H TANS760101
D Statistical contact potential derived from 25 x-ray protein structures
R PMID:1004017
A Tanaka, S. and Scheraga, H.A.
T Medium- and long-range interaction parameters between amino acids 
  for predicting three-dimensional structures of proteins
J Macromolecules 9, 945-950 (1976)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
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  -4.3 -4.9 -4.3 -4.0 -6.0 -4.7 -4.2 -5.1 -5.3 -7.3 -6.2 -4.2 -6.0 -6.5 -4.7 -4.2 -4.4 -6.5 -5.9 -5.5
//
H TANS760102
D Number of contacts between side chains derived from 25 x-ray protein structures
R PMID:1004017
A Tanaka, S. and Scheraga, H.A.
T Medium- and long-range interaction parameters between amino acids
  for predicting three-dimensional structures of proteins
J Macromolecules 9, 945-950 (1976)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   36
   20 14
   39 34 22
   36 35 31 24
   15 13 21 10 48
   34 29 30 17 13  7
   27 34 27 38  9 19  9
  115 58 80 83 53 75 54  75
   25 17 25 32 11 17 24  40  8
  119 33 51 43 33 29 35 109 27  81
  174 47 63 60 49 53 53 155 49 230 167
   55 20 39 54 14 32 70  92 21  53  86 20
   26  9  7 13 11  1 12  32  7  44  58 21  6
   62 32 27 32 32 21 22  67 38 103 175 32 20  53
   33 20 22 23 24 23 17  62 15  41  46 34 16  19 11
   64 44 42 37 28 44 41 145 43  65  93 51 14  36 38  34
   70 36 46 38 22 28 28 116 36  67 110 50 16  39 32  69  29
   38 15 21 24 17 22 15  52 23  40  68 20 17  41 19  31  20  7
   65 45 50 52 43 32 40 103 44  81 105 64 19  45 42  71  53 32  33
  101 44 50 53 53 46 39 183 42 216 306 67 52 114 58 106  79 62  85 152
//
H ROBB790102
D Interaction energies derived from side chain contacts in the interiors of
  known protein structures
R PMID:513136
A Robson, B. and Osguthorpe, D.J.
T 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
J J. Mol. Biol. 132, 19-51 (1979)
* (Glu is not available)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.268
   0.529 3.717
   0.010 1.153  0.130
   0.926 5.172  1.921  6.271
  -0.180 5.014  0.245 10.310 -20.000
   0.017 1.212  0.149  2.021   0.296  0.169
   0.902 4.911  1.835  6.052   9.050  1.926  5.832
    NA    NA     NA     NA      NA     NA     NA    NA
  -0.187 1.759  0.088  3.336  -0.099  0.112  3.090   NA  -0.106
  -0.899 1.278 -0.577  3.643  -0.811 -0.547  3.248   NA  -0.818 -1.530
  -0.865 2.952 -0.542  8.760  -0.777 -0.513  7.540   NA  -0.784 -1.496 -1.461
   0.920 4.514  1.808  5.256   8.223  1.910  5.139   NA   3.084  3.368  7.538  4.533
  -0.525 6.049 -0.202 14.958  -0.437 -0.173 12.775   NA  -0.443 -1.156 -1.121 11.998 -0.781
  -0.961 0.394 -0.638  1.098  -0.873 -0.609  1.021   NA  -0.879 -1.592 -1.557  1.135 -1.217 -1.653
  -1.470 0.099 -1.148  0.322  -1.382 -1.118  0.449   NA  -1.389 -2.101 -2.066  0.817 -1.726 -2.162 -2.672
   0.022 1.048  0.134  1.660   0.376  0.153  1.603   NA   0.133 -0.476 -0.441  1.554 -0.101 -0.537 -1.047  0.128
  -0.177 1.054  0.053  1.890  -0.089  0.067  1.792   NA  -0.096 -0.808 -0.773  1.786 -0.433 -0.869 -1.379  0.072 -0.085
  -1.052 2.069 -0.730  7.299  -0.964 -0.700  6.288   NA  -0.971 -1.683 -1.649  6.663 -1.308 -1.744 -2.254 -0.629 -0.961 -1.836
  -0.899 2.657 -0.577  8.069  -0.811 -0.547  6.961   NA  -0.818 -1.530 -1.495  7.042 -1.155 -1.591 -2.101 -0.476 -0.807 -1.683 -1.530
  -0.617 0.944 -0.295  2.100  -0.529 -0.265  1.944   NA  -0.536 -1.248 -1.214  2.000 -0.874 -1.310 -1.819 -0.194 -0.526 -1.401 -1.248 -0.966
//
H BRYS930101
D Distance-dependent statistical potential (only energies of contacts within
   0-5 Angstrooms are included)
R PMID:8497488
A Bryant, S.H. and Lawrence, C.E.
T An Empirical Energy Function for Threading Protein-Sequence Through the
  Folding Motif
J Proteins 16, 92-112 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.230
   0.237 -0.145
   0.159 -0.303 -0.206
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  -0.008  0.222 -0.187 -0.128  0.487 -0.430
   0.182 -0.717 -0.262 -0.178  0.121 -0.728  1.060
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  -0.535 -0.014  0.456  0.229 -0.415  0.020  0.385  0.127 -0.062 -0.051
  -0.245  0.374  0.430  0.316 -0.061  0.391  0.480 -0.004  0.029 -0.223 -0.070
   0.063  0.734  0.222 -0.759  1.115 -0.181 -0.782  0.065 -0.235 -0.058 -0.015  0.567
  -0.364  0.509  0.405  0.097 -0.032  0.013  0.188  0.084  0.293 -0.103 -0.253  0.347 -0.006
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   0.022 -0.176  0.109  0.175 -0.199 -0.545 -0.064  0.127  0.037  0.382 -0.170  0.068 -0.104 -0.083  0.033
   0.115 -0.263 -0.334 -0.565 -0.164  0.298 -0.207 -0.100  0.080  0.254  0.390 -0.246  0.259  0.357  0.057 -0.150
   0.002  0.250 -0.018 -0.433  0.021  0.060 -0.006 -0.106  0.061  0.167  0.075 -0.170  0.087  0.058  0.108 -0.430 -0.315
   0.117 -0.244  0.538  1.287  0.080  0.459 -0.089  0.036 -0.098 -0.505 -0.635 -0.822 -0.783 -0.185 -0.312  0.298  0.040  0.707
  -0.030  0.044 -0.491  0.694  0.069 -0.036 -0.004  0.121 -0.305 -0.100 -0.289 -0.294 -0.218 -0.335  0.071  0.442  0.492 -0.105  0.211
  -0.359 -0.011  0.158  0.442 -0.026 -0.191  0.255  0.141  0.006 -0.253 -0.454  0.253 -0.265 -0.288  0.358  0.316  0.251 -0.034  0.075 -0.641
//
H THOP960101
D Mixed quasichemical and optimization-based protein contact potential
R PMID:8876187 
A Thomas, P.D. and Dill, K.A.
T An iterative method for extracting energy-like quantities 
  from protein structures
J Proc. Natl. Acad. Sci. USA 93, 11628-11633 (1996)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.08
   0.07  0.23
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   0.00  0.30  0.18 -0.09  0.00  0.04 -0.09  0.10  0.14 -0.26  0.10  1.45
   0.05 -0.43  0.31  1.07 -1.23 -0.54  0.02  0.00 -0.35 -0.41 -0.31  0.55  0.36
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   0.41 -0.02  0.11  0.84  0.07 -0.21  0.33  0.40 -0.22  0.25  0.09  0.51 -0.25 -0.43  0.28
  -0.01  0.61  0.37 -0.09 -0.20  0.40  0.30 -0.04 -0.59 -0.13 -0.07  0.18 -0.47  0.14  0.44 -0.13
  -0.22 -0.17 -0.27 -0.03 -0.38 -0.17  0.15  0.13 -0.27 -0.29 -0.39  0.09  0.06 -0.19  0.36  0.05  0.26
  -0.08 -0.78 -0.68  0.24 -0.30  0.40  0.32 -0.14 -0.41 -0.89 -0.97 -0.30 -0.07 -0.89 -0.44 -0.20  0.07  0.02
  -0.37  0.21 -0.74  0.11 -0.96 -0.39  0.22 -0.32 -0.67 -0.87 -0.60 -0.20 -1.10 -0.82 -0.45  0.25 -0.23 -0.99  0.35
  -0.60 -0.48 -0.24  0.25 -0.94 -0.09 -0.02 -0.20 -0.35 -0.98 -1.03 -0.08 -0.94 -0.78 -0.08 -0.31  0.06 -0.60 -0.70 -1.15
//
H MIRL960101
D Statistical potential derived by the maximization of the harmonic mean of Z
  scores
R PMID:9000638
A Mirny, L.A. and Shakhnovich, E.I.
T How to derive a protein folding potential? A new approach 
  to an old problem
J J. Mol. Biol. 264, 1164-1179 (1996)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
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   0.43  0.11
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   0.12 -0.72 -0.30  0.04
   0.00  0.24  0.13  0.03 -1.06
   0.08 -0.52 -0.25 -0.17  0.05  0.29
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  -0.22  0.42  0.53  0.59  0.16  0.36  0.35  0.25  0.49 -0.22
  -0.01  0.35  0.30  0.67 -0.08  0.26  0.43  0.23  0.16 -0.41 -0.27
   0.14  0.75 -0.33 -0.76  0.71 -0.38 -0.97  0.11  0.22  0.36  0.19  0.25
   0.25  0.31  0.08  0.65  0.19  0.46  0.44  0.19  0.99 -0.28 -0.20  0.00  0.04
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   0.10 -0.38 -0.18  0.04  0.00 -0.42 -0.10 -0.11 -0.21  0.25  0.42  0.11 -0.34  0.20  0.26
  -0.06  0.17 -0.14 -0.31 -0.02 -0.14 -0.26 -0.16 -0.05  0.21  0.25 -0.13  0.14  0.29  0.01 -0.20
  -0.09 -0.35 -0.11 -0.29  0.19 -0.14  0.00 -0.26 -0.19  0.14  0.20 -0.09  0.19  0.31 -0.07 -0.08  0.03
  -0.09 -0.16  0.06  0.24  0.08  0.08  0.29  0.18 -0.12  0.02 -0.09  0.22 -0.67 -0.16 -0.28  0.34  0.22 -0.12
   0.09 -0.25 -0.20  0.00  0.04 -0.20 -0.10  0.14 -0.34  0.11  0.24 -0.21 -0.13  0.00 -0.33  0.09  0.13 -0.04  0.06
  -0.10  0.30  0.50  0.58  0.06  0.24  0.34  0.16  0.19 -0.25 -0.29  0.44 -0.14 -0.22  0.09  0.18  0.25 -0.07  0.02 -0.29
//
H VENM980101
D Statistical potential derived by the maximization of the perceptron criterion
R 
A Vendruscolo, M. and Domany E.
T Pairwise contact potentials are unsuitable for protein folding
J J. Chem. Phys. 109, 11101-11108 (1998)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
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   0.00069  0.1005  0.00943  0.01585 -0.18164
   0.02297 -0.1314  0.04386 -0.08755  0.03575  0.0197
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   0.00916 -0.0218 -0.00094 -0.03380 -0.03699  0.0522 -0.1188  0.0876 -0.02649
  -0.10044  0.0338  0.04248  0.01813 -0.00256  0.0548  0.0500  0.0339 -0.00602 -0.0449
  -0.00789  0.0164  0.01271  0.02074  0.07471  0.0215  0.0173  0.0932  0.01358 -0.1608 -0.0980
   0.04718  0.0131  0.00884 -0.09309  0.01137 -0.0489 -0.1536  0.0376  0.02636  0.0175  0.0509  0.1122
   0.07572  0.0583  0.03734  0.06106  0.13069  0.0304  0.1327  0.0944 -0.01512 -0.0974 -0.0624  0.0602  0.0140
   0.03878  0.0041  0.00294  0.01164 -0.04520 -0.1336  0.0136 -0.1882 -0.09404 -0.1160 -0.0551  0.0384 -0.0876 -0.11542
   0.07816 -0.0620  0.01251  0.04375 -0.01505 -0.0837  0.0724  0.0982 -0.07370  0.0427  0.0211  0.1598 -0.0395  0.06601  0.013
   0.00648  0.0856 -0.00054  0.00055  0.01582 -0.0284 -0.1229 -0.0505  0.00167  0.0070  0.0255 -0.0366  0.0551 -0.00013  0.112 -0.06670
  -0.03831 -0.0930  0.00302 -0.04220  0.14216  0.0725  0.0788 -0.0574 -0.00499  0.0158  0.0169  0.0082  0.0894  0.01352  0.062  0.00262  0.06636
   0.00950 -0.0219 -0.01788 -0.00609  0.04886 -0.0157  0.1134  0.1083 -0.01956  0.0093 -0.0410  0.0117 -0.2448  0.00303 -0.174  0.07002  0.06563 -0.0382
   0.01587 -0.0652 -0.07248  0.00165  0.02167 -0.0290 -0.0183  0.0607 -0.07678 -0.0112  0.0540 -0.1090  0.0085  0.01074 -0.091  0.06797  0.05679  0.0610 -0.0484
  -0.08515  0.0230  0.01472  0.06840 -0.06069  0.0097  0.0595  0.0406 -0.00100 -0.1095 -0.1274  0.0331 -0.0634 -0.03358  0.027  0.03116 -0.00024  0.0260 -0.0303 -0.07182
//
H BASU010101
D Optimization-based potential derived by the modified perceptron criterion
R PMID:11391771
A Bastolla, U., Farwer, J., Knapp, E.W. and Vendruscolo, M.
T How to guarantee optimal stability for most representative 
  structures in the protein data bank
J Proteins 44, 79-96 (2001)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
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   0.1049  0.0306
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   0.0310 -0.0210  0.0155  0.1043 -0.0013 -0.0243  0.0675  0.1763  0.0681 -0.0700 -0.0316  0.0467  0.0018 -0.1120  0.1908  0.0228  0.0150
  -0.0880 -0.2070 -0.0250 -0.0124 -0.1176 -0.0540 -0.0967 -0.1567 -0.0200 -0.1961 -0.2639 -0.1152 -0.0775 -0.3405 -0.0910 -0.0802  0.0052 -0.1066
  -0.1408 -0.1369 -0.1149 -0.1165 -0.2444 -0.1431 -0.0522 -0.0176 -0.1976 -0.3164 -0.2614 -0.1120 -0.1621 -0.4212 -0.1326  0.0214 -0.1445 -0.3209 -0.2793
  -0.1431  0.0475  0.1180  0.2728 -0.2349  0.1061  0.1010  0.1859 -0.0039 -0.4223 -0.4593  0.0609 -0.2127 -0.4001  0.0868  0.1766  0.0119 -0.2898 -0.2792 -0.5193
//
H MIYS850102
D Quasichemical energy of transfer of amino acids from water to the protein
  environment
A Miyazawa, S. and Jernigan, R.L.
