Bork Group Sunyaev Lab
PolyPhen report
New Prediction
 
Citation Help
refSNP Predictions found for proteins:
rs671 P05091

 
Query
Acc number Position AA1 AA2 Description
P05091 504 E K Aldehyde dehydrogenase, mitochondrial precursor (EC 1.2.1.3) (ALDH class 2) (ALDHI) (ALDH-E2). LENGTH: 517 AA

Prediction
This variant is predicted to be possibly damaging
Prediction Available data Prediction basis Substitution effect Prediction data
possibly
damaging
FT
alignment
structure
structure 1.1.1: structural effect, buried site, hydrophobicity
Hydrophobicity change at buried site
PSIC score difference: 1.078
normed accessibility: 0.07
hydrophobicity change: 1.3
Remarks
Closest contact with ligand: GAI, distance 4.364
Closest contact with other chains: ARG 475D, distance 2.719
Charge change at buried site: substitution E -> K, normed accessibility: 0.07

Details
Sequence features of the substitution site
Region Site Feature table Critical sites
N/A N/A show FT fields for P05091 285, 319
PSIC profile scores for two amino acid variants
Score1 Score2 |Score1-Score2| Observations Diagnostics Multiple alignment around substitution position
+1.490 +0.412 1.078 127 precomputed Sequences:  Flanks:  
Mapping of the substitution site to known protein 3D structures
Database Initial number of structures Number of structures
PQS 155 90

Num ID   Res AA E-value Len Ide Gaps Params Cont PDB TITLE
1 1o01_1 C 487 E 0.0e+00 495 1.00 Params Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
2 1o05_2 H 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
3 1o05_2 G 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
4 1o05_2 F 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
5 1o05_2 E 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
6 1o05_1 D 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
7 1o05_1 C 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
8 1o05_1 B 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
9 1o05_1 A 487 E 0.0e+00 494 1.00   Chain APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
10 1o02_2 H 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
11 1o02_2 G 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
12 1o02_2 F 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
13 1o02_2 E 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
14 1o02_1 D 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
15 1o02_1 C 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
16 1o02_1 B 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
17 1o02_1 A 487 E 0.0e+00 494 1.00   Het
Chain
NADH IN THE PRESENCE OF MG2+
18 1o01_2 H 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
19 1o01_2 G 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
20 1o01_2 F 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
21 1o01_2 E 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
22 1o01_1 D 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
23 1o01_1 B 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
24 1o01_1 A 487 E 0.0e+00 494 1.00   Het
Chain
CROTONALDEHYDE, NAD(H) AND MG2+
25 1o00_2 H 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
26 1o00_2 G 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
27 1o00_2 F 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
28 1o00_2 E 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
29 1o00_1 D 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
30 1o00_1 C 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
31 1o00_1 B 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
32 1o00_1 A 487 E 0.0e+00 494 1.00   Chain NAD+ AND MG2+ SHOWING DUAL NAD(H) CONFORMATIONS
33 1nzz_2 H 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
34 1nzz_2 G 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
35 1nzz_2 F 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
36 1nzz_2 E 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
37 1nzz_1 D 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
38 1nzz_1 C 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
39 1nzz_1 B 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
40 1nzz_1 A 487 E 0.0e+00 494 1.00   Chain NADH IN THE PRESENCE OF LOW MG2+
41 1nzx_2 H 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
42 1nzx_2 G 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
43 1nzx_2 F 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
44 1nzx_2 E 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
45 1nzx_1 D 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
46 1nzx_1 C 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
47 1nzx_1 B 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
48 1nzx_1 A 487 E 0.0e+00 494 1.00   Chain NAD+ IN THE PRESENCE OF LOW MG2+
49 1cw3 H 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
50 1cw3 G 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
51 1cw3 F 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
52 1cw3 E 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
53 1cw3 D 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
54 1cw3 C 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
55 1cw3 B 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
56 1cw3 A 487 E 0.0e+00 494 1.00   Chain NAD+ AND MN2+
57 1o04_2 H 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
58 1o04_2 G 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
59 1o04_2 F 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
60 1o04_2 E 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
61 1o04_1 D 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
62 1o04_1 C 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
63 1o04_1 B 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
64 1o04_1 A 487 E 0.0e+00 494 1.00   Het
Chain
DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
65 1nzw_2 H 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
66 1nzw_2 G 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
67 1nzw_2 F 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
68 1nzw_2 E 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
69 1nzw_1 D 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
70 1nzw_1 C 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
71 1nzw_1 B 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
72 1nzw_1 A 487 E 0.0e+00 494 1.00   Chain DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
73 1ag8 D 487 E 0.0e+00 493 0.94   Chain ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
74 1ag8 C 487 E 0.0e+00 493 0.94   Chain ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
75 1ag8 B 487 E 0.0e+00 493 0.94   Chain ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
76 1ag8 A 487 E 0.0e+00 493 0.94   Chain ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
77 1a4z D 487 E 0.0e+00 493 0.94   Chain NAD (REDUCED) AND SAMARIUM (III)
78 1a4z C 487 E 0.0e+00 493 0.94   Chain NAD (REDUCED) AND SAMARIUM (III)
79 1a4z B 487 E 0.0e+00 493 0.94   Chain NAD (REDUCED) AND SAMARIUM (III)
80 1a4z A 487 E 0.0e+00 493 0.94   Chain NAD (REDUCED) AND SAMARIUM (III)
81 1bxs D 487 E 0.0e+00 493 0.68   Chain SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND
82 1bxs C 487 E 0.0e+00 493 0.68   Chain SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND
83 1bxs B 487 E 0.0e+00 493 0.68   Chain SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND
84 1bxs A 487 E 0.0e+00 493 0.68   Chain SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND
85 1bi9 D 487 E 0.0e+00 498 0.67 17   Chain RETINAL DEHYDROGENASE TYPE TWO WITH NAD BOUND
86 1bi9 C 487 E 0.0e+00 498 0.67 19     RETINAL DEHYDROGENASE TYPE TWO WITH NAD BOUND
87 1o9j D 487 E 0.0e+00 493 0.66   Chain THE X-RAY CRYSTAL STRUCTURE OF ETA-CRYSTALLIN
88 1o9j C 487 E 0.0e+00 493 0.66   Chain THE X-RAY CRYSTAL STRUCTURE OF ETA-CRYSTALLIN
89 1o9j B 487 E 0.0e+00 493 0.66   Chain THE X-RAY CRYSTAL STRUCTURE OF ETA-CRYSTALLIN
90 1o9j A 487 E 0.0e+00 493 0.66   Chain THE X-RAY CRYSTAL STRUCTURE OF ETA-CRYSTALLIN

