FMO DATABASE

FMODB ID: 4L42N

Calculation Name: 1CEI-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1CEI

Chain ID: A

ChEMBL ID:

UniProt ID: Q03708

Base Structure: X-ray

Registration Date: 2025-07-11

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	161
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-579529.123433
FMO2-HF: Nuclear repulsion	546332.75986
FMO2-HF: Total energy	-33196.363573
FMO2-MP2: Total energy	-33295.28043

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:3:LEU)

Summations of interaction energy for fragment #1(A:3: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.
-9.056	-5.356	2.869	-3.083	-3.487	0.005

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.104 / q_NPA : -0.007

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	4	LYS	1	0.749	0.983	3.237	-7.002	-5.878	0.117	-0.509	-0.733	0.005
5	A	5	ASN	0	0.138	-0.031	3.890	-1.358	0.256	-0.013	-1.016	-0.586	0.005
6	A	5	ASN	0	-0.122	0.047	8.140	-0.198	-0.198	0.000	0.000	0.000	0.000
7	A	6	SER	0	0.046	-0.091	6.929	-0.173	-0.173	0.000	0.000	0.000	0.000
8	A	6	SER	0	-0.082	0.026	9.615	0.010	0.010	0.000	0.000	0.000	0.000
9	A	7	ILE	0	0.134	-0.100	7.574	0.551	0.551	0.000	0.000	0.000	0.000
10	A	7	ILE	0	-0.075	0.143	9.122	0.003	0.003	0.000	0.000	0.000	0.000
11	A	8	SER	0	0.035	-0.094	9.416	0.332	0.332	0.000	0.000	0.000	0.000
12	A	8	SER	0	-0.044	0.069	12.384	-0.094	-0.094	0.000	0.000	0.000	0.000
13	A	9	ASP	0	0.011	-0.112	7.992	-0.109	-0.109	0.000	0.000	0.000	0.000
14	A	9	ASP	-1	-0.881	-0.791	7.161	0.561	0.561	0.000	0.000	0.000	0.000
15	A	10	TYR	0	-0.015	-0.160	7.997	0.457	0.457	0.000	0.000	0.000	0.000
16	A	10	TYR	0	0.006	0.147	2.312	-1.087	-1.075	2.618	-1.320	-1.309	-0.003
17	A	11	THR	0	0.041	-0.067	8.770	-0.447	-0.447	0.000	0.000	0.000	0.000
18	A	11	THR	0	-0.074	0.030	11.547	0.002	0.002	0.000	0.000	0.000	0.000
19	A	12	GLU	0	0.153	-0.072	10.771	0.427	0.427	0.000	0.000	0.000	0.000
20	A	12	GLU	-1	-0.879	-0.765	14.369	0.766	0.766	0.000	0.000	0.000	0.000
21	A	13	ALA	0	0.110	-0.085	12.496	0.055	0.055	0.000	0.000	0.000	0.000
22	A	13	ALA	0	-0.092	0.095	13.152	-0.042	-0.042	0.000	0.000	0.000	0.000
23	A	14	GLU	0	0.092	-0.093	8.543	-0.163	-0.163	0.000	0.000	0.000	0.000
24	A	14	GLU	-1	-0.820	-0.758	7.459	2.810	2.810	0.000	0.000	0.000	0.000
25	A	15	PHE	0	0.089	-0.063	7.553	1.254	1.254	0.000	0.000	0.000	0.000
26	A	15	PHE	0	-0.057	0.100	7.592	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	16	VAL	0	0.082	-0.119	8.817	0.072	0.072	0.000	0.000	0.000	0.000
28	A	16	VAL	0	-0.065	0.114	12.719	-0.041	-0.041	0.000	0.000	0.000	0.000
29	A	17	GLN	0	0.044	-0.095	8.742	-0.409	-0.409	0.000	0.000	0.000	0.000
30	A	17	GLN	0	-0.090	0.065	8.130	0.285	0.285	0.000	0.000	0.000	0.000
31	A	18	LEU	0	0.128	-0.068	5.882	-0.357	-0.357	0.000	0.000	0.000	0.000
32	A	18	LEU	0	-0.101	0.094	3.612	0.344	0.589	0.006	-0.079	-0.172	0.000
33	A	19	LEU	0	0.073	-0.100	6.608	-0.531	-0.531	0.000	0.000	0.000	0.000
34	A	19	LEU	0	-0.094	0.110	9.130	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	20	LYS	0	0.074	-0.109	10.146	-0.300	-0.300	0.000	0.000	0.000	0.000
