{"AccNo":"ANDN920101","PropDesc":"alpha-CH chemical shifts (Andersen et al., 1992)","LITDBNo":"LIT:1810048b PMID:1575719","Author":"Andersen, N.H., Cao, B. and Chen, C.","ArtTitle":"Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and aL sites","JournalRef":"Biochem. and Biophys. Res. Comm. 184, 1008-1014 (1992)","A":4.35,"R":4.38,"N":4.75,"D":4.76,"C":4.65,"E":4.29,"Q":4.37,"G":3.97,"H":4.63,"I":3.95,"L":4.17,"K":4.36,"M":4.52,"F":4.66,"P":4.44,"S":4.5,"T":4.35,"W":4.7,"Y":4.6,"V":3.95}
{"AccNo":"ARGP820101","PropDesc":"Hydrophobicity index (Argos et al., 1982)","LITDBNo":"LIT:0901079b PMID:7151796","Author":"Argos, P., Rao, J.K.M. and Hargrave, P.A.","ArtTitle":"Structural prediction of membrane-bound proteins","JournalRef":"Eur. J. Biochem. 128, 565-575 (1982)","A":0.61,"R":0.6,"N":0.06,"D":0.46,"C":1.07,"E":0.47,"Q":0,"G":0.07,"H":0.61,"I":2.22,"L":1.53,"K":1.15,"M":1.18,"F":2.02,"P":1.95,"S":0.05,"T":0.05,"W":2.65,"Y":1.88,"V":1.32}
{"AccNo":"ARGP820102","PropDesc":"Signal sequence helical potential (Argos et al., 1982)","LITDBNo":"LIT:0901079b PMID:7151796","Author":"Argos, P., Rao, J.K.M. and Hargrave, P.A.","ArtTitle":"Structural prediction of membrane-bound proteins","JournalRef":"Eur. J. Biochem. 128, 565-575 (1982)","A":1.18,"R":0.2,"N":0.23,"D":0.05,"C":1.89,"E":0.11,"Q":0.72,"G":0.49,"H":0.31,"I":1.45,"L":3.23,"K":0.06,"M":2.67,"F":1.96,"P":0.76,"S":0.97,"T":0.84,"W":0.77,"Y":0.39,"V":1.08}
{"AccNo":"ARGP820103","PropDesc":"Membrane-buried preference parameters (Argos et al., 1982)","LITDBNo":"LIT:0901079b PMID:7151796","Author":"Argos, P., Rao, J.K.M. and Hargrave, P.A.","ArtTitle":"Structural prediction of membrane-bound proteins","JournalRef":"Eur. J. Biochem. 128, 565-575 (1982)","A":1.56,"R":0.45,"N":0.27,"D":0.14,"C":1.23,"E":0.23,"Q":0.51,"G":0.62,"H":0.29,"I":1.67,"L":2.93,"K":0.15,"M":2.96,"F":2.03,"P":0.76,"S":0.81,"T":0.91,"W":1.08,"Y":0.68,"V":1.14}
{"AccNo":"BEGF750101","PropDesc":"Conformational parameter of inner helix (Beghin-Dirkx, 1975)","LITDBNo":"LIT:1309065 PMID:50789","Author":"Beghin, F. and Dirkx, J.","ArtTitle":"Une methode statistique simple de prediction des conformations proteiques","JournalRef":"Arch. Int. Physiol. Biochim. 83, 167-168 (1975)","A":1,"R":0.52,"N":0.35,"D":0.44,"C":0.06,"E":0.73,"Q":0.44,"G":0.35,"H":0.6,"I":0.73,"L":1,"K":0.6,"M":1,"F":0.6,"P":0.06,"S":0.35,"T":0.44,"W":0.73,"Y":0.44,"V":0.82}
{"AccNo":"BEGF750102","PropDesc":"Conformational parameter of beta-structure (Beghin-Dirkx, 1975)","LITDBNo":"LIT:1309065 PMID:50789","Author":"Beghin, F. and Dirkx, J.","ArtTitle":"Une methode statistique simple de prediction des conformations proteiques","JournalRef":"Arch. Int. Physiol. Biochim. 83, 167-168 (1975)","A":0.77,"R":0.72,"N":0.55,"D":0.65,"C":0.65,"E":0.55,"Q":0.72,"G":0.65,"H":0.83,"I":0.98,"L":0.83,"K":0.55,"M":0.98,"F":0.98,"P":0.55,"S":0.55,"T":0.83,"W":0.77,"Y":0.83,"V":0.98}
{"AccNo":"BEGF750103","PropDesc":"Conformational parameter of beta-turn (Beghin-Dirkx, 1975)","LITDBNo":"LIT:1309065 PMID:50789","Author":"Beghin, F. and Dirkx, J.","ArtTitle":"Une methode statistique simple de prediction des conformations proteiques","JournalRef":"Arch. Int. Physiol. Biochim. 83, 167-168 (1975)","A":0.37,"R":0.84,"N":0.97,"D":0.97,"C":0.84,"E":0.53,"Q":0.64,"G":0.97,"H":0.75,"I":0.37,"L":0.53,"K":0.75,"M":0.64,"F":0.53,"P":0.97,"S":0.84,"T":0.75,"W":0.97,"Y":0.84,"V":0.37}
{"AccNo":"BHAR880101","PropDesc":"Average flexibility indices (Bhaskaran-Ponnuswamy, 1988)","LITDBNo":"LIT:1414112","Author":"Bhaskaran, R. and Ponnuswamy, P.K.","ArtTitle":"Positional flexibilities of amino acid residues in globular proteins","JournalRef":"Int. J. Peptide Protein Res. 32, 241-255 (1988)","A":0.357,"R":0.529,"N":0.463,"D":0.511,"C":0.346,"E":0.497,"Q":0.493,"G":0.544,"H":0.323,"I":0.462,"L":0.365,"K":0.466,"M":0.295,"F":0.314,"P":0.509,"S":0.507,"T":0.444,"W":0.305,"Y":0.42,"V":0.386}
{"AccNo":"BIGC670101","PropDesc":"Residue volume (Bigelow, 1967)","LITDBNo":"LIT:2004108b PMID:6048539","Author":"Bigelow, C.C.","ArtTitle":"On the average hydrophobicity of proteins and the relation between it and protein structure","JournalRef":"J. Theor. Biol. 16, 187-211 (1967) (Asn Gln 5.0)","A":52.6,"R":109.1,"N":75.7,"D":68.4,"C":68.3,"E":84.7,"Q":89.7,"G":36.3,"H":91.9,"I":102,"L":102,"K":105.1,"M":97.7,"F":113.9,"P":73.6,"S":54.9,"T":71.2,"W":135.4,"Y":116.2,"V":85.1}
{"AccNo":"BIOV880101","PropDesc":"Information value for accessibility; average fraction 35% (Biou et al., 1988)","LITDBNo":"LIT:1413106b PMID:3237683","Author":"Biou, V., Gibrat, J.F., Levin, J.M., Robson, B. and Garnier, J.","ArtTitle":"Secondary structure prediction: combination of three different methods","JournalRef":"Protein Engineering 2, 185-191 (1988)","A":16,"R":-70,"N":-74,"D":-78,"C":168,"E":-106,"Q":-73,"G":-13,"H":50,"I":151,"L":145,"K":-141,"M":124,"F":189,"P":-20,"S":-70,"T":-38,"W":145,"Y":53,"V":123}
{"AccNo":"BIOV880102","PropDesc":"Information value for accessibility; average fraction 23% (Biou et al., 1988)","LITDBNo":"LIT:1413106b PMID:3237683","Author":"Biou, V., Gibrat, J.F., Levin, J.M., Robson, B. and Garnier, J.","ArtTitle":"Secondary structure prediction: combination of three different methods","JournalRef":"Protein Engineering 2, 185-191 (1988)","A":44,"R":-68,"N":-72,"D":-91,"C":90,"E":-139,"Q":-117,"G":-8,"H":47,"I":100,"L":108,"K":-188,"M":121,"F":148,"P":-36,"S":-60,"T":-54,"W":163,"Y":22,"V":117}
{"AccNo":"BROC820101","PropDesc":"Retention coefficient in TFA (Browne et al., 1982)","LITDBNo":"LIT:0809229 PMID:7125223","Author":"Browne, C.A., Bennett, H.P.J. and Solomon, S.","ArtTitle":"The isolation of peptides by high-performance liquid chromatography using predicted elution positions","JournalRef":"Anal. Biochem. 124, 201-208 (1982)","A":7.3,"R":-3.6,"N":-5.7,"D":-2.9,"C":-9.2,"E":-7.1,"Q":-0.3,"G":-1.2,"H":-2.1,"I":6.6,"L":20,"K":-3.7,"M":5.6,"F":19.2,"P":5.1,"S":-4.1,"T":0.8,"W":16.3,"Y":5.9,"V":3.5}
{"AccNo":"BROC820102","PropDesc":"Retention coefficient in HFBA (Browne et al., 1982)","LITDBNo":"LIT:0809229 PMID:7125223","Author":"Browne, C.A., Bennett, H.P.J. and Solomon, S.","ArtTitle":"The isolation of peptides by high-performance liquid chromatography using predicted elution positions","JournalRef":"Anal. Biochem. 124, 201-208 (1982)","A":3.9,"R":3.2,"N":-2.8,"D":-2.8,"C":-14.3,"E":-7.5,"Q":1.8,"G":-2.3,"H":2,"I":11,"L":15,"K":-2.5,"M":4.1,"F":14.7,"P":5.6,"S":-3.5,"T":1.1,"W":17.8,"Y":3.8,"V":2.1}
{"AccNo":"BULH740101","PropDesc":"Transfer free energy to surface (Bull-Breese, 1974)","LITDBNo":"PMID:4839053","Author":"Bull, H.B. and Breese, K.","ArtTitle":"Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues","JournalRef":"Arch. Biochem. Biophys. 161, 665-670 (1974)","A":-0.2,"R":-0.12,"N":0.08,"D":-0.2,"C":-0.45,"E":-0.3,"Q":0.16,"G":0,"H":-0.12,"I":-2.26,"L":-2.46,"K":-0.35,"M":-1.47,"F":-2.33,"P":-0.98,"S":-0.39,"T":-0.52,"W":-2.01,"Y":-2.24,"V":-1.56}
{"AccNo":"BULH740102","PropDesc":"Apparent partial specific volume (Bull-Breese, 1974)","LITDBNo":"PMID:4839053","Author":"Bull, H.B. and Breese, K.","ArtTitle":"Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues","JournalRef":"Arch. Biochem. Biophys. 161, 665-670 (1974) (Tyr !)","A":0.691,"R":0.728,"N":0.596,"D":0.558,"C":0.624,"E":0.632,"Q":0.649,"G":0.592,"H":0.646,"I":0.809,"L":0.842,"K":0.767,"M":0.709,"F":0.756,"P":0.73,"S":0.594,"T":0.655,"W":0.743,"Y":0.743,"V":0.777}
{"AccNo":"BUNA790101","PropDesc":"alpha-NH chemical shifts (Bundi-Wuthrich, 1979)","LITDBNo":"LIT:0503064b","Author":"Bundi, A. and Wuthrich, K.","ArtTitle":"1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH","JournalRef":"Biopolymers 18, 285-297 (1979) (Pro !)","A":8.249,"R":8.274,"N":8.747,"D":8.41,"C":8.312,"E":8.368,"Q":8.411,"G":8.391,"H":8.415,"I":8.195,"L":8.423,"K":8.408,"M":8.418,"F":8.228,"P":0,"S":8.38,"T":8.236,"W":8.094,"Y":8.183,"V":8.436}
{"AccNo":"BUNA790102","PropDesc":"alpha-CH chemical shifts (Bundi-Wuthrich, 1979)","LITDBNo":"LIT:0503064b","Author":"Bundi, A. and Wuthrich, K.","ArtTitle":"1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH","JournalRef":"Biopolymers 18, 285-297 (1979)","A":4.349,"R":4.396,"N":4.755,"D":4.765,"C":4.686,"E":4.295,"Q":4.373,"G":3.972,"H":4.63,"I":4.224,"L":4.385,"K":4.358,"M":4.513,"F":4.663,"P":4.471,"S":4.498,"T":4.346,"W":4.702,"Y":4.604,"V":4.184}
{"AccNo":"BUNA790103","PropDesc":"Spin-spin coupling constants 3JHalpha-NH (Bundi-Wuthrich, 1979)","LITDBNo":"LIT:0503064b","Author":"Bundi, A. and Wuthrich, K.","ArtTitle":"1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH","JournalRef":"Biopolymers 18, 285-297 (1979) (Met Pro Trp !)","A":6.5,"R":6.9,"N":7.5,"D":7,"C":7.7,"E":7,"Q":6,"G":5.6,"H":8,"I":7,"L":6.5,"K":6.5,"M":0,"F":9.4,"P":0,"S":6.5,"T":6.9,"W":0,"Y":6.8,"V":7}
{"AccNo":"BURA740101","PropDesc":"Normalized frequency of alpha-helix (Burgess et al., 1974)","LITDBNo":"LIT:2004075b","Author":"Burgess, A.W., Ponnuswamy, P.K. and Scheraga, H.A.","ArtTitle":"Analysis of conformations of amino acid residues and prediction of backbone topography in proteins","JournalRef":"Isr. J. Chem. 12, 239-286 (1974)","A":0.486,"R":0.262,"N":0.193,"D":0.288,"C":0.2,"E":0.538,"Q":0.418,"G":0.12,"H":0.4,"I":0.37,"L":0.42,"K":0.402,"M":0.417,"F":0.318,"P":0.208,"S":0.2,"T":0.272,"W":0.462,"Y":0.161,"V":0.379}
{"AccNo":"BURA740102","PropDesc":"Normalized frequency of extended structure (Burgess et al., 1974)","LITDBNo":"LIT:2004075b","Author":"Burgess, A.W., Ponnuswamy, P.K. and Scheraga, H.A.","ArtTitle":"Analysis of conformations of amino acid residues and prediction of backbone topography in proteins","JournalRef":"Isr. J. Chem. 12, 239-286 (1974)","A":0.288,"R":0.362,"N":0.229,"D":0.271,"C":0.533,"E":0.262,"Q":0.327,"G":0.312,"H":0.2,"I":0.411,"L":0.4,"K":0.265,"M":0.375,"F":0.318,"P":0.34,"S":0.354,"T":0.388,"W":0.231,"Y":0.429,"V":0.495}
{"AccNo":"CHAM810101","PropDesc":"Steric parameter (Charton, 1981)","LITDBNo":"LIT:2004112b PMID:7300379","Author":"Charton, M.","ArtTitle":"Protein folding and the genetic code: An alternative quantitative model","JournalRef":"J. Theor. Biol. 91, 115-123 (1981) (Pro !)","A":0.52,"R":0.68,"N":0.76,"D":0.76,"C":0.62,"E":0.68,"Q":0.68,"G":0,"H":0.7,"I":1.02,"L":0.98,"K":0.68,"M":0.78,"F":0.7,"P":0.36,"S":0.53,"T":0.5,"W":0.7,"Y":0.7,"V":0.76}
{"AccNo":"CHAM820101","PropDesc":"Polarizability parameter (Charton-Charton, 1982)","LITDBNo":"LIT:0902079b PMID:7183857","Author":"Charton, M. and Charton, B.I.","ArtTitle":"The structural dependence of amino acid hydrophobicity parameters","JournalRef":"J. Theor. Biol. 99, 629-644 (1982) (Pro 0.018)","A":0.046,"R":0.291,"N":0.134,"D":0.105,"C":0.128,"E":0.151,"Q":0.18,"G":0,"H":0.23,"I":0.186,"L":0.186,"K":0.219,"M":0.221,"F":0.29,"P":0.131,"S":0.062,"T":0.108,"W":0.409,"Y":0.298,"V":0.14}
{"AccNo":"CHAM820102","PropDesc":"Free energy of solution in water, kcal/mole (Charton-Charton, 1982)","LITDBNo":"LIT:0902079b PMID:7183857","Author":"Charton, M. and Charton, B.I.","ArtTitle":"The structural dependence of amino acid hydrophobicity parameters","JournalRef":"J. Theor. Biol. 99, 629-644 (1982) (Asn His Lys Thr !)","A":-0.368,"R":-1.03,"N":0,"D":2.06,"C":4.53,"E":1.77,"Q":0.731,"G":-0.525,"H":0,"I":0.791,"L":1.07,"K":0,"M":0.656,"F":1.06,"P":-2.24,"S":-0.524,"T":0,"W":1.6,"Y":4.91,"V":0.401}
{"AccNo":"CHAM830101","PropDesc":"The Chou-Fasman parameter of the coil conformation (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983)","A":0.71,"R":1.06,"N":1.37,"D":1.21,"C":1.19,"E":0.84,"Q":0.87,"G":1.52,"H":1.07,"I":0.66,"L":0.69,"K":0.99,"M":0.59,"F":0.71,"P":1.61,"S":1.34,"T":1.08,"W":0.76,"Y":1.07,"V":0.63}
{"AccNo":"CHAM830102","PropDesc":"A parameter defined from the residuals obtained from the best correlation of the Chou-Fasman parameter of beta-sheet (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":-0.118,"R":0.124,"N":0.289,"D":0.048,"C":0.083,"E":-0.245,"Q":-0.105,"G":0.104,"H":0.138,"I":0.23,"L":-0.052,"K":0.032,"M":-0.258,"F":0.015,"P":0,"S":0.225,"T":0.166,"W":0.158,"Y":0.094,"V":0.513}
{"AccNo":"CHAM830103","PropDesc":"The number of atoms in the side chain labelled 1+1 (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":0,"R":1,"N":1,"D":1,"C":1,"E":1,"Q":1,"G":0,"H":1,"I":2,"L":1,"K":1,"M":1,"F":1,"P":0,"S":1,"T":2,"W":1,"Y":1,"V":2}
{"AccNo":"CHAM830104","PropDesc":"The number of atoms in the side chain labelled 2+1 (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":0,"R":1,"N":1,"D":1,"C":0,"E":1,"Q":1,"G":0,"H":1,"I":1,"L":2,"K":1,"M":1,"F":1,"P":0,"S":0,"T":0,"W":1,"Y":1,"V":0}
{"AccNo":"CHAM830105","PropDesc":"The number of atoms in the side chain labelled 3+1 (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":0,"R":1,"N":0,"D":0,"C":0,"E":1,"Q":1,"G":0,"H":1,"I":0,"L":0,"K":1,"M":1,"F":1,"P":0,"S":0,"T":0,"W":1.5,"Y":1,"V":0}
{"AccNo":"CHAM830106","PropDesc":"The number of bonds in the longest chain (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":0,"R":5,"N":2,"D":2,"C":1,"E":3,"Q":3,"G":0,"H":3,"I":2,"L":2,"K":4,"M":3,"F":4,"P":0,"S":1,"T":1,"W":5,"Y":5,"V":1}
{"AccNo":"CHAM830107","PropDesc":"A parameter of charge transfer capability (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":0,"R":0,"N":1,"D":1,"C":0,"E":1,"Q":0,"G":1,"H":0,"I":0,"L":0,"K":0,"M":0,"F":0,"P":0,"S":0,"T":0,"W":0,"Y":0,"V":0}
{"AccNo":"CHAM830108","PropDesc":"A parameter of charge transfer donor capability (Charton-Charton, 1983)","LITDBNo":"LIT:0907093b PMID:6876837","Author":"Charton, M. and Charton, B.","ArtTitle":"The dependence of the Chou-Fasman parameters on amino acid side chain structure","JournalRef":"J. Theor. Biol. 111, 447-450 (1983) (Pro !)","A":0,"R":1,"N":1,"D":0,"C":1,"E":0,"Q":1,"G":0,"H":1,"I":0,"L":0,"K":1,"M":1,"F":1,"P":0,"S":0,"T":0,"W":1,"Y":1,"V":0}
{"AccNo":"CHOC750101","PropDesc":"Average volume of buried residue (Chothia, 1975)","LITDBNo":"PMID:1118010","Author":"Chothia, C.","ArtTitle":"Structural invariants in protein folding","JournalRef":"Nature 254, 304-308 (1975) (Arg missing)","A":91.5,"R":202,"N":135.2,"D":124.5,"C":117.7,"E":155.1,"Q":161.1,"G":66.4,"H":167.3,"I":168.8,"L":167.9,"K":171.3,"M":170.8,"F":203.4,"P":129.3,"S":99.1,"T":122.1,"W":237.6,"Y":203.6,"V":141.7}
{"AccNo":"CHOC760101","PropDesc":"Residue accessible surface area in tripeptide (Chothia, 1976)","LITDBNo":"LIT:2004094b PMID:994183","Author":"Chothia, C.","ArtTitle":"The nature of the accessible and buried surfaces in proteins","JournalRef":"J. Mol. Biol. 105, 1-14 (1976)","A":115,"R":225,"N":160,"D":150,"C":135,"E":190,"Q":180,"G":75,"H":195,"I":175,"L":170,"K":200,"M":185,"F":210,"P":145,"S":115,"T":140,"W":255,"Y":230,"V":155}
{"AccNo":"CHOC760102","PropDesc":"Residue accessible surface area in folded protein (Chothia, 1976)","LITDBNo":"LIT:2004094b PMID:994183","Author":"Chothia, C.","ArtTitle":"The nature of the accessible and buried surfaces in proteins","JournalRef":"J. Mol. Biol. 105, 1-14 (1976)","A":25,"R":90,"N":63,"D":50,"C":19,"E":49,"Q":71,"G":23,"H":43,"I":18,"L":23,"K":97,"M":31,"F":24,"P":50,"S":44,"T":47,"W":32,"Y":60,"V":18}
{"AccNo":"CHOC760103","PropDesc":"Proportion of residues 95% buried (Chothia, 1976)","LITDBNo":"LIT:2004094b PMID:994183","Author":"Chothia, C.","ArtTitle":"The nature of the accessible and buried surfaces in proteins","JournalRef":"J. Mol. Biol. 105, 1-14 (1976)","A":0.38,"R":0.01,"N":0.12,"D":0.15,"C":0.45,"E":0.18,"Q":0.07,"G":0.36,"H":0.17,"I":0.6,"L":0.45,"K":0.03,"M":0.4,"F":0.5,"P":0.18,"S":0.22,"T":0.23,"W":0.27,"Y":0.15,"V":0.54}
{"AccNo":"CHOC760104","PropDesc":"Proportion of residues 100% buried (Chothia, 1976)","LITDBNo":"LIT:2004094b PMID:994183","Author":"Chothia, C.","ArtTitle":"The nature of the accessible and buried surfaces in proteins","JournalRef":"J. Mol. Biol. 105, 1-14 (1976) (normalized by the total number)","A":0.2,"R":0,"N":0.03,"D":0.04,"C":0.22,"E":0.03,"Q":0.01,"G":0.18,"H":0.02,"I":0.19,"L":0.16,"K":0,"M":0.11,"F":0.14,"P":0.04,"S":0.08,"T":0.08,"W":0.04,"Y":0.03,"V":0.18}
{"AccNo":"CHOP780101","PropDesc":"Normalized frequency of beta-turn (Chou-Fasman, 1978a)","LITDBNo":"LIT:2004003a PMID:354496","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Empirical predictions of protein conformation","JournalRef":"Ann. Rev. Biochem. 47, 251-276 (1978)","A":0.66,"R":0.95,"N":1.56,"D":1.46,"C":1.19,"E":0.74,"Q":0.98,"G":1.56,"H":0.95,"I":0.47,"L":0.59,"K":1.01,"M":0.6,"F":0.6,"P":1.52,"S":1.43,"T":0.96,"W":0.96,"Y":1.14,"V":0.5}
{"AccNo":"CHOP780201","PropDesc":"Normalized frequency of alpha-helix (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":1.42,"R":0.98,"N":0.67,"D":1.01,"C":0.7,"E":1.51,"Q":1.11,"G":0.57,"H":1,"I":1.08,"L":1.21,"K":1.16,"M":1.45,"F":1.13,"P":0.57,"S":0.77,"T":0.83,"W":1.08,"Y":0.69,"V":1.06}
{"AccNo":"CHOP780202","PropDesc":"Normalized frequency of beta-sheet (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.83,"R":0.93,"N":0.89,"D":0.54,"C":1.19,"E":0.37,"Q":1.1,"G":0.75,"H":0.87,"I":1.6,"L":1.3,"K":0.74,"M":1.05,"F":1.38,"P":0.55,"S":0.75,"T":1.19,"W":1.37,"Y":1.47,"V":1.7}
{"AccNo":"CHOP780203","PropDesc":"Normalized frequency of beta-turn (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.74,"R":1.01,"N":1.46,"D":1.52,"C":0.96,"E":0.95,"Q":0.96,"G":1.56,"H":0.95,"I":0.47,"L":0.5,"K":1.19,"M":0.6,"F":0.66,"P":1.56,"S":1.43,"T":0.98,"W":0.6,"Y":1.14,"V":0.59}
{"AccNo":"CHOP780204","PropDesc":"Normalized frequency of N-terminal helix (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":1.29,"R":0.44,"N":0.81,"D":2.02,"C":0.66,"E":2.44,"Q":1.22,"G":0.76,"H":0.73,"I":0.67,"L":0.58,"K":0.66,"M":0.71,"F":0.61,"P":2.01,"S":0.74,"T":1.08,"W":1.47,"Y":0.68,"V":0.61}
{"AccNo":"CHOP780205","PropDesc":"Normalized frequency of C-terminal helix (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":1.2,"R":1.25,"N":0.59,"D":0.61,"C":1.11,"E":1.24,"Q":1.22,"G":0.42,"H":1.77,"I":0.98,"L":1.13,"K":1.83,"M":1.57,"F":1.1,"P":0,"S":0.96,"T":0.75,"W":0.4,"Y":0.73,"V":1.25}
{"AccNo":"CHOP780206","PropDesc":"Normalized frequency of N-terminal non helical region (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.7,"R":0.34,"N":1.42,"D":0.98,"C":0.65,"E":1.04,"Q":0.75,"G":1.41,"H":1.22,"I":0.78,"L":0.85,"K":1.01,"M":0.83,"F":0.93,"P":1.1,"S":1.55,"T":1.09,"W":0.62,"Y":0.99,"V":0.75}
{"AccNo":"CHOP780207","PropDesc":"Normalized frequency of C-terminal non helical region (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.52,"R":1.24,"N":1.64,"D":1.06,"C":0.94,"E":0.59,"Q":0.7,"G":1.64,"H":1.86,"I":0.87,"L":0.84,"K":1.49,"M":0.52,"F":1.04,"P":1.58,"S":0.93,"T":0.86,"W":0.16,"Y":0.96,"V":0.32}
{"AccNo":"CHOP780208","PropDesc":"Normalized frequency of N-terminal beta-sheet (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.86,"R":0.9,"N":0.66,"D":0.38,"C":0.87,"E":0.35,"Q":1.65,"G":0.63,"H":0.54,"I":1.94,"L":1.3,"K":1,"M":1.43,"F":1.5,"P":0.66,"S":0.63,"T":1.17,"W":1.49,"Y":1.07,"V":1.69}
{"AccNo":"CHOP780209","PropDesc":"Normalized frequency of C-terminal beta-sheet (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.75,"R":0.9,"N":1.21,"D":0.85,"C":1.11,"E":0.55,"Q":0.65,"G":0.74,"H":0.9,"I":1.35,"L":1.27,"K":0.74,"M":0.95,"F":1.5,"P":0.4,"S":0.79,"T":0.75,"W":1.19,"Y":1.96,"V":1.79}
{"AccNo":"CHOP780210","PropDesc":"Normalized frequency of N-terminal non beta region (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.67,"R":0.89,"N":1.86,"D":1.39,"C":1.34,"E":0.92,"Q":1.09,"G":1.46,"H":0.78,"I":0.59,"L":0.46,"K":1.09,"M":0.52,"F":0.3,"P":1.58,"S":1.41,"T":1.09,"W":0.48,"Y":1.23,"V":0.42}
{"AccNo":"CHOP780211","PropDesc":"Normalized frequency of C-terminal non beta region (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.74,"R":1.05,"N":1.13,"D":1.32,"C":0.53,"E":0.85,"Q":0.77,"G":1.68,"H":0.96,"I":0.53,"L":0.59,"K":0.82,"M":0.85,"F":0.44,"P":1.69,"S":1.49,"T":1.16,"W":1.59,"Y":1.01,"V":0.59}
{"AccNo":"CHOP780212","PropDesc":"Frequency of the 1st residue in turn (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.06,"R":0.07,"N":0.161,"D":0.147,"C":0.149,"E":0.056,"Q":0.074,"G":0.102,"H":0.14,"I":0.043,"L":0.061,"K":0.055,"M":0.068,"F":0.059,"P":0.102,"S":0.12,"T":0.086,"W":0.077,"Y":0.082,"V":0.062}
{"AccNo":"CHOP780213","PropDesc":"Frequency of the 2nd residue in turn (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.076,"R":0.106,"N":0.083,"D":0.11,"C":0.053,"E":0.06,"Q":0.098,"G":0.085,"H":0.047,"I":0.034,"L":0.025,"K":0.115,"M":0.082,"F":0.041,"P":0.301,"S":0.139,"T":0.108,"W":0.013,"Y":0.065,"V":0.048}
{"AccNo":"CHOP780214","PropDesc":"Frequency of the 3rd residue in turn (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.035,"R":0.099,"N":0.191,"D":0.179,"C":0.117,"E":0.077,"Q":0.037,"G":0.19,"H":0.093,"I":0.013,"L":0.036,"K":0.072,"M":0.014,"F":0.065,"P":0.034,"S":0.125,"T":0.065,"W":0.064,"Y":0.114,"V":0.028}
{"AccNo":"CHOP780215","PropDesc":"Frequency of the 4th residue in turn (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.058,"R":0.085,"N":0.091,"D":0.081,"C":0.128,"E":0.064,"Q":0.098,"G":0.152,"H":0.054,"I":0.056,"L":0.07,"K":0.095,"M":0.055,"F":0.065,"P":0.068,"S":0.106,"T":0.079,"W":0.167,"Y":0.125,"V":0.053}
{"AccNo":"CHOP780216","PropDesc":"Normalized frequency of the 2nd and 3rd residues in turn (Chou-Fasman, 1978b)","LITDBNo":"PMID:364941","Author":"Chou, P.Y. and Fasman, G.D.","ArtTitle":"Prediction of the secondary structure of proteins from their amino acid sequence","JournalRef":"Adv. Enzymol. 47, 45-148 (1978)","A":0.64,"R":1.05,"N":1.56,"D":1.61,"C":0.92,"E":0.8,"Q":0.84,"G":1.63,"H":0.77,"I":0.29,"L":0.36,"K":1.13,"M":0.51,"F":0.62,"P":2.04,"S":1.52,"T":0.98,"W":0.48,"Y":1.08,"V":0.43}
{"AccNo":"CIDH920101","PropDesc":"Normalized hydrophobicity scales for alpha-proteins (Cid et al., 1992)","LITDBNo":"LIT:1817105b PMID:1518784","Author":"Cid, H., Bunster, M., Canales, M. and Gazitua, F.","ArtTitle":"Hydrophobicity and structural classes in proteins","JournalRef":"Protein Engineering 5, 373-375 (1992)","A":-0.45,"R":-0.24,"N":-0.2,"D":-1.52,"C":0.79,"E":-0.8,"Q":-0.99,"G":-1,"H":1.07,"I":0.76,"L":1.29,"K":-0.36,"M":1.37,"F":1.48,"P":-0.12,"S":-0.98,"T":-0.7,"W":1.38,"Y":1.49,"V":1.26}
{"AccNo":"CIDH920102","PropDesc":"Normalized hydrophobicity scales for beta-proteins (Cid et al., 1992)","LITDBNo":"LIT:1817105b PMID:1518784","Author":"Cid, H., Bunster, M., Canales, M. and Gazitua, F.","ArtTitle":"Hydrophobicity and structural classes in proteins","JournalRef":"Protein Engineering 5, 373-375 (1992)","A":-0.08,"R":-0.09,"N":-0.7,"D":-0.71,"C":0.76,"E":-1.31,"Q":-0.4,"G":-0.84,"H":0.43,"I":1.39,"L":1.24,"K":-0.09,"M":1.27,"F":1.53,"P":-0.01,"S":-0.93,"T":-0.59,"W":2.25,"Y":1.53,"V":1.09}
{"AccNo":"CIDH920103","PropDesc":"Normalized hydrophobicity scales for alpha+beta-proteins (Cid et al., 1992)","LITDBNo":"LIT:1817105b PMID:1518784","Author":"Cid, H., Bunster, M., Canales, M. and Gazitua, F.","ArtTitle":"Hydrophobicity and structural classes in proteins","JournalRef":"Protein Engineering 5, 373-375 (1992)","A":0.36,"R":-0.52,"N":-0.9,"D":-1.09,"C":0.7,"E":-0.83,"Q":-1.05,"G":-0.82,"H":0.16,"I":2.17,"L":1.18,"K":-0.56,"M":1.21,"F":1.01,"P":-0.06,"S":-0.6,"T":-1.2,"W":1.31,"Y":1.05,"V":1.21}
{"AccNo":"CIDH920104","PropDesc":"Normalized hydrophobicity scales for alpha/beta-proteins (Cid et al., 1992)","LITDBNo":"LIT:1817105b PMID:1518784","Author":"Cid, H., Bunster, M., Canales, M. and Gazitua, F.","ArtTitle":"Hydrophobicity and structural classes in proteins","JournalRef":"Protein Engineering 5, 373-375 (1992)","A":0.17,"R":-0.7,"N":-0.9,"D":-1.05,"C":1.24,"E":-1.19,"Q":-1.2,"G":-0.57,"H":-0.25,"I":2.06,"L":0.96,"K":-0.62,"M":0.6,"F":1.29,"P":-0.21,"S":-0.83,"T":-0.62,"W":1.51,"Y":0.66,"V":1.21}
{"AccNo":"CIDH920105","PropDesc":"Normalized average hydrophobicity scales (Cid et al., 1992)","LITDBNo":"LIT:1817105b PMID:1518784","Author":"Cid, H., Bunster, M., Canales, M. and Gazitua, F.","ArtTitle":"Hydrophobicity and structural classes in proteins","JournalRef":"Protein Engineering 5, 373-375 (1992)","A":0.02,"R":-0.42,"N":-0.77,"D":-1.04,"C":0.77,"E":-1.14,"Q":-1.1,"G":-0.8,"H":0.26,"I":1.81,"L":1.14,"K":-0.41,"M":1,"F":1.35,"P":-0.09,"S":-0.97,"T":-0.77,"W":1.71,"Y":1.11,"V":1.13}
{"AccNo":"COHE430101","PropDesc":"Partial specific volume (Cohn-Edsall, 1943)","Author":"Cohn, E.J. and Edsall, J.T.","JournalRef":"\"Protein, Amino Acid, and Peptides\", Reinhold, New York (1943)","A":0.75,"R":0.7,"N":0.61,"D":0.6,"C":0.61,"E":0.66,"Q":0.67,"G":0.64,"H":0.67,"I":0.9,"L":0.9,"K":0.82,"M":0.75,"F":0.77,"P":0.76,"S":0.68,"T":0.7,"W":0.74,"Y":0.71,"V":0.86}
{"AccNo":"CRAJ730101","PropDesc":"Normalized frequency of middle helix (Crawford et al., 1973)","LITDBNo":"PMID:4510294","Author":"Crawford, J.L., Lipscomb, W.N. and Schellman, C.G.","ArtTitle":"The reverse turn as a polypeptide conformation in globular proteins","JournalRef":"Proc. Natl. Acad. Sci. USA 70, 538-542 (1973) Reported values normalized by the total percentage","A":1.33,"R":0.79,"N":0.72,"D":0.97,"C":0.93,"E":1.66,"Q":1.42,"G":0.58,"H":1.49,"I":0.99,"L":1.29,"K":1.03,"M":1.4,"F":1.15,"P":0.49,"S":0.83,"T":0.94,"W":1.33,"Y":0.49,"V":0.96}
{"AccNo":"CRAJ730102","PropDesc":"Normalized frequency of beta-sheet (Crawford et al., 1973)","LITDBNo":"PMID:4510294","Author":"Crawford, J.L., Lipscomb, W.N. and Schellman, C.G.","ArtTitle":"The reverse turn as a polypeptide conformation in globular proteins","JournalRef":"Proc. Natl. Acad. Sci. USA 70, 538-542 (1973) Reported values normalized by the total percentage","A":1,"R":0.74,"N":0.75,"D":0.89,"C":0.99,"E":0.37,"Q":0.87,"G":0.56,"H":0.36,"I":1.75,"L":1.53,"K":1.18,"M":1.4,"F":1.26,"P":0.36,"S":0.65,"T":1.15,"W":0.84,"Y":1.41,"V":1.61}
{"AccNo":"CRAJ730103","PropDesc":"Normalized frequency of turn (Crawford et al., 1973)","LITDBNo":"PMID:4510294","Author":"Crawford, J.L., Lipscomb, W.N. and Schellman, C.G.","ArtTitle":"The reverse turn as a polypeptide conformation in globular proteins","JournalRef":"Proc. Natl. Acad. Sci. USA 70, 538-542 (1973) Reported values normalized by the total percentage","A":0.6,"R":0.79,"N":1.42,"D":1.24,"C":1.29,"E":0.64,"Q":0.92,"G":1.38,"H":0.95,"I":0.67,"L":0.7,"K":1.1,"M":0.67,"F":1.05,"P":1.47,"S":1.26,"T":1.05,"W":1.23,"Y":1.35,"V":0.48}
{"AccNo":"DAWD720101","PropDesc":"Size (Dawson, 1972)","Author":"Dawson, D.M.","JournalRef":"In \"The Biochemical Genetics of Man\" (Brock, D.J.H. and Mayo, O., eds.), Academic Press, New York, pp.1-38 (1972)","A":2.5,"R":7.5,"N":5,"D":2.5,"C":3,"E":5,"Q":6,"G":0.5,"H":6,"I":5.5,"L":5.5,"K":7,"M":6,"F":6.5,"P":5.5,"S":3,"T":5,"W":7,"Y":7,"V":5}
{"AccNo":"DAYM780101","PropDesc":"Amino acid composition (Dayhoff et al., 1978a)","Author":"Dayhoff, M.O., Hunt, L.T. and Hurst-Calderone, S.","ArtTitle":"Composition of proteins","JournalRef":"In \"Atlas of Protein Sequence and Structure\", Vol.5, Suppl.3 (Dayhoff, M.O., ed.), National Biomedical Research Foundation, Washington, D.C., p.363 (1978)","A":8.6,"R":4.9,"N":4.3,"D":5.5,"C":2.9,"E":6,"Q":3.9,"G":8.4,"H":2,"I":4.5,"L":7.4,"K":6.6,"M":1.7,"F":3.6,"P":5.2,"S":7,"T":6.1,"W":1.3,"Y":3.4,"V":6.6}
{"AccNo":"DAYM780201","PropDesc":"Relative mutability (Dayhoff et al., 1978b)","Author":"Dayhoff, M.O., Schwartz, R.M. and Orcutt, B.C.","ArtTitle":"A model of evolutionary change in proteins","JournalRef":"In \"Atlas of Protein Sequence and Structure\", Vol.5, Suppl.3 (Dayhoff, M.O., ed.), National Biomedical Research Foundation, Washington, D.C. pp. 345-352 (1978)","A":100,"R":65,"N":134,"D":106,"C":20,"E":102,"Q":93,"G":49,"H":66,"I":96,"L":40,"K":56,"M":94,"F":41,"P":56,"S":120,"T":97,"W":18,"Y":41,"V":74}
