FMO DATABASE

FMODB ID: Z6QQN

Calculation Name: 3VOE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3VOE

Chain ID: A

ChEMBL ID:

UniProt ID: P27245

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	136
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1096379.314166
FMO2-HF: Nuclear repulsion	1042536.18646
FMO2-HF: Total energy	-53843.127706
FMO2-MP2: Total energy	-53996.899413

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:9:ASN)

Summations of interaction energy for fragment #1(A:9:ASN)

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.
4.026	5.449	-0.019	-0.717	-0.688	0.001

Interaction energy analysis for fragmet #1(A:9:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.042 / q_NPA : -0.037

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	11	ILE	0	-0.008	0.012	3.872	2.572	3.995	-0.019	-0.717	-0.688	0.001
4	A	12	ILE	0	-0.033	-0.019	6.260	0.128	0.128	0.000	0.000	0.000	0.000
5	A	13	PRO	0	-0.002	-0.009	8.741	0.202	0.202	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.088	0.039	12.047	0.120	0.120	0.000	0.000	0.000	0.000
7	A	15	GLY	0	0.034	0.020	13.399	0.065	0.065	0.000	0.000	0.000	0.000
8	A	16	ARG	1	0.941	0.966	12.520	0.285	0.285	0.000	0.000	0.000	0.000
9	A	17	LEU	0	0.051	0.028	8.214	0.025	0.025	0.000	0.000	0.000	0.000
10	A	18	ILE	0	0.046	0.021	12.287	0.037	0.037	0.000	0.000	0.000	0.000
11	A	19	HIS	0	0.002	0.011	15.962	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	20	MET	0	-0.006	-0.012	8.939	-0.069	-0.069	0.000	0.000	0.000	0.000
13	A	21	VAL	0	0.041	0.026	12.943	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	22	ASN	0	-0.011	0.000	15.269	-0.044	-0.044	0.000	0.000	0.000	0.000
15	A	23	GLN	0	0.006	-0.001	17.081	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	24	LYS	1	0.812	0.901	14.602	-0.699	-0.699	0.000	0.000	0.000	0.000
17	A	25	LYS	1	0.874	0.946	17.605	-0.358	-0.358	0.000	0.000	0.000	0.000
18	A	26	ASP	-1	-0.795	-0.908	20.328	0.221	0.221	0.000	0.000	0.000	0.000
19	A	27	ARG	1	0.871	0.947	15.988	-0.359	-0.359	0.000	0.000	0.000	0.000
20	A	28	LEU	0	0.077	0.036	18.733	-0.015	-0.015	0.000	0.000	0.000	0.000
21	A	29	LEU	0	-0.019	-0.001	22.675	-0.021	-0.021	0.000	0.000	0.000	0.000
22	A	30	ASN	0	-0.023	-0.036	25.569	-0.034	-0.034	0.000	0.000	0.000	0.000
23	A	31	GLU	-1	-0.923	-0.953	21.995	0.284	0.284	0.000	0.000	0.000	0.000
24	A	32	TYR	0	-0.021	-0.035	23.728	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	33	LEU	0	-0.050	-0.015	28.187	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	34	SER	0	-0.015	-0.018	29.845	-0.018	-0.018	0.000	0.000	0.000	0.000
27	A	35	PRO	0	-0.045	-0.023	31.016	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	36	LEU	0	-0.018	-0.006	34.188	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	37	ASP	-1	-0.920	-0.939	36.192	0.099	0.099	0.000	0.000	0.000	0.000
30	A	38	ILE	0	-0.080	-0.053	33.797	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	39	THR	0	0.038	0.016	31.818	0.008	0.008	0.000	0.000	0.000	0.000
32	A	40	ALA	0	0.072	0.023	27.993	0.000	0.000	0.000	0.000	0.000	0.000
33	A	41	ALA	0	-0.056	-0.025	29.945	0.001	0.001	0.000	0.000	0.000	0.000
34	A	42	GLN	0	0.061	0.013	32.032	0.000	0.000	0.000	0.000	0.000	0.000
35	A	43	PHE	0	0.071	0.041	29.920	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.892	0.939	26.050	-0.202	-0.202	0.000	0.000	0.000	0.000
37	A	45	VAL	0	-0.008	0.006	32.636	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	46	LEU	0	-0.007	-0.001	36.304	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	47	CYS	0	0.002	-0.003	33.415	0.001	0.001	0.000	0.000	0.000	0.000
