FMO DATABASE

FMODB ID: VR381

Calculation Name: 3MTV-A-Xray372

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: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	202
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2241825.430598
FMO2-HF: Nuclear repulsion	2162045.176539
FMO2-HF: Total energy	-79780.254058
FMO2-MP2: Total energy	-80016.409476

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.
-1.863	-0.215	3.797	-3.262	-2.183	-0.003

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 : 0 / q_Mulliken : -0.032 / q_NPA : -0.025

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	-0.050	-0.024	3.990	0.518	2.073	-0.006	-0.916	-0.633	0.001
4	A	4	TYR	0	-0.031	-0.035	6.378	0.385	0.385	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.794	-0.887	10.188	-0.151	-0.151	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.030	-0.023	12.366	-0.017	-0.017	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.006	0.008	15.238	0.047	0.047	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.829	0.885	17.485	0.172	0.172	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.016	0.018	18.692	0.021	0.021	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.018	-0.001	14.470	0.024	0.024	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.017	-0.009	10.016	-0.056	-0.056	0.000	0.000	0.000	0.000
12	A	12	MET	0	-0.018	-0.015	9.274	0.153	0.153	0.000	0.000	0.000	0.000
13	A	13	TYR	0	-0.007	0.001	4.248	-0.223	-0.154	-0.001	-0.010	-0.059	0.000
14	A	14	VAL	0	-0.001	-0.024	4.566	0.514	0.642	-0.001	-0.015	-0.111	0.000
15	A	15	ALA	0	0.056	0.030	1.979	-2.071	-2.298	3.797	-2.305	-1.266	-0.004
16	A	16	GLY	0	0.027	0.033	3.748	0.405	0.528	0.008	-0.016	-0.114	0.000
17	A	17	GLY	0	0.004	-0.001	7.269	-0.405	-0.405	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.876	0.932	7.777	-0.956	-0.956	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.035	0.020	6.857	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.009	0.003	7.935	0.072	0.072	0.000	0.000	0.000	0.000
21	A	21	TRP	0	0.039	0.011	9.585	-0.165	-0.165	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.036	0.024	10.722	0.082	0.082	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.020	-0.007	12.489	-0.061	-0.061	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.834	0.946	13.681	0.235	0.235	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.059	0.017	14.281	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.065	0.029	17.028	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.063	-0.022	18.378	-0.034	-0.034	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.824	-0.923	17.458	-0.135	-0.135	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.073	-0.029	13.035	-0.043	-0.043	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.841	0.900	14.691	0.242	0.242	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.044	0.029	9.135	-0.019	-0.019	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.884	-0.941	11.892	-0.900	-0.900	0.000	0.000	0.000	0.000
33	A	33	PRO	0	-0.019	-0.010	12.782	-0.013	-0.013	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.038	0.028	12.477	-0.067	-0.067	0.000	0.000	0.000	0.000
35	A	35	PRO	0	0.080	0.043	11.808	0.142	0.142	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.751	0.870	14.925	0.414	0.414	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.836	-0.926	15.415	-0.408	-0.408	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.048	0.016	10.422	0.025	0.025	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.933	0.973	14.615	0.344	0.344	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.031	-0.005	17.044	0.039	0.039	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.070	-0.002	12.247	0.037	0.037	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.040	0.047	14.385	0.036	0.036	0.000	0.000	0.000	0.000
43	A	43	ASN	0	0.043	0.019	15.249	0.031	0.031	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.940	1.004	17.337	0.080	0.080	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.077	0.042	12.247	0.022	0.022	0.000	0.000	0.000	0.000
