H ALTS910101
D The PAM-120 matrix (Altschul, 1991)
R LIT:1713145 PMID:2051488
A Altschul, S.F.
T Amino acid substitution matrices from an information theoretic perspective
J J. Mol. Biol. 219, 555-565 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      3.
     -3.      6.
      0.     -1.      4.
      0.     -3.      2.      5.
     -3.     -4.     -5.     -7.      9.
     -1.      1.      0.      1.     -7.      6.
      0.     -3.      1.      3.     -7.      2.      5.
      1.     -4.      0.      0.     -5.     -3.     -1.      5.
     -3.      1.      2.      0.     -4.      3.     -1.     -4.      7.
     -1.     -2.     -2.     -3.     -3.     -3.     -3.     -4.     -4.      6.
     -3.     -4.     -4.     -5.     -7.     -2.     -4.     -5.     -3.      1.      5.
     -2.      2.      1.     -1.     -7.      0.     -1.     -3.     -2.     -2.     -4.      5.
     -2.     -1.     -3.     -4.     -6.     -1.     -4.     -4.     -4.      1.      3.      0.      8.
     -4.     -4.     -4.     -7.     -6.     -6.     -6.     -5.     -2.      0.      0.     -6.     -1.      8.
      1.     -1.     -2.     -2.     -3.      0.     -1.     -2.     -1.     -3.     -3.     -2.     -3.     -5.      6.
      1.     -1.      1.      0.     -1.     -2.     -1.      1.     -2.     -2.     -4.     -1.     -2.     -3.      1.      3.
      1.     -2.      0.     -1.     -3.     -2.     -2.     -1.     -3.      0.     -3.     -1.     -1.     -4.     -1.      2.      4.
     -7.      1.     -5.     -8.     -8.     -6.     -8.     -8.     -5.     -7.     -5.     -5.     -7.     -1.     -7.     -2.     -6.     12.
     -4.     -6.     -2.     -5.     -1.     -5.     -4.     -6.     -1.     -2.     -3.     -6.     -4.      4.     -6.     -3.     -3.     -1.      8.
      0.     -3.     -3.     -3.     -2.     -3.     -3.     -2.     -3.      3.      1.     -4.      1.     -3.     -2.     -2.      0.     -8.     -3.      5.
//
H BENS940101
D Log-odds scoring matrix collected in 6.4-8.7 PAM (Benner et al., 1994)
R LIT:2023094 PMID:7700864
A Benner, S.A., Cohen, M.A. and Gonnet, G.H.
T Amino acid substitution during functionally constrained divergent
  evolution of protein sequences
J Protein Engineering 7, 1323-1332 (1994)
* extrapolated to 250 PAM
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     2.5
    -1.7     5.1
     0.0    -0.1     3.6
    -0.6    -1.5     2.5     5.2
    -1.7    -0.4    -1.6    -3.7    12.1
    -1.7     2.5     0.1     0.6    -3.2     5.3
    -0.7    -0.4     1.1     4.4    -4.7     2.1     5.2
     0.8    -0.1    -0.1     0.8    -1.3    -1.6     0.5     5.8
    -2.1     1.8     1.4     0.1    -1.2     3.2    -0.2    -2.1     6.1
     0.1    -3.8    -2.5    -4.2    -3.6    -3.8    -4.1    -3.4    -3.7     4.4
    -1.3    -3.2    -3.4    -5.3    -3.8    -2.4    -5.0    -4.6    -2.2     2.4     4.8
    -1.9     4.3     1.0    -0.2    -2.8     2.5     0.9    -1.4     0.9    -3.8    -4.1     5.6
    -0.2    -3.0    -2.5    -4.3    -3.7    -3.1    -4.1    -3.7    -3.4     4.0     2.9    -2.9     4.8
    -3.2    -4.9    -3.5    -5.7    -0.1    -4.4    -6.7    -5.7     0.1     0.0     2.4    -6.3    -0.1     8.3
     1.1    -1.3    -1.1    -2.8    -2.7     0.1    -2.6    -1.7    -0.4    -2.0    -0.2    -2.3    -1.8    -3.2     6.5
     1.4    -0.9     1.2    -0.4     0.9    -1.4    -1.2     0.8    -0.9    -1.2    -1.5    -1.2    -1.3    -1.8     1.4     2.1
     1.7    -1.3     0.5    -1.2    -1.5    -1.7    -1.6    -0.5    -1.7     0.7    -0.4    -1.1     0.6    -2.4     0.6     1.5     2.4
    -4.3     2.0    -4.4    -6.3     1.6    -2.6    -5.6    -1.7    -2.8    -5.0    -3.0    -1.4    -4.4    -1.6    -4.8    -2.9    -2.6    14.7
    -4.0    -2.6    -0.9    -2.3     2.6    -1.4    -4.1    -4.9     4.4    -3.3    -1.6    -4.0    -3.6     5.6    -3.8    -1.8    -3.4    -0.3     9.5
     0.7    -3.7    -2.4    -3.3    -3.1    -3.5    -3.0    -2.3    -3.8     3.9     1.9    -3.8     3.3    -0.5    -1.6    -0.9     0.6    -4.8    -3.8     4.0
//
H BENS940102
D Log-odds scoring matrix collected in 22-29 PAM (Benner et al., 1994)
R LIT:2023094 PMID:7700864
A Benner, S.A., Cohen, M.A. and Gonnet, G.H.
T Amino acid substitution during functionally constrained divergent
  evolution of protein sequences
J Protein Engineering 7, 1323-1332 (1994)
* extrapolated to 250 PAM
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     2.5
    -1.2     5.0
     0.0     0.4     3.3
    -0.2    -1.0     2.4     4.8
    -1.2    -1.6    -1.9    -3.7    12.6
    -0.9     2.2     0.5     0.6    -3.3     4.2
    -0.3    -0.1     1.2     3.9    -4.3     1.7     4.6
     0.8    -0.7     0.4     0.7    -1.7    -1.4     0.5     6.2
    -1.6     1.5     1.4     0.3    -1.5     2.4    -0.2    -2.0     6.1
    -0.4    -3.2    -2.7    -4.0    -2.4    -2.7    -3.6    -3.8    -3.2     4.2
    -1.7    -2.9    -3.5    -4.9    -2.6    -2.0    -4.4    -4.9    -2.1     2.7     4.6
    -1.0     3.9     1.0     0.2    -3.3     2.2     1.0    -1.0     0.8    -3.0    -3.3     4.4
    -0.8    -2.1    -2.6    -3.9    -2.5    -1.7    -3.4    -3.8    -2.4     3.1     3.2    -2.0     4.9
    -3.1    -4.3    -3.5    -5.4    -0.1    -3.6    -5.7    -5.8     0.3     0.5     2.2    -5.1     0.7     7.7
     0.8    -1.2    -1.1    -1.8    -3.1    -0.1    -1.7    -1.8    -0.4    -2.3    -1.3    -1.6    -2.0    -3.4     7.0
     1.3    -0.5     1.1     0.1     0.3    -0.6    -0.5     0.6    -0.5    -1.4    -2.1    -0.4    -1.5    -2.2     1.1     2.0
     1.4    -0.7     0.5    -0.7    -1.1    -0.7    -0.9    -0.7    -1.1     0.3    -1.0    -0.4     0.1    -2.6     0.4     1.5     2.5
    -5.5    -1.1    -5.2    -6.4     0.5    -3.3    -6.3    -4.5    -2.7    -4.4    -1.8    -3.7    -2.8     0.5    -5.8    -3.9    -4.5    15.7
    -3.5    -2.7    -1.2    -3.0     0.6    -1.9    -4.0    -4.8     3.7    -2.2    -0.7    -3.6    -1.8     5.9    -3.5    -1.9    -3.0     1.5     9.0
     0.4    -2.9    -2.3    -3.0    -1.7    -2.4    -2.7    -2.5    -3.0     3.6     2.0    -2.7     2.5    -0.1    -1.7    -0.9     0.4    -4.5    -2.6     3.7
//
H BENS940103
D Log-odds scoring matrix collected in 74-100 PAM (Benner et al., 1994)
R LIT:2023094 PMID:7700864
A Benner, S.A., Cohen, M.A. and Gonnet, G.H.
T Amino acid substitution during functionally constrained divergent
  evolution of protein sequences
J Protein Engineering 7, 1323-1332 (1994)
* extrapolated to 250 PAM
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     2.4
    -0.8     4.8
    -0.2     0.3     3.6
    -0.3    -0.5     2.2     4.8
     0.3    -2.2    -1.8    -3.2    11.8
    -0.3     1.6     0.7     0.8    -2.6     3.0
    -0.1     0.3     1.0     2.9    -3.2     1.7     3.7
     0.6    -1.0     0.4     0.2    -2.0    -1.1    -0.5     6.6
    -1.0     1.0     1.2     0.4    -1.3     1.4     0.2    -1.6     6.1
    -0.8    -2.6    -2.8    -3.9    -1.2    -2.0    -2.9    -4.3    -2.3     4.0
    -1.4    -2.4    -3.1    -4.2    -1.6    -1.7    -3.1    -4.6    -1.9     2.8     4.2
    -0.4     2.9     0.9     0.4    -2.9     1.7     1.2    -1.1     0.6    -2.3    -2.4     3.4
    -0.8    -1.8    -2.2    -3.2    -1.2    -1.0    -2.2    -3.5    -1.5     2.6     2.9    -1.5     4.5
    -2.6    -3.5    -3.2    -4.7    -0.7    -2.8    -4.3    -5.4     0.0     0.9     2.1    -3.6     1.3     7.2
     0.4    -1.0    -1.0    -1.0    -3.1    -0.2    -0.7    -1.7    -1.0    -2.6    -2.2    -0.8    -2.4    -3.8     7.5
     1.1    -0.2     0.9     0.4     0.1     0.1     0.1     0.4    -0.3    -1.8    -2.2     0.0    -1.4    -2.6     0.5     2.1
     0.7    -0.3     0.4    -0.2    -0.6    -0.1    -0.2    -1.0    -0.5    -0.3    -1.1     0.1    -0.4    -2.2     0.1     1.4     2.5
    -4.1    -1.6    -4.0    -5.5    -0.9    -2.8    -4.7    -4.1    -1.0    -2.3    -0.9    -3.6    -1.3     3.0    -5.2    -3.4    -3.7    14.7
    -2.6    -2.0    -1.4    -2.8    -0.4    -1.8    -3.0    -4.3     2.5    -1.0    -0.1    -2.4    -0.5     5.3    -3.4    -1.9    -2.1     3.6     8.1
     0.1    -2.2    -2.2    -2.9    -0.2    -1.7    -2.1    -3.1    -2.1     3.2     1.9    -1.9     1.8     0.1    -1.9    -1.0     0.2    -2.9    -1.4     3.4
//
H BENS940104
D Genetic code matrix (Benner et al., 1994)
R LIT:2023094 PMID:7700864
A Benner, S.A., Cohen, M.A. and Gonnet, G.H.
T Amino acid substitution during functionally constrained divergent
  evolution of protein sequences
J Protein Engineering 7, 1323-1332 (1994)
* extrapolated to 250 PAM
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     4.0
    -1.6     2.9
    -1.7    -1.5     4.7
     1.0    -2.3     1.7     4.8
    -1.9     0.7    -1.5    -1.6     5.5
    -2.1     0.3     0.4     0.3    -3.1     5.5
     1.3    -2.0     0.3     3.8    -3.0     2.0     5.7
     1.2     0.8    -2.6     1.1     1.0    -2.1     1.4     4.2
    -2.1     3.6     1.8     1.7    -1.6     3.6     0.3    -2.2     4.7
    -1.8    -1.2     0.9    -2.1    -1.9    -1.9    -2.3    -2.5    -1.8     4.1
    -2.3    -0.4    -2.2    -2.4    -1.3     0.1    -2.5    -2.2    -0.1     1.2     3.4
    -1.9    -0.2     3.5     0.3    -3.2     2.2     2.0    -2.2     0.6     0.7    -2.0     5.6
    -2.0    -0.4     0.1    -2.5    -2.7    -1.2    -1.8    -2.3    -1.8     3.3     1.5     1.6     5.4
    -2.4    -1.5    -1.3    -1.7     1.8    -2.1    -2.9    -1.9    -1.1     1.3     2.2    -2.8     0.5     4.5
     0.8     0.3    -1.6    -2.2    -1.9     1.0    -2.1    -1.8     0.7    -1.6     0.0    -1.5    -1.4    -1.8     3.8
     0.1     0.3    -0.3    -2.1     1.5    -2.3    -2.8    -0.6    -1.6    -0.5    -1.2    -1.5    -1.3     0.0     0.4     2.6
     0.9    -0.6     0.9    -2.1    -1.9    -1.7    -2.1    -2.1    -1.8     0.8    -1.9     1.0     0.7    -2.1     1.1     1.0     4.0
    -2.2     1.8    -3.0    -2.9     4.1    -2.3    -3.2     1.4    -2.1    -2.2    -0.3    -3.0    -2.0     0.0    -1.6     0.8    -2.2     7.5
    -2.4    -1.9     2.5     2.3     2.6    -0.8    -0.9    -1.8     2.3    -1.6    -1.6    -0.8    -2.9     2.0    -2.3     0.3    -2.1    -0.5     6.5
     1.0    -2.1    -2.2     1.0    -2.2    -2.0     1.3     1.1    -2.1     1.0     1.1    -2.1     1.0     1.0    -2.1    -2.2    -2.2    -2.1    -2.2     4.1
//
H CSEM940101
D Residue replace ability matrix (Cserzo et al., 1994)
R LIT:2022066 PMID:7966267
A Cserzo, M., Bernassau, J.-M., Simon, I. and Maigret, B.
T New alignment strategy for transmembrane proteins
J J. Mol. Biol. 243, 388-396 (1994)
* Diagonal elements are missing.
* We use 1 as diagonal elements.
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      1.
   -0.07      1.
   -0.14    0.12      1.
   -0.08   -0.01    0.56      1.
    0.04   -0.20   -0.14   -0.24      1.
   -0.01    0.57    0.20    0.19   -0.29      1.
    0.08    0.34    0.13    0.37   -0.51    0.51      1.
    0.11   -0.11    0.22    0.11    0.25   -0.13   -0.23      1.
   -0.11    0.13    0.32    0.22    0.18    0.05   -0.19    0.18      1.
   -0.10   -0.29   -0.37   -0.54    0.26   -0.43   -0.51   -0.22   -0.14      1.
    0.20   -0.20   -0.39   -0.55    0.23   -0.30   -0.45   -0.14   -0.12    0.60      1.
   -0.07    0.47    0.22    0.18   -0.43    0.52    0.54   -0.23   -0.09   -0.40   -0.34      1.
    0.15   -0.17   -0.11   -0.25    0.10   -0.18   -0.14   -0.01   -0.19    0.36    0.38   -0.16      1.
   -0.25   -0.31   -0.33   -0.40    0.30   -0.44   -0.50   -0.09   -0.06    0.60    0.44   -0.41    0.22      1.
   -0.07   -0.17    0.05    0.09    0.02   -0.03   -0.11    0.25    0.05   -0.19   -0.20   -0.17   -0.17   -0.12      1.
    0.14   -0.16    0.14    0.22    0.10   -0.06   -0.17    0.29    0.14   -0.27   -0.19   -0.24   -0.17   -0.01    0.27      1.
    0.11   -0.32    0.13    0.23    0.14   -0.15   -0.27   -0.02    0.08    0.00   -0.04   -0.24   -0.02    0.02    0.20    0.45      1.
   -0.25   -0.03   -0.39   -0.41    0.18   -0.17   -0.22   -0.08   -0.11    0.36    0.22   -0.22    0.16    0.41   -0.13   -0.17   -0.12      1.
   -0.36   -0.03   -0.27   -0.34    0.21   -0.28   -0.32   -0.24    0.08    0.43    0.17   -0.20    0.07    0.54   -0.23   -0.21   -0.14    0.43      1.
    0.06   -0.29   -0.46   -0.48    0.33   -0.38   -0.44   -0.12   -0.18    0.70    0.49   -0.36    0.23    0.47   -0.17   -0.18    0.07    0.29    0.31      1.
//
H DAYM780301
D Log odds matrix for 250 PAMs (Dayhoff et al., 1978)
R
A Dayhoff, M.O., Schwartz, R.M. and Orcutt, B.C.
T A model of evolutionary change in proteins
J In "Atlas of Protein Sequence and Structure", Vol.5, Suppl.3 (Dayhoff,
  M.O., ed.), National Biomedical Research Foundation, Washington, D.C.,
  p.352 (1978)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      2.
     -2.      6.
      0.      0.      2.
      0.     -1.      2.      4.
     -2.     -4.     -4.     -5.     12.
      0.      1.      1.      2.     -5.      4.
      0.     -1.      1.      3.     -5.      2.      4.
      1.     -3.      0.      1.     -3.     -1.      0.      5.
     -1.      2.      2.      1.     -3.      3.      1.     -2.      6.
     -1.     -2.     -2.     -2.     -2.     -2.     -2.     -3.     -2.      5.
     -2.     -3.     -3.     -4.     -6.     -2.     -3.     -4.     -2.      2.      6.
     -1.      3.      1.      0.     -5.      1.      0.     -2.      0.     -2.     -3.      5.
     -1.      0.     -2.     -3.     -5.     -1.     -2.     -3.     -2.      2.      4.      0.      6.
     -4.     -4.     -4.     -6.     -4.     -5.     -5.     -5.     -2.      1.      2.     -5.      0.      9.
      1.      0.     -1.     -1.     -3.      0.     -1.     -1.      0.     -2.     -3.     -1.     -2.     -5.      6.
