315402043014403510663210021113434655666564355246768
	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 DeepPotential. 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

CCCHHHHHHCCCCCCHHHHHHHHHCHCCCCCCCCCCCHHHHHHHHHCHHHHHHHHHHHHCHCCCCCHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHCCCCCCCHHHHHHHHHCC
PTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERW

2iveA

0.26

0.24

7.44

1.17

DEthreader

--SPPAFLA-SDILPLGARLRVAGELFSRRAPEVDESLAAFGRRHLGHRATQVLLDAVQTGIYAGDVEQLSVAATFPMLVKMEREHRSLILGAIRAQKAQA----KG--LNDCIRA

3nksA1

1.00

0.80

22.45

1.56

SPARKS-K

PTGLRG---PSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLG--------------------

2iveA

0.23

7.28

1.21

MapAlign

PASPPAFLA-SDILPLGARLRVAGELFSRRAEGVDESLAAFGRRHLGHRATQVLLDAVQTGIYAGDVEQLSVAATFPMLVKMEREHRSLILGAIRAQKAQTFDGGLQVLIDALAAS

2iveA1

0.27

0.23

7.15

1.16

CEthreader

--SPPAFLA-SDILPLGARLRVAGELFSRRAPGVDESLAAFGRRHLGHRATQVLLDAVQTGIYAGDVEQLSVAATFPMLVKMEREHRSLILGAIRAQKAQRQA-------------

3nksA1

1.00

0.80

22.45

1.75

MUSTER

PTGLRG---PSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLG--------------------

3nksA1

0.99

0.79

22.22

3.27

HHsearch

PTGLRG--P-SPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLG--------------------

3nksA1

0.98

0.78

21.74

1.38

FFAS-3D

PTG---LRGPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLL---------------------

2iveA

0.22

7.05

1.40

EigenThreader

PASPPAFLASDILPLGARLRVAGELFSRRAPEGVDESLAAFGRRHLGHRATQVLLDAVQTGIYAGDVEQLSVAATFPMLVKMEREHRSLILGAIRAQKAQRQAGTAALAASLGDAA

3nksA

1.00

0.93

26.07

0.96

CNFpred

PTGLRG---PSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLG-----QPDSALIRQALAERW

2iveA1

0.28

0.23

7.13

1.17

DEthreader

-S-PPAFLA-SDILPLGARLRVAGELFSRRAPEVDESLAAFGRRHLGHRATQVLLDAVQTGIYAGDVEQLSVAATFPMLVKMEREHRSLILGAIRAQKAQR---------------

(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	0.7359

(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 DeepPotential, 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	2iveA	0.77	2.00	0.243	0.871	model1_2iveA.pdb.gz
2	3nksA	0.74	1.65	0.777	0.802	model1_3nksA.pdb.gz
3	1sezA2	0.70	1.47	0.267	0.776	model1_1sezA2.pdb.gz
4	3lovA2	0.67	2.07	0.202	0.810	model1_3lovA2.pdb.gz
5	2iidA	0.45	4.11	0.053	0.759	model1_2iidA.pdb.gz
6	3i6dB2	0.43	2.77	0.299	0.543	model1_3i6dB2.pdb.gz
7	2vvmA	0.41	4.92	0.050	0.759	model1_2vvmA.pdb.gz
8	1b5qB	0.40	4.66	0.080	0.741	model1_1b5qB.pdb.gz
9	1w4xA	0.38	4.74	0.073	0.690	model1_1w4xA.pdb.gz
10	2xdoA2	0.36	5.18	0.087	0.707	model1_2xdoA2.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:0004729	1.00	oxygen-dependent protoporphyrinogen oxidase 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:0006779	1.00	porphyrin-containing compound biosynthetic process
GO:0044699	0.97	single-organism process
GO:0044763	0.96	single-organism cellular process
GO:0044710	0.96	single-organism metabolic process
GO:0006783	0.95	heme biosynthetic process
GO:0055114	0.69	oxidation-reduction 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:0044444	1.00	cytoplasmic part
GO:0044446	0.96	intracellular organelle part
GO:0044429	0.91	mitochondrial part
GO:0044425	0.91	membrane part
GO:0031304	0.90	intrinsic component of mitochondrial inner membrane
GO:0016020	0.75	membrane
GO:0031090	0.71	organelle membrane
GO:0031966	0.70	mitochondrial membrane
GO:0043226	0.68	organelle
GO:0043229	0.67	intracellular organelle
GO:0043227	0.66	membrane-bounded organelle
GO:0043231	0.65	intracellular membrane-bounded organelle
GO:0005739	0.52	mitochondrion

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	3f6tB	0.429	4.43	0.066	0.750	2.6.1.1	NA
2	0.060	1ml4A	0.463	3.97	0.068	0.733	2.1.3.2	NA
3	0.060	2bi7A	0.466	4.39	0.088	0.733	5.4.99.9	NA
4	0.060	1ofdA	0.473	4.74	0.054	0.871	1.4.7.1	NA
5	0.060	3g4dA	0.442	4.31	0.056	0.733	4.2.3.13	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	0.08	2ivdB	0.775	2.04	0.243	0.871	0.55	TWN	complex1.pdb.gz	50,51,54,55,57,58
2	0.01	1llwA	0.473	4.93	0.088	0.897	0.47	F3S	complex2.pdb.gz	62,63,64,65,66,70,75
3	0.01	2bcgG	0.491	3.76	0.078	0.750	0.41	GER	complex3.pdb.gz	51,52,55,59,60,62,63
4	0.01	1lm1A	0.475	4.69	0.054	0.871	0.62	F3S	complex4.pdb.gz	56,57,58,59,60,64,65,68,69

	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.