FMO DATABASE

FMODB ID: 5Y82Z

Calculation Name: 4ZW0-C-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4ZW0

Chain ID: C

ChEMBL ID:

UniProt ID: C6XFU0

Base Structure: X-ray

Registration Date: 2025-10-04

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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1392982.598635
FMO2-HF: Nuclear repulsion	1334033.159859
FMO2-HF: Total energy	-58949.438775
FMO2-MP2: Total energy	-59116.087344

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:7:LEU)

Summations of interaction energy for fragment #1(A:7:LEU)

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.
32.067	39.39	7.656	-4.535	-10.443	-0.055

Interaction energy analysis for fragmet #1(A:7:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.786 / q_NPA : 0.894

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	9	ALA	0	-0.063	-0.039	3.645	-0.892	0.572	-0.003	-0.665	-0.796	-0.001
27	A	33	ASN	0	0.002	-0.020	2.272	-1.466	-1.480	3.662	-1.266	-2.382	0.000
28	A	34	ILE	0	0.039	0.035	2.744	-4.000	-1.899	1.669	-0.636	-3.135	-0.030
29	A	35	GLN	0	-0.054	-0.039	2.393	-20.926	-16.828	2.216	-2.518	-3.795	-0.024
30	A	36	ARG	1	0.939	0.958	3.151	37.655	37.236	0.113	0.553	-0.247	0.000
34	A	40	ALA	0	0.034	0.030	5.160	-4.826	-4.733	-0.001	-0.003	-0.088	0.000
4	A	10	LYS	1	0.842	0.931	6.400	34.595	34.595	0.000	0.000	0.000	0.000
5	A	11	ASP	-1	-0.824	-0.913	10.001	-19.431	-19.431	0.000	0.000	0.000	0.000
6	A	12	ILE	0	0.046	0.010	13.218	0.247	0.247	0.000	0.000	0.000	0.000
7	A	13	VAL	0	0.011	0.004	16.393	0.806	0.806	0.000	0.000	0.000	0.000
8	A	14	GLU	-1	-0.865	-0.939	11.998	-26.377	-26.377	0.000	0.000	0.000	0.000
9	A	15	LEU	0	-0.009	-0.002	11.822	0.368	0.368	0.000	0.000	0.000	0.000
10	A	16	MET	0	-0.042	-0.023	15.140	0.734	0.734	0.000	0.000	0.000	0.000
11	A	17	ARG	1	0.907	0.972	15.745	19.652	19.652	0.000	0.000	0.000	0.000
12	A	18	PHE	0	0.016	0.009	13.603	-0.115	-0.115	0.000	0.000	0.000	0.000
13	A	19	LEU	0	-0.010	0.014	16.023	0.342	0.342	0.000	0.000	0.000	0.000
14	A	20	PRO	0	0.033	0.018	18.887	0.195	0.195	0.000	0.000	0.000	0.000
15	A	21	HIS	0	-0.033	-0.010	20.882	0.291	0.291	0.000	0.000	0.000	0.000
16	A	22	ARG	1	0.864	0.919	21.181	13.175	13.175	0.000	0.000	0.000	0.000
17	A	23	TYR	0	0.052	0.034	24.522	0.060	0.060	0.000	0.000	0.000	0.000
18	A	24	PRO	0	-0.038	-0.025	26.262	0.230	0.230	0.000	0.000	0.000	0.000
19	A	25	PHE	0	0.024	-0.018	24.835	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	26	LEU	0	-0.018	0.021	18.215	-0.282	-0.282	0.000	0.000	0.000	0.000
21	A	27	LEU	0	-0.048	-0.039	19.938	0.254	0.254	0.000	0.000	0.000	0.000
22	A	28	VAL	0	-0.001	-0.014	14.387	-0.304	-0.304	0.000	0.000	0.000	0.000
23	A	29	ASP	-1	-0.846	-0.920	15.893	-15.683	-15.683	0.000	0.000	0.000	0.000
24	A	30	LYS	1	0.923	0.949	10.935	22.121	22.121	0.000	0.000	0.000	0.000
