FMO DATABASE

FMODB ID: J29J9

Calculation Name: 3ZIG-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3ZIG

Chain ID: A

ChEMBL ID:

UniProt ID: I6V3Q6

Base Structure: X-ray

Registration Date: 2025-07-09

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	155
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-524228.04729
FMO2-HF: Nuclear repulsion	493273.46392
FMO2-HF: Total energy	-30954.58337
FMO2-MP2: Total energy	-31045.710756

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:49:LYS)

Summations of interaction energy for fragment #1(A:49: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.
-2.874	-0.306	-0.011	-1.383	-1.174	0.005

Interaction energy analysis for fragmet #1(A:49:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.172 / q_NPA : 0.054

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	50	VAL	0	-0.081	0.107	3.877	-0.136	0.331	0.004	-0.187	-0.284	0.000
5	A	51	VAL	0	0.113	-0.108	3.817	-2.133	-0.032	-0.015	-1.196	-0.890	0.005
6	A	51	VAL	0	-0.068	0.137	5.000	0.051	0.051	0.000	0.000	0.000	0.000
7	A	52	TYR	0	0.063	-0.104	6.620	0.374	0.374	0.000	0.000	0.000	0.000
8	A	52	TYR	0	-0.115	0.084	7.720	0.102	0.102	0.000	0.000	0.000	0.000
9	A	53	ILE	0	0.133	-0.082	10.127	-0.028	-0.028	0.000	0.000	0.000	0.000
10	A	53	ILE	0	-0.092	0.097	12.454	0.024	0.024	0.000	0.000	0.000	0.000
11	A	54	LYS	0	0.073	-0.119	13.502	0.079	0.079	0.000	0.000	0.000	0.000
12	A	54	LYS	1	0.775	1.027	12.286	0.778	0.778	0.000	0.000	0.000	0.000
13	A	55	LYS	0	0.079	-0.060	15.732	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	55	LYS	1	0.865	1.049	19.024	0.432	0.432	0.000	0.000	0.000	0.000
15	A	56	ILE	0	0.002	-0.136	19.462	0.006	0.006	0.000	0.000	0.000	0.000
16	A	56	ILE	0	-0.041	0.111	18.247	0.003	0.003	0.000	0.000	0.000	0.000
17	A	57	VAL	0	0.068	-0.111	21.654	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	57	VAL	0	-0.058	0.119	25.118	0.001	0.001	0.000	0.000	0.000	0.000
19	A	58	ILE	0	0.038	-0.133	25.415	0.003	0.003	0.000	0.000	0.000	0.000
20	A	58	ILE	0	-0.050	0.124	23.677	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	59	SER	0	0.021	-0.062	26.915	0.009	0.009	0.000	0.000	0.000	0.000
22	A	59	SER	0	-0.022	0.069	29.082	0.006	0.006	0.000	0.000	0.000	0.000
23	A	60	THR	0	-0.002	-0.095	29.369	0.012	0.012	0.000	0.000	0.000	0.000
24	A	60	THR	0	-0.047	0.044	28.594	0.001	0.001	0.000	0.000	0.000	0.000
25	A	61	HIS	0	0.176	-0.046	28.837	-0.014	-0.014	0.000	0.000	0.000	0.000
26	A	61	HIS	0	-0.066	0.088	29.674	0.001	0.001	0.000	0.000	0.000	0.000
27	A	62	ALA	0	0.083	-0.111	27.055	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	62	ALA	0	-0.056	0.127	26.844	0.002	0.002	0.000	0.000	0.000	0.000
29	A	63	ASP	0	-0.019	-0.131	24.283	-0.017	-0.017	0.000	0.000	0.000	0.000
30	A	63	ASP	-1	-0.777	-0.742	24.773	-0.236	-0.236	0.000	0.000	0.000	0.000
31	A	64	LEU	0	0.105	-0.125	22.959	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	64	LEU	0	-0.033	0.129	24.684	0.001	0.001	0.000	0.000	0.000	0.000
33	A	65	LYS	0	0.083	-0.063	21.839	-0.030	-0.030	0.000	0.000	0.000	0.000
