FMO DATABASE

FMODB ID: V5QY1

Calculation Name: 1OW1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OW1

Chain ID: A

ChEMBL ID:

UniProt ID: Q96T58

Base Structure: X-ray

Registration Date: 2023-06-22

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

DOI:

IFIE MAP

IFIE Diagram

Modeling method

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	170
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1688549.382936
FMO2-HF: Nuclear repulsion	1623278.625081
FMO2-HF: Total energy	-65270.757855
FMO2-MP2: Total energy	-65459.972602

3D Structure

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:3495:PRO)

Summations of interaction energy for fragment #1(A:3495:PRO)

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.
0.003	1.523	-0.02	-0.718	-0.782	0.001

Interaction energy analysis for fragmet #1(A:3495:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : -0.028

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	3497	ASP	-1	-0.770	-0.863	3.879	-0.010	1.510	-0.020	-0.718	-0.782	0.001
4	A	3498	MET	0	-0.062	-0.036	6.950	-0.084	-0.084	0.000	0.000	0.000	0.000
5	A	3499	VAL	0	0.014	0.004	10.594	-0.056	-0.056	0.000	0.000	0.000	0.000
6	A	3500	GLN	0	-0.010	-0.014	13.362	0.015	0.015	0.000	0.000	0.000	0.000
7	A	3501	LEU	0	0.079	0.047	14.906	0.048	0.048	0.000	0.000	0.000	0.000
8	A	3502	LEU	0	0.016	-0.007	15.995	0.034	0.034	0.000	0.000	0.000	0.000
9	A	3503	LYS	1	0.879	0.946	15.328	-0.116	-0.116	0.000	0.000	0.000	0.000
10	A	3504	LYS	1	0.797	0.883	9.673	-0.133	-0.133	0.000	0.000	0.000	0.000
11	A	3505	TYR	0	0.000	-0.018	13.011	0.068	0.068	0.000	0.000	0.000	0.000
12	A	3506	PRO	0	0.011	0.023	16.460	-0.043	-0.043	0.000	0.000	0.000	0.000
13	A	3507	ILE	0	-0.045	-0.020	19.418	0.000	0.000	0.000	0.000	0.000	0.000
14	A	3508	VAL	0	-0.004	-0.010	21.505	0.011	0.011	0.000	0.000	0.000	0.000
15	A	3509	TRP	0	-0.046	-0.023	24.286	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	3510	GLN	0	-0.017	-0.024	27.663	0.000	0.000	0.000	0.000	0.000	0.000
17	A	3511	GLY	0	0.092	0.054	30.396	0.001	0.001	0.000	0.000	0.000	0.000
18	A	3512	LEU	0	-0.022	-0.002	33.815	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	3513	LEU	0	0.034	0.024	32.064	0.004	0.004	0.000	0.000	0.000	0.000
20	A	3514	ALA	0	0.005	-0.023	36.057	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	3515	LEU	0	0.001	0.013	38.565	0.003	0.003	0.000	0.000	0.000	0.000
22	A	3516	LYS	1	0.792	0.898	41.080	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	3517	ASN	0	0.017	0.010	44.842	0.003	0.003	0.000	0.000	0.000	0.000
24	A	3518	ASP	-1	-0.743	-0.853	42.039	0.031	0.031	0.000	0.000	0.000	0.000
25	A	3519	THR	0	0.007	-0.017	39.833	0.003	0.003	0.000	0.000	0.000	0.000
