FMO DATABASE

FMODB ID: V53R1

Calculation Name: 2E0T-A-Xray372

Preferred Name: Dual specificity protein phosphatase 26

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2E0T

Chain ID: A

ChEMBL ID: CHEMBL2295562

UniProt ID: Q9BV47

Base Structure: X-ray

Registration Date: 2023-09-20

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	150
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1357872.968898
FMO2-HF: Nuclear repulsion	1298931.662024
FMO2-HF: Total energy	-58941.306875
FMO2-MP2: Total energy	-59115.038595

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:61:HIS)

Summations of interaction energy for fragment #1(A:61:HIS)

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.
-48.042	-37.819	16.514	-11.148	-15.591	-0.081

Interaction energy analysis for fragmet #1(A:61:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.049 / q_NPA : -0.034

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	63	ASP	-1	-0.838	-0.892	2.110	-34.605	-30.640	6.210	-4.348	-5.826	-0.044
4	A	64	GLU	-1	-0.788	-0.862	4.226	0.417	0.598	0.000	-0.040	-0.141	0.000
5	A	65	VAL	0	-0.041	-0.040	6.630	-0.062	-0.062	0.000	0.000	0.000	0.000
6	A	66	TRP	0	0.005	0.000	9.033	0.214	0.214	0.000	0.000	0.000	0.000
7	A	67	PRO	0	0.004	0.006	12.226	-0.006	-0.006	0.000	0.000	0.000	0.000
8	A	68	GLY	0	0.031	0.020	13.424	0.047	0.047	0.000	0.000	0.000	0.000
9	A	69	LEU	0	-0.039	-0.023	11.115	0.125	0.125	0.000	0.000	0.000	0.000
10	A	70	TYR	0	-0.062	-0.066	7.493	-0.208	-0.208	0.000	0.000	0.000	0.000
11	A	71	LEU	0	-0.004	0.007	5.922	0.450	0.450	0.000	0.000	0.000	0.000
12	A	72	GLY	0	0.030	-0.014	3.668	-1.932	-1.691	0.002	-0.074	-0.170	0.000
13	A	73	ASP	-1	-0.853	-0.919	2.135	-16.401	-13.703	6.745	-4.339	-5.105	-0.056
14	A	74	GLN	0	-0.004	-0.023	4.381	1.230	1.308	-0.001	-0.007	-0.070	0.000
15	A	75	ASP	-1	-0.851	-0.931	4.001	0.443	0.550	-0.001	-0.021	-0.086	0.000
16	A	76	MET	0	-0.067	-0.032	2.298	-2.030	-0.575	3.453	-1.860	-3.049	0.017
17	A	77	ALA	0	-0.036	-0.011	3.930	-0.383	-0.206	0.012	-0.102	-0.087	0.001
18	A	78	ASN	0	0.022	0.027	6.828	-0.117	-0.117	0.000	0.000	0.000	0.000
19	A	79	ASN	0	-0.001	0.010	5.765	-0.861	-0.861	0.000	0.000	0.000	0.000
20	A	80	ARG	1	0.990	0.993	8.307	-0.592	-0.592	0.000	0.000	0.000	0.000
21	A	81	ARG	1	0.948	0.969	11.024	-1.743	-1.743	0.000	0.000	0.000	0.000
22	A	82	GLU	-1	-0.770	-0.856	5.516	4.446	4.446	0.000	0.000	0.000	0.000
23	A	83	LEU	0	0.029	0.019	8.180	-0.270	-0.270	0.000	0.000	0.000	0.000
24	A	84	ARG	1	0.927	0.965	9.854	-1.251	-1.251	0.000	0.000	0.000	0.000
25	A	85	ARG	1	0.761	0.851	7.526	-3.428	-3.428	0.000	0.000	0.000	0.000
26	A	86	LEU	0	-0.008	-0.011	6.218	-0.238	-0.238	0.000	0.000	0.000	0.000
27	A	87	GLY	0	0.013	0.020	10.933	-0.310	-0.310	0.000	0.000	0.000	0.000
28	A	88	ILE	0	-0.039	-0.007	9.496	-0.200	-0.200	0.000	0.000	0.000	0.000
29	A	89	THR	0	0.030	-0.012	13.129	0.020	0.020	0.000	0.000	0.000	0.000