T Estimation of Effective Interresidue Contact Energies
  from Protein Crystal-Structures-Quasi-Chemical Approximation
J Macromolecules 18, 534-552 (1985)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -2.51
  -1.50 -1.39
  -1.44 -1.41 -1.59
  -1.57 -1.98 -1.33 -0.96
  -3.38 -2.70 -2.59 -2.66 -5.44
  -1.70 -1.85 -1.36 -1.26 -2.73 -0.89
  -1.51 -2.07 -1.43 -1.23 -2.08 -1.33 -1.18
  -2.15 -1.68 -1.56 -1.62 -3.16 -1.54 -1.22 -2.17
  -2.09 -2.12 -2.01 -2.14 -3.63 -1.85 -2.27 -1.94 -2.78
  -4.41 -3.33 -2.99 -2.91 -5.03 -3.22 -3.23 -3.65 -3.76 -6.22
  -3.96 -3.15 -2.99 -2.59 -5.03 -3.09 -2.91 -3.43 -3.84 -6.17 -5.79
  -1.10 -0.06 -0.91 -1.32 -1.54 -1.02 -1.60 -0.84 -1.09 -2.70 -2.63  0.13
  -3.99 -3.49 -3.50 -2.90 -5.05 -3.17 -3.19 -3.75 -3.31 -6.33 -6.01 -3.11 -6.06
  -4.36 -3.54 -3.55 -3.31 -5.63 -3.30 -3.51 -3.72 -4.61 -6.39 -6.26 -2.83 -6.68 -6.85
  -1.81 -1.85 -1.43 -1.19 -2.92 -1.73 -1.40 -1.72 -2.17 -3.47 -3.06 -0.67 -4.11 -3.73 -1.18
  -1.89 -1.22 -1.31 -1.46 -2.86 -1.37 -1.48 -1.70 -1.94 -3.43 -3.16 -0.83 -3.55 -3.56 -1.35 -1.48
  -2.15 -1.97 -1.51 -1.66 -2.88 -1.59 -1.45 -2.03 -2.31 -3.74 -3.43 -1.02 -3.73 -3.76 -1.66 -1.59 -1.72
  -3.93 -3.56 -3.11 -2.91 -4.76 -3.16 -2.94 -3.37 -4.02 -5.64 -5.50 -2.49 -6.37 -6.02 -3.66 -2.95 -3.31 -5.42
  -2.85 -2.75 -2.47 -2.25 -3.89 -2.53 -2.42 -2.50 -3.33 -4.63 -4.26 -2.01 -4.92 -4.95 -2.80 -2.30 -2.48 -4.44 -3.55
  -3.62 -2.78 -2.36 -2.25 -4.46 -2.67 -2.56 -3.06 -3.38 -5.58 -5.38 -1.95 -5.52 -5.75 -2.96 -2.79 -2.95 -5.05 -4.05 -4.94
//
H MIYS850103
D Quasichemical energy of interactions in an average buried environment
A Miyazawa, S. and Jernigan, R.L.
T Estimation of Effective Interresidue Contact Energies 
  from Protein Crystal-Structures-Quasi-Chemical Approximation
J Macromolecules 18, 534-552 (1985)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.13
   0.44  0.11
   0.28 -0.13 -0.53
   0.12 -0.73 -0.30  0.04
   0.00  0.24  0.13  0.03 -1.06
   0.07 -0.52 -0.25 -0.18  0.04  0.27
   0.25 -0.75 -0.33 -0.16  0.68 -0.18 -0.04
  -0.07 -0.04 -0.14 -0.23 -0.08 -0.07  0.24 -0.39
   0.34 -0.13 -0.24 -0.40 -0.20 -0.03 -0.46  0.19 -0.30
  -0.22  0.42  0.54  0.59  0.16  0.36  0.34  0.24  0.48 -0.22
  -0.01  0.36  0.30  0.67 -0.08  0.25  0.42  0.22  0.16 -0.41 -0.27
   0.15  0.75 -0.32 -0.76  0.71 -0.38 -0.97  0.11  0.21  0.36  0.19  0.25
   0.25  0.31  0.08  0.65  0.19  0.46  0.43  0.19  0.98 -0.28 -0.20  0.00  0.04
   0.03  0.41  0.18  0.39 -0.24  0.48  0.26  0.37 -0.17 -0.19 -0.30  0.43 -0.43 -0.45
   0.10 -0.38 -0.18  0.03 -0.01 -0.43 -0.11 -0.11 -0.21  0.25  0.42  0.11 -0.34  0.19  0.26
  -0.06  0.17 -0.14 -0.32 -0.03 -0.15 -0.27 -0.17 -0.06  0.21  0.24 -0.13  0.14  0.28  0.01 -0.20
  -0.09 -0.35 -0.11 -0.29  0.18 -0.14 -0.01 -0.27 -0.20  0.13  0.20 -0.09  0.19  0.31 -0.07 -0.08  0.02
  -0.09 -0.16  0.07  0.24  0.08  0.07  0.28  0.17 -0.13  0.01 -0.09  0.22 -0.67 -0.17 -0.29  0.34  0.21 -0.12
   0.08 -0.26 -0.20 -0.01  0.04 -0.21 -0.11  0.13 -0.35  0.11  0.24 -0.21 -0.13 -0.01 -0.34  0.08  0.13 -0.05 -0.07
  -0.11  0.29  0.49  0.57  0.05  0.23  0.33  0.15  0.18 -0.26 -0.30  0.43 -0.15 -0.23  0.08  0.17  0.24 -0.08  0.01 -0.30
//
H MIYS960101
D Quasichemical energy of transfer of amino acids from water to the protein
  environment
R PMID:8604144
A Miyazawa, S. and Jernigan, R.L.
T Residue-residue potentials with a favorable contact pair term
  and an unfavorable high packing density term, for simulation
  and threading
J J. Mol. Biol. 256, 623-644 (1996)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -2.72
  -1.83 -1.55
  -1.84 -1.64 -1.68
  -1.70 -2.29 -1.68 -1.21
  -3.57 -2.57 -2.59 -2.41 -5.44
  -1.89 -1.80 -1.71 -1.46 -2.85 -1.54
  -1.51 -2.27 -1.51 -1.02 -2.27 -1.42 -0.91
  -2.31 -1.72 -1.74 -1.59 -3.16 -1.66 -1.22 -2.24
  -2.41 -2.16 -2.08 -2.32 -3.60 -1.98 -2.15 -2.15 -3.05
  -4.58 -3.63 -3.24 -3.17 -5.50 -3.67 -3.27 -3.78 -4.14 -6.54
  -4.91 -4.03 -3.74 -3.40 -5.83 -4.04 -3.59 -4.16 -4.54 -7.04 -7.37
  -1.31 -0.59 -1.21 -1.68 -1.95 -1.29 -1.80 -1.15 -1.35 -3.01 -3.37 -0.12
  -3.94 -3.12 -2.95 -2.57 -4.99 -3.30 -2.89 -3.39 -3.98 -6.02 -6.41 -2.48 -5.46
  -4.81 -3.98 -3.75 -3.48 -5.80 -4.10 -3.56 -4.13 -4.77 -6.84 -7.28 -3.36 -6.56 -7.26
  -2.03 -1.70 -1.53 -1.33 -3.07 -1.73 -1.26 -1.87 -2.25 -3.76 -4.20 -0.97 -3.45 -4.25 -1.75
  -2.01 -1.62 -1.58 -1.63 -2.86 -1.49 -1.48 -1.82 -2.11 -3.52 -3.92 -1.05 -3.03 -4.02 -1.57 -1.67
  -2.32 -1.90 -1.88 -1.80 -3.11 -1.90 -1.74 -2.08 -2.42 -4.03 -4.34 -1.31 -3.51 -4.28 -1.90 -1.96 -2.12
  -3.82 -3.41 -3.07 -2.84 -4.95 -3.11 -2.99 -3.42 -3.98 -5.78 -6.14 -2.69 -5.55 -6.16 -3.73 -2.99 -3.22 -5.06
  -3.36 -3.16 -2.76 -2.76 -4.16 -2.97 -2.79 -3.01 -3.52 -5.25 -5.67 -2.60 -4.91 -5.66 -3.19 -2.78 -3.01 -4.66 -4.17
  -4.04 -3.07 -2.83 -2.48 -4.96 -3.07 -2.67 -3.38 -3.58 -6.05 -6.48 -2.49 -5.32 -6.29 -3.32 -3.05 -3.46 -5.18 -4.62 -5.52
//
H MIYS960102
D Quasichemical energy of interactions in an average buried environment
R PMID:8604144
A Miyazawa, S. and Jernigan, R.L.
T Residue-residue potentials with a favorable contact pair term
  and an unfavorable high packing density term, for simulation
  and threading
J J. Mol. Biol. 256, 623-644 (1996)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.13
   0.30  0.12
   0.10 -0.16 -0.39
   0.16 -0.89 -0.47 -0.08
   0.02  0.56  0.35  0.45 -0.85
   0.13 -0.24 -0.34 -0.17  0.17 -0.09
   0.30 -0.92 -0.35  0.06  0.54 -0.18  0.12
  -0.10  0.03 -0.18 -0.11  0.05 -0.02  0.21 -0.41
   0.17 -0.04 -0.15 -0.47 -0.02  0.03 -0.35  0.05 -0.48
  -0.14  0.35  0.55  0.54 -0.06  0.20  0.39  0.28  0.29 -0.25
  -0.08  0.34  0.44  0.70  0.00  0.22  0.46  0.29  0.28 -0.36 -0.30
   0.23  0.49 -0.32 -0.87  0.59 -0.32 -1.04  0.01  0.18  0.38  0.41  0.37
   0.00  0.36  0.34  0.64 -0.05  0.07  0.27  0.17 -0.05 -0.23 -0.23  0.41 -0.17
  -0.03  0.34  0.38  0.57 -0.02  0.11  0.44  0.27  0.00 -0.21 -0.26  0.37 -0.43 -0.29
   0.08 -0.05 -0.07  0.05  0.04 -0.19  0.07 -0.14 -0.15  0.20  0.15  0.09  0.01  0.05 -0.12
  -0.01 -0.08 -0.23 -0.36  0.14 -0.06 -0.26 -0.20 -0.12  0.33  0.32 -0.10  0.32  0.17 -0.05 -0.26
  -0.01 -0.05 -0.22 -0.22  0.20 -0.16 -0.21 -0.15 -0.12  0.13  0.21 -0.05  0.15  0.22 -0.07 -0.24 -0.09
   0.01 -0.04  0.11  0.26 -0.12  0.15  0.06  0.03 -0.16 -0.10 -0.07  0.09 -0.37 -0.14 -0.38  0.25  0.33  0.01
   0.07 -0.19  0.02 -0.06  0.27 -0.11 -0.14  0.04 -0.10  0.03  0.00 -0.22 -0.13 -0.04 -0.24  0.06  0.14  0.01  0.10
  -0.13  0.38  0.43  0.70 -0.05  0.27  0.46  0.15  0.32 -0.29 -0.33  0.37 -0.06 -0.19  0.11  0.27  0.17 -0.03  0.13 -0.29
//
H MIYS960103
D Number of contacts between side chains derived from 1168 x-ray protein
  structures
R PMID:8604144
A Miyazawa, S. and Jernigan, R.L.
T Residue-residue potentials with a favorable contact pair term
  and an unfavorable high packing density term, for simulation
  and threading
J J. Mol. Biol. 256, 623-644 (1996)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  11789
   5205 1558
   6465 3325 2605
   7836 8981 6075 2951
   4306 1120 1549 1584 5003
   5037 3062 3368 3550 1375 1253
   5933 8570 4550 4001 1189 3096  1884
  17079 5656 7319 8632 4168 4918  5248 10881
   3600 1883 2053 3603 1209 1332  2800  3425 1224
  16465 4065 3331 4318 3830 3772  4498  9071 2525  8432
  24837 6653 5751 5729 5395 6091  6706 13533 4133 26396 21432
   6019 1803 4260 9501 1200 3304 10234  6054 1554  4199  6531  1354
   5014 1463 1410 1389 1247 1490  1827  3376 1273  5188  8218  1456 1125
  10516 2956 2940 3217 2573 3056  3114  6523 2581 10183 17228  3098 4546  4778
   6368 3036 3077 3483 1983 2779  2989  6827 2097  4600  7632  2665 1916  3930 1824
  11447 4790 5920 8327 3012 3957  6343 12019 3073  6443 10084  5117 2205  5567 4843  5458
  11323 4720 5790 7362 2475 4412  6172 11312 3071  7958 11387  4940 2595  5281 4806  9465  4387
   3453 1588 1381 1444 1168 1057  1521  2946 1091  3101  4810  1367 1393  2498 2253  1889  1708  519
   7942 4433 3792 5105 2045 3350  4601  7235 2441  6770 10806  4678 2765  5549 4653  5537  5102 1975  2491
  21733 4867 4792 4606 4768 4541  5241 13584 3215 19830 32623  5437 5343 12746 6518  9059  9906 3723  7777 14091
//
H MIYS990106
D Quasichemical energy of transfer of amino acids from water to the protein
  environment
R PMID:10336383
A Miyazawa, S. and Jernigan, R.L.
T Self-consistent estimation of inter-residue protein contact energies
  based on an equilibrium mixture approximation of residues
J Proteins 34, 49-68 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.12
   0.24  0.19
   0.15  0.10 -0.06
   0.27 -0.24  0.02  0.29
  -0.33  0.08 -0.01  0.12 -1.19
   0.22  0.09  0.06  0.24 -0.07  0.20
   0.38 -0.22  0.12  0.44  0.20  0.27  0.46
  -0.08  0.09 -0.01  0.11 -0.31  0.13  0.32 -0.29
   0.07  0.05  0.00 -0.10 -0.36  0.15  0.00  0.00 -0.40
  -0.37  0.00  0.14  0.22 -0.64 -0.01  0.17 -0.13 -0.13 -0.74
  -0.38 -0.04  0.04  0.27 -0.65 -0.04  0.17 -0.16 -0.18 -0.81 -0.84
   0.41  0.66  0.22 -0.01  0.33  0.28 -0.06  0.29  0.38  0.24  0.22  0.76
  -0.27  0.03  0.04  0.30 -0.61 -0.06  0.12 -0.17 -0.29 -0.66 -0.70  0.29 -0.70
  -0.36 -0.05 -0.01  0.18 -0.67 -0.11  0.14 -0.19 -0.34 -0.73 -0.80  0.19 -0.83 -0.88
   0.15  0.17  0.18  0.33 -0.18  0.17  0.37  0.02  0.01 -0.05 -0.12  0.47 -0.13 -0.19  0.11
   0.10  0.16  0.09  0.10 -0.13  0.22  0.18 -0.01  0.04  0.03 -0.02  0.36  0.05 -0.12  0.20  0.05
   0.04  0.11  0.04  0.11 -0.15  0.12  0.16 -0.04 -0.03 -0.15 -0.15  0.33 -0.11 -0.15  0.13  0.04  0.03
  -0.27 -0.21 -0.10  0.07 -0.66 -0.02  0.00 -0.25 -0.37 -0.60 -0.62  0.09 -0.73 -0.68 -0.37 -0.01 -0.02 -0.64
  -0.20 -0.25 -0.11 -0.07 -0.39 -0.14 -0.08 -0.22 -0.30 -0.49 -0.55 -0.05 -0.56 -0.58 -0.25 -0.08 -0.09 -0.49 -0.45
  -0.32  0.08  0.12  0.36 -0.59  0.08  0.26 -0.15 -0.06 -0.67 -0.74  0.29 -0.51 -0.67 -0.05  0.04 -0.07 -0.51 -0.38 -0.65
//
H MIYS990107
D Quasichemical energy of interactions in an average buried environment
R PMID:10336383
A Miyazawa, S. and Jernigan, R.L.
