bioinf.org.uk - Prof. Andrew C.R. Martin's group at UCL

Overall Summary
Hydrogen bonding
Substitutions to proline
Substitutions from glycine
Bad clashes
DNA-binding residues
Zn-binding residues
Cavity-creating mutations
Mutation to residues at protein-interaction sites
Mutations to conserved residues
Summary explanation of mutants

Overall Summary

	Total	Distinct
Total mutations	18584	1827
Complex mutations	78	68
Deletions	1661	282
Insertions	512	200
Silent	1320	212
Tandem	147	75
Point	15216	1216
Tandem/point mutations leading to a substitution	13602	1179
Tandem/point mutations leading to a substitution in the core	13115	944

We can only calculate these in the core TotalDistinct Total substitutions involving HBonds 6390327 Substitutions involving HBond Acceptors 1990164 Explained sc/sc substitutions involving HBond acceptors)137794 Explained sc/mc substitutions involving HBond acceptors37540 Substitutions involving HBond Donors 5246212 Explained sc/sc substitutions involving HBond donors3836104 Explained sc/mc substitutions involving HBond donors105583

Mutations to Proline

	Total	Distinct
Silent mutations of Proline	111	25
Substitutions to Proline	439	70
Substitutions to Proline in the Core	418	58
Disallowed substitutions to Proline in the Core	398	54

Disallowed

Codon	Amino acid	Secondary Structure	Phi	Psi
96	ser	-	-	-157.73
110	arg	E	-144.137	151.752
111	leu	E	-113.239	147.026
116	ser	-	-76.39	-39.217
127	ser	E	-109.949	100.816
130	leu	T	-85.38	-25.01
136	gln	-	-100.488	152.672
137	leu	T	-56.519	131.157
138	ala	T	71.046	-6.909
144	gln	E	-92.668	136.71
145	leu	E	-100.898	118.692
149	ser	S	-146.477	133.016
156	arg	E	-119.194	161.537
158	arg	E	-127.57	139.746
159	ala	E	-119.554	146.868
161	ala	E	-106.536	157.296
165	gln	S	-71.981	138.63
166	ser	T	-40.607	-64.889
168	his	G	-66.524	-13.923
170	thr	G	-88.444	-18.605
175	arg	-	-65.109	147.266
178	his	H	-56.791	-61.784
179	his	H	-57.75	-31.935
181	arg	H	-62.976	-43.551
183	ser	-	-62.278	154.117
192	gln	T	-84.358	-23.48
193	his	-	-70.794	133.586
194	leu	S	-81.987	-44.986
196	arg	E	-122.688	161.578
200	asn	-	-141.907	84.965
201	leu	T	-52.114	2.257
202	arg	T	-115.442	7.853
213	arg	-	-37.348	132.738
214	his	E	-102.983	146.49
228	asp	S	-113.534	-26.425
230	thr	E	-120.353	127.212
241	ser	T	-92.341	12.954
248	arg	T	86.753	7.922
252	leu	E	-118.307	137.257
253	thr	E	-103.296	127.718
256	thr	E	-128.545	123.29
257	leu	E	-83.297	136.58
260	ser	T	-47.916	-18.882
264	leu	E	-63.609	126.162
265	leu	E	-114.011	-21.378
267	arg	E	-158.106	140.954
271	glu	E	-89.422	163.063
273	arg	E	-126.608	110.838
276	ala	S	-90.697	143.622
280	arg	H	-64.084	-35.902
282	arg	H	-80.193	-38.59
283	arg	H	-50.147	-57.613
284	thr	H	-52.739	-57.402
289	leu	-	90.022	-

Allowed

Codon	Amino acid	Secondary Structure	Phi	Psi
140	thr	-	-66.207	125.858
150	thr	-	-56.578	129.841
155	thr	-	-61.553	129.245
189	ala	-	-63.187	129.726

Mutations from Glycine

	Total	Distinct
Silent mutations of Glycine	80	16
Substitutions from Glycine	1063	78
Substitutions from Glycine in the Core	1027	61

Disallowed

Codon	Substitution	Secondary Structure	Phi	Psi
117	arg	-	107.595	165.374
117	glu	-	107.595	165.374
154	ala	T	93.49	-18.147
154	asp	T	93.49	-18.147
154	cys	T	93.49	-18.147
154	ile	T	93.49	-18.147
154	ser	T	93.49	-18.147
154	val	T	93.49	-18.147
187	arg	S	96.541	-9.697
187	asn	S	96.541	-9.697
187	asp	S	96.541	-9.697
187	cys	S	96.541	-9.697
187	ser	S	96.541	-9.697
187	val	S	96.541	-9.697
244	ala	T	97.695	-23.373
244	arg	T	97.695	-23.373
244	asp	T	97.695	-23.373
244	cys	T	97.695	-23.373
244	glu	T	97.695	-23.373
244	ser	T	97.695	-23.373
244	val	T	97.695	-23.373
245	ala	T	-117.227	-115.488
245	arg	T	-117.227	-115.488
245	asn	T	-117.227	-115.488
245	asp	T	-117.227	-115.488
245	cys	T	-117.227	-115.488
245	glu	T	-117.227	-115.488
245	his	T	-117.227	-115.488
245	leu	T	-117.227	-115.488
245	phe	T	-117.227	-115.488
245	ser	T	-117.227	-115.488
245	val	T	-117.227	-115.488
262	asp	-	106.316	8.547
262	cys	-	106.316	8.547
262	his	-	106.316	8.547
262	ser	-	106.316	8.547
262	val	-	106.316	8.547

Allowed

Codon	Substitution	Secondary Structure	Phi	Psi
105	arg	-	-101.432	-162.392
105	cys	-	-101.432	-162.392
105	val	-	-101.432	-162.392
108	asp	-	73.438	59.243
108	ser	-	73.438	59.243
112	asp	E	-122.894	159.618
112	ser	E	-122.894	159.618
199	ala	S	54.791	42.745
199	arg	S	54.791	42.745
199	glu	S	54.791	42.745
199	val	S	54.791	42.745
226	ala	T	79.884	2.235
226	asn	T	79.884	2.235
226	asp	T	79.884	2.235
226	ser	T	79.884	2.235
226	val	T	79.884	2.235
266	ala	E	-167.723	162.972
266	arg	E	-167.723	162.972
266	glu	E	-167.723	162.972
266	val	E	-167.723	162.972
279	arg	H	-68.848	-54.811
279	glu	H	-68.848	-54.811
279	trp	H	-68.848	-54.811
279	val	H	-68.848	-54.811

Structural Clashes

We can only calculate these in the core

	Total	Distinct
Distinct BAD clash mutations	-	24
Distinct OK non-clash mutations	-	920

DNA Binding

	Total	Distinct
Total residues involved in DNA binding	-	14
Number of these actually mutated	-	14
Substitutions of residues involved in DNA binding	3155	73

Residues involved

Codon	Amino Acid
119	ala
120	lys
121	ser
239	asn
241	ser
243	met
247	asn
248	arg
273	arg
275	cys
276	ala
277	cys
280	arg
283	arg

Zinc Binding

	Total	Distinct
Total residues involved in Zinc binding	-	4
Number of these actually mutated	-	4
Total residues involved in Zinc binding	810	26

Residues Cys176, His 179, Cys238 and Cys242 are the 4 residues involved in Zinc binding

Cavity-creating Mutations

	Total	Distinct
Number of cavity-creating mutations	445	26

Mutations Affecting Protein-Interaction Sites

	Total	Distinct
Number of mutations to residues present at protein-interaction sites	3033	438

