FMO DATABASE

FMODB ID: YN4R2

Calculation Name: 1WZ3-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1WZ3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LVK3

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	160
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-460612.31566
FMO2-HF: Nuclear repulsion	428032.808743
FMO2-HF: Total energy	-32579.506917
FMO2-MP2: Total energy	-32674.829379

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:10:GLN)

Summations of interaction energy for fragment #1(A:10:GLN)

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.
-1.296	1.173	-0.017	-1.192	-1.258	0.004

Interaction energy analysis for fragmet #1(A:10:GLN)

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 : 0.040

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	11	LYS	1	0.773	1.050	4.106	-1.550	-1.204	0.003	-0.162	-0.187	0.000
5	A	12	ILE	0	0.071	-0.140	3.798	-1.477	-0.034	-0.014	-0.785	-0.643	0.004
6	A	12	ILE	0	-0.019	0.157	4.335	0.026	0.100	-0.001	-0.009	-0.063	0.000
7	A	13	VAL	0	0.059	-0.115	6.502	0.543	0.543	0.000	0.000	0.000	0.000
8	A	13	VAL	0	-0.078	0.098	8.855	0.055	0.055	0.000	0.000	0.000	0.000
9	A	14	VAL	0	0.083	-0.115	9.947	-0.143	-0.143	0.000	0.000	0.000	0.000
10	A	14	VAL	0	-0.047	0.141	10.390	0.002	0.002	0.000	0.000	0.000	0.000
11	A	15	HIS	0	-0.013	-0.130	12.608	0.118	0.118	0.000	0.000	0.000	0.000
12	A	15	HIS	0	-0.071	0.087	14.578	0.034	0.034	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.097	-0.121	16.230	-0.055	-0.055	0.000	0.000	0.000	0.000
14	A	16	LEU	0	-0.079	0.129	17.056	0.005	0.005	0.000	0.000	0.000	0.000
15	A	17	ARG	0	0.152	-0.073	18.997	0.036	0.036	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.852	1.063	21.154	0.229	0.229	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.076	-0.102	22.159	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.026	0.132	25.848	0.004	0.004	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.077	-0.125	25.560	0.002	0.002	0.000	0.000	0.000	0.000
20	A	19	THR	0	0.013	0.089	25.293	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	20	GLY	0	0.049	-0.074	27.948	0.005	0.005	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.008	0.008	31.408	0.007	0.007	0.000	0.000	0.000	0.000
23	A	22	ALA	0	0.079	0.015	28.772	0.014	0.014	0.000	0.000	0.000	0.000
24	A	22	ALA	0	-0.060	0.103	28.077	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	23	PRO	0	-0.019	-0.108	28.558	0.000	0.000	0.000	0.000	0.000	0.000
26	A	24	ILE	0	0.158	0.007	26.561	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	24	ILE	0	-0.073	0.116	26.087	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	25	LEU	0	0.021	-0.125	23.584	0.017	0.017	0.000	0.000	0.000	0.000
29	A	25	LEU	0	-0.048	0.134	21.989	0.001	0.001	0.000	0.000	0.000	0.000
30	A	26	LYS	0	0.144	-0.066	24.012	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	26	LYS	1	0.883	1.069	24.457	-0.042	-0.042	0.000	0.000	0.000	0.000
32	A	27	GLN	0	0.042	-0.122	20.845	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	27	GLN	0	-0.130	0.104	17.253	0.012	0.012	0.000	0.000	0.000	0.000
34	A	28	SER	0	0.059	-0.112	19.650	0.000	0.000	0.000	0.000	0.000	0.000
