FMO DATABASE

FMODB ID: 24JJR

Calculation Name: 1CMI-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1CMI

Chain ID: A

ChEMBL ID:

UniProt ID: P63167

Base Structure: X-ray

Registration Date: 2025-07-14

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	165
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-615266.125292
FMO2-HF: Nuclear repulsion	580449.76788
FMO2-HF: Total energy	-34816.357413
FMO2-MP2: Total energy	-34916.683575

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:5:LYS)

Summations of interaction energy for fragment #1(A:5:LYS)

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.
-1.51	0.418	0.021	-0.865	-1.084	0.002

Interaction energy analysis for fragmet #1(A:5:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.140 / 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].
4	A	6	ALA	0	-0.044	0.135	4.206	0.157	0.359	0.000	-0.099	-0.102	0.000
5	A	7	VAL	0	0.029	-0.117	3.794	-1.188	-0.024	-0.010	-0.560	-0.594	0.002
6	A	7	VAL	0	-0.116	0.076	4.499	0.044	0.100	-0.001	-0.018	-0.036	0.000
7	A	8	ILE	0	0.094	-0.112	6.453	0.293	0.293	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.034	0.154	7.838	-0.007	-0.007	0.000	0.000	0.000	0.000
9	A	9	LYS	0	0.013	-0.124	9.931	-0.040	-0.040	0.000	0.000	0.000	0.000
10	A	9	LYS	1	0.868	1.068	9.891	0.771	0.771	0.000	0.000	0.000	0.000
11	A	10	ASN	0	0.135	-0.057	12.669	0.027	0.027	0.000	0.000	0.000	0.000
12	A	10	ASN	0	-0.168	0.042	16.468	0.017	0.017	0.000	0.000	0.000	0.000
13	A	11	ALA	0	0.122	-0.105	15.098	0.024	0.024	0.000	0.000	0.000	0.000
14	A	11	ALA	0	-0.062	0.119	14.124	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	12	ASP	0	0.055	-0.093	16.105	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	12	ASP	-1	-0.961	-0.845	20.161	-0.116	-0.116	0.000	0.000	0.000	0.000
17	A	13	MET	0	0.045	-0.075	18.068	0.013	0.013	0.000	0.000	0.000	0.000
18	A	13	MET	0	-0.138	0.079	16.211	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	14	SER	0	0.086	-0.070	18.076	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	14	SER	0	-0.009	0.082	19.779	0.002	0.002	0.000	0.000	0.000	0.000
21	A	15	GLU	0	0.080	-0.140	15.450	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	15	GLU	-1	-0.945	-0.805	15.742	-0.139	-0.139	0.000	0.000	0.000	0.000
23	A	16	GLU	0	0.056	-0.127	14.878	-0.017	-0.017	0.000	0.000	0.000	0.000
24	A	16	GLU	-1	-1.001	-0.850	18.521	-0.049	-0.049	0.000	0.000	0.000	0.000
25	A	17	MET	0	0.130	-0.098	15.699	0.012	0.012	0.000	0.000	0.000	0.000
26	A	17	MET	0	-0.098	0.122	17.496	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	18	GLN	0	0.089	-0.120	13.911	0.023	0.023	0.000	0.000	0.000	0.000
28	A	18	GLN	0	-0.116	0.100	11.896	-0.071	-0.071	0.000	0.000	0.000	0.000
29	A	19	GLN	0	0.081	-0.133	11.080	-0.042	-0.042	0.000	0.000	0.000	0.000
30	A	19	GLN	0	-0.060	0.137	11.126	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	20	ASP	0	0.133	-0.107	11.105	0.025	0.025	0.000	0.000	0.000	0.000
32	A	20	ASP	-1	-0.898	-0.758	15.024	0.012	0.012	0.000	0.000	0.000	0.000
33	A	21	SER	0	-0.010	-0.076	12.208	0.061	0.061	0.000	0.000	0.000	0.000
34	A	21	SER	0	-0.032	0.064	11.928	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	22	VAL	0	0.059	-0.089	7.773	0.089	0.089	0.000	0.000	0.000	0.000