30	A	90	HIS	0	0.000	0.026	14.791	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	91	VAL	0	0.013	0.011	10.828	0.004	0.004	0.000	0.000	0.000	0.000
32	A	92	LEU	0	-0.022	-0.006	12.683	0.028	0.028	0.000	0.000	0.000	0.000
33	A	93	ASN	0	0.033	0.011	12.290	-0.330	-0.330	0.000	0.000	0.000	0.000
34	A	94	ALA	0	-0.003	-0.024	12.831	0.086	0.086	0.000	0.000	0.000	0.000
35	A	95	SER	0	-0.002	-0.007	13.439	-0.070	-0.070	0.000	0.000	0.000	0.000
36	A	96	HIS	0	0.007	0.039	15.172	0.004	0.004	0.000	0.000	0.000	0.000
37	A	97	SER	0	-0.021	-0.015	16.849	0.010	0.010	0.000	0.000	0.000	0.000
38	A	98	ARG	1	1.030	1.007	18.763	0.218	0.218	0.000	0.000	0.000	0.000
39	A	99	TRP	0	-0.036	-0.011	19.403	0.005	0.005	0.000	0.000	0.000	0.000
40	A	100	ARG	1	0.943	0.987	13.721	0.146	0.146	0.000	0.000	0.000	0.000
41	A	101	GLY	0	0.063	0.028	20.218	-0.025	-0.025	0.000	0.000	0.000	0.000
42	A	102	THR	0	-0.042	-0.038	17.899	-0.044	-0.044	0.000	0.000	0.000	0.000
43	A	103	PRO	0	0.012	0.026	13.556	0.030	0.030	0.000	0.000	0.000	0.000
44	A	104	GLU	-1	-0.834	-0.918	15.637	0.283	0.283	0.000	0.000	0.000	0.000
45	A	105	ALA	0	-0.088	-0.054	14.026	0.029	0.029	0.000	0.000	0.000	0.000
46	A	106	TYR	0	-0.037	-0.058	10.293	-0.043	-0.043	0.000	0.000	0.000	0.000
47	A	107	GLU	-1	-0.867	-0.916	16.293	0.201	0.201	0.000	0.000	0.000	0.000
48	A	108	GLY	0	-0.001	-0.005	19.521	0.002	0.002	0.000	0.000	0.000	0.000
49	A	109	LEU	0	-0.147	-0.077	13.116	0.038	0.038	0.000	0.000	0.000	0.000
50	A	110	GLY	0	0.028	0.031	17.399	0.016	0.016	0.000	0.000	0.000	0.000
51	A	111	ILE	0	-0.062	-0.019	12.748	-0.035	-0.035	0.000	0.000	0.000	0.000
52	A	112	ARG	1	0.911	0.967	17.042	0.036	0.036	0.000	0.000	0.000	0.000
53	A	113	TYR	0	0.013	-0.030	13.772	-0.041	-0.041	0.000	0.000	0.000	0.000
54	A	114	LEU	0	-0.008	0.002	16.644	0.013	0.013	0.000	0.000	0.000	0.000
55	A	115	GLY	0	0.019	0.009	16.522	-0.060	-0.060	0.000	0.000	0.000	0.000
56	A	116	VAL	0	-0.017	-0.001	17.390	0.038	0.038	0.000	0.000	0.000	0.000
57	A	117	GLU	-1	-0.924	-0.961	18.086	-0.327	-0.327	0.000	0.000	0.000	0.000
58	A	118	ALA	0	0.037	0.010	18.399	0.006	0.006	0.000	0.000	0.000	0.000
59	A	119	HIS	0	-0.004	0.015	18.638	-0.070	-0.070	0.000	0.000	0.000	0.000
60	A	120	ASP	-1	-0.785	-0.865	14.690	-1.174	-1.174	0.000	0.000	0.000	0.000
61	A	121	SER	0	0.011	-0.004	18.300	0.021	0.021	0.000	0.000	0.000	0.000
62	A	122	PRO	0	0.024	0.006	21.663	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	123	ALA	0	-0.010	0.001	23.424	0.016	0.016	0.000	0.000	0.000	0.000
64	A	124	PHE	0	-0.026	-0.008	21.713	0.036	0.036	0.000	0.000	0.000	0.000
65	A	125	ASP	-1	-0.782	-0.869	23.205	-0.531	-0.531	0.000	0.000	0.000	0.000
66	A	126	MET	0	-0.014	-0.019	18.303	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	127	SER	0	0.004	-0.030	21.608	-0.024	-0.024	0.000	0.000	0.000	0.000
68	A	128	ILE	0	-0.060	-0.013	23.913	0.021	0.021	0.000	0.000	0.000	0.000
69	A	129	HIS	0	-0.021	-0.026	20.759	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	130	PHE	0	-0.009	0.001	19.866	-0.032	-0.032	0.000	0.000	0.000	0.000
