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<------------------   Z-Score cutoff = -0.691  -------------------->
Stable Association (BINIDER,   Z-score <= -0.691) Unstable Association (NON-BINIDER   Z-score > -0.691)

PDB structure pdb1gzx.ent
Number of Interacting Interfaces6
Number of Chains4
Interface(s) Details
Index Interface(s) Raw Score Z Score Binding Prediction
1 1gzx_B-1gzx_C -138.086 -1.322 Stable association (BINDER)
2 1gzx_C-1gzx_D -216.160 -0.228 Unstable association (NON-BINDER)
3 1gzx_B-1gzx_D -8.522 -3.120 Stable association (BINDER)
4 1gzx_A-1gzx_C -42.283 -0.973 Stable association (BINDER)
5 1gzx_A-1gzx_B -220.000 -0.348 Unstable association (NON-BINDER)
6 1gzx_A-1gzx_D -143.225 -1.166 Stable association (BINDER)
Chain Color Legend
Index Chain
1 A
2 B
3 C
4 D

The Interface scores for the selected interface are given below.

Parameter Scores Download Scores File
Parameters Values
Input_pdb1gzx.pdb
Interface1gzx_B-1gzx_C
Number of Interacting Residue Pairs87
Distance Threshold (A)4.00
Potential Typess
Raw Score-138.086
Average Background Score-126.474
Standard Deviation8.780
Z-score-1.322
Z-score threshold-0.691
Binding PredictionStable association (BINDER)
Parameters Values

The Interface scores for the selected interface are given below.

Parameter Scores Download Scores File
Parameters Values
Input_pdb1gzx.pdb
Interface1gzx_C-1gzx_D
Number of Interacting Residue Pairs146
Distance Threshold (A)4.00
Potential Typess
Raw Score-216.160
Average Background Score-213.673
Standard Deviation10.859
Z-score-0.228
Z-score threshold-0.691
Binding PredictionUnstable association (NON-BINDER)
Parameters Values

The Interface scores for the selected interface are given below.

Parameter Scores Download Scores File
Parameters Values
Input_pdb1gzx.pdb
Interface1gzx_B-1gzx_D
Number of Interacting Residue Pairs3
Distance Threshold (A)4.00
Potential Typess
Raw Score-8.522
Average Background Score-4.695
Standard Deviation1.227
Z-score-3.120
Z-score threshold-0.691
Binding PredictionStable association (BINDER)
Parameters Values

The Interface scores for the selected interface are given below.

Parameter Scores Download Scores File
Parameters Values
Input_pdb1gzx.pdb
Interface1gzx_A-1gzx_C
Number of Interacting Residue Pairs23
Distance Threshold (A)4.00
Potential Typess
Raw Score-42.283
Average Background Score-39.862
Standard Deviation2.486
Z-score-0.973
Z-score threshold-0.691
Binding PredictionStable association (BINDER)
Parameters Values

The Interface scores for the selected interface are given below.

Parameter Scores Download Scores File
Parameters Values
Input_pdb1gzx.pdb
Interface1gzx_A-1gzx_B
Number of Interacting Residue Pairs144
Distance Threshold (A)4.00
Potential Typess
Raw Score-220.000
Average Background Score-216.217
Standard Deviation10.850
Z-score-0.348
Z-score threshold-0.691
Binding PredictionUnstable association (NON-BINDER)
Parameters Values

The Interface scores for the selected interface are given below.

Parameter Scores Download Scores File
Parameters Values
Input_pdb1gzx.pdb
Interface1gzx_A-1gzx_D
Number of Interacting Residue Pairs90
Distance Threshold (A)4.00
Potential Typess
Raw Score-143.225
Average Background Score-133.295
Standard Deviation8.515
Z-score-1.166
Z-score threshold-0.691
Binding PredictionStable association (BINDER)
Parameters Values

The interacting residues for the selected interface are given below. Hover the cursor over the row to highlight the interacting residue pair in the visualisaion panel. You can also search the table entries by residue name, for example to see all entries containing 'VAL', type VAL in the search box. Currently, the table is sorted by the 'Raw Score' column, to sort by other column, click on the specific column label, for example 'Residue number', 'Residue Name' etc.

