FMO DATABASE

FMODB ID: YZVR2

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	OptHSide
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	-1685308.72566
FMO2-HF: Nuclear repulsion	1620038.18047
FMO2-HF: Total energy	-65270.54519
FMO2-MP2: Total energy	-65459.768638

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.
0.046	2.022	-0.031	-0.953	-0.992	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 : -0.018

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].
3	A	3497	ASP	-1	-0.773	-0.864	3.809	-0.339	1.637	-0.031	-0.953	-0.992	0.001
4	A	3498	MET	0	-0.068	-0.036	6.947	-0.077	-0.077	0.000	0.000	0.000	0.000
5	A	3499	VAL	0	0.022	0.010	10.437	-0.044	-0.044	0.000	0.000	0.000	0.000
6	A	3500	GLN	0	-0.016	-0.019	13.322	0.038	0.038	0.000	0.000	0.000	0.000
7	A	3501	LEU	0	0.093	0.049	14.565	0.044	0.044	0.000	0.000	0.000	0.000
8	A	3502	LEU	0	0.017	-0.010	15.663	0.046	0.046	0.000	0.000	0.000	0.000
9	A	3503	LYS	1	0.880	0.948	15.238	-0.021	-0.021	0.000	0.000	0.000	0.000
10	A	3504	LYS	1	0.800	0.890	9.300	-0.052	-0.052	0.000	0.000	0.000	0.000
11	A	3505	TYR	0	-0.018	-0.023	12.685	0.092	0.092	0.000	0.000	0.000	0.000
12	A	3506	PRO	0	0.020	0.020	16.261	-0.045	-0.045	0.000	0.000	0.000	0.000
13	A	3507	ILE	0	-0.022	-0.003	19.228	0.009	0.009	0.000	0.000	0.000	0.000
14	A	3508	VAL	0	-0.020	-0.017	21.407	0.006	0.006	0.000	0.000	0.000	0.000
15	A	3509	TRP	0	-0.036	-0.027	24.183	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	3510	GLN	0	-0.015	-0.013	27.663	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	3511	GLY	0	0.084	0.049	30.296	0.001	0.001	0.000	0.000	0.000	0.000
18	A	3512	LEU	0	-0.023	0.000	33.666	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	3513	LEU	0	0.015	0.022	31.606	0.005	0.005	0.000	0.000	0.000	0.000
20	A	3514	ALA	0	0.026	-0.013	35.899	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	3515	LEU	0	0.004	0.011	38.305	0.004	0.004	0.000	0.000	0.000	0.000
22	A	3516	LYS	1	0.863	0.942	40.767	-0.040	-0.040	0.000	0.000	0.000	0.000
23	A	3517	ASN	0	0.027	0.004	44.546	0.003	0.003	0.000	0.000	0.000	0.000
24	A	3518	ASP	-1	-0.829	-0.895	41.634	0.032	0.032	0.000	0.000	0.000	0.000
25	A	3519	THR	0	0.014	-0.012	39.611	0.003	0.003	0.000	0.000	0.000	0.000
26	A	3520	ALA	0	0.004	0.016	35.427	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	3521	ALA	0	0.015	0.019	34.839	0.006	0.006	0.000	0.000	0.000	0.000
28	A	3522	VAL	0	-0.013	-0.025	29.728	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	3523	GLN	0	-0.004	-0.015	26.403	0.003	0.003	0.000	0.000	0.000	0.000
30	A	3524	LEU	0	-0.040	-0.025	25.304	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	3525	HIS	1	0.852	0.917	20.082	-0.095	-0.095	0.000	0.000	0.000	0.000
