FMO DATABASE

FMODB ID: 8959Y

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	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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1275811.148528
FMO2-HF: Nuclear repulsion	1220245.694934
FMO2-HF: Total energy	-55565.453594
FMO2-MP2: Total energy	-55728.885838

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.
-44.533	-36.992	23.104	-13.624	-17.021	-0.085

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 : -0.026 / q_NPA : -0.020

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	-0.005	-0.010	3.853	-0.562	2.515	-0.022	-1.627	-1.428	0.008
4	A	5	TYR	0	-0.023	-0.027	5.255	0.425	0.425	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.011	-0.009	9.553	-0.138	-0.138	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.014	0.008	11.081	0.158	0.158	0.000	0.000	0.000	0.000
7	A	8	TYR	0	-0.020	-0.009	14.664	-0.074	-0.074	0.000	0.000	0.000	0.000
8	A	9	CYS	0	-0.005	0.013	17.068	0.083	0.083	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.897	0.938	19.404	-0.214	-0.214	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.979	0.970	22.518	0.022	0.022	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.031	0.027	24.393	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.065	-0.034	20.733	0.022	0.022	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.060	0.044	16.832	0.044	0.044	0.000	0.000	0.000	0.000
14	A	15	GLN	0	0.053	0.027	16.683	0.010	0.010	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.981	0.984	16.982	-0.060	-0.060	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.014	-0.010	15.027	0.067	0.067	0.000	0.000	0.000	0.000
17	A	18	GLN	0	-0.019	-0.022	12.328	0.144	0.144	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.826	-0.895	12.310	0.069	0.069	0.000	0.000	0.000	0.000
19	A	20	HIS	0	-0.064	-0.047	13.457	0.109	0.109	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.026	-0.021	9.042	0.194	0.194	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.792	-0.897	8.778	-0.390	-0.390	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.766	0.872	10.118	-0.105	-0.105	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.055	-0.014	8.925	0.523	0.523	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.001	-0.007	5.799	-0.250	-0.250	0.000	0.000	0.000	0.000
25	A	26	VAL	0	-0.036	-0.008	4.269	-0.438	-0.251	-0.001	-0.014	-0.172	0.000
26	A	27	ASN	0	0.008	0.012	2.972	2.563	3.102	0.020	-0.177	-0.382	0.000
27	A	28	CYS	0	-0.054	-0.026	5.483	0.466	0.466	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.001	0.002	8.791	-0.101	-0.101	0.000	0.000	0.000	0.000
29	A	30	ALA	0	0.040	0.015	11.665	0.096	0.096	0.000	0.000	0.000	0.000
30	A	31	PRO	0	0.004	0.008	14.747	0.054	0.054	0.000	0.000	0.000	0.000
31	A	32	MET	0	-0.020	0.013	17.293	0.092	0.092	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.040	0.021	20.963	-0.045	-0.045	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.018	-0.011	23.840	0.021	0.021	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.034	0.024	27.214	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.854	-0.905	30.504	-0.183	-0.183	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.846	0.906	30.524	0.217	0.217	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.003	-0.010	35.271	0.007	0.007	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.010	0.016	35.414	0.006	0.006	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.940	0.941	38.084	0.097	0.097	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.019	0.012	41.821	0.003	0.003	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.950	0.980	41.632	0.107	0.107	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.906	0.946	38.014	0.178	0.178	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.015	-0.002	35.299	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.040	0.025	32.583	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.028	-0.018	29.702	0.010	0.010	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.043	-0.037	25.232	-0.025	-0.025	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.794	-0.874	25.608	-0.239	-0.239	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.039	0.002	21.043	-0.033	-0.033	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.032	-0.007	19.292	0.026	0.026	0.000	0.000	0.000	0.000
