FMO DATABASE

FMODB ID: L7V69

Calculation Name: 2E43-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2E43

Chain ID: A

ChEMBL ID:

UniProt ID: P17676

Base Structure: X-ray

Registration Date: 2025-07-08

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-287410.904429
FMO2-HF: Nuclear repulsion	261270.175459
FMO2-HF: Total energy	-26140.728971
FMO2-MP2: Total energy	-26217.548032

3D Structure Molmil

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:271:SER)

Summations of interaction energy for fragment #1(A:271:SER)

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.
8.065	9.189	0.037	0.613	-1.772	0.004

Interaction energy analysis for fragmet #1(A:271:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.173 / q_NPA : 0.087

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].
4	A	272	ASP	-1	-0.895	-0.788	3.894	-1.758	-1.043	0.009	-0.298	-0.427	-0.001
5	A	273	GLU	0	0.112	-0.088	3.573	-0.569	1.007	0.004	-0.851	-0.729	0.004
6	A	273	GLU	-1	-0.861	-0.756	3.969	-3.894	-3.759	0.001	-0.052	-0.084	0.000
7	A	274	TYR	0	0.135	-0.090	2.907	2.901	2.229	-0.007	0.804	-0.124	0.000
8	A	274	TYR	0	-0.086	0.095	3.130	1.205	0.261	0.031	1.159	-0.244	0.001
9	A	275	LYS	0	0.097	-0.115	4.309	1.431	1.745	-0.001	-0.149	-0.164	0.000
10	A	275	LYS	1	0.775	1.042	4.866	1.800	1.800	0.000	0.000	0.000	0.000
11	A	276	ILE	0	0.036	-0.118	6.146	0.796	0.796	0.000	0.000	0.000	0.000
12	A	276	ILE	0	-0.044	0.132	7.539	0.085	0.085	0.000	0.000	0.000	0.000
13	A	277	ARG	0	0.087	-0.100	7.485	0.552	0.552	0.000	0.000	0.000	0.000
14	A	277	ARG	1	0.767	0.990	5.701	2.151	2.151	0.000	0.000	0.000	0.000
15	A	278	ARG	0	0.013	-0.144	8.397	0.390	0.390	0.000	0.000	0.000	0.000
16	A	278	ARG	1	0.823	1.049	8.236	0.933	0.933	0.000	0.000	0.000	0.000
17	A	279	GLU	0	0.125	-0.096	10.243	0.278	0.278	0.000	0.000	0.000	0.000
18	A	279	GLU	-1	-0.983	-0.808	11.006	-1.070	-1.070	0.000	0.000	0.000	0.000
19	A	280	ARG	0	0.055	-0.142	12.127	0.190	0.190	0.000	0.000	0.000	0.000
20	A	280	ARG	1	0.896	1.103	12.436	0.694	0.694	0.000	0.000	0.000	0.000
21	A	281	ASN	0	0.078	-0.067	12.969	0.143	0.143	0.000	0.000	0.000	0.000
22	A	281	ASN	0	-0.033	0.105	13.138	0.012	0.012	0.000	0.000	0.000	0.000
23	A	282	ASN	0	0.065	-0.091	14.265	0.104	0.104	0.000	0.000	0.000	0.000
24	A	282	ASN	0	-0.046	0.091	13.377	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	283	ILE	0	0.084	-0.084	16.056	0.086	0.086	0.000	0.000	0.000	0.000
26	A	283	ILE	0	-0.085	0.105	16.261	0.009	0.009	0.000	0.000	0.000	0.000
27	A	284	ALA	0	0.080	-0.109	17.600	0.071	0.071	0.000	0.000	0.000	0.000
28	A	284	ALA	0	-0.069	0.109	17.806	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	285	VAL	0	0.099	-0.112	18.520	0.053	0.053	0.000	0.000	0.000	0.000
30	A	285	VAL	0	-0.102	0.112	17.920	0.005	0.005	0.000	0.000	0.000	0.000
31	A	286	ARG	0	0.093	-0.097	20.216	0.046	0.046	0.000	0.000	0.000	0.000
32	A	286	ARG	1	0.861	1.068	20.857	0.307	0.307	0.000	0.000	0.000	0.000
33	A	287	LYS	0	0.094	-0.091	21.986	0.036	0.036	0.000	0.000	0.000	0.000
34	A	287	LYS	1	0.870	1.069	22.541	0.312	0.312	0.000	0.000	0.000	0.000
35	A	288	SER	0	0.028	-0.076	23.215	0.026	0.026	0.000	0.000	0.000	0.000
36	A	288	SER	0	-0.048	0.064	23.498	0.007	0.007	0.000	0.000	0.000	0.000
