FMO DATABASE

FMODB ID: ZYR6N

Calculation Name: 3MTV-A-Xray317

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3MTV

Chain ID: A

ChEMBL ID:

UniProt ID: B2ZAB4

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	203
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-2245205.346084
FMO2-HF: Nuclear repulsion	2165410.191261
FMO2-HF: Total energy	-79795.154823
FMO2-MP2: Total energy	-80032.006551

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1:ALA )

Summations of interaction energy for fragment #1(A:1:ALA )

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
72.913	73.935	4.936	-3.708	-2.249	-0.019

Interaction energy analysis for fragmet #1(A:1:ALA )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.763 / q_NPA : 0.864

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	VAL	0	-0.058	-0.027	3.894	2.517	3.722	-0.003	-0.663	-0.539	-0.002
4	A	4	TYR	0	0.042	0.028	6.186	2.506	2.506	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.826	-0.902	9.982	-17.349	-17.349	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.023	-0.032	12.228	0.418	0.418	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.002	0.002	14.996	0.998	0.998	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.874	0.921	17.180	15.293	15.293	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.021	0.019	18.481	0.097	0.097	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.013	0.006	14.116	-0.313	-0.313	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.010	-0.002	9.870	0.151	0.151	0.000	0.000	0.000	0.000
12	A	12	MET	0	0.002	-0.014	8.727	0.807	0.807	0.000	0.000	0.000	0.000
13	A	13	TYR	0	-0.050	-0.015	4.010	-2.573	-2.488	0.000	-0.016	-0.069	0.000
14	A	14	VAL	0	0.046	-0.001	4.493	4.357	4.477	0.000	-0.015	-0.104	0.000
15	A	15	ALA	0	-0.020	-0.011	1.836	-16.507	-17.041	4.930	-2.973	-1.423	-0.017
16	A	16	GLY	0	0.037	0.037	3.720	5.981	6.127	0.009	-0.041	-0.114	0.000
17	A	17	GLY	0	0.021	0.011	7.237	0.266	0.266	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.878	0.933	7.683	28.081	28.081	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.054	0.026	6.852	-4.137	-4.137	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.003	0.000	7.628	2.986	2.986	0.000	0.000	0.000	0.000
21	A	21	TRP	0	0.029	0.006	9.333	-0.728	-0.728	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.039	0.021	10.600	0.577	0.577	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.031	0.001	12.289	0.001	0.001	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.862	0.967	13.515	15.392	15.392	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.076	0.024	14.147	-0.897	-0.897	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.086	0.033	16.901	0.632	0.632	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.083	-0.041	18.262	-0.850	-0.850	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.869	-0.950	16.975	-15.329	-15.329	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.056	-0.025	13.121	-0.798	-0.798	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.856	0.929	14.653	14.857	14.857	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.048	0.034	8.637	-0.295	-0.295	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.886	-0.951	11.699	-22.951	-22.951	0.000	0.000	0.000	0.000
33	A	33	PRO	0	-0.030	-0.014	12.606	-0.854	-0.854	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.027	0.026	12.439	-0.772	-0.772	0.000	0.000	0.000	0.000
35	A	35	PRO	0	0.075	0.037	11.675	2.033	2.033	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.840	0.917	14.902	15.261	15.261	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.895	-0.950	14.764	-17.845	-17.845	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.036	0.001	10.298	-0.532	-0.532	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.932	0.975	14.594	15.840	15.840	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.015	0.007	17.032	0.391	0.391	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.081	-0.008	12.462	0.615	0.615	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.036	0.055	14.282	-0.260	-0.260	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.006	-0.019	15.215	-0.266	-0.266	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.961	0.997	17.429	15.184	15.184	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.086	0.039	11.796	0.767	0.767	0.000	0.000	0.000	0.000
