FMO DATABASE

FMODB ID: G5Y11

Calculation Name: 2CVB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CVB

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SKQ0

Base Structure: X-ray

Registration Date: 2023-09-22

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	OptAll
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	186
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2152534.117319
FMO2-HF: Nuclear repulsion	2078528.303618
FMO2-HF: Total energy	-74005.813701
FMO2-MP2: Total energy	-74223.736601

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-16.06	-6.724	9.055	-6.648	-11.744	-0.037

Interaction energy analysis for fragmet #1(A:2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : 0.009

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	4	TYR	0	0.011	-0.004	3.891	-0.692	1.443	-0.016	-1.058	-1.061	0.004
4	A	5	PRO	0	0.032	0.031	2.347	-1.347	0.006	1.590	-0.462	-2.481	0.000
5	A	6	GLU	-1	-0.773	-0.854	4.352	-0.173	-0.050	0.000	-0.029	-0.094	0.000
6	A	7	LEU	0	-0.003	0.011	6.818	-0.020	-0.020	0.000	0.000	0.000	0.000
7	A	8	PRO	0	-0.018	0.003	7.388	0.040	0.040	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.058	0.023	9.546	-0.023	-0.023	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.778	-0.866	12.590	0.010	0.010	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.068	-0.034	11.572	-0.017	-0.017	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.033	-0.008	13.713	0.001	0.001	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.016	0.003	15.928	-0.023	-0.023	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.040	-0.003	12.973	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.769	-0.862	17.618	-0.146	-0.146	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.016	0.005	20.503	-0.025	-0.025	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.835	-0.893	22.624	-0.121	-0.121	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.005	0.012	22.813	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.017	0.002	27.251	0.011	0.011	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.723	-0.827	29.533	-0.105	-0.105	0.000	0.000	0.000	0.000
20	A	21	PRO	0	-0.053	-0.043	30.765	0.004	0.004	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.748	0.861	33.442	0.087	0.087	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.021	-0.007	35.673	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	GLY	0	-0.009	0.005	35.626	0.001	0.001	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.770	0.843	27.939	0.139	0.139	0.000	0.000	0.000	0.000
25	A	26	TYR	0	-0.004	0.000	29.337	0.009	0.009	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.898	0.942	25.601	0.133	0.133	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.009	-0.003	21.299	0.010	0.010	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.008	-0.040	24.801	0.011	0.011	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.046	-0.019	26.161	0.002	0.002	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.015	0.001	27.110	0.007	0.007	0.000	0.000	0.000	0.000
31	A	32	HIS	0	0.008	0.012	28.091	0.000	0.000	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.888	-0.936	29.906	-0.058	-0.058	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.006	0.013	28.822	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.039	0.028	24.877	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.018	-0.008	23.155	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.017	0.011	22.652	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	38	VAL	0	0.018	0.015	19.956	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.023	-0.027	20.674	0.000	0.000	0.000	0.000	0.000	0.000
39	A	40	PHE	0	0.042	0.037	17.281	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.030	-0.039	20.669	0.015	0.015	0.000	0.000	0.000	0.000
41	A	42	CYS	0	-0.048	-0.019	23.474	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	43	ASN	0	0.059	0.034	26.034	0.008	0.008	0.000	0.000	0.000	0.000
43	A	44	HIS	0	-0.049	-0.056	24.234	0.009	0.009	0.000	0.000	0.000	0.000
44	A	45	CYS	0	-0.054	0.021	19.694	0.011	0.011	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.036	-0.001	26.904	0.005	0.005	0.000	0.000	0.000	0.000
46	A	47	TYR	0	0.035	-0.005	24.094	0.006	0.006	0.000	0.000	0.000	0.000
47	A	48	VAL	0	0.037	0.034	24.643	0.002	0.002	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.769	0.862	26.980	0.089	0.089	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.011	0.011	29.674	0.004	0.004	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.038	-0.037	26.615	0.004	0.004	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.008	0.005	28.756	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.042	0.022	30.196	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.793	-0.876	28.705	-0.032	-0.032	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.008	-0.007	25.656	0.002	0.002	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.016	0.017	29.401	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	57	ALA	0	0.007	0.008	32.622	0.002	0.002	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.029	-0.012	27.855	0.003	0.003	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.016	0.008	30.873	0.002	0.002	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.850	-0.890	32.136	-0.040	-0.040	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.872	0.932	33.827	0.025	0.025	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.049	-0.069	31.018	0.002	0.002	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.881	0.915	32.844	0.044	0.044	0.000	0.000	0.000	0.000
