FMO DATABASE

FMODB ID: 52JGZ

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	OptH
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	-1684191.282225
FMO2-HF: Nuclear repulsion	1618921.463054
FMO2-HF: Total energy	-65269.819171
FMO2-MP2: Total energy	-65459.096781

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.
-0.076	2.248	-0.031	-1.161	-1.131	0.003

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 : 0.018 / q_NPA : -0.002

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	-0.789	-0.882	3.809	-0.748	1.576	-0.031	-1.161	-1.131	0.003
4	A	3498	MET	0	-0.074	-0.040	6.948	-0.083	-0.083	0.000	0.000	0.000	0.000
5	A	3499	VAL	0	0.040	0.024	10.449	-0.005	-0.005	0.000	0.000	0.000	0.000
6	A	3500	GLN	0	-0.034	-0.026	13.322	0.048	0.048	0.000	0.000	0.000	0.000
7	A	3501	LEU	0	0.104	0.053	14.263	0.033	0.033	0.000	0.000	0.000	0.000
8	A	3502	LEU	0	0.015	-0.012	15.663	0.047	0.047	0.000	0.000	0.000	0.000
9	A	3503	LYS	1	0.883	0.947	15.267	0.099	0.099	0.000	0.000	0.000	0.000
10	A	3504	LYS	1	0.829	0.925	9.164	0.030	0.030	0.000	0.000	0.000	0.000
11	A	3505	TYR	0	-0.031	-0.023	12.879	0.105	0.105	0.000	0.000	0.000	0.000
12	A	3506	PRO	0	0.015	0.019	16.304	-0.035	-0.035	0.000	0.000	0.000	0.000
13	A	3507	ILE	0	-0.013	-0.003	19.252	0.017	0.017	0.000	0.000	0.000	0.000
14	A	3508	VAL	0	-0.020	-0.015	21.497	0.003	0.003	0.000	0.000	0.000	0.000
15	A	3509	TRP	0	-0.024	-0.018	24.212	0.000	0.000	0.000	0.000	0.000	0.000
16	A	3510	GLN	0	-0.014	-0.015	27.688	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	3511	GLY	0	0.093	0.053	30.318	0.002	0.002	0.000	0.000	0.000	0.000
18	A	3512	LEU	0	-0.021	0.006	33.685	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	3513	LEU	0	0.008	0.019	31.676	0.006	0.006	0.000	0.000	0.000	0.000
20	A	3514	ALA	0	0.029	-0.007	35.909	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	3515	LEU	0	0.004	0.009	38.512	0.005	0.005	0.000	0.000	0.000	0.000
22	A	3516	LYS	1	0.932	0.971	40.771	-0.034	-0.034	0.000	0.000	0.000	0.000
23	A	3517	ASN	0	0.000	-0.009	44.549	0.002	0.002	0.000	0.000	0.000	0.000
24	A	3518	ASP	-1	-0.866	-0.911	41.764	0.022	0.022	0.000	0.000	0.000	0.000
25	A	3519	THR	0	-0.032	-0.035	39.628	0.003	0.003	0.000	0.000	0.000	0.000
26	A	3520	ALA	0	0.044	0.040	35.406	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	3521	ALA	0	0.014	0.010	34.821	0.006	0.006	0.000	0.000	0.000	0.000
28	A	3522	VAL	0	-0.020	-0.020	29.713	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	3523	GLN	0	-0.012	-0.020	26.529	0.000	0.000	0.000	0.000	0.000	0.000
30	A	3524	LEU	0	-0.038	-0.020	25.306	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	3525	HIS	1	0.854	0.918	20.068	-0.045	-0.045	0.000	0.000	0.000	0.000
