FMO DATABASE

FMODB ID: JQLQ9

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	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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1218695.814283
FMO2-HF: Nuclear repulsion	1164735.024283
FMO2-HF: Total energy	-53960.79
FMO2-MP2: Total energy	-54115.714164

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.
60.236	66.634	13.581	-8.507	-11.474	-0.078

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 : 0.973 / 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	0.017	3.799	1.122	3.243	-0.026	-1.121	-0.974	0.001
4	A	151	TYR	0	0.045	0.026	6.558	-0.689	-0.689	0.000	0.000	0.000	0.000
5	A	152	PRO	0	0.095	0.042	10.099	0.823	0.823	0.000	0.000	0.000	0.000
6	A	153	ASN	0	0.065	0.039	13.303	0.769	0.769	0.000	0.000	0.000	0.000
7	A	154	ASP	-1	-0.842	-0.919	10.128	-18.559	-18.559	0.000	0.000	0.000	0.000
8	A	155	LEU	0	-0.027	-0.010	11.034	0.242	0.242	0.000	0.000	0.000	0.000
9	A	156	ALA	0	0.013	-0.002	12.382	0.756	0.756	0.000	0.000	0.000	0.000
10	A	157	LYS	1	0.890	0.948	13.884	16.735	16.735	0.000	0.000	0.000	0.000
11	A	158	LYS	1	0.772	0.865	8.174	22.169	22.169	0.000	0.000	0.000	0.000
12	A	159	MET	0	-0.045	-0.002	14.592	0.022	0.022	0.000	0.000	0.000	0.000
13	A	160	THR	0	-0.023	-0.001	16.974	0.688	0.688	0.000	0.000	0.000	0.000
14	A	161	LYS	1	0.916	0.969	13.677	15.962	15.962	0.000	0.000	0.000	0.000
15	A	172	PRO	0	0.001	-0.011	11.877	0.256	0.256	0.000	0.000	0.000	0.000
16	A	173	VAL	0	0.034	0.033	12.585	0.662	0.662	0.000	0.000	0.000	0.000
17	A	174	ILE	0	0.026	0.012	11.700	-1.533	-1.533	0.000	0.000	0.000	0.000
18	A	175	ILE	0	-0.006	-0.001	11.653	0.989	0.989	0.000	0.000	0.000	0.000
19	A	176	ASP	-1	-0.744	-0.835	12.914	-17.749	-17.749	0.000	0.000	0.000	0.000
20	A	177	CYS	0	-0.055	-0.031	12.542	0.072	0.072	0.000	0.000	0.000	0.000
21	A	178	ARG	1	0.838	0.909	15.011	15.110	15.110	0.000	0.000	0.000	0.000
22	A	179	PRO	0	0.046	0.019	17.950	0.442	0.442	0.000	0.000	0.000	0.000
23	A	180	PHE	0	0.022	0.014	21.436	0.156	0.156	0.000	0.000	0.000	0.000
24	A	181	MET	0	0.024	0.001	23.357	0.134	0.134	0.000	0.000	0.000	0.000
25	A	182	GLU	-1	-0.808	-0.880	21.528	-12.233	-12.233	0.000	0.000	0.000	0.000
26	A	183	TYR	0	-0.068	-0.042	19.736	0.264	0.264	0.000	0.000	0.000	0.000
27	A	184	ASN	0	0.004	-0.010	22.140	0.006	0.006	0.000	0.000	0.000	0.000
28	A	185	LYS	1	0.851	0.931	25.600	11.988	11.988	0.000	0.000	0.000	0.000
29	A	186	SER	0	-0.017	-0.020	23.127	0.041	0.041	0.000	0.000	0.000	0.000
30	A	187	HIS	1	0.826	0.922	19.559	12.070	12.070	0.000	0.000	0.000	0.000
