FMO DATABASE

FMODB ID: 7MQRK

Calculation Name: 2VQC-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2VQC

Chain ID: A

ChEMBL ID:

UniProt ID: P20220

Base Structure: X-ray

Registration Date: 2025-07-09

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	OptH
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	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-467259.391615
FMO2-HF: Nuclear repulsion	437805.698027
FMO2-HF: Total energy	-29453.693587
FMO2-MP2: Total energy	-29537.869137

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:4:THR)

Summations of interaction energy for fragment #1(A:4:THR)

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.
1.014	3.814	-0.012	-1.484	-1.303	0.007

Interaction energy analysis for fragmet #1(A:4:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.085 / q_NPA : 0.018

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	5	LEU	0	-0.036	0.143	3.518	-0.368	0.239	0.006	-0.242	-0.370	0.000
5	A	6	ASN	0	0.136	-0.067	3.804	-1.273	0.920	-0.018	-1.242	-0.933	0.007
6	A	6	ASN	0	-0.117	0.068	7.222	0.326	0.326	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.084	-0.078	6.838	0.239	0.239	0.000	0.000	0.000	0.000
8	A	7	SER	0	0.007	0.078	7.107	0.146	0.146	0.000	0.000	0.000	0.000
9	A	8	TYR	0	0.151	-0.061	8.714	0.176	0.176	0.000	0.000	0.000	0.000
10	A	8	TYR	0	-0.106	0.097	12.008	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	9	LYS	0	0.127	-0.067	10.689	0.153	0.153	0.000	0.000	0.000	0.000
12	A	9	LYS	1	0.854	1.043	9.562	1.476	1.476	0.000	0.000	0.000	0.000
13	A	10	MET	0	0.019	-0.109	10.355	0.074	0.074	0.000	0.000	0.000	0.000
14	A	10	MET	0	-0.058	0.115	8.464	0.028	0.028	0.000	0.000	0.000	0.000
15	A	11	ALA	0	0.137	-0.099	11.500	0.109	0.109	0.000	0.000	0.000	0.000
16	A	11	ALA	0	-0.052	0.119	13.570	0.003	0.003	0.000	0.000	0.000	0.000
17	A	12	GLU	0	0.104	-0.108	14.221	0.089	0.089	0.000	0.000	0.000	0.000
18	A	12	GLU	-1	-0.972	-0.845	15.313	-0.617	-0.617	0.000	0.000	0.000	0.000
19	A	13	ILE	0	0.020	-0.115	15.007	0.054	0.054	0.000	0.000	0.000	0.000
20	A	13	ILE	0	-0.084	0.085	13.023	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	14	MET	0	0.007	-0.146	15.841	0.040	0.040	0.000	0.000	0.000	0.000
22	A	14	MET	0	-0.056	0.122	14.882	0.019	0.019	0.000	0.000	0.000	0.000
23	A	15	TYR	0	0.152	-0.055	17.588	0.045	0.045	0.000	0.000	0.000	0.000
24	A	15	TYR	0	-0.121	0.050	19.097	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	16	LYS	0	0.093	-0.059	20.034	0.025	0.025	0.000	0.000	0.000	0.000
26	A	16	LYS	1	0.864	1.058	19.003	0.315	0.315	0.000	0.000	0.000	0.000
27	A	17	ILE	0	0.037	-0.119	20.586	0.016	0.016	0.000	0.000	0.000	0.000
28	A	17	ILE	0	-0.065	0.091	18.672	0.000	0.000	0.000	0.000	0.000	0.000