T Self-consistent estimation of inter-residue protein contact energies
  based on an equilibrium mixture approximation of residues
J Proteins 34, 49-68 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.08
   0.18  0.03
   0.07 -0.08 -0.26
   0.10 -0.51 -0.27 -0.09
   0.01  0.32  0.21  0.25 -0.55
   0.09 -0.14 -0.19 -0.10  0.10 -0.10
   0.19 -0.51 -0.19  0.04  0.31 -0.09  0.04
  -0.04  0.03 -0.09 -0.06  0.03  0.00  0.13 -0.25
   0.11 -0.01 -0.08 -0.27 -0.02  0.02 -0.19  0.04 -0.36
  -0.07  0.20  0.32  0.31 -0.04  0.12  0.24  0.17  0.17 -0.18
  -0.04  0.20  0.26  0.40 -0.01  0.13  0.28  0.18  0.16 -0.21 -0.20
   0.13  0.28 -0.18 -0.50  0.35 -0.17 -0.57  0.01  0.10  0.22  0.24  0.16
   0.00  0.20  0.19  0.36 -0.04  0.04  0.16  0.10 -0.02 -0.13 -0.13  0.24 -0.20
  -0.01  0.20  0.22  0.32 -0.02  0.07  0.26  0.16  0.01 -0.12 -0.15  0.22 -0.25 -0.22
   0.06 -0.02 -0.03  0.03  0.03 -0.09  0.05 -0.07 -0.08  0.12  0.09  0.06  0.01  0.03 -0.11
   0.01 -0.03 -0.12 -0.20  0.08 -0.04 -0.14 -0.10 -0.05  0.20  0.19 -0.05  0.19  0.10 -0.02 -0.17
   0.01 -0.02 -0.11 -0.13  0.12 -0.08 -0.10 -0.07 -0.06  0.08  0.12 -0.02  0.09  0.13 -0.03 -0.12 -0.07
   0.02 -0.02  0.07  0.15 -0.07  0.10  0.06  0.04 -0.08 -0.05 -0.03  0.06 -0.21 -0.08 -0.21  0.15  0.20 -0.10
   0.05 -0.10  0.02 -0.03  0.16 -0.06 -0.06  0.03 -0.05  0.02  0.00 -0.12 -0.08 -0.02 -0.13  0.04  0.09  0.01  0.01
  -0.07  0.23  0.25  0.40 -0.04  0.16  0.28  0.10  0.19 -0.16 -0.19  0.22 -0.03 -0.11  0.07  0.16  0.11 -0.01  0.08 -0.19
//
H LIWA970101
D Modified version of the Miyazawa-Jernigan transfer energy
A Liwo, A., Oldziej, S., Pincus, M.R., Wawak, R.J., Rackovsky, S. and Scheraga,
  H.A.
T A united-residue force field for off-lattice protein-structure simulations:
   1. Functional forms and parameters of long-range side-chain interaction
  potentials from protein crystal data.
J J. Comp. Chem. 18, 849-873 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -3.28
  -2.56 -2.03
  -2.59 -2.19 -2.24
  -2.52 -2.67 -2.21 -1.85
  -3.93 -3.02 -3.14 -3.12 -4.54
  -2.67 -2.25 -2.26 -2.09 -3.31 -1.94
  -2.45 -2.61 -2.14 -1.77 -2.97 -1.93 -1.60
  -2.91 -2.43 -2.41 -2.34 -3.68 -2.39 -2.12 -2.62
  -2.95 -2.60 -2.60 -2.70 -3.87 -2.48 -2.49 -2.77 -3.27
  -4.18 -3.42 -3.13 -3.09 -4.90 -3.30 -3.11 -3.61 -3.74 -5.29
  -4.06 -3.24 -3.09 -2.84 -4.72 -3.17 -2.85 -3.56 -3.69 -5.21 -5.03
  -2.28 -1.47 -1.95 -2.22 -2.71 -1.84 -2.20 -2.08 -2.02 -2.95 -2.74 -1.14
  -3.93 -3.15 -3.04 -2.80 -4.72 -3.24 -2.90 -3.40 -3.80 -4.95 -4.91 -2.58 -4.80
  -4.04 -3.26 -3.17 -2.95 -4.94 -3.25 -2.89 -3.52 -3.95 -5.25 -5.18 -2.70 -5.03 -5.22
  -2.81 -2.29 -2.28 -2.16 -3.50 -2.35 -2.09 -2.60 -2.69 -3.62 -3.55 -1.95 -3.43 -3.54 -2.53
  -2.76 -2.46 -2.36 -2.31 -3.56 -2.34 -2.22 -2.61 -2.76 -3.58 -3.47 -2.01 -3.35 -3.46 -2.57 -2.47
  -2.97 -2.55 -2.43 -2.43 -3.73 -2.46 -2.33 -2.78 -2.97 -3.87 -3.61 -2.13 -3.62 -3.70 -2.68 -2.74 -2.81
  -3.81 -3.42 -3.23 -3.12 -4.60 -3.25 -3.04 -3.47 -3.94 -4.98 -4.87 -2.84 -4.87 -5.07 -3.60 -3.30 -3.44 -4.74
  -3.41 -3.01 -2.82 -2.84 -4.08 -2.90 -2.71 -3.12 -3.42 -4.51 -4.32 -2.58 -4.30 -4.43 -3.23 -2.97 -3.16 -4.20 -3.69
  -3.93 -3.00 -3.02 -2.82 -4.53 -3.05 -2.84 -3.42 -3.44 -5.01 -4.85 -2.69 -4.59 -4.89 -3.39 -3.35 -3.58 -4.63 -4.04 -4.64
//
H KESO980101
D Quasichemical transfer energy derived from interfacial regions of
  protein-protein complexes
R PMID:9865952
A Keskin, O., Bahar, I., Badretdinov, A.Y., Ptitsyn, O.B. and Jernigan, R.L.
T Empirical solvent-mediated potentials hold for both intra-molecular
  and inter-molecular inter-residue interactions
J Protein Science 7, 2578-2586 (1998)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -3.51
  -3.26 -3.98
  -2.06 -2.67 -1.99
  -2.74 -3.92 -2.50 -2.47
  -3.99 -4.41 -1.76 -3.56 -7.23
  -3.65 -4.13 -3.00 -3.15 -4.37 -4.71
  -2.69 -4.05 -2.43 -2.35 -3.02 -3.45 -2.85
  -2.24 -2.71 -1.63 -1.84 -3.43 -3.02 -1.58 -1.77
  -3.29 -3.24 -3.05 -2.93 -4.79 -4.20 -3.15 -2.47 -3.08
  -4.45 -4.29 -3.42 -3.46 -5.53 -4.65 -3.99 -3.50 -4.55 -5.97
  -5.02 -5.01 -3.94 -4.16 -6.13 -5.36 -4.35 -3.79 -4.85 -6.67 -7.16
  -1.91 -2.11 -1.63 -2.47 -2.28 -2.56 -2.83 -1.32 -2.14 -2.88 -3.24 -1.02
  -4.42 -4.13 -3.05 -3.69 -5.07 -4.46 -3.76 -3.02 -4.47 -5.37 -6.24 -2.36 -5.89
  -4.43 -4.51 -3.89 -3.52 -4.81 -4.89 -4.10 -3.76 -3.82 -6.11 -6.65 -2.70 -5.58 -6.45
  -1.78 -2.43 -1.01 -1.24 -2.97 -2.67 -1.70 -1.01 -1.80 -3.09 -3.75 -0.50 -3.11 -3.46 -0.83
  -2.49 -2.78 -2.13 -2.34 -3.41 -3.06 -2.57 -1.68 -3.12 -3.47 -4.12 -1.91 -3.33 -4.01 -1.56 -2.14
  -2.38 -2.43 -2.05 -2.41 -2.92 -3.44 -2.34 -1.81 -2.73 -3.61 -4.28 -1.64 -3.33 -3.85 -1.24 -2.22 -2.12
  -4.66 -4.54 -3.31 -3.81 -4.70 -4.87 -3.84 -3.77 -4.50 -5.79 -6.40 -3.12 -5.49 -5.72 -3.96 -2.86 -3.48 -5.16
  -3.96 -4.32 -3.14 -3.63 -4.71 -4.75 -3.62 -3.34 -3.78 -5.39 -5.67 -2.64 -5.01 -5.33 -2.92 -3.43 -3.33 -5.12 -4.58
  -3.86 -3.70 -2.76 -3.28 -4.82 -4.29 -3.20 -2.77 -4.14 -5.31 -6.03 -2.19 -5.16 -5.33 -2.43 -2.95 -2.87 -4.70 -4.54 -4.86
//
H KESO980102
D Quasichemical energy in an average protein environment derived from interfacial
  regions of protein-protein complexes
R PMID:9865952
A Keskin, O., Bahar, I., Badretdinov, A.Y., Ptitsyn, O.B. and Jernigan, R.L.
T Empirical solvent-mediated potentials hold for both intra-molecular
  and inter-molecular inter-residue interactions
J Protein Science 7, 2578-2586 (1998)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.38
   0.16 -0.26
   0.31 -0.02 -0.40
   0.02 -0.87 -0.51 -0.07
   0.00 -0.12  1.46  0.06 -2.38
   0.08 -0.11 -0.05  0.21  0.21 -0.38
   0.20 -0.87 -0.30  0.17  0.72  0.03 -0.20
   0.08 -0.10 -0.09  0.11 -0.26 -0.11  0.50 -0.27
   0.01  0.35 -0.52  0.00 -0.64 -0.31 -0.10  0.01  0.38
  -0.08  0.37  0.16  0.54 -0.30  0.33  0.13  0.05 -0.02 -0.37
  -0.09  0.21  0.23  0.41 -0.34  0.17  0.34  0.33  0.25 -0.50 -0.42
   0.06  0.15 -0.44 -0.87 -0.50  0.00 -1.11 -0.17 -0.01  0.32  0.52 -0.22
  -0.27  0.30  0.32  0.09 -0.08  0.27  0.13  0.31 -0.17  0.00 -0.30  0.61 -0.74
   0.01  0.22 -0.22  0.55  0.49  0.14  0.09 -0.15  0.79 -0.44 -0.40  0.57 -0.14 -0.71
   0.19 -0.17  0.19  0.36 -0.15 -0.11  0.01  0.13  0.33  0.11  0.01  0.30 -0.14 -0.19 -0.03
   0.08  0.08 -0.32 -0.13  0.02  0.10 -0.25  0.08 -0.38  0.33  0.26 -0.50  0.25 -0.14 -0.15 -0.14
   0.14  0.38 -0.30 -0.26  0.46 -0.32 -0.07 -0.11 -0.05  0.14  0.04 -0.29  0.19 -0.02  0.11 -0.27 -0.22
  -0.38  0.04  0.20  0.11  0.44  0.01  0.20 -0.31 -0.05 -0.26 -0.31  1.00 -0.20 -0.13 -0.85  0.86  0.18  0.27
   0.00 -0.07  0.04 -0.04  0.10 -0.21  0.08 -0.21  0.34 -0.12  0.08  0.14 -0.05 -0.07 -0.13 -0.03  0.00 -0.02  0.20
  -0.11  0.35  0.22  0.11 -0.22  0.05  0.30  0.17 -0.23 -0.33 -0.48  0.40 -0.40 -0.27  0.16  0.25  0.27  0.20  0.03 -0.49
//
H MOOG990101
D Quasichemical potential derived from interfacial regions of protein-protein
  complexes
R PMID:10328272
A Moont, G., Gabb, H.A. and Sternberg, M.J.E.
T Use of pair potentials across protein interfaces in screening predicted
  docked complexes
J Proteins 35, 364-373 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.48
  -0.20 -0.11
  -0.21  0.24 -0.18
  -0.39  0.45 -0.12 -0.65
  -0.12  0.17 -0.30 -0.49  0.00
  -0.16  0.24  0.08 -0.01  0.23 -0.29
  -0.39  0.37 -0.01 -0.35 -0.14 -0.05 -0.67
  -0.29  0.01 -0.18 -0.24  0.11  0.05 -0.37 -0.39
   0.04  0.10 -0.14  0.06  0.00  0.01  0.14  0.08  0.03
  -0.10  0.10 -0.05 -0.24  0.00  0.15 -0.28 -0.20  0.24 -0.20
   0.01  0.07 -0.29 -0.21  0.09  0.02 -0.29 -0.13  0.13  0.35 -0.06
  -0.53 -0.01 -0.17  0.16 -0.03 -0.17  0.16 -0.19 -0.02 -0.21 -0.07 -0.78
   0.15  0.37 -0.01  0.02  0.00  0.23  0.10  0.34  0.00  0.33  0.44  0.09  0.00
   0.13  0.31 -0.10 -0.01  0.18  0.16 -0.11 -0.12  0.34  0.59  0.41 -0.05  0.58  0.33
  -0.56  0.03  0.02 -0.22 -0.28 -0.14 -0.30 -0.27 -0.22 -0.43 -0.06 -0.46  0.39  0.08 -0.57
  -0.15  0.19 -0.16  0.00  0.15 -0.10 -0.10 -0.19  0.08 -0.14 -0.19 -0.24 -0.01  0.05 -0.13 -0.63
  -0.43  0.00 -0.23 -0.24 -0.17 -0.17 -0.23 -0.21  0.06 -0.05 -0.05 -0.22  0.10  0.03 -0.13 -0.05 -0.58
   0.08  0.37  0.04  0.02  0.00  0.22  0.00  0.10  0.00  0.43  0.25  0.06  0.00  0.34  0.35  0.05  0.03 0.00
   0.15  0.42  0.26  0.25  0.25  0.26  0.08  0.07  0.47  0.34  0.27  0.26  0.47  0.43  0.24  0.12  0.15 0.59 0.09
  -0.01 -0.04 -0.12 -0.29 -0.09  0.08 -0.13 -0.13 -0.10  0.20  0.21 -0.20  0.38  0.23 -0.10 -0.19 -0.13 0.40 0.27  0.00
//
H BETM990101
D Modified version of the Miyazawa-Jernigan transfer energy
R PMID:10048329
A Betancourt,M.R. and Thirumalai,D.
T Pair potentials for protein folding: Choice of reference states
  and sensitivity of predicted native states to variations 
  in the interaction schemes
J Protein Science 8, 361-369 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.20
   0.27  0.13
   0.24  0.02 -0.04
   0.30 -0.71 -0.12  0.27
  -0.26  0.32  0.28  0.38 -1.34
   0.21 -0.12 -0.05  0.12  0.04  0.14
   0.43 -0.75 -0.01  0.40  0.46  0.10  0.45
  -0.03  0.14  0.10  0.17 -0.09  0.20  0.48 -0.20
   0.21  0.04  0.10 -0.22 -0.19  0.22 -0.11  0.23 -0.33
  -0.35  0.18  0.55  0.54 -0.48  0.14  0.38  0.21  0.19 -0.60
  -0.37  0.09  0.36  0.62 -0.50  0.08  0.37  0.14  0.10 -0.79 -0.81
   0.20  0.50 -0.14 -0.69  0.35 -0.20 -0.87  0.12  0.26  0.21  0.16  0.38
  -0.23  0.17  0.32  0.62 -0.49 -0.01  0.24  0.08 -0.17 -0.60 -0.68  0.22 -0.56
  -0.33  0.08  0.29  0.48 -0.53 -0.04  0.34  0.11 -0.19 -0.65 -0.78  0.11 -0.89 -0.82
   0.07 -0.02  0.13  0.25 -0.18 -0.05  0.26 -0.01 -0.05  0.05 -0.08  0.12 -0.16 -0.19 -0.07
   0.15  0.12  0.14  0.01  0.09  0.25  0.10  0.10  0.15  0.35  0.26  0.10  0.32  0.10  0.17 0.13
   0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00  0.00 0.00 0.00
  -0.40 -0.41 -0.09  0.06 -0.74 -0.11 -0.15 -0.24 -0.46 -0.65 -0.70 -0.28 -0.94 -0.78 -0.73 0.07 0.00 -0.74
  -0.15 -0.37  0.01 -0.07 -0.16 -0.18 -0.16 -0.04 -0.21 -0.33 -0.44 -0.40 -0.51 -0.49 -0.40 0.07 0.00 -0.55 -0.27
  -0.38  0.17  0.39  0.66 -0.51  0.17  0.41  0.04  0.18 -0.68 -0.80  0.16 -0.47 -0.67 -0.08 0.25 0.00 -0.62 -0.27 -0.72
//
H TOBD000101
D Optimization-derived potential obtained for small set of decoys
R PMID:10813832
A Tobi, D., Shafran, G., Linial, N. and Elber, R.