63	A	64	GLY	0	-0.015	-0.008	34.326	0.004	0.004	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.784	0.891	32.351	0.034	0.034	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.006	-0.003	26.633	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.000	0.025	27.649	0.000	0.000	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.012	-0.008	26.584	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	69	VAL	0	0.005	0.006	24.951	0.000	0.000	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.002	0.012	24.691	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.015	-0.011	20.878	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.006	-0.023	22.995	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.046	0.019	19.965	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.050	-0.031	21.294	-0.041	-0.041	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.787	-0.899	23.339	-0.196	-0.196	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.025	-0.053	25.079	0.016	0.016	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.852	-0.903	28.593	-0.160	-0.160	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.838	0.929	21.900	0.248	0.248	0.000	0.000	0.000	0.000
78	A	79	TYR	0	-0.025	-0.025	24.432	0.003	0.003	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.059	0.029	28.978	0.001	0.001	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.830	-0.902	30.973	-0.085	-0.085	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.729	-0.829	26.767	-0.136	-0.136	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.030	0.019	29.533	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.068	0.015	30.663	0.007	0.007	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.844	-0.898	32.554	-0.079	-0.079	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.845	0.895	33.462	0.088	0.088	0.000	0.000	0.000	0.000
86	A	87	MET	0	-0.076	0.023	28.448	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.031	0.025	32.645	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.024	0.016	35.832	0.004	0.004	0.000	0.000	0.000	0.000
89	A	90	PHE	0	0.004	-0.006	29.920	0.005	0.005	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.008	-0.006	33.570	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.839	-0.924	34.761	-0.068	-0.068	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.927	-0.954	36.332	-0.060	-0.060	0.000	0.000	0.000	0.000
93	A	94	HIS	1	0.743	0.864	33.666	0.068	0.068	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.040	0.033	35.626	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	ILE	0	-0.018	-0.008	30.726	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	PHE	0	-0.019	-0.016	34.291	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	98	PHE	0	-0.035	-0.001	28.286	0.001	0.001	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.017	0.004	29.595	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	100	TYR	0	-0.023	-0.047	26.750	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.018	0.000	25.569	0.000	0.000	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.004	0.001	26.242	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.790	-0.913	19.475	-0.297	-0.297	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.804	-0.875	22.446	-0.202	-0.202	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.023	-0.055	21.092	0.000	0.000	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.039	-0.014	18.438	-0.071	-0.071	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.850	-0.893	16.849	-0.350	-0.350	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.010	0.007	16.113	-0.036	-0.036	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.001	-0.012	15.895	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.817	0.902	12.521	0.563	0.563	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.017	-0.003	11.384	-0.092	-0.092	0.000	0.000	0.000	0.000
111	A	112	TYR	0	-0.021	-0.050	11.883	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.766	0.884	6.822	0.621	0.621	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.000	0.033	10.584	0.030	0.030	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.024	-0.036	9.592	-0.059	-0.059	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.800	0.899	14.059	0.151	0.151	0.000	0.000	0.000	0.000
116	A	117	THR	0	0.022	0.040	17.283	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	118	PRO	0	-0.038	-0.024	20.861	0.008	0.008	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.762	-0.881	13.757	-0.248	-0.248	0.000	0.000	0.000	0.000
119	A	120	VAL	0	-0.027	-0.003	18.296	-0.010	-0.010	0.000	0.000	0.000	0.000
