FMO DATABASE

FMODB ID: 8GMZY

Calculation Name: 1VJX-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VJX

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X1L2

Base Structure: X-ray

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

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. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1543413.724415
FMO2-HF: Nuclear repulsion	1481691.933547
FMO2-HF: Total energy	-61721.790867
FMO2-MP2: Total energy	-61904.06697

3D Structure Molmil

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:-3:HIS)

Summations of interaction energy for fragment #1(A:-3: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.
-182.484	-172.768	7.429	-6.032	-11.115	-0.029

Interaction energy analysis for fragmet #1(A:-3:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / q_NPA : 0.931

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	-1	HIS	0	0.052	0.035	2.290	-9.234	-4.663	6.119	-3.684	-7.007	-0.006
4	A	0	HIS	0	-0.043	-0.030	2.891	-13.360	-10.494	1.252	-1.322	-2.796	-0.015
5	A	1	MET	0	0.008	0.032	3.905	-9.602	-8.613	0.026	-0.455	-0.561	-0.004
73	A	69	TYR	0	-0.060	-0.050	4.764	-4.715	-4.573	-0.001	-0.008	-0.132	0.000
76	A	72	TYR	0	-0.015	-0.033	2.943	-2.080	-0.932	0.033	-0.563	-0.619	-0.004
6	A	2	LYS	1	0.844	0.911	5.744	30.473	30.473	0.000	0.000	0.000	0.000
7	A	3	VAL	0	0.033	0.025	9.279	-1.421	-1.421	0.000	0.000	0.000	0.000
8	A	4	SER	0	0.038	0.012	10.213	0.653	0.653	0.000	0.000	0.000	0.000
9	A	5	ASP	-1	-0.869	-0.911	6.374	-37.587	-37.587	0.000	0.000	0.000	0.000
10	A	6	ILE	0	0.001	-0.009	7.902	-0.557	-0.557	0.000	0.000	0.000	0.000
11	A	7	LEU	0	0.028	0.010	9.923	1.538	1.538	0.000	0.000	0.000	0.000
12	A	8	THR	0	-0.041	-0.028	9.744	1.615	1.615	0.000	0.000	0.000	0.000
13	A	9	VAL	0	-0.047	-0.029	7.263	0.690	0.690	0.000	0.000	0.000	0.000
14	A	10	ALA	0	0.026	0.009	10.496	1.600	1.600	0.000	0.000	0.000	0.000
15	A	11	ILE	0	-0.053	-0.023	13.971	1.445	1.445	0.000	0.000	0.000	0.000
16	A	12	ARG	1	0.953	0.979	11.063	24.740	24.740	0.000	0.000	0.000	0.000
17	A	13	LEU	0	-0.022	-0.002	11.816	0.821	0.821	0.000	0.000	0.000	0.000
18	A	14	GLU	0	-0.016	-0.027	15.107	1.289	1.289	0.000	0.000	0.000	0.000
19	A	15	GLU	-1	-0.859	-0.923	17.125	-16.170	-16.170	0.000	0.000	0.000	0.000
20	A	16	GLU	-1	-0.867	-0.937	15.654	-15.598	-15.598	0.000	0.000	0.000	0.000
21	A	17	GLY	0	0.025	0.029	18.505	0.642	0.642	0.000	0.000	0.000	0.000
22	A	18	GLU	-1	-0.853	-0.934	20.336	-11.330	-11.330	0.000	0.000	0.000	0.000
23	A	19	ARG	1	0.760	0.859	19.599	14.908	14.908	0.000	0.000	0.000	0.000
24	A	20	PHE	0	0.061	0.038	21.071	0.656	0.656	0.000	0.000	0.000	0.000
25	A	21	TYR	0	-0.017	-0.018	22.335	0.759	0.759	0.000	0.000	0.000	0.000
26	A	22	ARG	1	0.845	0.906	25.938	11.428	11.428	0.000	0.000	0.000	0.000
27	A	23	GLU	-1	-0.819	-0.886	23.851	-12.218	-12.218	0.000	0.000	0.000	0.000
28	A	24	LEU	0	0.000	-0.007	25.445	0.484	0.484	0.000	0.000	0.000	0.000