      1.      0.      1.      0.      0.     -1.      0.      1.     -1.     -1.     -3.      0.     -2.     -3.      1.      2.
      1.     -1.      0.      0.     -2.     -1.      0.      0.     -1.      0.     -2.      0.     -1.     -3.      0.      1.      3.
     -6.      2.     -4.     -7.     -8.     -5.     -7.     -7.     -3.     -5.     -2.     -3.     -4.      0.     -6.     -2.     -5.     17.
     -3.     -4.     -2.     -4.      0.     -4.     -4.     -5.      0.     -1.     -1.     -4.     -2.      7.     -5.     -3.     -3.      0.     10.
      0.     -2.     -2.     -2.     -2.     -2.     -2.     -1.     -2.      4.      2.     -2.      2.     -1.     -1.     -1.      0.     -6.     -2.      4.
//
H FEND850101
D Structure-Genetic matrix (Feng et al., 1985)
R LIT:1107900 PMID:6100188
A Feng, D.F., Johnson, M.S. and Doolittle, R.F.
T Aligning amino acid sequences: comparison of commonly used methods
J J. Mol. Evol. 21, 112-125 (1985)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      6.
      2.      6.
      3.      2.      6.
      4.      2.      5.      6.
      2.      2.      2.      1.      6.
      3.      3.      3.      4.      1.      6.
      4.      2.      3.      5.      0.      4.      6.
      5.      3.      3.      4.      3.      2.      4.      6.
      2.      4.      4.      3.      2.      4.      2.      1.      6.
      2.      2.      2.      1.      2.      1.      1.      2.      1.      6.
      2.      2.      1.      1.      2.      2.      1.      2.      3.      5.      6.
      3.      5.      4.      3.      0.      4.      4.      2.      3.      2.      2.      6.
      2.      2.      1.      0.      2.      2.      1.      1.      1.      4.      5.      2.      6.
      2.      1.      1.      1.      3.      1.      0.      1.      2.      4.      4.      0.      2.      6.
      5.      3.      2.      2.      2.      3.      3.      3.      3.      2.      3.      2.      2.      2.      6.
      5.      3.      5.      3.      4.      3.      3.      5.      3.      2.      2.      3.      1.      3.      4.      6.
      5.      3.      4.      2.      2.      3.      3.      2.      2.      3.      2.      4.      3.      1.      4.      5.      6.
      2.      2.      0.      0.      3.      1.      1.      3.      1.      2.      4.      1.      3.      3.      2.      2.      1.      6.
      2.      1.      3.      2.      3.      2.      1.      2.      3.      3.      3.      1.      2.      5.      2.      3.      2.      3.      6.
      5.      2.      2.      3.      2.      2.      4.      4.      1.      5.      5.      3.      4.      4.      3.      2.      3.      3.      3.      6.
//
H FITW660101
D Mutation values for the interconversion of amino acid pairs (Fitch, 1966)
R PMID:5917736
A Fitch, W.M.
T An improved method of testing for evolutionary homology
J J. Mol. Biol. 16, 9-16 (1966)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      0.
      2.      0.
      2.      2.      0.
      1.      2.      1.      0.
      2.      1.      2.      2.      0.
      2.      1.      2.      2.      2.      0.
      1.      2.      2.      1.      3.      1.      0.
      1.      1.      2.      1.      1.      2.      1.      0.
      2.      1.      1.      1.      2.      1.      2.      2.      0.
      2.      2.      1.      2.      2.      3.      3.      2.      2.      0.
      2.      1.      2.      2.      2.      1.      2.      1.      1.      1.      0.
      2.      1.      1.      2.      3.      1.      1.      2.      2.      2.      2.      0.
      2.      1.      2.      3.      3.      2.      2.      2.      3.      1.      1.      1.      0.
      2.      2.      2.      2.      1.      2.      3.      2.      2.      1.      1.      3.      2.      0.
      1.      1.      2.      2.      2.      1.      2.      2.      1.      2.      1.      2.      2.      2.      0.
      1.      1.      1.      2.      1.      1.      2.      1.      2.      1.      1.      2.      2.      1.      1.      0.
      1.      1.      1.      2.      2.      2.      2.      2.      2.      1.      2.      1.      1.      2.      1.      1.      0.
      2.      1.      3.      3.      1.      1.      2.      1.      3.      3.      1.      2.      2.      2.      2.      1.      2.      0.
      2.      2.      1.      1.      1.      1.      2.      2.      1.      2.      2.      2.      3.      1.      2.      1.      2.      2.      0.
      1.      2.      2.      1.      1.      2.      1.      1.      2.      1.      1.      2.      1.      1.      2.      2.      2.      2.      2.      0.
//
H GEOD900101
D Hydrophobicity scoring matrix (George et al., 1990)
R PMID:2314281
A George, D.G., Barker, W.C. and Hunt, L.T.
T Mutation data matrix and its uses
J Methods Enzymol. 183, 333-351 (1990)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     10.
      5.     10.
      9.      6.     10.
      5.      9.      6.     10.
      9.      4.      8.      5.     10.
      9.      6.     10.      6.      8.     10.
      5.      9.      6.     10.      5.      6.     10.
      9.      5.     10.      6.      8.     10.      6.     10.
     10.      5.      9.      5.      9.      9.      5.      9.     10.
      8.      3.      7.      3.      9.      7.      3.      7.      8.     10.
      8.      3.      7.      3.      9.      7.      3.      7.      8.     10.     10.
      5.     10.      6.      9.      4.      6.      9.      5.      5.      3.      3.     10.
      9.      3.      8.      4.     10.      8.      4.      8.      9.      9.      9.      3.     10.
      7.      1.      6.      2.      8.      6.      2.      6.      7.      9.      9.      1.      8.     10.
      9.      3.      8.      4.      9.      8.      4.      8.      9.      9.      9.      3.     10.      8.     10.
      9.      6.     10.      7.      8.     10.      7.     10.      9.      7.      7.      6.      8.      6.      7.     10.
     10.      5.      9.      5.      9.      9.      5.      9.     10.      8.      8.      5.      9.      7.      8.      9.     10.
      5.      0.      4.      1.      6.      4.      1.      5.      5.      8.      8.      0.      7.      9.      7.      4.      5.     10.
      7.      2.      6.      3.      8.      6.      3.      6.      7.      9.      9.      2.      8.     10.      9.      6.      7.      8.     10.
      8.      3.      7.      4.      9.      7.      4.      8.      8.     10.     10.      3.     10.      8.     10.      7.      8.      7.      9.     10.
//
H GONG920101
D The mutation matrix for initially aligning (Gonnet et al., 1992)
R LIT:1813110 PMID:1604319
A Gonnet, G.H., Cohen, M.A. and Benner, S.A.
T Exhaustive matching of the entire protein sequence database
J Science 256, 1443-1445 (1992)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     2.4
    -0.6     4.7
    -0.3     0.3     3.8
    -0.3    -0.3     2.2     4.7
     0.5    -2.2    -1.8    -3.2    11.5
    -0.2     1.5     0.7     0.9    -2.4     2.7
     0.0     0.4     0.9     2.7    -3.0     1.7     3.6
     0.5    -1.0     0.4     0.1    -2.0    -1.0    -0.8     6.6
    -0.8     0.6     1.2     0.4    -1.3     1.2     0.4    -1.4     6.0
    -0.8    -2.4    -2.8    -3.8    -1.1    -1.9    -2.7    -4.5    -2.2     4.0
    -1.2    -2.2    -3.0    -4.0    -1.5    -1.6    -2.8    -4.4    -1.9     2.8     4.0
    -0.4     2.7     0.8     0.5    -2.8     1.5     1.2    -1.1     0.6    -2.1    -2.1     3.2
    -0.7    -1.7    -2.2    -3.0    -0.9    -1.0    -2.0    -3.5    -1.3     2.5     2.8    -1.4     4.3
    -2.3    -3.2    -3.1    -4.5    -0.8    -2.6    -3.9    -5.2    -0.1     1.0     2.0    -3.3     1.6     7.0
     0.3    -0.9    -0.9    -0.7    -3.1    -0.2    -0.5    -1.6    -1.1    -2.6    -2.3    -0.6    -2.4    -3.8     7.6
     1.1    -0.2     0.9     0.5     0.1     0.2     0.2     0.4    -0.2    -1.8    -2.1     0.1    -1.4    -2.8     0.4     2.2
     0.6    -0.2     0.5     0.0    -0.5     0.0    -0.1    -1.1    -0.3    -0.6    -1.3     0.1    -0.6    -2.2     0.1     1.5     2.5
    -3.6    -1.6    -3.6    -5.2    -1.0    -2.7    -4.3    -4.0    -0.8    -1.8    -0.7    -3.5    -1.0     3.6    -5.0    -3.3    -3.5    14.2
    -2.2    -1.8    -1.4    -2.8    -0.5    -1.7    -2.7    -4.0     2.2    -0.7     0.0    -2.1    -0.2     5.1    -3.1    -1.9    -1.9     4.1     7.8
     0.1    -2.0    -2.2    -2.9     0.0    -1.5    -1.9    -3.3    -2.0     3.1     1.8    -1.7     1.6     0.1    -1.8    -1.0     0.0    -2.6    -1.1     3.4
//
H GRAR740104
D Chemical distance (Grantham, 1974)
R LIT:2004143 PMID:4843792
A Grantham, R.
T Amino acid difference formula to help explain protein evolution
J Science 185, 862-864 (1974)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      0.
    112.      0.
    111.     86.      0.
    126.     96.     23.      0.
    195.    180.    139.    154.      0.
     91.     43.     46.     61.    154.      0.
    107.     54.     42.     45.    170.     29.      0.
     60.    125.     80.     94.    159.     87.     98.      0.
     86.     29.     68.     81.    174.     24.     40.     98.      0.
     94.     97.    149.    168.    198.    109.    134.    135.     94.      0.
     96.    102.    153.    172.    198.    113.    138.    138.     99.      5.      0.
    106.     26.     94.    101.    202.     53.     56.    127.     32.    102.    107.      0.
     84.     91.    142.    160.    196.    101.    126.    127.     87.     10.     15.     95.      0.
    113.     97.    158.    177.    205.    116.    140.    153.    100.     21.     22.    102.     28.      0.
     27.    103.     91.    108.    169.     76.     93.     42.     77.     95.     98.    103.     87.    114.      0.
     99.    110.     46.     65.    112.     68.     80.     56.     89.    142.    145.    121.    135.    155.     74.      0.
     58.     71.     65.     85.    149.     42.     65.     59.     47.     89.     92.     78.     81.    103.     38.     58.      0.
    148.    101.    174.    181.    215.    130.    152.    184.    115.     61.     61.    110.     67.     40.    147.    177.    128.      0.
    112.     77.    143.    160.    194.     99.    122.    147.     83.     33.     36.     85.     36.     22.    110.    144.     92.     37.      0.
     64.     96.    133.    152.    192.     96.    121.    109.     84.     29.     32.     97.     21.     50.     68.    124.     69.     88.     55.      0.
//
H HENS920101
D BLOSUM45 substitution matrix (Henikoff-Henikoff, 1992)
R LIT:1902106 PMID:1438297
A Henikoff, S. and Henikoff, J.G.
T Amino acid substitution matrices from protein blocks
J Proc. Natl. Acad. Sci. USA 89, 10915-10919 (1992)
* matrix in 1/3 Bit Units
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      5.
     -2.      7.
     -1.      0.      6.
     -2.     -1.      2.      7.
     -1.     -3.     -2.     -3.     12.
     -1.      1.      0.      0.     -3.      6.
     -1.      0.      0.      2.     -3.      2.      6.
      0.     -2.      0.     -1.     -3.     -2.     -2.      7.
     -2.      0.      1.      0.     -3.      1.      0.     -2.     10.
     -1.     -3.     -2.     -4.     -3.     -2.     -3.     -4.     -3.      5.
     -1.     -2.     -3.     -3.     -2.     -2.     -2.     -3.     -2.      2.      5.
     -1.      3.      0.      0.     -3.      1.      1.     -2.     -1.     -3.     -3.      5.
     -1.     -1.     -2.     -3.     -2.      0.     -2.     -2.      0.      2.      2.     -1.      6.
     -2.     -2.     -2.     -4.     -2.     -4.     -3.     -3.     -2.      0.      1.     -3.      0.      8.
     -1.     -2.     -2.     -1.     -4.     -1.      0.     -2.     -2.     -2.     -3.     -1.     -2.     -3.      9.
      1.     -1.      1.      0.     -1.      0.      0.      0.     -1.     -2.     -3.     -1.     -2.     -2.     -1.      4.
      0.     -1.      0.     -1.     -1.     -1.     -1.     -2.     -2.     -1.     -1.     -1.     -1.     -1.     -1.      2.      5.
     -2.     -2.     -4.     -4.     -5.     -2.     -3.     -2.     -3.     -2.     -2.     -2.     -2.      1.     -3.     -4.     -3.     15.
     -2.     -1.     -2.     -2.     -3.     -1.     -2.     -3.      2.      0.      0.     -1.      0.      3.     -3.     -2.     -1.      3.      8.
      0.     -2.     -3.     -3.     -1.     -3.     -3.     -3.     -3.      3.      1.     -2.      1.      0.     -3.     -1.      0.     -3.     -1.      5.
//
H HENS920102
D BLOSUM62 substitution matrix (Henikoff-Henikoff, 1992)
R LIT:1902106 PMID:1438297
A Henikoff, S. and Henikoff, J.G.
T Amino acid substitution matrices from protein blocks
J Proc. Natl. Acad. Sci. USA 89, 10915-10919 (1992)
* matrix in 1/3 Bit Units
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      6.
     -2.      8.
     -2.     -1.      8.
     -3.     -2.      2.      9.
     -1.     -5.     -4.     -5.     13.
     -1.      1.      0.      0.     -4.      8.
     -1.      0.      0.      2.     -5.      3.      7.
      0.     -3.     -1.     -2.     -4.     -3.     -3.      8.
     -2.      0.      1.     -2.     -4.      1.      0.     -3.     11.
     -2.     -4.     -5.     -5.     -2.     -4.     -5.     -6.     -5.      6.
     -2.     -3.     -5.     -5.     -2.     -3.     -4.     -5.     -4.      2.      6.
     -1.      3.      0.     -1.     -5.      2.      1.     -2.     -1.     -4.     -4.      7.
     -1.     -2.     -3.     -5.     -2.     -1.     -3.     -4.     -2.      2.      3.     -2.      8.
     -3.     -4.     -4.     -5.     -4.     -5.     -5.     -5.     -2.      0.      1.     -5.      0.      9.
     -1.     -3.     -3.     -2.     -4.     -2.     -2.     -3.     -3.     -4.     -4.     -2.     -4.     -5.     11.
      2.     -1.      1.      0.     -1.      0.      0.      0.     -1.     -4.     -4.      0.     -2.     -4.     -1.      6.
      0.     -2.      0.     -2.     -1.     -1.     -1.     -2.     -3.     -1.     -2.     -1.     -1.     -3.     -2.      2.      7.
     -4.     -4.     -6.     -6.     -3.     -3.     -4.     -4.     -4.     -4.     -2.     -4.     -2.      1.     -5.     -4.     -4.     16.
     -3.     -3.     -3.     -5.     -4.     -2.     -3.     -5.      3.     -2.     -2.     -3.     -1.      4.     -4.     -3.     -2.      3.     10.
      0.     -4.     -4.     -5.     -1.     -3.     -4.     -5.     -5.      4.      1.     -3.      1.     -1.     -4.     -2.      0.     -4.     -2.      6.
//
H HENS920103
D BLOSUM80 substitution matrix (Henikoff-Henikoff, 1992)
R LIT:1902106 PMID:1438297
A Henikoff, S. and Henikoff, J.G.
T Amino acid substitution matrices from protein blocks
J Proc. Natl. Acad. Sci. USA 89, 10915-10919 (1992)
* matrix in 1/3 Bit Units
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      7.
     -3.      9.
     -3.     -1.      9.
     -3.     -3.      2.     10.
     -1.     -6.     -5.     -7.     13.
     -2.      1.      0.     -1.     -5.      9.
     -2.     -1.     -1.      2.     -7.      3.      8.
      0.     -4.     -1.     -3.     -6.     -4.     -4.      9.
     -3.      0.      1.     -2.     -7.      1.      0.     -4.     12.
     -3.     -5.     -6.     -7.     -2.     -5.     -6.     -7.     -6.      7.
     -3.     -4.     -6.     -7.     -3.     -4.     -6.     -7.     -5.      2.      6.
     -1.      3.      0.     -2.     -6.      2.      1.     -3.     -1.     -5.     -4.      8.
     -2.     -3.     -4.     -6.     -3.     -1.     -4.     -5.     -4.      2.      3.     -3.      9.
     -4.     -5.     -6.     -6.     -4.     -5.     -6.     -6.     -2.     -1.      0.     -5.      0.     10.
     -1.     -3.     -4.     -3.     -6.     -3.     -2.     -5.     -4.     -5.     -5.     -2.     -4.     -6.     12.
      2.     -2.      1.     -1.     -2.     -1.     -1.     -1.     -2.     -4.     -4.     -1.     -3.     -4.     -2.      7.
      0.     -2.      0.     -2.     -2.     -1.     -2.     -3.     -3.     -2.     -3.     -1.     -1.     -4.     -3.      2.      8.
     -5.     -5.     -7.     -8.     -5.     -4.     -6.     -6.     -4.     -5.     -4.     -6.     -3.      0.     -7.     -6.     -5.     16.
     -4.     -4.     -4.     -6.     -5.     -3.     -5.     -6.      3.     -3.     -2.     -4.     -3.      4.     -6.     -3.     -3.      3.     11.
