FMO DATABASE

FMODB ID: VY1R1

Calculation Name: 5WEZ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5WEZ

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-06

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	129
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1080912.561409
FMO2-HF: Nuclear repulsion	1029389.749142
FMO2-HF: Total energy	-51522.812267
FMO2-MP2: Total energy	-51670.931513

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:1:ALA)

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

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.
-175.741	-174.391	-0.012	-0.421	-0.917	-0.003

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.787 / q_NPA : 0.872

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	3	SER	0	0.085	0.054	3.343	5.980	7.330	-0.012	-0.421	-0.917	-0.003
4	A	4	ARG	1	0.929	0.965	7.159	21.340	21.340	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.060	0.019	9.549	1.183	1.183	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.837	-0.909	6.018	-46.343	-46.343	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.029	0.009	6.122	1.421	1.421	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.060	-0.028	8.579	2.427	2.427	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.015	0.023	11.101	1.900	1.900	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.910	-0.946	8.116	-31.708	-31.708	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.911	0.936	11.528	26.239	26.239	0.000	0.000	0.000	0.000
12	A	12	PHE	0	-0.021	0.000	13.773	1.478	1.478	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.008	0.004	14.896	1.182	1.182	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.951	-0.987	12.868	-21.707	-21.707	0.000	0.000	0.000	0.000
15	A	15	LYS	0	-0.083	-0.009	17.060	1.151	1.151	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.010	-0.001	19.758	0.771	0.771	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.017	-0.002	20.570	0.582	0.582	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.037	-0.015	18.694	0.354	0.354	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.033	-0.007	17.927	-0.058	-0.058	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.026	-0.018	13.448	-0.916	-0.916	0.000	0.000	0.000	0.000
21	A	21	ILE	0	0.020	0.011	13.671	1.077	1.077	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.030	-0.032	11.385	-2.497	-2.497	0.000	0.000	0.000	0.000
23	A	23	PHE	0	0.001	0.003	10.373	1.455	1.455	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.002	-0.006	12.501	-1.653	-1.653	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.884	-0.950	14.504	-17.823	-17.823	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.090	-0.042	16.353	-0.077	-0.077	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.788	0.873	8.865	29.813	29.813	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.023	0.006	15.585	0.338	0.338	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.022	-0.003	14.977	-0.487	-0.487	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.007	-0.009	17.054	0.457	0.457	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.001	0.000	19.160	-0.252	-0.252	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.005	0.006	22.622	0.241	0.241	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.009	0.007	24.392	-0.121	-0.121	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.886	-0.954	27.427	-10.093	-10.093	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-1.005	-1.001	29.596	-9.160	-9.160	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.037	-0.011	30.877	0.130	0.130	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.036	0.006	29.483	0.061	0.061	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.040	-0.010	26.923	-0.634	-0.634	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.023	0.013	22.207	0.159	0.159	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.033	-0.014	21.153	-0.252	-0.252	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.016	0.014	16.848	0.209	0.209	0.000	0.000	0.000	0.000
42	A	42	SER	0	0.004	-0.006	16.852	-0.323	-0.323	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.810	-0.895	11.502	-25.815	-25.815	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.002	0.008	15.012	-0.547	-0.547	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.030	-0.022	16.623	0.395	0.395	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.878	-0.931	12.752	-24.726	-24.726	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.960	-0.992	14.607	-18.493	-18.493	0.000	0.000	0.000	0.000
48	A	48	TYR	0	-0.092	-0.063	17.355	0.855	0.855	0.000	0.000	0.000	0.000
49	A	49	MET	0	0.019	0.029	14.990	-1.018	-1.018	0.000	0.000	0.000	0.000
50	A	50	MET	0	-0.070	-0.016	17.700	1.010	1.010	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.005	0.003	19.993	-0.790	-0.790	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.010	-0.010	22.037	0.466	0.466	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.103	0.032	25.032	-0.243	-0.243	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.046	-0.031	26.391	0.396	0.396	0.000	0.000	0.000	0.000
55	A	55	CYS	0	-0.037	-0.014	29.193	0.149	0.149	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.039	0.028	32.373	0.325	0.325	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.815	0.878	34.216	8.865	8.865	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.025	0.010	36.565	0.097	0.097	0.000	0.000	0.000	0.000