32	A	3526	PHE	0	0.017	-0.004	15.175	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	3527	VAL	0	-0.016	-0.010	16.307	0.004	0.004	0.000	0.000	0.000	0.000
34	A	3528	SER	0	0.043	0.013	15.059	0.050	0.050	0.000	0.000	0.000	0.000
35	A	3529	GLY	0	0.039	0.044	16.219	-0.055	-0.055	0.000	0.000	0.000	0.000
36	A	3530	ASN	0	0.006	-0.027	17.634	0.048	0.048	0.000	0.000	0.000	0.000
37	A	3531	ASN	0	0.032	-0.005	18.142	-0.061	-0.061	0.000	0.000	0.000	0.000
38	A	3532	VAL	0	0.019	0.010	21.254	-0.034	-0.034	0.000	0.000	0.000	0.000
39	A	3533	LEU	0	-0.022	-0.002	23.942	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	3534	ALA	0	0.018	0.025	24.162	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	3535	HIS	0	-0.022	-0.006	25.839	-0.014	-0.014	0.000	0.000	0.000	0.000
42	A	3536	ARG	1	0.920	0.957	27.718	-0.203	-0.203	0.000	0.000	0.000	0.000
43	A	3537	SER	0	-0.068	-0.041	28.462	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	3538	LEU	0	-0.001	0.002	27.094	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	3539	PRO	0	0.007	0.003	31.215	0.000	0.000	0.000	0.000	0.000	0.000
46	A	3540	LEU	0	0.010	0.025	32.598	0.006	0.006	0.000	0.000	0.000	0.000
47	A	3541	SER	0	0.028	0.004	30.253	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	3542	GLU	-1	-0.904	-0.930	32.301	0.057	0.057	0.000	0.000	0.000	0.000
49	A	3543	GLY	0	0.016	-0.010	34.168	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	3544	GLY	0	0.006	0.002	37.198	0.002	0.002	0.000	0.000	0.000	0.000
51	A	3545	PRO	0	-0.040	-0.022	40.090	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	3546	PRO	0	-0.015	0.013	38.029	0.004	0.004	0.000	0.000	0.000	0.000
53	A	3547	LEU	0	0.026	0.011	32.175	0.001	0.001	0.000	0.000	0.000	0.000
54	A	3548	ARG	1	0.835	0.910	36.495	-0.052	-0.052	0.000	0.000	0.000	0.000
55	A	3549	ILE	0	0.003	0.014	34.801	0.003	0.003	0.000	0.000	0.000	0.000
56	A	3550	ALA	0	-0.021	-0.021	38.392	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	3551	GLN	0	-0.015	-0.003	39.197	0.000	0.000	0.000	0.000	0.000	0.000
58	A	3552	ARG	1	0.934	0.959	37.633	-0.046	-0.046	0.000	0.000	0.000	0.000
59	A	3553	MET	0	-0.012	0.016	31.784	0.000	0.000	0.000	0.000	0.000	0.000
60	A	3554	ARG	1	0.872	0.926	36.398	-0.051	-0.051	0.000	0.000	0.000	0.000
61	A	3555	LEU	0	-0.012	0.015	31.720	0.006	0.006	0.000	0.000	0.000	0.000
62	A	3556	GLU	-1	-0.794	-0.892	34.663	0.049	0.049	0.000	0.000	0.000	0.000
63	A	3557	ALA	0	0.047	0.014	33.746	0.006	0.006	0.000	0.000	0.000	0.000
64	A	3558	THR	0	0.060	0.032	33.149	0.006	0.006	0.000	0.000	0.000	0.000
65	A	3559	GLN	0	-0.015	-0.021	33.795	0.009	0.009	0.000	0.000	0.000	0.000