32	A	3526	PHE	0	0.013	-0.006	15.279	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	3527	VAL	0	-0.013	-0.009	16.265	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	3528	SER	0	0.026	0.004	15.069	0.053	0.053	0.000	0.000	0.000	0.000
35	A	3529	GLY	0	0.045	0.045	16.237	-0.056	-0.056	0.000	0.000	0.000	0.000
36	A	3530	ASN	0	0.017	-0.015	17.662	0.034	0.034	0.000	0.000	0.000	0.000
37	A	3531	ASN	0	0.037	-0.002	18.468	-0.061	-0.061	0.000	0.000	0.000	0.000
38	A	3532	VAL	0	0.024	0.015	21.288	-0.033	-0.033	0.000	0.000	0.000	0.000
39	A	3533	LEU	0	-0.017	-0.002	23.972	-0.026	-0.026	0.000	0.000	0.000	0.000
40	A	3534	ALA	0	0.023	0.047	24.143	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	3535	HIS	0	-0.023	-0.007	25.870	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	3536	ARG	1	0.910	0.953	27.754	-0.192	-0.192	0.000	0.000	0.000	0.000
43	A	3537	SER	0	-0.070	-0.062	28.375	-0.010	-0.010	0.000	0.000	0.000	0.000
44	A	3538	LEU	0	-0.003	-0.001	27.216	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	3539	PRO	0	-0.003	0.001	31.241	0.000	0.000	0.000	0.000	0.000	0.000
46	A	3540	LEU	0	0.009	0.020	32.628	0.004	0.004	0.000	0.000	0.000	0.000
47	A	3541	SER	0	0.028	0.006	30.263	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	3542	GLU	-1	-0.921	-0.953	32.332	0.027	0.027	0.000	0.000	0.000	0.000
49	A	3543	GLY	0	0.016	0.009	34.506	0.000	0.000	0.000	0.000	0.000	0.000
50	A	3544	GLY	0	0.008	-0.006	38.120	0.001	0.001	0.000	0.000	0.000	0.000
51	A	3545	PRO	0	-0.054	-0.032	40.168	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	3546	PRO	0	0.002	0.019	38.047	0.003	0.003	0.000	0.000	0.000	0.000
53	A	3547	LEU	0	0.027	0.011	32.029	0.002	0.002	0.000	0.000	0.000	0.000
54	A	3548	ARG	1	0.864	0.930	36.511	-0.045	-0.045	0.000	0.000	0.000	0.000
55	A	3549	ILE	0	0.002	0.013	34.831	0.004	0.004	0.000	0.000	0.000	0.000
56	A	3550	ALA	0	-0.022	-0.024	38.399	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	3551	GLN	0	-0.021	-0.011	39.267	0.001	0.001	0.000	0.000	0.000	0.000
58	A	3552	ARG	1	0.940	0.972	37.636	-0.048	-0.048	0.000	0.000	0.000	0.000
59	A	3553	MET	0	-0.008	0.015	31.680	0.001	0.001	0.000	0.000	0.000	0.000
60	A	3554	ARG	1	0.961	0.979	36.389	-0.058	-0.058	0.000	0.000	0.000	0.000
61	A	3555	LEU	0	-0.017	0.015	31.809	0.007	0.007	0.000	0.000	0.000	0.000
62	A	3556	GLU	-1	-0.900	-0.961	34.646	0.057	0.057	0.000	0.000	0.000	0.000
63	A	3557	ALA	0	0.049	0.016	33.731	0.006	0.006	0.000	0.000	0.000	0.000
64	A	3558	THR	0	0.034	0.024	33.133	0.006	0.006	0.000	0.000	0.000	0.000
65	A	3559	GLN	0	0.002	-0.007	33.786	0.009	0.009	0.000	0.000	0.000	0.000
66	A	3560	LEU	0	0.014	0.003	29.653	0.008	0.008	0.000	0.000	0.000	0.000