29	A	25	SER	0	-0.088	-0.047	28.599	0.538	0.538	0.000	0.000	0.000	0.000
30	A	26	GLU	-1	-0.948	-0.973	30.580	-9.642	-9.642	0.000	0.000	0.000	0.000
31	A	27	HIS	1	0.807	0.918	29.826	10.298	10.298	0.000	0.000	0.000	0.000
32	A	28	PHE	0	0.034	0.023	30.486	0.188	0.188	0.000	0.000	0.000	0.000
33	A	29	ASN	0	-0.009	-0.019	35.542	0.009	0.009	0.000	0.000	0.000	0.000
34	A	30	GLY	0	0.029	0.015	38.815	0.059	0.059	0.000	0.000	0.000	0.000
35	A	31	GLU	-1	-0.789	-0.904	38.188	-7.995	-7.995	0.000	0.000	0.000	0.000
36	A	32	ILE	0	0.004	0.023	33.589	-0.183	-0.183	0.000	0.000	0.000	0.000
37	A	33	LYS	1	0.866	0.945	33.564	8.315	8.315	0.000	0.000	0.000	0.000
38	A	34	LYS	1	0.861	0.920	33.623	7.735	7.735	0.000	0.000	0.000	0.000
39	A	35	THR	0	0.013	-0.004	31.230	-0.163	-0.163	0.000	0.000	0.000	0.000
40	A	36	PHE	0	-0.001	-0.006	27.984	-0.275	-0.275	0.000	0.000	0.000	0.000
41	A	37	LEU	0	0.008	0.003	29.097	-0.339	-0.339	0.000	0.000	0.000	0.000
42	A	38	GLU	-1	-0.943	-0.980	30.601	-9.078	-9.078	0.000	0.000	0.000	0.000
43	A	39	LEU	0	-0.054	-0.026	26.693	-0.190	-0.190	0.000	0.000	0.000	0.000
44	A	40	ALA	0	0.030	0.018	25.748	-0.375	-0.375	0.000	0.000	0.000	0.000
45	A	41	ASP	-1	-0.813	-0.892	26.139	-10.595	-10.595	0.000	0.000	0.000	0.000
46	A	42	GLN	0	-0.017	0.003	27.100	-0.249	-0.249	0.000	0.000	0.000	0.000
47	A	43	GLU	-1	-0.828	-0.923	21.285	-14.259	-14.259	0.000	0.000	0.000	0.000
48	A	44	ARG	1	0.770	0.877	22.705	10.390	10.390	0.000	0.000	0.000	0.000
49	A	45	ILE	0	-0.024	-0.009	24.303	-0.229	-0.229	0.000	0.000	0.000	0.000
50	A	46	HIS	0	-0.036	-0.028	21.486	0.405	0.405	0.000	0.000	0.000	0.000
51	A	47	ALA	0	0.051	0.026	19.855	-0.578	-0.578	0.000	0.000	0.000	0.000
52	A	48	GLU	-1	-0.925	-0.960	20.787	-11.863	-11.863	0.000	0.000	0.000	0.000
53	A	49	ILE	0	-0.052	-0.019	22.206	0.031	0.031	0.000	0.000	0.000	0.000
54	A	50	PHE	0	0.024	-0.001	17.240	-0.166	-0.166	0.000	0.000	0.000	0.000
55	A	51	ARG	1	0.894	0.933	18.485	13.972	13.972	0.000	0.000	0.000	0.000
56	A	52	LYS	1	0.931	0.984	19.694	11.301	11.301	0.000	0.000	0.000	0.000
57	A	53	MET	0	-0.019	-0.004	18.994	-0.076	-0.076	0.000	0.000	0.000	0.000
58	A	54	SER	0	-0.063	-0.048	16.039	-0.364	-0.364	0.000	0.000	0.000	0.000
59	A	55	ASP	-1	-0.949	-0.967	17.797	-13.754	-13.754	0.000	0.000	0.000	0.000
60	A	56	GLN	0	-0.061	-0.040	20.877	0.648	0.648	0.000	0.000	0.000	0.000
61	A	57	GLU	-1	-0.822	-0.877	19.409	-13.407	-13.407	0.000	0.000	0.000	0.000
62	A	58	ASN	0	-0.066	-0.044	21.209	-0.454	-0.454	0.000	0.000	0.000	0.000
63	A	59	TRP	0	0.021	0.010	15.271	-0.708	-0.708	0.000	0.000	0.000	0.000
64	A	60	ASP	-1	-0.841	-0.917	17.682	-15.502	-15.502	0.000	0.000	0.000	0.000
65	A	61	GLU	-1	-0.807	-0.882	17.322	-16.659	-16.659	0.000	0.000	0.000	0.000
66	A	62	VAL	0	0.022	-0.001	14.844	-1.458	-1.458	0.000	0.000	0.000	0.000
67	A	63	ASP	-1	-0.839	-0.908	13.288	-24.631	-24.631	0.000	0.000	0.000	0.000
68	A	64	SER	0	-0.024	-0.024	12.687	-1.034	-1.034	0.000	0.000	0.000	0.000
