FMO DATABASE

FMODB ID: 1N6RZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2150524.117187
FMO2-HF: Nuclear repulsion	2076518.546654
FMO2-HF: Total energy	-74005.570533
FMO2-MP2: Total energy	-74223.504758

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.
-15.441	-5.181	7.734	-6.583	-11.41	-0.038

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 : -0.017 / q_NPA : 0.006

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	0.007	-0.004	3.814	-1.288	1.350	-0.029	-1.325	-1.284	0.005
4	A	5	PRO	0	0.031	0.034	2.478	-1.369	0.119	0.842	-0.363	-1.966	0.001
5	A	6	GLU	-1	-0.763	-0.854	4.421	-0.179	-0.066	0.000	-0.025	-0.088	0.000
6	A	7	LEU	0	-0.034	-0.016	6.923	0.019	0.019	0.000	0.000	0.000	0.000
7	A	8	PRO	0	0.005	0.012	7.429	0.032	0.032	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.048	0.022	9.603	-0.022	-0.022	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.793	-0.893	12.798	0.012	0.012	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.064	-0.031	11.619	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.036	-0.003	13.706	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.010	0.012	15.858	-0.023	-0.023	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.037	0.000	13.040	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.763	-0.868	17.698	-0.134	-0.134	0.000	0.000	0.000	0.000
15	A	16	ALA	0	-0.006	-0.011	20.626	-0.023	-0.023	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.854	-0.897	22.818	-0.113	-0.113	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.012	0.002	22.878	-0.010	-0.010	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.000	0.001	27.234	0.011	0.011	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.704	-0.819	29.690	-0.104	-0.104	0.000	0.000	0.000	0.000
20	A	21	PRO	0	-0.047	-0.032	30.973	0.004	0.004	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.767	0.866	33.399	0.088	0.088	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.028	-0.009	35.724	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	GLY	0	-0.023	-0.010	35.769	0.000	0.000	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.798	0.859	28.290	0.129	0.129	0.000	0.000	0.000	0.000
25	A	26	TYR	0	0.014	0.006	29.454	0.008	0.008	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.933	0.971	26.425	0.117	0.117	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.007	-0.007	21.334	0.009	0.009	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.038	-0.056	24.667	0.012	0.012	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.019	0.000	26.043	0.003	0.003	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.027	-0.005	27.124	0.007	0.007	0.000	0.000	0.000	0.000
31	A	32	HIS	0	0.022	0.015	28.304	0.000	0.000	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.915	-0.939	29.843	-0.056	-0.056	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.030	0.017	28.764	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.021	0.019	25.226	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.009	0.005	23.160	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.021	0.009	22.900	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	38	VAL	0	0.018	0.011	20.148	0.000	0.000	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.008	-0.018	20.691	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	40	PHE	0	0.031	0.035	17.497	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.026	-0.044	20.951	0.012	0.012	0.000	0.000	0.000	0.000
41	A	42	CYS	0	-0.053	-0.014	23.749	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	43	ASN	0	0.043	0.028	26.341	0.009	0.009	0.000	0.000	0.000	0.000
43	A	44	HIS	0	-0.053	-0.057	24.701	0.008	0.008	0.000	0.000	0.000	0.000
44	A	45	CYS	0	-0.091	-0.002	19.906	0.007	0.007	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.039	0.001	27.011	0.005	0.005	0.000	0.000	0.000	0.000
46	A	47	TYR	0	0.038	-0.005	24.202	0.006	0.006	0.000	0.000	0.000	0.000
47	A	48	VAL	0	0.040	0.036	24.683	0.004	0.004	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.827	0.914	26.944	0.094	0.094	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.018	0.011	29.636	0.005	0.005	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.002	-0.028	26.751	0.003	0.003	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.002	0.008	29.031	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.019	0.017	30.380	0.002	0.002	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.794	-0.879	28.835	-0.041	-0.041	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.016	-0.005	25.335	0.002	0.002	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.001	0.011	29.569	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	ALA	0	0.007	0.009	32.826	0.003	0.003	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.022	-0.011	28.226	0.003	0.003	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.008	0.009	30.984	0.002	0.002	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.852	-0.893	32.328	-0.042	-0.042	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.893	0.950	34.213	0.030	0.030	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.078	-0.086	31.273	0.002	0.002	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.894	0.931	33.368	0.046	0.046	0.000	0.000	0.000	0.000