66	A	3560	LEU	0	0.007	0.001	29.771	0.008	0.008	0.000	0.000	0.000	0.000
67	A	3561	GLU	-1	-0.918	-0.960	29.061	0.098	0.098	0.000	0.000	0.000	0.000
68	A	3562	GLY	0	-0.046	-0.026	29.248	0.011	0.011	0.000	0.000	0.000	0.000
69	A	3563	VAL	0	-0.028	-0.019	26.465	0.010	0.010	0.000	0.000	0.000	0.000
70	A	3564	ALA	0	0.020	-0.002	24.948	0.015	0.015	0.000	0.000	0.000	0.000
71	A	3565	ARG	1	0.949	0.985	24.592	-0.102	-0.102	0.000	0.000	0.000	0.000
72	A	3566	ARG	1	0.911	0.960	25.710	-0.121	-0.121	0.000	0.000	0.000	0.000
73	A	3567	MET	0	-0.048	-0.016	20.945	0.005	0.005	0.000	0.000	0.000	0.000
74	A	3568	THR	0	-0.064	-0.031	20.515	0.025	0.025	0.000	0.000	0.000	0.000
75	A	3569	VAL	0	0.040	0.028	20.336	0.030	0.030	0.000	0.000	0.000	0.000
76	A	3570	GLU	-1	-0.943	-0.968	14.300	0.638	0.638	0.000	0.000	0.000	0.000
77	A	3571	THR	0	-0.035	-0.039	18.741	0.006	0.006	0.000	0.000	0.000	0.000
78	A	3572	ASP	-1	-0.852	-0.917	21.374	0.229	0.229	0.000	0.000	0.000	0.000
79	A	3573	TYR	0	-0.015	-0.015	17.532	-0.028	-0.028	0.000	0.000	0.000	0.000
80	A	3574	CYS	0	-0.032	0.012	20.961	0.037	0.037	0.000	0.000	0.000	0.000
81	A	3575	LEU	0	-0.034	-0.007	18.357	-0.031	-0.031	0.000	0.000	0.000	0.000
82	A	3576	LEU	0	0.016	-0.008	20.188	0.017	0.017	0.000	0.000	0.000	0.000
83	A	3577	LEU	0	0.001	0.013	21.063	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	3578	ALA	0	-0.019	-0.014	23.158	0.000	0.000	0.000	0.000	0.000	0.000
85	A	3579	LEU	0	0.015	-0.001	23.214	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	3580	PRO	0	0.037	0.017	27.483	0.005	0.005	0.000	0.000	0.000	0.000
87	A	3581	CYS	0	-0.048	-0.005	29.884	0.000	0.000	0.000	0.000	0.000	0.000
88	A	3582	GLY	0	0.047	0.003	31.922	0.000	0.000	0.000	0.000	0.000	0.000
89	A	3583	ARG	1	0.795	0.881	34.498	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	3584	ASP	-1	-0.804	-0.893	36.792	0.007	0.007	0.000	0.000	0.000	0.000
91	A	3585	GLN	0	0.011	-0.007	34.143	0.003	0.003	0.000	0.000	0.000	0.000
92	A	3586	GLU	-1	-0.866	-0.922	37.228	0.009	0.009	0.000	0.000	0.000	0.000
93	A	3587	ASP	-1	-0.796	-0.894	38.231	0.027	0.027	0.000	0.000	0.000	0.000
94	A	3588	VAL	0	-0.002	0.008	32.863	0.003	0.003	0.000	0.000	0.000	0.000
95	A	3589	VAL	0	0.006	0.020	35.709	0.002	0.002	0.000	0.000	0.000	0.000
96	A	3590	SER	0	0.023	0.012	37.606	0.001	0.001	0.000	0.000	0.000	0.000
97	A	3591	GLN	0	-0.032	-0.021	35.609	0.005	0.005	0.000	0.000	0.000	0.000
98	A	3592	THR	0	-0.032	-0.035	33.119	0.004	0.004	0.000	0.000	0.000	0.000
99	A	3593	GLU	-1	-0.831	-0.895	35.154	0.014	0.014	0.000	0.000	0.000	0.000
100	A	3594	SER	0	0.008	-0.002	38.191	0.001	0.001	0.000	0.000	0.000	0.000
101	A	3595	LEU	0	0.004	0.000	30.841	0.002	0.002	0.000	0.000	0.000	0.000