120	A	121	PHE	0	-0.001	-0.013	12.774	0.005	0.005	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.009	0.008	17.985	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	123	PHE	0	0.016	-0.003	16.403	0.005	0.005	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.717	-0.845	20.755	-0.031	-0.031	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.832	-0.913	23.416	-0.037	-0.037	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.651	0.786	20.176	0.011	0.011	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.737	0.839	21.822	0.063	0.063	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.027	-0.003	17.645	-0.017	-0.017	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.055	-0.020	12.961	0.005	0.005	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.838	0.877	16.084	0.017	0.017	0.000	0.000	0.000	0.000
130	A	131	TYR	0	-0.012	-0.030	17.333	0.018	0.018	0.000	0.000	0.000	0.000
131	A	132	HIS	1	0.818	0.890	11.229	0.143	0.143	0.000	0.000	0.000	0.000
132	A	133	GLY	0	-0.019	-0.006	15.390	0.018	0.018	0.000	0.000	0.000	0.000
133	A	134	ARG	1	0.802	0.910	16.836	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.054	0.039	19.926	0.004	0.004	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.019	-0.028	23.534	0.006	0.006	0.000	0.000	0.000	0.000
136	A	137	ASP	-1	-0.772	-0.905	23.234	-0.012	-0.012	0.000	0.000	0.000	0.000
137	A	138	ASN	0	-0.034	-0.020	24.320	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	139	PRO	0	0.003	0.012	23.006	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.868	0.936	26.301	0.048	0.048	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.776	-0.853	28.460	-0.024	-0.024	0.000	0.000	0.000	0.000
141	A	142	PRO	0	0.069	0.028	31.308	0.005	0.005	0.000	0.000	0.000	0.000
142	A	143	SER	0	-0.104	-0.063	32.572	0.004	0.004	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.819	0.879	31.431	0.020	0.020	0.000	0.000	0.000	0.000
144	A	145	VAL	0	-0.076	0.002	28.142	0.003	0.003	0.000	0.000	0.000	0.000
145	A	146	GLN	0	-0.065	-0.040	28.691	0.004	0.004	0.000	0.000	0.000	0.000
146	A	147	SER	0	-0.069	-0.047	24.803	0.005	0.005	0.000	0.000	0.000	0.000
147	A	148	HIS	1	0.871	0.901	26.905	0.015	0.015	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.759	-0.862	21.679	-0.006	-0.006	0.000	0.000	0.000	0.000
149	A	150	LEU	0	0.015	0.022	22.450	0.002	0.002	0.000	0.000	0.000	0.000
150	A	151	GLU	-1	-0.855	-0.917	24.031	-0.022	-0.022	0.000	0.000	0.000	0.000
151	A	152	ALA	0	-0.008	-0.009	25.354	0.002	0.002	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.009	-0.008	22.205	0.004	0.004	0.000	0.000	0.000	0.000
153	A	154	ILE	0	0.017	0.003	24.120	0.000	0.000	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.836	-0.893	26.645	-0.010	-0.010	0.000	0.000	0.000	0.000
155	A	156	ALA	0	-0.031	0.000	25.446	0.002	0.002	0.000	0.000	0.000	0.000
156	A	157	LEU	0	0.013	0.011	22.305	0.001	0.001	0.000	0.000	0.000	0.000
157	A	158	LEU	0	-0.038	-0.017	26.589	0.000	0.000	0.000	0.000	0.000	0.000
158	A	159	ARG	1	0.760	0.863	29.808	-0.002	-0.002	0.000	0.000	0.000	0.000
159	A	160	GLY	0	-0.034	-0.009	28.080	0.003	0.003	0.000	0.000	0.000	0.000
160	A	161	GLU	-1	-0.907	-0.932	27.267	0.020	0.020	0.000	0.000	0.000	0.000
161	A	162	GLU	-1	-0.818	-0.889	20.657	0.015	0.015	0.000	0.000	0.000	0.000
162	A	163	PRO	0	-0.019	-0.013	20.360	0.002	0.002	0.000	0.000	0.000	0.000
163	A	164	PRO	0	-0.032	-0.023	21.256	0.010	0.010	0.000	0.000	0.000	0.000
164	A	165	LEU	0	0.045	0.025	18.711	0.000	0.000	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.888	0.959	17.147	-0.068	-0.068	0.000	0.000	0.000	0.000
166	A	167	GLH	0	-0.012	-0.042	10.317	-0.013	-0.013	0.000	0.000	0.000	0.000
167	A	168	ALA	0	0.019	0.013	15.611	0.009	0.009	0.000	0.000	0.000	0.000
168	A	169	PRO	0	0.031	0.021	12.922	-0.022	-0.022	0.000	0.000	0.000	0.000
169	A	170	ALA	0	0.029	0.018	15.028	0.011	0.011	0.000	0.000	0.000	0.000
170	A	171	ILE	0	-0.038	-0.007	16.992	-0.003	-0.003	0.000	0.000	0.000	0.000
171	A	172	GLY	0	0.065	0.011	19.479	0.005	0.005	0.000	0.000	0.000	0.000
172	A	174	THR	0	0.013	0.003	16.380	0.003	0.003	0.000	0.000	0.000	0.000
173	A	175	ILE	0	0.045	0.031	16.196	0.021	0.021	0.000	0.000	0.000	0.000
174	A	176	LYS	1	0.792	0.917	18.698	0.159	0.159	0.000	0.000	0.000	0.000
175	A	177	TRP	0	0.049	0.011	14.478	-0.004	-0.004	0.000	0.000	0.000	0.000
176	A	178	ARG	1	0.803	0.868	19.511	0.235	0.235	0.000	0.000	0.000	0.000
177	A	179	PRO	0	-0.044	-0.031	20.411	-0.032	-0.032	0.000	0.000	0.000	0.000
178	A	180	GLY	0	-0.018	0.007	18.799	0.009	0.009	0.000	0.000	0.000	0.000
179	A	181	ASN	0	-0.014	-0.008	17.054	-0.096	-0.096	0.000	0.000	0.000	0.000
180	A	182	GLU	-1	-0.868	-0.933	15.414	-0.396	-0.396	0.000	0.000	0.000	0.000
181	A	183	PRO	0	-0.024	0.011	10.403	-0.080	-0.080	0.000	0.000	0.000	0.000
182	A	184	GLU	-1	-0.845	-0.919	8.267	-1.077	-1.077	0.000	0.000	0.000	0.000
183	A	185	VAL	0	-0.030	-0.010	6.082	-0.537	-0.537	0.000	0.000	0.000	0.000
184	A	186	ARG	1	0.782	0.875	3.558	1.293	1.694	0.009	-0.108	-0.302	0.000
185	A	187	ILE	0	0.038	0.010	2.475	-5.160	-2.860	3.099	-2.384	-3.015	-0.028
186	A	188	GLY	0	0.015	0.022	2.563	-8.030	-5.006	4.373	-2.607	-4.791	-0.013

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)