FMO DATABASE

FMODB ID: JKJ29

Calculation Name: 1VHX-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VHX

Chain ID: A

ChEMBL ID:

UniProt ID: O34634

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1205408.74501
FMO2-HF: Nuclear repulsion	1150984.014504
FMO2-HF: Total energy	-54424.730506
FMO2-MP2: Total energy	-54581.761846

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:0:SER)

Summations of interaction energy for fragment #1(A:0:SER)

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.
-204.048	-201.581	25.017	-13.565	-13.917	-0.127

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.777 / q_NPA : 0.879

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	2	ARG	1	0.778	0.891	1.873	36.121	37.778	7.475	-4.775	-4.356	-0.035
4	A	3	ILE	0	0.064	0.041	4.323	4.469	4.584	-0.001	-0.043	-0.071	0.000
21	A	20	GLU	-1	-0.807	-0.909	1.855	-122.917	-123.010	17.542	-8.563	-8.885	-0.092
22	A	21	MET	0	-0.062	-0.032	3.900	-3.371	-3.018	0.003	-0.019	-0.337	0.000
53	A	52	TYR	0	-0.062	-0.033	4.634	-6.306	-6.157	-0.001	-0.012	-0.136	0.000
54	A	53	THR	0	-0.031	-0.011	4.088	3.362	3.725	0.000	-0.141	-0.222	0.000
55	A	54	ILE	0	-0.005	-0.013	5.748	-6.190	-6.267	-0.001	-0.012	0.090	0.000
5	A	4	LEU	0	0.016	0.003	7.908	0.157	0.157	0.000	0.000	0.000	0.000
6	A	5	GLY	0	0.025	0.014	10.773	1.285	1.285	0.000	0.000	0.000	0.000
7	A	6	LEU	0	-0.030	-0.016	13.904	0.238	0.238	0.000	0.000	0.000	0.000
8	A	7	ASP	-1	-0.908	-0.963	17.383	-12.817	-12.817	0.000	0.000	0.000	0.000
9	A	8	LEU	0	0.045	0.029	21.016	0.015	0.015	0.000	0.000	0.000	0.000
10	A	9	GLY	0	0.031	0.019	24.044	0.580	0.580	0.000	0.000	0.000	0.000
11	A	10	THR	0	-0.022	-0.028	27.133	-0.114	-0.114	0.000	0.000	0.000	0.000
12	A	11	LYS	1	0.841	0.905	29.460	9.723	9.723	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.013	-0.018	24.872	0.161	0.161	0.000	0.000	0.000	0.000
14	A	13	LEU	0	0.020	0.035	19.795	0.250	0.250	0.000	0.000	0.000	0.000
15	A	14	GLY	0	-0.035	-0.009	20.203	-0.282	-0.282	0.000	0.000	0.000	0.000
16	A	15	VAL	0	0.019	-0.008	14.033	-0.201	-0.201	0.000	0.000	0.000	0.000
17	A	16	ALA	0	0.000	-0.005	13.419	0.406	0.406	0.000	0.000	0.000	0.000
18	A	17	LEU	0	0.040	0.026	6.989	-0.302	-0.302	0.000	0.000	0.000	0.000
19	A	18	SER	0	0.037	0.030	5.016	2.060	2.060	0.000	0.000	0.000	0.000
20	A	19	ASP	-1	-0.767	-0.853	6.614	-33.444	-33.444	0.000	0.000	0.000	0.000
23	A	22	GLY	0	0.008	0.025	6.076	1.173	1.173	0.000	0.000	0.000	0.000
24	A	23	TRP	0	-0.027	-0.001	7.184	2.750	2.750	0.000	0.000	0.000	0.000
25	A	24	THR	0	-0.041	-0.056	10.028	2.006	2.006	0.000	0.000	0.000	0.000
26	A	25	ALA	0	0.011	0.004	9.982	-2.360	-2.360	0.000	0.000	0.000	0.000
27	A	26	GLN	0	-0.008	-0.013	9.065	0.008	0.008	0.000	0.000	0.000	0.000
