Single Sequence Results
Summary
View basic information related to this submission
Request ID: d2db23f2-044f-4521-ba4e-3486ba442ace
Predictor Type: dynamine,disomine,efoldmine,agmata
Status: FINISHED
Count: 1
Min: 1114
Max: 1114
Avg: 1114
Created At: 2026-01-13 16:18:28
Last Updated: 2026-01-13 16:18:59
Input File:
>sp|P07949|RET_HUMAN Proto-oncogene tyrosine-protein kinase receptor Ret OS=Homo sapiens OX=9606 GN=RET PE=1 SV=3
MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAP
EEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLT
VYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENR
PPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELV
AVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFD
ADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNR
NLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFA
QIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAE
LHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGR
CEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPR
GIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCY
HKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFP
RKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLK
QVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDH
PDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVY
EEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERL
FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAA
STPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRA
DGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDSOverview for Sequence
The biophysical predictions calculated for the selected sequence are shown below in one single plot.
DynaMine's backbone dynamics
- Values > 1.0: Membrane spanning regions
- Values > 0.80 and < 1.0: Rigid conformations
- Values > 0.69 and < 0.80: Context dependent
- Values < 0.69: Flexible regions
DynaMine's side chain dynamics
Higher values mean more likely rigid. These values are highly dependent on the amino acid type (i.e. a Trp will be rigid, an Asp flexible).
DynaMine's conformational propensities
- Sheet: Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet.
- Helix: Alpha helices are right-handed coiled or spiral structures where each amino acid residue is hydrogen bonded to residues four positions away, forming a stable helical conformation.
- Coil: Coil regions lack regular secondary structure and are characterized by their flexibility and lack of specific hydrogen bonding patterns.
- ppII (polyproline II): A left-handed helical structure commonly found in proline-rich regions, characterized by three residues per turn and specific dihedral angles.
Higher values indicate higher propensities for each structural element.
EFoldMine's earlyFolding propensity
Values above 0.169 indicate residues that are likely to start the protein folding process, based on only local interactions with other amino acids.
DisoMine's disorder prediction
Values above 0.50 indicate that this is likely a disordered residue.
Agmata beta-sheet aggregation propensity
These values are divided by a factor of 20 from the original. Peaks indicate residues likely to be involved in beta-sheet aggregation.
The biophysical predictions calculated for the selected sequence are shown below tool by tool.
DynaMine's backbone dynamics
- Values > 1.0: Membrane spanning regions
- Values > 0.80 and < 1.0: Rigid conformations
- Values > 0.69 and < 0.80: Context dependent
- Values < 0.69: Flexible regions
DynaMine's side chain dynamics
Higher values mean more likely rigid. These values are highly dependent on the amino acid type (i.e. a Trp will be rigid, an Asp flexible).
DynaMine's conformational propensities
- Sheet: Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet.
- Helix: Alpha helices are right-handed coiled or spiral structures where each amino acid residue is hydrogen bonded to residues four positions away, forming a stable helical conformation.
- Coil: Coil regions lack regular secondary structure and are characterized by their flexibility and lack of specific hydrogen bonding patterns.
- ppII (polyproline II): A left-handed helical structure commonly found in proline-rich regions, characterized by three residues per turn and specific dihedral angles.
Higher values indicate higher propensities for each structural element.
EFoldMine's earlyFolding propensity
Values above 0.169 indicate residues that are likely to start the protein folding process, based on only local interactions with other amino acids.
DisoMine's disorder prediction
Values above 0.50 indicate that this is likely a disordered residue.
Agmata beta-sheet aggregation propensity
These values are divided by a factor of 20 from the original. Peaks indicate residues likely to be involved in beta-sheet aggregation.
The biophysical predictions calculated for the selected sequence are shown below in a table.
| Position | Residue | Backbone | Sidechain | DisoMine | Coil | Helix | PPII | Sheet | Early Folding | Agmata |
|---|