{"AccNo":"DESM900101","PropDesc":"Membrane preference for cytochrome b: MPH89 (Degli Esposti et al., 1990)","LITDBNo":"LIT:1612111b PMID:2364947","Author":"Degli Esposti, M., Crimi, M. and Venturoli, G.","ArtTitle":"A critical evaluation of the hydropathy profile of membrane proteins","JournalRef":"Eur. J. Biochem. 190, 207-219 (1990)","A":1.56,"R":0.59,"N":0.51,"D":0.23,"C":1.8,"E":0.19,"Q":0.39,"G":1.03,"H":1,"I":1.27,"L":1.38,"K":0.15,"M":1.93,"F":1.42,"P":0.27,"S":0.96,"T":1.11,"W":0.91,"Y":1.1,"V":1.58}
{"AccNo":"DESM900102","PropDesc":"Average membrane preference: AMP07 (Degli Esposti et al., 1990)","LITDBNo":"LIT:1612111b PMID:2364947","Author":"Degli Esposti, M., Crimi, M. and Venturoli, G.","ArtTitle":"A critical evaluation of the hydropathy profile of membrane proteins","JournalRef":"Eur. J. Biochem. 190, 207-219 (1990)","A":1.26,"R":0.38,"N":0.59,"D":0.27,"C":1.6,"E":0.23,"Q":0.39,"G":1.08,"H":1,"I":1.44,"L":1.36,"K":0.33,"M":1.52,"F":1.46,"P":0.54,"S":0.98,"T":1.01,"W":1.06,"Y":0.89,"V":1.33}
{"AccNo":"EISD840101","PropDesc":"Consensus normalized hydrophobicity scale (Eisenberg, 1984)","LITDBNo":"LIT:2004004a PMID:6383201","Author":"Eisenberg, D.","ArtTitle":"Three-dimensional structure of membrane and surface proteins","JournalRef":"Ann. Rev. Biochem. 53, 595-623 (1984) Original references: Eisenberg, D., Weiss, R.M., Terwilliger, T.C. and Wilcox, W. Faraday Symp. Chem. Soc. 17, 109-120 (1982) Eisenberg, D., Weiss, R.M. and Terwilliger, T.C. The hydrophobic moment detects periodicity in protein hydrophobicity Proc. Natl. Acad. Sci. USA 81, 140-144 (1984)","A":0.25,"R":-1.76,"N":-0.64,"D":-0.72,"C":0.04,"E":-0.62,"Q":-0.69,"G":0.16,"H":-0.4,"I":0.73,"L":0.53,"K":-1.1,"M":0.26,"F":0.61,"P":-0.07,"S":-0.26,"T":-0.18,"W":0.37,"Y":0.02,"V":0.54}
{"AccNo":"EISD860101","PropDesc":"Solvation free energy (Eisenberg-McLachlan, 1986)","LITDBNo":"LIT:2004121b PMID: 3945310","Author":"Eisenberg, D. and McLachlan, A.D.","ArtTitle":"Solvation energy in protein folding and binding","JournalRef":"Nature 319, 199-203 (1986)","A":0.67,"R":-2.1,"N":-0.6,"D":-1.2,"C":0.38,"E":-0.76,"Q":-0.22,"G":0,"H":0.64,"I":1.9,"L":1.9,"K":-0.57,"M":2.4,"F":2.3,"P":1.2,"S":0.01,"T":0.52,"W":2.6,"Y":1.6,"V":1.5}
{"AccNo":"EISD860102","PropDesc":"Atom-based hydrophobic moment (Eisenberg-McLachlan, 1986)","LITDBNo":"LIT:2004121b PMID: 3945310","Author":"Eisenberg, D. and McLachlan, A.D.","ArtTitle":"Solvation energy in protein folding and binding","JournalRef":"Nature 319, 199-203 (1986)","A":0,"R":10,"N":1.3,"D":1.9,"C":0.17,"E":3,"Q":1.9,"G":0,"H":0.99,"I":1.2,"L":1,"K":5.7,"M":1.9,"F":1.1,"P":0.18,"S":0.73,"T":1.5,"W":1.6,"Y":1.8,"V":0.48}
{"AccNo":"EISD860103","PropDesc":"Direction of hydrophobic moment (Eisenberg-McLachlan, 1986)","LITDBNo":"LIT:2004121b PMID: 3945310","Author":"Eisenberg, D. and McLachlan, A.D.","ArtTitle":"Solvation energy in protein folding and binding","JournalRef":"Nature 319, 199-203 (1986) (Gly Ala missing)","A":0,"R":-0.96,"N":-0.86,"D":-0.98,"C":0.76,"E":-0.89,"Q":-1,"G":0,"H":-0.75,"I":0.99,"L":0.89,"K":-0.99,"M":0.94,"F":0.92,"P":0.22,"S":-0.67,"T":0.09,"W":0.67,"Y":-0.93,"V":0.84}
{"AccNo":"FASG760101","PropDesc":"Molecular weight (Fasman, 1976)","Author":"Fasman, G.D., ed.","JournalRef":"\"Handbook of Biochemistry and Molecular Biology\", 3rd ed., Proteins - Volume 1, CRC Press, Cleveland (1976)","A":89.09,"R":174.2,"N":132.12,"D":133.1,"C":121.15,"E":147.13,"Q":146.15,"G":75.07,"H":155.16,"I":131.17,"L":131.17,"K":146.19,"M":149.21,"F":165.19,"P":115.13,"S":105.09,"T":119.12,"W":204.24,"Y":181.19,"V":117.15}
{"AccNo":"FASG760102","PropDesc":"Melting point (Fasman, 1976)","Author":"Fasman, G.D., ed.","JournalRef":"\"Handbook of Biochemistry and Molecular Biology\", 3rd ed., Proteins - Volume 1, CRC Press, Cleveland (1976)","A":297,"R":238,"N":236,"D":270,"C":178,"E":249,"Q":185,"G":290,"H":277,"I":284,"L":337,"K":224,"M":283,"F":284,"P":222,"S":228,"T":253,"W":282,"Y":344,"V":293}
{"AccNo":"FASG760103","PropDesc":"Optical rotation (Fasman, 1976)","Author":"Fasman, G.D., ed.","JournalRef":"\"Handbook of Biochemistry and Molecular Biology\", 3rd ed., Proteins - Volume 1, CRC Press, Cleveland (1976)","A":1.8,"R":12.5,"N":-5.6,"D":5.05,"C":-16.5,"E":12,"Q":6.3,"G":0,"H":-38.5,"I":12.4,"L":-11,"K":14.6,"M":-10,"F":-34.5,"P":-86.2,"S":-7.5,"T":-28,"W":-33.7,"Y":-10,"V":5.63}
{"AccNo":"FASG760104","PropDesc":"pK-N (Fasman, 1976)","Author":"Fasman, G.D., ed.","JournalRef":"\"Handbook of Biochemistry and Molecular Biology\", 3rd ed., Proteins - Volume 1, CRC Press, Cleveland (1976)","A":9.69,"R":8.99,"N":8.8,"D":9.6,"C":8.35,"E":9.67,"Q":9.13,"G":9.78,"H":9.17,"I":9.68,"L":9.6,"K":9.18,"M":9.21,"F":9.18,"P":10.64,"S":9.21,"T":9.1,"W":9.44,"Y":9.11,"V":9.62}
{"AccNo":"FASG760105","PropDesc":"pK-C (Fasman, 1976)","Author":"Fasman, G.D., ed.","JournalRef":"\"Handbook of Biochemistry and Molecular Biology\", 3rd ed., Proteins - Volume 1, CRC Press, Cleveland (1976)","A":2.34,"R":1.82,"N":2.02,"D":1.88,"C":1.92,"E":2.1,"Q":2.17,"G":2.35,"H":1.82,"I":2.36,"L":2.36,"K":2.16,"M":2.28,"F":2.16,"P":1.95,"S":2.19,"T":2.09,"W":2.43,"Y":2.2,"V":2.32}
{"AccNo":"FAUJ830101","PropDesc":"Hydrophobic parameter pi (Fauchere-Pliska, 1983)","LITDBNo":"LIT:0912085","Author":"Fauchere, J.L. and Pliska, V.","ArtTitle":"Hydrophobic parameters pi of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides","JournalRef":"Eur. J. Med. Chem. 18, 369-375 (1983)","A":0.31,"R":-1.01,"N":-0.6,"D":-0.77,"C":1.54,"E":-0.64,"Q":-0.22,"G":0,"H":0.13,"I":1.8,"L":1.7,"K":-0.99,"M":1.23,"F":1.79,"P":0.72,"S":-0.04,"T":0.26,"W":2.25,"Y":0.96,"V":1.22}
{"AccNo":"FAUJ880101","PropDesc":"Graph shape index (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) Original reference: Kier, L.B. Quant. Struct. Act. Relat. 6, 117-122 (1987)","A":1.28,"R":2.34,"N":1.6,"D":1.6,"C":1.77,"E":1.56,"Q":1.56,"G":0,"H":2.99,"I":4.19,"L":2.59,"K":1.89,"M":2.35,"F":2.94,"P":2.67,"S":1.31,"T":3.03,"W":3.21,"Y":2.94,"V":3.67}
{"AccNo":"FAUJ880102","PropDesc":"Smoothed upsilon steric parameter (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) (Pro missing) Original reference of these two data: Fauchere, L.J. In \"QSAR in Design of Bioactive Compounds\", (Kuchar, M., ed.), Prous, Barcelona pp.135-144 (1984)","A":0.53,"R":0.69,"N":0.58,"D":0.59,"C":0.66,"E":0.72,"Q":0.71,"G":0,"H":0.64,"I":0.96,"L":0.92,"K":0.78,"M":0.77,"F":0.71,"P":0,"S":0.55,"T":0.63,"W":0.84,"Y":0.71,"V":0.89}
{"AccNo":"FAUJ880103","PropDesc":"Normalized van der Waals volume (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) (Pro !) Original reference of these two data: Fauchere, L.J. In \"QSAR in Design of Bioactive Compounds\", (Kuchar, M., ed.), Prous, Barcelona pp.135-144 (1984)","A":1,"R":6.13,"N":2.95,"D":2.78,"C":2.43,"E":3.78,"Q":3.95,"G":0,"H":4.66,"I":4,"L":4,"K":4.77,"M":4.43,"F":5.89,"P":2.72,"S":1.6,"T":2.6,"W":8.08,"Y":6.47,"V":3}
{"AccNo":"FAUJ880104","PropDesc":"STERIMOL length of the side chain (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) (Pro !) Original reference of these three data: Verloop, A. In \"IUPAC, Pesticide Chemistry\", Vol.1 (Miyamoto, J. and Kearney, P.C., eds.),Pergamon, Oxford pp.339-334 (1983)","A":2.87,"R":7.82,"N":4.58,"D":4.74,"C":4.47,"E":5.97,"Q":6.11,"G":2.06,"H":5.23,"I":4.92,"L":4.92,"K":6.89,"M":6.36,"F":4.62,"P":4.11,"S":3.97,"T":4.11,"W":7.68,"Y":4.73,"V":4.11}
{"AccNo":"FAUJ880105","PropDesc":"STERIMOL minimum width of the side chain (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) (Pro !) Original reference of these three data: Verloop, A. In \"IUPAC, Pesticide Chemistry\", Vol.1 (Miyamoto, J. and Kearney, P.C., eds.),Pergamon, Oxford pp.339-334 (1983)","A":1.52,"R":1.52,"N":1.52,"D":1.52,"C":1.52,"E":1.52,"Q":1.52,"G":1,"H":1.52,"I":1.9,"L":1.52,"K":1.52,"M":1.52,"F":1.52,"P":1.52,"S":1.52,"T":1.73,"W":1.52,"Y":1.52,"V":1.9}
{"AccNo":"FAUJ880106","PropDesc":"STERIMOL maximum width of the side chain (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) Original reference of these three data: Verloop, A. In \"IUPAC, Pesticide Chemistry\", Vol.1 (Miyamoto, J. and Kearney, P.C., eds.),Pergamon, Oxford pp.339-334 (1983)","A":2.04,"R":6.24,"N":4.37,"D":3.78,"C":3.41,"E":3.31,"Q":3.53,"G":1,"H":5.66,"I":3.49,"L":4.45,"K":4.87,"M":4.8,"F":6.02,"P":4.31,"S":2.7,"T":3.17,"W":5.9,"Y":6.72,"V":3.17}
{"AccNo":"FAUJ880107","PropDesc":"N.m.r. chemical shift of alpha-carbon (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) Original reference: Fauchere, J.L. and Lauterwein, J. Quant. Struct. Act. Rel. 4, 11-13 (1985)","A":7.3,"R":11.1,"N":8,"D":9.2,"C":14.4,"E":11.4,"Q":10.6,"G":0,"H":10.2,"I":16.1,"L":10.1,"K":10.9,"M":10.4,"F":13.9,"P":17.8,"S":13.1,"T":16.7,"W":13.2,"Y":13.9,"V":17.2}
{"AccNo":"FAUJ880108","PropDesc":"Localized electrical effect (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) (Pro missing) Original reference: Charton, M. and Charton, B.I. J. Theor. Biol. 102, 121-134 (1983)","A":-0.01,"R":0.04,"N":0.06,"D":0.15,"C":0.12,"E":0.07,"Q":0.05,"G":0,"H":0.08,"I":-0.01,"L":-0.01,"K":0,"M":0.04,"F":0.03,"P":0,"S":0.11,"T":0.04,"W":0,"Y":0.03,"V":0.01}
{"AccNo":"FAUJ880109","PropDesc":"Number of hydrogen bond donors (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) Original reference of these two data: IUPAC-IUB Joint Commission on Biochemical Nomenclature Eur. J. Biochem. 138, 9-37 (1984)","A":0,"R":4,"N":2,"D":1,"C":0,"E":1,"Q":2,"G":0,"H":1,"I":0,"L":0,"K":2,"M":0,"F":0,"P":0,"S":1,"T":1,"W":1,"Y":1,"V":0}
{"AccNo":"FAUJ880110","PropDesc":"Number of full nonbonding orbitals (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) Original reference of these two data: IUPAC-IUB Joint Commission on Biochemical Nomenclature Eur. J. Biochem. 138, 9-37 (1984)","A":0,"R":3,"N":3,"D":4,"C":0,"E":4,"Q":3,"G":0,"H":1,"I":0,"L":0,"K":1,"M":0,"F":0,"P":0,"S":2,"T":2,"W":0,"Y":2,"V":0}
{"AccNo":"FAUJ880111","PropDesc":"Positive charge (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988)","A":0,"R":1,"N":0,"D":0,"C":0,"E":0,"Q":0,"G":0,"H":1,"I":0,"L":0,"K":1,"M":0,"F":0,"P":0,"S":0,"T":0,"W":0,"Y":0,"V":0}
{"AccNo":"FAUJ880112","PropDesc":"Negative charge (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988)","A":0,"R":0,"N":0,"D":1,"C":0,"E":1,"Q":0,"G":0,"H":0,"I":0,"L":0,"K":0,"M":0,"F":0,"P":0,"S":0,"T":0,"W":0,"Y":0,"V":0}
{"AccNo":"FAUJ880113","PropDesc":"pK-a(RCOOH) (Fauchere et al., 1988)","LITDBNo":"LIT:1414114 PMID:3209351","Author":"Fauchere, J.L., Charton, M., Kier, L.B., Verloop, A. and Pliska, V.","ArtTitle":"Amino acid side chain parameters for correlation studies in biology and pharmacology","JournalRef":"Int. J. Peptide Protein Res. 32, 269-278 (1988) (Pro missing)","A":4.76,"R":4.3,"N":3.64,"D":5.69,"C":3.67,"E":5.48,"Q":4.54,"G":3.77,"H":2.84,"I":4.81,"L":4.79,"K":4.27,"M":4.25,"F":4.31,"P":0,"S":3.83,"T":3.87,"W":4.75,"Y":4.3,"V":4.86}
{"AccNo":"FINA770101","PropDesc":"Helix-coil equilibrium constant (Finkelstein-Ptitsyn, 1977)","LITDBNo":"LIT:2004052b PMID:843599","Author":"Finkelstein, A.V. and Ptitsyn, O.B.","ArtTitle":"Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments","JournalRef":"Biopolymers 16, 497-524 (1977) (Pro 0.096)","A":1.08,"R":1.05,"N":0.85,"D":0.85,"C":0.95,"E":1.15,"Q":0.95,"G":0.55,"H":1,"I":1.05,"L":1.25,"K":1.15,"M":1.15,"F":1.1,"P":0.71,"S":0.75,"T":0.75,"W":1.1,"Y":1.1,"V":0.95}
{"AccNo":"FINA910101","PropDesc":"Helix initiation parameter at posision i-1 (Finkelstein et al., 1991)","LITDBNo":"LIT:1716158b PMID:1946339","Author":"Finkelstein, A.V., Badretdinov, A.Y. and Ptitsyn, O.B.","ArtTitle":"Physical reasons for secondary structure stability: alpha-helices in short peptides","JournalRef":"Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1.7 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 0.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 )","A":1,"R":0.7,"N":1.7,"D":3.2,"C":1,"E":1.7,"Q":1,"G":1,"H":1,"I":0.6,"L":1,"K":0.7,"M":1,"F":1,"P":1,"S":1.7,"T":1.7,"W":1,"Y":1,"V":0.6}
{"AccNo":"FINA910102","PropDesc":"Helix initiation parameter at posision i,i+1,i+2 (Finkelstein et al., 1991)","LITDBNo":"LIT:1716158b PMID:1946339","Author":"Finkelstein, A.V., Badretdinov, A.Y. and Ptitsyn, O.B.","ArtTitle":"Physical reasons for secondary structure stability: alpha-helices in short peptides","JournalRef":"Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 0.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 ) (Pro !)","A":1,"R":0.7,"N":1,"D":1.7,"C":1,"E":1.7,"Q":1,"G":1.3,"H":1,"I":1,"L":1,"K":0.7,"M":1,"F":1,"P":13,"S":1,"T":1,"W":1,"Y":1,"V":1}
{"AccNo":"FINA910103","PropDesc":"Helix termination parameter at posision j-2,j-1,j (Finkelstein et al., 1991)","LITDBNo":"LIT:1716158b PMID:1946339","Author":"Finkelstein, A.V., Badretdinov, A.Y. and Ptitsyn, O.B.","ArtTitle":"Physical reasons for secondary structure stability: alpha-helices in short peptides","JournalRef":"Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 1.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 )","A":1.2,"R":1.7,"N":1.2,"D":0.7,"C":1,"E":0.7,"Q":1,"G":0.8,"H":1.2,"I":0.8,"L":1,"K":1.7,"M":1,"F":1,"P":1,"S":1.5,"T":1,"W":1,"Y":1,"V":0.8}
{"AccNo":"FINA910104","PropDesc":"Helix termination parameter at posision j+1 (Finkelstein et al., 1991)","LITDBNo":"LIT:1716158b PMID:1946339","Author":"Finkelstein, A.V., Badretdinov, A.Y. and Ptitsyn, O.B.","ArtTitle":"Physical reasons for secondary structure stability: alpha-helices in short peptides","JournalRef":"Proteins 10, 287-299 (1991) In these four data, each of Arg, Asp, Glu, His and Lys has two value. See comment lines. Arg pH < 12 ( 1 when pH > 12 ) Asp pH > 4 ( 1 when pH < 4 ) Glu pH > 4.3 ( 1 when pH < 4.3 ) His pH > 6.3 ( 1.7 when pH < 6.3 ) Lys pH < 10.5 ( 1 when pH > 10.5 )","A":1,"R":1.7,"N":1,"D":0.7,"C":1,"E":0.7,"Q":1,"G":1.5,"H":1,"I":1,"L":1,"K":1.7,"M":1,"F":1,"P":0.1,"S":1,"T":1,"W":1,"Y":1,"V":1}
{"AccNo":"GARJ730101","PropDesc":"Partition coefficient (Garel et al., 1973)","LITDBNo":"LIT:2004092b PMID:4700470","Author":"Garel, J.P., Filliol, D. and Mandel, P.","ArtTitle":"Coefficients de partage d'aminoacides, nucleobases, nucleosides et nucleotides dans un systeme solvant salin","JournalRef":"J. Chromatogr. 78, 381-391 (1973)","A":0.28,"R":0.1,"N":0.25,"D":0.21,"C":0.28,"E":0.33,"Q":0.35,"G":0.17,"H":0.21,"I":0.82,"L":1,"K":0.09,"M":0.74,"F":2.18,"P":0.39,"S":0.12,"T":0.21,"W":5.7,"Y":1.26,"V":0.6}
{"AccNo":"GEIM800101","PropDesc":"Alpha-helix indices (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":1.29,"R":1,"N":0.81,"D":1.1,"C":0.79,"E":1.49,"Q":1.07,"G":0.63,"H":1.33,"I":1.05,"L":1.31,"K":1.33,"M":1.54,"F":1.13,"P":0.63,"S":0.78,"T":0.77,"W":1.18,"Y":0.71,"V":0.81}
{"AccNo":"GEIM800102","PropDesc":"Alpha-helix indices for alpha-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":1.13,"R":1.09,"N":1.06,"D":0.94,"C":1.32,"E":1.2,"Q":0.93,"G":0.83,"H":1.09,"I":1.05,"L":1.13,"K":1.08,"M":1.23,"F":1.01,"P":0.82,"S":1.01,"T":1.17,"W":1.32,"Y":0.88,"V":1.13}
{"AccNo":"GEIM800103","PropDesc":"Alpha-helix indices for beta-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":1.55,"R":0.2,"N":1.2,"D":1.55,"C":1.44,"E":1.67,"Q":1.13,"G":0.59,"H":1.21,"I":1.27,"L":1.25,"K":1.2,"M":1.37,"F":0.4,"P":0.21,"S":1.01,"T":0.55,"W":1.86,"Y":1.08,"V":0.64}
{"AccNo":"GEIM800104","PropDesc":"Alpha-helix indices for alpha/beta-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":1.19,"R":1,"N":0.94,"D":1.07,"C":0.95,"E":1.64,"Q":1.32,"G":0.6,"H":1.03,"I":1.12,"L":1.18,"K":1.27,"M":1.49,"F":1.02,"P":0.68,"S":0.81,"T":0.85,"W":1.18,"Y":0.77,"V":0.74}
{"AccNo":"GEIM800105","PropDesc":"Beta-strand indices (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":0.84,"R":1.04,"N":0.66,"D":0.59,"C":1.27,"E":0.57,"Q":1.02,"G":0.94,"H":0.81,"I":1.29,"L":1.1,"K":0.86,"M":0.88,"F":1.15,"P":0.8,"S":1.05,"T":1.2,"W":1.15,"Y":1.39,"V":1.56}
{"AccNo":"GEIM800106","PropDesc":"Beta-strand indices for beta-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":0.86,"R":1.15,"N":0.6,"D":0.66,"C":0.91,"E":0.37,"Q":1.11,"G":0.86,"H":1.07,"I":1.17,"L":1.28,"K":1.01,"M":1.15,"F":1.34,"P":0.61,"S":0.91,"T":1.14,"W":1.13,"Y":1.37,"V":1.31}
{"AccNo":"GEIM800107","PropDesc":"Beta-strand indices for alpha/beta-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":0.91,"R":0.99,"N":0.72,"D":0.74,"C":1.12,"E":0.41,"Q":0.9,"G":0.91,"H":1.01,"I":1.29,"L":1.23,"K":0.86,"M":0.96,"F":1.26,"P":0.65,"S":0.93,"T":1.05,"W":1.15,"Y":1.21,"V":1.58}
{"AccNo":"GEIM800108","PropDesc":"Aperiodic indices (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":0.91,"R":1,"N":1.64,"D":1.4,"C":0.93,"E":0.97,"Q":0.94,"G":1.51,"H":0.9,"I":0.65,"L":0.59,"K":0.82,"M":0.58,"F":0.72,"P":1.66,"S":1.23,"T":1.04,"W":0.67,"Y":0.92,"V":0.6}
{"AccNo":"GEIM800109","PropDesc":"Aperiodic indices for alpha-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":0.8,"R":0.96,"N":1.1,"D":1.6,"C":0,"E":0.4,"Q":1.6,"G":2,"H":0.96,"I":0.85,"L":0.8,"K":0.94,"M":0.39,"F":1.2,"P":2.1,"S":1.3,"T":0.6,"W":0,"Y":1.8,"V":0.8}
{"AccNo":"GEIM800110","PropDesc":"Aperiodic indices for beta-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":1.1,"R":0.93,"N":1.57,"D":1.41,"C":1.05,"E":1.4,"Q":0.81,"G":1.3,"H":0.85,"I":0.67,"L":0.52,"K":0.94,"M":0.69,"F":0.6,"P":1.77,"S":1.13,"T":0.88,"W":0.62,"Y":0.41,"V":0.58}
{"AccNo":"GEIM800111","PropDesc":"Aperiodic indices for alpha/beta-proteins (Geisow-Roberts, 1980)","LITDBNo":"LIT:0701087b","Author":"Geisow, M.J. and Roberts, R.D.B.","ArtTitle":"Amino acid preferences for secondary structure vary with protein class","JournalRef":"Int. J. Biol. Macromol. 2, 387-389 (1980)","A":0.93,"R":1.01,"N":1.36,"D":1.22,"C":0.92,"E":1.05,"Q":0.83,"G":1.45,"H":0.96,"I":0.58,"L":0.59,"K":0.91,"M":0.6,"F":0.71,"P":1.67,"S":1.25,"T":1.08,"W":0.68,"Y":0.98,"V":0.62}
{"AccNo":"GOLD730101","PropDesc":"Hydrophobicity factor (Goldsack-Chalifoux, 1973)","LITDBNo":"LIT:2004110b PMID:4354159","Author":"Goldsack, D.E. and Chalifoux, R.C.","ArtTitle":"Contribution of the free energy of mixing of hydrophobic side chains to the stability of the tertiary structure","JournalRef":"J. Theor. Biol. 39, 645-651 (1973) (Asn Gln !)","A":0.75,"R":0.75,"N":0.69,"D":0,"C":1,"E":0,"Q":0.59,"G":0,"H":0,"I":2.95,"L":2.4,"K":1.5,"M":1.3,"F":2.65,"P":2.6,"S":0,"T":0.45,"W":3,"Y":2.85,"V":1.7}
{"AccNo":"GOLD730102","PropDesc":"Residue volume (Goldsack-Chalifoux, 1973)","LITDBNo":"LIT:2004110b PMID:4354159","Author":"Goldsack, D.E. and Chalifoux, R.C.","ArtTitle":"Contribution of the free energy of mixing of hydrophobic side chains to the stability of the tertiary structure","JournalRef":"J. Theor. Biol. 39, 645-651 (1973) (Asn Gln 8.8)","A":88.3,"R":181.2,"N":125.1,"D":110.8,"C":112.4,"E":140.5,"Q":148.7,"G":60,"H":152.6,"I":168.5,"L":168.5,"K":175.6,"M":162.2,"F":189,"P":122.2,"S":88.7,"T":118.2,"W":227,"Y":193,"V":141.4}
{"AccNo":"GRAR740101","PropDesc":"Composition (Grantham, 1974)","LITDBNo":"LIT:2004143b PMID:4843792","Author":"Grantham, R.","ArtTitle":"Amino acid difference formula to help explain protein evolution","JournalRef":"Science 185, 862-864 (1974) (Atomic weight ratio of noncarbons to carbons in the side chain)","A":0,"R":0.65,"N":1.33,"D":1.38,"C":2.75,"E":0.92,"Q":0.89,"G":0.74,"H":0.58,"I":0,"L":0,"K":0.33,"M":0,"F":0,"P":0.39,"S":1.42,"T":0.71,"W":0.13,"Y":0.2,"V":0}
{"AccNo":"GRAR740102","PropDesc":"Polarity (Grantham, 1974)","LITDBNo":"LIT:2004143b PMID:4843792","Author":"Grantham, R.","ArtTitle":"Amino acid difference formula to help explain protein evolution","JournalRef":"Science 185, 862-864 (1974)","A":8.1,"R":10.5,"N":11.6,"D":13,"C":5.5,"E":12.3,"Q":10.5,"G":9,"H":10.4,"I":5.2,"L":4.9,"K":11.3,"M":5.7,"F":5.2,"P":8,"S":9.2,"T":8.6,"W":5.4,"Y":6.2,"V":5.9}
{"AccNo":"GRAR740103","PropDesc":"Volume (Grantham, 1974)","LITDBNo":"LIT:2004143b PMID:4843792","Author":"Grantham, R.","ArtTitle":"Amino acid difference formula to help explain protein evolution","JournalRef":"Science 185, 862-864 (1974)","A":31,"R":124,"N":56,"D":54,"C":55,"E":83,"Q":85,"G":3,"H":96,"I":111,"L":111,"K":119,"M":105,"F":132,"P":32.5,"S":32,"T":61,"W":170,"Y":136,"V":84}
{"AccNo":"GUYH850101","PropDesc":"Partition energy (Guy, 1985)","LITDBNo":"LIT:2004051b PMID:3978191","Author":"Guy, H.R.","ArtTitle":"Amino acid side-chain partition energies and distribution of residues in soluble proteins","JournalRef":"Biophys. J. 47, 61-70 (1985)","A":0.1,"R":1.91,"N":0.48,"D":0.78,"C":-1.42,"E":0.83,"Q":0.95,"G":0.33,"H":-0.5,"I":-1.13,"L":-1.18,"K":1.4,"M":-1.59,"F":-2.12,"P":0.73,"S":0.52,"T":0.07,"W":-0.51,"Y":-0.21,"V":-1.27}
{"AccNo":"HOPA770101","PropDesc":"Hydration number (Hopfinger, 1971), Cited by Charton-Charton (1982)","Author":"Hopfinger, A.J.","JournalRef":"\"Intermolecular Interactions and Biomolecular Organizations\", Wiley, New York (1977) Cited by Charton-Charton (1982) (Cys !)","A":1,"R":2.3,"N":2.2,"D":6.5,"C":0.1,"E":6.2,"Q":2.1,"G":1.1,"H":2.8,"I":0.8,"L":0.8,"K":5.3,"M":0.7,"F":1.4,"P":0.9,"S":1.7,"T":1.5,"W":1.9,"Y":2.1,"V":0.9}
{"AccNo":"HOPT810101","PropDesc":"Hydrophilicity value (Hopp-Woods, 1981)","LITDBNo":"LIT:0707598 PMID:6167991","Author":"Hopp, T.P. and Woods, K.R.","ArtTitle":"Prediction of protein antigenic determinants from amino acid sequecces","JournalRef":"Proc. Natl. Acad. Sci. USA 78, 3824-3828 (1981)","A":-0.5,"R":3,"N":0.2,"D":3,"C":-1,"E":3,"Q":0.2,"G":0,"H":-0.5,"I":-1.8,"L":-1.8,"K":3,"M":-1.3,"F":-2.5,"P":0,"S":0.3,"T":-0.4,"W":-3.4,"Y":-2.3,"V":-1.5}
{"AccNo":"HUTJ700101","PropDesc":"Heat capacity (Hutchens, 1970)","Author":"Hutchens, J.O.","ArtTitle":"Heat capacities, absolute entropies, and entropies of formation of amino acids and related compounds","JournalRef":"In \"Handbook of Biochemistry\", 2nd ed. (Sober, H.A., ed.), Chemical Rubber Co., Cleveland, Ohio, pp. B60-B61 (1970)","A":29.22,"R":26.37,"N":38.3,"D":37.09,"C":50.7,"E":41.84,"Q":44.02,"G":23.71,"H":59.64,"I":45,"L":48.03,"K":57.1,"M":69.32,"F":48.52,"P":36.13,"S":32.4,"T":35.2,"W":56.92,"Y":51.73,"V":40.35}
{"AccNo":"HUTJ700102","PropDesc":"Absolute entropy (Hutchens, 1970)","Author":"Hutchens, J.O.","ArtTitle":"Heat capacities, absolute entropies, and entropies of formation of amino acids and related compounds","JournalRef":"In \"Handbook of Biochemistry\", 2nd ed. (Sober, H.A., ed.), Chemical Rubber Co., Cleveland, Ohio, pp. B60-B61 (1970)","A":30.88,"R":68.43,"N":41.7,"D":40.66,"C":53.83,"E":44.98,"Q":46.62,"G":24.74,"H":65.99,"I":49.71,"L":50.62,"K":63.21,"M":55.32,"F":51.06,"P":39.21,"S":35.65,"T":36.5,"W":60,"Y":51.15,"V":42.75}
{"AccNo":"HUTJ700103","PropDesc":"Entropy of formation (Hutchens, 1970)","Author":"Hutchens, J.O.","ArtTitle":"Heat capacities, absolute entropies, and entropies of formation of amino acids and related compounds","JournalRef":"In \"Handbook of Biochemistry\", 2nd ed. (Sober, H.A., ed.), Chemical Rubber Co., Cleveland, Ohio, pp. B60-B61 (1970)","A":154.33,"R":341.01,"N":207.9,"D":194.91,"C":219.79,"E":223.16,"Q":235.51,"G":127.9,"H":242.54,"I":233.21,"L":232.3,"K":300.46,"M":202.65,"F":204.74,"P":179.93,"S":174.06,"T":205.8,"W":237.01,"Y":229.15,"V":207.6}
{"AccNo":"ISOY800101","PropDesc":"Normalized relative frequency of alpha-helix (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":1.53,"R":1.17,"N":0.6,"D":1,"C":0.89,"E":1.63,"Q":1.27,"G":0.44,"H":1.03,"I":1.07,"L":1.32,"K":1.26,"M":1.66,"F":1.22,"P":0.25,"S":0.65,"T":0.86,"W":1.05,"Y":0.7,"V":0.93}
{"AccNo":"ISOY800102","PropDesc":"Normalized relative frequency of extended structure (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":0.86,"R":0.98,"N":0.74,"D":0.69,"C":1.39,"E":0.66,"Q":0.89,"G":0.7,"H":1.06,"I":1.31,"L":1.01,"K":0.77,"M":1.06,"F":1.16,"P":1.16,"S":1.09,"T":1.24,"W":1.17,"Y":1.28,"V":1.4}
{"AccNo":"ISOY800103","PropDesc":"Normalized relative frequency of bend (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":0.78,"R":1.06,"N":1.56,"D":1.5,"C":0.6,"E":0.97,"Q":0.78,"G":1.73,"H":0.83,"I":0.4,"L":0.57,"K":1.01,"M":0.3,"F":0.67,"P":1.55,"S":1.19,"T":1.09,"W":0.74,"Y":1.14,"V":0.44}
{"AccNo":"ISOY800104","PropDesc":"Normalized relative frequency of bend R (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":1.09,"R":0.97,"N":1.14,"D":0.77,"C":0.5,"E":0.92,"Q":0.83,"G":1.25,"H":0.67,"I":0.66,"L":0.44,"K":1.25,"M":0.45,"F":0.5,"P":2.96,"S":1.21,"T":1.33,"W":0.62,"Y":0.94,"V":0.56}
{"AccNo":"ISOY800105","PropDesc":"Normalized relative frequency of bend S (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":0.35,"R":0.75,"N":2.12,"D":2.16,"C":0.5,"E":0.65,"Q":0.73,"G":2.4,"H":1.19,"I":0.12,"L":0.58,"K":0.83,"M":0.22,"F":0.89,"P":0.43,"S":1.24,"T":0.85,"W":0.62,"Y":1.44,"V":0.43}
{"AccNo":"ISOY800106","PropDesc":"Normalized relative frequency of helix end (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":1.09,"R":1.07,"N":0.88,"D":1.24,"C":1.04,"E":1.14,"Q":1.09,"G":0.27,"H":1.07,"I":0.97,"L":1.3,"K":1.2,"M":0.55,"F":0.8,"P":1.78,"S":1.2,"T":0.99,"W":1.03,"Y":0.69,"V":0.77}
{"AccNo":"ISOY800107","PropDesc":"Normalized relative frequency of double bend (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":1.34,"R":2.78,"N":0.92,"D":1.77,"C":1.44,"E":2.54,"Q":0.79,"G":0.95,"H":0,"I":0.52,"L":1.05,"K":0.79,"M":0,"F":0.43,"P":0.37,"S":0.87,"T":1.14,"W":1.79,"Y":0.73,"V":0}
{"AccNo":"ISOY800108","PropDesc":"Normalized relative frequency of coil (Isogai et al., 1980)","LITDBNo":"LIT:2004053b PMID:7378550","Author":"Isogai, Y., Nemethy, G., Rackovsky, S., Leach, S.J. and Scheraga,H.A","ArtTitle":"Characterization of multiple bends in proteins","JournalRef":"Biopolymers 19, 1183-1210 (1980) Recalculated by Kidera using a different set of proteins","A":0.47,"R":0.52,"N":2.16,"D":1.15,"C":0.41,"E":0.64,"Q":0.95,"G":3.03,"H":0.89,"I":0.62,"L":0.53,"K":0.98,"M":0.68,"F":0.61,"P":0.63,"S":1.03,"T":0.39,"W":0.63,"Y":0.83,"V":0.76}
{"AccNo":"JANJ780101","PropDesc":"Average accessible surface area (Janin et al., 1978)","LITDBNo":"LIT:0502087 PMID:731698","Author":"Janin, J., Wodak, S., Levitt, M. and Maigret, B.","ArtTitle":"Conformation of amino acid side-chains in proteins","JournalRef":"J. Mol. Biol. 125, 357-386 (1978)","A":27.8,"R":94.7,"N":60.1,"D":60.6,"C":15.5,"E":68.2,"Q":68.7,"G":24.5,"H":50.7,"I":22.8,"L":27.6,"K":103,"M":33.5,"F":25.5,"P":51.5,"S":42,"T":45,"W":34.7,"Y":55.2,"V":23.7}
{"AccNo":"JANJ780102","PropDesc":"Percentage of buried residues (Janin et al., 1978)","LITDBNo":"LIT:0502087 PMID:731698","Author":"Janin, J., Wodak, S., Levitt, M. and Maigret, B.","ArtTitle":"Conformation of amino acid side-chains in proteins","JournalRef":"J. Mol. Biol. 125, 357-386 (1978)","A":51,"R":5,"N":22,"D":19,"C":74,"E":16,"Q":16,"G":52,"H":34,"I":66,"L":60,"K":3,"M":52,"F":58,"P":25,"S":35,"T":30,"W":49,"Y":24,"V":64}
{"AccNo":"JANJ780103","PropDesc":"Percentage of exposed residues (Janin et al., 1978)","LITDBNo":"LIT:0502087 PMID:731698","Author":"Janin, J., Wodak, S., Levitt, M. and Maigret, B.","ArtTitle":"Conformation of amino acid side-chains in proteins","JournalRef":"J. Mol. Biol. 125, 357-386 (1978)","A":15,"R":67,"N":49,"D":50,"C":5,"E":55,"Q":56,"G":10,"H":34,"I":13,"L":16,"K":85,"M":20,"F":10,"P":45,"S":32,"T":32,"W":17,"Y":41,"V":14}
{"AccNo":"JANJ790101","PropDesc":"Ratio of buried and accessible molar fractions (Janin, 1979)","LITDBNo":"LIT:2004120b PMID:763335","Author":"Janin, J.","ArtTitle":"Surface and inside volumes in globular proteins","JournalRef":"Nature 277, 491-492 (1979)","A":1.7,"R":0.1,"N":0.4,"D":0.4,"C":4.6,"E":0.3,"Q":0.3,"G":1.8,"H":0.8,"I":3.1,"L":2.4,"K":0.05,"M":1.9,"F":2.2,"P":0.6,"S":0.8,"T":0.7,"W":1.6,"Y":0.5,"V":2.9}
