FMO DATABASE

FMODB ID: LJLQ9

Calculation Name: 4MVE-A-Xray322

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4MVE

Chain ID: A

ChEMBL ID:

UniProt ID: D1A7M7

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:

Apendix: None

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1468350.452944
FMO2-HF: Nuclear repulsion	1408107.531213
FMO2-HF: Total energy	-60242.921731
FMO2-MP2: Total energy	-60414.646352

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:0:ACE )

Summations of interaction energy for fragment #1(A:0:ACE )

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.
0.991	4.176	2.703	-3.199	-2.688	-0.026

Interaction energy analysis for fragmet #1(A:0:ACE )

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 : 0.015

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	2	ASP	-1	-0.820	-0.906	3.836	0.331	1.217	-0.005	-0.369	-0.511	0.000
4	A	3	ALA	0	0.024	0.011	4.921	0.209	0.209	0.000	0.000	0.000	0.000
5	A	4	GLU	-1	-0.805	-0.902	2.582	-1.452	0.687	2.708	-2.819	-2.029	-0.026
6	A	5	GLN	0	-0.030	-0.020	6.165	0.284	0.284	0.000	0.000	0.000	0.000
7	A	6	ARG	1	0.900	0.943	8.661	0.429	0.429	0.000	0.000	0.000	0.000
8	A	7	LEU	0	0.015	0.011	8.833	0.078	0.078	0.000	0.000	0.000	0.000
9	A	8	ALA	0	0.014	0.007	10.145	0.050	0.050	0.000	0.000	0.000	0.000
10	A	9	LYS	1	0.903	0.949	11.826	0.370	0.370	0.000	0.000	0.000	0.000
11	A	10	ILE	0	0.027	0.026	13.655	0.026	0.026	0.000	0.000	0.000	0.000
12	A	11	ILE	0	-0.003	-0.007	12.519	0.023	0.023	0.000	0.000	0.000	0.000
13	A	12	ALA	0	-0.056	-0.031	15.881	0.014	0.014	0.000	0.000	0.000	0.000
14	A	13	SER	0	-0.061	-0.024	17.680	0.010	0.010	0.000	0.000	0.000	0.000
15	A	14	GLY	0	0.011	0.021	19.570	0.012	0.012	0.000	0.000	0.000	0.000
16	A	15	ASP	-1	-0.898	-0.953	19.623	-0.086	-0.086	0.000	0.000	0.000	0.000
17	A	16	GLU	-1	-0.920	-0.954	20.252	-0.016	-0.016	0.000	0.000	0.000	0.000
18	A	17	CYS	0	-0.087	-0.055	15.702	-0.012	-0.012	0.000	0.000	0.000	0.000
19	A	18	ASP	-1	-0.821	-0.878	19.408	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	19	ARG	1	0.936	0.954	18.518	-0.073	-0.073	0.000	0.000	0.000	0.000
21	A	20	ALA	0	-0.012	-0.004	17.742	0.015	0.015	0.000	0.000	0.000	0.000
22	A	21	THR	0	0.048	0.000	14.888	0.010	0.010	0.000	0.000	0.000	0.000
23	A	22	VAL	0	-0.034	-0.022	13.770	0.001	0.001	0.000	0.000	0.000	0.000
24	A	23	GLU	-1	-0.792	-0.852	12.847	0.155	0.155	0.000	0.000	0.000	0.000
25	A	24	GLU	-1	-0.921	-0.957	12.487	0.075	0.075	0.000	0.000	0.000	0.000
26	A	25	LEU	0	-0.086	-0.045	8.801	0.035	0.035	0.000	0.000	0.000	0.000
27	A	26	TYR	0	-0.025	-0.046	8.245	0.133	0.133	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.867	-0.939	9.462	0.404	0.404	0.000	0.000	0.000	0.000
29	A	28	ARG	1	0.777	0.888	5.280	0.066	0.066	0.000	0.000	0.000	0.000
30	A	29	LEU	0	-0.052	-0.005	4.776	0.517	0.677	0.000	-0.011	-0.148	0.000
31	A	30	ALA	0	0.010	0.004	5.346	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	31	PRO	0	0.015	-0.002	7.014	-0.249	-0.249	0.000	0.000	0.000	0.000