29	A	18	LEU	0	0.084	-0.134	21.782	0.025	0.025	0.000	0.000	0.000	0.000
30	A	18	LEU	0	-0.105	0.113	21.961	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	19	GLU	0	0.127	-0.091	23.536	0.021	0.021	0.000	0.000	0.000	0.000
32	A	19	GLU	-1	-1.027	-0.848	25.504	-0.173	-0.173	0.000	0.000	0.000	0.000
33	A	20	LYS	0	0.023	-0.098	25.431	0.011	0.011	0.000	0.000	0.000	0.000
34	A	20	LYS	1	0.819	1.025	23.934	0.162	0.162	0.000	0.000	0.000	0.000
35	A	21	LYS	0	0.059	-0.086	25.712	0.010	0.010	0.000	0.000	0.000	0.000
36	A	21	LYS	1	0.841	1.062	24.035	0.046	0.046	0.000	0.000	0.000	0.000
37	A	22	GLY	0	-0.008	-0.100	26.978	0.012	0.012	0.000	0.000	0.000	0.000
38	A	23	GLU	0	0.115	-0.032	26.469	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	23	GLU	-1	-1.035	-0.858	27.188	-0.034	-0.034	0.000	0.000	0.000	0.000
40	A	24	LEU	0	-0.001	-0.132	21.899	0.003	0.003	0.000	0.000	0.000	0.000
41	A	24	LEU	0	-0.076	0.107	19.669	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	25	THR	0	0.005	-0.064	21.911	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	25	THR	0	-0.054	0.033	22.658	0.000	0.000	0.000	0.000	0.000	0.000
44	A	26	LEU	0	0.204	-0.076	18.004	-0.019	-0.019	0.000	0.000	0.000	0.000
45	A	26	LEU	0	-0.136	0.104	15.372	0.002	0.002	0.000	0.000	0.000	0.000
46	A	27	GLU	0	-0.003	-0.154	17.715	0.011	0.011	0.000	0.000	0.000	0.000
47	A	27	GLU	-1	-0.797	-0.726	21.339	0.055	0.055	0.000	0.000	0.000	0.000
48	A	28	ASP	0	0.068	-0.085	19.519	0.019	0.019	0.000	0.000	0.000	0.000
49	A	28	ASP	-1	-0.873	-0.818	20.363	-0.030	-0.030	0.000	0.000	0.000	0.000
50	A	29	ILE	0	0.116	-0.073	15.542	-0.021	-0.021	0.000	0.000	0.000	0.000
51	A	29	ILE	0	-0.123	0.059	13.578	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	30	LEU	0	0.008	-0.117	14.862	-0.017	-0.017	0.000	0.000	0.000	0.000
53	A	30	LEU	0	-0.086	0.077	14.253	0.007	0.007	0.000	0.000	0.000	0.000
54	A	31	ALA	0	0.090	-0.076	15.697	0.029	0.029	0.000	0.000	0.000	0.000
55	A	31	ALA	0	-0.069	0.102	19.619	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	32	GLN	0	0.108	-0.065	16.821	0.011	0.011	0.000	0.000	0.000	0.000
57	A	32	GLN	0	-0.131	0.062	15.522	0.009	0.009	0.000	0.000	0.000	0.000
58	A	33	PHE	0	0.000	-0.113	12.155	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	33	PHE	0	-0.141	0.026	11.117	-0.039	-0.039	0.000	0.000	0.000	0.000
60	A	34	GLU	0	0.118	-0.105	11.975	0.001	0.001	0.000	0.000	0.000	0.000
61	A	34	GLU	-1	-0.978	-0.796	13.495	0.117	0.117	0.000	0.000	0.000	0.000
62	A	35	ILE	0	0.050	-0.084	10.355	0.077	0.077	0.000	0.000	0.000	0.000
63	A	35	ILE	0	-0.129	0.058	8.869	0.015	0.015	0.000	0.000	0.000	0.000
64	A	36	SER	0	0.118	-0.037	10.369	-0.068	-0.068	0.000	0.000	0.000	0.000