Mutations most likely to affect protein-protein or domain-domain interactions (from top 10 scoring patches)

Codon	Residue	Mutation
199	gly	glu
166	ser	leu
166	ser	thr
174	arg	trp
190	pro	leu
208	asp	val
177	pro	arg
177	pro	leu
177	pro	ser
202	arg	his
211	thr	ile
158	arg	cys
158	arg	gly
158	arg	his
158	arg	leu
158	arg	pro
168	his	arg
168	his	tyr
154	gly	val
244	gly	asp
244	gly	cys
244	gly	ser
244	gly	val
169	met	ile
232	ile	asn
232	ile	thr
142	pro	leu
243	met	ile
152	pro	leu
152	pro	ser
110	arg	cys
110	arg	leu
271	glu	lys
258	glu	asp
258	glu	gln
258	glu	gly
258	glu	lys
156	arg	his
156	arg	pro
195	ile	phe
195	ile	thr
237	met	ile
132	lys	arg
132	lys	asn
132	lys	gln
132	lys	glu
259	asp	tyr
259	asp	val
153	pro	ser
172	val	asp
172	val	phe
196	arg	pro
235	asn	ser
265	leu	pro
140	thr	ile

Mutations to Conserved Residues

We can only calculate these in the core

	Total	Distinct
Conserved residues	-	63
Mutations to conserved residues	6421	349

Conserved Residues

Codon	Amino Acid	Conservation
98	pro	100
113	phe	100
120	lys	100
121	ser	100
122	val	100
125	thr	100
127	ser	100
130	leu	100
132	lys	100
137	leu	100
139	lys	100
142	pro	100
151	pro	100
152	pro	100
158	arg	100
159	ala	100
164	lys	100
172	val	100
173	val	100
175	arg	100
177	pro	100
178	his	100
179	his	100
196	arg	100
198	glu	100
199	gly	100
205	tyr	100
208	asp	100
215	ser	100
216	val	100
218	val	100
219	pro	100
220	tyr	100
221	glu	100
223	pro	100
230	thr	100
239	asn	100
240	ser	100
241	ser	100
242	cys	100
243	met	100
244	gly	100
245	gly	100
247	asn	100
249	arg	100
251	ile	100
253	thr	100
257	leu	100
262	gly	100
265	leu	100
266	gly	100
267	arg	100
270	phe	100
271	glu	100
272	val	100
275	cys	100
276	ala	100
277	cys	100
278	pro	100
279	gly	100
280	arg	100
281	asp	100
282	arg	100

Summary of explained mutants

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Accessibility
100arg	1	0	1				1	39.50
101arg	1	0	1				1	73.60
101asn	1	0	1				1	73.60
102ile	0	0	5					68.70
104his	1	0	2				1	55.00
104leu	1	0	1				1	55.00
105arg	1	0	1				1	16.00
105cys	1	0	1				1	16.00
105val	1	0	3				1	16.00
106arg	1	0	6				1	87.00
106gly	1	0	1				1	87.00
108asp	1	0	1				1	9.00
108ser	1	0	1				1	9.00
109cys	1	1	1			1		0.40
109leu	0	0	1					0.40
109ser	1	1	3			1		0.40
110cys	1	1	10	1			1	32.90
110gly	1	1	1	1			1	32.90
110leu	1	1	12	1			1	32.90
110pro	1	1	6	1	1		1	32.90

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Pro	Gly	In Patch	Conserved	Accessibility
110ser	1	1	1		1			1		32.90
111arg	1	0	2					1		17.90
111gln	1	0	4					1		17.90
111pro	1	1	2			1		1		17.90
112asp	1	0	1					1		18.60
112ser	1	0	1					1		18.60
113cys	1	0	9					1	1	19.80
113gly	1	0	1					1	1	19.80
113leu	1	0	1					1	1	19.80
113ser	1	0	3					1	1	19.80
113val	1	0	5					1	1	19.80
115tyr	1	0	2					1		98.90
116cys	1	1	2		1			1		40.70
116pro	1	1	1		1	1		1		40.70
117arg	1	1	2				1			40.60
117glu	1	1	3				1			40.60
119thr	1	1	1	1						60.40
120arg	1	1	2	1					1	60.60
120met	1	1	1	1					1	60.60
121phe	1	1	1	1	1				1	39.20
122leu	1	0	1						1	19.60

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Clash	In Patch	Conserved	Accessibility
123asn	0	0	1						39.70
123ile	0	0	1						39.70
124arg	1	0	3				1		8.70
124ser	1	0	1				1		8.70
124trp	1	0	1				1		8.70
125arg	1	1	1	1				1	0.60
125lys	1	1	3	1				1	0.60
125met	1	1	7	1				1	0.60
126asn	1	1	3	1					17.00
126asp	1	1	4	1					17.00
126cys	1	1	7	1					17.00
126gly	1	1	1	1					17.00
126his	1	1	2	1					17.00
126phe	1	1	1	1					17.00
126ser	1	1	1	1					17.00
127cys	1	1	1	1				1	0.00
127phe	1	1	16	1		1		1	0.00
127pro	1	1	5	1	1			1	0.00
127thr	1	0	2					1	0.00
127tyr	1	1	4			1		1	0.00
128ala	0	0	1						72.00

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	In Patch	Conserved	Accessibility
128arg	0	0	1					72.00
128leu	0	0	3					72.00
128ser	0	0	8					72.00
129asp	0	0	3					87.60
129thr	0	0	3					87.60
129val	0	0	3					87.60
130arg	1	0	9				1	27.70
130his	1	0	1				1	27.70
130ile	1	0	1				1	27.70
130phe	1	0	10				1	27.70
130pro	1	1	2		1		1	27.70
130val	1	0	15				1	27.70
131asp	0	0	1					42.60
131his	1	1	3	1				42.60
131ile	1	1	5	1				42.60
131lys	0	0	2					42.60
131ser	0	0	3					42.60
131tyr	1	1	3	1				42.60
132arg	1	0	41			1	1	6.10
132asn	1	0	34			1	1	6.10
132gln	1	0	14			1	1	6.10

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Clash	Cavities	In Patch	Conserved	Accessibility
132glu	1	1	19	1			1	1	6.10
132leu	1	1	1	1			1	1	6.10
132met	1	1	9	1			1	1	6.10
132thr	1	0	3				1	1	6.10
132trp	1	0	1				1	1	6.10
133arg	0	0	3						0.10
133ile	0	0	6						0.10
133leu	0	0	3						0.10
133lys	0	0	9						0.10
133thr	1	1	4			1			0.10
133val	1	1	2			1			0.10
134cys	0	0	5						0.00
134ile	0	0	2						0.00
134leu	0	0	17						0.00
134ser	0	0	1						0.00
134val	0	0	3						0.00
135arg	1	1	8	1	1				0.00
135gly	1	1	7	1					0.00
135phe	1	1	35	1					0.00
135ser	1	1	12	1					0.00
135trp	1	1	21	1	1				0.00

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Clash	In Patch	Conserved	Accessibility
135tyr	1	1	57	1		1			0.00
136arg	0	0	6						17.80
136glu	0	0	5						17.80
136his	0	0	3						17.80
136lys	0	0	1						17.80
136pro	1	1	2		1				17.80
137gln	1	0	3					1	27.40
137met	1	0	3					1	27.40
137pro	1	1	3		1			1	27.40
137val	1	0	3					1	27.40
138asp	0	0	3						45.60
138pro	1	1	22		1				45.60
138thr	0	0	5						45.60
138val	0	0	38						45.60
139arg	1	0	3					1	44.00
139asn	1	0	10					1	44.00
139gln	1	0	2					1	44.00
139glu	1	0	2					1	44.00
139thr	1	0	1					1	44.00
140ala	1	1	4	1			1		30.70
140ile	1	1	11	1			1		30.70

