FMO DATABASE

FMODB ID: 1N7NZ

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:

Apendix: None

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1280488.604112
FMO2-HF: Nuclear repulsion	1224926.239815
FMO2-HF: Total energy	-55562.364297
FMO2-MP2: Total energy	-55726.305807

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.
-16.383	-20.458	25.832	-11.364	-10.391	-0.061

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 : -0.039 / q_NPA : -0.026

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	0.006	0.009	3.766	-1.901	1.326	-0.042	-1.648	-1.537	0.009
4	A	5	TYR	0	-0.058	-0.024	4.805	-0.609	-0.609	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.026	0.015	9.478	0.082	0.082	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.018	0.002	12.098	-0.144	-0.144	0.000	0.000	0.000	0.000
7	A	8	TYR	0	0.042	0.027	14.896	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	9	CYS	0	-0.033	-0.023	17.732	0.017	0.017	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.939	0.950	20.278	-0.435	-0.435	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.985	0.977	23.669	-0.236	-0.236	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.055	0.024	25.341	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.105	-0.035	21.819	0.007	0.007	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.070	0.063	17.851	0.017	0.017	0.000	0.000	0.000	0.000
14	A	15	GLN	0	0.031	0.007	18.179	0.069	0.069	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.972	0.983	18.816	-0.310	-0.310	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.014	-0.001	16.514	0.016	0.016	0.000	0.000	0.000	0.000
17	A	18	GLN	0	0.035	0.000	13.687	0.139	0.139	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.882	-0.938	13.687	0.549	0.549	0.000	0.000	0.000	0.000
19	A	20	HIS	0	-0.041	-0.029	14.032	-0.093	-0.093	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.053	-0.046	10.402	-0.033	-0.033	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.855	-0.912	9.868	1.456	1.456	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.834	0.926	11.483	-0.649	-0.649	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.050	-0.018	10.509	-0.087	-0.087	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.011	-0.012	6.138	0.059	0.059	0.000	0.000	0.000	0.000
25	A	26	VAL	0	-0.064	-0.010	5.625	0.669	0.669	0.000	0.000	0.000	0.000
26	A	27	ASN	0	0.012	0.011	4.325	-1.935	-1.862	-0.001	-0.013	-0.058	0.000
27	A	28	CYS	0	-0.038	-0.019	7.113	0.131	0.131	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.011	0.010	10.393	-0.181	-0.181	0.000	0.000	0.000	0.000
29	A	30	ALA	0	0.017	0.005	12.827	-0.031	-0.031	0.000	0.000	0.000	0.000
30	A	31	PRO	0	-0.018	-0.012	15.456	-0.082	-0.082	0.000	0.000	0.000	0.000
31	A	32	MET	0	-0.018	0.011	18.416	-0.029	-0.029	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.025	0.011	22.111	0.003	0.003	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.040	-0.021	24.692	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.033	0.019	27.950	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.951	-0.962	30.748	0.146	0.146	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.985	1.002	33.318	-0.212	-0.212	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.034	-0.034	35.664	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	39	VAL	0	0.001	0.013	36.778	0.003	0.003	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.953	0.959	39.100	-0.129	-0.129	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.008	0.014	42.837	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.963	0.977	41.942	-0.116	-0.116	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.991	0.991	39.304	-0.123	-0.123	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.031	-0.006	36.245	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.069	0.037	33.383	0.007	0.007	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.068	-0.043	30.157	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.056	0.028	25.694	0.005	0.005	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.904	-0.969	26.656	0.280	0.280	0.000	0.000	0.000	0.000