69	A	65	TYR	0	-0.086	-0.050	7.593	-1.643	-1.643	0.000	0.000	0.000	0.000
70	A	66	LEU	0	0.028	0.029	9.211	2.382	2.382	0.000	0.000	0.000	0.000
71	A	67	ALA	0	-0.028	-0.014	8.910	-2.199	-2.199	0.000	0.000	0.000	0.000
72	A	68	GLY	0	-0.025	-0.009	8.256	0.658	0.658	0.000	0.000	0.000	0.000
74	A	70	ALA	0	0.053	0.043	7.316	2.883	2.883	0.000	0.000	0.000	0.000
75	A	71	PHE	0	-0.032	-0.034	7.332	-5.642	-5.642	0.000	0.000	0.000	0.000
77	A	73	GLU	-1	-0.902	-0.927	8.141	-28.914	-28.914	0.000	0.000	0.000	0.000
78	A	74	VAL	0	-0.044	-0.034	7.638	-0.417	-0.417	0.000	0.000	0.000	0.000
79	A	75	PHE	0	0.046	0.012	10.333	1.303	1.303	0.000	0.000	0.000	0.000
80	A	76	PRO	0	-0.013	-0.003	14.110	-0.221	-0.221	0.000	0.000	0.000	0.000
81	A	77	ASP	-1	-0.828	-0.889	15.743	-14.527	-14.527	0.000	0.000	0.000	0.000
82	A	78	THR	0	0.001	-0.003	17.880	0.676	0.676	0.000	0.000	0.000	0.000
83	A	79	SER	0	-0.038	-0.034	21.303	0.944	0.944	0.000	0.000	0.000	0.000
84	A	80	GLU	-1	-0.842	-0.921	23.348	-11.128	-11.128	0.000	0.000	0.000	0.000
85	A	81	ILE	0	-0.036	-0.022	23.780	0.529	0.529	0.000	0.000	0.000	0.000
86	A	82	LEU	0	0.021	0.008	23.787	0.536	0.536	0.000	0.000	0.000	0.000
87	A	83	ARG	1	0.876	0.925	25.390	11.806	11.806	0.000	0.000	0.000	0.000
88	A	84	ARG	1	0.773	0.883	28.825	10.306	10.306	0.000	0.000	0.000	0.000
89	A	85	LYS	1	0.925	0.941	31.468	8.426	8.426	0.000	0.000	0.000	0.000
90	A	86	ASP	-1	-0.873	-0.927	34.038	-8.875	-8.875	0.000	0.000	0.000	0.000
91	A	87	LEU	0	-0.055	-0.004	28.641	-0.030	-0.030	0.000	0.000	0.000	0.000
92	A	88	THR	0	-0.019	-0.039	31.796	0.183	0.183	0.000	0.000	0.000	0.000
93	A	89	LEU	0	0.026	-0.002	31.204	-0.296	-0.296	0.000	0.000	0.000	0.000
94	A	90	LYS	1	0.922	0.955	30.059	9.817	9.817	0.000	0.000	0.000	0.000
95	A	91	GLU	-1	-0.795	-0.863	27.832	-10.489	-10.489	0.000	0.000	0.000	0.000
96	A	92	VAL	0	0.032	0.020	26.178	-0.499	-0.499	0.000	0.000	0.000	0.000
97	A	93	LEU	0	0.010	0.005	25.600	-0.506	-0.506	0.000	0.000	0.000	0.000
98	A	94	ASP	-1	-0.821	-0.881	25.622	-11.177	-11.177	0.000	0.000	0.000	0.000
99	A	95	ILE	0	-0.009	-0.001	20.706	-0.545	-0.545	0.000	0.000	0.000	0.000
100	A	96	ALA	0	0.016	0.009	21.056	-0.700	-0.700	0.000	0.000	0.000	0.000
101	A	97	ILE	0	-0.026	-0.027	21.648	-0.490	-0.490	0.000	0.000	0.000	0.000
102	A	98	SER	0	-0.048	-0.015	17.984	-0.107	-0.107	0.000	0.000	0.000	0.000
103	A	99	VAL	0	0.074	0.037	16.684	-0.512	-0.512	0.000	0.000	0.000	0.000
104	A	100	GLU	0	-0.033	-0.022	17.069	-0.848	-0.848	0.000	0.000	0.000	0.000
105	A	101	LYS	1	0.886	0.937	18.988	13.625	13.625	0.000	0.000	0.000	0.000
106	A	102	ASP	-1	-0.859	-0.937	13.704	-19.315	-19.315	0.000	0.000	0.000	0.000
107	A	103	SER	0	-0.018	-0.025	14.096	-1.593	-1.593	0.000	0.000	0.000	0.000
108	A	104	ILE	0	-0.044	-0.024	15.509	-0.204	-0.204	0.000	0.000	0.000	0.000
109	A	105	ILE	0	-0.027	-0.005	13.755	0.303	0.303	0.000	0.000	0.000	0.000
110	A	106	LEU	0	0.046	0.038	9.855	-0.059	-0.059	0.000	0.000	0.000	0.000