36	A	20	LYS	1	0.705	0.951	10.729	-0.797	-0.797	0.000	0.000	0.000	0.000
37	A	21	GLU	0	0.137	-0.056	7.290	-0.330	-0.330	0.000	0.000	0.000	0.000
38	A	21	GLU	-1	-0.978	-0.827	5.917	0.855	0.855	0.000	0.000	0.000	0.000
39	A	22	ILE	0	0.109	-0.079	8.805	-0.351	-0.351	0.000	0.000	0.000	0.000
40	A	22	ILE	0	-0.077	0.090	8.075	0.006	0.006	0.000	0.000	0.000	0.000
41	A	23	GLU	0	0.081	-0.096	10.240	-0.200	-0.200	0.000	0.000	0.000	0.000
42	A	23	GLU	-1	-0.875	-0.788	13.478	0.716	0.716	0.000	0.000	0.000	0.000
43	A	24	LYS	0	0.109	-0.074	12.255	-0.098	-0.098	0.000	0.000	0.000	0.000
44	A	24	LYS	1	0.650	0.947	9.758	-0.080	-0.080	0.000	0.000	0.000	0.000
45	A	25	GLU	0	0.055	-0.118	11.573	-0.031	-0.031	0.000	0.000	0.000	0.000
46	A	25	GLU	-1	-0.901	-0.817	9.717	-0.328	-0.328	0.000	0.000	0.000	0.000
47	A	26	ASN	0	0.085	-0.053	12.750	-0.094	-0.094	0.000	0.000	0.000	0.000
48	A	26	ASN	0	-0.141	0.045	13.690	-0.028	-0.028	0.000	0.000	0.000	0.000
49	A	27	VAL	0	0.020	-0.083	15.717	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	27	VAL	0	-0.126	0.058	16.769	0.008	0.008	0.000	0.000	0.000	0.000
51	A	28	ALA	0	0.083	-0.118	15.478	0.034	0.034	0.000	0.000	0.000	0.000
52	A	28	ALA	0	-0.031	0.131	14.563	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	29	ALA	0	0.060	-0.101	16.701	0.017	0.017	0.000	0.000	0.000	0.000
54	A	29	ALA	0	-0.130	0.061	19.246	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	30	THR	0	-0.083	-0.116	17.534	0.032	0.032	0.000	0.000	0.000	0.000
56	A	30	THR	0	-0.074	0.007	17.320	0.012	0.012	0.000	0.000	0.000	0.000
57	A	31	ASP	0	0.111	-0.086	15.601	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	31	ASP	-1	-0.915	-0.811	16.022	-0.257	-0.257	0.000	0.000	0.000	0.000
59	A	32	ASP	0	0.051	-0.093	13.752	-0.051	-0.051	0.000	0.000	0.000	0.000
60	A	32	ASP	-1	-0.922	-0.837	13.988	-0.563	-0.563	0.000	0.000	0.000	0.000
61	A	33	VAL	0	0.034	-0.123	9.995	-0.244	-0.244	0.000	0.000	0.000	0.000
62	A	33	VAL	0	-0.093	0.105	8.572	-0.043	-0.043	0.000	0.000	0.000	0.000
63	A	34	LEU	0	0.141	-0.089	9.392	-0.205	-0.205	0.000	0.000	0.000	0.000
64	A	34	LEU	0	-0.089	0.122	11.946	0.017	0.017	0.000	0.000	0.000	0.000
65	A	35	ASP	0	0.092	-0.113	10.905	0.052	0.052	0.000	0.000	0.000	0.000
66	A	35	ASP	-1	-0.987	-0.833	12.844	-0.527	-0.527	0.000	0.000	0.000	0.000
67	A	36	VAL	0	0.099	-0.099	8.180	0.217	0.217	0.000	0.000	0.000	0.000
68	A	36	VAL	0	-0.095	0.095	7.150	-0.143	-0.143	0.000	0.000	0.000	0.000
69	A	37	LEU	0	0.012	-0.130	6.306	-0.722	-0.722	0.000	0.000	0.000	0.000
70	A	37	LEU	0	-0.091	0.102	5.258	-0.051	-0.051	0.000	0.000	0.000	0.000
71	A	38	LEU	0	0.079	-0.115	7.347	0.459	0.459	0.000	0.000	0.000	0.000
72	A	38	LEU	0	-0.066	0.125	10.959	0.033	0.033	0.000	0.000	0.000	0.000
73	A	39	GLU	0	0.118	-0.139	9.937	0.293	0.293	0.000	0.000	0.000	0.000
74	A	39	GLU	-1	-0.999	-0.844	9.085	-1.338	-1.338	0.000	0.000	0.000	0.000
75	A	40	HIS	0	0.017	-0.091	5.284	0.182	0.188	-0.002	-0.001	-0.003	0.000
76	A	40	HIS	0	-0.047	0.105	3.384	-2.814	-2.115	0.143	-0.158	-0.684	-0.002
77	A	41	PHE	0	0.087	-0.092	6.632	0.414	0.414	0.000	0.000	0.000	0.000
78	A	41	PHE	0	-0.072	0.099	8.150	0.081	0.081	0.000	0.000	0.000	0.000
