FMO DATABASE

FMODB ID: 37Z8L

Calculation Name: 1CF7-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1CF7

Chain ID: A

ChEMBL ID:

UniProt ID: Q16254

Base Structure: X-ray

Registration Date: 2025-07-07

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	OptHSide
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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-392266.939283
FMO2-HF: Nuclear repulsion	366468.284448
FMO2-HF: Total energy	-25798.654836
FMO2-MP2: Total energy	-25876.151787

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:16:SER)

Summations of interaction energy for fragment #1(A:16: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.
-0.379	3.528	3.326	-3.518	-3.716	-0.016

Interaction energy analysis for fragmet #1(A:16:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.221 / q_NPA : 0.093

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	17	ARG	1	0.919	1.073	4.529	-1.408	-1.142	0.000	-0.119	-0.147	0.000
5	A	18	HIS	0	0.083	-0.115	3.113	-1.404	0.593	0.043	-0.919	-1.121	0.003
6	A	18	HIS	0	-0.057	0.106	3.973	0.162	0.287	0.000	-0.025	-0.099	0.000
7	A	19	GLU	0	0.096	-0.098	3.493	0.314	0.812	0.007	-0.244	-0.261	0.001
8	A	19	GLU	-1	-0.899	-0.799	2.332	-4.587	-3.540	3.256	-2.413	-1.890	-0.021
9	A	20	LYS	0	0.037	-0.094	5.211	0.334	0.374	-0.002	-0.004	-0.035	0.000
10	A	20	LYS	1	0.796	1.026	2.970	4.930	4.864	0.022	0.206	-0.163	0.001
11	A	21	SER	0	0.064	-0.114	7.422	0.316	0.316	0.000	0.000	0.000	0.000
12	A	21	SER	0	0.013	0.119	8.431	0.055	0.055	0.000	0.000	0.000	0.000
13	A	22	LEU	0	0.093	-0.111	9.613	-0.079	-0.079	0.000	0.000	0.000	0.000
14	A	22	LEU	0	-0.069	0.128	13.856	0.007	0.007	0.000	0.000	0.000	0.000
15	A	23	GLY	0	0.078	-0.065	12.910	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	24	LEU	0	0.149	0.030	10.634	0.056	0.056	0.000	0.000	0.000	0.000
17	A	24	LEU	0	-0.077	0.118	7.988	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	25	LEU	0	0.038	-0.103	12.070	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	25	LEU	0	-0.061	0.068	12.218	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	26	THR	0	0.036	-0.087	14.162	0.004	0.004	0.000	0.000	0.000	0.000
21	A	26	THR	0	-0.052	0.061	16.055	0.019	0.019	0.000	0.000	0.000	0.000
22	A	27	THR	0	0.056	-0.063	15.666	0.022	0.022	0.000	0.000	0.000	0.000
23	A	27	THR	0	-0.013	0.081	14.962	0.005	0.005	0.000	0.000	0.000	0.000
24	A	28	LYS	0	0.079	-0.076	15.921	0.022	0.022	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.868	1.050	11.489	0.571	0.571	0.000	0.000	0.000	0.000
26	A	29	PHE	0	0.171	-0.021	17.313	0.009	0.009	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.106	0.062	19.093	0.002	0.002	0.000	0.000	0.000	0.000
28	A	30	VAL	0	0.016	-0.110	19.803	0.012	0.012	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.098	0.097	20.426	0.003	0.003	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.077	-0.059	20.432	0.019	0.019	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.045	0.050	19.598	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.137	-0.055	21.270	0.011	0.011	0.000	0.000	0.000	0.000
33	A	32	LEU	0	-0.140	0.080	21.124	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	33	LEU	0	0.075	-0.091	22.964	0.006	0.006	0.000	0.000	0.000	0.000
35	A	33	LEU	0	-0.148	0.053	24.608	0.002	0.002	0.000	0.000	0.000	0.000
36	A	34	GLN	0	0.072	-0.064	25.190	0.006	0.006	0.000	0.000	0.000	0.000
37	A	34	GLN	0	-0.121	0.051	23.899	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	35	GLU	0	0.092	-0.097	25.933	0.011	0.011	0.000	0.000	0.000	0.000
