DrLLPS - Data resource of LLPS

Compute pI/Mw
AAindex

Compute pI/Mw
Isoelectric Point	Molecular Weight
5.27	104854.04

AAindex
Physicochemical Property	A	L	R	K	N	M	D	F	C	P	Q	S	E	T	G	W	H	Y	I	V
Alpha-ch chemical shifts	4.35	4.17	4.38	4.36	4.75	4.52	4.76	4.66	4.65	4.44	4.37	4.50	4.29	4.35	3.97	4.70	4.63	4.60	3.95	3.95
Hydrophobicity index	0.61	1.53	0.60	1.15	0.06	1.18	0.46	2.02	1.07	1.95	0	0.05	0.47	0.05	0.07	2.65	0.61	1.88	2.22	1.32
Signal sequence helical potential	1.18	3.23	0.20	0.06	0.23	2.67	0.05	1.96	1.89	0.76	0.72	0.97	0.11	0.84	0.49	0.77	0.31	0.39	1.45	1.08
Membrane-buried preference parameters	1.56	2.93	0.45	0.15	0.27	2.96	0.14	2.03	1.23	0.76	0.51	0.81	0.23	0.91	0.62	1.08	0.29	0.68	1.67	1.14
Conformational parameter of inner helix	1	1	0.52	0.60	0.35	1	0.44	0.60	0.06	0.06	0.44	0.35	0.73	0.44	0.35	0.73	0.60	0.44	0.73	0.82
Conformational parameter of beta-structure	0.77	0.83	0.72	0.55	0.55	0.98	0.65	0.98	0.65	0.55	0.72	0.55	0.55	0.83	0.65	0.77	0.83	0.83	0.98	0.98
Conformational parameter of beta-turn	0.37	0.53	0.84	0.75	0.97	0.64	0.97	0.53	0.84	0.97	0.64	0.84	0.53	0.75	0.97	0.97	0.75	0.84	0.37	0.37
Average flexibility indices	0.357	0.365	0.529	0.466	0.463	0.295	0.511	0.314	0.346	0.509	0.493	0.507	0.497	0.444	0.544	0.305	0.323	0.420	0.462	0.386
Residue volume	52.6	102.0	109.1	105.1	75.7	97.7	68.4	113.9	68.3	73.6	89.7	54.9	84.7	71.2	36.3	135.4	91.9	116.2	102.0	85.1
Information value for accessibility; average fraction 35%	16	145	-70	-141	-74	124	-78	189	168	-20	-73	-70	-106	-38	-13	145	50	53	151	123
Information value for accessibility; average fraction 23%	44	108	-68	-188	-72	121	-91	148	90	-36	-117	-60	-139	-54	-8	163	47	22	100	117
Retention coefficient in TFA	7.3	20.0	-3.6	-3.7	-5.7	5.6	-2.9	19.2	-9.2	5.1	-0.3	-4.1	-7.1	0.8	-1.2	16.3	-2.1	5.9	6.6	3.5
Retention coefficient in HFBA	3.9	15.0	3.2	-2.5	-2.8	4.1	-2.8	14.7	-14.3	5.6	1.8	-3.5	-7.5	1.1	-2.3	17.8	2.0	3.8	11.0	2.1
Transfer free energy to surface	-0.20	-2.46	-0.12	-0.35	0.08	-1.47	-0.20	-2.33	-0.45	-0.98	0.16	-0.39	-0.30	-0.52	0	-2.01	-0.12	-2.24	-2.26	-1.56
Apparent partial specific volume	0.691	0.842	0.728	0.767	0.596	0.709	0.558	0.756	0.624	0.730	0.649	0.594	0.632	0.655	0.592	0.743	0.646	0.743	0.809	0.777
Alpha-nh chemical shifts	8.249	8.423	8.274	8.408	8.747	8.418	8.410	8.228	8.312	0	8.411	8.380	8.368	8.236	8.391	8.094	8.415	8.183	8.195	8.436
Alpha-ch chemical shifts	4.349	4.385	4.396	4.358	4.755	4.513	4.765	4.663	4.686	4.471	4.373	4.498	4.295	4.346	3.972	4.702	4.630	4.604	4.224	4.184
Spin-spin coupling constants 3JHalpha-NH	6.5	6.5	6.9	6.5	7.5	0	7.0	9.4	7.7	0	6.0	6.5	7.0	6.9	5.6	0	8.0	6.8	7.0	7.0
Normalized frequency of alpha-helix	0.486	0.420	0.262	0.402	0.193	0.417	0.288	0.318	0.200	0.208	0.418	0.200	0.538	0.272	0.120	0.462	0.400	0.161	0.370	0.379
Normalized frequency of extended structure	0.288	0.400	0.362	0.265	0.229	0.375	0.271	0.318	0.533	0.340	0.327	0.354	0.262	0.388	0.312	0.231	0.200	0.429	0.411	0.495
Steric parameter	0.52	0.98	0.68	0.68	0.76	0.78	0.76	0.70	0.62	0.36	0.68	0.53	0.68	0.50	0	0.70	0.70	0.70	1.02	0.76
Polarizability parameter	0.046	0.186	0.291	0.219	0.134	0.221	0.105	0.290	0.128	0.131	0.180	0.062	0.151	0.108	0.000	0.409	0.230	0.298	0.186	0.140
Free energy of solution in water, kcal/mole	-0.368	1.07	-1.03	0	0	0.656	2.06	1.06	4.53	-2.24	0.731	-0.524	1.77	0	-0.525	1.60	0	4.91	0.791	0.401
The Chou-Fasman parameter of the coil conformation	0.71	0.69	1.06	0.99	1.37	0.59	1.21	0.71	1.19	1.61	0.87	1.34	0.84	1.08	1.52	0.76	1.07	1.07	0.66	0.63
A parameter defined from the residuals obtained from the best correlation o	-0.118	-0.052	0.124	0.032	0.289	-0.258	0.048	0.015	0.083	0	-0.105	0.225	-0.245	0.166	0.104	0.158	0.138	0.094	0.230	0.513
The number of atoms in the side chain labelled 1+1	0	1	1	1	1	1	1	1	1	0	1	1	1	2	0	1	1	1	2	2
The number of atoms in the side chain labelled 2+1	0	2	1	1	1	1	1	1	0	0	1	0	1	0	0	1	1	1	1	0
The number of atoms in the side chain labelled 3+1	0	0	1	1	0	1	0	1	0	0	1	0	1	0	0	1.5	1	1	0	0
The number of bonds in the longest chain	0	2	5	4	2	3	2	4	1	0	3	1	3	1	0	5	3	5	2	1
A parameter of charge transfer capability	0	0	0	0	1	0	1	0	0	0	0	0	1	0	1	0	0	0	0	0
A parameter of charge transfer donor capability	0	0	1	1	1	1	0	1	1	0	1	0	0	0	0	1	1	1	0	0
Average volume of buried residue	91.5	167.9	202.0	171.3	135.2	170.8	124.5	203.4	117.7	129.3	161.1	99.1	155.1	122.1	66.4	237.6	167.3	203.6	168.8	141.7
Residue accessible surface area in tripeptide	115	170	225	200	160	185	150	210	135	145	180	115	190	140	75	255	195	230	175	155
Residue accessible surface area in folded protein	25	23	90	97	63	31	50	24	19	50	71	44	49	47	23	32	43	60	18	18
Proportion of residues 95% buried	0.38	0.45	0.01	0.03	0.12	0.40	0.15	0.50	0.45	0.18	0.07	0.22	0.18	0.23	0.36	0.27	0.17	0.15	0.60	0.54
Proportion of residues 100% buried	0.20	0.16	0	0	0.03	0.11	0.04	0.14	0.22	0.04	0.01	0.08	0.03	0.08	0.18	0.04	0.02	0.03	0.19	0.18
Normalized frequency of beta-turn	0.66	0.59	0.95	1.01	1.56	0.60	1.46	0.60	1.19	1.52	0.98	1.43	0.74	0.96	1.56	0.96	0.95	1.14	0.47	0.50
Normalized frequency of alpha-helix	1.42	1.21	0.98	1.16	0.67	1.45	1.01	1.13	0.70	0.57	1.11	0.77	1.51	0.83	0.57	1.08	1	0.69	1.08	1.06
Normalized frequency of beta-sheet	0.83	1.30	0.93	0.74	0.89	1.05	0.54	1.38	1.19	0.55	1.10	0.75	0.37	1.19	0.75	1.37	0.87	1.47	1.60	1.70
Normalized frequency of beta-turn	0.74	0.50	1.01	1.19	1.46	0.60	1.52	0.66	0.96	1.56	0.96	1.43	0.95	0.98	1.56	0.60	0.95	1.14	0.47	0.59
Normalized frequency of N-terminal helix	1.29	0.58	0.44	0.66	0.81	0.71	2.02	0.61	0.66	2.01	1.22	0.74	2.44	1.08	0.76	1.47	0.73	0.68	0.67	0.61
Normalized frequency of C-terminal helix	1.20	1.13	1.25	1.83	0.59	1.57	0.61	1.10	1.11	0	1.22	0.96	1.24	0.75	0.42	0.40	1.77	0.73	0.98	1.25
Normalized frequency of N-terminal non helical region	0.70	0.85	0.34	1.01	1.42	0.83	0.98	0.93	0.65	1.10	0.75	1.55	1.04	1.09	1.41	0.62	1.22	0.99	0.78	0.75
Normalized frequency of C-terminal non helical region	0.52	0.84	1.24	1.49	1.64	0.52	1.06	1.04	0.94	1.58	0.70	0.93	0.59	0.86	1.64	0.16	1.86	0.96	0.87	0.32
Normalized frequency of N-terminal beta-sheet	0.86	1.30	0.90	1	0.66	1.43	0.38	1.50	0.87	0.66	1.65	0.63	0.35	1.17	0.63	1.49	0.54	1.07	1.94	1.69
Normalized frequency of C-terminal beta-sheet	0.75	1.27	0.90	0.74	1.21	0.95	0.85	1.50	1.11	0.40	0.65	0.79	0.55	0.75	0.74	1.19	0.90	1.96	1.35	1.79
Normalized frequency of N-terminal non beta region	0.67	0.46	0.89	1.09	1.86	0.52	1.39	0.30	1.34	1.58	1.09	1.41	0.92	1.09	1.46	0.48	0.78	1.23	0.59	0.42
Normalized frequency of C-terminal non beta region	0.74	0.59	1.05	0.82	1.13	0.85	1.32	0.44	0.53	1.69	0.77	1.49	0.85	1.16	1.68	1.59	0.96	1.01	0.53	0.59
Frequency of the 1st residue in turn	0.060	0.061	0.070	0.055	0.161	0.068	0.147	0.059	0.149	0.102	0.074	0.120	0.056	0.086	0.102	0.077	0.140	0.082	0.043	0.062
Frequency of the 2nd residue in turn	0.076	0.025	0.106	0.115	0.083	0.082	0.110	0.041	0.053	0.301	0.098	0.139	0.060	0.108	0.085	0.013	0.047	0.065	0.034	0.048
Frequency of the 3rd residue in turn	0.035	0.036	0.099	0.072	0.191	0.014	0.179	0.065	0.117	0.034	0.037	0.125	0.077	0.065	0.190	0.064	0.093	0.114	0.013	0.028
Frequency of the 4th residue in turn	0.058	0.070	0.085	0.095	0.091	0.055	0.081	0.065	0.128	0.068	0.098	0.106	0.064	0.079	0.152	0.167	0.054	0.125	0.056	0.053
Normalized frequency of the 2nd and 3rd residues in turn	0.64	0.36	1.05	1.13	1.56	0.51	1.61	0.62	0.92	2.04	0.84	1.52	0.80	0.98	1.63	0.48	0.77	1.08	0.29	0.43
Normalized hydrophobicity scales for alpha-proteins	-0.45	1.29	-0.24	-0.36	-0.20	1.37	-1.52	1.48	0.79	-0.12	-0.99	-0.98	-0.80	-0.70	-1	1.38	1.07	1.49	0.76	1.26
Normalized hydrophobicity scales for beta-proteins	-0.08	1.24	-0.09	-0.09	-0.70	1.27	-0.71	1.53	0.76	-0.01	-0.40	-0.93	-1.31	-0.59	-0.84	2.25	0.43	1.53	1.39	1.09
Normalized hydrophobicity scales for alpha+beta-proteins	0.36	1.18	-0.52	-0.56	-0.90	1.21	-1.09	1.01	0.70	-0.06	-1.05	-0.60	-0.83	-1.20	-0.82	1.31	0.16	1.05	2.17	1.21
Normalized hydrophobicity scales for alpha/beta-proteins	0.17	0.96	-0.70	-0.62	-0.90	0.60	-1.05	1.29	1.24	-0.21	-1.20	-0.83	-1.19	-0.62	-0.57	1.51	-0.25	0.66	2.06	1.21
Normalized average hydrophobicity scales	0.02	1.14	-0.42	-0.41	-0.77	1	-1.04	1.35	0.77	-0.09	-1.10	-0.97	-1.14	-0.77	-0.80	1.71	0.26	1.11	1.81	1.13
Partial specific volume	0.75	0.90	0.70	0.82	0.61	0.75	0.60	0.77	0.61	0.76	0.67	0.68	0.66	0.70	0.64	0.74	0.67	0.71	0.90	0.86
Normalized frequency of middle helix	1.33	1.29	0.79	1.03	0.72	1.40	0.97	1.15	0.93	0.49	1.42	0.83	1.66	0.94	0.58	1.33	1.49	0.49	0.99	0.96
Normalized frequency of beta-sheet	1	1.53	0.74	1.18	0.75	1.40	0.89	1.26	0.99	0.36	0.87	0.65	0.37	1.15	0.56	0.84	0.36	1.41	1.75	1.61
Normalized frequency of turn	0.60	0.70	0.79	1.10	1.42	0.67	1.24	1.05	1.29	1.47	0.92	1.26	0.64	1.05	1.38	1.23	0.95	1.35	0.67	0.48
Size	2.5	5.5	7.5	7.0	5.0	6.0	2.5	6.5	3.0	5.5	6.0	3.0	5.0	5.0	0.5	7.0	6.0	7.0	5.5	5.0
Amino acid composition	8.6	7.4	4.9	6.6	4.3	1.7	5.5	3.6	2.9	5.2	3.9	7.0	6.0	6.1	8.4	1.3	2.0	3.4	4.5	6.6
Relative mutability	100	40	65	56	134	94	106	41	20	56	93	120	102	97	49	18	66	41	96	74
Membrane preference for cytochrome b: MPH89	1.56	1.38	0.59	0.15	0.51	1.93	0.23	1.42	1.80	0.27	0.39	0.96	0.19	1.11	1.03	0.91	1	1.10	1.27	1.58
Average membrane preference: AMP07	1.26	1.36	0.38	0.33	0.59	1.52	0.27	1.46	1.60	0.54	0.39	0.98	0.23	1.01	1.08	1.06	1	0.89	1.44	1.33
Consensus normalized hydrophobicity scale	0.25	0.53	-1.76	-1.10	-0.64	0.26	-0.72	0.61	0.04	-0.07	-0.69	-0.26	-0.62	-0.18	0.16	0.37	-0.40	0.02	0.73	0.54
Solvation free energy	0.67	1.9	-2.1	-0.57	-0.6	2.4	-1.2	2.3	0.38	1.2	-0.22	0.01	-0.76	0.52	0	2.6	0.64	1.6	1.9	1.5
Atom-based hydrophobic moment	0	1.0	10	5.7	1.3	1.9	1.9	1.1	0.17	0.18	1.9	0.73	3	1.5	0	1.6	0.99	1.8	1.2	0.48
Direction of hydrophobic moment	0	0.89	-0.96	-0.99	-0.86	0.94	-0.98	0.92	0.76	0.22	-1.0	-0.67	-0.89	0.09	0	0.67	-0.75	-0.93	0.99	0.84
Molecular weight	89.09	131.17	174.20	146.19	132.12	149.21	133.10	165.19	121.15	115.13	146.15	105.09	147.13	119.12	75.07	204.24	155.16	181.19	131.17	117.15
Melting point	297	337	238	224	236	283	270	284	178	222	185	228	249	253	290	282	277	344	284	293
