FMO DATABASE

FMODB ID: G5651

Calculation Name: 2OUG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OUG

Chain ID: A

ChEMBL ID:

UniProt ID: P0AFW0

Base Structure: X-ray

Registration Date: 2023-09-21

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1278793.642897
FMO2-HF: Nuclear repulsion	1223229.528171
FMO2-HF: Total energy	-55564.114726
FMO2-MP2: Total energy	-55727.756831

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:GLN)

Summations of interaction energy for fragment #1(A:2:GLN)

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.
-25.636	-20.396	15.095	-8.889	-11.446	-0.046

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.003 / q_NPA : -0.023

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	TRP	0	0.004	-0.003	3.766	0.283	2.608	-0.036	-1.143	-1.146	0.004
4	A	5	TYR	0	-0.067	-0.040	4.825	-0.357	-0.357	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.015	0.010	9.489	0.038	0.038	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.002	0.013	11.969	-0.057	-0.057	0.000	0.000	0.000	0.000
7	A	8	TYR	0	0.023	0.023	14.912	-0.081	-0.081	0.000	0.000	0.000	0.000
8	A	9	CYS	0	-0.037	-0.023	17.945	0.063	0.063	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.923	0.945	20.231	-0.511	-0.511	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.973	0.975	23.572	-0.188	-0.188	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.064	0.027	25.486	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.098	-0.039	21.788	0.017	0.017	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.063	0.060	18.326	0.039	0.039	0.000	0.000	0.000	0.000
14	A	15	GLN	0	0.045	0.014	18.373	0.062	0.062	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.967	0.976	19.016	-0.284	-0.284	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.015	0.000	16.418	0.032	0.032	0.000	0.000	0.000	0.000
17	A	18	GLN	0	-0.043	-0.036	13.942	0.117	0.117	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.796	-0.876	13.779	0.443	0.443	0.000	0.000	0.000	0.000
19	A	20	HIS	0	-0.061	-0.037	14.135	-0.051	-0.051	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.039	-0.033	10.233	0.060	0.060	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.782	-0.877	9.782	0.872	0.872	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.756	0.860	10.802	-0.538	-0.538	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.062	-0.017	9.623	0.199	0.199	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.012	-0.014	5.610	0.029	0.029	0.000	0.000	0.000	0.000
25	A	26	VAL	0	-0.057	-0.011	5.434	0.091	0.091	0.000	0.000	0.000	0.000
26	A	27	ASN	0	-0.012	0.009	4.242	-1.061	-0.983	-0.001	-0.006	-0.071	0.000
27	A	28	CYS	0	-0.033	-0.008	7.362	0.408	0.408	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.007	-0.004	10.967	-0.229	-0.229	0.000	0.000	0.000	0.000
29	A	30	ALA	0	0.032	0.013	12.923	0.021	0.021	0.000	0.000	0.000	0.000
30	A	31	PRO	0	-0.007	-0.004	15.558	-0.040	-0.040	0.000	0.000	0.000	0.000
31	A	32	MET	0	-0.022	0.013	18.466	0.018	0.018	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.010	0.000	22.159	-0.021	-0.021	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.021	-0.014	24.750	0.005	0.005	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.043	0.025	28.004	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.893	-0.931	30.809	0.018	0.018	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.968	0.993	32.836	-0.084	-0.084	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.019	-0.027	35.724	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.006	0.011	36.641	0.005	0.005	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.953	0.958	39.147	-0.056	-0.056	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.002	0.010	42.883	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.955	0.977	42.254	-0.038	-0.038	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.963	0.976	38.923	