FMO DATABASE

FMODB ID: 3J9JL

Calculation Name: 2OUC-A-Xray372

Preferred Name: Dual specificity protein phosphatase 10

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2OUC

Chain ID: A

ChEMBL ID: CHEMBL2396511

UniProt ID: Q9Y6W6

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	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1218851.829261
FMO2-HF: Nuclear repulsion	1164890.541737
FMO2-HF: Total energy	-53961.287525
FMO2-MP2: Total energy	-54116.143901

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:148:LYS)

Summations of interaction energy for fragment #1(A:148:LYS)

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.
50.225	56.665	14.515	-9.046	-11.909	-0.088

Interaction energy analysis for fragmet #1(A:148:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.964 / q_NPA : 0.971

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	150	ILE	0	0.021	0.014	3.882	1.650	3.460	-0.017	-0.995	-0.799	0.002
4	A	151	TYR	0	0.058	0.030	6.889	-0.760	-0.760	0.000	0.000	0.000	0.000
5	A	152	PRO	0	0.048	0.014	10.413	0.878	0.878	0.000	0.000	0.000	0.000
6	A	153	ASN	0	0.075	0.037	13.600	1.043	1.043	0.000	0.000	0.000	0.000
7	A	154	ASP	-1	-0.831	-0.898	10.468	-17.960	-17.960	0.000	0.000	0.000	0.000
8	A	155	LEU	0	-0.001	0.003	11.327	0.302	0.302	0.000	0.000	0.000	0.000
9	A	156	ALA	0	0.041	0.017	12.583	0.731	0.731	0.000	0.000	0.000	0.000
10	A	157	LYS	1	0.866	0.931	14.142	16.546	16.546	0.000	0.000	0.000	0.000
11	A	158	LYS	1	0.758	0.854	8.239	21.772	21.772	0.000	0.000	0.000	0.000
12	A	159	MET	0	-0.040	-0.008	14.580	-0.053	-0.053	0.000	0.000	0.000	0.000
13	A	160	THR	0	-0.016	0.002	17.194	0.670	0.670	0.000	0.000	0.000	0.000
14	A	161	LYS	1	0.916	0.974	13.679	15.871	15.871	0.000	0.000	0.000	0.000
15	A	172	PRO	0	0.008	0.004	12.032	0.193	0.193	0.000	0.000	0.000	0.000
16	A	173	VAL	0	0.033	0.032	12.551	0.808	0.808	0.000	0.000	0.000	0.000
17	A	174	ILE	0	0.014	0.003	11.761	-1.515	-1.515	0.000	0.000	0.000	0.000
18	A	175	ILE	0	0.006	0.010	11.492	0.986	0.986	0.000	0.000	0.000	0.000
19	A	176	ASP	-1	-0.753	-0.848	12.885	-18.012	-18.012	0.000	0.000	0.000	0.000
20	A	177	CYS	0	-0.045	-0.027	12.263	0.097	0.097	0.000	0.000	0.000	0.000
21	A	178	ARG	1	0.769	0.876	14.918	15.414	15.414	0.000	0.000	0.000	0.000
22	A	179	PRO	0	0.025	0.010	17.827	0.430	0.430	0.000	0.000	0.000	0.000
23	A	180	PHE	0	0.019	0.013	21.422	0.163	0.163	0.000	0.000	0.000	0.000
24	A	181	MET	0	0.030	0.007	23.322	0.128	0.128	0.000	0.000	0.000	0.000
25	A	182	GLU	-1	-0.794	-0.875	21.682	-12.025	-12.025	0.000	0.000	0.000	0.000
26	A	183	TYR	0	-0.073	-0.043	19.486	0.069	0.069	0.000	0.000	0.000	0.000