Structural parameters
Num ID   Res SecStr Acc Acc Normed dPropens (Phi, Psi) Map Region dVol Normed B-factor
1 1o01_1 C 487 E 14 0.07 1.3 (-114.3, 122.8) B 30 -0.31

Contacts
Num ID   Res Heteroatoms Interchain Critical sites
  1 1o01_1 C 487 4803C GAI 4.681
467D GLY 3.339
468D TYR 3.483
469D LYS 5.430
472D GLY 5.304
473D SER 5.530
474D GLY 5.395
475D ARG 2.890
 
  2 1o05_2 H 487   467G GLY 3.386
468G TYR 3.506
469G LYS 5.528
472G GLY 5.318
473G SER 5.421
474G GLY 5.326
475G ARG 2.886
 
  3 1o05_2 G 487   467H GLY 3.356
468H TYR 3.548
469H LYS 5.499
472H GLY 5.424
473H SER 5.649
474H GLY 5.457
475H ARG 2.972
 
  4 1o05_2 F 487   467E GLY 3.468
468E TYR 3.431
469E LYS 5.390
472E GLY 5.397
473E SER 5.614
474E GLY 5.503
475E ARG 2.913
 
  5 1o05_2 E 487   467F GLY 3.458
468F TYR 3.451
469F LYS 5.567
472F GLY 5.377
473F SER 5.629
474F GLY 5.469
475F ARG 2.941
 
  6 1o05_1 D 487   467C GLY 3.584
468C TYR 3.554
469C LYS 5.753
472C GLY 5.470
473C SER 5.579
474C GLY 5.323
475C ARG 2.860
 
  7 1o05_1 C 487   467D GLY 3.655
468D TYR 3.461
469D LYS 5.561
472D GLY 5.520
473D SER 5.525
474D GLY 5.322
475D ARG 2.944
 