79	A	42	VAL	0	0.098	-0.092	8.172	0.180	0.180	0.000	0.000	0.000	0.000
80	A	42	VAL	0	-0.061	0.119	11.865	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	43	LYS	0	0.079	-0.097	9.425	0.150	0.150	0.000	0.000	0.000	0.000
82	A	43	LYS	1	0.747	1.016	5.729	2.512	2.512	0.000	0.000	0.000	0.000
83	A	44	ILE	0	0.008	-0.116	7.708	-0.142	-0.142	0.000	0.000	0.000	0.000
84	A	44	ILE	0	-0.132	0.081	5.079	0.125	0.125	0.000	0.000	0.000	0.000
85	A	45	THR	0	0.048	-0.114	9.057	0.147	0.147	0.000	0.000	0.000	0.000
86	A	45	THR	0	-0.064	0.074	10.073	-0.031	-0.031	0.000	0.000	0.000	0.000
87	A	46	GLU	0	0.007	-0.074	11.721	0.020	0.020	0.000	0.000	0.000	0.000
88	A	46	GLU	-1	-0.929	-0.826	13.148	0.115	0.115	0.000	0.000	0.000	0.000
89	A	47	HIS	0	0.142	-0.089	14.617	-0.020	-0.020	0.000	0.000	0.000	0.000
90	A	47	HIS	0	-0.056	0.114	15.573	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	48	PRO	0	-0.062	-0.132	16.644	-0.036	-0.036	0.000	0.000	0.000	0.000
92	A	49	ASP	0	0.137	0.005	19.205	-0.048	-0.048	0.000	0.000	0.000	0.000
93	A	49	ASP	-1	-0.967	-0.822	18.804	0.169	0.169	0.000	0.000	0.000	0.000
94	A	50	GLY	0	-0.034	-0.122	15.063	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	51	THR	0	0.032	-0.031	14.408	0.101	0.101	0.000	0.000	0.000	0.000
96	A	51	THR	0	-0.013	0.094	13.712	-0.029	-0.029	0.000	0.000	0.000	0.000
97	A	52	ASP	0	0.099	-0.086	15.396	0.055	0.055	0.000	0.000	0.000	0.000
98	A	52	ASP	-1	-0.956	-0.816	19.652	0.042	0.042	0.000	0.000	0.000	0.000
99	A	53	LEU	0	0.030	-0.111	16.230	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	53	LEU	0	-0.059	0.086	14.460	0.025	0.025	0.000	0.000	0.000	0.000
101	A	54	ILE	0	0.110	-0.064	15.383	0.055	0.055	0.000	0.000	0.000	0.000
102	A	54	ILE	0	-0.101	0.071	11.978	0.021	0.021	0.000	0.000	0.000	0.000
103	A	55	TYR	0	0.022	-0.087	16.678	0.012	0.012	0.000	0.000	0.000	0.000
104	A	55	TYR	0	-0.122	0.038	15.299	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	56	TYR	0	-0.001	-0.110	19.752	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	56	TYR	0	-0.123	0.071	22.126	-0.006	-0.006	0.000	0.000	0.000	0.000
107	A	57	PRO	0	0.074	-0.072	20.763	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	58	SER	0	0.165	0.056	22.096	-0.027	-0.027	0.000	0.000	0.000	0.000
109	A	58	SER	0	-0.069	0.056	23.759	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	59	ASP	0	0.052	-0.114	24.669	0.028	0.028	0.000	0.000	0.000	0.000
111	A	59	ASP	-1	-0.960	-0.845	28.706	0.140	0.140	0.000	0.000	0.000	0.000
112	A	60	ASN	0	-0.047	-0.085	27.246	0.001	0.001	0.000	0.000	0.000	0.000
113	A	60	ASN	0	-0.161	0.017	27.262	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	61	ARG	0	0.070	-0.134	23.475	0.003	0.003	0.000	0.000	0.000	0.000
115	A	61	ARG	1	0.648	0.950	18.583	-0.379	-0.379	0.000	0.000	0.000	0.000
116	A	62	ASP	0	0.077	-0.073	23.642	-0.025	-0.025	0.000	0.000	0.000	0.000
117	A	62	ASP	-1	-0.942	-0.815	22.346	0.422	0.422	0.000	0.000	0.000	0.000
118	A	63	ASP	0	0.019	-0.135	21.176	0.040	0.040	0.000	0.000	0.000	0.000
119	A	63	ASP	-1	-0.859	-0.764	20.686	0.324	0.324	0.000	0.000	0.000	0.000