36	A	22	VAL	0	-0.085	0.090	5.801	-0.051	-0.051	0.000	0.000	0.000	0.000
37	A	23	GLU	0	0.120	-0.102	8.081	0.151	0.151	0.000	0.000	0.000	0.000
38	A	23	GLU	-1	-1.002	-0.823	10.371	0.120	0.120	0.000	0.000	0.000	0.000
39	A	24	CYS	0	0.145	-0.092	9.492	0.110	0.110	0.000	0.000	0.000	0.000
40	A	24	CYS	0	-0.137	0.120	12.776	0.001	0.001	0.000	0.000	0.000	0.000
41	A	25	ALA	0	0.101	-0.105	9.588	0.040	0.040	0.000	0.000	0.000	0.000
42	A	25	ALA	0	-0.071	0.077	8.711	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	26	THR	0	-0.038	-0.133	7.293	0.150	0.150	0.000	0.000	0.000	0.000
44	A	26	THR	0	-0.052	0.056	6.347	0.029	0.029	0.000	0.000	0.000	0.000
45	A	27	GLN	0	0.088	-0.077	7.926	0.135	0.135	0.000	0.000	0.000	0.000
46	A	27	GLN	0	-0.092	0.101	11.397	-0.035	-0.035	0.000	0.000	0.000	0.000
47	A	28	ALA	0	0.038	-0.084	11.390	0.009	0.009	0.000	0.000	0.000	0.000
48	A	28	ALA	0	-0.066	0.069	12.294	-0.016	-0.016	0.000	0.000	0.000	0.000
49	A	29	LEU	0	0.013	-0.122	9.251	-0.122	-0.122	0.000	0.000	0.000	0.000
50	A	29	LEU	0	-0.090	0.090	7.066	0.054	0.054	0.000	0.000	0.000	0.000
51	A	30	GLU	0	0.067	-0.122	10.470	0.050	0.050	0.000	0.000	0.000	0.000
52	A	30	GLU	-1	-1.003	-0.837	9.079	0.724	0.724	0.000	0.000	0.000	0.000
53	A	31	LYS	0	0.054	-0.082	11.445	-0.053	-0.053	0.000	0.000	0.000	0.000
54	A	31	LYS	1	0.814	1.046	15.094	-0.255	-0.255	0.000	0.000	0.000	0.000
55	A	32	TYR	0	0.033	-0.101	14.304	-0.044	-0.044	0.000	0.000	0.000	0.000
56	A	32	TYR	0	-0.099	0.054	15.613	-0.026	-0.026	0.000	0.000	0.000	0.000
57	A	33	ASN	0	0.178	-0.049	14.545	0.062	0.062	0.000	0.000	0.000	0.000
58	A	33	ASN	0	-0.125	0.054	16.607	0.035	0.035	0.000	0.000	0.000	0.000
59	A	34	ILE	0	0.107	-0.082	16.690	0.015	0.015	0.000	0.000	0.000	0.000
60	A	34	ILE	0	-0.134	0.091	19.940	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	35	GLU	0	0.090	-0.122	15.945	0.010	0.010	0.000	0.000	0.000	0.000
62	A	35	GLU	-1	-0.932	-0.815	15.278	0.247	0.247	0.000	0.000	0.000	0.000
63	A	36	LYS	0	0.131	-0.070	16.995	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	36	LYS	1	0.871	1.057	21.427	-0.120	-0.120	0.000	0.000	0.000	0.000
65	A	37	ASP	0	0.026	-0.128	19.325	-0.025	-0.025	0.000	0.000	0.000	0.000
66	A	37	ASP	-1	-0.945	-0.838	18.789	0.186	0.186	0.000	0.000	0.000	0.000
67	A	38	ILE	0	0.144	-0.108	14.582	-0.018	-0.018	0.000	0.000	0.000	0.000
68	A	38	ILE	0	-0.110	0.121	12.590	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	39	ALA	0	0.100	-0.097	15.651	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	39	ALA	0	-0.098	0.083	17.701	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	40	ALA	0	0.050	-0.106	17.265	-0.025	-0.025	0.000	0.000	0.000	0.000
72	A	40	ALA	0	-0.123	0.078	20.339	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	41	HIS	0	0.024	-0.106	16.821	-0.031	-0.031	0.000	0.000	0.000	0.000
74	A	41	HIS	0	-0.021	0.120	14.538	0.002	0.002	0.000	0.000	0.000	0.000
75	A	42	ILE	0	0.133	-0.083	15.242	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	42	ILE	0	-0.041	0.113	12.251	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	43	LYS	0	0.107	-0.067	16.211	-0.022	-0.022	0.000	0.000	0.000	0.000
78	A	43	LYS	1	0.677	0.970	19.923	-0.046	-0.046	0.000	0.000	0.000	0.000
79	A	44	LYS	0	0.065	-0.093	19.611	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	44	LYS	1	0.824	1.025	20.960	-0.096	-0.096	0.000	0.000	0.000	0.000