27	A	184	ASN	0	-0.013	-0.005	22.040	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	185	LYS	1	0.828	0.894	25.751	11.734	11.734	0.000	0.000	0.000	0.000
29	A	186	SER	0	-0.017	-0.016	22.905	0.043	0.043	0.000	0.000	0.000	0.000
30	A	187	HIS	1	0.841	0.927	19.494	12.159	12.159	0.000	0.000	0.000	0.000
31	A	188	ILE	0	0.015	0.005	14.532	0.396	0.396	0.000	0.000	0.000	0.000
32	A	189	GLN	0	-0.032	-0.027	18.567	-0.120	-0.120	0.000	0.000	0.000	0.000
33	A	190	GLY	0	-0.010	0.003	19.213	-0.372	-0.372	0.000	0.000	0.000	0.000
34	A	191	ALA	0	-0.056	-0.012	16.218	-0.252	-0.252	0.000	0.000	0.000	0.000
35	A	192	VAL	0	0.002	0.009	16.735	0.708	0.708	0.000	0.000	0.000	0.000
36	A	193	HIS	0	-0.011	-0.011	16.893	-0.492	-0.492	0.000	0.000	0.000	0.000
37	A	194	ILE	0	0.035	0.010	14.691	0.350	0.350	0.000	0.000	0.000	0.000
38	A	195	ASN	0	0.051	0.024	18.307	-0.679	-0.679	0.000	0.000	0.000	0.000
39	A	196	CYS	0	0.031	0.035	16.961	-0.191	-0.191	0.000	0.000	0.000	0.000
40	A	197	ALA	0	0.016	0.016	19.523	-0.237	-0.237	0.000	0.000	0.000	0.000
41	A	198	ASP	-1	-0.780	-0.894	22.665	-11.354	-11.354	0.000	0.000	0.000	0.000
42	A	199	LYS	1	0.911	0.948	23.786	12.237	12.237	0.000	0.000	0.000	0.000
43	A	200	ILE	0	-0.004	-0.004	25.171	-0.263	-0.263	0.000	0.000	0.000	0.000
44	A	201	SER	0	-0.023	-0.031	21.621	-0.122	-0.122	0.000	0.000	0.000	0.000
45	A	202	ARG	1	0.832	0.919	17.322	16.576	16.576	0.000	0.000	0.000	0.000
46	A	203	ARG	1	0.921	0.959	20.434	11.168	11.168	0.000	0.000	0.000	0.000
47	A	204	ARG	1	0.940	0.974	22.261	11.212	11.212	0.000	0.000	0.000	0.000
48	A	205	LEU	0	0.032	0.021	16.896	-0.106	-0.106	0.000	0.000	0.000	0.000
49	A	206	GLN	0	0.023	0.001	16.973	-0.311	-0.311	0.000	0.000	0.000	0.000
50	A	207	GLN	0	-0.029	-0.003	18.535	0.216	0.216	0.000	0.000	0.000	0.000
51	A	208	GLY	0	0.032	0.019	18.868	0.380	0.380	0.000	0.000	0.000	0.000
52	A	209	LYS	1	0.861	0.931	19.710	12.346	12.346	0.000	0.000	0.000	0.000
53	A	210	ILE	0	-0.048	-0.029	20.646	0.712	0.712	0.000	0.000	0.000	0.000
54	A	211	THR	0	-0.004	-0.018	17.665	-0.508	-0.508	0.000	0.000	0.000	0.000
55	A	212	VAL	0	-0.018	-0.028	13.101	0.582	0.582	0.000	0.000	0.000	0.000
56	A	213	LEU	0	-0.025	-0.018	12.924	0.415	0.415	0.000	0.000	0.000	0.000
57	A	214	ASP	-1	-0.812	-0.884	16.565	-12.942	-12.942	0.000	0.000	0.000	0.000
58	A	215	LEU	0	-0.031	-0.017	18.573	0.640	0.640	0.000	0.000	0.000	0.000
59	A	216	ILE	0	-0.041	-0.012	15.348	0.348	0.348	0.000	0.000	0.000	0.000
60	A	217	SER	0	0.017	-0.024	19.594	0.642	0.642	0.000	0.000	0.000	0.000
61	A	218	CYS	0	-0.077	-0.039	21.174	0.556	0.556	0.000	0.000	0.000	0.000
62	A	219	ARG	1	0.899	0.955	22.641	12.263	12.263	0.000	0.000	0.000	0.000
