Learn more about ThermoMutDB in less than 3 minutes.

Check some examples of using ThermoMutDB API

You can use the API form to choose an endpoint and setup parameters to get data, like in the following examples:

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STEP 1: Choose one of the endpoints available.
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STEP 2: (1) To start click on "Try it out". (2)Type the desired parameters.
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STEP 3: (3) Execute query button. (4) CURL command request for your query. (5) URL request for your query and (6) the response body.

ThermoMutDB API also allows requests by URL.
To perform your URL follow the pattern: API url + name of endpoint + attribute + parameter
To know what variables could be used, check the API documentation form, select an endpoint, copy the GET operation path, and replace variables in brackets to your parameters.
For example, to request data which number of mutations are between 2 and 5 use the URL: http://biosig.unimelb.edu.au/thermomutdb/api/v1/VariantInformation/number_mutations/from/2/to/5

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Request URL variables: (1) name of endpoint, (2) attribute, and (3) parameter.

Request by Curl are accepted and needs URL presented in "Request by URL", for example, to request data which have ΔΔG between 1 and 5 use:
curl -X GET "http://biosig.unimelb.edu.au/thermomutdb/api/v1/ThermodynamicData/ddg/from/1/to/5" -H "accept: application/json"

Note: Soon we will provide more flexible criteria to be used in curl and URL requests. All improvements will be published here.

Information content of ThermoMutDB

Content Description Measure* API attribute

Protein Information

Protein name

Protein Name

  

-

Source

Protein Organism

  

-

Uniprot

Uniprot Code

  

-

PDB wild

Protein Data Bank code 

  

-

PDB mutant

PDB code for mutant (when is available)

  

-

PDBs template

PDBs used as a template to model wild_type (when is available and necessary)

  

-

Length

Length of sequence

  

-

Weight

Molecular weight

  

-

PIR ID

Protein Information Resource

  

-

SWISSPROT ID

Code of Swiss-Prot (Revised Entries)

  

-

Mutation

Three-digits mutation code

  

-

Mutated chain

Mutated chain

  

-

Mutation count

Number of mutations

  

-

Experimental Conditions

Temperature

Experimental temperature

Kelvin (K)

-

pH

Experimental pH

  

-

Measure

Experimental techniques for studying protein folding. 

  

-

Method

Techniques to denature a protein

  

-

Thermodynamic data

ΔΔG

Variation of Free Gibbs Energy on the experiment

kcal/mol-1

-

ΔTm

Variation of Melting Temperature on the experiment

Kelvin (K)

-

Structural environment

SST

Secondary Structure classification

  

-

RSA

Relative accessible surface area

  

-

PHI

Phi angle value

  

-

PSI

Psi angle value

  

-

Residue Depth

The average distance of atoms of wild-type residue from the solvent accessible area

  

-

CA Depth

The average distance of atoms of CA from the solvent accessible area

  

-

Relative B Factor

Temperature factor

  

-

Substitution matrices scores

Blosum 62

BLOSUM 62 matrix score

  

-

Pam 250

PAM 250 matrix score

  

-

Pharmacophore changes

POS

Positive

  

-

NEG

Negative

  

-

ACC

Hydrogen bond acceptors

  

-

DON

Hydrogen bond donors 

  

-

ARO

Aromatic rings

  

-

SUL

Sulfuric acid

  

-

NEU

Neutral

  

-

Literature information

Reference

Publication reference

  

-

PMID

Pubmed code of publication

  

-

DOI

Digital Object Identifier of publication

  

-

YEAR

Year of publication

  

-

* If there is.