     -1.     -4.     -5.     -6.     -2.     -4.     -4.     -6.     -5.      4.      1.     -4.      1.     -2.     -4.     -3.      0.     -5.     -3.      7.
//
H JOHM930101
D Structure-based amino acid scoring table (Johnson-Overington, 1993)
R LIT:1923112 PMID:8411177
A Johnson, M.S. and Overington, J.P.
T A structural basis for sequence comparisons
  An evaluation of scoring methodologies
J J. Mol. Biol. 233, 716-738 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     6.0
    -1.6    10.0
    -1.4    -1.5     8.0
    -1.6    -3.4     2.6     8.5
    -3.4    -5.6    -7.6    -9.7    16.1
    -0.6     2.1    -0.8    -1.1    -6.9     9.0
    -0.7    -0.2    -0.7     2.4    -6.9     2.4     8.6
    -0.5    -2.8    -1.4    -2.1    -8.2    -2.8    -2.5     8.0
    -3.1     0.1     1.7    -0.7    -8.2     1.4    -2.3    -3.2    12.7
    -2.2    -5.4    -4.7    -4.8    -7.7    -7.0    -4.8    -5.5    -5.1     8.1
    -3.3    -3.7    -4.8    -8.0    -8.7    -4.4    -5.6    -7.2    -4.2     2.6     7.3
    -0.9     3.2     0.1    -1.5    -8.7     1.1     1.1    -3.5     0.1    -4.7    -3.4     7.6
    -1.5    -4.2    -3.7    -5.9    -4.4    -0.6    -2.8    -5.2    -2.3     2.6     4.4    -1.9    11.2
    -3.2    -6.0    -3.8    -7.0    -4.4    -6.4    -6.4    -8.6    -1.7     0.5     1.8    -5.6    -0.6    10.4
    -1.0    -3.6    -2.4    -1.0    -8.9    -3.6    -1.5    -2.5    -4.3    -5.7    -2.8    -0.6    -9.8    -5.0    10.3
     0.0    -0.6     1.0    -0.2    -7.7    -1.2    -2.2    -1.3    -2.6    -4.7    -5.2    -1.5    -4.8    -4.8    -1.0     5.8
    -0.8    -1.4     0.1    -1.8    -6.0    -0.4    -0.5    -3.8    -3.0    -3.2    -4.6    -0.2    -3.2    -5.0    -2.0     2.0     6.8
    -5.8    -3.8    -6.1    -6.0    -9.1    -8.2    -7.6    -6.3    -4.0    -3.3    -1.0    -5.4    -0.9     3.4    -7.4    -6.2    -9.3    15.2
    -4.0    -2.1    -1.3    -3.8    -7.7    -5.1    -3.7    -5.4    -0.4    -2.5    -2.4    -3.7    -1.3     3.4    -7.0    -3.4    -2.7     2.3    10.5
    -0.5    -4.9    -5.7    -5.2    -4.8    -3.6    -4.2    -5.6    -3.9     3.9     1.8    -3.7     0.7    -1.3    -5.2    -4.3    -1.9    -4.9    -1.8     7.0
//
H JOND920103
D The 250 PAM PET91 matrix (Jones et al., 1992)
R LIT:1814076 PMID:1633570
A Jones, D.T., Taylor, W.R. and Thornton, J.M.
T The rapid generation of mutation data matrices from protein sequences
J CABIOS 8, 275-282 (1992)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      2.
     -1.      5.
      0.      0.      3.
      0.     -1.      2.      5.
     -1.     -1.     -1.     -3.     11.
     -1.      2.      0.      1.     -3.      5.
     -1.      0.      1.      4.     -4.      2.      5.
      1.      0.      0.      1.     -1.     -1.      0.      5.
     -2.      2.      1.      0.      0.      2.      0.     -2.      6.
      0.     -3.     -2.     -3.     -2.     -3.     -3.     -3.     -3.      4.
     -1.     -3.     -3.     -4.     -3.     -2.     -4.     -4.     -2.      2.      5.
     -1.      4.      1.      0.     -3.      2.      1.     -1.      1.     -3.     -3.      5.
     -1.     -2.     -2.     -3.     -2.     -2.     -3.     -3.     -2.      3.      3.     -2.      6.
     -3.     -4.     -3.     -5.      0.     -4.     -5.     -5.      0.      0.      2.     -5.      0.      8.
      1.     -1.     -1.     -2.     -2.      0.     -2.     -1.      0.     -2.      0.     -2.     -2.     -3.      6.
      1.     -1.      1.      0.      1.     -1.     -1.      1.     -1.     -1.     -2.     -1.     -1.     -2.      1.      2.
      2.     -1.      1.     -1.     -1.     -1.     -1.     -1.     -1.      1.     -1.     -1.      0.     -2.      1.      1.      2.
     -4.      0.     -5.     -5.      1.     -3.     -5.     -2.     -3.     -4.     -2.     -3.     -3.     -1.     -4.     -3.     -4.     15.
     -3.     -2.     -1.     -2.      2.     -2.     -4.     -4.      4.     -2.     -1.     -3.     -2.      5.     -3.     -1.     -3.      0.      9.
      1.     -3.     -2.     -2.     -2.     -3.     -2.     -2.     -3.      4.      2.     -3.      2.      0.     -1.     -1.      0.     -3.     -3.      4.
//
H JOND940101
D The 250 PAM transmembrane protein exchange matrix (Jones et al., 1994)
R LIT:2006072 PMID:8112466
A Jones, D.T., Taylor, W.R. and Thornton, J.M.
T A mutation data matrix for transmembrane proteins
J FEBS Lett. 339, 269-275 (1994)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      2.
     -1.      7.
     -1.      2.     11.
      0.      1.      6.     12.
      0.     -1.     -1.     -3.      6.
     -2.      6.      3.      2.     -3.     11.
      0.      2.      1.      8.     -3.      7.     13.
      1.      0.     -2.      3.     -1.     -1.      3.      6.
     -3.      5.      3.      3.     -1.      7.      2.     -3.     11.
      0.     -3.     -3.     -3.     -1.     -4.     -4.     -2.     -4.      2.
     -2.     -3.     -4.     -5.     -1.     -2.     -5.     -4.     -4.      1.      3.
     -2.      9.      5.      3.     -3.      6.      1.     -1.      4.     -4.     -4.     12.
     -1.      0.     -2.     -3.     -1.     -2.     -3.     -3.     -3.      1.      1.     -1.      3.
     -2.     -4.     -4.     -6.      1.     -4.     -6.     -4.     -3.     -1.      1.     -5.      0.      5.
      0.     -3.     -2.     -2.     -4.      0.     -3.     -2.     -4.     -3.     -1.     -4.     -3.     -4.     11.
      2.     -1.      2.      0.      1.     -1.      0.      1.     -2.     -1.     -2.     -1.     -2.     -1.     -1.      3.
      1.     -1.      1.      0.      0.     -2.     -1.      0.     -2.      0.     -1.     -2.      0.     -2.     -1.      2.      3.
     -4.      5.     -3.     -4.      1.      0.     -3.     -2.     -1.     -3.     -2.      3.     -2.     -3.     -6.     -3.     -4.     12.
     -3.     -1.     -1.     -2.      3.      0.     -5.     -5.      6.     -4.     -3.      1.     -3.      2.     -5.      0.     -3.     -2.     10.
      0.     -2.     -3.     -3.      0.     -4.     -2.     -1.     -4.      2.      0.     -4.      1.     -1.     -3.     -1.      0.     -2.     -4.      2.
//
H KOLA920101
D Conformational similarity weight matrix (Kolaskar-Kulkarni-Kale, 1992)
R LIT:1806109 PMID:1538389
A Kolaskar, A.S. and Kulkarni-Kale, U.
T Sequence alignment approach to pick up conformationally similar
  protein fragments
J J. Mol. Biol. 223, 1053-1061 (1992)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     10.
     6.6     10.
      0.      0.     10.
      0.      0.      9.     10.
      0.      0.      0.      0.     10.
     6.6      9.      0.      0.      0.     10.
      9.     6.6      0.      0.      0.     6.6     10.
      0.      0.      0.      0.      0.      0.      0.     10.
      0.      5.      5.     6.6      9.      5.      0.      0.     10.
      0.      0.      0.      0.      0.      0.      0.      0.      0.     10.
      5.     6.6      0.      0.      0.      9.      5.      0.      0.      0.     10.
     6.6      9.      0.      5.      0.      9.      9.      0.      0.      0.      9.     10.
      5.      9.      0.      0.      0.      5.      0.      0.      0.      0.     6.6      5.     10.
      0.      9.      0.      0.      5.     6.6      0.      0.      5.      0.      5.      5.     6.6     10.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.     10.
      0.      5.     6.6     6.6      9.      0.      0.      0.      9.      0.      0.      5.      0.      5.      0.     10.
      0.      5.      0.      0.     6.6      5.      0.      0.      5.      0.      0.      5.      0.      5.      0.     6.6     10.
      0.     6.6      0.      0.      5.      5.      0.      0.      5.      0.      5.      0.     6.6      9.      0.      5.      5.     10.
      0.      5.      0.      0.      5.      5.      0.      0.     6.6      0.      0.      0.      0.      9.      0.     6.6      9.      5.     10.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      9.      0.      0.      0.      0.      0.      0.      0.      0.      0.     10.
//
H LEVJ860101
D The secondary structure similarity matrix (Levin et al., 1986)
R LIT:1210126 PMID:3743779
A Levin, J.M., Robson, B. and Garnier, J.
T An algorithm for secondary structure determination in proteins based on
  sequence similarity
J FEBS Lett. 205, 303-308 (1986)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      2.
      0.      2.
      0.      0.      3.
      0.      0.      1.      2.
      0.      0.      0.      0.      2.
      0.      0.      1.      0.      0.      2.
      1.      0.      0.      1.      0.      1.      2.
      0.      0.      0.      0.      0.      0.      0.      2.
      0.      0.      0.      0.      0.      0.      0.      0.      2.
      0.     -1.     -1.     -1.      0.     -1.     -1.     -1.     -1.      2.
      0.     -1.     -1.     -1.      0.     -1.     -1.     -1.     -1.      0.      2.
      0.      1.      1.      0.      0.      0.      0.      0.      0.     -1.     -1.      2.
      0.     -1.     -1.     -1.      0.     -1.     -1.     -1.     -1.      0.      2.     -1.      2.
     -1.     -1.     -1.     -1.     -1.     -1.     -1.     -1.     -1.      1.      0.     -1.      0.      2.
     -1.      0.      0.      0.      0.      0.     -1.      0.      0.     -1.     -1.      0.     -1.     -1.      3.
      1.      0.      0.      0.      0.      0.      0.      0.      0.     -1.     -1.      0.     -1.     -1.      0.      2.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.      0.     -1.      0.      0.      2.
     -1.      0.     -1.     -1.     -1.     -1.     -1.     -1.     -1.      0.      0.     -1.      0.      0.     -1.     -1.     -1.      2.
     -1.     -1.     -1.     -1.     -1.     -1.     -1.     -1.      0.      0.      0.     -1.      0.      1.     -1.     -1.     -1.      0.      2.
      0.     -1.     -1.     -1.      0.     -1.     -1.     -1.     -1.      1.      1.     -1.      0.      0.     -1.     -1.      0.      0.      0.      2.
//
H LUTR910101
D Structure-based comparison table for outside other class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     11.
      0.     32.
      2.      2.     11.
      1.     -2.      4.     29.
     -5.     -6.     -7.    -13.    109.
      2.      6.      3.      2.    -10.     16.
      3.      2.      2.      6.    -12.      5.     15.
     -5.     -7.     -4.     -7.    -15.     -8.     -6.     39.
     -4.     -1.      2.     -5.    -23.      2.     -3.    -13.     54.
      1.     -4.     -3.     -7.    -13.     -3.     -3.    -16.    -10.     50.
      1.     -4.     -4.    -10.     -1.     -2.     -4.    -17.     -6.     19.     45.
     -1.      6.     -1.     -2.    -16.      5.      3.    -15.     -8.    -10.    -11.     39.
      1.      0.     -1.     -7.     -3.      0.     -4.    -11.     -3.     20.     24.     -8.     40.
    -13.    -14.    -11.    -15.    -12.    -15.    -18.    -24.     -6.      7.     11.    -26.     13.     85.
      1.     -9.     -8.     -9.    -28.     -6.     -3.    -19.    -12.    -11.    -10.     -9.    -11.    -24.     55.
      4.      1.      3.      2.    -10.      2.      2.     -6.     -4.     -5.     -5.     -1.     -4.    -14.     -3.     17.
      3.     -1.      2.     -2.     -7.      1.      1.    -12.     -5.      0.     -4.     -3.     -2.    -13.     -6.      4.     30.
     -6.      3.     -6.    -10.     -3.    -13.    -14.    -12.     -3.      1.      1.    -19.      9.     10.    -11.     -7.    -14.    124.
     -6.     -3.     -4.    -10.      3.     -9.    -10.    -16.      2.     -3.      2.    -16.      4.     22.    -17.     -6.     -9.     29.     64.
      3.     -3.     -3.     -7.     -7.     -2.     -2.    -12.     -9.     24.     13.     -9.     14.      0.     -8.     -4.     -1.     -1.     -2.     39.
//
H LUTR910102
D Structure-based comparison table for inside other class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     12.
      5.      9.
      5.      5.      6.
      6.      8.      8.     17.
      1.    -10.    -11.    -14.     93.
      6.      6.      6.      8.     -5.      7.
      7.      8.      8.     12.    -16.      9.     15.
      5.     -2.      5.      6.    -36.      3.      8.     52.
     -2.      5.      6.      5.    -20.      4.     -3.    -14.     65.
     -1.     -4.     -3.     -6.    -17.     -4.     -5.    -20.    -10.     31.
    -10.    -10.    -10.    -16.    -35.    -12.    -14.    -32.    -18.      9.     37.
      6.     10.     10.     13.    -22.     10.     13.      2.      6.     -5.    -15.     31.
     -6.     -6.     -8.    -13.    -17.     -5.    -12.    -32.     -5.     18.     13.    -11.     61.
    -24.    -11.    -19.    -25.    -36.    -20.    -30.    -52.    -10.     -4.      2.    -30.      2.     67.
     -5.    -12.    -11.     -7.    -30.     -7.     -7.    -11.    -23.    -28.    -36.     -5.    -25.    -28.     83.
      9.      6.      8.      8.    -11.      8.      9.      7.     -1.    -11.    -25.      8.    -18.    -37.     -9.     36.
      8.      6.      6.      8.      1.      8.     10.      0.     -5.     -1.    -18.      6.     -9.    -37.    -14.     10.     35.
    -20.      2.     -6.    -16.      0.     -2.    -18.    -23.    -21.    -19.    -18.    -21.    -20.     11.    -47.    -29.    -29.    129.
     -4.      3.      0.      0.     -7.      0.     -3.    -16.      5.      0.     -2.     -1.      1.     21.    -20.     -6.     -8.     44.     26.
      0.     -3.     -3.     -4.    -12.     -3.     -4.    -20.     -6.     17.      8.     -4.     12.     -9.    -20.    -10.     -2.     -8.     -2.     26.
//
H LUTR910103
D Structure-based comparison table for outside alpha class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     24.
     -2.     18.
     -1.      2.     16.
     -2.      0.      4.     23.
      2.      2.      1.     -1.      9.
     -1.      2.      2.      3.      2.     13.
     -2.     -1.      1.      6.     -3.      3.     24.
      1.      2.      4.      2.      4.      2.      1.     29.
     -5.      0.      3.      1.      0.      2.     -1.      0.     43.
     -5.     -3.     -6.     -9.      4.     -4.    -10.     -5.     -4.     41.
    -18.     -7.    -12.    -18.     -3.    -13.    -16.    -15.    -12.     13.     54.
    -10.      5.     -2.     -4.     -4.     -1.     -4.     -4.     -6.    -11.    -21.     32.
     -3.      0.     -5.     -7.      4.      0.     -5.     -5.     -5.     17.     13.     -7.     44.
    -20.    -18.    -18.    -18.      4.    -13.    -24.    -21.     -9.     10.     12.    -30.     13.     99.
     -2.     -2.     -2.      1.     -1.      1.     -1.      0.     -7.     -8.    -24.     -8.    -10.    -32.     67.
      1.      2.      4.      3.      5.      2.      1.      5.      0.     -4.    -12.     -3.     -3.    -18.      1.     17.
      1.      2.      3.      1.      4.      2.      0.      3.      1.      3.     -6.     -3.      2.    -16.     -3.      4.     16.
    -20.     -8.    -18.    -12.     16.     -3.    -16.    -21.      7.    -14.     -3.    -31.    -14.     36.    -29.    -19.     -2.    170.
    -21.    -10.    -10.    -14.     -7.    -12.    -21.    -14.     -1.    -14.    -13.    -25.    -19.     40.    -17.    -16.    -15.     47.    105.
     -5.     -3.     -6.     -4.      5.     -5.     -6.     -5.     -8.     18.     -1.    -11.      7.    -11.     -6.     -2.      3.     -9.    -18.     44.
//
H LUTR910104
D Structure-based comparison table for inside alpha class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     22.
     -2.     38.
      4.      5.      4.
     -1.      5.     11.     71.
      8.     -1.      4.    -13.     50.
      2.      9.      4.     10.      0.      6.
      4.     12.      5.     20.     -2.      7.     12.
      5.      0.      7.      0.      3.      5.      8.     53.
    -30.      4.     -3.      7.    -30.     13.     -3.    -32.     95.
