FMO DATABASE

FMODB ID: J4LN9

Calculation Name: 1VJQ-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VJQ

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-07-14

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-447599.351882
FMO2-HF: Nuclear repulsion	418949.598262
FMO2-HF: Total energy	-28649.75362
FMO2-MP2: Total energy	-28733.610996

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:LYS)

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

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.
0.175	-0.266	3.865	1.253	-4.671	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.148 / q_NPA : 0.043

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].
4	A	2	THR	0	-0.028	0.045	4.011	0.459	0.974	0.000	-0.244	-0.270	0.001
5	A	3	ILE	0	0.103	-0.074	3.838	-1.989	0.246	-0.018	-1.344	-0.872	0.005
6	A	3	ILE	0	-0.088	0.092	4.445	0.036	0.094	-0.001	-0.007	-0.049	0.000
7	A	4	PHE	0	0.061	-0.091	6.180	-0.007	-0.007	0.000	0.000	0.000	0.000
8	A	4	PHE	0	-0.064	0.091	7.590	0.045	0.045	0.000	0.000	0.000	0.000
9	A	5	VAL	0	0.121	-0.083	9.633	0.096	0.096	0.000	0.000	0.000	0.000
10	A	5	VAL	0	-0.128	0.099	11.082	0.013	0.013	0.000	0.000	0.000	0.000
11	A	6	ILE	0	0.110	-0.111	12.494	-0.025	-0.025	0.000	0.000	0.000	0.000
12	A	6	ILE	0	-0.070	0.102	11.927	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	7	VAL	0	0.056	-0.101	15.005	0.043	0.043	0.000	0.000	0.000	0.000
14	A	7	VAL	0	-0.121	0.112	18.475	0.002	0.002	0.000	0.000	0.000	0.000
15	A	8	PRO	0	0.043	-0.091	18.451	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	9	THR	0	0.025	0.013	21.080	0.019	0.019	0.000	0.000	0.000	0.000
17	A	9	THR	0	-0.059	0.062	22.973	0.003	0.003	0.000	0.000	0.000	0.000
18	A	10	ASN	0	0.092	-0.058	24.628	0.012	0.012	0.000	0.000	0.000	0.000
19	A	10	ASN	0	-0.085	0.052	25.718	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	11	GLU	0	0.156	-0.104	24.997	-0.012	-0.012	0.000	0.000	0.000	0.000
21	A	11	GLU	-1	-0.892	-0.820	27.291	-0.070	-0.070	0.000	0.000	0.000	0.000
22	A	12	GLU	0	-0.006	-0.106	25.717	0.004	0.004	0.000	0.000	0.000	0.000
23	A	12	GLU	-1	-0.924	-0.836	26.845	-0.113	-0.113	0.000	0.000	0.000	0.000
24	A	13	GLN	0	0.057	-0.107	22.539	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	13	GLN	0	-0.037	0.105	21.523	0.002	0.002	0.000	0.000	0.000	0.000
26	A	14	VAL	0	0.068	-0.124	20.944	-0.027	-0.027	0.000	0.000	0.000	0.000
27	A	14	VAL	0	-0.023	0.146	22.011	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	15	ALA	0	0.127	-0.072	21.286	0.001	0.001	0.000	0.000	0.000	0.000
29	A	15	ALA	0	-0.099	0.103	25.067	0.002	0.002	0.000	0.000	0.000	0.000
