FMO DATABASE

FMODB ID: 4J37N

Calculation Name: 2E7S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2E7S

Chain ID: A

ChEMBL ID:

UniProt ID: P17065

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-585577.166772
FMO2-HF: Nuclear repulsion	538704.413339
FMO2-HF: Total energy	-46872.753433
FMO2-MP2: Total energy	-47010.21873

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:31:LEU)

Summations of interaction energy for fragment #1(A:31:LEU)

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.
-2.43	1.024	1.944	-1.592	-3.806	0.004

Interaction energy analysis for fragmet #1(A:31:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.030

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	33	GLU	-1	-0.947	-0.964	3.354	-0.868	0.929	0.015	-0.721	-1.091	0.001
4	A	34	GLN	0	-0.065	-0.049	2.323	-1.697	-0.770	1.927	-0.696	-2.158	0.003
5	A	35	LEU	0	-0.018	0.017	3.818	-0.492	0.115	0.003	-0.168	-0.441	0.000
6	A	36	ASN	0	0.026	0.030	4.901	0.317	0.440	-0.001	-0.007	-0.116	0.000
7	A	37	LYS	1	1.021	0.994	8.321	-0.215	-0.215	0.000	0.000	0.000	0.000
8	A	38	SER	0	0.028	0.030	7.375	0.112	0.112	0.000	0.000	0.000	0.000
9	A	39	LEU	0	0.087	0.046	9.181	0.066	0.066	0.000	0.000	0.000	0.000
10	A	40	LYS	1	0.961	0.971	10.898	0.164	0.164	0.000	0.000	0.000	0.000
11	A	41	THR	0	-0.057	-0.040	12.350	0.067	0.067	0.000	0.000	0.000	0.000
12	A	42	ILE	0	0.011	0.007	12.514	0.033	0.033	0.000	0.000	0.000	0.000
13	A	43	ALA	0	-0.039	-0.011	14.655	0.031	0.031	0.000	0.000	0.000	0.000
14	A	44	SER	0	-0.002	-0.023	16.660	0.030	0.030	0.000	0.000	0.000	0.000
15	A	45	GLN	0	-0.009	0.013	17.505	0.003	0.003	0.000	0.000	0.000	0.000
16	A	46	LYS	1	0.915	0.954	18.857	0.191	0.191	0.000	0.000	0.000	0.000
17	A	47	ALA	0	0.015	0.010	20.769	0.014	0.014	0.000	0.000	0.000	0.000
18	A	48	ALA	0	-0.011	0.006	22.165	0.015	0.015	0.000	0.000	0.000	0.000
19	A	49	ILE	0	-0.045	-0.028	21.992	0.011	0.011	0.000	0.000	0.000	0.000
20	A	50	GLU	-1	-0.904	-0.967	24.656	-0.132	-0.132	0.000	0.000	0.000	0.000
21	A	51	ASN	0	0.012	0.022	26.516	0.006	0.006	0.000	0.000	0.000	0.000
22	A	52	TYR	0	0.019	0.001	28.631	0.006	0.006	0.000	0.000	0.000	0.000
23	A	53	ASN	0	-0.043	-0.035	27.543	0.008	0.008	0.000	0.000	0.000	0.000
24	A	54	GLN	0	0.065	0.045	30.624	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	55	LEU	0	0.034	0.031	32.496	0.005	0.005	0.000	0.000	0.000	0.000
26	A	56	LYS	1	0.897	0.927	33.881	0.058	0.058	0.000	0.000	0.000	0.000
27	A	57	GLU	-1	-0.959	-0.962	33.671	-0.082	-0.082	0.000	0.000	0.000	0.000
28	A	58	ASP	-1	-0.870	-0.935	36.389	-0.059	-0.059	0.000	0.000	0.000	0.000
29	A	59	TYR	0	-0.070	-0.034	38.349	0.005	0.005	0.000	0.000	0.000	0.000
30	A	60	ASN	0	-0.054	-0.057	38.911	0.006	0.006	0.000	0.000	0.000	0.000
31	A	61	THR	0	-0.002	0.013	40.427	0.001	0.001	0.000	0.000	0.000	0.000
32	A	62	LEU	0	0.064	0.026	42.671	0.002	0.002	0.000	0.000	0.000	0.000
33	A	63	LYS	1	0.860	0.937	42.713	0.046	0.046	0.000	0.000	0.000	0.000
34	A	64	ARG	1	0.938	0.989	42.111	0.052	0.052	0.000	0.000	0.000	0.000