26	A	3520	ALA	0	0.007	0.025	35.758	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	3521	ALA	0	-0.008	0.008	35.012	0.005	0.005	0.000	0.000	0.000	0.000
28	A	3522	VAL	0	-0.011	-0.022	29.922	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	3523	GLN	0	0.026	0.001	26.347	0.007	0.007	0.000	0.000	0.000	0.000
30	A	3524	LEU	0	-0.033	-0.017	25.689	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	3525	HIS	1	0.838	0.909	20.644	-0.109	-0.109	0.000	0.000	0.000	0.000
32	A	3526	PHE	0	0.022	-0.004	15.351	-0.015	-0.015	0.000	0.000	0.000	0.000
33	A	3527	VAL	0	-0.016	-0.004	16.570	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	3528	SER	0	0.041	0.026	15.251	0.030	0.030	0.000	0.000	0.000	0.000
35	A	3529	GLY	0	0.046	0.030	16.526	-0.046	-0.046	0.000	0.000	0.000	0.000
36	A	3530	ASN	0	-0.002	-0.021	18.497	0.035	0.035	0.000	0.000	0.000	0.000
37	A	3531	ASN	0	0.012	-0.005	18.536	-0.050	-0.050	0.000	0.000	0.000	0.000
38	A	3532	VAL	0	0.012	0.006	21.864	-0.026	-0.026	0.000	0.000	0.000	0.000
39	A	3533	LEU	0	-0.018	-0.011	24.548	-0.022	-0.022	0.000	0.000	0.000	0.000
40	A	3534	ALA	0	0.008	0.025	24.849	-0.016	-0.016	0.000	0.000	0.000	0.000
41	A	3535	HIS	0	-0.002	-0.002	26.349	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	3536	ARG	1	0.901	0.959	28.250	-0.174	-0.174	0.000	0.000	0.000	0.000
43	A	3537	SER	0	-0.064	-0.050	29.173	-0.010	-0.010	0.000	0.000	0.000	0.000
44	A	3538	LEU	0	0.006	0.011	27.500	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	3539	PRO	0	0.007	-0.002	31.790	0.001	0.001	0.000	0.000	0.000	0.000
46	A	3540	LEU	0	0.013	0.022	32.919	0.006	0.006	0.000	0.000	0.000	0.000
47	A	3541	SER	0	0.017	-0.003	30.594	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	3542	GLU	-1	-0.889	-0.916	32.613	0.071	0.071	0.000	0.000	0.000	0.000
49	A	3543	GLY	0	-0.005	-0.023	34.627	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	3544	GLY	0	0.006	0.009	37.939	0.003	0.003	0.000	0.000	0.000	0.000
51	A	3545	PRO	0	-0.028	-0.022	40.436	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	3546	PRO	0	-0.001	0.020	38.335	0.004	0.004	0.000	0.000	0.000	0.000
53	A	3547	LEU	0	0.029	0.009	32.393	0.000	0.000	0.000	0.000	0.000	0.000
54	A	3548	ARG	1	0.812	0.900	36.654	-0.048	-0.048	0.000	0.000	0.000	0.000
55	A	3549	ILE	0	0.011	0.012	35.047	0.002	0.002	0.000	0.000	0.000	0.000
56	A	3550	ALA	0	-0.013	-0.018	38.671	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	3551	GLN	0	-0.009	0.008	39.379	0.001	0.001	0.000	0.000	0.000	0.000
58	A	3552	ARG	1	0.924	0.953	37.722	-0.037	-0.037	0.000	0.000	0.000	0.000
59	A	3553	MET	0	-0.014	0.014	31.987	0.000	0.000	0.000	0.000	0.000	0.000
60	A	3554	ARG	1	0.865	0.916	36.332	-0.035	-0.035	0.000	0.000	0.000	0.000
61	A	3555	LEU	0	-0.004	0.002	32.017	0.004	0.004	0.000	0.000	0.000	0.000
62	A	3556	GLU	-1	-0.781	-0.869	34.873	0.033	0.033	0.000	0.000	0.000	0.000