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Cavities	In Patch	Conserved	Accessibility
140pro	1	1	1	1		1		30.70
140ser	1	0	2			1		30.70
141arg	1	1	15	1				0.00
141gly	1	1	1	1				0.00
141phe	1	1	5	1				0.00
141ser	1	1	3	1				0.00
141trp	1	1	11	1				0.00
141tyr	1	1	67	1				0.00
142ala	1	0	2			1	1	16.40
142his	1	0	1			1	1	16.40
142leu	1	0	12			1	1	16.40
142phe	1	0	3			1	1	16.40
142ser	1	0	6			1	1	16.40
142thr	1	0	1			1	1	16.40
143ala	1	1	16		1			0.00
143glu	0	0	4					0.00
143gly	1	1	1		1			0.00
143leu	0	0	3					0.00
143met	0	0	20					0.00
144arg	1	1	7	1		1		18.80
144his	1	1	5	1		1		18.80

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Accessibility
144leu	1	1	5	1			1	18.80
144lys	1	1	1	1			1	18.80
144pro	1	1	7	1	1		1	18.80
145arg	0	0	3					0.70
145gln	0	0	12					0.70
145met	0	0	2					0.70
145pro	1	1	13		1	1		0.70
145val	0	0	4					0.70
146arg	1	0	6				1	33.10
146cys	1	1	1	1			1	33.10
146gly	1	1	1	1			1	33.10
146leu	1	1	2	1			1	33.10
146ser	1	0	3				1	33.10
147ala	1	0	4				1	16.90
147asp	1	0	5				1	16.90
147glu	1	0	4				1	16.90
147gly	1	0	6				1	16.90
147ile	1	0	6				1	16.90
148ala	1	0	1				1	75.00
148asn	1	0	4				1	75.00
148glu	1	0	4				1	75.00

Mutation	Explained?	Struc-Explained?	NExamples	Pro	Cavities	In Patch	Conserved	Accessibility
148tyr	1	0	3			1		75.00
148val	1	0	1			1		75.00
149phe	1	0	5			1		45.00
149pro	1	1	4	1		1		45.00
149thr	1	0	3			1		45.00
150ala	1	0	1			1		60.30
150arg	1	0	1			1		60.30
150ile	1	0	6			1		60.30
150lys	1	0	3			1		60.30
150pro	1	0	1			1		60.30
151ala	1	1	9		1		1	3.10
151arg	1	0	11				1	3.10
151his	1	0	28				1	3.10
151leu	1	0	12				1	3.10
151ser	1	1	72		1		1	3.10
151thr	1	0	15				1	3.10
152ala	1	0	2			1	1	43.90
152arg	1	0	3			1	1	43.90
152gln	1	0	4			1	1	43.90
152leu	1	0	57			1	1	43.90
152ser	1	0	23			1	1	43.90

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Gly	In Patch	Conserved	Accessibility
152thr	1	0	6			1	1	43.90
153ala	1	0	2			1		93.00
153his	1	0	1			1		93.00
153leu	1	0	5			1		93.00
153ser	1	0	10			1		93.00
153thr	1	0	4			1		93.00
154ala	1	1	1		1	1		45.00
154asp	1	1	7		1	1		45.00
154cys	1	1	1		1	1		45.00
154ile	1	1	1		1	1		45.00
154ser	1	1	9		1	1		45.00
154val	1	1	44		1	1		45.00
155ala	1	1	8	1				2.50
155asn	1	1	14	1				2.50
155ile	1	1	13	1				2.50
155met	1	1	1	1				2.50
155pro	1	1	14	1				2.50
155ser	1	1	5	1				2.50
156cys	1	0	7			1		23.20
156gly	1	0	4			1		23.20
156his	1	0	14			1		23.20

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	In Patch	Conserved	Accessibility
156leu	1	0	1			1		23.20
156pro	1	1	31		1	1		23.20
156ser	1	0	4			1		23.20
157ala	0	0	1					0.70
157asp	0	0	9					0.70
157gly	0	0	11					0.70
157ile	0	0	11					0.70
157leu	0	0	9					0.70
157phe	0	0	126					0.70
158cys	1	1	11	1		1	1	14.00
158gln	1	0	1			1	1	14.00
158gly	1	1	20	1		1	1	14.00
158his	1	1	68	1		1	1	14.00
158leu	1	1	73	1		1	1	14.00
158phe	1	1	1	1		1	1	14.00
158pro	1	1	13	1	1	1	1	14.00
158ser	1	0	2			1	1	14.00
158tyr	1	0	1			1	1	14.00
159asp	1	0	11				1	0.20
159gly	1	0	2				1	0.20
159pro	1	1	22		1		1	0.20

Mutation	Explained?	Struc-Explained?	NExamples	Pro	In Patch	Conserved	Accessibility
159ser	1	0	3			1	0.20
159thr	1	0	8			1	0.20
159val	1	0	37			1	0.20
160ile	1	0	9		1		14.10
160leu	1	0	5		1		14.10
160lys	1	0	3		1		14.10
160val	1	0	8		1		14.10
161asp	1	0	11		1		8.80
161gly	1	0	4		1		8.80
161phe	1	0	1		1		8.80
161pro	1	1	2	1	1		8.80
161ser	1	0	1		1		8.80
161thr	1	0	52		1		8.80
161val	1	0	10		1		8.80
162asn	0	0	2				0.20
162met	0	0	6				0.20
162phe	0	0	7				0.20
162ser	0	0	7				0.20
162thr	0	0	3				0.20
162val	0	0	5				0.20
163asn	0	0	21				1.00

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	In Patch	Conserved	Accessibility
163asp	0	0	3					1.00
163cys	0	0	99					1.00
163his	0	0	16					1.00
163ser	0	0	3					1.00
164arg	1	0	2				1	46.80
164asn	1	0	8				1	46.80
164gln	1	0	5				1	46.80
164glu	1	0	15				1	46.80
164met	1	0	4				1	46.80
164thr	1	0	2				1	46.80
165arg	0	0	4					38.10
165glu	0	0	2					38.10
165his	0	0	1					38.10
165leu	0	0	4					38.10
165pro	1	1	3		1			38.10
166ala	1	0	3			1		76.90
166gly	1	0	1			1		76.90
166leu	1	0	10			1		76.90
166pro	1	1	2		1	1		76.90
166thr	1	0	13			1		76.90
167arg	1	1	9	1		1		67.10

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	In Patch	Accessibility
167his	1	1	9	1		1	67.10
167leu	1	1	2	1		1	67.10
167lys	1	1	1	1		1	67.10
168arg	1	0	21			1	28.30
168asn	1	0	2			1	28.30
168asp	1	0	2			1	28.30
168gln	1	0	2			1	28.30
168leu	1	0	5			1	28.30
168pro	1	1	6		1	1	28.30
168tyr	1	0	10			1	28.30
168val	1	0	1			1	28.30
169ile	1	0	14			1	21.20
169lys	1	0	2			1	21.20
169thr	1	0	4			1	21.20
169val	1	0	6			1	21.20
170ala	1	1	4	1		1	65.90
170lys	1	0	1			1	65.90
170met	1	1	7	1		1	65.90
170pro	1	1	1	1	1	1	65.90
170ser	1	1	2	1		1	65.90
171ala	1	1	1	1		1	45.30

