FMO DATABASE

FMODB ID: ZL7JN

Calculation Name: 3V30-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3V30

Chain ID: A

ChEMBL ID:

UniProt ID: P48382

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	161
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1527186.351917
FMO2-HF: Nuclear repulsion	1465619.625667
FMO2-HF: Total energy	-61566.726249
FMO2-MP2: Total energy	-61749.778046

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:92:LEU)

Summations of interaction energy for fragment #1(A:92: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.
-145.25	-137.271	6.503	-4.518	-9.964	-0.037

Interaction energy analysis for fragmet #1(A:92:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.854 / q_NPA : 0.927

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	94	ILE	0	0.083	0.030	3.133	-4.433	-2.295	0.126	-1.020	-1.244	-0.004
5	A	96	GLN	0	-0.006	0.002	2.280	-0.614	0.536	2.033	-0.808	-2.376	-0.004
6	A	97	LEU	0	-0.040	-0.019	2.327	-2.730	-0.996	3.134	-1.325	-3.544	-0.013
7	A	98	ALA	0	0.002	-0.001	4.233	4.371	4.527	0.004	-0.028	-0.132	0.000
9	A	100	GLN	0	-0.046	-0.029	2.820	-2.827	-0.695	1.170	-1.194	-2.108	-0.015
11	A	102	GLU	-1	-0.895	-0.922	3.083	-37.411	-36.989	0.038	-0.099	-0.360	-0.001
14	A	105	GLN	0	-0.071	-0.054	4.132	-8.612	-8.427	-0.001	-0.028	-0.156	0.000
18	A	109	HIS	0	-0.109	-0.074	4.450	-4.074	-4.012	-0.001	-0.016	-0.044	0.000
4	A	95	HIS	0	-0.016	-0.007	5.852	-1.434	-1.434	0.000	0.000	0.000	0.000
8	A	99	ALA	0	-0.018	-0.014	5.617	2.883	2.883	0.000	0.000	0.000	0.000
10	A	101	GLY	0	0.096	0.070	5.764	0.411	0.411	0.000	0.000	0.000	0.000
12	A	103	LEU	0	-0.014	-0.019	6.176	-2.181	-2.181	0.000	0.000	0.000	0.000
13	A	104	ASP	-1	-0.845	-0.932	9.529	-21.962	-21.962	0.000	0.000	0.000	0.000
15	A	106	LEU	0	-0.016	-0.002	7.345	-1.044	-1.044	0.000	0.000	0.000	0.000
16	A	107	LYS	1	0.909	0.958	8.147	22.443	22.443	0.000	0.000	0.000	0.000
17	A	108	GLU	-1	-0.846	-0.904	9.182	-22.003	-22.003	0.000	0.000	0.000	0.000
19	A	110	LEU	0	-0.001	0.004	9.247	1.562	1.562	0.000	0.000	0.000	0.000
20	A	111	ARG	1	0.866	0.930	12.592	21.871	21.871	0.000	0.000	0.000	0.000
21	A	112	LYS	1	0.821	0.906	14.791	18.373	18.373	0.000	0.000	0.000	0.000
22	A	113	GLY	0	0.026	0.016	16.500	1.057	1.057	0.000	0.000	0.000	0.000
23	A	114	ASP	-1	-0.854	-0.914	16.833	-17.688	-17.688	0.000	0.000	0.000	0.000
24	A	115	ASN	0	0.044	0.001	17.619	-0.484	-0.484	0.000	0.000	0.000	0.000
25	A	116	LEU	0	-0.035	-0.003	10.976	-0.338	-0.338	0.000	0.000	0.000	0.000
26	A	117	VAL	0	0.018	0.002	13.084	-1.668	-1.668	0.000	0.000	0.000	0.000
27	A	118	ASN	0	0.019	0.013	13.948	-0.744	-0.744	0.000	0.000	0.000	0.000
28	A	119	LYS	1	0.923	0.974	11.186	25.020	25.020	0.000	0.000	0.000	0.000
29	A	120	PRO	0	0.024	0.019	12.636	-1.280	-1.280	0.000	0.000	0.000	0.000
30	A	121	ASP	-1	-0.777	-0.887	10.174	-24.218	-24.218	0.000	0.000	0.000	0.000
31	A	122	GLU	-1	-0.900	-0.966	11.122	-24.165	-24.165	0.000	0.000	0.000	0.000
32	A	123	ARG	1	0.904	0.956	11.263	22.129	22.129	0.000	0.000	0.000	0.000
33	A	124	GLY	0	0.007	0.008	14.887	1.151	1.151	0.000	0.000	0.000	0.000
34	A	125	PHE	0	-0.005	0.005	12.122	0.392	0.392	0.000	0.000	0.000	0.000
35	A	126	THR	0	0.059	0.023	12.462	-1.520	-1.520	0.000	0.000	0.000	0.000
36	A	127	PRO	0	-0.001	-0.022	9.250	-0.350	-0.350	0.000	0.000	0.000	0.000
37	A	128	LEU	0	0.043	0.039	10.449	-0.351	-0.351	0.000	0.000	0.000	0.000
38	A	129	ILE	0	0.001	0.027	13.761	0.461	0.461	0.000	0.000	0.000	0.000
