Result|PIZSA

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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 Interfaces	6
Number of Chains	4

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_pdb	1gzx.pdb
Interface	1gzx_B-1gzx_C
Number of Interacting Residue Pairs	87
Distance Threshold (A)	4.00
Potential Type	ss
Raw Score	-138.086
Average Background Score	-126.474
Standard Deviation	8.780
Z-score	-1.322
Z-score threshold	-0.691
Binding Prediction	Stable association (BINDER)
Parameters	Values

The Interface scores for the selected interface are given below.

Parameter Scores	Download Scores File
Parameters	Values
Input_pdb	1gzx.pdb
Interface	1gzx_C-1gzx_D
Number of Interacting Residue Pairs	146
Distance Threshold (A)	4.00
Potential Type	ss
Raw Score	-216.160
Average Background Score	-213.673
Standard Deviation	10.859
Z-score	-0.228
Z-score threshold	-0.691
Binding Prediction	Unstable association (NON-BINDER)
Parameters	Values

The Interface scores for the selected interface are given below.

Parameter Scores	Download Scores File
Parameters	Values
Input_pdb	1gzx.pdb
Interface	1gzx_B-1gzx_D
Number of Interacting Residue Pairs	3
Distance Threshold (A)	4.00
Potential Type	ss
Raw Score	-8.522
Average Background Score	-4.695
Standard Deviation	1.227
Z-score	-3.120
Z-score threshold	-0.691
Binding Prediction	Stable association (BINDER)
Parameters	Values

The Interface scores for the selected interface are given below.

Parameter Scores	Download Scores File
Parameters	Values
Input_pdb	1gzx.pdb
Interface	1gzx_A-1gzx_C
Number of Interacting Residue Pairs	23
Distance Threshold (A)	4.00
Potential Type	ss
Raw Score	-42.283
Average Background Score	-39.862
Standard Deviation	2.486
Z-score	-0.973
Z-score threshold	-0.691
Binding Prediction	Stable association (BINDER)
Parameters	Values

The Interface scores for the selected interface are given below.

Parameter Scores	Download Scores File
Parameters	Values
Input_pdb	1gzx.pdb
Interface	1gzx_A-1gzx_B
Number of Interacting Residue Pairs	144
Distance Threshold (A)	4.00
Potential Type	ss
Raw Score	-220.000
Average Background Score	-216.217
Standard Deviation	10.850
Z-score	-0.348
Z-score threshold	-0.691
Binding Prediction	Unstable association (NON-BINDER)
Parameters	Values

The Interface scores for the selected interface are given below.

Parameter Scores	Download Scores File
Parameters	Values
Input_pdb	1gzx.pdb
Interface	1gzx_A-1gzx_D
Number of Interacting Residue Pairs	90
Distance Threshold (A)	4.00
Potential Type	ss
Raw Score	-143.225
Average Background Score	-133.295
Standard Deviation	8.515
Z-score	-1.166
Z-score threshold	-0.691
Binding Prediction	Stable 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