Interacting Residues on the Interface Download Interacting Residues File
Interface Residue One Interface Residue Two
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp
184 PHE B 442 TYR C -2.222
180 TRP B 488 ALA C -0.696
242 ASP B 493 VAL C -1.325
236 CYS B 437 PRO C -0.570
180 TRP B 537 THR C -0.530
244 GLU B 442 TYR C -1.171
289 HIS B 437 PRO C -1.733
247 ARG B 496 VAL C -1.816
180 TRP B 442 TYR C -1.239
186 GLU B 492 ARG C -2.812
184 PHE B 441 THR C -1.178
241 VAL B 441 THR C -2.004
245 ASN B 441 THR C -0.694
242 ASP B 438 THR C -2.500
182 GLN B 492 ARG C -3.519
246 PHE B 438 THR C -0.392
183 ARG B 491 LEU C -2.105
183 ARG B 445 HIS C -0.439
243 PRO B 441 THR C -1.557
240 HIS B 440 LYS C -0.507
180 TRP B 494 ASP C -2.420
179 PRO B 492 ARG C -1.269
236 CYS B 438 THR C -0.707
244 GLU B 438 THR C -1.095
180 TRP B 540 TYR C -3.306
244 GLU B 497 ASN C -2.552
177 VAL B 541 ARG C -2.575
245 ASN B 494 ASP C -2.841
235 HIS B 441 THR C -0.420
183 ARG B 490 LYS C -0.409
242 ASP B 497 ASN C -2.788
248 LEU B 495 PRO C -0.944
288 TYR B 440 LYS C -0.381
244 GLU B 494 ASP C -2.402
179 PRO B 541 ARG C -1.904
243 PRO B 442 TYR C -0.701
242 ASP B 494 ASP C -3.579
236 CYS B 440 LYS C -0.343
179 PRO B 540 TYR C -1.314
244 GLU B 495 PRO C -1.673
240 HIS B 444 PRO C -1.733
184 PHE B 492 ARG C -0.439
184 PHE B 494 ASP C -0.510
242 ASP B 442 TYR C -3.122
247 ARG B 500 LEU C -0.421
180 TRP B 492 ARG C -2.622
242 ASP B 441 THR C -2.500
240 HIS B 442 TYR C -0.529
181 THR B 492 ARG C -0.433
243 PRO B 438 THR C -1.557
248 LEU B 496 VAL C -0.811
186 GLU B 490 LYS C -0.766
183 ARG B 441 THR C -1.748
240 HIS B 441 THR C -2.515
183 ARG B 494 ASP C -0.971
183 ARG B 492 ARG C -4.855
248 LEU B 494 ASP C -2.354
245 ASN B 442 TYR C -2.016
181 THR B 494 ASP C -1.593
242 ASP B 495 PRO C -0.542
183 ARG B 442 TYR C -3.338
242 ASP B 496 VAL C -1.767
247 ARG B 438 THR C -1.748
244 GLU B 496 VAL C -2.212
288 TYR B 437 PRO C -1.339
288 TYR B 441 THR C -2.924
180 TRP B 495 PRO C -1.974
191 LEU B 492 ARG C -0.446
242 ASP B 500 LEU C -0.551
289 HIS B 440 LYS C -1.823
183 ARG B 444 PRO C -1.432
243 PRO B 497 ASN C -0.595
183 ARG B 493 VAL C -1.816
245 ASN B 497 ASN C -1.245
178 TYR B 541 ARG C -3.549
288 TYR B 438 THR C -2.924
180 TRP B 541 ARG C -3.278
178 TYR B 494 ASP C -1.645
180 TRP B 493 VAL C -1.043
183 ARG B 540 TYR C -0.417
178 TYR B 495 PRO C -0.893
236 CYS B 441 THR C -1.413
247 ARG B 494 ASP C -0.555
178 TYR B 540 TYR C -0.577
248 LEU B 541 ARG C -0.446
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp

The interacting residues for the selected interface are given below. Hover the cursor over the row to highlight the interacting residue pair in the visualisaion panel. You can also search the table entries by residue name, for example to see all entries containing 'VAL', type VAL in the search box. Currently, the table is sorted by the 'Raw Score' column, to sort by other column, click on the specific column label, for example 'Residue number', 'Residue Name' etc.

