FMO DATABASE

FMODB ID: LQ4K9

Calculation Name: 1VAP-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VAP

Chain ID: A

ChEMBL ID:

UniProt ID: P51972

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1051365.533135
FMO2-HF: Nuclear repulsion	998514.01497
FMO2-HF: Total energy	-52851.518164
FMO2-MP2: Total energy	-52992.127679

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:ASN)

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

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.
-38.237	-20.546	31.062	-21.204	-27.549	-0.157

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.794 / q_NPA : 0.910

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].	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	PHE	0	-0.004	0.006	2.616	2.727	6.358	2.499	-2.182	-3.948	0.020
4	A	4	GLN	0	-0.029	-0.016	2.142	-29.019	-25.702	7.169	-4.197	-6.289	-0.010
5	A	5	PHE	0	0.069	0.038	3.910	6.211	6.768	0.006	-0.204	-0.360	0.001
59	A	60	LYS	1	0.988	1.001	2.967	14.835	17.356	0.166	-1.381	-1.306	-0.013
60	A	61	MET	0	0.008	-0.012	2.465	-16.603	-13.843	3.338	-2.915	-3.182	-0.036
61	A	62	ASP	-1	-0.827	-0.914	2.467	-58.964	-56.623	3.257	-2.543	-3.056	-0.033
62	A	63	ILE	0	-0.051	-0.019	1.859	-41.536	-40.739	10.135	-4.897	-6.034	-0.057
63	A	64	TYR	0	-0.042	-0.058	1.989	10.471	10.941	4.471	-2.215	-2.726	-0.024
64	A	65	THR	0	0.009	0.001	5.338	0.296	0.306	-0.001	0.000	-0.009	0.000
83	A	85	ILE	0	-0.011	0.004	3.367	-0.901	-0.533	0.014	-0.114	-0.268	-0.001
85	A	89	ASP	-1	-0.722	-0.813	3.311	-65.034	-64.115	0.008	-0.556	-0.371	-0.004
6	A	6	GLU	-1	-0.745	-0.840	5.533	-18.560	-18.560	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.894	0.943	6.873	29.276	29.276	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.016	0.006	6.656	3.566	3.566	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.039	0.024	9.520	2.806	2.806	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.974	1.011	11.597	20.392	20.392	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.863	0.944	11.900	22.934	22.934	0.000	0.000	0.000	0.000
12	A	12	MET	0	0.007	0.016	12.828	1.188	1.188	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.008	-0.013	15.212	1.425	1.425	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.006	0.009	16.913	0.916	0.916	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.796	0.914	17.138	15.803	15.803	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.042	-0.043	12.987	-0.821	-0.821	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.083	0.014	11.792	0.907	0.907	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.009	-0.023	9.670	1.039	1.039	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.020	0.016	13.139	0.927	0.927	0.000	0.000	0.000	0.000
20	A	20	TRP	0	-0.026	-0.010	16.348	0.943	0.943	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.050	0.029	13.720	0.948	0.948	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.026	-0.017	13.622	-0.521	-0.521	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.004	-0.007	14.583	0.001	0.001	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.076	-0.070	17.890	0.798	0.798	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.029	0.023	19.046	-0.465	-0.465	0.000	0.000	0.000	0.000
26	A	26	CYS	0	-0.118	-0.067	21.310	0.309	0.309	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.022	-0.044	16.576	-0.289	-0.289	0.000	0.000	0.000	0.000
28	A	28	CYS	0	-0.116	-0.012	13.941	-2.465	-2.465	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.036	0.017	13.031	1.011	1.011	0.000	0.000	0.000	0.000
30	A	30	TRP	0	-0.028	-0.011	13.192	-0.597	-0.597	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.013	0.010	14.672	1.237	1.237	0.000	0.000	0.000	0.000
32	A	32	GLY	0	0.048	0.018	16.488	-0.479	-0.479	0.000	0.000	0.000	0.000
33	A	33	GLN	0	-0.054	-0.020	18.235	0.675	0.675	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.090	0.055	21.754	0.087	0.087	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.917	0.966	23.582	9.959	9.959	0.000	0.000	0.000	0.000
36	A	36	PRO	0	-0.006	-0.007	21.073	0.127	0.127	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.876	0.928	23.039	12.333	12.333	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.755	-0.847	22.451	-13.188	-13.188	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.045	0.019	22.459	-0.434	-0.434	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.001	-0.004	17.815	-0.879	-0.879	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.734	-0.882	17.857	-16.049	-16.049	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.820	0.888	18.605	12.895	12.895	0.000	0.000	0.000	0.000
43	A	43	CYS	0	0.014	0.031	14.996	1.094	1.094	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.059	0.038	14.321	-1.262	-1.262	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.034	0.011	14.813	-0.453	-0.453	0.000	0.000	0.000	0.000