Optical rotation	1.80	-11	12.50	14.60	-5.60	-10	5.05	-34.50	-16.50	-86.20	6.30	-7.50	12	-28	0	-33.70	-38.50	-10	12.40	5.63
pK-N	9.69	9.60	8.99	9.18	8.80	9.21	9.60	9.18	8.35	10.64	9.13	9.21	9.67	9.10	9.78	9.44	9.17	9.11	9.68	9.62
pK-C	2.34	2.36	1.82	2.16	2.02	2.28	1.88	2.16	1.92	1.95	2.17	2.19	2.10	2.09	2.35	2.43	1.82	2.20	2.36	2.32
Hydrophobic parameter pi	0.31	1.70	-1.01	-0.99	-0.60	1.23	-0.77	1.79	1.54	0.72	-0.22	-0.04	-0.64	0.26	0	2.25	0.13	0.96	1.80	1.22
Graph shape index	1.28	2.59	2.34	1.89	1.60	2.35	1.60	2.94	1.77	2.67	1.56	1.31	1.56	3.03	0	3.21	2.99	2.94	4.19	3.67
Smoothed upsilon steric parameter	0.53	0.92	0.69	0.78	0.58	0.77	0.59	0.71	0.66	0	0.71	0.55	0.72	0.63	0	0.84	0.64	0.71	0.96	0.89
Normalized van der Waals volume	1	4	6.13	4.77	2.95	4.43	2.78	5.89	2.43	2.72	3.95	1.60	3.78	2.60	0	8.08	4.66	6.47	4	3
STERIMOL length of the side chain	2.87	4.92	7.82	6.89	4.58	6.36	4.74	4.62	4.47	4.11	6.11	3.97	5.97	4.11	2.06	7.68	5.23	4.73	4.92	4.11
STERIMOL minimum width of the side chain	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.52	1.73	1	1.52	1.52	1.52	1.90	1.90
STERIMOL maximum width of the side chain	2.04	4.45	6.24	4.87	4.37	4.80	3.78	6.02	3.41	4.31	3.53	2.70	3.31	3.17	1	5.90	5.66	6.72	3.49	3.17
N.m.r. chemical shift of alpha-carbon	7.3	10.1	11.1	10.9	8.0	10.4	9.2	13.9	14.4	17.8	10.6	13.1	11.4	16.7	0.0	13.2	10.2	13.9	16.1	17.2
Localized electrical effect	-0.01	-0.01	0.04	0	0.06	0.04	0.15	0.03	0.12	0	0.05	0.11	0.07	0.04	0	0	0.08	0.03	-0.01	0.01
Number of hydrogen bond donors	0	0	4	2	2	0	1	0	0	0	2	1	1	1	0	1	1	1	0	0
Number of full nonbonding orbitals	0	0	3	1	3	0	4	0	0	0	3	2	4	2	0	0	1	2	0	0
Positive charge	0	0	1	1	0	0	0	0	0	0	0	0	0	0	0	0	1	0	0	0
Negative charge	0	0	0	0	0	0	1	0	0	0	0	0	1	0	0	0	0	0	0	0
pK-	4.76	4.79	4.30	4.27	3.64	4.25	5.69	4.31	3.67	0	4.54	3.83	5.48	3.87	3.77	4.75	2.84	4.30	4.81	4.86
Helix-coil equilibrium constant	1.08	1.25	1.05	1.15	0.85	1.15	0.85	1.10	0.95	0.71	0.95	0.75	1.15	0.75	0.55	1.10	1	1.10	1.05	0.95
Helix initiation parameter at posision i-1	1	1	0.70	0.70	1.70	1	3.20	1	1	1	1	1.70	1.70	1.70	1	1	1	1	0.60	0.60
Helix initiation parameter at posision i, i+1, i+2	1	1	0.70	0.70	1	1	1.70	1	1	13	1	1	1.70	1	1.30	1	1	1	1	1
Helix termination parameter at posision j-2, j-1, j	1.20	1	1.70	1.70	1.20	1	0.70	1	1	1	1	1.50	0.70	1	0.80	1	1.20	1	0.80	0.80
Helix termination parameter at posision j+1	1	1	1.70	1.70	1	1	0.70	1	1	0.10	1	1	0.70	1	1.50	1	1	1	1	1
Partition coefficient	0.28	1	0.10	0.09	0.25	0.74	0.21	2.18	0.28	0.39	0.35	0.12	0.33	0.21	0.17	5.70	0.21	1.26	0.82	0.60
Alpha-helix indices	1.29	1.31	1	1.33	0.81	1.54	1.10	1.13	0.79	0.63	1.07	0.78	1.49	0.77	0.63	1.18	1.33	0.71	1.05	0.81
Alpha-helix indices for alpha-proteins	1.13	1.13	1.09	1.08	1.06	1.23	0.94	1.01	1.32	0.82	0.93	1.01	1.20	1.17	0.83	1.32	1.09	0.88	1.05	1.13
Alpha-helix indices for beta-proteins	1.55	1.25	0.20	1.20	1.20	1.37	1.55	0.40	1.44	0.21	1.13	1.01	1.67	0.55	0.59	1.86	1.21	1.08	1.27	0.64
Alpha-helix indices for alpha/beta-proteins	1.19	1.18	1	1.27	0.94	1.49	1.07	1.02	0.95	0.68	1.32	0.81	1.64	0.85	0.60	1.18	1.03	0.77	1.12	0.74
Beta-strand indices	0.84	1.10	1.04	0.86	0.66	0.88	0.59	1.15	1.27	0.80	1.02	1.05	0.57	1.20	0.94	1.15	0.81	1.39	1.29	1.56
Beta-strand indices for beta-proteins	0.86	1.28	1.15	1.01	0.60	1.15	0.66	1.34	0.91	0.61	1.11	0.91	0.37	1.14	0.86	1.13	1.07	1.37	1.17	1.31
Beta-strand indices for alpha/beta-proteins	0.91	1.23	0.99	0.86	0.72	0.96	0.74	1.26	1.12	0.65	0.90	0.93	0.41	1.05	0.91	1.15	1.01	1.21	1.29	1.58
Aperiodic indices	0.91	0.59	1	0.82	1.64	0.58	1.40	0.72	0.93	1.66	0.94	1.23	0.97	1.04	1.51	0.67	0.90	0.92	0.65	0.60
Aperiodic indices for alpha-proteins	0.80	0.80	0.96	0.94	1.10	0.39	1.60	1.20	0	2.10	1.60	1.30	0.40	0.60	2	0	0.96	1.80	0.85	0.80
Aperiodic indices for beta-proteins	1.10	0.52	0.93	0.94	1.57	0.69	1.41	0.60	1.05	1.77	0.81	1.13	1.40	0.88	1.30	0.62	0.85	0.41	0.67	0.58
Aperiodic indices for alpha/beta-proteins	0.93	0.59	1.01	0.91	1.36	0.60	1.22	0.71	0.92	1.67	0.83	1.25	1.05	1.08	1.45	0.68	0.96	0.98	0.58	0.62
Hydrophobicity factor	0.75	2.40	0.75	1.50	0.69	1.30	0	2.65	1	2.60	0.59	0	0	0.45	0	3	0	2.85	2.95	1.70
Residue volume	88.3	168.5	181.2	175.6	125.1	162.2	110.8	189.0	112.4	122.2	148.7	88.7	140.5	118.2	60.0	227.0	152.6	193.0	168.5	141.4
Composition	0	0	0.65	0.33	1.33	0	1.38	0	2.75	0.39	0.89	1.42	0.92	0.71	0.74	0.13	0.58	0.20	0	0
Polarity	8.1	4.9	10.5	11.3	11.6	5.7	13.0	5.2	5.5	8.0	10.5	9.2	12.3	8.6	9.0	5.4	10.4	6.2	5.2	5.9
Volume	31	111	124	119	56	105	54	132	55	32.5	85	32	83	61	3	170	96	136	111	84
Partition energy	0.10	-1.18	1.91	1.40	0.48	-1.59	0.78	-2.12	-1.42	0.73	0.95	0.52	0.83	0.07	0.33	-0.51	-0.50	-0.21	-1.13	-1.27
Hydration number	1.0	0.8	2.3	5.3	2.2	0.7	6.5	1.4	0.1	0.9	2.1	1.7	6.2	1.5	1.1	1.9	2.8	2.1	0.8	0.9
Hydrophilicity value	-0.5	-1.8	3.0	3.0	0.2	-1.3	3.0	-2.5	-1.0	0.0	0.2	0.3	3.0	-0.4	0.0	-3.4	-0.5	-2.3	-1.8	-1.5
Heat capacity	29.22	48.03	26.37	57.10	38.30	69.32	37.09	48.52	50.70	36.13	44.02	32.40	41.84	35.20	23.71	56.92	59.64	51.73	45	40.35
Absolute entropy	30.88	50.62	68.43	63.21	41.70	55.32	40.66	51.06	53.83	39.21	46.62	35.65	44.98	36.50	24.74	60	65.99	51.15	49.71	42.75
Entropy of formation	154.33	232.30	341.01	300.46	207.90	202.65	194.91	204.74	219.79	179.93	235.51	174.06	223.16	205.80	127.90	237.01	242.54	229.15	233.21	207.60
Normalized relative frequency of alpha-helix	1.53	1.32	1.17	1.26	0.60	1.66	1	1.22	0.89	0.25	1.27	0.65	1.63	0.86	0.44	1.05	1.03	0.70	1.07	0.93
Normalized relative frequency of extended structure	0.86	1.01	0.98	0.77	0.74	1.06	0.69	1.16	1.39	1.16	0.89	1.09	0.66	1.24	0.70	1.17	1.06	1.28	1.31	1.40
Normalized relative frequency of bend	0.78	0.57	1.06	1.01	1.56	0.30	1.50	0.67	0.60	1.55	0.78	1.19	0.97	1.09	1.73	0.74	0.83	1.14	0.40	0.44
Normalized relative frequency of bend R	1.09	0.44	0.97	1.25	1.14	0.45	0.77	0.50	0.50	2.96	0.83	1.21	0.92	1.33	1.25	0.62	0.67	0.94	0.66	0.56
Normalized relative frequency of bend S	0.35	0.58	0.75	0.83	2.12	0.22	2.16	0.89	0.50	0.43	0.73	1.24	0.65	0.85	2.40	0.62	1.19	1.44	0.12	0.43
Normalized relative frequency of helix end	1.09	1.30	1.07	1.20	0.88	0.55	1.24	0.80	1.04	1.78	1.09	1.20	1.14	0.99	0.27	1.03	1.07	0.69	0.97	0.77
Normalized relative frequency of double bend	1.34	1.05	2.78	0.79	0.92	0	1.77	0.43	1.44	0.37	0.79	0.87	2.54	1.14	0.95	1.79	0	0.73	0.52	0
Normalized relative frequency of coil	0.47	0.53	0.52	0.98	2.16	0.68	1.15	0.61	0.41	0.63	0.95	1.03	0.64	0.39	3.03	0.63	0.89	0.83	0.62	0.76
Average accessible surface area	27.8	27.6	94.7	103.0	60.1	33.5	60.6	25.5	15.5	51.5	68.7	42.0	68.2	45.0	24.5	34.7	50.7	55.2	22.8	23.7
Percentage of buried residues	51	60	5	3	22	52	19	58	74	25	16	35	16	30	52	49	34	24	66	64
Percentage of exposed residues	15	16	67	85	49	20	50	10	5	45	56	32	55	32	10	17	34	41	13	14
Ratio of buried and accessible molar fractions	1.7	2.4	0.1	0.05	0.4	1.9	0.4	2.2	4.6	0.6	0.3	0.8	0.3	0.7	1.8	1.6	0.8	0.5	3.1	2.9
Transfer free energy	0.3	0.5	-1.4	-1.8	-0.5	0.4	-0.6	0.5	0.9	-0.3	-0.7	-0.1	-0.7	-0.2	0.3	0.3	-0.1	-0.4	0.7	0.6
Hydrophobicity	0.87	2.17	0.85	1.64	0.09	1.67	0.66	2.87	1.52	2.77	0	0.07	0.67	0.07	0.10	3.77	0.87	2.67	3.15	1.87
pK	2.34	2.36	1.18	2.18	2.02	2.28	2.01	1.83	1.65	1.99	2.17	2.21	2.19	2.10	2.34	2.38	1.82	2.20	2.36	2.32
Relative frequency of occurrence	0.077	0.091	0.051	0.059	0.043	0.024	0.052	0.040	0.020	0.051	0.041	0.069	0.062	0.059	0.074	0.014	0.023	0.032	0.053	0.066
Relative mutability	100	54	83	72	104	93	86	51	44	58	84	117	77	107	50	25	91	50	103	98
Amino acid distribution	5.3	4.7	2.6	4.1	3.0	1.1	3.6	2.3	1.3	2.5	2.4	4.5	3.3	3.7	4.8	0.8	1.4	2.3	3.1	4.2
Sequence frequency	685	581	382	575	397	132	400	303	241	366	313	593	427	490	707	99	155	292	394	553
Average relative probability of helix	1.36	1.21	1	1.22	0.89	1.45	1.04	1.05	0.82	0.52	1.14	0.74	1.48	0.81	0.63	0.97	1.11	0.79	1.08	0.94
Average relative probability of beta-sheet	0.81	1.24	0.85	0.77	0.62	1.05	0.71	1.20	1.17	0.61	0.98	0.92	0.53	1.18	0.88	1.18	0.92	1.23	1.48	1.66
Average relative probability of inner helix	1.45	1.56	1.15	1.27	0.64	1.83	0.91	1.20	0.70	0.21	1.14	0.48	1.29	0.77	0.53	1.17	1.13	0.74	1.23	1.10
Average relative probability of inner beta-sheet	0.75	1.56	0.79	0.66	0.33	0.86	0.31	1.37	1.46	0.52	0.75	0.82	0.46	1.36	0.83	0.79	0.83	1.08	1.87	2
Flexibility parameter for no rigid neighbors	1.041	0.967	1.038	1.093	1.117	0.947	1.033	0.930	0.960	1.055	1.165	1.169	1.094	1.073	1.142	0.925	0.982	0.961	1.002	0.982
Flexibility parameter for one rigid neighbor	0.946	0.961	1.028	1.082	1.006	0.862	1.089	0.912	0.878	1.085	1.025	1.048	1.036	1.051	1.042	0.917	0.952	0.930	0.892	0.927
Flexibility parameter for two rigid neighbors	0.892	0.921	0.901	1.057	0.930	0.804	0.932	0.914	0.925	0.932	0.885	0.923	0.933	0.934	0.923	0.803	0.894	0.837	0.872	0.913
The Kerr-constant increments	49.1	15.6	133	0	-3.6	6.8	0	54.7	0	43.8	20	44.4	0	31.0	64.6	70.5	75.7	0	18.9	29.5
Net charge	0	0	1	1	0	0	-1	0	0	0	0	0	-1	0	0	0	0	0	0	0
Side chain interaction parameter	4.60	3.25	6.50	7.90	5.90	1.40	5.70	3.20	-1	7	6.10	5.25	5.60	4.80	7.60	4	4.50	4.35	2.60	3.40
Side chain interaction parameter	4.32	3.93	6.55	7.92	6.24	2.44	6.04	2.59	1.73	7.19	6.13	5.37	6.17	5.16	6.09	2.78	5.66	3.58	2.31	3.31
Fraction of site occupied by water	0.28	0.16	0.34	0.59	0.31	0.08	0.33	0.10	0.11	0.46	0.39	0.27	0.37	0.26	0.28	0.15	0.23	0.25	0.12	0.22
Side chain volume	27.5	93.5	105.0	100.0	58.7	94.1	40.0	115.5	44.6	41.9	80.7	29.3	62.0	51.3	0.0	145.5	79.0	117.3	93.5	71.5
Hydropathy index	1.8	3.8	-4.5	-3.9	-3.5	1.9	-3.5	2.8	2.5	-1.6	-3.5	-0.8	-3.5	-0.7	-0.4	-0.9	-3.2	-1.3	4.5	4.2
Transfer free energy, CHP/water	-0.48	1.02	-0.06	-0.09	-0.87	0.81	-0.75	1.03	-0.32	2.03	-0.32	0.05	-0.71	-0.35	0	0.66	-0.51	1.24	0.81	0.56
Hydrophobic parameter	-0.5	-1.8	3.0	3.0	0.2	-1.3	2.5	-2.5	-1.0	-1.4	0.2	0.3	2.5	-0.4	0.0	-3.4	-0.5	-2.3	-1.8	-1.5
Distance between C-alpha and centroid of side chain	0.77	2.08	3.72	2.94	1.98	2.34	1.99	2.97	1.38	1.42	2.58	1.28	2.63	1.43	0	3.58	2.76	3.36	1.83	1.49
Side chain angle thet	121.9	118.1	121.4	122.0	117.5	113.1	121.2	118.2	113.7	81.9	118.0	117.9	118.2	117.1	0	118.4	118.2	110.0	118.9	121.7
