FMO DATABASE

FMODB ID: 5J3MZ

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-585101.997394
FMO2-HF: Nuclear repulsion	538227.712011
FMO2-HF: Total energy	-46874.285383
FMO2-MP2: Total energy	-47011.606919

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.
-3.075	0.551	1.337	-1.468	-3.495	0.003

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 : -0.028

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	-0.864	-0.910	3.323	-0.917	0.861	0.016	-0.721	-1.074	0.001
4	A	34	GLN	0	-0.045	-0.038	2.424	-1.860	-0.692	1.320	-0.592	-1.896	0.002
5	A	35	LEU	0	-0.003	0.021	3.909	-0.523	0.029	0.002	-0.149	-0.404	0.000
6	A	36	ASN	0	0.000	0.014	5.015	0.297	0.425	-0.001	-0.006	-0.121	0.000
7	A	37	LYS	1	0.929	0.937	8.420	-0.498	-0.498	0.000	0.000	0.000	0.000
8	A	38	SER	0	0.027	0.042	7.594	0.086	0.086	0.000	0.000	0.000	0.000
9	A	39	LEU	0	0.082	0.039	9.263	0.057	0.057	0.000	0.000	0.000	0.000
10	A	40	LYS	1	0.964	0.975	10.996	0.115	0.115	0.000	0.000	0.000	0.000
11	A	41	THR	0	-0.057	-0.054	12.398	0.059	0.059	0.000	0.000	0.000	0.000
12	A	42	ILE	0	0.005	0.005	12.548	0.028	0.028	0.000	0.000	0.000	0.000
13	A	43	ALA	0	-0.026	-0.006	14.748	0.027	0.027	0.000	0.000	0.000	0.000
14	A	44	SER	0	-0.004	-0.021	16.754	0.026	0.026	0.000	0.000	0.000	0.000
15	A	45	GLN	0	-0.015	0.007	17.390	0.002	0.002	0.000	0.000	0.000	0.000
16	A	46	LYS	1	0.841	0.901	18.937	0.171	0.171	0.000	0.000	0.000	0.000
17	A	47	ALA	0	0.027	0.008	20.851	0.013	0.013	0.000	0.000	0.000	0.000
18	A	48	ALA	0	-0.008	0.009	22.242	0.013	0.013	0.000	0.000	0.000	0.000
19	A	49	ILE	0	-0.030	-0.025	22.133	0.009	0.009	0.000	0.000	0.000	0.000
20	A	50	GLU	-1	-0.845	-0.910	24.734	-0.125	-0.125	0.000	0.000	0.000	0.000
21	A	51	ASN	0	0.001	0.015	26.601	0.007	0.007	0.000	0.000	0.000	0.000
22	A	52	TYR	0	0.064	0.025	28.710	0.006	0.006	0.000	0.000	0.000	0.000
23	A	53	ASN	0	-0.028	-0.025	27.700	0.009	0.009	0.000	0.000	0.000	0.000
24	A	54	GLN	0	0.023	0.023	30.707	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	55	LEU	0	0.010	0.019	32.584	0.005	0.005	0.000	0.000	0.000	0.000
26	A	56	LYS	1	0.869	0.911	33.956	0.052	0.052	0.000	0.000	0.000	0.000
27	A	57	GLU	-1	-0.955	-0.960	34.057	-0.073	-0.073	0.000	0.000	0.000	0.000
28	A	58	ASP	-1	-0.834	-0.919	36.470	-0.051	-0.051	0.000	0.000	0.000	0.000
29	A	59	TYR	0	-0.057	-0.029	38.435	0.004	0.004	0.000	0.000	0.000	0.000
30	A	60	ASN	0	-0.043	-0.046	38.564	0.006	0.006	0.000	0.000	0.000	0.000
31	A	61	THR	0	0.047	0.028	40.609	0.001	0.001	0.000	0.000	0.000	0.000
32	A	62	LEU	0	0.057	0.034	42.750	0.002	0.002	0.000	0.000	0.000	0.000
33	A	63	LYS	1	0.844	0.929	42.180	0.042	0.042	0.000	0.000	0.000	0.000
34	A	64	ARG	1	0.907	0.979	42.392	0.047	0.047	0.000	0.000	0.000	0.000
35	A	65	GLU	-1	-0.699	-0.844	47.401	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	66	LEU	0	-0.085	-0.035	48.819	0.002	0.002	0.000	0.000	0.000	0.000
37	A	67	SER	0	-0.051	-0.060	49.695	0.002	0.002	0.000	0.000	0.000	0.000