30	A	16	PHE	0	0.063	-0.081	21.495	0.011	0.011	0.000	0.000	0.000	0.000
31	A	16	PHE	0	-0.079	0.061	17.867	0.004	0.004	0.000	0.000	0.000	0.000
32	A	17	LEU	0	0.030	-0.122	17.463	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	17	LEU	0	-0.053	0.101	15.458	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	18	GLU	0	0.114	-0.109	17.389	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	18	GLU	-1	-0.946	-0.798	20.750	-0.035	-0.035	0.000	0.000	0.000	0.000
36	A	19	ALA	0	0.103	-0.081	19.493	0.027	0.027	0.000	0.000	0.000	0.000
37	A	19	ALA	0	-0.101	0.087	20.945	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	20	LEU	0	0.017	-0.105	16.086	0.029	0.029	0.000	0.000	0.000	0.000
39	A	20	LEU	0	-0.080	0.077	14.963	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	21	ALA	0	0.141	-0.064	14.774	0.000	0.000	0.000	0.000	0.000	0.000
41	A	21	ALA	0	-0.068	0.100	15.575	0.004	0.004	0.000	0.000	0.000	0.000
42	A	22	LYS	0	0.035	-0.076	15.827	0.045	0.045	0.000	0.000	0.000	0.000
43	A	22	LYS	1	0.694	0.951	20.133	0.032	0.032	0.000	0.000	0.000	0.000
44	A	23	GLN	0	-0.017	-0.116	17.060	0.036	0.036	0.000	0.000	0.000	0.000
45	A	23	GLN	0	-0.147	0.038	16.070	0.006	0.006	0.000	0.000	0.000	0.000
46	A	24	ASP	0	0.161	-0.080	14.899	-0.028	-0.028	0.000	0.000	0.000	0.000
47	A	24	ASP	-1	-1.048	-0.864	14.719	0.232	0.232	0.000	0.000	0.000	0.000
48	A	25	GLU	0	0.082	-0.128	12.948	0.035	0.035	0.000	0.000	0.000	0.000
49	A	25	GLU	-1	-1.062	-0.861	11.668	-0.366	-0.366	0.000	0.000	0.000	0.000
50	A	26	LEU	0	0.164	-0.079	10.998	0.031	0.031	0.000	0.000	0.000	0.000
51	A	26	LEU	0	-0.143	0.080	10.398	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	27	ASN	0	-0.002	-0.067	6.966	-0.169	-0.169	0.000	0.000	0.000	0.000
53	A	27	ASN	0	-0.120	0.024	5.898	0.298	0.298	0.000	0.000	0.000	0.000
54	A	28	PHE	0	0.207	-0.062	5.770	-0.222	-0.222	0.000	0.000	0.000	0.000
55	A	28	PHE	0	-0.139	0.079	9.079	-0.146	-0.146	0.000	0.000	0.000	0.000
56	A	29	ASP	0	0.145	-0.084	6.751	-0.082	-0.082	0.000	0.000	0.000	0.000
57	A	29	ASP	-1	-1.025	-0.848	6.385	1.257	1.257	0.000	0.000	0.000	0.000
58	A	30	TRP	0	0.059	-0.107	8.062	-0.078	-0.078	0.000	0.000	0.000	0.000
59	A	30	TRP	0	-0.041	0.105	11.903	-0.067	-0.067	0.000	0.000	0.000	0.000
60	A	31	GLN	0	0.113	-0.086	10.710	0.089	0.089	0.000	0.000	0.000	0.000
61	A	31	GLN	0	-0.179	0.038	8.258	0.073	0.073	0.000	0.000	0.000	0.000
62	A	32	ASN	0	0.005	-0.086	11.503	0.043	0.043	0.000	0.000	0.000	0.000
63	A	32	ASN	0	-0.102	0.048	14.192	-0.013	-0.013	0.000	0.000	0.000	0.000
64	A	33	PRO	0	0.019	-0.091	14.841	-0.042	-0.042	0.000	0.000	0.000	0.000
