FMO DATABASE

FMODB ID: L7389

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	OptH
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	-523636.01475
FMO2-HF: Nuclear repulsion	492683.001769
FMO2-HF: Total energy	-30953.012982
FMO2-MP2: Total energy	-31044.134377

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.
-3.194	-0.453	-0.01	-1.49	-1.241	0.006

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 : 0.170 / q_NPA : 0.046

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	-0.074	0.122	3.802	-0.229	0.313	0.006	-0.227	-0.321	0.001
5	A	51	VAL	0	0.084	-0.098	3.817	-2.365	-0.166	-0.016	-1.263	-0.920	0.005
6	A	51	VAL	0	-0.039	0.139	5.129	0.055	0.055	0.000	0.000	0.000	0.000
7	A	52	TYR	0	0.058	-0.105	6.620	0.370	0.370	0.000	0.000	0.000	0.000
8	A	52	TYR	0	-0.108	0.090	7.909	0.104	0.104	0.000	0.000	0.000	0.000
9	A	53	ILE	0	0.147	-0.095	10.127	-0.018	-0.018	0.000	0.000	0.000	0.000
10	A	53	ILE	0	-0.095	0.113	12.543	0.024	0.024	0.000	0.000	0.000	0.000
11	A	54	LYS	0	0.044	-0.126	13.502	0.074	0.074	0.000	0.000	0.000	0.000
12	A	54	LYS	1	0.859	1.084	12.422	0.754	0.754	0.000	0.000	0.000	0.000
13	A	55	LYS	0	0.054	-0.065	15.702	0.000	0.000	0.000	0.000	0.000	0.000
14	A	55	LYS	1	0.877	1.053	18.866	0.441	0.441	0.000	0.000	0.000	0.000
15	A	56	ILE	0	0.009	-0.142	19.437	0.003	0.003	0.000	0.000	0.000	0.000
16	A	56	ILE	0	-0.028	0.121	18.285	0.003	0.003	0.000	0.000	0.000	0.000
17	A	57	VAL	0	0.078	-0.115	21.630	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	57	VAL	0	-0.053	0.131	25.051	0.001	0.001	0.000	0.000	0.000	0.000
19	A	58	ILE	0	0.046	-0.133	25.392	0.002	0.002	0.000	0.000	0.000	0.000
20	A	58	ILE	0	-0.058	0.139	23.986	0.000	0.000	0.000	0.000	0.000	0.000
21	A	59	SER	0	-0.011	-0.061	26.901	0.009	0.009	0.000	0.000	0.000	0.000
22	A	59	SER	0	-0.034	0.053	28.793	0.005	0.005	0.000	0.000	0.000	0.000
23	A	60	THR	0	0.023	-0.093	29.313	0.013	0.013	0.000	0.000	0.000	0.000
24	A	60	THR	0	-0.038	0.069	28.636	0.002	0.002	0.000	0.000	0.000	0.000
25	A	61	HIS	0	0.172	-0.062	28.823	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	61	HIS	0	-0.077	0.083	29.389	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	62	ALA	0	0.096	-0.114	27.038	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	62	ALA	0	-0.060	0.134	26.758	0.002	0.002	0.000	0.000	0.000	0.000
29	A	63	ASP	0	-0.012	-0.143	24.265	-0.017	-0.017	0.000	0.000	0.000	0.000
30	A	63	ASP	-1	-0.817	-0.779	24.699	-0.237	-0.237	0.000	0.000	0.000	0.000
31	A	64	LEU	0	0.102	-0.123	22.945	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	64	LEU	0	-0.041	0.134	24.679	0.001	0.001	0.000	0.000	0.000	0.000
33	A	65	LYS	0	0.102	-0.079	21.847	-0.028	-0.028	0.000	0.000	0.000	0.000
34	A	65	LYS	1	0.876	1.065	21.088	0.270	0.270	0.000	0.000	0.000	0.000
35	A	66	ARG	0	0.091	-0.064	19.628	-0.029	-0.029	0.000	0.000	0.000	0.000
36	A	66	ARG	1	0.810	1.028	20.189	0.314	0.314	0.000	0.000	0.000	0.000
37	A	67	VAL	0	0.086	-0.089	17.939	-0.058	-0.058	0.000	0.000	0.000	0.000