Side chain torsion angle ph	243.2	205.6	206.6	210.9	207.1	204.0	215.0	203.7	209.4	237.4	205.4	232.0	213.6	226.7	300.0	203.7	219.9	195.6	217.9	220.3
Radius of gyration of side chain	0.77	1.54	2.38	2.08	1.45	1.80	1.43	1.90	1.22	1.25	1.75	1.08	1.77	1.24	0.58	2.21	1.78	2.13	1.56	1.29
Van der waals parameter r0	5.2	7.0	6.0	6.0	5.0	6.8	5.0	7.1	6.1	6.2	6.0	4.9	6.0	5.0	4.2	7.6	6.0	7.1	7.0	6.4
Van der waals parameter epsilon	0.025	0.19	0.20	0.20	0.10	0.19	0.10	0.39	0.10	0.17	0.10	0.025	0.10	0.10	0.025	0.56	0.10	0.39	0.19	0.15
Normalized frequency of alpha-helix, with weights	1.29	1.30	0.96	1.23	0.90	1.47	1.04	1.07	1.11	0.52	1.27	0.82	1.44	0.82	0.56	0.99	1.22	0.72	0.97	0.91
Normalized frequency of beta-sheet, with weights	0.90	1.02	0.99	0.77	0.76	0.97	0.72	1.32	0.74	0.64	0.80	0.95	0.75	1.21	0.92	1.14	1.08	1.25	1.45	1.49
Normalized frequency of reverse turn, with weights	0.77	0.58	0.88	0.96	1.28	0.41	1.41	0.59	0.81	1.91	0.98	1.32	0.99	1.04	1.64	0.76	0.68	1.05	0.51	0.47
Normalized frequency of alpha-helix, unweighted	1.32	1.31	0.98	1.25	0.95	1.39	1.03	1.02	0.92	0.58	1.10	0.76	1.44	0.79	0.61	0.97	1.31	0.73	0.93	0.93
Normalized frequency of beta-sheet, unweighted	0.86	1.04	0.97	0.77	0.73	0.93	0.69	1.21	1.04	0.68	1	1.02	0.66	1.27	0.89	1.26	0.85	1.31	1.47	1.43
Normalized frequency of reverse turn, unweighted	0.79	0.57	0.90	0.99	1.25	0.51	1.47	0.77	0.79	1.78	0.92	1.30	1.02	0.97	1.67	0.79	0.81	0.93	0.50	0.46
Frequency of occurrence in beta-bends	0.22	0.19	0.28	0.27	0.42	0.38	0.73	0.08	0.20	0.46	0.26	0.55	0.08	0.49	0.58	0.43	0.14	0.46	0.22	0.08
Conformational preference for all beta-strands	0.92	1.30	0.93	0.70	0.60	1.19	0.48	1.25	1.16	0.40	0.95	0.82	0.61	1.12	0.61	1.54	0.93	1.53	1.81	1.81
Conformational preference for parallel beta-strands	1	1.42	0.68	0.59	0.54	1.49	0.50	1.30	0.91	0.35	0.28	0.70	0.59	0.59	0.79	0.89	0.38	1.08	2.60	2.63
Conformational preference for antiparallel beta-strands	0.90	1.26	1.02	0.74	0.62	1.09	0.47	1.23	1.24	0.42	1.18	0.87	0.62	1.30	0.56	1.75	1.12	1.68	1.54	1.53
Average surrounding hydrophobicity	12.97	14.90	11.72	11.36	11.42	14.39	10.85	14	14.63	11.37	11.76	11.23	11.89	11.69	12.43	13.93	12.16	13.42	15.67	15.71
Normalized frequency of alpha-helix	1.43	1.36	1.18	1.27	0.64	1.53	0.92	1.19	0.94	0.49	1.22	0.70	1.67	0.78	0.46	1.01	0.98	0.69	1.04	0.98
Normalized frequency of extended structure	0.86	0.98	0.94	0.79	0.74	1.08	0.72	1.16	1.17	1.22	0.89	1.04	0.62	1.18	0.97	1.07	1.06	1.25	1.24	1.33
Normalized frequency of zeta R	0.64	0.37	0.62	0.89	3.14	1.07	1.92	0.86	0.32	0.50	0.80	1.01	1.01	0.92	0.63	1	2.05	1.31	0.92	0.87
Normalized frequency of left-handed alpha-helix	0.17	0.21	0.76	1.17	2.62	0	1.08	0.28	0.95	0.12	0.91	0.57	0.28	0.23	5.02	0	0.57	0.97	0.26	0.24
Normalized frequency of zeta L	1.13	0.65	0.48	1.13	1.11	0	1.18	0.45	0.38	0	0.41	0.81	1.02	0.71	3.84	0.93	0.30	0.38	0.40	0.48
Normalized frequency of alpha region	1	1.01	1.18	1.05	0.87	0.36	1.39	0.65	1.09	1.95	1.13	1.56	1.04	1.23	0.46	1.10	0.71	0.87	0.68	0.58
Refractivity	4.34	18.78	26.66	21.29	13.28	21.64	12	29.40	35.77	10.93	17.56	6.35	17.26	11.01	0	42.53	21.81	31.53	19.06	13.92
Retention coefficient in HPLC, pH7.4	0.5	8.8	0.8	0.1	0.8	4.8	-8.2	13.2	-6.8	6.1	-4.8	1.2	-16.9	2.7	0.0	14.9	-3.5	6.1	13.9	2.7
Retention coefficient in HPLC, pH2.1	-0.1	10.0	-4.5	-3.2	-1.6	7.1	-2.8	13.9	-2.2	8.0	-2.5	-3.7	-7.5	1.5	-0.5	18.1	0.8	8.2	11.8	3.3
Retention coefficient in NaClO4	1.1	11.0	-0.4	-1.9	-4.2	5.4	-1.6	13.4	7.1	4.4	-2.9	-3.2	0.7	-1.7	-0.2	17.1	-0.7	7.4	8.5	5.9
Retention coefficient in NaH2PO4	1.0	9.6	-2.0	-3.0	-3.0	4.0	-0.5	12.6	4.6	3.1	-2.0	-2.9	1.1	-0.6	0.2	15.1	-2.2	6.7	7.0	4.6
Average reduced distance for C-alpha	0.93	0.85	0.98	1.05	0.98	0.84	1.01	0.78	0.88	1	1.02	1.02	1.02	0.99	1.01	0.83	0.89	0.93	0.79	0.81
Average reduced distance for side chain	0.94	0.82	1.09	1.23	1.04	0.83	1.08	0.73	0.84	1.04	1.11	1.04	1.12	1.02	1.01	0.87	0.92	1.03	0.76	0.81
Average side chain orientation angle	87	104	81	65	70	100	71	108	104	78	66	83	72	83	90	94	90	83	105	94
Effective partition energy	2.36	3.93	1.92	1.23	1.70	4.22	1.67	4.37	3.36	1.89	1.75	1.81	1.74	2.04	2.06	3.82	2.41	2.91	4.17	3.49
Normalized frequency of alpha-helix	1.29	1.23	0.83	1.23	0.77	1.23	1	1.23	0.94	0.70	1.10	0.78	1.54	0.87	0.72	1.06	1.29	0.63	0.94	0.97
Normalized frequency of bata-structure	0.96	1.26	0.67	0.81	0.72	1.29	0.90	1.37	1.13	0.75	1.18	0.77	0.33	1.23	0.90	1.13	0.87	1.07	1.54	1.41
Normalized frequency of coil	0.72	0.63	1.33	0.84	1.38	0.62	1.04	0.58	1.01	1.43	0.81	1.34	0.75	1.03	1.35	0.87	0.76	1.35	0.80	0.83
AA composition of total proteins	7.99	9.16	5.86	6.01	4.33	2.50	5.14	3.83	1.81	4.95	3.98	6.84	6.10	5.77	6.91	1.34	2.17	3.15	5.48	6.65
SD of AA composition of total proteins	3.73	3.40	3.34	3.36	2.33	1.37	2.23	1.94	2.30	3.18	2.36	2.83	3	2.63	3.36	1.15	1.55	1.76	2.52	2.53
AA composition of mt-proteins	5.74	15.36	1.92	3.20	5.25	5.30	2.11	6.51	1.03	4.79	2.30	7.55	2.63	7.51	5.66	2.51	2.30	4.08	9.12	5.12
Normalized composition of mt-proteins	-0.60	1.82	-1.18	-0.84	0.39	2.04	-1.36	1.38	-0.34	-0.05	-0.71	0.25	-1.16	0.66	-0.37	1.02	0.08	0.53	1.44	-0.60
AA composition of mt-proteins from animal	5.88	16.52	1.54	2.58	4.38	6	1.70	6.58	1.11	5.29	2.30	7.68	2.60	8.38	5.29	2.89	2.33	3.51	8.78	4.66
Normalized composition from animal	-0.57	2.16	-1.29	-1.02	0.02	2.55	-1.54	1.42	-0.30	0.11	-0.71	0.30	-1.17	0.99	-0.48	1.35	0.10	0.20	1.31	-0.79
AA composition of mt-proteins from fungi and plant	5.39	12.64	2.81	4.67	7.31	3.68	3.07	6.34	0.86	3.62	2.31	7.24	2.70	5.44	6.52	1.64	2.23	5.42	9.94	6.18
Normalized composition from fungi and plant	-0.70	1.02	-0.91	-0.40	1.28	0.86	-0.93	1.29	-0.41	-0.42	-0.71	0.14	-1.13	-0.13	-0.12	0.26	0.04	1.29	1.77	-0.19
AA composition of membrane proteins	9.25	10.94	3.96	3.50	3.71	3.14	3.89	6.36	1.07	4.36	3.17	6.26	4.80	5.66	8.51	2.22	1.88	3.28	6.47	7.55
Normalized composition of membrane proteins	0.34	0.52	-0.57	-0.75	-0.27	0.47	-0.56	1.30	-0.32	-0.19	-0.34	-0.20	-0.43	-0.04	0.48	0.77	-0.19	0.07	0.39	0.36
Transmembrane regions of non-mt-proteins	10.17	16.22	1.21	1.04	1.36	4.12	1.18	9.60	1.48	2.24	1.57	5.38	1.15	5.61	8.87	2.67	1.07	2.68	10.91	11.44
Transmembrane regions of mt-proteins	6.61	21.66	0.41	1.15	1.84	7.17	0.59	7.76	0.83	3.51	1.20	6.84	1.63	8.89	4.88	2.11	1.14	2.57	12.91	6.30
Ratio of average and computed composition	1.61	1.37	0.40	0.62	0.73	1.59	0.75	1.24	0.37	0.67	0.61	0.68	1.50	0.92	3.12	1.63	0.46	0.67	1.61	1.30
AA composition of CYT of single-spanning proteins	8.63	8.44	6.75	6.25	4.18	2.14	6.24	2.73	1.03	6.28	4.76	8.53	7.82	4.43	6.80	0.80	2.70	2.54	3.48	5.44
AA composition of CYT2 of single-spanning proteins	10.88	8.03	6.01	6.11	5.75	3.79	6.13	2.93	0.69	7.21	4.68	7.25	9.34	3.51	7.72	0.47	2.15	1.01	1.80	4.57
AA composition of EXT of single-spanning proteins	5.15	8.11	4.38	5.25	4.81	1.60	5.75	3.52	3.24	5.65	4.45	8.04	7.05	7.41	6.38	1.68	2.69	3.42	4.40	7
AA composition of EXT2 of single-spanning proteins	5.04	9.88	3.73	6.31	5.94	1.85	5.26	3.72	2.20	6.22	4.50	8.05	6.07	5.20	7.09	2.10	2.99	3.32	4.32	6.19
AA composition of MEM of single-spanning proteins	9.90	22.28	0.09	0.16	0.94	1.85	0.35	6.47	2.55	2.38	0.87	4.17	0.08	4.33	8.14	2.21	0.20	3.42	15.25	14.34
AA composition of CYT of multi-spanning proteins	6.69	8.23	6.65	8.36	4.49	2.46	4.97	3.59	1.70	5.20	5.39	7.40	7.76	5.18	6.32	1.06	2.11	2.75	4.51	5.27
AA composition of EXT of multi-spanning proteins	5.08	8.03	4.75	4.93	5.75	2.61	5.96	4.36	2.95	4.84	4.24	6.41	6.04	5.87	8.20	2.31	2.10	4.55	4.95	6.07
AA composition of MEM of multi-spanning proteins	9.36	16.64	0.27	0.58	2.31	3.93	0.94	10.99	2.56	1.96	1.14	5.58	0.94	4.68	6.17	2.20	0.47	3.13	13.73	12.43
8 A contact number	0.23	1.03	-0.26	-1.05	-0.94	0.66	-1.13	0.48	1.78	-0.76	-0.57	-0.67	-0.75	-0.36	-0.07	0.90	0.11	0.59	1.19	1.24
14 A contact number	-0.22	5.01	-0.93	-4.18	-2.65	3.51	-4.12	5.27	4.66	-3.03	-2.76	-2.84	-3.64	-1.20	-1.62	5.20	1.28	2.15	5.58	4.45
Transfer energy, organic solvent/water	0.5	1.8	0.0	0.0	0.0	1.3	0.0	2.5	0.0	0.0	0.0	0.0	0.0	0.4	0.0	3.4	0.5	2.3	1.8	1.5
Average non-bonded energy per atom	-1.895	-1.966	-1.475	-1.374	-1.560	-1.963	-1.518	-1.864	-2.035	-1.699	-1.521	-1.753	-1.535	-1.767	-1.898	-1.869	-1.755	-1.686	-1.951	-1.981
Short and medium range non-bonded energy per atom	-1.404	-1.315	-0.921	-1.074	-1.178	-1.303	-1.162	-1.135	-1.365	-1.236	-1.116	-1.297	-1.163	-1.252	-1.364	-1.030	-1.215	-1.030	-1.189	-1.254
Long range non-bonded energy per atom	-0.491	-0.650	-0.554	-0.300	-0.382	-0.659	-0.356	-0.729	-0.670	-0.463	-0.405	-0.455	-0.371	-0.515	-0.534	-0.839	-0.540	-0.656	-0.762	-0.728
Average non-bonded energy per residue	-9.475	-15.728	-16.225	-12.366	-12.480	-15.704	-12.144	-20.504	-12.210	-11.893	-13.689	-10.518	-13.815	-12.369	-7.592	-26.166	-17.550	-20.232	-15.608	-13.867
Short and medium range non-bonded energy per residue	-7.020	-10.520	-10.131	-9.666	-9.424	-10.424	-9.296	-12.485	-8.190	-8.652	-10.044	-7.782	-10.467	-8.764	-5.456	-14.420	-12.150	-12.360	-9.512	-8.778
Optimized beta-structure-coil equilibrium constant	2.01	2.73	0.84	2.55	0.03	1.75	-2.05	2.68	1.98	0.41	1.02	1.47	0.93	2.39	0.12	2.49	-0.14	2.23	3.70	3.50
Optimized propensity to form reverse turn	1.34	0.54	0.95	0.61	2.49	0.70	3.32	0.80	1.07	2.12	1.49	0.94	2.20	1.09	2.07	-4.65	1.27	-0.17	0.66	1.32
Optimized transfer energy parameter	0.46	0.43	-1.54	-1.71	1.31	0.15	-0.33	0.52	0.20	-0.58	-1.12	-0.83	0.48	-1.52	0.64	1.25	-1.31	-2.21	3.28	0.54
Optimized average non-bonded energy per atom	-2.49	-7.16	2.55	-9.97	2.27	-4.96	8.86	-6.64	-3.13	5.19	1.79	-1.60	4.04	-4.75	-0.56	-17.84	4.22	9.25	-10.87	-3.97
Optimized side chain interaction parameter	4.55	3.24	5.97	10.68	5.56	2.18	2.85	4.37	-0.78	5.14	4.15	6.78	5.16	8.60	9.14	1.97	4.48	2.40	2.10	3.81
Normalized frequency of alpha-helix from LG	1.30	1.30	0.93	1.23	0.90	1.32	1.02	1.09	0.92	0.63	1.04	0.78	1.43	0.80	0.63	1.03	1.33	0.71	0.87	0.95
Normalized frequency of alpha-helix from CF	1.32	1.22	1.04	1.13	0.74	1.47	0.97	1.10	0.70	0.57	1.25	0.77	1.48	0.86	0.59	1.02	1.06	0.72	1.01	1.05