48	A	49	PRO	0	-0.003	-0.006	21.884	0.010	0.010	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.004	0.015	19.383	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	51	PHE	0	0.074	0.022	17.826	-0.033	-0.033	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.074	0.028	20.556	0.049	0.049	0.000	0.000	0.000	0.000
52	A	53	ASN	0	-0.058	0.009	20.931	0.040	0.040	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.070	-0.043	16.895	0.015	0.015	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.002	-0.008	12.093	-0.031	-0.031	0.000	0.000	0.000	0.000
55	A	56	PHE	0	-0.024	-0.005	10.360	0.011	0.011	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.008	-0.022	8.405	0.007	0.007	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.813	-0.909	2.475	2.994	3.786	0.364	-0.288	-0.868	0.000
58	A	59	PHE	0	0.009	0.001	3.076	0.316	2.056	0.138	-0.646	-1.231	0.004
59	A	60	ASP	-1	-0.780	-0.906	1.696	-15.050	-24.893	25.282	-9.025	-6.414	-0.073
60	A	61	PRO	0	-0.059	-0.024	3.188	0.298	0.234	0.091	0.256	-0.283	-0.001
61	A	62	GLU	-1	-0.896	-0.956	5.693	-0.565	-0.565	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.066	-0.009	5.018	0.190	0.190	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.004	0.011	7.065	0.190	0.190	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.052	0.020	7.802	0.203	0.203	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.031	-0.035	9.775	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	THR	0	-0.018	-0.012	11.567	0.081	0.081	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.031	0.015	12.595	-0.048	-0.048	0.000	0.000	0.000	0.000
68	A	69	ILE	0	0.040	0.030	9.013	-0.058	-0.058	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.023	-0.016	12.837	-0.039	-0.039	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.010	0.008	15.985	-0.037	-0.037	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.055	-0.012	14.256	-0.045	-0.045	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.967	0.966	16.859	-0.380	-0.380	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.025	-0.002	19.508	0.021	0.021	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.006	0.011	15.420	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.094	-0.061	18.650	-0.051	-0.051	0.000	0.000	0.000	0.000
76	A	77	HIS	0	0.009	0.027	17.825	-0.037	-0.037	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.042	0.037	9.863	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.023	0.008	14.846	-0.100	-0.100	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.942	0.920	14.640	-0.371	-0.371	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.011	0.025	15.407	-0.033	-0.033	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.011	0.002	16.310	-0.042	-0.042	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.024	-0.001	17.328	0.015	0.015	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.004	0.010	16.762	0.014	0.014	0.000	0.000	0.000	0.000
84	A	85	PRO	0	-0.019	-0.010	13.322	0.023	0.023	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.047	0.048	11.157	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	ILE	0	-0.092	-0.051	11.663	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.081	0.040	7.469	0.093	0.093	0.000	0.000	0.000	0.000
88	A	89	PRO	0	-0.069	-0.021	9.697	-0.088	-0.088	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.064	0.022	9.613	0.109	0.109	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.065	0.018	8.805	0.019	0.019	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.005	-0.006	10.050	-0.020	-0.020	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.002	0.004	13.468	-0.044	-0.044	0.000	0.000	0.000	0.000