46	A	46	HIS	0	0.008	0.015	16.051	0.019	0.019	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.024	-0.014	17.209	0.015	0.015	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.052	-0.047	19.605	0.018	0.018	0.000	0.000	0.000	0.000
49	A	49	PHE	0	0.016	0.016	16.643	0.019	0.019	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.046	0.019	18.050	-0.026	-0.026	0.000	0.000	0.000	0.000
51	A	51	PRO	0	-0.002	-0.006	14.520	0.033	0.033	0.000	0.000	0.000	0.000
52	A	52	HIS	0	0.006	0.017	11.691	0.045	0.045	0.000	0.000	0.000	0.000
53	A	53	HIS	0	-0.066	-0.009	12.756	0.087	0.087	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.036	0.024	8.947	-0.029	-0.029	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.018	0.018	11.295	-0.042	-0.042	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.769	-0.852	11.630	0.313	0.313	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.043	-0.019	13.054	-0.039	-0.039	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.026	-0.041	15.132	-0.038	-0.038	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.797	0.886	16.426	-0.253	-0.253	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.030	0.025	16.636	0.004	0.004	0.000	0.000	0.000	0.000
61	A	61	THR	0	0.016	0.009	20.461	-0.019	-0.019	0.000	0.000	0.000	0.000
62	A	62	PHE	0	-0.017	-0.026	17.968	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.038	0.019	23.559	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.005	0.004	26.229	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	PRO	0	-0.016	-0.022	24.745	0.007	0.007	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.015	0.019	27.129	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.031	-0.025	29.268	0.003	0.003	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.059	0.031	27.968	0.004	0.004	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.009	0.005	27.078	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.018	-0.013	23.357	0.009	0.009	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.014	-0.004	21.664	0.005	0.005	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.776	0.887	19.945	-0.019	-0.019	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.021	0.025	23.534	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.853	-0.924	22.764	0.051	0.051	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.048	-0.009	22.688	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	76	GLN	0	0.027	0.011	27.017	0.004	0.004	0.000	0.000	0.000	0.000
77	A	77	TYR	0	-0.010	-0.007	29.201	0.005	0.005	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.018	-0.020	25.454	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	79	CYS	0	-0.101	-0.054	22.518	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.025	0.017	21.235	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.098	0.067	25.052	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.017	0.006	27.519	0.012	0.012	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.885	-0.927	29.723	0.061	0.061	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.110	-0.081	25.151	0.011	0.011	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.015	-0.008	23.832	0.019	0.019	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.001	0.000	25.516	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.844	-0.905	28.757	0.069	0.069	0.000	0.000	0.000	0.000
88	A	88	GLY	0	-0.022	-0.001	31.467	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	89	ASN	0	-0.024	-0.044	32.325	0.005	0.005	0.000	0.000	0.000	0.000
90	A	90	CYS	0	-0.071	0.007	31.651	0.003	0.003	0.000	0.000	0.000	0.000
91	A	91	TRP	0	0.021	-0.022	34.130	0.001	0.001	0.000	0.000	0.000	0.000
92	A	92	TRP	0	0.016	0.003	35.843	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.955	0.988	33.747	-0.108	-0.108	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.022	-0.030	35.750	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.083	-0.042	39.575	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.843	-0.933	41.607	0.077	0.077	0.000	0.000	0.000	0.000
