FMO DATABASE

FMODB ID: 98GZ2

Calculation Name: 1VJX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VJX

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X1L2

Base Structure: X-ray

Registration Date: 2023-09-21

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	148
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1525064.126416
FMO2-HF: Nuclear repulsion	1463811.834011
FMO2-HF: Total energy	-61252.292405
FMO2-MP2: Total energy	-61433.147208

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:HIS)

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

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.
-250.422	-236.384	23.045	-14.108	-22.972	-0.154

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.916

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	0	HIS	0	-0.041	-0.025	3.334	-2.008	-0.167	0.007	-0.896	-0.951	-0.001
4	A	1	MET	0	0.025	0.037	2.526	-1.764	-0.869	1.012	-0.535	-1.372	-0.002
5	A	2	LYS	1	0.846	0.907	5.281	22.351	22.377	-0.001	-0.002	-0.022	0.000
6	A	3	VAL	0	0.043	0.017	8.562	-2.529	-2.529	0.000	0.000	0.000	0.000
7	A	4	SER	0	0.021	0.015	11.055	-0.290	-0.290	0.000	0.000	0.000	0.000
8	A	5	ASP	-1	-0.886	-0.936	7.328	-28.746	-28.746	0.000	0.000	0.000	0.000
9	A	6	ILE	0	-0.001	-0.008	5.348	-1.969	-1.969	0.000	0.000	0.000	0.000
10	A	7	LEU	0	0.029	0.012	8.962	0.463	0.463	0.000	0.000	0.000	0.000
11	A	8	THR	0	-0.029	-0.009	11.033	1.439	1.439	0.000	0.000	0.000	0.000
12	A	9	VAL	0	-0.039	-0.020	6.039	0.741	0.741	0.000	0.000	0.000	0.000
13	A	10	ALA	0	0.008	-0.006	9.248	0.834	0.834	0.000	0.000	0.000	0.000
14	A	11	ILE	0	-0.047	-0.021	11.583	1.568	1.568	0.000	0.000	0.000	0.000
15	A	12	ARG	1	0.957	0.979	11.030	24.014	24.014	0.000	0.000	0.000	0.000
16	A	13	LEU	0	-0.019	0.008	7.900	1.037	1.037	0.000	0.000	0.000	0.000
17	A	14	GLH	0	-0.038	-0.039	12.080	1.642	1.642	0.000	0.000	0.000	0.000
18	A	15	GLU	-1	-0.835	-0.919	15.659	-16.776	-16.776	0.000	0.000	0.000	0.000
19	A	16	GLU	-1	-0.872	-0.936	13.453	-17.741	-17.741	0.000	0.000	0.000	0.000
20	A	17	GLY	0	0.022	0.017	15.526	0.759	0.759	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.851	-0.929	16.853	-12.451	-12.451	0.000	0.000	0.000	0.000
22	A	19	ARG	1	0.756	0.831	17.373	16.944	16.944	0.000	0.000	0.000	0.000
23	A	20	PHE	0	0.049	0.034	17.612	0.662	0.662	0.000	0.000	0.000	0.000
24	A	21	TYR	0	-0.004	-0.010	17.942	0.859	0.859	0.000	0.000	0.000	0.000
25	A	22	ARG	1	0.846	0.893	22.202	12.746	12.746	0.000	0.000	0.000	0.000
26	A	23	GLU	-1	-0.770	-0.833	21.441	-13.683	-13.683	0.000	0.000	0.000	0.000
27	A	24	LEU	0	-0.013	-0.015	21.064	0.555	0.555	0.000	0.000	0.000	0.000
28	A	25	SER	0	-0.109	-0.054	24.811	0.667	0.667	0.000	0.000	0.000	0.000
29	A	26	GLU	-1	-0.942	-0.972	27.723	-10.486	-10.486	0.000	0.000	0.000	0.000
30	A	27	HIS	1	0.806	0.915	26.504	11.685	11.685	0.000	0.000	0.000	0.000
31	A	28	PHE	0	-0.006	-0.001	26.044	0.241	0.241	0.000	0.000	0.000	0.000