71	A	131	GLN	0	0.013	0.007	21.751	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	132	THR	0	0.034	0.018	23.076	0.005	0.005	0.000	0.000	0.000	0.000
73	A	133	ALA	0	0.003	0.001	17.936	0.016	0.016	0.000	0.000	0.000	0.000
74	A	134	ALA	0	0.016	0.013	19.298	-0.017	-0.017	0.000	0.000	0.000	0.000
75	A	135	ASP	-1	-0.787	-0.881	20.542	-0.353	-0.353	0.000	0.000	0.000	0.000
76	A	136	PHE	0	-0.120	-0.065	16.540	0.059	0.059	0.000	0.000	0.000	0.000
77	A	137	ILE	0	0.014	0.001	15.568	0.037	0.037	0.000	0.000	0.000	0.000
78	A	138	HIS	0	0.061	0.041	18.436	0.006	0.006	0.000	0.000	0.000	0.000
79	A	139	ARG	1	0.904	0.966	21.517	0.281	0.281	0.000	0.000	0.000	0.000
80	A	140	ALA	0	-0.031	-0.019	18.064	0.045	0.045	0.000	0.000	0.000	0.000
81	A	141	LEU	0	-0.008	-0.019	15.560	0.044	0.044	0.000	0.000	0.000	0.000
82	A	142	SER	0	-0.029	-0.001	19.711	0.019	0.019	0.000	0.000	0.000	0.000
83	A	143	GLN	0	-0.060	-0.017	21.974	0.018	0.018	0.000	0.000	0.000	0.000
84	A	144	PRO	0	0.054	0.016	21.944	0.002	0.002	0.000	0.000	0.000	0.000
85	A	145	GLY	0	-0.015	-0.005	19.840	0.036	0.036	0.000	0.000	0.000	0.000
86	A	146	GLY	0	-0.030	-0.008	18.331	0.080	0.080	0.000	0.000	0.000	0.000
87	A	147	LYS	1	0.817	0.905	13.243	-0.394	-0.394	0.000	0.000	0.000	0.000
88	A	148	ILE	0	0.005	0.007	13.547	0.126	0.126	0.000	0.000	0.000	0.000
89	A	149	LEU	0	-0.001	0.021	6.088	-0.135	-0.135	0.000	0.000	0.000	0.000
90	A	150	VAL	0	-0.003	0.000	9.517	0.126	0.126	0.000	0.000	0.000	0.000
91	A	151	HIS	0	-0.002	-0.011	7.275	-0.400	-0.400	0.000	0.000	0.000	0.000
92	A	152	CYS	0	-0.028	-0.008	8.899	0.442	0.442	0.000	0.000	0.000	0.000
93	A	153	ALA	0	0.025	-0.004	8.956	-0.257	-0.257	0.000	0.000	0.000	0.000
94	A	154	VAL	0	-0.022	-0.010	10.123	0.018	0.018	0.000	0.000	0.000	0.000
95	A	155	GLY	0	0.066	0.034	8.251	-0.030	-0.030	0.000	0.000	0.000	0.000
96	A	156	VAL	0	-0.026	-0.026	5.727	-0.372	-0.372	0.000	0.000	0.000	0.000
97	A	157	SER	0	-0.049	-0.027	8.758	0.117	0.117	0.000	0.000	0.000	0.000
98	A	158	ARG	1	0.886	0.908	12.516	0.949	0.949	0.000	0.000	0.000	0.000
99	A	159	SER	0	0.011	0.011	8.504	0.154	0.154	0.000	0.000	0.000	0.000
100	A	160	ALA	0	0.024	0.004	9.945	0.066	0.066	0.000	0.000	0.000	0.000
101	A	161	THR	0	-0.017	-0.005	11.429	0.157	0.157	0.000	0.000	0.000	0.000
102	A	162	LEU	0	0.012	0.005	14.588	0.115	0.115	0.000	0.000	0.000	0.000
103	A	163	VAL	0	-0.006	0.005	10.884	0.107	0.107	0.000	0.000	0.000	0.000
104	A	164	LEU	0	-0.027	-0.014	13.934	0.105	0.105	0.000	0.000	0.000	0.000
105	A	165	ALA	0	0.036	0.018	16.084	0.109	0.109	0.000	0.000	0.000	0.000
106	A	166	TYR	0	-0.003	-0.024	16.412	0.099	0.099	0.000	0.000	0.000	0.000
107	A	167	LEU	0	-0.020	-0.008	14.002	0.070	0.070	0.000	0.000	0.000	0.000
108	A	168	MET	0	-0.066	-0.026	18.417	0.045	0.045	0.000	0.000	0.000	0.000
109	A	169	LEU	0	-0.055	-0.024	21.396	0.064	0.064	0.000	0.000	0.000	0.000
110	A	170	TYR	0	-0.030	-0.046	21.400	0.062	0.062	0.000	0.000	0.000	0.000
111	A	171	HIS	0	-0.059	-0.018	18.344	0.000	0.000	0.000	0.000	0.000	0.000
