I-TASSER-MTD Results for job ITM552669806



Query Sequence and Predicted Domain Definition

>query_protein (159 residues)
MTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK
  • domain 1: 1-159
  • 1 domains in total. Different colors represent different domains. The domain definition is used for the domain structure modeling, see the domain boundary prediction part for details.

    Final Full-length Models Predicted by I-TASSER-MTD

    Top 5 models constructed by I-TASSER-MTD

    Click
    to view
    eTM-score eRMSD(Å) P-score PDB file
    Model 1 0.95+-0.05 1.7+-1.5 1.00 Download model

    (a)Colored by domain: domain 1 in red.
    (b)For each target, I-TASSER-MTD generates an ensemble of structural conformations by starting from a set of initial models generated by different templates. The server reports up to five final models sorted by the energy. The accuracy of each model is quantitatively evaluated by estimated TM-score (eTM-score) and estimated RMSD (eRMSD) that are calculated based on the significance of the structural analogous templates for domain models assembly, convergence parameters of the domain assembly simulations, satisfaction degrees of the inter-domain distances/interfaces, and the estimated accuracy of the individual domain model. eTM-score is typically in the range of [0,1], where an eTM-score of higher value signifies a model with a high confidence and vice-versa.
    (d)Since the top 5 models are ranked by the energy or cluster size, it is possible that the lower-rank models have a higher eTM-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.
    More about eTM-score
    (e)P-score is used to estimate the population formed in the modeling simulations based on the structural similarity or SPICKER clustering. P-score ranges from 0 to 1, and a higher value means the structure occurs more often in the simulation trajectory.
    (f)The inter-domain interaction is defined as ≥1 residue pairs with distance <8Å apart from the linker region. The probability ranges from 0 to 1, and a large value indicates the two domains have a large probability of interaction.

    Predicted Individual Domain Structures

    Structure of domain 1
    Download dom1.pdb
     

    Predicted Secondary Structure

    1                 20                  40                  60                  80                 100                 120                 140                 
    |                  |                   |                   |                   |                   |                   |                   |                   
    Sequence MTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK
     
    Prediction CSSSSSSSSCCCCCSCCCCCCCCCCHHHHHHHHHHHCCCSSSSSCCHHHHCCCCCCCCSSSSSSCCCCCCCCCSSSSSCHHHHHHHCCCSSSSCCHHHHHHHHHHCCSSSSSSSCCCCCCCSSCCCCCHHHCSSSSSSSCCCCCCCCCCSSSSSSSSCC
     
    Conf.Score 959999999289964289971762749999999985698399936715538887899859999368887899979990899998626967998469999999997999999997774365332899994656999998535677899646999999869
     
    H: Helix; S: Strand; C: Coil

    Predicted Solvent Accessibility

    1                 20                  40                  60                  80                 100                 120                 140                 
    |                  |                   |                   |                   |                   |                   |                   |                   
    Sequence MTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK
     
    Conf.Score 440100000043310046450213146115303511443000102111420441256220000023451526302003124301620640000112200420052033010030465160002005134740531455635346746150312334458
     
    Values range from 0 (buried residue) to 8 (highly exposed residue)

    Information for Domain Boundary Detection

    Predicted domain boundary on contact map FU-score curve of continuous domain FU-score heatmap of discontinuous domain    Predicted domain(s)   
    Contact map
    Download contact map
    Contact map
    Download the FU-score (continuous)
    Contact map
    Download the FU-score (discontinuous)

    Modelinga
    Domain 1(D1): 1-159
    Without linkerb
    Domain 1(D1): 1-159

    (a) Domain definition for the domain structure modeling. (b) Domain definition without including the linker.

    Top 10 Full-length Templates for Domain Assembly

     Rank  Template  SeqId  TplScore  1                 20                  40                  60                  80                 100                 120                 140                 
    |                  |                   |                   |                   |                   |                   |                   |                   
    QueryMTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK 
    18ssx0.450.86MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEAIGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELEEEIFIFGGAQIYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNPYTYYYHVYEKQQ
    23fl80.450.97MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEAIGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCEEIFIFGGAQIYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNPYTYYYHVYEKQQ
    33fyv0.990.99-TLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK
    44q6a0.970.98-TLSILVAHDLQRVIGFENQLPWHLPNDLKHLKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLYEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRK-
    53fl80.440.96MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEAIGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFLNEEEIFIFGGAQIYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNPYTYYYHVYEKQQ
    63fyv0.990.98--LSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK
    73ia40.390.94MIVSMIAALANNRVIGLDNKMPWHLPAELQLFKRATLGKPIVMGRNTFESIGRPLPGRLNIVLSRQTDYQPEGVTVVATLEDAVVAVEELMIIGGATIYNQCLAAADRLYLTHIELTTEGDTWFPDYEQYNWQEIEHESYAADDKNPHNYRFSLLERV-
    88ssx0.450.85MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEAIGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNIFIFGGAQIYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNPYTYYYHVYEKQQ
    97fgw0.330.83-PVCLVVAMTPKRGIGINNGLPWHLTTDFKHFSRVTKTTPVVMGRKTWESMPRPLVDRLNIVVSSSLKEEQQRVRVCASLPAALSLLDQIFVVGGAGLYEAALGVASHLYITRVAREFPCDVFFPAFPGDDILSNKSTASKTFSDNGVPYDFVVLEK--
    107t7q0.990.98-TLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRK-
    (a)All the residues are colored in black; however, those residues in template which are identical to the residue in the query sequence are highlighted in color. Coloring scheme is based on the property of amino acids, where polar are brightly coloured while non-polar residues are colored in dark shade. (more about the colors used) 
    (b)Rank of templates represents the top five structural aligenment templates identified by using TM-align.
    (c)SeqId is the ratio between the number of identical residues and query length.
    (d)TplScore is the score of the template calculated based on harmonic mean of TM-scores between all domain models and the template.

    Predicted Distance/Interface Map for Domain Assembly

    CA distance map with distance < 20Å CB distance map with distance < 20Å CA interface map with distance < 18Å CB interface map with distance < 18Å
    CA20
    Download CA distance map
    CB20
    Download CB distance map
    CA19
    Download CA interface map
    CB19
    Download CB interface map

    [Back to server]
    Reference:
  • Xiaogen Zhou, Wei Zheng, Yang Li, Robin Pearce, Chengxin Zhang, Eric W. Bell, Guijun Zhang, and Yang Zhang. I-TASSER-MTD: A deep-learning based platform for multi-domain protein structure and function prediction, Nature Protocols, 17: 2326-2353 (2022).
  • Xiaogen Zhou, Jun Hu, Chengxin Zhang, Guijun Zhang, Yang Zhang. Assembling multidomain protein structures through analogous global structural alignments. Proceedings of the National Academy of Sciences, 116: 15930-15938 (2019).
  • yangzhanglabumich.edu | (734) 647-1549 | 100 Washtenaw Avenue, Ann Arbor, MI 48109-2218