{"AccNo":"JANJ790102","PropDesc":"Transfer free energy (Janin, 1979)","LITDBNo":"LIT:2004120b PMID:763335","Author":"Janin, J.","ArtTitle":"Surface and inside volumes in globular proteins","JournalRef":"Nature 277, 491-492 (1979)","A":0.3,"R":-1.4,"N":-0.5,"D":-0.6,"C":0.9,"E":-0.7,"Q":-0.7,"G":0.3,"H":-0.1,"I":0.7,"L":0.5,"K":-1.8,"M":0.4,"F":0.5,"P":-0.3,"S":-0.1,"T":-0.2,"W":0.3,"Y":-0.4,"V":0.6}
{"AccNo":"JOND750101","PropDesc":"Hydrophobicity (Jones, 1975)","LITDBNo":"PMID:1127956","Author":"Jones, D.D.","ArtTitle":"Amino acid properties and side-chain orientation in proteins: A cross correlation approach","JournalRef":"J. Theor. Biol. 50, 167-183 (1975)","A":0.87,"R":0.85,"N":0.09,"D":0.66,"C":1.52,"E":0.67,"Q":0,"G":0.1,"H":0.87,"I":3.15,"L":2.17,"K":1.64,"M":1.67,"F":2.87,"P":2.77,"S":0.07,"T":0.07,"W":3.77,"Y":2.67,"V":1.87}
{"AccNo":"JOND750102","PropDesc":"pK (-COOH) (Jones, 1975)","LITDBNo":"PMID:1127956","Author":"Jones, D.D.","ArtTitle":"Amino acid properties and side-chain orientation in proteins: A cross correlation approach","JournalRef":"J. Theor. Biol. 50, 167-183 (1975) Original reference of this data: McMeekin, T.L., Groves, M.L. and Hipp, N.J. In \"Amino Acids and Serum Proteins\" (Stekol, J.A., ed.), American Chemical Society, Washington, D.C., p. 54 (1964)","A":2.34,"R":1.18,"N":2.02,"D":2.01,"C":1.65,"E":2.19,"Q":2.17,"G":2.34,"H":1.82,"I":2.36,"L":2.36,"K":2.18,"M":2.28,"F":1.83,"P":1.99,"S":2.21,"T":2.1,"W":2.38,"Y":2.2,"V":2.32}
{"AccNo":"JOND920101","PropDesc":"Relative frequency of occurrence (Jones et al., 1992)","LITDBNo":"LIT:1814076 PMID:1633570","Author":"Jones, D.T., Taylor, W.R. and Thornton, J.M.","ArtTitle":"The rapid generation of mutation data matrices from protein sequences","JournalRef":"CABIOS 8, 275-282 (1992)","A":0.077,"R":0.051,"N":0.043,"D":0.052,"C":0.02,"E":0.062,"Q":0.041,"G":0.074,"H":0.023,"I":0.053,"L":0.091,"K":0.059,"M":0.024,"F":0.04,"P":0.051,"S":0.069,"T":0.059,"W":0.014,"Y":0.032,"V":0.066}
{"AccNo":"JOND920102","PropDesc":"Relative mutability (Jones et al., 1992)","LITDBNo":"LIT:1814076 PMID:1633570","Author":"Jones, D.T., Taylor, W.R. and Thornton, J.M.","ArtTitle":"The rapid generation of mutation data matrices from protein sequences","JournalRef":"CABIOS 8, 275-282 (1992)","A":100,"R":83,"N":104,"D":86,"C":44,"E":77,"Q":84,"G":50,"H":91,"I":103,"L":54,"K":72,"M":93,"F":51,"P":58,"S":117,"T":107,"W":25,"Y":50,"V":98}
{"AccNo":"JUKT750101","PropDesc":"Amino acid distribution (Jukes et al., 1975)","LITDBNo":"PMID:237322","Author":"Jukes, T.H., Holmquist, R. and Moise, H.","ArtTitle":"Amino acid composition of proteins: Selection against the genetic code","JournalRef":"Science 189, 50-51 (1975)","A":5.3,"R":2.6,"N":3,"D":3.6,"C":1.3,"E":3.3,"Q":2.4,"G":4.8,"H":1.4,"I":3.1,"L":4.7,"K":4.1,"M":1.1,"F":2.3,"P":2.5,"S":4.5,"T":3.7,"W":0.8,"Y":2.3,"V":4.2}
{"AccNo":"JUNJ780101","PropDesc":"Sequence frequency (Jungck, 1978)","LITDBNo":"LIT:2004107b PMID:691072","Author":"Jungck, J.R.","ArtTitle":"The genetic code as a periodic table","JournalRef":"J. Mol. Evol. 11, 211-224 (1978)","A":685,"R":382,"N":397,"D":400,"C":241,"E":427,"Q":313,"G":707,"H":155,"I":394,"L":581,"K":575,"M":132,"F":303,"P":366,"S":593,"T":490,"W":99,"Y":292,"V":553}
{"AccNo":"KANM800101","PropDesc":"Average relative probability of helix (Kanehisa-Tsong, 1980)","LITDBNo":"LIT:0611060 PMID:7426680","Author":"Kanehisa, M.I. and Tsong, T.Y.","ArtTitle":"Local hydrophobicity stabilizes secondary structures in proteins","JournalRef":"Biopolymers 19, 1617-1628 (1980)","A":1.36,"R":1,"N":0.89,"D":1.04,"C":0.82,"E":1.48,"Q":1.14,"G":0.63,"H":1.11,"I":1.08,"L":1.21,"K":1.22,"M":1.45,"F":1.05,"P":0.52,"S":0.74,"T":0.81,"W":0.97,"Y":0.79,"V":0.94}
{"AccNo":"KANM800102","PropDesc":"Average relative probability of beta-sheet (Kanehisa-Tsong, 1980)","LITDBNo":"LIT:0611060 PMID:7426680","Author":"Kanehisa, M.I. and Tsong, T.Y.","ArtTitle":"Local hydrophobicity stabilizes secondary structures in proteins","JournalRef":"Biopolymers 19, 1617-1628 (1980)","A":0.81,"R":0.85,"N":0.62,"D":0.71,"C":1.17,"E":0.53,"Q":0.98,"G":0.88,"H":0.92,"I":1.48,"L":1.24,"K":0.77,"M":1.05,"F":1.2,"P":0.61,"S":0.92,"T":1.18,"W":1.18,"Y":1.23,"V":1.66}
{"AccNo":"KANM800103","PropDesc":"Average relative probability of inner helix (Kanehisa-Tsong, 1980)","LITDBNo":"LIT:0611060 PMID:7426680","Author":"Kanehisa, M.I. and Tsong, T.Y.","ArtTitle":"Local hydrophobicity stabilizes secondary structures in proteins","JournalRef":"Biopolymers 19, 1617-1628 (1980)","A":1.45,"R":1.15,"N":0.64,"D":0.91,"C":0.7,"E":1.29,"Q":1.14,"G":0.53,"H":1.13,"I":1.23,"L":1.56,"K":1.27,"M":1.83,"F":1.2,"P":0.21,"S":0.48,"T":0.77,"W":1.17,"Y":0.74,"V":1.1}
{"AccNo":"KANM800104","PropDesc":"Average relative probability of inner beta-sheet (Kanehisa-Tsong, 1980)","LITDBNo":"LIT:0611060 PMID:7426680","Author":"Kanehisa, M.I. and Tsong, T.Y.","ArtTitle":"Local hydrophobicity stabilizes secondary structures in proteins","JournalRef":"Biopolymers 19, 1617-1628 (1980)","A":0.75,"R":0.79,"N":0.33,"D":0.31,"C":1.46,"E":0.46,"Q":0.75,"G":0.83,"H":0.83,"I":1.87,"L":1.56,"K":0.66,"M":0.86,"F":1.37,"P":0.52,"S":0.82,"T":1.36,"W":0.79,"Y":1.08,"V":2}
{"AccNo":"KARP850101","PropDesc":"Flexibility parameter for no rigid neighbors (Karplus-Schulz, 1985)","LITDBNo":"LIT:1110994","Author":"Karplus, P.A. and Schulz, G.E.","ArtTitle":"Prediction of chain flexibility in proteins","JournalRef":"Naturwiss. 72, 212-213 (1985)","A":1.041,"R":1.038,"N":1.117,"D":1.033,"C":0.96,"E":1.094,"Q":1.165,"G":1.142,"H":0.982,"I":1.002,"L":0.967,"K":1.093,"M":0.947,"F":0.93,"P":1.055,"S":1.169,"T":1.073,"W":0.925,"Y":0.961,"V":0.982}
{"AccNo":"KARP850102","PropDesc":"Flexibility parameter for one rigid neighbor (Karplus-Schulz, 1985)","LITDBNo":"LIT:1110994","Author":"Karplus, P.A. and Schulz, G.E.","ArtTitle":"Prediction of chain flexibility in proteins","JournalRef":"Naturwiss. 72, 212-213 (1985)","A":0.946,"R":1.028,"N":1.006,"D":1.089,"C":0.878,"E":1.036,"Q":1.025,"G":1.042,"H":0.952,"I":0.892,"L":0.961,"K":1.082,"M":0.862,"F":0.912,"P":1.085,"S":1.048,"T":1.051,"W":0.917,"Y":0.93,"V":0.927}
{"AccNo":"KARP850103","PropDesc":"Flexibility parameter for two rigid neighbors (Karplus-Schulz, 1985)","LITDBNo":"LIT:1110994","Author":"Karplus, P.A. and Schulz, G.E.","ArtTitle":"Prediction of chain flexibility in proteins","JournalRef":"Naturwiss. 72, 212-213 (1985)","A":0.892,"R":0.901,"N":0.93,"D":0.932,"C":0.925,"E":0.933,"Q":0.885,"G":0.923,"H":0.894,"I":0.872,"L":0.921,"K":1.057,"M":0.804,"F":0.914,"P":0.932,"S":0.923,"T":0.934,"W":0.803,"Y":0.837,"V":0.913}
{"AccNo":"KHAG800101","PropDesc":"The Kerr-constant increments (Khanarian-Moore, 1980)","LITDBNo":"LIT:0611050b","Author":"Khanarian, G. and Moore, W.J.","ArtTitle":"The Kerr effect of amino acids in water","JournalRef":"Aust. J. Chem. 33, 1727-1741 (1980) (Cys Lys Tyr !)","A":49.1,"R":133,"N":-3.6,"D":0,"C":0,"E":0,"Q":20,"G":64.6,"H":75.7,"I":18.9,"L":15.6,"K":0,"M":6.8,"F":54.7,"P":43.8,"S":44.4,"T":31,"W":70.5,"Y":0,"V":29.5}
{"AccNo":"KLEP840101","PropDesc":"Net charge (Klein et al., 1984)","LITDBNo":"LIT:1008055 PMID:6547351","Author":"Klein, P., Kanehisa, M. and DeLisi, C.","ArtTitle":"Prediction of protein function from sequence properties: Discriminant analysis of a data base","JournalRef":"Biochim. Biophys. Acta 787, 221-226 (1984)","A":0,"R":1,"N":0,"D":-1,"C":0,"E":-1,"Q":0,"G":0,"H":0,"I":0,"L":0,"K":1,"M":0,"F":0,"P":0,"S":0,"T":0,"W":0,"Y":0,"V":0}
{"AccNo":"KRIW710101","PropDesc":"Side chain interaction parameter (Krigbaum-Rubin, 1971)","LITDBNo":"LIT:2004046b PMID:5553983","Author":"Krigbaum, W.R. and Rubin, B.H.","ArtTitle":"Local interactions as structure determinant for globular proteins","JournalRef":"Biochim. Biophys. Acta 229, 368-383 (1971)","A":4.6,"R":6.5,"N":5.9,"D":5.7,"C":-1,"E":5.6,"Q":6.1,"G":7.6,"H":4.5,"I":2.6,"L":3.25,"K":7.9,"M":1.4,"F":3.2,"P":7,"S":5.25,"T":4.8,"W":4,"Y":4.35,"V":3.4}
{"AccNo":"KRIW790101","PropDesc":"Side chain interaction parameter (Krigbaum-Komoriya, 1979)","LITDBNo":"LIT:0502056 PMID:760806","Author":"Krigbaum, W.R. and Komoriya, A.","ArtTitle":"Local interactions as a structure determinant for protein molecules: II","JournalRef":"Biochim. Biophys. Acta 576, 204-228 (1979)","A":4.32,"R":6.55,"N":6.24,"D":6.04,"C":1.73,"E":6.17,"Q":6.13,"G":6.09,"H":5.66,"I":2.31,"L":3.93,"K":7.92,"M":2.44,"F":2.59,"P":7.19,"S":5.37,"T":5.16,"W":2.78,"Y":3.58,"V":3.31}
{"AccNo":"KRIW790102","PropDesc":"Fraction of site occupied by water (Krigbaum-Komoriya, 1979)","LITDBNo":"LIT:0502056 PMID:760806","Author":"Krigbaum, W.R. and Komoriya, A.","ArtTitle":"Local interactions as a structure determinant for protein molecules: II","JournalRef":"Biochim. Biophys. Acta 576, 204-228 (1979)","A":0.28,"R":0.34,"N":0.31,"D":0.33,"C":0.11,"E":0.37,"Q":0.39,"G":0.28,"H":0.23,"I":0.12,"L":0.16,"K":0.59,"M":0.08,"F":0.1,"P":0.46,"S":0.27,"T":0.26,"W":0.15,"Y":0.25,"V":0.22}
{"AccNo":"KRIW790103","PropDesc":"Side chain volume (Krigbaum-Komoriya, 1979)","LITDBNo":"LIT:0502056 PMID:760806","Author":"Krigbaum, W.R. and Komoriya, A.","ArtTitle":"Local interactions as a structure determinant for protein molecules: II","JournalRef":"Biochim. Biophys. Acta 576, 204-228 (1979) (Gly Pro 7.8)","A":27.5,"R":105,"N":58.7,"D":40,"C":44.6,"E":62,"Q":80.7,"G":0,"H":79,"I":93.5,"L":93.5,"K":100,"M":94.1,"F":115.5,"P":41.9,"S":29.3,"T":51.3,"W":145.5,"Y":117.3,"V":71.5}
{"AccNo":"KYTJ820101","PropDesc":"Hydropathy index (Kyte-Doolittle, 1982)","LITDBNo":"LIT:0807099 PMID:7108955","Author":"Kyte, J. and Doolittle, R.F.","ArtTitle":"A simple method for displaying the hydropathic character of a protein","JournalRef":"J. Mol. Biol. 157, 105-132 (1982)","A":1.8,"R":-4.5,"N":-3.5,"D":-3.5,"C":2.5,"E":-3.5,"Q":-3.5,"G":-0.4,"H":-3.2,"I":4.5,"L":3.8,"K":-3.9,"M":1.9,"F":2.8,"P":-1.6,"S":-0.8,"T":-0.7,"W":-0.9,"Y":-1.3,"V":4.2}
{"AccNo":"LAWE840101","PropDesc":"Transfer free energy, CHP/water (Lawson et al., 1984)","LITDBNo":"LIT:1004126 PMID:6699000","Author":"Lawson, E.Q., Sadler, A.J., Harmatz, D., Brandau, D.T., Micanovic, R. MacElroy, R.D. and Middaught, C.R.","ArtTitle":"A simple experimental model for hydrophobic interactions in proteins","JournalRef":"J. Biol. Chem. 259, 2910-2912 (1984)","A":-0.48,"R":-0.06,"N":-0.87,"D":-0.75,"C":-0.32,"E":-0.71,"Q":-0.32,"G":0,"H":-0.51,"I":0.81,"L":1.02,"K":-0.09,"M":0.81,"F":1.03,"P":2.03,"S":0.05,"T":-0.35,"W":0.66,"Y":1.24,"V":0.56}
{"AccNo":"LEVM760101","PropDesc":"Hydrophobic parameter (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976)","A":-0.5,"R":3,"N":0.2,"D":2.5,"C":-1,"E":2.5,"Q":0.2,"G":0,"H":-0.5,"I":-1.8,"L":-1.8,"K":3,"M":-1.3,"F":-2.5,"P":-1.4,"S":0.3,"T":-0.4,"W":-3.4,"Y":-2.3,"V":-1.5}
{"AccNo":"LEVM760102","PropDesc":"Distance between C-alpha and centroid of side chain (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976)","A":0.77,"R":3.72,"N":1.98,"D":1.99,"C":1.38,"E":2.63,"Q":2.58,"G":0,"H":2.76,"I":1.83,"L":2.08,"K":2.94,"M":2.34,"F":2.97,"P":1.42,"S":1.28,"T":1.43,"W":3.58,"Y":3.36,"V":1.49}
{"AccNo":"LEVM760103","PropDesc":"Side chain angle theta(AAR) (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976) (Gly missing)","A":121.9,"R":121.4,"N":117.5,"D":121.2,"C":113.7,"E":118.2,"Q":118,"G":0,"H":118.2,"I":118.9,"L":118.1,"K":122,"M":113.1,"F":118.2,"P":81.9,"S":117.9,"T":117.1,"W":118.4,"Y":110,"V":121.7}
{"AccNo":"LEVM760104","PropDesc":"Side chain torsion angle phi(AAAR) (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976)","A":243.2,"R":206.6,"N":207.1,"D":215,"C":209.4,"E":213.6,"Q":205.4,"G":300,"H":219.9,"I":217.9,"L":205.6,"K":210.9,"M":204,"F":203.7,"P":237.4,"S":232,"T":226.7,"W":203.7,"Y":195.6,"V":220.3}
{"AccNo":"LEVM760105","PropDesc":"Radius of gyration of side chain (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976) (Gly 0.089)","A":0.77,"R":2.38,"N":1.45,"D":1.43,"C":1.22,"E":1.77,"Q":1.75,"G":0.58,"H":1.78,"I":1.56,"L":1.54,"K":2.08,"M":1.8,"F":1.9,"P":1.25,"S":1.08,"T":1.24,"W":2.21,"Y":2.13,"V":1.29}
{"AccNo":"LEVM760106","PropDesc":"van der Waals parameter R0 (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976)","A":5.2,"R":6,"N":5,"D":5,"C":6.1,"E":6,"Q":6,"G":4.2,"H":6,"I":7,"L":7,"K":6,"M":6.8,"F":7.1,"P":6.2,"S":4.9,"T":5,"W":7.6,"Y":7.1,"V":6.4}
{"AccNo":"LEVM760107","PropDesc":"van der Waals parameter epsilon (Levitt, 1976)","LITDBNo":"LIT:2004093b PMID:957439","Author":"Levitt, M.","ArtTitle":"A simplified representation of protein conformations for rapid simulation of protein folfing","JournalRef":"J. Mol. Biol. 104, 59-107 (1976)","A":0.025,"R":0.2,"N":0.1,"D":0.1,"C":0.1,"E":0.1,"Q":0.1,"G":0.025,"H":0.1,"I":0.19,"L":0.19,"K":0.2,"M":0.19,"F":0.39,"P":0.17,"S":0.025,"T":0.1,"W":0.56,"Y":0.39,"V":0.15}
{"AccNo":"LEVM780101","PropDesc":"Normalized frequency of alpha-helix, with weights (Levitt, 1978)","LITDBNo":"LIT:0411042 PMID:708713","Author":"Levitt, M.","ArtTitle":"Conformational preferences of amino acids in globular proteins","JournalRef":"Biochemistry 17, 4277-4285 (1978)","A":1.29,"R":0.96,"N":0.9,"D":1.04,"C":1.11,"E":1.44,"Q":1.27,"G":0.56,"H":1.22,"I":0.97,"L":1.3,"K":1.23,"M":1.47,"F":1.07,"P":0.52,"S":0.82,"T":0.82,"W":0.99,"Y":0.72,"V":0.91}
{"AccNo":"LEVM780102","PropDesc":"Normalized frequency of beta-sheet, with weights (Levitt, 1978)","LITDBNo":"LIT:0411042 PMID:708713","Author":"Levitt, M.","ArtTitle":"Conformational preferences of amino acids in globular proteins","JournalRef":"Biochemistry 17, 4277-4285 (1978)","A":0.9,"R":0.99,"N":0.76,"D":0.72,"C":0.74,"E":0.75,"Q":0.8,"G":0.92,"H":1.08,"I":1.45,"L":1.02,"K":0.77,"M":0.97,"F":1.32,"P":0.64,"S":0.95,"T":1.21,"W":1.14,"Y":1.25,"V":1.49}
{"AccNo":"LEVM780103","PropDesc":"Normalized frequency of reverse turn, with weights (Levitt, 1978)","LITDBNo":"LIT:0411042 PMID:708713","Author":"Levitt, M.","ArtTitle":"Conformational preferences of amino acids in globular proteins","JournalRef":"Biochemistry 17, 4277-4285 (1978)","A":0.77,"R":0.88,"N":1.28,"D":1.41,"C":0.81,"E":0.99,"Q":0.98,"G":1.64,"H":0.68,"I":0.51,"L":0.58,"K":0.96,"M":0.41,"F":0.59,"P":1.91,"S":1.32,"T":1.04,"W":0.76,"Y":1.05,"V":0.47}
{"AccNo":"LEVM780104","PropDesc":"Normalized frequency of alpha-helix, unweighted (Levitt, 1978)","LITDBNo":"LIT:0411042 PMID:708713","Author":"Levitt, M.","ArtTitle":"Conformational preferences of amino acids in globular proteins","JournalRef":"Biochemistry 17, 4277-4285 (1978)","A":1.32,"R":0.98,"N":0.95,"D":1.03,"C":0.92,"E":1.44,"Q":1.1,"G":0.61,"H":1.31,"I":0.93,"L":1.31,"K":1.25,"M":1.39,"F":1.02,"P":0.58,"S":0.76,"T":0.79,"W":0.97,"Y":0.73,"V":0.93}
{"AccNo":"LEVM780105","PropDesc":"Normalized frequency of beta-sheet, unweighted (Levitt, 1978)","LITDBNo":"LIT:0411042 PMID:708713","Author":"Levitt, M.","ArtTitle":"Conformational preferences of amino acids in globular proteins","JournalRef":"Biochemistry 17, 4277-4285 (1978)","A":0.86,"R":0.97,"N":0.73,"D":0.69,"C":1.04,"E":0.66,"Q":1,"G":0.89,"H":0.85,"I":1.47,"L":1.04,"K":0.77,"M":0.93,"F":1.21,"P":0.68,"S":1.02,"T":1.27,"W":1.26,"Y":1.31,"V":1.43}
{"AccNo":"LEVM780106","PropDesc":"Normalized frequency of reverse turn, unweighted (Levitt, 1978)","LITDBNo":"LIT:0411042 PMID:708713","Author":"Levitt, M.","ArtTitle":"Conformational preferences of amino acids in globular proteins","JournalRef":"Biochemistry 17, 4277-4285 (1978)","A":0.79,"R":0.9,"N":1.25,"D":1.47,"C":0.79,"E":1.02,"Q":0.92,"G":1.67,"H":0.81,"I":0.5,"L":0.57,"K":0.99,"M":0.51,"F":0.77,"P":1.78,"S":1.3,"T":0.97,"W":0.79,"Y":0.93,"V":0.46}
{"AccNo":"LEWP710101","PropDesc":"Frequency of occurrence in beta-bends (Lewis et al., 1971)","LITDBNo":"PMID:5289387","Author":"Lewis, P. N., Momany, F.A. and Scheraga, H.A.","ArtTitle":"Folding of polypeptide chains in proteins: A proposed mechanism for folding","JournalRef":"Proc. Natl. Acad. Sci. USA 68, 2293-2297 (1971)","A":0.22,"R":0.28,"N":0.42,"D":0.73,"C":0.2,"E":0.08,"Q":0.26,"G":0.58,"H":0.14,"I":0.22,"L":0.19,"K":0.27,"M":0.38,"F":0.08,"P":0.46,"S":0.55,"T":0.49,"W":0.43,"Y":0.46,"V":0.08}
{"AccNo":"LIFS790101","PropDesc":"Conformational preference for all beta-strands (Lifson-Sander, 1979)","LITDBNo":"LIT:0512128 PMID:503185","Author":"Lifson, S. and Sander, C.","ArtTitle":"Antiparallel and parallel beta-strands differ in amino acid residue preference","JournalRef":"Nature 282, 109-111 (1979)","A":0.92,"R":0.93,"N":0.6,"D":0.48,"C":1.16,"E":0.61,"Q":0.95,"G":0.61,"H":0.93,"I":1.81,"L":1.3,"K":0.7,"M":1.19,"F":1.25,"P":0.4,"S":0.82,"T":1.12,"W":1.54,"Y":1.53,"V":1.81}
{"AccNo":"LIFS790102","PropDesc":"Conformational preference for parallel beta-strands (Lifson-Sander, 1979)","LITDBNo":"LIT:0512128 PMID:503185","Author":"Lifson, S. and Sander, C.","ArtTitle":"Antiparallel and parallel beta-strands differ in amino acid residue preference","JournalRef":"Nature 282, 109-111 (1979)","A":1,"R":0.68,"N":0.54,"D":0.5,"C":0.91,"E":0.59,"Q":0.28,"G":0.79,"H":0.38,"I":2.6,"L":1.42,"K":0.59,"M":1.49,"F":1.3,"P":0.35,"S":0.7,"T":0.59,"W":0.89,"Y":1.08,"V":2.63}
{"AccNo":"LIFS790103","PropDesc":"Conformational preference for antiparallel beta-strands (Lifson-Sander, 1979)","LITDBNo":"LIT:0512128 PMID:503185","Author":"Lifson, S. and Sander, C.","ArtTitle":"Antiparallel and parallel beta-strands differ in amino acid residue preference","JournalRef":"Nature 282, 109-111 (1979)","A":0.9,"R":1.02,"N":0.62,"D":0.47,"C":1.24,"E":0.62,"Q":1.18,"G":0.56,"H":1.12,"I":1.54,"L":1.26,"K":0.74,"M":1.09,"F":1.23,"P":0.42,"S":0.87,"T":1.3,"W":1.75,"Y":1.68,"V":1.53}
{"AccNo":"MANP780101","PropDesc":"Average surrounding hydrophobicity (Manavalan-Ponnuswamy, 1978)","LITDBNo":"LIT:0411088 PMID:703834","Author":"Manavalan, P. and Ponnuswamy, P.K.","ArtTitle":"Hydrophobic character of amino acid residues in globular proteins","JournalRef":"Nature 275, 673-674 (1978)","A":12.97,"R":11.72,"N":11.42,"D":10.85,"C":14.63,"E":11.89,"Q":11.76,"G":12.43,"H":12.16,"I":15.67,"L":14.9,"K":11.36,"M":14.39,"F":14,"P":11.37,"S":11.23,"T":11.69,"W":13.93,"Y":13.42,"V":15.71}
{"AccNo":"MAXF760101","PropDesc":"Normalized frequency of alpha-helix (Maxfield-Scheraga, 1976)","LITDBNo":"LIT:2004036b PMID:990270","Author":"Maxfield, F.R. and Scheraga, H.A.","ArtTitle":"Status of empirical methods for the prediction of protein backbone topography","JournalRef":"Biochemistry 15, 5138-5153 (1976) Recalculated by Kidera using a different set of proteins Reported values normalized by the total number","A":1.43,"R":1.18,"N":0.64,"D":0.92,"C":0.94,"E":1.67,"Q":1.22,"G":0.46,"H":0.98,"I":1.04,"L":1.36,"K":1.27,"M":1.53,"F":1.19,"P":0.49,"S":0.7,"T":0.78,"W":1.01,"Y":0.69,"V":0.98}
{"AccNo":"MAXF760102","PropDesc":"Normalized frequency of extended structure (Maxfield-Scheraga, 1976)","LITDBNo":"LIT:2004036b PMID:990270","Author":"Maxfield, F.R. and Scheraga, H.A.","ArtTitle":"Status of empirical methods for the prediction of protein backbone topography","JournalRef":"Biochemistry 15, 5138-5153 (1976) Recalculated by Kidera using a different set of proteins Reported values normalized by the total number","A":0.86,"R":0.94,"N":0.74,"D":0.72,"C":1.17,"E":0.62,"Q":0.89,"G":0.97,"H":1.06,"I":1.24,"L":0.98,"K":0.79,"M":1.08,"F":1.16,"P":1.22,"S":1.04,"T":1.18,"W":1.07,"Y":1.25,"V":1.33}
{"AccNo":"MAXF760103","PropDesc":"Normalized frequency of zeta R (Maxfield-Scheraga, 1976)","LITDBNo":"LIT:2004036b PMID:990270","Author":"Maxfield, F.R. and Scheraga, H.A.","ArtTitle":"Status of empirical methods for the prediction of protein backbone topography","JournalRef":"Biochemistry 15, 5138-5153 (1976) Recalculated by Kidera using a different set of proteins Reported values normalized by the total number","A":0.64,"R":0.62,"N":3.14,"D":1.92,"C":0.32,"E":1.01,"Q":0.8,"G":0.63,"H":2.05,"I":0.92,"L":0.37,"K":0.89,"M":1.07,"F":0.86,"P":0.5,"S":1.01,"T":0.92,"W":1,"Y":1.31,"V":0.87}
{"AccNo":"MAXF760104","PropDesc":"Normalized frequency of left-handed alpha-helix (Maxfield-Scheraga, 1976)","LITDBNo":"LIT:2004036b PMID:990270","Author":"Maxfield, F.R. and Scheraga, H.A.","ArtTitle":"Status of empirical methods for the prediction of protein backbone topography","JournalRef":"Biochemistry 15, 5138-5153 (1976) Recalculated by Kidera using a different set of proteins Reported values normalized by the total number","A":0.17,"R":0.76,"N":2.62,"D":1.08,"C":0.95,"E":0.28,"Q":0.91,"G":5.02,"H":0.57,"I":0.26,"L":0.21,"K":1.17,"M":0,"F":0.28,"P":0.12,"S":0.57,"T":0.23,"W":0,"Y":0.97,"V":0.24}
{"AccNo":"MAXF760105","PropDesc":"Normalized frequency of zeta L (Maxfield-Scheraga, 1976)","LITDBNo":"LIT:2004036b PMID:990270","Author":"Maxfield, F.R. and Scheraga, H.A.","ArtTitle":"Status of empirical methods for the prediction of protein backbone topography","JournalRef":"Biochemistry 15, 5138-5153 (1976) Recalculated by Kidera using a different set of proteins Reported values normalized by the total number","A":1.13,"R":0.48,"N":1.11,"D":1.18,"C":0.38,"E":1.02,"Q":0.41,"G":3.84,"H":0.3,"I":0.4,"L":0.65,"K":1.13,"M":0,"F":0.45,"P":0,"S":0.81,"T":0.71,"W":0.93,"Y":0.38,"V":0.48}
{"AccNo":"MAXF760106","PropDesc":"Normalized frequency of alpha region (Maxfield-Scheraga, 1976)","LITDBNo":"LIT:2004036b PMID:990270","Author":"Maxfield, F.R. and Scheraga, H.A.","ArtTitle":"Status of empirical methods for the prediction of protein backbone topography","JournalRef":"Biochemistry 15, 5138-5153 (1976) Recalculated by Kidera using a different set of proteins Reported values normalized by the total number","A":1,"R":1.18,"N":0.87,"D":1.39,"C":1.09,"E":1.04,"Q":1.13,"G":0.46,"H":0.71,"I":0.68,"L":1.01,"K":1.05,"M":0.36,"F":0.65,"P":1.95,"S":1.56,"T":1.23,"W":1.1,"Y":0.87,"V":0.58}
{"AccNo":"MCMT640101","PropDesc":"Refractivity (McMeekin et al., 1964), Cited by Jones (1975)","Author":"McMeekin, T.L., Groves, M.L. and Hipp, N.J.","JournalRef":"In \"Amino Acids and Serum Proteins\" (Stekol, J.A., ed.), American Chemical Society, Washington, D.C., p. 54 (1964)","A":4.34,"R":26.66,"N":13.28,"D":12,"C":35.77,"E":17.26,"Q":17.56,"G":0,"H":21.81,"I":19.06,"L":18.78,"K":21.29,"M":21.64,"F":29.4,"P":10.93,"S":6.35,"T":11.01,"W":42.53,"Y":31.53,"V":13.92}
{"AccNo":"MEEJ800101","PropDesc":"Retention coefficient in HPLC, pH7.4 (Meek, 1980)","LITDBNo":"LIT:0604247 PMID:6929513","Author":"Meek, J.L.","ArtTitle":"Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition","JournalRef":"Proc. Natl. Acad. Sci. USA 77, 1632-1636 (1980)","A":0.5,"R":0.8,"N":0.8,"D":-8.2,"C":-6.8,"E":-16.9,"Q":-4.8,"G":0,"H":-3.5,"I":13.9,"L":8.8,"K":0.1,"M":4.8,"F":13.2,"P":6.1,"S":1.2,"T":2.7,"W":14.9,"Y":6.1,"V":2.7}
{"AccNo":"MEEJ800102","PropDesc":"Retention coefficient in HPLC, pH2.1 (Meek, 1980)","LITDBNo":"LIT:0604247 PMID:6929513","Author":"Meek, J.L.","ArtTitle":"Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition","JournalRef":"Proc. Natl. Acad. Sci. USA 77, 1632-1636 (1980)","A":-0.1,"R":-4.5,"N":-1.6,"D":-2.8,"C":-2.2,"E":-7.5,"Q":-2.5,"G":-0.5,"H":0.8,"I":11.8,"L":10,"K":-3.2,"M":7.1,"F":13.9,"P":8,"S":-3.7,"T":1.5,"W":18.1,"Y":8.2,"V":3.3}
{"AccNo":"MEEJ810101","PropDesc":"Retention coefficient in NaClO4 (Meek-Rossetti, 1981)","LITDBNo":"LIT:0708201","Author":"Meek, J.L. and Rossetti, Z.L.","ArtTitle":"Factors affecting retention and resolution of peptides in high-performance liquid chromatography","JournalRef":"J. Chromatogr. 211, 15-28 (1981)","A":1.1,"R":-0.4,"N":-4.2,"D":-1.6,"C":7.1,"E":0.7,"Q":-2.9,"G":-0.2,"H":-0.7,"I":8.5,"L":11,"K":-1.9,"M":5.4,"F":13.4,"P":4.4,"S":-3.2,"T":-1.7,"W":17.1,"Y":7.4,"V":5.9}
{"AccNo":"MEEJ810102","PropDesc":"Retention coefficient in NaH2PO4 (Meek-Rossetti, 1981)","LITDBNo":"LIT:0708201","Author":"Meek, J.L. and Rossetti, Z.L.","ArtTitle":"Factors affecting retention and resolution of peptides in high-performance liquid chromatography","JournalRef":"J. Chromatogr. 211, 15-28 (1981)","A":1,"R":-2,"N":-3,"D":-0.5,"C":4.6,"E":1.1,"Q":-2,"G":0.2,"H":-2.2,"I":7,"L":9.6,"K":-3,"M":4,"F":12.6,"P":3.1,"S":-2.9,"T":-0.6,"W":15.1,"Y":6.7,"V":4.6}
{"AccNo":"MEIH800101","PropDesc":"Average reduced distance for C-alpha (Meirovitch et al., 1980)","LITDBNo":"LIT:0702089","Author":"Meirovitch, H., Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Empirical studies of hydrophobicity. 1. Effect of protein size on the hydrophobic behavior of amino acids","JournalRef":"Macromolecules 13, 1398-1405 (1980) Database taken from group C","A":0.93,"R":0.98,"N":0.98,"D":1.01,"C":0.88,"E":1.02,"Q":1.02,"G":1.01,"H":0.89,"I":0.79,"L":0.85,"K":1.05,"M":0.84,"F":0.78,"P":1,"S":1.02,"T":0.99,"W":0.83,"Y":0.93,"V":0.81}
{"AccNo":"MEIH800102","PropDesc":"Average reduced distance for side chain (Meirovitch et al., 1980)","LITDBNo":"LIT:0702089","Author":"Meirovitch, H., Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Empirical studies of hydrophobicity. 1. Effect of protein size on the hydrophobic behavior of amino acids","JournalRef":"Macromolecules 13, 1398-1405 (1980) Database taken from group C (Gly 0.067)","A":0.94,"R":1.09,"N":1.04,"D":1.08,"C":0.84,"E":1.12,"Q":1.11,"G":1.01,"H":0.92,"I":0.76,"L":0.82,"K":1.23,"M":0.83,"F":0.73,"P":1.04,"S":1.04,"T":1.02,"W":0.87,"Y":1.03,"V":0.81}
{"AccNo":"MEIH800103","PropDesc":"Average side chain orientation angle (Meirovitch et al., 1980)","LITDBNo":"LIT:0702089","Author":"Meirovitch, H., Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Empirical studies of hydrophobicity. 1. Effect of protein size on the hydrophobic behavior of amino acids","JournalRef":"Macromolecules 13, 1398-1405 (1980) Database taken from group C (Gly 7.4)","A":87,"R":81,"N":70,"D":71,"C":104,"E":72,"Q":66,"G":90,"H":90,"I":105,"L":104,"K":65,"M":100,"F":108,"P":78,"S":83,"T":83,"W":94,"Y":83,"V":94}
{"AccNo":"MIYS850101","PropDesc":"Effective partition energy (Miyazawa-Jernigan, 1985)","LITDBNo":"LIT:2004114b","Author":"Miyazawa, S. and Jernigan, R.L.","ArtTitle":"Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation","JournalRef":"Macromolecules 18, 534-552 (1985)","A":2.36,"R":1.92,"N":1.7,"D":1.67,"C":3.36,"E":1.74,"Q":1.75,"G":2.06,"H":2.41,"I":4.17,"L":3.93,"K":1.23,"M":4.22,"F":4.37,"P":1.89,"S":1.81,"T":2.04,"W":3.82,"Y":2.91,"V":3.49}
{"AccNo":"NAGK730101","PropDesc":"Normalized frequency of alpha-helix (Nagano, 1973)","LITDBNo":"PMID:4728695","Author":"Nagano, K.","ArtTitle":"Local analysis of the mechanism of protein folding. I. Prediction of helices, loops, and beta-structures from primary structure","JournalRef":"J. Mol. Biol. 75, 401-420 (1973)","A":1.29,"R":0.83,"N":0.77,"D":1,"C":0.94,"E":1.54,"Q":1.1,"G":0.72,"H":1.29,"I":0.94,"L":1.23,"K":1.23,"M":1.23,"F":1.23,"P":0.7,"S":0.78,"T":0.87,"W":1.06,"Y":0.63,"V":0.97}
{"AccNo":"NAGK730102","PropDesc":"Normalized frequency of bata-structure (Nagano, 1973)","LITDBNo":"PMID:4728695","Author":"Nagano, K.","ArtTitle":"Local analysis of the mechanism of protein folding. I. Prediction of helices, loops, and beta-structures from primary structure","JournalRef":"J. Mol. Biol. 75, 401-420 (1973)","A":0.96,"R":0.67,"N":0.72,"D":0.9,"C":1.13,"E":0.33,"Q":1.18,"G":0.9,"H":0.87,"I":1.54,"L":1.26,"K":0.81,"M":1.29,"F":1.37,"P":0.75,"S":0.77,"T":1.23,"W":1.13,"Y":1.07,"V":1.41}
{"AccNo":"NAGK730103","PropDesc":"Normalized frequency of coil (Nagano, 1973)","LITDBNo":"PMID:4728695","Author":"Nagano, K.","ArtTitle":"Local analysis of the mechanism of protein folding. I. Prediction of helices, loops, and beta-structures from primary structure","JournalRef":"J. Mol. Biol. 75, 401-420 (1973)","A":0.72,"R":1.33,"N":1.38,"D":1.04,"C":1.01,"E":0.75,"Q":0.81,"G":1.35,"H":0.76,"I":0.8,"L":0.63,"K":0.84,"M":0.62,"F":0.58,"P":1.43,"S":1.34,"T":1.03,"W":0.87,"Y":1.35,"V":0.83}
{"AccNo":"NAKH900101","PropDesc":"AA composition of total proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":7.99,"R":5.86,"N":4.33,"D":5.14,"C":1.81,"E":6.1,"Q":3.98,"G":6.91,"H":2.17,"I":5.48,"L":9.16,"K":6.01,"M":2.5,"F":3.83,"P":4.95,"S":6.84,"T":5.77,"W":1.34,"Y":3.15,"V":6.65}