Interacting Residues on the Interface Download Interacting Residues File
Interface Residue One Interface Residue Two
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp
519 PRO C 597 VAL D -0.477
508 THR C 667 PRO D -0.811
503 HIS C 652 VAL D -0.801
519 PRO C 659 HIS D -1.149
517 PHE C 656 VAL D -1.123
522 HIS C 655 CYS D -2.991
511 ALA C 670 GLN D -0.600
500 LEU C 674 GLN D -0.559
526 ASP C 655 CYS D -1.113
522 HIS C 651 ASN D -0.471
430 GLU C 668 PRO D -1.673
518 THR C 569 GLU D -0.560
507 VAL C 658 ALA D -2.398
522 HIS C 573 ARG D -3.338
431 ARG C 654 VAL D -0.848
450 HIS C 668 PRO D -1.155
518 THR C 595 ASP D -0.797
527 LYS C 579 PRO D -0.757
435 SER C 670 GLN D -3.191
523 ALA C 579 PRO D -1.160
519 PRO C 569 GLU D -1.682
511 ALA C 658 ALA D -3.809
510 ALA C 573 ARG D -1.698
512 HIS C 663 LYS D -1.520
518 THR C 594 PRO D -0.972
435 SER C 673 TYR D -0.416
436 PHE C 651 ASN D -1.876
511 ALA C 659 HIS D -1.423
520 ALA C 595 ASP D -1.878
499 LYS C 651 ASN D -0.709
435 SER C 654 VAL D -1.404
518 THR C 576 VAL D -0.761
506 LEU C 655 CYS D -1.507
522 HIS C 578 TYR D -1.983
503 HIS C 651 ASN D -2.826
427 GLU C 667 PRO D -1.673
526 ASP C 578 TYR D -3.122
517 PHE C 658 ALA D -1.767
434 LEU C 666 THR D -0.600
522 HIS C 577 VAL D -2.399
507 VAL C 667 PRO D -0.416
431 ARG C 668 PRO D -1.336
431 ARG C 670 GLN D -3.295
409 ASN C 594 PRO D -0.570
435 SER C 665 PHE D -0.708
523 ALA C 576 VAL D -2.285
431 ARG C 665 PHE D -2.903
436 PHE C 674 GLN D -2.652
511 ALA C 661 PHE D -0.462
519 PRO C 573 ARG D -1.904
527 LYS C 577 VAL D -1.036
520 ALA C 594 PRO D -1.740
507 VAL C 670 GLN D -2.397
431 ARG C 667 PRO D -2.004
507 VAL C 654 VAL D -3.549
503 HIS C 670 GLN D -3.017
519 PRO C 577 VAL D -1.432
526 ASP C 648 LEU D -0.551
510 ALA C 655 CYS D -1.669
515 ALA C 659 HIS D -1.423
519 PRO C 576 VAL D -1.432
506 LEU C 578 TYR D -1.517
435 SER C 671 ALA D -2.537
519 PRO C 656 VAL D -0.477
430 GLU C 666 THR D -0.547
431 ARG C 671 ALA D -0.870
427 GLU C 665 PHE D -0.458
427 GLU C 666 THR D -0.547
518 THR C 659 HIS D -1.279
519 PRO C 598 MET D -1.379
507 VAL C 651 ASN D -0.744
435 SER C 668 PRO D -0.513
507 VAL C 674 GLN D -1.917
435 SER C 667 PRO D -1.026
431 ARG C 666 THR D -2.622
431 ARG C 658 ALA D -2.176
517 PHE C 577 VAL D -0.874
510 ALA C 658 ALA D -3.809
517 PHE C 569 GLU D -0.702
522 HIS C 659 HIS D -2.690
450 HIS C 667 PRO D -1.733
522 HIS C 576 VAL D -1.600
431 ARG C 669 VAL D -1.089
427 GLU C 670 GLN D -1.152
522 HIS C 569 GLU D -1.240
506 LEU C 577 VAL D -1.821
522 HIS C 656 VAL D -2.000
431 ARG C 674 GLN D -0.942
436 PHE C 654 VAL D -0.749
507 VAL C 665 PHE D -2.653
503 HIS C 655 CYS D -2.991
500 LEU C 651 ASN D -0.629
514 PRO C 659 HIS D -1.724
510 ALA C 656 VAL D -1.524
527 LYS C 578 TYR D -0.368
523 ALA C 577 VAL D -2.285
507 VAL C 655 CYS D -1.394
436 PHE C 678 ALA D -0.441
434 LEU C 670 GLN D -1.400
511 ALA C 665 PHE D -2.310
523 ALA C 578 TYR D -1.601
503 HIS C 674 GLN D -3.017
516 GLU C 659 HIS D -0.558
503 HIS C 654 VAL D -2.399
499 LYS C 648 LEU D -0.462
523 ALA C 573 ARG D -0.424
527 LYS C 580 TRP D -0.258
436 PHE C 670 GLN D -2.121
504 CYS C 670 GLN D -1.292
517 PHE C 573 ARG D -3.072
432 MET C 670 GLN D -1.504
435 SER C 674 GLN D -3.191
522 HIS C 652 VAL D -2.000
513 LEU C 659 HIS D -0.682
511 ALA C 663 LYS D -0.430
526 ASP C 577 VAL D -1.767
517 PHE C 659 HIS D -2.567
437 PRO C 671 ALA D -1.044
503 HIS C 578 TYR D -0.396
434 LEU C 671 ALA D -2.797
435 SER C 675 LYS D -0.573
503 HIS C 665 PHE D -0.713
526 ASP C 580 TRP D -0.730
518 THR C 573 ARG D -1.732
523 ALA C 594 PRO D -1.740
510 ALA C 665 PHE D -0.462
519 PRO C 594 PRO D -2.389
510 ALA C 659 HIS D -2.846
437 PRO C 675 LYS D -0.794
521 VAL C 573 ARG D -1.104
518 THR C 598 MET D -0.611
506 LEU C 651 ASN D -0.629
504 CYS C 654 VAL D -0.472
436 PHE C 677 VAL D -0.374
430 GLU C 667 PRO D -1.673
504 CYS C 674 GLN D -1.033
499 LYS C 578 TYR D -0.368
434 LEU C 668 PRO D -1.417
519 PRO C 595 ASP D -1.581
503 HIS C 677 VAL D -0.801
520 ALA C 576 VAL D -2.285
499 LYS C 644 GLU D -0.771
434 LEU C 667 PRO D -1.417
427 GLU C 658 ALA D -0.551
508 THR C 670 GLN D -1.753
517 PHE C 655 CYS D -2.205
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp

The interacting residues for the selected interface are given below. Hover the cursor over the row to highlight the interacting residue pair in the visualisaion panel. You can also search the table entries by residue name, for example to see all entries containing 'VAL', type VAL in the search box. Currently, the table is sorted by the 'Raw Score' column, to sort by other column, click on the specific column label, for example 'Residue number', 'Residue Name' etc.

Interacting Residues on the Interface Download Interacting Residues File
Interface Residue One Interface Residue Two
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp
286 HIS B 545 HIS D -5.380
145 HIS B 686 HIS D -1.796
225 LYS B 545 HIS D -1.345
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp

The interacting residues for the selected interface are given below. Hover the cursor over the row to highlight the interacting residue pair in the visualisaion panel. You can also search the table entries by residue name, for example to see all entries containing 'VAL', type VAL in the search box. Currently, the table is sorted by the 'Raw Score' column, to sort by other column, click on the specific column label, for example 'Residue number', 'Residue Name' etc.

Interacting Residues on the Interface Download Interacting Residues File
Interface Residue One Interface Residue Two
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp
126 ASP A 541 ARG C -3.947
130 ALA A 541 ARG C -2.547
141 ARG A 527 LYS C -2.867
139 LYS A 401 VAL C -1.036
141 ARG A 526 ASP C -3.886
1 VAL A 539 LYS C -1.058
94 ASP A 499 LYS C -0.692
141 ARG A 522 HIS C -0.439
141 ARG A 406 ASP C -1.667
106 LEU A 541 ARG C -0.446
127 LYS A 541 ARG C -2.860
95 PRO A 499 LYS C -0.757
141 ARG A 401 VAL C -0.848
141 ARG A 530 ALA C -2.611
6 ASP A 541 ARG C -1.111
138 SER A 401 VAL C -2.106
1 VAL A 538 SER C -1.366
123 ALA A 541 ARG C -2.969
141 ARG A 506 LEU C -0.421
141 ARG A 523 ALA C -3.044
96 VAL A 499 LYS C -1.036
134 THR A 534 THR C -4.086
122 HIS A 541 ARG C -0.477
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp

The interacting residues for the selected interface are given below. Hover the cursor over the row to highlight the interacting residue pair in the visualisaion panel. You can also search the table entries by residue name, for example to see all entries containing 'VAL', type VAL in the search box. Currently, the table is sorted by the 'Raw Score' column, to sort by other column, click on the specific column label, for example 'Residue number', 'Residue Name' etc.