97	A	97	SER	0	-0.031	-0.011	44.249	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.094	-0.041	45.953	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.049	0.033	48.650	0.000	0.000	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.119	0.055	49.363	0.001	0.001	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.813	-0.909	49.551	0.047	0.047	0.000	0.000	0.000	0.000
102	A	102	VAL	0	-0.017	-0.008	48.498	0.000	0.000	0.000	0.000	0.000	0.000
103	A	103	GLN	0	0.013	0.024	45.237	0.001	0.001	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.037	-0.003	45.690	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.801	0.893	46.790	-0.045	-0.045	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.744	-0.861	43.707	0.064	0.064	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.055	-0.003	41.666	0.002	0.002	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.963	0.973	42.568	-0.042	-0.042	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.020	-0.001	44.084	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.040	-0.028	39.004	0.000	0.000	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.006	-0.028	39.952	0.001	0.001	0.000	0.000	0.000	0.000
112	A	112	GLN	0	-0.076	-0.002	41.373	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.052	-0.018	39.067	0.000	0.000	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.020	0.011	36.611	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	115	TYR	0	0.004	-0.036	34.588	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	GLN	0	0.040	0.069	35.462	0.006	0.006	0.000	0.000	0.000	0.000
117	A	117	THR	0	-0.048	-0.039	31.754	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.882	0.945	26.742	-0.065	-0.065	0.000	0.000	0.000	0.000
119	A	119	HIS	0	-0.015	-0.017	26.347	0.008	0.008	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.072	0.047	29.293	0.010	0.010	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.051	-0.033	32.286	-0.006	-0.006	0.000	0.000	0.000	0.000
122	A	122	PRO	0	-0.001	-0.003	31.535	0.008	0.008	0.000	0.000	0.000	0.000
123	A	123	GLY	0	0.077	0.038	31.475	0.009	0.009	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.859	0.929	31.600	-0.120	-0.120	0.000	0.000	0.000	0.000
125	A	125	TYR	0	-0.025	0.005	35.603	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	126	LEU	0	0.038	0.013	34.103	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.013	-0.027	36.373	0.002	0.002	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.974	0.999	38.273	-0.084	-0.084	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.827	0.915	40.511	-0.070	-0.070	0.000	0.000	0.000	0.000
130	A	130	LEU	0	0.098	0.015	39.289	0.003	0.003	0.000	0.000	0.000	0.000
131	A	131	GLN	0	-0.016	0.018	42.282	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.047	-0.037	44.029	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	133	ASN	0	-0.087	-0.059	45.629	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	134	GLY	0	0.014	0.031	47.402	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.012	0.004	43.471	0.002	0.002	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.782	0.854	41.870	-0.085	-0.085	0.000	0.000	0.000	0.000
137	A	137	ALA	0	-0.031	0.011	37.407	0.000	0.000	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.007	-0.008	38.274	0.004	0.004	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.011	-0.006	33.513	0.005	0.005	0.000	0.000	0.000	0.000
140	A	140	ASP	-1	-0.716	-0.853	35.419	0.117	0.117	0.000	0.000	0.000	0.000
141	A	141	THR	0	0.001	-0.027	34.067	0.006	0.006	0.000	0.000	0.000	0.000
142	A	142	HIS	0	-0.100	-0.031	34.581	0.012	0.012	0.000	0.000	0.000	0.000
143	A	143	GLY	0	-0.003	0.010	36.587	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	144	PRO	0	-0.016	-0.010	35.947	0.007	0.007	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.034	0.014	33.512	0.001	0.001	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.002	0.032	28.298	0.006	0.006	0.000	0.000	0.000	0.000
147	A	147	ILE	0	-0.036	-0.017	27.365	-0.005	-0.005	0.000	0.000	0.000	0.000
148	A	148	GLN	0	-0.014	-0.025	24.717	0.004	0.004	0.000	0.000	0.000	0.000