31	A	188	ILE	0	0.020	0.010	14.505	0.408	0.408	0.000	0.000	0.000	0.000
32	A	189	GLN	0	-0.007	-0.004	18.534	-0.147	-0.147	0.000	0.000	0.000	0.000
33	A	190	GLY	0	-0.014	-0.006	18.840	-0.415	-0.415	0.000	0.000	0.000	0.000
34	A	191	ALA	0	-0.063	-0.019	16.564	-0.291	-0.291	0.000	0.000	0.000	0.000
35	A	192	VAL	0	0.016	0.012	16.679	0.767	0.767	0.000	0.000	0.000	0.000
36	A	193	HIS	0	-0.021	-0.009	16.993	-0.481	-0.481	0.000	0.000	0.000	0.000
37	A	194	ILE	0	0.026	0.015	14.683	0.478	0.478	0.000	0.000	0.000	0.000
38	A	195	ASN	0	0.035	0.014	18.240	-0.495	-0.495	0.000	0.000	0.000	0.000
39	A	196	CYS	0	0.029	0.023	17.104	-0.304	-0.304	0.000	0.000	0.000	0.000
40	A	197	ALA	0	-0.013	0.002	19.734	-0.045	-0.045	0.000	0.000	0.000	0.000
41	A	198	ASP	-1	-0.790	-0.904	22.843	-11.305	-11.305	0.000	0.000	0.000	0.000
42	A	199	LYS	1	0.984	0.989	23.944	11.992	11.992	0.000	0.000	0.000	0.000
43	A	200	ILE	0	-0.008	0.000	24.998	-0.316	-0.316	0.000	0.000	0.000	0.000
44	A	201	SER	0	-0.008	-0.022	21.670	-0.123	-0.123	0.000	0.000	0.000	0.000
45	A	202	ARG	1	0.853	0.928	17.860	16.123	16.123	0.000	0.000	0.000	0.000
46	A	203	ARG	1	0.916	0.952	20.446	11.109	11.109	0.000	0.000	0.000	0.000
47	A	204	ARG	1	0.963	0.988	22.034	11.028	11.028	0.000	0.000	0.000	0.000
48	A	205	LEU	0	0.033	0.024	17.073	-0.075	-0.075	0.000	0.000	0.000	0.000
49	A	206	GLN	0	0.016	0.003	17.262	-0.512	-0.512	0.000	0.000	0.000	0.000
50	A	207	GLN	0	-0.063	-0.027	18.705	0.137	0.137	0.000	0.000	0.000	0.000
51	A	208	GLY	0	0.037	0.025	19.167	0.321	0.321	0.000	0.000	0.000	0.000
52	A	209	LYS	1	0.841	0.918	20.024	12.203	12.203	0.000	0.000	0.000	0.000
53	A	210	ILE	0	-0.025	-0.012	20.725	0.593	0.593	0.000	0.000	0.000	0.000
54	A	211	THR	0	0.003	-0.006	17.816	-0.506	-0.506	0.000	0.000	0.000	0.000
55	A	212	VAL	0	-0.017	-0.026	13.490	0.592	0.592	0.000	0.000	0.000	0.000
56	A	213	LEU	0	-0.014	-0.022	13.405	0.422	0.422	0.000	0.000	0.000	0.000
57	A	214	ASP	-1	-0.833	-0.895	16.763	-12.685	-12.685	0.000	0.000	0.000	0.000
58	A	215	LEU	0	-0.063	-0.030	18.633	0.607	0.607	0.000	0.000	0.000	0.000
59	A	216	ILE	0	-0.053	-0.019	15.138	0.222	0.222	0.000	0.000	0.000	0.000
60	A	217	SER	0	0.016	-0.033	19.402	0.603	0.603	0.000	0.000	0.000	0.000
61	A	218	CYS	0	-0.067	-0.025	21.100	0.538	0.538	0.000	0.000	0.000	0.000
62	A	219	ARG	1	0.936	0.973	23.231	11.993	11.993	0.000	0.000	0.000	0.000
63	A	220	GLU	-1	-0.879	-0.902	20.392	-12.503	-12.503	0.000	0.000	0.000	0.000
64	A	221	GLY	0	0.050	0.015	24.838	0.398	0.398	0.000	0.000	0.000	0.000