50	A	51	PHE	0	0.082	0.019	17.769	0.010	0.010	0.000	0.000	0.000	0.000
51	A	52	PRO	0	-0.022	0.002	20.138	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	53	ASN	0	-0.047	-0.019	20.561	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.020	-0.023	17.053	0.049	0.049	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.031	-0.020	11.503	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	56	PHE	0	-0.010	0.003	10.621	0.125	0.125	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.009	-0.009	7.202	0.006	0.006	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.822	-0.909	2.038	-23.601	-22.360	6.729	-3.565	-4.405	-0.041
58	A	59	PHE	0	0.014	0.003	2.487	-7.540	-4.662	2.570	-2.497	-2.951	0.009
59	A	60	ASP	-1	-0.730	-0.863	1.852	-14.184	-14.692	13.711	-5.849	-7.354	-0.061
60	A	61	PRO	0	-0.060	-0.039	3.233	-0.732	-0.681	0.098	0.106	-0.255	0.000
61	A	62	GLU	-1	-0.906	-0.947	5.775	1.205	1.205	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.074	-0.028	5.129	-0.312	-0.236	-0.001	-0.001	-0.074	0.000
63	A	64	ILE	0	-0.042	-0.033	5.843	-1.041	-1.041	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.086	0.063	7.758	-0.571	-0.571	0.000	0.000	0.000	0.000
65	A	66	THR	0	0.003	-0.013	10.096	-0.119	-0.119	0.000	0.000	0.000	0.000
66	A	67	THR	0	-0.018	-0.019	11.658	-0.177	-0.177	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.008	0.002	11.335	-0.266	-0.266	0.000	0.000	0.000	0.000
68	A	69	ILE	0	0.033	0.040	7.715	-0.260	-0.260	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.031	-0.031	11.778	-0.289	-0.289	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.017	0.004	15.275	-0.123	-0.123	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.020	0.008	13.127	-0.039	-0.039	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.944	0.964	15.758	-0.403	-0.403	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.006	-0.026	18.698	-0.038	-0.038	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.055	0.045	13.999	-0.071	-0.071	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.090	-0.057	17.382	0.033	0.033	0.000	0.000	0.000	0.000
76	A	77	HIS	0	0.012	0.017	18.244	0.079	0.079	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.052	0.036	9.998	-0.083	-0.083	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.023	-0.005	15.506	0.012	0.012	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.893	0.934	15.187	-0.154	-0.154	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.044	0.020	16.093	-0.040	-0.040	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.012	0.013	17.286	0.016	0.016	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.010	-0.016	18.270	0.020	0.020	0.000	0.000	0.000	0.000
83	A	84	SER	0	-0.012	0.013	18.440	0.038	0.038	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.046	0.008	14.226	0.056	0.056	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.024	0.023	11.528	-0.052	-0.052	0.000	0.000	0.000	0.000
86	A	87	ILE	0	-0.056	-0.034	12.275	-0.083	-0.083	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.072	0.050	7.876	0.035	0.035	0.000	0.000	0.000	0.000
88	A	89	PRO	0	-0.043	-0.013	9.856	0.059	0.059	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.048	0.021	10.149	-0.318	-0.318	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.054	0.012	9.412	0.017	0.017	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.020	0.005	10.477	0.012	0.012	0.000	0.000	0.000	0.000
