FMO DATABASE

FMODB ID: 37VYL

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

Total energy (hartree)

FMO2-HF: Electronic energy	-525975.534057
FMO2-HF: Nuclear repulsion	495020.807899
FMO2-HF: Total energy	-30954.726158
FMO2-MP2: Total energy	-31045.841361

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.
-4.647	-2.435	-0.006	-1.18	-1.026	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 : 0.155 / q_NPA : 0.032

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	-0.078	0.103	4.046	-0.032	0.329	0.001	-0.141	-0.222	0.000
5	A	51	VAL	0	0.066	-0.127	3.857	-2.562	-0.776	-0.006	-1.028	-0.752	0.006
6	A	51	VAL	0	-0.065	0.135	4.194	0.026	0.091	-0.001	-0.011	-0.052	0.000
7	A	52	TYR	0	0.059	-0.086	6.268	0.507	0.507	0.000	0.000	0.000	0.000
8	A	52	TYR	0	-0.108	0.076	7.448	0.099	0.099	0.000	0.000	0.000	0.000
9	A	53	ILE	0	0.121	-0.084	9.924	-0.065	-0.065	0.000	0.000	0.000	0.000
10	A	53	ILE	0	-0.085	0.099	12.322	0.024	0.024	0.000	0.000	0.000	0.000
11	A	54	LYS	0	0.099	-0.099	13.299	0.113	0.113	0.000	0.000	0.000	0.000
12	A	54	LYS	1	0.737	1.001	11.967	0.893	0.893	0.000	0.000	0.000	0.000
13	A	55	LYS	0	0.070	-0.080	15.356	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	55	LYS	1	0.849	1.047	18.658	0.474	0.474	0.000	0.000	0.000	0.000
15	A	56	ILE	0	0.020	-0.128	19.082	0.021	0.021	0.000	0.000	0.000	0.000
16	A	56	ILE	0	-0.054	0.110	17.786	0.003	0.003	0.000	0.000	0.000	0.000
17	A	57	VAL	0	0.073	-0.101	21.327	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	57	VAL	0	-0.040	0.114	25.106	0.002	0.002	0.000	0.000	0.000	0.000
19	A	58	ILE	0	0.021	-0.133	25.108	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	58	ILE	0	-0.060	0.118	23.243	0.000	0.000	0.000	0.000	0.000	0.000
21	A	59	SER	0	0.012	-0.097	26.529	0.010	0.010	0.000	0.000	0.000	0.000
22	A	59	SER	0	-0.018	0.075	28.375	0.006	0.006	0.000	0.000	0.000	0.000
23	A	60	THR	0	-0.038	-0.116	28.512	0.017	0.017	0.000	0.000	0.000	0.000
24	A	60	THR	0	-0.027	0.074	28.080	0.001	0.001	0.000	0.000	0.000	0.000
25	A	61	HIS	0	0.160	-0.052	28.035	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	61	HIS	0	-0.057	0.093	29.637	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	62	ALA	0	0.088	-0.114	26.261	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	62	ALA	0	-0.058	0.126	26.221	0.003	0.003	0.000	0.000	0.000	0.000
29	A	63	ASP	0	0.006	-0.118	23.759	-0.019	-0.019	0.000	0.000	0.000	0.000
30	A	63	ASP	-1	-0.762	-0.726	24.330	-0.253	-0.253	0.000	0.000	0.000	0.000
31	A	64	LEU	0	0.106	-0.116	22.233	-0.042	-0.042	0.000	0.000	0.000	0.000
32	A	64	LEU	0	-0.042	0.128	23.950	0.001	0.001	0.000	0.000	0.000	0.000
33	A	65	LYS	0	0.086	-0.065	21.158	-0.040	-0.040	0.000	0.000	0.000	0.000
34	A	65	LYS	1	0.802	0.998	19.736	0.307	0.307	0.000	0.000	0.000	0.000
35	A	66	ARG	0	0.067	-0.081	19.104	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	66	ARG	1	0.800	0.995	19.719	0.326	0.326	0.000	0.000	0.000	0.000
37	A	67	VAL	0	0.087	-0.091	17.380	-0.066	-0.066	0.000	0.000	0.000	0.000