39	A	35	GLU	-1	-0.993	-0.848	25.723	-0.123	-0.123	0.000	0.000	0.000	0.000
40	A	36	ALA	0	0.124	-0.083	27.277	0.008	0.008	0.000	0.000	0.000	0.000
41	A	36	ALA	0	-0.097	0.090	28.081	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	37	LYS	0	0.130	-0.025	29.300	0.002	0.002	0.000	0.000	0.000	0.000
43	A	37	LYS	1	0.741	0.969	30.838	0.098	0.098	0.000	0.000	0.000	0.000
44	A	38	ASP	0	0.091	-0.111	32.584	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	38	ASP	-1	-0.999	-0.833	34.616	-0.073	-0.073	0.000	0.000	0.000	0.000
46	A	39	GLY	0	-0.059	-0.149	31.946	0.006	0.006	0.000	0.000	0.000	0.000
47	A	40	VAL	0	0.065	-0.014	31.712	0.001	0.001	0.000	0.000	0.000	0.000
48	A	40	VAL	0	-0.101	0.093	32.507	0.001	0.001	0.000	0.000	0.000	0.000
49	A	41	LEU	0	0.150	-0.081	27.683	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	41	LEU	0	-0.101	0.110	24.410	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	42	ASP	0	0.081	-0.106	28.314	0.009	0.009	0.000	0.000	0.000	0.000
52	A	42	ASP	-1	-0.889	-0.797	28.819	-0.105	-0.105	0.000	0.000	0.000	0.000
53	A	43	LEU	0	0.068	-0.122	25.537	-0.014	-0.014	0.000	0.000	0.000	0.000
54	A	43	LEU	0	-0.142	0.056	25.202	0.000	0.000	0.000	0.000	0.000	0.000
55	A	44	LYS	0	0.038	-0.149	24.607	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	44	LYS	1	0.897	1.067	27.254	0.105	0.105	0.000	0.000	0.000	0.000
57	A	45	LEU	0	0.131	-0.033	24.661	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	45	LEU	0	-0.075	0.109	24.513	0.002	0.002	0.000	0.000	0.000	0.000
59	A	46	ALA	0	0.166	-0.061	21.757	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	46	ALA	0	-0.064	0.092	21.428	0.003	0.003	0.000	0.000	0.000	0.000
61	A	47	ALA	0	0.050	-0.063	20.145	-0.031	-0.031	0.000	0.000	0.000	0.000
62	A	47	ALA	0	-0.085	0.063	21.781	0.005	0.005	0.000	0.000	0.000	0.000
63	A	48	ASP	0	0.057	-0.119	19.325	-0.032	-0.032	0.000	0.000	0.000	0.000
64	A	48	ASP	-1	-0.986	-0.850	21.760	-0.200	-0.200	0.000	0.000	0.000	0.000
65	A	49	THR	0	0.029	-0.104	18.669	-0.042	-0.042	0.000	0.000	0.000	0.000
66	A	49	THR	0	-0.047	0.053	19.689	0.007	0.007	0.000	0.000	0.000	0.000
67	A	50	LEU	0	-0.072	-0.110	16.470	-0.040	-0.040	0.000	0.000	0.000	0.000
68	A	50	LEU	0	-0.125	0.066	16.313	0.000	0.000	0.000	0.000	0.000	0.000
69	A	51	ALA	0	0.176	-0.039	13.322	0.012	0.012	0.000	0.000	0.000	0.000
70	A	51	ALA	0	-0.157	0.044	12.684	-0.026	-0.026	0.000	0.000	0.000	0.000
71	A	52	VAL	0	0.129	-0.100	14.751	-0.043	-0.043	0.000	0.000	0.000	0.000
72	A	52	VAL	0	-0.063	0.151	16.919	0.004	0.004	0.000	0.000	0.000	0.000
73	A	53	ARG	0	0.062	-0.109	13.493	0.002	0.002	0.000	0.000	0.000	0.000
74	A	53	ARG	1	0.744	1.005	10.063	0.359	0.359	0.000	0.000	0.000	0.000
75	A	54	GLN	0	-0.005	-0.116	14.369	0.003	0.003	0.000	0.000	0.000	0.000
76	A	54	GLN	0	-0.009	0.098	16.025	0.039	0.039	0.000	0.000	0.000	0.000
77	A	55	LYS	0	0.117	-0.064	17.548	0.001	0.001	0.000	0.000	0.000	0.000
78	A	55	LYS	1	0.827	1.064	22.045	0.116	0.116	0.000	0.000	0.000	0.000
79	A	56	ARG	0	0.159	-0.075	20.179	0.001	0.001	0.000	0.000	0.000	0.000
80	A	56	ARG	1	0.767	1.003	19.133	0.026	0.026	0.000	0.000	0.000	0.000
81	A	57	ARG	0	0.047	-0.121	16.597	0.033	0.033	0.000	0.000	0.000	0.000
82	A	57	ARG	1	0.772	1.000	14.335	0.067	0.067	0.000	0.000	0.000	0.000
83	A	58	ILE	0	0.101	-0.075	17.968	0.008	0.008	0.000	0.000	0.000	0.000
84	A	58	ILE	0	-0.068	0.108	19.026	0.001	0.001	0.000	0.000	0.000	0.000
85	A	59	TYR	0	0.127	-0.067	20.498	0.006	0.006	0.000	0.000	0.000	0.000