63	A	3557	ALA	0	0.039	0.018	33.944	0.004	0.004	0.000	0.000	0.000	0.000
64	A	3558	THR	0	0.047	0.019	33.441	0.005	0.005	0.000	0.000	0.000	0.000
65	A	3559	GLN	0	0.001	-0.011	34.325	0.006	0.006	0.000	0.000	0.000	0.000
66	A	3560	LEU	0	-0.004	-0.001	30.195	0.007	0.007	0.000	0.000	0.000	0.000
67	A	3561	GLU	-1	-0.862	-0.922	29.327	0.065	0.065	0.000	0.000	0.000	0.000
68	A	3562	GLY	0	-0.038	-0.018	29.566	0.008	0.008	0.000	0.000	0.000	0.000
69	A	3563	VAL	0	-0.023	-0.013	26.836	0.007	0.007	0.000	0.000	0.000	0.000
70	A	3564	ALA	0	0.007	-0.010	25.288	0.012	0.012	0.000	0.000	0.000	0.000
71	A	3565	ARG	1	0.891	0.936	24.854	-0.067	-0.067	0.000	0.000	0.000	0.000
72	A	3566	ARG	1	0.925	0.971	26.198	-0.092	-0.092	0.000	0.000	0.000	0.000
73	A	3567	MET	0	-0.068	-0.021	21.394	0.008	0.008	0.000	0.000	0.000	0.000
74	A	3568	THR	0	-0.033	-0.030	21.037	0.012	0.012	0.000	0.000	0.000	0.000
75	A	3569	VAL	0	0.030	0.021	20.616	0.018	0.018	0.000	0.000	0.000	0.000
76	A	3570	GLU	-1	-0.882	-0.947	14.822	0.445	0.445	0.000	0.000	0.000	0.000
77	A	3571	THR	0	-0.046	-0.052	19.412	0.015	0.015	0.000	0.000	0.000	0.000
78	A	3572	ASP	-1	-0.833	-0.887	22.004	0.179	0.179	0.000	0.000	0.000	0.000
79	A	3573	TYR	0	-0.054	-0.035	18.128	-0.024	-0.024	0.000	0.000	0.000	0.000
80	A	3574	CYS	0	-0.037	-0.002	21.189	0.033	0.033	0.000	0.000	0.000	0.000
81	A	3575	LEU	0	-0.023	-0.006	18.757	-0.028	-0.028	0.000	0.000	0.000	0.000
82	A	3576	LEU	0	0.018	-0.006	20.428	0.020	0.020	0.000	0.000	0.000	0.000
83	A	3577	LEU	0	-0.002	0.004	21.571	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	3578	ALA	0	-0.016	-0.007	23.727	0.003	0.003	0.000	0.000	0.000	0.000
85	A	3579	LEU	0	0.021	0.002	23.310	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	3580	PRO	0	0.029	0.017	27.673	0.005	0.005	0.000	0.000	0.000	0.000
87	A	3581	CYS	0	-0.056	-0.011	30.207	0.001	0.001	0.000	0.000	0.000	0.000
88	A	3582	GLY	0	0.041	-0.002	32.134	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	3583	ARG	1	0.755	0.849	34.852	-0.025	-0.025	0.000	0.000	0.000	0.000
90	A	3584	ASP	-1	-0.793	-0.886	36.664	0.023	0.023	0.000	0.000	0.000	0.000
91	A	3585	GLN	0	0.021	-0.003	34.239	0.002	0.002	0.000	0.000	0.000	0.000
92	A	3586	GLU	-1	-0.855	-0.898	37.413	0.019	0.019	0.000	0.000	0.000	0.000
93	A	3587	ASP	-1	-0.799	-0.886	38.389	0.037	0.037	0.000	0.000	0.000	0.000
94	A	3588	VAL	0	0.002	0.008	33.088	0.002	0.002	0.000	0.000	0.000	0.000
95	A	3589	VAL	0	0.016	0.025	35.700	0.001	0.001	0.000	0.000	0.000	0.000
96	A	3590	SER	0	0.027	0.013	37.739	0.000	0.000	0.000	0.000	0.000	0.000
97	A	3591	GLN	0	-0.039	-0.028	35.805	0.003	0.003	0.000	0.000	0.000	0.000
98	A	3592	THR	0	-0.016	-0.029	33.404	0.003	0.003	0.000	0.000	0.000	0.000