65	A	222	LYS	1	0.887	0.942	25.802	9.288	9.288	0.000	0.000	0.000	0.000
66	A	223	ASP	-1	-0.862	-0.930	24.248	-10.213	-10.213	0.000	0.000	0.000	0.000
67	A	224	SER	0	-0.082	-0.044	21.575	-0.559	-0.559	0.000	0.000	0.000	0.000
68	A	225	PHE	0	0.073	0.031	18.542	-0.501	-0.501	0.000	0.000	0.000	0.000
69	A	226	LYS	1	0.975	0.981	18.724	11.471	11.471	0.000	0.000	0.000	0.000
70	A	227	ARG	1	0.977	0.988	18.473	10.980	10.980	0.000	0.000	0.000	0.000
71	A	228	ILE	0	0.009	0.005	14.875	-0.672	-0.672	0.000	0.000	0.000	0.000
72	A	229	PHE	0	0.001	0.009	14.109	-0.975	-0.975	0.000	0.000	0.000	0.000
73	A	230	SER	0	-0.019	0.002	13.680	-0.731	-0.731	0.000	0.000	0.000	0.000
74	A	231	LYS	1	0.870	0.951	13.284	14.420	14.420	0.000	0.000	0.000	0.000
75	A	232	GLU	-1	-0.802	-0.875	8.304	-22.349	-22.349	0.000	0.000	0.000	0.000
76	A	233	ILE	0	0.007	-0.008	8.033	1.182	1.182	0.000	0.000	0.000	0.000
77	A	234	ILE	0	-0.022	-0.011	7.088	-2.752	-2.752	0.000	0.000	0.000	0.000
78	A	235	VAL	0	0.027	0.024	6.919	2.003	2.003	0.000	0.000	0.000	0.000
79	A	236	TYR	0	-0.053	-0.063	8.776	-2.158	-2.158	0.000	0.000	0.000	0.000
80	A	237	ASP	-1	-0.749	-0.853	11.179	-22.535	-22.535	0.000	0.000	0.000	0.000
81	A	238	GLU	-1	-0.872	-0.956	13.029	-15.337	-15.337	0.000	0.000	0.000	0.000
82	A	239	ASN	0	-0.057	-0.043	14.055	1.338	1.338	0.000	0.000	0.000	0.000
83	A	240	THR	0	0.008	-0.006	7.847	-0.356	-0.356	0.000	0.000	0.000	0.000
84	A	241	ASN	0	-0.014	-0.006	8.617	-0.200	-0.200	0.000	0.000	0.000	0.000
85	A	242	GLU	-1	-0.772	-0.862	3.904	-57.892	-57.384	0.000	-0.226	-0.283	-0.001
86	A	243	PRO	0	0.040	0.013	2.518	-2.078	-0.487	1.333	-0.544	-2.380	-0.004
87	A	244	SER	0	-0.021	-0.050	1.819	-26.135	-27.104	9.434	-4.320	-4.146	-0.060
88	A	245	ARG	1	0.878	0.946	3.436	41.344	41.732	0.057	-0.135	-0.309	-0.002
89	A	246	VAL	0	-0.015	0.011	6.432	5.217	5.217	0.000	0.000	0.000	0.000
90	A	247	MET	0	0.026	0.015	8.365	0.380	0.380	0.000	0.000	0.000	0.000
91	A	248	PRO	0	0.064	0.015	11.020	0.403	0.403	0.000	0.000	0.000	0.000
92	A	249	SER	0	-0.005	0.002	12.392	0.802	0.802	0.000	0.000	0.000	0.000
93	A	250	GLN	0	0.016	0.014	12.330	1.993	1.993	0.000	0.000	0.000	0.000
94	A	251	PRO	0	0.064	0.015	13.244	-1.161	-1.161	0.000	0.000	0.000	0.000
95	A	252	LEU	0	-0.005	0.010	7.694	-0.738	-0.738	0.000	0.000	0.000	0.000
96	A	253	HIS	0	0.005	-0.004	9.110	-3.892	-3.892	0.000	0.000	0.000	0.000
97	A	254	ILE	0	-0.030	-0.008	10.271	0.014	0.014	0.000	0.000	0.000	0.000
98	A	255	VAL	0	0.014	-0.010	10.809	0.127	0.127	0.000	0.000	0.000	0.000
99	A	256	LEU	0	-0.023	-0.008	4.468	-0.510	-0.385	-0.001	-0.008	-0.117	0.000
