FMO DATABASE

FMODB ID: 7MZLK

Calculation Name: 3FB9-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3FB9

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

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	171
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-626705.476991
FMO2-HF: Nuclear repulsion	590688.766546
FMO2-HF: Total energy	-36016.710445
FMO2-MP2: Total energy	-36121.202785

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:0:GLY)

Summations of interaction energy for fragment #1(A:0:GLY)

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.
-0.409	0.758	-0.001	-0.503	-0.664	0.001

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.021

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].
3	A	1	MET	0	-0.081	0.112	3.985	0.167	0.442	0.001	-0.108	-0.168	0.000
4	A	2	SER	0	0.008	-0.079	3.849	-1.079	-0.187	-0.002	-0.395	-0.496	0.001
5	A	2	SER	0	-0.061	0.042	6.841	0.150	0.150	0.000	0.000	0.000	0.000
6	A	3	ASP	0	0.124	-0.084	6.260	0.330	0.330	0.000	0.000	0.000	0.000
7	A	3	ASP	-1	-0.867	-0.809	9.925	-0.868	-0.868	0.000	0.000	0.000	0.000
8	A	4	ALA	0	0.098	-0.105	9.294	0.184	0.184	0.000	0.000	0.000	0.000
9	A	4	ALA	0	-0.081	0.119	10.458	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	5	PHE	0	0.001	-0.088	8.474	0.141	0.141	0.000	0.000	0.000	0.000
11	A	5	PHE	0	-0.070	0.073	7.489	0.032	0.032	0.000	0.000	0.000	0.000
12	A	6	THR	0	0.070	-0.070	9.481	0.168	0.168	0.000	0.000	0.000	0.000
13	A	6	THR	0	-0.086	0.031	8.322	0.045	0.045	0.000	0.000	0.000	0.000
14	A	7	ASP	0	0.092	-0.091	10.054	-0.019	-0.019	0.000	0.000	0.000	0.000
15	A	7	ASP	-1	-0.915	-0.817	12.768	0.131	0.131	0.000	0.000	0.000	0.000
16	A	8	VAL	0	0.069	-0.110	13.376	0.019	0.019	0.000	0.000	0.000	0.000
17	A	8	VAL	0	-0.079	0.089	14.194	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	9	ALA	0	0.105	-0.095	13.472	0.041	0.041	0.000	0.000	0.000	0.000
19	A	9	ALA	0	-0.055	0.123	12.629	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	10	LYS	0	0.055	-0.117	13.816	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	10	LYS	1	0.748	1.018	12.027	-0.123	-0.123	0.000	0.000	0.000	0.000
22	A	11	MET	0	0.162	-0.066	15.385	0.013	0.013	0.000	0.000	0.000	0.000
23	A	11	MET	0	-0.122	0.094	18.031	0.002	0.002	0.000	0.000	0.000	0.000
24	A	12	LYS	0	0.073	-0.090	18.052	0.018	0.018	0.000	0.000	0.000	0.000
25	A	12	LYS	1	0.702	0.966	18.235	0.150	0.150	0.000	0.000	0.000	0.000
26	A	13	LYS	0	0.092	-0.087	18.136	0.014	0.014	0.000	0.000	0.000	0.000
27	A	13	LYS	1	0.781	1.010	17.540	0.122	0.122	0.000	0.000	0.000	0.000
28	A	14	ILE	0	0.079	-0.097	19.259	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	14	ILE	0	-0.037	0.110	17.873	0.003	0.003	0.000	0.000	0.000	0.000
30	A	15	LYS	0	0.102	-0.078	21.068	0.009	0.009	0.000	0.000	0.000	0.000
31	A	15	LYS	1	0.727	0.998	22.843	0.024	0.024	0.000	0.000	0.000	0.000
32	A	16	GLU	0	0.071	-0.107	22.850	0.011	0.011	0.000	0.000	0.000	0.000
33	A	16	GLU	-1	-0.926	-0.804	21.562	-0.136	-0.136	0.000	0.000	0.000	0.000
34	A	17	GLU	0	0.026	-0.126	23.234	0.000	0.000	0.000	0.000	0.000	0.000
35	A	17	GLU	-1	-0.870	-0.766	20.631	-0.075	-0.075	0.000	0.000	0.000	0.000
36	A	18	ILE	0	0.107	-0.056	24.680	0.002	0.002	0.000	0.000	0.000	0.000
37	A	18	ILE	0	-0.120	0.077	24.862	0.001	0.001	0.000	0.000	0.000	0.000
38	A	19	LYS	0	0.127	-0.066	26.935	0.005	0.005	0.000	0.000	0.000	0.000