46	A	47	HIS	0	-0.092	-0.047	6.933	1.798	1.798	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.881	-0.945	11.425	-24.492	-24.492	0.000	0.000	0.000	0.000
48	A	123	CYS	-1	-0.932	-0.967	12.844	-15.211	-15.211	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.101	-0.023	7.584	2.398	2.398	0.000	0.000	0.000	0.000
50	A	51	TYR	0	-0.040	-0.083	4.939	-1.648	-1.648	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.009	0.002	10.322	-0.284	-0.284	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.962	0.984	13.272	18.911	18.911	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.061	-0.018	8.412	0.107	0.107	0.000	0.000	0.000	0.000
54	A	55	THR	0	0.014	0.005	11.769	0.577	0.577	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.021	0.006	13.237	0.366	0.366	0.000	0.000	0.000	0.000
56	A	57	CYS	0	-0.062	0.004	7.901	-2.135	-2.135	0.000	0.000	0.000	0.000
57	A	58	ASN	0	0.071	0.026	6.476	-1.606	-1.606	0.000	0.000	0.000	0.000
58	A	59	PRO	0	0.051	0.018	4.964	-9.364	-9.364	0.000	0.000	0.000	0.000
65	A	66	TYR	0	-0.042	-0.025	5.929	-0.265	-0.265	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.009	-0.002	9.949	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	68	VAL	0	-0.052	-0.051	12.633	-0.990	-0.990	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.779	-0.864	14.931	-16.672	-16.672	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.006	-0.019	18.363	0.129	0.129	0.000	0.000	0.000	0.000
70	A	71	GLY	0	0.015	0.014	18.240	0.406	0.406	0.000	0.000	0.000	0.000
71	A	72	ASN	0	-0.046	-0.014	16.771	-0.817	-0.817	0.000	0.000	0.000	0.000
72	A	73	ILE	0	0.005	0.004	9.829	-0.446	-0.446	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.016	0.020	13.127	-0.133	-0.133	0.000	0.000	0.000	0.000
74	A	75	CYS	0	-0.035	-0.003	5.526	-1.320	-1.320	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.027	0.010	11.124	2.115	2.115	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.011	-0.005	11.125	-2.194	-2.194	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.032	0.005	12.698	0.075	0.075	0.000	0.000	0.000	0.000
78	A	79	ASN	0	0.015	0.017	10.564	-0.182	-0.182	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.082	0.023	11.047	-2.280	-2.280	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.909	0.935	6.337	39.283	39.283	0.000	0.000	0.000	0.000
81	A	83	LYS	1	0.860	0.942	6.724	18.170	18.170	0.000	0.000	0.000	0.000
82	A	84	GLN	0	0.053	0.028	8.942	-1.415	-1.415	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.932	-0.983	6.324	-20.664	-20.664	0.000	0.000	0.000	0.000
86	A	90	ARG	1	0.902	0.932	6.993	26.412	26.412	0.000	0.000	0.000	0.000
87	A	91	ALA	0	0.003	0.010	9.703	2.235	2.235	0.000	0.000	0.000	0.000
88	A	92	ALA	0	0.027	0.017	10.062	1.806	1.806	0.000	0.000	0.000	0.000
89	A	93	ALA	0	-0.012	-0.010	10.246	1.643	1.643	0.000	0.000	0.000	0.000
90	A	94	ILE	0	-0.022	-0.019	12.157	1.449	1.449	0.000	0.000	0.000	0.000
91	A	96	PHE	0	0.002	-0.023	11.586	0.911	0.911	0.000	0.000	0.000	0.000
92	A	97	ARG	1	0.866	0.931	16.643	16.249	16.249	0.000	0.000	0.000	0.000
93	A	98	ASP	-1	-0.896	-0.942	18.457	-14.244	-14.244	0.000	0.000	0.000	0.000
94	A	99	ASN	0	-0.026	-0.025	19.769	1.332	1.332	0.000	0.000	0.000	0.000
95	A	100	LEU	0	-0.004	0.002	19.306	0.413	0.413	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.889	0.936	22.367	11.534	11.534	0.000	0.000	0.000	0.000
97	A	102	THR	0	-0.029	-0.015	24.208	0.400	0.400	0.000	0.000	0.000	0.000
98	A	103	TYR	0	-0.013	-0.020	19.454	0.128	0.128	0.000	0.000	0.000	0.000
99	A	104	ASP	-1	-0.769	-0.871	23.786	-10.474	-10.474	0.000	0.000	0.000	0.000
100	A	105	SER	0	-0.021	-0.024	23.716	0.075	0.075	0.000	0.000	0.000	0.000
101	A	106	LYS	1	0.876	0.940	25.140	10.661	10.661	0.000	0.000	0.000	0.000
102	A	107	THR	0	-0.015	-0.011	28.118	0.331	0.331	0.000	0.000	0.000	0.000
103	A	108	TYR	0	0.001	-0.009	23.422	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	109	TRP	0	0.039	0.010	20.146	-0.299	-0.299	0.000	0.000	0.000	0.000
105	A	110	LYS	1	0.869	0.941	21.665	13.340	13.340	0.000	0.000	0.000	0.000
106	A	111	TYR	0	0.020	0.023	22.915	0.540	0.540	0.000	0.000	0.000	0.000
107	A	112	PRO	0	0.001	0.011	23.118	-0.435	-0.435	0.000	0.000	0.000	0.000
108	A	113	LYS	1	0.853	0.904	17.053	17.627	17.627	0.000	0.000	0.000	0.000
109	A	114	LYS	1	0.945	0.977	23.706	10.053	10.053	0.000	0.000	0.000	0.000
110	A	115	ASN	0	-0.047	-0.028	27.141	0.427	0.427	0.000	0.000	0.000	0.000
111	A	117	LYS	1	0.925	0.966	25.859	10.916	10.916	0.000	0.000	0.000	0.000
112	A	118	GLU	-1	-0.810	-0.906	28.092	-9.481	-9.481	0.000	0.000	0.000	0.000
113	A	119	GLU	-1	-0.947	-0.966	27.918	-10.191	-10.191	0.000	0.000	0.000	0.000
114	A	120	SER	0	-0.033	-0.023	23.350	-0.248	-0.248	0.000	0.000	0.000	0.000
115	A	121	GLU	-1	-0.852	-0.873	23.482	-12.672	-12.672	0.000	0.000	0.000	0.000
116	A	122	PRO	0	-0.024	-0.015	23.013	-0.503	-0.503	0.000	0.000	0.000	0.000

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