38	A	67	VAL	0	-0.057	0.096	18.674	0.002	0.002	0.000	0.000	0.000	0.000
39	A	68	SER	0	0.077	-0.060	16.951	-0.076	-0.076	0.000	0.000	0.000	0.000
40	A	68	SER	0	-0.071	0.060	19.276	0.014	0.014	0.000	0.000	0.000	0.000
41	A	69	ASP	0	0.086	-0.124	16.145	-0.048	-0.048	0.000	0.000	0.000	0.000
42	A	69	ASP	-1	-1.019	-0.847	16.351	-0.357	-0.357	0.000	0.000	0.000	0.000
43	A	70	GLU	0	0.062	-0.105	13.332	-0.062	-0.062	0.000	0.000	0.000	0.000
44	A	70	GLU	-1	-0.935	-0.830	13.360	-0.781	-0.781	0.000	0.000	0.000	0.000
45	A	71	LEU	0	0.080	-0.106	11.920	-0.204	-0.204	0.000	0.000	0.000	0.000
46	A	71	LEU	0	-0.077	0.096	13.992	0.025	0.025	0.000	0.000	0.000	0.000
47	A	72	LYS	0	0.059	-0.084	11.933	-0.119	-0.119	0.000	0.000	0.000	0.000
48	A	72	LYS	1	0.855	1.048	13.759	0.397	0.397	0.000	0.000	0.000	0.000
49	A	73	SER	0	-0.019	-0.111	9.933	0.015	0.015	0.000	0.000	0.000	0.000
50	A	73	SER	0	-0.070	0.073	9.569	0.035	0.035	0.000	0.000	0.000	0.000
51	A	74	GLY	0	-0.009	-0.086	7.459	-0.411	-0.411	0.000	0.000	0.000	0.000
52	A	75	ASN	0	0.070	0.007	8.365	-0.343	-0.343	0.000	0.000	0.000	0.000
53	A	75	ASN	0	-0.117	0.049	8.894	-0.304	-0.304	0.000	0.000	0.000	0.000
54	A	76	ILE	0	0.199	-0.081	10.216	0.132	0.132	0.000	0.000	0.000	0.000
55	A	76	ILE	0	-0.116	0.103	11.225	0.012	0.012	0.000	0.000	0.000	0.000
56	A	77	VAL	0	-0.016	-0.130	13.114	-0.021	-0.021	0.000	0.000	0.000	0.000
57	A	77	VAL	0	-0.072	0.113	15.228	0.012	0.012	0.000	0.000	0.000	0.000
58	A	78	ILE	0	0.124	-0.094	16.507	0.033	0.033	0.000	0.000	0.000	0.000
59	A	78	ILE	0	-0.121	0.091	18.019	0.008	0.008	0.000	0.000	0.000	0.000
60	A	79	VAL	0	0.063	-0.100	19.609	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	79	VAL	0	-0.068	0.101	20.524	0.002	0.002	0.000	0.000	0.000	0.000
62	A	80	GLU	0	0.130	-0.127	22.410	0.012	0.012	0.000	0.000	0.000	0.000
63	A	80	GLU	-1	-0.980	-0.792	25.270	-0.247	-0.247	0.000	0.000	0.000	0.000
64	A	81	LEU	0	0.047	-0.130	25.708	0.000	0.000	0.000	0.000	0.000	0.000
65	A	81	LEU	0	-0.086	0.106	26.342	0.002	0.002	0.000	0.000	0.000	0.000
66	A	82	THR	0	0.074	-0.082	28.732	0.013	0.013	0.000	0.000	0.000	0.000
67	A	82	THR	0	-0.061	0.054	30.103	0.000	0.000	0.000	0.000	0.000	0.000
68	A	83	PRO	0	-0.010	-0.103	30.049	0.014	0.014	0.000	0.000	0.000	0.000
69	A	84	LEU	0	-0.001	-0.059	32.281	0.014	0.014	0.000	0.000	0.000	0.000
70	A	84	LEU	0	-0.052	0.117	30.153	0.000	0.000	0.000	0.000	0.000	0.000
71	A	85	GLU	0	0.076	-0.127	33.719	0.005	0.005	0.000	0.000	0.000	0.000
72	A	85	GLU	-1	-0.919	-0.788	32.768	-0.175	-0.175	0.000	0.000	0.000	0.000
73	A	86	GLN	0	0.005	-0.087	35.087	0.004	0.004	0.000	0.000	0.000	0.000
74	A	86	GLN	0	-0.089	0.082	38.856	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	87	LYS	0	0.075	-0.102	37.222	0.009	0.009	0.000	0.000	0.000	0.000
76	A	87	LYS	1	0.851	1.062	36.564	0.131	0.131	0.000	0.000	0.000	0.000
77	A	88	PRO	0	0.135	-0.062	37.009	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	89	GLU	0	0.086	-0.026	36.707	-0.009	-0.009	0.000	0.000	0.000	0.000