38	A	68	ASP	-1	-0.924	-0.952	50.219	-0.035	-0.035	0.000	0.000	0.000	0.000
39	A	69	ARG	1	0.730	0.839	51.462	0.029	0.029	0.000	0.000	0.000	0.000
40	A	70	ASP	-1	-0.833	-0.913	54.894	-0.021	-0.021	0.000	0.000	0.000	0.000
41	A	71	ASP	-1	-0.835	-0.909	56.360	-0.026	-0.026	0.000	0.000	0.000	0.000
42	A	72	GLU	-1	-0.924	-0.950	56.718	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	73	VAL	0	-0.013	-0.013	59.104	0.001	0.001	0.000	0.000	0.000	0.000
44	A	74	LYS	1	0.815	0.900	57.813	0.024	0.024	0.000	0.000	0.000	0.000
45	A	75	ARG	1	0.921	0.955	57.422	0.027	0.027	0.000	0.000	0.000	0.000
46	A	76	LEU	0	0.066	0.042	62.590	0.001	0.001	0.000	0.000	0.000	0.000
47	A	77	ARG	1	0.861	0.922	64.462	0.016	0.016	0.000	0.000	0.000	0.000
48	A	78	GLU	-1	-0.929	-0.960	65.166	-0.020	-0.020	0.000	0.000	0.000	0.000
49	A	79	ASP	-1	-0.899	-0.936	67.804	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	80	ILE	0	-0.098	-0.045	69.140	0.001	0.001	0.000	0.000	0.000	0.000
51	A	81	ALA	0	0.028	0.022	71.502	0.001	0.001	0.000	0.000	0.000	0.000
52	A	82	LYS	1	1.022	1.000	72.960	0.018	0.018	0.000	0.000	0.000	0.000
53	A	83	GLU	-1	-0.930	-0.979	73.887	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	84	ASN	0	-0.100	-0.062	74.402	0.001	0.001	0.000	0.000	0.000	0.000
55	A	85	GLU	-1	-0.975	-0.960	77.141	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	86	LEU	0	-0.040	-0.034	77.377	0.000	0.000	0.000	0.000	0.000	0.000
57	A	87	ARG	1	0.882	0.934	79.781	0.012	0.012	0.000	0.000	0.000	0.000
58	A	88	THR	0	0.002	-0.001	81.116	0.000	0.000	0.000	0.000	0.000	0.000
59	A	89	LYS	1	1.048	1.030	83.101	0.013	0.013	0.000	0.000	0.000	0.000
60	A	90	ALA	0	-0.096	-0.040	84.302	0.000	0.000	0.000	0.000	0.000	0.000
61	A	91	GLU	-1	-0.890	-0.942	85.105	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	92	GLU	-1	-0.896	-0.936	87.019	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	93	GLU	-1	-0.985	-0.999	89.449	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	94	ALA	0	-0.007	-0.004	89.913	0.000	0.000	0.000	0.000	0.000	0.000
65	A	95	ASP	-1	-0.838	-0.917	91.905	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	96	LYS	1	0.834	0.917	93.415	0.010	0.010	0.000	0.000	0.000	0.000
67	A	97	LEU	0	0.001	0.003	94.824	0.000	0.000	0.000	0.000	0.000	0.000
68	A	98	ASN	0	0.030	-0.006	94.724	0.000	0.000	0.000	0.000	0.000	0.000
69	A	99	LYS	1	0.920	0.949	96.977	0.008	0.008	0.000	0.000	0.000	0.000
70	A	100	GLU	-1	-0.926	-0.937	99.644	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	101	VAL	0	-0.086	-0.044	99.983	0.000	0.000	0.000	0.000	0.000	0.000
72	A	102	GLU	-1	-0.982	-0.977	101.907	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	103	ASP	-1	-0.896	-0.954	103.946	-0.007	-0.007	0.000	0.000	0.000	0.000
74	A	104	LEU	0	-0.044	-0.015	105.097	0.000	0.000	0.000	0.000	0.000	0.000
75	A	105	THR	0	-0.047	-0.053	105.353	0.000	0.000	0.000	0.000	0.000	0.000
76	A	106	ALA	0	-0.003	-0.011	108.020	0.000	0.000	0.000	0.000	0.000	0.000