34	A	65	LYS	1	0.789	0.992	20.124	0.298	0.298	0.000	0.000	0.000	0.000
35	A	66	ARG	0	0.085	-0.067	19.641	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	66	ARG	1	0.795	0.995	20.220	0.304	0.304	0.000	0.000	0.000	0.000
37	A	67	VAL	0	0.077	-0.092	17.958	-0.056	-0.056	0.000	0.000	0.000	0.000
38	A	67	VAL	0	-0.064	0.092	18.663	0.002	0.002	0.000	0.000	0.000	0.000
39	A	68	SER	0	0.118	-0.052	16.949	-0.077	-0.077	0.000	0.000	0.000	0.000
40	A	68	SER	0	-0.059	0.067	19.330	0.011	0.011	0.000	0.000	0.000	0.000
41	A	69	ASP	0	0.084	-0.097	16.137	-0.054	-0.054	0.000	0.000	0.000	0.000
42	A	69	ASP	-1	-0.956	-0.798	16.472	-0.343	-0.343	0.000	0.000	0.000	0.000
43	A	70	GLU	0	0.079	-0.097	13.346	-0.059	-0.059	0.000	0.000	0.000	0.000
44	A	70	GLU	-1	-0.875	-0.785	13.085	-0.797	-0.797	0.000	0.000	0.000	0.000
45	A	71	LEU	0	0.095	-0.086	11.923	-0.203	-0.203	0.000	0.000	0.000	0.000
46	A	71	LEU	0	-0.083	0.089	14.145	0.027	0.027	0.000	0.000	0.000	0.000
47	A	72	LYS	0	0.079	-0.082	11.904	-0.132	-0.132	0.000	0.000	0.000	0.000
48	A	72	LYS	1	0.835	1.043	13.818	0.416	0.416	0.000	0.000	0.000	0.000
49	A	73	SER	0	-0.038	-0.105	9.946	0.000	0.000	0.000	0.000	0.000	0.000
50	A	73	SER	0	-0.089	0.056	9.742	0.047	0.047	0.000	0.000	0.000	0.000
51	A	74	GLY	0	0.001	-0.092	7.432	-0.401	-0.401	0.000	0.000	0.000	0.000
52	A	75	ASN	0	0.056	0.043	8.336	-0.358	-0.358	0.000	0.000	0.000	0.000
53	A	75	ASN	0	-0.125	0.030	8.861	-0.286	-0.286	0.000	0.000	0.000	0.000
54	A	76	ILE	0	0.206	-0.077	10.214	0.128	0.128	0.000	0.000	0.000	0.000
55	A	76	ILE	0	-0.107	0.090	11.235	0.013	0.013	0.000	0.000	0.000	0.000
56	A	77	VAL	0	0.022	-0.119	13.099	-0.011	-0.011	0.000	0.000	0.000	0.000
57	A	77	VAL	0	-0.098	0.110	15.186	0.013	0.013	0.000	0.000	0.000	0.000
58	A	78	ILE	0	0.099	-0.095	16.503	0.031	0.031	0.000	0.000	0.000	0.000
59	A	78	ILE	0	-0.106	0.080	17.898	0.007	0.007	0.000	0.000	0.000	0.000
60	A	79	VAL	0	0.089	-0.092	19.607	0.002	0.002	0.000	0.000	0.000	0.000
61	A	79	VAL	0	-0.082	0.103	20.517	0.003	0.003	0.000	0.000	0.000	0.000
62	A	80	GLU	0	0.136	-0.108	22.409	0.012	0.012	0.000	0.000	0.000	0.000
63	A	80	GLU	-1	-0.910	-0.762	25.206	-0.248	-0.248	0.000	0.000	0.000	0.000
64	A	81	LEU	0	0.034	-0.120	25.715	0.001	0.001	0.000	0.000	0.000	0.000
65	A	81	LEU	0	-0.076	0.099	26.237	0.001	0.001	0.000	0.000	0.000	0.000
66	A	82	THR	0	0.094	-0.073	28.734	0.013	0.013	0.000	0.000	0.000	0.000
67	A	82	THR	0	-0.013	0.065	30.012	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	83	PRO	0	0.000	-0.088	30.166	0.014	0.014	0.000	0.000	0.000	0.000
69	A	84	LEU	0	0.007	-0.042	32.289	0.016	0.016	0.000	0.000	0.000	0.000
70	A	84	LEU	0	-0.045	0.115	30.105	0.000	0.000	0.000	0.000	0.000	0.000
71	A	85	GLU	0	0.085	-0.106	33.721	0.004	0.004	0.000	0.000	0.000	0.000
72	A	85	GLU	-1	-0.901	-0.802	32.423	-0.179	-0.179	0.000	0.000	0.000	0.000
73	A	86	GLN	0	0.020	-0.078	35.085	0.004	0.004	0.000	0.000	0.000	0.000
74	A	86	GLN	0	-0.098	0.074	38.339	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	87	LYS	0	0.040	-0.102	37.228	0.009	0.009	0.000	0.000	0.000	0.000