  8 1o05_1 B 487   467A GLY 3.550
468A TYR 3.613
469A LYS 5.711
472A GLY 5.486
473A SER 5.561
474A GLY 5.339
475A ARG 2.899
 
  9 1o05_1 A 487   467B GLY 3.487
468B TYR 3.530
469B LYS 5.616
472B GLY 5.341
473B SER 5.438
474B GLY 5.279
475B ARG 2.888
 
  10 1o02_2 H 487 4808H GAI 4.634
467G GLY 3.265
468G TYR 3.379
469G LYS 5.571
472G GLY 5.368
473G SER 5.517
474G GLY 5.314
475G ARG 2.898
 
  11 1o02_2 G 487 4807G GAI 4.609
467H GLY 3.456
468H TYR 3.466
469H LYS 5.655
472H GLY 5.363
473H SER 5.548
474H GLY 5.363
475H ARG 2.903
 
  12 1o02_2 F 487 4806F GAI 4.607
467E GLY 3.333
468E TYR 3.518
469E LYS 5.509
472E GLY 5.344
473E SER 5.446
474E GLY 5.352
475E ARG 2.883
 
  13 1o02_2 E 487 4805E GAI 4.635
467F GLY 3.395
468F TYR 3.468
469F LYS 5.604
472F GLY 5.374
473F SER 5.502
474F GLY 5.350
475F ARG 2.892
 
  14 1o02_1 D 487 4804D GAI 4.619
467C GLY 3.327
468C TYR 3.516
469C LYS 5.608
472C GLY 5.339
473C SER 5.492
474C GLY 5.356
475C ARG 2.801
 
  15 1o02_1 C 487 4803C GAI 4.619
467D GLY 3.416
468D TYR 3.527
469D LYS 5.599
472D GLY 5.335
473D SER 5.504
474D GLY 5.420
475D ARG 2.839
 
  16 1o02_1 B 487 4802B GAI 4.741
467A GLY 3.373
468A TYR 3.432
469A LYS 5.582
472A GLY 5.254
473A SER 5.377
474A GLY 5.270
475A ARG 2.930
 
  17 1o02_1 A 487 4801A GAI 4.464
467B GLY 3.343
468B TYR 3.493
469B LYS 5.496
472B GLY 5.284
473B SER 5.500
474B GLY 5.361
475B ARG 2.911
 
  18 1o01_2 H 487 4808H GAI 4.861
467G GLY 3.243
468G TYR 3.510
469G LYS 5.266
472G GLY 5.162
473G SER 5.448
474G GLY 5.347
475G ARG 2.950
 
  19 1o01_2 G 487 4807G GAI 4.592
467H GLY 3.477
468H TYR 3.466
469H LYS 5.452
472H GLY 5.338
473H SER 5.537
474H GLY 5.291
475H ARG 2.792
 
  20 1o01_2 F 487 4806F GAI 4.550
467E GLY 3.351
468E TYR 3.489
469E LYS 5.423
472E GLY 5.385
473E SER 5.404
474E GLY 5.285
475E ARG 2.832
 
  21 1o01_2 E 487 4805E GAI 4.697
467F GLY 3.378
468F TYR 3.549
469F LYS 5.515
472F GLY 5.463
473F SER 5.514
474F GLY 5.268
475F ARG 2.887
 
  22 1o01_1 D 487 4804D GAI 4.442
467C GLY 3.401
468C TYR 3.519
469C LYS 5.425
472C GLY 5.330
473C SER 5.397
474C GLY 5.252
475C ARG 2.875
 
  23 1o01_1 B 487 4802B GAI 4.528
467A GLY 3.470
468A TYR 3.517
469A LYS 5.499
472A GLY 5.238
473A SER 5.357
474A GLY 5.203
475A ARG 2.871
 
  24 1o01_1 A 487 0.000
467B GLY 3.327
468B TYR 3.517
469B LYS 5.335
472B GLY 5.158
473B SER 5.372
474B GLY 5.245
475B ARG 2.907
 
  25 1o00_2 H 487   467G GLY 3.318
468G TYR 3.484
469G LYS 5.595
472G GLY 5.343
473G SER 5.574
474G GLY 5.390
475G ARG 2.843
 
  26 1o00_2 G 487   467H GLY 3.384
468H TYR 3.467
469H LYS 5.622
472H GLY 5.432
473H SER 5.664
474H GLY 5.424
475H ARG 2.754
 
