FMO DATABASE

FMODB ID: NN9NQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1218134.759631
FMO2-HF: Nuclear repulsion	1164175.153506
FMO2-HF: Total energy	-53959.606125
FMO2-MP2: Total energy	-54114.62629

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.
82.779	86.971	13.716	-6.815	-11.095	-0.035

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 : 1.021 / q_NPA : 1.008

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	0.018	0.025	3.799	3.225	5.446	-0.025	-1.157	-1.039	0.002
4	A	151	TYR	0	0.044	0.023	7.051	-1.293	-1.293	0.000	0.000	0.000	0.000
5	A	152	PRO	0	0.093	0.039	10.590	0.892	0.892	0.000	0.000	0.000	0.000
6	A	153	ASN	0	0.093	0.046	13.572	0.632	0.632	0.000	0.000	0.000	0.000
7	A	154	ASP	-1	-0.912	-0.954	10.851	-18.430	-18.430	0.000	0.000	0.000	0.000
8	A	155	LEU	0	-0.036	-0.017	11.416	0.318	0.318	0.000	0.000	0.000	0.000
9	A	156	ALA	0	-0.002	-0.010	12.707	0.769	0.769	0.000	0.000	0.000	0.000
10	A	157	LYS	1	0.967	0.986	15.345	15.423	15.423	0.000	0.000	0.000	0.000
11	A	158	LYS	1	0.796	0.864	9.038	20.830	20.830	0.000	0.000	0.000	0.000
12	A	159	MET	0	-0.028	0.007	15.040	-0.010	-0.010	0.000	0.000	0.000	0.000
13	A	160	THR	0	-0.013	0.012	17.019	0.667	0.667	0.000	0.000	0.000	0.000
14	A	161	LYS	1	0.907	0.969	14.141	15.732	15.732	0.000	0.000	0.000	0.000
15	A	172	PRO	0	-0.007	-0.016	11.820	0.078	0.078	0.000	0.000	0.000	0.000
16	A	173	VAL	0	0.003	0.015	12.568	0.602	0.602	0.000	0.000	0.000	0.000
17	A	174	ILE	0	0.018	0.010	11.693	-1.455	-1.455	0.000	0.000	0.000	0.000
18	A	175	ILE	0	-0.006	-0.005	11.732	0.965	0.965	0.000	0.000	0.000	0.000
19	A	176	ASP	-1	-0.752	-0.836	12.919	-17.812	-17.812	0.000	0.000	0.000	0.000
20	A	177	CYS	0	-0.048	-0.029	12.597	0.063	0.063	0.000	0.000	0.000	0.000
21	A	178	ARG	1	0.826	0.885	15.035	15.126	15.126	0.000	0.000	0.000	0.000
22	A	179	PRO	0	0.047	0.015	17.895	0.481	0.481	0.000	0.000	0.000	0.000
23	A	180	PHE	0	0.020	0.011	21.441	0.156	0.156	0.000	0.000	0.000	0.000
24	A	181	MET	0	0.027	-0.001	23.380	0.122	0.122	0.000	0.000	0.000	0.000
25	A	182	GLU	-1	-0.858	-0.926	21.214	-12.642	-12.642	0.000	0.000	0.000	0.000
26	A	183	TYR	0	-0.062	-0.036	19.848	0.330	0.330	0.000	0.000	0.000	0.000
27	A	184	ASN	0	-0.016	-0.012	22.166	0.147	0.147	0.000	0.000	0.000	0.000
28	A	185	LYS	1	0.916	0.993	25.212	12.119	12.119	0.000	0.000	0.000	0.000
29	A	186	SER	0	-0.010	-0.010	22.506	0.038	0.038	0.000	0.000	0.000	0.000
30	A	187	HIS	1	0.881	0.948	19.409	12.230	12.230	0.000	0.000	0.000	0.000
31	A	188	ILE	0	0.020	0.026	14.548	0.403	0.403	0.000	0.000	0.000	0.000