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Cavities	In Patch	Conserved	Accessibility
171asp	1	0	2			1		45.30
171gln	1	0	1			1		45.30
171gly	1	1	5	1		1		45.30
171lys	1	1	8	1		1		45.30
171val	1	1	1	1		1		45.30
172ala	1	0	9			1	1	24.50
172asp	1	0	10			1	1	24.50
172gly	1	0	5			1	1	24.50
172ile	1	0	4			1	1	24.50
172phe	1	0	12			1	1	24.50
173ala	1	0	15			1	1	6.10
173glu	1	0	2			1	1	6.10
173gly	1	1	13		1	1	1	6.10
173leu	1	0	71			1	1	6.10
173met	1	0	52			1	1	6.10
173trp	1	0	1			1	1	6.10
174gly	1	0	1			1		40.80
174lys	1	0	8			1		40.80
174met	1	0	2			1		40.80
174ser	1	0	7			1		40.80
174thr	1	0	1			1		40.80

Mutation	Explained?	Struc-Explained?	NExamples	Zinc	HBond	Pro	In Patch	Conserved	Accessibility
174trp	1	0	12				1		40.80
175cys	1	1	19		1			1	6.50
175gln	1	0	1					1	6.50
175gly	1	1	19		1			1	6.50
175his	1	1	828		1			1	6.50
175leu	1	1	22		1			1	6.50
175pro	1	1	5		1	1		1	6.50
175ser	1	1	10		1			1	6.50
176arg	1	1	10	1	1				4.10
176gly	1	1	6	1	1				4.10
176phe	1	1	143	1	1				4.10
176ser	1	1	25	1	1				4.10
176trp	1	1	12	1	1				4.10
176tyr	1	1	59	1	1				4.10
177ala	1	0	1				1	1	64.10
177arg	1	0	12				1	1	64.10
177his	1	0	3				1	1	64.10
177ile	1	0	1				1	1	64.10
177leu	1	0	27				1	1	64.10
177phe	1	0	3				1	1	64.10
177ser	1	0	12				1	1	64.10

Mutation	Explained?	Struc-Explained?	NExamples	Zinc	HBond	Pro	Conserved	Accessibility
178arg	1	0	2				1	60.50
178asn	1	0	7				1	60.50
178asp	1	0	9				1	60.50
178gln	1	0	1				1	60.50
178leu	1	0	1				1	60.50
178pro	1	1	7			1	1	60.50
178tyr	1	0	9				1	60.50
179arg	1	1	113	1	1		1	27.50
179asn	1	1	14	1	1		1	27.50
179asp	1	1	18	1	1		1	27.50
179gln	1	1	15	1	1		1	27.50
179leu	1	1	30	1	1		1	27.50
179pro	1	1	3	1	1	1	1	27.50
179tyr	1	1	73	1	1		1	27.50
180ala	0	0	1					30.90
180asp	0	0	1					30.90
180gln	0	0	1					30.90
180gly	0	0	1					30.90
180lys	0	0	6					30.90
180val	0	0	1					30.90
181cys	0	0	20					82.30

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Accessibility
181gly	0	0	2			82.30
181his	0	0	26			82.30
181leu	0	0	4			82.30
181pro	1	1	19		1	82.30
181ser	0	0	2			82.30
182arg	0	0	3			54.80
182ser	0	0	6			54.80
182tyr	0	0	4			54.80
183leu	1	1	2	1		27.70
183pro	1	1	3	1	1	27.70
184asn	0	0	11			63.30
184gly	1	1	1	1		63.30
184his	1	1	4	1		63.30
184tyr	0	0	3			63.30
185arg	1	1	2	1		52.70
185asn	1	1	1	1		52.70
185cys	1	1	1	1		52.70
185gly	1	1	2	1		52.70
185ile	1	1	2	1		52.70
186asn	1	1	2	1		55.50
186glu	1	1	1	1		55.50

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Gly	In Patch	Accessibility
186gly	1	1	2	1			55.50
186his	1	1	2	1			55.50
186tyr	1	1	1	1			55.50
186val	1	1	2	1			55.50
187arg	1	1	2		1		95.20
187asn	1	1	1		1		95.20
187asp	1	1	3		1		95.20
187cys	1	1	5		1		95.20
187ser	1	1	7		1		95.20
187val	1	1	2		1		95.20
188val	0	0	4				42.30
189asp	0	0	1				3.60
189gly	0	0	2				3.60
189pro	0	0	4				3.60
189thr	0	0	5				3.60
189val	0	0	12				3.60
190ala	1	0	1			1	23.00
190arg	1	0	3			1	23.00
190his	1	0	1			1	23.00
190leu	1	0	26			1	23.00
190ser	1	0	3			1	23.00

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Accessibility
190thr	1	0	3				1	23.00
191arg	1	0	1				1	43.90
191his	1	0	3				1	43.90
191leu	1	0	4				1	43.90
191ser	1	0	3				1	43.90
191thr	1	0	4				1	43.90
192arg	1	0	8				1	21.10
192his	1	1	5	1			1	21.10
192leu	1	1	3	1			1	21.10
192lys	1	0	1				1	21.10
192pro	1	1	1	1	1		1	21.10
193arg	0	0	52					1.90
193asn	0	0	3					1.90
193asp	0	0	10					1.90
193gln	0	0	2					1.90
193leu	0	0	38					1.90
193pro	1	1	11		1			1.90
193tyr	0	0	28					1.90
194arg	0	0	39					3.10
194his	0	0	5					3.10
194ile	1	1	4			1		3.10

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Conserved	Accessibility
194phe	0	0	19						3.10
194pro	1	1	12		1	1			3.10
194val	0	0	2						3.10
195asn	1	0	6				1		5.30
195phe	1	0	20				1		5.30
195ser	1	0	5				1		5.30
195thr	1	0	56				1		5.30
195tyr	1	0	1				1		5.30
195val	1	0	1				1		5.30
196gln	1	1	6	1			1	1	5.40
196leu	1	1	2	1			1	1	5.40
196pro	1	1	14	1	1		1	1	5.40
196ser	1	1	1	1			1	1	5.40
197glu	0	0	5						3.90
197gly	0	0	10						3.90
197leu	0	0	3						3.90
197met	0	0	5						3.90
198asp	1	0	1				1	1	40.50
198gln	1	0	2				1	1	40.50
198gly	1	1	1	1			1	1	40.50
198lys	1	0	4				1	1	40.50

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Clash	In Patch	Conserved	Accessibility
199ala	1	0	1				1	1	104.50
199arg	1	0	6				1	1	104.50
199glu	1	0	11				1	1	104.50
199val	1	0	3				1	1	104.50
200asp	1	0	1				1		32.20
200lys	1	1	1	1			1		32.20
200pro	1	1	1	1	1		1		32.20
200ser	1	0	2				1		32.20
201phe	1	0	8				1		92.20
201pro	1	1	1		1		1		92.20
202cys	1	0	4				1		70.60
202gly	1	0	1				1		70.60
202his	1	0	10				1		70.60
202leu	1	0	5				1		70.60
202pro	1	1	5		1		1		70.60
202ser	1	0	6				1		70.60
203ala	1	0	2				1		7.80
203glu	1	0	9				1		7.80
203leu	1	0	6				1		7.80
203met	1	0	1				1		7.80
203trp	1	1	1			1	1		7.80