93	A	94	HIS	0	-0.003	0.007	9.359	-0.036	-0.036	0.000	0.000	0.000	0.000
94	A	95	GLN	0	0.004	-0.015	12.481	-0.036	-0.036	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.035	-0.037	14.276	-0.044	-0.044	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.001	0.016	14.838	-0.028	-0.028	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.047	-0.017	13.800	-0.025	-0.025	0.000	0.000	0.000	0.000
98	A	99	TYR	0	-0.002	0.018	12.758	-0.055	-0.055	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.942	1.003	19.144	-0.301	-0.301	0.000	0.000	0.000	0.000
100	A	115	LYS	1	0.998	0.984	21.382	-0.091	-0.091	0.000	0.000	0.000	0.000
101	A	116	VAL	0	0.073	0.058	22.782	0.011	0.011	0.000	0.000	0.000	0.000
102	A	117	ILE	0	0.055	0.042	23.588	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	118	ILE	0	-0.015	0.001	17.571	0.013	0.013	0.000	0.000	0.000	0.000
104	A	119	THR	0	-0.109	-0.112	20.704	0.024	0.024	0.000	0.000	0.000	0.000
105	A	120	GLU	-1	-0.913	-0.960	22.372	0.161	0.161	0.000	0.000	0.000	0.000
106	A	121	GLY	0	0.009	0.039	22.745	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	122	ALA	0	-0.004	-0.026	19.069	0.017	0.017	0.000	0.000	0.000	0.000
108	A	123	PHE	0	-0.059	-0.039	20.922	0.006	0.006	0.000	0.000	0.000	0.000
109	A	124	GLU	-1	-0.861	-0.933	23.674	0.196	0.196	0.000	0.000	0.000	0.000
110	A	125	GLY	0	-0.015	0.011	23.185	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	126	PHE	0	0.016	-0.027	17.036	0.013	0.013	0.000	0.000	0.000	0.000
112	A	127	GLN	0	-0.018	0.004	22.909	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	128	ALA	0	0.020	0.044	26.399	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	129	ILE	0	-0.036	-0.022	21.052	0.002	0.002	0.000	0.000	0.000	0.000
115	A	130	PHE	0	-0.023	-0.033	20.624	0.005	0.005	0.000	0.000	0.000	0.000
116	A	131	THR	0	-0.063	-0.044	25.915	-0.019	-0.019	0.000	0.000	0.000	0.000
117	A	132	GLU	-1	-0.911	-0.954	27.861	0.210	0.210	0.000	0.000	0.000	0.000
118	A	133	PRO	0	0.025	0.039	28.705	0.018	0.018	0.000	0.000	0.000	0.000
119	A	134	ASP	-1	-0.907	-0.944	29.735	0.259	0.259	0.000	0.000	0.000	0.000
120	A	135	GLY	0	0.088	0.017	25.678	0.007	0.007	0.000	0.000	0.000	0.000
121	A	136	GLU	-1	-0.896	-0.961	25.276	0.376	0.376	0.000	0.000	0.000	0.000
122	A	137	ALA	0	0.013	0.011	26.506	0.010	0.010	0.000	0.000	0.000	0.000
123	A	138	ARG	1	0.749	0.849	23.445	-0.307	-0.307	0.000	0.000	0.000	0.000
124	A	139	SER	0	0.014	-0.002	21.731	0.033	0.033	0.000	0.000	0.000	0.000
125	A	140	MET	0	-0.051	-0.003	22.082	0.022	0.022	0.000	0.000	0.000	0.000
126	A	141	LEU	0	0.060	0.034	23.706	0.008	0.008	0.000	0.000	0.000	0.000
127	A	142	LEU	0	-0.013	0.015	16.612	0.007	0.007	0.000	0.000	0.000	0.000
128	A	143	LEU	0	-0.017	-0.015	18.751	0.023	0.023	0.000	0.000	0.000	0.000
129	A	144	ASN	0	-0.096	-0.064	20.376	-0.015	-0.015	0.000	0.000	0.000	0.000
130	A	145	LEU	0	0.043	0.025	18.905	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	146	ILE	0	0.022	0.009	14.484	0.007	0.007	0.000	0.000	0.000	0.000
132	A	147	ASN	0	-0.019	-0.023	17.554	0.003	0.003	0.000	0.000	0.000	0.000
133	A	148	LYS	1	0.873	0.941	19.617	-0.280	-0.280	0.000	0.000	0.000	0.000
134	A	149	GLU	-1	-0.793	-0.911	17.002	0.306	0.306	0.000	0.000	0.000	0.000
135	A	150	ILE	0	-0.030	-0.005	14.570	-0.012	-0.012	0.000	0.000	0.000	0.000
136	A	151	LYS	1	0.896	0.937	16.683	-0.282	-0.282	0.000	0.000	0.000	0.000
137	A	152	HIS	0	0.049	0.040	19.286	-0.029	-0.029	0.000	0.000	0.000	0.000
138	A	153	SER	0	-0.002	-0.001	13.903	-0.036	-0.036	0.000	0.000	0.000	0.000
139	A	154	VAL	0	-0.036	0.001	16.458	-0.024	-0.024	0.000	0.000	0.000	0.000
140	A	155	LYS	1	0.892	0.936	18.365	-0.229	-0.229	0.000	0.000	0.000	0.000
141	A	156	ASN	0	-0.054	-0.012	18.850	-0.044	-0.044	0.000	0.000	0.000	0.000

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