25	A	31	VAL	0	0.023	0.027	7.506	0.887	0.887	0.000	0.000	0.000	0.000
26	A	32	VAL	0	-0.010	-0.007	5.832	-1.704	-1.704	0.000	0.000	0.000	0.000
31	A	37	ASP	-1	-0.683	-0.811	6.677	-20.498	-20.498	0.000	0.000	0.000	0.000
32	A	38	GLU	-1	-0.958	-0.982	6.781	-26.699	-26.699	0.000	0.000	0.000	0.000
33	A	39	SER	0	0.018	-0.003	5.441	1.352	1.352	0.000	0.000	0.000	0.000
35	A	41	ILE	0	-0.006	0.007	5.810	3.148	3.148	0.000	0.000	0.000	0.000
36	A	42	GLY	0	0.011	0.015	8.238	-1.359	-1.359	0.000	0.000	0.000	0.000
37	A	43	ILE	0	-0.073	-0.040	10.373	0.752	0.752	0.000	0.000	0.000	0.000
38	A	44	LYS	1	0.871	0.932	13.401	14.214	14.214	0.000	0.000	0.000	0.000
39	A	45	ASN	0	-0.002	-0.005	17.200	-0.011	-0.011	0.000	0.000	0.000	0.000
40	A	46	VAL	0	0.016	0.018	19.739	0.317	0.317	0.000	0.000	0.000	0.000
41	A	47	THR	0	-0.004	-0.010	23.045	0.337	0.337	0.000	0.000	0.000	0.000
42	A	48	PHE	0	0.064	0.019	26.191	0.093	0.093	0.000	0.000	0.000	0.000
43	A	49	ASN	0	-0.014	0.003	29.001	0.481	0.481	0.000	0.000	0.000	0.000
44	A	50	GLU	-1	-0.754	-0.872	24.534	-12.663	-12.663	0.000	0.000	0.000	0.000
45	A	51	PRO	0	0.025	0.015	28.322	0.237	0.237	0.000	0.000	0.000	0.000
46	A	52	HIS	1	0.874	0.926	25.537	11.514	11.514	0.000	0.000	0.000	0.000
47	A	53	PHE	0	-0.057	-0.035	26.780	0.161	0.161	0.000	0.000	0.000	0.000
48	A	54	MET	0	0.014	0.022	32.333	0.260	0.260	0.000	0.000	0.000	0.000
49	A	55	GLY	0	0.019	0.012	34.731	0.259	0.259	0.000	0.000	0.000	0.000
50	A	56	HIS	0	-0.062	-0.032	30.482	0.253	0.253	0.000	0.000	0.000	0.000
51	A	57	PHE	0	0.029	-0.008	32.080	-0.304	-0.304	0.000	0.000	0.000	0.000
52	A	58	PRO	0	0.055	0.042	35.662	-0.100	-0.100	0.000	0.000	0.000	0.000
53	A	59	GLY	0	0.005	0.001	37.848	0.149	0.149	0.000	0.000	0.000	0.000
54	A	60	ARG	1	0.898	0.951	33.923	8.563	8.563	0.000	0.000	0.000	0.000
55	A	61	PRO	0	-0.013	0.012	31.028	-0.079	-0.079	0.000	0.000	0.000	0.000
56	A	62	VAL	0	0.001	-0.016	28.716	-0.117	-0.117	0.000	0.000	0.000	0.000
57	A	63	MET	0	-0.011	0.003	21.879	0.265	0.265	0.000	0.000	0.000	0.000
58	A	64	PRO	0	-0.003	0.003	26.672	0.046	0.046	0.000	0.000	0.000	0.000
59	A	65	GLY	0	0.065	0.025	25.100	-0.385	-0.385	0.000	0.000	0.000	0.000
60	A	66	VAL	0	0.035	-0.005	24.422	-0.413	-0.413	0.000	0.000	0.000	0.000
61	A	67	LEU	0	0.008	0.000	24.103	-0.238	-0.238	0.000	0.000	0.000	0.000
62	A	68	ILE	0	-0.027	0.007	19.810	-0.587	-0.587	0.000	0.000	0.000	0.000
63	A	69	LEU	0	-0.015	-0.009	19.692	-0.673	-0.673	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.803	-0.882	20.358	-13.667	-13.667	0.000	0.000	0.000	0.000
65	A	71	GLY	0	0.011	0.002	18.532	-0.538	-0.538	0.000	0.000	0.000	0.000
66	A	72	MET	0	-0.054	-0.040	15.722	-0.955	-0.955	0.000	0.000	0.000	0.000
67	A	73	ALA	0	0.039	0.013	15.779	-0.902	-0.902	0.000	0.000	0.000	0.000
68	A	74	GLN	0	-0.018	-0.014	16.932	-0.976	-0.976	0.000	0.000	0.000	0.000