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

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

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

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

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	ALA	75.513
41	A	THR	ALA	42.100
6	A	ASP	ALA	35.608
541	C	ARG	ALA	25.333
670	D	GLN	ALA	20.251
141	A	ARG	ALA	20.196
242	B	ASP	ALA	19.715
270	B	GLN	ALA	19.185
522	C	HIS	ALA	18.890
494	C	ASP	ALA	18.515
642	D	ASP	ALA	17.822
183	B	ARG	ALA	17.206
431	C	ARG	ALA	17.005
94	A	ASP	ALA	16.808
122	A	HIS	ALA	16.423
503	C	HIS	ALA	16.278
492	C	ARG	ALA	16.075
580	D	TRP	ALA	16.017
103	A	HIS	ALA	15.771
441	C	THR	ALA	15.626
583	D	ARG	ALA	15.406
31	A	ARG	ALA	15.248
259	B	HIS	ALA	14.991
180	B	TRP	ALA	14.988
107	A	VAL	ALA	14.477
263	B	LYS	ALA	14.181
92	A	ARG	ALA	14.137
658	D	ALA	ALA	14.034
258	B	ALA	ALA	13.648
178	B	TYR	ALA	13.353
435	C	SER	ALA	13.208
578	D	TYR	ALA	12.982
35	A	SER	ALA	12.961
42	A	TYR	ALA	12.754
38	A	THR	ALA	12.722
442	C	TYR	ALA	12.715
519	C	PRO	ALA	12.611
659	D	HIS	ALA	12.608
119	A	PRO	ALA	12.402
23	A	GLU	ALA	11.862
644	D	GLU	ALA	11.740
507	C	VAL	ALA	11.739
110	A	ALA	ALA	11.203
274	B	GLN	ALA	11.032
27	A	GLU	ALA	11.006
173	B	ARG	ALA	10.865
655	D	CYS	ALA	10.856
674	D	GLN	ALA	10.850
517	C	PHE	ALA	10.721
34	A	LEU	ALA	10.677
510	C	ALA	ALA	10.564
255	B	CYS	ALA	10.440
573	D	ARG	ALA	10.258
267	B	PRO	ALA	9.786
665	D	PHE	ALA	9.738
577	D	VAL	ALA	9.619
244	B	GLU	ALA	9.441
265	B	PHE	ALA	9.402
438	C	THR	ALA	9.316
667	D	PRO	ALA	9.151
523	C	ALA	ALA	9.150
654	D	VAL	ALA	8.792
111	A	ALA	ALA	8.385
40	A	LYS	ALA	8.307
177	B	VAL	ALA	7.979
436	C	PHE	ALA	7.966
117	A	PHE	ALA	7.895
511	C	ALA	ALA	7.691
526	C	ASP	ALA	7.358
651	D	ASN	ALA	7.261
251	B	ASN	ALA	7.132
176	B	VAL	ALA	6.872
645	D	ASN	ALA	6.818
96	A	VAL	ALA	6.700
497	C	ASN	ALA	6.579
126	A	ASP	ALA	6.499
518	C	THR	ALA	6.202
95	A	PRO	ALA	6.030
254	B	VAL	ALA	6.021
271	B	ALA	ALA	5.999
434	C	LEU	ALA	5.971
594	D	PRO	ALA	5.920
545	D	HIS	ALA	5.726
97	A	ASN	ALA	5.690
640	D	HIS	ALA	5.681
268	B	PRO	ALA	5.677
30	A	GLU	ALA	5.362
194	B	PRO	ALA	5.306
118	A	THR	ALA	5.301
123	A	ALA	ALA	5.267
540	C	TYR	ALA	5.261
495	C	PRO	ALA	5.241
688	D	TYR	ALA	5.094
288	B	TYR	ALA	4.985
20	A	HIS	ALA	4.910
245	B	ASN	ALA	4.870
506	C	LEU	ALA	4.852
36	A	PHE	ALA	4.789
576	D	VAL	ALA	4.630
140	A	TYR	ALA	4.548
671	D	ALA	ALA	4.527
668	D	PRO	ALA	4.492
256	B	VAL	ALA	4.278
247	B	ARG	ALA	4.258
248	B	LEU	ALA	4.139
643	D	PRO	ALA	4.086
184	B	PHE	ALA	4.000
243	B	PRO	ALA	3.936
496	C	VAL	ALA	3.927
106	A	LEU	ALA	3.864
579	D	PRO	ALA	3.734
427	C	GLU	ALA	3.699
520	C	ALA	ALA	3.698
179	B	PRO	ALA	3.573
595	D	ASP	ALA	3.471
430	C	GLU	ALA	3.441
437	C	PRO	ALA	3.401
266	B	THR	ALA	3.323
647	D	ARG	ALA	3.300
186	B	GLU	ALA	3.223
569	D	GLU	ALA	3.194
120	A	ALA	ALA	2.993
499	C	LYS	ALA	2.952
493	C	VAL	ALA	2.872
240	B	HIS	ALA	2.701
656	D	VAL	ALA	2.659
252	B	VAL	ALA	2.626
286	B	HIS	ALA	2.610
584	D	PHE	ALA	2.505
648	D	LEU	ALA	2.497
93	A	VAL	ALA	2.411
289	B	HIS	ALA	2.340
37	A	PRO	ALA	2.152
636	D	CYS	ALA	2.129
504	C	CYS	ALA	2.114
527	C	LYS	ALA	1.983
444	C	PRO	ALA	1.939
44	A	PRO	ALA	1.893
689	D	HIS	ALA	1.847
108	A	THR	ALA	1.824
586	D	GLU	ALA	1.807
666	D	THR	ALA	1.780
127	A	LYS	ALA	1.685
534	C	THR	ALA	1.588
401	C	VAL	ALA	1.533
134	A	THR	ALA	1.509
598	D	MET	ALA	1.422
198	B	MET	ALA	1.422
50	A	HIS	ALA	1.388
236	B	CYS	ALA	1.335
195	B	ASP	ALA	1.305
663	D	LYS	ALA	1.264
450	C	HIS	ALA	1.228
440	C	LYS	ALA	1.219
100	A	LEU	ALA	1.088
39	A	THR	ALA	1.041
45	A	HIS	ALA	0.982
112	A	HIS	ALA	0.968
500	C	LEU	ALA	0.934
145	B	HIS	ALA	0.921
508	C	THR	ALA	0.843
490	C	LYS	ALA	0.820
686	D	HIS	ALA	0.806
582	D	GLN	ALA	0.626
182	B	GLN	ALA	0.626
24	A	TYR	ALA	0.618
512	C	HIS	ALA	0.523
275	B	LYS	ALA	0.507
89	A	HIS	ALA	0.495
406	C	ASP	ALA	0.441
181	B	THR	ALA	0.432
675	D	LYS	ALA	0.399
90	A	LYS	ALA	0.296
116	A	GLU	ALA	0.247
652	D	VAL	ALA	0.215
169	B	GLU	ALA	0.191
677	D	VAL	ALA	0.185
673	D	TYR	ALA	0.175
516	C	GLU	ALA	0.163
273	B	TYR	ALA	0.144
104	A	CYS	ALA	0.137
646	D	PHE	ALA	0.114
641	D	VAL	ALA	0.111
114	A	PRO	ALA	0.098
591	D	LEU	ALA	0.097
191	B	LEU	ALA	0.097
439	C	THR	ALA	0.097
514	C	PRO	ALA	0.096
246	B	PHE	ALA	0.088
99	A	LYS	ALA	0.087
445	C	HIS	ALA	0.084
432	C	MET	ALA	0.083
115	A	ALA	ALA	0.082
88	A	ALA	ALA	0.082
130	A	ALA	ALA	0.082
515	C	ALA	ALA	0.080
488	C	ALA	ALA	0.080
530	C	ALA	ALA	0.079
278	B	ALA	ALA	0.076
685	D	ALA	ALA	0.075
285	B	ALA	ALA	0.075
678	D	ALA	ALA	0.075
257	B	LEU	ALA	0.072
409	C	ASN	ALA	0.070
113	A	LEU	ALA	0.053
235	B	HIS	ALA	0.052
513	C	LEU	ALA	0.050
597	D	VAL	ALA	0.031
637	D	ASP	ALA	0.029
91	A	LEU	ALA	0.011
491	C	LEU	ALA	0.009
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