100	A	257	GLU	-1	-0.850	-0.912	8.667	-23.529	-23.529	0.000	0.000	0.000	0.000
101	A	258	SER	0	-0.024	-0.031	10.666	1.290	1.290	0.000	0.000	0.000	0.000
102	A	259	LEU	0	0.007	0.001	9.244	0.818	0.818	0.000	0.000	0.000	0.000
103	A	260	LYS	1	0.841	0.910	5.981	37.386	37.386	0.000	0.000	0.000	0.000
104	A	261	ARG	1	0.853	0.928	9.920	21.186	21.186	0.000	0.000	0.000	0.000
105	A	262	GLU	-1	-0.763	-0.869	13.303	-16.820	-16.820	0.000	0.000	0.000	0.000
106	A	263	GLY	0	0.006	0.007	12.961	1.016	1.016	0.000	0.000	0.000	0.000
107	A	264	LYS	1	0.777	0.871	9.451	20.484	20.484	0.000	0.000	0.000	0.000
108	A	265	GLU	-1	-0.801	-0.889	5.008	-38.034	-38.034	0.000	0.000	0.000	0.000
109	A	266	PRO	0	-0.054	-0.017	4.962	-0.052	0.095	-0.001	-0.025	-0.121	0.000
110	A	267	LEU	0	-0.037	-0.010	2.225	-8.416	-6.814	2.780	-1.786	-2.596	-0.013
111	A	268	VAL	0	0.003	-0.016	3.751	3.160	4.045	0.005	-0.342	-0.548	0.001
112	A	269	LEU	0	-0.025	-0.012	5.908	-0.302	-0.302	0.000	0.000	0.000	0.000
113	A	270	LYS	1	0.878	0.942	6.989	30.026	30.026	0.000	0.000	0.000	0.000
114	A	271	GLY	0	0.036	0.002	8.492	2.187	2.187	0.000	0.000	0.000	0.000
115	A	272	GLY	0	-0.031	-0.002	10.812	1.660	1.660	0.000	0.000	0.000	0.000
116	A	273	LEU	0	0.067	0.021	12.642	0.381	0.381	0.000	0.000	0.000	0.000
117	A	274	SER	0	-0.052	-0.025	16.104	1.162	1.162	0.000	0.000	0.000	0.000
118	A	275	SER	0	0.020	-0.005	14.104	0.878	0.878	0.000	0.000	0.000	0.000
119	A	276	PHE	0	-0.028	-0.015	14.630	0.202	0.202	0.000	0.000	0.000	0.000
120	A	277	LYS	1	0.950	0.967	16.643	14.545	14.545	0.000	0.000	0.000	0.000
121	A	278	GLN	0	-0.089	-0.026	19.002	0.981	0.981	0.000	0.000	0.000	0.000
122	A	279	ASN	0	0.008	0.000	19.770	0.974	0.974	0.000	0.000	0.000	0.000
123	A	280	HIS	1	0.850	0.905	17.480	14.335	14.335	0.000	0.000	0.000	0.000
124	A	281	GLU	-1	-0.748	-0.855	20.969	-12.649	-12.649	0.000	0.000	0.000	0.000
125	A	282	ASN	0	0.006	-0.010	22.890	-0.169	-0.169	0.000	0.000	0.000	0.000
126	A	283	LEU	0	-0.056	-0.019	18.619	0.145	0.145	0.000	0.000	0.000	0.000
127	A	284	CYS	0	-0.007	0.002	20.307	-0.973	-0.973	0.000	0.000	0.000	0.000
128	A	285	ASP	-1	-0.833	-0.915	22.052	-11.296	-11.296	0.000	0.000	0.000	0.000
129	A	286	ASN	0	-0.033	-0.032	24.653	-0.523	-0.523	0.000	0.000	0.000	0.000
130	A	287	SER	0	-0.046	-0.038	27.047	0.482	0.482	0.000	0.000	0.000	0.000
131	A	288	LYS	1	0.856	0.922	29.629	9.621	9.621	0.000	0.000	0.000	0.000
132	A	289	GLU	-1	-0.849	-0.897	29.985	-10.184	-10.184	0.000	0.000	0.000	0.000

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