69	A	75	THR	0	-0.037	-0.015	11.088	-1.288	-1.288	0.000	0.000	0.000	0.000
70	A	76	ALA	0	0.015	0.007	12.071	-1.337	-1.337	0.000	0.000	0.000	0.000
71	A	77	GLY	0	0.049	0.018	13.262	-0.537	-0.537	0.000	0.000	0.000	0.000
72	A	78	ALA	0	-0.001	0.005	12.601	0.010	0.010	0.000	0.000	0.000	0.000
73	A	79	ILE	0	-0.021	-0.015	7.974	-0.788	-0.788	0.000	0.000	0.000	0.000
74	A	80	CYS	0	-0.032	-0.012	10.936	-0.131	-0.131	0.000	0.000	0.000	0.000
75	A	81	ALA	0	-0.020	0.000	13.666	0.501	0.501	0.000	0.000	0.000	0.000
76	A	82	ILE	0	-0.018	-0.015	9.509	-0.174	-0.174	0.000	0.000	0.000	0.000
77	A	83	HIS	0	-0.055	-0.026	10.063	-0.909	-0.909	0.000	0.000	0.000	0.000
78	A	84	ASN	0	-0.069	-0.036	12.090	-0.399	-0.399	0.000	0.000	0.000	0.000
79	A	85	GLY	0	0.006	0.016	14.976	1.050	1.050	0.000	0.000	0.000	0.000
80	A	86	PHE	0	-0.053	-0.026	16.717	1.151	1.151	0.000	0.000	0.000	0.000
81	A	87	ASP	-1	-0.877	-0.953	17.031	-15.512	-15.512	0.000	0.000	0.000	0.000
82	A	88	GLN	0	-0.024	-0.012	19.253	0.521	0.521	0.000	0.000	0.000	0.000
83	A	89	TYR	0	-0.007	-0.016	21.685	0.131	0.131	0.000	0.000	0.000	0.000
84	A	90	ALA	0	0.019	0.026	22.235	0.542	0.542	0.000	0.000	0.000	0.000
85	A	91	PRO	0	-0.031	-0.011	22.486	-0.575	-0.575	0.000	0.000	0.000	0.000
86	A	92	PRO	0	-0.004	-0.003	20.616	0.147	0.147	0.000	0.000	0.000	0.000
87	A	93	TYR	0	0.003	-0.008	22.752	0.452	0.452	0.000	0.000	0.000	0.000
88	A	94	LEU	0	-0.010	-0.010	22.750	-0.223	-0.223	0.000	0.000	0.000	0.000
89	A	95	MET	0	-0.030	-0.019	24.611	0.355	0.355	0.000	0.000	0.000	0.000
90	A	96	SER	0	-0.035	-0.024	24.804	0.267	0.267	0.000	0.000	0.000	0.000
91	A	97	ILE	0	0.022	0.014	23.387	-0.557	-0.557	0.000	0.000	0.000	0.000
92	A	98	ASP	-1	-0.811	-0.891	23.892	-9.994	-9.994	0.000	0.000	0.000	0.000
93	A	99	LYS	1	0.838	0.890	23.516	10.074	10.074	0.000	0.000	0.000	0.000
94	A	100	ALA	0	-0.003	0.017	23.548	-0.273	-0.273	0.000	0.000	0.000	0.000
95	A	101	ARG	1	0.927	0.968	23.585	10.929	10.929	0.000	0.000	0.000	0.000
96	A	102	PHE	0	0.010	0.006	23.514	-0.464	-0.464	0.000	0.000	0.000	0.000
97	A	103	ARG	1	0.788	0.870	22.001	12.782	12.782	0.000	0.000	0.000	0.000
98	A	104	LYS	1	0.964	0.987	23.580	11.980	11.980	0.000	0.000	0.000	0.000
99	A	105	PRO	0	-0.027	0.002	25.232	-0.240	-0.240	0.000	0.000	0.000	0.000
100	A	106	VAL	0	0.031	0.009	21.985	-0.210	-0.210	0.000	0.000	0.000	0.000
101	A	107	PHE	0	-0.010	-0.017	25.141	0.403	0.403	0.000	0.000	0.000	0.000
102	A	108	PRO	0	-0.045	-0.034	25.260	-0.445	-0.445	0.000	0.000	0.000	0.000
103	A	109	GLY	0	0.013	0.013	25.001	0.340	0.340	0.000	0.000	0.000	0.000
104	A	110	ASP	-1	-0.815	-0.886	21.661	-12.498	-12.498	0.000	0.000	0.000	0.000
105	A	111	ARG	1	0.839	0.895	11.935	19.878	19.878	0.000	0.000	0.000	0.000
106	A	112	LEU	0	-0.020	-0.006	17.162	-0.048	-0.048	0.000	0.000	0.000	0.000
107	A	113	GLU	-1	-0.842	-0.916	11.812	-21.970	-21.970	0.000	0.000	0.000	0.000