{"AccNo":"NAKH900102","PropDesc":"SD of AA composition of total proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":3.73,"R":3.34,"N":2.33,"D":2.23,"C":2.3,"E":3,"Q":2.36,"G":3.36,"H":1.55,"I":2.52,"L":3.4,"K":3.36,"M":1.37,"F":1.94,"P":3.18,"S":2.83,"T":2.63,"W":1.15,"Y":1.76,"V":2.53}
{"AccNo":"NAKH900103","PropDesc":"AA composition of mt-proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":5.74,"R":1.92,"N":5.25,"D":2.11,"C":1.03,"E":2.63,"Q":2.3,"G":5.66,"H":2.3,"I":9.12,"L":15.36,"K":3.2,"M":5.3,"F":6.51,"P":4.79,"S":7.55,"T":7.51,"W":2.51,"Y":4.08,"V":5.12}
{"AccNo":"NAKH900104","PropDesc":"Normalized composition of mt-proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":-0.6,"R":-1.18,"N":0.39,"D":-1.36,"C":-0.34,"E":-1.16,"Q":-0.71,"G":-0.37,"H":0.08,"I":1.44,"L":1.82,"K":-0.84,"M":2.04,"F":1.38,"P":-0.05,"S":0.25,"T":0.66,"W":1.02,"Y":0.53,"V":-0.6}
{"AccNo":"NAKH900105","PropDesc":"AA composition of mt-proteins from animal (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":5.88,"R":1.54,"N":4.38,"D":1.7,"C":1.11,"E":2.6,"Q":2.3,"G":5.29,"H":2.33,"I":8.78,"L":16.52,"K":2.58,"M":6,"F":6.58,"P":5.29,"S":7.68,"T":8.38,"W":2.89,"Y":3.51,"V":4.66}
{"AccNo":"NAKH900106","PropDesc":"Normalized composition from animal (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":-0.57,"R":-1.29,"N":0.02,"D":-1.54,"C":-0.3,"E":-1.17,"Q":-0.71,"G":-0.48,"H":0.1,"I":1.31,"L":2.16,"K":-1.02,"M":2.55,"F":1.42,"P":0.11,"S":0.3,"T":0.99,"W":1.35,"Y":0.2,"V":-0.79}
{"AccNo":"NAKH900107","PropDesc":"AA composition of mt-proteins from fungi and plant (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":5.39,"R":2.81,"N":7.31,"D":3.07,"C":0.86,"E":2.7,"Q":2.31,"G":6.52,"H":2.23,"I":9.94,"L":12.64,"K":4.67,"M":3.68,"F":6.34,"P":3.62,"S":7.24,"T":5.44,"W":1.64,"Y":5.42,"V":6.18}
{"AccNo":"NAKH900108","PropDesc":"Normalized composition from fungi and plant (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":-0.7,"R":-0.91,"N":1.28,"D":-0.93,"C":-0.41,"E":-1.13,"Q":-0.71,"G":-0.12,"H":0.04,"I":1.77,"L":1.02,"K":-0.4,"M":0.86,"F":1.29,"P":-0.42,"S":0.14,"T":-0.13,"W":0.26,"Y":1.29,"V":-0.19}
{"AccNo":"NAKH900109","PropDesc":"AA composition of membrane proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":9.25,"R":3.96,"N":3.71,"D":3.89,"C":1.07,"E":4.8,"Q":3.17,"G":8.51,"H":1.88,"I":6.47,"L":10.94,"K":3.5,"M":3.14,"F":6.36,"P":4.36,"S":6.26,"T":5.66,"W":2.22,"Y":3.28,"V":7.55}
{"AccNo":"NAKH900110","PropDesc":"Normalized composition of membrane proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":0.34,"R":-0.57,"N":-0.27,"D":-0.56,"C":-0.32,"E":-0.43,"Q":-0.34,"G":0.48,"H":-0.19,"I":0.39,"L":0.52,"K":-0.75,"M":0.47,"F":1.3,"P":-0.19,"S":-0.2,"T":-0.04,"W":0.77,"Y":0.07,"V":0.36}
{"AccNo":"NAKH900111","PropDesc":"Transmembrane regions of non-mt-proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":10.17,"R":1.21,"N":1.36,"D":1.18,"C":1.48,"E":1.15,"Q":1.57,"G":8.87,"H":1.07,"I":10.91,"L":16.22,"K":1.04,"M":4.12,"F":9.6,"P":2.24,"S":5.38,"T":5.61,"W":2.67,"Y":2.68,"V":11.44}
{"AccNo":"NAKH900112","PropDesc":"Transmembrane regions of mt-proteins (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":6.61,"R":0.41,"N":1.84,"D":0.59,"C":0.83,"E":1.63,"Q":1.2,"G":4.88,"H":1.14,"I":12.91,"L":21.66,"K":1.15,"M":7.17,"F":7.76,"P":3.51,"S":6.84,"T":8.89,"W":2.11,"Y":2.57,"V":6.3}
{"AccNo":"NAKH900113","PropDesc":"Ratio of average and computed composition (Nakashima et al., 1990)","LITDBNo":"LIT:2004138b PMID:2235995","Author":"Nakashima, H., Nishikawa, K. and Ooi, T.","ArtTitle":"Distinct character in hydrophobicity of amino acid composition of mitochondrial proteins","JournalRef":"Proteins 8, 173-178 (1990)","A":1.61,"R":0.4,"N":0.73,"D":0.75,"C":0.37,"E":1.5,"Q":0.61,"G":3.12,"H":0.46,"I":1.61,"L":1.37,"K":0.62,"M":1.59,"F":1.24,"P":0.67,"S":0.68,"T":0.92,"W":1.63,"Y":0.67,"V":1.3}
{"AccNo":"NAKH920101","PropDesc":"AA composition of CYT of single-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":8.63,"R":6.75,"N":4.18,"D":6.24,"C":1.03,"E":7.82,"Q":4.76,"G":6.8,"H":2.7,"I":3.48,"L":8.44,"K":6.25,"M":2.14,"F":2.73,"P":6.28,"S":8.53,"T":4.43,"W":0.8,"Y":2.54,"V":5.44}
{"AccNo":"NAKH920102","PropDesc":"AA composition of CYT2 of single-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":10.88,"R":6.01,"N":5.75,"D":6.13,"C":0.69,"E":9.34,"Q":4.68,"G":7.72,"H":2.15,"I":1.8,"L":8.03,"K":6.11,"M":3.79,"F":2.93,"P":7.21,"S":7.25,"T":3.51,"W":0.47,"Y":1.01,"V":4.57}
{"AccNo":"NAKH920103","PropDesc":"AA composition of EXT of single-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":5.15,"R":4.38,"N":4.81,"D":5.75,"C":3.24,"E":7.05,"Q":4.45,"G":6.38,"H":2.69,"I":4.4,"L":8.11,"K":5.25,"M":1.6,"F":3.52,"P":5.65,"S":8.04,"T":7.41,"W":1.68,"Y":3.42,"V":7}
{"AccNo":"NAKH920104","PropDesc":"AA composition of EXT2 of single-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":5.04,"R":3.73,"N":5.94,"D":5.26,"C":2.2,"E":6.07,"Q":4.5,"G":7.09,"H":2.99,"I":4.32,"L":9.88,"K":6.31,"M":1.85,"F":3.72,"P":6.22,"S":8.05,"T":5.2,"W":2.1,"Y":3.32,"V":6.19}
{"AccNo":"NAKH920105","PropDesc":"AA composition of MEM of single-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":9.9,"R":0.09,"N":0.94,"D":0.35,"C":2.55,"E":0.08,"Q":0.87,"G":8.14,"H":0.2,"I":15.25,"L":22.28,"K":0.16,"M":1.85,"F":6.47,"P":2.38,"S":4.17,"T":4.33,"W":2.21,"Y":3.42,"V":14.34}
{"AccNo":"NAKH920106","PropDesc":"AA composition of CYT of multi-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":6.69,"R":6.65,"N":4.49,"D":4.97,"C":1.7,"E":7.76,"Q":5.39,"G":6.32,"H":2.11,"I":4.51,"L":8.23,"K":8.36,"M":2.46,"F":3.59,"P":5.2,"S":7.4,"T":5.18,"W":1.06,"Y":2.75,"V":5.27}
{"AccNo":"NAKH920107","PropDesc":"AA composition of EXT of multi-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":5.08,"R":4.75,"N":5.75,"D":5.96,"C":2.95,"E":6.04,"Q":4.24,"G":8.2,"H":2.1,"I":4.95,"L":8.03,"K":4.93,"M":2.61,"F":4.36,"P":4.84,"S":6.41,"T":5.87,"W":2.31,"Y":4.55,"V":6.07}
{"AccNo":"NAKH920108","PropDesc":"AA composition of MEM of multi-spanning proteins (Nakashima-Nishikawa, 1992)","LITDBNo":"LIT:1811095b PMID:1607012","Author":"Nakashima, H. and Nishikawa, K.","ArtTitle":"The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins","JournalRef":"FEBS Lett. 303, 141-146 (1992)","A":9.36,"R":0.27,"N":2.31,"D":0.94,"C":2.56,"E":0.94,"Q":1.14,"G":6.17,"H":0.47,"I":13.73,"L":16.64,"K":0.58,"M":3.93,"F":10.99,"P":1.96,"S":5.58,"T":4.68,"W":2.2,"Y":3.13,"V":12.43}
{"AccNo":"NISK800101","PropDesc":"8 A contact number (Nishikawa-Ooi, 1980)","LITDBNo":"LIT:2004068b PMID:7440060","Author":"Nishikawa, K. and Ooi, T.","ArtTitle":"Prediction of the surface-interior diagram of globular proteins by an empirical method","JournalRef":"Int. J. Peptide Protein Res. 16, 19-32 (1980)","A":0.23,"R":-0.26,"N":-0.94,"D":-1.13,"C":1.78,"E":-0.75,"Q":-0.57,"G":-0.07,"H":0.11,"I":1.19,"L":1.03,"K":-1.05,"M":0.66,"F":0.48,"P":-0.76,"S":-0.67,"T":-0.36,"W":0.9,"Y":0.59,"V":1.24}
{"AccNo":"NISK860101","PropDesc":"14 A contact number (Nishikawa-Ooi, 1986)","LITDBNo":"LIT:1211490 PMID:3818558","Author":"Nishikawa, K. and Ooi, T.","ArtTitle":"Radial locations of amino acid residues in a globular protein: Correlation with the sequence","JournalRef":"J. Biochem. 100, 1043-1047 (1986) Values supplied by the author","A":-0.22,"R":-0.93,"N":-2.65,"D":-4.12,"C":4.66,"E":-3.64,"Q":-2.76,"G":-1.62,"H":1.28,"I":5.58,"L":5.01,"K":-4.18,"M":3.51,"F":5.27,"P":-3.03,"S":-2.84,"T":-1.2,"W":5.2,"Y":2.15,"V":4.45}
{"AccNo":"NOZY710101","PropDesc":"Transfer energy, organic solvent/water (Nozaki-Tanford, 1971)","LITDBNo":"PMID:5555568","Author":"Nozaki, Y. and Tanford, C.","ArtTitle":"The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions","JournalRef":"J. Biol. Chem. 246, 2211-2217 (1971) Missing values filled with zeros","A":0.5,"R":0,"N":0,"D":0,"C":0,"E":0,"Q":0,"G":0,"H":0.5,"I":1.8,"L":1.8,"K":0,"M":1.3,"F":2.5,"P":0,"S":0,"T":0.4,"W":3.4,"Y":2.3,"V":1.5}
{"AccNo":"OOBM770101","PropDesc":"Average non-bonded energy per atom (Oobatake-Ooi, 1977)","LITDBNo":"LIT:2004111b PMID:904331","Author":"Oobatake, M. and Ooi, T.","ArtTitle":"An analysis of non-bonded energy of proteins","JournalRef":"J. Theor. Biol. 67, 567-584 (1977) Last two calcualted by Kidera; multiplied by the number of heavy atoms","A":-1.895,"R":-1.475,"N":-1.56,"D":-1.518,"C":-2.035,"E":-1.535,"Q":-1.521,"G":-1.898,"H":-1.755,"I":-1.951,"L":-1.966,"K":-1.374,"M":-1.963,"F":-1.864,"P":-1.699,"S":-1.753,"T":-1.767,"W":-1.869,"Y":-1.686,"V":-1.981}
{"AccNo":"OOBM770102","PropDesc":"Short and medium range non-bonded energy per atom (Oobatake-Ooi, 1977)","LITDBNo":"LIT:2004111b PMID:904331","Author":"Oobatake, M. and Ooi, T.","ArtTitle":"An analysis of non-bonded energy of proteins","JournalRef":"J. Theor. Biol. 67, 567-584 (1977) Last two calcualted by Kidera; multiplied by the number of heavy atoms","A":-1.404,"R":-0.921,"N":-1.178,"D":-1.162,"C":-1.365,"E":-1.163,"Q":-1.116,"G":-1.364,"H":-1.215,"I":-1.189,"L":-1.315,"K":-1.074,"M":-1.303,"F":-1.135,"P":-1.236,"S":-1.297,"T":-1.252,"W":-1.03,"Y":-1.03,"V":-1.254}
{"AccNo":"OOBM770103","PropDesc":"Long range non-bonded energy per atom (Oobatake-Ooi, 1977)","LITDBNo":"LIT:2004111b PMID:904331","Author":"Oobatake, M. and Ooi, T.","ArtTitle":"An analysis of non-bonded energy of proteins","JournalRef":"J. Theor. Biol. 67, 567-584 (1977) Last two calcualted by Kidera; multiplied by the number of heavy atoms","A":-0.491,"R":-0.554,"N":-0.382,"D":-0.356,"C":-0.67,"E":-0.371,"Q":-0.405,"G":-0.534,"H":-0.54,"I":-0.762,"L":-0.65,"K":-0.3,"M":-0.659,"F":-0.729,"P":-0.463,"S":-0.455,"T":-0.515,"W":-0.839,"Y":-0.656,"V":-0.728}
{"AccNo":"OOBM770104","PropDesc":"Average non-bonded energy per residue (Oobatake-Ooi, 1977)","LITDBNo":"LIT:2004111b PMID:904331","Author":"Oobatake, M. and Ooi, T.","ArtTitle":"An analysis of non-bonded energy of proteins","JournalRef":"J. Theor. Biol. 67, 567-584 (1977) Last two calcualted by Kidera; multiplied by the number of heavy atoms","A":-9.475,"R":-16.225,"N":-12.48,"D":-12.144,"C":-12.21,"E":-13.815,"Q":-13.689,"G":-7.592,"H":-17.55,"I":-15.608,"L":-15.728,"K":-12.366,"M":-15.704,"F":-20.504,"P":-11.893,"S":-10.518,"T":-12.369,"W":-26.166,"Y":-20.232,"V":-13.867}
{"AccNo":"OOBM770105","PropDesc":"Short and medium range non-bonded energy per residue (Oobatake-Ooi, 1977)","LITDBNo":"LIT:2004111b PMID:904331","Author":"Oobatake, M. and Ooi, T.","ArtTitle":"An analysis of non-bonded energy of proteins","JournalRef":"J. Theor. Biol. 67, 567-584 (1977) Last two calcualted by Kidera; multiplied by the number of heavy atoms","A":-7.02,"R":-10.131,"N":-9.424,"D":-9.296,"C":-8.19,"E":-10.467,"Q":-10.044,"G":-5.456,"H":-12.15,"I":-9.512,"L":-10.52,"K":-9.666,"M":-10.424,"F":-12.485,"P":-8.652,"S":-7.782,"T":-8.764,"W":-14.42,"Y":-12.36,"V":-8.778}
{"AccNo":"OOBM850101","PropDesc":"Optimized beta-structure-coil equilibrium constant (Oobatake et al., 1985)","LITDBNo":"LIT:1207075b","Author":"Oobatake, M., Kubota, Y. and Ooi, T.","ArtTitle":"Optimization of amino acid parameters for correspondence of sequence to tertiary structures of proteuins","JournalRef":"Bull. Inst. Chem. Res., Kyoto Univ. 63, 82-94 (1985)","A":2.01,"R":0.84,"N":0.03,"D":-2.05,"C":1.98,"E":0.93,"Q":1.02,"G":0.12,"H":-0.14,"I":3.7,"L":2.73,"K":2.55,"M":1.75,"F":2.68,"P":0.41,"S":1.47,"T":2.39,"W":2.49,"Y":2.23,"V":3.5}
{"AccNo":"OOBM850102","PropDesc":"Optimized propensity to form reverse turn (Oobatake et al., 1985)","LITDBNo":"LIT:1207075b","Author":"Oobatake, M., Kubota, Y. and Ooi, T.","ArtTitle":"Optimization of amino acid parameters for correspondence of sequence to tertiary structures of proteuins","JournalRef":"Bull. Inst. Chem. Res., Kyoto Univ. 63, 82-94 (1985)","A":1.34,"R":0.95,"N":2.49,"D":3.32,"C":1.07,"E":2.2,"Q":1.49,"G":2.07,"H":1.27,"I":0.66,"L":0.54,"K":0.61,"M":0.7,"F":0.8,"P":2.12,"S":0.94,"T":1.09,"W":-4.65,"Y":-0.17,"V":1.32}
{"AccNo":"OOBM850103","PropDesc":"Optimized transfer energy parameter (Oobatake et al., 1985)","LITDBNo":"LIT:1207075b","Author":"Oobatake, M., Kubota, Y. and Ooi, T.","ArtTitle":"Optimization of amino acid parameters for correspondence of sequence to tertiary structures of proteuins","JournalRef":"Bull. Inst. Chem. Res., Kyoto Univ. 63, 82-94 (1985)","A":0.46,"R":-1.54,"N":1.31,"D":-0.33,"C":0.2,"E":0.48,"Q":-1.12,"G":0.64,"H":-1.31,"I":3.28,"L":0.43,"K":-1.71,"M":0.15,"F":0.52,"P":-0.58,"S":-0.83,"T":-1.52,"W":1.25,"Y":-2.21,"V":0.54}
{"AccNo":"OOBM850104","PropDesc":"Optimized average non-bonded energy per atom (Oobatake et al., 1985)","LITDBNo":"LIT:1207075b","Author":"Oobatake, M., Kubota, Y. and Ooi, T.","ArtTitle":"Optimization of amino acid parameters for correspondence of sequence to tertiary structures of proteuins","JournalRef":"Bull. Inst. Chem. Res., Kyoto Univ. 63, 82-94 (1985)","A":-2.49,"R":2.55,"N":2.27,"D":8.86,"C":-3.13,"E":4.04,"Q":1.79,"G":-0.56,"H":4.22,"I":-10.87,"L":-7.16,"K":-9.97,"M":-4.96,"F":-6.64,"P":5.19,"S":-1.6,"T":-4.75,"W":-17.84,"Y":9.25,"V":-3.97}
{"AccNo":"OOBM850105","PropDesc":"Optimized side chain interaction parameter (Oobatake et al., 1985)","LITDBNo":"LIT:1207075b","Author":"Oobatake, M., Kubota, Y. and Ooi, T.","ArtTitle":"Optimization of amino acid parameters for correspondence of sequence to tertiary structures of proteuins","JournalRef":"Bull. Inst. Chem. Res., Kyoto Univ. 63, 82-94 (1985)","A":4.55,"R":5.97,"N":5.56,"D":2.85,"C":-0.78,"E":5.16,"Q":4.15,"G":9.14,"H":4.48,"I":2.1,"L":3.24,"K":10.68,"M":2.18,"F":4.37,"P":5.14,"S":6.78,"T":8.6,"W":1.97,"Y":2.4,"V":3.81}
{"AccNo":"PALJ810101","PropDesc":"Normalized frequency of alpha-helix from LG (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":1.3,"R":0.93,"N":0.9,"D":1.02,"C":0.92,"E":1.43,"Q":1.04,"G":0.63,"H":1.33,"I":0.87,"L":1.3,"K":1.23,"M":1.32,"F":1.09,"P":0.63,"S":0.78,"T":0.8,"W":1.03,"Y":0.71,"V":0.95}
{"AccNo":"PALJ810102","PropDesc":"Normalized frequency of alpha-helix from CF (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":1.32,"R":1.04,"N":0.74,"D":0.97,"C":0.7,"E":1.48,"Q":1.25,"G":0.59,"H":1.06,"I":1.01,"L":1.22,"K":1.13,"M":1.47,"F":1.1,"P":0.57,"S":0.77,"T":0.86,"W":1.02,"Y":0.72,"V":1.05}
{"AccNo":"PALJ810103","PropDesc":"Normalized frequency of beta-sheet from LG (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.81,"R":1.03,"N":0.81,"D":0.71,"C":1.12,"E":0.59,"Q":1.03,"G":0.94,"H":0.85,"I":1.47,"L":1.03,"K":0.77,"M":0.96,"F":1.13,"P":0.75,"S":1.02,"T":1.19,"W":1.24,"Y":1.35,"V":1.44}
{"AccNo":"PALJ810104","PropDesc":"Normalized frequency of beta-sheet from CF (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.9,"R":0.75,"N":0.82,"D":0.75,"C":1.12,"E":0.44,"Q":0.95,"G":0.83,"H":0.86,"I":1.59,"L":1.24,"K":0.75,"M":0.94,"F":1.41,"P":0.46,"S":0.7,"T":1.2,"W":1.28,"Y":1.45,"V":1.73}
{"AccNo":"PALJ810105","PropDesc":"Normalized frequency of turn from LG (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.84,"R":0.91,"N":1.48,"D":1.28,"C":0.69,"E":0.78,"Q":1,"G":1.76,"H":0.53,"I":0.55,"L":0.49,"K":0.95,"M":0.52,"F":0.88,"P":1.47,"S":1.29,"T":1.05,"W":0.88,"Y":1.28,"V":0.51}
{"AccNo":"PALJ810106","PropDesc":"Normalized frequency of turn from CF (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.65,"R":0.93,"N":1.45,"D":1.47,"C":1.43,"E":0.75,"Q":0.94,"G":1.53,"H":0.96,"I":0.57,"L":0.56,"K":0.95,"M":0.71,"F":0.72,"P":1.51,"S":1.46,"T":0.96,"W":0.9,"Y":1.12,"V":0.55}
{"AccNo":"PALJ810107","PropDesc":"Normalized frequency of alpha-helix in all-alpha class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":1.08,"R":0.93,"N":1.05,"D":0.86,"C":1.22,"E":1.09,"Q":0.95,"G":0.85,"H":1.02,"I":0.98,"L":1.04,"K":1.01,"M":1.11,"F":0.96,"P":0.91,"S":0.95,"T":1.15,"W":1.17,"Y":0.8,"V":1.03}
{"AccNo":"PALJ810108","PropDesc":"Normalized frequency of alpha-helix in alpha+beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":1.34,"R":0.91,"N":0.83,"D":1.06,"C":1.27,"E":1.69,"Q":1.13,"G":0.47,"H":1.11,"I":0.84,"L":1.39,"K":1.08,"M":0.9,"F":1.02,"P":0.48,"S":1.05,"T":0.74,"W":0.64,"Y":0.73,"V":1.18}
{"AccNo":"PALJ810109","PropDesc":"Normalized frequency of alpha-helix in alpha/beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":1.15,"R":1.06,"N":0.87,"D":1,"C":1.03,"E":1.37,"Q":1.43,"G":0.64,"H":0.95,"I":0.99,"L":1.22,"K":1.2,"M":1.45,"F":0.92,"P":0.72,"S":0.84,"T":0.97,"W":1.11,"Y":0.72,"V":0.82}
{"AccNo":"PALJ810110","PropDesc":"Normalized frequency of beta-sheet in all-beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.89,"R":1.06,"N":0.67,"D":0.71,"C":1.04,"E":0.72,"Q":1.06,"G":0.87,"H":1.04,"I":1.14,"L":1.02,"K":1,"M":1.41,"F":1.32,"P":0.69,"S":0.86,"T":1.15,"W":1.06,"Y":1.35,"V":1.66}
{"AccNo":"PALJ810111","PropDesc":"Normalized frequency of beta-sheet in alpha+beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.82,"R":0.99,"N":1.27,"D":0.98,"C":0.71,"E":0.54,"Q":1.01,"G":0.94,"H":1.26,"I":1.67,"L":0.94,"K":0.73,"M":1.3,"F":1.56,"P":0.69,"S":0.65,"T":0.98,"W":1.25,"Y":1.26,"V":1.22}
{"AccNo":"PALJ810112","PropDesc":"Normalized frequency of beta-sheet in alpha/beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.98,"R":1.03,"N":0.66,"D":0.74,"C":1.01,"E":0.59,"Q":0.63,"G":0.9,"H":1.17,"I":1.38,"L":1.05,"K":0.83,"M":0.82,"F":1.23,"P":0.73,"S":0.98,"T":1.2,"W":1.26,"Y":1.23,"V":1.62}
{"AccNo":"PALJ810113","PropDesc":"Normalized frequency of turn in all-alpha class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins. (Arg Cys Leu Trp missing)","A":0.69,"R":0,"N":1.52,"D":2.42,"C":0,"E":0.63,"Q":1.44,"G":2.64,"H":0.22,"I":0.43,"L":0,"K":1.18,"M":0.88,"F":2.2,"P":1.34,"S":1.43,"T":0.28,"W":0,"Y":1.53,"V":0.14}
{"AccNo":"PALJ810114","PropDesc":"Normalized frequency of turn in all-beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins. (Met missing)","A":0.87,"R":1.3,"N":1.36,"D":1.24,"C":0.83,"E":0.91,"Q":1.06,"G":1.69,"H":0.91,"I":0.27,"L":0.67,"K":0.66,"M":0,"F":0.47,"P":1.54,"S":1.08,"T":1.12,"W":1.24,"Y":0.54,"V":0.69}
{"AccNo":"PALJ810115","PropDesc":"Normalized frequency of turn in alpha+beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.91,"R":0.77,"N":1.32,"D":0.9,"C":0.5,"E":0.53,"Q":1.06,"G":1.61,"H":1.08,"I":0.36,"L":0.77,"K":1.27,"M":0.76,"F":0.37,"P":1.62,"S":1.34,"T":0.87,"W":1.1,"Y":1.24,"V":0.52}
{"AccNo":"PALJ810116","PropDesc":"Normalized frequency of turn in alpha/beta class (Palau et al., 1981)","LITDBNo":"LIT:0805095 PMID:7118409","Author":"Palau, J., Argos, P. and Puigdomenech, P.","ArtTitle":"Protein secondary structure","JournalRef":"Int. J. Peptide Protein Res. 19, 394-401 (1981) LG :a set of protein samples formed by 44 proteins. CF :a set of protein samples formed by 33 proteins.","A":0.92,"R":0.9,"N":1.57,"D":1.22,"C":0.62,"E":0.92,"Q":0.66,"G":1.61,"H":0.39,"I":0.79,"L":0.5,"K":0.86,"M":0.5,"F":0.96,"P":1.3,"S":1.4,"T":1.11,"W":0.57,"Y":1.78,"V":0.5}
{"AccNo":"PARJ860101","PropDesc":"HPLC parameter (Parker et al., 1986)","LITDBNo":"LIT:1211071 PMID:2430611","Author":"Parker, J.M.R., Guo, D. and Hodges, R.S.","ArtTitle":"New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: Correlation of predicted surface residues with antigencity and x-ray-derived accessible sites","JournalRef":"Biochemistry 25, 5425-5432 (1986)","A":2.1,"R":4.2,"N":7,"D":10,"C":1.4,"E":7.8,"Q":6,"G":5.7,"H":2.1,"I":-8,"L":-9.2,"K":5.7,"M":-4.2,"F":-9.2,"P":2.1,"S":6.5,"T":5.2,"W":-10,"Y":-1.9,"V":-3.7}
{"AccNo":"PLIV810101","PropDesc":"Partition coefficient (Pliska et al., 1981)","LITDBNo":"LIT:0712223","Author":"Pliska, V., Schmidt, M. and Fauchere, J.L.","ArtTitle":"Partition coefficients of amino acids and hydrophobic parameters pi of their side-chains as measured by thin-layer chromatography","JournalRef":"J. Chromatogr. 216, 79-92 (1981) (Arg 0.25)","A":-2.89,"R":-3.3,"N":-3.41,"D":-3.38,"C":-2.49,"E":-2.94,"Q":-3.15,"G":-3.25,"H":-2.84,"I":-1.72,"L":-1.61,"K":-3.31,"M":-1.84,"F":-1.63,"P":-2.5,"S":-3.3,"T":-2.91,"W":-1.75,"Y":-2.42,"V":-2.08}
{"AccNo":"PONP800101","PropDesc":"Surrounding hydrophobicity in folded form (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":12.28,"R":11.49,"N":11,"D":10.97,"C":14.93,"E":11.19,"Q":11.28,"G":12.01,"H":12.84,"I":14.77,"L":14.1,"K":10.8,"M":14.33,"F":13.43,"P":11.19,"S":11.26,"T":11.65,"W":12.95,"Y":13.29,"V":15.07}
{"AccNo":"PONP800102","PropDesc":"Average gain in surrounding hydrophobicity (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":7.62,"R":6.81,"N":6.17,"D":6.18,"C":10.93,"E":6.38,"Q":6.67,"G":7.31,"H":7.85,"I":9.99,"L":9.37,"K":5.72,"M":9.83,"F":8.99,"P":6.64,"S":6.93,"T":7.08,"W":8.41,"Y":8.53,"V":10.38}
{"AccNo":"PONP800103","PropDesc":"Average gain ratio in surrounding hydrophobicity (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":2.63,"R":2.45,"N":2.27,"D":2.29,"C":3.36,"E":2.31,"Q":2.45,"G":2.55,"H":2.57,"I":3.08,"L":2.98,"K":2.12,"M":3.18,"F":3.02,"P":2.46,"S":2.6,"T":2.55,"W":2.85,"Y":2.79,"V":3.21}
{"AccNo":"PONP800104","PropDesc":"Surrounding hydrophobicity in alpha-helix (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":13.65,"R":11.28,"N":12.24,"D":10.98,"C":14.49,"E":12.55,"Q":11.3,"G":15.36,"H":11.59,"I":14.63,"L":14.01,"K":11.96,"M":13.4,"F":14.08,"P":11.51,"S":11.26,"T":13,"W":12.06,"Y":12.64,"V":12.88}
{"AccNo":"PONP800105","PropDesc":"Surrounding hydrophobicity in beta-sheet (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":14.6,"R":13.24,"N":11.79,"D":13.78,"C":15.9,"E":13.59,"Q":12.02,"G":14.18,"H":15.35,"I":14.1,"L":16.49,"K":13.28,"M":16.23,"F":14.18,"P":14.1,"S":13.36,"T":14.5,"W":13.9,"Y":14.76,"V":16.3}
{"AccNo":"PONP800106","PropDesc":"Surrounding hydrophobicity in turn (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":10.67,"R":11.05,"N":10.85,"D":10.21,"C":14.15,"E":11.71,"Q":11.71,"G":10.95,"H":12.07,"I":12.95,"L":13.07,"K":9.93,"M":15,"F":13.27,"P":10.62,"S":11.18,"T":10.53,"W":11.41,"Y":11.52,"V":13.86}
{"AccNo":"PONP800107","PropDesc":"Accessibility reduction ratio (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":3.7,"R":2.53,"N":2.12,"D":2.6,"C":3.03,"E":3.3,"Q":2.7,"G":3.13,"H":3.57,"I":7.69,"L":5.88,"K":1.79,"M":5.21,"F":6.6,"P":2.12,"S":2.43,"T":2.6,"W":6.25,"Y":3.03,"V":7.14}
{"AccNo":"PONP800108","PropDesc":"Average number of surrounding residues (Ponnuswamy et al., 1980)","LITDBNo":"LIT:0608056 PMID:7397216","Author":"Ponnuswamy, P.K., Prabhakaran, M. and Manavalan, P.","ArtTitle":"Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins","JournalRef":"Biochim. Biophys. Acta 623, 301-316 (1980)","A":6.05,"R":5.7,"N":5.04,"D":4.95,"C":7.86,"E":5.1,"Q":5.45,"G":6.16,"H":5.8,"I":7.51,"L":7.37,"K":4.88,"M":6.39,"F":6.62,"P":5.65,"S":5.53,"T":5.81,"W":6.98,"Y":6.73,"V":7.62}
{"AccNo":"PRAM820101","PropDesc":"Intercept in regression analysis (Prabhakaran-Ponnuswamy, 1982)","LITDBNo":"LIT:2004113b","Author":"Prabhakaran, M. and Ponnuswamy, P.K.","ArtTitle":"Shape and surface features of globular proteins","JournalRef":"Macromolecules 15, 314-320 (1982) Regression analysis of solvent contact area and spatial position","A":0.305,"R":0.227,"N":0.322,"D":0.335,"C":0.339,"E":0.282,"Q":0.306,"G":0.352,"H":0.215,"I":0.278,"L":0.262,"K":0.391,"M":0.28,"F":0.195,"P":0.346,"S":0.326,"T":0.251,"W":0.291,"Y":0.293,"V":0.291}
{"AccNo":"PRAM820102","PropDesc":"Slope in regression analysis x 1.0E1 (Prabhakaran-Ponnuswamy, 1982)","LITDBNo":"LIT:2004113b","Author":"Prabhakaran, M. and Ponnuswamy, P.K.","ArtTitle":"Shape and surface features of globular proteins","JournalRef":"Macromolecules 15, 314-320 (1982) Regression analysis of solvent contact area and spatial position","A":0.175,"R":0.083,"N":0.09,"D":0.14,"C":0.074,"E":0.135,"Q":0.093,"G":0.201,"H":0.125,"I":0.1,"L":0.104,"K":0.058,"M":0.054,"F":0.104,"P":0.136,"S":0.155,"T":0.152,"W":0.092,"Y":0.081,"V":0.096}
{"AccNo":"PRAM820103","PropDesc":"Correlation coefficient in regression analysis (Prabhakaran-Ponnuswamy, 1982)","LITDBNo":"LIT:2004113b","Author":"Prabhakaran, M. and Ponnuswamy, P.K.","ArtTitle":"Shape and surface features of globular proteins","JournalRef":"Macromolecules 15, 314-320 (1982) Regression analysis of solvent contact area and spatial position","A":0.687,"R":0.59,"N":0.489,"D":0.632,"C":0.263,"E":0.669,"Q":0.527,"G":0.67,"H":0.594,"I":0.564,"L":0.541,"K":0.407,"M":0.328,"F":0.577,"P":0.6,"S":0.692,"T":0.713,"W":0.632,"Y":0.495,"V":0.529}
{"AccNo":"PRAM900101","PropDesc":"Hydrophobicity (Prabhakaran, 1990)","LITDBNo":"LIT:1614053b PMID:2390062","Author":"Prabhakaran, M.","ArtTitle":"The distribution of physical, chemical and conformational properties in signal and nascent peptides","JournalRef":"Biochem. J. 269, 691-696 (1990) Original references: Engelman, D.M., Steitz, T.A. and Terwilliger, T.C. Annu. Rev. Biophys. Chem. 15, 321-353 (1986)","A":-6.7,"R":51.5,"N":20.1,"D":38.5,"C":-8.4,"E":34.3,"Q":17.2,"G":-4.2,"H":12.6,"I":-13,"L":-11.7,"K":36.8,"M":-14.2,"F":-15.5,"P":0.8,"S":-2.5,"T":-5,"W":-7.9,"Y":2.9,"V":-10.9}
{"AccNo":"PRAM900102","PropDesc":"Relative frequency in alpha-helix (Prabhakaran, 1990)","LITDBNo":"LIT:1614053b PMID:2390062","Author":"Prabhakaran, M.","ArtTitle":"The distribution of physical, chemical and conformational properties in signal and nascent peptides","JournalRef":"Biochem. J. 269, 691-696 (1990) Original reference of these three data: Creighton, T.E. In \"Protein Structure and Melecular Properties\", (Freeman, W.H., ed.), San Francisco P.235 (1983)","A":1.29,"R":0.96,"N":0.9,"D":1.04,"C":1.11,"E":1.44,"Q":1.27,"G":0.56,"H":1.22,"I":0.97,"L":1.3,"K":1.23,"M":1.47,"F":1.07,"P":0.52,"S":0.82,"T":0.82,"W":0.99,"Y":0.72,"V":0.91}
{"AccNo":"PRAM900103","PropDesc":"Relative frequency in beta-sheet (Prabhakaran, 1990)","LITDBNo":"LIT:1614053b PMID:2390062","Author":"Prabhakaran, M.","ArtTitle":"The distribution of physical, chemical and conformational properties in signal and nascent peptides","JournalRef":"Biochem. J. 269, 691-696 (1990) Original reference of these three data: Creighton, T.E. In \"Protein Structure and Melecular Properties\", (Freeman, W.H., ed.), San Francisco P.235 (1983)","A":0.9,"R":0.99,"N":0.76,"D":0.72,"C":0.74,"E":0.75,"Q":0.8,"G":0.92,"H":1.08,"I":1.45,"L":1.02,"K":0.77,"M":0.97,"F":1.32,"P":0.64,"S":0.95,"T":1.21,"W":1.14,"Y":1.25,"V":1.49}
{"AccNo":"PRAM900104","PropDesc":"Relative frequency in reverse-turn (Prabhakaran, 1990)","LITDBNo":"LIT:1614053b PMID:2390062","Author":"Prabhakaran, M.","ArtTitle":"The distribution of physical, chemical and conformational properties in signal and nascent peptides","JournalRef":"Biochem. J. 269, 691-696 (1990) Original reference of these three data: Creighton, T.E. In \"Protein Structure and Melecular Properties\", (Freeman, W.H., ed.), San Francisco P.235 (1983)","A":0.78,"R":0.88,"N":1.28,"D":1.41,"C":0.8,"E":1,"Q":0.97,"G":1.64,"H":0.69,"I":0.51,"L":0.59,"K":0.96,"M":0.39,"F":0.58,"P":1.91,"S":1.33,"T":1.03,"W":0.75,"Y":1.05,"V":0.47}
{"AccNo":"PTIO830101","PropDesc":"Helix-coil equilibrium constant (Ptitsyn-Finkelstein, 1983)","LITDBNo":"LIT:0904057 PMID:6673754","Author":"Ptitsyn, O.B. and Finkelstein, A.V.","ArtTitle":"Theory of protein secondary structure and algorithm of its prediction","JournalRef":"Biopolymers 22, 15-25 (1983) Charged state for Arg, His, Lys, Asp, and Glu","A":1.1,"R":0.95,"N":0.8,"D":0.65,"C":0.95,"E":1,"Q":1,"G":0.6,"H":0.85,"I":1.1,"L":1.25,"K":1,"M":1.15,"F":1.1,"P":0.1,"S":0.75,"T":0.75,"W":1.1,"Y":1.1,"V":0.95}
{"AccNo":"PTIO830102","PropDesc":"Beta-coil equilibrium constant (Ptitsyn-Finkelstein, 1983)","LITDBNo":"LIT:0904057 PMID:6673754","Author":"Ptitsyn, O.B. and Finkelstein, A.V.","ArtTitle":"Theory of protein secondary structure and algorithm of its prediction","JournalRef":"Biopolymers 22, 15-25 (1983) Charged state for Arg, His, Lys, Asp, and Glu","A":1,"R":0.7,"N":0.6,"D":0.5,"C":1.9,"E":0.7,"Q":1,"G":0.3,"H":0.8,"I":4,"L":2,"K":0.7,"M":1.9,"F":3.1,"P":0.2,"S":0.9,"T":1.7,"W":2.2,"Y":2.8,"V":4}