63	A	64	GLY	0	-0.034	-0.019	34.607	0.004	0.004	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.838	0.927	32.595	0.034	0.034	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.022	0.002	27.076	0.000	0.000	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.014	0.017	28.185	0.000	0.000	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.013	-0.004	26.705	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	69	VAL	0	0.021	0.009	25.082	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.014	0.008	24.923	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.008	-0.004	21.137	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.008	-0.032	23.114	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.031	0.014	20.220	0.000	0.000	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.031	-0.024	21.991	-0.037	-0.037	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.795	-0.893	23.469	-0.197	-0.197	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.026	-0.059	25.021	0.015	0.015	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.831	-0.878	28.389	-0.158	-0.158	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.902	0.958	23.489	0.207	0.207	0.000	0.000	0.000	0.000
78	A	79	TYR	0	-0.041	-0.032	24.663	0.003	0.003	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.086	0.040	29.227	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.869	-0.942	31.407	-0.092	-0.092	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.754	-0.844	26.777	-0.139	-0.139	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.041	0.020	29.350	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.069	0.014	30.753	0.007	0.007	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.862	-0.916	32.569	-0.078	-0.078	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.861	0.914	33.368	0.089	0.089	0.000	0.000	0.000	0.000
86	A	87	MET	0	-0.049	0.028	28.529	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.010	0.015	32.773	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.048	0.025	35.970	0.004	0.004	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.008	-0.004	30.122	0.004	0.004	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.009	-0.019	33.972	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.892	-0.957	35.164	-0.067	-0.067	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.936	-0.950	36.656	-0.063	-0.063	0.000	0.000	0.000	0.000
93	A	94	HIS	1	0.752	0.864	34.115	0.071	0.071	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.049	0.038	35.979	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	ILE	0	-0.033	-0.015	30.945	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	PHE	0	-0.010	-0.009	34.368	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	98	PHE	0	-0.043	-0.002	28.305	0.001	0.001	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.028	0.012	29.616	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	100	TYR	0	-0.027	-0.038	26.992	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.014	-0.012	25.880	0.002	0.002	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.004	0.009	26.247	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.817	-0.933	19.978	-0.276	-0.276	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.807	-0.882	23.101	-0.193	-0.193	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.012	-0.048	21.447	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.016	-0.001	18.662	-0.068	-0.068	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.860	-0.902	17.075	-0.324	-0.324	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.023	0.018	16.421	-0.030	-0.030	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.007	-0.003	16.212	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.826	0.907	12.977	0.577	0.577	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.023	-0.003	11.711	-0.086	-0.086	0.000	0.000	0.000	0.000
111	A	112	TYR	0	-0.036	-0.052	12.222	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.801	0.899	6.638	0.578	0.578	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.004	0.033	10.737	0.015	0.015	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.018	-0.037	9.728	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.800	0.901	13.825	0.185	0.185	0.000	0.000	0.000	0.000
116	A	117	THR	0	0.006	0.039	17.403	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	118	PRO	0	-0.034	-0.036	20.898	0.007	0.007	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.772	-0.882	13.865	-0.264	-0.264	0.000	0.000	0.000	0.000
119	A	120	VAL	0	-0.022	-0.009	18.582	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	121	PHE	0	0.006	-0.006	13.023	0.004	0.004	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.006	0.004	18.319	0.000	0.000	0.000	0.000	0.000	0.000
