FMO DATABASE

FMODB ID: 66Q3Z

Calculation Name: 4O2H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4O2H

Chain ID: A

ChEMBL ID:

UniProt ID: B4EMD1

Base Structure: X-ray

Registration Date: 2023-06-20

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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1014357.455428
FMO2-HF: Nuclear repulsion	965227.829112
FMO2-HF: Total energy	-49129.626317
FMO2-MP2: Total energy	-49275.212509

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:2:THR)

Summations of interaction energy for fragment #1(A:2: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.
-2.999	2.566	1.222	-2.716	-4.071	0.011

Interaction energy analysis for fragmet #1(A:2:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.062 / q_NPA : 0.029

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	4	PRO	0	0.061	0.005	3.560	1.678	3.798	0.049	-1.140	-1.030	0.005
4	A	5	LEU	0	-0.002	-0.003	6.167	0.160	0.160	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.023	-0.002	2.620	-1.617	-0.653	0.987	-0.579	-1.372	0.006
6	A	7	HIS	0	-0.068	-0.020	2.951	-3.413	-1.029	0.187	-0.992	-1.578	0.000
7	A	8	PRO	0	0.025	0.009	5.021	0.239	0.336	-0.001	-0.005	-0.091	0.000
8	A	9	VAL	0	0.019	0.013	7.843	0.020	0.020	0.000	0.000	0.000	0.000
9	A	10	PRO	0	-0.069	-0.007	11.236	-0.012	-0.012	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.039	0.006	13.504	0.041	0.041	0.000	0.000	0.000	0.000
11	A	12	PRO	0	-0.030	-0.030	17.148	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.024	-0.016	19.535	-0.014	-0.014	0.000	0.000	0.000	0.000
13	A	14	PRO	0	-0.020	-0.029	20.467	0.010	0.010	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.802	-0.877	23.160	-0.078	-0.078	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.009	0.015	24.519	0.007	0.007	0.000	0.000	0.000	0.000
16	A	17	TYR	0	-0.005	-0.004	24.504	0.002	0.002	0.000	0.000	0.000	0.000
17	A	18	VAL	0	-0.008	0.001	19.171	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.737	0.821	20.423	0.109	0.109	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.009	-0.004	19.426	-0.020	-0.020	0.000	0.000	0.000	0.000
20	A	21	SER	0	0.034	0.016	21.363	0.014	0.014	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.808	-0.890	23.295	-0.079	-0.079	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.001	-0.002	24.994	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	ALA	0	-0.012	-0.009	20.432	0.001	0.001	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.017	-0.009	22.279	0.006	0.006	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.026	0.010	25.006	0.009	0.009	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.028	-0.014	22.722	0.007	0.007	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.031	0.000	21.865	0.000	0.000	0.000	0.000	0.000	0.000
28	A	29	VAL	0	0.013	0.014	21.802	0.008	0.008	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.021	-0.017	23.545	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.896	-0.938	24.113	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	32	HIS	0	0.041	0.036	27.353	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	33	VAL	0	-0.077	-0.033	27.738	0.004	0.004	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.023	-0.023	30.541	0.003	0.003	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.064	0.010	34.205	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.001	0.016	37.589	0.002	0.002	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.011	-0.009	41.038	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.816	-0.905	44.273	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	39	PRO	0	-0.029	-0.024	46.127	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	40	SER	0	0.016	0.009	48.609	0.000	0.000	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.039	0.022	44.051	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.066	-0.030	48.169	0.000	0.000	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.040	-0.023	50.265	0.000	0.000	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.901	-0.949	48.868	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.003	-0.002	46.961	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	ARG	1	0.797	0.899	51.350	0.010	0.010	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.952	-0.962	54.856	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	48	ASN	0	-0.089	-0.051	52.536	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	49	ALA	0	-0.038	-0.019	54.310	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.017	0.019	49.254	0.000	0.000	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.824	-0.879	53.149	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	52	ALA	0	0.010	0.007	49.713	0.000	0.000	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.859	0.937	49.553	0.012	0.012	0.000	0.000	0.000	0.000
53	A	54	LEU	0	-0.020	-0.023	47.375	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.050	0.017	45.653	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.015	0.014	43.233	0.002	0.002	0.000	0.000	0.000	0.000
56	A	57	TYR	0	0.086	0.068	36.915	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	58	THR	0	-0.034	-0.029	35.229	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.732	-0.832	31.483	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	60	TRP	0	-0.001	0.014	29.044	0.003	0.003	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.009	0.003	24.361	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.913	0.964	18.311	0.103	0.103	0.000	0.000	0.000	0.000
62	A	63	THR	0	0.021	0.004	18.663	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	64	ALA	0	-0.006	-0.006	15.701	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.033	0.008	13.007	0.038	0.038	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.007	0.013	7.587	-0.063	-0.063	0.000	0.000	0.000	0.000