{"AccNo":"QIAN880101","PropDesc":"Weights for alpha-helix at the window position of -6 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.12,"R":0.04,"N":-0.1,"D":0.01,"C":-0.25,"E":-0.02,"Q":-0.03,"G":-0.02,"H":-0.06,"I":-0.07,"L":0.05,"K":0.26,"M":0,"F":0.05,"P":-0.19,"S":-0.19,"T":-0.04,"W":-0.06,"Y":-0.14,"V":-0.03}
{"AccNo":"QIAN880102","PropDesc":"Weights for alpha-helix at the window position of -5 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.26,"R":-0.14,"N":-0.03,"D":0.15,"C":-0.15,"E":0.21,"Q":-0.13,"G":-0.37,"H":0.1,"I":-0.03,"L":-0.02,"K":0.12,"M":0,"F":0.12,"P":-0.08,"S":0.01,"T":-0.34,"W":-0.01,"Y":-0.29,"V":0.02}
{"AccNo":"QIAN880103","PropDesc":"Weights for alpha-helix at the window position of -4 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.64,"R":-0.1,"N":0.09,"D":0.33,"C":0.03,"E":0.51,"Q":-0.23,"G":-0.09,"H":-0.23,"I":-0.22,"L":0.41,"K":-0.17,"M":0.13,"F":-0.03,"P":-0.43,"S":-0.1,"T":-0.07,"W":-0.02,"Y":-0.38,"V":-0.01}
{"AccNo":"QIAN880104","PropDesc":"Weights for alpha-helix at the window position of -3 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.29,"R":-0.03,"N":-0.04,"D":0.11,"C":-0.05,"E":0.28,"Q":0.26,"G":-0.67,"H":-0.26,"I":0,"L":0.47,"K":-0.19,"M":0.27,"F":0.24,"P":-0.34,"S":-0.17,"T":-0.2,"W":0.25,"Y":-0.3,"V":-0.01}
{"AccNo":"QIAN880105","PropDesc":"Weights for alpha-helix at the window position of -2 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.68,"R":-0.22,"N":-0.09,"D":-0.02,"C":-0.15,"E":0.44,"Q":-0.15,"G":-0.73,"H":-0.14,"I":-0.08,"L":0.61,"K":0.03,"M":0.39,"F":0.06,"P":-0.76,"S":-0.26,"T":-0.1,"W":0.2,"Y":-0.04,"V":0.12}
{"AccNo":"QIAN880106","PropDesc":"Weights for alpha-helix at the window position of -1 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.34,"R":0.22,"N":-0.33,"D":0.06,"C":-0.18,"E":0.2,"Q":0.01,"G":-0.88,"H":-0.09,"I":-0.03,"L":0.2,"K":-0.11,"M":0.43,"F":0.15,"P":-0.81,"S":-0.35,"T":-0.37,"W":0.07,"Y":-0.31,"V":0.13}
{"AccNo":"QIAN880107","PropDesc":"Weights for alpha-helix at the window position of 0 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.57,"R":0.23,"N":-0.36,"D":-0.46,"C":-0.15,"E":0.26,"Q":0.15,"G":-0.71,"H":-0.05,"I":0,"L":0.48,"K":0.16,"M":0.41,"F":0.03,"P":-1.12,"S":-0.47,"T":-0.54,"W":-0.1,"Y":-0.35,"V":0.31}
{"AccNo":"QIAN880108","PropDesc":"Weights for alpha-helix at the window position of 1 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.33,"R":0.1,"N":-0.19,"D":-0.44,"C":-0.03,"E":0.21,"Q":0.19,"G":-0.46,"H":0.27,"I":-0.33,"L":0.57,"K":0.23,"M":0.79,"F":0.48,"P":-1.86,"S":-0.23,"T":-0.33,"W":0.15,"Y":-0.19,"V":0.24}
{"AccNo":"QIAN880109","PropDesc":"Weights for alpha-helix at the window position of 2 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.13,"R":0.08,"N":-0.07,"D":-0.71,"C":-0.09,"E":0.13,"Q":0.12,"G":-0.39,"H":0.32,"I":0,"L":0.5,"K":0.37,"M":0.63,"F":0.15,"P":-1.4,"S":-0.28,"T":-0.21,"W":0.02,"Y":-0.1,"V":0.17}
{"AccNo":"QIAN880110","PropDesc":"Weights for alpha-helix at the window position of 3 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.31,"R":0.18,"N":-0.1,"D":-0.81,"C":-0.26,"E":-0.06,"Q":0.41,"G":-0.42,"H":0.51,"I":-0.15,"L":0.56,"K":0.47,"M":0.58,"F":0.1,"P":-1.33,"S":-0.49,"T":-0.44,"W":0.14,"Y":-0.08,"V":-0.01}
{"AccNo":"QIAN880111","PropDesc":"Weights for alpha-helix at the window position of 4 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.21,"R":0.07,"N":-0.04,"D":-0.58,"C":-0.12,"E":-0.23,"Q":0.13,"G":-0.15,"H":0.37,"I":0.31,"L":0.7,"K":0.28,"M":0.61,"F":-0.06,"P":-1.03,"S":-0.28,"T":-0.25,"W":0.21,"Y":0.16,"V":0}
{"AccNo":"QIAN880112","PropDesc":"Weights for alpha-helix at the window position of 5 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.18,"R":0.21,"N":-0.03,"D":-0.32,"C":-0.29,"E":-0.25,"Q":-0.27,"G":-0.4,"H":0.28,"I":-0.03,"L":0.62,"K":0.41,"M":0.21,"F":0.05,"P":-0.84,"S":-0.05,"T":-0.16,"W":0.32,"Y":0.11,"V":0.06}
{"AccNo":"QIAN880113","PropDesc":"Weights for alpha-helix at the window position of 6 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":-0.08,"R":0.05,"N":-0.08,"D":-0.24,"C":-0.25,"E":-0.19,"Q":-0.28,"G":-0.1,"H":0.29,"I":-0.01,"L":0.28,"K":0.45,"M":0.11,"F":0,"P":-0.42,"S":0.07,"T":-0.33,"W":0.36,"Y":0,"V":-0.13}
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{"AccNo":"QIAN880128","PropDesc":"Weights for coil at the window position of -5 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":-0.19,"R":0.17,"N":-0.38,"D":0.09,"C":0.41,"E":-0.2,"Q":0.04,"G":0.28,"H":-0.19,"I":-0.06,"L":0.34,"K":-0.2,"M":0.45,"F":0.07,"P":0.04,"S":-0.23,"T":-0.02,"W":0.16,"Y":0.22,"V":0.05}
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{"AccNo":"QIAN880133","PropDesc":"Weights for coil at the window position of 0 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":-0.42,"R":-0.23,"N":0.81,"D":0.95,"C":-0.18,"E":-0.09,"Q":-0.01,"G":1.24,"H":0.05,"I":-1.17,"L":-0.69,"K":0.09,"M":-0.86,"F":-0.39,"P":1.77,"S":0.63,"T":0.29,"W":-0.37,"Y":-0.41,"V":-1.32}
{"AccNo":"QIAN880134","PropDesc":"Weights for coil at the window position of 1 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":-0.24,"R":-0.04,"N":0.45,"D":0.65,"C":-0.38,"E":0.07,"Q":0.01,"G":0.85,"H":-0.21,"I":-0.65,"L":-0.8,"K":0.17,"M":-0.71,"F":-0.61,"P":2.27,"S":0.33,"T":0.13,"W":-0.44,"Y":-0.49,"V":-0.99}
{"AccNo":"QIAN880135","PropDesc":"Weights for coil at the window position of 2 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988) (Gin !)","A":-0.14,"R":0.21,"N":0.35,"D":0.66,"C":-0.09,"E":0.06,"Q":0.11,"G":0.36,"H":-0.31,"I":-0.51,"L":-0.8,"K":-0.14,"M":-0.56,"F":-0.25,"P":1.59,"S":0.32,"T":0.21,"W":-0.17,"Y":-0.35,"V":-0.7}
{"AccNo":"QIAN880136","PropDesc":"Weights for coil at the window position of 3 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.01,"R":-0.13,"N":-0.11,"D":0.78,"C":-0.31,"E":0.09,"Q":-0.13,"G":0.14,"H":-0.56,"I":-0.09,"L":-0.81,"K":-0.43,"M":-0.49,"F":-0.2,"P":1.14,"S":0.13,"T":-0.02,"W":-0.2,"Y":0.1,"V":-0.11}
{"AccNo":"QIAN880137","PropDesc":"Weights for coil at the window position of 4 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":-0.3,"R":-0.09,"N":-0.12,"D":0.44,"C":0.03,"E":0.18,"Q":0.24,"G":-0.12,"H":-0.2,"I":-0.07,"L":-0.18,"K":0.06,"M":-0.44,"F":0.11,"P":0.77,"S":-0.09,"T":-0.27,"W":-0.09,"Y":-0.25,"V":-0.06}
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{"AccNo":"QIAN880139","PropDesc":"Weights for coil at the window position of 6 (Qian-Sejnowski, 1988)","LITDBNo":"LIT:1411084 PMID:3172241","Author":"Qian, N. and Sejnowski, T.J.","ArtTitle":"Predicting the secondary structure of globular proteins using neural network models","JournalRef":"J. Mol. Biol. 202, 865-884 (1988)","A":0.08,"R":-0.01,"N":-0.06,"D":0.04,"C":0.37,"E":0.36,"Q":0.48,"G":-0.02,"H":-0.45,"I":0.09,"L":0.24,"K":-0.27,"M":0.16,"F":0.34,"P":0.16,"S":-0.35,"T":-0.04,"W":-0.06,"Y":-0.2,"V":0.18}
{"AccNo":"RACS770101","PropDesc":"Average reduced distance for C-alpha (Rackovsky-Scheraga, 1977)","LITDBNo":"LIT:2004126b PMID:271950","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Hydrophobicity, hydrophilicity, and the radial and orientational distributions of residues in native proteins","JournalRef":"Proc. Natl. Acad. Sci. USA 74, 5248-5251 (1977)","A":0.934,"R":0.962,"N":0.986,"D":0.994,"C":0.9,"E":0.986,"Q":1.047,"G":1.015,"H":0.882,"I":0.766,"L":0.825,"K":1.04,"M":0.804,"F":0.773,"P":1.047,"S":1.056,"T":1.008,"W":0.848,"Y":0.931,"V":0.825}
{"AccNo":"RACS770102","PropDesc":"Average reduced distance for side chain (Rackovsky-Scheraga, 1977)","LITDBNo":"LIT:2004126b PMID:271950","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Hydrophobicity, hydrophilicity, and the radial and orientational distributions of residues in native proteins","JournalRef":"Proc. Natl. Acad. Sci. USA 74, 5248-5251 (1977) (Gly 0.080)","A":0.941,"R":1.112,"N":1.038,"D":1.071,"C":0.866,"E":1.1,"Q":1.15,"G":1.055,"H":0.911,"I":0.742,"L":0.798,"K":1.232,"M":0.781,"F":0.723,"P":1.093,"S":1.082,"T":1.043,"W":0.867,"Y":1.05,"V":0.817}
{"AccNo":"RACS770103","PropDesc":"Side chain orientational preference (Rackovsky-Scheraga, 1977)","LITDBNo":"LIT:2004126b PMID:271950","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Hydrophobicity, hydrophilicity, and the radial and orientational distributions of residues in native proteins","JournalRef":"Proc. Natl. Acad. Sci. USA 74, 5248-5251 (1977) (Gly !) (Ratio of the numbers of occurrences in two orientations)","A":1.16,"R":1.72,"N":1.97,"D":2.66,"C":0.5,"E":2.4,"Q":3.87,"G":1.63,"H":0.86,"I":0.57,"L":0.51,"K":3.9,"M":0.4,"F":0.43,"P":2.04,"S":1.61,"T":1.48,"W":0.75,"Y":1.72,"V":0.59}
{"AccNo":"RACS820101","PropDesc":"Average relative fractional occurrence in A0(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.85,"R":2.02,"N":0.88,"D":1.5,"C":0.9,"E":1.79,"Q":1.71,"G":1.54,"H":1.59,"I":0.67,"L":1.03,"K":0.88,"M":1.17,"F":0.85,"P":1.47,"S":1.5,"T":1.96,"W":0.83,"Y":1.34,"V":0.89}
{"AccNo":"RACS820102","PropDesc":"Average relative fractional occurrence in AR(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":1.58,"R":1.14,"N":0.77,"D":0.98,"C":1.04,"E":1.49,"Q":1.24,"G":0.66,"H":0.99,"I":1.09,"L":1.21,"K":1.27,"M":1.41,"F":1,"P":1.46,"S":1.05,"T":0.87,"W":1.23,"Y":0.68,"V":0.88}
{"AccNo":"RACS820103","PropDesc":"Average relative fractional occurrence in AL(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.82,"R":2.6,"N":2.07,"D":2.64,"C":0,"E":2.62,"Q":0,"G":1.63,"H":0,"I":2.32,"L":0,"K":2.86,"M":0,"F":0,"P":0,"S":1.23,"T":2.48,"W":0,"Y":1.9,"V":1.62}
{"AccNo":"RACS820104","PropDesc":"Average relative fractional occurrence in EL(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.78,"R":1.75,"N":1.32,"D":1.25,"C":3.14,"E":0.94,"Q":0.93,"G":1.13,"H":1.03,"I":1.26,"L":0.91,"K":0.85,"M":0.41,"F":1.07,"P":1.73,"S":1.31,"T":1.57,"W":0.98,"Y":1.31,"V":1.11}
{"AccNo":"RACS820105","PropDesc":"Average relative fractional occurrence in E0(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.88,"R":0.99,"N":1.02,"D":1.16,"C":1.14,"E":1.01,"Q":0.93,"G":0.7,"H":1.87,"I":1.61,"L":1.09,"K":0.83,"M":1.71,"F":1.52,"P":0.87,"S":1.14,"T":0.96,"W":1.96,"Y":1.68,"V":1.56}
{"AccNo":"RACS820106","PropDesc":"Average relative fractional occurrence in ER(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.3,"R":0.9,"N":2.73,"D":1.26,"C":0.72,"E":1.33,"Q":0.97,"G":3.09,"H":1.33,"I":0.45,"L":0.96,"K":0.71,"M":1.89,"F":1.2,"P":0.83,"S":1.16,"T":0.97,"W":1.58,"Y":0.86,"V":0.64}
{"AccNo":"RACS820107","PropDesc":"Average relative fractional occurrence in A0(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.4,"R":1.2,"N":1.24,"D":1.59,"C":2.98,"E":1.26,"Q":0.5,"G":1.89,"H":2.71,"I":1.31,"L":0.57,"K":0.87,"M":0,"F":1.27,"P":0.38,"S":0.92,"T":1.38,"W":1.53,"Y":1.79,"V":0.95}
{"AccNo":"RACS820108","PropDesc":"Average relative fractional occurrence in AR(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":1.48,"R":1.02,"N":0.99,"D":1.19,"C":0.86,"E":1.43,"Q":1.42,"G":0.46,"H":1.27,"I":1.12,"L":1.33,"K":1.36,"M":1.41,"F":1.3,"P":0.25,"S":0.89,"T":0.81,"W":1.27,"Y":0.91,"V":0.93}
{"AccNo":"RACS820109","PropDesc":"Average relative fractional occurrence in AL(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0,"R":0,"N":4.14,"D":2.15,"C":0,"E":0,"Q":0,"G":6.49,"H":0,"I":0,"L":0,"K":0,"M":0,"F":2.11,"P":1.99,"S":0,"T":1.24,"W":0,"Y":1.9,"V":0}
{"AccNo":"RACS820110","PropDesc":"Average relative fractional occurrence in EL(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":1.02,"R":1,"N":1.31,"D":1.76,"C":1.05,"E":0.83,"Q":1.05,"G":2.39,"H":0.4,"I":0.83,"L":1.06,"K":0.94,"M":1.33,"F":0.41,"P":2.73,"S":1.18,"T":0.77,"W":1.22,"Y":1.09,"V":0.88}
{"AccNo":"RACS820111","PropDesc":"Average relative fractional occurrence in E0(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.93,"R":1.52,"N":0.92,"D":0.6,"C":1.08,"E":0.73,"Q":0.94,"G":0.78,"H":1.08,"I":1.74,"L":1.03,"K":1,"M":1.31,"F":1.51,"P":1.37,"S":0.97,"T":1.38,"W":1.12,"Y":1.65,"V":1.7}
{"AccNo":"RACS820112","PropDesc":"Average relative fractional occurrence in ER(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":0.99,"R":1.19,"N":1.15,"D":1.18,"C":2.32,"E":1.36,"Q":1.52,"G":1.4,"H":1.06,"I":0.81,"L":1.26,"K":0.91,"M":1,"F":1.25,"P":0,"S":1.5,"T":1.18,"W":1.33,"Y":1.09,"V":1.01}
{"AccNo":"RACS820113","PropDesc":"Value of theta(i) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":17.05,"R":21.25,"N":34.81,"D":19.27,"C":28.84,"E":20.12,"Q":15.42,"G":38.14,"H":23.07,"I":16.66,"L":10.89,"K":16.46,"M":20.61,"F":16.26,"P":23.94,"S":19.95,"T":18.92,"W":23.36,"Y":26.49,"V":17.06}
{"AccNo":"RACS820114","PropDesc":"Value of theta(i-1) (Rackovsky-Scheraga, 1982)","LITDBNo":"LIT:0903736","Author":"Rackovsky, S. and Scheraga, H.A.","ArtTitle":"Differential geometry and polymer conformation. 4. Conformational and nucleation properties of individual amino acids","JournalRef":"Macromolecules 15, 1340-1346 (1982)","A":14.53,"R":17.82,"N":13.59,"D":19.78,"C":30.57,"E":18.19,"Q":22.18,"G":37.16,"H":22.63,"I":20.28,"L":14.3,"K":14.07,"M":20.61,"F":19.61,"P":52.63,"S":18.56,"T":21.09,"W":19.78,"Y":26.36,"V":21.87}
{"AccNo":"RADA880101","PropDesc":"Transfer free energy from chx to wat (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro missing)","A":1.81,"R":-14.92,"N":-6.64,"D":-8.72,"C":1.28,"E":-6.81,"Q":-5.54,"G":0.94,"H":-4.66,"I":4.92,"L":4.92,"K":-5.55,"M":2.35,"F":2.98,"P":0,"S":-3.4,"T":-2.57,"W":2.33,"Y":-0.14,"V":4.04}
{"AccNo":"RADA880102","PropDesc":"Transfer free energy from oct to wat (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro Cys Asp missing)","A":0.52,"R":-1.32,"N":-0.01,"D":0,"C":0,"E":-0.79,"Q":-0.07,"G":0,"H":0.95,"I":2.04,"L":1.76,"K":0.08,"M":1.32,"F":2.09,"P":0,"S":0.04,"T":0.27,"W":2.51,"Y":1.63,"V":1.18}
{"AccNo":"RADA880103","PropDesc":"Transfer free energy from vap to chx (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro missing)","A":0.13,"R":-5,"N":-3.04,"D":-2.23,"C":-2.52,"E":-3.43,"Q":-3.84,"G":1.45,"H":-5.61,"I":-2.77,"L":-2.64,"K":-3.97,"M":-3.83,"F":-3.74,"P":0,"S":-1.66,"T":-2.31,"W":-8.21,"Y":-5.97,"V":-2.05}
{"AccNo":"RADA880104","PropDesc":"Transfer free energy from chx to oct (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro Cys Asp missing)","A":1.29,"R":-13.6,"N":-6.63,"D":0,"C":0,"E":-6.02,"Q":-5.47,"G":0.94,"H":-5.61,"I":2.88,"L":3.16,"K":-5.63,"M":1.03,"F":0.89,"P":0,"S":-3.44,"T":-2.84,"W":-0.18,"Y":-1.77,"V":2.86}
{"AccNo":"RADA880105","PropDesc":"Transfer free energy from vap to oct (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro Cys Asp missing)","A":1.42,"R":-18.6,"N":-9.67,"D":0,"C":0,"E":-9.45,"Q":-9.31,"G":2.39,"H":-11.22,"I":0.11,"L":0.52,"K":-9.6,"M":-2.8,"F":-2.85,"P":0,"S":-5.1,"T":-5.15,"W":-8.39,"Y":-7.74,"V":0.81}
{"AccNo":"RADA880106","PropDesc":"Accessible surface area (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro missing)","A":93.7,"R":250.4,"N":146.3,"D":142.6,"C":135.2,"E":182.9,"Q":177.7,"G":52.6,"H":188.1,"I":182.2,"L":173.7,"K":215.2,"M":197.6,"F":228.6,"P":0,"S":109.5,"T":142.1,"W":271.6,"Y":239.9,"V":157.2}
{"AccNo":"RADA880107","PropDesc":"Energy transfer from out to in(95%buried) (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro missing)","A":-0.29,"R":-2.71,"N":-1.18,"D":-1.02,"C":0,"E":-0.9,"Q":-1.53,"G":-0.34,"H":-0.94,"I":0.24,"L":-0.12,"K":-2.05,"M":-0.24,"F":0,"P":0,"S":-0.75,"T":-0.71,"W":-0.59,"Y":-1.02,"V":0.09}
{"AccNo":"RADA880108","PropDesc":"Mean polarity (Radzicka-Wolfenden, 1988)","LITDBNo":"LIT:1405051b","Author":"Radzicka, A. and Wolfenden, R.","ArtTitle":"Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution","JournalRef":"Biochemistry 27, 1664-1670 (1988) (Pro missing)","A":-0.06,"R":-0.84,"N":-0.48,"D":-0.8,"C":1.36,"E":-0.77,"Q":-0.73,"G":-0.41,"H":0.49,"I":1.31,"L":1.21,"K":-1.18,"M":1.27,"F":1.27,"P":0,"S":-0.5,"T":-0.27,"W":0.88,"Y":0.33,"V":1.09}
{"AccNo":"RICJ880101","PropDesc":"Relative preference value at N\" (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":0.7,"R":0.4,"N":1.2,"D":1.4,"C":0.6,"E":1,"Q":1,"G":1.6,"H":1.2,"I":0.9,"L":0.9,"K":1,"M":0.3,"F":1.2,"P":0.7,"S":1.6,"T":0.3,"W":1.1,"Y":1.9,"V":0.7}
{"AccNo":"RICJ880102","PropDesc":"Relative preference value at N' (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":0.7,"R":0.4,"N":1.2,"D":1.4,"C":0.6,"E":1,"Q":1,"G":1.6,"H":1.2,"I":0.9,"L":0.9,"K":1,"M":0.3,"F":1.2,"P":0.7,"S":1.6,"T":0.3,"W":1.1,"Y":1.9,"V":0.7}
{"AccNo":"RICJ880103","PropDesc":"Relative preference value at N-cap (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":0.5,"R":0.4,"N":3.5,"D":2.1,"C":0.6,"E":0.4,"Q":0.4,"G":1.8,"H":1.1,"I":0.2,"L":0.2,"K":0.7,"M":0.8,"F":0.2,"P":0.8,"S":2.3,"T":1.6,"W":0.3,"Y":0.8,"V":0.1}
{"AccNo":"RICJ880104","PropDesc":"Relative preference value at N1 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.2,"R":0.7,"N":0.7,"D":0.8,"C":0.8,"E":2.2,"Q":0.7,"G":0.3,"H":0.7,"I":0.9,"L":0.9,"K":0.6,"M":0.3,"F":0.5,"P":2.6,"S":0.7,"T":0.8,"W":2.1,"Y":1.8,"V":1.1}
{"AccNo":"RICJ880105","PropDesc":"Relative preference value at N2 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.6,"R":0.9,"N":0.7,"D":2.6,"C":1.2,"E":2,"Q":0.8,"G":0.9,"H":0.7,"I":0.7,"L":0.3,"K":1,"M":1,"F":0.9,"P":0.5,"S":0.8,"T":0.7,"W":1.7,"Y":0.4,"V":0.6}
{"AccNo":"RICJ880106","PropDesc":"Relative preference value at N3 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1,"R":0.4,"N":0.7,"D":2.2,"C":0.6,"E":3.3,"Q":1.5,"G":0.6,"H":0.7,"I":0.4,"L":0.6,"K":0.8,"M":1,"F":0.6,"P":0.4,"S":0.4,"T":1,"W":1.4,"Y":1.2,"V":1.1}
{"AccNo":"RICJ880107","PropDesc":"Relative preference value at N4 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.1,"R":1.5,"N":0,"D":0.3,"C":1.1,"E":0.5,"Q":1.3,"G":0.4,"H":1.5,"I":1.1,"L":2.6,"K":0.8,"M":1.7,"F":1.9,"P":0.1,"S":0.4,"T":0.5,"W":3.1,"Y":0.6,"V":1.5}
{"AccNo":"RICJ880108","PropDesc":"Relative preference value at N5 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.4,"R":1.2,"N":1.2,"D":0.6,"C":1.6,"E":0.9,"Q":1.4,"G":0.6,"H":0.9,"I":0.9,"L":1.1,"K":1.9,"M":1.7,"F":1,"P":0.3,"S":1.1,"T":0.6,"W":1.4,"Y":0.2,"V":0.8}
{"AccNo":"RICJ880109","PropDesc":"Relative preference value at Mid (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.8,"R":1.3,"N":0.9,"D":1,"C":0.7,"E":0.8,"Q":1.3,"G":0.5,"H":1,"I":1.2,"L":1.2,"K":1.1,"M":1.5,"F":1.3,"P":0.3,"S":0.6,"T":1,"W":1.5,"Y":0.8,"V":1.2}
{"AccNo":"RICJ880110","PropDesc":"Relative preference value at C5 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.8,"R":1,"N":0.6,"D":0.7,"C":0,"E":1.1,"Q":1,"G":0.5,"H":2.4,"I":1.3,"L":1.2,"K":1.4,"M":2.7,"F":1.9,"P":0.3,"S":0.5,"T":0.5,"W":1.1,"Y":1.3,"V":0.4}
{"AccNo":"RICJ880111","PropDesc":"Relative preference value at C4 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.3,"R":0.8,"N":0.6,"D":0.5,"C":0.7,"E":0.7,"Q":0.2,"G":0.5,"H":1.9,"I":1.6,"L":1.4,"K":1,"M":2.8,"F":2.9,"P":0,"S":0.5,"T":0.6,"W":2.1,"Y":0.8,"V":1.4}
{"AccNo":"RICJ880112","PropDesc":"Relative preference value at C3 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":0.7,"R":0.8,"N":0.8,"D":0.6,"C":0.2,"E":1.6,"Q":1.3,"G":0.1,"H":1.1,"I":1.4,"L":1.9,"K":2.2,"M":1,"F":1.8,"P":0,"S":0.6,"T":0.7,"W":0.4,"Y":1.1,"V":1.3}
{"AccNo":"RICJ880113","PropDesc":"Relative preference value at C2 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.4,"R":2.1,"N":0.9,"D":0.7,"C":1.2,"E":1.7,"Q":1.6,"G":0.2,"H":1.8,"I":0.4,"L":0.8,"K":1.9,"M":1.3,"F":0.3,"P":0.2,"S":1.6,"T":0.9,"W":0.4,"Y":0.3,"V":0.7}
{"AccNo":"RICJ880114","PropDesc":"Relative preference value at C1 (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1.1,"R":1,"N":1.2,"D":0.4,"C":1.6,"E":0.8,"Q":2.1,"G":0.2,"H":3.4,"I":0.7,"L":0.7,"K":2,"M":1,"F":0.7,"P":0,"S":1.7,"T":1,"W":0,"Y":1.2,"V":0.7}
{"AccNo":"RICJ880115","PropDesc":"Relative preference value at C-cap (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":0.8,"R":0.9,"N":1.6,"D":0.7,"C":0.4,"E":0.3,"Q":0.9,"G":3.9,"H":1.3,"I":0.7,"L":0.7,"K":1.3,"M":0.8,"F":0.5,"P":0.7,"S":0.8,"T":0.3,"W":0,"Y":0.8,"V":0.2}
{"AccNo":"RICJ880116","PropDesc":"Relative preference value at C' (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":1,"R":1.4,"N":0.9,"D":1.4,"C":0.8,"E":0.8,"Q":1.4,"G":1.2,"H":1.2,"I":1.1,"L":0.9,"K":1.2,"M":0.8,"F":0.1,"P":1.9,"S":0.7,"T":0.8,"W":0.4,"Y":0.9,"V":0.6}
{"AccNo":"RICJ880117","PropDesc":"Relative preference value at C\" (Richardson-Richardson, 1988)","LITDBNo":"LIT:1408116 PMID:3381086","Author":"Richardson, J.S. and Richardson, D.C.","ArtTitle":"Amino acid preferences for specific locations at the ends of alpha helices","JournalRef":"Science 240, 1648-1652 (1988)","A":0.7,"R":1.1,"N":1.5,"D":1.4,"C":0.4,"E":0.7,"Q":1.1,"G":0.6,"H":1,"I":0.7,"L":0.5,"K":1.3,"M":0,"F":1.2,"P":1.5,"S":0.9,"T":2.1,"W":2.7,"Y":0.5,"V":1}
{"AccNo":"ROBB760101","PropDesc":"Information measure for alpha-helix (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":6.5,"R":-0.9,"N":-5.1,"D":0.5,"C":-1.3,"E":7.8,"Q":1,"G":-8.6,"H":1.2,"I":0.6,"L":3.2,"K":2.3,"M":5.3,"F":1.6,"P":-7.7,"S":-3.9,"T":-2.6,"W":1.2,"Y":-4.5,"V":1.4}
{"AccNo":"ROBB760102","PropDesc":"Information measure for N-terminal helix (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":2.3,"R":-5.2,"N":0.3,"D":7.4,"C":0.8,"E":10.3,"Q":-0.7,"G":-5.2,"H":-2.8,"I":-4,"L":-2.1,"K":-4.1,"M":-3.5,"F":-1.1,"P":8.1,"S":-3.5,"T":2.3,"W":-0.9,"Y":-3.7,"V":-4.4}
{"AccNo":"ROBB760103","PropDesc":"Information measure for middle helix (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":6.7,"R":0.3,"N":-6.1,"D":-3.1,"C":-4.9,"E":2.2,"Q":0.6,"G":-6.8,"H":-1,"I":3.2,"L":5.5,"K":0.5,"M":7.2,"F":2.8,"P":-22.8,"S":-3,"T":-4,"W":4,"Y":-4.6,"V":2.5}
{"AccNo":"ROBB760104","PropDesc":"Information measure for C-terminal helix (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":2.3,"R":1.4,"N":-3.3,"D":-4.4,"C":6.1,"E":2.5,"Q":2.7,"G":-8.3,"H":5.9,"I":-0.5,"L":0.1,"K":7.3,"M":3.5,"F":1.6,"P":-24.4,"S":-1.9,"T":-3.7,"W":-0.9,"Y":-0.6,"V":2.3}
{"AccNo":"ROBB760105","PropDesc":"Information measure for extended (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-2.3,"R":0.4,"N":-4.1,"D":-4.4,"C":4.4,"E":-5,"Q":1.2,"G":-4.2,"H":-2.5,"I":6.7,"L":2.3,"K":-3.3,"M":2.3,"F":2.6,"P":-1.8,"S":-1.7,"T":1.3,"W":-1,"Y":4,"V":6.8}
{"AccNo":"ROBB760106","PropDesc":"Information measure for pleated-sheet (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-2.7,"R":0.4,"N":-4.2,"D":-4.4,"C":3.7,"E":-8.1,"Q":0.8,"G":-3.9,"H":-3,"I":7.7,"L":3.7,"K":-2.9,"M":3.7,"F":3,"P":-6.6,"S":-2.4,"T":1.7,"W":0.3,"Y":3.3,"V":7.1}
{"AccNo":"ROBB760107","PropDesc":"Information measure for extended without H-bond (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":0,"R":1.1,"N":-2,"D":-2.6,"C":5.4,"E":3.1,"Q":2.4,"G":-3.4,"H":0.8,"I":-0.1,"L":-3.7,"K":-3.1,"M":-2.1,"F":0.7,"P":7.4,"S":1.3,"T":0,"W":-3.4,"Y":4.8,"V":2.7}
{"AccNo":"ROBB760108","PropDesc":"Information measure for turn (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-5,"R":2.1,"N":4.2,"D":3.1,"C":4.4,"E":-4.7,"Q":0.4,"G":5.7,"H":-0.3,"I":-4.6,"L":-5.6,"K":1,"M":-4.8,"F":-1.8,"P":2.6,"S":2.6,"T":0.3,"W":3.4,"Y":2.9,"V":-6}
{"AccNo":"ROBB760109","PropDesc":"Information measure for N-terminal turn (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-3.3,"R":0,"N":5.4,"D":3.9,"C":-0.3,"E":-1.8,"Q":-0.4,"G":-1.2,"H":3,"I":-0.5,"L":-2.3,"K":-1.2,"M":-4.3,"F":0.8,"P":6.5,"S":1.8,"T":-0.7,"W":-0.8,"Y":3.1,"V":-3.5}
{"AccNo":"ROBB760110","PropDesc":"Information measure for middle turn (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-4.7,"R":2,"N":3.9,"D":1.9,"C":6.2,"E":-4.2,"Q":-2,"G":5.7,"H":-2.6,"I":-7,"L":-6.2,"K":2.8,"M":-4.8,"F":-3.7,"P":3.6,"S":2.1,"T":0.6,"W":3.3,"Y":3.8,"V":-6.2}
{"AccNo":"ROBB760111","PropDesc":"Information measure for C-terminal turn (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-3.7,"R":1,"N":-0.6,"D":-0.6,"C":4,"E":-4.3,"Q":3.4,"G":5.9,"H":-0.8,"I":-0.5,"L":-2.8,"K":1.3,"M":-1.6,"F":1.6,"P":-6,"S":1.5,"T":1.2,"W":6.5,"Y":1.3,"V":-4.6}
{"AccNo":"ROBB760112","PropDesc":"Information measure for coil (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-2.5,"R":-1.2,"N":4.6,"D":0,"C":-4.7,"E":-4.4,"Q":-0.5,"G":4.9,"H":1.6,"I":-3.3,"L":-2,"K":-0.8,"M":-4.1,"F":-4.1,"P":5.8,"S":2.5,"T":1.7,"W":1.2,"Y":-0.6,"V":-3.5}
{"AccNo":"ROBB760113","PropDesc":"Information measure for loop (Robson-Suzuki, 1976)","LITDBNo":"PMID:1003471","Author":"Robson, B. and Suzuki, E.","ArtTitle":"Conformational properties of amino acid residues in globular proteins","JournalRef":"J. Mol. Biol. 107, 327-356 (1976)","A":-5.1,"R":2.6,"N":4.7,"D":3.1,"C":3.8,"E":-5.2,"Q":0.2,"G":5.6,"H":-0.9,"I":-4.5,"L":-5.4,"K":1,"M":-5.3,"F":-2.4,"P":3.5,"S":3.2,"T":0,"W":2.9,"Y":3.2,"V":-6.3}
{"AccNo":"ROBB790101","PropDesc":"Hydration free energy (Robson-Osguthorpe, 1979)","LITDBNo":"LIT:0511124 PMID:513136","Author":"Robson, B. and Osguthorpe, D.J.","ArtTitle":"Refined models for computer simulation of protein folding: Applications to the study of conserved secondary structure and flexible hinge points during the folding of pancreatic trypsin inhibitor","JournalRef":"J. Mol. Biol. 132, 19-51 (1979) (Gly 0.67)","A":-1,"R":0.3,"N":-0.7,"D":-1.2,"C":2.1,"E":-0.7,"Q":-0.1,"G":0.3,"H":1.1,"I":4,"L":2,"K":-0.9,"M":1.8,"F":2.8,"P":0.4,"S":-1.2,"T":-0.5,"W":3,"Y":2.1,"V":1.4}
{"AccNo":"ROSG850101","PropDesc":"Mean area buried on transfer (Rose et al., 1985)","LITDBNo":"LIT:1109092 PMID:4023714","Author":"Rose, G.D., Geselowitz, A.R., Lesser, G.J., Lee, R.H. and Zehfus, M.H.","ArtTitle":"Hydrophobicity of amino acid residues in globular proteins","JournalRef":"Science 229, 834-838 (1985)","A":86.6,"R":162.2,"N":103.3,"D":97.8,"C":132.3,"E":113.9,"Q":119.2,"G":62.9,"H":155.8,"I":158,"L":164.1,"K":115.5,"M":172.9,"F":194.1,"P":92.9,"S":85.6,"T":106.5,"W":224.6,"Y":177.7,"V":141}
{"AccNo":"ROSG850102","PropDesc":"Mean fractional area loss (Rose et al., 1985)","LITDBNo":"LIT:1109092 PMID:4023714","Author":"Rose, G.D., Geselowitz, A.R., Lesser, G.J., Lee, R.H. and Zehfus, M.H.","ArtTitle":"Hydrophobicity of amino acid residues in globular proteins","JournalRef":"Science 229, 834-838 (1985)","A":0.74,"R":0.64,"N":0.63,"D":0.62,"C":0.91,"E":0.62,"Q":0.62,"G":0.72,"H":0.78,"I":0.88,"L":0.85,"K":0.52,"M":0.85,"F":0.88,"P":0.64,"S":0.66,"T":0.7,"W":0.85,"Y":0.76,"V":0.86}
{"AccNo":"ROSM880101","PropDesc":"Side chain hydropathy, uncorrected for solvation (Roseman, 1988)","LITDBNo":"LIT:1405111b PMID:3398047","Author":"Roseman, M.A.","ArtTitle":"Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds","JournalRef":"J. Mol. Biol. 200, 513-522 (1988)","A":-0.67,"R":12.1,"N":7.23,"D":8.72,"C":-0.34,"E":7.35,"Q":6.39,"G":0,"H":3.82,"I":-3.02,"L":-3.02,"K":6.13,"M":-1.3,"F":-3.24,"P":-1.75,"S":4.35,"T":3.86,"W":-2.86,"Y":0.98,"V":-2.18}
{"AccNo":"ROSM880102","PropDesc":"Side chain hydropathy, corrected for solvation (Roseman, 1988)","LITDBNo":"LIT:1405111b PMID:3398047","Author":"Roseman, M.A.","ArtTitle":"Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds","JournalRef":"J. Mol. Biol. 200, 513-522 (1988)","A":-0.67,"R":3.89,"N":2.27,"D":1.57,"C":-2,"E":1.78,"Q":2.12,"G":0,"H":1.09,"I":-3.02,"L":-3.02,"K":2.46,"M":-1.67,"F":-3.24,"P":-1.75,"S":0.1,"T":-0.42,"W":-2.86,"Y":0.98,"V":-2.18}
{"AccNo":"ROSM880103","PropDesc":"Loss of Side chain hydropathy by helix formation (Roseman, 1988)","LITDBNo":"LIT:1405111b PMID:3398047","Author":"Roseman, M.A.","ArtTitle":"Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds","JournalRef":"J. Mol. Biol. 200, 513-522 (1988)","A":0.4,"R":0.3,"N":0.9,"D":0.8,"C":0.5,"E":1.3,"Q":0.7,"G":0,"H":1,"I":0.4,"L":0.6,"K":0.4,"M":0.3,"F":0.7,"P":0.9,"S":0.4,"T":0.4,"W":0.6,"Y":1.2,"V":0.4}
