I-TASSER results

I-TASSER results for job id Rv3768

[Click on result.tar.bz2 to download the tarball file including all modelling results listed on this page]

Input Sequence in FASTA format

>protein (119 residues)
MGSTPPRTPQEVFAHHGQALAAGDLDEIVADYADDSFVITPAGIARGKEGIRQLFVKLLD
DIPNALWDLKTQIFEGDILFLEWTANSAVSRVDDGVDTFVFRDGTIWAHTVRYTPHPKT

Predicted Secondary Structure

Sequence	20 40 60 80 100 \| \| \| \| \| MGSTPPRTPQEVFAHHGQALAAGDLDEIVADYADDSFVITPAGIARGKEGIRQLFVKLLDDIPNALWDLKTQIFEGDILFLEWTANSAVSRVDDGVDTFVFRDGTIWAHTVRYTPHPKT
Prediction	CCCCCCCHHHHHHHHHHHHHHHCCHHHHHHHCCCCEEEEHCCCCEHCHHHHHHHHHHHHHHCCCEEEEEEEEEEHCCEEEEEEEEHCCCCEEEEEEEEEEEHCCEEEEEEEEHCCCCCC
Conf.Score	99888765999999999999989999999977898699958975657899999999999979985899988999898999999997898667766899999699999999876578899
	H:Helix; S:Strand; C:Coil

Predicted Solvent Accessibility

Sequence	20 40 60 80 100 \| \| \| \| \| MGSTPPRTPQEVFAHHGQALAAGDLDEIVADYADDSFVITPAGIARGKEGIRQLFVKLLDDIPNALWDLKTQIFEGDILFLEWTANSAVSRVDDGVDTFVFRDGTIWAHTVRYTPHPKT
Prediction	86656563044015401511564304301621253002223634341262025004401651452415244332444202020214376442330001020443301222043435568
	Values range from 0 (buried residue) to 8 (highly exposed residue)

Predicted Normalized B-facotr

(B-factor is a value to indicate the extent of the inherent thermal mobility of residues/atoms in proteins. In I-TASSER, this value is deduced from threading template proteins from the PDB in combination with the sequence profiles derived from sequence databases. The reported B-factor profile in the figure below corresponds to the normalized B-factor of the target protein, defined by B=(B'-u)/s, where B' is the raw B-factor value, u and s are respectively the mean and standard deviation of the raw B-factors along the sequence. (Click here to read more about predicted normalized B-factor)

Top 10 threading templates used by I-TASSER

Rank

PDB
Hit

Iden1

Iden2

Cov

Norm.
Zscore

Download
Align.

                  20                  40                  60                  80                 100

                   |                   |                   |                   |                   |

Sec.Str
Seq

CCCCCCCHHHHHHHHHHHHHHHCCHHHHHHHCCCCEEEEHCCCCEHCHHHHHHHHHHHHHHCCCEEEEEEEEEEHCCEEEEEEEEHCCCCEEEEEEEEEEEHCCEEEEEEEEHCCCCCC
MGSTPPRTPQEVFAHHGQALAAGDLDEIVADYADDSFVITPAGIARGKEGIRQLFVKLLDDIPNALWDLKTQIFEGDILFLEWTANSAVSRVDDGVDTFVFRDGTIWAHTVRYTPHPKT

5aifA

0.16

0.15

0.95

2.43

MUSTER

MT------PIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNIPMPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

5aifA

0.17

0.16

0.95

2.74

dPPAS

------MTPIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNPMEPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

5aifA

0.16

0.15

0.95

3.11

wdPPAS

MT------PIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNIPEPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

3k0zA

0.16

0.98

2.50

wMUSTER

SLSQKEATEVHAAQRFYAFWDTGKEELIPQTVTENFFDHTLKGRPQGTEGLKFAAQNFRKIVPNIHCEIEDLLVVGDKVTARLSFTGDKKIDFFAIDILHVKDGKITEDWHLEDNL--T

5aifA

0.16

0.15

0.95

3.40

wPPAS

MT------PIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNIPEPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