T On the design and analysis of protein folding potentials
J Proteins 40, 71-85 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.17
   0.03  1.01
   0.33  0.82 -0.68
   0.58 -0.40  0.28 -0.24
  -0.48  0.80 -1.89 -0.32 -2.94
  -0.14  0.50  0.87 -0.26 -0.84  0.73
   0.29 -0.91  0.78  0.18  0.16  0.48  1.03
   0.43  0.12  0.46 -0.55  0.14 -0.08  0.88 -0.30
   0.66 -0.62  0.95  0.63 -2.34  0.83 -0.17  0.19 -3.30
  -0.79  0.31  0.48  0.19 -0.26  0.31 -0.47  0.31 -0.37 -0.27
  -0.13  0.28  1.17  0.41 -0.25 -0.22 -0.05  0.23 -0.17 -0.58 -1.42
   0.18  0.56  0.00 -0.71  0.45  0.86 -0.34  0.82  0.79 -0.08  0.43  1.01
  -0.82  0.40  1.92  0.08 -1.99  0.16  0.06  0.08 -0.52  0.03 -0.36  0.77 -1.08
  -0.49 -0.89  0.36  0.50 -2.52 -0.65 -0.12  0.90 -1.03 -0.72 -0.89  0.32 -1.37 -2.38
   0.87 -0.59  0.08  0.20 -0.19  0.24 -0.18 -0.81 -1.01 -0.33  0.08  0.42 -0.75  1.41  0.06
   0.18  0.84 -0.78  0.32  0.47  0.18  0.15 -0.05  1.17  0.49  0.80 -0.04 -0.20 -0.79  0.60  0.03
  -0.45 -0.19  0.13  0.49 -1.38 -0.20  0.81  0.10  0.80 -0.29  0.30  0.38 -0.40  0.32  0.47  0.32 -0.38
  -0.04  0.23  1.45 -0.05 -2.09 -1.14 -0.41  0.51  1.10 -0.63 -0.44 -0.38 -0.33 -0.80 -2.24 -0.08 -0.61 -0.97
  -0.08 -1.64  0.43  0.04 -0.65 -0.64 -0.16 -0.56 -1.02 -1.34  0.25 -0.20 -0.19 -0.79 -0.68 -0.83  0.67 -0.85 -2.22
  -0.54  0.41  0.71  0.31 -0.46  0.37  0.34 -0.12  0.67 -0.98 -1.03  0.17 -0.93 -0.43  0.32  0.52  0.24 -0.41 -0.50 -0.53
//
H TOBD000102
D Optimization-derived potential obtained for large set of decoys
R PMID:10813832
A Tobi, D., Shafran, G., Linial, N. and Elber, R.
T On the design and analysis of protein folding potentials
J Proteins 40, 71-85 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.15
  -0.16  0.65
   1.01  0.14 -0.45
   0.62 -0.57 -0.53  0.89
  -0.96 -0.25  0.18 -0.50 -2.11
   0.16  1.24  0.57  0.78 -0.54  0.41
  -0.02 -0.70 -0.19  0.83  0.65  0.28  1.59
   0.23  0.84  0.12  0.37 -0.74 -0.36  0.48  0.01
   0.29  0.36 -0.06 -0.07 -0.66 -0.60  1.27  0.42 -2.26
  -0.85 -0.22  0.22 -0.18 -1.02  0.66  0.31 -0.04 -0.31 -1.10
  -0.72 -0.04 -0.19  1.12 -0.24  0.10  0.99 -0.20 -0.31 -1.15 -1.60
   0.96  1.24  0.38 -0.55 -0.38 -0.04 -0.36  0.95 -0.01 -0.01  1.02  2.28
  -0.85  0.67  0.66  0.42 -1.30  0.41  0.00 -0.63  0.18  0.07 -1.39  1.66 -1.89
  -0.79  0.43  0.50  0.35 -0.96 -0.10 -0.56 -0.10  0.52 -0.76 -1.24 -0.01 -1.04 -1.39
   0.08 -0.31 -0.25  0.83 -0.45 -0.07  0.24  0.16  0.93  0.43 -0.27  0.45 -0.22 -0.09  0.41
   0.24  0.91 -0.17  0.29 -0.41  0.27  1.14 -0.09 -0.28 -0.14  1.13  0.13 -0.59 -0.01  0.48  1.31
   0.33 -0.44  1.23 -0.35  0.00 -0.28 -0.11  0.73 -0.27 -0.18 -0.18 -0.16 -0.62 -0.29  0.34  0.03 -0.41
   0.24 -0.14 -0.04 -1.41 -0.32  0.00  1.13  0.87  0.91 -1.90 -0.85  0.33 -0.30  0.58 -2.51 -0.77  0.32 -1.35
  -0.50  0.54  0.22 -0.27 -0.23 -0.79 -0.84 -0.62 -1.34 -1.42 -0.53 -1.06  0.02 -1.43 -0.17 -0.86 -0.19 -1.96 -1.35
  -0.36  0.53  0.54  0.20 -0.58 -0.06  0.47 -0.43  0.51 -1.46 -0.77  0.75 -1.22 -0.89  0.75  0.14  0.29 -0.18 -0.30 -1.32
//
H PARB960101
D Statistical contact potential derived by the quasichemical approximation
R PMID:8627632
A Park, B. and Levitt, M.
T Energy functions that discriminate X-ray and near-native folds
  from well-constructed decoys
J J. Mol. Biol. 258, 367-392 (1996)
* (Glu is not available)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.5
   0.2 -0.9
   0.3 -0.8 -0.7
   0.3 -1.4 -0.6  0.0
   0.3  0.0  0.0  0.0 -2.7
   0.0 -0.9 -0.7 -0.3 -0.2 -0.5
   0.6 -1.5 -0.6  0.0  0.1 -0.4  0.1
   NA   NA   NA   NA   NA   NA   NA   NA
   0.0 -1.0 -0.8 -1.1 -0.6 -0.5 -1.0   NA  -1.6
  -0.4 -0.7 -0.1  0.0 -0.8 -0.4 -0.2   NA  -0.8 -1.5
  -0.4 -0.6 -0.1  0.0 -0.8 -0.6 -0.1   NA  -0.7 -1.4 -1.4
   1.0  0.1 -0.3 -1.0  0.5 -0.4 -1.1   NA   0.0  0.0  0.1  0.7
  -0.5 -0.5 -0.3  0.1 -0.8 -0.6 -0.3   NA  -0.9 -1.4 -1.3 -0.1 -1.5
  -0.8 -0.9 -0.6 -0.3 -1.2 -0.8 -0.5   NA  -1.2 -1.7 -1.6 -0.4 -1.9 -2.0
   0.6 -0.2 -0.1  0.1  0.0 -0.3  0.1   NA  -0.4 -0.1 -0.1  0.6 -0.5 -0.7  0.1
   0.5 -0.4 -0.1 -0.3 -0.1  0.0 -0.2   NA  -0.6 -0.1  0.0  0.1 -0.1 -0.4  0.2  0.0
   0.0 -0.6 -0.4 -0.3 -0.3 -0.5 -0.3   NA  -0.7 -0.6 -0.3  0.0 -0.6 -0.7  0.0 -0.2 -0.5
  -0.8 -1.3 -0.8 -0.6 -1.3 -1.0 -0.8   NA  -1.5 -1.8 -1.7 -0.8 -2.0 -2.0 -1.3 -0.6 -0.9 -2.2
  -0.7 -1.4 -0.8 -1.0 -0.8 -1.1 -1.0   NA  -1.5 -1.4 -1.4 -1.0 -1.5 -1.7 -1.0 -0.6 -0.8 -1.8 -1.6
  -0.3 -0.5  0.0  0.4 -0.5 -0.4  0.0   NA  -0.5 -1.2 -1.2  0.1 -1.0 -1.5  0.0  0.0 -0.3 -1.6 -1.2 -1.1
//
H PARB960102
D Modified version of the Miyazawa-Jernigan transfer energy
R PMID:8627632
A Park, B. and Levitt, M.
T Energy functions that discriminate X-ray and near-native folds
  from well-constructed decoys
J J. Mol. Biol. 258, 367-392 (1996)
* (Glu is not available)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -2.9
  -2.4 -2.9
  -2.8 -3.2 -3.6
  -2.6 -3.7 -3.3 -2.6
  -3.1 -2.6 -3.2 -2.9 -6.1
  -2.7 -2.9 -3.2 -2.7 -2.9 -2.6
  -1.9 -3.2 -2.8 -2.0 -2.4 -2.2 -1.5
  NA   NA   NA   NA   NA   NA   NA   NA
  -2.6 -2.9 -3.2 -3.3 -3.3 -2.5 -2.8  NA -3.5
  -3.9 -3.3 -3.2 -2.9 -4.2 -3.2 -2.7  NA -3.4 -4.9
  -3.7 -3.0 -3.0 -2.7 -4.0 -3.1 -2.4  NA -3.1 -4.6 -4.3
  -1.9 -2.0 -3.0 -3.5 -2.4 -2.7 -3.2  NA -2.2 -2.9 -2.5 -1.7
  -3.8 -3.1 -3.3 -2.7 -4.2 -3.3 -2.7  NA -3.5 -4.7 -4.4 -2.9 -4.8
  -3.7 -3.0 -3.2 -2.7 -4.1 -3.0 -2.4  NA -3.3 -4.5 -4.2 -2.8 -4.6 -4.3
  -2.3 -2.4 -2.7 -2.3 -2.8 -2.5 -1.8  NA -2.6 -3.0 -2.8 -1.8 -3.4 -3.1 -2.2
  -2.4 -2.6 -2.8 -2.8 -3.0 -2.3 -2.3  NA -2.7 -3.0 -2.6 -2.3 -3.0 -2.8 -2.2 -2.4
  -3.2 -3.1 -3.4 -3.2 -3.5 -3.1 -2.7  NA -3.2 -3.8 -3.3 -2.8 -3.8 -3.4 -2.8 -2.9 -3.5
  -3.8 -3.5 -3.5 -3.2 -4.3 -3.3 -2.8  NA -3.6 -4.7 -4.4 -3.3 -4.8 -4.4 -3.7 -3.1 -3.7 -4.7
  -3.7 -3.6 -3.5 -3.5 -3.8 -3.4 -3.0  NA -3.7 -4.4 -4.1 -3.5 -4.4 -4.1 -3.5 -3.1 -3.6 -4.3 -4.1
  -4.1 -3.5 -3.5 -2.8 -4.3 -3.4 -2.8  NA -3.5 -5.0 -4.7 -3.1 -4.7 -4.6 -3.2 -3.1 -3.9 -4.8 -4.5 -5.1
//
H KOLA930101
D Statistical potential derived by the quasichemical approximation
A Kolinski, A., Godzik, A. and Skolnick, J.
T A general method for the prediction of the three dimensional structure
  and folding pathway of globular proteins: Application to designed helical
  proteins
J J. Chem. Phys. 98, 7420-7433 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.1
   0.5  0.2
   0.1  0.0 -0.4
   0.1 -1.1 -0.6  0.3
   0.1  0.4  0.3  0.3 -3.3
   0.0 -0.5 -0.4  0.0  0.1  0.0
   0.5 -0.9 -0.4  0.3  0.8  0.2  0.6
   0.1  0.5 -0.1 -0.4  0.1 -0.1  0.6  0.3
  -0.1 -0.4 -0.5 -1.0 -1.2  0.9 -0.9  0.3 -1.4
  -0.6  0.4  0.7  0.6 -1.1  0.3  0.4  0.3 -0.2 -0.8
  -0.4  0.2  0.5  0.8 -0.5  0.4  0.7  0.5 -0.3 -0.6 -0.6
   1.0  1.7  0.1 -0.6  1.6  0.4 -0.7  1.2  0.3  0.8  1.1  1.9
   0.1  0.1  0.2  1.0 -1.8  0.2  0.0  0.4 -0.9 -0.7 -0.6  0.5 -1.1
  -0.6 -0.4  0.2  0.4 -1.5  0.0  0.1  0.1 -1.0 -0.8 -0.9  0.3 -1.1 -1.5
   0.3  0.5  0.4  0.6  0.0 -0.1  0.6  0.4 -0.5  0.3  0.5  1.1 -0.2 -0.2  0.1
  -0.1  0.0 -0.3 -0.9 -0.4  0.0 -0.2  0.0 -0.6  0.4  0.4  0.5  0.0  0.0  0.4 -0.6
  -0.3  0.1 -0.3 -0.6  0.0 -0.2 -0.2  0.0 -0.6  0.0  0.3  0.6  0.2  0.0  0.3 -0.5 -0.3
  -0.7 -0.9 -0.1 -0.2 -0.5 -0.2  0.1 -0.5 -1.2 -0.9 -0.8  0.1 -1.3 -1.3 -0.7 -0.1  0.0 -0.8
  -0.5 -0.4 -0.5 -0.3 -0.1 -0.5  0.0 -0.4 -0.8 -0.5 -0.1 -0.2 -0.6 -0.5 -0.9 -0.1 -0.2 -0.5 -0.8
  -0.6  0.3  0.2  0.7 -0.8  0.2  0.4  0.2 -0.2 -0.7 -0.6  0.9 -0.5 -0.8  0.1  0.3  0.2 -0.8 -0.3 -0.9
//
H GODA950101
D Quasichemical statistical potential derived from  buried contacts
R PMID:8535247
A Godzik, A., Kolinski, A. and Skolnick, J.
T Are Proteins Ideal Mixtures of Amino-Acids-Analysis
  of Energy Parameter Sets
J Protein Science 4, 2107-2117 (1995)
* (Glu is not available)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.1
   0.3 -0.4
   0.1 -0.5 -0.7
   0.2 -1.0 -0.6 -0.3
   0.1  0.4 -0.1  0.3 -0.9
   0.0 -0.4 -0.6 -0.3  0.1 -0.4
   0.3 -1.0 -0.5 -0.3  0.4 -0.3 -0.4
  NA   NA   NA   NA   NA   NA   NA   NA
   0.2 -0.2 -0.3 -0.7  0.0 -0.2 -0.6  NA  -0.8
  -0.1  0.3  0.4  0.5  0.2  0.2  0.5  NA   0.4 -0.1
  -0.1  0.3  0.3  0.6  0.1  0.3  0.5  NA   0.4 -0.1 -0.2
   0.3  0.3 -0.5 -0.9  0.4 -0.3 -0.8  NA   0.0  0.2  0.3  0.1
   0.0  0.3  0.1  0.5  0.1  0.1  0.3  NA   0.2  0.0  0.0  0.2 -0.2
  -0.1  0.2  0.1  0.3  0.1  0.1  0.3  NA   0.1  0.0 -0.1  0.1 -0.1 -0.2
   0.0 -0.3 -0.3  0.0 -0.1 -0.4 -0.1  NA  -0.1  0.2  0.1  0.1  0.0 -0.1 -0.3
   0.1 -0.3 -0.4 -0.5  0.1 -0.3 -0.5  NA  -0.3  0.4  0.4 -0.3  0.3  0.1 -0.3 -0.4
   0.0 -0.1 -0.3 -0.3  0.0 -0.2 -0.2  NA  -0.1  0.1  0.2 -0.1  0.1  0.1 -0.2 -0.2  0.0
   0.0 -0.1  0.0  0.0  0.2 -0.1  0.0  NA   0.0  0.1  0.1 -0.1 -0.1 -0.1 -0.4  0.2  0.2  0.0
  -0.1 -0.3 -0.2 -0.2  0.1 -0.2 -0.3  NA  -0.1  0.1  0.0 -0.3 -0.1  0.0 -0.4 -0.1  0.0  0.1 -0.1
  -0.1  0.4  0.3  0.6  0.0  0.2  0.4  NA   0.5 -0.1 -0.1  0.4  0.1  0.0  0.1  0.3  0.2  0.1  0.1 -0.2
//
H SKOJ970101
D Statistical potential derived by the quasichemical approximation
R PMID:9070450
A Skolnick, J., Jaroszewski, L., Kolinski, A. and Godzik, A.