65	A	34	PRO	0	0.020	-0.014	16.703	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	35	THR	0	0.018	0.065	19.143	0.018	0.018	0.000	0.000	0.000	0.000
67	A	35	THR	0	-0.090	0.025	20.945	0.000	0.000	0.000	0.000	0.000	0.000
68	A	36	GLU	0	0.114	-0.112	22.576	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	36	GLU	-1	-0.972	-0.852	25.235	-0.033	-0.033	0.000	0.000	0.000	0.000
70	A	37	PRO	0	-0.057	-0.114	23.161	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	38	GLY	0	-0.034	-0.027	23.426	0.012	0.012	0.000	0.000	0.000	0.000
72	A	39	GLN	0	0.047	-0.037	21.104	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	39	GLN	0	-0.103	0.112	20.812	0.000	0.000	0.000	0.000	0.000	0.000
74	A	40	PRO	0	-0.029	-0.117	16.126	-0.015	-0.015	0.000	0.000	0.000	0.000
75	A	41	VAL	0	0.089	-0.002	15.047	0.059	0.059	0.000	0.000	0.000	0.000
76	A	41	VAL	0	-0.092	0.116	13.710	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	42	VAL	0	0.094	-0.080	11.201	-0.108	-0.108	0.000	0.000	0.000	0.000
78	A	42	VAL	0	-0.100	0.091	9.037	0.006	0.006	0.000	0.000	0.000	0.000
79	A	43	ILE	0	0.117	-0.087	8.591	0.207	0.207	0.000	0.000	0.000	0.000
80	A	43	ILE	0	-0.094	0.101	7.583	-0.028	-0.028	0.000	0.000	0.000	0.000
81	A	44	LEU	0	0.055	-0.116	4.609	-0.606	-0.589	-0.002	-0.010	-0.005	0.000
82	A	44	LEU	0	-0.081	0.099	2.055	0.015	-0.692	2.829	-0.949	-1.173	0.001
83	A	45	ILE	0	0.020	-0.064	3.631	0.511	0.810	0.002	-0.104	-0.197	-0.001
84	A	45	ILE	0	-0.040	0.099	5.352	0.054	0.054	0.000	0.000	0.000	0.000
85	A	46	PRO	0	0.048	-0.098	2.534	-4.279	-3.974	0.800	0.116	-1.220	-0.016
86	A	47	SER	0	0.107	0.021	2.694	3.499	0.777	0.251	2.752	-0.281	0.002
87	A	47	SER	0	0.000	0.073	3.383	-0.822	-1.712	0.005	1.108	-0.223	-0.001
88	A	48	ASP	0	-0.031	-0.095	4.273	0.780	0.862	0.000	0.021	-0.102	0.000
89	A	48	ASP	-1	-0.907	-0.837	6.416	-2.096	-2.096	0.000	0.000	0.000	0.000
90	A	49	MET	0	0.028	-0.137	6.841	0.481	0.481	0.000	0.000	0.000	0.000
91	A	49	MET	0	-0.060	0.133	7.729	0.120	0.120	0.000	0.000	0.000	0.000
92	A	50	VAL	0	0.124	-0.095	7.905	0.352	0.352	0.000	0.000	0.000	0.000
93	A	50	VAL	0	-0.106	0.117	6.485	-0.040	-0.040	0.000	0.000	0.000	0.000
94	A	51	GLU	0	0.088	-0.099	9.114	0.182	0.182	0.000	0.000	0.000	0.000
95	A	51	GLU	-1	-1.026	-0.870	12.256	-0.779	-0.779	0.000	0.000	0.000	0.000
96	A	52	TRP	0	0.104	-0.086	12.474	0.110	0.110	0.000	0.000	0.000	0.000
97	A	52	TRP	0	-0.073	0.081	11.601	0.015	0.015	0.000	0.000	0.000	0.000
98	A	53	PHE	0	0.100	-0.099	11.025	0.188	0.188	0.000	0.000	0.000	0.000
99	A	53	PHE	0	-0.059	0.105	10.523	-0.032	-0.032	0.000	0.000	0.000	0.000
100	A	54	LEU	0	0.106	-0.091	12.509	0.122	0.122	0.000	0.000	0.000	0.000