     -2.     -1.      0.    -13.      3.      0.     -2.     -6.    -17.     17.
    -14.     -3.     -6.    -20.    -11.     -7.    -10.    -21.    -10.      0.     25.
      1.     22.      6.      9.     -2.      9.     14.      2.     -9.     -1.     -8.     33.
     -2.      2.      0.    -11.      0.     -1.     -3.     -6.     -8.      3.      2.     -3.     17.
    -18.    -14.    -15.    -26.    -12.    -14.    -21.    -25.     -7.     -4.     -4.    -23.      1.     58.
      5.      2.      2.      5.      2.      2.      4.      6.    -14.      1.     -7.      3.     -1.     -8.      4.
      9.      4.      4.      3.     10.      4.      5.      7.    -19.      1.    -10.      5.      0.    -14.      9.     23.
      6.      3.      3.      1.      8.      3.      4.      4.    -16.      2.     -6.      5.      1.    -13.      4.      9.     10.
    -50.    -35.    -34.    -55.    -45.    -15.    -40.    -57.    -41.    -27.    -30.    -23.    -12.      4.    -33.    -45.    -39.    130.
    -15.     -3.     -4.     -8.     -8.      0.     -8.    -17.     23.     -4.     -5.    -13.     -2.     25.     -3.    -10.     -9.     31.     68.
     -1.     -3.     -1.    -15.      1.     -2.     -3.    -10.    -27.      5.     -6.     -4.      3.     -9.      0.     -1.      2.    -23.    -14.     21.
//
H LUTR910105
D Structure-based comparison table for outside beta class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     27.
     -3.     32.
     -2.      0.     18.
     -4.      0.      9.     38.
    -22.    -28.      6.    -26.    156.
     -3.      2.      1.      3.    -29.     30.
     -3.     -1.      0.     10.    -30.      6.     25.
      9.      6.     -4.      3.    -33.      3.      4.     59.
    -11.     -7.     14.     12.    -33.      4.     -5.     -4.     84.
     -2.     -2.     -8.    -10.    -26.     -7.     -7.     -8.    -13.     29.
     -7.     -8.    -11.    -21.    -34.    -13.    -13.    -21.     -9.     16.     42.
     -6.      9.     -1.     -2.    -32.      4.      2.     -1.    -19.     -9.    -14.     30.
      2.      2.     -3.     -7.    -17.     -5.     -5.     -2.    -11.     10.     12.     -5.      7.
     -4.     -9.     -8.    -17.     12.     -9.    -12.    -10.     -3.      7.      6.    -11.      2.     47.
      6.     -1.      5.     -2.    -22.      1.    -10.    -10.     -9.      8.      3.    -12.      6.      2.     56.
      5.     -4.      0.      0.      6.     -6.     -3.      0.    -11.    -10.    -15.     -4.     -2.     -9.     -4.     25.
      3.      2.     -4.     -1.     -7.      2.      0.     -1.    -19.     -3.    -12.     -1.      2.     -8.     -2.      4.     20.
     -2.    -31.    -30.    -40.    -34.    -34.    -35.    -33.    -36.    -25.    -29.    -14.    -21.     32.    -25.    -13.    -31.    150.
    -10.    -13.     -2.    -13.    -25.    -14.    -13.    -14.     18.    -10.     -1.    -14.     -4.     24.      3.     -7.    -16.     11.     56.
     -2.     -4.     -9.    -13.    -11.     -8.     -8.    -14.    -19.     11.      8.     -8.      7.     -3.      1.     -7.     -1.    -15.    -13.     24.
//
H LUTR910106
D Structure-based comparison table for inside beta class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     18.
      1.     60.
      6.     10.     18.
      4.     -1.     18.     80.
      0.     -7.      5.      0.     66.
      6.     24.     18.     18.      7.     42.
      8.     -1.     22.     29.     -1.     15.     59.
     14.     -8.      6.     -4.    -10.      4.     13.     48.
      2.     11.     13.     24.     -2.     13.     16.     -3.     18.
     -8.    -14.    -14.    -22.    -29.    -14.    -18.     -9.    -15.     20.
     -6.    -12.    -15.    -27.    -29.     -9.    -21.     -9.    -15.     11.     25.
      4.     22.     16.     30.      2.     22.     10.     -2.     14.    -13.    -11.     35.
      1.      3.      3.      5.    -23.      4.      5.      4.      3.      3.      2.      6.     35.
    -12.    -10.     -6.    -24.    -40.    -16.     -7.    -17.      6.    -10.     -4.    -14.     -2.     58.
      4.    -20.    -13.    -26.     -8.    -17.    -19.    -14.    -15.     -9.     -3.    -16.    -16.     -9.     95.
     12.      3.     13.     17.     -1.     10.     13.     16.     10.    -12.    -15.     11.     -2.    -16.     -4.     28.
      6.     10.      8.      2.    -11.      4.      9.      8.      5.     -7.    -11.      7.      3.    -17.     -1.     12.     24.
    -23.     16.    -11.    -24.    -43.    -14.    -19.    -32.     18.     -8.     -8.    -11.    -15.      3.    -32.    -21.     -7.    115.
      0.      7.     13.      7.     -9.      9.     14.     -9.     20.    -16.    -12.     11.      2.     16.     -7.      3.      1.     15.     37.
     -7.    -11.    -17.    -30.    -28.    -15.    -24.     -9.    -19.     11.      9.    -12.     -5.    -13.     -9.    -14.     -7.    -15.    -18.     21.
//
H LUTR910107
D Structure-based comparison table for other class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     11.
      1.     28.
      2.      3.     10.
      2.      1.      5.     27.
     -5.     -9.     -9.    -15.    108.
      3.      7.      4.      4.    -11.     14.
      3.      3.      3.      8.    -15.      6.     15.
     -4.     -6.     -2.     -5.    -21.     -6.     -4.     41.
     -3.      0.      2.     -3.    -23.      2.     -2.    -12.     55.
     -1.     -6.     -4.     -9.    -13.     -4.     -5.    -18.    -12.     49.
     -3.     -7.     -7.    -14.    -10.     -6.     -8.    -22.    -10.     19.     48.
      1.      7.      2.      1.    -19.      6.      5.    -12.     -6.    -11.    -15.     38.
     -1.     -2.     -3.     -9.     -7.     -2.     -7.    -15.     -4.     22.     24.    -10.     52.
    -16.    -15.    -14.    -20.    -19.    -18.    -22.    -30.     -9.      5.     10.    -29.     11.     83.
      0.     -8.     -7.     -8.    -30.     -6.     -3.    -17.    -12.    -15.    -16.     -8.    -15.    -26.     58.
      4.      2.      4.      3.    -11.      3.      3.     -4.     -3.     -8.    -10.      1.     -7.    -19.     -3.     19.
      3.      0.      3.     -1.     -6.      2.      2.    -10.     -5.     -1.     -9.     -2.     -4.    -19.     -7.      5.     31.
     -9.      2.     -7.    -13.     -1.    -13.    -17.    -15.     -7.     -5.     -5.    -21.      4.     10.    -16.    -11.    -18.    129.
     -5.     -1.     -2.     -7.      0.     -6.     -9.    -16.      3.     -2.      0.    -12.      3.     22.    -16.     -5.     -9.     35.     59.
      2.     -4.     -4.     -7.     -8.     -3.     -3.    -14.     -9.     24.     14.     -9.     15.     -2.    -11.     -6.     -2.     -3.     -3.     37.
//
H LUTR910108
D Structure-based comparison table for alpha helix class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     23.
     -1.     19.
      1.      5.     13.
      0.      3.      7.     28.
      4.      1.      1.     -4.     51.
      1.      5.      5.      6.      1.     11.
      0.      4.      5.     10.     -5.      7.     23.
      2.      3.      6.      4.      4.      3.      3.     37.
     -6.      2.      5.      3.     -5.      4.      1.     -1.     52.
     -6.     -6.     -7.    -12.      5.     -6.    -10.     -8.     -9.     38.
    -19.    -10.    -14.    -21.     -8.    -14.    -18.    -19.    -14.      7.     45.
     -6.      9.      3.      2.     -6.      4.      3.     -1.     -2.    -12.    -21.     34.
     -4.     -2.     -5.     -9.      3.     -2.     -7.     -6.     -7.     12.      8.     -8.     40.
    -23.    -22.    -22.    -24.     -4.    -19.    -28.    -26.    -13.      3.      4.    -34.      8.     88.
      1.      2.      3.      5.     -2.      5.      6.      3.     -4.     -7.    -21.     -1.     -8.    -28.     59.
      3.      4.      5.      5.      7.      4.      4.      6.      0.     -5.    -15.      1.     -4.    -21.      6.     17.
      2.      2.      4.      2.      6.      3.      2.      4.      0.      1.     -9.      0.      0.    -19.      1.      5.     14.
    -43.    -29.    -38.    -35.    -13.    -19.    -38.    -46.    -17.    -25.    -22.    -43.    -11.     19.    -46.    -41.    -25.    162.
    -19.     -8.     -7.    -12.     -8.     -8.    -16.    -14.      4.    -11.    -12.    -20.    -12.     33.    -10.    -14.    -13.     36.     97.
     -6.     -6.     -8.     -9.      3.     -7.     -8.     -9.    -14.     13.     -4.    -13.      6.     -9.     -7.     -4.      1.    -18.    -19.     40.
//
H LUTR910109
D Structure-based comparison table for beta strand class (Luthy et al., 1991)
R LIT:1712085 PMID:1881879
A Luthy, R., McLachlan, A.D. and Eisenberg, D.
T Secondary structure-based profiles: Use of structure-conserving scoring
  tables in searching protein sequence databases for structural similarities
J Proteins 10, 229-239 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     23.
     -2.     40.
      1.      4.     15.
     -1.      2.     13.     49.
     -5.    -19.     -5.    -16.     97.
      0.      9.      7.      9.    -11.     31.
      0.      2.      8.     17.    -21.     11.     31.
     12.      2.      0.      1.    -18.      4.      6.     54.
     -4.      2.     13.     17.    -12.      8.      5.     -5.     55.
     -7.     -9.    -12.    -17.    -30.    -13.    -13.    -11.    -15.     28.
     -7.    -10.    -13.    -22.    -34.    -12.    -14.    -15.    -13.     13.     34.
     -3.     14.      7.      8.    -23.     12.     10.      0.     -1.    -14.    -13.     34.
      1.      2.     -2.     -5.    -28.     -3.     -3.      2.     -3.      8.      8.     -4.     25.
     -9.    -11.     -9.    -21.    -31.    -12.    -13.    -15.      3.     -3.      1.    -14.     -1.     57.
      5.     -6.      2.     -7.    -12.     -2.    -13.    -13.    -10.     -1.     -1.    -14.      0.     -4.     78.
      7.      1.      6.      8.    -10.      2.      5.      8.      3.    -13.    -15.      4.     -3.    -14.     -4.     26.
      4.      6.      2.      2.    -18.      4.      4.      3.     -4.     -7.    -12.      4.      2.    -13.     -3.      8.     21.
    -17.     -5.    -22.    -32.    -53.    -26.    -29.    -33.      7.    -12.    -15.    -15.    -20.     16.    -28.    -19.    -20.    133.
     -5.     -5.      4.     -5.    -19.     -4.     -3.    -13.     21.    -15.     -7.     -5.     -3.     20.     -1.     -3.     -8.     13.     47.
     -5.     -7.    -12.    -18.    -27.    -11.    -12.    -12.    -18.     11.      8.    -10.      2.     -9.     -4.    -10.     -4.    -17.    -15.     23.
//
H MCLA710101
D The similarity of pairs of amino acids (McLachlan, 1971)
R PMID:5167087
A McLachlan, A.D.
T Tests for comparing related amino-acid sequences
  cytochrome c and cytochrome c551
J J. Mol. Biol. 61, 409-424 (1971)
* (RR 9.)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      8.
      2.      8.
      3.      3.      8.
      3.      1.      5.      8.
      1.      1.      1.      1.      9.
      3.      5.      4.      4.      0.      8.
      4.      3.      4.      5.      0.      5.      8.
      3.      3.      3.      3.      1.      2.      3.      8.
      3.      5.      4.      4.      3.      4.      2.      2.      8.
      2.      1.      1.      0.      1.      0.      1.      1.      2.      8.
      2.      2.      1.      1.      0.      3.      1.      1.      2.      5.      8.
      3.      5.      4.      3.      0.      4.      4.      3.      4.      1.      2.      8.
      3.      1.      2.      2.      3.      3.      1.      1.      3.      5.      6.      1.      8.
      1.      1.      0.      1.      0.      0.      0.      0.      4.      3.      5.      0.      5.      9.
      4.      3.      1.      3.      0.      3.      4.      3.      3.      1.      1.      3.      1.      1.      8.
      4.      4.      5.      3.      2.      4.      4.      3.      3.      2.      2.      3.      2.      2.      3.      8.
      3.      3.      3.      3.      2.      3.      4.      2.      4.      3.      3.      3.      3.      1.      3.      5.      8.
      1.      3.      0.      0.      2.      2.      1.      1.      3.      3.      3.      1.      1.      6.      0.      3.      2.      9.
      1.      2.      2.      1.      1.      1.      2.      0.      4.      3.      3.      1.      2.      6.      0.      3.      1.      6.      9.
      3.      2.      1.      1.      1.      2.      2.      2.      2.      5.      5.      2.      4.      3.      2.      2.      3.      2.      3.      8.
//
H MCLA720101
D Chemical similarity scores (McLachlan, 1972)
R PMID:5023183
A McLachlan, A.D.
T Repeating sequences and gene duplication in proteins
J J. Mol. Biol. 64, 417-437 (1972)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      5.
      0.      6.
      0.      0.      5.
      0.      0.      3.      5.
      0.      0.      0.      0.      6.
      0.      0.      2.      1.      0.      5.
      0.      0.      1.      2.      0.      3.      5.
      3.      0.      0.      0.      0.      0.      0.      6.
      0.      0.      1.      0.      0.      2.      0.      0.      6.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      5.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      3.      5.
      0.      3.      0.      0.      0.      1.      0.      0.      0.      0.      0.      5.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      3.      3.      0.      6.
      0.      0.      0.      0.      0.      0.      0.      0.      2.      1.      2.      0.      2.      6.
      1.      0.      0.      0.      0.      0.      0.      0.      0.      0.      1.      0.      0.      0.      5.
      1.      0.      1.      0.      2.      1.      0.      0.      0.      0.      0.      0.      0.      0.      0.      5.
      1.      0.      1.      0.      0.      0.      0.      0.      0.      1.      0.      0.      0.      0.      1.      3.      5.
      0.      0.      0.      0.      0.      0.      0.      0.      1.      1.      1.      0.      1.      3.      0.      0.      0.      6.
      0.      0.      0.      0.      0.      0.      0.      0.      2.      1.      1.      0.      1.      3.      0.      0.      0.      2.      6.
      0.      0.      0.      0.      0.      0.      0.      0.      0.      2.      1.      0.      1.      1.      1.      0.      0.      0.      0.      5.
//
H MIYS930101
D Base-substitution-protein-stability matrix (Miyazawa-Jernigan, 1993)
R LIT:1913158 PMID:8506261
A Miyazawa, S. and Jernigan, R.L.
T A new substitution matrix for protein sequence searches based on
  contact frequencies in protein structures
J Protein Engineering 6, 267-278 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    0.34
   -0.08    0.65
   -0.16    0.01    0.38
    0.04   -0.06    0.20    0.36
   -0.51   -0.35   -0.46   -0.41    1.02
   -0.16    0.15    0.20    0.16   -0.74    0.48
    0.03   -0.02    0.19    0.32   -0.64    0.25    0.36
    0.19    0.20   -0.11    0.15   -0.18   -0.14    0.13    0.43
   -0.21    0.11    0.21    0.18   -0.29    0.37    0.13   -0.19    0.54
   -0.45   -0.82   -0.83   -0.78   -0.13   -0.95   -0.86   -0.58   -0.69    0.75
   -0.45   -0.74   -0.90   -0.75   -0.02   -0.74   -0.80   -0.56   -0.50    0.48    0.61
   -0.20    0.04    0.38    0.16   -0.81    0.30    0.25   -0.16    0.14   -1.01   -1.06    0.49
   -0.47   -0.83   -0.97   -0.90   -0.29   -0.97   -0.87   -0.61   -0.86    0.67    0.50   -1.03    0.97
   -0.47   -0.79   -0.71   -0.62    0.39   -0.85   -0.81   -0.52   -0.43    0.45    0.48   -1.03    0.35    0.61
    0.17    0.14   -0.12   -0.15   -0.65    0.15   -0.13   -0.14    0.14   -0.78   -0.67   -0.14   -0.82   -0.76    0.56
    0.16    0.05   -0.02   -0.14   -0.20   -0.20   -0.19    0.00   -0.15   -0.68   -0.70   -0.14   -0.75   -0.53    0.24    0.48
    0.18    0.00    0.11   -0.10   -0.62   -0.07   -0.09   -0.09   -0.13   -0.59   -0.77    0.09   -0.61   -0.75    0.25    0.28    0.45
   -0.51   -0.26   -0.79   -0.64    0.82   -0.83   -0.66   -0.15   -0.70   -0.23    0.13   -0.92    0.04    0.25   -0.71   -0.29   -0.70    1.42
   -0.34   -0.31    0.12    0.09    0.40   -0.02   -0.11   -0.35    0.35   -0.35   -0.27   -0.12   -0.56    0.14   -0.20   -0.04   -0.27    0.00    0.84
   -0.06   -0.54   -0.69   -0.39   -0.19   -0.68   -0.42   -0.15   -0.59    0.41    0.41   -0.79    0.41    0.36   -0.47   -0.44   -0.44   -0.17   -0.39    0.54
//
H MIYT790101
D Amino acid pair distance (Miyata et al., 1979)
R LIT:0601606 PMID:439147
A Miyata, T., Miyazawa, S. and Yasunaga, T.