{"AccNo":"SIMZ760101","PropDesc":"Transfer free energy (Simon, 1976), Cited by Charton-Charton (1982)","Author":"Simon, Z.","JournalRef":"Quantum Biochemistry and Specific Interactions, Abacus Press, Tunbridge Wells, Kent, England (1976) Cited by Charton-Charton (1982)","A":0.73,"R":0.73,"N":-0.01,"D":0.54,"C":0.7,"E":0.55,"Q":-0.1,"G":0,"H":1.1,"I":2.97,"L":2.49,"K":1.5,"M":1.3,"F":2.65,"P":2.6,"S":0.04,"T":0.44,"W":3,"Y":2.97,"V":1.69}
{"AccNo":"SNEP660101","PropDesc":"Principal component I (Sneath, 1966)","LITDBNo":"PMID:4291386","Author":"Sneath, P.H.A.","ArtTitle":"Relations between chemical structure and biological activity in peptides","JournalRef":"J. Theor. Biol. 12, 157-195 (1966)","A":0.239,"R":0.211,"N":0.249,"D":0.171,"C":0.22,"E":0.187,"Q":0.26,"G":0.16,"H":0.205,"I":0.273,"L":0.281,"K":0.228,"M":0.253,"F":0.234,"P":0.165,"S":0.236,"T":0.213,"W":0.183,"Y":0.193,"V":0.255}
{"AccNo":"SNEP660102","PropDesc":"Principal component II (Sneath, 1966)","LITDBNo":"PMID:4291386","Author":"Sneath, P.H.A.","ArtTitle":"Relations between chemical structure and biological activity in peptides","JournalRef":"J. Theor. Biol. 12, 157-195 (1966)","A":0.33,"R":-0.176,"N":-0.233,"D":-0.371,"C":0.074,"E":-0.409,"Q":-0.254,"G":0.37,"H":-0.078,"I":0.149,"L":0.129,"K":-0.075,"M":-0.092,"F":-0.011,"P":0.37,"S":0.022,"T":0.136,"W":-0.011,"Y":-0.138,"V":0.245}
{"AccNo":"SNEP660103","PropDesc":"Principal component III (Sneath, 1966)","LITDBNo":"PMID:4291386","Author":"Sneath, P.H.A.","ArtTitle":"Relations between chemical structure and biological activity in peptides","JournalRef":"J. Theor. Biol. 12, 157-195 (1966)","A":-0.11,"R":0.079,"N":-0.136,"D":-0.285,"C":-0.184,"E":-0.246,"Q":-0.067,"G":-0.073,"H":0.32,"I":0.001,"L":-0.008,"K":0.049,"M":-0.041,"F":0.438,"P":-0.016,"S":-0.153,"T":-0.208,"W":0.493,"Y":0.381,"V":-0.155}
{"AccNo":"SNEP660104","PropDesc":"Principal component IV (Sneath, 1966)","LITDBNo":"PMID:4291386","Author":"Sneath, P.H.A.","ArtTitle":"Relations between chemical structure and biological activity in peptides","JournalRef":"J. Theor. Biol. 12, 157-195 (1966)","A":-0.062,"R":-0.167,"N":0.166,"D":-0.079,"C":0.38,"E":-0.184,"Q":-0.025,"G":-0.017,"H":0.056,"I":-0.309,"L":-0.264,"K":-0.371,"M":0.077,"F":0.074,"P":-0.036,"S":0.47,"T":0.348,"W":0.05,"Y":0.22,"V":-0.212}
{"AccNo":"SUEM840101","PropDesc":"Zimm-Bragg parameter s at 20 C (Sueki et al., 1984)","LITDBNo":"LIT:1004141","Author":"Sueki, M., Lee, S., Powers, S.P., Denton, J.B., Konishi, Y. and Scheraga, H.A.","ArtTitle":"Helix-coil stability constants for the naturally occurring amino acids in water. 22. Histidine parameters from random poly{(hydroxybutyl)glutamine-co-L-histidine}","JournalRef":"Macromolecules 17, 148-155 (1984) Charged state for Arg, His, Asp, and Glu (Cys Pro 0.100)","A":1.071,"R":1.033,"N":0.784,"D":0.68,"C":0.922,"E":0.97,"Q":0.977,"G":0.591,"H":0.85,"I":1.14,"L":1.14,"K":0.939,"M":1.2,"F":1.086,"P":0.659,"S":0.76,"T":0.817,"W":1.107,"Y":1.02,"V":0.95}
{"AccNo":"SUEM840102","PropDesc":"Zimm-Bragg parameter sigma x 1.0E4 (Sueki et al., 1984)","LITDBNo":"LIT:1004141","Author":"Sueki, M., Lee, S., Powers, S.P., Denton, J.B., Konishi, Y. and Scheraga, H.A.","ArtTitle":"Helix-coil stability constants for the naturally occurring amino acids in water. 22. Histidine parameters from random poly{(hydroxybutyl)glutamine-co-L-histidine}","JournalRef":"Macromolecules 17, 148-155 (1984) Charged state for Arg, His, Asp, and Glu (Cys Pro !)","A":8,"R":0.1,"N":0.1,"D":70,"C":26,"E":6,"Q":33,"G":0.1,"H":0.1,"I":55,"L":33,"K":1,"M":54,"F":18,"P":42,"S":0.1,"T":0.1,"W":77,"Y":66,"V":0.1}
{"AccNo":"SWER830101","PropDesc":"Optimal matching hydrophobicity (Sweet-Eisenberg, 1983)","LITDBNo":"LIT:2004095b PMID:6663622","Author":"Sweet, R.M. and Eisenberg, D.","ArtTitle":"Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure","JournalRef":"J. Mol. Biol. 171, 479-488 (1983)","A":-0.4,"R":-0.59,"N":-0.92,"D":-1.31,"C":0.17,"E":-1.22,"Q":-0.91,"G":-0.67,"H":-0.64,"I":1.25,"L":1.22,"K":-0.67,"M":1.02,"F":1.92,"P":-0.49,"S":-0.55,"T":-0.28,"W":0.5,"Y":1.67,"V":0.91}
{"AccNo":"TANS770101","PropDesc":"Normalized frequency of alpha-helix (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":1.42,"R":1.06,"N":0.71,"D":1.01,"C":0.73,"E":1.63,"Q":1.02,"G":0.5,"H":1.2,"I":1.12,"L":1.29,"K":1.24,"M":1.21,"F":1.16,"P":0.65,"S":0.71,"T":0.78,"W":1.05,"Y":0.67,"V":0.99}
{"AccNo":"TANS770102","PropDesc":"Normalized frequency of isolated helix (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.946,"R":1.128,"N":0.432,"D":1.311,"C":0.481,"E":0.698,"Q":1.615,"G":0.36,"H":2.168,"I":1.283,"L":1.192,"K":1.203,"M":0,"F":0.963,"P":2.093,"S":0.523,"T":1.961,"W":1.925,"Y":0.802,"V":0.409}
{"AccNo":"TANS770103","PropDesc":"Normalized frequency of extended structure (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.79,"R":1.087,"N":0.832,"D":0.53,"C":1.268,"E":0.643,"Q":1.038,"G":0.725,"H":0.864,"I":1.361,"L":1.111,"K":0.735,"M":1.092,"F":1.052,"P":1.249,"S":1.093,"T":1.214,"W":1.114,"Y":1.34,"V":1.428}
{"AccNo":"TANS770104","PropDesc":"Normalized frequency of chain reversal R (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":1.194,"R":0.795,"N":0.659,"D":1.056,"C":0.678,"E":0.928,"Q":1.29,"G":1.015,"H":0.611,"I":0.603,"L":0.595,"K":1.06,"M":0.831,"F":0.377,"P":3.159,"S":1.444,"T":1.172,"W":0.452,"Y":0.816,"V":0.64}
{"AccNo":"TANS770105","PropDesc":"Normalized frequency of chain reversal S (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.497,"R":0.677,"N":2.072,"D":1.498,"C":1.348,"E":0.651,"Q":0.711,"G":1.848,"H":1.474,"I":0.471,"L":0.656,"K":0.932,"M":0.425,"F":1.348,"P":0.179,"S":1.151,"T":0.749,"W":1.283,"Y":1.283,"V":0.654}
{"AccNo":"TANS770106","PropDesc":"Normalized frequency of chain reversal D (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.937,"R":1.725,"N":1.08,"D":1.64,"C":1.004,"E":0.679,"Q":1.078,"G":0.901,"H":1.085,"I":0.178,"L":0.808,"K":1.254,"M":0.886,"F":0.803,"P":0.748,"S":1.145,"T":1.487,"W":0.803,"Y":1.227,"V":0.625}
{"AccNo":"TANS770107","PropDesc":"Normalized frequency of left-handed helix (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.289,"R":1.38,"N":3.169,"D":0.917,"C":1.767,"E":0.285,"Q":2.372,"G":4.259,"H":1.061,"I":0.262,"L":0,"K":1.288,"M":0,"F":0.393,"P":0,"S":0.16,"T":0.218,"W":0,"Y":0.654,"V":0.167}
{"AccNo":"TANS770108","PropDesc":"Normalized frequency of zeta R (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.328,"R":2.088,"N":1.498,"D":3.379,"C":0,"E":0,"Q":0,"G":0.5,"H":1.204,"I":2.078,"L":0.414,"K":0.835,"M":0.982,"F":1.336,"P":0.415,"S":1.089,"T":1.732,"W":1.781,"Y":0,"V":0.946}
{"AccNo":"TANS770109","PropDesc":"Normalized frequency of coil (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.945,"R":0.364,"N":1.202,"D":1.315,"C":0.932,"E":1.014,"Q":0.704,"G":2.355,"H":0.525,"I":0.673,"L":0.758,"K":0.947,"M":1.028,"F":0.622,"P":0.579,"S":1.14,"T":0.863,"W":0.777,"Y":0.907,"V":0.561}
{"AccNo":"TANS770110","PropDesc":"Normalized frequency of chain reversal (Tanaka-Scheraga, 1977)","LITDBNo":"PMID:557155","Author":"Tanaka, S. and Scheraga, H.A.","ArtTitle":"Statistical mechanical treatment of protein conformation. 5. A multiphasic model for specific-sequence copolymers of amino acids","JournalRef":"Macromolecules 10, 9-20 (1977) Recalculated by Kidera as normalized frequencies","A":0.842,"R":0.936,"N":1.352,"D":1.366,"C":1.032,"E":0.758,"Q":0.998,"G":1.349,"H":1.079,"I":0.459,"L":0.665,"K":1.045,"M":0.668,"F":0.881,"P":1.385,"S":1.257,"T":1.055,"W":0.881,"Y":1.101,"V":0.643}
{"AccNo":"VASM830101","PropDesc":"Relative population of conformational state A (Vasquez et al., 1983)","LITDBNo":"LIT:0908110","Author":"Vasquez, M., Nemethy, G. and Scheraga, H.A.","ArtTitle":"Computed conformational states of the 20 naturally occurring amino acid residues and of the prototype residue alpha-aminobutyric acid","JournalRef":"Macromolecules 16, 1043-1049 (1983)","A":0.135,"R":0.296,"N":0.196,"D":0.289,"C":0.159,"E":0.184,"Q":0.236,"G":0.051,"H":0.223,"I":0.173,"L":0.215,"K":0.17,"M":0.239,"F":0.087,"P":0.151,"S":0.01,"T":0.1,"W":0.166,"Y":0.066,"V":0.285}
{"AccNo":"VASM830102","PropDesc":"Relative population of conformational state C (Vasquez et al., 1983)","LITDBNo":"LIT:0908110","Author":"Vasquez, M., Nemethy, G. and Scheraga, H.A.","ArtTitle":"Computed conformational states of the 20 naturally occurring amino acid residues and of the prototype residue alpha-aminobutyric acid","JournalRef":"Macromolecules 16, 1043-1049 (1983)","A":0.507,"R":0.459,"N":0.287,"D":0.223,"C":0.592,"E":0.445,"Q":0.383,"G":0.39,"H":0.31,"I":0.111,"L":0.619,"K":0.559,"M":0.431,"F":0.077,"P":0.739,"S":0.689,"T":0.785,"W":0.16,"Y":0.06,"V":0.356}
{"AccNo":"VASM830103","PropDesc":"Relative population of conformational state E (Vasquez et al., 1983)","LITDBNo":"LIT:0908110","Author":"Vasquez, M., Nemethy, G. and Scheraga, H.A.","ArtTitle":"Computed conformational states of the 20 naturally occurring amino acid residues and of the prototype residue alpha-aminobutyric acid","JournalRef":"Macromolecules 16, 1043-1049 (1983) (Pro !)","A":0.159,"R":0.194,"N":0.385,"D":0.283,"C":0.187,"E":0.206,"Q":0.236,"G":0.049,"H":0.233,"I":0.581,"L":0.083,"K":0.159,"M":0.198,"F":0.682,"P":0.366,"S":0.15,"T":0.074,"W":0.463,"Y":0.737,"V":0.301}
{"AccNo":"VELV850101","PropDesc":"Electron-ion interaction potential (Veljkovic et al., 1985)","LITDBNo":"LIT:2004067b","Author":"Veljkovic, V., Cosic, I., Dimitrijevic, B. and Lalovic, D.","ArtTitle":"Is it possible to analyze DNA and protein sequences by the method of digital signal processing?","JournalRef":"IEEE Trans. Biomed. Eng. 32, 337-341 (1985)","A":0.03731,"R":0.09593,"N":0.00359,"D":0.1263,"C":0.08292,"E":0.0058,"Q":0.07606,"G":0.00499,"H":0.02415,"I":0,"L":0,"K":0.0371,"M":0.08226,"F":0.0946,"P":0.01979,"S":0.08292,"T":0.09408,"W":0.05481,"Y":0.05159,"V":0.00569}
{"AccNo":"VENT840101","PropDesc":"Bitterness (Venanzi, 1984)","LITDBNo":"LIT:1103107b PMID:6521488","Author":"Venanzi, T.J.","ArtTitle":"Hydrophobicity parameters and the bitter taste of L-amino acids","JournalRef":"J. Theor. Biol. 111, 447-450 (1984)","A":0,"R":0,"N":0,"D":0,"C":0,"E":0,"Q":0,"G":0,"H":0,"I":1,"L":1,"K":0,"M":0,"F":1,"P":0,"S":0,"T":0,"W":1,"Y":1,"V":1}
{"AccNo":"VHEG790101","PropDesc":"Transfer free energy to lipophilic phase (von Heijne-Blomberg, 1979)","LITDBNo":"LIT:0509382 PMID:477664","Author":"von Heijne, G. and Blomberg, C.","ArtTitle":"Trans-membrane translocation of proteins: The direct transfer model","JournalRef":"Eur. J. Biochem. 97, 175-181 (1979)","A":-12.04,"R":39.23,"N":4.25,"D":23.22,"C":3.95,"E":16.81,"Q":2.16,"G":-7.85,"H":6.28,"I":-18.32,"L":-17.79,"K":9.71,"M":-8.86,"F":-21.98,"P":5.82,"S":-1.54,"T":-4.15,"W":-16.19,"Y":-1.51,"V":-16.22}
{"AccNo":"WARP780101","PropDesc":"Average interactions per side chain atom (Warme-Morgan, 1978)","LITDBNo":"LIT:0405099 PMID:633361","Author":"Warme, P.K. and Morgan, R.S.","ArtTitle":"A survey of amino acid side-chain interactions in 21 proteins","JournalRef":"J. Mol. Biol. 118, 289-304 (1978) (Gly 0.81)","A":10.04,"R":6.18,"N":5.63,"D":5.76,"C":8.89,"E":5.37,"Q":5.41,"G":7.99,"H":7.49,"I":8.72,"L":8.79,"K":4.4,"M":9.15,"F":7.98,"P":7.79,"S":7.08,"T":7,"W":8.07,"Y":6.9,"V":8.88}
{"AccNo":"WEBA780101","PropDesc":"RF value in high salt chromatography (Weber-Lacey, 1978)","LITDBNo":"LIT:2004106b PMID:691071","Author":"Weber, A.L. and Lacey, J.C.,Jr.","ArtTitle":"Genetic code correlations: Amino acids and their anticodon nucleotides","JournalRef":"J. Mol. Evol. 11, 199-210 (1978)","A":0.89,"R":0.88,"N":0.89,"D":0.87,"C":0.85,"E":0.84,"Q":0.82,"G":0.92,"H":0.83,"I":0.76,"L":0.73,"K":0.97,"M":0.74,"F":0.52,"P":0.82,"S":0.96,"T":0.92,"W":0.2,"Y":0.49,"V":0.85}
{"AccNo":"WERD780101","PropDesc":"Propensity to be buried inside (Wertz-Scheraga, 1978)","LITDBNo":"LIT:0405105 PMID:621952","Author":"Wertz, D.H. and Scheraga, H.A.","ArtTitle":"Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule","JournalRef":"Macromolecules 11, 9-15 (1978) Adjusted values","A":0.52,"R":0.49,"N":0.42,"D":0.37,"C":0.83,"E":0.38,"Q":0.35,"G":0.41,"H":0.7,"I":0.79,"L":0.77,"K":0.31,"M":0.76,"F":0.87,"P":0.35,"S":0.49,"T":0.38,"W":0.86,"Y":0.64,"V":0.72}
{"AccNo":"WERD780102","PropDesc":"Free energy change of epsilon(i) to epsilon(ex) (Wertz-Scheraga, 1978)","LITDBNo":"LIT:0405105 PMID:621952","Author":"Wertz, D.H. and Scheraga, H.A.","ArtTitle":"Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule","JournalRef":"Macromolecules 11, 9-15 (1978) Adjusted values","A":0.16,"R":-0.2,"N":1.03,"D":-0.24,"C":-0.12,"E":-0.45,"Q":-0.55,"G":-0.16,"H":-0.18,"I":-0.19,"L":-0.44,"K":-0.12,"M":-0.79,"F":-0.25,"P":-0.59,"S":-0.01,"T":0.05,"W":-0.33,"Y":-0.42,"V":-0.46}
{"AccNo":"WERD780103","PropDesc":"Free energy change of alpha(Ri) to alpha(Rh) (Wertz-Scheraga, 1978)","LITDBNo":"LIT:0405105 PMID:621952","Author":"Wertz, D.H. and Scheraga, H.A.","ArtTitle":"Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule","JournalRef":"Macromolecules 11, 9-15 (1978) Adjusted values (Met !)","A":0.15,"R":-0.37,"N":0.69,"D":-0.22,"C":-0.19,"E":0.14,"Q":-0.06,"G":0.36,"H":-0.25,"I":0.02,"L":0.06,"K":-0.16,"M":0.11,"F":1.18,"P":0.11,"S":0.13,"T":0.28,"W":-0.12,"Y":0.19,"V":-0.08}
{"AccNo":"WERD780104","PropDesc":"Free energy change of epsilon(i) to alpha(Rh) (Wertz-Scheraga, 1978)","LITDBNo":"LIT:0405105 PMID:621952","Author":"Wertz, D.H. and Scheraga, H.A.","ArtTitle":"Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule","JournalRef":"Macromolecules 11, 9-15 (1978) Adjusted values","A":-0.07,"R":-0.4,"N":-0.57,"D":-0.8,"C":0.17,"E":-0.63,"Q":-0.26,"G":0.27,"H":-0.49,"I":0.06,"L":-0.17,"K":-0.45,"M":0.03,"F":0.4,"P":-0.47,"S":-0.11,"T":0.09,"W":-0.61,"Y":-0.61,"V":-0.11}
{"AccNo":"WOEC730101","PropDesc":"Polar requirement (Woese, 1973)","LITDBNo":"PMID:4588588","Author":"Woese, C.R.","ArtTitle":"Evolution of genetic code","JournalRef":"Naturwiss. 60, 447-459 (1973)","A":7,"R":9.1,"N":10,"D":13,"C":5.5,"E":12.5,"Q":8.6,"G":7.9,"H":8.4,"I":4.9,"L":4.9,"K":10.1,"M":5.3,"F":5,"P":6.6,"S":7.5,"T":6.6,"W":5.3,"Y":5.7,"V":5.6}
{"AccNo":"WOLR810101","PropDesc":"Hydration potential (Wolfenden et al., 1981)","LITDBNo":"LIT:0704095 PMID:7213619","Author":"Wolfenden, R. andersson, L., Cullis, P.M. and Southgate, C.C.B.","ArtTitle":"Affinties of amino acid side chains for solvent water","JournalRef":"Biochemistry 20, 849-855 (1981) (Pro 2.9)","A":1.94,"R":-19.92,"N":-9.68,"D":-10.95,"C":-1.24,"E":-10.2,"Q":-9.38,"G":2.39,"H":-10.27,"I":2.15,"L":2.28,"K":-9.52,"M":-1.48,"F":-0.76,"P":-3.68,"S":-5.06,"T":-4.88,"W":-5.88,"Y":-6.11,"V":1.99}
{"AccNo":"WOLS870101","PropDesc":"Principal property value z1 (Wold et al., 1987)","LITDBNo":"LIT:1312098b","Author":"Wold, S., Eriksson, L., Hellberg, S., Jonsson, J., Sjostrom, M., Skagerberg, B. and Wikstrom, C.","ArtTitle":"Principal property values for six non-natural amino acids and their application to a structure-activity relationship for oxytocin peptide analogues","JournalRef":"Can. J. Chem. 65, 1814-1820 (1987)","A":0.07,"R":2.88,"N":3.22,"D":3.64,"C":0.71,"E":3.08,"Q":2.18,"G":2.23,"H":2.41,"I":-4.44,"L":-4.19,"K":2.84,"M":-2.49,"F":-4.92,"P":-1.22,"S":1.96,"T":0.92,"W":-4.75,"Y":-1.39,"V":-2.69}
{"AccNo":"WOLS870102","PropDesc":"Principal property value z2 (Wold et al., 1987)","LITDBNo":"LIT:1312098b","Author":"Wold, S., Eriksson, L., Hellberg, S., Jonsson, J., Sjostrom, M., Skagerberg, B. and Wikstrom, C.","ArtTitle":"Principal property values for six non-natural amino acids and their application to a structure-activity relationship for oxytocin peptide analogues","JournalRef":"Can. J. Chem. 65, 1814-1820 (1987)","A":-1.73,"R":2.52,"N":1.45,"D":1.13,"C":-0.97,"E":0.39,"Q":0.53,"G":-5.36,"H":1.74,"I":-1.68,"L":-1.03,"K":1.41,"M":-0.27,"F":1.3,"P":0.88,"S":-1.63,"T":-2.09,"W":3.65,"Y":2.32,"V":-2.53}
{"AccNo":"WOLS870103","PropDesc":"Principal property value z3 (Wold et al., 1987)","LITDBNo":"LIT:1312098b","Author":"Wold, S., Eriksson, L., Hellberg, S., Jonsson, J., Sjostrom, M., Skagerberg, B. and Wikstrom, C.","ArtTitle":"Principal property values for six non-natural amino acids and their application to a structure-activity relationship for oxytocin peptide analogues","JournalRef":"Can. J. Chem. 65, 1814-1820 (1987)","A":0.09,"R":-3.44,"N":0.84,"D":2.36,"C":4.13,"E":-0.07,"Q":-1.14,"G":0.3,"H":1.11,"I":-1.03,"L":-0.98,"K":-3.14,"M":-0.41,"F":0.45,"P":2.23,"S":0.57,"T":-1.4,"W":0.85,"Y":0.01,"V":-1.29}
{"AccNo":"YUTK870101","PropDesc":"Unfolding Gibbs energy in water, pH7.0 (Yutani et al., 1987)","LITDBNo":"LIT:2004127b PMID:3299367","Author":"Yutani, K., Ogasahara, K., Tsujita, T. and Sugino, Y.","ArtTitle":"Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit","JournalRef":"Proc. Natl. Acad. Sci. USA 84, 4441-4444 (1987) (Arg missing)","A":8.5,"R":0,"N":8.2,"D":8.5,"C":11,"E":8.8,"Q":6.3,"G":7.1,"H":10.1,"I":16.8,"L":15,"K":7.9,"M":13.3,"F":11.2,"P":8.2,"S":7.4,"T":8.8,"W":9.9,"Y":8.8,"V":12}
{"AccNo":"YUTK870102","PropDesc":"Unfolding Gibbs energy in water, pH9.0 (Yutani et al., 1987)","LITDBNo":"LIT:2004127b PMID:3299367","Author":"Yutani, K., Ogasahara, K., Tsujita, T. and Sugino, Y.","ArtTitle":"Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit","JournalRef":"Proc. Natl. Acad. Sci. USA 84, 4441-4444 (1987) (Arg missing)","A":6.8,"R":0,"N":6.2,"D":7,"C":8.3,"E":4.9,"Q":8.5,"G":6.4,"H":9.2,"I":10,"L":12.2,"K":7.5,"M":8.4,"F":8.3,"P":6.9,"S":8,"T":7,"W":5.7,"Y":6.8,"V":9.4}
{"AccNo":"YUTK870103","PropDesc":"Activation Gibbs energy of unfolding, pH7.0 (Yutani et al., 1987)","LITDBNo":"LIT:2004127b PMID:3299367","Author":"Yutani, K., Ogasahara, K., Tsujita, T. and Sugino, Y.","ArtTitle":"Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit","JournalRef":"Proc. Natl. Acad. Sci. USA 84, 4441-4444 (1987) (Arg missing)","A":18.08,"R":0,"N":17.47,"D":17.36,"C":18.17,"E":18.16,"Q":17.93,"G":18.24,"H":18.49,"I":18.62,"L":18.6,"K":17.96,"M":18.11,"F":17.3,"P":18.16,"S":17.57,"T":17.54,"W":17.19,"Y":17.99,"V":18.3}
{"AccNo":"YUTK870104","PropDesc":"Activation Gibbs energy of unfolding, pH9.0 (Yutani et al., 1987)","LITDBNo":"LIT:2004127b PMID:3299367","Author":"Yutani, K., Ogasahara, K., Tsujita, T. and Sugino, Y.","ArtTitle":"Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit","JournalRef":"Proc. Natl. Acad. Sci. USA 84, 4441-4444 (1987) (Arg missing)","A":18.56,"R":0,"N":18.24,"D":17.94,"C":17.84,"E":17.97,"Q":18.51,"G":18.57,"H":18.64,"I":19.21,"L":19.01,"K":18.36,"M":18.49,"F":17.95,"P":18.77,"S":18.06,"T":17.71,"W":16.87,"Y":18.23,"V":18.98}
{"AccNo":"ZASB820101","PropDesc":"Dependence of partition coefficient on ionic strength (Zaslavsky et al., 1982)","LITDBNo":"LIT:0806206","Author":"Zaslavsky, B.Yu, Mestechkina, N.M., Miheeva, L.M. and Rogozhin, S.V.","ArtTitle":"Measurement of relative hydrophobicity of amino acid side-chains by partition in an aqueous two-phase polymeric system: Hydrophobicity scale for non-polar and ionogenic side-chains","JournalRef":"J. Chromatogr. 240, 21-28 (1982) (C H Y missing?)","A":-0.152,"R":-0.089,"N":-0.203,"D":-0.355,"C":0,"E":-0.411,"Q":-0.181,"G":-0.19,"H":0,"I":-0.086,"L":-0.102,"K":-0.062,"M":-0.107,"F":0.001,"P":-0.181,"S":-0.203,"T":-0.17,"W":0.275,"Y":0,"V":-0.125}
{"AccNo":"ZIMJ680101","PropDesc":"Hydrophobicity (Zimmerman et al., 1968)","LITDBNo":"LIT:2004109b PMID:5700434","Author":"Zimmerman, J.M., Eliezer, N. and Simha, R.","ArtTitle":"The characterization of amino acid sequences in proteins by statistical methods","JournalRef":"J. Theor. Biol. 21, 170-201 (1968)","A":0.83,"R":0.83,"N":0.09,"D":0.64,"C":1.48,"E":0.65,"Q":0,"G":0.1,"H":1.1,"I":3.07,"L":2.52,"K":1.6,"M":1.4,"F":2.75,"P":2.7,"S":0.14,"T":0.54,"W":0.31,"Y":2.97,"V":1.79}
{"AccNo":"ZIMJ680102","PropDesc":"Bulkiness (Zimmerman et al., 1968)","LITDBNo":"LIT:2004109b PMID:5700434","Author":"Zimmerman, J.M., Eliezer, N. and Simha, R.","ArtTitle":"The characterization of amino acid sequences in proteins by statistical methods","JournalRef":"J. Theor. Biol. 21, 170-201 (1968)","A":11.5,"R":14.28,"N":12.82,"D":11.68,"C":13.46,"E":13.57,"Q":14.45,"G":3.4,"H":13.69,"I":21.4,"L":21.4,"K":15.71,"M":16.25,"F":19.8,"P":17.43,"S":9.47,"T":15.77,"W":21.67,"Y":18.03,"V":21.57}
{"AccNo":"ZIMJ680103","PropDesc":"Polarity (Zimmerman et al., 1968)","LITDBNo":"LIT:2004109b PMID:5700434","Author":"Zimmerman, J.M., Eliezer, N. and Simha, R.","ArtTitle":"The characterization of amino acid sequences in proteins by statistical methods","JournalRef":"J. Theor. Biol. 21, 170-201 (1968)","A":0,"R":52,"N":3.38,"D":49.7,"C":1.48,"E":49.9,"Q":3.53,"G":0,"H":51.6,"I":0.13,"L":0.13,"K":49.5,"M":1.43,"F":0.35,"P":1.58,"S":1.67,"T":1.66,"W":2.1,"Y":1.61,"V":0.13}
{"AccNo":"ZIMJ680104","PropDesc":"Isoelectric point (Zimmerman et al., 1968)","LITDBNo":"LIT:2004109b PMID:5700434","Author":"Zimmerman, J.M., Eliezer, N. and Simha, R.","ArtTitle":"The characterization of amino acid sequences in proteins by statistical methods","JournalRef":"J. Theor. Biol. 21, 170-201 (1968)","A":6,"R":10.76,"N":5.41,"D":2.77,"C":5.05,"E":3.22,"Q":5.65,"G":5.97,"H":7.59,"I":6.02,"L":5.98,"K":9.74,"M":5.74,"F":5.48,"P":6.3,"S":5.68,"T":5.66,"W":5.89,"Y":5.66,"V":5.96}
{"AccNo":"ZIMJ680105","PropDesc":"RF rank (Zimmerman et al., 1968)","LITDBNo":"LIT:2004109b PMID:5700434","Author":"Zimmerman, J.M., Eliezer, N. and Simha, R.","ArtTitle":"The characterization of amino acid sequences in proteins by statistical methods","JournalRef":"J. Theor. Biol. 21, 170-201 (1968)","A":9.9,"R":4.6,"N":5.4,"D":2.8,"C":2.8,"E":3.2,"Q":9,"G":5.6,"H":8.2,"I":17.1,"L":17.6,"K":3.5,"M":14.9,"F":18.8,"P":14.8,"S":6.9,"T":9.5,"W":17.1,"Y":15,"V":14.3}
{"AccNo":"AURR980101","PropDesc":"Normalized positional residue frequency at helix termini N4'(Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.94,"R":1.15,"N":0.79,"D":1.19,"C":0.6,"E":1.41,"Q":0.94,"G":1.18,"H":1.15,"I":1.07,"L":0.95,"K":1.03,"M":0.88,"F":1.06,"P":1.18,"S":0.69,"T":0.87,"W":0.91,"Y":1.04,"V":0.9}
{"AccNo":"AURR980102","PropDesc":"Normalized positional residue frequency at helix termini N\"' (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.98,"R":1.14,"N":1.05,"D":1.05,"C":0.41,"E":1.04,"Q":0.9,"G":1.25,"H":1.01,"I":0.88,"L":0.8,"K":1.06,"M":1.12,"F":1.12,"P":1.31,"S":1.02,"T":0.8,"W":0.9,"Y":1.12,"V":0.87}
{"AccNo":"AURR980103","PropDesc":"Normalized positional residue frequency at helix termini N\" (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.05,"R":0.81,"N":0.91,"D":1.39,"C":0.6,"E":1.11,"Q":0.87,"G":1.26,"H":1.43,"I":0.95,"L":0.96,"K":0.97,"M":0.99,"F":0.95,"P":1.05,"S":0.96,"T":1.03,"W":1.06,"Y":0.94,"V":0.62}
{"AccNo":"AURR980104","PropDesc":"Normalized positional residue frequency at helix termini N'(Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.75,"R":0.9,"N":1.24,"D":1.72,"C":0.66,"E":1.1,"Q":1.08,"G":1.14,"H":0.96,"I":0.8,"L":1.01,"K":0.66,"M":1.02,"F":0.88,"P":1.33,"S":1.2,"T":1.13,"W":0.68,"Y":0.8,"V":0.58}
{"AccNo":"AURR980105","PropDesc":"Normalized positional residue frequency at helix termini Nc (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.67,"R":0.76,"N":1.28,"D":1.58,"C":0.37,"E":0.94,"Q":1.05,"G":0.98,"H":0.83,"I":0.78,"L":0.79,"K":0.84,"M":0.98,"F":0.96,"P":1.12,"S":1.25,"T":1.41,"W":0.94,"Y":0.82,"V":0.67}
{"AccNo":"AURR980106","PropDesc":"Normalized positional residue frequency at helix termini N1 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.1,"R":1.05,"N":0.72,"D":1.14,"C":0.26,"E":2.3,"Q":1.31,"G":0.55,"H":0.83,"I":1.06,"L":0.84,"K":1.08,"M":0.9,"F":0.9,"P":1.67,"S":0.81,"T":0.77,"W":1.26,"Y":0.99,"V":0.76}
{"AccNo":"AURR980107","PropDesc":"Normalized positional residue frequency at helix termini N2 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.39,"R":0.95,"N":0.67,"D":1.64,"C":0.52,"E":2.07,"Q":1.6,"G":0.65,"H":1.36,"I":0.64,"L":0.91,"K":0.8,"M":1.1,"F":1,"P":0.94,"S":0.69,"T":0.92,"W":1.1,"Y":0.73,"V":0.7}
{"AccNo":"AURR980108","PropDesc":"Normalized positional residue frequency at helix termini N3 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.43,"R":1.33,"N":0.55,"D":0.9,"C":0.52,"E":1.7,"Q":1.43,"G":0.56,"H":0.66,"I":1.18,"L":1.52,"K":0.82,"M":1.68,"F":1.1,"P":0.15,"S":0.61,"T":0.75,"W":1.68,"Y":0.65,"V":1.14}
{"AccNo":"AURR980109","PropDesc":"Normalized positional residue frequency at helix termini N4 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.55,"R":1.39,"N":0.6,"D":0.61,"C":0.59,"E":1.34,"Q":1.43,"G":0.37,"H":0.89,"I":1.47,"L":1.36,"K":1.27,"M":2.13,"F":1.39,"P":0.03,"S":0.44,"T":0.65,"W":1.1,"Y":0.93,"V":1.18}
{"AccNo":"AURR980110","PropDesc":"Normalized positional residue frequency at helix termini N5 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.8,"R":1.73,"N":0.73,"D":0.9,"C":0.55,"E":1.73,"Q":0.97,"G":0.32,"H":0.46,"I":1.09,"L":1.47,"K":1.24,"M":1.64,"F":0.96,"P":0.15,"S":0.67,"T":0.7,"W":0.68,"Y":0.91,"V":0.81}
{"AccNo":"AURR980111","PropDesc":"Normalized positional residue frequency at helix termini C5 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.52,"R":1.49,"N":0.58,"D":1.04,"C":0.26,"E":1.76,"Q":1.41,"G":0.3,"H":0.83,"I":1.25,"L":1.26,"K":1.1,"M":1.14,"F":1.14,"P":0.44,"S":0.66,"T":0.73,"W":0.68,"Y":1.04,"V":1.03}
{"AccNo":"AURR980112","PropDesc":"Normalized positional residue frequency at helix termini C4 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.49,"R":1.41,"N":0.67,"D":0.94,"C":0.37,"E":1.55,"Q":1.52,"G":0.29,"H":0.96,"I":1.04,"L":1.4,"K":1.17,"M":1.84,"F":0.86,"P":0.2,"S":0.68,"T":0.79,"W":1.52,"Y":1.06,"V":0.94}
{"AccNo":"AURR980113","PropDesc":"Normalized positional residue frequency at helix termini C3 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.73,"R":1.24,"N":0.7,"D":0.68,"C":0.63,"E":1.16,"Q":0.88,"G":0.32,"H":0.76,"I":1.15,"L":1.8,"K":1.22,"M":2.21,"F":1.35,"P":0.07,"S":0.65,"T":0.46,"W":1.57,"Y":1.1,"V":0.94}
{"AccNo":"AURR980114","PropDesc":"Normalized positional residue frequency at helix termini C2 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.33,"R":1.39,"N":0.64,"D":0.6,"C":0.44,"E":1.43,"Q":1.37,"G":0.2,"H":1.02,"I":1.58,"L":1.63,"K":1.71,"M":1.76,"F":1.22,"P":0.07,"S":0.42,"T":0.57,"W":1,"Y":1.02,"V":1.08}
{"AccNo":"AURR980115","PropDesc":"Normalized positional residue frequency at helix termini C1 (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.87,"R":1.66,"N":0.7,"D":0.91,"C":0.33,"E":1.88,"Q":1.24,"G":0.33,"H":0.89,"I":0.9,"L":1.65,"K":1.63,"M":1.35,"F":0.67,"P":0.03,"S":0.71,"T":0.5,"W":1,"Y":0.73,"V":0.51}
{"AccNo":"AURR980116","PropDesc":"Normalized positional residue frequency at helix termini Cc (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.19,"R":1.45,"N":1.33,"D":0.72,"C":0.44,"E":1.27,"Q":1.43,"G":0.74,"H":1.55,"I":0.61,"L":1.36,"K":1.45,"M":1.35,"F":1.2,"P":0.1,"S":1.02,"T":0.82,"W":0.58,"Y":1.06,"V":0.46}
{"AccNo":"AURR980117","PropDesc":"Normalized positional residue frequency at helix termini C' (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.77,"R":1.11,"N":1.39,"D":0.79,"C":0.44,"E":0.92,"Q":0.95,"G":2.74,"H":1.65,"I":0.64,"L":0.66,"K":1.19,"M":0.74,"F":1.04,"P":0.66,"S":0.64,"T":0.82,"W":0.58,"Y":0.93,"V":0.53}
{"AccNo":"AURR980118","PropDesc":"Normalized positional residue frequency at helix termini C\" (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.93,"R":0.96,"N":0.82,"D":1.15,"C":0.67,"E":1.07,"Q":1.02,"G":1.08,"H":1.4,"I":1.14,"L":1.16,"K":1.27,"M":1.11,"F":1.05,"P":1.01,"S":0.71,"T":0.84,"W":1.06,"Y":1.15,"V":0.74}