5aifA

0.17

0.16

0.95

4.33

dPPAS2

MT------PIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNPMEPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

5aifA

0.17

0.16

0.95

3.16

PPAS

MT------PIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNPMEPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

5aifA

0.17

0.16

0.95

2.62

Env-PPAS

MT------PIETVTAFIAHWNSGDMEAMYDLCAEDVVWHNPMEPIAGKPAMRAAVEGFMANVSQCDWQVHAIAANGATVLTERTDGFGRRATIRVMGTFECAERRIIAWRDYFDMLEFQ

5cxoA

0.18

0.97

2.21

MUSTER

MQD--EQKRKEIVAEYFRKVNEGDVDAIVEMFTENATIEDPVGVREGRAAQREYFNSNVTAEVTIEPGHLSAGQDGKSVAVALAAEMRTRVKINAVDVFTLPEGKIDSMRVFWG--MTD

4kvhA

0.17

0.16

0.92

2.58

dPPAS

----NAMDRVATARAYYRALDEHDYDLLSDVLAPDFVHDRPDRTIEGRERFVRFMREERP-QTDTSHPIATIYTGASTVAVEGRLLSDGAEITQFVDVFAFEDGVIGRIRTHTPE----

(a)	Iden1 is the number of template residues identical to query divided by number of aligned residues.
(b)	Iden2 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.
(e)	Download Align. list the threading program used to identify the template provide the 3D structure of aligned regions of threading templates.

Top 3 final models predicted by I-TASSER

(For each target, I-TASSER simulations generate a large ensemble of structural conformations, called decoys. To select the final models, I-TASSER uses the SPICKER program to cluster all the decoys based on the pair-wise structure similarity, and reports up to five models which corresponds to the five largest structure clusters. The confidence of each model is quantitatively measured by C-score that is calculated based on the significance of threading template alignments and the convergence parameters of the structure assembly simulations. C-score is typically in the range of [-5, 2], where a C-score of higher value signifies a model with a high confidence and vice-versa. TM-score and RMSD are estimated based on C-score and protein length following the correlation observed between these qualities. Since the top 5 models are ranked by the cluster size, it is possible that the lower-rank models have a higher C-score in rare cases. Although the first model has a better quality in most cases, it is also possible that the lower-rank models have a better quality than the higher-rank models as seen in our benchmark tests. If the I-TASSER simulations converge, it is possible to have less than 5 clusters generated. This is usually an indication that the models have a good quality because of the converged simulations.)

More about C-score

Local structure accuracy of first model

Download Model 1

C-score=0.90

Estimated TM-score = 0.84±0.08

Estimated RMSD = 2.6±1.9Å

Download Model 2

C-score=-4.34

Download Model 3

C-score=-1.24

Proteins structureally close to the target in PDB (as identified by TM-align

(After the structure assembly simulation, I-TASSER uses the TM-align structural alignment program to match the first I-TASSER model to all structures in the PDB library. This section reports the top 10 proteins from the PDB that have the closest structural similarity, i.e. the highest TM-score, to the predicted I-TASSER model. Due to the structural similarity, these proteins often have similar function to the target. However, users are encouraged to use the data in the next section 'Predicted function using COACH' to infer the function of the target protein, since COACH has been extensively trained to derive biological functions from multi-source of sequence and structure features which has on average a higher accuracy than the function annotations derived only from the global structure comparison.)