T Two types of amino acid substitutions in protein evolution
J J. Mol. Evol. 12, 219-236 (1979)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      0.
    2.92      0.
    1.78    2.04      0.
    2.37    2.34    0.65      0.
    1.39    3.06    2.83    3.48      0.
    1.92    1.13    0.99    1.47    2.48      0.
    2.46    1.45    0.85    0.90    3.26    0.84      0.
    0.91    3.58    1.96    2.37    2.22    2.48    2.78      0.
    2.17    0.82    1.29    1.72    2.56    0.32    0.96    2.78      0.
    2.69    2.49    3.37    3.98    1.63    2.57    3.39    3.60    2.45      0.
    2.76    2.62    3.49    4.10    1.65    2.70    3.53    3.67    2.59    0.14      0.
    2.96    0.40    1.84    2.05    3.27    1.06    1.14    3.54    0.79    2.84    2.98      0.
    2.42    2.29    3.08    3.69    1.46    2.30    3.13    3.34    2.19    0.29    0.41    2.63      0.
    3.23    2.47    3.70    4.27    2.24    2.81    3.59    4.14    2.63    0.61    0.63    2.85    0.82      0.
    0.06    2.90    1.80    2.40    1.33    1.92    2.48    0.97    2.15    2.62    2.70    2.94    2.36    3.17      0.
    0.51    2.74    1.31    1.87    1.84    1.65    2.06    0.85    1.94    2.95    3.04    2.71    2.67    3.45    0.56      0.
    0.90    2.03    1.40    2.05    1.45    1.12    1.83    1.70    1.32    2.14    2.25    2.10    1.86    2.60    0.87    0.89      0.
    4.23    2.72    4.39    4.88    3.34    3.42    4.08    5.13    3.16    1.72    1.73    3.11    1.89    1.11    4.17    4.38    3.50      0.
    3.18    2.02    3.42    3.95    2.38    2.48    3.22    4.08    2.27    0.86    0.94    2.42    0.93    0.48    3.12    3.33    2.45    1.06      0.
    1.85    2.43    2.76    3.40    0.86    2.13    2.97    2.76    2.11    0.85    0.91    2.70    0.62    1.43    1.79    2.15    1.42    2.51    1.52      0.
//
H MOHR870101
D EMPAR matrix (Mohana Rao, 1987)
R LIT:1304091 PMID:3570667
A Mohana Rao, J.K.
T New scoring matrix for amino acid residue exchanges based on residue
  characteristic physical parameters
J Int. J. Peptide Protein Res. 29, 276-281 (1987)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     16.
      8.     16.
      9.     10.     16.
      9.     10.     11.     16.
     11.      8.      9.      8.     16.
     11.     10.     11.     11.     10.     16.
     10.      9.     10.     11.      9.     11.     16.
      8.      7.     10.      9.      8.      8.      6.     16.
     11.     10.     10.      9.     10.     11.     11.      7.     16.
      9.      4.      5.      3.      8.      6.      4.      6.      8.     16.
     11.      6.      7.      6.     11.      9.      7.      6.     10.     10.     16.
     10.     11.     11.     11.      9.     12.     11.      7.     11.      4.      7.     16.
     11.      6.      6.      5.     10.      9.      8.      4.     10.      9.     11.      8.     16.
     10.      5.      6.      4.     10.      7.      6.      7.      9.     12.     11.      6.     10.     16.
      6.      6.      9.      8.      7.      7.      5.     11.      5.      3.      4.      6.      2.      4.     16.
     10.      9.     11.     10.     10.     10.      9.     11.     10.      8.      8.     10.      7.      8.     10.     16.
     10.      9.     10.      9.     10.     10.      8.     10.     10.     10.      9.      9.      8.     10.      8.     11.     16.
     11.      7.      8.      6.     11.      9.      7.      8.     10.     11.     11.      7.     10.     11.      6.     10.     11.     16.
      9.      7.      8.      7.     10.      8.      6.     10.      9.     10.      9.      7.      8.     10.      8.     11.     11.     11.     16.
      9.      5.      5.      3.      8.      6.      4.      6.      9.     12.     10.      5.      9.     11.      3.      8.     10.     11.     10.     16.
//
H NIEK910101
D Structure-derived correlation matrix 1 (Niefind-Schomburg, 1991)
R LIT:1713140 PMID:2051484
A Niefind, K. and Schomburg, D.
T Amino acid similarity coefficients for protein modeling and sequence
  alignment derived from main-chain folding angles
J J. Mol. Biol. 219, 481-497 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    1.00
    0.09    1.00
   -0.29   -0.10    1.00
    0.05   -0.08    0.30    1.00
   -0.35   -0.17    0.04   -0.10    1.00
    0.32    0.05   -0.14    0.11   -0.16    1.00
    0.70    0.09   -0.24    0.07   -0.34    0.39    1.00
   -0.40   -0.18    0.37    0.08    0.12   -0.28   -0.45    1.00
   -0.18    0.15    0.04   -0.01   -0.04    0.08   -0.14    0.06    1.00
   -0.25    0.05   -0.06   -0.28   -0.15   -0.13   -0.14   -0.23    0.01    1.00
    0.51    0.00   -0.23    0.01   -0.27    0.29    0.57   -0.54   -0.09    0.25    1.00
    0.55    0.14   -0.19    0.13   -0.25    0.16    0.50   -0.34   -0.23   -0.17    0.31    1.00
    0.39   -0.10   -0.13   -0.09   -0.25    0.22    0.36   -0.29   -0.08    0.15    0.41    0.05    1.00
   -0.18    0.15   -0.13   -0.31   -0.05   -0.25   -0.24   -0.05    0.17    0.27   -0.08   -0.16   -0.02    1.00
    0.10   -0.18   -0.10    0.02    0.13   -0.18   -0.08    0.10   -0.32   -0.53   -0.25    0.04   -0.31   -0.28    1.00
   -0.38   -0.10    0.04    0.02    0.31   -0.23   -0.41    0.28   -0.05   -0.34   -0.61   -0.18   -0.48   -0.13    0.35    1.00
   -0.59   -0.12    0.01   -0.18    0.12   -0.21   -0.50    0.10    0.10    0.30   -0.31   -0.33   -0.31    0.19   -0.21    0.33    1.00
   -0.11    0.00   -0.21   -0.19    0.00   -0.17   -0.12   -0.10   -0.01    0.03   -0.12    0.02   -0.19    0.15   -0.03    0.05    0.07    1.00
   -0.59   -0.01    0.04   -0.19    0.25   -0.28   -0.57    0.19    0.13    0.13   -0.46   -0.43   -0.31    0.24   -0.13    0.34    0.46    0.06    1.00
   -0.23   -0.03   -0.15   -0.22   -0.10   -0.03   -0.09   -0.24   -0.11    0.67    0.23   -0.13    0.08    0.13   -0.42   -0.25    0.35   -0.04    0.15    1.00
//
H NIEK910102
D Structure-derived correlation matrix 2 (Niefind-Schomburg, 1991)
R LIT:1713140 PMID:2051484
A Niefind, K. and Schomburg, D.
T Amino acid similarity coefficients for protein modeling and sequence
  alignment derived from main-chain folding angles
J J. Mol. Biol. 219, 481-497 (1991)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    1.00
    0.11    1.00
   -0.31   -0.12    1.00
    0.07   -0.08    0.35    1.00
   -0.38   -0.20    0.04   -0.10    1.00
    0.36    0.10   -0.16    0.13   -0.16    1.00
    0.74    0.11   -0.27    0.09   -0.36    0.42    1.00
   -0.41   -0.21    0.40    0.08    0.13   -0.32   -0.46    1.00
   -0.20    0.19    0.04    0.00   -0.01    0.12   -0.14    0.09    1.00
   -0.26    0.06   -0.07   -0.29   -0.16   -0.15   -0.13   -0.24    0.00    1.00
    0.54    0.03   -0.24    0.01   -0.29    0.35    0.62   -0.56   -0.13    0.27    1.00
    0.60    0.21   -0.22    0.14   -0.31    0.23    0.58   -0.38   -0.26   -0.18    0.36    1.00
    0.43   -0.09   -0.13   -0.08   -0.29    0.22    0.38   -0.30   -0.06    0.18    0.47    0.09    1.00
   -0.19    0.20   -0.12   -0.35   -0.07   -0.26   -0.27   -0.05    0.20    0.32   -0.08   -0.18   -0.01    1.00
    0.11   -0.21   -0.10    0.01    0.14   -0.18    0.07    0.09   -0.34   -0.55   -0.26    0.04   -0.32   -0.31    1.00
   -0.40   -0.13    0.06    0.03    0.35   -0.22   -0.43    0.28   -0.02   -0.37   -0.66   -0.21   -0.53   -0.13    0.35    1.00
   -0.63   -0.12    0.01   -0.19    0.15   -0.22   -0.54    0.11    0.09    0.32   -0.36   -0.38   -0.35    0.21   -0.21    0.36    1.00
   -0.11    0.03   -0.24   -0.22   -0.02   -0.18   -0.12   -0.11   -0.02    0.04   -0.15    0.02   -0.19    0.18   -0.02    0.07    0.12    1.00
   -0.63   -0.01    0.05   -0.22    0.29   -0.32   -0.62    0.20    0.14    0.15   -0.48   -0.48   -0.33    0.29   -0.15    0.36    0.52    0.11    1.00
   -0.25   -0.04   -0.16   -0.25   -0.10   -0.04   -0.09   -0.25   -0.13    0.72    0.25   -0.16    0.11    0.16   -0.44   -0.27    0.38   -0.02    0.17    1.00
//
H OVEJ920101
D STR matrix from structure-based alignments (Overington et al., 1992)
R LIT:1811128 PMID:1304904
A Overington, J., Donnelly, D., Johnson, M.S., Sali, A. and Blundell, T.L.
T Environment-specific amino acid substitution tables: tertiary templates
  and prediction of protein folds
J Protein Science 1, 216-226 (1992)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      4.
     -1.      7.
     -1.     -1.      5.
     -1.     -2.      2.      6.
     -2.     -2.     -6.     -7.     11.
      0.      1.      0.      0.     -3.      6.
      0.      0.      0.      2.     -3.      2.      5.
      0.     -2.     -1.     -1.     -6.     -2.     -2.      5.
     -2.      0.      2.      0.     -6.      0.     -2.     -3.      8.
     -2.     -3.     -3.     -3.     -4.     -5.     -3.     -5.     -5.      6.
     -2.     -3.     -3.     -6.     -6.     -3.     -4.     -5.     -3.      2.      5.
     -1.      2.      0.     -1.     -4.      1.      1.     -3.      0.     -3.     -2.      5.
      0.     -4.     -2.     -4.     -5.      1.     -2.     -4.     -2.      1.      3.     -1.      8.
     -3.     -4.     -3.     -5.     -2.     -4.     -4.     -6.     -2.      1.      2.     -3.      0.      7.
     -1.     -2.     -2.     -1.     -8.     -2.     -1.     -2.     -3.     -4.     -3.     -1.     -6.     -5.      7.
      0.      0.      0.      0.     -4.     -1.     -1.     -1.     -2.     -3.     -4.     -1.     -4.     -3.     -1.      4.
     -1.     -1.      0.     -1.     -5.      0.      0.     -3.     -2.     -2.     -3.      0.     -2.     -3.     -1.      1.      5.
     -3.     -2.     -5.     -6.     -6.     -5.     -6.     -4.     -3.     -2.     -1.     -3.     -2.      2.     -4.     -5.     -5.     10.
     -3.     -1.     -1.     -3.     -6.     -3.     -2.     -3.      0.     -1.     -2.     -2.     -1.      3.     -6.     -2.     -2.      2.      7.
      0.     -3.     -4.     -4.     -4.     -2.     -2.     -4.     -2.      2.      1.     -3.      0.     -1.     -4.     -3.     -1.     -4.     -1.      5.
//
H QU_C930101
D Cross-correlation coefficients of preference factors
  main chain (Qu et al., 1993)
R LIT:1906100 PMID:8381879
A Qu, C., Lai, L., Xu, X. and Tang, Y.
T Phyletic relationships of protein structures based on spatial prefernce
  of residues
J J. Mol. Evol. 36, 67-78 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   1.000
   0.390   1.000
   0.370   0.266   1.000
   0.299  -0.109   0.037   1.000
   0.270   0.273   0.105   0.035   1.000
   0.261  -0.084   0.082   0.321   0.191   1.000
   0.300   0.375   0.206   0.137   0.341   0.228   1.000
   0.407   0.394   0.293   0.250   0.246   0.494   0.164   1.000
   0.356   0.093   0.299  -0.117   0.527   0.630   0.121   0.497   1.000
   0.476   0.305   0.452   0.242  -0.029   0.372   0.212   0.429   0.406   1.000
   0.555   0.446   0.191   0.261   0.501   0.251   0.291   0.327   0.457   0.570   1.000
   0.398   0.236   0.208   0.184   0.054   0.323   0.247   0.006   0.072   0.088  -0.080   1.000
   0.207   0.374   0.438  -0.295  -0.006   0.211   0.128   0.326   0.461   0.440   0.112   0.285   1.000
   0.628   0.552   0.278   0.475   0.550   0.364   0.433   0.455   0.405   0.532   0.769   0.217   0.111   1.000
   0.183  -0.037   0.156   0.008   0.355  -0.168  -0.216  -0.023   0.304   0.065   0.079   0.099   0.266   0.091   1.000
   0.193  -0.043  -0.051   0.012  -0.178   0.404  -0.081   0.015   0.144   0.166  -0.042   0.102   0.165  -0.012  -0.363   1.000
  -0.083   0.037   0.076   0.328   0.087   0.344   0.220   0.335   0.259   0.385   0.386  -0.206  -0.141   0.306  -0.336  -0.124   1.000
   0.081  -0.059   0.277   0.578   0.174   0.515   0.149   0.136   0.232   0.357   0.268   0.436  -0.075   0.451  -0.118  -0.023   0.564   1.000
   0.683   0.201   0.387   0.320   0.195   0.207   0.273   0.372   0.083   0.333   0.246   0.436  -0.057   0.428  -0.054  -0.093   0.000   0.293   1.000
   0.565   0.531   0.512   0.149   0.427   0.334   0.444   0.639   0.534   0.641   0.598   0.249   0.278   0.626   0.020  -0.103   0.329   0.378   0.614   1.000
//
H QU_C930102
D Cross-correlation coefficients of preference factors
  side chain (Qu et al., 1993)
R LIT:1906100 PMID:8381879
A Qu, C., Lai, L., Xu, X. and Tang, Y.
T Phyletic relationships of protein structures based on spatial prefernce
  of residues
J J. Mol. Evol. 36, 67-78 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   1.000
   0.250   1.000
   0.138   0.558   1.000
  -0.018  -0.054   0.452   1.000
   0.799   0.113   0.032   0.015   1.000
   0.550   0.243   0.222   0.257   0.418   1.000
  -0.116   0.037   0.408   0.851  -0.167   0.254   1.000
   0.000   0.000   0.000   0.000   0.000   0.000   0.000   0.000
   0.523   0.392   0.305   0.067   0.425   0.614  -0.102   0.000   1.000
   0.888   0.108  -0.101  -0.185   0.717   0.511  -0.135   0.000   0.378   1.000
   0.862   0.049  -0.172  -0.249   0.787   0.439  -0.223   0.000   0.289   0.960   1.000
   0.281   0.872   0.490  -0.064   0.002   0.377  -0.051   0.000   0.488   0.099  -0.004   1.000
   0.858   0.058  -0.090  -0.109   0.912   0.450  -0.180   0.000   0.441   0.842   0.881  -0.044   1.000
   0.874   0.108  -0.072  -0.107   0.857   0.482  -0.187   0.000   0.511   0.893   0.927   0.061   0.903   1.000
   0.656   0.133   0.265   0.276   0.558   0.598   0.097   0.000   0.651   0.572   0.504   0.206   0.523   0.661   1.000
   0.281   0.804   0.661   0.245   0.104   0.357   0.204   0.000   0.568   0.083   0.003   0.745   0.054   0.152   0.200   1.000
   0.574   0.427   0.519   0.382   0.326   0.610   0.287   0.000   0.399   0.382   0.346   0.540   0.313   0.410   0.435   0.601   1.000
   0.825   0.169   0.003  -0.079   0.779   0.478  -0.216   0.000   0.460   0.792   0.843   0.111   0.785   0.907   0.597   0.204   0.471   1.000
   0.772   0.266   0.338   0.225   0.817   0.550   0.036   0.000   0.492   0.573   0.625   0.182   0.764   0.743   0.632   0.307   0.540   0.802   1.000
   0.850   0.045  -0.203  -0.196   0.755   0.458  -0.186   0.000   0.284   0.946   0.973   0.024   0.874   0.909   0.462   0.005   0.396   0.835   0.632   1.000
//
H QU_C930103
D The mutant distance based on spatial preference factor (Qu et al., 1993)
R LIT:1906100 PMID:8381879
A Qu, C., Lai, L., Xu, X. and Tang, Y.
T Phyletic relationships of protein structures based on spatial prefernce
  of residues
J J. Mol. Evol. 36, 67-78 (1993)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      8.
      2.      8.
      1.      2.      8.
      0.     -1.      3.      8.
      5.      0.      0.      0.      8.
      2.      0.      1.      2.      3.      8.
      0.      0.      3.      4.      0.      2.      8.