35	A	28	SER	0	-0.027	0.097	20.285	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	29	LYS	0	0.047	-0.089	15.973	-0.066	-0.066	0.000	0.000	0.000	0.000
37	A	29	LYS	1	0.867	1.073	15.539	0.133	0.133	0.000	0.000	0.000	0.000
38	A	30	PHE	0	0.076	-0.093	13.306	0.101	0.101	0.000	0.000	0.000	0.000
39	A	30	PHE	0	-0.036	0.103	12.959	0.004	0.004	0.000	0.000	0.000	0.000
40	A	31	LYS	0	0.102	-0.047	9.226	-0.218	-0.218	0.000	0.000	0.000	0.000
41	A	31	LYS	1	0.879	1.037	7.472	-0.072	-0.072	0.000	0.000	0.000	0.000
42	A	32	VAL	0	-0.001	-0.162	8.086	0.480	0.480	0.000	0.000	0.000	0.000
43	A	32	VAL	0	-0.001	0.173	8.458	0.018	0.018	0.000	0.000	0.000	0.000
44	A	33	SER	0	-0.019	-0.111	4.310	-0.901	-0.892	-0.002	-0.026	0.018	0.000
45	A	33	SER	0	0.012	0.110	4.575	0.511	0.568	-0.001	-0.005	-0.050	0.000
46	A	34	GLY	0	0.050	-0.077	3.545	0.004	0.417	0.000	-0.199	-0.214	0.000
47	A	35	SER	0	0.059	0.025	4.595	0.209	0.336	-0.002	-0.006	-0.119	0.000
48	A	35	SER	0	-0.027	0.078	5.536	0.235	0.235	0.000	0.000	0.000	0.000
49	A	36	ASP	0	0.051	-0.128	6.479	0.330	0.330	0.000	0.000	0.000	0.000
50	A	36	ASP	-1	-0.953	-0.838	8.446	0.012	0.012	0.000	0.000	0.000	0.000
51	A	37	LYS	0	0.041	-0.116	9.039	-0.230	-0.230	0.000	0.000	0.000	0.000
52	A	37	LYS	1	0.914	1.108	11.406	0.506	0.506	0.000	0.000	0.000	0.000
53	A	38	PHE	0	0.116	-0.088	12.427	0.055	0.055	0.000	0.000	0.000	0.000
54	A	38	PHE	0	-0.005	0.119	13.916	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	39	ALA	0	0.082	-0.103	14.369	0.025	0.025	0.000	0.000	0.000	0.000
56	A	39	ALA	0	-0.030	0.119	16.439	0.006	0.006	0.000	0.000	0.000	0.000
57	A	40	ASN	0	0.080	-0.082	13.903	0.044	0.044	0.000	0.000	0.000	0.000
58	A	40	ASN	0	-0.117	0.068	11.822	0.004	0.004	0.000	0.000	0.000	0.000
59	A	41	VAL	0	0.086	-0.099	15.032	0.076	0.076	0.000	0.000	0.000	0.000
60	A	41	VAL	0	-0.079	0.096	13.564	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	42	ILE	0	0.084	-0.110	16.094	0.034	0.034	0.000	0.000	0.000	0.000
62	A	42	ILE	0	-0.089	0.099	18.382	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	43	ASP	0	0.080	-0.096	18.783	0.016	0.016	0.000	0.000	0.000	0.000
64	A	43	ASP	-1	-0.903	-0.812	18.734	-0.051	-0.051	0.000	0.000	0.000	0.000
65	A	44	PHE	0	0.071	-0.080	18.315	0.034	0.034	0.000	0.000	0.000	0.000
66	A	44	PHE	0	-0.110	0.057	17.502	0.004	0.004	0.000	0.000	0.000	0.000
67	A	45	LEU	0	0.041	-0.102	19.549	0.032	0.032	0.000	0.000	0.000	0.000
68	A	45	LEU	0	-0.039	0.098	19.905	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	46	ARG	0	0.030	-0.104	21.947	0.012	0.012	0.000	0.000	0.000	0.000
70	A	46	ARG	1	0.769	1.018	22.855	0.108	0.108	0.000	0.000	0.000	0.000
71	A	47	ARG	0	0.138	-0.067	23.151	0.006	0.006	0.000	0.000	0.000	0.000
72	A	47	ARG	1	0.774	1.017	18.324	0.016	0.016	0.000	0.000	0.000	0.000
73	A	48	GLN	0	0.077	-0.082	23.566	0.015	0.015	0.000	0.000	0.000	0.000
74	A	48	GLN	0	-0.168	0.051	22.119	0.012	0.012	0.000	0.000	0.000	0.000
75	A	49	LEU	0	-0.018	-0.116	24.985	0.012	0.012	0.000	0.000	0.000	0.000
76	A	49	LEU	0	-0.068	0.088	25.477	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	50	HIS	0	0.029	-0.084	27.371	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	50	HIS	0	-0.105	0.093	29.494	0.000	0.000	0.000	0.000	0.000	0.000