111	A	107	TYR	0	0.023	0.002	13.444	-0.222	-0.222	0.000	0.000	0.000	0.000
112	A	108	TYR	0	-0.026	-0.032	16.707	1.092	1.092	0.000	0.000	0.000	0.000
113	A	109	GLU	-1	-0.818	-0.902	11.334	-26.756	-26.756	0.000	0.000	0.000	0.000
114	A	110	LEU	0	0.002	0.004	14.105	-0.065	-0.065	0.000	0.000	0.000	0.000
115	A	111	LYS	1	0.824	0.919	15.005	15.804	15.804	0.000	0.000	0.000	0.000
116	A	112	ASP	-1	-0.925	-0.978	16.651	-15.713	-15.713	0.000	0.000	0.000	0.000
117	A	113	GLY	0	-0.020	-0.012	14.620	0.065	0.065	0.000	0.000	0.000	0.000
118	A	114	LEU	0	-0.070	-0.017	15.491	0.238	0.238	0.000	0.000	0.000	0.000
119	A	115	VAL	0	-0.010	-0.016	18.506	0.480	0.480	0.000	0.000	0.000	0.000
120	A	116	ASN	0	-0.039	-0.043	21.248	1.327	1.327	0.000	0.000	0.000	0.000
121	A	117	SER	0	0.024	0.005	23.645	-0.231	-0.231	0.000	0.000	0.000	0.000
122	A	118	ASP	-1	-0.811	-0.890	26.004	-10.767	-10.767	0.000	0.000	0.000	0.000
123	A	119	ALA	0	0.061	0.042	21.404	0.112	0.112	0.000	0.000	0.000	0.000
124	A	120	GLN	0	-0.022	-0.017	20.829	0.540	0.540	0.000	0.000	0.000	0.000
125	A	121	LYS	1	0.768	0.873	23.043	10.973	10.973	0.000	0.000	0.000	0.000
126	A	122	THR	0	-0.059	-0.038	23.801	0.359	0.359	0.000	0.000	0.000	0.000
127	A	123	VAL	0	0.042	0.016	18.631	0.129	0.129	0.000	0.000	0.000	0.000
128	A	124	LYS	1	0.848	0.912	21.909	11.493	11.493	0.000	0.000	0.000	0.000
129	A	125	LYS	1	0.883	0.938	24.329	10.832	10.832	0.000	0.000	0.000	0.000
130	A	126	ILE	0	0.023	0.029	20.873	0.354	0.354	0.000	0.000	0.000	0.000
131	A	127	ILE	0	0.017	0.011	20.067	0.297	0.297	0.000	0.000	0.000	0.000
132	A	128	ASP	-1	-0.836	-0.906	22.903	-11.419	-11.419	0.000	0.000	0.000	0.000
133	A	129	GLN	0	0.000	-0.002	26.128	0.695	0.695	0.000	0.000	0.000	0.000
134	A	130	GLU	-1	-0.746	-0.809	21.012	-14.013	-14.013	0.000	0.000	0.000	0.000
135	A	131	LYS	1	0.826	0.910	23.962	12.186	12.186	0.000	0.000	0.000	0.000
136	A	132	GLU	-1	-0.852	-0.910	25.753	-9.736	-9.736	0.000	0.000	0.000	0.000
137	A	133	HIS	1	0.813	0.909	23.609	12.744	12.744	0.000	0.000	0.000	0.000
138	A	134	LEU	0	0.011	0.006	23.052	0.227	0.227	0.000	0.000	0.000	0.000
139	A	135	ARG	1	0.794	0.867	25.761	9.777	9.777	0.000	0.000	0.000	0.000
140	A	136	LYS	1	0.880	0.934	29.426	9.382	9.382	0.000	0.000	0.000	0.000
141	A	137	LEU	0	0.017	0.005	24.538	0.301	0.301	0.000	0.000	0.000	0.000
142	A	138	LEU	0	-0.018	-0.019	27.154	0.212	0.212	0.000	0.000	0.000	0.000
143	A	139	GLU	-1	-0.833	-0.883	30.131	-8.660	-8.660	0.000	0.000	0.000	0.000
144	A	140	MET	0	0.019	0.008	31.779	0.196	0.196	0.000	0.000	0.000	0.000
145	A	141	LYS	1	0.849	0.915	28.974	10.596	10.596	0.000	0.000	0.000	0.000
146	A	142	ARG	1	0.809	0.892	32.450	8.459	8.459	0.000	0.000	0.000	0.000
147	A	143	GLU	-1	-0.887	-0.919	35.274	-8.018	-8.018	0.000	0.000	0.000	0.000
148	A	144	SER	0	-0.072	-0.043	35.729	0.258	0.258	0.000	0.000	0.000	0.000
149	A	145	THR	-1	-0.968	-0.975	32.260	-8.985	-8.985	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:HIS)