33	A	32	VAL	0	-0.040	-0.019	10.080	0.035	0.035	0.000	0.000	0.000	0.000
34	A	33	PRO	0	0.035	0.019	12.424	-0.023	-0.023	0.000	0.000	0.000	0.000
35	A	34	VAL	0	0.028	-0.015	15.791	-0.016	-0.016	0.000	0.000	0.000	0.000
36	A	35	ASP	-1	-0.870	-0.946	19.009	0.086	0.086	0.000	0.000	0.000	0.000
37	A	36	PHE	0	-0.058	-0.016	11.670	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	37	MET	0	0.023	0.004	16.325	-0.010	-0.010	0.000	0.000	0.000	0.000
39	A	38	LEU	0	-0.058	0.008	18.306	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	39	GLY	0	0.033	0.018	20.926	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	40	THR	0	-0.008	-0.010	22.926	0.009	0.009	0.000	0.000	0.000	0.000
42	A	41	TRP	0	-0.016	-0.017	14.783	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	42	ARG	1	0.965	0.991	21.120	0.053	0.053	0.000	0.000	0.000	0.000
44	A	43	GLY	0	-0.027	-0.032	20.404	0.000	0.000	0.000	0.000	0.000	0.000
45	A	44	GLY	0	0.006	0.007	20.775	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	45	ILE	0	-0.031	-0.020	20.709	0.010	0.010	0.000	0.000	0.000	0.000
47	A	46	PHE	0	-0.009	-0.008	14.653	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	47	ASP	-1	-0.848	-0.915	20.429	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	48	ARG	1	0.816	0.892	23.131	0.040	0.040	0.000	0.000	0.000	0.000
50	A	49	GLY	0	0.003	0.014	26.783	0.000	0.000	0.000	0.000	0.000	0.000
51	A	50	ASP	-1	-0.839	-0.922	26.724	0.030	0.030	0.000	0.000	0.000	0.000
52	A	51	ALA	0	0.009	0.000	28.676	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	52	LEU	0	-0.015	-0.011	27.026	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	53	ALA	0	0.037	0.025	26.502	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	54	GLY	0	0.044	0.020	28.122	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	55	MET	0	-0.064	-0.037	31.654	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	56	LEU	0	-0.030	-0.016	26.200	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	57	LEU	0	-0.002	-0.006	27.300	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	58	GLY	0	-0.010	0.009	30.821	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	59	MET	0	-0.076	-0.044	32.725	0.000	0.000	0.000	0.000	0.000	0.000
61	A	60	ASN	0	-0.047	-0.017	31.784	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	61	TRP	0	-0.009	-0.014	22.272	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	62	TYR	0	-0.101	-0.084	25.617	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	63	GLY	0	0.062	0.012	24.264	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.816	0.939	21.655	-0.045	-0.045	0.000	0.000	0.000	0.000
66	A	65	ARG	1	0.900	0.942	24.151	-0.026	-0.026	0.000	0.000	0.000	0.000
67	A	66	PHE	0	-0.019	0.000	20.723	0.007	0.007	0.000	0.000	0.000	0.000
68	A	67	ILE	0	-0.023	-0.013	24.458	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	68	ASP	-1	-0.763	-0.885	26.016	0.052	0.052	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.942	0.961	24.356	-0.092	-0.092	0.000	0.000	0.000	0.000
71	A	70	ASP	-1	-0.900	-0.959	25.626	0.074	0.074	0.000	0.000	0.000	0.000
