{"feature_sets":[{"about":"Physico-chemical properties of a protein sequence (ProtParam-compatible) and its composition","features":[{"name":"length","group":"size","unit":"residues","description":"Number of residues"},{"name":"molecular_weight","group":"size","unit":"Da","description":"Average molecular weight (average residue masses plus one water)","reference":"Gasteiger et al. (2005) Protein identification and analysis tools on the ExPASy server"},{"name":"isoelectric_point","group":"charge","unit":"pH","description":"Theoretical pI: the pH at which the net charge is zero (Bjellqvist pK values with terminal-dependent values)","reference":"Bjellqvist et al. (1993) Electrophoresis 14:1023; (1994) 15:529"},{"name":"net_charge_ph7","group":"charge","unit":"e","description":"Net charge at pH 7.0 with the same pK values","reference":"Henderson–Hasselbalch"},{"name":"charge_density_ph7","group":"charge","unit":"e/residue","description":"Net charge at pH 7.0 per residue"},{"name":"extinction_280_reduced","group":"optics","unit":"M^-1 cm^-1","description":"Molar extinction coefficient at 280 nm with every cysteine reduced: 5500·W + 1490·Y","reference":"Pace et al. (1995) Protein Sci 4:2411"},{"name":"extinction_280_cystines","group":"optics","unit":"M^-1 cm^-1","description":"Molar extinction coefficient at 280 nm with every cysteine pair forming a cystine: + 125 per cystine","reference":"Pace et al. (1995) Protein Sci 4:2411"},{"name":"absorbance_280_1mgml","group":"optics","unit":"AU","description":"Absorbance at 280 nm of a 1 mg/mL solution (1 cm, cysteines reduced)"},{"name":"instability_index","group":"stability","description":"Instability index; above 40 suggests a protein unstable in vitro","reference":"Guruprasad et al. (1990) Protein Eng 4:155"},{"name":"aliphatic_index","group":"stability","description":"Relative volume of aliphatic side chains: X(Ala) + 2.9·X(Val) + 3.9·(X(Ile) + X(Leu)), mole percent","reference":"Ikai (1980) J Biochem 88:1895"},{"name":"gravy","group":"hydropathy","description":"Grand average of hydropathy (Kyte–Doolittle)","reference":"Kyte & Doolittle (1982) J Mol Biol 157:105"},{"name":"aromaticity","group":"hydropathy","unit":"fraction","description":"Fraction of F, W and Y","reference":"Lobry & Gautier (1994) Nucleic Acids Res 22:3174"},{"name":"frac_tiny","group":"classes","unit":"fraction","description":"Fraction of tiny residues (ACGST)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_small","group":"classes","unit":"fraction","description":"Fraction of small residues (ABCDGNPSTV)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_aliphatic","group":"classes","unit":"fraction","description":"Fraction of aliphatic residues (AILV)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_aromatic","group":"classes","unit":"fraction","description":"Fraction of aromatic residues (FHWY)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_nonpolar","group":"classes","unit":"fraction","description":"Fraction of nonpolar residues (ACFGILMPVWY)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_polar","group":"classes","unit":"fraction","description":"Fraction of polar residues (DEHKNQRSTZ)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_charged","group":"classes","unit":"fraction","description":"Fraction of charged residues (BDEHKRZ)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_basic","group":"classes","unit":"fraction","description":"Fraction of basic residues (HKR)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_acidic","group":"classes","unit":"fraction","description":"Fraction of acidic residues (BDEZ)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"cysteine_count","group":"composition","unit":"residues","description":"Number of cysteines (disulfide capacity)"},{"name":"entropy_bits","group":"complexity","unit":"bits","description":"Shannon entropy of the amino-acid composition"},{"name":"entropy_normalized","group":"complexity","unit":"fraction","description":"Shannon entropy divided by its maximum, log2(20)"},{"name":"low_complexity_fraction","group":"complexity","unit":"fraction","description":"Fraction of residues SEG masks as low complexity (window 12, 2.2, 2.5, as BLAST)","reference":"Wootton & Federhen (1993) Comput Chem 17:149"},{"name":"ambiguous_fraction","group":"complexity","unit":"fraction","description":"Fraction of letters outside the 20 standard amino acids (X, B, Z, J, U, 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leucine"},{"name":"aa_M","group":"composition","unit":"fraction","description":"Fraction of methionine"},{"name":"aa_N","group":"composition","unit":"fraction","description":"Fraction of asparagine"},{"name":"aa_P","group":"composition","unit":"fraction","description":"Fraction