37	A	289	ARG	0	0.071	-0.072	24.467	0.023	0.023	0.000	0.000	0.000	0.000
38	A	289	ARG	1	0.886	1.060	21.174	0.261	0.261	0.000	0.000	0.000	0.000
39	A	290	ASP	0	0.103	-0.105	26.134	0.022	0.022	0.000	0.000	0.000	0.000
40	A	290	ASP	-1	-0.909	-0.794	25.880	-0.237	-0.237	0.000	0.000	0.000	0.000
41	A	291	LYS	0	0.137	-0.062	27.815	0.018	0.018	0.000	0.000	0.000	0.000
42	A	291	LYS	1	0.847	1.058	28.265	0.200	0.200	0.000	0.000	0.000	0.000
43	A	292	ALA	0	0.076	-0.110	29.008	0.014	0.014	0.000	0.000	0.000	0.000
44	A	292	ALA	0	-0.093	0.093	29.218	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	293	LYS	0	0.033	-0.088	30.535	0.011	0.011	0.000	0.000	0.000	0.000
46	A	293	LYS	1	0.837	1.003	26.927	0.192	0.192	0.000	0.000	0.000	0.000
47	A	294	MET	0	0.126	-0.073	32.340	0.012	0.012	0.000	0.000	0.000	0.000
48	A	294	MET	0	-0.096	0.101	32.462	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	295	ARG	0	0.082	-0.051	33.724	0.008	0.008	0.000	0.000	0.000	0.000
50	A	295	ARG	1	0.882	1.035	29.610	0.166	0.166	0.000	0.000	0.000	0.000
51	A	296	ASN	0	0.141	-0.023	35.123	0.007	0.007	0.000	0.000	0.000	0.000
52	A	296	ASN	0	-0.128	0.051	34.145	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	297	LEU	0	0.143	-0.072	36.638	0.008	0.008	0.000	0.000	0.000	0.000
54	A	297	LEU	0	-0.116	0.081	35.407	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	298	GLU	0	0.145	-0.067	38.143	0.007	0.007	0.000	0.000	0.000	0.000
56	A	298	GLU	-1	-0.963	-0.842	38.456	-0.103	-0.103	0.000	0.000	0.000	0.000
57	A	299	THR	0	-0.025	-0.096	39.742	0.004	0.004	0.000	0.000	0.000	0.000
58	A	299	THR	0	-0.061	0.050	39.231	0.000	0.000	0.000	0.000	0.000	0.000
59	A	300	GLN	0	0.077	-0.072	41.146	0.005	0.005	0.000	0.000	0.000	0.000
60	A	300	GLN	0	-0.077	0.058	39.052	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	301	HIS	0	0.052	-0.099	42.615	0.006	0.006	0.000	0.000	0.000	0.000
62	A	301	HIS	0	-0.078	0.099	40.366	0.003	0.003	0.000	0.000	0.000	0.000
63	A	302	LYS	0	0.201	-0.054	44.457	0.004	0.004	0.000	0.000	0.000	0.000
64	A	302	LYS	1	0.788	1.012	42.066	0.095	0.095	0.000	0.000	0.000	0.000
65	A	303	VAL	0	0.089	-0.074	46.099	0.003	0.003	0.000	0.000	0.000	0.000
66	A	303	VAL	0	-0.096	0.098	45.769	0.000	0.000	0.000	0.000	0.000	0.000
67	A	304	LEU	0	0.064	-0.079	47.443	0.004	0.004	0.000	0.000	0.000	0.000
68	A	304	LEU	0	-0.086	0.084	45.971	0.000	0.000	0.000	0.000	0.000	0.000
69	A	305	GLU	0	0.133	-0.098	48.688	0.004	0.004	0.000	0.000	0.000	0.000
70	A	305	GLU	-1	-1.044	-0.858	48.304	-0.077	-0.077	0.000	0.000	0.000	0.000
71	A	306	LEU	0	0.046	-0.111	50.268	0.003	0.003	0.000	0.000	0.000	0.000
72	A	306	LEU	0	-0.053	0.104	49.430	0.000	0.000	0.000	0.000	0.000	0.000
73	A	307	THR	0	0.034	-0.075	51.907	0.003	0.003	0.000	0.000	0.000	0.000
74	A	307	THR	0	-0.073	0.042	51.579	0.001	0.001	0.000	0.000	0.000	0.000
75	A	308	ALA	0	0.111	-0.095	53.428	0.003	0.003	0.000	0.000	0.000	0.000
76	A	308	ALA	0	-0.097	0.108	53.872	0.000	0.000	0.000	0.000	0.000	0.000
77	A	309	GLU	0	0.074	-0.108	54.608	0.003	0.003	0.000	0.000	0.000	0.000
78	A	309	GLU	-1	-0.883	-0.754	54.763	-0.055	-0.055	0.000	0.000	0.000	0.000
79	A	310	ASN	0	0.064	-0.086	56.136	0.002	0.002	0.000	0.000	0.000	0.000
80	A	310	ASN	0	-0.140	0.044	54.958	0.001	0.001	0.000	0.000	0.000	0.000