102	A	3596	LYS	1	0.826	0.890	34.572	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	3597	ALA	0	0.009	0.025	36.291	0.001	0.001	0.000	0.000	0.000	0.000
104	A	3598	ALA	0	-0.010	-0.006	39.383	0.000	0.000	0.000	0.000	0.000	0.000
105	A	3599	PHE	0	-0.081	-0.043	35.238	0.004	0.004	0.000	0.000	0.000	0.000
106	A	3600	ILE	0	0.009	0.005	31.649	0.002	0.002	0.000	0.000	0.000	0.000
107	A	3601	THR	0	0.014	-0.004	35.103	0.000	0.000	0.000	0.000	0.000	0.000
108	A	3602	TYR	0	-0.023	-0.007	38.369	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	3603	LEU	0	-0.031	-0.030	33.678	0.000	0.000	0.000	0.000	0.000	0.000
110	A	3604	GLN	0	0.011	-0.007	32.451	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	3605	ALA	0	-0.021	0.004	36.721	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	3606	LYS	1	0.837	0.916	39.840	-0.034	-0.034	0.000	0.000	0.000	0.000
113	A	3607	GLN	0	0.022	0.030	36.852	0.001	0.001	0.000	0.000	0.000	0.000
114	A	3608	ALA	0	-0.028	-0.036	36.258	0.003	0.003	0.000	0.000	0.000	0.000
115	A	3609	ALA	0	0.033	0.031	32.069	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	3610	GLY	0	0.007	-0.014	33.668	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	3611	ILE	0	-0.042	-0.025	33.563	0.007	0.007	0.000	0.000	0.000	0.000
118	A	3612	ILE	0	0.016	0.003	34.106	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	3613	ASN	0	-0.034	-0.012	34.442	0.012	0.012	0.000	0.000	0.000	0.000
120	A	3614	VAL	0	0.016	0.009	33.103	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	3615	PRO	0	0.004	0.009	35.778	0.005	0.005	0.000	0.000	0.000	0.000
122	A	3616	ASN	0	0.034	0.014	34.782	0.006	0.006	0.000	0.000	0.000	0.000
123	A	3617	PRO	0	0.033	-0.008	37.845	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	3618	GLY	0	0.007	0.009	40.926	0.002	0.002	0.000	0.000	0.000	0.000
125	A	3619	SER	0	-0.025	-0.009	40.399	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	3620	ASN	0	-0.016	-0.006	41.889	0.003	0.003	0.000	0.000	0.000	0.000
127	A	3621	GLN	0	-0.020	0.002	38.836	0.002	0.002	0.000	0.000	0.000	0.000
128	A	3622	PRO	0	-0.005	-0.009	36.687	0.002	0.002	0.000	0.000	0.000	0.000
129	A	3623	ALA	0	0.004	0.013	34.404	0.003	0.003	0.000	0.000	0.000	0.000
130	A	3624	TYR	0	0.037	0.009	29.451	0.015	0.015	0.000	0.000	0.000	0.000
131	A	3625	VAL	0	-0.039	-0.008	31.045	-0.011	-0.011	0.000	0.000	0.000	0.000
132	A	3626	LEU	0	0.004	0.005	29.596	0.011	0.011	0.000	0.000	0.000	0.000
133	A	3627	GLN	0	-0.014	-0.029	28.417	-0.013	-0.013	0.000	0.000	0.000	0.000
134	A	3628	ILE	0	-0.005	-0.008	28.815	0.007	0.007	0.000	0.000	0.000	0.000
135	A	3629	PHE	0	0.039	0.004	27.737	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	3630	PRO	0	0.020	0.031	29.226	0.001	0.001	0.000	0.000	0.000	0.000