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Cavities	In Patch	Conserved	Accessibility
204ala	1	0	1			1		43.50
204gly	1	0	1			1		43.50
204lys	1	0	3			1		43.50
204val	1	0	1			1		43.50
205asn	1	1	2	1		1	1	16.20
205asp	1	1	11	1		1	1	16.20
205cys	1	1	86	1	1	1	1	16.20
205his	1	1	6	1		1	1	16.20
205phe	1	1	4	1		1	1	16.20
205ser	1	1	12	1	1	1	1	16.20
206met	1	0	1			1		32.80
206phe	1	0	1			1		32.80
207asn	1	1	1	1		1		35.40
207glu	1	1	2	1		1		35.40
207gly	1	1	3	1		1		35.40
207his	1	1	2	1		1		35.40
207val	1	1	1	1		1		35.40
208asn	1	0	6			1	1	36.60
208glu	1	0	2			1	1	36.60
208gly	1	0	4			1	1	36.60
208his	1	0	1			1	1	36.60

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	In Patch	Conserved	Accessibility
208tyr	1	0	1			1	1	36.60
208val	1	0	12			1	1	36.60
209ile	1	0	1			1		88.20
209lys	1	0	5			1		88.20
209thr	1	0	3			1		88.20
210asp	1	0	3			1		87.10
210his	1	0	3			1		87.10
210ile	1	0	1			1		87.10
210ser	1	0	3			1		87.10
211ala	1	0	4			1		24.70
211asn	1	0	3			1		24.70
211ile	1	0	13			1		24.70
212leu	1	0	7			1		69.00
212ser	1	0	3			1		69.00
212tyr	1	0	1			1		69.00
212val	1	0	1			1		69.00
213gln	1	1	30	1				3.60
213gly	1	1	5	1				3.60
213leu	1	1	24	1				3.60
213pro	1	1	3	1	1			3.60
214arg	1	0	51			1		9.60

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Conserved	Accessibility
214asp	1	1	3	1			1		9.60
214gln	1	0	4				1		9.60
214pro	1	1	1	1	1		1		9.60
214tyr	1	0	5				1		9.60
215arg	1	1	11	1				1	2.40
215asn	1	0	12					1	2.40
215cys	1	1	4	1				1	2.40
215gly	1	1	7	1				1	2.40
215ile	1	1	12	1				1	2.40
215lys	1	1	2	1				1	2.40
215thr	1	0	2					1	2.40
216ala	1	0	4					1	1.30
216glu	1	0	4					1	1.30
216gly	1	1	3			1		1	1.30
216leu	1	0	12					1	1.30
216met	1	0	45					1	1.30
216trp	1	0	1					1	1.30
217ala	0	0	3						1.50
217glu	0	0	4						1.50
217gly	0	0	3						1.50
217leu	0	0	2						1.50

Mutation	Explained?	Struc-Explained?	NExamples	Cavities	In Patch	Conserved	Accessibility
217met	0	0	3				1.50
218ala	1	0	4			1	1.70
218glu	1	0	7			1	1.70
218gly	1	0	8			1	1.70
218leu	1	0	3			1	1.70
218met	1	0	15			1	1.70
219cys	1	0	1		1	1	20.50
219his	1	0	1		1	1	20.50
219leu	1	0	7		1	1	20.50
219ser	1	0	4		1	1	20.50
219thr	1	0	2		1	1	20.50
220asn	1	1	8	1	1	1	8.00
220asp	1	0	2		1	1	8.00
220cys	1	0	233		1	1	8.00
220his	1	0	11		1	1	8.00
220ser	1	0	10		1	1	8.00
221ala	1	0	3		1	1	68.30
221asp	1	0	5		1	1	68.30
221gln	1	0	2		1	1	68.30
221gly	1	0	2		1	1	68.30
221lys	1	0	3		1	1	68.30

Mutation	Explained?	NExamples	In Patch	Conserved	Accessibility
222arg	1	1	1		54.70
222gln	1	4	1		54.70
222leu	1	5	1		54.70
222ser	1	2	1		54.70
222thr	1	1	1		54.70
223ala	1	1	1	1	28.10
223his	1	4	1	1	28.10
223leu	1	2	1	1	28.10
223ser	1	1	1	1	28.10
224asp	1	8	1		82.10
224gly	1	2	1		82.10
224lys	1	6	1		82.10
224val	1	2	1		82.10
225ala	1	2	1		103.80
225asp	1	1	1		103.80
225gly	1	1	1		103.80
225ile	1	1	1		103.80
225leu	1	1	1		103.80
225phe	1	2	1		103.80
226ala	1	3	1		104.90
226asn	1	1	1		104.90

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	In Patch	Conserved	Accessibility
226asp	1	0	3			1		104.90
226ser	1	0	1			1		104.90
226val	1	0	1			1		104.90
227cys	1	0	1			1		49.40
227phe	1	0	7			1		49.40
227thr	1	0	1			1		49.40
228ala	1	0	2			1		77.30
228asn	1	0	6			1		77.30
228glu	1	0	5			1		77.30
228gly	1	0	6			1		77.30
228his	1	0	2			1		77.30
228pro	1	1	1		1	1		77.30
228tyr	1	0	1			1		77.30
228val	1	0	1			1		77.30
229arg	1	0	2			1		21.60
229asn	1	0	1			1		21.60
229gly	1	0	1			1		21.60
229ser	1	0	5			1		21.60
229tyr	1	0	3			1		21.60
230ala	1	1	3	1		1	1	11.70
230asn	1	0	3			1	1	11.70

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Conserved	Accessibility
230ile	1	1	8	1			1	1	11.70
230pro	1	1	2	1	1		1	1	11.70
230ser	1	0	2				1	1	11.70
231ala	1	0	3				1		40.60
231asn	1	0	2				1		40.60
231ile	1	0	3				1		40.60
231ser	1	0	3				1		40.60
232asn	1	0	10				1		6.40
232leu	1	0	2				1		6.40
232phe	1	0	6				1		6.40
232ser	1	0	7				1		6.40
232thr	1	0	10				1		6.40
232val	1	0	4				1		6.40
233arg	1	0	1				1		40.00
233asp	1	0	1				1		40.00
233gln	1	0	3				1		40.00
233leu	1	0	1				1		40.00
233tyr	1	0	4				1		40.00
234asn	0	0	10						1.10
234asp	1	1	3			1			1.10
234cys	1	1	83			1			1.10

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Clash	Cavities	In Patch	Accessibility
234his	0	0	15					1.10
234phe	0	0	1					1.10
234ser	1	1	6			1		1.10
235asp	1	1	6	1			1	11.00
235his	1	1	1	1			1	11.00
235ile	1	1	4	1			1	11.00
235ser	1	1	13	1			1	11.00
235thr	1	1	4	1			1	11.00
235tyr	1	1	4		1		1	11.00
236asn	1	1	15	1				0.00
236asp	1	1	6	1				0.00
236cys	1	1	45	1		1		0.00
236his	1	1	8	1				0.00
236phe	1	1	1	1				0.00
236ser	1	1	3	1		1		0.00
237arg	1	0	6				1	7.70
237ile	1	0	132				1	7.70
237leu	1	0	5				1	7.70
237lys	1	0	6				1	7.70
237thr	1	0	3				1	7.70
237val	1	0	8				1	7.70