79	A	89	GLU	-1	-0.929	-0.810	39.260	-0.103	-0.103	0.000	0.000	0.000	0.000
80	A	90	LEU	0	0.098	-0.112	35.611	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	90	LEU	0	-0.127	0.102	33.756	0.001	0.001	0.000	0.000	0.000	0.000
82	A	91	LEU	0	0.096	-0.118	32.568	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	91	LEU	0	-0.105	0.117	31.198	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	92	LYS	0	0.096	-0.107	31.860	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	92	LYS	1	0.848	1.082	34.751	0.135	0.135	0.000	0.000	0.000	0.000
86	A	93	LYS	0	0.131	-0.068	32.442	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	93	LYS	1	0.852	1.059	32.394	0.143	0.143	0.000	0.000	0.000	0.000
88	A	94	ILE	0	0.039	-0.127	29.405	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	94	ILE	0	-0.065	0.112	27.765	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	95	ALA	0	0.111	-0.075	27.732	-0.021	-0.021	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.058	0.098	29.277	0.002	0.002	0.000	0.000	0.000	0.000
92	A	96	GLU	0	0.062	-0.149	27.456	-0.020	-0.020	0.000	0.000	0.000	0.000
93	A	96	GLU	-1	-0.979	-0.820	30.746	-0.141	-0.141	0.000	0.000	0.000	0.000
94	A	97	GLN	0	0.087	-0.116	27.372	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	97	GLN	0	-0.106	0.103	26.872	0.002	0.002	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.066	-0.127	23.652	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.083	0.117	22.529	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	99	MET	0	0.107	-0.082	22.761	-0.038	-0.038	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.093	0.101	25.546	0.005	0.005	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.043	-0.075	23.789	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	100	THR	0	-0.058	0.065	25.160	0.008	0.008	0.000	0.000	0.000	0.000
102	A	101	THR	0	0.011	-0.086	21.614	0.006	0.006	0.000	0.000	0.000	0.000
103	A	101	THR	0	-0.080	0.040	19.515	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.109	-0.086	18.893	-0.024	-0.024	0.000	0.000	0.000	0.000
105	A	102	ALA	0	-0.061	0.122	19.641	0.001	0.001	0.000	0.000	0.000	0.000
106	A	103	SER	0	0.075	-0.077	19.149	-0.030	-0.030	0.000	0.000	0.000	0.000
107	A	103	SER	0	-0.071	0.075	23.291	0.011	0.011	0.000	0.000	0.000	0.000
108	A	104	ILE	0	0.003	-0.112	21.003	0.008	0.008	0.000	0.000	0.000	0.000
109	A	104	ILE	0	-0.107	0.092	20.288	0.003	0.003	0.000	0.000	0.000	0.000
110	A	105	ILE	0	-0.037	-0.103	16.979	0.034	0.034	0.000	0.000	0.000	0.000
111	A	105	ILE	0	-0.111	0.073	15.040	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	106	GLY	0	0.045	-0.102	15.978	-0.037	-0.037	0.000	0.000	0.000	0.000
113	A	107	GLY	0	-0.011	-0.003	15.834	-0.021	-0.021	0.000	0.000	0.000	0.000
114	A	108	ASP	0	0.117	-0.002	16.714	0.066	0.066	0.000	0.000	0.000	0.000
115	A	108	ASP	-1	-0.980	-0.852	17.126	-0.370	-0.370	0.000	0.000	0.000	0.000
116	A	109	TYR	0	0.163	-0.104	18.679	-0.042	-0.042	0.000	0.000	0.000	0.000
