FMO DATABASE

FMODB ID: 9M7K2

Calculation Name: 1CF7-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-392300.889489
FMO2-HF: Nuclear repulsion	366504.176431
FMO2-HF: Total energy	-25796.713058
FMO2-MP2: Total energy	-25874.300065

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: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.
-3.127	1.404	1.32	-2.804	-3.049	-0.007

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 : 0.193 / q_NPA : 0.068

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	0.918	1.068	4.524	-1.487	-1.256	0.000	-0.099	-0.132	0.000
5	A	18	HIS	0	0.114	-0.134	3.111	-1.821	0.192	0.055	-0.950	-1.118	0.004
6	A	18	HIS	0	-0.033	0.149	4.188	0.044	0.158	-0.001	-0.021	-0.093	0.000
7	A	19	GLU	0	0.038	-0.135	3.490	-0.005	0.618	0.009	-0.329	-0.303	0.001
8	A	19	GLU	-1	-0.924	-0.805	2.391	-2.976	-1.521	1.260	-1.397	-1.319	-0.012
9	A	20	LYS	0	-0.006	-0.097	5.184	0.229	0.274	-0.002	-0.003	-0.040	0.000
10	A	20	LYS	1	0.844	1.051	4.523	1.897	1.947	-0.001	-0.005	-0.044	0.000
11	A	21	SER	0	0.077	-0.116	7.422	0.264	0.264	0.000	0.000	0.000	0.000
12	A	21	SER	0	0.035	0.130	8.483	0.028	0.028	0.000	0.000	0.000	0.000
13	A	22	LEU	0	0.074	-0.122	9.613	-0.090	-0.090	0.000	0.000	0.000	0.000
14	A	22	LEU	0	-0.076	0.141	13.832	0.005	0.005	0.000	0.000	0.000	0.000
15	A	23	GLY	0	0.094	-0.051	12.885	-0.032	-0.032	0.000	0.000	0.000	0.000
16	A	24	LEU	0	0.163	0.024	10.625	0.036	0.036	0.000	0.000	0.000	0.000
17	A	24	LEU	0	-0.096	0.121	8.021	-0.016	-0.016	0.000	0.000	0.000	0.000
18	A	25	LEU	0	0.028	-0.129	12.048	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	25	LEU	0	-0.051	0.077	12.407	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	26	THR	0	0.046	-0.083	14.136	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	26	THR	0	-0.070	0.054	15.980	0.016	0.016	0.000	0.000	0.000	0.000
22	A	27	THR	0	0.095	-0.093	15.638	0.011	0.011	0.000	0.000	0.000	0.000
23	A	27	THR	0	-0.004	0.103	15.037	0.006	0.006	0.000	0.000	0.000	0.000
24	A	28	LYS	0	0.007	-0.064	15.901	0.017	0.017	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.866	1.030	11.253	0.507	0.507	0.000	0.000	0.000	0.000
26	A	29	PHE	0	0.174	-0.023	17.287	0.002	0.002	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.111	0.058	19.025	0.001	0.001	0.000	0.000	0.000	0.000
28	A	30	VAL	0	0.013	-0.119	19.782	0.006	0.006	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.073	0.109	20.304	0.003	0.003	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.132	-0.039	20.405	0.015	0.015	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.045	0.072	19.833	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.082	-0.087	21.244	0.007	0.007	0.000	0.000	0.000	0.000
33	A	32	LEU	0	-0.125	0.083	21.001	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	33	LEU	0	0.126	-0.093	22.937	0.003	0.003	0.000	0.000	0.000	0.000
35	A	33	LEU	0	-0.177	0.040	24.440	0.002	0.002	0.000	0.000	0.000	0.000
36	A	34	GLN	0	0.047	-0.073	25.157	0.003	0.003	0.000	0.000	0.000	0.000
37	A	34	GLN	0	-0.126	0.051	23.883	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	35	GLU	0	0.101	-0.072	25.906	0.010	0.010	0.000	0.000	0.000	0.000
39	A	35	GLU	-1	-1.083	-0.898	25.559	-0.106	-0.106	0.000	0.000	0.000	0.000
40	A	36	ALA	0	0.091	-0.096	27.256	0.006	0.006	0.000	0.000	0.000	0.000
41	A	36	ALA	0	-0.088	0.085	28.108	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	37	LYS	0	0.101	-0.024	29.273	0.004	0.004	0.000	0.000	0.000	0.000
