FMO DATABASE

FMODB ID: VV381

Calculation Name: 1VR9-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VR9

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZZ4

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1074064.187205
FMO2-HF: Nuclear repulsion	1023933.086014
FMO2-HF: Total energy	-50131.10119
FMO2-MP2: Total energy	-50275.545509

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:1:MET)

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

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.
-239.057	-227.317	6.749	-6.855	-11.63	-0.059

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.868 / q_NPA : 0.958

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	3	VAL	0	0.052	0.022	2.640	-9.066	-5.886	0.618	-1.631	-2.167	-0.014
5	A	5	LYS	1	0.811	0.927	2.160	42.220	43.173	2.747	-0.842	-2.858	-0.003
6	A	6	TRP	0	0.009	-0.012	1.953	2.675	4.065	2.372	-1.216	-2.545	-0.012
79	A	79	ILE	0	0.049	0.021	2.342	1.604	3.508	0.720	-0.967	-1.657	-0.011
80	A	80	THR	0	0.005	-0.017	4.546	4.050	4.256	-0.001	-0.015	-0.189	0.000
115	A	115	ALA	0	-0.025	-0.021	3.819	-2.254	-2.110	0.000	-0.027	-0.117	0.000
118	A	118	GLU	-1	-0.962	-0.979	3.002	-79.650	-75.771	0.294	-2.148	-2.024	-0.019
119	A	119	ALA	0	-0.117	-0.056	4.365	-0.365	-0.281	-0.001	-0.009	-0.073	0.000
4	A	4	LYS	1	0.874	0.935	5.457	23.227	23.227	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.002	0.022	6.060	2.009	2.009	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.033	0.022	9.262	1.131	1.131	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.018	-0.052	12.440	0.960	0.960	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.920	-0.925	15.749	-13.653	-13.653	0.000	0.000	0.000	0.000
11	A	11	PHE	0	0.005	0.001	16.518	-0.485	-0.485	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.026	0.008	18.803	0.669	0.669	0.000	0.000	0.000	0.000
13	A	13	MET	0	-0.007	0.004	21.253	-0.055	-0.055	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.016	-0.032	23.137	0.528	0.528	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.804	-0.881	25.780	-9.905	-9.905	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.850	-0.950	28.203	-9.846	-9.846	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.101	-0.078	29.960	0.301	0.301	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.014	0.032	30.881	0.293	0.293	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.003	-0.037	32.834	0.044	0.044	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.018	0.011	33.397	-0.323	-0.323	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.790	0.860	33.887	7.535	7.535	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.855	-0.900	31.528	-9.174	-9.174	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.008	0.015	28.917	-0.459	-0.459	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.058	0.015	29.108	-0.339	-0.339	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.038	-0.011	30.892	-0.014	-0.014	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.934	0.964	25.533	10.777	10.777	0.000	0.000	0.000	0.000
27	A	27	MET	0	0.038	0.026	25.920	-0.185	-0.185	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.873	0.949	26.918	9.125	9.125	0.000	0.000	0.000	0.000
29	A	29	GLN	0	-0.085	-0.042	26.450	0.163	0.163	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.028	-0.026	20.378	0.120	0.120	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.085	-0.038	23.340	-0.132	-0.132	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.023	0.023	22.038	-0.126	-0.126	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.018	-0.038	24.127	0.286	0.286	0.000	0.000	0.000	0.000
34	A	34	GLU	0	0.067	0.031	18.980	0.144	0.144	0.000	0.000	0.000	0.000
35	A	35	CYS	0	-0.085	-0.039	23.307	-0.023	-0.023	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.036	0.022	17.697	0.097	0.097	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.003	0.004	22.014	0.409	0.409	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.939	0.981	22.680	11.719	11.719	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.737	-0.882	24.626	-10.654	-10.654	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.882	0.922	26.893	8.772	8.772	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.956	-0.958	27.244	-9.993	-9.993	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.059	-0.021	23.758	-0.328	-0.328	0.000	0.000	0.000	0.000
43	A	43	HIS	0	-0.043	-0.028	22.231	-0.312	-0.312	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.004	-0.003	19.896	0.313	0.313	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.875	0.929	22.040	11.137	11.137	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.036	0.022	23.147	0.317	0.317	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.035	-0.013	21.116	-0.330	-0.330	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.000	-0.005	23.963	0.537	0.537	0.000	0.000	0.000	0.000