Normalized frequency of beta-sheet from LG	0.81	1.03	1.03	0.77	0.81	0.96	0.71	1.13	1.12	0.75	1.03	1.02	0.59	1.19	0.94	1.24	0.85	1.35	1.47	1.44
Normalized frequency of beta-sheet from CF	0.90	1.24	0.75	0.75	0.82	0.94	0.75	1.41	1.12	0.46	0.95	0.70	0.44	1.20	0.83	1.28	0.86	1.45	1.59	1.73
Normalized frequency of turn from LG	0.84	0.49	0.91	0.95	1.48	0.52	1.28	0.88	0.69	1.47	1	1.29	0.78	1.05	1.76	0.88	0.53	1.28	0.55	0.51
Normalized frequency of turn from CF	0.65	0.56	0.93	0.95	1.45	0.71	1.47	0.72	1.43	1.51	0.94	1.46	0.75	0.96	1.53	0.90	0.96	1.12	0.57	0.55
Normalized frequency of alpha-helix in all-alpha class	1.08	1.04	0.93	1.01	1.05	1.11	0.86	0.96	1.22	0.91	0.95	0.95	1.09	1.15	0.85	1.17	1.02	0.80	0.98	1.03
Normalized frequency of alpha-helix in alpha+beta class	1.34	1.39	0.91	1.08	0.83	0.90	1.06	1.02	1.27	0.48	1.13	1.05	1.69	0.74	0.47	0.64	1.11	0.73	0.84	1.18
Normalized frequency of alpha-helix in alpha/beta class	1.15	1.22	1.06	1.20	0.87	1.45	1	0.92	1.03	0.72	1.43	0.84	1.37	0.97	0.64	1.11	0.95	0.72	0.99	0.82
Normalized frequency of beta-sheet in all-beta class	0.89	1.02	1.06	1	0.67	1.41	0.71	1.32	1.04	0.69	1.06	0.86	0.72	1.15	0.87	1.06	1.04	1.35	1.14	1.66
Normalized frequency of beta-sheet in alpha+beta class	0.82	0.94	0.99	0.73	1.27	1.30	0.98	1.56	0.71	0.69	1.01	0.65	0.54	0.98	0.94	1.25	1.26	1.26	1.67	1.22
Normalized frequency of beta-sheet in alpha/beta class	0.98	1.05	1.03	0.83	0.66	0.82	0.74	1.23	1.01	0.73	0.63	0.98	0.59	1.20	0.90	1.26	1.17	1.23	1.38	1.62
Normalized frequency of turn in all-alpha class	0.69	0	0	1.18	1.52	0.88	2.42	2.20	0	1.34	1.44	1.43	0.63	0.28	2.64	0	0.22	1.53	0.43	0.14
Normalized frequency of turn in all-beta class	0.87	0.67	1.30	0.66	1.36	0	1.24	0.47	0.83	1.54	1.06	1.08	0.91	1.12	1.69	1.24	0.91	0.54	0.27	0.69
Normalized frequency of turn in alpha+beta class	0.91	0.77	0.77	1.27	1.32	0.76	0.90	0.37	0.50	1.62	1.06	1.34	0.53	0.87	1.61	1.10	1.08	1.24	0.36	0.52
Normalized frequency of turn in alpha/beta class	0.92	0.50	0.90	0.86	1.57	0.50	1.22	0.96	0.62	1.30	0.66	1.40	0.92	1.11	1.61	0.57	0.39	1.78	0.79	0.50
HPLC parameter	2.1	-9.2	4.2	5.7	7.0	-4.2	10.0	-9.2	1.4	2.1	6.0	6.5	7.8	5.2	5.7	-10.0	2.1	-1.9	-8.0	-3.7
Partition coefficient	-2.89	-1.61	-3.30	-3.31	-3.41	-1.84	-3.38	-1.63	-2.49	-2.50	-3.15	-3.30	-2.94	-2.91	-3.25	-1.75	-2.84	-2.42	-1.72	-2.08
Surrounding hydrophobicity in folded form	12.28	14.10	11.49	10.80	11	14.33	10.97	13.43	14.93	11.19	11.28	11.26	11.19	11.65	12.01	12.95	12.84	13.29	14.77	15.07
Average gain in surrounding hydrophobicity	7.62	9.37	6.81	5.72	6.17	9.83	6.18	8.99	10.93	6.64	6.67	6.93	6.38	7.08	7.31	8.41	7.85	8.53	9.99	10.38
Average gain ratio in surrounding hydrophobicity	2.63	2.98	2.45	2.12	2.27	3.18	2.29	3.02	3.36	2.46	2.45	2.60	2.31	2.55	2.55	2.85	2.57	2.79	3.08	3.21
Surrounding hydrophobicity in alpha-helix	13.65	14.01	11.28	11.96	12.24	13.40	10.98	14.08	14.49	11.51	11.30	11.26	12.55	13	15.36	12.06	11.59	12.64	14.63	12.88
Surrounding hydrophobicity in beta-sheet	14.60	16.49	13.24	13.28	11.79	16.23	13.78	14.18	15.90	14.10	12.02	13.36	13.59	14.50	14.18	13.90	15.35	14.76	14.10	16.30
Surrounding hydrophobicity in turn	10.67	13.07	11.05	9.93	10.85	15	10.21	13.27	14.15	10.62	11.71	11.18	11.71	10.53	10.95	11.41	12.07	11.52	12.95	13.86
Accessibility reduction ratio	3.70	5.88	2.53	1.79	2.12	5.21	2.60	6.60	3.03	2.12	2.70	2.43	3.30	2.60	3.13	6.25	3.57	3.03	7.69	7.14
Average number of surrounding residues	6.05	7.37	5.70	4.88	5.04	6.39	4.95	6.62	7.86	5.65	5.45	5.53	5.10	5.81	6.16	6.98	5.80	6.73	7.51	7.62
Intercept in regression analysis	0.305	0.262	0.227	0.391	0.322	0.280	0.335	0.195	0.339	0.346	0.306	0.326	0.282	0.251	0.352	0.291	0.215	0.293	0.278	0.291
Slope in regression analysis x 1.0E1	0.175	0.104	0.083	0.058	0.090	0.054	0.140	0.104	0.074	0.136	0.093	0.155	0.135	0.152	0.201	0.092	0.125	0.081	0.100	0.096
Correlation coefficient in regression analysis	0.687	0.541	0.590	0.407	0.489	0.328	0.632	0.577	0.263	0.600	0.527	0.692	0.669	0.713	0.670	0.632	0.594	0.495	0.564	0.529
Hydrophobicity	-6.70	-11.70	51.50	36.80	20.10	-14.20	38.50	-15.50	-8.40	0.80	17.20	-2.50	34.30	-5	-4.20	-7.90	12.60	2.90	-13	-10.90
Relative frequency in alpha-helix	1.29	1.30	0.96	1.23	0.90	1.47	1.04	1.07	1.11	0.52	1.27	0.82	1.44	0.82	0.56	0.99	1.22	0.72	0.97	0.91
Relative frequency in beta-sheet	0.90	1.02	0.99	0.77	0.76	0.97	0.72	1.32	0.74	0.64	0.80	0.95	0.75	1.21	0.92	1.14	1.08	1.25	1.45	1.49
Relative frequency in reverse-turn	0.78	0.59	0.88	0.96	1.28	0.39	1.41	0.58	0.80	1.91	0.97	1.33	1	1.03	1.64	0.75	0.69	1.05	0.51	0.47
Helix-coil equilibrium constant	1.10	1.25	0.95	1	0.80	1.15	0.65	1.10	0.95	0.10	1	0.75	1	0.75	0.60	1.10	0.85	1.10	1.10	0.95
Beta-coil equilibrium constant	1	2	0.70	0.70	0.60	1.90	0.50	3.10	1.90	0.20	1	0.90	0.70	1.70	0.30	2.20	0.80	2.80	4	4
Weights for alpha-helix at the window position of -6	0.12	0.05	0.04	0.26	-0.10	0	0.01	0.05	-0.25	-0.19	-0.03	-0.19	-0.02	-0.04	-0.02	-0.06	-0.06	-0.14	-0.07	-0.03
Weights for alpha-helix at the window position of -5	0.26	-0.02	-0.14	0.12	-0.03	0	0.15	0.12	-0.15	-0.08	-0.13	0.01	0.21	-0.34	-0.37	-0.01	0.10	-0.29	-0.03	0.02
Weights for alpha-helix at the window position of -4	0.64	0.41	-0.10	-0.17	0.09	0.13	0.33	-0.03	0.03	-0.43	-0.23	-0.10	0.51	-0.07	-0.09	-0.02	-0.23	-0.38	-0.22	-0.01
Weights for alpha-helix at the window position of -3	0.29	0.47	-0.03	-0.19	-0.04	0.27	0.11	0.24	-0.05	-0.34	0.26	-0.17	0.28	-0.20	-0.67	0.25	-0.26	-0.30	0	-0.01
Weights for alpha-helix at the window position of -2	0.68	0.61	-0.22	0.03	-0.09	0.39	-0.02	0.06	-0.15	-0.76	-0.15	-0.26	0.44	-0.10	-0.73	0.20	-0.14	-0.04	-0.08	0.12
Weights for alpha-helix at the window position of -1	0.34	0.20	0.22	-0.11	-0.33	0.43	0.06	0.15	-0.18	-0.81	0.01	-0.35	0.20	-0.37	-0.88	0.07	-0.09	-0.31	-0.03	0.13
Weights for alpha-helix at the window position of 0	0.57	0.48	0.23	0.16	-0.36	0.41	-0.46	0.03	-0.15	-1.12	0.15	-0.47	0.26	-0.54	-0.71	-0.10	-0.05	-0.35	0	0.31
Weights for alpha-helix at the window position of 1	0.33	0.57	0.10	0.23	-0.19	0.79	-0.44	0.48	-0.03	-1.86	0.19	-0.23	0.21	-0.33	-0.46	0.15	0.27	-0.19	-0.33	0.24
Weights for alpha-helix at the window position of 2	0.13	0.50	0.08	0.37	-0.07	0.63	-0.71	0.15	-0.09	-1.40	0.12	-0.28	0.13	-0.21	-0.39	0.02	0.32	-0.10	0	0.17
Weights for alpha-helix at the window position of 3	0.31	0.56	0.18	0.47	-0.10	0.58	-0.81	0.10	-0.26	-1.33	0.41	-0.49	-0.06	-0.44	-0.42	0.14	0.51	-0.08	-0.15	-0.01
Weights for alpha-helix at the window position of 4	0.21	0.70	0.07	0.28	-0.04	0.61	-0.58	-0.06	-0.12	-1.03	0.13	-0.28	-0.23	-0.25	-0.15	0.21	0.37	0.16	0.31	0
Weights for alpha-helix at the window position of 5	0.18	0.62	0.21	0.41	-0.03	0.21	-0.32	0.05	-0.29	-0.84	-0.27	-0.05	-0.25	-0.16	-0.40	0.32	0.28	0.11	-0.03	0.06
Weights for alpha-helix at the window position of 6	-0.08	0.28	0.05	0.45	-0.08	0.11	-0.24	0	-0.25	-0.42	-0.28	0.07	-0.19	-0.33	-0.10	0.36	0.29	0	-0.01	-0.13
Weights for beta-sheet at the window position of -6	-0.18	-0.23	-0.13	0.03	0.28	-0.42	0.05	-0.18	-0.26	-0.13	0.21	0.41	-0.06	0.33	0.23	-0.10	0.24	-0.10	-0.42	-0.07
Weights for beta-sheet at the window position of -5	-0.01	-0.25	0.02	0.08	0.41	-0.57	-0.09	-0.12	-0.27	0.26	0.01	0.44	0.09	0.35	0.13	-0.15	0.22	0.15	-0.27	-0.09
Weights for beta-sheet at the window position of -4	-0.19	-0.42	0.03	-0.09	0.02	-0.38	-0.06	-0.32	-0.29	0.05	0.02	0.25	-0.10	0.22	0.19	-0.19	-0.16	0.05	-0.08	-0.15
Weights for beta-sheet at the window position of -3	-0.14	-0.57	0.14	0.04	-0.27	0.24	-0.10	0.08	-0.64	0.02	-0.11	-0.12	-0.39	0	0.46	-0.10	-0.04	0.18	0.16	0.29
Weights for beta-sheet at the window position of -2	-0.31	0.09	0.25	-0.29	-0.53	0.29	-0.54	0.24	-0.06	-0.31	0.07	0.11	-0.52	0.03	0.37	0.15	-0.32	0.29	0.57	0.48
Weights for beta-sheet at the window position of -1	-0.10	0.32	0.19	-0.46	-0.89	0.43	-0.89	0.36	0.13	-0.91	-0.04	-0.12	-0.34	0.49	-0.45	0.34	-0.34	0.42	0.95	0.76
Weights for beta-sheet at the window position of 0	-0.25	0.23	-0.02	-0.59	-0.77	0.32	-1.01	0.48	0.13	-1.24	-0.12	-0.31	-0.62	0.17	-0.72	0.45	-0.16	0.77	1.10	0.69
Weights for beta-sheet at the window position of 1	-0.26	0.25	-0.09	-0.55	-0.34	-0.05	-0.55	0.20	0.47	-1.28	-0.33	-0.28	-0.75	0.08	-0.56	0.22	-0.04	0.53	0.94	0.67
Weights for beta-sheet at the window position of 2	0.05	0.32	-0.11	-0.51	-0.40	-0.10	-0.11	0.20	0.36	-0.79	-0.67	0.03	-0.35	-0.15	0.14	0.09	0.02	0.34	0.47	0.58
Weights for beta-sheet at the window position of 3	-0.44	-0.12	-0.13	-0.33	0.05	-0.21	-0.20	-0.13	0.13	-0.48	-0.58	0.27	-0.28	0.47	0.08	-0.22	0.09	-0.11	-0.04	0.06
Weights for beta-sheet at the window position of 4	-0.31	-0.44	-0.10	-0.44	0.06	-0.28	0.13	-0.04	-0.11	-0.29	-0.47	0.34	-0.05	0.27	0.45	-0.08	-0.06	0.06	-0.25	0.11
Weights for beta-sheet at the window position of 5	-0.02	-0.26	0.04	-0.39	0.03	-0.14	0.11	-0.03	-0.02	-0.04	-0.17	0.41	0.10	0.36	0.38	-0.01	-0.09	-0.08	-0.48	-0.18
Weights for beta-sheet at the window position of 6	-0.06	-0.46	0.02	-0.43	0.10	-0.52	0.24	-0.33	-0.19	0.37	-0.04	0.43	-0.04	0.50	0.17	-0.32	0.19	0.35	-0.20	0
Weights for coil at the window position of -6	-0.05	0.04	0.06	-0.42	0	0.25	0.15	0.09	0.30	0.31	-0.08	-0.11	-0.02	-0.06	-0.14	0.19	-0.07	0.33	0.26	0.04
Weights for coil at the window position of -5	-0.19	0.34	0.17	-0.20	-0.38	0.45	0.09	0.07	0.41	0.04	0.04	-0.23	-0.20	-0.02	0.28	0.16	-0.19	0.22	-0.06	0.05
Weights for coil at the window position of -4	-0.43	-0.10	0.06	0.33	0	-0.01	-0.31	0.25	0.19	0.28	0.14	-0.23	-0.41	-0.26	-0.21	0.15	0.21	0.09	0.29	-0.10
Weights for coil at the window position of -3	-0.19	-0.22	-0.07	0	0.17	-0.53	-0.27	-0.31	0.42	0.14	-0.29	0.22	-0.22	0.10	0.17	-0.15	0.17	-0.02	-0.34	-0.33
Weights for coil at the window position of -2	-0.25	-0.55	0.12	0.14	0.61	-0.47	0.60	-0.29	0.18	0.89	0.09	0.24	-0.12	0.16	0.09	-0.44	0.42	-0.19	-0.54	-0.45
Weights for coil at the window position of -1	-0.27	-0.54	-0.40	0.45	0.71	-0.76	0.54	-0.47	0	1.40	-0.08	0.40	-0.12	-0.10	1.14	-0.46	0.18	-0.05	-0.74	-0.86