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.035	-0.017	36.751	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.064	0.035	33.442	0.004	0.004	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.066	-0.045	30.668	0.004	0.004	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.049	0.025	25.826	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.877	-0.915	26.702	0.105	0.105	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.043	0.007	21.946	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.022	-0.002	19.597	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	51	PHE	0	0.092	0.023	17.986	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.065	0.023	20.611	0.036	0.036	0.000	0.000	0.000	0.000
52	A	53	ASN	0	-0.055	0.008	20.977	0.013	0.013	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.074	-0.044	17.132	0.053	0.053	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.013	-0.015	12.538	-0.030	-0.030	0.000	0.000	0.000	0.000
55	A	56	PHE	0	-0.005	0.000	10.512	0.085	0.085	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.001	-0.021	8.364	0.013	0.013	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.822	-0.904	2.475	-1.749	-1.047	0.396	-0.249	-0.849	-0.001
58	A	59	PHE	0	0.019	0.009	2.541	-1.732	-0.060	1.253	-1.102	-1.823	0.010
59	A	60	ASP	-1	-0.764	-0.899	1.863	-19.190	-18.692	13.390	-6.584	-7.303	-0.059
60	A	61	PRO	0	-0.056	-0.032	3.178	-0.800	-0.835	0.093	0.195	-0.254	0.000
61	A	62	GLU	-1	-0.907	-0.951	5.908	0.102	0.102	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.085	-0.024	5.350	-0.026	-0.026	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.009	0.006	6.154	-0.523	-0.523	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.058	0.041	7.799	0.216	0.216	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.023	-0.032	9.767	-0.128	-0.128	0.000	0.000	0.000	0.000
66	A	67	THR	0	-0.023	-0.025	11.562	0.008	0.008	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.029	0.013	11.834	-0.179	-0.179	0.000	0.000	0.000	0.000
68	A	69	ILE	0	0.030	0.024	8.193	-0.184	-0.184	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.003	-0.018	12.300	-0.153	-0.153	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.036	-0.003	15.872	-0.092	-0.092	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.009	0.020	13.659	-0.078	-0.078	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.949	0.959	16.342	-0.514	-0.514	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.034	-0.001	19.257	0.001	0.001	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.018	0.025	14.977	-0.058	-0.058	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.098	-0.062	18.335	-0.030	-0.030	0.000	0.000	0.000	0.000
76	A	77	HIS	0	-0.018	0.010	17.833	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.043	0.034	9.771	-0.027	-0.027	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.007	0.013	14.853	-0.090	-0.090	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.901	0.925	14.638	-0.368	-0.368	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.032	0.018	15.149	-0.037	-0.037	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.010	0.005	16.040	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.017	0.005	17.312	0.029	0.029	0.000	0.000	0.000	0.000
83	A	84	SER	0	-0.015	-0.006	17.995	0.045	0.045	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.039	0.013	13.107	0.056	0.056	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.042	0.046	11.148	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	87	ILE	0	-0.104	-0.053	11.651	-0.079	-0.079	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.102	0.040	7.208	0.136	0.136	0.000	0.000	0.000	0.000
88	A	89	PRO	0	-0.084	-0.023	9.692	-0.096	-0.096	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.079	0.028	9.613	-0.110	-0.110	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.066	0.018	8.759	0.039	0.039	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.003	-0.009	10.060	0.023	0.023	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.008	-0.001	13.585	0.029	0.029	0.000	0.000	0.000	0.000