39	A	19	LYS	1	0.828	1.033	27.908	0.050	0.050	0.000	0.000	0.000	0.000
40	A	20	ALA	0	0.057	-0.105	27.856	0.004	0.004	0.000	0.000	0.000	0.000
41	A	20	ALA	0	-0.100	0.083	27.518	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	21	HIS	0	0.041	-0.067	29.396	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	21	HIS	0	-0.125	0.063	28.570	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	22	GLU	0	0.154	-0.116	30.580	0.006	0.006	0.000	0.000	0.000	0.000
45	A	22	GLU	-1	-0.962	-0.827	32.765	-0.017	-0.017	0.000	0.000	0.000	0.000
46	A	23	GLY	0	-0.091	-0.135	33.264	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	24	GLN	0	0.045	-0.010	33.670	0.003	0.003	0.000	0.000	0.000	0.000
48	A	24	GLN	0	-0.102	0.089	32.350	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	25	VAL	0	0.114	-0.108	33.552	0.002	0.002	0.000	0.000	0.000	0.000
50	A	25	VAL	0	-0.087	0.106	33.043	0.000	0.000	0.000	0.000	0.000	0.000
51	A	26	VAL	0	0.039	-0.097	29.487	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	26	VAL	0	-0.052	0.109	28.514	0.000	0.000	0.000	0.000	0.000	0.000
53	A	27	GLU	0	0.167	-0.102	28.628	0.002	0.002	0.000	0.000	0.000	0.000
54	A	27	GLU	-1	-0.963	-0.812	28.075	0.037	0.037	0.000	0.000	0.000	0.000
55	A	28	MET	0	0.039	-0.126	26.953	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	28	MET	0	-0.116	0.111	26.236	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	29	THR	0	0.056	-0.053	26.384	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	29	THR	0	-0.074	0.034	24.954	0.004	0.004	0.000	0.000	0.000	0.000
59	A	30	LEU	0	0.059	-0.105	25.174	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	30	LEU	0	-0.071	0.089	26.202	0.000	0.000	0.000	0.000	0.000	0.000
61	A	31	GLU	0	0.069	-0.104	21.474	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	31	GLU	-1	-0.824	-0.723	19.124	0.226	0.226	0.000	0.000	0.000	0.000
63	A	32	ASN	0	0.021	-0.108	22.473	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	32	ASN	0	-0.158	0.043	25.605	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	33	GLY	0	0.060	-0.087	22.220	0.017	0.017	0.000	0.000	0.000	0.000
66	A	34	ARG	0	0.127	0.045	21.401	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	34	ARG	1	0.879	1.056	19.743	-0.158	-0.158	0.000	0.000	0.000	0.000
68	A	35	LYS	0	0.054	-0.080	22.240	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	35	LYS	1	0.804	1.021	26.797	-0.088	-0.088	0.000	0.000	0.000	0.000
70	A	36	ARG	0	0.091	-0.105	25.391	0.004	0.004	0.000	0.000	0.000	0.000
71	A	36	ARG	1	0.798	1.009	19.359	-0.175	-0.175	0.000	0.000	0.000	0.000
72	A	37	GLN	0	0.068	-0.106	26.312	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	37	GLN	0	-0.091	0.092	29.366	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	38	LYS	0	0.022	-0.045	29.649	0.003	0.003	0.000	0.000	0.000	0.000
75	A	38	LYS	1	0.881	1.037	32.061	-0.056	-0.056	0.000	0.000	0.000	0.000
76	A	39	ASN	0	0.135	-0.080	29.900	0.001	0.001	0.000	0.000	0.000	0.000
77	A	39	ASN	0	-0.095	0.049	26.904	0.009	0.009	0.000	0.000	0.000	0.000
78	A	40	ARG	0	0.099	-0.052	30.615	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	40	ARG	1	0.693	0.933	30.168	-0.047	-0.047	0.000	0.000	0.000	0.000
80	A	41	LEU	0	0.012	-0.134	31.527	0.002	0.002	0.000	0.000	0.000	0.000
81	A	41	LEU	0	-0.041	0.122	31.918	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	42	GLY	0	0.043	-0.108	33.109	0.001	0.001	0.000	0.000	0.000	0.000