Weights for coil at the window position of 0	-0.42	-0.69	-0.23	0.09	0.81	-0.86	0.95	-0.39	-0.18	1.77	-0.01	0.63	-0.09	0.29	1.24	-0.37	0.05	-0.41	-1.17	-1.32
Weights for coil at the window position of 1	-0.24	-0.80	-0.04	0.17	0.45	-0.71	0.65	-0.61	-0.38	2.27	0.01	0.33	0.07	0.13	0.85	-0.44	-0.21	-0.49	-0.65	-0.99
Weights for coil at the window position of 2	-0.14	-0.80	0.21	-0.14	0.35	-0.56	0.66	-0.25	-0.09	1.59	0.11	0.32	0.06	0.21	0.36	-0.17	-0.31	-0.35	-0.51	-0.70
Weights for coil at the window position of 3	0.01	-0.81	-0.13	-0.43	-0.11	-0.49	0.78	-0.20	-0.31	1.14	-0.13	0.13	0.09	-0.02	0.14	-0.20	-0.56	0.10	-0.09	-0.11
Weights for coil at the window position of 4	-0.30	-0.18	-0.09	0.06	-0.12	-0.44	0.44	0.11	0.03	0.77	0.24	-0.09	0.18	-0.27	-0.12	-0.09	-0.20	-0.25	-0.07	-0.06
Weights for coil at the window position of 5	-0.23	-0.36	-0.20	-0.15	0.06	-0.19	0.34	-0.02	0.19	0.78	0.47	-0.29	0.28	-0.30	0.14	-0.18	-0.22	0.07	0.42	0.29
Weights for coil at the window position of 6	0.08	0.24	-0.01	-0.27	-0.06	0.16	0.04	0.34	0.37	0.16	0.48	-0.35	0.36	-0.04	-0.02	-0.06	-0.45	-0.20	0.09	0.18
Average reduced distance for C-alpha	0.934	0.825	0.962	1.040	0.986	0.804	0.994	0.773	0.900	1.047	1.047	1.056	0.986	1.008	1.015	0.848	0.882	0.931	0.766	0.825
Average reduced distance for side chain	0.941	0.798	1.112	1.232	1.038	0.781	1.071	0.723	0.866	1.093	1.150	1.082	1.100	1.043	1.055	0.867	0.911	1.050	0.742	0.817
Side chain orientational preference	1.16	0.51	1.72	3.90	1.97	0.40	2.66	0.43	0.50	2.04	3.87	1.61	2.40	1.48	1.63	0.75	0.86	1.72	0.57	0.59
Average relative fractional occurrence in A	0.85	1.03	2.02	0.88	0.88	1.17	1.50	0.85	0.90	1.47	1.71	1.50	1.79	1.96	1.54	0.83	1.59	1.34	0.67	0.89
Average relative fractional occurrence in A	1.58	1.21	1.14	1.27	0.77	1.41	0.98	1	1.04	1.46	1.24	1.05	1.49	0.87	0.66	1.23	0.99	0.68	1.09	0.88
Average relative fractional occurrence in A	0.82	0	2.60	2.86	2.07	0	2.64	0	0	0	0	1.23	2.62	2.48	1.63	0	0	1.90	2.32	1.62
Average relative fractional occurrence in E	0.78	0.91	1.75	0.85	1.32	0.41	1.25	1.07	3.14	1.73	0.93	1.31	0.94	1.57	1.13	0.98	1.03	1.31	1.26	1.11
Average relative fractional occurrence in E	0.88	1.09	0.99	0.83	1.02	1.71	1.16	1.52	1.14	0.87	0.93	1.14	1.01	0.96	0.70	1.96	1.87	1.68	1.61	1.56
Average relative fractional occurrence in E	0.30	0.96	0.90	0.71	2.73	1.89	1.26	1.20	0.72	0.83	0.97	1.16	1.33	0.97	3.09	1.58	1.33	0.86	0.45	0.64
Average relative fractional occurrence in A	0.40	0.57	1.20	0.87	1.24	0	1.59	1.27	2.98	0.38	0.50	0.92	1.26	1.38	1.89	1.53	2.71	1.79	1.31	0.95
Average relative fractional occurrence in A	1.48	1.33	1.02	1.36	0.99	1.41	1.19	1.30	0.86	0.25	1.42	0.89	1.43	0.81	0.46	1.27	1.27	0.91	1.12	0.93
Average relative fractional occurrence in A	0	0	0	0	4.14	0	2.15	2.11	0	1.99	0	0	0	1.24	6.49	0	0	1.90	0	0
Average relative fractional occurrence in E	1.02	1.06	1	0.94	1.31	1.33	1.76	0.41	1.05	2.73	1.05	1.18	0.83	0.77	2.39	1.22	0.40	1.09	0.83	0.88
Average relative fractional occurrence in E	0.93	1.03	1.52	1	0.92	1.31	0.60	1.51	1.08	1.37	0.94	0.97	0.73	1.38	0.78	1.12	1.08	1.65	1.74	1.70
Average relative fractional occurrence in E	0.99	1.26	1.19	0.91	1.15	1	1.18	1.25	2.32	0	1.52	1.50	1.36	1.18	1.40	1.33	1.06	1.09	0.81	1.01
Value of thet	17.05	10.89	21.25	16.46	34.81	20.61	19.27	16.26	28.84	23.94	15.42	19.95	20.12	18.92	38.14	23.36	23.07	26.49	16.66	17.06
Value of thet	14.53	14.30	17.82	14.07	13.59	20.61	19.78	19.61	30.57	52.63	22.18	18.56	18.19	21.09	37.16	19.78	22.63	26.36	20.28	21.87
Transfer free energy from chx to wat	1.81	4.92	-14.92	-5.55	-6.64	2.35	-8.72	2.98	1.28	0	-5.54	-3.40	-6.81	-2.57	0.94	2.33	-4.66	-0.14	4.92	4.04
Transfer free energy from oct to wat	0.52	1.76	-1.32	0.08	-0.01	1.32	0	2.09	0	0	-0.07	0.04	-0.79	0.27	0	2.51	0.95	1.63	2.04	1.18
Transfer free energy from vap to chx	0.13	-2.64	-5	-3.97	-3.04	-3.83	-2.23	-3.74	-2.52	0	-3.84	-1.66	-3.43	-2.31	1.45	-8.21	-5.61	-5.97	-2.77	-2.05
Transfer free energy from chx to oct	1.29	3.16	-13.60	-5.63	-6.63	1.03	0	0.89	0	0	-5.47	-3.44	-6.02	-2.84	0.94	-0.18	-5.61	-1.77	2.88	2.86
Transfer free energy from vap to oct	1.42	0.52	-18.60	-9.60	-9.67	-2.80	0	-2.85	0	0	-9.31	-5.10	-9.45	-5.15	2.39	-8.39	-11.22	-7.74	0.11	0.81
Accessible surface area	93.7	173.7	250.4	215.2	146.3	197.6	142.6	228.6	135.2	0	177.7	109.5	182.9	142.1	52.6	271.6	188.1	239.9	182.2	157.2
Energy transfer from out to i	-0.29	-0.12	-2.71	-2.05	-1.18	-0.24	-1.02	0	0	0	-1.53	-0.75	-0.90	-0.71	-0.34	-0.59	-0.94	-1.02	0.24	0.09
Mean polarity	-0.06	1.21	-0.84	-1.18	-0.48	1.27	-0.80	1.27	1.36	0	-0.73	-0.50	-0.77	-0.27	-0.41	0.88	0.49	0.33	1.31	1.09
Relative preference value at N"	0.7	0.9	0.4	1	1.2	0.3	1.4	1.2	0.6	0.7	1	1.6	1	0.3	1.6	1.1	1.2	1.9	0.9	0.7
Relative preference value at N'	0.7	0.9	0.4	1	1.2	0.3	1.4	1.2	0.6	0.7	1	1.6	1	0.3	1.6	1.1	1.2	1.9	0.9	0.7
Relative preference value at N-cap	0.5	0.2	0.4	0.7	3.5	0.8	2.1	0.2	0.6	0.8	0.4	2.3	0.4	1.6	1.8	0.3	1.1	0.8	0.2	0.1
Relative preference value at N1	1.2	0.9	0.7	0.6	0.7	0.3	0.8	0.5	0.8	2.6	0.7	0.7	2.2	0.8	0.3	2.1	0.7	1.8	0.9	1.1
Relative preference value at N2	1.6	0.3	0.9	1	0.7	1	2.6	0.9	1.2	0.5	0.8	0.8	2	0.7	0.9	1.7	0.7	0.4	0.7	0.6
Relative preference value at N3	1	0.6	0.4	0.8	0.7	1	2.2	0.6	0.6	0.4	1.5	0.4	3.3	1	0.6	1.4	0.7	1.2	0.4	1.1
Relative preference value at N4	1.1	2.6	1.5	0.8	0	1.7	0.3	1.9	1.1	0.1	1.3	0.4	0.5	0.5	0.4	3.1	1.5	0.6	1.1	1.5
Relative preference value at N5	1.4	1.1	1.2	1.9	1.2	1.7	0.6	1	1.6	0.3	1.4	1.1	0.9	0.6	0.6	1.4	0.9	0.2	0.9	0.8
Relative preference value at Mid	1.8	1.2	1.3	1.1	0.9	1.5	1	1.3	0.7	0.3	1.3	0.6	0.8	1	0.5	1.5	1	0.8	1.2	1.2
Relative preference value at C5	1.8	1.2	1	1.4	0.6	2.7	0.7	1.9	0	0.3	1	0.5	1.1	0.5	0.5	1.1	2.4	1.3	1.3	0.4
Relative preference value at C4	1.3	1.4	0.8	1	0.6	2.8	0.5	2.9	0.7	0	0.2	0.5	0.7	0.6	0.5	2.1	1.9	0.8	1.6	1.4
Relative preference value at C3	0.7	1.9	0.8	2.2	0.8	1	0.6	1.8	0.2	0	1.3	0.6	1.6	0.7	0.1	0.4	1.1	1.1	1.4	1.3
Relative preference value at C2	1.4	0.8	2.1	1.9	0.9	1.3	0.7	0.3	1.2	0.2	1.6	1.6	1.7	0.9	0.2	0.4	1.8	0.3	0.4	0.7
Relative preference value at C1	1.1	0.7	1	2	1.2	1	0.4	0.7	1.6	0	2.1	1.7	0.8	1	0.2	0	3.4	1.2	0.7	0.7
Relative preference value at C-cap	0.8	0.7	0.9	1.3	1.6	0.8	0.7	0.5	0.4	0.7	0.9	0.8	0.3	0.3	3.9	0	1.3	0.8	0.7	0.2
Relative preference value at C'	1	0.9	1.4	1.2	0.9	0.8	1.4	0.1	0.8	1.9	1.4	0.7	0.8	0.8	1.2	0.4	1.2	0.9	1.1	0.6
Relative preference value at C"	0.7	0.5	1.1	1.3	1.5	0	1.4	1.2	0.4	1.5	1.1	0.9	0.7	2.1	0.6	2.7	1	0.5	0.7	1
Information measure for alpha-helix	6.5	3.2	-0.9	2.3	-5.1	5.3	0.5	1.6	-1.3	-7.7	1.0	-3.9	7.8	-2.6	-8.6	1.2	1.2	-4.5	0.6	1.4
Information measure for N-terminal helix	2.3	-2.1	-5.2	-4.1	0.3	-3.5	7.4	-1.1	0.8	8.1	-0.7	-3.5	10.3	2.3	-5.2	-0.9	-2.8	-3.7	-4.0	-4.4
Information measure for middle helix	6.7	5.5	0.3	0.5	-6.1	7.2	-3.1	2.8	-4.9	-22.8	0.6	-3.0	2.2	-4.0	-6.8	4.0	-1.0	-4.6	3.2	2.5
Information measure for C-terminal helix	2.3	0.1	1.4	7.3	-3.3	3.5	-4.4	1.6	6.1	-24.4	2.7	-1.9	2.5	-3.7	-8.3	-0.9	5.9	-0.6	-0.5	2.3
Information measure for extended	-2.3	2.3	0.4	-3.3	-4.1	2.3	-4.4	2.6	4.4	-1.8	1.2	-1.7	-5.0	1.3	-4.2	-1.0	-2.5	4.0	6.7	6.8
Information measure for pleated-sheet	-2.7	3.7	0.4	-2.9	-4.2	3.7	-4.4	3.0	3.7	-6.6	0.8	-2.4	-8.1	1.7	-3.9	0.3	-3.0	3.3	7.7	7.1
Information measure for extended without H-bond	0.0	-3.7	1.1	-3.1	-2.0	-2.1	-2.6	0.7	5.4	7.4	2.4	1.3	3.1	0.0	-3.4	-3.4	0.8	4.8	-0.1	2.7
Information measure for turn	-5.0	-5.6	2.1	1.0	4.2	-4.8	3.1	-1.8	4.4	2.6	0.4	2.6	-4.7	0.3	5.7	3.4	-0.3	2.9	-4.6	-6.0
Information measure for N-terminal turn	-3.3	-2.3	0.0	-1.2	5.4	-4.3	3.9	0.8	-0.3	6.5	-0.4	1.8	-1.8	-0.7	-1.2	-0.8	3.0	3.1	-0.5	-3.5
Information measure for middle turn	-4.7	-6.2	2.0	2.8	3.9	-4.8	1.9	-3.7	6.2	3.6	-2.0	2.1	-4.2	0.6	5.7	3.3	-2.6	3.8	-7.0	-6.2
Information measure for C-terminal turn	-3.7	-2.8	1.0	1.3	-0.6	-1.6	-0.6	1.6	4.0	-6.0	3.4	1.5	-4.3	1.2	5.9	6.5	-0.8	1.3	-0.5	-4.6
Information measure for coil	-2.5	-2.0	-1.2	-0.8	4.6	-4.1	0.0	-4.1	-4.7	5.8	-0.5	2.5	-4.4	1.7	4.9	1.2	1.6	-0.6	-3.3	-3.5
Information measure for loop	-5.1	-5.4	2.6	1.0	4.7	-5.3	3.1	-2.4	3.8	3.5	0.2	3.2	-5.2	0.0	5.6	2.9	-0.9	3.2	-4.5	-6.3
Hydration free energy	-1.0	2.0	0.3	-0.9	-0.7	1.8	-1.2	2.8	2.1	0.4	-0.1	-1.2	-0.7	-0.5	0.3	3.0	1.1	2.1	4.0	1.4
Mean area buried on transfer	86.6	164.1	162.2	115.5	103.3	172.9	97.8	194.1	132.3	92.9	119.2	85.6	113.9	106.5	62.9	224.6	155.8	177.7	158.0	141.0
Mean fractional area loss	0.74	0.85	0.64	0.52	0.63	0.85	0.62	0.88	0.91	0.64	0.62	0.66	0.62	0.70	0.72	0.85	0.78	0.76	0.88	0.86
Side chain hydropathy, uncorrected for solvation	-0.67	-3.02	12.1	6.13	7.23	-1.30	8.72	-3.24	-0.34	-1.75	6.39	4.35	7.35	3.86	0	-2.86	3.82	0.98	-3.02	-2.18
Side chain hydropathy, corrected for solvation	-0.67	-3.02	3.89	2.46	2.27	-1.67	1.57	-3.24	-2	-1.75	2.12	0.10	1.78	-0.42	0	-2.86	1.09	0.98	-3.02	-2.18
Loss of Side chain hydropathy by helix formation	0.4	0.6	0.3	0.4	0.9	0.3	0.8	0.7	0.5	0.9	0.7	0.4	1.3	0.4	0.0	0.6	1.0	1.2	0.4	0.4
Transfer free energy	0.73	2.49	0.73	1.50	-0.01	1.30	0.54	2.65	0.70	2.60	-0.10	0.04	0.55	0.44	0	3	1.10	2.97	2.97	1.69
Principal component I	0.239	0.281	0.211	0.228	0.249	0.253	0.171	0.234	0.220	0.165	0.260	0.236	0.187	0.213	0.160	0.183	0.205	0.193	0.273	0.255
Principal component II	0.330	0.129	-0.176	-0.075	-0.233	-0.092	-0.371	-0.011	0.074	0.370	-0.254	0.022	-0.409	0.136	0.370	-0.011	-0.078	-0.138	0.149	0.245
Principal component III	-0.110	-0.008	0.079	0.049	-0.136	-0.041	-0.285	0.438	-0.184	-0.016	-0.067	-0.153	-0.246	-0.208	-0.073	0.493	0.320	0.381	0.001	-0.155
Principal component IV	-0.062	-0.264	-0.167	-0.371	0.166	0.077	-0.079	0.074	0.380	-0.036	-0.025	0.470	-0.184	0.348	-0.017	0.050	0.056	0.220	-0.309	-0.212
Zimm-Bragg parameter s at 20 C	1.071	1.140	1.033	0.939	0.784	1.200	0.680	1.086	0.922	0.659	0.977	0.760	0.970	0.817	0.591	1.107	0.850	1.020	1.140	0.950
Zimm-Bragg parameter sigma x 1.0E4	8.0	33.0	0.1	1.0	0.1	54.0	70.0	18.0	26.0	42.0	33.0	0.1	6.0	0.1	0.1	77.0	0.1	66.0	55.0	0.1
Optimal matching hydrophobicity	-0.40	1.22	-0.59	-0.67	-0.92	1.02	-1.31	1.92	0.17	-0.49	-0.91	-0.55	-1.22	-0.28	-0.67	0.50	-0.64	1.67	1.25	0.91