  27 1o00_2 F 487   467E GLY 3.487
468E TYR 3.486
469E LYS 5.521
472E GLY 5.505
473E SER 5.639
474E GLY 5.439
475E ARG 2.932
 
  28 1o00_2 E 487   467F GLY 3.358
468F TYR 3.524
469F LYS 5.437
472F GLY 5.303
473F SER 5.618
474F GLY 5.405
475F ARG 2.924
 
  29 1o00_1 D 487   467C GLY 3.389
468C TYR 3.488
469C LYS 5.561
472C GLY 5.341
473C SER 5.517
474C GLY 5.311
475C ARG 2.859
 
  30 1o00_1 C 487   467D GLY 3.378
468D TYR 3.508
469D LYS 5.463
472D GLY 5.418
473D SER 5.629
474D GLY 5.486
475D ARG 2.953
 
  31 1o00_1 B 487   467A GLY 3.490
468A TYR 3.560
469A LYS 5.639
472A GLY 5.470
473A SER 5.585
474A GLY 5.336
475A ARG 2.961
 
  32 1o00_1 A 487   467B GLY 3.367
468B TYR 3.498
469B LYS 5.566
472B GLY 5.394
473B SER 5.571
474B GLY 5.340
475B ARG 2.843
 
  33 1nzz_2 H 487   467G GLY 3.426
468G TYR 3.528
469G LYS 5.578
472G GLY 5.291
473G SER 5.608
474G GLY 5.411
475G ARG 3.141
 
  34 1nzz_2 G 487   467H GLY 3.970
468H TYR 3.432
469H LYS 5.476
472H GLY 5.731
473H SER 5.896
474H GLY 5.530
475H ARG 2.792
 
  35 1nzz_2 F 487   467E GLY 3.548
468E TYR 3.420
469E LYS 5.423
472E GLY 5.254
473E SER 5.516
474E GLY 5.436
475E ARG 2.981
 
  36 1nzz_2 E 487   467F GLY 3.653
468F TYR 3.462
469F LYS 5.551
472F GLY 5.486
473F SER 5.736
474F GLY 5.473
475F ARG 2.963
 
  37 1nzz_1 D 487   467C GLY 3.609
468C TYR 3.478
469C LYS 5.662
472C GLY 5.572
473C SER 5.808
474C GLY 5.563
475C ARG 2.771
 
  38 1nzz_1 C 487   467D GLY 3.675
468D TYR 3.424
469D LYS 5.592
472D GLY 5.320
473D SER 5.602
474D GLY 5.529
475D ARG 3.119
 
  39 1nzz_1 B 487   467A GLY 3.662
468A TYR 3.553
469A LYS 5.663
472A GLY 5.312
473A SER 5.512
474A GLY 5.324
475A ARG 2.957
 
  40 1nzz_1 A 487   467B GLY 3.776
468B TYR 3.537
469B LYS 5.768
472B GLY 5.552
473B SER 5.678
474B GLY 5.338
475B ARG 2.722
 
  41 1nzx_2 H 487   467G GLY 3.260
468G TYR 3.577
469G LYS 5.385
472G GLY 5.097
473G SER 5.417
474G GLY 5.373
475G ARG 3.255
 
  42 1nzx_2 G 487   467H GLY 3.548
468H TYR 3.626
469H LYS 5.696
472H GLY 5.426
473H SER 5.616
474H GLY 5.421
475H ARG 2.842
 
  43 1nzx_2 F 487   467E GLY 3.375
468E TYR 3.336
469E LYS 5.554
472E GLY 5.339
473E SER 5.544
474E GLY 5.374
475E ARG 2.801
 
  44 1nzx_2 E 487   467F GLY 3.473
468F TYR 3.540
469F LYS 5.606
472F GLY 5.270
473F SER 5.500
474F GLY 5.303
475F ARG 3.109
 
  45 1nzx_1 D 487   467C GLY 3.438
468C TYR 3.590
469C LYS 5.584
472C GLY 5.380
473C SER 5.608
474C GLY 5.404
475C ARG 2.808
 
  46 1nzx_1 C 487   467D GLY 3.724
468D TYR 3.442
469D LYS 5.834
472D GLY 5.491
473D SER 5.621
474D GLY 5.402
475D ARG 3.010
 