Mutation	Explained?	Struc-Explained?	NExamples	DNA	Zinc	HBond	Clash	Conserved	Accessibility
238arg	1	1	18		1	1			0.50
238gly	1	1	9		1	1			0.50
238his	1	1	1		1	1			0.50
238phe	1	1	29		1	1	1		0.50
238ser	1	1	19		1	1			0.50
238trp	1	1	5		1	1	1		0.50
238tyr	1	1	58		1	1	1		0.50
239asp	1	1	31	1				1	30.60
239his	1	1	1	1				1	30.60
239ile	1	1	1	1				1	30.60
239lys	1	1	9	1				1	30.60
239ser	1	1	27	1				1	30.60
239thr	1	1	9	1				1	30.60
239tyr	1	1	8	1				1	30.60
240arg	1	1	11			1		1	8.70
240asn	1	1	4			1		1	8.70
240cys	1	1	4			1		1	8.70
240gly	1	1	15			1		1	8.70
240ile	1	1	6			1		1	8.70
240thr	1	1	5			1		1	8.70
241ala	1	1	9	1				1	40.10

Mutation	Explained?	Struc-Explained?	NExamples	DNA	Zinc	HBond	Pro	Gly	Clash	In Patch	Conserved	Accessibility
241cys	1	1	24	1							1	40.10
241phe	1	1	83	1							1	40.10
241pro	1	1	8	1			1				1	40.10
241thr	1	1	7	1							1	40.10
241tyr	1	1	11	1							1	40.10
242arg	1	1	8		1	1					1	10.10
242gly	1	1	5		1	1					1	10.10
242phe	1	1	57		1	1			1		1	10.10
242ser	1	1	28		1	1					1	10.10
242trp	1	1	13		1	1			1		1	10.10
242tyr	1	1	39		1	1			1		1	10.10
243arg	1	1	2	1						1	1	61.20
243ile	1	1	10	1						1	1	61.20
243leu	1	1	6	1						1	1	61.20
243lys	1	1	3	1						1	1	61.20
243thr	1	1	6	1						1	1	61.20
243val	1	1	2	1						1	1	61.20
244ala	1	1	4					1		1	1	69.10
244arg	1	1	4					1		1	1	69.10
244asp	1	1	42					1		1	1	69.10
244cys	1	1	36					1		1	1	69.10

Mutation	Explained?	Struc-Explained?	NExamples	DNA	Gly	Clash	In Patch	Conserved	Accessibility
244glu	1	1	1		1		1	1	69.10
244ser	1	1	47		1		1	1	69.10
244val	1	1	14		1		1	1	69.10
245ala	1	1	8		1			1	7.50
245arg	1	1	13		1	1		1	7.50
245asn	1	1	3		1			1	7.50
245asp	1	1	105		1			1	7.50
245cys	1	1	68		1			1	7.50
245glu	1	1	1		1			1	7.50
245his	1	1	1		1	1		1	7.50
245leu	1	1	9		1			1	7.50
245phe	1	1	1		1	1		1	7.50
245ser	1	1	296		1			1	7.50
245val	1	1	56		1			1	7.50
246arg	0	0	13						0.50
246ile	0	0	35						0.50
246leu	0	0	7						0.50
246lys	0	0	7						0.50
246thr	0	0	10						0.50
246val	0	0	38						0.50
247asp	1	1	6	1			1	1	47.30

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Pro	In Patch	Conserved	Accessibility
247ile	1	1	7	1			1	1	47.30
247lys	1	1	3	1			1	1	47.30
247ser	1	1	2	1			1	1	47.30
247thr	1	1	7	1			1	1	47.30
247tyr	1	1	1	1			1	1	47.30
248gln	1	1	613	1					70.90
248gly	1	1	17	1					70.90
248leu	1	1	78	1					70.90
248pro	1	1	13	1		1			70.90
248trp	1	1	499	1					70.90
249asn	1	1	1		1			1	14.20
249gly	1	1	29		1			1	14.20
249ile	1	1	1		1			1	14.20
249lys	1	1	16		1			1	14.20
249met	1	1	52		1			1	14.20
249ser	1	1	311		1			1	14.20
249thr	1	1	19		1			1	14.20
249trp	1	1	25		1			1	14.20
250ala	0	0	11						32.50
250asn	0	0	2						32.50
250gln	0	0	2						32.50

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Conserved	Accessibility
250his	0	0	2				32.50
250leu	0	0	36				32.50
250phe	0	0	2				32.50
250ser	0	0	14				32.50
250thr	0	0	5				32.50
251asn	1	0	8			1	0.10
251leu	1	0	3			1	0.10
251phe	1	0	5			1	0.10
251ser	1	0	22			1	0.10
251thr	1	0	4			1	0.10
251val	1	0	5			1	0.10
252his	0	0	1				7.80
252phe	0	0	4				7.80
252pro	1	1	6		1		7.80
252val	0	0	1				7.80
253ala	1	1	4	1		1	0.00
253asn	1	0	2			1	0.00
253ile	1	1	7	1		1	0.00
253pro	1	1	3	1	1	1	0.00
253ser	1	0	4			1	0.00
254asn	0	0	12				5.00

Mutation	Explained?	Struc-Explained?	NExamples	Pro	Cavities	In Patch	Conserved	Accessibility
254asp	0	0	3					5.00
254leu	0	0	1					5.00
254met	0	0	1					5.00
254phe	0	0	1					5.00
254ser	0	0	5					5.00
254thr	0	0	6					5.00
254val	0	0	4					5.00
255asn	0	0	5					0.00
255met	0	0	2					0.00
255phe	0	0	29					0.00
255ser	0	0	6					0.00
255thr	0	0	9					0.00
255val	0	0	2					0.00
256ala	1	0	6			1		13.00
256arg	1	0	1			1		13.00
256ile	1	0	3			1		13.00
256lys	1	0	3			1		13.00
256pro	1	1	1	1		1		13.00
256ser	1	0	2			1		13.00
257arg	1	0	2				1	0.20
257gln	1	1	12		1		1	0.20

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Cavities	In Patch	Conserved	Accessibility
257pro	1	1	9		1	1		1	0.20
257val	1	1	5			1		1	0.20
258ala	1	1	1	1			1		6.80
258asp	1	0	11				1		6.80
258gln	1	0	13				1		6.80
258gly	1	1	14	1			1		6.80
258leu	1	1	1	1			1		6.80
258lys	1	1	50	1			1		6.80
258val	1	1	2	1			1		6.80
259asn	1	0	5				1		12.90
259glu	1	0	4				1		12.90
259gly	1	1	4	1			1		12.90
259his	1	1	3	1			1		12.90
259pro	1	0	0				1		12.90
259tyr	1	1	14	1			1		12.90
259val	1	1	16	1			1		12.90
260ala	1	1	3	1			1		71.80
260cys	1	1	1	1			1		71.80
260phe	1	1	3	1			1		71.80
260pro	1	1	2	1	1		1		71.80
260thr	1	0	1				1		71.80

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Gly	In Patch	Conserved	Accessibility
260tyr	1	1	1	1			1		71.80
261arg	1	0	4				1		69.60
261asn	1	0	2				1		69.60
261cys	1	1	1	1			1		69.60
261gly	1	1	2	1			1		69.60
261ile	1	1	2	1			1		69.60
262asp	1	1	2			1	1	1	46.90
262cys	1	1	1			1	1	1	46.90
262his	1	1	1			1	1	1	46.90
262ser	1	1	5			1	1	1	46.90
262val	1	1	6			1	1	1	46.90
263asp	1	0	3				1		66.10
263his	1	0	1				1		66.10
263ile	1	0	2				1		66.10
263ser	1	0	1				1		66.10
264gln	1	0	1				1		42.70
264ile	1	0	3				1		42.70
264pro	1	1	1		1		1		42.70
265arg	1	0	3				1	1	16.20
265gln	1	0	4				1	1	16.20
265met	1	0	3				1	1	16.20