65	A	36	SER	0	-0.020	0.051	10.067	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	37	VAL	0	0.083	-0.092	12.061	-0.040	-0.040	0.000	0.000	0.000	0.000
67	A	37	VAL	0	-0.034	0.122	15.472	0.000	0.000	0.000	0.000	0.000	0.000
68	A	38	PRO	0	0.010	-0.109	10.601	-0.064	-0.064	0.000	0.000	0.000	0.000
69	A	39	SER	0	0.016	-0.003	8.431	-0.076	-0.076	0.000	0.000	0.000	0.000
70	A	39	SER	0	-0.009	0.085	7.742	0.143	0.143	0.000	0.000	0.000	0.000
71	A	40	ALA	0	0.140	-0.101	9.137	-0.159	-0.159	0.000	0.000	0.000	0.000
72	A	40	ALA	0	-0.048	0.144	13.149	0.000	0.000	0.000	0.000	0.000	0.000
73	A	41	TYR	0	0.055	-0.108	12.205	-0.103	-0.103	0.000	0.000	0.000	0.000
74	A	41	TYR	0	-0.089	0.092	13.435	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	42	ASN	0	0.086	-0.087	9.452	-0.068	-0.068	0.000	0.000	0.000	0.000
76	A	42	ASN	0	-0.093	0.074	7.657	-0.092	-0.092	0.000	0.000	0.000	0.000
77	A	43	ILE	0	0.064	-0.086	10.905	-0.123	-0.123	0.000	0.000	0.000	0.000
78	A	43	ILE	0	-0.056	0.110	9.226	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	44	GLN	0	0.130	-0.088	11.754	-0.065	-0.065	0.000	0.000	0.000	0.000
80	A	44	GLN	0	-0.071	0.104	15.545	0.011	0.011	0.000	0.000	0.000	0.000
81	A	45	ARG	0	0.063	-0.085	14.267	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	45	ARG	1	0.863	1.059	11.585	0.045	0.045	0.000	0.000	0.000	0.000
83	A	46	ALA	0	0.089	-0.108	13.206	0.020	0.020	0.000	0.000	0.000	0.000
84	A	46	ALA	0	-0.096	0.104	12.486	-0.027	-0.027	0.000	0.000	0.000	0.000
85	A	47	LEU	0	0.115	-0.110	14.505	-0.035	-0.035	0.000	0.000	0.000	0.000
86	A	47	LEU	0	-0.108	0.109	16.159	0.001	0.001	0.000	0.000	0.000	0.000
87	A	48	LYS	0	0.078	-0.085	16.982	0.000	0.000	0.000	0.000	0.000	0.000
88	A	48	LYS	1	0.822	1.049	18.780	0.097	0.097	0.000	0.000	0.000	0.000
89	A	49	ALA	0	0.137	-0.057	17.984	0.023	0.023	0.000	0.000	0.000	0.000
90	A	49	ALA	0	-0.117	0.074	17.314	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	50	ILE	0	-0.008	-0.123	18.423	0.005	0.005	0.000	0.000	0.000	0.000
92	A	50	ILE	0	-0.055	0.092	16.031	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	51	CYS	0	0.062	-0.124	19.911	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	51	CYS	0	-0.257	0.154	22.182	0.001	0.001	0.000	0.000	0.000	0.000
95	A	52	GLU	0	0.120	-0.069	22.482	0.011	0.011	0.000	0.000	0.000	0.000
96	A	52	GLU	-1	-0.985	-0.854	22.219	-0.144	-0.144	0.000	0.000	0.000	0.000
97	A	53	ARG	0	0.062	-0.085	23.122	0.014	0.014	0.000	0.000	0.000	0.000
98	A	53	ARG	1	0.807	1.033	18.046	0.351	0.351	0.000	0.000	0.000	0.000
99	A	54	HIS	0	-0.063	-0.097	24.567	0.000	0.000	0.000	0.000	0.000	0.000
100	A	54	HIS	1	0.830	1.030	22.961	0.223	0.223	0.000	0.000	0.000	0.000