35	A	65	GLU	-1	-0.827	-0.925	47.042	-0.037	-0.037	0.000	0.000	0.000	0.000
36	A	66	LEU	0	-0.089	-0.040	48.740	0.002	0.002	0.000	0.000	0.000	0.000
37	A	67	SER	0	-0.037	-0.037	50.280	0.001	0.001	0.000	0.000	0.000	0.000
38	A	68	ASP	-1	-0.889	-0.920	50.420	-0.038	-0.038	0.000	0.000	0.000	0.000
39	A	69	ARG	1	0.842	0.915	51.290	0.032	0.032	0.000	0.000	0.000	0.000
40	A	70	ASP	-1	-0.884	-0.942	54.112	-0.026	-0.026	0.000	0.000	0.000	0.000
41	A	71	ASP	-1	-0.916	-0.973	55.305	-0.030	-0.030	0.000	0.000	0.000	0.000
42	A	72	GLU	-1	-0.979	-0.997	57.061	-0.027	-0.027	0.000	0.000	0.000	0.000
43	A	73	VAL	0	-0.006	-0.001	58.971	0.001	0.001	0.000	0.000	0.000	0.000
44	A	74	LYS	1	0.905	0.941	59.014	0.026	0.026	0.000	0.000	0.000	0.000
45	A	75	ARG	1	1.006	1.013	57.557	0.030	0.030	0.000	0.000	0.000	0.000
46	A	76	LEU	0	0.076	0.051	62.680	0.001	0.001	0.000	0.000	0.000	0.000
47	A	77	ARG	1	0.856	0.918	64.713	0.018	0.018	0.000	0.000	0.000	0.000
48	A	78	GLU	-1	-0.945	-0.963	65.092	-0.022	-0.022	0.000	0.000	0.000	0.000
49	A	79	ASP	-1	-0.891	-0.937	67.481	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	80	ILE	0	-0.097	-0.043	68.966	0.001	0.001	0.000	0.000	0.000	0.000
51	A	81	ALA	0	0.029	0.016	71.434	0.001	0.001	0.000	0.000	0.000	0.000
52	A	82	LYS	1	1.019	0.997	72.880	0.019	0.019	0.000	0.000	0.000	0.000
53	A	83	GLU	-1	-0.920	-0.980	73.768	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	84	ASN	0	-0.097	-0.054	74.474	0.001	0.001	0.000	0.000	0.000	0.000
55	A	85	GLU	-1	-0.973	-0.957	77.053	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	86	LEU	0	-0.067	-0.035	77.409	0.000	0.000	0.000	0.000	0.000	0.000
57	A	87	ARG	1	0.949	0.966	79.792	0.014	0.014	0.000	0.000	0.000	0.000
58	A	88	THR	0	0.031	0.016	81.058	0.000	0.000	0.000	0.000	0.000	0.000
59	A	89	LYS	1	1.044	1.027	82.926	0.015	0.015	0.000	0.000	0.000	0.000
60	A	90	ALA	0	-0.102	-0.044	84.252	0.000	0.000	0.000	0.000	0.000	0.000
61	A	91	GLU	-1	-0.977	-0.985	85.571	-0.011	-0.011	0.000	0.000	0.000	0.000
62	A	92	GLU	-1	-0.896	-0.942	87.120	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	93	GLU	-1	-1.056	-1.043	89.104	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	94	ALA	0	-0.009	-0.008	89.827	0.000	0.000	0.000	0.000	0.000	0.000
65	A	95	ASP	-1	-0.910	-0.968	91.818	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	96	LYS	1	0.917	0.966	93.733	0.011	0.011	0.000	0.000	0.000	0.000
67	A	97	LEU	0	-0.005	0.002	94.663	0.000	0.000	0.000	0.000	0.000	0.000
68	A	98	ASN	0	0.028	-0.010	94.614	0.000	0.000	0.000	0.000	0.000	0.000
69	A	99	LYS	1	1.008	1.012	97.516	0.009	0.009	0.000	0.000	0.000	0.000
70	A	100	GLU	-1	-0.922	-0.933	99.812	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	101	VAL	0	-0.074	-0.032	99.725	0.000	0.000	0.000	0.000	0.000	0.000
72	A	102	GLU	-1	-0.992	-0.971	101.549	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	103	ASP	-1	-0.892	-0.946	103.858	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	104	LEU	0	-0.041	-0.016	104.913	0.000	0.000	0.000	0.000	0.000	0.000
75	A	105	THR	0	-0.063	-0.084	105.244	0.000	0.000	0.000	0.000	0.000	0.000