Normalized frequency of alpha-helix	1.42	1.29	1.06	1.24	0.71	1.21	1.01	1.16	0.73	0.65	1.02	0.71	1.63	0.78	0.50	1.05	1.20	0.67	1.12	0.99
Normalized frequency of isolated helix	0.946	1.192	1.128	1.203	0.432	0.000	1.311	0.963	0.481	2.093	1.615	0.523	0.698	1.961	0.360	1.925	2.168	0.802	1.283	0.409
Normalized frequency of extended structure	0.790	1.111	1.087	0.735	0.832	1.092	0.530	1.052	1.268	1.249	1.038	1.093	0.643	1.214	0.725	1.114	0.864	1.340	1.361	1.428
Normalized frequency of chain reversal R	1.194	0.595	0.795	1.060	0.659	0.831	1.056	0.377	0.678	3.159	1.290	1.444	0.928	1.172	1.015	0.452	0.611	0.816	0.603	0.640
Normalized frequency of chain reversal S	0.497	0.656	0.677	0.932	2.072	0.425	1.498	1.348	1.348	0.179	0.711	1.151	0.651	0.749	1.848	1.283	1.474	1.283	0.471	0.654
Normalized frequency of chain reversal D	0.937	0.808	1.725	1.254	1.080	0.886	1.640	0.803	1.004	0.748	1.078	1.145	0.679	1.487	0.901	0.803	1.085	1.227	0.178	0.625
Normalized frequency of left-handed helix	0.289	0.000	1.380	1.288	3.169	0.000	0.917	0.393	1.767	0.000	2.372	0.160	0.285	0.218	4.259	0.000	1.061	0.654	0.262	0.167
Normalized frequency of zeta R	0.328	0.414	2.088	0.835	1.498	0.982	3.379	1.336	0.000	0.415	0.000	1.089	0.000	1.732	0.500	1.781	1.204	0.000	2.078	0.946
Normalized frequency of coil	0.945	0.758	0.364	0.947	1.202	1.028	1.315	0.622	0.932	0.579	0.704	1.140	1.014	0.863	2.355	0.777	0.525	0.907	0.673	0.561
Normalized frequency of chain reversal	0.842	0.665	0.936	1.045	1.352	0.668	1.366	0.881	1.032	1.385	0.998	1.257	0.758	1.055	1.349	0.881	1.079	1.101	0.459	0.643
Relative population of conformational state A	0.135	0.215	0.296	0.170	0.196	0.239	0.289	0.087	0.159	0.151	0.236	0.010	0.184	0.100	0.051	0.166	0.223	0.066	0.173	0.285
Relative population of conformational state C	0.507	0.619	0.459	0.559	0.287	0.431	0.223	0.077	0.592	0.739	0.383	0.689	0.445	0.785	0.390	0.160	0.310	0.060	0.111	0.356
Relative population of conformational state E	0.159	0.083	0.194	0.159	0.385	0.198	0.283	0.682	0.187	0.366	0.236	0.150	0.206	0.074	0.049	0.463	0.233	0.737	0.581	0.301
Electron-ion interaction potential	.03731	.00000	.09593	.03710	.00359	.08226	.12630	.09460	.08292	.01979	.07606	.08292	.00580	.09408	.00499	.05481	.02415	.05159	.00000	.00569
Bitterness	0	1	0	0	0	0	0	1	0	0	0	0	0	0	0	1	0	1	1	1
Transfer free energy to lipophilic phase	-12.04	-17.79	39.23	9.71	4.25	-8.86	23.22	-21.98	3.95	5.82	2.16	-1.54	16.81	-4.15	-7.85	-16.19	6.28	-1.51	-18.32	-16.22
Average interactions per side chain atom	10.04	8.79	6.18	4.40	5.63	9.15	5.76	7.98	8.89	7.79	5.41	7.08	5.37	7	7.99	8.07	7.49	6.90	8.72	8.88
RF value in high salt chromatography	0.89	0.73	0.88	0.97	0.89	0.74	0.87	0.52	0.85	0.82	0.82	0.96	0.84	0.92	0.92	0.20	0.83	0.49	0.76	0.85
Propensity to be buried inside	0.52	0.77	0.49	0.31	0.42	0.76	0.37	0.87	0.83	0.35	0.35	0.49	0.38	0.38	0.41	0.86	0.70	0.64	0.79	0.72
Free energy change of epsilo	0.16	-0.44	-0.20	-0.12	1.03	-0.79	-0.24	-0.25	-0.12	-0.59	-0.55	-0.01	-0.45	0.05	-0.16	-0.33	-0.18	-0.42	-0.19	-0.46
Free energy change of alph	0.15	0.06	-0.37	-0.16	0.69	0.11	-0.22	1.18	-0.19	0.11	-0.06	0.13	0.14	0.28	0.36	-0.12	-0.25	0.19	0.02	-0.08
Free energy change of epsilo	-0.07	-0.17	-0.40	-0.45	-0.57	0.03	-0.80	0.40	0.17	-0.47	-0.26	-0.11	-0.63	0.09	0.27	-0.61	-0.49	-0.61	0.06	-0.11
Polar requirement	7.0	4.9	9.1	10.1	10.0	5.3	13.0	5.0	5.5	6.6	8.6	7.5	12.5	6.6	7.9	5.3	8.4	5.7	4.9	5.6
Hydration potential	1.94	2.28	-19.92	-9.52	-9.68	-1.48	-10.95	-0.76	-1.24	-3.68	-9.38	-5.06	-10.20	-4.88	2.39	-5.88	-10.27	-6.11	2.15	1.99
Principal property value z1	0.07	-4.19	2.88	2.84	3.22	-2.49	3.64	-4.92	0.71	-1.22	2.18	1.96	3.08	0.92	2.23	-4.75	2.41	-1.39	-4.44	-2.69
Principal property value z2	-1.73	-1.03	2.52	1.41	1.45	-0.27	1.13	1.30	-0.97	0.88	0.53	-1.63	0.39	-2.09	-5.36	3.65	1.74	2.32	-1.68	-2.53
Principal property value z3	0.09	-0.98	-3.44	-3.14	0.84	-0.41	2.36	0.45	4.13	2.23	-1.14	0.57	-0.07	-1.40	0.30	0.85	1.11	0.01	-1.03	-1.29
Unfolding Gibbs energy in water, pH7.0	8.5	15.0	0	7.9	8.2	13.3	8.5	11.2	11.0	8.2	6.3	7.4	8.8	8.8	7.1	9.9	10.1	8.8	16.8	12.0
Unfolding Gibbs energy in water, pH9.0	6.8	12.2	0	7.5	6.2	8.4	7.0	8.3	8.3	6.9	8.5	8.0	4.9	7.0	6.4	5.7	9.2	6.8	10.0	9.4
Activation Gibbs energy of unfolding, pH7.0	18.08	18.60	0	17.96	17.47	18.11	17.36	17.30	18.17	18.16	17.93	17.57	18.16	17.54	18.24	17.19	18.49	17.99	18.62	18.30
Activation Gibbs energy of unfolding, pH9.0	18.56	19.01	0	18.36	18.24	18.49	17.94	17.95	17.84	18.77	18.51	18.06	17.97	17.71	18.57	16.87	18.64	18.23	19.21	18.98
Dependence of partition coefficient on ionic strength	-0.152	-0.102	-0.089	-0.062	-0.203	-0.107	-0.355	0.001	0	-0.181	-0.181	-0.203	-0.411	-0.170	-0.190	0.275	0	0	-0.086	-0.125
Hydrophobicity	0.83	2.52	0.83	1.60	0.09	1.40	0.64	2.75	1.48	2.70	0	0.14	0.65	0.54	0.10	0.31	1.10	2.97	3.07	1.79
Bulkiness	11.50	21.40	14.28	15.71	12.82	16.25	11.68	19.80	13.46	17.43	14.45	9.47	13.57	15.77	3.40	21.67	13.69	18.03	21.40	21.57
Polarity	0	0.13	52	49.50	3.38	1.43	49.70	0.35	1.48	1.58	3.53	1.67	49.90	1.66	0	2.10	51.60	1.61	0.13	0.13
Isoelectric point	6	5.98	10.76	9.74	5.41	5.74	2.77	5.48	5.05	6.30	5.65	5.68	3.22	5.66	5.97	5.89	7.59	5.66	6.02	5.96
RF rank	9.9	17.6	4.6	3.5	5.4	14.9	2.8	18.8	2.8	14.8	9.0	6.9	3.2	9.5	5.6	17.1	8.2	15.0	17.1	14.3
Normalized positional residue frequency at helix termini N4	0.94	0.95	1.15	1.03	0.79	0.88	1.19	1.06	0.60	1.18	0.94	0.69	1.41	0.87	1.18	0.91	1.15	1.04	1.07	0.90
Normalized positional residue frequency at helix termini N"'	0.98	0.80	1.14	1.06	1.05	1.12	1.05	1.12	0.41	1.31	0.90	1.02	1.04	0.80	1.25	0.90	1.01	1.12	0.88	0.87
Normalized positional residue frequency at helix termini N"	1.05	0.96	0.81	0.97	0.91	0.99	1.39	0.95	0.60	1.05	0.87	0.96	1.11	1.03	1.26	1.06	1.43	0.94	0.95	0.62
Normalized positional residue frequency at helix termini N	0.75	1.01	0.90	0.66	1.24	1.02	1.72	0.88	0.66	1.33	1.08	1.20	1.10	1.13	1.14	0.68	0.96	0.80	0.80	0.58
Normalized positional residue frequency at helix termini Nc	0.67	0.79	0.76	0.84	1.28	0.98	1.58	0.96	0.37	1.12	1.05	1.25	0.94	1.41	0.98	0.94	0.83	0.82	0.78	0.67
Normalized positional residue frequency at helix termini N1	1.10	0.84	1.05	1.08	0.72	0.90	1.14	0.90	0.26	1.67	1.31	0.81	2.30	0.77	0.55	1.26	0.83	0.99	1.06	0.76
Normalized positional residue frequency at helix termini N2	1.39	0.91	0.95	0.80	0.67	1.10	1.64	1	0.52	0.94	1.60	0.69	2.07	0.92	0.65	1.10	1.36	0.73	0.64	0.70
Normalized positional residue frequency at helix termini N3	1.43	1.52	1.33	0.82	0.55	1.68	0.90	1.10	0.52	0.15	1.43	0.61	1.70	0.75	0.56	1.68	0.66	0.65	1.18	1.14
Normalized positional residue frequency at helix termini N4	1.55	1.36	1.39	1.27	0.60	2.13	0.61	1.39	0.59	0.03	1.43	0.44	1.34	0.65	0.37	1.10	0.89	0.93	1.47	1.18
Normalized positional residue frequency at helix termini N5	1.80	1.47	1.73	1.24	0.73	1.64	0.90	0.96	0.55	0.15	0.97	0.67	1.73	0.70	0.32	0.68	0.46	0.91	1.09	0.81
Normalized positional residue frequency at helix termini C5	1.52	1.26	1.49	1.10	0.58	1.14	1.04	1.14	0.26	0.44	1.41	0.66	1.76	0.73	0.30	0.68	0.83	1.04	1.25	1.03
Normalized positional residue frequency at helix termini C4	1.49	1.40	1.41	1.17	0.67	1.84	0.94	0.86	0.37	0.20	1.52	0.68	1.55	0.79	0.29	1.52	0.96	1.06	1.04	0.94
Normalized positional residue frequency at helix termini C3	1.73	1.80	1.24	1.22	0.70	2.21	0.68	1.35	0.63	0.07	0.88	0.65	1.16	0.46	0.32	1.57	0.76	1.10	1.15	0.94
Normalized positional residue frequency at helix termini C2	1.33	1.63	1.39	1.71	0.64	1.76	0.60	1.22	0.44	0.07	1.37	0.42	1.43	0.57	0.20	1	1.02	1.02	1.58	1.08
Normalized positional residue frequency at helix termini C1	1.87	1.65	1.66	1.63	0.70	1.35	0.91	0.67	0.33	0.03	1.24	0.71	1.88	0.50	0.33	1	0.89	0.73	0.90	0.51
Normalized positional residue frequency at helix termini Cc	1.19	1.36	1.45	1.45	1.33	1.35	0.72	1.20	0.44	0.10	1.43	1.02	1.27	0.82	0.74	0.58	1.55	1.06	0.61	0.46
Normalized positional residue frequency at helix termini C'	0.77	0.66	1.11	1.19	1.39	0.74	0.79	1.04	0.44	0.66	0.95	0.64	0.92	0.82	2.74	0.58	1.65	0.93	0.64	0.53
Normalized positional residue frequency at helix termini C"	0.93	1.16	0.96	1.27	0.82	1.11	1.15	1.05	0.67	1.01	1.02	0.71	1.07	0.84	1.08	1.06	1.40	1.15	1.14	0.74
Normalized positional residue frequency at helix termini C"'	1.09	0.87	1.29	1.13	1.03	0.96	1.17	0.84	0.26	2.01	1.08	0.76	1.31	0.79	0.97	0.91	0.88	0.64	0.97	0.77
Normalized positional residue frequency at helix termini C4'	0.71	0.84	1.09	1.10	0.95	0.80	1.43	0.95	0.65	1.70	0.87	0.65	1.19	.086	1.07	1.25	1.13	0.85	1.05	1.12
Delta G values for the peptides extrapolated to 0 M urea	13.4	13.0	13.3	13.0	12.0	12.8	11.7	12.1	11.6	6.5	12.8	12.2	12.2	11.7	11.3	12.4	11.6	12.1	12.0	11.9
Helix formation parameters	-0.77	-0.62	-0.68	-0.65	-0.07	-0.50	-0.15	-0.41	-0.23	3	-0.33	-0.35	-0.27	-0.11	0	-0.45	-0.06	-0.17	-0.23	-0.14
Normalized flexibility parameters	0.984	0.935	1.008	1.102	1.048	0.952	1.068	0.915	0.906	1.049	1.037	1.046	1.094	0.997	1.031	0.904	0.950	0.929	0.927	0.931
Normalized flexibility parameters	1.315	1.234	1.310	1.367	1.380	1.269	1.372	1.247	1.196	1.342	1.342	1.381	1.376	1.324	1.382	1.186	1.279	1.199	1.241	1.235
Normalized flexibility parameters	0.994	0.982	1.026	1.029	1.022	0.963	1.022	0.934	0.939	1.050	1.041	1.025	1.052	0.998	1.018	0.938	0.967	0.981	0.977	0.968
Normalized flexibility parameters	0.783	0.783	0.807	0.834	0.799	0.806	0.822	0.774	0.785	0.809	0.817	0.811	0.826	0.795	0.784	0.796	0.777	0.788	0.776	0.781
Free energy in alpha-helical conformation	0.423	0.494	0.503	0.615	0.906	0.444	0.870	0.706	0.877	1.945	0.594	0.928	0.167	0.884	1.162	0.690	0.802	0.778	0.566	0.706
Free energy in alpha-helical region	0.619	0.740	0.753	0.784	1.089	0.736	0.932	0.968	1.107	1.780	0.770	0.969	0.675	1.053	1.361	0.910	1.034	1.009	0.876	0.939
Free energy in beta-strand conformation	1.080	0.789	0.976	1.026	1.197	0.812	1.266	0.685	0.733	1.412	1.050	0.987	1.085	0.784	1.104	0.755	0.906	0.665	0.583	0.546
Free energy in beta-strand region	0.978	0.766	0.784	0.841	0.915	0.729	1.038	0.585	0.573	2.613	0.863	0.784	0.962	0.569	1.405	0.671	0.724	0.560	0.502	0.444