38	A	67	VAL	0	-0.077	0.093	18.015	0.001	0.001	0.000	0.000	0.000	0.000
39	A	68	SER	0	0.168	-0.043	16.316	-0.091	-0.091	0.000	0.000	0.000	0.000
40	A	68	SER	0	-0.066	0.069	19.093	0.007	0.007	0.000	0.000	0.000	0.000
41	A	69	ASP	0	0.036	-0.112	15.568	-0.046	-0.046	0.000	0.000	0.000	0.000
42	A	69	ASP	-1	-0.913	-0.785	15.893	-0.362	-0.362	0.000	0.000	0.000	0.000
43	A	70	GLU	0	0.084	-0.080	12.680	-0.062	-0.062	0.000	0.000	0.000	0.000
44	A	70	GLU	-1	-0.836	-0.772	12.464	-0.896	-0.896	0.000	0.000	0.000	0.000
45	A	71	LEU	0	0.084	-0.091	11.300	-0.253	-0.253	0.000	0.000	0.000	0.000
46	A	71	LEU	0	-0.072	0.099	13.443	0.031	0.031	0.000	0.000	0.000	0.000
47	A	72	LYS	0	0.062	-0.087	11.369	-0.169	-0.169	0.000	0.000	0.000	0.000
48	A	72	LYS	1	0.782	1.011	13.363	0.490	0.490	0.000	0.000	0.000	0.000
49	A	73	SER	0	0.005	-0.095	9.485	0.036	0.036	0.000	0.000	0.000	0.000
50	A	73	SER	0	-0.077	0.062	9.197	0.059	0.059	0.000	0.000	0.000	0.000
51	A	74	GLY	0	-0.018	-0.100	6.821	-0.525	-0.525	0.000	0.000	0.000	0.000
52	A	75	ASN	0	0.076	0.035	7.293	-0.617	-0.617	0.000	0.000	0.000	0.000
53	A	75	ASN	0	-0.111	0.035	8.374	-0.326	-0.326	0.000	0.000	0.000	0.000
54	A	76	ILE	0	0.167	-0.073	9.606	0.173	0.173	0.000	0.000	0.000	0.000
55	A	76	ILE	0	-0.095	0.092	10.738	0.017	0.017	0.000	0.000	0.000	0.000
56	A	77	VAL	0	-0.008	-0.131	12.477	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	77	VAL	0	-0.104	0.108	14.286	0.014	0.014	0.000	0.000	0.000	0.000
58	A	78	ILE	0	0.129	-0.080	15.844	0.041	0.041	0.000	0.000	0.000	0.000
59	A	78	ILE	0	-0.094	0.085	17.401	0.007	0.007	0.000	0.000	0.000	0.000
60	A	79	VAL	0	0.091	-0.093	18.993	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	79	VAL	0	-0.089	0.099	19.681	0.003	0.003	0.000	0.000	0.000	0.000
62	A	80	GLU	0	0.118	-0.104	21.862	0.009	0.009	0.000	0.000	0.000	0.000
63	A	80	GLU	-1	-0.904	-0.767	24.870	-0.271	-0.271	0.000	0.000	0.000	0.000
64	A	81	LEU	0	0.052	-0.102	25.427	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	81	LEU	0	-0.063	0.099	26.019	0.002	0.002	0.000	0.000	0.000	0.000
66	A	82	THR	0	0.068	-0.063	28.618	0.016	0.016	0.000	0.000	0.000	0.000
67	A	82	THR	0	-0.028	0.063	29.500	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	83	PRO	0	0.016	-0.112	29.872	0.014	0.014	0.000	0.000	0.000	0.000
69	A	84	LEU	0	0.011	-0.036	32.143	0.016	0.016	0.000	0.000	0.000	0.000
70	A	84	LEU	0	-0.048	0.105	29.448	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	85	GLU	0	0.101	-0.094	33.303	0.005	0.005	0.000	0.000	0.000	0.000
72	A	85	GLU	-1	-0.895	-0.804	32.109	-0.195	-0.195	0.000	0.000	0.000	0.000
73	A	86	GLN	0	0.026	-0.082	34.620	0.004	0.004	0.000	0.000	0.000	0.000
74	A	86	GLN	0	-0.081	0.084	37.704	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	87	LYS	0	0.026	-0.090	36.692	0.010	0.010	0.000	0.000	0.000	0.000
76	A	87	LYS	1	0.804	1.011	35.365	0.151	0.151	0.000	0.000	0.000	0.000
77	A	88	PRO	0	0.136	-0.067	36.296	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	89	GLU	0	0.054	-0.025	36.009	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	89	GLU	-1	-0.888	-0.800	38.701	-0.120	-0.120	0.000	0.000	0.000	0.000