Interacting Residues on the Interface Download Interacting Residues File
Interface Residue One Interface Residue Two
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp
107 VAL A 258 ALA B -2.398
123 ALA A 177 VAL B -2.285
119 PRO A 195 ASP B -0.659
107 VAL A 251 ASN B -0.744
31 ARG A 270 GLN B -3.519
34 LEU A 271 ALA B -2.808
119 PRO A 198 MET B -1.379
103 HIS A 251 ASN B -2.826
118 THR A 173 ARG B -1.732
117 PHE A 252 VAL B -0.374
31 ARG A 268 PRO B -1.269
111 ALA A 258 ALA B -3.809
111 ALA A 261 PHE B -0.462
122 HIS A 251 ASN B -0.471
112 HIS A 263 LYS B -3.040
36 PHE A 278 ALA B -0.462
126 ASP A 178 TYR B -3.122
23 GLU A 263 LYS B -3.064
116 GLU A 259 HIS B -1.116
99 LYS A 251 ASN B -0.550
103 HIS A 277 VAL B -0.801
127 LYS A 179 PRO B -0.757
30 GLU A 268 PRO B -1.682
31 ARG A 266 THR B -2.165
106 LEU A 255 CYS B -1.507
126 ASP A 255 CYS B -1.113
103 HIS A 252 VAL B -0.801
32 MET A 270 GLN B -1.370
110 ALA A 259 HIS B -2.846
36 PHE A 254 VAL B -0.379
117 PHE A 255 CYS B -1.891
106 LEU A 178 TYR B -1.517
50 HIS A 267 PRO B -1.724
118 THR A 195 ASP B -0.597
117 PHE A 256 VAL B -1.123
119 PRO A 194 PRO B -2.389
104 CYS A 254 VAL B -0.472
104 CYS A 274 GLN B -1.292
117 PHE A 258 ALA B -0.883
27 GLU A 266 THR B -0.560
35 SER A 254 VAL B -0.684
121 VAL A 173 ARG B -1.104
110 ALA A 173 ARG B -1.273
100 LEU A 274 GLN B -0.700
30 GLU A 266 THR B -0.936
122 HIS A 178 TYR B -2.379
31 ARG A 265 PHE B -2.635
36 PHE A 251 ASN B -1.976
111 ALA A 265 PHE B -2.310
113 LEU A 259 HIS B -0.682
31 ARG A 254 VAL B -0.860
119 PRO A 197 VAL B -0.955
107 VAL A 267 PRO B -0.416
119 PRO A 177 VAL B -1.432
110 ALA A 258 ALA B -3.809
35 SER A 270 GLN B -3.082
122 HIS A 177 VAL B -2.399
115 ALA A 259 HIS B -1.423
110 ALA A 255 CYS B -1.669
126 ASP A 180 TRP B -0.730
118 THR A 176 VAL B -0.761
35 SER A 274 GLN B -3.082
103 HIS A 270 GLN B -3.017
117 PHE A 177 VAL B -0.749
127 LYS A 177 VAL B -1.036
50 HIS A 268 PRO B -1.149
114 PRO A 259 HIS B -1.724
120 ALA A 176 VAL B -2.285
34 LEU A 268 PRO B -1.512
31 ARG A 274 GLN B -1.407
118 THR A 259 HIS B -1.706
34 LEU A 267 PRO B -1.512
36 PHE A 270 GLN B -2.186
24 TYR A 263 LYS B -1.828
34 LEU A 266 THR B -0.509
107 VAL A 270 GLN B -2.397
108 THR A 267 PRO B -0.811
117 PHE A 173 ARG B -3.072
27 GLU A 258 ALA B -0.552
111 ALA A 263 LYS B -1.723
122 HIS A 252 VAL B -2.000
31 ARG A 263 LYS B -0.408
20 HIS A 263 LYS B -0.608
31 ARG A 269 VAL B -1.104
31 ARG A 271 ALA B -0.424
104 CYS A 270 GLN B -1.292
106 LEU A 251 ASN B -0.629
126 ASP A 252 VAL B -0.441
107 VAL A 274 GLN B -1.917
37 PRO A 275 LYS B -0.378
27 GLU A 263 LYS B -3.859
120 ALA A 195 ASP B -0.626
107 VAL A 265 PHE B -2.653
103 HIS A 178 TYR B -0.793
120 ALA A 194 PRO B -1.740
119 PRO A 256 VAL B -0.477
103 HIS A 265 PHE B -0.713
35 SER A 267 PRO B -1.055
119 PRO A 176 VAL B -1.432
31 ARG A 258 ALA B -2.122
100 LEU A 251 ASN B -1.259
103 HIS A 254 VAL B -2.399
122 HIS A 259 HIS B -1.796
126 ASP A 248 LEU B -0.551
36 PHE A 274 GLN B -2.733
122 HIS A 173 ARG B -3.338
126 ASP A 177 VAL B -1.767
30 GLU A 267 PRO B -1.682
35 SER A 265 PHE B -0.747
31 ARG A 267 PRO B -1.904
119 PRO A 169 GLU B -1.682
34 LEU A 150 GLU B -0.417
108 THR A 258 ALA B -1.719
108 THR A 270 GLN B -1.753
103 HIS A 274 GLN B -3.017
35 SER A 271 ALA B -2.691
122 HIS A 256 VAL B -1.600
107 VAL A 254 VAL B -3.549
103 HIS A 255 CYS B -2.991
111 ALA A 259 HIS B -0.950
122 HIS A 176 VAL B -1.600
127 LYS A 180 TRP B -0.258
106 LEU A 177 VAL B -1.821
27 GLU A 265 PHE B -0.351
107 VAL A 257 LEU B -0.596
107 VAL A 255 CYS B -1.394
110 ALA A 256 VAL B -1.524
118 THR A 194 PRO B -0.972
123 ALA A 179 PRO B -1.740
37 PRO A 271 ALA B -0.580
122 HIS A 255 CYS B -2.991
35 SER A 273 TYR B -0.404
118 THR A 198 MET B -0.611
27 GLU A 270 GLN B -0.576
123 ALA A 176 VAL B -2.285
117 PHE A 259 HIS B -2.567
110 ALA A 265 PHE B -0.462
119 PRO A 173 ARG B -1.904
27 GLU A 267 PRO B -1.682
119 PRO A 259 HIS B -1.149
35 SER A 275 LYS B -1.129
123 ALA A 194 PRO B -1.160
34 LEU A 270 GLN B -2.023
35 SER A 268 PRO B -0.527
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp

The interacting residues for the selected interface are given below. Hover the cursor over the row to highlight the interacting residue pair in the visualisaion panel. You can also search the table entries by residue name, for example to see all entries containing 'VAL', type VAL in the search box. Currently, the table is sorted by the 'Raw Score' column, to sort by other column, click on the specific column label, for example 'Residue number', 'Residue Name' etc.

Interacting Residues on the Interface Download Interacting Residues File
Interface Residue One Interface Residue Two
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp
94 ASP A 584 PHE D -0.583
100 LEU A 644 GLU D -0.459
40 LYS A 640 HIS D -0.449
92 ARG A 583 ARG D -4.855
94 ASP A 645 ASN D -2.841
89 HIS A 579 PRO D -0.479
41 THR A 583 ARG D -1.732
42 TYR A 642 ASP D -3.290
95 PRO A 648 LEU D -0.944
96 VAL A 642 ASP D -1.767
41 THR A 584 PHE D -1.631
42 TYR A 644 GLU D -1.208
37 PRO A 636 CYS D -0.543
97 ASN A 643 PRO D -0.595
97 ASN A 645 ASN D -1.245
40 LYS A 688 TYR D -0.736
45 HIS A 583 ARG D -0.477
92 ARG A 579 PRO D -1.269
41 THR A 645 ASN D -0.687
38 THR A 646 PHE D -0.407
40 LYS A 636 CYS D -1.035
39 THR A 642 ASP D -1.593
93 VAL A 580 TRP D -1.043
42 TYR A 641 VAL D -0.334
42 TYR A 645 ASN D -1.979
88 ALA A 580 TRP D -0.696
93 VAL A 642 ASP D -1.325
97 ASN A 644 GLU D -3.190
141 ARG A 648 LEU D -0.421
37 PRO A 688 TYR D -1.314
42 TYR A 580 TRP D -1.106
97 ASN A 580 TRP D -0.264
94 ASP A 647 ARG D -0.555
90 LYS A 586 GLU D -0.766
95 PRO A 644 GLU D -1.673
40 LYS A 689 HIS D -1.614
140 TYR A 580 TRP D -2.950
41 THR A 637 ASP D -0.597
91 LEU A 583 ARG D -2.105
38 THR A 636 CYS D -1.221
95 PRO A 642 ASP D -0.542
94 ASP A 581 THR D -1.593
41 THR A 643 PRO D -1.458
38 THR A 643 PRO D -1.458
45 HIS A 640 HIS D -0.898
97 ASN A 642 ASP D -2.788
140 TYR A 579 PRO D -1.339
95 PRO A 578 TYR D -0.893
140 TYR A 578 TYR D -0.577
92 ARG A 580 TRP D -2.622
95 PRO A 580 TRP D -1.974
141 ARG A 579 PRO D -2.004
141 ARG A 577 VAL D -2.540
41 THR A 640 HIS D -2.559
42 TYR A 583 ARG D -3.549
96 VAL A 643 PRO D -0.477
93 VAL A 583 ARG D -1.816
41 THR A 688 TYR D -2.773
92 ARG A 586 GLU D -3.934
38 THR A 642 ASP D -2.389
38 THR A 688 TYR D -2.773
94 ASP A 644 GLU D -2.402
96 VAL A 647 ARG D -2.540
41 THR A 641 VAL D -2.279
41 THR A 636 CYS D -1.832
96 VAL A 644 GLU D -2.212
100 LEU A 642 ASP D -0.588
92 ARG A 591 LEU D -0.446
95 PRO A 645 ASN D -0.570
96 VAL A 648 LEU D -0.811
42 TYR A 643 PRO D -0.714
38 THR A 647 ARG D -0.866
94 ASP A 648 LEU D -2.354
94 ASP A 578 TYR D -2.056
94 ASP A 583 ARG D -0.555
94 ASP A 580 TRP D -2.420
38 THR A 644 GLU D -2.242
92 ARG A 584 PHE D -0.439
141 ARG A 580 TRP D -2.499
141 ARG A 578 TYR D -3.338
38 THR A 685 ALA D -1.719
89 HIS A 580 TRP D -0.282
44 PRO A 583 ARG D -1.361
41 THR A 642 ASP D -2.389
94 ASP A 642 ASP D -3.579
37 PRO A 689 HIS D -1.724
42 TYR A 640 HIS D -0.553
42 TYR A 584 PHE D -2.250
44 PRO A 640 HIS D -1.724
92 ARG A 582 GLN D -3.519
Residue Number Residue Name Chain Residue Number Residue Name Chain Raw ScoreHelp