28	A	27	GLY	0	0.000	-0.015	12.487	-0.223	-0.223	0.000	0.000	0.000	0.000
29	A	28	ILE	0	-0.044	-0.007	10.561	-0.270	-0.270	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.770	-0.873	14.580	-15.675	-15.675	0.000	0.000	0.000	0.000
31	A	30	THR	0	-0.094	-0.051	17.990	0.325	0.325	0.000	0.000	0.000	0.000
32	A	31	ILE	0	0.040	0.044	18.139	0.671	0.671	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.859	0.925	22.038	11.804	11.804	0.000	0.000	0.000	0.000
34	A	33	ILE	0	0.044	0.057	24.270	-0.152	-0.152	0.000	0.000	0.000	0.000
35	A	34	ASN	0	-0.096	-0.084	27.201	0.717	0.717	0.000	0.000	0.000	0.000
36	A	35	GLU	-1	-0.700	-0.833	29.735	-10.420	-10.420	0.000	0.000	0.000	0.000
37	A	36	ALA	0	-0.071	-0.019	31.836	0.161	0.161	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.892	-0.922	32.404	-9.348	-9.348	0.000	0.000	0.000	0.000
39	A	38	GLY	0	-0.010	0.001	31.850	-0.059	-0.059	0.000	0.000	0.000	0.000
40	A	39	ASP	-1	-0.883	-0.936	26.531	-12.401	-12.401	0.000	0.000	0.000	0.000
41	A	40	TYR	0	-0.003	-0.024	25.125	0.174	0.174	0.000	0.000	0.000	0.000
42	A	41	GLY	0	0.028	-0.008	22.649	-0.563	-0.563	0.000	0.000	0.000	0.000
43	A	42	LEU	0	0.039	0.015	20.553	-0.606	-0.606	0.000	0.000	0.000	0.000
44	A	43	SER	0	-0.006	0.012	19.700	-0.833	-0.833	0.000	0.000	0.000	0.000
45	A	44	ARG	1	0.822	0.890	17.816	16.303	16.303	0.000	0.000	0.000	0.000
46	A	45	LEU	0	0.019	-0.004	15.124	-0.791	-0.791	0.000	0.000	0.000	0.000
47	A	46	SER	0	0.018	-0.003	15.094	-1.515	-1.515	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.942	-0.969	14.579	-17.386	-17.386	0.000	0.000	0.000	0.000
49	A	48	LEU	0	-0.046	-0.023	13.586	-1.345	-1.345	0.000	0.000	0.000	0.000
50	A	49	ILE	0	0.005	-0.003	10.386	-1.996	-1.996	0.000	0.000	0.000	0.000
51	A	50	LYS	1	0.924	0.978	9.531	17.923	17.923	0.000	0.000	0.000	0.000
52	A	51	ASP	-1	-0.950	-0.963	8.632	-26.405	-26.405	0.000	0.000	0.000	0.000
56	A	55	ASP	-1	-0.895	-0.954	7.420	-33.160	-33.160	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.919	0.961	9.150	26.501	26.501	0.000	0.000	0.000	0.000
58	A	57	ILE	0	0.011	0.007	10.590	-1.586	-1.586	0.000	0.000	0.000	0.000
59	A	58	VAL	0	-0.004	0.013	12.825	1.168	1.168	0.000	0.000	0.000	0.000
60	A	59	LEU	0	-0.030	-0.015	15.270	-0.186	-0.186	0.000	0.000	0.000	0.000
61	A	60	GLY	0	0.003	-0.002	18.709	0.438	0.438	0.000	0.000	0.000	0.000
62	A	61	PHE	0	-0.024	-0.017	21.221	0.345	0.345	0.000	0.000	0.000	0.000
63	A	62	PRO	0	-0.048	-0.014	24.326	0.188	0.188	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.842	0.893	27.584	10.926	10.926	0.000	0.000	0.000	0.000
65	A	64	ASN	0	0.039	0.016	29.748	0.130	0.130	0.000	0.000	0.000	0.000
66	A	65	MET	0	-0.024	-0.007	32.251	0.036	0.036	0.000	0.000	0.000	0.000
67	A	66	ASN	0	-0.012	-0.020	35.652	0.046	0.046	0.000	0.000	0.000	0.000