137	A	3631	PRO	0	0.053	0.023	28.060	0.005	0.005	0.000	0.000	0.000	0.000
138	A	3632	CYS	0	-0.062	-0.018	27.998	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	3633	GLU	-1	-0.811	-0.911	27.410	0.047	0.047	0.000	0.000	0.000	0.000
140	A	3634	PHE	0	0.012	-0.002	26.148	0.007	0.007	0.000	0.000	0.000	0.000
141	A	3635	SER	0	0.065	-0.014	24.452	0.010	0.010	0.000	0.000	0.000	0.000
142	A	3636	GLU	-1	-0.877	-0.926	22.788	0.038	0.038	0.000	0.000	0.000	0.000
143	A	3637	SER	0	-0.021	0.011	21.659	0.007	0.007	0.000	0.000	0.000	0.000
144	A	3638	HIS	0	0.050	0.018	20.086	0.029	0.029	0.000	0.000	0.000	0.000
145	A	3639	LEU	0	0.022	0.007	18.394	0.030	0.030	0.000	0.000	0.000	0.000
146	A	3640	SER	0	-0.012	-0.015	17.134	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	3641	ARG	1	0.848	0.926	15.937	-0.258	-0.258	0.000	0.000	0.000	0.000
148	A	3642	LEU	0	-0.076	-0.047	14.049	0.041	0.041	0.000	0.000	0.000	0.000
149	A	3643	ALA	0	-0.007	0.006	13.158	0.055	0.055	0.000	0.000	0.000	0.000
150	A	3644	PRO	0	0.067	0.032	12.733	-0.042	-0.042	0.000	0.000	0.000	0.000
151	A	3645	ASP	-1	-0.781	-0.860	12.660	0.043	0.043	0.000	0.000	0.000	0.000
152	A	3646	LEU	0	-0.005	0.000	14.901	-0.017	-0.017	0.000	0.000	0.000	0.000
153	A	3647	LEU	0	0.014	0.022	17.258	-0.013	-0.013	0.000	0.000	0.000	0.000
154	A	3648	ALA	0	-0.007	0.004	18.022	-0.009	-0.009	0.000	0.000	0.000	0.000
155	A	3649	SER	0	-0.089	-0.053	19.301	-0.008	-0.008	0.000	0.000	0.000	0.000
156	A	3650	ILE	0	0.013	-0.005	21.040	0.003	0.003	0.000	0.000	0.000	0.000
157	A	3651	SER	0	-0.006	-0.009	22.998	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	3652	ASN	0	-0.082	-0.045	24.811	-0.008	-0.008	0.000	0.000	0.000	0.000
159	A	3653	ILE	0	-0.020	0.011	24.399	-0.007	-0.007	0.000	0.000	0.000	0.000
160	A	3654	SER	0	-0.001	-0.008	26.296	-0.002	-0.002	0.000	0.000	0.000	0.000
161	A	3655	PRO	0	-0.034	-0.013	27.842	0.007	0.007	0.000	0.000	0.000	0.000
162	A	3656	HIS	0	-0.011	-0.019	25.774	0.008	0.008	0.000	0.000	0.000	0.000
163	A	3657	LEU	0	-0.013	-0.002	27.419	-0.003	-0.003	0.000	0.000	0.000	0.000
164	A	3658	MET	0	-0.020	0.037	23.031	0.007	0.007	0.000	0.000	0.000	0.000
165	A	3659	ILE	0	-0.024	-0.020	25.003	-0.006	-0.006	0.000	0.000	0.000	0.000
166	A	3660	VAL	0	0.030	0.021	23.980	0.017	0.017	0.000	0.000	0.000	0.000
167	A	3661	ILE	0	-0.033	0.000	25.022	-0.016	-0.016	0.000	0.000	0.000	0.000
168	A	3662	ALA	0	0.008	-0.003	25.492	0.018	0.018	0.000	0.000	0.000	0.000
169	A	3663	SER	0	0.015	0.005	27.570	-0.008	-0.008	0.000	0.000	0.000	0.000
170	A	3664	VAL	0	-0.035	-0.007	29.476	0.001	0.001	0.000	0.000	0.000	0.000

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