FMO DATABASE

FMODB ID: 98LJ2

Calculation Name: 2EA9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EA9

Chain ID: A

ChEMBL ID:

UniProt ID: P52141

Base Structure: X-ray

Registration Date: 2023-09-22

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	103
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-779053.753892
FMO2-HF: Nuclear repulsion	738010.646151
FMO2-HF: Total energy	-41043.107741
FMO2-MP2: Total energy	-41160.080802

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:8:MET)

Summations of interaction energy for fragment #1(A:8:MET)

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.
-8.35	-1.778	5.111	-3.239	-8.441	-0.028

Interaction energy analysis for fragmet #1(A:8:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.052 / q_NPA : -0.044

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	10	ASN	0	0.058	0.033	2.921	-0.605	1.976	0.109	-0.892	-1.798	0.002
4	A	11	THR	0	0.022	-0.002	2.563	-4.175	-2.131	2.733	-1.869	-2.907	-0.028
5	A	12	THR	0	0.031	-0.001	2.983	-1.541	-0.949	0.544	0.151	-1.287	-0.003
6	A	13	TRP	0	0.063	0.031	3.504	0.151	0.178	0.013	0.091	-0.130	0.000
7	A	14	GLY	0	0.045	0.023	5.893	0.150	0.150	0.000	0.000	0.000	0.000
8	A	15	LEU	0	-0.034	-0.042	2.503	-0.249	-0.116	1.103	-0.168	-1.068	-0.002
9	A	16	GLN	0	-0.058	-0.021	6.122	0.301	0.301	0.000	0.000	0.000	0.000
10	A	17	ARG	1	0.833	0.951	8.901	0.740	0.740	0.000	0.000	0.000	0.000
11	A	18	ASP	-1	-0.860	-0.930	11.331	-0.382	-0.382	0.000	0.000	0.000	0.000
12	A	19	ILE	0	-0.019	-0.005	14.274	0.009	0.009	0.000	0.000	0.000	0.000
13	A	20	THR	0	-0.063	0.001	14.600	-0.116	-0.116	0.000	0.000	0.000	0.000
14	A	21	PRO	0	-0.024	-0.024	15.674	0.047	0.047	0.000	0.000	0.000	0.000
15	A	22	ARG	1	0.898	0.931	8.968	0.937	0.937	0.000	0.000	0.000	0.000
16	A	23	LEU	0	0.007	0.010	12.553	-0.087	-0.087	0.000	0.000	0.000	0.000
17	A	24	GLY	0	-0.028	-0.010	9.090	0.071	0.071	0.000	0.000	0.000	0.000
18	A	25	ALA	0	0.013	-0.011	9.248	-0.141	-0.141	0.000	0.000	0.000	0.000
19	A	26	ARG	1	0.913	0.981	6.933	0.742	0.742	0.000	0.000	0.000	0.000
20	A	27	LEU	0	-0.015	-0.007	9.753	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	28	VAL	0	0.005	-0.003	12.708	0.037	0.037	0.000	0.000	0.000	0.000
22	A	29	GLN	0	-0.010	-0.008	14.675	0.005	0.005	0.000	0.000	0.000	0.000
23	A	30	GLU	-1	-0.916	-0.958	18.016	-0.186	-0.186	0.000	0.000	0.000	0.000
24	A	31	GLY	0	-0.020	-0.004	21.004	0.005	0.005	0.000	0.000	0.000	0.000
25	A	32	ASN	0	-0.019	-0.032	22.834	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	33	GLN	0	-0.025	-0.005	22.395	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	34	LEU	0	-0.026	-0.006	17.250	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	35	HIS	0	0.021	0.018	16.658	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	36	TYR	0	0.006	-0.020	13.438	-0.073	-0.073	0.000	0.000	0.000	0.000