79	A	51	SER	0	0.149	-0.064	27.934	0.006	0.006	0.000	0.000	0.000	0.000
80	A	51	SER	0	-0.056	0.058	28.695	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	52	ASP	0	0.064	-0.110	27.317	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	52	ASP	-1	-0.912	-0.801	28.069	-0.070	-0.070	0.000	0.000	0.000	0.000
83	A	53	SER	0	-0.037	-0.102	28.276	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	53	SER	0	0.001	0.083	30.633	0.006	0.006	0.000	0.000	0.000	0.000
85	A	54	LEU	0	0.035	-0.128	26.184	0.004	0.004	0.000	0.000	0.000	0.000
86	A	54	LEU	0	-0.059	0.111	24.693	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	55	PHE	0	0.077	-0.083	26.256	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	55	PHE	0	-0.050	0.119	26.751	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	56	VAL	0	0.095	-0.134	21.750	0.009	0.009	0.000	0.000	0.000	0.000
90	A	56	VAL	0	-0.106	0.118	19.812	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	57	TYR	0	0.022	-0.125	21.185	-0.022	-0.022	0.000	0.000	0.000	0.000
92	A	57	TYR	0	-0.078	0.111	22.878	0.004	0.004	0.000	0.000	0.000	0.000
93	A	58	VAL	0	0.079	-0.117	18.222	0.015	0.015	0.000	0.000	0.000	0.000
94	A	58	VAL	0	-0.056	0.114	16.410	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	59	ASN	0	0.110	-0.057	19.543	0.023	0.023	0.000	0.000	0.000	0.000
96	A	59	ASN	0	-0.124	0.049	20.797	0.027	0.027	0.000	0.000	0.000	0.000
97	A	60	SER	0	0.096	-0.085	19.674	-0.062	-0.062	0.000	0.000	0.000	0.000
98	A	60	SER	0	-0.049	0.079	21.448	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	61	ALA	0	0.088	-0.076	21.488	0.035	0.035	0.000	0.000	0.000	0.000
100	A	61	ALA	0	-0.080	0.095	22.202	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	62	PHE	0	-0.030	-0.123	23.448	-0.026	-0.026	0.000	0.000	0.000	0.000
102	A	62	PHE	0	-0.036	0.122	26.175	0.000	0.000	0.000	0.000	0.000	0.000
103	A	63	SER	0	0.043	-0.113	26.384	0.006	0.006	0.000	0.000	0.000	0.000
104	A	63	SER	0	-0.034	0.094	27.583	0.002	0.002	0.000	0.000	0.000	0.000
105	A	64	PRO	0	-0.015	-0.106	29.339	0.005	0.005	0.000	0.000	0.000	0.000
106	A	65	ASN	0	0.156	0.026	32.548	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	65	ASN	0	-0.081	0.106	35.694	0.001	0.001	0.000	0.000	0.000	0.000
108	A	66	PRO	0	-0.047	-0.128	35.374	0.004	0.004	0.000	0.000	0.000	0.000
109	A	67	ASP	0	0.100	-0.006	37.855	0.005	0.005	0.000	0.000	0.000	0.000
110	A	67	ASP	-1	-1.028	-0.862	40.722	-0.122	-0.122	0.000	0.000	0.000	0.000
111	A	68	GLU	0	0.068	-0.084	38.558	0.008	0.008	0.000	0.000	0.000	0.000
112	A	68	GLU	-1	-1.017	-0.867	36.817	-0.162	-0.162	0.000	0.000	0.000	0.000
113	A	69	SER	0	0.020	-0.093	39.879	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	69	SER	0	-0.027	0.075	42.457	0.001	0.001	0.000	0.000	0.000	0.000
115	A	70	VAL	0	0.109	-0.088	39.189	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	70	VAL	0	-0.058	0.094	38.848	0.001	0.001	0.000	0.000	0.000	0.000
117	A	71	ILE	0	0.052	-0.113	39.348	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	71	ILE	0	-0.080	0.111	42.214	0.001	0.001	0.000	0.000	0.000	0.000