40	A	48	SER	0	-0.017	-0.020	34.749	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	49	ILE	0	-0.031	-0.019	36.642	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	50	ARG	1	0.794	0.883	37.984	-0.143	-0.143	0.000	0.000	0.000	0.000
43	A	51	CYS	0	-0.082	-0.037	36.099	0.003	0.003	0.000	0.000	0.000	0.000
44	A	52	ALA	0	-0.024	-0.005	38.790	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	53	ALA	0	0.042	0.016	41.599	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	54	CYS	0	-0.064	-0.029	44.458	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.012	0.030	40.329	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	56	THR	0	-0.004	-0.011	44.634	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	57	PRO	0	0.028	0.011	42.974	0.002	0.002	0.000	0.000	0.000	0.000
50	A	58	VAL	0	0.024	0.001	41.846	0.002	0.002	0.000	0.000	0.000	0.000
51	A	59	GLU	-1	-0.884	-0.920	41.738	0.059	0.059	0.000	0.000	0.000	0.000
52	A	60	LEU	0	0.088	0.040	37.805	0.003	0.003	0.000	0.000	0.000	0.000
53	A	61	LYS	1	0.913	0.959	37.348	-0.031	-0.031	0.000	0.000	0.000	0.000
54	A	62	LYS	1	0.846	0.919	36.662	-0.049	-0.049	0.000	0.000	0.000	0.000
55	A	63	VAL	0	0.005	0.005	34.822	0.002	0.002	0.000	0.000	0.000	0.000
56	A	64	LEU	0	0.001	0.000	32.807	0.009	0.009	0.000	0.000	0.000	0.000
57	A	65	SER	0	-0.038	-0.014	31.539	0.000	0.000	0.000	0.000	0.000	0.000
58	A	66	VAL	0	-0.012	0.016	32.354	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	67	ASP	-1	-0.789	-0.913	34.254	0.026	0.026	0.000	0.000	0.000	0.000
60	A	68	LEU	0	0.021	0.009	37.171	0.006	0.006	0.000	0.000	0.000	0.000
61	A	69	GLY	0	0.036	0.029	40.587	0.002	0.002	0.000	0.000	0.000	0.000
62	A	70	ALA	0	-0.049	-0.040	36.760	0.002	0.002	0.000	0.000	0.000	0.000
63	A	71	LEU	0	0.006	0.012	37.675	0.004	0.004	0.000	0.000	0.000	0.000
64	A	72	THR	0	-0.026	-0.024	39.361	0.003	0.003	0.000	0.000	0.000	0.000
65	A	73	ARG	1	0.970	0.980	40.525	-0.030	-0.030	0.000	0.000	0.000	0.000
66	A	74	MET	0	-0.054	-0.014	34.934	0.004	0.004	0.000	0.000	0.000	0.000
67	A	75	LEU	0	0.015	0.005	40.151	0.004	0.004	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.769	-0.869	42.609	0.051	0.051	0.000	0.000	0.000	0.000
69	A	77	ARG	1	0.934	0.971	40.299	-0.059	-0.059	0.000	0.000	0.000	0.000
70	A	78	LEU	0	0.014	0.007	38.640	0.003	0.003	0.000	0.000	0.000	0.000
71	A	79	VAL	0	-0.014	0.002	42.818	0.002	0.002	0.000	0.000	0.000	0.000
72	A	80	CYS	0	-0.074	-0.041	45.640	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	81	LYS	1	0.852	0.948	39.969	-0.098	-0.098	0.000	0.000	0.000	0.000
74	A	82	GLY	0	0.036	0.037	45.011	0.003	0.003	0.000	0.000	0.000	0.000
75	A	83	TRP	0	-0.038	-0.039	38.665	0.005	0.005	0.000	0.000	0.000	0.000
76	A	84	VAL	0	0.011	-0.004	42.059	0.004	0.004	0.000	0.000	0.000	0.000
77	A	85	GLU	-1	-0.777	-0.866	45.138	0.067	0.067	0.000	0.000	0.000	0.000
78	A	86	ARG	1	0.843	0.885	46.984	-0.048	-0.048	0.000	0.000	0.000	0.000
79	A	87	LEU	0	0.044	0.029	50.043	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	88	PRO	0	0.034	0.001	52.086	0.000	0.000	0.000	0.000	0.000	0.000
81	A	89	ASN	0	0.025	0.020	50.235	0.001	0.001	0.000	0.000	0.000	0.000
82	A	90	PRO	0	0.045	0.023	53.492	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	91	ASN	0	0.010	-0.004	52.777	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	92	ASP	-1	-0.848	-0.911	52.895	0.029	0.029	0.000	0.000	0.000	0.000
85	A	93	LYS	1	0.853	0.923	55.493	-0.035	-0.035	0.000	0.000	0.000	0.000
86	A	94	ARG	1	0.894	0.942	52.811	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	95	GLY	0	0.016	0.027	51.273	0.000	0.000	0.000	0.000	0.000	0.000
88	A	96	VAL	0	-0.062	-0.042	48.451	0.000	0.000	0.000	0.000	0.000	0.000