76	A	106	ALA	0	-0.005	-0.013	107.930	0.000	0.000	0.000	0.000	0.000	0.000
77	A	107	SER	0	0.007	0.021	109.825	0.000	0.000	0.000	0.000	0.000	0.000
78	A	108	LEU	0	-0.031	0.000	110.835	0.000	0.000	0.000	0.000	0.000	0.000
79	A	109	PHE	0	-0.049	-0.048	112.189	0.000	0.000	0.000	0.000	0.000	0.000
80	A	110	ASP	-1	-0.857	-0.923	114.050	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	111	GLU	-1	-0.932	-0.954	115.781	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	112	ALA	0	-0.049	-0.028	116.874	0.000	0.000	0.000	0.000	0.000	0.000
83	A	113	ASN	0	-0.009	-0.007	117.002	0.000	0.000	0.000	0.000	0.000	0.000
84	A	114	ASN	0	-0.036	-0.038	118.945	0.000	0.000	0.000	0.000	0.000	0.000
85	A	115	LEU	0	0.035	0.038	121.449	0.000	0.000	0.000	0.000	0.000	0.000
86	A	116	VAL	0	-0.033	-0.024	122.251	0.000	0.000	0.000	0.000	0.000	0.000
87	A	117	ALA	0	-0.025	-0.010	123.947	0.000	0.000	0.000	0.000	0.000	0.000
88	A	118	ASP	-1	-0.778	-0.904	125.623	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	119	ALA	0	-0.065	-0.033	126.955	0.000	0.000	0.000	0.000	0.000	0.000
90	A	120	ARG	1	0.841	0.912	127.575	0.006	0.006	0.000	0.000	0.000	0.000
91	A	121	MET	0	-0.006	0.017	130.029	0.000	0.000	0.000	0.000	0.000	0.000
92	A	122	GLU	-1	-0.920	-0.966	130.610	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	123	LYS	1	0.899	0.967	132.732	0.005	0.005	0.000	0.000	0.000	0.000
94	A	124	TYR	0	0.030	-0.027	133.018	0.000	0.000	0.000	0.000	0.000	0.000
95	A	125	ALA	0	0.004	0.021	136.638	0.000	0.000	0.000	0.000	0.000	0.000
96	A	126	ILE	0	0.006	-0.002	137.046	0.000	0.000	0.000	0.000	0.000	0.000
97	A	127	GLU	-1	-0.985	-0.970	138.555	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	128	ILE	0	-0.001	-0.016	140.352	0.000	0.000	0.000	0.000	0.000	0.000
99	A	129	LEU	0	-0.040	-0.007	141.560	0.000	0.000	0.000	0.000	0.000	0.000
100	A	130	ASN	0	0.061	0.011	141.560	0.000	0.000	0.000	0.000	0.000	0.000
101	A	131	LYS	1	0.941	0.984	143.674	0.004	0.004	0.000	0.000	0.000	0.000
102	A	132	ARG	1	0.997	1.004	146.578	0.004	0.004	0.000	0.000	0.000	0.000
103	A	133	LEU	0	-0.018	-0.011	145.936	0.000	0.000	0.000	0.000	0.000	0.000
104	A	134	THR	0	-0.028	-0.011	147.062	0.000	0.000	0.000	0.000	0.000	0.000
105	A	135	GLU	-1	-0.981	-0.996	149.863	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	136	GLN	0	0.020	-0.006	152.249	0.000	0.000	0.000	0.000	0.000	0.000
107	A	137	LEU	0	-0.067	-0.032	151.088	0.000	0.000	0.000	0.000	0.000	0.000
108	A	138	ARG	1	0.995	1.012	152.642	0.004	0.004	0.000	0.000	0.000	0.000
109	A	139	GLU	-1	-0.983	-0.980	156.210	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	140	LYS	1	0.902	0.956	156.606	0.004	0.004	0.000	0.000	0.000	0.000
111	A	141	ASP	-1	-0.875	-0.945	157.528	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	142	MET	0	-0.082	-0.038	160.279	0.000	0.000	0.000	0.000	0.000	0.000
113	A	143	LEU	0	-0.030	-0.006	162.485	0.000	0.000	0.000	0.000	0.000	0.000
114	A	144	LEU	0	-0.039	-0.006	162.130	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:LEU)