30	A	37	LEU	0	-0.004	-0.003	10.441	0.068	0.068	0.000	0.000	0.000	0.000
31	A	38	ALA	0	0.034	0.009	10.498	-0.199	-0.199	0.000	0.000	0.000	0.000
32	A	39	ASP	-1	-0.917	-0.960	6.569	-1.794	-1.794	0.000	0.000	0.000	0.000
33	A	40	ARG	1	0.844	0.931	2.731	-0.853	0.342	0.609	-0.552	-1.251	0.003
34	A	41	ALA	0	0.028	0.028	6.984	0.202	0.202	0.000	0.000	0.000	0.000
35	A	42	SER	0	-0.067	-0.039	7.303	-0.141	-0.141	0.000	0.000	0.000	0.000
36	A	43	ILE	0	0.048	0.029	9.450	0.106	0.106	0.000	0.000	0.000	0.000
37	A	44	THR	0	-0.046	-0.008	9.397	-0.077	-0.077	0.000	0.000	0.000	0.000
38	A	45	GLY	0	0.044	0.009	11.579	0.075	0.075	0.000	0.000	0.000	0.000
39	A	46	LYS	1	0.932	0.948	15.050	0.195	0.195	0.000	0.000	0.000	0.000
40	A	47	PHE	0	0.045	0.038	15.735	0.020	0.020	0.000	0.000	0.000	0.000
41	A	48	SER	0	-0.044	-0.027	20.130	0.023	0.023	0.000	0.000	0.000	0.000
42	A	49	ASP	-1	-0.842	-0.942	23.536	-0.187	-0.187	0.000	0.000	0.000	0.000
43	A	50	ALA	0	-0.045	-0.025	25.351	0.000	0.000	0.000	0.000	0.000	0.000
44	A	51	GLU	-1	-0.878	-0.961	22.337	-0.271	-0.271	0.000	0.000	0.000	0.000
45	A	52	CYS	0	0.002	0.017	21.063	-0.023	-0.023	0.000	0.000	0.000	0.000
46	A	53	PRO	0	0.053	0.043	22.523	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	54	LYS	1	0.886	0.934	25.047	0.187	0.187	0.000	0.000	0.000	0.000
48	A	55	LEU	0	0.020	-0.001	17.158	0.001	0.001	0.000	0.000	0.000	0.000
49	A	56	ASP	-1	-0.882	-0.950	20.473	-0.350	-0.350	0.000	0.000	0.000	0.000
50	A	57	VAL	0	-0.076	-0.031	22.077	0.005	0.005	0.000	0.000	0.000	0.000
51	A	58	VAL	0	-0.030	-0.005	21.298	0.007	0.007	0.000	0.000	0.000	0.000
52	A	59	PHE	0	0.009	0.015	15.238	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	60	PRO	0	0.009	0.001	20.419	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	61	HIS	0	0.012	0.022	22.443	0.020	0.020	0.000	0.000	0.000	0.000
55	A	62	PHE	0	0.047	0.013	19.648	0.010	0.010	0.000	0.000	0.000	0.000
56	A	63	ILE	0	-0.007	0.010	17.105	0.002	0.002	0.000	0.000	0.000	0.000
57	A	64	SER	0	0.011	0.011	20.718	0.020	0.020	0.000	0.000	0.000	0.000
58	A	65	GLN	0	-0.040	-0.045	23.270	0.011	0.011	0.000	0.000	0.000	0.000
59	A	66	ILE	0	0.031	0.002	17.626	0.011	0.011	0.000	0.000	0.000	0.000
60	A	67	GLU	-1	-0.864	-0.938	21.781	-0.237	-0.237	0.000	0.000	0.000	0.000
61	A	68	SER	0	-0.051	-0.027	23.398	0.024	0.024	0.000	0.000	0.000	0.000
62	A	69	MET	0	0.013	0.006	23.253	0.005	0.005	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.053	-0.015	20.017	0.011	0.011	0.000	0.000	0.000	0.000
64	A	71	THR	0	-0.082	-0.027	24.219	0.017	0.017	0.000	0.000	0.000	0.000
65	A	72	THR	0	-0.067	-0.041	27.808	0.011	0.011	0.000	0.000	0.000	0.000
66	A	73	GLY	0	-0.005	0.008	26.536	0.012	0.012	0.000	0.000	0.000	0.000