92	A	93	ILE	0	0.010	0.005	13.445	0.101	0.101	0.000	0.000	0.000	0.000
93	A	94	HIS	0	0.033	0.020	9.606	0.121	0.121	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.023	-0.014	12.379	0.164	0.164	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.056	-0.035	14.271	0.103	0.103	0.000	0.000	0.000	0.000
96	A	97	SER	0	-0.022	-0.010	14.677	0.113	0.113	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.034	-0.015	13.484	0.051	0.051	0.000	0.000	0.000	0.000
98	A	99	TYR	0	-0.015	-0.005	12.699	0.069	0.069	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.941	1.000	18.678	0.803	0.803	0.000	0.000	0.000	0.000
100	A	115	LYS	1	0.985	0.971	21.653	0.525	0.525	0.000	0.000	0.000	0.000
101	A	116	VAL	0	0.029	0.040	22.852	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	117	ILE	0	0.076	0.037	23.579	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	118	ILE	0	-0.016	0.006	18.165	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	119	THR	0	-0.063	-0.048	21.071	-0.047	-0.047	0.000	0.000	0.000	0.000
105	A	120	GLU	-1	-0.873	-0.945	22.844	-0.379	-0.379	0.000	0.000	0.000	0.000
106	A	121	GLY	0	0.023	0.019	23.214	0.011	0.011	0.000	0.000	0.000	0.000
107	A	122	ALA	0	0.000	-0.016	19.071	0.001	0.001	0.000	0.000	0.000	0.000
108	A	123	PHE	0	-0.037	-0.030	21.068	-0.018	-0.018	0.000	0.000	0.000	0.000
109	A	124	GLU	-1	-0.893	-0.940	23.761	-0.340	-0.340	0.000	0.000	0.000	0.000
110	A	125	GLY	0	-0.027	-0.009	23.015	0.021	0.021	0.000	0.000	0.000	0.000
111	A	126	PHE	0	0.011	-0.014	16.780	0.006	0.006	0.000	0.000	0.000	0.000
112	A	127	GLN	0	-0.024	-0.004	22.575	0.017	0.017	0.000	0.000	0.000	0.000
113	A	128	ALA	0	-0.001	0.016	26.208	0.025	0.025	0.000	0.000	0.000	0.000
114	A	129	ILE	0	-0.034	-0.020	20.879	0.019	0.019	0.000	0.000	0.000	0.000
115	A	130	PHE	0	-0.023	-0.035	20.154	0.017	0.017	0.000	0.000	0.000	0.000
116	A	131	THR	0	-0.039	-0.017	25.704	0.022	0.022	0.000	0.000	0.000	0.000
117	A	132	GLU	-1	-0.881	-0.934	27.824	-0.218	-0.218	0.000	0.000	0.000	0.000
118	A	133	PRO	0	0.014	0.010	28.988	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	134	ASP	-1	-0.858	-0.937	29.536	-0.204	-0.204	0.000	0.000	0.000	0.000
120	A	135	GLY	0	0.064	0.030	25.667	-0.021	-0.021	0.000	0.000	0.000	0.000
121	A	136	GLU	-1	-0.796	-0.899	24.209	-0.245	-0.245	0.000	0.000	0.000	0.000
122	A	137	ALA	0	-0.013	-0.001	26.441	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	138	ARG	1	0.751	0.875	23.524	0.311	0.311	0.000	0.000	0.000	0.000
124	A	139	SER	0	-0.014	-0.034	21.834	-0.053	-0.053	0.000	0.000	0.000	0.000
125	A	140	MET	0	-0.023	0.003	22.326	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	141	LEU	0	0.019	0.013	24.261	-0.011	-0.011	0.000	0.000	0.000	0.000
127	A	142	LEU	0	0.007	0.012	16.811	-0.028	-0.028	0.000	0.000	0.000	0.000
128	A	143	LEU	0	-0.015	-0.011	19.035	-0.042	-0.042	0.000	0.000	0.000	0.000
129	A	144	ASN	0	-0.087	-0.058	20.805	0.005	0.005	0.000	0.000	0.000	0.000
130	A	145	LEU	0	-0.028	0.003	18.947	0.004	0.004	0.000	0.000	0.000	0.000
131	A	146	ILE	0	0.034	0.012	15.259	-0.025	-0.025	0.000	0.000	0.000	0.000
132	A	147	ASN	0	-0.006	-0.005	18.027	-0.012	-0.012	0.000	0.000	0.000	0.000
133	A	148	LYS	1	0.940	0.977	20.465	0.403	0.403	0.000	0.000	0.000	0.000
134	A	149	GLU	-1	-0.815	-0.926	17.398	-0.577	-0.577	0.000	0.000	0.000	0.000
135	A	150	ILE	0	0.004	0.011	14.626	-0.029	-0.029	0.000	0.000	0.000	0.000
136	A	151	LYS	1	0.832	0.922	17.215	0.354	0.354	0.000	0.000	0.000	0.000
137	A	152	HIS	0	0.024	0.021	19.586	0.058	0.058	0.000	0.000	0.000	0.000
138	A	153	SER	0	-0.021	-0.024	15.047	-0.031	-0.031	0.000	0.000	0.000	0.000
139	A	154	VAL	0	-0.039	-0.003	17.068	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	155	LYS	1	0.910	0.946	18.652	0.318	0.318	0.000	0.000	0.000	0.000
141	A	156	ASN	0	-0.049	-0.003	19.478	0.013	0.013	0.000	0.000	0.000	0.000

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