43	A	37	LYS	1	0.866	1.035	32.714	0.067	0.067	0.000	0.000	0.000	0.000
44	A	38	ASP	0	0.067	-0.111	32.558	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	38	ASP	-1	-0.987	-0.851	34.221	-0.063	-0.063	0.000	0.000	0.000	0.000
46	A	39	GLY	0	-0.019	-0.119	31.923	0.006	0.006	0.000	0.000	0.000	0.000
47	A	40	VAL	0	0.064	-0.015	31.685	0.002	0.002	0.000	0.000	0.000	0.000
48	A	40	VAL	0	-0.114	0.097	32.436	0.001	0.001	0.000	0.000	0.000	0.000
49	A	41	LEU	0	0.156	-0.107	27.701	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	41	LEU	0	-0.114	0.129	24.546	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	42	ASP	0	0.096	-0.115	28.303	0.009	0.009	0.000	0.000	0.000	0.000
52	A	42	ASP	-1	-0.940	-0.818	28.577	-0.100	-0.100	0.000	0.000	0.000	0.000
53	A	43	LEU	0	0.083	-0.143	25.501	-0.013	-0.013	0.000	0.000	0.000	0.000
54	A	43	LEU	0	-0.130	0.082	25.395	0.000	0.000	0.000	0.000	0.000	0.000
55	A	44	LYS	0	-0.003	-0.135	24.577	-0.012	-0.012	0.000	0.000	0.000	0.000
56	A	44	LYS	1	0.892	1.076	26.812	0.106	0.106	0.000	0.000	0.000	0.000
57	A	45	LEU	0	0.196	-0.050	24.630	-0.014	-0.014	0.000	0.000	0.000	0.000
58	A	45	LEU	0	-0.080	0.114	24.189	0.002	0.002	0.000	0.000	0.000	0.000
59	A	46	ALA	0	0.135	-0.094	21.745	-0.023	-0.023	0.000	0.000	0.000	0.000
60	A	46	ALA	0	-0.052	0.101	21.336	0.003	0.003	0.000	0.000	0.000	0.000
61	A	47	ALA	0	0.051	-0.084	20.114	-0.028	-0.028	0.000	0.000	0.000	0.000
62	A	47	ALA	0	-0.092	0.069	21.892	0.004	0.004	0.000	0.000	0.000	0.000
63	A	48	ASP	0	0.045	-0.120	19.297	-0.033	-0.033	0.000	0.000	0.000	0.000
64	A	48	ASP	-1	-0.974	-0.854	21.742	-0.200	-0.200	0.000	0.000	0.000	0.000
65	A	49	THR	0	0.039	-0.081	18.637	-0.045	-0.045	0.000	0.000	0.000	0.000
66	A	49	THR	0	-0.023	0.065	19.483	0.007	0.007	0.000	0.000	0.000	0.000
67	A	50	LEU	0	-0.071	-0.112	16.438	-0.035	-0.035	0.000	0.000	0.000	0.000
68	A	50	LEU	0	-0.164	0.105	16.463	0.001	0.001	0.000	0.000	0.000	0.000
69	A	51	ALA	0	0.167	-0.060	13.392	0.006	0.006	0.000	0.000	0.000	0.000
70	A	51	ALA	0	-0.142	0.038	12.702	-0.020	-0.020	0.000	0.000	0.000	0.000
71	A	52	VAL	0	0.103	-0.087	14.719	-0.049	-0.049	0.000	0.000	0.000	0.000
72	A	52	VAL	0	-0.043	0.150	16.827	0.004	0.004	0.000	0.000	0.000	0.000
73	A	53	ARG	0	0.083	-0.096	13.492	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	53	ARG	1	0.765	1.011	10.254	0.340	0.340	0.000	0.000	0.000	0.000
75	A	54	GLN	0	0.042	-0.117	14.365	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	54	GLN	0	-0.098	0.101	15.715	0.043	0.043	0.000	0.000	0.000	0.000
77	A	55	LYS	0	0.138	-0.088	17.542	0.007	0.007	0.000	0.000	0.000	0.000
78	A	55	LYS	1	0.845	1.083	22.004	0.114	0.114	0.000	0.000	0.000	0.000
79	A	56	ARG	0	0.170	-0.110	19.943	0.006	0.006	0.000	0.000	0.000	0.000
80	A	56	ARG	1	0.808	1.038	18.873	0.016	0.016	0.000	0.000	0.000	0.000
81	A	57	ARG	0	0.057	-0.097	16.621	0.034	0.034	0.000	0.000	0.000	0.000
82	A	57	ARG	1	0.782	1.025	14.311	0.059	0.059	0.000	0.000	0.000	0.000
83	A	58	ILE	0	0.134	-0.095	17.968	0.015	0.015	0.000	0.000	0.000	0.000
84	A	58	ILE	0	-0.069	0.134	19.150	0.001	0.001	0.000	0.000	0.000	0.000
85	A	59	TYR	0	0.106	-0.084	20.498	0.009	0.009	0.000	0.000	0.000	0.000
86	A	59	TYR	0	-0.107	0.087	22.922	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	60	ASP	0	0.083	-0.063	19.083	0.013	0.013	0.000	0.000	0.000	0.000