77	A	107	SER	0	0.020	0.025	109.914	0.000	0.000	0.000	0.000	0.000	0.000
78	A	108	LEU	0	-0.036	-0.010	111.152	0.000	0.000	0.000	0.000	0.000	0.000
79	A	109	PHE	0	-0.042	-0.039	112.271	0.000	0.000	0.000	0.000	0.000	0.000
80	A	110	ASP	-1	-0.816	-0.896	114.141	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	111	GLU	-1	-0.911	-0.940	115.970	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	112	ALA	0	-0.064	-0.035	116.915	0.000	0.000	0.000	0.000	0.000	0.000
83	A	113	ASN	0	-0.072	-0.044	116.813	0.000	0.000	0.000	0.000	0.000	0.000
84	A	114	ASN	0	-0.016	-0.029	118.971	0.000	0.000	0.000	0.000	0.000	0.000
85	A	115	LEU	0	-0.008	0.014	121.536	0.000	0.000	0.000	0.000	0.000	0.000
86	A	116	VAL	0	-0.038	-0.032	122.379	0.000	0.000	0.000	0.000	0.000	0.000
87	A	117	ALA	0	-0.021	-0.006	124.028	0.000	0.000	0.000	0.000	0.000	0.000
88	A	118	ASP	-1	-0.855	-0.932	125.714	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	119	ALA	0	-0.009	0.003	127.056	0.000	0.000	0.000	0.000	0.000	0.000
90	A	120	ARG	1	0.877	0.927	128.057	0.005	0.005	0.000	0.000	0.000	0.000
91	A	121	MET	0	-0.006	0.009	130.672	0.000	0.000	0.000	0.000	0.000	0.000
92	A	122	GLU	-1	-0.915	-0.962	131.096	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	123	LYS	1	0.774	0.895	133.064	0.004	0.004	0.000	0.000	0.000	0.000
94	A	124	TYR	0	0.023	-0.034	133.079	0.000	0.000	0.000	0.000	0.000	0.000
95	A	125	ALA	0	-0.001	0.020	136.730	0.000	0.000	0.000	0.000	0.000	0.000
96	A	126	ILE	0	0.010	-0.001	137.120	0.000	0.000	0.000	0.000	0.000	0.000
97	A	127	GLU	-1	-0.857	-0.898	138.741	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	128	ILE	0	-0.004	-0.017	140.445	0.000	0.000	0.000	0.000	0.000	0.000
99	A	129	LEU	0	-0.025	-0.002	141.567	0.000	0.000	0.000	0.000	0.000	0.000
100	A	130	ASN	0	0.047	0.005	141.292	0.000	0.000	0.000	0.000	0.000	0.000
101	A	131	LYS	1	0.942	0.996	143.869	0.004	0.004	0.000	0.000	0.000	0.000
102	A	132	ARG	1	0.992	1.002	146.568	0.004	0.004	0.000	0.000	0.000	0.000
103	A	133	LEU	0	0.002	-0.004	146.081	0.000	0.000	0.000	0.000	0.000	0.000
104	A	134	THR	0	-0.038	-0.026	147.146	0.000	0.000	0.000	0.000	0.000	0.000
105	A	135	GLU	-1	-0.968	-0.993	149.960	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	136	GLN	0	-0.034	-0.033	152.413	0.000	0.000	0.000	0.000	0.000	0.000
107	A	137	LEU	0	-0.056	-0.027	151.212	0.000	0.000	0.000	0.000	0.000	0.000
108	A	138	ARG	1	0.979	1.003	153.065	0.004	0.004	0.000	0.000	0.000	0.000
109	A	139	GLU	-1	-0.903	-0.934	156.307	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	140	LYS	1	0.903	0.955	157.001	0.004	0.004	0.000	0.000	0.000	0.000
111	A	141	ASP	-1	-0.875	-0.945	157.813	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	142	MET	0	-0.081	-0.040	160.090	0.000	0.000	0.000	0.000	0.000	0.000
113	A	143	LEU	0	-0.026	-0.005	162.589	0.000	0.000	0.000	0.000	0.000	0.000
114	A	144	LEU	0	-0.075	-0.022	162.222	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)