The mutational results are sorted as per the score-diff.

Mutational Analysis Output Download Mutational Analysis File
Stability Prediction: "Positive values indicate the mutation is destabilising whereas Negative values indicate the mutation is stabilizing"
Residue Number Residue Chain Residue Name Mutant type Score-Diff
1 A VAL ALA75.513
41 A THR ALA42.100
6 A ASP ALA35.608
541 C ARG ALA25.333
670 D GLN ALA20.251
141 A ARG ALA20.196
242 B ASP ALA19.715
270 B GLN ALA19.185
522 C HIS ALA18.890
494 C ASP ALA18.515
642 D ASP ALA17.822
183 B ARG ALA17.206
431 C ARG ALA17.005
94 A ASP ALA16.808
122 A HIS ALA16.423
503 C HIS ALA16.278
492 C ARG ALA16.075
580 D TRP ALA16.017
103 A HIS ALA15.771
441 C THR ALA15.626
583 D ARG ALA15.406
31 A ARG ALA15.248
259 B HIS ALA14.991
180 B TRP ALA14.988
107 A VAL ALA14.477
263 B LYS ALA14.181
92 A ARG ALA14.137
658 D ALA ALA14.034
258 B ALA ALA13.648
178 B TYR ALA13.353
435 C SER ALA13.208
578 D TYR ALA12.982
35 A SER ALA12.961
42 A TYR ALA12.754
38 A THR ALA12.722
442 C TYR ALA12.715
519 C PRO ALA12.611
659 D HIS ALA12.608
119 A PRO ALA12.402
23 A GLU ALA11.862
644 D GLU ALA11.740
507 C VAL ALA11.739
110 A ALA ALA11.203
274 B GLN ALA11.032
27 A GLU ALA11.006
173 B ARG ALA10.865
655 D CYS ALA10.856
674 D GLN ALA10.850
517 C PHE ALA10.721
34 A LEU ALA10.677
510 C ALA ALA10.564
255 B CYS ALA10.440
573 D ARG ALA10.258
267 B PRO ALA9.786
665 D PHE ALA9.738
577 D VAL ALA9.619
244 B GLU ALA9.441
265 B PHE ALA9.402
438 C THR ALA9.316
667 D PRO ALA9.151
523 C ALA ALA9.150
654 D VAL ALA8.792
111 A ALA ALA8.385
40 A LYS ALA8.307
177 B VAL ALA7.979
436 C PHE ALA7.966
117 A PHE ALA7.895
511 C ALA ALA7.691
526 C ASP ALA7.358
651 D ASN ALA7.261
251 B ASN ALA7.132
176 B VAL ALA6.872
645 D ASN ALA6.818
96 A VAL ALA6.700
497 C ASN ALA6.579
126 A ASP ALA6.499
518 C THR ALA6.202
95 A PRO ALA6.030
254 B VAL ALA6.021
271 B ALA ALA5.999
434 C LEU ALA5.971
594 D PRO ALA5.920
545 D HIS ALA5.726
97 A ASN ALA5.690
640 D HIS ALA5.681
268 B PRO ALA5.677
30 A GLU ALA5.362
194 B PRO ALA5.306
118 A THR ALA5.301
123 A ALA ALA5.267
540 C TYR ALA5.261
495 C PRO ALA5.241
688 D TYR ALA5.094
288 B TYR ALA4.985
20 A HIS ALA4.910
245 B ASN ALA4.870
506 C LEU ALA4.852
36 A PHE ALA4.789
576 D VAL ALA4.630
140 A TYR ALA4.548
671 D ALA ALA4.527
668 D PRO ALA4.492
256 B VAL ALA4.278
247 B ARG ALA4.258
248 B LEU ALA4.139
643 D PRO ALA4.086
184 B PHE ALA4.000