80	A	90	LEU	0	0.109	-0.098	34.802	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	90	LEU	0	-0.117	0.095	33.050	0.001	0.001	0.000	0.000	0.000	0.000
82	A	91	LEU	0	0.108	-0.114	31.965	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	91	LEU	0	-0.126	0.117	30.839	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	92	LYS	0	0.084	-0.096	31.104	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	92	LYS	1	0.742	0.999	33.855	0.154	0.154	0.000	0.000	0.000	0.000
86	A	93	LYS	0	0.145	-0.060	31.291	-0.012	-0.012	0.000	0.000	0.000	0.000
87	A	93	LYS	1	0.780	1.024	30.692	0.178	0.178	0.000	0.000	0.000	0.000
88	A	94	ILE	0	0.000	-0.130	28.728	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	94	ILE	0	-0.091	0.087	27.207	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	95	ALA	0	0.167	-0.082	27.045	-0.025	-0.025	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.073	0.109	28.467	0.002	0.002	0.000	0.000	0.000	0.000
92	A	96	GLU	0	0.084	-0.115	26.628	-0.025	-0.025	0.000	0.000	0.000	0.000
93	A	96	GLU	-1	-0.867	-0.759	29.960	-0.162	-0.162	0.000	0.000	0.000	0.000
94	A	97	GLN	0	0.086	-0.093	26.448	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	97	GLN	0	-0.041	0.113	26.007	0.008	0.008	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.050	-0.079	22.794	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.076	0.093	21.840	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	99	MET	0	0.116	-0.097	22.036	-0.044	-0.044	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.097	0.101	24.914	0.005	0.005	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.054	-0.067	22.885	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	100	THR	0	-0.070	0.045	24.290	0.009	0.009	0.000	0.000	0.000	0.000
102	A	101	THR	0	0.024	-0.060	20.836	0.003	0.003	0.000	0.000	0.000	0.000
103	A	101	THR	0	-0.119	0.014	18.727	0.000	0.000	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.120	-0.073	17.873	-0.036	-0.036	0.000	0.000	0.000	0.000
105	A	102	ALA	0	-0.079	0.099	18.817	0.002	0.002	0.000	0.000	0.000	0.000
106	A	103	SER	0	0.052	-0.088	18.169	-0.041	-0.041	0.000	0.000	0.000	0.000
107	A	103	SER	0	-0.076	0.044	22.375	0.012	0.012	0.000	0.000	0.000	0.000
108	A	104	ILE	0	0.006	-0.083	20.119	0.003	0.003	0.000	0.000	0.000	0.000
109	A	104	ILE	0	-0.104	0.081	19.887	0.006	0.006	0.000	0.000	0.000	0.000
110	A	105	ILE	0	0.016	-0.103	16.039	0.042	0.042	0.000	0.000	0.000	0.000
111	A	105	ILE	0	-0.113	0.082	14.032	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	106	GLY	0	0.018	-0.100	15.052	-0.049	-0.049	0.000	0.000	0.000	0.000
113	A	107	GLY	0	-0.010	0.000	15.364	-0.034	-0.034	0.000	0.000	0.000	0.000
114	A	108	ASP	0	0.089	0.006	16.031	0.076	0.076	0.000	0.000	0.000	0.000
115	A	108	ASP	-1	-0.899	-0.793	17.729	-0.469	-0.469	0.000	0.000	0.000	0.000
116	A	109	TYR	0	0.174	-0.094	18.252	-0.056	-0.056	0.000	0.000	0.000	0.000