  47 1nzx_1 B 487   467A GLY 3.365
468A TYR 3.620
469A LYS 5.402
472A GLY 5.192
473A SER 5.484
474A GLY 5.404
475A ARG 2.936
 
  48 1nzx_1 A 487   467B GLY 3.422
468B TYR 3.560
469B LYS 5.612
472B GLY 5.255
473B SER 5.478
474B GLY 5.263
475B ARG 2.857
 
  49 1cw3 H 487   467G GLY 3.519
468G TYR 3.440
469G LYS 5.658
472G GLY 5.509
473G SER 5.509
474G GLY 5.347
475G ARG 2.956
 
  50 1cw3 G 487   467H GLY 3.424
468H TYR 3.425
469H LYS 5.526
472H GLY 5.518
473H SER 5.571
474H GLY 5.409
475H ARG 2.795
 
  51 1cw3 F 487   467E GLY 3.513
468E TYR 3.531
469E LYS 5.264
472E GLY 5.378
473E SER 5.323
474E GLY 5.189
475E ARG 3.039
 
  52 1cw3 E 487   467F GLY 3.608
468F TYR 3.330
469F LYS 5.608
472F GLY 5.550
473F SER 5.540
474F GLY 5.197
475F ARG 2.870
 
  53 1cw3 D 487   467C GLY 3.204
468C TYR 3.338
469C LYS 5.350
472C GLY 5.222
473C SER 5.376
474C GLY 5.273
475C ARG 2.768
 
  54 1cw3 C 487   467D GLY 3.146
468D TYR 3.375
469D LYS 5.230
472D GLY 5.336
473D SER 5.523
474D GLY 5.421
475D ARG 2.895
 
  55 1cw3 B 487   467A GLY 3.413
468A TYR 3.450
469A LYS 5.654
472A GLY 5.465
473A SER 5.582
474A GLY 5.257
475A ARG 2.791
 
  56 1cw3 A 487   467B GLY 3.475
468B TYR 3.547
469B LYS 5.643
472B GLY 5.599
473B SER 5.515
474B GLY 5.278
475B ARG 2.813
 
  57 1o04_2 H 487 6808H GAI 4.702
467G GLY 3.225
468G TYR 3.439
469G LYS 5.585
472G GLY 5.253
473G SER 5.448
474G GLY 5.317
475G ARG 2.945
 
  58 1o04_2 G 487 6807G GAI 4.682
467H GLY 3.247
468H TYR 3.477
469H LYS 5.592
472H GLY 5.195
473H SER 5.467
474H GLY 5.316
475H ARG 2.916
 
  59 1o04_2 F 487 6806F GAI 4.627
467E GLY 3.216
468E TYR 3.428
469E LYS 5.548
472E GLY 5.211
473E SER 5.414
474E GLY 5.374
475E ARG 2.924
 
  60 1o04_2 E 487 6805E GAI 4.627
467F GLY 3.277
468F TYR 3.488
469F LYS 5.593
472F GLY 5.237
473F SER 5.531
474F GLY 5.414
475F ARG 2.935
 
  61 1o04_1 D 487 6804D GAI 4.618
467C GLY 3.298
468C TYR 3.471
469C LYS 5.635
472C GLY 5.253
473C SER 5.494
474C GLY 5.357
475C ARG 2.911
 
  62 1o04_1 C 487 6803C GAI 4.642
467D GLY 3.250
468D TYR 3.494
469D LYS 5.592
472D GLY 5.219
473D SER 5.416
474D GLY 5.363
475D ARG 2.880
 
  63 1o04_1 B 487 6802B GAI 4.563
467A GLY 3.208
468A TYR 3.455
469A LYS 5.553
472A GLY 5.230
473A SER 5.417
474A GLY 5.350
475A ARG 2.922
 
  64 1o04_1 A 487 6801A GAI 4.644
467B GLY 3.217
468B TYR 3.484
469B LYS 5.630
472B GLY 5.231
473B SER 5.497
474B GLY 5.348
475B ARG 2.864
 
  65 1nzw_2 H 487   467G GLY 3.711
468G TYR 3.539
469G LYS 5.870
472G GLY 5.532
473G SER 5.486
474G GLY 5.203
475G ARG 3.078
 
  66 1nzw_2 G 487   467H GLY 3.816
468H TYR 3.505
469H LYS 5.561
472H GLY 5.661
473H SER 5.645
474H GLY 5.325
475H ARG 2.903
 