68	A	67	GLY	0	0.036	0.024	34.157	0.155	0.155	0.000	0.000	0.000	0.000
69	A	68	THR	0	-0.029	-0.004	34.905	-0.039	-0.039	0.000	0.000	0.000	0.000
70	A	69	VAL	0	0.004	0.014	30.848	-0.127	-0.127	0.000	0.000	0.000	0.000
71	A	70	GLY	0	0.046	0.024	32.763	0.268	0.268	0.000	0.000	0.000	0.000
72	A	71	PRO	0	0.012	-0.014	32.649	-0.280	-0.280	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.817	0.876	28.044	10.552	10.552	0.000	0.000	0.000	0.000
74	A	73	GLY	0	0.061	0.056	28.494	-0.425	-0.425	0.000	0.000	0.000	0.000
75	A	74	GLU	-1	-0.781	-0.885	28.280	-10.792	-10.792	0.000	0.000	0.000	0.000
76	A	75	ALA	0	-0.012	-0.003	29.151	-0.223	-0.223	0.000	0.000	0.000	0.000
77	A	76	SER	0	0.025	-0.003	24.420	-0.474	-0.474	0.000	0.000	0.000	0.000
78	A	77	GLN	0	-0.063	-0.039	24.287	-0.665	-0.665	0.000	0.000	0.000	0.000
79	A	78	THR	0	-0.064	-0.038	25.616	-0.226	-0.226	0.000	0.000	0.000	0.000
80	A	79	PHE	0	0.017	0.000	20.529	-0.274	-0.274	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.035	0.013	21.059	-0.566	-0.566	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.939	0.974	21.426	10.464	10.464	0.000	0.000	0.000	0.000
83	A	82	VAL	0	0.001	0.023	22.778	-0.195	-0.195	0.000	0.000	0.000	0.000
84	A	83	LEU	0	-0.009	0.008	17.545	-0.486	-0.486	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.938	-0.968	18.393	-15.648	-15.648	0.000	0.000	0.000	0.000
86	A	85	THR	0	-0.072	-0.064	19.363	-0.360	-0.360	0.000	0.000	0.000	0.000
87	A	86	THR	0	-0.086	-0.044	18.676	0.280	0.280	0.000	0.000	0.000	0.000
88	A	87	TYR	0	-0.059	-0.057	14.703	-0.350	-0.350	0.000	0.000	0.000	0.000
89	A	88	ASN	0	-0.050	-0.010	15.228	-0.527	-0.527	0.000	0.000	0.000	0.000
90	A	89	VAL	0	0.001	0.012	11.703	-0.822	-0.822	0.000	0.000	0.000	0.000
91	A	90	PRO	0	0.004	-0.005	13.612	1.050	1.050	0.000	0.000	0.000	0.000
92	A	91	VAL	0	-0.001	0.007	14.891	-1.143	-1.143	0.000	0.000	0.000	0.000
93	A	92	VAL	0	-0.035	-0.013	15.570	0.964	0.964	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.016	-0.007	17.857	-0.178	-0.178	0.000	0.000	0.000	0.000
95	A	94	TRP	0	0.001	-0.009	18.588	0.023	0.023	0.000	0.000	0.000	0.000
96	A	95	ASP	-1	-0.801	-0.900	20.655	-11.138	-11.138	0.000	0.000	0.000	0.000
97	A	96	GLU	-1	-0.872	-0.905	21.033	-13.022	-13.022	0.000	0.000	0.000	0.000
98	A	97	ARG	1	0.943	0.966	20.359	12.092	12.092	0.000	0.000	0.000	0.000
99	A	98	LEU	0	0.050	0.031	21.857	0.731	0.731	0.000	0.000	0.000	0.000
100	A	99	THR	0	0.039	0.019	23.925	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	100	THR	0	0.036	0.002	26.903	-0.067	-0.067	0.000	0.000	0.000	0.000
102	A	101	MET	0	0.014	0.010	28.703	0.214	0.214	0.000	0.000	0.000	0.000
103	A	102	ALA	0	0.017	0.013	28.024	0.280	0.280	0.000	0.000	0.000	0.000
104	A	103	ALA	0	0.050	0.027	26.645	0.095	0.095	0.000	0.000	0.000	0.000