99	A	3593	GLU	-1	-0.837	-0.893	35.377	0.018	0.018	0.000	0.000	0.000	0.000
100	A	3594	SER	0	-0.011	-0.017	38.528	0.000	0.000	0.000	0.000	0.000	0.000
101	A	3595	LEU	0	0.001	-0.008	31.101	0.001	0.001	0.000	0.000	0.000	0.000
102	A	3596	LYS	1	0.838	0.893	35.136	-0.017	-0.017	0.000	0.000	0.000	0.000
103	A	3597	ALA	0	0.010	0.026	36.714	0.000	0.000	0.000	0.000	0.000	0.000
104	A	3598	ALA	0	-0.013	-0.006	39.904	0.000	0.000	0.000	0.000	0.000	0.000
105	A	3599	PHE	0	-0.077	-0.039	35.552	0.002	0.002	0.000	0.000	0.000	0.000
106	A	3600	ILE	0	0.014	0.010	32.050	0.000	0.000	0.000	0.000	0.000	0.000
107	A	3601	THR	0	0.012	-0.009	35.367	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	3602	TYR	0	-0.013	-0.001	38.624	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	3603	LEU	0	-0.033	-0.023	33.856	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	3604	GLN	0	0.026	0.006	32.735	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	3605	ALA	0	0.008	0.015	37.045	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	3606	LYS	1	0.798	0.890	39.727	-0.028	-0.028	0.000	0.000	0.000	0.000
113	A	3607	GLN	0	0.012	0.018	37.281	0.001	0.001	0.000	0.000	0.000	0.000
114	A	3608	ALA	0	-0.023	-0.015	36.534	0.002	0.002	0.000	0.000	0.000	0.000
115	A	3609	ALA	0	0.044	0.032	32.284	0.000	0.000	0.000	0.000	0.000	0.000
116	A	3610	GLY	0	0.010	-0.008	34.088	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	3611	ILE	0	-0.047	-0.027	33.843	0.005	0.005	0.000	0.000	0.000	0.000
118	A	3612	ILE	0	0.019	0.005	34.643	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	3613	ASN	0	-0.027	-0.015	34.693	0.009	0.009	0.000	0.000	0.000	0.000
120	A	3614	VAL	0	0.009	0.006	33.741	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	3615	PRO	0	0.015	0.022	36.207	0.004	0.004	0.000	0.000	0.000	0.000
122	A	3616	ASN	0	0.053	0.012	35.157	0.007	0.007	0.000	0.000	0.000	0.000
123	A	3617	PRO	0	0.007	-0.014	38.043	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	3618	GLY	0	0.019	0.016	41.010	0.002	0.002	0.000	0.000	0.000	0.000
125	A	3619	SER	0	-0.042	-0.018	41.098	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	3620	ASN	0	0.007	-0.004	42.602	0.003	0.003	0.000	0.000	0.000	0.000
127	A	3621	GLN	0	-0.013	0.012	39.130	0.002	0.002	0.000	0.000	0.000	0.000
128	A	3622	PRO	0	-0.007	-0.005	37.062	0.002	0.002	0.000	0.000	0.000	0.000
129	A	3623	ALA	0	0.017	0.027	34.841	0.002	0.002	0.000	0.000	0.000	0.000
130	A	3624	TYR	0	0.027	-0.002	30.170	0.012	0.012	0.000	0.000	0.000	0.000
131	A	3625	VAL	0	-0.036	-0.010	31.344	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	3626	LEU	0	0.022	0.020	29.834	0.009	0.009	0.000	0.000	0.000	0.000
133	A	3627	GLN	0	-0.006	-0.025	28.891	-0.012	-0.012	0.000	0.000	0.000	0.000
134	A	3628	ILE	0	-0.008	0.000	29.052	0.006	0.006	0.000	0.000	0.000	0.000