T Derivation and testing of pair potentials for protein folding.
  When is the quasichemical approximation correct?
J Protein Science 6, 676-688 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.8
   0.6 -0.1
   0.9  0.0  0.1
   1.2 -0.5  0.4  0.9
   0.6  0.7  0.6  0.8 -1.3
   0.6  0.2  0.2  0.6  0.3  0.3
   1.2 -0.4  0.5  0.9  0.9  0.8  1.2
   1.2  0.2  0.7  0.8  1.3  0.8  1.1  1.5
   0.4 -0.1  0.2 -0.1  0.1  0.1  0.1  0.7 -0.8
  -0.6 -0.2  0.5  0.5 -0.5  0.1  0.4  0.4 -0.1 -1.4
  -0.3 -0.1  0.4  0.7 -0.4  0.2  0.6  0.4 -0.1 -1.3 -1.2
   1.3  1.1  0.7  0.2  1.3  0.5  0.0  0.9  1.0  0.5  0.5  2.1
  -0.3  0.2  0.3  0.6 -0.3  0.1  0.4  0.5 -0.4 -1.0 -1.0  0.6 -1.1
  -0.2 -0.4  0.1  0.5 -0.6 -0.1  0.4  0.3 -0.4 -1.3 -1.3  0.4 -1.3 -1.5
   0.6  0.1  0.5  0.9  0.4  0.2  0.7  0.8  0.0  0.0  0.0  0.9 -0.2 -0.1  0.4
   0.9  0.2  0.7  0.7  0.6  0.6  0.6  0.8  0.0  0.3  0.4  0.9  0.4  0.1  0.6  0.6
   0.5  0.0  0.3  0.5  0.5  0.4  0.4  0.5  0.1 -0.3  0.0  0.8  0.0 -0.2  0.2  0.4  0.1
  -0.6 -0.6  0.0  0.0 -0.7 -0.4 -0.1  0.0 -0.9 -1.3 -1.4 -0.1 -1.5 -1.5 -0.8 -0.1 -0.2 -1.2
  -0.4 -0.7 -0.2 -0.2 -0.1 -0.3 -0.2  0.1 -0.8 -1.0 -0.9 -0.2 -1.1 -1.0 -0.5  0.1 -0.2 -1.2 -0.8
  -0.4  0.0  0.5  1.0 -0.6  0.2  0.5  0.5  0.0 -1.2 -1.2  0.7 -0.8 -1.1 -0.1  0.4 -0.2 -1.1 -0.8 -1.2
//
H SKOJ000101
D Statistical quasichemical potential with the partially composition-corrected
  pair scale
R PMID:10651034
A Skolnick, J., Kolinski, A. and Ortiz, A.
T Derivation of protein-specific pair potentials based on weak sequence
  fragment similarity
J Proteins 38, 3-16 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   1.0
   0.4 -0.1
   0.8  0.0  0.1
   1.1 -0.6  0.0  0.6
   0.6  0.2  0.5  0.5 -1.7
   0.6  0.0  0.0  0.2  0.2  0.0
   1.1 -0.5  0.3  0.7  0.8  0.2  1.0
   1.4  0.3  0.6  0.8  0.9  0.8  1.1 1.7
   0.5 -0.1  0.0 -0.2 -0.2 -0.1 -0.1 0.7 -0.6
  -0.3 -0.2  0.4  0.6 -0.5  0.0  0.3 0.5  0.0 -1.1
  -0.1 -0.2  0.3  0.6 -0.5  0.0  0.4 0.7  0.0 -1.2 -1.1
   1.0  0.6  0.3 -0.2  0.9  0.1 -0.4 0.7  0.6  0.4  0.3  1.6
  -0.2  0.0  0.1  0.4 -0.5 -0.1  0.4 0.6 -0.3 -0.8 -1.0  0.3 -1.0
  -0.2 -0.4  0.0  0.4 -0.8 -0.1  0.2 0.4 -0.3 -1.1 -1.1  0.3 -1.1 -1.2
   0.8  0.1  0.6  0.9  0.4  0.4  0.5 1.1  0.3  0.1  0.1  0.8  0.0 -0.2  0.9
   0.9  0.3  0.4  0.3  0.4  0.2  0.4 0.9  0.1  0.4  0.4  0.7  0.3  0.1  0.6  0.5
   0.6  0.0  0.2  0.1  0.1  0.1  0.2 0.6  0.0 -0.2  0.0  0.5 -0.1 -0.2  0.5  0.2  0.2
  -0.5 -0.6 -0.2  0.0 -0.7 -0.5 -0.2 0.2 -0.7 -1.1 -1.1 -0.1 -1.2 -1.3 -0.7 -0.2 -0.3 -1.1
  -0.2 -0.7 -0.2 -0.1 -0.3 -0.3 -0.2 0.3 -0.7 -0.8 -0.9 -0.2 -0.8 -0.9 -0.5  0.1 -0.2 -1.1 -0.7
  -0.1  0.1  0.5  0.8 -0.5  0.3  0.5 0.8 -0.1 -1.0 -0.9  0.5 -0.8 -0.9  0.2  0.4 -0.1 -0.9 -0.7 -0.8
//
H SKOJ000102
D Statistical quasichemical potential with the composition-corrected pair scale
R PMID:10651034
A Skolnick, J., Kolinski, A. and Ortiz, A.
T Derivation of protein-specific pair potentials based on weak sequence
  fragment similarity
J Proteins 38, 3-16 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.8
   0.3 -0.3
   0.7 -0.2 -0.2
   0.9 -0.6  0.0  0.2
   0.0 -0.6 -0.5 -0.3 -2.4
   0.4 -0.2 -0.2  0.0 -0.7 -0.5
   1.0 -0.5  0.2  0.5 -0.2  0.1  0.5
   1.2  0.2  0.4  0.7  0.1  0.5  0.9  1.1
   0.2 -0.4 -0.4 -0.4 -1.4 -0.5 -0.3  0.3 -1.2
  -0.3 -0.2  0.2  0.5 -0.8 -0.1  0.3  0.4 -0.3 -1.1
  -0.1 -0.2  0.3  0.5 -0.6  0.0  0.4  0.6 -0.2 -1.2 -1.1
   0.8  0.4  0.2 -0.2 -0.3  0.0 -0.4  0.6  0.1  0.3  0.3  0.6
  -0.3 -0.4 -0.3  0.0 -1.3 -0.5  0.0  0.2 -0.9 -0.9 -1.0 -0.1 -1.4
  -0.2 -0.4 -0.2  0.2 -1.1 -0.3  0.1  0.3 -0.6 -1.1 -1.1  0.1 -1.2 -1.3
   0.7  0.0  0.3  0.6 -0.4  0.0  0.4  0.8 -0.2  0.0  0.1  0.5 -0.4 -0.3  0.3
   0.8  0.2  0.2  0.2 -0.4  0.1  0.3  0.8 -0.2  0.3  0.4  0.5 -0.1  0.0  0.4  0.2
   0.5  0.0  0.1  0.1 -0.5  0.0  0.1  0.6 -0.2 -0.2  0.0  0.4 -0.3 -0.3  0.3  0.2  0.0
  -0.6 -0.9 -0.6 -0.4 -1.5 -0.9 -0.5 -0.2 -1.2 -1.2 -1.2 -0.5 -1.6 -1.4 -0.9 -0.5 -0.6 -1.7
  -0.3 -0.7 -0.3 -0.2 -1.0 -0.4 -0.2  0.2 -0.9 -0.9 -0.9 -0.3 -1.0 -1.0 -0.6  0.0 -0.2 -1.3 -0.9
   0.0  0.0  0.3  0.6 -0.7  0.1  0.4  0.7 -0.3 -1.0 -0.9  0.4 -0.8 -0.9  0.2  0.4 -0.1 -1.0 -0.7 -0.7
//
H BONM030101
D Quasichemical statistical potential for the antiparallel orientation of
  interacting side groups
R PMID:15072433
A Boniecki, M., Rotkiewicz, P., Skolnick, J. and Kolinski, A.
T Protein fragment reconstruction using various modeling techniques
J J. Comput. Aided Mol. Des. 17, 725-738 (2003)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.1
   0.6  0.4
   0.7  0.1  0.6
   1.0 -0.2  0.8  1.8
  -0.3 -0.7  0.2  0.6 -2.3
   0.6  0.2  0.8  1.2  0.1  0.8
   1.0 -0.1  1.2  2.1  0.7  1.6  2.3
   0.1  0.7  0.3  0.5 -0.4  0.6  1.0  0.1
   0.4  0.0 -0.2 -0.3 -1.2 -0.1  0.0  0.5 -0.9
  -0.4 -0.4  0.7  0.9 -0.2  0.3  0.7  0.2 -0.8 -0.5
  -0.4 -0.4  0.8  1.0 -0.4  0.3  0.7  0.3 -0.6 -0.4 -0.4
   1.0  1.0  1.4  0.9  0.4  1.5  1.4  1.0  0.3  0.7  0.6  2.5
  -0.2 -0.3  0.5  1.1 -0.4  0.3  1.1  0.2 -0.7 -0.3 -0.3  0.7 -0.7
  -0.3 -0.5 -0.4 -0.1 -1.4 -0.4 -0.1  0.3 -0.8 -1.4 -1.4 -0.2 -1.4 -1.6
   0.4 -0.1  0.6  1.0 -0.1  0.6  1.0  0.4 -0.6  0.4  0.4  1.3  0.3 -0.7  0.4
   0.3 -0.2  0.5  0.7 -0.1  0.7  0.9  0.1 -0.6  0.4  0.3  1.3  0.6 -0.7  0.5  0.3
   0.2 -0.1  0.5  0.9 -0.1  0.6  1.0  0.2 -0.6  0.3  0.3  1.2  0.5 -0.8  0.6  0.5  0.6
   0.1 -0.5 -0.4 -0.2 -1.2 -0.4 -0.2  0.3 -0.9 -1.2 -1.1  0.0 -1.1 -1.2 -0.8 -0.5 -0.8 -1.4
   0.0 -0.3 -0.3 -0.2 -1.2 -0.3 -0.1  0.4 -0.6 -1.1 -1.1  0.0 -0.9 -1.2 -0.8 -0.6 -0.6 -1.1 -0.9
  -0.5 -0.3  0.7  1.0 -0.3  0.4  0.8  0.1 -0.7 -0.5 -0.4  0.7 -0.2 -1.3  0.3  0.3  0.3 -1.1 -1.0 -0.6
//
H BONM030102
D Quasichemical statistical potential for the intermediate orientation of
  interacting side groups
R PMID:15072433 
A Boniecki, M., Rotkiewicz, P., Skolnick, J. and Kolinski, A.
T Protein fragment reconstruction using various modeling techniques
J J. Comput. Aided Mol. Des. 17, 725-738 (2003)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.1
   0.5 -0.2
   0.4 -0.3  0.1
   0.6 -0.8  0.2  0.6
  -0.2 -0.6  0.3  0.3 -1.7
   0.4 -0.4  0.3  0.6  0.3  0.6
   0.8 -0.7  0.6  1.1  0.8  0.7  1.2
   0.4  0.4  0.2  0.5 -0.3  0.5  0.9  0.1
   0.5 -0.4 -0.5 -0.6 -1.1 -0.2 -0.4  0.4 -1.0
  -0.1 -0.2  0.7  0.9 -0.2  0.7  0.8  0.3 -0.5 -0.3
  -0.2 -0.4  0.6  0.8 -0.4  0.4  0.8  0.3 -0.5 -0.3 -0.5
   0.8  0.2  0.6  0.1  0.8  0.8  0.2  0.7  0.0  1.0  0.8  1.6
   0.0 -0.4  0.6  0.9 -0.3  0.5  0.9  0.2 -0.6 -0.2 -0.3  1.0 -0.5
   0.0 -0.4 -0.4 -0.2 -1.2 -0.3 -0.1  0.2 -0.6 -1.1 -1.2 -0.1 -1.2 -1.4
   0.5 -0.4  0.6  0.8  0.1  0.5  0.7  0.5 -0.5  0.4  0.4  1.1  0.3 -0.6  0.5
   0.3 -0.4  0.3  0.2 -0.1  0.3  0.5  0.1 -0.6  0.4  0.4  0.7  0.4 -0.6  0.5  0.1
   0.2 -0.3  0.4  0.3  0.0  0.4  0.5  0.2 -0.5  0.4  0.4  0.8  0.3 -0.6  0.5  0.2  0.3
   0.3 -0.6 -0.5 -0.5 -1.1 -0.5 -0.3  0.2 -0.8 -1.0 -1.0 -0.2 -1.0 -1.2 -0.8 -0.7 -0.6 -1.1
   0.2 -0.5 -0.6 -0.5 -1.0 -0.4 -0.4  0.2 -0.7 -0.8 -0.9 -0.3 -1.0 -1.0 -0.8 -0.6 -0.5 -1.0 -0.8
  -0.2 -0.3  0.7  0.8 -0.3  0.6  0.9  0.3 -0.4 -0.2 -0.4  1.0 -0.2 -1.0  0.3  0.4  0.3 -0.9 -0.7 -0.2
//
H BONM030103
D Quasichemical statistical potential for the parallel orientation of interacting
  side groups
R PMID:15072433 
A Boniecki, M., Rotkiewicz, P., Skolnick, J. and Kolinski, A.
T Protein fragment reconstruction using various modeling techniques
J J. Comput. Aided Mol. Des. 17, 725-738 (2003)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.1
   0.3 -0.8
   0.1 -0.8 -0.6
   0.1 -1.2 -0.6 -0.2
  -0.5 -0.6 -0.1  0.2 -1.6
   0.2 -1.0 -0.3 -0.3  0.0 -0.3
   0.4 -1.4 -0.2  0.1  0.6 -0.2  0.2
   0.3  0.3  0.1  0.2 -0.2  0.2  0.4  0.1
   0.0 -0.9 -0.8 -1.0 -1.3 -0.9 -1.0  0.3 -1.5
  -0.4 -0.6  0.2  0.4 -0.8  0.0  0.2  0.1 -0.7 -1.0
  -0.4 -0.6  0.2  0.5 -0.9 -0.2  0.2  0.2 -0.8 -1.0 -1.2
   0.4 -0.4 -0.2 -0.8  0.5 -0.3 -1.0  0.4 -0.6  0.2  0.3  0.3
  -0.3 -0.6  0.2  0.4 -0.7  0.0  0.3  0.2 -0.9 -0.8 -0.9  0.3 -1.0
  -0.2 -0.6 -0.6 -0.3 -1.5 -0.6 -0.4  0.1 -0.9 -1.4 -1.4 -0.2 -1.4 -1.5
   0.4 -0.5  0.3  0.5 -0.1  0.3  0.4  0.4 -0.6  0.3  0.4  0.6  0.2 -0.6  0.8
  -0.2 -0.8 -0.4 -0.5 -0.5 -0.2 -0.2  0.0 -0.9  0.0  0.0 -0.1  0.0 -0.8  0.3 -0.5
  -0.1 -0.9 -0.4 -0.4 -0.4 -0.4 -0.4  0.0 -0.9 -0.3 -0.3 -0.2 -0.2 -0.8  0.2 -0.5 -0.5
   0.2 -0.7 -0.8 -0.5 -1.3 -0.9 -0.6  0.1 -1.1 -1.2 -1.1 -0.5 -1.1 -1.4 -0.9 -0.8 -0.8 -1.6
  -0.1 -1.0 -0.8 -0.7 -1.1 -0.8 -0.7  0.0 -1.2 -1.2 -1.1 -0.8 -1.1 -1.3 -0.8 -0.8 -0.8 -1.3 -1.1
  -0.4 -0.6  0.1  0.4 -0.9  0.0  0.2  0.1 -0.9 -0.9 -1.0  0.1 -0.8 -1.4  0.2 -0.2 -0.3 -1.1 -1.1 -1.0
//
H BONM030104
D Distances between centers of interacting side chains in the antiparallel
  orientation
R PMID:15072433
A Boniecki, M., Rotkiewicz, P., Skolnick, J. and Kolinski, A.