      2.      2.      2.      0.      1.      2.     -1.      8.
      4.      2.      2.      0.      4.      4.      0.      0.      8.
      5.      0.      0.      0.      4.      2.      0.      0.      3.      8.
      5.      0.      0.      0.      5.      3.      0.      1.      2.      6.      8.
      2.      6.      2.      0.      0.      1.      1.     -1.      3.      1.      0.      8.
      5.      0.      0.      0.      5.      2.      0.      2.      3.      5.      6.      0.      8.
      5.      0.      1.      0.      6.      3.      0.      0.      4.      5.      6.      1.      5.      8.
      3.      1.      3.      1.      4.      2.      0.      0.      4.      3.      2.      1.      3.      3.      8.
      2.      3.      3.      2.      1.      2.      2.      1.      3.      0.      0.      3.      0.      0.      1.      8.
      3.      2.      3.      4.      1.      3.      3.      1.      2.      1.      1.      3.      1.      2.      2.      4.      8.
      4.      0.      0.      0.      5.      2.      0.     -1.      3.      4.      4.      1.      4.      6.      3.      1.      2.      8.
      4.      0.      2.      1.      4.      2.      1.      0.      3.      4.      4.      1.      4.      4.      3.      2.      3.      5.      8.
      5.      0.      0.      0.      5.      3.      0.      2.      2.      6.      6.      0.      6.      5.      2.      0.      2.      5.      5.      8.
//
H RISJ880101
D Scoring matrix (Risler et al., 1988)
R LIT:1505154 PMID:3221397
A Risler, J.L., Delorme, M.O., Delacroix, H. and Henaut, A.
T Amino acid substitutions in structurally related proteins
  A pattern recognition approach
  Determination of a new and efficient scoring matrix
J J. Mol. Biol. 204, 1019-1029 (1988)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     2.2
     1.5     2.2
     1.3     1.2     2.2
     0.2    -0.1     0.8     2.2
    -1.5    -1.5    -1.6    -1.7     2.2
     1.8     2.0     1.6     0.6    -1.4     2.2
     1.7     1.9     1.4     1.0    -1.5     2.1     2.2
     0.6     0.1     0.2    -0.4    -1.7     0.2     0.3     2.2
    -0.6    -0.4    -0.3    -1.3    -1.8    -0.5    -0.6    -1.2     2.2
     1.7     1.4     0.9     0.0    -1.6     1.4     1.5     0.0    -0.8     2.2
     1.3     1.2     0.8    -0.2    -1.5     1.1     0.9    -0.2    -0.9     2.1     2.2
     1.4     2.1     1.0     0.1    -1.6     1.7     1.4    -0.1    -1.0     1.0     0.7     2.2
     1.0     1.1     0.0    -0.5    -1.6     1.2     0.6    -0.4    -1.2     0.9     1.8     0.4     2.2
     0.6     0.4     0.4    -0.3    -1.6     0.7     0.6    -0.4    -1.1     1.0     1.0     0.1    -0.2     2.2
    -0.2    -0.3    -1.0    -1.2    -1.8    -0.6    -0.1    -1.2    -1.6    -0.6    -0.8    -0.7    -1.2    -1.1     2.2
     2.0     2.0     1.9     0.7    -1.3     1.8     1.8     0.7    -0.4     1.6     1.3     1.4     0.6     0.5    -0.3     2.2
     1.9     1.9     1.1     0.0    -1.4     1.7     1.6     0.2    -0.9     1.6     1.2     1.2     0.8     0.3    -0.5     2.1     2.2
    -0.9    -0.8    -1.1    -1.4    -1.8    -1.0    -1.0    -1.3    -1.7    -0.7    -0.8    -1.1    -1.3    -0.9    -1.6    -0.8    -1.0     2.2
     0.2     0.8    -0.1    -0.4    -1.1     0.5     0.2    -0.2    -0.8     0.4     0.5     0.5    -0.2     2.0    -1.2     0.4     0.3    -0.6     2.2
     2.0     1.5     1.1     0.0    -1.4     1.5     1.6     0.1    -0.7     2.2     2.0     1.2     0.8     0.8    -0.6     1.8     1.6    -0.7     0.3     2.2
//
H TUDE900101
D isomorphicity of replacements (Tudos et al., 1990)
R LIT:1616619 PMID:2279846
A Tudos, E., Cserzo, M. and Simon, I.
T Predicting isomorphic residue replacements for protein design
J Int. J. Peptide Protein Res. 36, 236-239 (1990)
* Diagonal elements are missing.
* We use 100 as diagonal elements.
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    100.
     -2.    100.
     -8.     11.    100.
      3.      2.     32.    100.
      4.    -12.     -7.    -20.    100.
      0.     26.     12.      8.     -8.    100.
     12.     11.     13.     34.    -18.     37.    100.
     -3.     -6.     10.      8.     -1.    -10.     -5.    100.
    -10.      0.      8.     10.      3.     -4.     -8.     -8.    100.
    -17.    -25.    -32.    -39.     12.    -20.    -36.    -21.      3.    100.
     -6.    -24.    -35.    -40.     15.    -26.    -40.    -16.     -9.     46.    100.
      2.     24.     17.     10.    -14.     26.     24.    -11.     -4.    -17.    -33.    100.
     -2.      0.    -12.    -16.      2.    -12.    -17.    -10.     -8.     18.     24.    -19.    100.
     -8.    -11.    -23.    -31.     11.    -22.    -40.    -12.    -10.     32.     36.    -26.     20.    100.
     -2.     -4.      8.      1.     -3.      0.     -7.      4.     -2.    -18.    -16.     -2.    -10.     -2.    100.
     10.    -10.      1.      7.     -6.     -7.    -10.      9.     -3.    -17.    -11.    -10.    -10.      0.     15.    100.
     -3.     -5.     12.     11.     -4.    -10.    -12.    -13.     -7.     -5.    -11.     -8.     -8.      4.      2.     24.    100.
    -12.     -7.     -6.    -20.      8.     -3.    -10.    -13.     -6.     12.      8.    -10.     12.      8.     -9.    -18.     -8.    100.
    -18.      0.    -13.    -22.      5.    -23.    -28.    -18.     12.     29.     16.    -21.      8.     24.     -9.    -16.     -2.      6.    100.
    -12.    -18.    -30.    -32.      8.    -12.    -20.    -14.    -10.     46.     26.    -14.     10.     16.    -18.    -16.     -4.     14.     17.    100.
//
H AZAE970101
D The single residue substitution matrix from interchanges of
  spatially neighbouring residues (Azarya-Sprinzak et al., 1997)
R PMID:9488136
A Azarya-Sprinzak, E., Naor, D., Wolfson, H.J. and Nussinov, R.
T Interchanges of spatially neighbouring residues in structurally conserved
  environments.
J Protein Engineering 10, 1109-1122 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      14
       1      16
       1      10      15
       0      13      16      26
       5      -9      -4      -8      18
       0      16      13      16     -10      21
       2      13      10      15      -8      17      11
       5       0       8       7       1       0       1      24
      -2       4       5       8      -2       6       4       6       7
      -6     -11     -11     -14       2     -12     -11     -10      -4      10
      -2      -8      -9     -11       1      -9      -8      -9      -5       8       9
       1      21      12      16     -11      22      17      -1       3     -13     -10      28
       2      -1      -3      -7       0      -2       1      -3      -1       2       5      -4       2
      -4      -8      -9     -10       2     -10      -7      -4      -1       6       5     -11       2       8
       2       2      11      11       0       1       5      13       4     -14     -12       5     -10      -6      51
       1       6       7       8      -1       6       6       8       3      -8      -7       6      -5      -5       6       9
      -2       5       4       4      -5       6       3       1       4      -4      -6       7      -4      -4       5       5      10
      -2      -3      -5      -5      -1      -3      -6      -1       3       4       2      -8       2       5      -5      -4      -2       8
      -2      -1      -3      -4      -1      -3      -1      -2       0       2       0      -3       1       3      -5      -1       0       2       4
      -5     -11     -11     -13       3     -12     -12      -8      -4       9       5     -14       0       5      -7      -6      -3       4       2      11
//
H AZAE970102
D The substitution matrix derived from spatially conserved motifs
  (Azarya-Sprinzak et al., 1997)
R PMID:9488136
A Azarya-Sprinzak, E., Naor, D., Wolfson, H.J. and Nussinov, R.
T Interchanges of spatially neighbouring residues in structurally conserved
  environments.
J Protein Engineering 10, 1109-1122 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       8
       1      11
       0       7      11
       0       9      12      16
       2      -7      -5      -8      14
       1      12      10      13      -9      17
       1      10       8      10      -6      13       8
       1       0       7       8       0       0       0      18
      -2       2       2       4      -1       2       1       5       5
      -3     -10     -11     -12       4     -12     -10      -8      -3      11
       0      -7      -9     -10       2      -9      -7      -8      -4       8      10
       1      14      10      11     -10      16      13       0       2     -12      -9      20
       1      -2      -4      -6       1      -3       0      -5      -2       3       6      -5       4
      -2      -8      -9      -9       3     -10      -7      -3      -1       7       6     -10       3       8
      -1       1       8       7      -2       0       0      10       3      -9      -9       1      -9      -5      33
       0       4       6       6      -2       4       3       6       2      -7      -6       4      -5      -5       5       7
      -2       2       2       3      -3       2       1       1       3      -2      -4       2      -3      -3       3       4       6
      -1      -4      -4      -4       0      -5      -5      -1      -1       4       3      -7       2       4      -4      -3      -1       6
      -1      -3      -4      -5       0      -4      -1      -1       0       3       2      -4       2       3      -4      -1       0       2       3
      -4     -10     -11     -12       5     -12     -11      -7      -3      11       6     -13       1       7      -5      -5      -1       4       2      12
//
H RIER950101
D Hydrophobicity scoring matrix (Riek et al., 1995)
R PMID:7715195
A Riek, R.P., Handschumacher, M.D., Sung, S.S., Tan, M., Glynias, M.J.,
  Schluchter, M.D., Novotny, J. and Graham, R.M.
T Evolutionary conservation of both the hydrophilic and hydrophobic nature of
  transmembrane residues.
J J. Theor. Biol. 172, 245-258 (1995)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     100
      13     100
      60      53     100
      33      81      73     100
      98      11      58      30     100
      64      49      96      68      62     100
      39      74      79      94      36      74     100
      96      17      64      36      94      68      43     100
      71      42      89      61      69      93      68      75     100
      91       4      51      23      93      55      29      87      62     100
      93       6      52      25      95      57      31      89      64      98     100
      35      78      75      98      33      71      96      39      64      26      27     100
      89       2      49      21      91      53      27      85      60      98      96      24     100
      87       0      47      19      89      51      26      83      58      96      94      22      98     100
      89      24      71      44      86      76      50      93      83      79      81      46      78      76     100
      94      19      66      39      91      71      45      98      78      84      86      41      83      81      95     100
      98      16      63      35      95      67      41      99      74      88      90      38      86      84      91      96     100
      98      11      58      31      99      63      37      94      69      93      94      33      91      89      87      92      96     100
      94      19      66      38      92      70      44      98      77      85      87      41      83      81      94      99      97      93     100
      94       7      54      26      96      58      33      90      65      97      99      29      95      93      83      88      91      96      88     100
//
H WEIL970101
D WAC matrix constructed from amino acid comparative profiles (Wei et al., 1997)
R PMID:9390315
A Wei, L., Altman, R.B. and Chang, J.T.
T Using the radial distributions of physical features to compare amino
  acid environments and align amino acid sequences.
J Pac. Symp. Biocomput. 1997 5, 465-476 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       4
      -1       4
       0       0       4
      -2      -1       0       4
       0      -1       0      -2       4
       0       0       1      -1       0       4
      -3      -1       0       0      -2       0       4
      -1      -1       0      -2       0       0      -2       4
       0       0       0      -1       0       0      -1      -1       4
       0      -2      -1      -4       0       0      -4      -2      -1       4
       0      -1      -1      -3       0       0      -3      -1      -1       1       4
      -1       2       0      -1      -2       0      -1      -1       0      -2      -2       4
       1       0       0      -1       1       1      -1       0       0       2       2       0       4
       0      -2      -1      -4       0       0      -4      -2       0       0       1      -2       2       4
       0       0       0      -1      -1       0      -1       0       0       0       0       0       1       0       4
       0      -1       1      -1       0       0      -2       0      -1      -1      -1       0       0      -2       0       4
       0       0       1      -1       0       1      -1       0      -1       0       0       0       0      -2       0       1       4
       0       0      -1      -3       0       0      -2      -2       0       0       1      -2       2       2       0      -1      -1       4
       0      -1       0      -3       0       1      -4      -2       0       0       0      -2       0       1      -1      -1      -1       1       4
       1      -2      -1      -3       0      -1      -4      -2      -1       2       1      -3       1       0       0      -1       0       0       0       4
//
H WEIL970102
D Difference matrix obtained by subtracting the BLOSUM62 from the WAC
  matrix (Wei et al., 1997)
R PMID:9390315
A Wei, L., Altman, R.B. and Chang, J.T.
T Using the radial distributions of physical features to compare amino
  acid environments and align amino acid sequences.
J Pac. Symp. Biocomput. 1997 5, 465-476 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       0
       0      -1
       2       0      -2
       0       1      -1      -2
       0       2       3       1      -5
       1      -1       1      -1       3      -1
      -2      -1       0      -2       2      -2      -1
      -1       1       0      -1       3       2       0      -2
       2       0      -1       0       3       0      -1       1      -4
       1       1       2      -1       1       3      -1       2       2       0
       1       1       2       1       1       2       0       3       2      -1       0
       0       0       0       0       1      -1      -2       1       1       1       0      -1
       2       1       2       2       2       1       1       3       2       1       0       1      -1
       2       1       2      -1       2       3      -1       1       1       0       1       1       2      -2
       1       2       2       0       2       1       0       2       2       3       3       1       3       4      -3
      -1       0       0      -1       1       0      -2       0       0       1       1       0       1       0       1       0
       0       1       1       0       1       2       0       2       1       1       1       1       1       0       1       0      -1
       3       3       3       1       2       2       1       0       2       3       3       1       3      -1       4       2       1      -7
       2       1       2       0       2       2      -2       1      -2       1       1       0       1       0       2       1       1      -1      -3
       1       1       2       0       1       1      -2       1       2      -1       0      -1       0       1       2       1       0       3       1       0
//
H MEHP950102
D (Mehta et al., 1995)
R LIT:2213135 PMID:8580842
A Mehta, P.K., Heringa, J. and Argos, P.
T A simple and fast approach to prediction of protein secondary structure from
  multiply aligned sequences with accuracy above 70%
J Protein Science 4, 2517-2525 (1995)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    0.75
    0.80    0.90
    0.71    0.88    0.80
    0.56    0.63    0.69    0.66
    0.75    0.84    0.72    0.67    1.07
    0.68    0.83    0.71    0.64    0.65    0.80
    0.63    0.82    0.74    0.58    0.69    0.73    0.74
    0.83    0.84    0.71    0.61    0.80    0.78    0.87    0.97
    0.79    0.92    0.78    0.68    0.69    0.79    0.78    0.71    0.99
    1.11    1.23    1.12    1.06    0.96    1.10    1.15    1.25    1.24    1.33
    0.97    1.05    0.97    0.96    0.84    1.07    1.12    1.09    1.07    1.21    1.12
    0.65    0.84    0.72    0.64    0.79    0.75    0.78    0.76    0.82    1.11    0.99    0.78
    0.97    1.14    0.92    0.93    0.97    0.97    0.96    1.18    0.96    1.16    1.06    1.03    1.05
    1.16    1.26    1.11    1.17    1.04    1.07    1.17    1.30    1.05    1.54    1.27    1.11    1.21    1.33
    0.77    1.03    0.91    0.75    0.67    0.83    0.75    0.75    0.83    1.30    1.21    0.92    1.34    1.07    0.82
    0.80    0.99    0.84    0.77    0.81    0.85    0.92    0.91    0.85    1.24    1.09    0.89    1.15    1.28    0.87    0.96
    0.97    1.08    0.99    0.88    0.93    1.02    1.11    1.03    0.91    1.27    1.18    1.09    1.11    1.32    0.93    1.10    1.16
    1.18    1.33    0.95    1.04    1.47    1.17    1.33    1.28    1.18    1.71    1.37    1.11    1.35    1.31    1.09    1.34    1.42    1.22
    1.23    1.25    1.08    1.12    1.22    1.11    1.31    1.27    1.23    1.51    1.41    1.18    1.23    1.34    1.29    1.41    1.46    1.29    1.31
    1.05    1.08    1.05    0.99    0.91    1.03    1.08    1.09    1.13    1.42    1.35    1.06    1.22    1.51    1.13    1.21    1.27    1.63    1.60    1.41
//
H KAPO950101
D (Kapp et al., 1995)
R LIT:2124159 PMID:8535255
A Kapp, O.H., Moens, L., Vanfleteren, J., Trotman, C.N., Suzuki, T. and
  Vinogradov, S.N.