112	A	172	HIS	0	0.013	0.012	22.216	-0.024	-0.024	0.000	0.000	0.000	0.000
113	A	173	LEU	0	-0.014	0.024	18.028	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	174	THR	0	0.017	-0.035	22.012	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	175	LEU	0	0.056	0.002	18.450	-0.069	-0.069	0.000	0.000	0.000	0.000
116	A	176	VAL	0	-0.016	-0.013	18.561	-0.114	-0.114	0.000	0.000	0.000	0.000
117	A	177	GLU	-1	-0.802	-0.865	18.287	-0.741	-0.741	0.000	0.000	0.000	0.000
118	A	178	ALA	0	0.017	0.015	16.524	-0.105	-0.105	0.000	0.000	0.000	0.000
119	A	179	ILE	0	0.004	-0.019	14.239	-0.234	-0.234	0.000	0.000	0.000	0.000
120	A	180	LYS	1	0.816	0.894	13.247	0.863	0.863	0.000	0.000	0.000	0.000
121	A	181	LYS	1	0.890	0.950	13.184	1.092	1.092	0.000	0.000	0.000	0.000
122	A	182	VAL	0	0.043	0.012	8.965	-0.278	-0.278	0.000	0.000	0.000	0.000
123	A	183	LYS	1	0.917	0.951	8.689	0.909	0.909	0.000	0.000	0.000	0.000
124	A	184	ASP	-1	-0.851	-0.895	9.224	-1.640	-1.640	0.000	0.000	0.000	0.000
125	A	185	HIS	0	-0.056	-0.020	8.271	0.506	0.506	0.000	0.000	0.000	0.000
126	A	186	ARG	1	0.868	0.954	2.688	9.293	10.232	0.097	-0.318	-0.717	0.001
127	A	187	GLY	0	-0.004	0.006	4.119	1.602	1.751	-0.001	-0.014	-0.134	0.000
128	A	188	ILE	0	0.034	0.006	4.423	-0.693	-0.590	-0.001	-0.015	-0.086	0.000
129	A	189	ILE	0	-0.057	-0.031	6.622	0.791	0.791	0.000	0.000	0.000	0.000
130	A	190	PRO	0	0.043	0.026	4.019	-0.319	-0.189	-0.001	-0.010	-0.120	0.000
131	A	191	ASN	0	0.007	0.026	6.082	0.191	0.191	0.000	0.000	0.000	0.000
132	A	192	ARG	1	1.042	0.994	9.605	-0.727	-0.727	0.000	0.000	0.000	0.000
133	A	193	GLY	0	0.025	0.016	12.070	-0.175	-0.175	0.000	0.000	0.000	0.000
134	A	194	PHE	0	0.030	-0.005	11.237	-0.094	-0.094	0.000	0.000	0.000	0.000
135	A	195	LEU	0	0.044	0.028	11.423	-0.114	-0.114	0.000	0.000	0.000	0.000
136	A	196	ARG	1	0.931	0.968	13.418	-0.556	-0.556	0.000	0.000	0.000	0.000
137	A	197	GLN	0	0.009	-0.005	16.603	0.000	0.000	0.000	0.000	0.000	0.000
138	A	198	LEU	0	0.037	0.021	13.386	-0.035	-0.035	0.000	0.000	0.000	0.000
139	A	199	LEU	0	0.000	0.004	16.115	-0.040	-0.040	0.000	0.000	0.000	0.000
140	A	200	ALA	0	-0.027	-0.007	18.840	-0.015	-0.015	0.000	0.000	0.000	0.000
141	A	201	LEU	0	-0.046	-0.029	20.428	-0.007	-0.007	0.000	0.000	0.000	0.000
142	A	202	ASP	-1	-0.787	-0.877	20.095	-0.208	-0.208	0.000	0.000	0.000	0.000
143	A	203	ARG	1	0.944	0.980	22.084	0.024	0.024	0.000	0.000	0.000	0.000
144	A	204	ARG	1	0.952	0.980	23.894	-0.053	-0.053	0.000	0.000	0.000	0.000
145	A	205	LEU	0	-0.013	-0.013	23.572	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	206	ARG	1	0.811	0.883	22.680	0.163	0.163	0.000	0.000	0.000	0.000
147	A	207	GLN	0	-0.043	-0.019	27.350	-0.008	-0.008	0.000	0.000	0.000	0.000
148	A	208	GLY	0	0.027	0.037	29.892	0.001	0.001	0.000	0.000	0.000	0.000
149	A	209	LEU	0	-0.038	-0.028	31.896	0.011	0.011	0.000	0.000	0.000	0.000
150	A	210	GLU	-1	-0.975	-0.978	34.310	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:61:HIS)