of proline"},{"name":"aa_Q","group":"composition","unit":"fraction","description":"Fraction of glutamine"},{"name":"aa_R","group":"composition","unit":"fraction","description":"Fraction of arginine"},{"name":"aa_S","group":"composition","unit":"fraction","description":"Fraction of serine"},{"name":"aa_T","group":"composition","unit":"fraction","description":"Fraction of threonine"},{"name":"aa_V","group":"composition","unit":"fraction","description":"Fraction of valine"},{"name":"aa_W","group":"composition","unit":"fraction","description":"Fraction of tryptophan"},{"name":"aa_Y","group":"composition","unit":"fraction","description":"Fraction of tyrosine"}],"kind":"protein","name":"gl1x-protein-1","prefix":"p_"},{"about":"Size, shape, secondary structure, contacts, confidence and GSA composition of a protein chain with coordinates","features":[{"name":"residues","group":"size","unit":"residues","description":"Residues with CA coordinates"},{"name":"radius_of_gyration","group":"shape","unit":"Å","description":"Radius of gyration of the CA atoms"},{"name":"rg_relative","group":"shape","unit":"ratio","description":"Radius of gyration over that of a compact chain of the same length, 2.2·N^0.38 Å; near 1 for a compact globule, larger for extended or multi-domain chains","reference":"Skolnick, Kolinski & Ortiz (1997) J Mol Biol 265:217"},{"name":"asphericity","group":"shape","description":"Relative shape anisotropy κ² of the CA gyration tensor: 0 for a sphere, 1 for a rod","reference":"Theodorou & Suter (1985) Macromolecules 18:1206"},{"name":"max_dimension","group":"shape","unit":"Å","description":"Largest distance between two CA 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quantize new inputs with the model's own scale_q","packing":"one little-endian int32 per input in feature order: the bytes the GL1F runtime's predict functions take","quantization":"q = clamp(round(x · scale_q)) to the int32 range, the GL1F Forest input rule (half rounds away from zero for positive x, toward +∞ as JavaScript's Math.round)"},"molnft_paths":{"0xbf7491af3407816dfa88a5ea4c82e8a2b1d721ed:4":"/molnft/Q43495"},"record":{"accession":"Q43495","collection_name":"MolNFT v1 / AlphaFold","contract_address":"0xbf7491af3407816dfa88a5ea4c82e8a2b1d721ed","molecular_id":"Q43495","molnft_version":"v1","pdb_id":null,"structure_available":true,"title":"ALPHAFOLD MONOMER V2.0 PREDICTION FOR PROTEIN 108 (Q43495)","token_id":"4","url":"/molnft/Q43495"},"sequences":[{"ambiguous":0,"chain_id":"A","chains":["A"],"is_primary":true,"length":102,"notes":["102 residues, 10,576.3 Da (10.6 kDa) average mass","Theoretical pI 5.42; net charge -1.5 at pH 7 (acidic)","Extinction at 280 nm: 500 M⁻¹cm⁻¹ with every cysteine pair a cystine, 0 reduced; A280 of 1 mg/mL ≈ 0.000","Instability index 88.99: classified unstable in vitro (40 or more)","GRAVY +0.536: hydrophobic on average; aliphatic index 101.4 (higher suggests more thermostable)","SEG masks 30.4% of the residues as low complexity"],"sequence":"MASVKSSSSSSSSSFISLLLLILLVIVLQSQVIECQPQQSCTASLTGLNVCAPFLVPGSPTASTECCNAVQSINHDCMCNTMRIAAQIPAQCNLPPLSCSAN","sequence_key":"pdb-chain:A","sequence_keys":["pdb-chain:A"],"sequence_type":"protein","set":"gl1x-protein-1","sha256":"6e2490bec8aa9914afa26def532c94ee58676a4e60fc5c1adc62319f766d4f78","values":[102,10576.28,5.4239,-1.4958,-0.014665,0,500,0,88.9931,101.3725,0.5363,0.019608,0.431373,0.637255,0.343137,0.029412,0.568627,0.431373,0.058824,0.029412,0.029412,9,3.71539,0.85966,0.303922,0,0.088235,0.088235,0.009804,0.019608,0.019608,0.019608,0.009804,0.068627,0.009804,0.117647,0.029412,0.058824,0.068627,0.078431,0.009804,0.186275,0.04902,0.068627,0,0]}],"sequences_truncated":false,"structure":{"chains":[{"accessions":["Q43495"],"chain_id":"A","chains":["A"],"kind":"protein","notes":["Radius of gyration 25.22 Å, 1.98× that of a compact chain of 102 residues: extended or made of several domains","Secondary structure (TM-align): 55.9% helix in 4 helices, 8.8% strand in 2 strands","0.28 CA contacts per residue, 27.6% long-range; relative contact order 0.170","Predicted model: mean pLDDT 79.8, 26.5% of residues below 70"],"residues":102,"secondary":"CCEEEEEEECTCCHHHHHHHHHHHHHHHHHHHHHCCCTHHHHHHHHHCHHCCHHCCTCCCCCCTHHHHHHHCCCTHHHHHHHHHHHHHHHHTCCCCCEECCC","set":"gl1x-structure-1","values":[102,25.2193,1.9772,0.5969,78.72,67.243,0.558824,0.088235,0.058824,0.294118,4,2,0.2843,0.310345,0.275862,0.170047,17.3448,0,79.824,15.132,1,0.264706,3.214075,0,0.029412,0.029412,0.088235,0,0.058824,0.009804,0.029412,0,0.303922,0,0.029412,0.029412,0.019608,0.058824,0.039216,0.205882,0,0.04902,0.019608]}],"entry_id":null,"method":null,"predicted":true,"skipped":[],"status":"complete"}}