32	A	189	GLN	0	0.018	0.009	18.523	-0.243	-0.243	0.000	0.000	0.000	0.000
33	A	190	GLY	0	-0.012	-0.004	18.832	-0.393	-0.393	0.000	0.000	0.000	0.000
34	A	191	ALA	0	-0.065	-0.022	16.629	-0.275	-0.275	0.000	0.000	0.000	0.000
35	A	192	VAL	0	0.025	0.011	16.665	0.750	0.750	0.000	0.000	0.000	0.000
36	A	193	HIS	0	-0.030	-0.009	16.975	-0.558	-0.558	0.000	0.000	0.000	0.000
37	A	194	ILE	0	0.022	0.017	14.349	0.499	0.499	0.000	0.000	0.000	0.000
38	A	195	ASN	0	0.042	0.020	18.230	-0.652	-0.652	0.000	0.000	0.000	0.000
39	A	196	CYS	0	0.021	0.020	17.011	-0.307	-0.307	0.000	0.000	0.000	0.000
40	A	197	ALA	0	-0.004	0.006	19.665	-0.051	-0.051	0.000	0.000	0.000	0.000
41	A	198	ASP	-1	-0.840	-0.923	22.615	-11.158	-11.158	0.000	0.000	0.000	0.000
42	A	199	LYS	1	0.984	0.978	23.785	11.930	11.930	0.000	0.000	0.000	0.000
43	A	200	ILE	0	0.017	0.011	24.811	-0.323	-0.323	0.000	0.000	0.000	0.000
44	A	201	SER	0	-0.015	-0.019	21.643	-0.079	-0.079	0.000	0.000	0.000	0.000
45	A	202	ARG	1	0.916	0.979	17.795	16.173	16.173	0.000	0.000	0.000	0.000
46	A	203	ARG	1	0.887	0.934	20.272	11.104	11.104	0.000	0.000	0.000	0.000
47	A	204	ARG	1	0.980	1.002	21.889	11.079	11.079	0.000	0.000	0.000	0.000
48	A	205	LEU	0	0.042	0.024	16.832	-0.063	-0.063	0.000	0.000	0.000	0.000
49	A	206	GLN	0	-0.006	-0.014	17.323	-1.220	-1.220	0.000	0.000	0.000	0.000
50	A	207	GLN	0	-0.062	-0.031	18.570	0.120	0.120	0.000	0.000	0.000	0.000
51	A	208	GLY	0	0.033	0.023	19.117	0.321	0.321	0.000	0.000	0.000	0.000
52	A	209	LYS	1	0.842	0.924	19.975	12.136	12.136	0.000	0.000	0.000	0.000
53	A	210	ILE	0	-0.009	-0.001	20.324	0.590	0.590	0.000	0.000	0.000	0.000
54	A	211	THR	0	0.027	0.021	17.631	-0.631	-0.631	0.000	0.000	0.000	0.000
55	A	212	VAL	0	0.016	-0.011	13.750	0.618	0.618	0.000	0.000	0.000	0.000
56	A	213	LEU	0	-0.024	-0.026	13.434	0.422	0.422	0.000	0.000	0.000	0.000
57	A	214	ASP	-1	-0.876	-0.926	16.750	-12.430	-12.430	0.000	0.000	0.000	0.000
58	A	215	LEU	0	-0.098	-0.053	18.559	0.611	0.611	0.000	0.000	0.000	0.000
59	A	216	ILE	0	-0.054	-0.015	15.164	0.204	0.204	0.000	0.000	0.000	0.000
60	A	217	SER	0	0.031	-0.006	19.389	0.579	0.579	0.000	0.000	0.000	0.000
61	A	218	CYS	0	-0.062	-0.029	21.091	0.500	0.500	0.000	0.000	0.000	0.000
62	A	219	ARG	1	0.948	0.980	23.440	11.803	11.803	0.000	0.000	0.000	0.000
63	A	220	GLU	-1	-0.882	-0.917	20.473	-12.579	-12.579	0.000	0.000	0.000	0.000
64	A	221	GLY	0	0.032	-0.003	24.813	0.402	0.402	0.000	0.000	0.000	0.000
65	A	222	LYS	1	0.921	0.957	25.798	8.784	8.784	0.000	0.000	0.000	0.000
