FMO DATABASE

FMODB ID: LQ299

Calculation Name: 2FVH-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FVH

Chain ID: A

ChEMBL ID:

UniProt ID: P9WFE7

Base Structure: X-ray

Registration Date: 2025-10-04

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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-698084.670313
FMO2-HF: Nuclear repulsion	659646.092014
FMO2-HF: Total energy	-38438.578299
FMO2-MP2: Total energy	-38550.762121

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:2:ARG)

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

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.
-154.824	-152.745	0	-1.025	-1.054	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.798 / q_NPA : 1.885

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

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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].	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	4	THR	0	-0.003	-0.023	3.531	-5.419	-3.340	-1.025	-1.054	-0.004
4	A	5	PRO	0	0.041	0.005	6.030	0.729	0.729	0.000	0.000	0.000
5	A	6	HIS	0	0.091	0.049	8.959	-0.156	-0.156	0.000	0.000	0.000
6	A	7	GLU	-1	-0.792	-0.868	5.904	-81.392	-81.392	0.000	0.000	0.000
7	A	8	GLN	0	-0.044	-0.029	5.729	3.559	3.559	0.000	0.000	0.000
8	A	9	GLU	-1	-0.840	-0.900	8.900	-35.154	-35.154	0.000	0.000	0.000
9	A	10	ARG	1	0.837	0.897	11.839	42.265	42.265	0.000	0.000	0.000
10	A	11	LEU	0	0.007	0.008	8.042	1.415	1.415	0.000	0.000	0.000
11	A	12	LEU	0	-0.026	-0.027	11.652	2.724	2.724	0.000	0.000	0.000
12	A	13	LEU	0	-0.002	0.014	14.022	2.528	2.528	0.000	0.000	0.000
13	A	14	SER	0	0.042	0.032	14.821	1.615	1.615	0.000	0.000	0.000
14	A	15	TYR	0	-0.012	-0.012	15.138	2.285	2.285	0.000	0.000	0.000
15	A	16	ALA	0	-0.020	-0.012	16.999	2.027	2.027	0.000	0.000	0.000
16	A	17	ALA	0	0.050	0.032	19.778	1.876	1.876	0.000	0.000	0.000
17	A	18	GLU	-1	-0.935	-0.961	18.427	-30.955	-30.955	0.000	0.000	0.000
18	A	19	LEU	0	-0.074	-0.043	20.916	1.820	1.820	0.000	0.000	0.000
19	A	20	ALA	0	0.007	0.000	22.644	1.342	1.342	0.000	0.000	0.000
20	A	21	ARG	1	0.930	0.955	19.624	30.043	30.043	0.000	0.000	0.000
21	A	22	ARG	1	0.940	0.969	23.931	25.510	25.510	0.000	0.000	0.000
22	A	23	ARG	1	0.811	0.885	25.037	24.632	24.632	0.000	0.000	0.000
23	A	24	ARG	1	0.852	0.912	28.807	19.231	19.231	0.000	0.000	0.000
24	A	25	ALA	0	-0.007	-0.003	28.970	0.718	0.718	0.000	0.000	0.000
25	A	26	ARG	1	0.841	0.933	27.883	21.475	21.475	0.000	0.000	0.000
26	A	27	GLY	0	0.027	0.016	32.940	0.430	0.430	0.000	0.000	0.000