243 B PRO ALA3.936
496 C VAL ALA3.927
106 A LEU ALA3.864
579 D PRO ALA3.734
427 C GLU ALA3.699
520 C ALA ALA3.698
179 B PRO ALA3.573
595 D ASP ALA3.471
430 C GLU ALA3.441
437 C PRO ALA3.401
266 B THR ALA3.323
647 D ARG ALA3.300
186 B GLU ALA3.223
569 D GLU ALA3.194
120 A ALA ALA2.993
499 C LYS ALA2.952
493 C VAL ALA2.872
240 B HIS ALA2.701
656 D VAL ALA2.659
252 B VAL ALA2.626
286 B HIS ALA2.610
584 D PHE ALA2.505
648 D LEU ALA2.497
93 A VAL ALA2.411
289 B HIS ALA2.340
37 A PRO ALA2.152
636 D CYS ALA2.129
504 C CYS ALA2.114
527 C LYS ALA1.983
444 C PRO ALA1.939
44 A PRO ALA1.893
689 D HIS ALA1.847
108 A THR ALA1.824
586 D GLU ALA1.807
666 D THR ALA1.780
127 A LYS ALA1.685
534 C THR ALA1.588
401 C VAL ALA1.533
134 A THR ALA1.509
598 D MET ALA1.422
198 B MET ALA1.422
50 A HIS ALA1.388
236 B CYS ALA1.335
195 B ASP ALA1.305
663 D LYS ALA1.264
450 C HIS ALA1.228
440 C LYS ALA1.219
100 A LEU ALA1.088
39 A THR ALA1.041
45 A HIS ALA0.982
112 A HIS ALA0.968
500 C LEU ALA0.934
145 B HIS ALA0.921
508 C THR ALA0.843
490 C LYS ALA0.820
686 D HIS ALA0.806
582 D GLN ALA0.626
182 B GLN ALA0.626
24 A TYR ALA0.618
512 C HIS ALA0.523
275 B LYS ALA0.507
89 A HIS ALA0.495
406 C ASP ALA0.441
181 B THR ALA0.432
675 D LYS ALA0.399
90 A LYS ALA0.296
116 A GLU ALA0.247
652 D VAL ALA0.215
169 B GLU ALA0.191
677 D VAL ALA0.185
673 D TYR ALA0.175
516 C GLU ALA0.163
273 B TYR ALA0.144
104 A CYS ALA0.137
646 D PHE ALA0.114
641 D VAL ALA0.111
114 A PRO ALA0.098
591 D LEU ALA0.097
191 B LEU ALA0.097
439 C THR ALA0.097
514 C PRO ALA0.096
246 B PHE ALA0.088
99 A LYS ALA0.087
445 C HIS ALA0.084
432 C MET ALA0.083
115 A ALA ALA0.082
88 A ALA ALA0.082
130 A ALA ALA0.082
515 C ALA ALA0.080
488 C ALA ALA0.080
530 C ALA ALA0.079
278 B ALA ALA0.076
685 D ALA ALA0.075
285 B ALA ALA0.075
678 D ALA ALA0.075
257 B LEU ALA0.072
409 C ASN ALA0.070
113 A LEU ALA0.053
235 B HIS ALA0.052
513 C LEU ALA0.050
597 D VAL ALA0.031
637 D ASP ALA0.029
91 A LEU ALA0.011
491 C LEU ALA0.009
581 D THR ALA-0.001
225 B LYS ALA-0.002
661 D PHE ALA-0.007
261 B PHE ALA-0.007
197 B VAL ALA-0.013
32 A MET ALA-0.062
150 B GLU ALA-0.069
537 C THR ALA-0.086
121 A VAL ALA-0.088
521 C VAL ALA-0.090
269 B VAL ALA-0.094
138 A SER ALA-0.097
669 D VAL ALA-0.141
538 C SER ALA-0.153
277 B VAL ALA-0.189
139 A LYS ALA-0.253
539 C LYS ALA-0.301
241 B VAL ALA-0.579
Residue Number Residue Chain Residue Name Mutant type Score-Diff