{"AccNo":"AURR980119","PropDesc":"Normalized positional residue frequency at helix termini C\"' (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":1.09,"R":1.29,"N":1.03,"D":1.17,"C":0.26,"E":1.31,"Q":1.08,"G":0.97,"H":0.88,"I":0.97,"L":0.87,"K":1.13,"M":0.96,"F":0.84,"P":2.01,"S":0.76,"T":0.79,"W":0.91,"Y":0.64,"V":0.77}
{"AccNo":"AURR980120","PropDesc":"Normalized positional residue frequency at helix termini C4' (Aurora-Rose, 1998)","LITDBNo":"LIT:2409041 PMID:9514257","Author":"Aurora, R. and Rose, G.","ArtTitle":"Helix capping","JournalRef":"Protein Science 7, 21-38 (1998)","A":0.71,"R":1.09,"N":0.95,"D":1.43,"C":0.65,"E":1.19,"Q":0.87,"G":1.07,"H":1.13,"I":1.05,"L":0.84,"K":1.1,"M":0.8,"F":0.95,"P":1.7,"S":0.65,"T":0.086,"W":1.25,"Y":0.85,"V":1.12}
{"AccNo":"ONEK900101","PropDesc":"Delta G values for the peptides extrapolated to 0 M urea (O'Neil-DeGrado, 1990)","LITDBNo":"LIT:1701155 PMID:2237415","Author":"O'Neil, K.T. and DeGrado, W.F.","ArtTitle":"A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids","JournalRef":"Science 250, 646-651 (1990)","A":13.4,"R":13.3,"N":12,"D":11.7,"C":11.6,"E":12.2,"Q":12.8,"G":11.3,"H":11.6,"I":12,"L":13,"K":13,"M":12.8,"F":12.1,"P":6.5,"S":12.2,"T":11.7,"W":12.4,"Y":12.1,"V":11.9}
{"AccNo":"ONEK900102","PropDesc":"Helix formation parameters (delta delta G) (O'Neil-DeGrado, 1990)","LITDBNo":"LIT:1701155 PMID:2237415","Author":"O'Neil, K.T. and DeGrado, W.F.","ArtTitle":"A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids","JournalRef":"Science 250, 646-651 (1990)","A":-0.77,"R":-0.68,"N":-0.07,"D":-0.15,"C":-0.23,"E":-0.27,"Q":-0.33,"G":0,"H":-0.06,"I":-0.23,"L":-0.62,"K":-0.65,"M":-0.5,"F":-0.41,"P":3,"S":-0.35,"T":-0.11,"W":-0.45,"Y":-0.17,"V":-0.14}
{"AccNo":"VINM940101","PropDesc":"Normalized flexibility parameters (B-values), average (Vihinen et al., 1994)","LITDBNo":"LIT:2014123 PMID:8090708","Author":"Vihinen, M., Torkkila, E. and Riikonen, P.","ArtTitle":"Accuracy of protein flexibility predictions","JournalRef":"Proteins 19, 141-149 (1994)","A":0.984,"R":1.008,"N":1.048,"D":1.068,"C":0.906,"E":1.094,"Q":1.037,"G":1.031,"H":0.95,"I":0.927,"L":0.935,"K":1.102,"M":0.952,"F":0.915,"P":1.049,"S":1.046,"T":0.997,"W":0.904,"Y":0.929,"V":0.931}
{"AccNo":"VINM940102","PropDesc":"Normalized flexibility parameters (B-values) for each residue surrounded by none rigid neighbours (Vihinen et al., 1994)","LITDBNo":"LIT:2014123 PMID:8090708","Author":"Vihinen, M., Torkkila, E. and Riikonen, P.","ArtTitle":"Accuracy of protein flexibility predictions","JournalRef":"Proteins 19, 141-149 (1994)","A":1.315,"R":1.31,"N":1.38,"D":1.372,"C":1.196,"E":1.376,"Q":1.342,"G":1.382,"H":1.279,"I":1.241,"L":1.234,"K":1.367,"M":1.269,"F":1.247,"P":1.342,"S":1.381,"T":1.324,"W":1.186,"Y":1.199,"V":1.235}
{"AccNo":"VINM940103","PropDesc":"Normalized flexibility parameters (B-values) for each residue surrounded by one rigid neighbours (Vihinen et al., 1994)","LITDBNo":"LIT:2014123 PMID:8090708","Author":"Vihinen, M., Torkkila, E. and Riikonen, P.","ArtTitle":"Accuracy of protein flexibility predictions","JournalRef":"Proteins 19, 141-149 (1994)","A":0.994,"R":1.026,"N":1.022,"D":1.022,"C":0.939,"E":1.052,"Q":1.041,"G":1.018,"H":0.967,"I":0.977,"L":0.982,"K":1.029,"M":0.963,"F":0.934,"P":1.05,"S":1.025,"T":0.998,"W":0.938,"Y":0.981,"V":0.968}
{"AccNo":"VINM940104","PropDesc":"Normalized flexibility parameters (B-values) for each residue surrounded by two rigid neighbours (Vihinen et al., 1994)","LITDBNo":"LIT:2014123 PMID:8090708","Author":"Vihinen, M., Torkkila, E. and Riikonen, P.","ArtTitle":"Accuracy of protein flexibility predictions","JournalRef":"Proteins 19, 141-149 (1994)","A":0.783,"R":0.807,"N":0.799,"D":0.822,"C":0.785,"E":0.826,"Q":0.817,"G":0.784,"H":0.777,"I":0.776,"L":0.783,"K":0.834,"M":0.806,"F":0.774,"P":0.809,"S":0.811,"T":0.795,"W":0.796,"Y":0.788,"V":0.781}
{"AccNo":"MUNV940101","PropDesc":"Free energy in alpha-helical conformation (Munoz-Serrano, 1994)","LITDBNo":"LIT:2105109 PMID:7731949","Author":"Munoz, V. and Serrano, L.","ArtTitle":"Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales","JournalRef":"Proteins 20, 301-311 (1994)","A":0.423,"R":0.503,"N":0.906,"D":0.87,"C":0.877,"E":0.167,"Q":0.594,"G":1.162,"H":0.802,"I":0.566,"L":0.494,"K":0.615,"M":0.444,"F":0.706,"P":1.945,"S":0.928,"T":0.884,"W":0.69,"Y":0.778,"V":0.706}
{"AccNo":"MUNV940102","PropDesc":"Free energy in alpha-helical region (Munoz-Serrano, 1994)","LITDBNo":"LIT:2105109 PMID:7731949","Author":"Munoz, V. and Serrano, L.","ArtTitle":"Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales","JournalRef":"Proteins 20, 301-311 (1994)","A":0.619,"R":0.753,"N":1.089,"D":0.932,"C":1.107,"E":0.675,"Q":0.77,"G":1.361,"H":1.034,"I":0.876,"L":0.74,"K":0.784,"M":0.736,"F":0.968,"P":1.78,"S":0.969,"T":1.053,"W":0.91,"Y":1.009,"V":0.939}
{"AccNo":"MUNV940103","PropDesc":"Free energy in beta-strand conformation (Munoz-Serrano, 1994)","LITDBNo":"LIT:2105109 PMID:7731949","Author":"Munoz, V. and Serrano, L.","ArtTitle":"Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales","JournalRef":"Proteins 20, 301-311 (1994)","A":1.08,"R":0.976,"N":1.197,"D":1.266,"C":0.733,"E":1.085,"Q":1.05,"G":1.104,"H":0.906,"I":0.583,"L":0.789,"K":1.026,"M":0.812,"F":0.685,"P":1.412,"S":0.987,"T":0.784,"W":0.755,"Y":0.665,"V":0.546}
{"AccNo":"MUNV940104","PropDesc":"Free energy in beta-strand region (Munoz-Serrano, 1994)","LITDBNo":"LIT:2105109 PMID:7731949","Author":"Munoz, V. and Serrano, L.","ArtTitle":"Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales","JournalRef":"Proteins 20, 301-311 (1994)","A":0.978,"R":0.784,"N":0.915,"D":1.038,"C":0.573,"E":0.962,"Q":0.863,"G":1.405,"H":0.724,"I":0.502,"L":0.766,"K":0.841,"M":0.729,"F":0.585,"P":2.613,"S":0.784,"T":0.569,"W":0.671,"Y":0.56,"V":0.444}
{"AccNo":"MUNV940105","PropDesc":"Free energy in beta-strand region (Munoz-Serrano, 1994)","LITDBNo":"LIT:2105109 PMID:7731949","Author":"Munoz, V. and Serrano, L.","ArtTitle":"Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales","JournalRef":"Proteins 20, 301-311 (1994)","A":1.4,"R":1.23,"N":1.61,"D":1.89,"C":1.14,"E":1.42,"Q":1.33,"G":2.06,"H":1.25,"I":1.02,"L":1.33,"K":1.34,"M":1.12,"F":1.07,"P":3.9,"S":1.2,"T":0.99,"W":1.1,"Y":0.98,"V":0.87}
{"AccNo":"WIMW960101","PropDesc":"Free energies of transfer of AcWl-X-LL peptides from bilayer interface to water (Wimley-White, 1996)","LITDBNo":"LIT:2223095 PMID:8836100","Author":"Wimley, W.C. and White, S.","ArtTitle":"Experimentally determined hydrophobicity scale for proteins at membrane interfaces","JournalRef":"Nature Structual biol. 3, 842-848 (1996)","A":4.08,"R":3.91,"N":3.83,"D":3.02,"C":4.49,"E":2.23,"Q":3.67,"G":4.24,"H":4.08,"I":4.52,"L":4.81,"K":3.77,"M":4.48,"F":5.38,"P":3.8,"S":4.12,"T":4.11,"W":6.1,"Y":5.19,"V":4.18}
{"AccNo":"KIMC930101","PropDesc":"Thermodynamic beta sheet propensity (Kim-Berg, 1993)","LITDBNo":"LIT:1909070 PMID:8459852","Author":"Kim, C.A. and Berg, J.M.","ArtTitle":"Thermodynamic beta-sheet propensities measured using a zinc-finger host peptide","JournalRef":"Nature 362, 267-270 (1993)","A":-0.35,"R":-0.44,"N":-0.38,"D":-0.41,"C":-0.47,"E":-0.41,"Q":-0.4,"G":0,"H":-0.46,"I":-0.56,"L":-0.48,"K":-0.41,"M":-0.46,"F":-0.55,"P":-0.23,"S":-0.39,"T":-0.48,"W":-0.48,"Y":-0.5,"V":-0.53}
{"AccNo":"MONM990101","PropDesc":"Turn propensity scale for transmembrane helices (Monne et al., 1999)","LITDBNo":"PMID:10329132","Author":"Monne, M., Hermansson, M. and von Heijne, G.","ArtTitle":"A turn propensity scale for transmembrane helices","JournalRef":"J. Mol. Biol. 288, 141-145 (1999)","A":0.5,"R":1.7,"N":1.7,"D":1.6,"C":0.6,"E":1.6,"Q":1.6,"G":1.3,"H":1.6,"I":0.6,"L":0.4,"K":1.6,"M":0.5,"F":0.4,"P":1.7,"S":0.7,"T":0.4,"W":0.7,"Y":0.6,"V":0.5}
{"AccNo":"BLAM930101","PropDesc":"Alpha helix propensity of position 44 in T4 lysozyme (Blaber et al., 1993)","LITDBNo":"LIT:1915114 PMID:8503008","Author":"Blaber, M., Zhang, X.J. and Matthews, B.W.","ArtTitle":"Structural basis of amino acid alpha helix propensity","JournalRef":"Science 260, 1637-1640 (1993)","A":0.96,"R":0.77,"N":0.39,"D":0.42,"C":0.42,"E":0.53,"Q":0.8,"G":0,"H":0.57,"I":0.84,"L":0.92,"K":0.73,"M":0.86,"F":0.59,"P":-2.5,"S":0.53,"T":0.54,"W":0.58,"Y":0.72,"V":0.63}
{"AccNo":"PARS000101","PropDesc":"p-Values of mesophilic proteins based on the distributions of B values (Parthasarathy-Murthy, 2000)","LITDBNo":"PMID:10679524","Author":"Parthasarathy, S. and Murthy, M.R.","ArtTitle":"Protein thermal stability: insights from atomic displacement parameters (B values)","JournalRef":"Protein Eng. 13, 9-13 (2000)","A":0.343,"R":0.353,"N":0.409,"D":0.429,"C":0.319,"E":0.405,"Q":0.395,"G":0.389,"H":0.307,"I":0.296,"L":0.287,"K":0.429,"M":0.293,"F":0.292,"P":0.432,"S":0.416,"T":0.362,"W":0.268,"Y":0.22,"V":0.307}
{"AccNo":"PARS000102","PropDesc":"p-Values of thermophilic proteins based on the distributions of B values (Parthasarathy-Murthy, 2000)","LITDBNo":"PMID:10679524","Author":"Parthasarathy, S. and Murthy, M.R.","ArtTitle":"Protein thermal stability: insights from atomic displacement parameters (B values)","JournalRef":"Protein Eng. 13, 9-13 (2000)","A":0.32,"R":0.327,"N":0.384,"D":0.424,"C":0.198,"E":0.514,"Q":0.436,"G":0.374,"H":0.299,"I":0.306,"L":0.34,"K":0.446,"M":0.313,"F":0.314,"P":0.354,"S":0.376,"T":0.339,"W":0.291,"Y":0.287,"V":0.294}
{"AccNo":"KUMS000101","PropDesc":"Distribution of amino acid residues in the 18 non-redundant families of thermophilic proteins (Kumar et al., 2000)","LITDBNo":"PMID:10775659","Author":"Kumar, S., Tsai, C.J. and Nussinov, R.","ArtTitle":"Factors enhancing protein thermostability","JournalRef":"Protein Eng. 13, 179-191 (2000)","A":8.9,"R":4.6,"N":4.4,"D":6.3,"C":0.6,"E":6.9,"Q":2.8,"G":9.4,"H":2.2,"I":7,"L":7.4,"K":6.1,"M":2.3,"F":3.3,"P":4.2,"S":4,"T":5.7,"W":1.3,"Y":4.5,"V":8.2}
{"AccNo":"KUMS000102","PropDesc":"Distribution of amino acid residues in the 18 non-redundant families of mesophilic proteins (Kumar et al., 2000)","LITDBNo":"PMID:10775659","Author":"Kumar, S., Tsai, C.J. and Nussinov, R.","ArtTitle":"Factors enhancing protein thermostability","JournalRef":"Protein Eng. 13, 179-191 (2000)","A":9.2,"R":3.6,"N":5.1,"D":6,"C":1,"E":6,"Q":2.9,"G":9.4,"H":2.1,"I":6,"L":7.7,"K":6.5,"M":2.4,"F":3.4,"P":4.2,"S":5.5,"T":5.7,"W":1.2,"Y":3.7,"V":8.2}
{"AccNo":"KUMS000103","PropDesc":"Distribution of amino acid residues in the alpha-helices in thermophilic proteins (Kumar et al., 2000)","LITDBNo":"PMID:10775659","Author":"Kumar, S., Tsai, C.J. and Nussinov, R.","ArtTitle":"Factors enhancing protein thermostability","JournalRef":"Protein Eng. 13, 179-191 (2000)","A":14.1,"R":5.5,"N":3.2,"D":5.7,"C":0.1,"E":8.8,"Q":3.7,"G":4.1,"H":2,"I":7.1,"L":9.1,"K":7.7,"M":3.3,"F":5,"P":0.7,"S":3.9,"T":4.4,"W":1.2,"Y":4.5,"V":5.9}
{"AccNo":"KUMS000104","PropDesc":"Distribution of amino acid residues in the alpha-helices in mesophilic proteins (Kumar et al., 2000)","LITDBNo":"PMID:10775659","Author":"Kumar, S., Tsai, C.J. and Nussinov, R.","ArtTitle":"Factors enhancing protein thermostability","JournalRef":"Protein Eng. 13, 179-191 (2000)","A":13.4,"R":3.9,"N":3.7,"D":4.6,"C":0.8,"E":7.8,"Q":4.8,"G":4.6,"H":3.3,"I":6.5,"L":10.6,"K":7.5,"M":3,"F":4.5,"P":1.3,"S":3.8,"T":4.6,"W":1,"Y":3.3,"V":7.1}
{"AccNo":"TAKK010101","PropDesc":"Side-chain contribution to protein stability (kJ/mol) (Takano-Yutani, 2001)","LITDBNo":"PMID:11579219","Author":"Takano, K., Yutani, K.","ArtTitle":"A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins","JournalRef":"Protein Eng. 14, 525-528 (2001)","A":9.8,"R":7.3,"N":3.6,"D":4.9,"C":3,"E":4.4,"Q":2.4,"G":0,"H":11.9,"I":17.2,"L":17,"K":10.5,"M":11.9,"F":23,"P":15,"S":2.6,"T":6.9,"W":24.2,"Y":17.2,"V":15.3}
{"AccNo":"FODM020101","PropDesc":"Propensity of amino acids within pi-helices (Fodje-Al-Karadaghi, 2002)","LITDBNo":"PMID:12034854","Author":"Fodje, M.N. and Al-Karadaghi, S.","ArtTitle":"Occurrence, conformational features and amino acid propensities for the pi-helix","JournalRef":"Protein Eng. 15, 353-358 (2002)","A":0.7,"R":0.95,"N":1.47,"D":0.87,"C":1.17,"E":0.96,"Q":0.73,"G":0.64,"H":1.39,"I":1.29,"L":1.44,"K":0.91,"M":0.91,"F":1.34,"P":0.12,"S":0.84,"T":0.74,"W":1.8,"Y":1.68,"V":1.2}
{"AccNo":"NADH010101","PropDesc":"Hydropathy scale based on self-information values in the two-state model (5% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":58,"R":-184,"N":-93,"D":-97,"C":116,"E":-131,"Q":-139,"G":-11,"H":-73,"I":107,"L":95,"K":-24,"M":78,"F":92,"P":-79,"S":-34,"T":-7,"W":59,"Y":-11,"V":100}
{"AccNo":"NADH010102","PropDesc":"Hydropathy scale based on self-information values in the two-state model (9% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":51,"R":-144,"N":-84,"D":-78,"C":137,"E":-115,"Q":-128,"G":-13,"H":-55,"I":106,"L":103,"K":-205,"M":73,"F":108,"P":-79,"S":-26,"T":-3,"W":69,"Y":11,"V":108}
{"AccNo":"NADH010103","PropDesc":"Hydropathy scale based on self-information values in the two-state model (16% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":41,"R":-109,"N":-74,"D":-47,"C":169,"E":-90,"Q":-104,"G":-18,"H":-35,"I":104,"L":103,"K":-148,"M":77,"F":128,"P":-81,"S":-31,"T":10,"W":102,"Y":36,"V":116}
{"AccNo":"NADH010104","PropDesc":"Hydropathy scale based on self-information values in the two-state model (20% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":32,"R":-95,"N":-73,"D":-29,"C":182,"E":-74,"Q":-95,"G":-22,"H":-25,"I":106,"L":104,"K":-124,"M":82,"F":132,"P":-82,"S":-34,"T":20,"W":118,"Y":44,"V":113}
{"AccNo":"NADH010105","PropDesc":"Hydropathy scale based on self-information values in the two-state model (25% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":24,"R":-79,"N":-76,"D":0,"C":194,"E":-57,"Q":-87,"G":-28,"H":-31,"I":102,"L":103,"K":-9,"M":90,"F":131,"P":-85,"S":-36,"T":34,"W":116,"Y":43,"V":111}
{"AccNo":"NADH010106","PropDesc":"Hydropathy scale based on self-information values in the two-state model (36% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":5,"R":-57,"N":-77,"D":45,"C":224,"E":-8,"Q":-67,"G":-47,"H":-50,"I":83,"L":82,"K":-38,"M":83,"F":117,"P":-103,"S":-41,"T":79,"W":130,"Y":27,"V":117}
{"AccNo":"NADH010107","PropDesc":"Hydropathy scale based on self-information values in the two-state model (50% accessibility) (Naderi-Manesh et al., 2001)","LITDBNo":"PMID:11170200","Author":"Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A.A.","ArtTitle":"Prediction of protein surface accessibility with information theory","JournalRef":"Proteins 42, 452-459 (2001)","A":-2,"R":-41,"N":-97,"D":248,"C":329,"E":117,"Q":-37,"G":-66,"H":-70,"I":28,"L":36,"K":115,"M":62,"F":120,"P":-132,"S":-52,"T":174,"W":179,"Y":-7,"V":114}
{"AccNo":"MONM990201","PropDesc":"Averaged turn propensities in a transmembrane helix (Monne et al., 1999)","LITDBNo":"PMID:10543969","Author":"Monne, M., Nilsson, I., Elofsson, A. and von Heijne, G.","ArtTitle":"Turns in transmembrane helices: determination of the minimal length of a \"helical hairpin\" and derivation of a fine-grained turn propensity scale","JournalRef":"J. Mol. Biol. 293, 807-814 (1999)","A":0.4,"R":1.5,"N":1.6,"D":15,"C":0.7,"E":1.3,"Q":1.4,"G":1.1,"H":1.4,"I":0.5,"L":0.3,"K":1.4,"M":0.5,"F":0.3,"P":1.6,"S":0.9,"T":0.7,"W":0.9,"Y":0.9,"V":0.4}
{"AccNo":"KOEP990101","PropDesc":"Alpha-helix propensity derived from designed sequences (Koehl-Levitt, 1999)","LITDBNo":"PMID:10535955","Author":"Koehl, P. and Levitt, M.","ArtTitle":"Structure-based conformational preferences of amino acids","JournalRef":"Proc Natl Acad Sci U S A. 96, 12524-12529 (1999) (Pro missing)","A":-0.04,"R":-0.3,"N":0.25,"D":0.27,"C":0.57,"E":-0.33,"Q":-0.02,"G":1.24,"H":-0.11,"I":-0.26,"L":-0.38,"K":-0.18,"M":-0.09,"F":-0.01,"P":0,"S":0.15,"T":0.39,"W":0.21,"Y":0.05,"V":-0.06}
{"AccNo":"KOEP990102","PropDesc":"Beta-sheet propensity derived from designed sequences (Koehl-Levitt, 1999)","LITDBNo":"PMID:10535955","Author":"Koehl, P. and Levitt, M.","ArtTitle":"Structure-based conformational preferences of amino acids","JournalRef":"Proc Natl Acad Sci U S A. 96, 12524-12529 (1999) (Pro!)","A":-0.12,"R":0.34,"N":1.05,"D":1.12,"C":-0.63,"E":0.91,"Q":1.67,"G":0.76,"H":1.34,"I":-0.77,"L":0.15,"K":0.29,"M":-0.71,"F":-0.67,"P":0,"S":1.45,"T":-0.7,"W":-0.14,"Y":-0.49,"V":-0.7}
{"AccNo":"CEDJ970101","PropDesc":"Composition of amino acids in extracellular proteins (percent) (Cedano et al., 1997)","LITDBNo":"PMID:9067612","Author":"Cedano, J., Aloy, P., Perez-Pons, J.A. and Querol, E.","ArtTitle":"Relation between amino acid composition and cellular location of proteins","JournalRef":"J. Mol. Biol. 266, 594-600 (1997)","A":8.6,"R":4.2,"N":4.6,"D":4.9,"C":2.9,"E":5.1,"Q":4,"G":7.8,"H":2.1,"I":4.6,"L":8.8,"K":6.3,"M":2.5,"F":3.7,"P":4.9,"S":7.3,"T":6,"W":1.4,"Y":3.6,"V":6.7}
{"AccNo":"CEDJ970102","PropDesc":"Composition of amino acids in anchored proteins (percent) (Cedano et al., 1997)","LITDBNo":"PMID:9067612","Author":"Cedano, J., Aloy, P., Perez-Pons, J.A. and Querol, E.","ArtTitle":"Relation between amino acid composition and cellular location of proteins","JournalRef":"J. Mol. Biol. 266, 594-600 (1997)","A":7.6,"R":5,"N":4.4,"D":5.2,"C":2.2,"E":6.2,"Q":4.1,"G":6.9,"H":2.1,"I":5.1,"L":9.4,"K":5.8,"M":2.1,"F":4,"P":5.4,"S":7.2,"T":6.1,"W":1.4,"Y":3.2,"V":6.7}
{"AccNo":"CEDJ970103","PropDesc":"Composition of amino acids in membrane proteins (percent) (Cedano et al., 1997)","LITDBNo":"PMID:9067612","Author":"Cedano, J., Aloy, P., Perez-Pons, J.A. and Querol, E.","ArtTitle":"Relation between amino acid composition and cellular location of proteins","JournalRef":"J. Mol. Biol. 266, 594-600 (1997)","A":8.1,"R":4.6,"N":3.7,"D":3.8,"C":2,"E":4.6,"Q":3.1,"G":7,"H":2,"I":6.7,"L":11,"K":4.4,"M":2.8,"F":5.6,"P":4.7,"S":7.3,"T":5.6,"W":1.8,"Y":3.3,"V":7.7}
{"AccNo":"CEDJ970104","PropDesc":"Composition of amino acids in intracellular proteins (percent) (Cedano et al., 1997)","LITDBNo":"PMID:9067612","Author":"Cedano, J., Aloy, P., Perez-Pons, J.A. and Querol, E.","ArtTitle":"Relation between amino acid composition and cellular location of proteins","JournalRef":"J. Mol. Biol. 266, 594-600 (1997)","A":7.9,"R":4.9,"N":4,"D":5.5,"C":1.9,"E":7.1,"Q":4.4,"G":7.1,"H":2.1,"I":5.2,"L":8.6,"K":6.7,"M":2.4,"F":3.9,"P":5.3,"S":6.6,"T":5.3,"W":1.2,"Y":3.1,"V":6.8}
{"AccNo":"CEDJ970105","PropDesc":"Composition of amino acids in nuclear proteins (percent) (Cedano et al., 1997)","LITDBNo":"PMID:9067612","Author":"Cedano, J., Aloy, P., Perez-Pons, J.A. and Querol, E.","ArtTitle":"Relation between amino acid composition and cellular location of proteins","JournalRef":"J. Mol. Biol. 266, 594-600 (1997)","A":8.3,"R":8.7,"N":3.7,"D":4.7,"C":1.6,"E":6.5,"Q":4.7,"G":6.3,"H":2.1,"I":3.7,"L":7.4,"K":7.9,"M":2.3,"F":2.7,"P":6.9,"S":8.8,"T":5.1,"W":0.7,"Y":2.4,"V":5.3}
{"AccNo":"FUKS010101","PropDesc":"Surface composition of amino acids in intracellular proteins of thermophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":4.47,"R":8.48,"N":3.89,"D":7.05,"C":0.29,"E":16.56,"Q":2.87,"G":8.29,"H":1.74,"I":3.3,"L":5.06,"K":12.98,"M":1.71,"F":2.32,"P":5.41,"S":4.27,"T":3.83,"W":0.67,"Y":2.75,"V":4.05}
{"AccNo":"FUKS010102","PropDesc":"Surface composition of amino acids in intracellular proteins of mesophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":6.77,"R":6.87,"N":5.5,"D":8.57,"C":0.31,"E":12.93,"Q":5.24,"G":7.95,"H":2.8,"I":2.72,"L":4.43,"K":10.2,"M":1.87,"F":1.92,"P":4.79,"S":5.41,"T":5.36,"W":0.54,"Y":2.26,"V":3.57}
{"AccNo":"FUKS010103","PropDesc":"Surface composition of amino acids in extracellular proteins of mesophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":7.43,"R":4.51,"N":9.12,"D":8.71,"C":0.42,"E":5.86,"Q":5.42,"G":9.4,"H":1.49,"I":1.76,"L":2.74,"K":9.67,"M":0.6,"F":1.18,"P":5.6,"S":9.6,"T":8.95,"W":1.18,"Y":3.26,"V":3.1}
{"AccNo":"FUKS010104","PropDesc":"Surface composition of amino acids in nuclear proteins (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":5.22,"R":7.3,"N":6.06,"D":7.91,"C":1.01,"E":10.66,"Q":6,"G":5.81,"H":2.27,"I":2.36,"L":4.52,"K":12.68,"M":1.85,"F":1.68,"P":5.7,"S":6.99,"T":5.16,"W":0.56,"Y":2.16,"V":4.1}
{"AccNo":"FUKS010105","PropDesc":"Interior composition of amino acids in intracellular proteins of thermophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":9.88,"R":3.71,"N":2.35,"D":3.5,"C":1.12,"E":4.02,"Q":1.66,"G":6.88,"H":1.88,"I":10.08,"L":13.21,"K":3.39,"M":2.44,"F":5.27,"P":3.8,"S":4.1,"T":4.98,"W":1.11,"Y":4.07,"V":12.53}
{"AccNo":"FUKS010106","PropDesc":"Interior composition of amino acids in intracellular proteins of mesophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":10.98,"R":3.26,"N":2.85,"D":3.37,"C":1.47,"E":3.51,"Q":2.3,"G":7.48,"H":2.2,"I":9.74,"L":12.79,"K":2.54,"M":3.1,"F":4.97,"P":3.42,"S":4.93,"T":5.55,"W":1.28,"Y":3.55,"V":10.69}
{"AccNo":"FUKS010107","PropDesc":"Interior composition of amino acids in extracellular proteins of mesophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":9.95,"R":3.05,"N":4.84,"D":4.46,"C":1.3,"E":2.58,"Q":2.64,"G":8.87,"H":1.99,"I":7.73,"L":9.66,"K":2,"M":2.45,"F":5.41,"P":3.2,"S":6.03,"T":5.62,"W":2.6,"Y":6.15,"V":9.46}
{"AccNo":"FUKS010108","PropDesc":"Interior composition of amino acids in nuclear proteins (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":8.26,"R":2.8,"N":2.54,"D":2.8,"C":2.67,"E":2.67,"Q":2.86,"G":5.62,"H":1.98,"I":8.95,"L":16.46,"K":1.89,"M":2.67,"F":7.32,"P":3.3,"S":6,"T":5,"W":2.01,"Y":3.96,"V":10.24}
{"AccNo":"FUKS010109","PropDesc":"Entire chain composition of amino acids in intracellular proteins of thermophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":7.39,"R":5.91,"N":3.06,"D":5.14,"C":0.74,"E":9.8,"Q":2.22,"G":7.53,"H":1.82,"I":6.96,"L":9.45,"K":7.81,"M":2.1,"F":3.91,"P":4.54,"S":4.18,"T":4.45,"W":0.9,"Y":3.46,"V":8.62}
{"AccNo":"FUKS010110","PropDesc":"Entire chain composition of amino acids in intracellular proteins of mesophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":9.07,"R":4.9,"N":4.05,"D":5.73,"C":0.95,"E":7.77,"Q":3.63,"G":7.69,"H":2.47,"I":6.56,"L":9,"K":6.01,"M":2.54,"F":3.59,"P":4.04,"S":5.15,"T":5.46,"W":0.95,"Y":2.96,"V":7.47}
{"AccNo":"FUKS010111","PropDesc":"Entire chain composition of amino acids in extracellular proteins of mesophiles (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":8.82,"R":3.71,"N":6.77,"D":6.38,"C":0.9,"E":4.05,"Q":3.89,"G":9.11,"H":1.77,"I":5.05,"L":6.54,"K":5.45,"M":1.62,"F":3.51,"P":4.28,"S":7.64,"T":7.12,"W":1.96,"Y":4.85,"V":6.6}
{"AccNo":"FUKS010112","PropDesc":"Entire chain compositino of amino acids in nuclear proteins (percent) (Fukuchi-Nishikawa, 2001)","LITDBNo":"PMID:11399062","Author":"Fukuchi, S. and Nishikawa, K.","ArtTitle":"Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria","JournalRef":"J. Mol. Biol. 309, 835-843 (2001)","A":6.65,"R":5.17,"N":4.4,"D":5.5,"C":1.79,"E":6.89,"Q":4.52,"G":5.72,"H":2.13,"I":5.47,"L":10.15,"K":7.59,"M":2.24,"F":4.34,"P":4.56,"S":6.52,"T":5.08,"W":1.24,"Y":3.01,"V":7}
{"AccNo":"AVBF000101","PropDesc":"Screening coefficients gamma, local (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":0.163,"R":0.22,"N":0.124,"D":0.212,"C":0.316,"E":0.212,"Q":0.274,"G":0.08,"H":0.315,"I":0.474,"L":0.315,"K":0.255,"M":0.356,"F":0.41,"S":0.29,"T":0.412,"W":0.325,"Y":0.354,"V":0.515}
{"AccNo":"AVBF000102","PropDesc":"Screening coefficients gamma, non-local (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":0.236,"R":0.233,"N":0.189,"D":0.168,"C":0.259,"E":0.306,"Q":0.314,"G":-0.17,"H":0.256,"I":0.391,"L":0.293,"K":0.231,"M":0.367,"F":0.328,"S":0.202,"T":0.308,"W":0.197,"Y":0.223,"V":0.436}
{"AccNo":"AVBF000103","PropDesc":"Slopes tripeptide, FDPB VFF neutral (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.49,"R":-0.429,"N":-0.387,"D":-0.375,"C":-0.352,"E":-0.382,"Q":-0.422,"G":-0.647,"H":-0.357,"I":-0.268,"L":-0.45,"K":-0.409,"M":-0.375,"F":-0.309,"S":-0.426,"T":-0.24,"W":-0.325,"Y":-0.288,"V":-0.22}
{"AccNo":"AVBF000104","PropDesc":"Slopes tripeptides, LD VFF neutral (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.871,"R":-0.727,"N":-0.741,"D":-0.737,"C":-0.666,"E":-0.773,"Q":-0.728,"G":-0.822,"H":-0.685,"I":-0.617,"L":-0.798,"K":-0.715,"M":-0.717,"F":-0.649,"S":-0.679,"T":-0.629,"W":-0.669,"Y":-0.655,"V":-0.599}
{"AccNo":"AVBF000105","PropDesc":"Slopes tripeptide, FDPB VFF noside (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.393,"R":-0.317,"N":-0.268,"D":-0.247,"C":-0.222,"E":-0.26,"Q":-0.291,"G":-0.57,"H":-0.244,"I":-0.144,"L":-0.281,"K":-0.294,"M":-0.274,"F":-0.189,"S":-0.28,"T":-0.152,"W":-0.206,"Y":-0.155,"V":-0.08}
{"AccNo":"AVBF000106","PropDesc":"Slopes tripeptide FDPB VFF all (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.378,"R":-0.369,"N":-0.245,"D":-0.113,"C":-0.206,"E":-0.165,"Q":-0.29,"G":-0.56,"H":-0.295,"I":-0.134,"L":-0.266,"K":-0.335,"M":-0.26,"F":-0.187,"S":-0.251,"T":-0.093,"W":-0.188,"Y":-0.147,"V":-0.084}
{"AccNo":"AVBF000107","PropDesc":"Slopes tripeptide FDPB PARSE neutral (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.729,"R":-0.535,"N":-0.597,"D":-0.545,"C":-0.408,"E":-0.532,"Q":-0.492,"G":-0.86,"H":-0.519,"I":-0.361,"L":-0.462,"K":-0.508,"M":-0.518,"F":-0.454,"S":-0.278,"T":-0.367,"W":-0.455,"Y":-0.439,"V":-0.323}
{"AccNo":"AVBF000108","PropDesc":"Slopes dekapeptide, FDPB VFF neutral (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.623,"R":-0.567,"N":-0.619,"D":-0.626,"C":-0.571,"E":-0.572,"Q":-0.559,"G":-0.679,"H":-0.508,"I":-0.199,"L":-0.527,"K":-0.581,"M":-0.571,"F":-0.461,"S":-0.458,"T":-0.233,"W":-0.327,"Y":-0.451,"V":-0.263}
{"AccNo":"AVBF000109","PropDesc":"Slopes proteins, FDPB VFF neutral (Avbelj, 2000)","LITDBNo":"PMID:10903873","Author":"Avbelj, F.","ArtTitle":"Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins","JournalRef":"J. Mol. Biol. 300, 1335-1359 (2000) (Pro missing)","A":-0.376,"R":-0.28,"N":-0.403,"D":-0.405,"C":-0.441,"E":-0.362,"Q":-0.362,"G":-0.392,"H":-0.345,"I":-0.194,"L":-0.317,"K":-0.412,"M":-0.312,"F":-0.237,"S":-0.374,"T":-0.243,"W":-0.111,"Y":-0.171,"V":-0.355}
{"AccNo":"YANJ020101","PropDesc":"Side-chain conformation by gaussian evolutionary method (Yang et al., 2002)","LITDBNo":"PMID:12142444","Author":"Yang, J.M., Tsai, C.H., Hwang, M.J., Tsai, H.K., Hwang, J.K. and Kao, C.Y.","ArtTitle":"GEM: a Gaussian Evolutionary Method for predicting protein side-chain conformations","JournalRef":"Protein Sci. 11, 1897-1907 (2002) (Gly Ala missing)","R":0.62,"N":0.76,"D":0.66,"C":0.83,"E":0.73,"Q":0.59,"H":0.92,"I":0.88,"L":0.89,"K":0.77,"M":0.77,"F":0.92,"P":0.94,"S":0.58,"T":0.73,"W":0.86,"Y":0.93,"V":0.88}
{"AccNo":"MITS020101","PropDesc":"Amphiphilicity index (Mitaku et al., 2002)","LITDBNo":"PMID:12016058","Author":"Mitaku, S., Hirokawa, T. and Tsuji, T.","ArtTitle":"Amphiphilicity index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces","JournalRef":"Bioinformatics. 18, 608-616 (2002)","A":0,"R":2.45,"N":0,"D":0,"C":0,"E":1.27,"Q":1.25,"G":0,"H":1.45,"I":0,"L":0,"K":3.67,"M":0,"F":0,"P":0,"S":0,"T":0,"W":6.93,"Y":5.06,"V":0}
{"AccNo":"TSAJ990101","PropDesc":"Volumes including the crystallographic waters using the ProtOr (Tsai et al., 1999)","LITDBNo":"PMID:10388571","Author":"Tsai, J., Taylor, R., Chothia, C. and Gerstein, M.","ArtTitle":"The packing density in proteins: standard radii and volumes","JournalRef":"J. Mol. Biol. 290, 253-266 (1999) (Cyh 112.8)","A":89.3,"R":190.3,"N":122.4,"D":114.4,"C":102.5,"E":138.8,"Q":146.9,"G":63.8,"H":157.5,"I":163,"L":163.1,"K":165.1,"M":165.8,"F":190.8,"P":121.6,"S":94.2,"T":119.6,"W":226.4,"Y":194.6,"V":138.2}