76	A	87	LYS	1	0.806	1.014	35.914	0.140	0.140	0.000	0.000	0.000	0.000
77	A	88	PRO	0	0.143	-0.058	36.999	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	89	GLU	0	0.067	-0.032	36.686	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	89	GLU	-1	-0.885	-0.795	39.275	-0.108	-0.108	0.000	0.000	0.000	0.000
80	A	90	LEU	0	0.087	-0.103	35.595	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	90	LEU	0	-0.116	0.096	33.867	0.001	0.001	0.000	0.000	0.000	0.000
82	A	91	LEU	0	0.091	-0.122	32.557	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	91	LEU	0	-0.104	0.124	31.146	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	92	LYS	0	0.071	-0.110	31.838	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	92	LYS	1	0.769	1.012	34.695	0.139	0.139	0.000	0.000	0.000	0.000
86	A	93	LYS	0	0.135	-0.057	32.411	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	93	LYS	1	0.788	1.030	31.524	0.161	0.161	0.000	0.000	0.000	0.000
88	A	94	ILE	0	0.010	-0.125	29.396	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	94	ILE	0	-0.081	0.092	27.813	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	95	ALA	0	0.158	-0.086	27.709	-0.022	-0.022	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.063	0.110	29.258	0.002	0.002	0.000	0.000	0.000	0.000
92	A	96	GLU	0	0.082	-0.120	27.420	-0.021	-0.021	0.000	0.000	0.000	0.000
93	A	96	GLU	-1	-0.874	-0.760	30.787	-0.146	-0.146	0.000	0.000	0.000	0.000
94	A	97	GLN	0	0.072	-0.111	27.341	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	97	GLN	0	-0.056	0.106	26.866	0.008	0.008	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.045	-0.078	23.630	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.076	0.098	22.463	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	99	MET	0	0.126	-0.094	22.723	-0.039	-0.039	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.082	0.108	25.512	0.005	0.005	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.040	-0.074	23.731	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	100	THR	0	-0.065	0.055	25.255	0.008	0.008	0.000	0.000	0.000	0.000
102	A	101	THR	0	0.006	-0.070	21.603	0.003	0.003	0.000	0.000	0.000	0.000
103	A	101	THR	0	-0.091	0.027	19.453	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.109	-0.081	18.841	-0.026	-0.026	0.000	0.000	0.000	0.000
105	A	102	ALA	0	-0.058	0.112	19.653	0.001	0.001	0.000	0.000	0.000	0.000
106	A	103	SER	0	0.048	-0.083	19.087	-0.034	-0.034	0.000	0.000	0.000	0.000
107	A	103	SER	0	-0.067	0.054	23.242	0.011	0.011	0.000	0.000	0.000	0.000
108	A	104	ILE	0	0.026	-0.071	20.933	0.004	0.004	0.000	0.000	0.000	0.000
109	A	104	ILE	0	-0.111	0.076	20.501	0.004	0.004	0.000	0.000	0.000	0.000
110	A	105	ILE	0	0.001	-0.115	16.962	0.033	0.033	0.000	0.000	0.000	0.000
111	A	105	ILE	0	-0.121	0.070	14.818	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	106	GLY	0	0.021	-0.103	15.909	-0.043	-0.043	0.000	0.000	0.000	0.000
113	A	107	GLY	0	-0.002	0.003	15.817	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	108	ASP	0	0.064	0.015	16.699	0.068	0.068	0.000	0.000	0.000	0.000