120	A	64	SER	0	-0.007	-0.121	19.045	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	64	SER	0	-0.023	0.059	19.432	0.031	0.031	0.000	0.000	0.000	0.000
122	A	65	PRO	0	0.024	-0.095	13.736	0.024	0.024	0.000	0.000	0.000	0.000
123	A	66	GLU	0	0.071	-0.010	15.162	0.104	0.104	0.000	0.000	0.000	0.000
124	A	66	GLU	-1	-1.004	-0.850	17.771	0.613	0.613	0.000	0.000	0.000	0.000
125	A	67	GLY	0	0.010	-0.109	17.383	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	68	ILE	0	0.128	0.027	15.528	-0.069	-0.069	0.000	0.000	0.000	0.000
127	A	68	ILE	0	-0.064	0.106	13.773	0.033	0.033	0.000	0.000	0.000	0.000
128	A	69	VAL	0	0.047	-0.127	14.334	-0.034	-0.034	0.000	0.000	0.000	0.000
129	A	69	VAL	0	-0.132	0.101	12.758	0.030	0.030	0.000	0.000	0.000	0.000
130	A	70	LYS	0	0.113	-0.095	15.171	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	70	LYS	1	0.771	0.998	19.994	-0.368	-0.368	0.000	0.000	0.000	0.000
132	A	71	GLU	0	0.092	-0.118	18.717	-0.024	-0.024	0.000	0.000	0.000	0.000
133	A	71	GLU	-1	-0.921	-0.782	18.328	0.329	0.329	0.000	0.000	0.000	0.000
134	A	72	ILE	0	0.054	-0.096	14.650	-0.097	-0.097	0.000	0.000	0.000	0.000
135	A	72	ILE	0	-0.069	0.092	12.166	0.021	0.021	0.000	0.000	0.000	0.000
136	A	73	LYS	0	0.098	-0.079	16.152	-0.045	-0.045	0.000	0.000	0.000	0.000
137	A	73	LYS	1	0.703	0.965	16.734	-0.661	-0.661	0.000	0.000	0.000	0.000
138	A	74	GLU	0	0.067	-0.132	17.506	-0.030	-0.030	0.000	0.000	0.000	0.000
139	A	74	GLU	-1	-0.934	-0.780	21.357	0.356	0.356	0.000	0.000	0.000	0.000
140	A	75	TRP	0	0.059	-0.111	19.432	-0.041	-0.041	0.000	0.000	0.000	0.000
141	A	75	TRP	0	-0.052	0.113	17.318	-0.010	-0.010	0.000	0.000	0.000	0.000
142	A	76	ARG	0	0.082	-0.098	17.180	-0.068	-0.068	0.000	0.000	0.000	0.000
143	A	76	ARG	1	0.669	0.942	14.017	-0.364	-0.364	0.000	0.000	0.000	0.000
144	A	77	ALA	0	0.099	-0.086	18.598	-0.037	-0.037	0.000	0.000	0.000	0.000
145	A	77	ALA	0	-0.094	0.088	20.919	0.003	0.003	0.000	0.000	0.000	0.000
146	A	78	ALA	0	0.056	-0.122	21.367	-0.025	-0.025	0.000	0.000	0.000	0.000
147	A	78	ALA	0	-0.069	0.118	23.543	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	79	ASN	0	0.054	-0.086	21.274	-0.029	-0.029	0.000	0.000	0.000	0.000
149	A	79	ASN	0	-0.149	0.064	20.597	-0.032	-0.032	0.000	0.000	0.000	0.000
150	A	80	GLY	0	-0.022	-0.103	22.577	-0.028	-0.028	0.000	0.000	0.000	0.000
151	A	81	LYS	0	0.042	-0.025	18.464	-0.030	-0.030	0.000	0.000	0.000	0.000
152	A	81	LYS	1	0.786	1.035	17.442	-0.119	-0.119	0.000	0.000	0.000	0.000
153	A	82	PRO	0	-0.035	-0.096	15.346	0.033	0.033	0.000	0.000	0.000	0.000
154	A	83	GLY	0	0.095	0.025	14.659	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	84	PHE	0	0.080	0.016	12.378	-0.007	-0.007	0.000	0.000	0.000	0.000
156	A	84	PHE	0	-0.051	0.097	10.304	-0.026	-0.026	0.000	0.000	0.000	0.000
157	A	85	LYS	0	0.137	-0.091	12.488	-0.209	-0.209	0.000	0.000	0.000	0.000
158	A	85	LYS	1	0.672	0.991	9.894	-1.869	-1.869	0.000	0.000	0.000	0.000
159	A	86	GLN	0	0.138	-0.104	14.190	0.100	0.100	0.000	0.000	0.000	0.000
160	A	86	GLN	0	-0.100	0.113	18.811	-0.034	-0.034	0.000	0.000	0.000	0.000
161	A	87	GLY	0	-0.060	-0.112	16.341	0.027	0.027	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)