Free energy in beta-strand region	1.40	1.33	1.23	1.34	1.61	1.12	1.89	1.07	1.14	3.90	1.33	1.20	1.42	0.99	2.06	1.10	1.25	0.98	1.02	0.87
Free energies of transfer of AcWl-X-LL peptides from bilayer interface t	4.08	4.81	3.91	3.77	3.83	4.48	3.02	5.38	4.49	3.80	3.67	4.12	2.23	4.11	4.24	6.10	4.08	5.19	4.52	4.18
Thermodynamic beta sheet propensity	-0.35	-0.48	-0.44	-0.41	-0.38	-0.46	-0.41	-0.55	-0.47	-0.23	-0.40	-0.39	-0.41	-0.48	0.0	-0.48	-0.46	-0.50	-0.56	-0.53
Turn propensity scale for transmembrane helices	0.5	0.4	1.7	1.6	1.7	0.5	1.6	0.4	0.6	1.7	1.6	0.7	1.6	0.4	1.3	0.7	1.6	0.6	0.6	0.5
Alpha helix propensity of position 44 in T4 lysozyme	0.96	0.92	0.77	0.73	0.39	0.86	0.42	0.59	0.42	-2.50	0.80	0.53	0.53	0.54	0	0.58	0.57	0.72	0.84	0.63
p-Values of mesophilic proteins based on the distributions of B value	0.343	0.287	0.353	0.429	0.409	0.293	0.429	0.292	0.319	0.432	0.395	0.416	0.405	0.362	0.389	0.268	0.307	0.22	0.296	0.307
p-Values of thermophilic proteins based on the distributions of B value	0.320	0.340	0.327	0.446	0.384	0.313	0.424	0.314	0.198	0.354	0.436	0.376	0.514	0.339	0.374	0.291	0.299	0.287	0.306	0.294
Distribution of amino acid residues in the 18 non-redundant families o	8.9	7.4	4.6	6.1	4.4	2.3	6.3	3.3	0.6	4.2	2.8	4.0	6.9	5.7	9.4	1.3	2.2	4.5	7.0	8.2
Distribution of amino acid residues in the 18 non-redundant families o	9.2	7.7	3.6	6.5	5.1	2.4	6.0	3.4	1.0	4.2	2.9	5.5	6.0	5.7	9.4	1.2	2.1	3.7	6.0	8.2
Distribution of amino acid residues in the alpha-helices in thermophili	14.1	9.1	5.5	7.7	3.2	3.3	5.7	5.0	0.1	0.7	3.7	3.9	8.8	4.4	4.1	1.2	2.0	4.5	7.1	5.9
Distribution of amino acid residues in the alpha-helices in mesophili	13.4	10.6	3.9	7.5	3.7	3.0	4.6	4.5	0.8	1.3	4.8	3.8	7.8	4.6	4.6	1.0	3.3	3.3	6.5	7.1
Side-chain contribution to protein stability	9.8	17.0	7.3	10.5	3.6	11.9	4.9	23.0	3.0	15.0	2.4	2.6	4.4	6.9	0	24.2	11.9	17.2	17.2	15.3
Propensity of amino acids within pi-helices	0.70	1.44	0.95	0.91	1.47	0.91	0.87	1.34	1.17	0.12	0.73	0.84	0.96	0.74	0.64	1.80	1.39	1.68	1.29	1.20
Hydropathy scale based on self-information values in the two-state model	58	95	-184	-24	-93	78	-97	92	116	-79	-139	-34	-131	-7	-11	59	-73	-11	107	100
Hydropathy scale based on self-information values in the two-state model	51	103	-144	-205	-84	73	-78	108	137	-79	-128	-26	-115	-3	-13	69	-55	11	106	108
Hydropathy scale based on self-information values in the two-state model	41	103	-109	-148	-74	77	-47	128	169	-81	-104	-31	-90	10	-18	102	-35	36	104	116
Hydropathy scale based on self-information values in the two-state model	32	104	-95	-124	-73	82	-29	132	182	-82	-95	-34	-74	20	-22	118	-25	44	106	113
Hydropathy scale based on self-information values in the two-state model	24	103	-79	-9	-76	90	0	131	194	-85	-87	-36	-57	34	-28	116	-31	43	102	111
Hydropathy scale based on self-information values in the two-state model	5	82	-57	-38	-77	83	45	117	224	-103	-67	-41	-8	79	-47	130	-50	27	83	117
Hydropathy scale based on self-information values in the two-state model	-2	36	-41	115	-97	62	248	120	329	-132	-37	-52	117	174	-66	179	-70	-7	28	114
Averaged turn propensities in a transmembrane helix	0.4	0.3	1.5	1.4	1.6	0.5	1.5	0.3	0.7	1.6	1.4	0.9	1.3	0.7	1.1	0.9	1.4	0.9	0.5	0.4
Alpha-helix propensity derived from designed sequences	-0.04	-0.38	-0.30	-0.18	0.25	-0.09	0.27	-0.01	0.57	0	-0.02	0.15	-0.33	0.39	1.24	0.21	-0.11	0.05	-0.26	-0.06
Beta-sheet propensity derived from designed sequences	-0.12	0.15	0.34	0.29	1.05	-0.71	1.12	-0.67	-0.63	0	1.67	1.45	0.91	-0.70	0.76	-0.14	1.34	-0.49	-0.77	-0.70
Composition of amino acids in extracellular proteins	8.6	8.8	4.2	6.3	4.6	2.5	4.9	3.7	2.9	4.9	4.0	7.3	5.1	6.0	7.8	1.4	2.1	3.6	4.6	6.7
Composition of amino acids in anchored proteins	7.6	9.4	5.0	5.8	4.4	2.1	5.2	4.0	2.2	5.4	4.1	7.2	6.2	6.1	6.9	1.4	2.1	3.2	5.1	6.7
Composition of amino acids in membrane proteins	8.1	11.0	4.6	4.4	3.7	2.8	3.8	5.6	2.0	4.7	3.1	7.3	4.6	5.6	7.0	1.8	2.0	3.3	6.7	7.7
Composition of amino acids in intracellular proteins	7.9	8.6	4.9	6.7	4.0	2.4	5.5	3.9	1.9	5.3	4.4	6.6	7.1	5.3	7.1	1.2	2.1	3.1	5.2	6.8
Composition of amino acids in nuclear proteins	8.3	7.4	8.7	7.9	3.7	2.3	4.7	2.7	1.6	6.9	4.7	8.8	6.5	5.1	6.3	0.7	2.1	2.4	3.7	5.3
Surface composition of amino acids in intracellular proteins of thermophile	4.47	5.06	8.48	12.98	3.89	1.71	7.05	2.32	0.29	5.41	2.87	4.27	16.56	3.83	8.29	0.67	1.74	2.75	3.30	4.05
Surface composition of amino acids in intracellular proteins of mesophile	6.77	4.43	6.87	10.20	5.50	1.87	8.57	1.92	0.31	4.79	5.24	5.41	12.93	5.36	7.95	0.54	2.80	2.26	2.72	3.57
Surface composition of amino acids in extracellular proteins of mesophile	7.43	2.74	4.51	9.67	9.12	0.60	8.71	1.18	0.42	5.60	5.42	9.60	5.86	8.95	9.40	1.18	1.49	3.26	1.76	3.10
Surface composition of amino acids in nuclear proteins	5.22	4.52	7.30	12.68	6.06	1.85	7.91	1.68	1.01	5.70	6	6.99	10.66	5.16	5.81	0.56	2.27	2.16	2.36	4.10
Interior composition of amino acids in intracellular proteins of thermophile	9.88	13.21	3.71	3.39	2.35	2.44	3.50	5.27	1.12	3.80	1.66	4.10	4.02	4.98	6.88	1.11	1.88	4.07	10.08	12.53
Interior composition of amino acids in intracellular proteins of mesophile	10.98	12.79	3.26	2.54	2.85	3.10	3.37	4.97	1.47	3.42	2.30	4.93	3.51	5.55	7.48	1.28	2.20	3.55	9.74	10.69
Interior composition of amino acids in extracellular proteins of mesophile	9.95	9.66	3.05	2	4.84	2.45	4.46	5.41	1.30	3.20	2.64	6.03	2.58	5.62	8.87	2.60	1.99	6.15	7.73	9.46
Interior composition of amino acids in nuclear proteins	8.26	16.46	2.80	1.89	2.54	2.67	2.80	7.32	2.67	3.30	2.86	6	2.67	5	5.62	2.01	1.98	3.96	8.95	10.24
Entire chain composition of amino acids in intracellular proteins o	7.39	9.45	5.91	7.81	3.06	2.10	5.14	3.91	0.74	4.54	2.22	4.18	9.80	4.45	7.53	0.90	1.82	3.46	6.96	8.62
Entire chain composition of amino acids in intracellular proteins o	9.07	9	4.90	6.01	4.05	2.54	5.73	3.59	0.95	4.04	3.63	5.15	7.77	5.46	7.69	0.95	2.47	2.96	6.56	7.47
Entire chain composition of amino acids in extracellular proteins o	8.82	6.54	3.71	5.45	6.77	1.62	6.38	3.51	0.90	4.28	3.89	7.64	4.05	7.12	9.11	1.96	1.77	4.85	5.05	6.60
Entire chain compositino of amino acids in nuclear proteins	6.65	10.15	5.17	7.59	4.40	2.24	5.50	4.34	1.79	4.56	4.52	6.52	6.89	5.08	5.72	1.24	2.13	3.01	5.47	7
Screening coefficients gamma, local	0.163	0.315	0.220	0.255	0.124	0.356	0.212	0.410	0.316	0	0.274	0.290	0.212	0.412	0.080	0.325	0.315	0.354	0.474	0.515
Screening coefficients gamma, non-local	0.236	0.293	0.233	0.231	0.189	0.367	0.168	0.328	0.259	0	0.314	0.202	0.306	0.308	-0.170	0.197	0.256	0.223	0.391	0.436
Slopes tripeptide, FDPB VFF neutral	-0.490	-0.450	-0.429	-0.409	-0.387	-0.375	-0.375	-0.309	-0.352	0	-0.422	-0.426	-0.382	-0.240	-0.647	-0.325	-0.357	-0.288	-0.268	-0.220
Slopes tripeptides, LD VFF neutral	-0.871	-0.798	-0.727	-0.715	-0.741	-0.717	-0.737	-0.649	-0.666	0	-0.728	-0.679	-0.773	-0.629	-0.822	-0.669	-0.685	-0.655	-0.617	-0.599
Slopes tripeptide, FDPB VFF noside	-0.393	-0.281	-0.317	-0.294	-0.268	-0.274	-0.247	-0.189	-0.222	0	-0.291	-0.280	-0.260	-0.152	-0.570	-0.206	-0.244	-0.155	-0.144	-0.080
Slopes tripeptide FDPB VFF all	-0.378	-0.266	-0.369	-0.335	-0.245	-0.260	-0.113	-0.187	-0.206	0	-0.290	-0.251	-0.165	-0.093	-0.560	-0.188	-0.295	-0.147	-0.134	-0.084
Slopes tripeptide FDPB PARSE neutral	-0.729	-0.462	-0.535	-0.508	-0.597	-0.518	-0.545	-0.454	-0.408	0	-0.492	-0.278	-0.532	-0.367	-0.860	-0.455	-0.519	-0.439	-0.361	-0.323
Slopes dekapeptide, FDPB VFF neutral	-0.623	-0.527	-0.567	-0.581	-0.619	-0.571	-0.626	-0.461	-0.571	0	-0.559	-0.458	-0.572	-0.233	-0.679	-0.327	-0.508	-0.451	-0.199	-0.263
Slopes proteins, FDPB VFF neutral	-0.376	-0.317	-0.280	-0.412	-0.403	-0.312	-0.405	-0.237	-0.441	0	-0.362	-0.374	-0.362	-0.243	-0.392	-0.111	-0.345	-0.171	-0.194	-0.355
Side-chain conformation by gaussian evolutionary method	0	0.89	0.62	0.77	0.76	0.77	0.66	0.92	0.83	0.94	0.59	0.58	0.73	0.73	0	0.86	0.92	0.93	0.88	0.88
Amphiphilicity index	0	0	2.45	3.67	0	0	0	0	0	0	1.25	0	1.27	0	0	6.93	1.45	5.06	0	0
Volumes including the crystallographic waters using the ProtOr	89.3	163.1	190.3	165.1	122.4	165.8	114.4	190.8	102.5	121.6	146.9	94.2	138.8	119.6	63.8	226.4	157.5	194.6	163.0	138.2
Volumes not including the crystallographic waters using the ProtOr	90.0	164.0	194.0	167.3	124.7	167.0	117.3	191.9	103.3	122.9	149.4	95.4	142.2	121.5	64.9	228.2	160.0	197.0	163.9	139.0
Electron-ion interaction potential values	0.0373	0.0000	0.0959	0.0371	0.0036	0.0823	0.1263	0.0946	0.0829	0.0198	0.0761	0.0829	0.0058	0.0941	0.0050	0.0548	0.0242	0.0516	0.0000	0.0057
Hydrophobicity scales	0.85	1.99	0.20	-1.19	-0.48	1.42	-1.10	1.69	2.10	-1.14	-0.42	-0.52	-0.79	-0.08	0	1.76	0.22	1.37	3.14	2.53
Hydrophobicity coefficient in RP-HPLC, C18 with 0.1%TFA/MeCN/H2O	0.06	3.50	-0.85	-1.62	0.25	0.21	-0.20	4.80	0.49	0.71	0.31	-0.62	-0.10	0.65	0.21	2.29	-2.24	1.89	3.48	1.59
Hydrophobicity coefficient in RP-HPLC, C8 with 0.1%TFA/MeCN/H2O	2.62	6.57	1.26	-2.78	-1.27	-3.12	-2.84	9.14	0.73	-0.12	-1.69	-1.39	-0.45	1.81	-1.15	5.91	-0.74	1.39	4.38	2.30
Hydrophobicity coefficient in RP-HPLC, C4 with 0.1%TFA/MeCN/H2O	-1.64	0.83	-3.28	-2.36	0.83	4.26	0.70	-1.36	9.30	3.12	-0.04	1.59	1.18	2.31	-1.85	2.61	7.17	2.37	3.02	0.52
Hydrophobicity coefficient in RP-HPLC, C18 with 0.1%TFA/2-PrOH/MeCN/H2	-2.34	1.09	1.60	1.56	2.81	0.62	-0.48	2.57	5.03	-0.15	0.16	1.93	1.30	0.19	-1.06	3.59	-3	-2.58	7.26	2.06
Hydrophilicity scale	0.78	0.56	1.58	1.10	1.20	0.66	1.35	0.47	0.55	0.69	1.19	1	1.45	1.05	0.68	0.70	0.99	1	0.47	0.51
Retention coefficient at pH 2	25	100	-7	-26	-7	68	2	100	32	25	0	-2	14	7	-2	109	-26	56	91	62
Modified Kyte-Doolittle hydrophobicity scale	1.10	3.80	-5.10	-4.11	-3.50	1.90	-3.60	2.80	2.50	-1.90	-3.68	-0.50	-3.20	-0.70	-0.64	-0.46	-3.20	-1.3	4.50	4.2
Interactivity scale obtained from the contact matrix	0.1366	0.4251	0.0363	-0.0101	-0.0345	0.1747	-0.1233	0.4076	0.2745	0.0019	0.0325	-0.0433	-0.0484	0.0589	-0.0464	0.2362	0.0549	0.3167	0.4172	0.4084