Top 10 Identified stuctural analogs in PDB

Rank	PDB Hit	TM-score	RMSD^a	IDEN^a	Cov
1	5aifA	0.913	0.85	0.168	0.950
2	5aihA	0.861	1.24	0.207	0.933
3	5cxoA	0.860	1.70	0.165	0.958
4	3rgaA	0.852	1.80	0.147	0.966
5	3soyA	0.851	1.79	0.134	0.941
6	1e3vB	0.850	2.01	0.178	0.983
7	3i0yA	0.846	1.66	0.165	0.950
8	3wmdA	0.846	1.79	0.149	0.958
9	2z7aC	0.842	1.97	0.155	0.958
10	1tuhA	0.840	1.85	0.129	0.975

(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 function using COACH

(This section reports biological annotations of the target protein by COACH based on the I-TASSER structure prediction. COACH is a meta-server approach that combines multiple function annotation results from the COFACTOR, TM-SITE and S-SITE programs.)

Enzyme Commission (EC) numbers and active sites

Rank	Cscore^EC	PDB Hit	TM-score	RMSD^a	IDEN^a	Cov	EC Number	Active Site Residues
1	0.340	1buqA	0.801	2.35	0.250	0.966	5.3.3.1	55,97
2	0.195	3e99A	0.795	2.38	0.112	0.966	1.14.12.10	83
3	0.191	2ux0A	0.757	2.49	0.096	0.933	2.7.11.17	98,100
4	0.153	3en1B	0.793	2.37	0.102	0.958	1.14.12.3,1.14.12.11	27,69
5	0.083	1o7hB	0.803	2.18	0.051	0.958	1.14.12.12	NA
6	0.060	1kv9A	0.503	4.03	0.083	0.781	1.1.99.-	77
7	0.060	3gzxB	0.795	2.30	0.127	0.958	1.14.12.18	18,69
8	0.060	1zjaA	0.493	4.23	0.064	0.798	5.4.99.11	NA
9	0.060	1izjA	0.496	4.26	0.063	0.798	3.2.1.135,3.2.1.1	NA
10	0.060	1g72A	0.558	3.97	0.112	0.874	1.1.99.8	41
11	0.060	2wkgA	0.495	4.03	0.046	0.756	3.2.1.54	26
12	0.060	2welA	0.321	4.56	0.036	0.563	2.7.11.17	NA
13	0.060	2d0gA	0.496	4.28	0.063	0.798	3.2.1.135	91
14	0.060	4stdA	0.820	2.25	0.067	0.983	4.2.1.94	NA
15	0.060	1hkxA	0.758	2.37	0.113	0.933	2.7.11.17	11,18,22,73
16	0.060	2bngC	0.825	2.16	0.147	0.966	3.3.2.8	84
17	0.060	1m7xB	0.524	3.73	0.062	0.798	2.4.1.18	NA
18	0.060	2z1kA	0.492	4.00	0.048	0.740	3.2.1.41	NA
19	0.060	1e3vB	0.850	2.01	0.178	0.983	5.3.3.1	32,97
20	0.060	3elqB	0.516	4.21	0.029	0.807	2.8.2.22	41
21	0.060	1nu3B	0.828	1.60	0.129	0.933	3.3.2.8	NA
22	0.060	1yiqA	0.498	4.01	0.093	0.790	1.1.99.-	77
23	0.060	3k1dA	0.520	3.80	0.071	0.798	2.4.1.18	NA
24	0.060	2d0vA	0.566	4.17	0.094	0.866	1.1.99.8	77

(a)	Cscore^EC is the confidence score for the 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.

[Click on result.tar.bz2 to download the tarball file including all modelling results listed on this page]

Please cite the following articles when you use the I-TASSER server:
1.	J Yang, R Yan, A Roy, D Xu, J Poisson, Y Zhang. The I-TASSER Suite: Protein structure and function prediction. Nature Methods, 12: 7-8, 2015.
2.	J Yang, Y Zhang. I-TASSER server: new development for protein structure and function predictions, Nucleic Acids Research, 43: W174-W181, 2015.
3.	A Roy, A Kucukural, Y Zhang. I-TASSER: a unified platform for automated protein structure and function prediction. Nature Protocols, 5: 725-738, 2010.
4.	Y Zhang. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics, 9: 40, 2008.