81	A	45	GLU	0	0.042	-0.126	18.101	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	45	GLU	-1	-0.968	-0.843	16.854	0.124	0.124	0.000	0.000	0.000	0.000
83	A	46	PHE	0	0.117	-0.074	19.088	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	46	PHE	0	-0.089	0.090	15.203	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	47	ASP	0	0.108	-0.102	19.978	-0.012	-0.012	0.000	0.000	0.000	0.000
86	A	47	ASP	-1	-0.866	-0.803	23.617	0.036	0.036	0.000	0.000	0.000	0.000
87	A	48	LYS	0	-0.054	-0.112	22.750	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	48	LYS	1	0.865	1.023	22.328	-0.090	-0.090	0.000	0.000	0.000	0.000
89	A	49	LYS	0	0.130	-0.055	21.043	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	49	LYS	1	0.774	1.029	17.587	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	50	TYR	0	0.025	-0.097	22.492	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	50	TYR	0	-0.124	0.040	18.023	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	51	ASN	0	0.160	-0.062	23.531	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	51	ASN	0	-0.130	0.056	27.308	0.005	0.005	0.000	0.000	0.000	0.000
95	A	52	PRO	0	0.021	-0.068	25.355	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	53	THR	0	0.016	-0.003	26.295	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	53	THR	0	-0.038	0.076	26.409	0.003	0.003	0.000	0.000	0.000	0.000
98	A	54	TRP	0	0.038	-0.119	21.799	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	54	TRP	0	-0.088	0.124	19.165	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	55	HIS	0	0.069	-0.114	21.584	0.012	0.012	0.000	0.000	0.000	0.000
101	A	55	HIS	0	-0.110	0.093	22.600	0.005	0.005	0.000	0.000	0.000	0.000
102	A	56	CYS	0	0.119	-0.120	17.943	-0.018	-0.018	0.000	0.000	0.000	0.000
103	A	56	CYS	0	-0.144	0.120	16.053	0.014	0.014	0.000	0.000	0.000	0.000
104	A	57	ILE	0	0.082	-0.113	17.482	0.017	0.017	0.000	0.000	0.000	0.000
105	A	57	ILE	0	-0.093	0.107	18.300	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	58	VAL	0	0.079	-0.132	14.770	-0.033	-0.033	0.000	0.000	0.000	0.000
107	A	58	VAL	0	-0.061	0.150	13.022	0.006	0.006	0.000	0.000	0.000	0.000
108	A	59	GLY	0	0.036	-0.090	14.554	0.007	0.007	0.000	0.000	0.000	0.000
109	A	60	ARG	0	0.075	0.000	14.497	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	60	ARG	1	0.834	1.044	12.133	-0.154	-0.154	0.000	0.000	0.000	0.000
111	A	61	ASN	0	0.071	-0.080	15.792	-0.038	-0.038	0.000	0.000	0.000	0.000
112	A	61	ASN	0	-0.113	0.062	19.270	0.002	0.002	0.000	0.000	0.000	0.000
113	A	62	PHE	0	0.060	-0.087	19.095	0.016	0.016	0.000	0.000	0.000	0.000
114	A	62	PHE	0	-0.045	0.093	16.410	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	63	GLY	0	0.031	-0.072	20.169	-0.020	-0.020	0.000	0.000	0.000	0.000
116	A	64	SER	0	-0.008	-0.003	22.521	0.015	0.015	0.000	0.000	0.000	0.000
117	A	64	SER	0	-0.005	0.068	21.141	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	65	TYR	0	0.093	-0.097	23.660	-0.014	-0.014	0.000	0.000	0.000	0.000
119	A	65	TYR	0	-0.077	0.119	26.245	0.002	0.002	0.000	0.000	0.000	0.000
120	A	66	VAL	0	-0.025	-0.098	24.839	0.010	0.010	0.000	0.000	0.000	0.000
121	A	66	VAL	0	-0.025	0.084	22.935	0.000	0.000	0.000	0.000	0.000	0.000