67	A	74	GLU	-1	-0.939	-0.964	25.618	-0.148	-0.148	0.000	0.000	0.000	0.000
68	A	75	LEU	0	0.003	0.007	19.093	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	76	ASN	0	0.084	0.021	21.460	0.015	0.015	0.000	0.000	0.000	0.000
70	A	77	PRO	0	0.014	-0.021	19.036	0.001	0.001	0.000	0.000	0.000	0.000
71	A	78	ARG	1	0.942	0.958	18.810	0.066	0.066	0.000	0.000	0.000	0.000
72	A	79	HIS	0	-0.086	-0.030	20.146	0.030	0.030	0.000	0.000	0.000	0.000
73	A	80	ALA	0	-0.019	0.005	15.888	-0.019	-0.019	0.000	0.000	0.000	0.000
74	A	81	GLN	0	-0.042	-0.027	17.392	0.036	0.036	0.000	0.000	0.000	0.000
75	A	82	CYS	0	-0.031	0.008	16.294	-0.035	-0.035	0.000	0.000	0.000	0.000
76	A	83	VAL	0	0.006	0.020	17.955	0.029	0.029	0.000	0.000	0.000	0.000
77	A	84	THR	0	-0.002	-0.013	19.028	-0.031	-0.031	0.000	0.000	0.000	0.000
78	A	85	LEU	0	-0.014	0.007	20.449	0.024	0.024	0.000	0.000	0.000	0.000
79	A	86	TYR	0	0.024	-0.012	22.333	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	87	HIS	0	0.018	-0.004	24.328	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	88	ASN	0	-0.019	-0.011	25.129	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	89	GLY	0	0.003	0.008	26.596	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	90	PHE	0	0.011	0.017	20.441	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	91	THR	0	0.024	0.007	19.915	0.029	0.029	0.000	0.000	0.000	0.000
85	A	92	CYS	0	-0.040	-0.011	17.520	-0.055	-0.055	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.846	-0.892	15.203	-0.371	-0.371	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.033	-0.006	15.025	-0.077	-0.077	0.000	0.000	0.000	0.000
88	A	95	ASP	-1	-0.730	-0.882	13.566	-0.189	-0.189	0.000	0.000	0.000	0.000
89	A	96	THR	0	0.037	0.050	13.733	-0.063	-0.063	0.000	0.000	0.000	0.000
90	A	97	LEU	0	-0.090	-0.059	9.924	0.019	0.019	0.000	0.000	0.000	0.000
91	A	98	GLY	0	-0.021	-0.005	14.106	0.047	0.047	0.000	0.000	0.000	0.000
92	A	99	SER	0	-0.050	-0.034	12.946	0.026	0.026	0.000	0.000	0.000	0.000
93	A	100	CYS	0	-0.084	-0.032	14.998	0.016	0.016	0.000	0.000	0.000	0.000
94	A	101	GLY	0	0.073	0.032	16.071	0.019	0.019	0.000	0.000	0.000	0.000
95	A	102	TYR	0	-0.073	-0.018	10.633	-0.030	-0.030	0.000	0.000	0.000	0.000
96	A	103	VAL	0	0.049	0.032	13.433	0.048	0.048	0.000	0.000	0.000	0.000
97	A	104	TYR	0	-0.086	-0.042	7.816	-0.104	-0.104	0.000	0.000	0.000	0.000
98	A	105	ILE	0	0.049	0.017	11.228	0.095	0.095	0.000	0.000	0.000	0.000
99	A	106	ALA	0	-0.035	-0.022	11.142	-0.184	-0.184	0.000	0.000	0.000	0.000
100	A	107	VAL	0	0.016	0.016	13.013	0.091	0.091	0.000	0.000	0.000	0.000
101	A	108	TYR	0	-0.025	-0.043	15.506	-0.040	-0.040	0.000	0.000	0.000	0.000
102	A	109	PRO	0	0.003	0.021	17.892	0.028	0.028	0.000	0.000	0.000	0.000
103	A	110	THR	0	-0.022	-0.021	21.448	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:MET)