101	A	54	LEU	0	-0.103	0.085	12.364	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	55	GLU	0	0.037	-0.117	14.016	0.087	0.087	0.000	0.000	0.000	0.000
103	A	55	GLU	-1	-0.835	-0.767	16.849	-0.508	-0.508	0.000	0.000	0.000	0.000
104	A	56	MET	0	0.111	-0.081	16.170	0.083	0.083	0.000	0.000	0.000	0.000
105	A	56	MET	0	-0.105	0.099	14.171	0.027	0.027	0.000	0.000	0.000	0.000
106	A	57	LEU	0	0.021	-0.136	15.958	0.081	0.081	0.000	0.000	0.000	0.000
107	A	57	LEU	0	-0.050	0.116	13.038	0.009	0.009	0.000	0.000	0.000	0.000
108	A	58	LYS	0	0.102	-0.104	17.220	0.057	0.057	0.000	0.000	0.000	0.000
109	A	58	LYS	1	0.707	0.977	18.217	0.479	0.479	0.000	0.000	0.000	0.000
110	A	59	ALA	0	0.089	-0.069	19.701	0.042	0.042	0.000	0.000	0.000	0.000
111	A	59	ALA	0	-0.101	0.096	20.878	0.001	0.001	0.000	0.000	0.000	0.000
112	A	60	LYS	0	-0.015	-0.120	20.628	0.034	0.034	0.000	0.000	0.000	0.000
113	A	60	LYS	1	0.779	1.032	20.267	0.232	0.232	0.000	0.000	0.000	0.000
114	A	61	GLY	0	-0.006	-0.128	21.974	0.027	0.027	0.000	0.000	0.000	0.000
115	A	62	ILE	0	0.021	-0.028	19.232	0.035	0.035	0.000	0.000	0.000	0.000
116	A	62	ILE	0	-0.088	0.098	18.247	0.002	0.002	0.000	0.000	0.000	0.000
117	A	63	PRO	0	-0.007	-0.104	18.551	-0.045	-0.045	0.000	0.000	0.000	0.000
118	A	64	PHE	0	0.058	0.029	14.945	0.033	0.033	0.000	0.000	0.000	0.000
119	A	64	PHE	0	-0.045	0.095	13.717	-0.031	-0.031	0.000	0.000	0.000	0.000
120	A	65	THR	0	-0.028	-0.070	14.166	0.017	0.017	0.000	0.000	0.000	0.000
121	A	65	THR	0	-0.057	0.046	14.358	-0.018	-0.018	0.000	0.000	0.000	0.000
122	A	66	VAL	0	0.146	-0.085	10.415	0.026	0.026	0.000	0.000	0.000	0.000
123	A	66	VAL	0	-0.062	0.104	8.990	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	67	TYR	0	0.019	-0.117	8.841	0.131	0.131	0.000	0.000	0.000	0.000
125	A	67	TYR	0	-0.099	0.100	8.676	0.084	0.084	0.000	0.000	0.000	0.000
126	A	68	VAL	0	0.099	-0.100	6.486	-0.517	-0.517	0.000	0.000	0.000	0.000
127	A	68	VAL	0	-0.051	0.110	7.282	0.002	0.002	0.000	0.000	0.000	0.000
128	A	69	GLU	0	0.179	-0.095	5.252	0.188	0.238	-0.002	-0.001	-0.047	0.000
129	A	69	GLU	-1	-0.978	-0.794	4.186	2.516	2.833	0.001	-0.085	-0.232	0.000
130	A	70	GLU	0	0.043	-0.131	6.403	-0.105	-0.105	0.000	0.000	0.000	0.000
131	A	70	GLU	-1	-1.004	-0.836	10.793	-0.104	-0.104	0.000	0.000	0.000	0.000
132	A	71	GLY	0	-0.055	-0.132	9.035	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	72	GLY	0	0.007	-0.002	9.810	0.124	0.124	0.000	0.000	0.000	0.000
134	A	73	SER	0	-0.111	-0.076	11.328	-0.111	-0.111	0.000	0.000	0.000	0.000
135	A	73	SER	0	0.072	0.073	13.619	0.033	0.033	0.000	0.000	0.000	0.000

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