122	A	123	PHE	0	0.010	-0.011	16.638	0.002	0.002	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.718	-0.848	21.057	-0.029	-0.029	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.830	-0.923	23.534	-0.036	-0.036	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.653	0.803	20.326	0.010	0.010	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.745	0.847	21.691	0.063	0.063	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.018	0.004	17.603	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.079	-0.030	13.071	0.004	0.004	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.873	0.911	16.550	0.021	0.021	0.000	0.000	0.000	0.000
130	A	131	TYR	0	-0.019	-0.029	17.877	0.014	0.014	0.000	0.000	0.000	0.000
131	A	132	HIS	1	0.811	0.897	11.496	0.167	0.167	0.000	0.000	0.000	0.000
132	A	133	GLY	0	-0.027	-0.009	15.557	0.011	0.011	0.000	0.000	0.000	0.000
133	A	134	ARG	1	0.836	0.937	16.732	0.021	0.021	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.050	0.041	19.856	0.006	0.006	0.000	0.000	0.000	0.000
135	A	136	ASN	0	0.002	-0.022	23.390	0.005	0.005	0.000	0.000	0.000	0.000
136	A	137	ASP	-1	-0.763	-0.892	23.371	-0.025	-0.025	0.000	0.000	0.000	0.000
137	A	138	ASN	0	-0.055	-0.030	24.465	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	139	PRO	0	-0.019	0.006	23.082	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.896	0.949	26.409	0.067	0.067	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.798	-0.866	28.594	-0.032	-0.032	0.000	0.000	0.000	0.000
141	A	142	PRO	0	0.066	0.031	31.160	0.004	0.004	0.000	0.000	0.000	0.000
142	A	143	SER	0	-0.098	-0.066	32.576	0.004	0.004	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.858	0.913	31.315	0.031	0.031	0.000	0.000	0.000	0.000
144	A	145	VAL	0	-0.073	-0.015	28.370	0.002	0.002	0.000	0.000	0.000	0.000
145	A	146	GLN	0	-0.084	-0.042	28.782	0.005	0.005	0.000	0.000	0.000	0.000
146	A	147	SER	0	-0.074	-0.044	24.821	0.006	0.006	0.000	0.000	0.000	0.000
147	A	148	HIS	1	0.868	0.905	26.795	0.025	0.025	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.808	-0.907	21.950	-0.021	-0.021	0.000	0.000	0.000	0.000
149	A	150	LEU	0	0.027	0.024	22.787	0.001	0.001	0.000	0.000	0.000	0.000
150	A	151	GLU	-1	-0.885	-0.945	24.406	-0.026	-0.026	0.000	0.000	0.000	0.000
151	A	152	ALA	0	-0.007	-0.008	25.706	0.003	0.003	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.004	-0.004	22.678	0.004	0.004	0.000	0.000	0.000	0.000
153	A	154	ILE	0	0.016	0.005	24.570	0.001	0.001	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.861	-0.912	27.052	-0.014	-0.014	0.000	0.000	0.000	0.000
155	A	156	ALA	0	-0.031	-0.004	25.790	0.003	0.003	0.000	0.000	0.000	0.000
156	A	157	LEU	0	0.007	0.001	22.690	0.002	0.002	0.000	0.000	0.000	0.000
157	A	158	LEU	0	-0.051	-0.017	26.900	0.001	0.001	0.000	0.000	0.000	0.000
158	A	159	ARG	1	0.784	0.883	30.237	0.004	0.004	0.000	0.000	0.000	0.000
159	A	160	GLY	0	-0.028	0.000	28.585	0.003	0.003	0.000	0.000	0.000	0.000
160	A	161	GLU	-1	-0.908	-0.941	27.496	0.014	0.014	0.000	0.000	0.000	0.000
161	A	162	GLU	-1	-0.861	-0.918	20.960	0.011	0.011	0.000	0.000	0.000	0.000
162	A	163	PRO	0	-0.004	-0.006	21.104	0.001	0.001	0.000	0.000	0.000	0.000
163	A	164	PRO	0	-0.029	-0.023	21.547	0.009	0.009	0.000	0.000	0.000	0.000
164	A	165	LEU	0	0.045	0.022	19.185	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.887	0.959	17.409	-0.044	-0.044	0.000	0.000	0.000	0.000
166	A	167	GLH	0	-0.009	-0.041	10.540	-0.008	-0.008	0.000	0.000	0.000	0.000
167	A	168	ALA	0	0.009	0.009	15.778	0.008	0.008	0.000	0.000	0.000	0.000
168	A	169	PRO	0	0.056	0.023	13.024	-0.017	-0.017	0.000	0.000	0.000	0.000
169	A	170	ALA	0	0.049	0.028	15.113	0.012	0.012	0.000	0.000	0.000	0.000
170	A	171	ILE	0	-0.024	-0.001	16.913	-0.002	-0.002	0.000	0.000	0.000	0.000
171	A	172	GLY	0	0.037	-0.001	19.680	0.004	0.004	0.000	0.000	0.000	0.000
172	A	174	THR	0	0.019	0.010	16.506	0.004	0.004	0.000	0.000	0.000	0.000
173	A	175	ILE	0	0.049	0.033	16.281	0.024	0.024	0.000	0.000	0.000	0.000
174	A	176	LYS	1	0.765	0.893	18.820	0.172	0.172	0.000	0.000	0.000	0.000
175	A	177	TRP	0	0.034	0.000	14.573	-0.003	-0.003	0.000	0.000	0.000	0.000
176	A	178	ARG	1	0.782	0.859	19.528	0.228	0.228	0.000	0.000	0.000	0.000
177	A	179	PRO	0	-0.018	-0.019	20.279	-0.033	-0.033	0.000	0.000	0.000	0.000
178	A	180	GLY	0	-0.012	0.008	18.376	0.009	0.009	0.000	0.000	0.000	0.000
179	A	181	ASN	0	-0.025	-0.024	16.845	-0.086	-0.086	0.000	0.000	0.000	0.000
180	A	182	GLU	-1	-0.904	-0.942	15.044	-0.427	-0.427	0.000	0.000	0.000	0.000
181	A	183	PRO	0	-0.031	0.009	10.232	-0.092	-0.092	0.000	0.000	0.000	0.000
182	A	184	GLU	-1	-0.868	-0.931	8.475	-0.989	-0.989	0.000	0.000	0.000	0.000
183	A	185	VAL	0	-0.037	-0.020	5.884	-0.519	-0.519	0.000	0.000	0.000	0.000
184	A	186	ARG	1	0.806	0.897	3.124	1.153	1.762	0.077	-0.183	-0.502	0.000
185	A	187	ILE	0	0.059	0.015	2.497	-4.855	-2.317	2.600	-2.260	-2.878	-0.028
186	A	188	GLY	0	0.013	0.023	2.440	-7.166	-4.292	4.244	-2.427	-4.692	-0.016

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