66	A	223	ASP	-1	-0.866	-0.923	24.298	-10.122	-10.122	0.000	0.000	0.000	0.000
67	A	224	SER	0	-0.097	-0.054	21.567	-0.433	-0.433	0.000	0.000	0.000	0.000
68	A	225	PHE	0	0.083	0.035	18.743	-0.457	-0.457	0.000	0.000	0.000	0.000
69	A	226	LYS	1	0.988	0.988	18.722	11.276	11.276	0.000	0.000	0.000	0.000
70	A	227	ARG	1	0.977	0.981	18.476	10.974	10.974	0.000	0.000	0.000	0.000
71	A	228	ILE	0	0.010	0.004	14.889	-0.602	-0.602	0.000	0.000	0.000	0.000
72	A	229	PHE	0	0.010	0.011	14.108	-0.924	-0.924	0.000	0.000	0.000	0.000
73	A	230	SER	0	-0.012	0.012	13.685	-0.688	-0.688	0.000	0.000	0.000	0.000
74	A	231	LYS	1	0.888	0.971	13.290	13.579	13.579	0.000	0.000	0.000	0.000
75	A	232	GLU	-1	-0.802	-0.865	8.315	-21.146	-21.146	0.000	0.000	0.000	0.000
76	A	233	ILE	0	0.013	-0.003	8.019	1.130	1.130	0.000	0.000	0.000	0.000
77	A	234	ILE	0	-0.012	-0.005	7.079	-2.596	-2.596	0.000	0.000	0.000	0.000
78	A	235	VAL	0	0.011	0.020	6.811	1.969	1.969	0.000	0.000	0.000	0.000
79	A	236	TYR	0	-0.051	-0.061	8.801	-2.178	-2.178	0.000	0.000	0.000	0.000
80	A	237	ASP	-1	-0.765	-0.871	10.894	-23.099	-23.099	0.000	0.000	0.000	0.000
81	A	238	GLU	-1	-0.877	-0.951	12.654	-15.799	-15.799	0.000	0.000	0.000	0.000
82	A	239	ASN	0	-0.054	-0.035	13.588	1.184	1.184	0.000	0.000	0.000	0.000
83	A	240	THR	0	0.011	0.003	7.310	-0.068	-0.068	0.000	0.000	0.000	0.000
84	A	241	ASN	0	-0.011	-0.004	8.242	-0.110	-0.110	0.000	0.000	0.000	0.000
85	A	242	GLU	-1	-0.861	-0.959	3.700	-54.596	-54.214	0.003	-0.093	-0.293	-0.001
86	A	243	PRO	0	0.024	0.007	1.972	-2.146	-3.356	6.440	-1.358	-3.872	-0.009
87	A	244	SER	0	-0.036	-0.024	1.863	-1.343	-1.812	4.557	-1.763	-2.325	-0.016
88	A	245	ARG	1	0.968	0.998	3.292	39.801	40.119	0.120	-0.049	-0.389	-0.002
89	A	246	VAL	0	-0.016	0.013	6.209	5.193	5.193	0.000	0.000	0.000	0.000
90	A	247	MET	0	0.016	0.012	8.156	0.445	0.445	0.000	0.000	0.000	0.000
91	A	248	PRO	0	0.070	0.016	11.137	0.261	0.261	0.000	0.000	0.000	0.000
92	A	249	SER	0	-0.027	-0.008	12.329	0.935	0.935	0.000	0.000	0.000	0.000
93	A	250	GLN	0	0.003	-0.003	12.188	1.811	1.811	0.000	0.000	0.000	0.000
94	A	251	PRO	0	0.071	0.014	13.050	-1.190	-1.190	0.000	0.000	0.000	0.000
95	A	252	LEU	0	0.036	0.025	7.141	-0.771	-0.771	0.000	0.000	0.000	0.000
96	A	253	HIS	0	0.011	-0.002	9.002	-3.961	-3.961	0.000	0.000	0.000	0.000
97	A	254	ILE	0	-0.030	-0.004	10.073	0.065	0.065	0.000	0.000	0.000	0.000
98	A	255	VAL	0	0.021	-0.008	10.605	0.173	0.173	0.000	0.000	0.000	0.000
99	A	256	LEU	0	-0.010	-0.011	5.201	-0.380	-0.380	0.000	0.000	0.000	0.000