T Protein fragment reconstruction using various modeling techniques
J J. Comput. Aided Mol. Des. 17, 725-738 (2003)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  4.7
  5.5 6.5
  5.0 5.5 5.4
  4.9 5.6 5.3 5.4
  5.0 5.9 5.7 5.2 4.4
  5.0 6.1 5.3 5.3 5.5 5.8
  5.2 5.7 5.3 5.5 5.7 5.4 6.1
  4.6 6.7 5.1 4.5 5.5 5.1 4.5 3.9
  5.2 5.7 5.4 5.2 5.4 5.2 5.5 4.5 5.3
  5.2 5.9 5.3 5.7 5.2 5.4 5.6 5.5 5.9 5.8
  5.2 5.8 5.7 5.5 5.5 5.8 5.8 5.9 5.7 5.6 5.7
  5.2 6.5 5.3 5.3 5.3 5.7 5.3 5.9 5.2 5.8 5.4 5.7
  5.0 5.8 5.2 6.1 5.3 4.9 5.9 4.7 5.0 5.7 5.4 5.8 5.9
  5.1 5.7 5.8 5.6 5.4 5.7 5.8 5.4 5.5 6.0 5.8 5.5 5.8 6.2
  5.2 5.7 5.3 5.2 5.9 5.7 5.5 5.6 5.5 5.7 5.6 5.9 5.4 5.5 4.9
  4.7 5.6 5.2 5.2 5.1 5.4 5.1 4.5 5.3 5.3 5.2 4.9 5.5 5.4 5.4 4.9
  5.2 5.9 5.3 5.5 5.6 5.6 5.4 5.9 5.5 5.6 5.6 5.3 5.5 5.7 5.4 4.8 5.4
  5.8 6.0 5.7 6.6 5.3 5.5 6.3 5.8 5.5 6.2 6.3 5.6 6.1 6.2 5.4 5.8 6.1 6.4
  5.5 6.0 5.7 5.7 6.1 5.6 5.8 4.3 5.7 6.0 5.8 5.6 6.3 5.9 5.8 5.8 5.9 6.5 6.3
  4.9 5.6 5.4 5.5 5.4 5.6 5.3 5.2 5.4 5.6 5.6 5.7 5.5 5.6 5.8 5.1 5.6 6.3 5.9 5.5
//
H BONM030105
D Distances between centers of interacting side chains in the intermediate
  orientation
R PMID:15072433
A Boniecki, M., Rotkiewicz, P., Skolnick, J. and Kolinski, A.
T Protein fragment reconstruction using various modeling techniques
J J. Comput. Aided Mol. Des. 17, 725-738 (2003)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  4.7
  5.5 6.6
  5.2 6.1 5.6
  5.0 5.6 5.2 5.5
  5.3 5.6 5.7 5.4 4.3
  5.4 6.0 5.9 5.5 5.4 5.4
  5.0 5.9 5.6 5.9 5.1 5.7 6.1
  4.7 6.3 5.6 4.7 5.3 5.9 5.6 4.5
  5.2 5.9 5.5 5.8 5.9 6.2 5.7 5.4 6.0
  5.5 6.1 5.7 5.6 5.5 5.7 5.9 5.1 5.9 6.2
  5.5 6.1 5.9 5.6 5.7 5.9 5.5 4.9 5.8 6.1 6.2
  5.2 6.3 5.7 5.6 6.2 5.8 5.8 4.7 5.6 5.9 5.8 6.1
  5.3 6.3 6.3 5.9 5.8 5.6 5.7 5.8 5.9 5.9 6.2 6.5 5.9
  5.5 6.1 6.1 5.9 5.8 6.1 5.9 6.0 6.0 6.2 6.2 5.5 6.2 6.3
  5.3 6.1 5.5 5.2 5.7 5.4 5.3 4.0 5.5 5.9 5.8 5.9 5.8 5.8 5.3
  4.7 5.4 5.1 4.7 5.3 5.3 5.2 4.4 5.4 5.4 5.6 5.5 5.2 5.6 5.2 5.0
  5.1 6.0 5.5 5.3 5.5 5.3 5.2 5.5 5.6 5.8 5.8 5.7 5.9 6.1 5.5 5.2 5.4
  5.9 5.9 6.5 6.0 6.1 6.2 6.2 5.2 6.0 6.3 6.3 5.7 6.5 6.5 5.8 5.7 6.5 7.5
  5.6 6.3 5.9 6.2 6.1 6.7 6.1 4.8 6.2 6.2 6.1 5.7 6.1 6.4 5.6 5.9 6.1 6.9 6.5
  5.4 6.0 5.6 5.6 5.7 5.4 5.4 4.6 5.6 6.0 6.0 5.9 5.9 6.0 5.7 5.4 5.7 6.3 6.0 5.8
//
H BONM030106
D Distances between centers of interacting side chains in the parallel
  orientation
R PMID:15072433
A Boniecki, M., Rotkiewicz, P., Skolnick, J. and Kolinski, A.
T Protein fragment reconstruction using various modeling techniques
J J. Comput. Aided Mol. Des. 17, 725-738 (2003)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  4.8
  5.5 6.7
  4.9 6.0 6.1
  5.0 6.0 5.0 5.0
  5.1 6.1 5.2 5.1 4.2
  5.3 6.4 5.9 5.5 6.1 6.1
  4.8 6.1 5.0 5.0 5.7 6.5 5.7
  4.5 6.7 5.3 6.1 5.2 7.2 5.3 4.5
  5.3 5.5 5.5 5.5 6.0 6.8 5.8 5.3 6.2
  5.5 6.2 5.3 6.0 5.9 6.0 5.9 5.2 6.3 6.4
  5.4 6.0 5.8 5.6 5.7 5.6 5.7 5.7 5.8 6.3 6.2
  5.4 5.3 5.9 5.8 6.5 5.8 6.3 4.9 5.9 5.9 6.0 5.5
  5.3 6.1 5.7 5.5 5.3 5.2 6.2 5.3 5.7 6.1 6.3 5.8 5.5
  5.8 5.9 6.1 5.6 5.9 6.1 6.0 5.3 6.1 6.4 6.3 5.8 6.0 6.4
  4.9 5.3 5.1 5.4 5.2 5.8 5.6 4.4 5.4 5.9 5.9 5.4 6.1 5.6 5.2
  4.9 5.7 5.2 5.4 5.5 5.3 4.9 5.1 5.5 5.8 5.5 5.4 5.5 5.5 5.1 5.0
  4.9 6.0 5.2 5.2 6.0 6.3 5.3 5.0 5.9 6.1 5.9 5.6 5.7 5.9 5.3 5.2 5.5
  5.8 6.3 6.2 6.3 6.5 6.7 6.8 4.5 6.6 6.6 6.6 5.0 6.6 6.3 5.9 5.6 6.5 7.0
  5.7 6.5 6.1 6.2 5.9 5.5 6.5 6.2 5.7 6.2 6.0 5.8 6.0 6.1 6.0 6.1 6.5 6.1 6.2
  5.2 6.0 5.4 5.6 5.8 6.0 5.5 4.9 5.8 6.1 6.1 6.3 5.9 6.1 5.5 5.4 5.8 6.4 6.1 5.8
//
H MICC010101
D Optimization-derived potential
R PMID:11151013 
A Micheletti, C., Seno, F., Banavar, J.R. and Maritan, A.
T Learning effective amino acid interactions through iterative
  stochastic techniques
J Proteins 42, 422-431 (2001)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.001461
  -0.002511  0.009875
   0.003323 -0.006728 -0.001962
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   0.005029 -0.001210  0.004502 -0.001466  0.001387  0.008438
  -0.002376 -0.004586 -0.003154  0.002194  0.002791 -0.005234  0.006456
  -0.003111  0.002466 -0.001649  0.001528  0.001847 -0.000425 -0.000113  0.000990
  -0.002432  0.009985  0.008099 -0.002501  0.054553  0.005803 -0.007232 -0.000951  0.001314
  -0.002119  0.001034  0.002317  0.002659  0.002965 -0.001875  0.007647  0.000446 -0.000476  0.006801
   0.000864 -0.001302 -0.000605  0.000585 -0.000196 -0.004168 -0.000453 -0.001538 -0.004529 -0.000782 -0.000748
   0.001754  0.007273  0.006158 -0.000642 -0.006040  0.002349 -0.009604 -0.001308  0.002934  0.000855  0.002119  0.005109
  -0.001496 -0.004676  0.018413  0.001491  0.014331 -0.002908  0.003231  0.002339  0.031785 -0.009283 -0.002531 -0.004667  0.031655
   0.005126  0.004855  0.003461  0.004899 -0.013925  0.003790 -0.001143  0.000189 -0.000190 -0.009792 -0.002127 -0.004479  0.001010 -0.013128
  -0.005081 -0.000067  0.003707  0.000755 -0.001720  0.000525  0.005402  0.009071 -0.002032  0.004353 -0.005026  0.009888 -0.008698 -0.006986 -0.003621
  -0.001515 -0.001180  0.006249 -0.001609  0.001837 -0.009002  0.002888 -0.003528  0.009858  0.001538  0.001004  0.005015  0.002007 -0.001223 -0.003125 -0.000802
  -0.000218  0.003967 -0.005914  0.002193  0.002620  0.001006  0.000948  0.001084 -0.005871 -0.004179  0.003770 -0.005895 -0.002190  0.004102  0.005402 -0.002393  0.003269
  -0.009737 -0.014845 -0.003028 -0.007832 -0.035239  0.012075 -0.009357 -0.012366 -0.006739  0.002734  0.010659 -0.001668  0.984886  0.006057  0.013914 -0.002330  0.003848  0.131813
  -0.000724  0.004237 -0.006968  0.000182  0.002585 -0.005137  0.003261 -0.000737  0.007276 -0.004792  0.003540  0.007956 -0.003258 -0.003256  0.000996 -0.001895 -0.001235  0.003708 -0.007699
   0.003642 -0.005168 -0.001040  0.000092  0.000296  0.000029  0.001387  0.001995 -0.006893  0.002618 -0.001940 -0.006987 -0.005331  0.000008  0.001362 -0.000443  0.004075 -0.001516 -0.002175  0.001445
//
H SIMK990101
D Distance-dependent statistical potential (contacts within 0-5 Angstrooms)
R PMID:10336385
A Simons, K.T., Ruczinski, I., Kooperberg, C., Fox, B.A., Bystroff, C. and Baker,
  D.
T Improved recognition of native-like protein structures using
  a combination of sequence-dependent and sequence-independent
  features of proteins
J Proteins 34, 82-95 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.13571
   0.37121  0.23245
   0.25935 -0.27050 -0.61455
   0.33397 -0.78243 -0.41830  0.06704
   0.23079  0.49103  0.32481  0.53024 -1.79243
   0.26575 -0.25307 -0.26143 -0.00061  0.25200 -0.24068
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   0.32413 -0.10894 -0.00420 -0.47402  0.24383 -0.03046 -0.10674  0.08603 -0.23317
  -0.22176  0.33584  0.38282  0.44972  0.12534  0.20555  0.21945  0.36527  0.10553 -0.3170
  -0.15025  0.19784  0.35359  0.38200  0.10747  0.07523  0.19892  0.30617  0.11443 -0.1261 -0.19983
   0.39894  0.55155 -0.07038 -0.90014  0.73178 -0.24804 -0.92364  0.00501  0.00361  0.2170  0.21292  0.56407
   0.03521  0.12999  0.02882  0.32317  0.04462 -0.03542  0.15161  0.14609  0.01416 -0.0879 -0.12860  0.15363 -0.13998
   0.08139  0.03136  0.26608  0.53784  0.09641  0.14340  0.25134  0.21293  0.03923 -0.1911 -0.22682  0.04828 -0.23360 -0.24651
   0.03615 -0.06999 -0.20175 -0.21449 -0.04477 -0.16569 -0.14194 -0.18438 -0.27877  0.5603  0.35217  0.04081  0.11287 -0.10484 -0.04170
   0.10475 -0.02548 -0.28825 -0.50285  0.11283 -0.06140 -0.35312 -0.27119 -0.11302  0.3130  0.27135  0.02715  0.19696  0.28005 -0.10791 -0.20955
  -0.04679 -0.05313 -0.28531 -0.36579  0.27539 -0.23014 -0.29144 -0.24551 -0.25624  0.2867  0.31011 -0.13219  0.30090  0.37472  0.02844 -0.32381 -0.19546
   0.20001 -0.33116  0.28602  0.50378  0.09401 -0.04570  0.16071  0.24344 -0.17229 -0.1598 -0.16843 -0.24586 -0.09998 -0.13588 -0.55908  0.36554  0.33614  0.05462
   0.12835 -0.14488  0.12638  0.46473  0.16464 -0.03777  0.18883  0.10640  0.02691 -0.1696 -0.20609 -0.16896 -0.22924 -0.01526 -0.41613  0.31614  0.36576 -0.03280 -0.01669
  -0.27134  0.33279  0.47451  0.44658  0.09778  0.08581  0.22764  0.23105  0.15787 -0.1963 -0.10641  0.23784  0.00637 -0.08226  0.39761  0.15369  0.14755  0.12174  0.02059 -0.29733
//
H SIMK990102
D Distance-dependent statistical potential (contacts within 5-7.5 Angstrooms)
R PMID:11782533
A Simons, K.T., Ruczinski, I., Kooperberg, C., Fox, B.A., Bystroff, C. and Baker,
  D.
T Improved recognition of native-like protein structures using
  a combination of sequence-dependent and sequence-independent
  features of proteins
J Proteins 34, 82-95 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.02226
   0.09517  0.07551
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   0.08891 -0.10846 -0.29003 -0.22107  0.06070 -0.25399
   0.15220 -0.73107 -0.29050 -0.05421  0.46641 -0.22637 -0.06802
  -0.05662 -0.11493 -0.20722 -0.13454 -0.15618 -0.16506 -0.01456 -0.14051
   0.02143  0.02841 -0.22095 -0.51082 -0.08947 -0.13022 -0.38576 -0.17065 -0.55055
  -0.03193  0.34774  0.49079  0.64069  0.08276  0.31459  0.51696  0.27635  0.51369 -0.38531
   0.01865  0.31116  0.49954  0.67107  0.03309  0.32215  0.47591  0.33203  0.31403 -0.35708 -0.36593
   0.14682  0.05722 -0.28908 -0.83773  0.30183 -0.21644 -0.84899 -0.13111  0.15045  0.37502  0.42522  0.06908
  -0.08634  0.23747  0.13447  0.34501 -0.03164  0.13752  0.21535  0.15193  0.04739 -0.15359 -0.14099  0.32782 -0.16514
  -0.14905  0.27997  0.27039  0.33380 -0.08872  0.11689  0.29542  0.05265  0.09431 -0.09249 -0.12690  0.31158 -0.11997 -0.19925
   0.08000 -0.11752 -0.22235 -0.10799 -0.09590 -0.18800 -0.08512 -0.05692 -0.05316  0.19667  0.20002 -0.01420  0.08185  0.16121 -0.20538
   0.00350 -0.18824 -0.23763 -0.17464 -0.06203 -0.19343 -0.21143 -0.20971 -0.19378  0.35197  0.34207 -0.13103  0.10816  0.09814 -0.11199 -0.18928
   0.00526 -0.05800 -0.15047 -0.04369 -0.02885 -0.16004 -0.12650 -0.08635 -0.08904  0.11428  0.15723 -0.12997  0.10441  0.14806 -0.13377 -0.07783 -0.08219
  -0.11261  0.04019  0.03693 -0.00891 -0.17325 -0.03032 -0.09799 -0.09435 -0.02796  0.13403  0.13555  0.14321  0.00104 -0.05715 -0.13591 -0.03151  0.03798 -0.05100
  -0.05314  0.01551  0.05800 -0.12981  0.00201 -0.02419 -0.03815 -0.00928  0.00739  0.08237  0.03594 -0.03110 -0.01117 -0.03704 -0.10661 -0.02162  0.06792 -0.00889  0.00158
  -0.02354  0.33249  0.40194  0.49624 -0.01849  0.28120  0.41691  0.14201  0.34177 -0.27482 -0.27941  0.33110 -0.07385 -0.12269  0.15123  0.25468  0.08308  0.07499  0.04100 -0.25929
//
H SIMK990103
D Distance-dependent statistical potential (contacts within 7.5-10 Angstrooms)
R PMID:11782533
A Simons, K.T., Ruczinski, I., Kooperberg, C., Fox, B.A., Bystroff, C. and Baker,
  D.