105	A	104	GLU	-1	-0.776	-0.881	28.533	-8.919	-8.919	0.000	0.000	0.000	0.000
106	A	105	LYS	1	0.911	0.950	32.047	8.892	8.892	0.000	0.000	0.000	0.000
107	A	106	MET	0	0.025	0.013	26.781	0.116	0.116	0.000	0.000	0.000	0.000
108	A	107	LEU	0	-0.018	-0.008	28.153	0.026	0.026	0.000	0.000	0.000	0.000
109	A	108	ILE	0	-0.075	-0.046	31.818	0.196	0.196	0.000	0.000	0.000	0.000
110	A	109	ALA	0	-0.029	-0.012	33.933	0.193	0.193	0.000	0.000	0.000	0.000
111	A	110	ALA	0	0.006	0.015	32.100	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	111	ASP	-1	-0.891	-0.928	34.050	-8.261	-8.261	0.000	0.000	0.000	0.000
113	A	112	VAL	0	-0.062	-0.019	31.188	0.026	0.026	0.000	0.000	0.000	0.000
114	A	113	SER	0	0.046	0.011	34.552	0.067	0.067	0.000	0.000	0.000	0.000
115	A	114	ARG	1	1.020	1.000	35.109	7.652	7.652	0.000	0.000	0.000	0.000
116	A	115	GLN	0	0.013	0.000	35.096	-0.419	-0.419	0.000	0.000	0.000	0.000
117	A	116	LYS	1	0.981	0.988	30.611	9.819	9.819	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.837	0.888	30.720	8.439	8.439	0.000	0.000	0.000	0.000
119	A	118	LYS	1	0.853	0.906	30.012	9.733	9.733	0.000	0.000	0.000	0.000
120	A	119	LYS	1	0.922	0.959	29.226	9.357	9.357	0.000	0.000	0.000	0.000
121	A	120	VAL	0	-0.038	-0.017	26.049	-0.442	-0.442	0.000	0.000	0.000	0.000
122	A	121	ILE	0	0.013	0.005	25.115	-0.456	-0.456	0.000	0.000	0.000	0.000
123	A	122	ASP	-1	-0.844	-0.891	25.428	-10.860	-10.860	0.000	0.000	0.000	0.000
124	A	123	LYS	1	0.937	0.967	22.272	12.614	12.614	0.000	0.000	0.000	0.000
125	A	124	MET	0	0.004	0.003	19.245	-0.575	-0.575	0.000	0.000	0.000	0.000
126	A	125	ALA	0	-0.003	0.024	20.402	-0.463	-0.463	0.000	0.000	0.000	0.000
127	A	126	ALA	0	0.066	0.023	17.149	-0.085	-0.085	0.000	0.000	0.000	0.000
128	A	127	VAL	0	0.012	0.012	15.689	-0.645	-0.645	0.000	0.000	0.000	0.000
129	A	128	MET	0	-0.063	-0.034	16.654	-0.009	-0.009	0.000	0.000	0.000	0.000
130	A	129	ILE	0	-0.039	-0.018	17.043	0.196	0.196	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.013	0.008	10.426	0.178	0.178	0.000	0.000	0.000	0.000
132	A	131	GLN	0	-0.047	-0.040	13.863	-1.295	-1.295	0.000	0.000	0.000	0.000
133	A	132	GLY	0	0.029	0.018	15.322	-0.015	-0.015	0.000	0.000	0.000	0.000
134	A	133	TYR	0	0.013	0.006	12.005	-0.456	-0.456	0.000	0.000	0.000	0.000
135	A	134	LEU	0	-0.033	-0.027	9.320	-0.607	-0.607	0.000	0.000	0.000	0.000
136	A	135	ASP	-1	-0.861	-0.918	13.003	-16.767	-16.767	0.000	0.000	0.000	0.000
137	A	136	SER	0	-0.042	-0.040	16.215	0.182	0.182	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.113	-0.048	10.573	-0.011	-0.011	0.000	0.000	0.000	0.000
139	A	138	ASN	0	-0.123	-0.085	11.287	-1.186	-1.186	0.000	0.000	0.000	0.000
140	A	139	GLU	-2	-1.918	-1.924	14.725	-28.791	-28.791	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)