T Alignment of 700 globin sequences: extent of amino acid substitution and its
  correlation with variation in volume
J Protein Science 4, 2179-2190 (1995)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
   23.40
   16.80   29.50
   17.10   17.10   27.40
   18.20   18.20   21.40   25.90
   21.50   14.40   14.70   14.00   31.90
   17.20   19.60   18.60   22.20   13.80   96.50
   18.10   18.70   20.00   22.80   12.20   20.40   26.50
   19.90   16.10   18.10   18.70   15.00   16.30   19.30   26.80
   11.50   13.70   18.90   17.20   13.50   21.20   15.70   12.20   30.80
   17.20   14.30   14.80   13.70   20.90   15.80   14.90   14.70   12.40   24.70
   13.60   12.20   11.70   12.50   15.50   13.30   11.40   11.50    9.07   21.00   24.80
   17.10   21.90   17.70   18.20    9.83   22.00   19.20   15.60   15.50   14.20   12.10   26.40
   16.20   15.50   13.70   15.50   19.80   17.80   15.20   15.00   11.40   20.90   22.40   15.40   25.90
   11.90   10.10   11.40    9.04   13.50   11.50    9.24    9.84   10.70   18.40   20.60    9.68   20.20   27.10
   17.70   15.70   14.60   19.40    5.43   18.00   19.10   17.00   11.70    9.35    7.28   16.80   11.60    3.14   32.20
   20.40   17.50   20.90   19.10   17.70   17.60   17.70   20.20   13.80   14.60   12.20   16.60   14.70    9.65   17.90   25.40
   18.10   20.60   20.20   19.00   16.20   17.40   18.80   18.20   14.80   17.50   14.30   17.60   16.90   12.80   14.90   19.50   26.10
   10.10    9.94    7.74    9.08    9.56   16.60   15.30    7.20    0.00   10.40   14.70    7.79   18.50   19.30    9.85    9.70   17.20   33.80
   15.30   13.80   20.10   14.90   17.30   14.60   12.70   13.70   19.40   17.60   17.90   14.70   20.00   22.60    6.99   14.40   17.70   19.50   29.20
   16.70   14.40   14.80   15.10   21.40   15.20   15.10   14.50   12.90   22.20   18.90   13.50   19.10   17.20   11.10   15.10   17.90   11.60   16.50   25.00
//
H VOGG950101
D (Vogt et al., 1995)
R LIT:2114150 PMID:7602593
A Vogt G, Etzold T, Argos P
T An assessment of amino acid exchange matrices in aligning protein sequences:
  the twilight zone revisited
J J. Mol. Biol. 249, 816-831 (1995)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     7.6
     4.6     9.9
     4.9     5.5     9.0
     4.9     4.9     7.4     9.9
     5.7     3.0     3.4     2.0    16.7
     5.0     6.7     5.9     6.1     2.8     7.9
     5.2     5.6     6.1     7.9     2.2     6.9     8.8
     5.7     4.2     5.6     5.3     3.2     4.2     4.4    11.8
     4.4     5.8     6.4     5.6     3.9     6.4     5.6     3.8    11.2
     4.4     2.8     2.4     1.4     4.1     3.3     2.5     0.7     3.0     9.2
     4.0     3.0     2.2     1.2     3.7     3.6     2.4     0.8     3.3     8.0     9.2
     4.8     7.9     6.0     5.7     2.4     6.7     6.4     4.1     5.8     3.1     3.1     8.4
     4.5     3.5     3.0     2.2     4.3     4.2     3.2     1.7     3.9     7.7     8.0     3.8     9.5
     2.9     2.0     2.1     0.7     4.4     2.6     1.3     0.0     5.1     6.2     7.2     1.9     6.8    12.2
     5.5     4.3     4.3     4.5     2.1     5.0     4.7     3.6     4.1     2.6     2.9     4.6     2.8     1.4    12.8
     6.3     5.0     6.1     5.7     5.3     5.4     5.4     5.6     5.0     3.4     3.1     5.3     3.8     2.4     5.6     7.4
     5.8     5.0     5.7     5.2     4.7     5.2     5.1     4.1     4.9     4.6     3.9     5.3     4.6     3.0     5.3     6.7     7.7
     1.6     3.6     1.6     0.0     4.2     2.5     0.9     1.2     4.4     3.4     4.5     1.7     4.2     8.8     0.2     1.9     1.7    19.4
     3.0     3.4     3.8     2.4     4.7     3.5     2.5     1.2     7.4     4.5     5.2     3.1     5.0    10.3     2.1     3.3     3.3     9.3    13.0
     5.3     3.2     3.0     2.3     5.2     3.7     3.3     1.9     3.2     8.3     7.0     3.5     6.8     5.3     3.4     4.2     5.2     2.6     4.1     8.6
//
H BLAJ010101
D Matrix built from structural superposition data for identifying potential
  remote homologues (Blake-Cohen, 2001)
R PMID:11254392
A Blake, J.D. and Cohen, F.E.
T Pairwise sequence alignment below the twilight zone
J J Mol Biol. 307, 721-735 (2001)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       9
       0      14
       0       1      11
       0      -2       5      17
      -5     -16     -13     -13      39
       1       7       1       1     -14      13
       0       3       1       5     -20       5      12
       1      -2       1       2     -15      -3       0      16
      -2       2       5       1     -18       2       0      -2      23
       0      -7      -8      -9      -3      -7      -8      -3      -4      10
      -2      -4      -7     -10     -11     -10      -8      -6      -4       7      10
       0       7       2       0     -23       4       6       0       1      -7      -4       9
      -2      -8      -6      -7      -9      -8      -6      -7      -5      10      11      -4      13
      -1      -6      -3      -6     -12      -4     -10      -8      -1       3       3      -8       0      16
      -1      -3      -1       2     -18      -4      -1       0      -4      -3       1       1      -4      -4      19
       0       2       3       0     -18       0       0       0       0      -6      -4       1      -7      -4       1       9
      -3       0       2       0     -19       2       3      -4       0      -3      -5       1      -3      -2      -1       5       7
     -11      -6      -9      -7     -24     -12      -3     -10      -9      -6       2      -7      -4       9      -5      -7       0      32
      -3      -1       1      -6      -1      -5      -5     -10       1      -2      -4      -5      -3       8      -8      -1       3       0      19
       0      -4      -4     -10       0      -2      -6      -5      -6       8       6      -6       6       1      -4      -5      -1      -5      -1       9
//
H PRLA000101
D Structure derived matrix (SDM) for alignment of distantly related sequences
  (Prlic et al., 2000)
R PMID:10964983
A Prlic, A., Domingues, F.S. and Sippl, M.J.
T Structure-derived substitution matrices for alignment of distantly 
  related sequences
J Protein Eng. 13, 545-550 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    2.09
   -0.50    2.87
   -0.57    0.60    3.60
   -0.73    0.13    1.78    4.02
    0.33   -1.30   -2.08   -2.51    6.99
   -0.75    0.13    0.33    0.34   -0.83    2.60
   -0.12    0.99   -0.16    1.20   -1.97    1.23    2.97
    0.27   -0.96    0.79   -1.20   -2.11   -0.12   -0.41    4.36
   -1.42    0.54    0.76   -0.01   -1.50   -0.46   -0.62   -0.40    5.89
   -0.97   -1.40   -2.43   -2.77    0.13   -1.47   -1.81   -2.93   -1.76    2.76
   -0.39   -1.19   -2.10   -2.65   -0.31   -1.49   -2.11   -1.98   -0.93    1.56    2.43
   -0.38    1.42    0.83    0.66   -2.19    0.92    1.11   -0.71    0.31   -1.81   -1.96    2.91
   -0.04   -0.63   -2.01   -2.58    1.04   -0.13   -1.86   -1.86   -1.04    0.99    1.61   -1.62    3.75
   -0.76   -1.40   -2.25   -2.19    1.13   -2.31   -1.61   -2.67   -0.22    0.76    1.23   -2.41    0.80    3.28
   -0.53    0.21   -1.10    0.72   -2.19    0.24   -0.26   -0.04   -1.44   -2.00   -1.56   -0.19   -1.09   -0.91    5.45
    0.34   -0.06    0.40    0.71    0.31    1.04    0.31    0.29   -0.74   -1.75   -2.30   -0.06   -1.34   -1.11   -0.29    2.36
    0.13   -0.15    0.30   -0.75   -0.59    0.60   -0.21   -0.81   -0.52   -0.96   -0.86   -0.10   -1.58   -0.69    0.93    1.20    2.04
   -0.66   -0.04   -2.89   -1.91   -0.76   -0.81   -2.70   -1.21   -1.48    0.25   -0.14   -1.94    0.87    2.29   -5.34   -1.18   -0.57    6.96
   -1.25   -0.75   -0.36   -1.21    0.13   -0.61   -1.64   -1.62   -0.12    0.08    0.70   -1.72   -0.41    1.96   -1.98   -1.56   -0.41    2.15    3.95
    0.02   -1.52   -2.17   -2.02    0.34   -1.38   -1.84   -1.96   -0.35    1.94    0.81   -1.27    0.61    0.51   -1.11   -1.11    0.05   -1.09    0.21    2.05
//
H PRLA000102
D Homologous structure dereived matrix (HSDM) for alignment of distantly
  related sequences (Prlic et al., 2000)
R PMID:10964983
A Prlic, A., Domingues, F.S. and Sippl, M.J.
T Structure-derived substitution matrices for alignment of distantly 
  related sequences
J Protein Eng. 13, 545-550 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    5.50
   -2.24    8.59
   -1.77    0.24   10.00
   -2.38   -0.33    4.07   11.01
    0.45   -6.29   -6.53   -6.98   19.05
   -2.16   -0.74    1.42    1.10   -2.47    7.85
   -0.47    2.83   -0.39    2.41   -4.70    3.16    8.43
    0.63   -3.39    1.16   -3.91   -5.70   -0.24   -1.80   11.64
   -3.01    0.70    1.77    0.32   -5.95   -2.24   -1.29   -1.24   15.72
   -1.72   -3.93   -5.78   -6.18   -0.13   -3.26   -5.89   -8.58   -4.44    6.74
   -1.09   -2.83   -5.64   -7.41   -0.82   -4.56   -5.62   -6.55   -2.49    3.86    6.38
   -1.22    3.89    1.64    1.53   -6.65    3.24    3.08   -1.82   -0.17   -4.82   -5.91    8.23
    0.16   -1.43   -4.67   -7.88    3.50   -1.76   -3.94   -5.29   -3.66    2.94    4.32   -5.47   10.21
   -2.42   -4.36   -6.22   -5.06    1.72   -5.54   -4.44   -7.46    0.25    2.30    3.90   -6.19    2.66    9.14
   -1.11    1.31   -3.23    0.81   -6.70    1.30   -0.43   -1.79   -3.55   -4.04   -2.88   -1.21   -2.02   -2.96   13.32
    1.27   -0.50    1.54    2.34    1.08    2.59    0.42    0.63   -2.38   -4.67   -6.22   -0.27   -3.92   -5.03   -1.28    6.35
    0.60    0.34    1.14   -1.36   -1.89    1.08   -0.61   -2.24   -1.14   -3.03   -2.40   -0.37   -5.18   -4.00    2.44    3.09    6.33
   -2.61    1.02   -6.29   -5.63   -3.01   -4.30   -6.28   -4.77   -5.71   -0.26   -0.58   -5.45    4.28    6.49  -11.46   -4.44   -3.55   18.08
   -4.22   -1.01   -0.93   -3.85   -0.44   -1.73   -4.50   -4.34    1.17   -0.08    1.81   -4.03   -4.95    5.38   -7.41   -4.17   -2.92    6.79   10.92
    0.16   -3.80   -5.65   -6.10    1.32   -4.97   -4.23   -5.32   -1.63    5.23    2.28   -3.57    1.18    0.52   -2.31   -2.69   -0.23   -2.13    0.66    5.28
//
H QUIB020101
D STROMA score matrix for the alignment of known distant homologs
  (Qian-Goldstein, 2002)
R PMID:12211027
A Qian, B. and Goldstein, R.A.
T Optimization of a new score function for the generation of accurate 
  alignments
J Proteins. 48, 605-610 (2002)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     2.5
     0.2     5.2
     1.1     0.7     2.5
       1     0.1     3.3     5.3
     1.2    -1.3    -1.9    -3.1    11.5
    -0.1       2     1.9     1.1    -2.5     3.6
     1.2     1.9     2.3     3.2    -2.4     1.7     3.7
     1.4    -0.2     0.7     0.9    -1.3    -0.3     0.5     7.5
    -1.4     1.5     1.4     0.5    -1.7     1.4     0.3    -1.7     6.8
     0.3    -1.9    -2.4    -2.9    -3.2    -0.9    -3.1    -3.7    -1.8     4.5
    -0.2    -1.5    -2.4    -3.4    -1.6    -1.2    -1.5    -3.8    -2.4     3.4     5.2
    -0.2     3.4     1.6     1.4      -3     2.2     1.2     0.4     1.1    -1.5      -2     3.9
    -0.2    -1.4    -2.1    -2.8    -1.3    -0.6      -2    -3.8    -0.8     2.2     3.1    -0.5     5.4
    -1.6    -3.2    -2.5    -3.7    -0.8    -1.7   -13.7    -4.7    -0.9     2.2     3.7    -2.8     1.7       7
     0.7    -0.6    -0.1    -0.2    -3.6       1       0    -0.8    -2.1    -2.4    -1.4     0.2    -1.9    -4.1     8.1
     1.7     0.2     1.4     1.7     0.7     0.9     1.1     1.6    -0.1    -1.1    -0.8     1.4    -1.1    -2.5       2     2.8
     1.7     0.2     1.4     0.1     0.3    -0.1     1.6    -0.6    -0.2       0     0.3       1    -0.3    -0.8     1.1     2.6     0.4
    -3.3    -1.5      -4    -5.7    -0.5    -2.9    -4.7    -4.2    -1.2    -1.8    -1.2      -3    -0.6     3.7      -5    -2.8    -2.9    14.9
    -1.8    -0.9    -0.8    -2.9    -0.3    -1.5    -2.2    -4.8     2.9     0.2     0.8    -1.5     0.5     5.2    -3.3    -0.9    -0.8     4.9     8.1
     1.9    -2.8    -0.9    -2.5     0.7    -1.5    -1.3    -1.4    -2.5     4.5     3.4      -1     1.7     0.9    -1.1      -3     1.5    -2.5     0.3     4.2
//
H NAOD960101
D Substitution matrix derived from the single residue interchanges at spatially
  conserved regions of proteins (Naor et al., 1996)
R PMID:8601843
A Naor, D., Fischer, D., Jernigan, R.L., Wolfson, H.J. and Nussinov, R.
T Amino Acid Pair Interchanges at Spatially Conserved Locations (Naor et al)
J Journal of Molecular Biology 256, 924-938 (1996)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       4
       0       7
       0       4       8
       0       4       8      11
       2      -5      -5      -4      14
       0       5       5       6      -4       7
       0       8       6       7      -6       8      11
       0       0       5       4       0       0       0      12
      -1       3       2       3      -2       1       2       3       5
      -2      -7      -9      -9       4      -7      -9      -7      -3      10
       0      -5      -7      -8       2      -5      -6      -6      -3       7       9
       0       9       6       7      -7       7       9       0       1      -9      -7      13
       0      -2      -3      -4       2      -2      -2      -3      -1       3       5      -4       4
      -1      -5      -6      -6       3      -5      -6      -3      -2       6       6      -7       3       6
       0       1       6       6      -1       1       0       6       2      -8      -8       3      -6      -4      19
       0       2       4       4      -3       2       3       4       2      -5      -5       3      -3      -4       3       5
       0       1       2       2      -2       1       3       0       0      -3      -3       2      -2      -2       1       2       3
       0      -3      -4      -4       0      -2      -3      -1      -1       4       2      -5       1       3      -5      -2       0       9
       0      -2      -2      -3       0      -1      -2      -1       0       2       1      -3       1       2      -3      -1       0       2       3
      -2      -6      -8      -9       4      -8      -9      -5      -2       9       5      -8       2       5      -5      -4      -1       4       2       9
//
H RUSR970101
D Substitution matrix based on structural alignments of analogous proteins
  (Russell et al., 1997)
R PMID:9199410
A Russell, R.B., Saqi, M.A.S., Sayle, R.A., Bates, P.A. and Sternberg, M.J.E.
T Recognition of analogous and homologous protein folds: Analysis of sequence
  and structure conservation
J Journal of Molecular Biology 269, 423-439 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      -2
       1       0
       0       2       0
       0       3       2      -2
       2      -3      -4       0      12
       1      -2       2       3       2       0
       2       2       2       6      -8       6      -2
       1       2       3       3      -1      -1       3       0
      -1       2       7       2       5       0     -11      -5      -3
       1       1      -4      -4      -1       1      -4       0       1       2
       3      -2       0      -1       4      -2      -1      -2       3       3      -3
       1       4       1       0      -1       3       2       2       2      -4       0       0
       4      -5      -1      -1       3      -1      -3       1       3       1       8       1      -9
      -1       5       1      -3      -1      -6      -4      -1       0       5       3       0       0      -3
       2       1       0       3      -1       1       1       0       2       2       0       4     -17       4      -1
       0       2       5       3      -5       0       2       4       1      -1      -1       0      -3      -2       5     -10
       1       0       1       3       2       3       2       0       5       0      -3      -2       3       3      -1       4       0
      -4      -5      -3      -4       1      -1      -1       0       2       2       4       3       0      11       2       0       3       5
       1       3      -3       0       0       2      -2       1       3       3       3       0       4       0      -3       2       1     -12      -4
      -1      -4      -1      -2       7       2      -3      -3       0       4       6       0       3       5      -1       1       0       2       3      -1
//
H RUSR970102
D Substitution matrix based on structural alignments of remote homolous proteins
  (Russell et al., 1997)
R PMID:919941
A Russell, R.B., Saqi, M.A.S., Sayle, R.A., Bates, P.A. and Sternberg, M.J.E.