27	A	28	LEU	0	-0.061	-0.019	30.848	0.360	0.360	0.000	0.000	0.000
28	A	29	ARG	1	0.788	0.888	33.622	16.169	16.169	0.000	0.000	0.000
29	A	30	LEU	0	-0.002	-0.004	28.283	-0.094	-0.094	0.000	0.000	0.000
30	A	31	ASN	0	-0.007	-0.021	28.371	0.102	0.102	0.000	0.000	0.000
31	A	32	HIS	0	0.110	0.040	29.747	-0.429	-0.429	0.000	0.000	0.000
32	A	33	PRO	0	-0.001	-0.003	24.665	-0.404	-0.404	0.000	0.000	0.000
33	A	34	GLU	-1	-0.825	-0.896	24.857	-23.128	-23.128	0.000	0.000	0.000
34	A	35	ALA	0	0.032	0.019	25.738	-0.628	-0.628	0.000	0.000	0.000
35	A	36	ILE	0	0.008	0.004	23.438	-0.436	-0.436	0.000	0.000	0.000
36	A	37	ALA	0	-0.005	-0.003	21.400	-0.744	-0.744	0.000	0.000	0.000
37	A	38	VAL	0	-0.017	-0.015	21.971	-0.971	-0.971	0.000	0.000	0.000
38	A	39	ILE	0	0.003	0.010	24.099	-0.316	-0.316	0.000	0.000	0.000
39	A	40	ALA	0	0.024	0.005	20.375	-0.314	-0.314	0.000	0.000	0.000
40	A	41	ASP	-1	-0.860	-0.928	18.975	-32.290	-32.290	0.000	0.000	0.000
41	A	42	HIS	0	0.022	0.008	20.296	-0.970	-0.970	0.000	0.000	0.000
42	A	43	ILE	0	-0.008	-0.005	21.350	0.137	0.137	0.000	0.000	0.000
43	A	44	LEU	0	-0.041	-0.017	15.465	-0.690	-0.690	0.000	0.000	0.000
44	A	45	GLU	-1	-0.913	-0.962	15.741	-38.237	-38.237	0.000	0.000	0.000
45	A	46	GLY	0	0.033	0.017	18.220	0.343	0.343	0.000	0.000	0.000
46	A	47	ALA	0	-0.004	-0.014	17.790	0.563	0.563	0.000	0.000	0.000
47	A	48	ARG	1	0.890	0.935	12.189	37.930	37.930	0.000	0.000	0.000
48	A	49	ASP	-1	-0.844	-0.918	16.127	-28.116	-28.116	0.000	0.000	0.000
49	A	50	GLY	0	-0.084	-0.038	19.016	0.821	0.821	0.000	0.000	0.000
50	A	51	ARG	1	0.806	0.912	20.311	25.494	25.494	0.000	0.000	0.000
51	A	52	THR	0	-0.015	-0.035	22.991	-0.427	-0.427	0.000	0.000	0.000
52	A	53	VAL	0	0.040	0.001	23.999	-0.008	-0.008	0.000	0.000	0.000
53	A	54	ALA	0	0.012	0.009	26.032	0.201	0.201	0.000	0.000	0.000
54	A	55	GLU	-1	-0.829	-0.898	27.138	-21.249	-21.249	0.000	0.000	0.000
55	A	56	LEU	0	-0.047	0.023	22.438	0.211	0.211	0.000	0.000	0.000
56	A	57	MET	0	-0.036	-0.020	26.831	0.103	0.103	0.000	0.000	0.000
57	A	58	ALA	0	-0.023	0.000	29.542	0.511	0.511	0.000	0.000	0.000
58	A	59	SER	0	0.012	-0.030	28.230	-0.111	-0.111	0.000	0.000	0.000
59	A	60	GLY	0	0.019	0.005	28.194	-0.054	-0.054	0.000	0.000	0.000
60	A	61	ARG	1	0.801	0.887	28.837	17.760	17.760	0.000	0.000	0.000
61	A	62	GLU	-1	-0.946	-0.953	31.819	-17.103	-17.103	0.000	0.000	0.000
62	A	63	VAL	0	-0.064	-0.018	27.222	-0.051	-0.051	0.000	0.000	0.000
63	A	64	LEU	0	-0.056	-0.033	28.681	-0.247	-0.247	0.000	0.000	0.000