89	A	97	LEU	0	-0.009	-0.010	47.885	0.000	0.000	0.000	0.000	0.000	0.000
90	A	98	VAL	0	-0.022	-0.014	43.477	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	99	LYS	1	0.904	0.937	45.137	-0.072	-0.072	0.000	0.000	0.000	0.000
92	A	100	LEU	0	0.004	0.008	40.390	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	101	THR	0	-0.007	-0.007	44.815	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	102	THR	0	0.007	-0.015	45.628	0.004	0.004	0.000	0.000	0.000	0.000
95	A	103	GLY	0	0.048	0.032	45.543	0.005	0.005	0.000	0.000	0.000	0.000
96	A	104	GLY	0	0.061	0.024	42.252	0.005	0.005	0.000	0.000	0.000	0.000
97	A	105	ALA	0	-0.040	-0.019	40.963	0.007	0.007	0.000	0.000	0.000	0.000
98	A	106	ALA	0	0.039	0.018	40.883	0.008	0.008	0.000	0.000	0.000	0.000
99	A	107	ILE	0	0.032	0.018	38.588	0.009	0.009	0.000	0.000	0.000	0.000
100	A	108	CYS	0	-0.048	-0.015	36.070	0.010	0.010	0.000	0.000	0.000	0.000
101	A	109	GLU	-1	-0.797	-0.886	35.863	0.156	0.156	0.000	0.000	0.000	0.000
102	A	110	GLN	0	0.026	0.016	36.061	0.006	0.006	0.000	0.000	0.000	0.000
103	A	111	CYS	0	-0.042	-0.019	33.301	0.009	0.009	0.000	0.000	0.000	0.000
104	A	112	HIS	0	-0.008	-0.014	31.253	0.008	0.008	0.000	0.000	0.000	0.000
105	A	113	GLN	0	-0.049	-0.027	31.465	0.017	0.017	0.000	0.000	0.000	0.000
106	A	114	LEU	0	-0.023	-0.004	31.534	0.014	0.014	0.000	0.000	0.000	0.000
107	A	115	VAL	0	-0.006	-0.006	26.890	0.014	0.014	0.000	0.000	0.000	0.000
108	A	116	GLY	0	-0.009	0.000	27.001	0.026	0.026	0.000	0.000	0.000	0.000
109	A	117	GLN	0	-0.036	-0.023	26.816	0.020	0.020	0.000	0.000	0.000	0.000
110	A	118	ASP	-1	-0.778	-0.883	25.274	0.342	0.342	0.000	0.000	0.000	0.000
111	A	119	LEU	0	-0.029	-0.006	21.966	0.036	0.036	0.000	0.000	0.000	0.000
112	A	120	HIS	0	-0.012	-0.006	21.340	0.054	0.054	0.000	0.000	0.000	0.000
113	A	121	GLN	0	0.022	0.031	20.708	0.059	0.059	0.000	0.000	0.000	0.000
114	A	122	GLU	-1	-0.720	-0.834	17.536	0.627	0.627	0.000	0.000	0.000	0.000
115	A	123	LEU	0	-0.105	-0.063	16.874	0.064	0.064	0.000	0.000	0.000	0.000
116	A	124	THR	0	-0.044	-0.043	15.858	0.102	0.102	0.000	0.000	0.000	0.000
117	A	125	LYS	1	0.840	0.916	15.946	-0.545	-0.545	0.000	0.000	0.000	0.000
118	A	126	ASN	0	-0.057	-0.030	10.748	-0.132	-0.132	0.000	0.000	0.000	0.000
119	A	127	LEU	0	-0.016	0.002	12.976	0.192	0.192	0.000	0.000	0.000	0.000
120	A	128	THR	0	-0.002	-0.009	15.206	-0.167	-0.167	0.000	0.000	0.000	0.000
121	A	129	ALA	0	0.017	-0.009	18.121	0.004	0.004	0.000	0.000	0.000	0.000
122	A	130	ASP	-1	-0.886	-0.939	19.513	0.654	0.654	0.000	0.000	0.000	0.000
123	A	131	GLU	-1	-0.813	-0.881	13.139	1.477	1.477	0.000	0.000	0.000	0.000
124	A	132	VAL	0	-0.013	-0.006	16.783	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	133	ALA	0	0.016	0.013	18.567	-0.042	-0.042	0.000	0.000	0.000	0.000
126	A	134	THR	0	0.000	-0.008	16.663	-0.067	-0.067	0.000	0.000	0.000	0.000
127	A	135	LEU	0	-0.012	-0.007	14.123	-0.050	-0.050	0.000	0.000	0.000	0.000
128	A	136	GLU	-1	-0.823	-0.924	17.080	0.366	0.366	0.000	0.000	0.000	0.000
129	A	137	TYR	0	-0.037	-0.012	20.633	-0.080	-0.080	0.000	0.000	0.000	0.000
130	A	138	LEU	0	-0.022	-0.023	15.535	-0.059	-0.059	0.000	0.000	0.000	0.000
131	A	139	LEU	0	-0.003	-0.009	16.753	-0.057	-0.057	0.000	0.000	0.000	0.000
132	A	140	LYS	1	0.867	0.924	19.775	-0.430	-0.430	0.000	0.000	0.000	0.000
133	A	141	LYS	1	0.895	0.952	21.466	-0.349	-0.349	0.000	0.000	0.000	0.000
134	A	142	VAL	0	-0.058	-0.023	18.855	-0.029	-0.029	0.000	0.000	0.000	0.000
135	A	143	LEU	0	-0.034	-0.003	22.233	-0.024	-0.024	0.000	0.000	0.000	0.000
136	A	144	PRO	0	-0.032	0.002	25.639	-0.024	-0.024	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ASN)