122	A	67	THR	0	0.050	-0.090	26.072	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	67	THR	0	0.002	0.104	29.231	0.000	0.000	0.000	0.000	0.000	0.000
124	A	68	HIS	0	0.035	-0.069	24.339	0.009	0.009	0.000	0.000	0.000	0.000
125	A	68	HIS	1	0.786	1.004	23.573	0.084	0.084	0.000	0.000	0.000	0.000
126	A	69	GLU	0	0.080	-0.140	25.556	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	69	GLU	-1	-0.932	-0.799	25.754	-0.027	-0.027	0.000	0.000	0.000	0.000
128	A	70	THR	0	0.056	-0.059	24.540	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	70	THR	0	-0.024	0.055	26.100	0.002	0.002	0.000	0.000	0.000	0.000
130	A	71	LYS	0	0.077	-0.066	22.320	0.008	0.008	0.000	0.000	0.000	0.000
131	A	71	LYS	1	0.896	1.073	23.270	0.076	0.076	0.000	0.000	0.000	0.000
132	A	72	HIS	0	0.027	-0.117	20.884	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	72	HIS	0	-0.179	0.068	22.329	0.008	0.008	0.000	0.000	0.000	0.000
134	A	73	PHE	0	0.240	-0.065	19.365	0.018	0.018	0.000	0.000	0.000	0.000
135	A	73	PHE	0	-0.129	0.058	18.227	0.007	0.007	0.000	0.000	0.000	0.000
136	A	74	ILE	0	0.077	-0.104	14.851	-0.020	-0.020	0.000	0.000	0.000	0.000
137	A	74	ILE	0	-0.058	0.110	12.008	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	75	TYR	0	0.139	-0.047	14.264	0.049	0.049	0.000	0.000	0.000	0.000
139	A	75	TYR	0	-0.117	0.066	14.061	-0.012	-0.012	0.000	0.000	0.000	0.000
140	A	76	PHE	0	-0.006	-0.135	9.900	-0.057	-0.057	0.000	0.000	0.000	0.000
141	A	76	PHE	0	-0.052	0.103	7.661	0.014	0.014	0.000	0.000	0.000	0.000
142	A	77	TYR	0	0.142	-0.087	7.883	0.266	0.266	0.000	0.000	0.000	0.000
143	A	77	TYR	0	-0.100	0.091	7.284	-0.069	-0.069	0.000	0.000	0.000	0.000
144	A	78	LEU	0	0.083	-0.115	4.764	-0.779	-0.800	-0.002	-0.016	0.038	0.000
145	A	78	LEU	0	-0.046	0.166	3.185	-0.397	-0.051	0.035	-0.129	-0.253	0.000
146	A	79	GLY	0	0.024	-0.075	4.354	-0.387	-0.206	-0.001	-0.043	-0.137	0.000
147	A	80	GLN	0	0.011	-0.014	6.006	-0.740	-0.740	0.000	0.000	0.000	0.000
148	A	80	GLN	0	-0.062	0.085	9.689	0.051	0.051	0.000	0.000	0.000	0.000
149	A	81	VAL	0	0.042	-0.101	8.928	-0.239	-0.239	0.000	0.000	0.000	0.000
150	A	81	VAL	0	-0.029	0.125	9.246	-0.010	-0.010	0.000	0.000	0.000	0.000
151	A	82	ALA	0	0.149	-0.100	9.513	-0.021	-0.021	0.000	0.000	0.000	0.000
152	A	82	ALA	0	-0.097	0.102	12.669	-0.019	-0.019	0.000	0.000	0.000	0.000
153	A	83	ILE	0	0.044	-0.132	11.521	0.061	0.061	0.000	0.000	0.000	0.000
154	A	83	ILE	0	-0.058	0.123	9.313	0.015	0.015	0.000	0.000	0.000	0.000
155	A	84	LEU	0	0.158	-0.082	12.837	-0.080	-0.080	0.000	0.000	0.000	0.000
156	A	84	LEU	0	-0.158	0.086	16.939	0.000	0.000	0.000	0.000	0.000	0.000
157	A	85	LEU	0	0.094	-0.131	15.986	0.036	0.036	0.000	0.000	0.000	0.000
158	A	85	LEU	0	-0.093	0.124	15.144	0.003	0.003	0.000	0.000	0.000	0.000
159	A	86	PHE	0	0.051	-0.089	17.066	-0.027	-0.027	0.000	0.000	0.000	0.000
160	A	86	PHE	0	-0.066	0.082	20.185	0.000	0.000	0.000	0.000	0.000	0.000
161	A	87	LYS	0	0.130	-0.094	20.395	0.015	0.015	0.000	0.000	0.000	0.000
162	A	87	LYS	1	0.804	1.057	22.813	0.007	0.007	0.000	0.000	0.000	0.000
163	A	88	SER	0	-0.001	-0.124	23.524	-0.011	-0.011	0.000	0.000	0.000	0.000
164	A	88	SER	0	-0.054	0.054	26.254	0.001	0.001	0.000	0.000	0.000	0.000
165	A	89	GLY	0	0.049	-0.023	27.043	0.006	0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LYS)