T Improved recognition of native-like protein structures using
  a combination of sequence-dependent and sequence-independent
  features of proteins
J Proteins 34, 82-95 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.06711
   0.06154 -0.08474
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   0.04917  0.10341  0.02032  0.08274 -0.17110
   0.07189 -0.13486 -0.11794 -0.12196  0.02698 -0.09693
   0.10110 -0.28982 -0.09284 -0.14442  0.12837 -0.10631 -0.17005
   0.02605 -0.05025 -0.02792 -0.01798 -0.06868 -0.02051  0.04571 -0.08089
   0.06456 -0.02235 -0.07118 -0.12234 -0.05122 -0.07235 -0.08473 -0.00788 -0.36006
  -0.10028  0.19111  0.16954  0.17048  0.00854  0.13563  0.14349  0.02672  0.16715 -0.12746
  -0.08988  0.18513  0.12818  0.14879 -0.00733  0.12921  0.14917  0.01380  0.12272 -0.08644 -0.06027
   0.06167 -0.03348 -0.17589 -0.28130  0.10403 -0.16154 -0.32208  0.00219  0.05396  0.16985  0.10764 -0.19507
  -0.03220  0.07068  0.11448  0.06630 -0.10678  0.01964  0.07144 -0.02177  0.03768 -0.00634  0.01406  0.15021 -0.00959
   0.02583  0.15212  0.09736  0.14568 -0.05523  0.06410  0.11831  0.07023  0.03701 -0.08883 -0.11808  0.14062 -0.11397 -0.10140
   0.04566 -0.16615 -0.09111 -0.05572  0.01966 -0.08858 -0.10634 -0.04698 -0.05851  0.12930  0.07467 -0.12627  0.09356  0.12370 -0.13648
   0.05356 -0.09178 -0.07509  0.00009 -0.00836 -0.05424  0.00702  0.00867 -0.06447  0.04214  0.01289 -0.03768 -0.02411 -0.01294 -0.02111  0.01170
   0.04740 -0.04650 -0.02649  0.00758 -0.04399 -0.01817 -0.02133 -0.00796 -0.03512  0.00418  0.01068 -0.01572 -0.00949  0.03108  0.02446 -0.01390 -0.01606
   0.08732  0.07735  0.00987  0.02263 -0.02572 -0.06867 -0.04921  0.10405 -0.11836  0.03430 -0.06007  0.14702 -0.06644 -0.11108  0.01048  0.01889  0.01650 -0.07522
   0.03904  0.02232 -0.01661 -0.05851 -0.01389 -0.04713 -0.08186  0.04000 -0.03306  0.02135  0.00677  0.06447 -0.00096 -0.02173 -0.05590  0.00139  0.00633 -0.09071 -0.03925
  -0.07279  0.17288  0.10802  0.14779  0.00772  0.11813  0.11895  0.02340  0.07075 -0.13605 -0.06701  0.12223 -0.01508 -0.04855  0.11169  0.03754  0.01024  0.01594  0.03319 -0.10756
//
H SIMK990104
D Distance-dependent statistical potential (contacts within 10-12 Angstrooms)
R PMID:11782533
A Simons, K.T., Ruczinski, I., Kooperberg, C., Fox, B.A., Bystroff, C. and Baker,
  D.
T Improved recognition of native-like protein structures using
  a combination of sequence-dependent and sequence-independent
  features of proteins
J Proteins 34, 82-95 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.01427
   0.00319 -0.07401
   0.03854 -0.05011 -0.03011
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   0.02023 -0.02214 -0.02505 -0.00434  0.02667 -0.06601
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   0.03371  0.00933 -0.00528 -0.02100 -0.02424 -0.02658  0.03380 -0.02023
   0.01652  0.02289 -0.02616  0.01351 -0.06586 -0.00106  0.01615 -0.08543 -0.11699
  -0.04417  0.06128  0.02517  0.00868  0.04323  0.04162  0.03018  0.00072  0.06119 -0.03438
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   0.02263 -0.01342 -0.07512 -0.08884 -0.02198 -0.06324 -0.05330 -0.01507  0.02330  0.07910  0.04662 -0.06779  0.02119  0.05823 -0.08318
   0.00275 -0.00075 -0.00988  0.01674 -0.01602  0.02246  0.04724 -0.02573  0.00237  0.00588 -0.00136  0.05413 -0.02691 -0.00236  0.00469 -0.01442
   0.00640  0.03515  0.00571 -0.01276 -0.01331  0.01648 -0.00250 -0.01628  0.01188 -0.02153  0.00533  0.02293  0.00568  0.01079  0.01434  0.00670 -0.00561
   0.01054 -0.03369 -0.01820 -0.03207 -0.09886  0.00147 -0.01159 -0.06240 -0.05614  0.09042  0.05414  0.03346 -0.01871 -0.02970 -0.01974 -0.03103  0.08390 -0.11149
   0.01209 -0.04663 -0.02262 -0.00868  0.03435 -0.03331  0.00113 -0.01505 -0.01576  0.07198  0.03288  0.00194 -0.01283  0.00165 -0.04774 -0.03088 -0.02709 -0.01196 -0.05834
  -0.02005  0.03622  0.04989  0.03410 -0.01558  0.01771  0.04775  0.00420  0.01640 -0.04232 -0.00721  0.01947  0.03434 -0.00626  0.06160 -0.00012 -0.01448  0.03785  0.03352 -0.06684
//
H SIMK990105
D Distance-dependent statistical potential (contacts longer than 12 Angstrooms)
R PMID:11782533
A Simons, K.T., Ruczinski, I., Kooperberg, C., Fox, B.A., Bystroff, C. and Baker,
  D.
T Improved recognition of native-like protein structures using
  a combination of sequence-dependent and sequence-independent
  features of proteins
J Proteins 34, 82-95 (1999)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.00347
   0.00335 -0.00407
   0.00391 -0.00739 -0.01002
   0.00414 -0.01600 -0.00825 -0.00786
   0.00180  0.01195  0.00797  0.01489 -0.10838
   0.00343 -0.00609 -0.00689 -0.00644  0.00991 -0.00745
   0.00406 -0.01522 -0.00681 -0.00727  0.01832 -0.00728 -0.00947
   0.00106 -0.00194 -0.00340 -0.00242 -0.00362 -0.00242  0.00092 -0.00526
   0.00321  0.00007 -0.00362 -0.00685 -0.00424 -0.00218 -0.00352 -0.00394 -0.02024
  -0.00746  0.01401  0.01338  0.01451 -0.00508  0.01197  0.01407  0.00567  0.01233 -0.02696
  -0.00482  0.01049  0.01113  0.01230 -0.00648  0.00870  0.01041  0.00659  0.00681 -0.01896 -0.01700
   0.00368 -0.00416 -0.00823 -0.01640  0.01873 -0.00765 -0.01791 -0.00007  0.00289  0.01311  0.01001 -0.00994
  -0.00177  0.00669  0.00508  0.00738 -0.00917  0.00385  0.00624  0.00184  0.00257 -0.00919 -0.00508  0.00853 -0.00882
  -0.00212  0.00902  0.00842  0.01138 -0.01487  0.00704  0.01030  0.00378  0.00222 -0.01376 -0.01304  0.01045 -0.00980 -0.01272
   0.00258 -0.00549 -0.00660 -0.00591  0.00302 -0.00606 -0.00588 -0.00235 -0.00167  0.01190  0.00832 -0.00579  0.00497  0.00807 -0.00713
   0.00167 -0.00364 -0.00464 -0.00305  0.00104 -0.00264 -0.00227 -0.00315 -0.00329  0.00742  0.00567 -0.00151  0.00105  0.00283 -0.00189 -0.00249
   0.00116 -0.00080 -0.00245 -0.00170 -0.00005 -0.00192 -0.00215 -0.00215 -0.00212  0.00232  0.00380 -0.00127  0.00236  0.00460 -0.00050 -0.00188 -0.00185
   0.00193  0.00135  0.00263  0.00341 -0.01294  0.00050  0.00199  0.00064 -0.00617  0.00233 -0.00152  0.00623 -0.00484 -0.00939 -0.00255  0.00112  0.00473 -0.00844
   0.00110  0.00062  0.00175  0.00156 -0.00260  0.00011  0.00221  0.00113 -0.00113  0.00035 -0.00204  0.00355 -0.00387 -0.00403 -0.00376  0.00071  0.00155 -0.00508 -0.00498
  -0.00590  0.01208  0.01170  0.01302 -0.00933  0.00952  0.01250  0.00366  0.00668 -0.02164 -0.01432  0.01161 -0.00330 -0.01012  0.00972  0.00522  0.00176  0.00082  0.00012 -0.02080
//
H ZHAC000101
D Environment-dependent residue contact energies (rows = helix, cols = helix)
R PMID:10706611
A Zhang, C. and Kim, S.H.
T Environment-dependent residue contact energies for proteins
J Proc. Natl. Acad. Sci. USA 97, 2550-2555 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -1.65
   0.02  1.08
  -0.25  0.25  0.14
  -0.06 -0.16  0.09  0.53
  -2.04 -0.54 -0.95 -1.04 -2.81
   0.00  0.41  0.20  0.15 -0.41  0.59
   0.29 -0.11  0.52  1.32 -0.38  0.47  1.24
  -1.74 -0.11 -0.62 -0.67 -2.35 -0.01  0.37 -1.68
  -0.48  0.34  0.10 -0.09 -1.21  0.43 -0.09 -0.42 -0.40
  -2.09 -0.77 -0.84 -0.65 -2.99 -1.00 -0.52 -2.15 -1.18 -2.72
  -1.89 -0.63 -0.63 -0.31 -2.74 -0.64 -0.22 -1.87 -0.79 -2.93 -2.69
   0.08  1.21  0.32  0.09 -0.46  0.53  0.09 -0.16  0.40 -0.56 -0.20  1.52
  -1.28 -0.10 -0.46  0.14 -2.17 -0.23  0.27 -1.50 -1.00 -2.44 -2.37  0.20 -1.85
  -1.70 -0.39 -0.43 -0.09 -2.87 -0.48 -0.06 -1.63 -1.21 -2.46 -2.58 -0.21 -2.25 -2.45
  -0.26  0.45  0.59  0.44 -1.12  0.94  0.87 -0.45  0.31 -1.14 -0.69  0.64  0.07 -0.42  1.19
  -0.83  0.24 -0.25  0.11 -1.36  0.24  0.50 -1.11 -0.08 -1.35 -1.24  0.37 -0.57 -1.13  0.32 -0.36
  -0.78  0.09 -0.23  0.08 -1.60 -0.03  0.31 -1.23 -0.40 -1.52 -1.48  0.09 -1.12 -1.08  0.00 -0.40 -0.37
  -1.40 -0.65 -0.48 -0.04 -2.02 -0.88 -0.43 -1.58 -0.78 -2.40 -2.27 -0.55 -2.20 -2.40 -0.75 -0.72 -1.22 -1.21
  -1.10 -0.49 -0.28 -0.22 -2.05 -0.33 -0.12 -1.05 -0.59 -2.01 -1.93 -0.41 -1.69 -2.05 -0.41 -0.62 -0.74 -1.82 -1.13
  -1.84 -0.47 -0.71 -0.37 -2.72 -0.32 -0.23 -1.98 -0.88 -2.66 -2.57 -0.37 -2.05 -2.39 -0.97 -1.19 -1.38 -1.82 -1.76 -2.35
//
H ZHAC000102
D Environment-dependent residue contact energies (rows = helix, cols = strand)
R PMID:10706611
A Zhang, C. and Kim, S.H.
T Environment-dependent residue contact energies for proteins
J Proc. Natl. Acad. Sci. USA 97, 2550-2555 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.94  1.26  0.55 0.76 -1.54  1.14 1.57 -0.78  0.44 -1.59 -1.64  1.91 -0.90 -1.49  0.28  0.20 -0.04  -0.92 -0.75 -1.45
   0.56  1.79  2.31 0.79 -0.67  2.54 0.72  1.09  0.94 -0.01  0.01  3.68  0.89 -0.05  1.37  0.83  1.35   0.00  0.33  0.44
   0.59  2.21  1.82 0.77 -0.90  0.46 3.06 -0.16  0.63 -0.33  0.20  2.43  0.99  0.63  0.54  0.24  0.63   0.11 -0.19  0.23
   0.66  0.76  0.76 1.19 -0.21  1.66 2.22  0.29  0.57  0.59  0.79  1.13  1.41  0.49  1.70  1.03  1.19   1.85  0.18  0.86
  -1.75  0.78 -1.00 0.32 -3.64  0.48 0.87 -1.67 -0.62 -2.77 -2.32  0.19 -1.22 -2.67 -1.62 -0.83 -1.14  -0.52 -1.94 -2.35
   0.33  2.15  1.22 1.26  1.37  1.17 2.56  0.92  1.02  0.11  0.00  2.58  0.79 -0.26  0.53  1.19  1.11   0.21  0.39  0.15
   0.82  1.05  2.18 2.11  0.01  2.42 2.58  1.15  0.97  0.20  0.31  1.31  1.25  0.12  2.00  1.09  1.13   0.58  0.31  0.39
  -0.40  0.95  0.03 0.14 -1.00  0.34 0.99 -1.32  0.13 -1.40 -1.36  1.58 -0.90 -1.41  0.82 -0.27  0.21  -0.59 -1.27 -1.09
  -0.75  2.19  0.13 0.68 -1.37  1.98 1.13  0.01  1.52 -0.83 -0.58  2.26 -0.82 -1.01  0.53 -0.17  0.02 -49.00 -0.61 -0.56
  -1.99  0.25 -0.20 1.00 -2.44 -0.12 0.88 -1.54 -0.05 -2.64 -2.33  0.75 -1.85 -2.46 -1.06 -0.59 -0.65  -1.82 -1.88 -2.45
  -2.02  0.34 -0.04 0.13 -2.29  0.24 0.73 -1.27 -0.46 -2.53 -2.44  0.67 -1.80 -2.28 -1.29 -0.40 -0.34  -1.76 -1.66 -2.26
   0.60  3.11  2.23 1.06  0.50  1.80 1.65  0.82  1.25  0.10  0.34  3.51  0.98 -0.21  1.15  2.09  1.30  -0.14  0.28  0.13
  -1.54 -0.06 -0.63 1.76 -2.51  0.14 0.72 -1.74  0.07 -2.27 -2.22  1.27 -1.77 -1.87  0.34 -0.02 -0.21  -0.93 -1.54 -1.81
  -2.12  0.33 -0.70 0.17 -2.30 -0.59 0.26 -1.60 -0.88 -2.53 -2.44 -0.42 -1.83 -2.68 -1.40 -0.82 -0.61  -1.63 -1.83 -2.25
   0.63  2.43 -0.19 1.31 -1.63  1.46 1.91  0.08  1.11 -0.20  0.47  1.94 -0.34  0.15  0.57  0.00  1.15   0.06  0.26 -0.06
  -0.41  0.88  1.02 1.04 -0.21  1.27 0.94  0.04  0.75 -0.48 -0.67  2.28  0.45 -0.92  0.75  0.50  0.96   0.22 -0.19 -0.54
  -0.32  1.48  0.35 0.43 -1.44  0.38 1.36 -0.38  0.20 -1.14 -1.00  1.38 -0.35 -0.97 -0.05 -0.16  0.29  -0.53 -0.76 -0.73
  -1.85  0.45 -0.03 0.80 -1.64 -0.23 0.11 -0.95  0.67 -1.58 -2.13  0.61 -1.75 -1.59 -1.07 -0.34 -0.40  -1.29 -1.27 -1.79
  -0.88 -0.20 -0.29 0.14 -1.31  0.09 0.71 -0.56 -0.57 -1.66 -1.38  1.40 -1.60 -1.97 -0.73 -0.32 -0.37  -1.40 -0.96 -1.38
  -1.74  0.85  0.24 0.72 -2.25  0.45 0.81 -1.29 -0.24 -2.46 -2.38  0.37 -1.21 -2.16 -1.00 -0.10 -0.57  -1.34 -1.52 -2.31
//
H ZHAC000103
D Environment-dependent residue contact energies (rows = helix, cols = coil)
R PMID:10706611
A Zhang, C. and Kim, S.H.