Mutation	Explained?	Struc-Explained?	NExamples	HBond	Pro	Clash	In Patch	Conserved	Accessibility
265pro	1	1	15		1		1	1	16.20
266ala	1	0	1					1	0.10
266arg	1	1	51			1		1	0.10
266glu	1	0	48					1	0.10
266val	1	0	29					1	0.10
267gln	1	0	9					1	12.90
267gly	1	1	3	1				1	12.90
267his	1	1	1	1				1	12.90
267pro	1	1	15	1	1			1	12.90
267trp	1	1	21	1				1	12.90
268his	1	1	3	1					15.80
268ile	1	1	1	1					15.80
268ser	1	1	8	1					15.80
268tyr	1	1	1	1					15.80
269arg	0	0	1						23.70
269asn	0	0	8						23.70
269cys	0	0	2						23.70
269gly	0	0	3						23.70
269ile	0	0	1						23.70
269thr	0	0	1						23.70
270cys	1	0	20					1	0.70

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Pro	Cavities	In Patch	Conserved	Accessibility
270ile	1	0	13						1	0.70
270leu	1	0	22						1	0.70
270ser	1	1	13				1		1	0.70
270tyr	1	0	5						1	0.70
270val	1	1	7				1		1	0.70
271ala	1	0	1					1	1	11.20
271arg	1	0	1					1	1	11.20
271asp	1	0	2					1	1	11.20
271gln	1	0	5					1	1	11.20
271gly	1	0	3					1	1	11.20
271lys	1	0	25					1	1	11.20
271pro	1	1	1			1		1	1	11.20
271val	1	0	4					1	1	11.20
272ala	1	0	7						1	1.10
272glu	1	0	8						1	1.10
272gly	1	0	5						1	1.10
272leu	1	0	34						1	1.10
272met	1	0	64						1	1.10
273asn	1	1	1	1						33.60
273cys	1	1	468	1	1					33.60
273gln	1	1	1	1						33.60

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Pro	Conserved	Accessibility
273gly	1	1	10	1	1			33.60
273his	1	1	544	1	1			33.60
273leu	1	1	108	1	1			33.60
273pro	1	1	26	1	1	1		33.60
273ser	1	1	11	1	1			33.60
273tyr	1	1	1	1				33.60
274ala	0	0	13					1.00
274asp	0	0	6					1.00
274gly	0	0	5					1.00
274ile	0	0	4					1.00
274leu	0	0	12					1.00
274phe	0	0	20					1.00
275arg	1	1	12	1	1		1	7.90
275gly	1	1	6	1	1		1	7.90
275phe	1	1	28	1	1		1	7.90
275ser	1	1	3	1			1	7.90
275trp	1	1	6	1	1		1	7.90
275tyr	1	1	52	1			1	7.90
276asp	1	1	9	1			1	62.60
276gly	1	1	4	1			1	62.60
276pro	1	1	15	1		1	1	62.60

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Clash	Conserved	Accessibility
276ser	1	1	19	1			1	62.60
276thr	1	1	10	1			1	62.60
276val	1	1	7	1			1	62.60
277arg	1	1	1	1			1	14.10
277gly	1	1	7	1	1		1	14.10
277phe	1	1	35	1	1		1	14.10
277ser	1	1	1	1			1	14.10
277trp	1	1	1	1	1		1	14.10
277tyr	1	1	24	1	1		1	14.10
278ala	1	0	15				1	0.00
278arg	1	1	29			1	1	0.00
278his	1	1	10			1	1	0.00
278leu	1	0	60				1	0.00
278phe	1	1	8			1	1	0.00
278ser	1	0	58				1	0.00
278thr	1	0	25				1	0.00
279arg	1	1	8			1	1	0.00
279glu	1	1	33			1	1	0.00
279trp	1	1	4			1	1	0.00
279val	1	1	2			1	1	0.00
280gly	1	1	28	1	1		1	47.80

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Pro	Conserved	Accessibility
280ile	1	1	15	1	1		1	47.80
280lys	1	1	51	1			1	47.80
280pro	1	1	1	1	1	1	1	47.80
280ser	1	1	13	1			1	47.80
280thr	1	1	67	1			1	47.80
281ala	1	1	2		1		1	12.00
281asn	1	1	24		1		1	12.00
281glu	1	1	39		1		1	12.00
281gly	1	1	13		1		1	12.00
281his	1	1	29		1		1	12.00
281tyr	1	1	7		1		1	12.00
281val	1	1	4		1		1	12.00
282gln	1	0	22				1	13.60
282gly	1	1	35		1		1	13.60
282his	1	1	1		1		1	13.60
282leu	1	1	8		1		1	13.60
282pro	1	1	12		1	1	1	13.60
282trp	1	0	399				1	13.60
283cys	1	1	18	1	1			45.70
283gly	1	1	4	1	1			45.70
283his	1	1	9	1	1			45.70

Mutation	Explained?	Struc-Explained?	NExamples	DNA	HBond	Pro	Accessibility
283leu	1	1	5	1	1		45.70
283pro	1	1	25	1	1	1	45.70
283ser	1	1	1	1			45.70
284ala	1	1	3		1		42.40
284ile	1	1	2		1		42.40
284lys	1	1	2		1		42.40
284pro	1	1	5		1	1	42.40
285ala	1	1	1		1		26.60
285asp	0	0	1				26.60
285gln	0	0	6				26.60
285gly	1	1	2		1		26.60
285lys	1	1	120		1		26.60
285val	1	1	14		1		26.60
286ala	1	1	2		1		32.10
286asp	0	0	1				32.10
286gln	0	0	11				32.10
286gly	1	1	17		1		32.10
286leu	1	1	1		1		32.10
286lys	0	0	61				32.10
286val	1	1	5		1		32.10
287asp	0	0	4				67.80

Mutation	Explained?	Struc-Explained?	NExamples	Pro	In Patch	Conserved	Accessibility
287gly	0	0	2				67.80
287lys	0	0	8				67.80
287val	0	0	2				67.80
288asp	0	0	1				67.20
288lys	0	0	1				67.20
288ser	0	0	5				67.20
288thr	0	0	2				67.20
288tyr	0	0	5				67.20
289arg	0	0	1				110.40
289his	0	0	1				110.40
289phe	0	0	10				110.40
289pro	1	1	3	1			110.40
289val	0	0	1				110.40
94leu	0	0	2				0.00
94thr	0	0	1				0.00
95thr	0	0	1				0.00
96cys	1	0	1		1		88.80
96phe	1	0	1		1		88.80
96pro	1	1	1	1	1		88.80
97phe	1	0	1		1		48.40
98leu	1	0	1		1	1	26.90

Mutation	Explained?	Struc-Explained?	NExamples	DNA	Zinc	HBond	Pro	Gly	Clash	Cavities	In Patch	Conserved	Accessibility
98ser	1	0	1								1	1	26.90
	82.43	42.22		7.72	2.75	26.88	5.71	3.92	2.54	2.75	46.35	36.93

Explained 779 mutants out of 945 distinct (82.433862%)
Structurally explained 399 mutants out of 945 distinct (42.222222%)
Mutations explained in structural terms and by patch analysis: 702 out of 945 distinct (74.285714%)
Mutations explained by patch analysis only: 438 out of 945 distinct (46.349206%)
Explained 11710 mutants out of 13115 observed (89.287076%)

p53 Mutations and Structure / Analysis

Contents

Overall Summary

Hydrogen Bonding

Mutations to Proline

Disallowed

Allowed

Mutations from Glycine

Disallowed

Allowed

Structural Clashes

DNA Binding

Residues involved

Zinc Binding

Cavity-creating Mutations

Mutations Affecting Protein-Interaction Sites

Mutations most likely to affect protein-protein or domain-domain interactions (from top 10 scoring patches)