108	A	114	TYR	0	0.008	0.003	13.010	0.917	0.917	0.000	0.000	0.000	0.000
109	A	115	HIS	0	0.017	0.010	9.130	-2.376	-2.376	0.000	0.000	0.000	0.000
110	A	116	VAL	0	-0.027	-0.012	9.821	1.889	1.889	0.000	0.000	0.000	0.000
111	A	117	ASN	0	-0.010	-0.022	9.494	-3.139	-3.139	0.000	0.000	0.000	0.000
112	A	118	LYS	1	0.852	0.925	10.688	22.425	22.425	0.000	0.000	0.000	0.000
113	A	119	VAL	0	-0.003	0.007	12.301	0.964	0.964	0.000	0.000	0.000	0.000
114	A	120	ARG	1	0.807	0.899	15.829	13.493	13.493	0.000	0.000	0.000	0.000
115	A	121	ASN	0	0.028	-0.007	13.696	1.135	1.135	0.000	0.000	0.000	0.000
116	A	122	ARG	1	0.950	0.970	16.746	13.487	13.487	0.000	0.000	0.000	0.000
117	A	123	VAL	0	0.002	-0.003	19.755	0.395	0.395	0.000	0.000	0.000	0.000
118	A	124	ASP	-1	-0.783	-0.880	21.611	-12.665	-12.665	0.000	0.000	0.000	0.000
119	A	125	LEU	0	-0.021	0.004	21.612	0.140	0.140	0.000	0.000	0.000	0.000
120	A	126	TRP	0	0.049	0.012	16.602	-0.482	-0.482	0.000	0.000	0.000	0.000
121	A	127	LYS	1	0.863	0.910	17.728	13.123	13.123	0.000	0.000	0.000	0.000
122	A	128	PHE	0	0.055	0.037	10.578	-0.417	-0.417	0.000	0.000	0.000	0.000
123	A	129	GLN	0	-0.016	0.007	15.089	1.260	1.260	0.000	0.000	0.000	0.000
124	A	130	CYS	0	-0.031	-0.017	14.257	-1.539	-1.539	0.000	0.000	0.000	0.000
125	A	131	CYS	0	-0.027	-0.021	14.072	1.030	1.030	0.000	0.000	0.000	0.000
126	A	132	ALA	0	0.010	0.016	14.324	-1.010	-1.010	0.000	0.000	0.000	0.000
127	A	133	LYS	1	0.915	0.950	12.364	19.406	19.406	0.000	0.000	0.000	0.000
128	A	134	VAL	0	0.053	0.028	16.385	-0.306	-0.306	0.000	0.000	0.000	0.000
129	A	135	GLU	-1	-0.889	-0.942	17.299	-13.042	-13.042	0.000	0.000	0.000	0.000
130	A	136	ASN	0	-0.048	-0.037	13.666	-0.184	-0.184	0.000	0.000	0.000	0.000
131	A	137	THR	0	0.001	0.022	16.501	0.570	0.570	0.000	0.000	0.000	0.000
132	A	138	VAL	0	-0.028	-0.028	16.938	-0.431	-0.431	0.000	0.000	0.000	0.000
133	A	139	VAL	0	-0.010	-0.002	19.144	0.695	0.695	0.000	0.000	0.000	0.000
134	A	140	ALA	0	0.015	-0.002	19.661	0.687	0.687	0.000	0.000	0.000	0.000
135	A	141	GLU	-1	-0.845	-0.895	18.849	-13.454	-13.454	0.000	0.000	0.000	0.000
136	A	142	ALA	0	0.039	0.009	19.049	0.724	0.724	0.000	0.000	0.000	0.000
137	A	143	GLU	-1	-0.845	-0.891	18.925	-13.301	-13.301	0.000	0.000	0.000	0.000
138	A	144	ILE	0	-0.002	-0.010	18.474	0.634	0.634	0.000	0.000	0.000	0.000
139	A	145	CYS	0	-0.075	-0.046	19.350	-0.469	-0.469	0.000	0.000	0.000	0.000
140	A	146	ALA	0	0.050	0.030	20.453	0.553	0.553	0.000	0.000	0.000	0.000
141	A	147	MET	0	0.022	0.016	21.309	-0.228	-0.228	0.000	0.000	0.000	0.000
142	A	148	VAL	0	-0.061	-0.023	20.222	-0.261	-0.261	0.000	0.000	0.000	0.000
143	A	149	MET	0	-0.042	-0.019	22.985	0.468	0.468	0.000	0.000	0.000	0.000
144	A	150	HIS	0	-0.023	0.003	22.371	1.600	1.600	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:LEU)