49	A	49	ASN	0	0.014	-0.003	24.518	-0.204	-0.204	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.924	0.938	27.627	10.708	10.708	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.970	-0.973	29.641	-10.228	-10.228	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.842	-0.921	30.406	-9.912	-9.912	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.083	-0.072	30.649	0.247	0.247	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.046	-0.005	34.403	0.176	0.176	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.929	-0.958	36.824	-7.696	-7.696	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.073	-0.037	35.875	0.120	0.120	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.861	-0.924	39.798	-7.233	-7.233	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.009	0.001	37.808	-0.202	-0.202	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.818	-0.884	38.466	-7.595	-7.595	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.080	-0.039	39.043	-0.033	-0.033	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.028	-0.040	35.282	-0.197	-0.197	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.004	-0.013	30.066	0.055	0.055	0.000	0.000	0.000	0.000
63	A	63	PHE	0	-0.013	0.026	32.085	-0.159	-0.159	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.056	-0.043	32.868	-0.204	-0.204	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.885	0.942	32.333	8.769	8.769	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.021	0.016	26.752	-0.218	-0.218	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.024	0.020	27.032	0.277	0.277	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.036	-0.024	22.070	-0.345	-0.345	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.045	0.015	22.871	-0.516	-0.516	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.908	-0.959	21.851	-13.296	-13.296	0.000	0.000	0.000	0.000
71	A	71	PHE	0	-0.054	-0.028	16.741	-0.860	-0.860	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.008	-0.004	15.983	0.006	0.006	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.018	-0.005	10.369	-0.873	-0.873	0.000	0.000	0.000	0.000
74	A	74	HIS	0	0.053	0.015	12.529	1.959	1.959	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.862	-0.953	9.827	-22.628	-22.628	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.874	-0.937	8.150	-28.837	-28.837	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.787	-0.870	9.159	-27.303	-27.303	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.033	-0.029	4.827	-6.424	-6.424	0.000	0.000	0.000	0.000
81	A	81	HIS	0	-0.009	0.007	6.459	3.506	3.506	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.058	0.025	8.312	2.819	2.819	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.007	-0.001	9.090	2.193	2.193	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.026	-0.002	10.799	2.036	2.036	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.049	0.026	13.063	1.438	1.438	0.000	0.000	0.000	0.000
86	A	86	PHE	0	0.006	-0.005	10.654	1.267	1.267	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.051	-0.005	14.927	1.187	1.187	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.955	-0.976	16.726	-15.254	-15.254	0.000	0.000	0.000	0.000
89	A	89	HIS	1	0.854	0.918	18.237	15.926	15.926	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.039	-0.011	18.023	-0.133	-0.133	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.845	-0.919	18.322	-13.472	-13.472	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.028	-0.017	17.078	-1.110	-1.110	0.000	0.000	0.000	0.000
93	A	93	TYR	0	-0.005	-0.011	15.369	-0.740	-0.740	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.030	0.044	11.407	1.013	1.013	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.001	-0.002	13.570	-1.067	-1.067	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.011	0.005	10.523	-1.111	-1.111	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.004	0.009	13.426	1.197	1.197	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.794	-0.907	14.218	-16.556	-16.556	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.902	-0.963	16.415	-16.606	-16.606	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.970	-0.972	18.791	-13.090	-13.090	0.000	0.000	0.000	0.000
101	A	101	MET	0	-0.015	-0.010	19.300	0.569	0.569	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.860	0.945	19.797	12.346	12.346	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.006	-0.013	17.170	-0.807	-0.807	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.779	0.892	13.779	16.561	16.561	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.032	0.024	13.846	-0.341	-0.341	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.013	-0.003	13.479	0.405	0.405	0.000	0.000	0.000	0.000
107	A	107	VAL	0	0.009	0.015	8.320	-1.052	-1.052	0.000	0.000	0.000	0.000
108	A	108	SER	0	-0.011	-0.019	10.808	1.536	1.536	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.013	-0.006	11.416	-1.970	-1.970	0.000	0.000	0.000	0.000
110	A	110	HIS	0	-0.056	-0.036	12.505	0.053	0.053	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.771	-0.873	9.083	-24.635	-24.635	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.033	-0.014	7.502	-4.222	-4.222	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.015	-0.014	8.011	-2.639	-2.639	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.922	-0.955	8.640	-27.303	-27.303	0.000	0.000	0.000	0.000
116	A	116	LEU	0	-0.048	-0.037	5.592	-5.049	-5.049	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.018	0.007	7.904	2.176	2.176	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.063	-0.048	6.142	2.974	2.974	0.000	0.000	0.000	0.000
121	A	121	ALA	-1	-0.953	-0.946	9.980	-21.947	-21.947	0.000	0.000	0.000	0.000

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