Mutations to Conserved Residues

Conserved Residues

Summary of explained mutants

Codon	Amino Acid
119	ala
120	lys
121	ser
239	asn
241	ser
243	met
247	asn
248	arg
273	arg
275	cys
276	ala
277	cys
280	arg
283	arg

Codon	Residue	Mutation
199	gly	glu
166	ser	leu
166	ser	thr
174	arg	trp
190	pro	leu
208	asp	val
177	pro	arg
177	pro	leu
177	pro	ser
202	arg	his
211	thr	ile
158	arg	cys
158	arg	gly
158	arg	his
158	arg	leu
158	arg	pro
168	his	arg
168	his	tyr
154	gly	val
244	gly	asp
244	gly	cys
244	gly	ser
244	gly	val
169	met	ile
232	ile	asn
232	ile	thr
142	pro	leu
243	met	ile
152	pro	leu
152	pro	ser
110	arg	cys
110	arg	leu
271	glu	lys
258	glu	asp
258	glu	gln
258	glu	gly
258	glu	lys
156	arg	his
156	arg	pro
195	ile	phe
195	ile	thr
237	met	ile
132	lys	arg
132	lys	asn
132	lys	gln
132	lys	glu
259	asp	tyr
259	asp	val
153	pro	ser
172	val	asp
172	val	phe
196	arg	pro
235	asn	ser
265	leu	pro
140	thr	ile

Codon	Amino Acid	Conservation
98	pro	100
113	phe	100
120	lys	100
121	ser	100
122	val	100
125	thr	100
127	ser	100
130	leu	100
132	lys	100
137	leu	100
139	lys	100
142	pro	100
151	pro	100
152	pro	100
158	arg	100
159	ala	100
164	lys	100
172	val	100
173	val	100
175	arg	100
177	pro	100
178	his	100
179	his	100
196	arg	100
198	glu	100
199	gly	100
205	tyr	100
208	asp	100
215	ser	100
216	val	100
218	val	100
219	pro	100
220	tyr	100
221	glu	100
223	pro	100
230	thr	100
239	asn	100
240	ser	100
241	ser	100
242	cys	100
243	met	100
244	gly	100
245	gly	100
247	asn	100
249	arg	100
251	ile	100
253	thr	100
257	leu	100
262	gly	100
265	leu	100
266	gly	100
267	arg	100
270	phe	100
271	glu	100
272	val	100
275	cys	100
276	ala	100
277	cys	100
278	pro	100
279	gly	100
280	arg	100
281	asp	100
282	arg	100

Codon	Amino Acid
119	ala
120	lys
121	ser
239	asn
241	ser
243	met
247	asn
248	arg
273	arg
275	cys
276	ala
277	cys
280	arg
283	arg

Codon	Residue	Mutation
199	gly	glu
166	ser	leu
166	ser	thr
174	arg	trp
190	pro	leu
208	asp	val
177	pro	arg
177	pro	leu
177	pro	ser
202	arg	his
211	thr	ile
158	arg	cys
158	arg	gly
158	arg	his
158	arg	leu
158	arg	pro
168	his	arg
168	his	tyr
154	gly	val
244	gly	asp
244	gly	cys
244	gly	ser
244	gly	val
169	met	ile
232	ile	asn
232	ile	thr
142	pro	leu
243	met	ile
152	pro	leu
152	pro	ser
110	arg	cys
110	arg	leu
271	glu	lys
258	glu	asp
258	glu	gln
258	glu	gly
258	glu	lys
156	arg	his
156	arg	pro
195	ile	phe
195	ile	thr
237	met	ile
132	lys	arg
132	lys	asn
132	lys	gln
132	lys	glu
259	asp	tyr
259	asp	val
153	pro	ser
172	val	asp
172	val	phe
196	arg	pro
235	asn	ser
265	leu	pro
140	thr	ile

Codon	Amino Acid	Conservation
98	pro	100
113	phe	100
120	lys	100
121	ser	100
122	val	100
125	thr	100
127	ser	100
130	leu	100
132	lys	100
137	leu	100
139	lys	100
142	pro	100
151	pro	100
152	pro	100
158	arg	100
159	ala	100
164	lys	100
172	val	100
173	val	100
175	arg	100
177	pro	100
178	his	100
179	his	100
196	arg	100
198	glu	100
199	gly	100
205	tyr	100
208	asp	100
215	ser	100
216	val	100
218	val	100
219	pro	100
220	tyr	100
221	glu	100
223	pro	100
230	thr	100
239	asn	100
240	ser	100
241	ser	100
242	cys	100
243	met	100
244	gly	100
245	gly	100
247	asn	100
249	arg	100
251	ile	100
253	thr	100
257	leu	100
262	gly	100
265	leu	100
266	gly	100
267	arg	100
270	phe	100
271	glu	100
272	val	100
275	cys	100
276	ala	100
277	cys	100
278	pro	100
279	gly	100
280	arg	100
281	asp	100
282	arg	100

Codon	Amino Acid
119	ala
120	lys
121	ser
239	asn
241	ser
243	met
247	asn
248	arg
273	arg
275	cys
276	ala
277	cys
280	arg
283	arg

Codon	Residue	Mutation
199	gly	glu
166	ser	leu
166	ser	thr
174	arg	trp
190	pro	leu
208	asp	val
177	pro	arg
177	pro	leu
177	pro	ser
202	arg	his
211	thr	ile
158	arg	cys
158	arg	gly
158	arg	his
158	arg	leu
158	arg	pro
168	his	arg
168	his	tyr
154	gly	val
244	gly	asp
244	gly	cys
244	gly	ser
244	gly	val
169	met	ile
232	ile	asn
232	ile	thr
142	pro	leu
243	met	ile
152	pro	leu
152	pro	ser
110	arg	cys
110	arg	leu
271	glu	lys
258	glu	asp
258	glu	gln
258	glu	gly
258	glu	lys
156	arg	his
156	arg	pro
195	ile	phe
195	ile	thr
237	met	ile
132	lys	arg
132	lys	asn
132	lys	gln
132	lys	glu
259	asp	tyr
259	asp	val
153	pro	ser
172	val	asp
172	val	phe
196	arg	pro
235	asn	ser
265	leu	pro
140	thr	ile

Codon	Amino Acid	Conservation
98	pro	100
113	phe	100
120	lys	100
121	ser	100
122	val	100
125	thr	100
127	ser	100
130	leu	100
132	lys	100
137	leu	100
139	lys	100
142	pro	100
151	pro	100
152	pro	100
158	arg	100
159	ala	100
164	lys	100
172	val	100
173	val	100
175	arg	100
177	pro	100
178	his	100
179	his	100
196	arg	100
198	glu	100
199	gly	100
205	tyr	100
208	asp	100
215	ser	100
216	val	100
218	val	100
219	pro	100
220	tyr	100
221	glu	100
223	pro	100
230	thr	100
239	asn	100
240	ser	100
241	ser	100
242	cys	100
243	met	100
244	gly	100
245	gly	100
247	asn	100
249	arg	100
251	ile	100
253	thr	100
257	leu	100
262	gly	100
265	leu	100
266	gly	100
267	arg	100
270	phe	100
271	glu	100
272	val	100
275	cys	100
276	ala	100
277	cys	100
278	pro	100
279	gly	100
280	arg	100
281	asp	100
282	arg	100