83	A	43	LYS	0	0.101	0.027	33.598	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	43	LYS	1	0.767	1.020	36.769	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	44	LEU	0	0.175	-0.090	31.974	0.005	0.005	0.000	0.000	0.000	0.000
86	A	44	LEU	0	-0.151	0.100	29.245	0.001	0.001	0.000	0.000	0.000	0.000
87	A	45	ILE	0	0.035	-0.106	33.235	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	45	ILE	0	-0.140	0.074	36.334	0.000	0.000	0.000	0.000	0.000	0.000
89	A	46	GLU	0	0.127	-0.085	34.609	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	46	GLU	-1	-0.922	-0.805	35.846	0.002	0.002	0.000	0.000	0.000	0.000
91	A	47	VAL	0	0.044	-0.107	31.616	0.006	0.006	0.000	0.000	0.000	0.000
92	A	47	VAL	0	-0.068	0.118	29.668	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	48	TYR	0	0.074	-0.098	31.326	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	48	TYR	0	-0.155	0.047	32.366	0.000	0.000	0.000	0.000	0.000	0.000
95	A	49	PRO	0	-0.011	-0.120	29.747	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	50	SER	0	0.032	0.026	28.038	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	50	SER	0	-0.015	0.061	29.483	0.000	0.000	0.000	0.000	0.000	0.000
98	A	51	LEU	0	0.036	-0.085	27.755	0.004	0.004	0.000	0.000	0.000	0.000
99	A	51	LEU	0	-0.067	0.086	29.951	0.001	0.001	0.000	0.000	0.000	0.000
100	A	52	PHE	0	0.068	-0.078	29.420	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	52	PHE	0	-0.026	0.103	25.366	0.000	0.000	0.000	0.000	0.000	0.000
102	A	53	ILE	0	0.066	-0.100	30.646	0.007	0.007	0.000	0.000	0.000	0.000
103	A	53	ILE	0	-0.067	0.088	34.081	0.000	0.000	0.000	0.000	0.000	0.000
104	A	54	VAL	0	0.036	-0.107	32.625	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	54	VAL	0	-0.026	0.104	30.502	0.001	0.001	0.000	0.000	0.000	0.000
106	A	55	GLU	0	0.149	-0.104	33.855	0.004	0.004	0.000	0.000	0.000	0.000
107	A	55	GLU	-1	-0.987	-0.815	37.723	0.005	0.005	0.000	0.000	0.000	0.000
108	A	56	PHE	0	0.063	-0.117	36.261	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	56	PHE	0	-0.092	0.092	31.005	0.001	0.001	0.000	0.000	0.000	0.000
110	A	57	GLY	0	0.050	-0.082	37.081	0.000	0.000	0.000	0.000	0.000	0.000
111	A	58	ASP	0	0.085	0.033	39.852	0.001	0.001	0.000	0.000	0.000	0.000
112	A	58	ASP	-1	-0.904	-0.827	41.981	0.009	0.009	0.000	0.000	0.000	0.000
113	A	59	VAL	0	0.100	-0.093	37.712	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	59	VAL	0	-0.059	0.116	35.926	0.000	0.000	0.000	0.000	0.000	0.000
115	A	60	GLU	0	0.032	-0.134	39.230	0.003	0.003	0.000	0.000	0.000	0.000
116	A	60	GLU	-1	-0.963	-0.835	40.537	0.005	0.005	0.000	0.000	0.000	0.000
117	A	61	GLY	0	-0.002	-0.116	38.655	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	62	ASP	0	0.045	0.009	37.411	0.002	0.002	0.000	0.000	0.000	0.000
119	A	62	ASP	-1	-0.910	-0.820	36.052	0.030	0.030	0.000	0.000	0.000	0.000
120	A	63	LYS	0	0.040	-0.113	38.879	0.001	0.001	0.000	0.000	0.000	0.000
121	A	63	LYS	1	0.735	1.002	42.613	-0.008	-0.008	0.000	0.000	0.000	0.000
122	A	64	GLN	0	0.048	-0.106	41.661	0.001	0.001	0.000	0.000	0.000	0.000
123	A	64	GLN	0	-0.127	0.054	39.028	0.001	0.001	0.000	0.000	0.000	0.000
124	A	65	VAL	0	0.063	-0.088	42.897	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	65	VAL	0	-0.097	0.075	45.930	0.000	0.000	0.000	0.000	0.000	0.000
126	A	66	ASN	0	0.117	-0.055	43.865	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	66	ASN	0	-0.176	0.037	41.744	0.000	0.000	0.000	0.000	0.000	0.000