86	A	59	TYR	0	-0.064	0.098	23.038	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	60	ASP	0	0.099	-0.047	19.140	0.014	0.014	0.000	0.000	0.000	0.000
88	A	60	ASP	-1	-0.836	-0.803	18.103	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	61	ILE	0	0.034	-0.086	20.205	0.021	0.021	0.000	0.000	0.000	0.000
90	A	61	ILE	0	-0.097	0.072	17.283	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	62	THR	0	0.048	-0.079	20.942	0.010	0.010	0.000	0.000	0.000	0.000
92	A	62	THR	0	-0.042	0.058	23.957	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	63	ASN	0	0.139	-0.036	24.214	0.003	0.003	0.000	0.000	0.000	0.000
94	A	63	ASN	0	-0.145	0.056	24.377	0.005	0.005	0.000	0.000	0.000	0.000
95	A	64	VAL	0	0.094	-0.088	23.583	0.006	0.006	0.000	0.000	0.000	0.000
96	A	64	VAL	0	-0.095	0.096	21.557	0.001	0.001	0.000	0.000	0.000	0.000
97	A	65	LEU	0	0.065	-0.103	24.653	0.008	0.008	0.000	0.000	0.000	0.000
98	A	65	LEU	0	-0.070	0.076	23.038	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	66	GLU	0	0.011	-0.123	26.086	0.001	0.001	0.000	0.000	0.000	0.000
100	A	66	GLU	-1	-0.847	-0.792	28.151	-0.038	-0.038	0.000	0.000	0.000	0.000
101	A	67	GLY	0	-0.031	-0.099	28.220	0.003	0.003	0.000	0.000	0.000	0.000
102	A	68	ILE	0	0.055	-0.011	28.705	0.006	0.006	0.000	0.000	0.000	0.000
103	A	68	ILE	0	-0.105	0.105	26.750	0.000	0.000	0.000	0.000	0.000	0.000
104	A	69	GLY	0	0.060	-0.061	29.906	0.001	0.001	0.000	0.000	0.000	0.000
105	A	70	LEU	0	0.012	-0.029	28.937	0.000	0.000	0.000	0.000	0.000	0.000
106	A	70	LEU	0	-0.039	0.107	26.732	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	71	ILE	0	0.028	-0.058	29.047	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	71	ILE	0	-0.094	0.051	26.833	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	72	GLU	0	0.092	-0.116	30.518	0.005	0.005	0.000	0.000	0.000	0.000
110	A	72	GLU	-1	-0.934	-0.806	33.867	-0.035	-0.035	0.000	0.000	0.000	0.000
111	A	73	LYS	0	0.068	-0.100	32.154	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	73	LYS	1	0.788	0.992	30.549	0.033	0.033	0.000	0.000	0.000	0.000
113	A	74	LYS	0	0.176	-0.062	33.011	0.005	0.005	0.000	0.000	0.000	0.000
114	A	74	LYS	1	0.787	1.068	34.362	0.061	0.061	0.000	0.000	0.000	0.000
115	A	75	SER	0	-0.043	-0.126	34.121	0.004	0.004	0.000	0.000	0.000	0.000
116	A	75	SER	0	0.013	0.065	35.544	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	76	LYS	0	0.091	0.001	33.148	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	76	LYS	1	0.909	1.060	33.722	0.054	0.054	0.000	0.000	0.000	0.000
119	A	77	ASN	0	-0.014	-0.076	29.471	0.000	0.000	0.000	0.000	0.000	0.000
120	A	77	ASN	0	-0.097	0.033	29.265	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	78	SER	0	0.153	-0.053	29.940	-0.010	-0.010	0.000	0.000	0.000	0.000
122	A	78	SER	0	-0.045	0.065	31.801	0.003	0.003	0.000	0.000	0.000	0.000
123	A	79	ILE	0	-0.019	-0.121	29.590	0.008	0.008	0.000	0.000	0.000	0.000
124	A	79	ILE	0	-0.057	0.089	27.051	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	80	GLN	0	0.154	-0.067	30.847	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	80	GLN	0	-0.101	0.104	33.995	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	81	TRP	0	0.088	-0.106	30.299	0.005	0.005	0.000	0.000	0.000	0.000
128	A	81	TRP	0	-0.078	0.092	27.034	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	82	LYS	0	-0.037	-0.108	31.049	0.003	0.003	0.000	0.000	0.000	0.000
130	A	82	LYS	1	0.917	0.960	32.427	0.030	0.030	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:SER)