115	A	108	ASP	-1	-0.889	-0.795	17.449	-0.409	-0.409	0.000	0.000	0.000	0.000
116	A	109	TYR	0	0.191	-0.092	18.675	-0.042	-0.042	0.000	0.000	0.000	0.000
117	A	109	TYR	0	-0.076	0.095	21.903	0.007	0.007	0.000	0.000	0.000	0.000
118	A	110	ALA	0	0.032	-0.142	21.372	0.028	0.028	0.000	0.000	0.000	0.000
119	A	110	ALA	0	-0.036	0.123	21.945	0.000	0.000	0.000	0.000	0.000	0.000
120	A	111	LYS	0	0.116	-0.053	23.041	-0.030	-0.030	0.000	0.000	0.000	0.000
121	A	111	LYS	1	0.839	1.066	27.247	0.201	0.201	0.000	0.000	0.000	0.000
122	A	112	ILE	0	-0.029	-0.130	23.449	0.009	0.009	0.000	0.000	0.000	0.000
123	A	112	ILE	0	-0.083	0.108	21.312	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	113	CYS	0	0.129	-0.103	24.849	0.007	0.007	0.000	0.000	0.000	0.000
125	A	113	CYS	0	-0.128	0.143	26.937	0.004	0.004	0.000	0.000	0.000	0.000
126	A	114	GLY	0	-0.025	-0.159	27.939	0.000	0.000	0.000	0.000	0.000	0.000
127	A	115	SER	0	0.075	0.019	31.270	0.002	0.002	0.000	0.000	0.000	0.000
128	A	115	SER	0	-0.035	0.100	33.198	0.006	0.006	0.000	0.000	0.000	0.000
129	A	116	PRO	0	0.006	-0.122	28.555	0.000	0.000	0.000	0.000	0.000	0.000
130	A	117	LEU	0	0.166	0.018	29.206	-0.012	-0.012	0.000	0.000	0.000	0.000
131	A	117	LEU	0	-0.102	0.123	29.372	0.001	0.001	0.000	0.000	0.000	0.000
132	A	118	LYS	0	-0.023	-0.129	25.362	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	118	LYS	1	0.790	0.996	24.262	0.279	0.279	0.000	0.000	0.000	0.000
134	A	119	VAL	0	0.060	-0.086	23.847	0.015	0.015	0.000	0.000	0.000	0.000
135	A	119	VAL	0	-0.043	0.117	22.965	0.003	0.003	0.000	0.000	0.000	0.000
136	A	120	ILE	0	0.066	-0.099	19.554	-0.007	-0.007	0.000	0.000	0.000	0.000
137	A	120	ILE	0	-0.094	0.080	16.654	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	121	LEU	0	0.074	-0.098	18.184	0.037	0.037	0.000	0.000	0.000	0.000
139	A	121	LEU	0	-0.085	0.085	17.948	0.008	0.008	0.000	0.000	0.000	0.000
140	A	122	THR	0	-0.079	-0.117	14.325	-0.072	-0.072	0.000	0.000	0.000	0.000
141	A	122	THR	0	0.008	0.061	13.607	0.032	0.032	0.000	0.000	0.000	0.000
142	A	123	PRO	0	0.007	-0.064	10.012	0.142	0.142	0.000	0.000	0.000	0.000
143	A	124	PRO	0	0.070	0.010	11.714	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	125	GLU	0	-0.022	-0.047	8.407	0.230	0.230	0.000	0.000	0.000	0.000
145	A	125	GLU	-1	-0.928	-0.827	7.189	-1.385	-1.385	0.000	0.000	0.000	0.000
146	A	126	ILE	0	0.085	-0.076	9.828	0.011	0.011	0.000	0.000	0.000	0.000
147	A	126	ILE	0	-0.115	0.081	8.093	-0.008	-0.008	0.000	0.000	0.000	0.000
148	A	127	LYS	0	0.117	-0.100	11.459	0.033	0.033	0.000	0.000	0.000	0.000
149	A	127	LYS	1	0.778	1.024	14.378	0.395	0.395	0.000	0.000	0.000	0.000
150	A	128	ILE	0	0.092	-0.107	15.031	-0.027	-0.027	0.000	0.000	0.000	0.000
151	A	128	ILE	0	-0.140	0.093	17.556	0.005	0.005	0.000	0.000	0.000	0.000
152	A	129	ALA	0	0.082	-0.112	17.928	0.036	0.036	0.000	0.000	0.000	0.000
153	A	129	ALA	0	-0.061	0.114	17.925	0.001	0.001	0.000	0.000	0.000	0.000
154	A	130	LYS	0	-0.092	-0.143	19.389	0.004	0.004	0.000	0.000	0.000	0.000
155	A	130	LYS	1	1.015	1.021	22.979	0.233	0.233	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:49:LYS)