128	A	67	VAL	0	0.119	-0.110	41.774	0.003	0.003	0.000	0.000	0.000	0.000
129	A	67	VAL	0	-0.064	0.127	41.656	0.000	0.000	0.000	0.000	0.000	0.000
130	A	68	TYR	0	0.023	-0.075	40.139	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	68	TYR	0	-0.135	0.058	35.705	0.002	0.002	0.000	0.000	0.000	0.000
132	A	69	VAL	0	0.076	-0.096	37.416	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	69	VAL	0	-0.038	0.114	37.741	0.000	0.000	0.000	0.000	0.000	0.000
134	A	70	GLU	0	0.057	-0.104	34.088	0.001	0.001	0.000	0.000	0.000	0.000
135	A	70	GLU	-1	-0.856	-0.759	31.810	0.049	0.049	0.000	0.000	0.000	0.000
136	A	71	SER	0	0.038	-0.107	32.233	-0.004	-0.004	0.000	0.000	0.000	0.000
137	A	71	SER	0	-0.038	0.079	32.732	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	72	PHE	0	0.031	-0.094	27.850	0.006	0.006	0.000	0.000	0.000	0.000
139	A	72	PHE	0	-0.069	0.103	26.858	0.001	0.001	0.000	0.000	0.000	0.000
140	A	73	THR	0	0.067	-0.069	26.402	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	73	THR	0	-0.080	0.025	25.488	0.002	0.002	0.000	0.000	0.000	0.000
142	A	74	TYR	0	0.124	-0.070	23.444	0.008	0.008	0.000	0.000	0.000	0.000
143	A	74	TYR	0	-0.076	0.068	22.519	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	75	SER	0	0.053	-0.064	20.925	0.000	0.000	0.000	0.000	0.000	0.000
145	A	75	SER	0	-0.016	0.056	21.972	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	76	ASP	0	0.052	-0.064	20.925	0.019	0.019	0.000	0.000	0.000	0.000
147	A	76	ASP	-1	-0.840	-0.773	24.667	0.066	0.066	0.000	0.000	0.000	0.000
148	A	77	ILE	0	0.085	-0.087	21.086	0.018	0.018	0.000	0.000	0.000	0.000
149	A	77	ILE	0	-0.057	0.122	19.914	-0.002	-0.002	0.000	0.000	0.000	0.000
150	A	78	LEU	0	0.161	-0.075	17.431	0.011	0.011	0.000	0.000	0.000	0.000
151	A	78	LEU	0	-0.166	0.082	15.724	-0.005	-0.005	0.000	0.000	0.000	0.000
152	A	79	THR	0	-0.072	-0.085	16.225	0.022	0.022	0.000	0.000	0.000	0.000
153	A	79	THR	0	-0.060	0.025	18.137	0.001	0.001	0.000	0.000	0.000	0.000
154	A	80	GLU	0	0.070	-0.080	17.427	0.018	0.018	0.000	0.000	0.000	0.000
155	A	80	GLU	-1	-0.976	-0.849	14.266	0.250	0.250	0.000	0.000	0.000	0.000
156	A	81	LYS	0	0.154	-0.092	18.716	0.010	0.010	0.000	0.000	0.000	0.000
157	A	81	LYS	1	0.736	0.999	21.975	-0.088	-0.088	0.000	0.000	0.000	0.000
158	A	82	ASN	0	0.019	-0.093	21.986	0.002	0.002	0.000	0.000	0.000	0.000
159	A	82	ASN	0	-0.101	0.047	24.490	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	83	LEU	0	0.120	-0.089	21.815	0.000	0.000	0.000	0.000	0.000	0.000
161	A	83	LEU	0	-0.097	0.096	19.438	0.000	0.000	0.000	0.000	0.000	0.000
162	A	84	ILE	0	0.053	-0.110	22.370	0.000	0.000	0.000	0.000	0.000	0.000
163	A	84	ILE	0	-0.061	0.099	22.325	0.000	0.000	0.000	0.000	0.000	0.000
164	A	85	HIS	0	0.081	-0.088	22.761	0.000	0.000	0.000	0.000	0.000	0.000
165	A	85	HIS	0	-0.070	0.092	24.182	0.001	0.001	0.000	0.000	0.000	0.000
166	A	86	TYR	0	0.031	-0.095	25.004	0.007	0.007	0.000	0.000	0.000	0.000
167	A	86	TYR	0	-0.086	0.057	22.052	0.004	0.004	0.000	0.000	0.000	0.000
168	A	87	LEU	0	0.087	-0.105	27.227	-0.006	-0.006	0.000	0.000	0.000	0.000
169	A	87	LEU	0	-0.100	0.096	28.650	0.001	0.001	0.000	0.000	0.000	0.000
170	A	88	ASP	0	-0.111	-0.162	30.254	0.004	0.004	0.000	0.000	0.000	0.000
171	A	88	ASP	-1	-0.837	-0.906	29.928	-0.037	-0.037	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)