81	A	311	GLU	0	0.156	-0.070	58.075	0.002	0.002	0.000	0.000	0.000	0.000
82	A	311	GLU	-1	-0.910	-0.803	58.873	-0.042	-0.042	0.000	0.000	0.000	0.000
83	A	312	ARG	0	0.078	-0.108	59.315	0.002	0.002	0.000	0.000	0.000	0.000
84	A	312	ARG	1	0.728	0.965	58.461	0.052	0.052	0.000	0.000	0.000	0.000
85	A	313	LEU	0	0.014	-0.130	60.397	0.002	0.002	0.000	0.000	0.000	0.000
86	A	313	LEU	0	-0.090	0.104	58.567	0.000	0.000	0.000	0.000	0.000	0.000
87	A	314	GLN	0	0.154	-0.087	62.029	0.002	0.002	0.000	0.000	0.000	0.000
88	A	314	GLN	0	-0.143	0.082	62.696	0.000	0.000	0.000	0.000	0.000	0.000
89	A	315	LYS	0	0.052	-0.128	63.912	0.002	0.002	0.000	0.000	0.000	0.000
90	A	315	LYS	1	0.727	1.005	64.203	0.040	0.040	0.000	0.000	0.000	0.000
91	A	316	LYS	0	0.106	-0.075	65.108	0.002	0.002	0.000	0.000	0.000	0.000
92	A	316	LYS	1	0.885	1.065	65.289	0.042	0.042	0.000	0.000	0.000	0.000
93	A	317	VAL	0	0.039	-0.122	66.299	0.001	0.001	0.000	0.000	0.000	0.000
94	A	317	VAL	0	-0.056	0.120	65.664	0.000	0.000	0.000	0.000	0.000	0.000
95	A	318	GLU	0	0.083	-0.130	68.101	0.001	0.001	0.000	0.000	0.000	0.000
96	A	318	GLU	-1	-0.804	-0.753	67.283	-0.036	-0.036	0.000	0.000	0.000	0.000
97	A	319	GLN	0	0.055	-0.086	69.645	0.002	0.002	0.000	0.000	0.000	0.000
98	A	319	GLN	0	-0.089	0.102	69.997	0.000	0.000	0.000	0.000	0.000	0.000
99	A	320	LEU	0	0.098	-0.100	70.802	0.001	0.001	0.000	0.000	0.000	0.000
100	A	320	LEU	0	-0.091	0.098	69.125	0.000	0.000	0.000	0.000	0.000	0.000
101	A	321	SER	0	0.034	-0.098	72.335	0.001	0.001	0.000	0.000	0.000	0.000
102	A	321	SER	0	-0.064	0.061	71.795	0.000	0.000	0.000	0.000	0.000	0.000
103	A	322	ARG	0	0.050	-0.084	74.114	0.001	0.001	0.000	0.000	0.000	0.000
104	A	322	ARG	1	0.769	1.005	69.922	0.034	0.034	0.000	0.000	0.000	0.000
105	A	323	GLU	0	0.105	-0.102	75.431	0.001	0.001	0.000	0.000	0.000	0.000
106	A	323	GLU	-1	-0.928	-0.786	73.965	-0.034	-0.034	0.000	0.000	0.000	0.000
107	A	324	LEU	0	0.071	-0.106	76.539	0.001	0.001	0.000	0.000	0.000	0.000
108	A	324	LEU	0	-0.083	0.093	74.960	0.000	0.000	0.000	0.000	0.000	0.000
109	A	325	SER	0	0.073	-0.077	78.225	0.001	0.001	0.000	0.000	0.000	0.000
110	A	325	SER	0	-0.039	0.076	78.810	0.000	0.000	0.000	0.000	0.000	0.000
111	A	326	THR	0	-0.016	-0.106	79.930	0.001	0.001	0.000	0.000	0.000	0.000
112	A	326	THR	0	-0.068	0.066	79.636	0.000	0.000	0.000	0.000	0.000	0.000
113	A	327	LEU	0	0.102	-0.084	81.142	0.001	0.001	0.000	0.000	0.000	0.000
114	A	327	LEU	0	-0.086	0.097	79.444	0.000	0.000	0.000	0.000	0.000	0.000
115	A	328	ARG	0	0.084	-0.073	82.406	0.001	0.001	0.000	0.000	0.000	0.000
116	A	328	ARG	1	0.862	1.055	78.139	0.028	0.028	0.000	0.000	0.000	0.000
117	A	329	ASN	0	0.078	-0.063	84.242	0.001	0.001	0.000	0.000	0.000	0.000
118	A	329	ASN	0	-0.098	0.071	83.582	0.001	0.001	0.000	0.000	0.000	0.000
119	A	330	LEU	0	0.049	-0.122	86.257	0.001	0.001	0.000	0.000	0.000	0.000
120	A	330	LEU	0	-0.041	0.121	85.382	0.000	0.000	0.000	0.000	0.000	0.000
121	A	331	PHE	0	0.026	-0.099	87.973	0.000	0.000	0.000	0.000	0.000	0.000
122	A	331	PHE	0	-0.046	0.103	85.095	0.000	0.000	0.000	0.000	0.000	0.000
123	A	332	LYS	0	-0.090	-0.118	89.861	0.001	0.001	0.000	0.000	0.000	0.000
124	A	332	LYS	1	0.869	0.918	88.194	0.022	0.022	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:271:SER)