46	A	46	HIS	0	-0.033	0.001	15.783	1.152	1.152	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.015	0.022	16.949	0.861	0.861	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.045	-0.042	19.427	0.565	0.565	0.000	0.000	0.000	0.000
49	A	49	PHE	0	0.021	0.020	16.383	0.295	0.295	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.032	0.017	17.711	0.176	0.176	0.000	0.000	0.000	0.000
51	A	51	PRO	0	0.009	0.000	14.302	-0.814	-0.814	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.013	0.007	11.535	-0.436	-0.436	0.000	0.000	0.000	0.000
53	A	53	HIS	0	-0.051	-0.025	12.591	0.441	0.441	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.015	0.016	8.731	-0.851	-0.851	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.010	0.006	11.324	1.712	1.712	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.802	-0.873	11.633	-22.668	-22.668	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.077	-0.039	13.045	1.778	1.778	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.022	-0.042	15.124	1.499	1.499	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.851	0.924	16.796	18.544	18.544	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.028	0.027	16.963	0.521	0.521	0.000	0.000	0.000	0.000
61	A	61	THR	0	0.002	-0.003	20.457	0.081	0.081	0.000	0.000	0.000	0.000
62	A	62	PHE	0	0.015	-0.009	17.994	0.032	0.032	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.054	0.028	23.553	0.248	0.248	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.048	-0.014	26.225	-0.293	-0.293	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.034	-0.009	24.806	0.067	0.067	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.023	0.026	27.130	0.332	0.332	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.052	-0.028	29.288	0.409	0.409	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.059	0.030	27.976	0.078	0.078	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.001	0.001	26.897	0.186	0.186	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.019	-0.008	23.176	-0.657	-0.657	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.036	-0.027	21.537	0.291	0.291	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.808	0.925	19.893	14.291	14.291	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.030	0.018	23.308	0.372	0.372	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.895	-0.952	23.134	-12.310	-12.310	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.071	-0.028	22.706	0.228	0.228	0.000	0.000	0.000	0.000
76	A	76	GLN	0	0.008	-0.006	26.773	-0.025	-0.025	0.000	0.000	0.000	0.000
77	A	77	TYR	0	0.017	0.018	28.963	0.008	0.008	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.033	-0.030	25.307	-0.316	-0.316	0.000	0.000	0.000	0.000
79	A	79	CYS	0	-0.082	-0.053	22.307	0.092	0.092	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.005	0.011	21.304	-0.370	-0.370	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.085	0.080	25.114	0.506	0.506	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.029	0.016	27.526	-0.273	-0.273	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.894	-0.922	29.652	-9.949	-9.949	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.109	-0.115	25.192	-0.311	-0.311	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.017	0.005	24.283	-0.594	-0.594	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.038	-0.014	25.547	0.396	0.396	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.866	-0.933	28.778	-8.923	-8.923	0.000	0.000	0.000	0.000
88	A	88	GLY	0	-0.036	-0.019	31.270	0.148	0.148	0.000	0.000	0.000	0.000
89	A	89	ASN	0	0.010	-0.007	32.149	-0.043	-0.043	0.000	0.000	0.000	0.000
90	A	90	CYS	0	-0.035	0.015	31.695	0.038	0.038	0.000	0.000	0.000	0.000
91	A	91	TRP	0	-0.010	-0.025	34.009	0.163	0.163	0.000	0.000	0.000	0.000
92	A	92	TRP	0	0.037	0.007	35.727	0.153	0.153	0.000	0.000	0.000	0.000
93	A	93	ARG	1	1.023	1.042	34.144	8.967	8.967	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.021	-0.030	35.811	0.130	0.130	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.086	-0.045	39.481	0.149	0.149	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.852	-0.933	42.117	-7.388	-7.388	0.000	0.000	0.000	0.000