67	A	3561	GLU	-1	-0.909	-0.955	29.049	0.122	0.122	0.000	0.000	0.000	0.000
68	A	3562	GLY	0	-0.054	-0.031	29.240	0.013	0.013	0.000	0.000	0.000	0.000
69	A	3563	VAL	0	-0.023	-0.012	26.388	0.011	0.011	0.000	0.000	0.000	0.000
70	A	3564	ALA	0	0.024	-0.002	24.939	0.016	0.016	0.000	0.000	0.000	0.000
71	A	3565	ARG	1	0.957	0.991	24.588	-0.126	-0.126	0.000	0.000	0.000	0.000
72	A	3566	ARG	1	0.917	0.955	25.712	-0.132	-0.132	0.000	0.000	0.000	0.000
73	A	3567	MET	0	-0.046	-0.012	20.931	0.003	0.003	0.000	0.000	0.000	0.000
74	A	3568	THR	0	-0.062	-0.024	20.516	0.031	0.031	0.000	0.000	0.000	0.000
75	A	3569	VAL	0	0.044	0.038	20.368	0.041	0.041	0.000	0.000	0.000	0.000
76	A	3570	GLU	-1	-0.954	-0.980	14.403	0.720	0.720	0.000	0.000	0.000	0.000
77	A	3571	THR	0	-0.006	-0.014	18.760	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	3572	ASP	-1	-0.878	-0.948	21.401	0.241	0.241	0.000	0.000	0.000	0.000
79	A	3573	TYR	0	-0.016	-0.016	17.533	-0.024	-0.024	0.000	0.000	0.000	0.000
80	A	3574	CYS	0	-0.034	0.011	20.980	0.033	0.033	0.000	0.000	0.000	0.000
81	A	3575	LEU	0	-0.040	-0.017	18.595	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	3576	LEU	0	0.022	-0.005	20.199	0.010	0.010	0.000	0.000	0.000	0.000
83	A	3577	LEU	0	0.004	0.016	21.066	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	3578	ALA	0	-0.017	-0.016	23.160	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	3579	LEU	0	0.013	-0.003	23.368	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	3580	PRO	0	0.028	0.015	27.484	0.004	0.004	0.000	0.000	0.000	0.000
87	A	3581	CYS	0	-0.033	-0.001	29.887	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	3582	GLY	0	0.049	0.007	31.929	0.003	0.003	0.000	0.000	0.000	0.000
89	A	3583	ARG	1	0.922	0.960	34.509	0.000	0.000	0.000	0.000	0.000	0.000
90	A	3584	ASP	-1	-0.864	-0.934	36.801	-0.016	-0.016	0.000	0.000	0.000	0.000
91	A	3585	GLN	0	-0.002	-0.013	34.405	0.005	0.005	0.000	0.000	0.000	0.000
92	A	3586	GLU	-1	-0.891	-0.941	37.228	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	3587	ASP	-1	-0.825	-0.911	38.188	0.007	0.007	0.000	0.000	0.000	0.000
94	A	3588	VAL	0	-0.013	0.000	32.849	0.004	0.004	0.000	0.000	0.000	0.000
95	A	3589	VAL	0	-0.001	0.016	35.707	0.003	0.003	0.000	0.000	0.000	0.000
96	A	3590	SER	0	0.005	0.003	37.601	0.003	0.003	0.000	0.000	0.000	0.000
97	A	3591	GLN	0	0.006	0.000	35.571	0.007	0.007	0.000	0.000	0.000	0.000
98	A	3592	THR	0	-0.053	-0.042	33.227	0.004	0.004	0.000	0.000	0.000	0.000
99	A	3593	GLU	-1	-0.943	-0.974	35.149	0.006	0.006	0.000	0.000	0.000	0.000
100	A	3594	SER	0	0.007	-0.008	38.141	0.003	0.003	0.000	0.000	0.000	0.000
101	A	3595	LEU	0	-0.004	-0.002	30.835	0.004	0.004	0.000	0.000	0.000	0.000