64	A	65	GLY	0	0.098	0.054	32.529	0.326	0.326	0.000	0.000	0.000
65	A	66	ARG	1	0.793	0.834	35.666	15.433	15.433	0.000	0.000	0.000
66	A	67	ASP	-1	-0.904	-0.941	37.995	-15.833	-15.833	0.000	0.000	0.000
67	A	68	ASP	-1	-0.819	-0.899	32.830	-18.606	-18.606	0.000	0.000	0.000
68	A	69	VAL	0	0.001	0.016	31.930	-0.634	-0.634	0.000	0.000	0.000
69	A	70	MET	0	-0.071	-0.040	32.930	0.628	0.628	0.000	0.000	0.000
70	A	71	GLU	-1	-0.784	-0.890	36.614	-15.454	-15.454	0.000	0.000	0.000
71	A	72	GLY	0	-0.017	0.000	38.663	-0.147	-0.147	0.000	0.000	0.000
72	A	73	VAL	0	-0.012	-0.016	32.609	-0.260	-0.260	0.000	0.000	0.000
73	A	74	PRO	0	-0.020	-0.010	34.694	-0.430	-0.430	0.000	0.000	0.000
74	A	75	GLU	-1	-0.753	-0.860	36.034	-16.058	-16.058	0.000	0.000	0.000
75	A	76	MET	0	-0.088	-0.030	33.320	-0.223	-0.223	0.000	0.000	0.000
76	A	77	LEU	0	-0.051	-0.009	29.735	-0.644	-0.644	0.000	0.000	0.000
77	A	78	ALA	0	0.038	0.018	32.836	0.198	0.198	0.000	0.000	0.000
78	A	79	GLU	-1	-0.894	-0.961	29.311	-20.779	-20.779	0.000	0.000	0.000
79	A	80	VAL	0	-0.032	-0.001	24.783	-0.307	-0.307	0.000	0.000	0.000
80	A	81	GLN	0	-0.045	-0.023	24.248	-0.444	-0.444	0.000	0.000	0.000
81	A	82	VAL	0	-0.027	-0.016	18.852	-0.948	-0.948	0.000	0.000	0.000
82	A	83	GLU	-1	-0.953	-0.965	17.319	-31.333	-31.333	0.000	0.000	0.000
83	A	84	ALA	0	0.005	0.000	16.736	-1.971	-1.971	0.000	0.000	0.000
84	A	85	THR	0	-0.018	-0.018	13.377	1.513	1.513	0.000	0.000	0.000
85	A	86	PHE	0	0.035	0.038	15.799	-0.484	-0.484	0.000	0.000	0.000
86	A	87	PRO	0	-0.018	-0.013	16.740	-1.064	-1.064	0.000	0.000	0.000
87	A	88	ASP	-1	-0.858	-0.909	17.771	-26.220	-26.220	0.000	0.000	0.000
88	A	89	GLY	0	0.015	0.013	17.040	0.708	0.708	0.000	0.000	0.000
89	A	90	THR	0	-0.072	-0.050	15.473	-0.190	-0.190	0.000	0.000	0.000
90	A	91	LYS	1	0.811	0.893	17.974	27.391	27.391	0.000	0.000	0.000
91	A	92	LEU	0	0.021	0.026	20.734	-0.959	-0.959	0.000	0.000	0.000
92	A	93	VAL	0	-0.016	-0.015	22.583	1.072	1.072	0.000	0.000	0.000
93	A	94	THR	0	0.012	0.000	24.505	-0.868	-0.868	0.000	0.000	0.000
94	A	95	VAL	0	-0.001	0.013	26.938	0.548	0.548	0.000	0.000	0.000
95	A	96	HIS	0	0.008	-0.008	29.241	-0.123	-0.123	0.000	0.000	0.000
96	A	97	GLN	0	-0.034	-0.023	32.632	0.239	0.239	0.000	0.000	0.000
97	A	98	PRO	0	-0.027	-0.016	29.894	0.287	0.287	0.000	0.000	0.000
98	A	99	ILE	0	-0.013	0.003	32.142	-0.090	-0.090	0.000	0.000	0.000
99	A	100	ALA	-1	-0.823	-0.892	35.169	-15.934	-15.934	0.000	0.000	0.000

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