32	A	29	ASN	0	0.035	-0.011	31.204	0.120	0.120	0.000	0.000	0.000	0.000
33	A	30	GLY	0	-0.010	0.007	33.859	0.184	0.184	0.000	0.000	0.000	0.000
34	A	31	GLU	-1	-0.790	-0.894	33.867	-9.056	-9.056	0.000	0.000	0.000	0.000
35	A	32	ILE	0	0.003	0.011	28.856	-0.211	-0.211	0.000	0.000	0.000	0.000
36	A	33	LYS	1	0.877	0.952	29.236	9.312	9.312	0.000	0.000	0.000	0.000
37	A	34	LYS	1	0.872	0.918	29.542	8.790	8.790	0.000	0.000	0.000	0.000
38	A	35	THR	0	-0.003	0.000	26.477	-0.186	-0.186	0.000	0.000	0.000	0.000
39	A	36	PHE	0	-0.023	-0.015	23.276	-0.312	-0.312	0.000	0.000	0.000	0.000
40	A	37	LEU	0	0.022	0.008	25.111	-0.393	-0.393	0.000	0.000	0.000	0.000
41	A	38	GLU	-1	-0.928	-0.961	26.877	-10.408	-10.408	0.000	0.000	0.000	0.000
42	A	39	LEU	0	-0.040	-0.019	22.228	-0.275	-0.275	0.000	0.000	0.000	0.000
43	A	40	ALA	0	0.005	0.005	22.282	-0.579	-0.579	0.000	0.000	0.000	0.000
44	A	41	ASP	-1	-0.784	-0.871	23.041	-11.670	-11.670	0.000	0.000	0.000	0.000
45	A	42	GLN	0	-0.054	-0.048	23.237	0.349	0.349	0.000	0.000	0.000	0.000
46	A	43	GLH	0	-0.051	-0.057	16.906	-0.635	-0.635	0.000	0.000	0.000	0.000
47	A	44	ARG	1	0.802	0.892	19.836	11.330	11.330	0.000	0.000	0.000	0.000
48	A	45	ILE	0	-0.044	-0.024	21.902	-0.252	-0.252	0.000	0.000	0.000	0.000
49	A	46	HIS	0	-0.029	-0.016	18.556	0.696	0.696	0.000	0.000	0.000	0.000
50	A	47	ALA	0	0.051	0.032	17.974	-0.512	-0.512	0.000	0.000	0.000	0.000
51	A	48	GLU	-1	-0.898	-0.948	18.974	-12.539	-12.539	0.000	0.000	0.000	0.000
52	A	49	ILE	0	-0.066	-0.019	20.653	0.323	0.323	0.000	0.000	0.000	0.000
53	A	50	PHE	0	0.030	-0.009	15.232	-0.030	-0.030	0.000	0.000	0.000	0.000
54	A	51	ARG	1	0.880	0.931	18.175	14.941	14.941	0.000	0.000	0.000	0.000
55	A	52	LYS	1	0.918	0.972	19.906	11.857	11.857	0.000	0.000	0.000	0.000
56	A	53	MET	0	-0.009	0.006	18.268	-0.093	-0.093	0.000	0.000	0.000	0.000
57	A	54	SER	0	-0.008	-0.012	16.470	-0.189	-0.189	0.000	0.000	0.000	0.000
58	A	55	ASP	-1	-0.947	-0.955	18.141	-12.855	-12.855	0.000	0.000	0.000	0.000
59	A	56	GLN	0	-0.079	-0.062	21.477	0.651	0.651	0.000	0.000	0.000	0.000
60	A	57	GLU	-1	-0.846	-0.896	18.914	-13.760	-13.760	0.000	0.000	0.000	0.000
61	A	58	ASN	0	-0.062	-0.046	20.901	-0.291	-0.291	0.000	0.000	0.000	0.000
62	A	59	TRP	0	0.010	-0.002	16.720	-0.711	-0.711	0.000	0.000	0.000	0.000
63	A	60	ASP	-1	-0.843	-0.918	18.057	-13.900	-13.900	0.000	0.000	0.000	0.000
64	A	61	GLU	-1	-0.793	-0.877	16.681	-16.724	-16.724	0.000	0.000	0.000	0.000
65	A	62	VAL	0	0.041	-0.001	14.801	-1.388	-1.388	0.000	0.000	0.000	0.000
66	A	63	ASP	-1	-0.851	-0.905	13.494	-19.841	-19.841	0.000	0.000	0.000	0.000
67	A	64	SER	0	-0.035	-0.015	13.704	-0.086	-0.086	0.000	0.000	0.000	0.000
68	A	65	TYR	0	-0.056	-0.034	8.582	-0.597	-0.597	0.000	0.000	0.000	0.000
69	A	66	LEU	0	0.012	0.030	7.419	1.929	1.929	0.000	0.000	0.000	0.000
70	A	67	ALA	0	-0.040	-0.028	8.016	-1.843	-1.843	0.000	0.000	0.000	0.000