101	A	55	PRO	0	0.117	-0.072	26.695	0.004	0.004	0.000	0.000	0.000	0.000
102	A	56	ASP	0	0.068	-0.006	28.903	0.012	0.012	0.000	0.000	0.000	0.000
103	A	56	ASP	-1	-0.921	-0.833	30.335	-0.141	-0.141	0.000	0.000	0.000	0.000
104	A	57	GLU	0	-0.004	-0.139	28.205	0.010	0.010	0.000	0.000	0.000	0.000
105	A	57	GLU	-1	-0.865	-0.777	26.710	-0.184	-0.184	0.000	0.000	0.000	0.000
106	A	58	CYS	0	0.102	-0.050	25.400	0.008	0.008	0.000	0.000	0.000	0.000
107	A	59	GLU	0	0.140	-0.132	26.899	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	59	GLU	-1	-0.964	-0.789	29.153	-0.061	-0.061	0.000	0.000	0.000	0.000
109	A	60	VAL	0	0.069	-0.102	24.803	0.003	0.003	0.000	0.000	0.000	0.000
110	A	60	VAL	0	-0.126	0.074	23.239	0.000	0.000	0.000	0.000	0.000	0.000
111	A	61	GLN	0	0.127	-0.097	25.745	0.002	0.002	0.000	0.000	0.000	0.000
112	A	61	GLN	0	-0.166	0.081	28.132	0.008	0.008	0.000	0.000	0.000	0.000
113	A	62	TYR	0	0.140	-0.104	26.193	0.008	0.008	0.000	0.000	0.000	0.000
114	A	62	TYR	0	-0.110	0.097	23.722	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	63	LYS	0	0.081	-0.074	27.000	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	63	LYS	1	0.823	1.047	28.610	0.016	0.016	0.000	0.000	0.000	0.000
117	A	64	ASN	0	0.138	-0.063	27.881	0.003	0.003	0.000	0.000	0.000	0.000
118	A	64	ASN	0	-0.078	0.072	30.266	0.004	0.004	0.000	0.000	0.000	0.000
119	A	65	ARG	0	0.098	-0.028	28.806	0.007	0.007	0.000	0.000	0.000	0.000
120	A	65	ARG	1	0.806	1.013	28.661	-0.019	-0.019	0.000	0.000	0.000	0.000
121	A	66	LYS	0	0.089	-0.089	25.078	0.012	0.012	0.000	0.000	0.000	0.000
122	A	66	LYS	1	0.764	0.965	24.095	-0.046	-0.046	0.000	0.000	0.000	0.000
123	A	67	THR	0	0.029	-0.071	22.591	-0.006	-0.006	0.000	0.000	0.000	0.000
124	A	67	THR	0	-0.012	0.063	21.590	0.002	0.002	0.000	0.000	0.000	0.000
125	A	68	THR	0	0.001	-0.062	23.261	0.006	0.006	0.000	0.000	0.000	0.000
126	A	68	THR	0	-0.034	0.043	25.802	0.005	0.005	0.000	0.000	0.000	0.000
127	A	69	PHE	0	0.025	-0.076	23.071	0.002	0.002	0.000	0.000	0.000	0.000
128	A	69	PHE	0	-0.084	0.072	19.300	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	70	LYS	0	0.171	-0.079	24.375	0.004	0.004	0.000	0.000	0.000	0.000
130	A	70	LYS	1	0.880	1.089	28.737	0.053	0.053	0.000	0.000	0.000	0.000
131	A	71	TRP	0	0.116	-0.086	27.572	-0.007	-0.007	0.000	0.000	0.000	0.000
132	A	71	TRP	0	-0.068	0.113	24.986	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	72	ILE	0	-0.068	-0.156	28.483	0.009	0.009	0.000	0.000	0.000	0.000
134	A	72	ILE	0	-0.076	0.110	30.029	0.002	0.002	0.000	0.000	0.000	0.000
135	A	73	LYS	0	-0.019	-0.108	30.935	0.010	0.010	0.000	0.000	0.000	0.000
136	A	73	LYS	1	0.899	0.963	29.742	0.146	0.146	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:THR)