Interactivity scale obtained by maximizing the mean of correlatio	0.0728	0.3819	0.0394	-0.0053	-0.0390	0.1613	-0.0552	0.4201	0.3557	-0.0492	0.0126	-0.0282	-0.0295	0.0239	-0.0589	0.4114	0.0874	0.3113	0.3805	0.2947
Interactivity scale obtained by maximizing the mean of correlatio	0.1510	0.3926	-0.0103	-0.0158	0.0381	0.2160	0.0047	0.3455	0.3222	0.0844	0.0246	0.0040	-0.0639	0.1462	0.0248	0.2657	0.1335	0.2998	0.4238	0.3997
Linker propensity index	-0.058	0.138	0.000	-0.112	0.027	0.275	0.016	0.240	0.447	-0.478	-0.073	-0.177	-0.128	-0.163	0.331	0.564	0.195	0.322	0.060	-0.052
Knowledge-based membrane-propensity scale from 1D_Helix in MPtopo database	-0.17	-0.28	0.37	0.32	0.18	-0.26	0.37	-0.41	-0.06	0.13	0.26	0.05	0.15	0.02	0.01	-0.15	-0.02	-0.09	-0.28	-0.17
Knowledge-based membrane-propensity scale from 3D_Helix in MPtopo database	-0.15	-0.36	0.32	0.24	0.22	-0.19	0.41	-0.22	-0.15	0.15	0.03	0.16	0.30	-0.08	0.08	-0.28	0.06	-0.03	-0.29	-0.24
Linker propensity from all dataset	0.964	1.085	1.143	0.944	0.944	1.032	0.916	1.119	0.778	1.299	1.047	0.947	1.051	1.017	0.835	0.895	1.014	1	0.922	0.955
Linker propensity from 1-linker dataset	0.974	1.11	1.129	0.946	0.988	0.923	0.892	1.122	0.972	1.362	1.092	0.932	1.054	1.023	0.845	0.879	0.949	0.902	0.928	0.923
Linker propensity from 2-linker dataset	0.938	1	1.137	0.952	0.902	1.077	0.857	1.11	0.6856	1.266	0.916	0.956	1.139	1.018	0.892	0.971	1.109	1.157	0.986	0.959
Linker propensity from 3-linker dataset	1.042	1.193	1.069	0.979	0.828	0.998	0.97	0.981	0.5	1.332	1.111	0.984	0.992	0.992	0.743	0.96	1.034	1.12	0.852	1.001
Linker propensity from small dataset	1.065	1.192	1.131	0.478	0.762	1.369	0.836	1.368	1.015	1.241	0.861	1.097	0.736	0.822	1.022	1.017	0.973	0.836	1.189	1.14
Linker propensity from medium dataset	0.99	1.106	1.132	1.003	0.873	1.093	0.915	1.121	0.644	1.314	0.999	0.911	1.053	0.988	0.785	0.939	1.054	1.09	0.95	0.957
Linker propensity from long dataset	0.892	0.994	1.154	0.944	1.144	0.782	0.925	1.058	1.035	1.309	1.2	0.986	1.115	1.11	0.917	0.841	0.992	0.866	0.817	0.9
Linker propensity from helical	1.092	1.276	1.239	1.008	0.927	1.171	0.919	1.09	0.662	0.8	1.124	0.886	1.199	0.832	0.698	0.981	1.012	1.075	0.912	0.908
Linker propensity from non-helical	0.843	0.885	1.038	0.893	0.956	0.878	0.906	1.151	0.896	1.816	0.968	1.003	0.9	1.189	0.978	0.852	1.05	0.945	0.946	0.999
The stability scale from the knowledge-based atom-atom potential	2.18	4.71	2.71	2.12	1.85	3.63	1.75	5.88	3.89	2.09	2.16	1.66	1.89	2.18	1.17	6.46	2.51	5.01	4.50	3.77
The relative stability scale extracted from mutation experiments	1.79	4.72	3.20	2.50	2.83	3.91	2.33	4.84	2.22	2.45	2.37	1.82	2.52	2.45	0.70	5.64	3.06	4.46	4.59	3.67
Buriability	13.4	20.8	8.5	6.1	7.6	15.7	8.2	23.9	22.6	9.9	8.5	8.2	7.3	10.3	7.0	24.5	11.3	19.5	20.3	19.5
Linker index	0.0166	0.2523	-0.0762	-0.2134	-0.0786	0.0197	-0.1278	0.3561	0.5724	-0.4188	-0.1051	-0.1629	-0.1794	-0.0701	-0.0442	0.3836	0.1643	0.2500	0.2758	0.1782
Mean volumes of residues buried in protein interiors	90.1	164.6	192.8	170.0	127.5	167.7	117.1	193.5	113.2	123.1	149.4	94.2	140.8	120.0	63.8	197.1	159.3	231.7	164.9	139.1
Average volumes of residues	91.5	163.4	196.1	162.5	138.3	165.9	135.2	198.8	114.4	123.4	156.4	102.0	154.6	126.0	67.5	209.8	163.2	237.2	162.6	138.4
Hydrostatic pressure asymmetry index, PAI	1.076	1.054	1.361	1.105	1.056	0.974	1.290	0.869	0.753	0.820	0.729	1.342	1.118	0.871	1.346	0.666	0.985	0.531	0.926	1.131
Hydrophobicity index	1.12	1.18	-2.55	-0.80	-0.83	0.55	-0.83	0.67	0.59	0.54	-0.78	-0.05	-0.92	-0.02	1.20	-0.19	-0.93	-0.23	1.16	1.13
Average internal preferences	1.38	1.47	0	0.15	0.37	1.78	0.52	1.72	1.43	0.85	0.22	0.86	0.71	0.89	1.34	0.82	0.66	0.47	2.32	1.99
Hydrophobicity-related index	-0.27	-1.10	1.87	1.70	0.81	-0.73	0.81	-1.43	-1.05	-0.75	1.10	0.42	1.17	0.63	-0.16	-1.57	0.28	-0.56	-0.77	-0.40
Apparent partition energies calculated from Wertz-Scheraga index	0.05	-0.62	0.12	0.57	0.29	-0.38	0.41	-0.45	-0.84	0.46	0.46	0.12	0.38	0.38	0.31	-0.98	-0.41	-0.25	-0.69	-0.46
Apparent partition energies calculated from Robson-Osguthorpe index	0.54	-1.08	-0.16	0.48	0.38	-0.97	0.65	-1.51	-1.13	-0.22	0.05	0.65	0.38	0.27	0	-1.61	-0.59	-1.13	-2.15	-0.75
Apparent partition energies calculated from Janin index	-0.31	-0.53	1.30	1.79	0.49	-0.38	0.58	-0.45	-0.87	0.34	0.70	0.10	0.68	0.21	-0.33	-0.27	0.13	0.40	-0.66	-0.62
Apparent partition energies calculated from Chothia index	-0.27	-0.44	2	1.17	0.61	-0.31	0.50	-0.55	-0.23	0.36	1	0.17	0.33	0.18	-0.22	0.05	0.37	0.48	-0.80	-0.65
Hydropathies of amino acid side chains, neutral form	0.39	1.82	0	0.32	-1.91	0.96	-0.71	2.27	0.25	0	-1.30	-1.24	-0.18	-1	0	2.13	-0.60	1.47	1.82	1.30
Hydropathies of amino acid side chains, pi-values in pH 7.0	0.39	1.82	-3.95	-2.77	-1.91	0.96	-3.81	2.27	0.25	0	-1.30	-1.24	-2.91	-1	0	2.13	-0.64	1.47	1.82	1.30
Weights from the IFH scale	0.18	0.41	-5.40	-2.53	-1.30	0.44	-2.36	0.50	0.27	-0.20	-1.22	-0.40	-2.10	-0.34	0.09	-0.01	-1.48	-0.08	0.37	0.32
Hydrophobicity index, 3.0 pH	0.42	1.80	-1.56	-2.03	-1.03	1.18	-0.51	1.74	0.84	0.86	-0.96	-0.64	-0.37	-0.26	0	1.46	-2.28	0.51	1.81	1.34
Scaled side chain hydrophobicity values	0.616	0.943	0.000	0.283	0.236	0.738	0.028	1.000	0.680	0.711	0.251	0.359	0.043	0.450	0.501	0.878	0.165	0.880	0.943	0.825
Hydrophobicity scale from native protein structures	0.2	0.5	-0.7	-1.6	-0.5	0.5	-1.4	1.0	1.9	-1.0	-1.1	-0.7	-1.3	-0.4	-0.1	1.6	0.4	0.5	1.4	0.7
NNEIG index	50.76	53.89	48.66	42.92	45.80	52.75	43.17	53.45	58.74	45.39	46.09	47.24	43.48	49.26	50.27	53.59	49.33	51.79	57.30	56.12
SWEIG index	-0.414	1.215	-0.584	-0.670	-0.916	1.020	-1.310	1.938	0.162	-0.503	-0.905	-0.563	-1.218	-0.289	-0.684	0.514	-0.630	1.699	1.237	0.899
PRIFT index	-0.96	6.81	0.75	-5.62	-1.94	4.76	-5.68	5.06	4.54	-4.47	-5.30	-1.92	-3.86	-3.99	-1.28	0.21	-0.62	3.34	5.54	5.39
PRILS index	-0.26	1.52	0.08	-1.01	-0.46	1.09	-1.30	1.09	0.83	-0.62	-0.83	-0.55	-0.73	-0.71	-0.40	-0.13	-0.18	0.69	1.10	1.15
ALTFT index	-0.73	4.91	-1.03	-5.99	-5.29	3.34	-6.13	5.20	0.64	-4.32	-0.96	-3	-2.90	-1.91	-2.67	0.51	3.03	2.87	5.04	3.98
ALTLS index	-1.35	9.88	-3.89	-11.92	-10.96	7.47	-11.88	11.35	4.37	-10.86	-1.34	-6.21	-4.56	-4.83	-5.82	1.80	6.54	7.61	10.93	8.20
TOTFT index	-0.56	4.09	-0.26	-4.08	-2.87	3.11	-4.31	3.67	1.78	-3.22	-2.31	-1.85	-2.35	-1.97	-1.35	-0.11	0.81	2.17	3.83	3.31
TOTLS index	1.37	-8.68	1.33	7.70	6.29	-7.13	8.93	-7.96	-4.47	6.25	3.88	4.08	4.04	4.02	3.39	0.79	-1.65	-4.73	-7.92	-6.94
Relative partition energies derived by the Bethe approximatio	-0.02	-2.29	0.44	1.01	0.63	-1.36	0.72	-2.22	-0.96	0.47	0.56	0.55	0.74	0.25	0.38	-1.28	0	-0.88	-1.89	-1.34
Optimized relative partition energies - method A	0	-0.37	0.07	0.17	0.10	-0.22	0.12	-0.36	-0.16	0.08	0.09	0.09	0.12	0.04	0.06	-0.21	0	-0.14	-0.31	-0.22
Optimized relative partition energies - method B	-0.03	-0.38	0.09	0.32	0.13	-0.30	0.17	-0.34	-0.36	0.20	0.13	0.10	0.23	0.01	0.09	-0.24	-0.04	-0.23	-0.33	-0.29
Optimized relative partition energies - method C	-0.04	-0.37	0.07	0.33	0.13	-0.30	0.19	-0.38	-0.38	0.19	0.14	0.12	0.23	0.03	0.09	-0.33	-0.04	-0.29	-0.34	-0.29
Optimized relative partition energies - method D	-0.02	-0.32	0.08	0.30	0.10	-0.25	0.19	-0.33	-0.32	0.11	0.15	0.11	0.21	0.05	-0.02	-0.27	-0.02	-0.23	-0.28	-0.23
Hydrophobicity index	-1.6	-2.8	12.3	8.8	4.8	-3.4	9.2	-3.7	-2.0	0.2	4.1	-0.6	8.2	-1.2	-1.0	-1.9	3.0	0.7	-3.1	-2.6
Hydrophobicity index	-0.21	-4.68	2.11	3.88	0.96	-3.66	1.36	-4.65	-6.04	0.75	1.52	1.74	2.30	0.78	0	-3.32	-1.23	-1.01	-4.81	-3.50
Number of vertices	2	5	8	6	5	5	5	8	3	4	6	3	6	4	1	11	7	9	5	4
Number of edges	1	4	7	5	4	4	4	8	2	4	5	2	5	3	0	12	6	9	4	3
Total weighted degree of the graph	2	8	12	10	8	8	8	14	4	8	10	4	10	6	0	24	14	18	8	6
Weighted domination number	1	4	6	4	4	4	4	6	2	4	4	2	5	3	1	8	6.000	7	4	3
Average eccentricity	1	5	8.120	7	5	5.40	5.17	7	2.33	4	5.860	1.670	6	3.250	0	11.10	6.71	8.88	3.25	3.25
Radius	1	3	6	5	3	3	3	6.000	1	4	4	2	4	1	0	9.000	6.000	6.000	3	1
Diameter	1	6	12	9	6	7	6	11.000	3	4.000	8	3	8	4	0	14.000	9	13.000	6	4
Average weighted degree	1	1.60	1.50	1.667	1.60	1.60	1.60	1.750	1.333	2	1.667	1.333	1.667	1.50	0	2.182	2	2.000	1.600	1.50
Maximum eigenvalue of the weighted Laplacian matrix of the grap	2	11.029	12.499	10.363	11.539	9.49	11.539	14.851	6.243	12	12.207	5	11.530	9.928	0	13.511	12.876	12.868	10.851	9.928
Minimum eigenvalue of the weighted Laplacian matrix of the grap	0	-4.729	-4.307	-3.151	-4.178	-2.812	-4.178	-4.801	-2.243	-4	-4.255	1	-3.425	-3.928	0	-6.324	-3.721	-4.793	-6.085	-3.928
Average eigenvalue of the Laplacian matrix of the the grap	1	3.20	3.500	3	3.20	2.80	3.20	4.25	2	4	3.333	2	3.333	3	0	4	4.286	4.333	1.80	3
Second smallest eigenvalue of the Laplacian matrix of the grap	2	1.052	-2.590	-0.536	0.528	0.678	0.528	-1.672	2	4	-1.043	2	-0.538	3	0	-2.576	-1.185	-2.054	-1.517	3
Weighted domination number using the atomic number	6	12	19	12	12	18	12	18	6	12	12	6	12	6	1	24	15	18	12	6
Average weighted eccentricity based on the the atomic numbe	6	15.60	31.444	24.50	16.50	27.20	16.40	23.25	16.670	12	21.167	13.33	21	12.40	3.50	27.50	23.10	27.78	15.60	10.50
Weighted radius based on the atomic number	6	12	20	18	14	18	12	18	12	12	15	8	14	8	1	18	18	20	12	6
Weighted diameter based on the atomic number	6	18	38	31	20	34	20	24	22	12	24	20	26	14	6	36	31	38	18	12
Total weighted atomic number of the graph	12	30	45	37	33.007	40	34	48	28	24	39	22	40	27	7	68	47	56	30	24.007
Average weighted atomic number or degree based on atomic number in the grap	6	6	5	6.17	6.60	8	6.80	6	9.33	6	6.50	7.33	6.67	5.40	3.50	5.667	4.70	6.22	6	6
Weighted maximum eigenvalue based on the atomic number	12	25.021	23.343	22.739	27.708	31.344	28.634	26.993	28	24	27.831	20	28.731	23.819	7	29.778	24.243	28.252	24.841	24
Weighted minimum eigenvalue based on the atomic number	0	0	0	-0.179	0	0	0	0	0	0	0	0	0	-4.227	0	0.211	-1.734	-0.96	-1.641	0
Weighted average eigenvalue based on the atomic number	6	9.60	10.667	10.167	10	13.60	10.40	12	11.333	12	10.50	8.667	10.667	9	3.50	12.75	10.400	12.222	9.60	9
Weighted second smallest eigenvalue of the weighted Laplacian matri	0	3.113	4.20	1.372	3	2.656	2.969	2.026	6	12	1.849	6	1.822	6	0	2.044	1.605	1.599	3.373	6