66	A	67	GLY	0	-0.015	-0.012	9.570	-0.056	-0.056	0.000	0.000	0.000	0.000
67	A	68	VAL	0	-0.061	-0.031	10.658	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.047	0.032	14.367	0.034	0.034	0.000	0.000	0.000	0.000
69	A	70	TYR	0	-0.013	-0.016	16.628	0.007	0.007	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.030	-0.009	19.538	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.023	-0.005	22.746	0.010	0.010	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.002	-0.025	26.386	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.043	0.029	29.532	0.004	0.004	0.000	0.000	0.000	0.000
74	A	75	TRP	0	-0.046	-0.029	32.176	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	76	ASP	-1	-0.821	-0.903	36.678	-0.018	-0.018	0.000	0.000	0.000	0.000
76	A	77	TRP	0	-0.100	-0.046	39.398	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	78	TYR	0	0.005	-0.026	42.171	0.002	0.002	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.022	0.004	45.100	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.787	-0.875	47.234	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.791	0.849	50.338	0.011	0.011	0.000	0.000	0.000	0.000
81	A	82	ALA	0	-0.026	-0.010	53.704	0.000	0.000	0.000	0.000	0.000	0.000
82	A	83	THR	0	0.006	-0.026	50.120	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	GLY	0	-0.040	-0.011	50.007	0.000	0.000	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.009	0.005	45.316	0.000	0.000	0.000	0.000	0.000	0.000
85	A	86	PHE	0	0.039	0.009	41.993	0.001	0.001	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.040	-0.015	42.769	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.005	0.000	36.742	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.021	0.002	40.948	0.000	0.000	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.035	0.027	41.759	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	91	GLY	0	-0.043	-0.028	40.054	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.956	-0.976	37.764	-0.035	-0.035	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.021	-0.025	32.221	0.001	0.001	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.768	0.866	31.852	0.024	0.024	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.029	0.001	27.793	0.002	0.002	0.000	0.000	0.000	0.000
95	A	96	ASN	0	0.005	0.010	22.614	0.003	0.003	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.005	-0.005	23.983	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	98	MET	0	-0.010	0.020	24.953	0.009	0.009	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.015	0.001	24.918	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.014	-0.005	21.261	0.003	0.003	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.815	-0.933	25.866	-0.104	-0.104	0.000	0.000	0.000	0.000
101	A	102	ALA	0	-0.038	-0.018	25.235	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.898	0.940	24.771	0.075	0.075	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.000	0.014	23.297	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	105	ALA	0	-0.024	-0.007	24.087	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.775	-0.865	26.405	-0.095	-0.095	0.000	0.000	0.000	0.000
106	A	107	ILE	0	-0.074	-0.042	28.386	0.006	0.006	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.038	0.020	30.658	0.005	0.005	0.000	0.000	0.000	0.000
108	A	109	MET	0	0.048	0.021	30.875	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	110	LEU	0	0.040	0.028	33.119	0.000	0.000	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.885	0.918	31.850	0.072	0.072	0.000	0.000	0.000	0.000
111	A	112	THR	0	-0.003	-0.008	28.340	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.023	0.020	30.911	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.034	0.020	33.483	0.002	0.002	0.000	0.000	0.000	0.000
114	A	115	ALA	0	-0.018	-0.012	29.901	0.001	0.001	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.016	-0.008	27.487	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.059	0.032	31.019	0.002	0.002	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.022	-0.010	33.230	0.002	0.002	0.000	0.000	0.000	0.000
118	A	119	ARG	1	0.821	0.899	26.042	0.067	0.067	0.000	0.000	0.000	0.000
119	A	120	LEU	0	0.025	0.007	30.893	0.002	0.002	0.000	0.000	0.000	0.000
120	A	121	ALA	0	-0.027	-0.010	32.644	0.004	0.004	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.079	-0.038	31.548	0.002	0.002	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.072	-0.037	27.911	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.874	-0.940	32.246	-0.018	-0.018	0.000	0.000	0.000	0.000
124	A	125	TRP	0	0.038	0.008	34.509	0.004	0.004	0.000	0.000	0.000	0.000
125	A	126	PRO	0	-0.012	-0.006	35.733	0.002	0.002	0.000	0.000	0.000	0.000
126	A	127	ALA	0	0.024	0.029	37.621	0.002	0.002	0.000	0.000	0.000	0.000
127	A	128	ALA	0	-0.004	-0.003	34.345	0.002	0.002	0.000	0.000	0.000	0.000
128	A	129	VAL	0	0.007	0.006	36.329	0.002	0.002	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.013	-0.010	38.397	0.002	0.002	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.011	-0.013	37.905	0.002	0.002	0.000	0.000	0.000	0.000
131	A	132	ALA	0	-0.038	-0.014	36.643	0.002	0.002	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.060	-0.035	38.622	0.001	0.001	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.028	-0.009	42.030	0.001	0.001	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.041	0.033	40.508	0.001	0.001	0.000	0.000	0.000	0.000
135	A	136	HIS	0	-0.051	-0.035	38.985	0.002	0.002	0.000	0.000	0.000	0.000
136	A	137	ASN	0	-0.117	-0.059	42.940	0.000	0.000	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-1.006	-0.982	43.334	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:2:THR)