  67 1nzw_2 F 487   467E GLY 3.491
468E TYR 3.429
469E LYS 5.484
472E GLY 5.352
473E SER 5.530
474E GLY 5.474
475E ARG 2.869
 
  68 1nzw_2 E 487   467F GLY 3.433
468F TYR 3.510
469F LYS 5.603
472F GLY 5.433
473F SER 5.540
474F GLY 5.401
475F ARG 2.929
 
  69 1nzw_1 D 487   467C GLY 3.789
468C TYR 3.519
469C LYS 5.659
472C GLY 5.648
473C SER 5.586
474C GLY 5.270
475C ARG 3.005
 
  70 1nzw_1 C 487   467D GLY 3.518
468D TYR 3.441
469D LYS 5.604
472D GLY 5.386
473D SER 5.541
474D GLY 5.467
475D ARG 3.072
 
  71 1nzw_1 B 487   467A GLY 3.539
468A TYR 3.666
469A LYS 5.761
472A GLY 5.371
473A SER 5.336
474A GLY 5.161
475A ARG 2.837
 
  72 1nzw_1 A 487   467B GLY 4.020
468B TYR 3.408
469B LYS 5.773
472B GLY 5.857
473B SER 5.710
474B GLY 5.267
475B ARG 2.725
 
  73 1ag8 D 487   467C GLY 4.037
468C TYR 3.626
473C SER 5.856
474C GLY 5.346
475C ARG 3.706
 
  74 1ag8 C 487   467D GLY 3.540
468D TYR 3.474
469D LYS 5.868
473D SER 5.989
474D GLY 5.653
475D ARG 3.077
 
  75 1ag8 B 487   467A GLY 3.940
468A TYR 3.315
474A GLY 5.564
475A ARG 3.285
 
  76 1ag8 A 487   467B GLY 3.531
468B TYR 3.353
469B LYS 5.865
474B GLY 5.783
475B ARG 2.747
 
  77 1a4z D 487   467C GLY 3.224
468C TYR 3.448
469C LYS 5.896
473C SER 5.634
474C GLY 5.375
475C ARG 3.259
 
  78 1a4z C 487   467D GLY 3.196
468D TYR 3.500
469D LYS 5.899
473D SER 5.630
474D GLY 5.375
0.000
 
  79 1a4z B 487   467A GLY 3.316
468A TYR 3.388
469A LYS 5.768
472A GLY 5.790
473A SER 5.360
474A GLY 5.237
475A ARG 3.003
 
  80 1a4z A 487   467B GLY 3.321
468B TYR 3.251
473B SER 5.622
474B GLY 5.358
475B ARG 2.918
 
  81 1bxs D 487   467C GLY 3.902
468C PHE 3.702
469C LYS 5.794
472C GLY 5.586
474C GLY 5.339
475C ARG 3.144
 
  82 1bxs C 487   467D GLY 3.939
468D PHE 3.718
469D LYS 5.796
472D GLY 5.620
474D GLY 5.391
475D ARG 3.186
 
  83 1bxs B 487   467A GLY 3.951
468A PHE 3.795
469A LYS 5.835
472A GLY 5.577
474A GLY 5.296
475A ARG 3.192
 
  84 1bxs A 487   467B GLY 3.923
468B PHE 3.768
469B LYS 5.837
472B GLY 5.563
474B GLY 5.266
475B ARG 3.140
 
  85 1bi9 D 487   448C ALA 5.944
 
  87 1o9j D 487   467C GLY 3.418
468C PHE 3.727
469C LYS 5.624
472C GLY 5.198
473C HIS 5.175
474C GLY 5.370
475C ARG 2.843
 
  88 1o9j C 487   467D GLY 3.387
468D PHE 3.720
469D LYS 5.321
472D GLY 4.841
473D HIS 5.045
474D GLY 5.248
475D ARG 3.166
 
  89 1o9j B 487   467A GLY 3.392
468A PHE 3.608
469A LYS 5.429
472A GLY 5.270
473A HIS 5.315
474A GLY 5.441
475A ARG 2.980
 
  90 1o9j A 487   467B GLY 3.423
468B PHE 3.761
469B LYS 5.431
472B GLY 5.279
473B HIS 5.390
474B GLY 5.576
475B ARG 2.735
480B TYR 5.949