93	A	94	HIS	0	0.029	0.015	9.560	0.087	0.087	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.037	-0.014	12.576	0.037	0.037	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.057	-0.038	14.285	0.007	0.007	0.000	0.000	0.000	0.000
96	A	97	SER	0	-0.009	0.012	14.981	0.037	0.037	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.039	-0.017	14.008	0.014	0.014	0.000	0.000	0.000	0.000
98	A	99	TYR	0	0.002	0.000	12.887	0.017	0.017	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.963	1.010	19.212	0.168	0.168	0.000	0.000	0.000	0.000
100	A	115	LYS	1	0.988	0.973	21.354	0.171	0.171	0.000	0.000	0.000	0.000
101	A	116	VAL	0	0.055	0.028	22.617	0.002	0.002	0.000	0.000	0.000	0.000
102	A	117	ILE	0	0.057	0.039	22.945	0.007	0.007	0.000	0.000	0.000	0.000
103	A	118	ILE	0	-0.025	0.002	17.347	0.003	0.003	0.000	0.000	0.000	0.000
104	A	119	THR	0	-0.065	-0.053	20.713	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	120	GLU	-1	-0.911	-0.964	22.384	-0.060	-0.060	0.000	0.000	0.000	0.000
106	A	121	GLY	0	0.004	0.032	22.734	0.011	0.011	0.000	0.000	0.000	0.000
107	A	122	ALA	0	0.014	-0.017	19.033	0.014	0.014	0.000	0.000	0.000	0.000
108	A	123	PHE	0	-0.036	-0.038	20.960	0.006	0.006	0.000	0.000	0.000	0.000
109	A	124	GLU	-1	-0.885	-0.937	23.682	-0.025	-0.025	0.000	0.000	0.000	0.000
110	A	125	GLY	0	-0.026	0.003	23.288	0.011	0.011	0.000	0.000	0.000	0.000
111	A	126	PHE	0	0.019	-0.021	16.931	0.013	0.013	0.000	0.000	0.000	0.000
112	A	127	GLN	0	-0.028	-0.002	23.005	0.007	0.007	0.000	0.000	0.000	0.000
113	A	128	ALA	0	0.022	0.031	26.494	0.006	0.006	0.000	0.000	0.000	0.000
114	A	129	ILE	0	-0.019	-0.008	21.097	0.010	0.010	0.000	0.000	0.000	0.000
115	A	130	PHE	0	-0.041	-0.038	20.618	0.012	0.012	0.000	0.000	0.000	0.000
116	A	131	THR	0	-0.060	-0.033	25.998	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	132	GLU	-1	-0.920	-0.960	27.847	0.061	0.061	0.000	0.000	0.000	0.000
118	A	133	PRO	0	0.009	0.023	28.782	0.008	0.008	0.000	0.000	0.000	0.000
119	A	134	ASP	-1	-0.915	-0.949	29.713	0.110	0.110	0.000	0.000	0.000	0.000
120	A	135	GLY	0	0.097	0.027	25.742	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	136	GLU	-1	-0.882	-0.934	24.970	0.212	0.212	0.000	0.000	0.000	0.000
122	A	137	ALA	0	0.018	0.015	26.579	0.006	0.006	0.000	0.000	0.000	0.000
123	A	138	ARG	1	0.707	0.808	23.742	-0.099	-0.099	0.000	0.000	0.000	0.000
124	A	139	SER	0	-0.005	-0.027	21.810	0.000	0.000	0.000	0.000	0.000	0.000
125	A	140	MET	0	-0.039	0.003	22.164	0.009	0.009	0.000	0.000	0.000	0.000
126	A	141	LEU	0	0.051	0.029	23.795	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	142	LEU	0	0.001	0.007	16.794	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	143	LEU	0	0.012	-0.001	18.545	-0.009	-0.009	0.000	0.000	0.000	0.000
129	A	144	ASN	0	-0.106	-0.063	20.379	-0.021	-0.021	0.000	0.000	0.000	0.000
130	A	145	LEU	0	-0.002	0.011	19.118	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	146	ILE	0	0.037	0.020	14.875	-0.022	-0.022	0.000	0.000	0.000	0.000
132	A	147	ASN	0	-0.006	-0.011	17.530	-0.028	-0.028	0.000	0.000	0.000	0.000
133	A	148	LYS	1	0.908	0.958	19.567	-0.034	-0.034	0.000	0.000	0.000	0.000
134	A	149	GLU	-1	-0.807	-0.922	16.883	-0.072	-0.072	0.000	0.000	0.000	0.000
135	A	150	ILE	0	-0.031	-0.011	13.884	-0.026	-0.026	0.000	0.000	0.000	0.000
136	A	151	LYS	1	0.851	0.923	16.225	-0.055	-0.055	0.000	0.000	0.000	0.000
137	A	152	HIS	0	0.035	0.026	18.817	0.003	0.003	0.000	0.000	0.000	0.000
138	A	153	SER	0	0.007	-0.002	14.060	-0.025	-0.025	0.000	0.000	0.000	0.000
139	A	154	VAL	0	-0.045	-0.016	15.645	-0.009	-0.009	0.000	0.000	0.000	0.000
140	A	155	LYS	1	0.917	0.953	17.563	0.022	0.022	0.000	0.000	0.000	0.000
141	A	156	ASN	0	-0.063	-0.005	18.731	-0.014	-0.014	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:GLN)