71	A	68	GLY	0	-0.024	-0.012	7.550	-0.770	-0.770	0.000	0.000	0.000	0.000
72	A	69	TYR	0	-0.049	-0.025	2.480	-9.712	-7.817	4.541	-1.668	-4.768	-0.008
73	A	70	ALA	0	0.053	0.036	3.014	3.575	5.014	0.059	-0.688	-0.808	-0.003
74	A	71	PHE	0	-0.055	-0.035	1.853	-42.034	-41.191	9.316	-5.072	-5.088	-0.071
75	A	72	TYR	0	-0.010	-0.032	2.566	-8.397	-3.547	5.847	-2.960	-7.737	-0.033
76	A	73	GLU	-1	-0.907	-0.944	2.262	-75.178	-72.973	2.265	-2.282	-2.188	-0.036
77	A	74	VAL	0	-0.043	-0.028	4.806	4.740	4.784	-0.001	-0.005	-0.038	0.000
78	A	75	PHE	0	0.027	0.003	7.189	1.176	1.176	0.000	0.000	0.000	0.000
79	A	76	PRO	0	0.003	0.003	10.686	0.199	0.199	0.000	0.000	0.000	0.000
80	A	77	ASP	-1	-0.808	-0.879	12.431	-16.199	-16.199	0.000	0.000	0.000	0.000
81	A	78	THR	0	-0.025	-0.024	15.354	0.665	0.665	0.000	0.000	0.000	0.000
82	A	79	SER	0	-0.039	-0.037	18.287	1.153	1.153	0.000	0.000	0.000	0.000
83	A	80	GLU	-1	-0.802	-0.868	20.959	-12.082	-12.082	0.000	0.000	0.000	0.000
84	A	81	ILE	0	0.008	-0.011	20.443	0.686	0.686	0.000	0.000	0.000	0.000
85	A	82	LEU	0	-0.004	0.008	20.543	0.682	0.682	0.000	0.000	0.000	0.000
86	A	83	ARG	1	0.844	0.894	24.108	12.836	12.836	0.000	0.000	0.000	0.000
87	A	84	ARG	1	0.724	0.849	25.518	11.913	11.913	0.000	0.000	0.000	0.000
88	A	85	LYS	1	0.940	0.950	28.499	9.186	9.186	0.000	0.000	0.000	0.000
89	A	86	ASP	-1	-0.874	-0.920	30.685	-10.010	-10.010	0.000	0.000	0.000	0.000
90	A	87	LEU	0	-0.044	0.002	24.794	-0.066	-0.066	0.000	0.000	0.000	0.000
91	A	88	THR	0	-0.027	-0.047	27.346	0.257	0.257	0.000	0.000	0.000	0.000
92	A	89	LEU	0	0.022	-0.006	26.565	-0.376	-0.376	0.000	0.000	0.000	0.000
93	A	90	LYS	1	0.914	0.945	24.459	12.024	12.024	0.000	0.000	0.000	0.000
94	A	91	GLU	-1	-0.783	-0.853	23.221	-12.435	-12.435	0.000	0.000	0.000	0.000
95	A	92	VAL	0	0.058	0.034	21.413	-0.719	-0.719	0.000	0.000	0.000	0.000
96	A	93	LEU	0	0.004	-0.004	20.601	-0.740	-0.740	0.000	0.000	0.000	0.000
97	A	94	ASP	-1	-0.843	-0.886	20.080	-14.294	-14.294	0.000	0.000	0.000	0.000
98	A	95	ILE	0	0.021	0.011	15.871	-0.907	-0.907	0.000	0.000	0.000	0.000
99	A	96	ALA	0	0.017	0.015	15.791	-1.196	-1.196	0.000	0.000	0.000	0.000
100	A	97	ILE	0	-0.025	-0.021	16.470	-0.732	-0.732	0.000	0.000	0.000	0.000
101	A	98	SER	0	-0.049	-0.034	12.739	-0.372	-0.372	0.000	0.000	0.000	0.000
102	A	99	VAL	0	0.083	0.050	11.374	-1.289	-1.289	0.000	0.000	0.000	0.000
103	A	100	GLH	0	-0.058	-0.036	11.697	-1.380	-1.380	0.000	0.000	0.000	0.000
104	A	101	LYS	1	0.909	0.940	13.284	18.702	18.702	0.000	0.000	0.000	0.000
105	A	102	ASP	-1	-0.856	-0.918	7.856	-30.567	-30.567	0.000	0.000	0.000	0.000
106	A	103	SER	0	-0.002	-0.033	8.730	-2.867	-2.867	0.000	0.000	0.000	0.000
107	A	104	ILE	0	-0.065	-0.031	10.471	0.380	0.380	0.000	0.000	0.000	0.000
108	A	105	ILE	0	-0.024	0.000	7.939	1.186	1.186	0.000	0.000	0.000	0.000
109	A	106	LEU	0	0.056	0.041	6.260	-0.162	-0.162	0.000	0.000	0.000	0.000
110	A	107	TYR	0	0.016	-0.011	8.496	0.616	0.616	0.000	0.000	0.000	0.000