102	A	3596	LYS	1	0.944	0.967	34.366	0.007	0.007	0.000	0.000	0.000	0.000
103	A	3597	ALA	0	0.035	0.039	36.279	0.003	0.003	0.000	0.000	0.000	0.000
104	A	3598	ALA	0	0.002	0.000	39.400	0.002	0.002	0.000	0.000	0.000	0.000
105	A	3599	PHE	0	-0.089	-0.045	35.193	0.005	0.005	0.000	0.000	0.000	0.000
106	A	3600	ILE	0	0.004	-0.001	31.767	0.004	0.004	0.000	0.000	0.000	0.000
107	A	3601	THR	0	0.017	0.003	35.091	0.001	0.001	0.000	0.000	0.000	0.000
108	A	3602	TYR	0	-0.038	-0.023	38.353	0.000	0.000	0.000	0.000	0.000	0.000
109	A	3603	LEU	0	-0.037	-0.033	33.781	0.001	0.001	0.000	0.000	0.000	0.000
110	A	3604	GLN	0	0.010	-0.003	32.500	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	3605	ALA	0	-0.019	0.006	36.702	0.000	0.000	0.000	0.000	0.000	0.000
112	A	3606	LYS	1	0.814	0.908	39.815	-0.034	-0.034	0.000	0.000	0.000	0.000
113	A	3607	GLN	0	0.033	0.035	36.842	0.002	0.002	0.000	0.000	0.000	0.000
114	A	3608	ALA	0	-0.025	-0.039	36.237	0.004	0.004	0.000	0.000	0.000	0.000
115	A	3609	ALA	0	0.031	0.030	32.065	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	3610	GLY	0	-0.002	-0.017	33.653	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	3611	ILE	0	-0.028	-0.018	33.635	0.008	0.008	0.000	0.000	0.000	0.000
118	A	3612	ILE	0	0.014	0.003	34.082	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	3613	ASN	0	-0.039	-0.010	34.456	0.013	0.013	0.000	0.000	0.000	0.000
120	A	3614	VAL	0	0.015	0.009	33.125	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	3615	PRO	0	0.002	0.004	35.803	0.006	0.006	0.000	0.000	0.000	0.000
122	A	3616	ASN	0	0.039	0.018	34.636	0.003	0.003	0.000	0.000	0.000	0.000
123	A	3617	PRO	0	0.031	-0.008	37.875	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	3618	GLY	0	0.016	0.012	40.960	0.003	0.003	0.000	0.000	0.000	0.000
125	A	3619	SER	0	-0.024	-0.001	40.389	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	3620	ASN	0	-0.021	-0.010	41.917	0.003	0.003	0.000	0.000	0.000	0.000
127	A	3621	GLN	0	-0.017	0.000	38.734	0.005	0.005	0.000	0.000	0.000	0.000
128	A	3622	PRO	0	-0.027	-0.014	36.750	0.001	0.001	0.000	0.000	0.000	0.000
129	A	3623	ALA	0	0.018	0.019	34.371	0.004	0.004	0.000	0.000	0.000	0.000
130	A	3624	TYR	0	0.036	0.008	28.925	0.016	0.016	0.000	0.000	0.000	0.000
131	A	3625	VAL	0	-0.034	-0.004	31.053	-0.011	-0.011	0.000	0.000	0.000	0.000
132	A	3626	LEU	0	0.001	-0.001	29.495	0.012	0.012	0.000	0.000	0.000	0.000
133	A	3627	GLN	0	-0.030	-0.031	28.291	-0.014	-0.014	0.000	0.000	0.000	0.000
134	A	3628	ILE	0	0.002	-0.005	28.817	0.006	0.006	0.000	0.000	0.000	0.000
135	A	3629	PHE	0	0.034	0.001	27.840	-0.007	-0.007	0.000	0.000	0.000	0.000