149	A	149	TYR	0	-0.019	0.000	17.948	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	150	PHE	0	0.052	0.012	17.728	0.016	0.016	0.000	0.000	0.000	0.000
151	A	151	SER	0	-0.026	-0.028	14.403	0.025	0.025	0.000	0.000	0.000	0.000
152	A	152	VAL	0	0.000	-0.002	13.214	0.087	0.087	0.000	0.000	0.000	0.000
153	A	153	LYS	1	0.890	0.944	15.426	-0.661	-0.661	0.000	0.000	0.000	0.000
154	A	154	GLU	-1	-0.862	-0.927	16.209	0.492	0.492	0.000	0.000	0.000	0.000
155	A	155	SER	0	0.016	-0.008	18.645	-0.050	-0.050	0.000	0.000	0.000	0.000
156	A	156	TRP	0	-0.080	-0.054	18.743	-0.005	-0.005	0.000	0.000	0.000	0.000
157	A	157	ILE	0	0.011	0.016	20.605	-0.026	-0.026	0.000	0.000	0.000	0.000
158	A	158	ARG	1	0.927	0.932	23.121	-0.201	-0.201	0.000	0.000	0.000	0.000
159	A	159	HIS	0	-0.010	-0.022	25.970	-0.028	-0.028	0.000	0.000	0.000	0.000
160	A	160	LEU	0	-0.021	0.001	28.220	0.011	0.011	0.000	0.000	0.000	0.000
161	A	161	LYS	1	0.879	0.968	27.434	-0.194	-0.194	0.000	0.000	0.000	0.000
162	A	162	LEU	0	-0.002	-0.016	32.231	0.006	0.006	0.000	0.000	0.000	0.000
163	A	163	VAL	0	-0.061	-0.052	32.433	0.006	0.006	0.000	0.000	0.000	0.000
164	A	164	GLU	-1	-0.884	-0.950	32.313	0.118	0.118	0.000	0.000	0.000	0.000
165	A	165	GLU	-1	-0.841	-0.873	32.527	0.108	0.108	0.000	0.000	0.000	0.000
166	A	166	PRO	0	0.018	0.005	29.030	0.011	0.011	0.000	0.000	0.000	0.000
167	A	167	SER	0	-0.025	-0.025	24.535	-0.011	-0.011	0.000	0.000	0.000	0.000
168	A	168	LEU	0	0.047	0.046	25.048	-0.006	-0.006	0.000	0.000	0.000	0.000
169	A	169	PRO	0	0.019	-0.005	21.226	0.028	0.028	0.000	0.000	0.000	0.000
170	A	170	GLY	0	-0.001	-0.004	18.268	-0.005	-0.005	0.000	0.000	0.000	0.000
171	A	171	PHE	0	-0.031	-0.026	19.132	0.018	0.018	0.000	0.000	0.000	0.000
172	A	172	GLU	-1	-0.934	-0.963	18.490	0.405	0.405	0.000	0.000	0.000	0.000
173	A	173	ASP	-1	-0.853	-0.928	21.946	0.214	0.214	0.000	0.000	0.000	0.000
174	A	174	LEU	0	-0.058	-0.035	23.276	0.020	0.020	0.000	0.000	0.000	0.000
175	A	175	LEU	0	-0.026	-0.025	25.066	0.001	0.001	0.000	0.000	0.000	0.000
176	A	176	ARG	1	0.922	0.986	28.752	-0.162	-0.162	0.000	0.000	0.000	0.000
177	A	177	ILE	0	-0.032	-0.024	32.263	-0.001	-0.001	0.000	0.000	0.000	0.000
178	A	178	ARG	1	0.792	0.847	35.316	-0.108	-0.108	0.000	0.000	0.000	0.000
179	A	179	VAL	0	-0.034	-0.028	38.902	0.002	0.002	0.000	0.000	0.000	0.000
180	A	180	GLU	-1	-0.791	-0.868	41.126	0.088	0.088	0.000	0.000	0.000	0.000
181	A	181	PRO	0	0.072	0.020	44.642	0.000	0.000	0.000	0.000	0.000	0.000
182	A	182	ASN	0	-0.047	-0.013	45.423	0.003	0.003	0.000	0.000	0.000	0.000
183	A	183	THR	0	0.020	-0.014	47.165	-0.002	-0.002	0.000	0.000	0.000	0.000
184	A	184	SER	0	-0.025	-0.008	49.667	-0.004	-0.004	0.000	0.000	0.000	0.000
185	A	185	PRO	0	0.018	0.011	48.948	0.003	0.003	0.000	0.000	0.000	0.000
186	A	186	LEU	0	0.013	0.003	42.381	0.001	0.001	0.000	0.000	0.000	0.000
187	A	187	ALA	0	0.041	0.024	45.827	-0.002	-0.002	0.000	0.000	0.000	0.000
188	A	188	GLY	0	0.039	0.037	45.057	0.003	0.003	0.000	0.000	0.000	0.000
189	A	189	LYS	1	0.894	0.918	43.381	-0.094	-0.094	0.000	0.000	0.000	0.000
190	A	190	ASP	-1	-0.827	-0.911	39.707	0.113	0.113	0.000	0.000	0.000	0.000
191	A	191	GLU	-1	-0.761	-0.833	38.527	0.118	0.118	0.000	0.000	0.000	0.000
192	A	192	LYS	1	0.789	0.873	36.444	-0.128	-0.128	0.000	0.000	0.000	0.000
193	A	193	ILE	0	0.049	0.044	37.624	0.003	0.003	0.000	0.000	0.000	0.000
194	A	194	PHE	0	0.020	0.008	30.196	0.007	0.007	0.000	0.000	0.000	0.000
195	A	195	ARG	1	0.956	0.993	32.403	-0.152	-0.152	0.000	0.000	0.000	0.000
196	A	196	PHE	0	0.062	0.023	31.827	0.012	0.012	0.000	0.000	0.000	0.000
197	A	197	GLY	0	0.018	0.034	29.082	0.006	0.006	0.000	0.000	0.000	0.000
198	A	198	SER	0	-0.009	-0.019	29.578	-0.015	-0.015	0.000	0.000	0.000	0.000
199	A	199	HIS	0	-0.010	-0.028	26.889	0.007	0.007	0.000	0.000	0.000	0.000
200	A	200	LYS	1	0.886	0.973	22.337	-0.239	-0.239	0.000	0.000	0.000	0.000
201	A	201	TRP	0	-0.013	0.002	26.996	-0.019	-0.019	0.000	0.000	0.000	0.000
202	A	202	TYR	0	0.017	0.001	27.883	0.007	0.007	0.000	0.000	0.000	0.000

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