111	A	108	TYR	0	-0.027	-0.032	11.925	2.552	2.552	0.000	0.000	0.000	0.000
112	A	109	GLU	-1	-0.842	-0.905	5.682	-46.067	-46.067	0.000	0.000	0.000	0.000
113	A	110	LEU	0	0.016	0.009	9.908	1.146	1.146	0.000	0.000	0.000	0.000
114	A	111	LYS	1	0.815	0.904	11.528	19.848	19.848	0.000	0.000	0.000	0.000
115	A	112	ASP	-1	-0.905	-0.966	12.805	-18.628	-18.628	0.000	0.000	0.000	0.000
116	A	113	GLY	0	0.008	0.008	12.586	0.432	0.432	0.000	0.000	0.000	0.000
117	A	114	LEU	0	-0.090	-0.023	13.495	0.808	0.808	0.000	0.000	0.000	0.000
118	A	115	VAL	0	-0.024	-0.026	16.618	0.326	0.326	0.000	0.000	0.000	0.000
119	A	116	ASN	0	-0.048	-0.036	19.585	1.286	1.286	0.000	0.000	0.000	0.000
120	A	117	SER	0	0.034	-0.004	21.579	-0.430	-0.430	0.000	0.000	0.000	0.000
121	A	118	ASP	-1	-0.858	-0.924	23.915	-11.417	-11.417	0.000	0.000	0.000	0.000
122	A	119	ALA	0	0.035	0.038	19.696	-0.078	-0.078	0.000	0.000	0.000	0.000
123	A	120	GLN	0	-0.001	-0.001	17.941	0.382	0.382	0.000	0.000	0.000	0.000
124	A	121	LYS	1	0.802	0.893	20.067	11.655	11.655	0.000	0.000	0.000	0.000
125	A	122	THR	0	-0.062	-0.038	21.321	0.250	0.250	0.000	0.000	0.000	0.000
126	A	123	VAL	0	0.050	0.015	15.321	0.028	0.028	0.000	0.000	0.000	0.000
127	A	124	LYS	1	0.865	0.919	18.374	13.154	13.154	0.000	0.000	0.000	0.000
128	A	125	LYS	1	0.893	0.950	20.140	12.202	12.202	0.000	0.000	0.000	0.000
129	A	126	ILE	0	0.027	0.019	17.455	0.315	0.315	0.000	0.000	0.000	0.000
130	A	127	ILE	0	0.028	0.023	15.237	0.044	0.044	0.000	0.000	0.000	0.000
131	A	128	ASP	-1	-0.840	-0.906	18.258	-13.816	-13.816	0.000	0.000	0.000	0.000
132	A	129	GLN	0	-0.006	-0.007	21.793	0.870	0.870	0.000	0.000	0.000	0.000
133	A	130	GLU	-1	-0.709	-0.756	16.339	-17.585	-17.585	0.000	0.000	0.000	0.000
134	A	131	LYS	1	0.810	0.895	18.589	14.989	14.989	0.000	0.000	0.000	0.000
135	A	132	GLU	-1	-0.827	-0.896	20.270	-11.535	-11.535	0.000	0.000	0.000	0.000
136	A	133	HIS	0	-0.017	0.015	19.208	1.196	1.196	0.000	0.000	0.000	0.000
137	A	134	LEU	0	0.006	0.003	17.270	0.306	0.306	0.000	0.000	0.000	0.000
138	A	135	ARG	1	0.795	0.873	20.479	11.756	11.756	0.000	0.000	0.000	0.000
139	A	136	LYS	1	0.888	0.946	23.951	11.118	11.118	0.000	0.000	0.000	0.000
140	A	137	LEU	0	0.030	0.002	19.436	0.435	0.435	0.000	0.000	0.000	0.000
141	A	138	LEU	0	-0.027	-0.021	21.221	0.268	0.268	0.000	0.000	0.000	0.000
142	A	139	GLU	-1	-0.846	-0.898	24.376	-10.216	-10.216	0.000	0.000	0.000	0.000
143	A	140	MET	0	0.018	0.014	26.247	0.327	0.327	0.000	0.000	0.000	0.000
144	A	141	LYS	1	0.827	0.893	23.227	13.388	13.388	0.000	0.000	0.000	0.000
145	A	142	ARG	1	0.805	0.881	26.782	10.180	10.180	0.000	0.000	0.000	0.000
146	A	143	GLU	-1	-0.873	-0.913	29.331	-9.455	-9.455	0.000	0.000	0.000	0.000
147	A	144	SER	0	-0.033	-0.011	30.835	0.380	0.380	0.000	0.000	0.000	0.000
148	A	145	THR	0	-0.045	-0.011	26.991	-0.238	-0.238	0.000	0.000	0.000	0.000

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