72	A	71	HIS	0	-0.053	-0.017	28.421	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	72	VAL	0	0.009	0.002	24.569	0.000	0.000	0.000	0.000	0.000	0.000
74	A	73	GLU	-1	-0.780	-0.887	27.427	0.021	0.021	0.000	0.000	0.000	0.000
75	A	74	PRO	0	-0.009	-0.010	26.122	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	75	LEU	0	-0.007	-0.013	26.589	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	76	LEU	0	0.030	0.034	26.908	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	77	CYS	0	-0.023	0.004	29.103	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	78	ARG	1	0.921	0.966	29.062	0.016	0.016	0.000	0.000	0.000	0.000
80	A	79	SER	0	0.017	0.016	33.413	0.001	0.001	0.000	0.000	0.000	0.000
81	A	80	PRO	0	-0.014	-0.030	37.131	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	81	ASP	-1	-0.865	-0.897	38.960	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	82	GLY	0	-0.006	0.004	35.747	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	83	SER	0	-0.068	-0.050	34.487	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	84	ILE	0	-0.011	-0.015	29.148	0.000	0.000	0.000	0.000	0.000	0.000
86	A	85	TYR	0	-0.018	-0.005	33.032	0.001	0.001	0.000	0.000	0.000	0.000
87	A	86	SER	0	0.027	0.007	32.181	0.001	0.001	0.000	0.000	0.000	0.000
88	A	87	TYR	0	-0.004	-0.001	32.704	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	88	GLU	-1	-0.798	-0.918	33.249	0.027	0.027	0.000	0.000	0.000	0.000
90	A	89	LYS	1	0.890	0.958	35.480	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	90	LEU	0	-0.026	-0.020	32.065	0.000	0.000	0.000	0.000	0.000	0.000
92	A	91	GLY	0	-0.024	-0.006	33.848	0.004	0.004	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.021	0.017	31.453	0.000	0.000	0.000	0.000	0.000	0.000
94	A	93	ALA	0	0.006	-0.001	26.840	0.003	0.003	0.000	0.000	0.000	0.000
95	A	94	ARG	1	0.883	0.970	26.881	-0.072	-0.072	0.000	0.000	0.000	0.000
96	A	95	LEU	0	-0.009	0.002	20.268	0.006	0.006	0.000	0.000	0.000	0.000
97	A	96	ARG	1	0.764	0.873	22.395	-0.094	-0.094	0.000	0.000	0.000	0.000
98	A	97	GLU	-1	-0.916	-0.951	18.429	0.212	0.212	0.000	0.000	0.000	0.000
99	A	98	VAL	0	-0.028	-0.017	19.370	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	99	ALA	0	-0.005	-0.005	18.292	0.025	0.025	0.000	0.000	0.000	0.000
101	A	100	LEU	0	0.046	0.015	16.002	-0.024	-0.024	0.000	0.000	0.000	0.000
102	A	101	ARG	1	0.798	0.879	14.975	-0.158	-0.158	0.000	0.000	0.000	0.000
103	A	102	GLY	0	0.001	0.004	15.762	0.029	0.029	0.000	0.000	0.000	0.000
104	A	103	THR	0	-0.024	-0.005	11.590	0.055	0.055	0.000	0.000	0.000	0.000
105	A	104	VAL	0	-0.021	-0.002	14.786	-0.038	-0.038	0.000	0.000	0.000	0.000
106	A	105	SER	0	0.026	-0.013	13.495	0.064	0.064	0.000	0.000	0.000	0.000
107	A	106	ALA	0	-0.006	0.020	15.332	-0.039	-0.039	0.000	0.000	0.000	0.000
108	A	107	ALA	0	0.030	0.007	16.918	0.009	0.009	0.000	0.000	0.000	0.000
109	A	108	MET	0	-0.027	0.000	19.650	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	109	ILE	0	-0.031	-0.017	22.524	0.001	0.001	0.000	0.000	0.000	0.000