88	A	60	ASP	-1	-0.874	-0.831	17.800	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	61	ILE	0	0.048	-0.088	20.205	0.023	0.023	0.000	0.000	0.000	0.000
90	A	61	ILE	0	-0.080	0.084	17.293	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	62	THR	0	0.024	-0.067	20.939	0.012	0.012	0.000	0.000	0.000	0.000
92	A	62	THR	0	-0.016	0.054	24.023	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	63	ASN	0	0.127	-0.048	24.195	0.002	0.002	0.000	0.000	0.000	0.000
94	A	63	ASN	0	-0.106	0.058	24.343	0.006	0.006	0.000	0.000	0.000	0.000
95	A	64	VAL	0	0.022	-0.059	23.592	0.003	0.003	0.000	0.000	0.000	0.000
96	A	64	VAL	0	-0.089	0.089	21.470	0.003	0.003	0.000	0.000	0.000	0.000
97	A	65	LEU	0	0.131	-0.117	24.644	0.008	0.008	0.000	0.000	0.000	0.000
98	A	65	LEU	0	-0.084	0.097	23.148	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	66	GLU	0	0.032	-0.138	26.066	0.001	0.001	0.000	0.000	0.000	0.000
100	A	66	GLU	-1	-0.965	-0.842	28.211	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	67	GLY	0	-0.052	-0.111	28.228	0.002	0.002	0.000	0.000	0.000	0.000
102	A	68	ILE	0	0.068	-0.032	28.680	0.004	0.004	0.000	0.000	0.000	0.000
103	A	68	ILE	0	-0.109	0.111	26.988	0.000	0.000	0.000	0.000	0.000	0.000
104	A	69	GLY	0	0.018	-0.064	29.889	0.000	0.000	0.000	0.000	0.000	0.000
105	A	70	LEU	0	0.008	-0.073	28.931	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	70	LEU	0	-0.044	0.119	26.815	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	71	ILE	0	0.011	-0.079	29.076	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	71	ILE	0	-0.125	0.078	26.743	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	72	GLU	0	0.128	-0.158	30.495	0.006	0.006	0.000	0.000	0.000	0.000
110	A	72	GLU	-1	-0.943	-0.762	33.705	-0.022	-0.022	0.000	0.000	0.000	0.000
111	A	73	LYS	0	0.083	-0.097	32.136	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	73	LYS	1	0.864	1.056	30.577	0.021	0.021	0.000	0.000	0.000	0.000
113	A	74	LYS	0	0.192	-0.073	32.985	0.004	0.004	0.000	0.000	0.000	0.000
114	A	74	LYS	1	0.828	1.114	34.421	0.049	0.049	0.000	0.000	0.000	0.000
115	A	75	SER	0	-0.022	-0.105	34.091	0.003	0.003	0.000	0.000	0.000	0.000
116	A	75	SER	0	-0.041	0.036	35.797	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	76	LYS	0	0.078	-0.029	33.161	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	76	LYS	1	0.902	1.062	33.700	0.054	0.054	0.000	0.000	0.000	0.000
119	A	77	ASN	0	0.002	-0.083	29.437	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	77	ASN	0	-0.115	0.037	29.981	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	78	SER	0	0.177	-0.052	29.910	-0.010	-0.010	0.000	0.000	0.000	0.000
122	A	78	SER	0	-0.062	0.064	31.895	0.003	0.003	0.000	0.000	0.000	0.000
123	A	79	ILE	0	-0.047	-0.126	29.606	0.007	0.007	0.000	0.000	0.000	0.000
124	A	79	ILE	0	-0.049	0.110	27.182	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	80	GLN	0	0.142	-0.086	30.820	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	80	GLN	0	-0.070	0.116	33.974	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	81	TRP	0	0.100	-0.110	30.301	0.005	0.005	0.000	0.000	0.000	0.000
128	A	81	TRP	0	-0.072	0.096	26.779	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	82	LYS	0	-0.045	-0.113	31.031	0.001	0.001	0.000	0.000	0.000	0.000
130	A	82	LYS	1	0.957	0.996	32.568	0.010	0.010	0.000	0.000	0.000	0.000

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