97	A	97	SER	0	-0.096	-0.026	44.165	0.205	0.205	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.034	-0.027	45.775	0.151	0.151	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.060	0.050	48.549	-0.031	-0.031	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.118	0.057	49.399	-0.111	-0.111	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.886	-0.961	49.454	-6.038	-6.038	0.000	0.000	0.000	0.000
102	A	102	VAL	0	-0.009	-0.014	48.201	-0.083	-0.083	0.000	0.000	0.000	0.000
103	A	103	GLN	0	0.000	0.018	45.084	-0.221	-0.221	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.029	-0.009	45.529	-0.046	-0.046	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.873	0.935	46.619	5.897	5.897	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.799	-0.896	43.425	-7.111	-7.111	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.026	0.000	41.453	-0.148	-0.148	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.964	0.974	42.391	6.251	6.251	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.033	-0.007	43.806	-0.024	-0.024	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.028	-0.034	38.883	-0.079	-0.079	0.000	0.000	0.000	0.000
111	A	111	ASN	0	0.023	-0.017	39.776	-0.334	-0.334	0.000	0.000	0.000	0.000
112	A	112	GLN	0	-0.079	0.008	41.188	0.128	0.128	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.071	-0.017	38.914	0.003	0.003	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.030	0.014	36.429	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	115	TYR	0	0.022	-0.027	34.164	0.102	0.102	0.000	0.000	0.000	0.000
116	A	116	GLN	0	0.011	0.054	35.279	-0.015	-0.015	0.000	0.000	0.000	0.000
117	A	117	THR	0	-0.044	-0.023	31.543	-0.079	-0.079	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.959	0.986	26.516	11.163	11.163	0.000	0.000	0.000	0.000
119	A	119	HIS	0	-0.042	-0.030	25.989	-0.527	-0.527	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.068	0.042	29.109	-0.107	-0.107	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.068	-0.041	32.114	0.150	0.150	0.000	0.000	0.000	0.000
122	A	122	PRO	0	-0.001	-0.006	31.401	-0.188	-0.188	0.000	0.000	0.000	0.000
123	A	123	GLY	0	0.081	0.042	31.355	-0.241	-0.241	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.933	0.963	31.814	9.593	9.593	0.000	0.000	0.000	0.000
125	A	125	TYR	0	-0.022	0.002	35.491	0.265	0.265	0.000	0.000	0.000	0.000
126	A	126	LEU	0	0.038	0.013	33.796	0.184	0.184	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.021	-0.020	36.499	-0.013	-0.013	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.977	1.004	38.103	8.028	8.028	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.880	0.954	40.364	7.295	7.295	0.000	0.000	0.000	0.000
130	A	130	LEU	0	0.101	0.017	39.235	-0.070	-0.070	0.000	0.000	0.000	0.000
131	A	131	GLN	0	-0.014	0.018	42.177	0.028	0.028	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.073	-0.031	43.909	0.144	0.144	0.000	0.000	0.000	0.000
133	A	133	ASN	0	-0.088	-0.068	45.190	0.261	0.261	0.000	0.000	0.000	0.000
134	A	134	GLY	0	0.017	0.037	47.285	0.086	0.086	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.009	0.001	43.348	-0.030	-0.030	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.766	0.854	42.004	6.941	6.941	0.000	0.000	0.000	0.000
137	A	137	ALA	0	-0.014	0.018	37.269	0.002	0.002	0.000	0.000	0.000	0.000
138	A	138	VAL	0	0.020	-0.006	38.206	-0.114	-0.114	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.071	-0.041	33.356	-0.126	-0.126	0.000	0.000	0.000	0.000
140	A	140	ASP	-1	-0.582	-0.810	35.343	-8.061	-8.061	0.000	0.000	0.000	0.000
141	A	141	THR	0	0.086	0.006	34.072	-0.260	-0.260	0.000	0.000	0.000	0.000
142	A	142	HIS	0	-0.127	-0.106	34.600	-0.296	-0.296	0.000	0.000	0.000	0.000
143	A	143	GLY	0	-0.169	-0.080	36.624	0.160	0.160	0.000	0.000	0.000	0.000
144	A	144	PRO	0	-0.006	-0.014	35.941	-0.211	-0.211	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.032	0.011	33.580	-0.164	-0.164	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.002	0.030	28.507	-0.060	-0.060	0.000	0.000	0.000	0.000
147	A	147	ILE	0	-0.058	-0.027	27.501	-0.010	-0.010	0.000	0.000	0.000	0.000