63	A	220	GLU	-1	-0.850	-0.878	20.098	-12.655	-12.655	0.000	0.000	0.000	0.000
64	A	221	GLY	0	0.046	0.008	24.684	0.444	0.444	0.000	0.000	0.000	0.000
65	A	222	LYS	1	0.908	0.949	25.595	9.232	9.232	0.000	0.000	0.000	0.000
66	A	223	ASP	-1	-0.816	-0.899	24.299	-10.492	-10.492	0.000	0.000	0.000	0.000
67	A	224	SER	0	-0.032	-0.015	21.210	-0.525	-0.525	0.000	0.000	0.000	0.000
68	A	225	PHE	0	0.076	0.040	18.004	-0.499	-0.499	0.000	0.000	0.000	0.000
69	A	226	LYS	1	0.963	0.978	18.429	11.622	11.622	0.000	0.000	0.000	0.000
70	A	227	ARG	1	0.883	0.942	18.399	10.717	10.717	0.000	0.000	0.000	0.000
71	A	228	ILE	0	0.017	0.001	14.834	-0.622	-0.622	0.000	0.000	0.000	0.000
72	A	229	PHE	0	-0.017	-0.006	14.190	-0.899	-0.899	0.000	0.000	0.000	0.000
73	A	230	SER	0	-0.015	-0.005	13.909	-0.658	-0.658	0.000	0.000	0.000	0.000
74	A	231	LYS	1	0.863	0.933	13.351	14.404	14.404	0.000	0.000	0.000	0.000
75	A	232	GLU	-1	-0.808	-0.884	8.743	-21.843	-21.843	0.000	0.000	0.000	0.000
76	A	233	ILE	0	0.014	0.001	8.242	1.259	1.259	0.000	0.000	0.000	0.000
77	A	234	ILE	0	-0.025	-0.008	7.069	-2.698	-2.698	0.000	0.000	0.000	0.000
78	A	235	VAL	0	0.020	0.013	6.809	1.617	1.617	0.000	0.000	0.000	0.000
79	A	236	TYR	0	-0.056	-0.058	8.964	-1.970	-1.970	0.000	0.000	0.000	0.000
80	A	237	ASP	-1	-0.759	-0.859	11.379	-22.543	-22.543	0.000	0.000	0.000	0.000
81	A	238	GLU	-1	-0.770	-0.891	13.540	-15.685	-15.685	0.000	0.000	0.000	0.000
82	A	239	ASN	0	-0.032	-0.019	14.230	1.207	1.207	0.000	0.000	0.000	0.000
83	A	240	THR	0	-0.020	-0.030	8.281	-0.494	-0.494	0.000	0.000	0.000	0.000
84	A	241	ASN	0	0.014	-0.004	8.869	-0.555	-0.555	0.000	0.000	0.000	0.000
85	A	242	GLU	-1	-0.760	-0.849	3.688	-65.467	-64.802	0.001	-0.359	-0.306	-0.002
86	A	243	PRO	0	0.036	0.001	2.309	-2.166	-0.967	2.067	-0.687	-2.578	-0.004
87	A	244	SER	0	-0.055	-0.040	1.798	-31.459	-32.594	10.451	-4.883	-4.433	-0.066
88	A	245	ARG	1	0.886	0.937	3.330	44.792	45.056	0.077	-0.047	-0.295	-0.002
89	A	246	VAL	0	-0.026	0.003	6.201	5.248	5.248	0.000	0.000	0.000	0.000
90	A	247	MET	0	0.041	0.025	8.137	0.074	0.074	0.000	0.000	0.000	0.000
91	A	248	PRO	0	0.051	0.012	10.528	0.731	0.731	0.000	0.000	0.000	0.000
92	A	249	SER	0	-0.009	-0.003	12.210	0.839	0.839	0.000	0.000	0.000	0.000
93	A	250	GLN	0	0.018	0.018	12.087	2.150	2.150	0.000	0.000	0.000	0.000
94	A	251	PRO	0	0.032	-0.003	13.201	-1.095	-1.095	0.000	0.000	0.000	0.000
95	A	252	LEU	0	0.016	0.008	7.790	-0.488	-0.488	0.000	0.000	0.000	0.000
96	A	253	HIS	0	-0.001	0.000	9.021	-3.680	-3.680	0.000	0.000	0.000	0.000
97	A	254	ILE	0	-0.006	0.001	10.100	-0.194	-0.194	0.000	0.000	0.000	0.000