117	A	109	TYR	0	-0.094	0.096	21.908	0.007	0.007	0.000	0.000	0.000	0.000
118	A	110	ALA	0	0.048	-0.153	21.371	0.028	0.028	0.000	0.000	0.000	0.000
119	A	110	ALA	0	-0.064	0.137	21.983	0.000	0.000	0.000	0.000	0.000	0.000
120	A	111	LYS	0	0.136	-0.064	23.027	-0.029	-0.029	0.000	0.000	0.000	0.000
121	A	111	LYS	1	0.843	1.071	27.227	0.195	0.195	0.000	0.000	0.000	0.000
122	A	112	ILE	0	-0.039	-0.135	23.449	0.009	0.009	0.000	0.000	0.000	0.000
123	A	112	ILE	0	-0.078	0.107	21.350	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	113	CYS	0	0.052	-0.120	24.825	0.007	0.007	0.000	0.000	0.000	0.000
125	A	113	CYS	0	-0.104	0.120	26.954	0.002	0.002	0.000	0.000	0.000	0.000
126	A	114	GLY	0	0.005	-0.135	27.912	0.000	0.000	0.000	0.000	0.000	0.000
127	A	115	SER	0	0.076	0.021	31.277	0.001	0.001	0.000	0.000	0.000	0.000
128	A	115	SER	0	-0.032	0.106	33.170	0.006	0.006	0.000	0.000	0.000	0.000
129	A	116	PRO	0	0.021	-0.112	28.557	0.000	0.000	0.000	0.000	0.000	0.000
130	A	117	LEU	0	0.186	0.021	29.182	-0.012	-0.012	0.000	0.000	0.000	0.000
131	A	117	LEU	0	-0.106	0.133	29.350	0.001	0.001	0.000	0.000	0.000	0.000
132	A	118	LYS	0	-0.006	-0.116	25.351	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	118	LYS	1	0.877	1.051	24.276	0.289	0.289	0.000	0.000	0.000	0.000
134	A	119	VAL	0	0.081	-0.122	23.870	0.015	0.015	0.000	0.000	0.000	0.000
135	A	119	VAL	0	-0.045	0.148	22.843	0.003	0.003	0.000	0.000	0.000	0.000
136	A	120	ILE	0	0.055	-0.119	19.549	-0.008	-0.008	0.000	0.000	0.000	0.000
137	A	120	ILE	0	-0.100	0.093	16.602	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	121	LEU	0	0.057	-0.095	18.220	0.038	0.038	0.000	0.000	0.000	0.000
139	A	121	LEU	0	-0.082	0.088	17.975	0.007	0.007	0.000	0.000	0.000	0.000
140	A	122	THR	0	-0.039	-0.111	14.342	-0.079	-0.079	0.000	0.000	0.000	0.000
141	A	122	THR	0	0.013	0.081	13.624	0.031	0.031	0.000	0.000	0.000	0.000
142	A	123	PRO	0	-0.015	-0.066	10.191	0.135	0.135	0.000	0.000	0.000	0.000
143	A	124	PRO	0	0.072	0.014	11.755	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	125	GLU	0	-0.022	-0.046	8.426	0.213	0.213	0.000	0.000	0.000	0.000
145	A	125	GLU	-1	-0.937	-0.831	7.243	-1.270	-1.270	0.000	0.000	0.000	0.000
146	A	126	ILE	0	0.073	-0.098	9.832	0.009	0.009	0.000	0.000	0.000	0.000
147	A	126	ILE	0	-0.105	0.094	8.385	-0.005	-0.005	0.000	0.000	0.000	0.000
148	A	127	LYS	0	0.128	-0.098	11.456	0.036	0.036	0.000	0.000	0.000	0.000
149	A	127	LYS	1	0.865	1.083	14.246	0.327	0.327	0.000	0.000	0.000	0.000
150	A	128	ILE	0	0.082	-0.110	15.027	-0.031	-0.031	0.000	0.000	0.000	0.000
151	A	128	ILE	0	-0.115	0.121	17.643	0.004	0.004	0.000	0.000	0.000	0.000
152	A	129	ALA	0	0.052	-0.125	17.931	0.037	0.037	0.000	0.000	0.000	0.000
153	A	129	ALA	0	-0.046	0.117	17.952	0.002	0.002	0.000	0.000	0.000	0.000
154	A	130	LYS	0	-0.091	-0.141	19.374	0.002	0.002	0.000	0.000	0.000	0.000
155	A	130	LYS	1	1.016	1.025	22.869	0.227	0.227	0.000	0.000	0.000	0.000

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