T Recognition of analogous and homologous protein folds: Analysis of sequence and
  structure conservation
J Journal of Molecular Biology 269, 423-439 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       0
       0       4
       0       0       3
      -1       0       5       5
       2      -1       0      -1      13
      -1       3       2       3      -6       4
       0       2       0       5      -4       2       3
       1       0       1       1      -1       0      -1       6
      -2       2       4       2       1       4       3      -1      11
       0       0      -8      -7       1      -3      -3      -4      -4       1
       0      -2      -2      -7       2      -5      -2      -4       0       7       2
       1       6       1       1       0       4       4       0       1      -6      -4       2
       0       0      -3      -6       1       0      -3      -3       1       5       6      -1       3
       0      -3      -1      -6       3      -2      -5      -6       0       4       4      -4       4       5
       0      -1       2       1      -1       0       2       0       1      -2      -5       0      -3      -1       7
       2       0       3       2      -1       4       1       0      -4      -4      -2       0      -2       0       2       0
       0       0       4       1      -2      -2       0       0       1       0       0       2       2      -2       1       4       0
      -1       2       0      -5       2      -3      -2      -2       0       3       0      -2       3       4      -2       1      -4      16
       0       2       0      -2       4       1      -1      -1       2       0       0       0       1       7       0       0      -1       8       3
       1      -1      -3      -3       2      -1      -2      -2      -3       7       3      -2       3       3       0      -1       0      -2       1       0
//
H RUSR970103
D Substitution matrix based on structural alignments of analogous and remote homolous
  proteins (Russell et al., 1997)
R PMID:9199410
A Russell, R.B., Saqi, M.A.S., Sayle, R.A., Bates, P.A. and Sternberg, M.J.E.
T Recognition of analogous and homologous protein folds: Analysis of sequence and
  structure conservation
J Journal of Molecular Biology 269, 423-439 (1997)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      -2
       1       0
       0       0       0
      -1       0       1       0
       2      -4      -1       0      12
       0       1       3       3      -4       0
       1       2       0       4      -8       4       0
       0       1       2       2       0       0       1       1
       0       3       3       3       2       0      -1      -3       1
       1       1      -7      -3      -4       0      -3      -1      -1       0
       2      -2       0      -3       2      -2       0      -2       2       5       0
       1       3       0       2       2       4       3       1       3      -5      -2      -1
       2       0      -3      -2       1       0      -1       0       3       4       6       0      -5
       0      -1       1      -4       3      -3      -5      -3       0       4       4      -1       0       0
       0       0       1       3       0       0       1       1       2       0      -2       1       0       1       0
       0       0       4       2      -3       1       2       0      -1      -3       0       0      -4       0       5      -3
       0       0       3       2       0       0       1       0       3       0      -1       1       2       0       1       3      -2
       0       0      -1      -5       2      -1      -3      -1       0       4       1       0       3       5       2       2       0       7
       0       3       0      -1       1       0      -1       0       1       2       0       0       1       5      -1       0       0       4      -1
       0       0       0      -1       5       0      -2      -1      -1       5       4       0       1       3      -1       0       0       0       2      -2
//
H OGAK980101
D Substitution matrix derived from structural alignments by maximizing entropy
  (Ogata et al., 1998)
R PMID:10522237
A Ogata, K., Ohya, M. and Umeyama, H.
T Amino acid similarity matrix for homology modeling derived from structural
  alignment and optimized by the Monte Carlo method
J Journal of Molecular Graphics and Modelling 16, 178-254 (1998)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
    -4.8
    -7.0    -6.2
    -7.1    -7.3    -4.8
    -6.9    -7.3    -6.3    -5.0
    -7.7    -8.3    -8.6    -8.3    -3.2
    -7.0    -7.5    -7.1    -7.3    -8.3    -6.5
    -6.7    -7.5    -6.5    -6.4   -10.2    -6.8    -5.4
    -5.8    -7.5    -6.8    -6.3    -7.5    -7.6    -7.4    -4.2
    -7.7    -8.1    -6.8    -8.1    -9.3    -7.7    -7.8    -7.7    -6.1
    -7.1    -7.7    -7.6    -8.3    -9.0    -7.9    -8.3    -8.0    -8.2    -5.5
    -6.7    -7.9    -7.7    -7.1    -7.7    -7.4    -7.4    -8.0    -8.1    -5.5    -4.0
    -6.7    -6.6    -6.8    -6.9    -8.5    -6.7    -6.7    -6.8    -7.6    -8.1    -7.2    -5.5
    -8.0    -7.8    -7.4    -8.2    -8.7    -8.5    -8.1    -8.2    -9.7    -7.4    -7.0    -8.2    -6.7
    -7.9    -8.1    -8.2    -9.5    -8.9    -8.6    -8.2    -8.1    -8.2    -7.2    -6.6    -8.8    -8.5    -5.7
    -6.8    -7.9    -8.0    -7.3    -8.3    -8.1    -7.8    -7.2    -7.5    -7.2    -6.6    -7.5    -8.8    -8.8    -5.7
    -5.6    -6.9    -6.5    -5.7    -8.2    -7.0    -6.6    -6.3    -7.0    -7.2    -6.4    -6.6    -7.5    -8.3    -6.8    -4.6
    -6.2    -6.8    -6.4    -6.5    -7.5    -7.0    -6.8    -6.7    -8.0    -7.1    -6.2    -6.3    -7.3    -7.7    -6.7    -5.5    -5.0
    -9.0    -9.4    -8.6    -9.8   -12.0    -8.3    -7.9    -7.2    -9.7    -7.7    -6.8    -9.5    -7.2    -6.9   -10.4    -7.6    -7.6    -5.0
    -7.5    -8.4    -7.0    -7.2   -10.6    -7.3    -7.5    -7.5    -6.8    -7.4    -6.6    -7.3    -7.9    -6.0    -8.1    -7.3    -6.8    -6.5    -4.7
    -5.9    -7.4    -7.2    -7.1    -8.1    -7.5    -7.3    -7.3    -7.5    -5.7    -5.8    -6.7    -7.2    -7.1    -7.5    -6.8    -6.2    -7.8    -7.2    -4.8
//
H KANM000101
D Substitution matrix (OPTIMA) derived by maximizing discrimination between
  homologs and non-homologs (Kann et al., 2000)
R PMID:11056037
A Kann, M., Qian, B. and Goldstein, R.A.
T Optimization of a new score function for the detection of remote homologs
J Proteins: Structure, Function, and Genetics 41, 498-503 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
      36
      -9      56
     -19       4      59
     -20     -18      18      65
       6     -29     -30     -30      99
      -3      12       2       2     -30      46
     -10       3       3      20     -39      19      40
       4     -18       7     -10     -29     -20     -23      67
     -19       3      12      -7     -29       3       2     -18      86
      -5     -28     -32     -34      -6     -30     -33     -41     -28      35
      -7     -20     -32     -43      -6     -23     -31     -42     -27      28      32
     -10      31       1      -4     -29      15      14     -18      -7     -31     -21      37
      -9     -10     -19     -30      -8       1     -21     -30     -19      12      24     -12      51
     -19     -30     -29     -33     -18     -29     -32     -32      -8       8      17     -29       2      57
      -5     -18     -17      -7     -30     -11      -7     -18     -18     -30     -33     -10     -21     -39      74
      12     -11      10       4     -10       0      -1       2      -9     -20     -22       3     -10     -19      -8      36
       0      -8       0     -10      -7      -7      -6     -17     -20      -8     -13      -8      -7     -18     -11      18      48
     -29     -29     -39     -40     -18     -19     -29     -19     -18     -28     -15     -30      -8      14     -38     -29     -19     110
     -19     -15     -19     -20     -18      -9     -21     -29      20      -8      -2     -17      -9      37     -28     -19     -17      22      69
       6     -32     -31     -31      -6     -19     -28     -30     -29      35      18     -23      10       0     -18     -22       6     -28      -9      38
//
H NGPC000101
D Substitution matrix (PHAT) built from hydrophobic and transmembrane regions
  of the Blocks database (Ng et al., 2000)
R PMID:11108698
A Ng, P.C., Henikoff, J.G. and Henikoff, S.
T PHAT: a transmembrane-specific substitution matrix
J Bioinformatics 16, 760-766 (2000)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       5
      -6       9
      -2      -3      11
      -5      -7       2      12
       1      -8      -2      -7       7
      -3      -2       2       0      -5       9
      -5      -6       0       6      -7       1      12
       1      -5      -1      -2      -2      -2      -3       9
      -3      -4       4      -1      -7       2      -1      -4      11
       0      -6      -3      -5      -3      -3      -5      -2      -5       5
      -1      -6      -3      -5      -2      -3      -5      -2      -4       2       4
      -7      -1      -2      -5     -10      -1      -4      -5      -5      -7      -7       5
      -1      -6      -2      -5      -2      -1      -5      -1      -4       3       2      -6       6
      -1      -7      -1      -5       0      -2      -5      -2      -2       0       1      -7       0       6
      -3      -7      -4      -5      -8      -3      -5      -3      -6      -4      -5      -4      -5      -5      13
       2      -6       1      -4       1      -1      -3       1      -2      -2      -2      -5      -2      -2      -3       6
       0      -6      -1      -5      -1      -3      -5      -1      -4      -1      -1      -6       0      -2      -4       1       3
      -4      -7      -5      -7      -4       1      -7      -5      -3      -4      -3      -8      -4       0      -6      -5      -7      11
      -3      -6       2      -4      -1       0      -2      -3       3      -3      -2      -4      -2       4      -5      -2      -3       1      11
       1      -7      -3      -5      -2      -3      -5      -2      -5       3       1      -8       1      -1      -4      -2       0      -4      -3       4
//
H MUET010101
D Non-symmetric substitution matrix (SLIM) for detection of homologous
  transmembrane proteins (Mueller et al., 2001)
R PMID:11473008
A Mueller, T., Rahmann, S. and Rehmsmeier, M.
T Non-symmetric score matrices and the detection of homologous transmembrane
  proteins
J Bioinformatics 17 Suppl 1, S182-S189 (2001)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
     5.0
    -5.5    10.0
    -3.0    -4.5     8.0
    -6.5    -9.5    -0.5     9.0
     2.5    -5.0    -2.5    -7.5    11.0
    -4.0    -2.5    -1.0    -2.5    -3.5     7.0
    -7.0    -9.0    -4.5     2.0    -7.0    -2.5     7.0
     0.5    -5.5    -3.0    -4.5    -1.5    -3.5    -6.5     7.0
    -3.0    -4.5     2.5    -3.5    -5.0    -0.5    -3.0    -5.5    10.0
     0.0    -5.5    -4.0    -6.5    -0.5    -3.5    -7.0    -2.5    -4.0     6.0
     0.0    -4.5    -3.5    -6.0     1.0    -3.5    -7.0    -2.0    -4.0     3.5     5.0
    -5.5    -0.5    -3.5    -5.0    -7.0    -2.0    -7.5    -4.5    -5.5    -5.5    -6.0     6.0
     0.0    -4.0    -3.0    -6.0     1.0    -1.5    -6.0    -1.5    -4.0     4.0     4.0    -5.5     7.0
     0.0    -5.5    -2.0    -5.5     2.5    -2.0    -5.5    -1.0    -1.0     1.5     2.5    -5.5     2.5     8.0
    -4.0    -8.0    -6.0    -7.0    -9.0    -6.0    -7.0    -4.5    -8.0    -4.0    -5.0    -4.5    -5.0    -4.5    11.0
     2.0    -6.0     0.5    -5.5     3.0    -2.5    -5.0     0.5    -2.5    -1.5    -1.5    -5.0    -1.0    -0.5    -4.0     6.0
     1.5    -5.0    -1.5    -5.5     1.0    -3.5    -6.5    -1.5    -3.5     0.5     0.5    -5.0     1.5     0.0    -3.5     1.5     4.0
    -2.5    -4.5    -4.0    -6.5    -0.5     1.0    -6.0    -4.0    -1.0    -1.5    -0.5    -5.5    -0.5     3.5    -4.5    -3.0    -4.5    15.0
    -3.5    -5.5     0.0    -5.5     0.5    -2.0    -5.5    -3.5     2.5    -2.5    -1.5    -3.5    -1.5     5.0    -5.5    -2.0    -2.5     2.0    11.0
     1.5    -6.0    -4.5    -6.0     1.0    -3.5    -6.5    -2.5    -4.5     4.5     2.5    -7.0     2.5     1.0    -4.0    -1.0     1.0    -2.0    -2.5     5.0
//
H MUET020101
D Substitution matrix (VTML160) obtained by maximum likelihood estimation
  (Mueller et al., 2002)
R PMID:11752185
A Mueller, T., Spang, R. and Vingron, M.
T Estimating amino acid substitution models: A comparison of Dayhoff's
  estimator, the resolvent approach and a maximum likelihood method
J Molecular Biology and Evolution 19, 8-13 (2002)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       5
      -2       7
      -1       0       7
      -1      -3       3       7
       1      -3      -3      -5      13
      -1       2       0       1      -4       6
      -1      -1       0       3      -5       2       6
       0      -3       0      -1      -2      -3      -2       8
      -2       1       1       0      -2       2      -1      -3       9
      -1      -4      -4      -6      -1      -4      -5      -7      -4       6
      -2      -3      -4      -6      -4      -2      -4      -6      -3       3       6
      -1       4       0       0      -4       2       1      -2       0      -4      -3       5
      -1      -2      -3      -5      -1      -1      -3      -5      -3       2       4      -2       8
      -3      -5      -5      -7      -4      -4      -6      -6       0       0       2      -5       1       9
       0      -2      -2      -1      -3      -1      -1      -3      -2      -4      -3      -1      -4      -5       9
       1      -1       1       0       1       0       0       0      -1      -3      -3      -1      -3      -3       0       4
       1      -1       0      -1       0      -1      -1      -2      -1      -1      -2      -1      -1      -3      -1       2       5
      -5      -4      -5      -7      -7      -6      -7      -5      -1      -2      -1      -5      -4       3      -5      -4      -6      16
      -3      -3      -2      -5      -1      -4      -3      -5       3      -2      -1      -3      -2       6      -6      -2      -3       4      10
       0      -4      -4      -4       1      -3      -3      -5      -3       4       2      -3       1      -1      -3      -2       0      -5      -3       5
//
H MUET020102
D Substitution matrix (VTML250) obtained by maximum likelihood estimation
  (Mueller et al., 2002)
R 11752185
A Mueller, T., Spang, R. and Vingron, M.
T Estimating amino acid substitution models: A comparison of Dayhoff's
  estimator, the resolvent approach and a maximum likelihood method
J Molecular Biology and Evolution 19, 8-13 (2002)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       2
      -1       5
       0       0       4
       0      -1       2       5
       1      -2      -1      -3      11
       0       2       1       1      -2       3
       0       0       1       3      -3       2       4
       1      -1       0       0      -1      -1      -1       7
      -1       1       1       0      -1       1       0      -1       6
      -1      -2      -3      -4       0      -2      -3      -4      -2       4
      -1      -2      -3      -4      -2      -2      -3      -4      -2       3       4
      -1       3       1       0      -2       2       1      -1       0      -2      -2       3
      -1      -1      -2      -3       0      -1      -2      -3      -2       2       3      -1       4
      -2      -3      -3      -5      -2      -2      -4      -4       0       1       2      -3       1       7
       0      -1      -1       0      -2       0       0      -1      -1      -3      -2       0      -2      -3       7
       1       0       1       0       1       0       0       0       0      -2      -2       0      -1      -2       0       2
       1      -1       0       0       0       0       0      -1       0       0      -1       0       0      -2       0       1       3
      -3      -3      -4      -5      -4      -4      -5      -4       0      -1       0      -3      -2       3      -3      -3      -4      14
      -2      -2      -1      -3       0      -2      -2      -4       2      -1       0      -2      -1       5      -4      -1      -2       4       8
       0      -2      -2      -3       1      -2      -2      -3      -2       3       2      -2       2       0      -2      -1       0      -3      -1       3
//
H CROG050101
D Substitution matrix computed from the Dirichlet Mixture Model
  (Crooks-Brenner, 2005)
R PMID:15531614
A Crooks, G.E. and Brenner, S.E.
T An alternative model of amino acid replacement
J Bioinformatics 21, 975-980 (2005)
M rows = ARNDCQEGHILKMFPSTWYV, cols = ARNDCQEGHILKMFPSTWYV
       4
      -2       6
      -2      -1       7
      -2      -1       1       7
       0      -4      -3      -4      12
      -1       1       0       0      -3       6
      -1       0       0       1      -4       1       5
      -1      -3      -1      -1      -3      -2      -2       7
      -2       0       0      -1      -3       0      -1      -2       9
      -2      -3      -5      -6      -1      -3      -4      -6      -3       5
      -2      -3      -4      -5      -2      -3      -4      -5      -3       2       5
      -2       2       0       0      -4       1       1      -2      -1      -4      -3       5
      -1      -2      -3      -4      -1      -2      -3      -4      -2       1       2      -2       7
      -2      -3      -4      -5      -2      -3      -4      -5      -1       0       1      -4       1       7
      -1      -2      -2      -1      -3      -1      -1      -2      -2      -4      -3      -1      -3      -3       8
       0      -1       0       0      -2       0      -1      -1      -1      -4      -3      -1      -2      -3      -1       4
      -1      -1      -1      -1      -1      -1      -1      -2      -1      -2      -2      -1      -1      -2      -2       1       5
      -3      -2      -3      -4      -2      -2      -3      -4       0      -1      -1      -3       0       3      -3      -3      -2      12
      -2      -2      -2      -3      -2      -2      -3      -4       0      -1      -1      -3       0       3      -3      -2      -2       3       8
      -1      -3      -4      -5       0      -3      -4      -5      -3       3       1      -3       1       0      -3      -3      -1      -2      -2       5
//