98	A	255	VAL	0	0.025	0.007	10.602	0.324	0.324	0.000	0.000	0.000	0.000
99	A	256	LEU	0	-0.022	-0.010	3.922	-0.458	-0.257	0.000	-0.027	-0.174	0.000
100	A	257	GLU	-1	-0.843	-0.905	8.093	-24.220	-24.220	0.000	0.000	0.000	0.000
101	A	258	SER	0	-0.038	-0.037	10.072	1.313	1.313	0.000	0.000	0.000	0.000
102	A	259	LEU	0	0.020	0.002	9.166	0.762	0.762	0.000	0.000	0.000	0.000
103	A	260	LYS	1	0.819	0.892	5.495	38.073	38.073	0.000	0.000	0.000	0.000
104	A	261	ARG	1	0.838	0.911	9.694	21.155	21.155	0.000	0.000	0.000	0.000
105	A	262	GLU	-1	-0.763	-0.852	13.096	-16.716	-16.716	0.000	0.000	0.000	0.000
106	A	263	GLY	0	0.007	0.010	12.760	1.019	1.019	0.000	0.000	0.000	0.000
107	A	264	LYS	1	0.773	0.861	9.389	20.085	20.085	0.000	0.000	0.000	0.000
108	A	265	GLU	-1	-0.783	-0.873	4.505	-38.918	-38.785	-0.001	-0.013	-0.119	0.000
109	A	266	PRO	0	-0.034	-0.007	4.875	0.831	0.831	0.000	0.000	0.000	0.000
110	A	267	LEU	0	-0.069	-0.027	2.488	-9.979	-7.419	1.934	-1.786	-2.708	-0.017
111	A	268	VAL	0	0.005	-0.010	3.781	4.048	4.791	0.003	-0.249	-0.497	0.001
112	A	269	LEU	0	-0.010	-0.007	6.009	-0.414	-0.414	0.000	0.000	0.000	0.000
113	A	270	LYS	1	0.882	0.947	7.331	29.075	29.075	0.000	0.000	0.000	0.000
114	A	271	GLY	0	0.047	0.012	8.655	2.077	2.077	0.000	0.000	0.000	0.000
115	A	272	GLY	0	-0.010	0.007	11.109	1.629	1.629	0.000	0.000	0.000	0.000
116	A	273	LEU	0	0.045	0.012	12.926	0.438	0.438	0.000	0.000	0.000	0.000
117	A	274	SER	0	-0.055	-0.036	16.399	1.228	1.228	0.000	0.000	0.000	0.000
118	A	275	SER	0	-0.014	-0.016	14.321	0.871	0.871	0.000	0.000	0.000	0.000
119	A	276	PHE	0	-0.041	-0.022	14.919	0.296	0.296	0.000	0.000	0.000	0.000
120	A	277	LYS	1	1.000	0.988	16.797	14.453	14.453	0.000	0.000	0.000	0.000
121	A	278	GLN	0	-0.076	-0.032	19.425	1.038	1.038	0.000	0.000	0.000	0.000
122	A	279	ASN	0	-0.014	-0.003	20.175	0.878	0.878	0.000	0.000	0.000	0.000
123	A	280	HIS	1	0.822	0.899	17.801	14.163	14.163	0.000	0.000	0.000	0.000
124	A	281	GLU	-1	-0.737	-0.855	21.168	-12.667	-12.667	0.000	0.000	0.000	0.000
125	A	282	ASN	0	0.012	0.002	22.905	-0.162	-0.162	0.000	0.000	0.000	0.000
126	A	283	LEU	0	-0.051	-0.012	18.725	0.141	0.141	0.000	0.000	0.000	0.000
127	A	284	CYS	0	-0.027	-0.002	20.295	-0.983	-0.983	0.000	0.000	0.000	0.000
128	A	285	ASP	-1	-0.800	-0.898	22.285	-11.403	-11.403	0.000	0.000	0.000	0.000
129	A	286	ASN	0	-0.021	-0.021	24.545	-0.564	-0.564	0.000	0.000	0.000	0.000
130	A	287	SER	0	-0.032	-0.034	26.878	0.555	0.555	0.000	0.000	0.000	0.000
131	A	288	LYS	1	0.844	0.910	29.399	9.692	9.692	0.000	0.000	0.000	0.000
132	A	289	GLU	-1	-0.831	-0.882	29.825	-10.242	-10.242	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:148:LYS)