100	A	257	GLU	-1	-0.878	-0.925	8.646	-23.604	-23.604	0.000	0.000	0.000	0.000
101	A	258	SER	0	-0.040	-0.033	10.563	1.257	1.257	0.000	0.000	0.000	0.000
102	A	259	LEU	0	0.026	0.009	8.933	0.844	0.844	0.000	0.000	0.000	0.000
103	A	260	LYS	1	0.993	1.000	6.814	34.423	34.423	0.000	0.000	0.000	0.000
104	A	261	ARG	1	0.824	0.917	9.839	21.485	21.485	0.000	0.000	0.000	0.000
105	A	262	GLU	-1	-0.771	-0.886	13.230	-16.688	-16.688	0.000	0.000	0.000	0.000
106	A	263	GLY	0	0.003	0.007	12.940	1.040	1.040	0.000	0.000	0.000	0.000
107	A	264	LYS	1	0.758	0.855	9.410	20.146	20.146	0.000	0.000	0.000	0.000
108	A	265	GLU	-1	-0.909	-0.954	5.002	-36.773	-36.773	0.000	0.000	0.000	0.000
109	A	266	PRO	0	-0.079	-0.037	4.962	-0.004	0.151	-0.001	-0.026	-0.128	0.000
110	A	267	LEU	0	-0.036	0.000	2.136	-8.734	-7.056	2.616	-1.888	-2.407	-0.010
111	A	268	VAL	0	0.011	-0.014	3.739	2.506	3.623	0.006	-0.481	-0.642	0.001
112	A	269	LEU	0	-0.024	-0.014	5.655	-0.125	-0.125	0.000	0.000	0.000	0.000
113	A	270	LYS	1	0.851	0.929	6.951	30.553	30.553	0.000	0.000	0.000	0.000
114	A	271	GLY	0	0.029	-0.003	8.275	2.347	2.347	0.000	0.000	0.000	0.000
115	A	272	GLY	0	-0.037	-0.008	10.517	1.701	1.701	0.000	0.000	0.000	0.000
116	A	273	LEU	0	0.074	0.025	12.321	0.421	0.421	0.000	0.000	0.000	0.000
117	A	274	SER	0	-0.082	-0.072	15.772	1.290	1.290	0.000	0.000	0.000	0.000
118	A	275	SER	0	0.063	0.009	13.856	0.889	0.889	0.000	0.000	0.000	0.000
119	A	276	PHE	0	-0.033	-0.006	14.711	0.258	0.258	0.000	0.000	0.000	0.000
120	A	277	LYS	1	0.937	0.986	16.374	15.075	15.075	0.000	0.000	0.000	0.000
121	A	278	GLN	0	-0.097	-0.023	18.886	0.961	0.961	0.000	0.000	0.000	0.000
122	A	279	ASN	0	0.015	0.007	19.610	0.912	0.912	0.000	0.000	0.000	0.000
123	A	280	HIS	1	0.821	0.877	17.792	14.561	14.561	0.000	0.000	0.000	0.000
124	A	281	GLU	-1	-0.743	-0.861	21.035	-12.789	-12.789	0.000	0.000	0.000	0.000
125	A	282	ASN	0	-0.005	-0.004	23.093	-0.108	-0.108	0.000	0.000	0.000	0.000
126	A	283	LEU	0	-0.052	-0.024	18.634	0.123	0.123	0.000	0.000	0.000	0.000
127	A	284	CYS	0	-0.037	-0.015	20.299	-0.974	-0.974	0.000	0.000	0.000	0.000
128	A	285	ASP	-1	-0.868	-0.932	22.042	-11.076	-11.076	0.000	0.000	0.000	0.000
129	A	286	ASN	0	-0.047	-0.041	24.639	-0.550	-0.550	0.000	0.000	0.000	0.000
130	A	287	SER	0	-0.013	-0.006	27.034	0.496	0.496	0.000	0.000	0.000	0.000
131	A	288	LYS	1	0.868	0.938	29.614	9.587	9.587	0.000	0.000	0.000	0.000
132	A	289	GLU	-1	-0.887	-0.944	29.174	-10.227	-10.227	0.000	0.000	0.000	0.000

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