148	A	148	GLN	0	-0.025	-0.043	24.541	-0.229	-0.229	0.000	0.000	0.000	0.000
149	A	149	TYR	0	-0.006	0.006	17.971	0.079	0.079	0.000	0.000	0.000	0.000
150	A	150	PHE	0	0.062	0.015	17.985	-0.434	-0.434	0.000	0.000	0.000	0.000
151	A	151	SER	0	-0.043	-0.006	14.571	-0.643	-0.643	0.000	0.000	0.000	0.000
152	A	152	VAL	0	-0.019	-0.022	13.580	-1.166	-1.166	0.000	0.000	0.000	0.000
153	A	153	LYS	1	0.985	0.999	14.239	19.953	19.953	0.000	0.000	0.000	0.000
154	A	154	GLU	-1	-0.953	-0.979	16.483	-16.158	-16.158	0.000	0.000	0.000	0.000
155	A	155	SER	0	-0.016	-0.001	18.575	0.767	0.767	0.000	0.000	0.000	0.000
156	A	156	TRP	0	-0.064	-0.047	18.826	0.471	0.471	0.000	0.000	0.000	0.000
157	A	157	ILE	0	-0.003	0.005	20.800	0.664	0.664	0.000	0.000	0.000	0.000
158	A	158	ARG	1	0.916	0.922	22.995	11.279	11.279	0.000	0.000	0.000	0.000
159	A	159	HIS	0	0.020	-0.010	25.849	0.453	0.453	0.000	0.000	0.000	0.000
160	A	160	LEU	0	-0.030	-0.002	28.117	-0.103	-0.103	0.000	0.000	0.000	0.000
161	A	161	LYS	1	0.879	0.952	28.135	10.919	10.919	0.000	0.000	0.000	0.000
162	A	162	LEU	0	0.035	0.005	32.250	-0.054	-0.054	0.000	0.000	0.000	0.000
163	A	163	VAL	0	-0.070	-0.050	32.453	-0.264	-0.264	0.000	0.000	0.000	0.000
164	A	164	GLU	-1	-0.899	-0.954	32.323	-8.677	-8.677	0.000	0.000	0.000	0.000
165	A	165	GLU	-1	-0.871	-0.901	32.522	-9.163	-9.163	0.000	0.000	0.000	0.000
166	A	166	PRO	0	0.047	0.021	29.255	-0.277	-0.277	0.000	0.000	0.000	0.000
167	A	167	SER	0	-0.050	-0.036	24.669	0.270	0.270	0.000	0.000	0.000	0.000
168	A	168	LEU	0	0.064	0.046	24.875	-0.108	-0.108	0.000	0.000	0.000	0.000
169	A	169	PRO	0	0.017	0.003	21.271	-0.489	-0.489	0.000	0.000	0.000	0.000
170	A	170	GLY	0	-0.006	-0.005	18.277	-0.186	-0.186	0.000	0.000	0.000	0.000
171	A	171	PHE	0	-0.034	-0.029	19.146	-0.187	-0.187	0.000	0.000	0.000	0.000
172	A	172	GLU	-1	-0.947	-0.971	18.318	-16.513	-16.513	0.000	0.000	0.000	0.000
173	A	173	ASP	-1	-0.884	-0.931	21.956	-11.611	-11.611	0.000	0.000	0.000	0.000
174	A	174	LEU	0	-0.074	-0.035	23.629	-0.308	-0.308	0.000	0.000	0.000	0.000
175	A	175	LEU	0	-0.016	-0.018	25.031	0.120	0.120	0.000	0.000	0.000	0.000
176	A	176	ARG	1	0.876	1.046	28.725	9.361	9.361	0.000	0.000	0.000	0.000
177	A	177	ILE	0	-0.027	0.009	32.239	0.104	0.104	0.000	0.000	0.000	0.000
178	A	178	ARG	1	0.886	0.927	35.277	7.608	7.608	0.000	0.000	0.000	0.000
179	A	179	VAL	0	-0.045	-0.029	38.858	-0.050	-0.050	0.000	0.000	0.000	0.000
180	A	180	GLU	-1	-0.805	-0.881	41.061	-7.037	-7.037	0.000	0.000	0.000	0.000
181	A	181	PRO	0	0.074	0.024	44.578	-0.034	-0.034	0.000	0.000	0.000	0.000
182	A	182	ASN	0	-0.042	-0.018	45.630	-0.042	-0.042	0.000	0.000	0.000	0.000
183	A	183	THR	0	0.015	-0.015	47.083	0.071	0.071	0.000	0.000	0.000	0.000
184	A	184	SER	0	0.000	0.011	49.602	0.170	0.170	0.000	0.000	0.000	0.000
185	A	185	PRO	0	0.006	-0.001	48.886	-0.163	-0.163	0.000	0.000	0.000	0.000
186	A	186	LEU	0	0.002	0.000	41.997	-0.017	-0.017	0.000	0.000	0.000	0.000
187	A	187	ALA	0	0.049	0.029	45.775	0.093	0.093	0.000	0.000	0.000	0.000
188	A	188	GLY	0	0.058	0.044	45.043	-0.122	-0.122	0.000	0.000	0.000	0.000
189	A	189	LYS	1	0.884	0.918	43.270	7.027	7.027	0.000	0.000	0.000	0.000
190	A	190	ASP	-1	-0.880	-0.938	39.667	-7.646	-7.646	0.000	0.000	0.000	0.000
191	A	191	GLU	-1	-0.866	-0.902	38.516	-7.951	-7.951	0.000	0.000	0.000	0.000
192	A	192	LYS	1	0.863	0.907	36.129	8.328	8.328	0.000	0.000	0.000	0.000
193	A	193	ILE	0	0.065	0.040	37.573	-0.127	-0.127	0.000	0.000	0.000	0.000
194	A	194	PHE	0	0.024	0.003	30.233	-0.226	-0.226	0.000	0.000	0.000	0.000
195	A	195	ARG	1	0.948	0.987	31.873	9.385	9.385	0.000	0.000	0.000	0.000
196	A	196	PHE	0	0.075	0.026	31.761	-0.347	-0.347	0.000	0.000	0.000	0.000
197	A	197	GLY	0	0.016	0.025	28.955	-0.289	-0.289	0.000	0.000	0.000	0.000
198	A	198	SER	0	-0.023	-0.030	29.415	0.354	0.354	0.000	0.000	0.000	0.000
199	A	199	HIS	0	-0.039	-0.041	26.556	-0.297	-0.297	0.000	0.000	0.000	0.000
200	A	200	LYS	1	0.913	0.989	22.757	12.253	12.253	0.000	0.000	0.000	0.000
201	A	201	TRP	0	-0.012	-0.004	26.979	0.474	0.474	0.000	0.000	0.000	0.000
202	A	202	TYR	0	-0.042	-0.040	27.748	-0.453	-0.453	0.000	0.000	0.000	0.000
203	A	203	NME	0	0.077	0.076	29.126	0.410	0.410	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1:ALA )