59	A	59	PRO	0	-0.022	-0.009	38.543	0.088	0.088	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.011	-0.024	42.096	-0.060	-0.060	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.911	-0.943	44.569	-6.889	-6.889	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.023	-0.019	47.938	0.046	0.046	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.022	0.033	44.796	0.009	0.009	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.016	-0.029	45.838	-0.194	-0.194	0.000	0.000	0.000	0.000
65	A	65	PHE	0	0.083	0.041	40.997	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	66	ALA	0	0.025	0.014	42.057	-0.165	-0.165	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.048	-0.032	42.369	-0.129	-0.129	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.862	-0.927	44.729	-7.014	-7.014	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.035	0.020	38.228	-0.090	-0.090	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.048	-0.030	39.237	-0.149	-0.149	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.069	-0.024	41.300	-0.023	-0.023	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.091	0.040	40.351	-0.028	-0.028	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.010	-0.017	35.921	-0.296	-0.296	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.052	-0.012	38.251	-0.136	-0.136	0.000	0.000	0.000	0.000
75	A	75	TRP	0	0.058	0.039	36.686	-0.085	-0.085	0.000	0.000	0.000	0.000
76	A	76	PHE	0	0.050	0.012	34.268	-0.070	-0.070	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.036	-0.011	35.510	-0.220	-0.220	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.991	-0.996	36.749	-7.610	-7.610	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.109	-0.064	36.290	0.008	0.008	0.000	0.000	0.000	0.000
80	A	80	GLY	0	-0.040	-0.005	33.466	-0.191	-0.191	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.008	0.012	31.447	-0.365	-0.365	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.056	-0.034	28.909	-0.105	-0.105	0.000	0.000	0.000	0.000
83	A	83	TYR	0	-0.003	0.002	29.924	0.331	0.331	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.036	0.024	31.572	-0.270	-0.270	0.000	0.000	0.000	0.000
85	A	85	CYS	0	-0.083	-0.047	31.242	0.083	0.083	0.000	0.000	0.000	0.000
86	A	86	TYR	0	0.007	0.006	33.364	0.102	0.102	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.779	-0.880	28.735	-10.848	-10.848	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.049	-0.024	32.068	0.265	0.265	0.000	0.000	0.000	0.000
89	A	89	GLY	0	-0.062	-0.040	31.097	0.268	0.268	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.003	-0.008	30.164	0.162	0.162	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.008	0.009	32.187	0.317	0.317	0.000	0.000	0.000	0.000
92	A	92	SER	0	0.015	0.013	30.585	0.261	0.261	0.000	0.000	0.000	0.000
93	A	93	LEU	0	0.031	0.019	33.651	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.033	-0.018	27.574	-0.316	-0.316	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.031	0.032	29.892	0.264	0.264	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.018	-0.013	26.868	-0.490	-0.490	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.043	0.024	25.029	0.365	0.365	0.000	0.000	0.000	0.000
98	A	98	ARG	1	0.907	0.958	22.192	13.568	13.568	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.026	0.012	17.119	0.306	0.306	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.003	-0.005	19.133	-0.807	-0.807	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.026	0.003	13.483	-0.409	-0.409	0.000	0.000	0.000	0.000
102	A	102	ASP	-1	-0.959	-0.986	15.407	-17.275	-17.275	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.920	-0.960	17.727	-14.706	-14.706	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.007	0.028	16.070	0.749	0.749	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.037	-0.038	16.144	-0.920	-0.920	0.000	0.000	0.000	0.000
106	A	106	PRO	0	0.066	0.018	15.403	0.441	0.441	0.000	0.000	0.000	0.000
107	A	107	GLU	0	-0.003	-0.020	17.838	0.471	0.471	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.847	0.918	20.435	15.029	15.029	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.031	0.013	15.937	0.351	0.351	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.863	-0.939	19.914	-13.315	-13.315	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.019	-0.011	22.216	0.714	0.714	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.874	-0.948	22.768	-11.875	-11.875	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.023	-0.011	19.462	0.231	0.231	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.812	-0.880	23.953	-10.019	-10.019	0.000	0.000	0.000	0.000
115	A	115	VAL	0	0.042	0.031	27.252	0.505	0.505	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.007	0.003	25.754	0.444	0.444	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.002	-0.003	27.115	0.326	0.326	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.848	0.898	29.686	10.311	10.311	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.031	-0.018	31.308	0.434	0.434	0.000	0.000	0.000	0.000
120	A	120	MET	0	-0.084	-0.035	29.707	0.114	0.114	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.933	-0.953	33.316	-8.813	-8.813	0.000	0.000	0.000	0.000
122	A	122	ASN	0	-0.076	-0.058	35.559	0.489	0.489	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.009	0.018	35.774	0.225	0.225	0.000	0.000	0.000	0.000
124	A	124	TYR	0	-0.025	-0.029	38.249	0.170	0.170	0.000	0.000	0.000	0.000
125	A	125	LEU	0	-0.040	-0.013	41.198	0.232	0.232	0.000	0.000	0.000	0.000
126	A	126	VAL	0	-0.071	-0.019	38.912	0.115	0.115	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.052	-0.016	40.816	0.038	0.038	0.000	0.000	0.000	0.000
128	A	128	HIS	0	-0.082	-0.049	44.124	0.194	0.194	0.000	0.000	0.000	0.000
129	A	129	ASN	-1	-0.978	-0.973	46.556	-6.641	-6.641	0.000	0.000	0.000	0.000

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