135	A	3629	PHE	0	0.038	0.000	28.111	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	3630	PRO	0	0.011	0.015	29.671	0.002	0.002	0.000	0.000	0.000	0.000
137	A	3631	PRO	0	0.056	0.031	28.215	0.003	0.003	0.000	0.000	0.000	0.000
138	A	3632	CYS	0	-0.070	-0.023	28.220	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	3633	GLU	-1	-0.835	-0.919	27.482	0.029	0.029	0.000	0.000	0.000	0.000
140	A	3634	PHE	0	0.012	-0.007	26.257	0.004	0.004	0.000	0.000	0.000	0.000
141	A	3635	SER	0	0.066	-0.006	24.718	0.007	0.007	0.000	0.000	0.000	0.000
142	A	3636	GLU	-1	-0.837	-0.895	22.970	0.028	0.028	0.000	0.000	0.000	0.000
143	A	3637	SER	0	-0.010	0.022	21.784	0.002	0.002	0.000	0.000	0.000	0.000
144	A	3638	HIS	0	0.042	0.010	20.459	0.018	0.018	0.000	0.000	0.000	0.000
145	A	3639	LEU	0	0.031	0.004	18.724	0.021	0.021	0.000	0.000	0.000	0.000
146	A	3640	SER	0	-0.016	-0.025	17.351	0.000	0.000	0.000	0.000	0.000	0.000
147	A	3641	ARG	1	0.811	0.912	16.080	-0.173	-0.173	0.000	0.000	0.000	0.000
148	A	3642	LEU	0	-0.060	-0.027	14.182	0.025	0.025	0.000	0.000	0.000	0.000
149	A	3643	ALA	0	0.001	0.010	13.475	0.048	0.048	0.000	0.000	0.000	0.000
150	A	3644	PRO	0	0.041	0.023	13.081	-0.027	-0.027	0.000	0.000	0.000	0.000
151	A	3645	ASP	-1	-0.769	-0.854	12.916	0.078	0.078	0.000	0.000	0.000	0.000
152	A	3646	LEU	0	-0.001	0.001	15.347	-0.009	-0.009	0.000	0.000	0.000	0.000
153	A	3647	LEU	0	-0.002	0.016	17.704	-0.010	-0.010	0.000	0.000	0.000	0.000
154	A	3648	ALA	0	-0.006	-0.005	18.178	-0.007	-0.007	0.000	0.000	0.000	0.000
155	A	3649	SER	0	-0.087	-0.050	19.721	-0.007	-0.007	0.000	0.000	0.000	0.000
156	A	3650	ILE	0	0.000	-0.010	21.453	0.003	0.003	0.000	0.000	0.000	0.000
157	A	3651	SER	0	-0.028	-0.035	23.456	-0.002	-0.002	0.000	0.000	0.000	0.000
158	A	3652	ASN	0	-0.087	-0.052	25.230	-0.007	-0.007	0.000	0.000	0.000	0.000
159	A	3653	ILE	0	-0.014	0.020	24.611	-0.004	-0.004	0.000	0.000	0.000	0.000
160	A	3654	SER	0	0.010	-0.006	26.538	0.000	0.000	0.000	0.000	0.000	0.000
161	A	3655	PRO	0	-0.041	-0.019	28.296	0.005	0.005	0.000	0.000	0.000	0.000
162	A	3656	HIS	0	0.005	-0.006	26.271	0.007	0.007	0.000	0.000	0.000	0.000
163	A	3657	LEU	0	-0.016	-0.004	28.082	-0.005	-0.005	0.000	0.000	0.000	0.000
164	A	3658	MET	0	-0.012	0.036	23.478	0.007	0.007	0.000	0.000	0.000	0.000
165	A	3659	ILE	0	-0.035	-0.022	25.445	-0.007	-0.007	0.000	0.000	0.000	0.000
166	A	3660	VAL	0	0.026	0.021	24.437	0.014	0.014	0.000	0.000	0.000	0.000
167	A	3661	ILE	0	-0.015	0.000	25.277	-0.013	-0.013	0.000	0.000	0.000	0.000
168	A	3662	ALA	0	0.002	-0.006	25.713	0.013	0.013	0.000	0.000	0.000	0.000
169	A	3663	SER	0	0.011	0.012	27.888	-0.006	-0.006	0.000	0.000	0.000	0.000
170	A	3664	VAL	0	-0.095	-0.047	29.879	-0.005	-0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3495:PRO)