{"AccNo":"TSAJ990102","PropDesc":"Volumes not including the crystallographic waters using the ProtOr (Tsai et al., 1999)","LITDBNo":"PMID:10388571","Author":"Tsai, J., Taylor, R., Chothia, C. and Gerstein, M.","ArtTitle":"The packing density in proteins: standard radii and volumes","JournalRef":"J. Mol. Biol. 290, 253-266 (1999) (Cyh 113.7)","A":90,"R":194,"N":124.7,"D":117.3,"C":103.3,"E":142.2,"Q":149.4,"G":64.9,"H":160,"I":163.9,"L":164,"K":167.3,"M":167,"F":191.9,"P":122.9,"S":95.4,"T":121.5,"W":228.2,"Y":197,"V":139}
{"AccNo":"COSI940101","PropDesc":"Electron-ion interaction potential values (Cosic, 1994)","LITDBNo":"PMID:7851912","Author":"Cosic, I.","ArtTitle":"Macromolecular bioactivity: is it resonant interaction between macromolecules?--Theory and applications","JournalRef":"IEEE Trans Biomed Eng. 41, 1101-1114 (1994) (values are cited from Protein Eng. 15:193-203)","A":0.0373,"R":0.0959,"N":0.0036,"D":0.1263,"C":0.0829,"E":0.0058,"Q":0.0761,"G":0.005,"H":0.0242,"I":0,"L":0,"K":0.0371,"M":0.0823,"F":0.0946,"P":0.0198,"S":0.0829,"T":0.0941,"W":0.0548,"Y":0.0516,"V":0.0057}
{"AccNo":"PONP930101","PropDesc":"Hydrophobicity scales (Ponnuswamy, 1993)","LITDBNo":"PMID:8419986","Author":"Ponnuswamy, P.K.","ArtTitle":"Hydrophobic characteristics of folded proteins","JournalRef":"Prog Biophys Mol Biol. 59, 57-103 (1993)","A":0.85,"R":0.2,"N":-0.48,"D":-1.1,"C":2.1,"E":-0.79,"Q":-0.42,"G":0,"H":0.22,"I":3.14,"L":1.99,"K":-1.19,"M":1.42,"F":1.69,"P":-1.14,"S":-0.52,"T":-0.08,"W":1.76,"Y":1.37,"V":2.53}
{"AccNo":"WILM950101","PropDesc":"Hydrophobicity coefficient in RP-HPLC, C18 with 0.1%TFA/MeCN/H2O (Wilce et al. 1995)","Author":"Wilce, M.C., Aguilar, M.I. and Hearn, M.T.","ArtTitle":"Physicochemical basis of amino acid hydrophobicity scales: evaluation of four new scales of amino acid hydrophobicity coefficients derived from RP-HPLC of peptides","JournalRef":"Anal Chem. 67, 1210-1219 (1995)","A":0.06,"R":-0.85,"N":0.25,"D":-0.2,"C":0.49,"E":-0.1,"Q":0.31,"G":0.21,"H":-2.24,"I":3.48,"L":3.5,"K":-1.62,"M":0.21,"F":4.8,"P":0.71,"S":-0.62,"T":0.65,"W":2.29,"Y":1.89,"V":1.59}
{"AccNo":"WILM950102","PropDesc":"Hydrophobicity coefficient in RP-HPLC, C8 with 0.1%TFA/MeCN/H2O (Wilce et al. 1995)","Author":"Wilce, M.C., Aguilar, M.I. and Hearn, M.T.","ArtTitle":"Physicochemical basis of amino acid hydrophobicity scales: evaluation of four new scales of amino acid hydrophobicity coefficients derived from RP-HPLC of peptides","JournalRef":"Anal Chem. 67, 1210-1219 (1995)","A":2.62,"R":1.26,"N":-1.27,"D":-2.84,"C":0.73,"E":-0.45,"Q":-1.69,"G":-1.15,"H":-0.74,"I":4.38,"L":6.57,"K":-2.78,"M":-3.12,"F":9.14,"P":-0.12,"S":-1.39,"T":1.81,"W":5.91,"Y":1.39,"V":2.3}
{"AccNo":"WILM950103","PropDesc":"Hydrophobicity coefficient in RP-HPLC, C4 with 0.1%TFA/MeCN/H2O (Wilce et al. 1995)","Author":"Wilce, M.C., Aguilar, M.I. and Hearn, M.T.","ArtTitle":"Physicochemical basis of amino acid hydrophobicity scales: evaluation of four new scales of amino acid hydrophobicity coefficients derived from RP-HPLC of peptides","JournalRef":"Anal Chem. 67, 1210-1219 (1995)","A":-1.64,"R":-3.28,"N":0.83,"D":0.7,"C":9.3,"E":1.18,"Q":-0.04,"G":-1.85,"H":7.17,"I":3.02,"L":0.83,"K":-2.36,"M":4.26,"F":-1.36,"P":3.12,"S":1.59,"T":2.31,"W":2.61,"Y":2.37,"V":0.52}
{"AccNo":"WILM950104","PropDesc":"Hydrophobicity coefficient in RP-HPLC, C18 with 0.1%TFA/2-PrOH/MeCN/H2O (Wilce et al. 1995)","Author":"Wilce, M.C., Aguilar, M.I. and Hearn, M.T.","ArtTitle":"Physicochemical basis of amino acid hydrophobicity scales: evaluation of four new scales of amino acid hydrophobicity coefficients derived from RP-HPLC of peptides","JournalRef":"Anal Chem. 67, 1210-1219 (1995)","A":-2.34,"R":1.6,"N":2.81,"D":-0.48,"C":5.03,"E":1.3,"Q":0.16,"G":-1.06,"H":-3,"I":7.26,"L":1.09,"K":1.56,"M":0.62,"F":2.57,"P":-0.15,"S":1.93,"T":0.19,"W":3.59,"Y":-2.58,"V":2.06}
{"AccNo":"KUHL950101","PropDesc":"Hydrophilicity scale (Kuhn et al., 1995)","LITDBNo":"PMID:8749849","Author":"Kuhn, L.A., Swanson, C.A., Pique, M.E., Tainer, J.A. and Getzoff, E.D.","ArtTitle":"Atomic and residue hydrophilicity in the context of folded protein structures","JournalRef":"Proteins 23, 536-547 (1995)","A":0.78,"R":1.58,"N":1.2,"D":1.35,"C":0.55,"E":1.45,"Q":1.19,"G":0.68,"H":0.99,"I":0.47,"L":0.56,"K":1.1,"M":0.66,"F":0.47,"P":0.69,"S":1,"T":1.05,"W":0.7,"Y":1,"V":0.51}
{"AccNo":"GUOD860101","PropDesc":"Retention coefficient at pH 2 (Guo et al., 1986)","Author":"Guo, D., Mant, C.T., Taneja, A.K., Parker, J.M. and Hodges, R.S.","ArtTitle":"Prediction of peptide retention times in reversed-phase high-performance liquid chromatography; I. determination of retention coefficients of amino acid residues of model synthetic peptides","JournalRef":"J Chromatogr. 359, 499-517 (1986)","A":25,"R":-7,"N":-7,"D":2,"C":32,"E":14,"Q":0,"G":-2,"H":-26,"I":91,"L":100,"K":-26,"M":68,"F":100,"P":25,"S":-2,"T":7,"W":109,"Y":56,"V":62}
{"AccNo":"JURD980101","PropDesc":"Modified Kyte-Doolittle hydrophobicity scale (Juretic et al., 1998)","Author":"Juretic, D., Lucic, B., Zucic, D. and Trinajstic, N.","ArtTitle":"Protein transmembrane structure: recognition and prediction by using hydrophobicity scales through preference functions","JournalRef":"Theoretical and Computational Chemistry, 5, 405-445 (1998)","A":1.1,"R":-5.1,"N":-3.5,"D":-3.6,"C":2.5,"E":-3.2,"Q":-3.68,"G":-0.64,"H":-3.2,"I":4.5,"L":3.8,"K":-4.11,"M":1.9,"F":2.8,"P":-1.9,"S":-0.5,"T":-0.7,"W":-0.46,"Y":-1.3,"V":4.2}
{"AccNo":"BASU050101","PropDesc":"Interactivity scale obtained from the contact matrix (Bastolla et al., 2005)","LITDBNo":"PMID:15523667","Author":"Bastolla, U., Porto M., Roman H.E. and Vendruscolo M.","ArtTitle":"Principal eigenvector of contact matrices and hydrophobicity profiles in prote","JournalRef":"Proteins 58, 22-30 (2005)","A":0.1366,"R":0.0363,"N":-0.0345,"D":-0.1233,"C":0.2745,"E":-0.0484,"Q":0.0325,"G":-0.0464,"H":0.0549,"I":0.4172,"L":0.4251,"K":-0.0101,"M":0.1747,"F":0.4076,"P":0.0019,"S":-0.0433,"T":0.0589,"W":0.2362,"Y":0.3167,"V":0.4084}
{"AccNo":"BASU050102","PropDesc":"Interactivity scale obtained by maximizing the mean of correlation coefficient over single-domain globular proteins (Bastolla et al., 2005)","LITDBNo":"PMID:15523667","Author":"Bastolla, U., Porto M., Roman H.E. and Vendruscolo M.","ArtTitle":"Principal eigenvector of contact matrices and hydrophobicity profiles in prote","JournalRef":"Proteins 58, 22-30 (2005)","A":0.0728,"R":0.0394,"N":-0.039,"D":-0.0552,"C":0.3557,"E":-0.0295,"Q":0.0126,"G":-0.0589,"H":0.0874,"I":0.3805,"L":0.3819,"K":-0.0053,"M":0.1613,"F":0.4201,"P":-0.0492,"S":-0.0282,"T":0.0239,"W":0.4114,"Y":0.3113,"V":0.2947}
{"AccNo":"BASU050103","PropDesc":"Interactivity scale obtained by maximizing the mean of correlation coefficient over pairs of sequences sharing the TIM barrel fold (Bastolla et al., 2005)","LITDBNo":"PMID:15523667","Author":"Bastolla, U., Porto M., Roman H.E. and Vendruscolo M.","ArtTitle":"Principal eigenvector of contact matrices and hydrophobicity profiles in prote","JournalRef":"Proteins 58, 22-30 (2005)","A":0.151,"R":-0.0103,"N":0.0381,"D":0.0047,"C":0.3222,"E":-0.0639,"Q":0.0246,"G":0.0248,"H":0.1335,"I":0.4238,"L":0.3926,"K":-0.0158,"M":0.216,"F":0.3455,"P":0.0844,"S":0.004,"T":0.1462,"W":0.2657,"Y":0.2998,"V":0.3997}
{"AccNo":"SUYM030101","PropDesc":"Linker propensity index (Suyama-Ohara, 2003)","LITDBNo":"PMID:12651735","Author":"Suyama, M. and Ohara, O.","ArtTitle":"DomCut: Prediction of inter-domain linker regions in amino acid sequences","JournalRef":"Bioinformatics 19, 673-674 (2003)","A":-0.058,"R":0,"N":0.027,"D":0.016,"C":0.447,"E":-0.128,"Q":-0.073,"G":0.331,"H":0.195,"I":0.06,"L":0.138,"K":-0.112,"M":0.275,"F":0.24,"P":-0.478,"S":-0.177,"T":-0.163,"W":0.564,"Y":0.322,"V":-0.052}
{"AccNo":"PUNT030101","PropDesc":"Knowledge-based membrane-propensity scale from 1D_Helix in MPtopo databases (Punta-Maritan, 2003)","LITDBNo":"PMID:12471604","Author":"Punta, M. and Maritan, A.","ArtTitle":"A knowledge-based scale for amino acid membrane propensity","JournalRef":"Proteins 50, 114-121 (2003)","A":-0.17,"R":0.37,"N":0.18,"D":0.37,"C":-0.06,"E":0.15,"Q":0.26,"G":0.01,"H":-0.02,"I":-0.28,"L":-0.28,"K":0.32,"M":-0.26,"F":-0.41,"P":0.13,"S":0.05,"T":0.02,"W":-0.15,"Y":-0.09,"V":-0.17}
{"AccNo":"PUNT030102","PropDesc":"Knowledge-based membrane-propensity scale from 3D_Helix in MPtopo databases (Punta-Maritan, 2003)","LITDBNo":"PMID:12471604","Author":"Punta, M. and Maritan, A.","ArtTitle":"A knowledge-based scale for amino acid membrane propensity","JournalRef":"Proteins 50, 114-121 (2003)","A":-0.15,"R":0.32,"N":0.22,"D":0.41,"C":-0.15,"E":0.3,"Q":0.03,"G":0.08,"H":0.06,"I":-0.29,"L":-0.36,"K":0.24,"M":-0.19,"F":-0.22,"P":0.15,"S":0.16,"T":-0.08,"W":-0.28,"Y":-0.03,"V":-0.24}
{"AccNo":"GEOR030101","PropDesc":"Linker propensity from all dataset (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":0.964,"R":1.143,"N":0.944,"D":0.916,"C":0.778,"E":1.051,"Q":1.047,"G":0.835,"H":1.014,"I":0.922,"L":1.085,"K":0.944,"M":1.032,"F":1.119,"P":1.299,"S":0.947,"T":1.017,"W":0.895,"Y":1,"V":0.955}
{"AccNo":"GEOR030102","PropDesc":"Linker propensity from 1-linker dataset (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":0.974,"R":1.129,"N":0.988,"D":0.892,"C":0.972,"E":1.054,"Q":1.092,"G":0.845,"H":0.949,"I":0.928,"L":1.11,"K":0.946,"M":0.923,"F":1.122,"P":1.362,"S":0.932,"T":1.023,"W":0.879,"Y":0.902,"V":0.923}
{"AccNo":"GEOR030103","PropDesc":"Linker propensity from 2-linker dataset (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":0.938,"R":1.137,"N":0.902,"D":0.857,"C":0.6856,"E":1.139,"Q":0.916,"G":0.892,"H":1.109,"I":0.986,"L":1,"K":0.952,"M":1.077,"F":1.11,"P":1.266,"S":0.956,"T":1.018,"W":0.971,"Y":1.157,"V":0.959}
{"AccNo":"GEOR030104","PropDesc":"Linker propensity from 3-linker dataset (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":1.042,"R":1.069,"N":0.828,"D":0.97,"C":0.5,"E":0.992,"Q":1.111,"G":0.743,"H":1.034,"I":0.852,"L":1.193,"K":0.979,"M":0.998,"F":0.981,"P":1.332,"S":0.984,"T":0.992,"W":0.96,"Y":1.12,"V":1.001}
{"AccNo":"GEOR030105","PropDesc":"Linker propensity from small dataset (linker length is less than six residues) (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":1.065,"R":1.131,"N":0.762,"D":0.836,"C":1.015,"E":0.736,"Q":0.861,"G":1.022,"H":0.973,"I":1.189,"L":1.192,"K":0.478,"M":1.369,"F":1.368,"P":1.241,"S":1.097,"T":0.822,"W":1.017,"Y":0.836,"V":1.14}
{"AccNo":"GEOR030106","PropDesc":"Linker propensity from medium dataset (linker length is between six and 14 residues) (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":0.99,"R":1.132,"N":0.873,"D":0.915,"C":0.644,"E":1.053,"Q":0.999,"G":0.785,"H":1.054,"I":0.95,"L":1.106,"K":1.003,"M":1.093,"F":1.121,"P":1.314,"S":0.911,"T":0.988,"W":0.939,"Y":1.09,"V":0.957}
{"AccNo":"GEOR030107","PropDesc":"Linker propensity from long dataset (linker length is greater than 14 residues) (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":0.892,"R":1.154,"N":1.144,"D":0.925,"C":1.035,"E":1.115,"Q":1.2,"G":0.917,"H":0.992,"I":0.817,"L":0.994,"K":0.944,"M":0.782,"F":1.058,"P":1.309,"S":0.986,"T":1.11,"W":0.841,"Y":0.866,"V":0.9}
{"AccNo":"GEOR030108","PropDesc":"Linker propensity from helical (annotated by DSSP) dataset (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":1.092,"R":1.239,"N":0.927,"D":0.919,"C":0.662,"E":1.199,"Q":1.124,"G":0.698,"H":1.012,"I":0.912,"L":1.276,"K":1.008,"M":1.171,"F":1.09,"P":0.8,"S":0.886,"T":0.832,"W":0.981,"Y":1.075,"V":0.908}
{"AccNo":"GEOR030109","PropDesc":"Linker propensity from non-helical (annotated by DSSP) dataset (George-Heringa, 2003)","LITDBNo":"PMID:12538906","Author":"George, R.A. and Heringa, J.","ArtTitle":"An analysis of protein domain linkers: their classification and role in protein folding","JournalRef":"Protein Eng. 15, 871-879 (2003)","A":0.843,"R":1.038,"N":0.956,"D":0.906,"C":0.896,"E":0.9,"Q":0.968,"G":0.978,"H":1.05,"I":0.946,"L":0.885,"K":0.893,"M":0.878,"F":1.151,"P":1.816,"S":1.003,"T":1.189,"W":0.852,"Y":0.945,"V":0.999}
{"AccNo":"ZHOH040101","PropDesc":"The stability scale from the knowledge-based atom-atom potential (Zhou-Zhou, 2004)","LITDBNo":"PMID:14696193","Author":"Zhou, H. and Zhou, Y.","ArtTitle":"Quantifying the effect of burial of amino acid residues on protein stability","JournalRef":"Proteins 54, 315-322 (2004)","A":2.18,"R":2.71,"N":1.85,"D":1.75,"C":3.89,"E":1.89,"Q":2.16,"G":1.17,"H":2.51,"I":4.5,"L":4.71,"K":2.12,"M":3.63,"F":5.88,"P":2.09,"S":1.66,"T":2.18,"W":6.46,"Y":5.01,"V":3.77}
{"AccNo":"ZHOH040102","PropDesc":"The relative stability scale extracted from mutation experiments (Zhou-Zhou, 2004)","LITDBNo":"PMID:14696193","Author":"Zhou, H. and Zhou, Y.","ArtTitle":"Quantifying the effect of burial of amino acid residues on protein stability","JournalRef":"Proteins 54, 315-322 (2004)","A":1.79,"R":3.2,"N":2.83,"D":2.33,"C":2.22,"E":2.52,"Q":2.37,"G":0.7,"H":3.06,"I":4.59,"L":4.72,"K":2.5,"M":3.91,"F":4.84,"P":2.45,"S":1.82,"T":2.45,"W":5.64,"Y":4.46,"V":3.67}
{"AccNo":"ZHOH040103","PropDesc":"Buriability (Zhou-Zhou, 2004)","LITDBNo":"PMID:14696193","Author":"Zhou, H. and Zhou, Y.","ArtTitle":"Quantifying the effect of burial of amino acid residues on protein stability","JournalRef":"Proteins 54, 315-322 (2004)","A":13.4,"R":8.5,"N":7.6,"D":8.2,"C":22.6,"E":7.3,"Q":8.5,"G":7,"H":11.3,"I":20.3,"L":20.8,"K":6.1,"M":15.7,"F":23.9,"P":9.9,"S":8.2,"T":10.3,"W":24.5,"Y":19.5,"V":19.5}
{"AccNo":"BAEK050101","PropDesc":"Linker index (Bae et al., 2005)","LITDBNo":"PMID:15746283","Author":"Bae, K., Mallick, B.K. and Elsik, C.G.","ArtTitle":"Prediction of protein inter-domain linker regions by a hidden Markov model","JournalRef":"Bioinformatics 21, ??-?? (2005)","A":0.0166,"R":-0.0762,"N":-0.0786,"D":-0.1278,"C":0.5724,"E":-0.1794,"Q":-0.1051,"G":-0.0442,"H":0.1643,"I":0.2758,"L":0.2523,"K":-0.2134,"M":0.0197,"F":0.3561,"P":-0.4188,"S":-0.1629,"T":-0.0701,"W":0.3836,"Y":0.25,"V":0.1782}
{"AccNo":"HARY940101","PropDesc":"Mean volumes of residues buried in protein interiors (Harpaz et al., 1994)","LITDBNo":"PMID: 7922041","Author":"Harpaz, Y., Gerstein, M. and Chothia, C.","ArtTitle":"Volume changes on protein folding","JournalRef":"Structure 2, 641-649 (1994) (Disulfide bonded cysteine, 103.5)","A":90.1,"R":192.8,"N":127.5,"D":117.1,"C":113.2,"E":140.8,"Q":149.4,"G":63.8,"H":159.3,"I":164.9,"L":164.6,"K":170,"M":167.7,"F":193.5,"P":123.1,"S":94.2,"T":120,"W":197.1,"Y":231.7,"V":139.1}
{"AccNo":"PONJ960101","PropDesc":"Average volumes of residues (Pontius et al., 1996)","LITDBNo":"PMID: 8950272","Author":"Pontius, J., Richelle, J. and Wodak, S.J.","ArtTitle":"Deviations from standard atomic volumes as a quality measure for protein crystal structures","JournalRef":"J. Mol. Biol 264, 121-136 (1996) (Disulfide bonded cysteine, 102.4)","A":91.5,"R":196.1,"N":138.3,"D":135.2,"C":114.4,"E":154.6,"Q":156.4,"G":67.5,"H":163.2,"I":162.6,"L":163.4,"K":162.5,"M":165.9,"F":198.8,"P":123.4,"S":102,"T":126,"W":209.8,"Y":237.2,"V":138.4}
{"AccNo":"DIGM050101","PropDesc":"Hydrostatic pressure asymmetry index, PAI (Di Giulio, 2005)","LITDBNo":"PMID: 15716096","Author":"Di Giulio M.","ArtTitle":"A comparison of proteins from Pyrococcus furiosus and Pyrococcus abyssi: barophily in the physicochemical properties of amino acids and in the genetic code","JournalRef":"Gene 346, 1-6 (2005)","A":1.076,"R":1.361,"N":1.056,"D":1.29,"C":0.753,"E":1.118,"Q":0.729,"G":1.346,"H":0.985,"I":0.926,"L":1.054,"K":1.105,"M":0.974,"F":0.869,"P":0.82,"S":1.342,"T":0.871,"W":0.666,"Y":0.531,"V":1.131}
{"AccNo":"WOLR790101","PropDesc":"Hydrophobicity index (Wolfenden et al., 1979)","LITDBNo":"PMID:493962","Author":"Wolfenden, R.V., Cullis, P.M. and Southgate, C.C.F.","ArtTitle":"Water, protein folding, and the genetic code","JournalRef":"Science 206, 575-577 (1979)","A":1.12,"R":-2.55,"N":-0.83,"D":-0.83,"C":0.59,"E":-0.92,"Q":-0.78,"G":1.2,"H":-0.93,"I":1.16,"L":1.18,"K":-0.8,"M":0.55,"F":0.67,"P":0.54,"S":-0.05,"T":-0.02,"W":-0.19,"Y":-0.23,"V":1.13}
{"AccNo":"OLSK800101","PropDesc":"Average internal preferences (Olsen, 1980)","LITDBNo":"PMID:7378453","Author":"Olsen, K.W.","ArtTitle":"Internal residue criteria for predicting three-dimensional protein structures","JournalRef":"Biochim. Biophys. Acta 622, 259-267 (1980)","A":1.38,"R":0,"N":0.37,"D":0.52,"C":1.43,"E":0.71,"Q":0.22,"G":1.34,"H":0.66,"I":2.32,"L":1.47,"K":0.15,"M":1.78,"F":1.72,"P":0.85,"S":0.86,"T":0.89,"W":0.82,"Y":0.47,"V":1.99}
{"AccNo":"KIDA850101","PropDesc":"Hydrophobicity-related index (Kidera et al., 1985)","Author":"Kidera, A., Konishi, Y., Oka, M., Ooi, T. and Scheraga, A.","ArtTitle":"Statistical Analysis of the Physical Properties of the 20 Naturally Occuring Amino Acids","JournalRef":"J. Prot. Chem. 4, 23-55 (1985)","A":-0.27,"R":1.87,"N":0.81,"D":0.81,"C":-1.05,"E":1.17,"Q":1.1,"G":-0.16,"H":0.28,"I":-0.77,"L":-1.1,"K":1.7,"M":-0.73,"F":-1.43,"P":-0.75,"S":0.42,"T":0.63,"W":-1.57,"Y":-0.56,"V":-0.4}
{"AccNo":"GUYH850102","PropDesc":"Apparent partition energies calculated from Wertz-Scheraga index (Guy, 1985)","LITDBNo":"PMID:3978191","Author":"Guy, H.R.","ArtTitle":"Amino acid side-chain partition energies and distribution of residues in soluble proteins","JournalRef":"Biophys. J. 47, 61-70 (1985)","A":0.05,"R":0.12,"N":0.29,"D":0.41,"C":-0.84,"E":0.38,"Q":0.46,"G":0.31,"H":-0.41,"I":-0.69,"L":-0.62,"K":0.57,"M":-0.38,"F":-0.45,"P":0.46,"S":0.12,"T":0.38,"W":-0.98,"Y":-0.25,"V":-0.46}
{"AccNo":"GUYH850103","PropDesc":"Apparent partition energies calculated from Robson-Osguthorpe index (Guy, 1985)","LITDBNo":"PMID:3978191","Author":"Guy, H.R.","ArtTitle":"Amino acid side-chain partition energies and distribution of residues in soluble proteins","JournalRef":"Biophys. J. 47, 61-70 (1985) (Gly missing)","A":0.54,"R":-0.16,"N":0.38,"D":0.65,"C":-1.13,"E":0.38,"Q":0.05,"H":-0.59,"I":-2.15,"L":-1.08,"K":0.48,"M":-0.97,"F":-1.51,"P":-0.22,"S":0.65,"T":0.27,"W":-1.61,"Y":-1.13,"V":-0.75}
{"AccNo":"GUYH850104","PropDesc":"Apparent partition energies calculated from Janin index (Guy, 1985)","LITDBNo":"PMID:3978191","Author":"Guy, H.R.","ArtTitle":"Amino acid side-chain partition energies and distribution of residues in soluble proteins","JournalRef":"Biophys. J. 47, 61-70 (1985)","A":-0.31,"R":1.3,"N":0.49,"D":0.58,"C":-0.87,"E":0.68,"Q":0.7,"G":-0.33,"H":0.13,"I":-0.66,"L":-0.53,"K":1.79,"M":-0.38,"F":-0.45,"P":0.34,"S":0.1,"T":0.21,"W":-0.27,"Y":0.4,"V":-0.62}
{"AccNo":"GUYH850105","PropDesc":"Apparent partition energies calculated from Chothia index (Guy, 1985)","LITDBNo":"PMID:3978191","Author":"Guy, H.R.","ArtTitle":"Amino acid side-chain partition energies and distribution of residues in soluble proteins","JournalRef":"Biophys. J. 47, 61-70 (1985)","A":-0.27,"R":2,"N":0.61,"D":0.5,"C":-0.23,"E":0.33,"Q":1,"G":-0.22,"H":0.37,"I":-0.8,"L":-0.44,"K":1.17,"M":-0.31,"F":-0.55,"P":0.36,"S":0.17,"T":0.18,"W":0.05,"Y":0.48,"V":-0.65}
{"AccNo":"ROSM880104","PropDesc":"Hydropathies of amino acid side chains, neutral form (Roseman, 1988)","LITDBNo":"PMID:3398047","Author":"Roseman, M.A.","ArtTitle":"Hydrophilicity of Polar Amino Acid Side-chains is Markedly Reduced by Flanking Peptide Bonds","JournalRef":"J. Mol. Biol. 200, 513-522 (1988) (Arg Pro missing)","A":0.39,"N":-1.91,"D":-0.71,"C":0.25,"E":-0.18,"Q":-1.3,"G":0,"H":-0.6,"I":1.82,"L":1.82,"K":0.32,"M":0.96,"F":2.27,"S":-1.24,"T":-1,"W":2.13,"Y":1.47,"V":1.3}
{"AccNo":"ROSM880105","PropDesc":"Hydropathies of amino acid side chains, pi-values in pH 7.0 (Roseman, 1988)","LITDBNo":"PMID:3398047","Author":"Roseman, M.A.","ArtTitle":"Hydrophilicity of Polar Amino Acid Side-chains is Markedly Reduced by Flanking Peptide Bonds","JournalRef":"J. Mol. Biol. 200, 513-522 (1988) (Pro missing)","A":0.39,"R":-3.95,"N":-1.91,"D":-3.81,"C":0.25,"E":-2.91,"Q":-1.3,"G":0,"H":-0.64,"I":1.82,"L":1.82,"K":-2.77,"M":0.96,"F":2.27,"S":-1.24,"T":-1,"W":2.13,"Y":1.47,"V":1.3}
{"AccNo":"JACR890101","PropDesc":"Weights from the IFH scale (Jacobs-White, 1989)","LITDBNo":"PMID:2742845","Author":"Jacobs, R. and White, S.H.","ArtTitle":"The nature of the hydrophobic bonding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices","JournalRef":"Biochemistry 28, 3421-3437 (1989)","A":0.18,"R":-5.4,"N":-1.3,"D":-2.36,"C":0.27,"E":-2.1,"Q":-1.22,"G":0.09,"H":-1.48,"I":0.37,"L":0.41,"K":-2.53,"M":0.44,"F":0.5,"P":-0.2,"S":-0.4,"T":-0.34,"W":-0.01,"Y":-0.08,"V":0.32}
{"AccNo":"COWR900101","PropDesc":"Hydrophobicity index, 3.0 pH (Cowan-Whittaker, 1990)","LITDBNo":"PMID:2134053","Author":"Cowan, R. and Whittaker, R.G.","ArtTitle":"Hydrophobicity indices for amino acid residues as determined by high-performance liquid chromatography","JournalRef":"Peptide Res. 3, 75-80 (1990)","A":0.42,"R":-1.56,"N":-1.03,"D":-0.51,"C":0.84,"E":-0.37,"Q":-0.96,"G":0,"H":-2.28,"I":1.81,"L":1.8,"K":-2.03,"M":1.18,"F":1.74,"P":0.86,"S":-0.64,"T":-0.26,"W":1.46,"Y":0.51,"V":1.34}
{"AccNo":"BLAS910101","PropDesc":"Scaled side chain hydrophobicity values (Black-Mould, 1991)","LITDBNo":"PMID:2042744","Author":"Black, S.D. and Mould D.R.","ArtTitle":"Development of Hydrophobicity Parameters to Analyze Proteins Which Bear Post- or Cotranslational Modifications","JournalRef":"Analytical Biochemistry 193, 72-82 (1991)","A":0.616,"R":0,"N":0.236,"D":0.028,"C":0.68,"E":0.043,"Q":0.251,"G":0.501,"H":0.165,"I":0.943,"L":0.943,"K":0.283,"M":0.738,"F":1,"P":0.711,"S":0.359,"T":0.45,"W":0.878,"Y":0.88,"V":0.825}
{"AccNo":"CASG920101","PropDesc":"Hydrophobicity scale from native protein structures (Casari-Sippl, 1992)","LITDBNo":"PMID:1569551","Author":"Casari, G. and Sippl, M.","ArtTitle":"Structure-derived Hydrophobic Potential. Hydrophobic Potential Derived from X-ray Structures of Globular Proteins is able to Identify Native Folds","JournalRef":"J. Mol. Biol. 224, 725-732 (1992)","A":0.2,"R":-0.7,"N":-0.5,"D":-1.4,"C":1.9,"E":-1.3,"Q":-1.1,"G":-0.1,"H":0.4,"I":1.4,"L":0.5,"K":-1.6,"M":0.5,"F":1,"P":-1,"S":-0.7,"T":-0.4,"W":1.6,"Y":0.5,"V":0.7}
{"AccNo":"CORJ870101","PropDesc":"NNEIG index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":50.76,"R":48.66,"N":45.8,"D":43.17,"C":58.74,"E":43.48,"Q":46.09,"G":50.27,"H":49.33,"I":57.3,"L":53.89,"K":42.92,"M":52.75,"F":53.45,"P":45.39,"S":47.24,"T":49.26,"W":53.59,"Y":51.79,"V":56.12}
{"AccNo":"CORJ870102","PropDesc":"SWEIG index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":-0.414,"R":-0.584,"N":-0.916,"D":-1.31,"C":0.162,"E":-1.218,"Q":-0.905,"G":-0.684,"H":-0.63,"I":1.237,"L":1.215,"K":-0.67,"M":1.02,"F":1.938,"P":-0.503,"S":-0.563,"T":-0.289,"W":0.514,"Y":1.699,"V":0.899}
{"AccNo":"CORJ870103","PropDesc":"PRIFT index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":-0.96,"R":0.75,"N":-1.94,"D":-5.68,"C":4.54,"E":-3.86,"Q":-5.3,"G":-1.28,"H":-0.62,"I":5.54,"L":6.81,"K":-5.62,"M":4.76,"F":5.06,"P":-4.47,"S":-1.92,"T":-3.99,"W":0.21,"Y":3.34,"V":5.39}
{"AccNo":"CORJ870104","PropDesc":"PRILS index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":-0.26,"R":0.08,"N":-0.46,"D":-1.3,"C":0.83,"E":-0.73,"Q":-0.83,"G":-0.4,"H":-0.18,"I":1.1,"L":1.52,"K":-1.01,"M":1.09,"F":1.09,"P":-0.62,"S":-0.55,"T":-0.71,"W":-0.13,"Y":0.69,"V":1.15}
{"AccNo":"CORJ870105","PropDesc":"ALTFT index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":-0.73,"R":-1.03,"N":-5.29,"D":-6.13,"C":0.64,"E":-2.9,"Q":-0.96,"G":-2.67,"H":3.03,"I":5.04,"L":4.91,"K":-5.99,"M":3.34,"F":5.2,"P":-4.32,"S":-3,"T":-1.91,"W":0.51,"Y":2.87,"V":3.98}
{"AccNo":"CORJ870106","PropDesc":"ALTLS index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":-1.35,"R":-3.89,"N":-10.96,"D":-11.88,"C":4.37,"E":-4.56,"Q":-1.34,"G":-5.82,"H":6.54,"I":10.93,"L":9.88,"K":-11.92,"M":7.47,"F":11.35,"P":-10.86,"S":-6.21,"T":-4.83,"W":1.8,"Y":7.61,"V":8.2}
{"AccNo":"CORJ870107","PropDesc":"TOTFT index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":-0.56,"R":-0.26,"N":-2.87,"D":-4.31,"C":1.78,"E":-2.35,"Q":-2.31,"G":-1.35,"H":0.81,"I":3.83,"L":4.09,"K":-4.08,"M":3.11,"F":3.67,"P":-3.22,"S":-1.85,"T":-1.97,"W":-0.11,"Y":2.17,"V":3.31}
{"AccNo":"CORJ870108","PropDesc":"TOTLS index (Cornette et al., 1987)","LITDBNo":"PMID:3656427","Author":"Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. and DeLisi, C.","ArtTitle":"Hydrophobicity Scales and Computational Techniques for Detecting Amphipathic Structures in Proteins","JournalRef":"J. Mol. Biol. 196, 659-685, (1987)","A":1.37,"R":1.33,"N":6.29,"D":8.93,"C":-4.47,"E":4.04,"Q":3.88,"G":3.39,"H":-1.65,"I":-7.92,"L":-8.68,"K":7.7,"M":-7.13,"F":-7.96,"P":6.25,"S":4.08,"T":4.02,"W":0.79,"Y":-4.73,"V":-6.94}
{"AccNo":"MIYS990101","PropDesc":"Relative partition energies derived by the Bethe approximation (Miyazawa-Jernigan, 1999)","LITDBNo":"PMID:10336383","Author":"Miyazawa, S. and Jernigan, R. L.","ArtTitle":"Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues","JournalRef":"Proteins 34, 49-68 (1999)","A":-0.02,"R":0.44,"N":0.63,"D":0.72,"C":-0.96,"E":0.74,"Q":0.56,"G":0.38,"H":0,"I":-1.89,"L":-2.29,"K":1.01,"M":-1.36,"F":-2.22,"P":0.47,"S":0.55,"T":0.25,"W":-1.28,"Y":-0.88,"V":-1.34}
{"AccNo":"MIYS990102","PropDesc":"Optimized relative partition energies - method A (Miyazawa-Jernigan, 1999)","LITDBNo":"PMID:10336383","Author":"Miyazawa, S. and Jernigan, R. L.","ArtTitle":"Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues","JournalRef":"Proteins 34, 49-68 (1999)","A":0,"R":0.07,"N":0.1,"D":0.12,"C":-0.16,"E":0.12,"Q":0.09,"G":0.06,"H":0,"I":-0.31,"L":-0.37,"K":0.17,"M":-0.22,"F":-0.36,"P":0.08,"S":0.09,"T":0.04,"W":-0.21,"Y":-0.14,"V":-0.22}
{"AccNo":"MIYS990103","PropDesc":"Optimized relative partition energies - method B (Miyazawa-Jernigan, 1999)","LITDBNo":"PMID:10336383","Author":"Miyazawa, S. and Jernigan, R. L.","ArtTitle":"Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues","JournalRef":"Proteins 34, 49-68 (1999)","A":-0.03,"R":0.09,"N":0.13,"D":0.17,"C":-0.36,"E":0.23,"Q":0.13,"G":0.09,"H":-0.04,"I":-0.33,"L":-0.38,"K":0.32,"M":-0.3,"F":-0.34,"P":0.2,"S":0.1,"T":0.01,"W":-0.24,"Y":-0.23,"V":-0.29}
{"AccNo":"MIYS990104","PropDesc":"Optimized relative partition energies - method C (Miyazawa-Jernigan, 1999)","LITDBNo":"PMID:10336383","Author":"Miyazawa, S. and Jernigan, R. L.","ArtTitle":"Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues","JournalRef":"Proteins 34, 49-68 (1999)","A":-0.04,"R":0.07,"N":0.13,"D":0.19,"C":-0.38,"E":0.23,"Q":0.14,"G":0.09,"H":-0.04,"I":-0.34,"L":-0.37,"K":0.33,"M":-0.3,"F":-0.38,"P":0.19,"S":0.12,"T":0.03,"W":-0.33,"Y":-0.29,"V":-0.29}
{"AccNo":"MIYS990105","PropDesc":"Optimized relative partition energies - method D (Miyazawa-Jernigan, 1999)","LITDBNo":"PMID:10336383","Author":"Miyazawa, S. and Jernigan, R. L.","ArtTitle":"Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues","JournalRef":"Proteins 34, 49-68 (1999)","A":-0.02,"R":0.08,"N":0.1,"D":0.19,"C":-0.32,"E":0.21,"Q":0.15,"G":-0.02,"H":-0.02,"I":-0.28,"L":-0.32,"K":0.3,"M":-0.25,"F":-0.33,"P":0.11,"S":0.11,"T":0.05,"W":-0.27,"Y":-0.23,"V":-0.23}
{"AccNo":"ENGD860101","PropDesc":"Hydrophobicity index (Engelman et al., 1986)","LITDBNo":"PMID:3521657","Author":"Engelman, D.M., Steitz, T.A. and Goldman, A.","ArtTitle":"Identifying Nonpolar Transbilayer Helices in Amino Acid Sequences of Membrane Proteins","JournalRef":"Ann.Rev.Biophys.Biophys.Chem. 15, 321-353 (1986)","A":-1.6,"R":12.3,"N":4.8,"D":9.2,"C":-2,"E":8.2,"Q":4.1,"G":-1,"H":3,"I":-3.1,"L":-2.8,"K":8.8,"M":-3.4,"F":-3.7,"P":0.2,"S":-0.6,"T":-1.2,"W":-1.9,"Y":0.7,"V":-2.6}
{"AccNo":"FASG890101","PropDesc":"Hydrophobicity index (Fasman, 1989)","Author":"Fasman, G.D.","ArtTitle":"Prediction of Protein Structure and the Principles of Protein Conformation","JournalRef":"Plenum, New York 1989, page 457, Table XVII","A":-0.21,"R":2.11,"N":0.96,"D":1.36,"C":-6.04,"E":2.3,"Q":1.52,"G":0,"H":-1.23,"I":-4.81,"L":-4.68,"K":3.88,"M":-3.66,"F":-4.65,"P":0.75,"S":1.74,"T":0.78,"W":-3.32,"Y":-1.01,"V":-3.5}