111	A	110	TYR	0	0.045	0.009	25.787	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	111	ASP	-1	-0.882	-0.950	28.825	0.056	0.056	0.000	0.000	0.000	0.000
113	A	112	LYS	1	0.855	0.918	31.970	-0.040	-0.040	0.000	0.000	0.000	0.000
114	A	113	GLN	0	-0.003	-0.001	30.749	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	114	PRO	0	-0.051	-0.005	30.524	0.004	0.004	0.000	0.000	0.000	0.000
116	A	115	ILE	0	0.022	-0.004	25.447	0.001	0.001	0.000	0.000	0.000	0.000
117	A	116	ILE	0	-0.006	0.000	21.565	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	117	ASP	-1	-0.839	-0.922	20.042	0.078	0.078	0.000	0.000	0.000	0.000
119	A	118	HIS	0	-0.028	-0.021	16.660	0.022	0.022	0.000	0.000	0.000	0.000
120	A	119	PHE	0	0.046	0.027	14.571	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	120	ARG	1	0.916	1.001	9.428	-0.429	-0.429	0.000	0.000	0.000	0.000
122	A	121	ARG	1	0.905	0.946	5.736	-0.113	-0.113	0.000	0.000	0.000	0.000
123	A	122	VAL	0	-0.004	0.009	7.041	0.108	0.108	0.000	0.000	0.000	0.000
124	A	123	ASN	0	-0.050	-0.062	6.716	-0.147	-0.147	0.000	0.000	0.000	0.000
125	A	124	ASP	-1	-0.810	-0.912	8.834	0.038	0.038	0.000	0.000	0.000	0.000
126	A	125	ASP	-1	-0.865	-0.919	11.841	-0.045	-0.045	0.000	0.000	0.000	0.000
127	A	126	MET	0	-0.029	0.007	11.505	-0.022	-0.022	0.000	0.000	0.000	0.000
128	A	127	VAL	0	0.024	0.017	11.094	0.027	0.027	0.000	0.000	0.000	0.000
129	A	128	VAL	0	0.016	0.013	11.702	-0.038	-0.038	0.000	0.000	0.000	0.000
130	A	129	GLY	0	-0.010	-0.008	13.589	0.041	0.041	0.000	0.000	0.000	0.000
131	A	130	ALA	0	-0.011	-0.006	16.251	-0.016	-0.016	0.000	0.000	0.000	0.000
132	A	131	MET	0	-0.010	-0.004	17.982	0.003	0.003	0.000	0.000	0.000	0.000
133	A	132	ASP	-1	-0.880	-0.948	21.797	0.111	0.111	0.000	0.000	0.000	0.000
134	A	133	ALA	0	0.026	0.012	23.512	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	134	LYS	1	0.969	0.961	27.235	-0.059	-0.059	0.000	0.000	0.000	0.000
136	A	135	GLY	0	-0.062	-0.027	30.093	-0.005	-0.005	0.000	0.000	0.000	0.000
137	A	136	GLN	0	0.003	0.005	26.924	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	137	PRO	0	-0.041	0.003	27.560	0.005	0.005	0.000	0.000	0.000	0.000
139	A	138	ASP	-1	-0.913	-0.963	23.219	0.060	0.060	0.000	0.000	0.000	0.000
140	A	139	ILE	0	-0.029	-0.009	18.458	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	140	LEU	0	0.009	0.011	21.181	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	141	TYR	0	-0.028	-0.042	15.391	0.019	0.019	0.000	0.000	0.000	0.000
143	A	142	PHE	0	-0.034	-0.015	18.197	-0.015	-0.015	0.000	0.000	0.000	0.000
144	A	143	HIS	0	0.025	0.013	15.864	0.009	0.009	0.000	0.000	0.000	0.000
145	A	144	LEU	0	-0.002	-0.005	16.026	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	145	THR	0	-0.036	-0.022	15.732	-0.012	-0.012	0.000	0.000	0.000	0.000
147	A	146	ARG	1	0.816	0.919	14.770	-0.021	-0.021	0.000	0.000	0.000	0.000
148	A	147	GLU	-1	-0.901	-0.935	18.704	-0.026	-0.026	0.000	0.000	0.000	0.000
149	A	148	ARG	0	-0.055	-0.015	17.395	0.041	0.041	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ACE )