T Environment-dependent residue contact energies for proteins
J Proc. Natl. Acad. Sci. USA 97, 2550-2555 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.12  1.17  0.84 0.90 -0.81  1.16 1.44  0.10  0.69 -0.81 -0.78 1.16 -0.22 -0.67  0.61  0.47  0.36 -0.72 -0.37 -0.43
   0.98  1.65  1.16 0.60 -0.21  1.26 1.12  1.09  1.16 -0.04 -0.09 2.37  0.47 -0.04  1.22  1.05  0.92 -0.09  0.06  0.32
   0.69  1.16  1.16 1.22 -0.06  1.23 1.45  0.96  0.88  0.26  0.12 1.48  0.32  0.03  1.14  0.73  0.62  0.62  0.53  0.23
   0.90  0.40  1.06 1.45  0.58  1.88 2.18  1.13  0.69  0.43  0.65 0.95  0.75  0.33  1.41  0.39  0.54 -0.10  0.12  0.77
  -0.83  0.10  0.40 0.12 -2.65 -0.24 0.96 -0.26 -0.26 -1.61 -1.77 0.80 -1.02 -1.47 -0.31 -0.31 -0.49 -1.30 -0.98 -1.62
   1.13  1.10  1.28 1.37  0.14  1.62 1.84  1.29  1.31  0.05 -0.05 1.50  0.41  0.20  1.14  0.86  0.62  0.45  0.31  0.48
   1.33  0.91  1.33 1.60  0.31  1.60 1.93  1.62  1.01  0.33  0.38 1.12  0.82  0.55  1.54  0.78  0.54  0.23  0.52  0.86
  -0.22  0.72  0.27 0.47 -0.95  0.42 1.39 -0.23  0.40 -0.48 -0.81 1.04 -0.62 -0.36  0.41  0.23 -0.04 -0.71  0.08 -0.35
   0.47  0.81  0.95 0.51 -1.56  0.90 0.89  0.86  0.20 -0.43 -0.48 1.31 -0.63 -0.41  0.56  0.40  0.28 -0.20 -0.22 -0.21
  -0.58  0.17  0.61 0.46 -1.17  0.24 0.80  0.04 -0.16 -1.64 -1.66 0.87 -0.89 -1.56 -0.27  0.02 -0.32 -1.40 -1.13 -1.36
  -0.44  0.20  0.50 0.71 -1.56  0.11 0.82  0.28 -0.15 -1.67 -1.62 0.72 -0.96 -1.55  0.02  0.19 -0.09 -1.46 -0.95 -1.32
   1.07  2.48  1.75 0.98  0.42  1.68 1.04  1.31  1.39  0.41  0.29 2.95  0.98  0.27  1.63  1.51  1.48  0.32  0.60  0.64
  -0.22  0.65  0.76 0.88 -0.95  0.68 1.92  0.27  0.31 -1.32 -1.04 1.02 -0.57 -1.60  0.07  0.47  0.04 -1.29 -0.85 -0.82
  -0.33 -0.06  0.42 0.42 -1.90  0.25 0.64  0.12 -0.01 -1.64 -1.50 0.58 -1.36 -1.77 -0.30  0.02  0.04 -1.41 -1.36 -1.34
   0.78  1.30  1.31 1.27 -0.04  1.44 1.71  0.69  0.84  0.05  0.15 1.68  0.38  0.27  1.05  1.19  0.83 -0.24  0.23  0.12
   0.46  1.07  1.04 0.73 -0.31  1.47 1.23  0.57  0.58 -0.11 -0.24 1.37  0.08 -0.34  0.76  0.51  0.48 -0.04  0.47  0.18
   0.50  0.90  0.75 0.91 -0.26  1.03 1.25  0.55  0.55 -0.20 -0.26 1.42  0.50 -0.22  0.88  0.69  0.56  0.41  0.11 -0.15
  -0.41 -0.06 -0.19 0.32 -0.79 -0.14 0.58  0.07 -0.62 -1.58 -1.16 0.18 -1.03 -1.33 -0.56  0.15 -0.19 -1.83 -0.67 -0.92
  -0.22 -0.07  0.52 0.46 -0.87  0.38 0.59  0.40 -0.17 -1.29 -1.15 0.83 -0.98 -1.16 -0.16  0.34 -0.12 -0.79 -0.77 -0.78
  -0.51  0.49  0.48 0.67 -1.40  0.66 0.63 -0.06  0.28 -1.25 -1.50 1.14 -0.93 -1.36 -0.04  0.10 -0.01 -1.11 -0.82 -1.14
//
H ZHAC000104
D Environment-dependent residue contact energies (rows = strand, cols = strand)
R PMID:10706611
A Zhang, C. and Kim, S.H.
T Environment-dependent residue contact energies for proteins
J Proc. Natl. Acad. Sci. USA 97, 2550-2555 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -2.52
  -1.24  0.03
  -1.22 -0.80 -0.48
  -1.22 -1.51 -1.17 -0.07
  -3.40 -0.78 -1.72 -1.34 -3.74
  -1.17 -0.68 -0.74 -0.71 -1.97 -0.10
  -0.77 -1.24 -0.67 -0.18 -0.83 -0.47  0.72
  -2.84 -1.25 -1.69 -1.64 -3.17 -1.60 -1.07 -2.60
  -1.69 -0.94 -0.67 -1.44 -2.31 -1.04 -1.17 -2.08 -1.69
  -3.27 -1.41 -1.41 -1.28 -3.73 -1.45 -1.48 -2.93 -1.86 -3.5
  -3.29 -1.18 -1.45 -1.26 -3.63 -1.38 -1.23 -2.98 -1.86 -3.7 -3.5
  -0.70  0.28 -0.35 -1.00 -0.74 -0.42 -1.06 -0.83 -0.61 -1.3 -1.2  0.47
  -2.63 -0.98 -1.32 -1.04 -3.48 -1.66 -0.64 -2.48 -1.55 -3.1 -3.1 -1.17 -1.95
  -2.99 -1.44 -1.41 -1.43 -3.61 -1.59 -1.22 -3.01 -1.83 -3.5 -3.5 -0.92 -3.13 -3.10
  -1.64 -0.84 -0.78 -0.27 -1.92 -0.58  0.38 -1.85 -0.81 -1.6 -1.9 -0.41 -1.43 -1.75  0.20
  -1.74 -0.81 -1.16 -1.09 -2.23 -1.10 -0.85 -2.03 -1.53 -1.6 -1.8 -0.83 -1.72 -1.77 -0.48 -1.03
  -1.87 -0.89 -0.90 -1.00 -2.39 -1.03 -1.17 -1.84 -1.29 -2.0 -1.8 -1.12 -1.40 -1.52 -0.72 -1.31 -1.29
  -2.20 -1.39 -1.13 -1.00 -3.03 -1.72 -1.21 -2.58 -1.50 -2.9 -2.8 -1.55 -2.31 -2.81 -2.05 -1.50 -1.00 -1.6
  -2.57 -1.57 -1.47 -1.50 -2.92 -1.31 -1.27 -2.69 -1.74 -2.9 -2.7 -1.42 -2.26 -2.73 -1.69 -1.61 -1.46 -2.0 -1.6
  -3.07 -1.26 -1.33 -1.08 -3.33 -1.33 -1.07 -2.78 -1.70 -3.5 -3.5 -1.21 -2.96 -3.21 -1.53 -1.83 -1.82 -2.4 -2.4 -3.1
//
H ZHAC000105
D Environment-dependent residue contact energies (rows = strand, cols = coil)
R PMID:10706611
A Zhang, C. and Kim, S.H.
T Environment-dependent residue contact energies for proteins
J Proc. Natl. Acad. Sci. USA 97, 2550-2555 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
  -0.57  0.47 0.30 0.62 -1.60 0.45 0.61 -0.24  0.07 -1.64 -1.63 0.62 -1.03 -1.55 -0.11 -0.10 -0.34 -1.44 -0.39 -1.55
   0.23  0.79 0.76 0.39 -0.41 0.92 0.76  0.52  0.51 -0.30  0.13 1.58  0.88 -0.07  0.60  0.65  0.37  0.14  0.32  0.17
  -0.28  0.74 0.57 0.87 -0.68 0.52 1.00 -0.07  0.32 -0.31 -0.08 0.87  0.29 -0.17  0.57  0.11  0.19  0.04  0.24 -0.23
   0.15 -0.25 0.46 0.69 -0.46 0.41 1.34  0.56 -0.51 -0.23  0.27 0.59  0.60 -0.38  1.02  0.08  0.05 -0.48  0.02  0.34
  -1.19 -0.46 0.21 0.51 -3.30 0.26 0.20 -1.03 -0.72 -1.55 -1.71 0.27 -1.24 -1.70 -0.50 -0.55 -0.97 -0.67 -1.26 -1.62
   0.63  1.18 0.92 1.37 -0.30 0.93 1.27  0.56  0.91 -0.28 -0.11 0.98  0.15 -0.30  0.64  0.88  0.68 -0.44  0.66  0.15
   0.97  0.89 1.37 1.89  0.30 1.25 2.34  0.98  0.58  0.20  0.50 0.67  1.23  0.58  1.26  0.95  1.06  0.04  0.87  0.48
  -0.64  0.12 0.27 0.31 -1.37 0.38 0.98 -0.40 -0.12 -1.58 -1.40 0.78 -0.46 -1.38 -0.21  0.05 -0.26 -1.41 -0.61 -1.13
  -0.02  0.75 0.68 0.14 -0.58 0.73 0.84  0.41 -0.64 -0.75  0.03 1.46 -0.16 -0.49  0.52  0.31 -0.11 -1.00 -0.58  0.03
  -0.94 -0.14 0.31 0.26 -1.70 0.07 0.46 -0.37 -0.50 -1.88 -1.79 0.84 -0.99 -1.82 -0.47 -0.05 -0.54 -1.65 -1.09 -1.64
  -0.76  0.32 0.43 0.25 -1.63 0.22 0.68 -0.17 -0.40 -1.84 -1.70 0.47 -1.06 -1.76 -0.39  0.09 -0.42 -1.81 -1.15 -1.64
   1.02  1.99 1.18 0.59  0.08 1.10 0.60  0.61  0.95  0.24  0.34 2.69  0.97 -0.03  1.23  1.07  0.83  0.00  0.26  0.36
  -0.16  0.83 0.47 0.92 -1.63 0.36 0.71 -0.20  0.90 -1.00 -1.12 1.55 -0.31 -1.35 -0.01  0.34  0.20 -1.70 -0.60 -0.79
  -0.70  0.03 0.63 0.15 -1.26 0.29 0.35 -0.11 -0.36 -1.73 -1.55 0.71 -0.97 -1.55 -0.28 -0.09 -0.32 -1.23 -0.91 -1.30
   0.17  0.50 0.60 0.67 -1.31 0.50 0.94  0.02 -0.45 -1.26 -0.91 1.08  0.83 -0.87  0.63  0.31  0.26 -0.50 -0.55 -0.79
  -0.06  0.99 0.73 0.86 -0.89 0.85 0.67  0.08  0.06 -0.22 -0.29 0.94 -0.08 -0.41  0.67  0.33  0.13 -1.01  0.13 -0.24
   0.26  0.93 0.70 0.87 -0.78 0.58 1.20  0.12  0.52 -0.30 -0.24 1.11  0.01 -0.08  0.65  0.47  0.41 -0.31  0.12 -0.32
  -0.03 -0.11 0.27 0.66 -1.50 0.65 0.50 -0.12 -0.32 -1.13 -1.01 0.52 -1.08 -1.04 -0.32 -0.03 -0.10 -0.67 -0.73 -0.64
  -0.44  0.20 0.20 0.20 -1.26 0.16 0.10 -0.21 -0.52 -1.26 -1.30 0.60 -0.76 -1.17 -0.42  0.05 -0.27 -1.20 -0.75 -0.84
  -0.83  0.20 0.48 0.62 -1.44 0.17 0.73 -0.12 -0.26 -1.64 -1.59 0.52 -0.70 -1.55 -0.28  0.12 -0.17 -1.16 -0.85 -1.42
//
H ZHAC000106
D Environment-dependent residue contact energies (rows = coil, cols = coil)
R PMID:10706611
A Zhang, C. and Kim, S.H.
T Environment-dependent residue contact energies for proteins
J Proc. Natl. Acad. Sci. USA 97, 2550-2555 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   0.12
   0.56  1.18
   0.59  0.83  0.83
   0.65  0.33  0.61  1.15
  -0.74 -0.25 -0.07 -0.12 -2.42
   0.70  0.94  0.87  0.96 -0.05  1.22
   1.32  0.54  1.09  1.48  0.20  1.11 2.18
   0.11  0.65  0.79  0.75 -0.56  0.73 1.16  0.35
   0.35  0.47  0.91  0.29 -0.83  0.83 0.74  0.53  0.28
  -0.45  0.05  0.40  0.47 -1.27  0.24 0.70  0.01 -0.21 -1.04
  -0.25  0.26  0.37  0.57 -1.25  0.38 0.82  0.13 -0.03 -1.15 -1.04
   1.06  1.65  1.11  0.58  0.76  1.29 0.93  1.08  1.23  0.48  0.78 2.23
   0.29  0.58  0.68  0.75 -0.74  0.65 1.08  0.54  0.19 -0.52 -0.68 1.15 -0.12
  -0.41  0.24  0.46  0.38 -1.44  0.39 0.55  0.09 -0.28 -1.09 -1.05 0.74 -0.60 -1.09
   0.48  0.82  1.09  1.26 -0.23  1.09 1.25  0.74  0.59  0.14  0.10 1.59  0.54 -0.04  1.11
   0.45  0.55  0.81  0.54 -0.47  0.75 0.87  0.61  0.46  0.09  0.01 1.24  0.56  0.17  0.94  0.87
   0.30  0.80  0.54  0.51 -0.37  0.81 0.81  0.38  0.31 -0.28 -0.05 1.10  0.46  0.08  0.67  0.54  0.69
  -0.28 -0.04  0.13  0.43 -0.63 -0.01 0.44 -0.17 -0.44 -1.28 -0.98 0.23 -0.50 -1.02 -0.33  0.14 -0.19 -0.46
  -0.07  0.22  0.40  0.38 -0.58  0.09 0.47  0.28 -0.18 -0.74 -0.56 0.62 -0.26 -0.63  0.04  0.23  0.27 -0.87 -0.18
  -0.18  0.43  0.54  0.59 -1.22  0.23 0.74  0.04  0.09 -0.90 -0.93 0.81 -0.31 -0.77  0.17  0.20 -0.10 -0.57 -0.38 -0.31
//