119	A	72	ASP	0	0.116	-0.129	40.029	0.000	0.000	0.000	0.000	0.000	0.000
120	A	72	ASP	-1	-0.950	-0.802	39.529	-0.120	-0.120	0.000	0.000	0.000	0.000
121	A	73	LEU	0	0.087	-0.096	35.975	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	73	LEU	0	-0.081	0.103	34.016	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	74	TYR	0	0.076	-0.112	35.358	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	74	TYR	0	-0.121	0.082	37.359	0.000	0.000	0.000	0.000	0.000	0.000
125	A	75	ASN	0	0.065	-0.074	36.768	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	75	ASN	0	-0.104	0.061	39.623	0.003	0.003	0.000	0.000	0.000	0.000
127	A	76	ASN	0	0.037	-0.077	35.271	0.003	0.003	0.000	0.000	0.000	0.000
128	A	76	ASN	0	-0.098	0.073	34.394	0.002	0.002	0.000	0.000	0.000	0.000
129	A	77	PHE	0	0.022	-0.110	32.037	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	77	PHE	0	-0.104	0.077	29.768	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	78	GLY	0	0.023	-0.095	31.964	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	79	PHE	0	0.078	-0.007	32.596	0.001	0.001	0.000	0.000	0.000	0.000
133	A	79	PHE	0	-0.124	0.058	31.763	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	80	ASP	0	-0.005	-0.136	34.056	0.000	0.000	0.000	0.000	0.000	0.000
135	A	80	ASP	-1	-1.022	-0.854	34.601	-0.113	-0.113	0.000	0.000	0.000	0.000
136	A	81	GLY	0	0.053	-0.077	36.234	0.003	0.003	0.000	0.000	0.000	0.000
137	A	82	LYS	0	0.041	0.016	36.533	0.006	0.006	0.000	0.000	0.000	0.000
138	A	82	LYS	1	0.882	1.054	32.373	0.148	0.148	0.000	0.000	0.000	0.000
139	A	83	LEU	0	0.159	-0.115	34.187	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	83	LEU	0	-0.057	0.149	33.090	0.001	0.001	0.000	0.000	0.000	0.000
141	A	84	VAL	0	0.001	-0.132	30.469	0.009	0.009	0.000	0.000	0.000	0.000
142	A	84	VAL	0	-0.092	0.093	28.753	0.000	0.000	0.000	0.000	0.000	0.000
143	A	85	VAL	0	0.066	-0.111	30.696	-0.014	-0.014	0.000	0.000	0.000	0.000
144	A	85	VAL	0	-0.026	0.139	31.713	0.001	0.001	0.000	0.000	0.000	0.000
145	A	86	ASN	0	0.059	-0.089	26.786	0.013	0.013	0.000	0.000	0.000	0.000
146	A	86	ASN	0	-0.107	0.058	26.165	0.000	0.000	0.000	0.000	0.000	0.000
147	A	87	TYR	0	0.084	-0.079	27.981	-0.004	-0.004	0.000	0.000	0.000	0.000
148	A	87	TYR	0	-0.056	0.108	29.897	0.003	0.003	0.000	0.000	0.000	0.000
149	A	88	ALA	0	0.057	-0.140	24.779	0.009	0.009	0.000	0.000	0.000	0.000
150	A	88	ALA	0	-0.052	0.125	24.095	-0.007	-0.007	0.000	0.000	0.000	0.000
151	A	89	CYS	0	0.045	-0.099	25.531	0.005	0.005	0.000	0.000	0.000	0.000
152	A	89	CYS	0	-0.076	0.091	25.401	0.007	0.007	0.000	0.000	0.000	0.000
153	A	90	SER	0	0.092	-0.058	21.697	0.006	0.006	0.000	0.000	0.000	0.000
154	A	90	SER	0	-0.046	0.066	19.997	-0.014	-0.014	0.000	0.000	0.000	0.000
155	A	91	MET	0	0.065	-0.123	20.359	0.016	0.016	0.000	0.000	0.000	0.000
156	A	91	MET	0	-0.078	0.127	19.963	0.008	0.008	0.000	0.000	0.000	0.000
157	A	92	ALA	0	0.075	-0.094	16.480	-0.036	-0.036	0.000	0.000	0.000	0.000
158	A	92	ALA	0	-0.092	0.103	15.569	-0.007	-0.007	0.000	0.000	0.000	0.000
159	A	93	TRP	0	-0.076	-0.135	14.700	-0.056	-0.056	0.000	0.000	0.000	0.000
160	A	93	TRP	0	0.064	0.035	18.170	0.002	0.002	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:10:GLN)