136	A	3630	PRO	0	0.016	0.027	29.217	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	3631	PRO	0	0.030	0.009	28.031	0.006	0.006	0.000	0.000	0.000	0.000
138	A	3632	CYS	0	-0.045	-0.013	27.974	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	3633	GLU	-1	-0.787	-0.899	27.384	0.062	0.062	0.000	0.000	0.000	0.000
140	A	3634	PHE	0	0.002	-0.005	26.065	0.010	0.010	0.000	0.000	0.000	0.000
141	A	3635	SER	0	0.061	-0.014	24.446	0.012	0.012	0.000	0.000	0.000	0.000
142	A	3636	GLU	-1	-0.924	-0.952	22.767	0.048	0.048	0.000	0.000	0.000	0.000
143	A	3637	SER	0	-0.019	0.020	21.630	0.012	0.012	0.000	0.000	0.000	0.000
144	A	3638	HIS	0	0.054	0.022	20.061	0.038	0.038	0.000	0.000	0.000	0.000
145	A	3639	LEU	0	0.021	0.009	18.376	0.033	0.033	0.000	0.000	0.000	0.000
146	A	3640	SER	0	-0.023	-0.030	17.111	-0.004	-0.004	0.000	0.000	0.000	0.000
147	A	3641	ARG	1	0.863	0.925	15.883	-0.313	-0.313	0.000	0.000	0.000	0.000
148	A	3642	LEU	0	-0.082	-0.048	14.038	0.058	0.058	0.000	0.000	0.000	0.000
149	A	3643	ALA	0	-0.012	0.002	13.146	0.051	0.051	0.000	0.000	0.000	0.000
150	A	3644	PRO	0	0.055	0.031	12.675	-0.051	-0.051	0.000	0.000	0.000	0.000
151	A	3645	ASP	-1	-0.767	-0.872	12.461	-0.046	-0.046	0.000	0.000	0.000	0.000
152	A	3646	LEU	0	-0.006	-0.002	14.873	-0.019	-0.019	0.000	0.000	0.000	0.000
153	A	3647	LEU	0	0.016	0.029	17.241	-0.013	-0.013	0.000	0.000	0.000	0.000
154	A	3648	ALA	0	-0.009	0.001	18.025	-0.008	-0.008	0.000	0.000	0.000	0.000
155	A	3649	SER	0	-0.091	-0.060	19.331	-0.009	-0.009	0.000	0.000	0.000	0.000
156	A	3650	ILE	0	0.011	-0.009	21.016	0.003	0.003	0.000	0.000	0.000	0.000
157	A	3651	SER	0	0.008	0.008	22.974	0.003	0.003	0.000	0.000	0.000	0.000
158	A	3652	ASN	0	-0.033	-0.018	24.782	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	3653	ILE	0	-0.041	0.000	24.125	-0.007	-0.007	0.000	0.000	0.000	0.000
160	A	3654	SER	0	-0.017	-0.017	26.274	-0.004	-0.004	0.000	0.000	0.000	0.000
161	A	3655	PRO	0	-0.027	-0.016	27.825	0.008	0.008	0.000	0.000	0.000	0.000
162	A	3656	HIS	0	-0.009	-0.012	25.502	0.007	0.007	0.000	0.000	0.000	0.000
163	A	3657	LEU	0	-0.004	0.004	27.404	0.000	0.000	0.000	0.000	0.000	0.000
164	A	3658	MET	0	-0.006	0.041	23.163	0.005	0.005	0.000	0.000	0.000	0.000
165	A	3659	ILE	0	-0.027	-0.021	25.003	-0.003	-0.003	0.000	0.000	0.000	0.000
166	A	3660	VAL	0	0.025	0.021	23.929	0.016	0.016	0.000	0.000	0.000	0.000
167	A	3661	ILE	0	-0.031	-0.007	25.035	-0.015	-0.015	0.000	0.000	0.000	0.000
168	A	3662	ALA	0	-0.003	-0.009	25.507	0.020	0.020	0.000	0.000	0.000	0.000
169	A	3663	SER	0	0.020	0.005	27.593	-0.011	-0.011	0.000	0.000	0.000	0.000
170	A	3664	VAL	0	-0.040	-0.011	29.497	0.004	0.004	0.000	0.000	0.000	0.000

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