117	A	109	TYR	0	-0.079	0.099	21.238	0.008	0.008	0.000	0.000	0.000	0.000
118	A	110	ALA	0	0.025	-0.131	20.983	0.034	0.034	0.000	0.000	0.000	0.000
119	A	110	ALA	0	-0.047	0.119	22.010	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	111	LYS	0	0.123	-0.067	23.006	-0.027	-0.027	0.000	0.000	0.000	0.000
121	A	111	LYS	1	0.839	1.063	27.146	0.223	0.223	0.000	0.000	0.000	0.000
122	A	112	ILE	0	-0.021	-0.127	23.507	0.008	0.008	0.000	0.000	0.000	0.000
123	A	112	ILE	0	-0.077	0.107	21.205	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	113	CYS	0	0.100	-0.118	24.919	0.008	0.008	0.000	0.000	0.000	0.000
125	A	113	CYS	0	-0.113	0.127	26.911	0.004	0.004	0.000	0.000	0.000	0.000
126	A	114	GLY	0	-0.026	-0.139	27.994	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	115	SER	0	0.083	0.027	31.156	0.005	0.005	0.000	0.000	0.000	0.000
128	A	115	SER	0	-0.031	0.100	33.307	0.006	0.006	0.000	0.000	0.000	0.000
129	A	116	PRO	0	0.002	-0.112	28.429	0.001	0.001	0.000	0.000	0.000	0.000
130	A	117	LEU	0	0.134	0.007	29.097	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	117	LEU	0	-0.106	0.112	29.137	0.002	0.002	0.000	0.000	0.000	0.000
132	A	118	LYS	0	-0.011	-0.123	25.215	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	118	LYS	1	0.806	0.999	24.124	0.301	0.301	0.000	0.000	0.000	0.000
134	A	119	VAL	0	0.041	-0.087	23.453	0.019	0.019	0.000	0.000	0.000	0.000
135	A	119	VAL	0	-0.038	0.107	22.389	0.003	0.003	0.000	0.000	0.000	0.000
136	A	120	ILE	0	0.073	-0.091	19.294	-0.007	-0.007	0.000	0.000	0.000	0.000
137	A	120	ILE	0	-0.076	0.088	16.540	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	121	LEU	0	0.068	-0.095	17.566	0.051	0.051	0.000	0.000	0.000	0.000
139	A	121	LEU	0	-0.077	0.087	17.316	0.008	0.008	0.000	0.000	0.000	0.000
140	A	122	THR	0	-0.071	-0.105	13.705	-0.074	-0.074	0.000	0.000	0.000	0.000
141	A	122	THR	0	-0.002	0.062	13.412	0.047	0.047	0.000	0.000	0.000	0.000
142	A	123	PRO	0	0.032	-0.067	9.200	0.142	0.142	0.000	0.000	0.000	0.000
143	A	124	PRO	0	0.054	0.014	10.732	0.010	0.010	0.000	0.000	0.000	0.000
144	A	125	GLU	0	0.005	-0.029	7.894	0.318	0.318	0.000	0.000	0.000	0.000
145	A	125	GLU	-1	-0.884	-0.819	6.077	-2.795	-2.795	0.000	0.000	0.000	0.000
146	A	126	ILE	0	0.059	-0.087	9.422	0.020	0.020	0.000	0.000	0.000	0.000
147	A	126	ILE	0	-0.081	0.084	8.125	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	127	LYS	0	0.102	-0.092	11.496	0.027	0.027	0.000	0.000	0.000	0.000
149	A	127	LYS	1	0.794	1.020	14.471	0.465	0.465	0.000	0.000	0.000	0.000
150	A	128	ILE	0	0.073	-0.104	15.250	-0.028	-0.028	0.000	0.000	0.000	0.000
151	A	128	ILE	0	-0.123	0.091	17.687	0.006	0.006	0.000	0.000	0.000	0.000
152	A	129	ALA	0	0.108	-0.108	17.990	0.044	0.044	0.000	0.000	0.000	0.000
153	A	129	ALA	0	-0.061	0.120	18.045	0.001	0.001	0.000	0.000	0.000	0.000
154	A	130	LYS	0	-0.120	-0.152	19.529	0.011	0.011	0.000	0.000	0.000	0.000
155	A	130	LYS	1	1.030	1.028	22.876	0.273	0.273	0.000	0.000	0.000	0.000

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