39	A	130	TRP	0	-0.060	-0.043	8.768	-0.483	-0.483	0.000	0.000	0.000	0.000
40	A	131	ALA	0	0.016	0.008	10.592	0.222	0.222	0.000	0.000	0.000	0.000
41	A	132	SER	0	-0.037	-0.043	11.377	1.223	1.223	0.000	0.000	0.000	0.000
42	A	133	ALA	0	-0.027	-0.017	12.796	0.911	0.911	0.000	0.000	0.000	0.000
43	A	134	PHE	0	-0.039	-0.027	9.625	0.099	0.099	0.000	0.000	0.000	0.000
44	A	135	GLY	0	0.024	0.025	12.133	0.193	0.193	0.000	0.000	0.000	0.000
45	A	136	GLU	-1	-0.916	-0.962	9.418	-22.071	-22.071	0.000	0.000	0.000	0.000
46	A	137	ILE	0	0.017	-0.004	12.884	-0.099	-0.099	0.000	0.000	0.000	0.000
47	A	138	GLU	-1	-0.945	-0.969	14.291	-17.554	-17.554	0.000	0.000	0.000	0.000
48	A	139	THR	0	0.010	0.001	9.882	-0.242	-0.242	0.000	0.000	0.000	0.000
49	A	140	VAL	0	0.013	0.004	12.978	0.024	0.024	0.000	0.000	0.000	0.000
50	A	141	ARG	1	0.854	0.908	15.556	14.767	14.767	0.000	0.000	0.000	0.000
51	A	142	PHE	0	0.003	0.007	12.481	0.440	0.440	0.000	0.000	0.000	0.000
52	A	143	LEU	0	-0.014	-0.005	11.599	0.192	0.192	0.000	0.000	0.000	0.000
53	A	144	LEU	0	0.033	0.019	15.838	0.612	0.612	0.000	0.000	0.000	0.000
54	A	145	GLU	-1	-0.942	-0.954	19.380	-13.185	-13.185	0.000	0.000	0.000	0.000
55	A	146	TRP	0	-0.047	-0.017	16.699	0.211	0.211	0.000	0.000	0.000	0.000
56	A	147	GLY	0	-0.014	0.001	19.048	0.234	0.234	0.000	0.000	0.000	0.000
57	A	148	ALA	0	-0.072	-0.042	16.242	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	149	ASP	-1	-0.849	-0.943	18.090	-13.028	-13.028	0.000	0.000	0.000	0.000
59	A	150	PRO	0	-0.044	-0.033	18.999	-0.693	-0.693	0.000	0.000	0.000	0.000
60	A	151	HIS	0	-0.019	-0.005	20.645	0.136	0.136	0.000	0.000	0.000	0.000
61	A	152	ILE	0	-0.079	-0.023	18.034	0.171	0.171	0.000	0.000	0.000	0.000
62	A	153	LEU	0	-0.029	-0.013	19.990	-0.124	-0.124	0.000	0.000	0.000	0.000
63	A	154	ALA	0	-0.038	-0.007	16.736	-0.289	-0.289	0.000	0.000	0.000	0.000
64	A	155	LYS	1	0.858	0.898	17.948	16.970	16.970	0.000	0.000	0.000	0.000
65	A	156	GLU	-1	-0.963	-0.975	20.687	-12.725	-12.725	0.000	0.000	0.000	0.000
66	A	157	ARG	1	0.828	0.910	22.206	11.673	11.673	0.000	0.000	0.000	0.000
67	A	158	GLU	-1	-0.824	-0.910	18.500	-15.056	-15.056	0.000	0.000	0.000	0.000
68	A	159	SER	0	0.067	0.029	19.604	-0.597	-0.597	0.000	0.000	0.000	0.000
69	A	160	ALA	0	0.035	0.007	17.696	-0.290	-0.290	0.000	0.000	0.000	0.000
70	A	161	LEU	0	0.044	0.038	18.691	-0.179	-0.179	0.000	0.000	0.000	0.000
71	A	162	SER	0	0.047	0.026	21.809	0.273	0.273	0.000	0.000	0.000	0.000
72	A	163	LEU	0	0.014	0.018	15.890	0.085	0.085	0.000	0.000	0.000	0.000
73	A	164	ALA	0	0.007	0.008	18.278	-0.065	-0.065	0.000	0.000	0.000	0.000
74	A	165	SER	0	-0.021	-0.041	19.143	0.380	0.380	0.000	0.000	0.000	0.000
75	A	166	THR	0	-0.042	-0.033	19.857	0.491	0.491	0.000	0.000	0.000	0.000
76	A	167	GLY	0	-0.024	-0.005	18.378	0.158	0.158	0.000	0.000	0.000	0.000
77	A	168	GLY	0	0.012	0.012	19.347	0.075	0.075	0.000	0.000	0.000	0.000
78	A	169	TYR	0	-0.012	0.010	15.340	0.533	0.533	0.000	0.000	0.000	0.000
79	A	170	THR	0	-0.009	-0.023	20.488	0.088	0.088	0.000	0.000	0.000	0.000
80	A	171	ASP	-1	-0.899	-0.949	21.717	-11.806	-11.806	0.000	0.000	0.000	0.000
81	A	172	ILE	0	-0.042	-0.005	16.148	0.028	0.028	0.000	0.000	0.000	0.000
82	A	173	VAL	0	0.025	0.000	20.353	0.051	0.051	0.000	0.000	0.000	0.000
83	A	174	GLY	0	0.003	-0.001	23.074	0.315	0.315	0.000	0.000	0.000	0.000
84	A	175	LEU	0	-0.028	-0.026	20.269	0.171	0.171	0.000	0.000	0.000	0.000
85	A	176	LEU	0	-0.017	-0.013	19.012	-0.032	-0.032	0.000	0.000	0.000	0.000
86	A	177	LEU	0	0.014	0.009	22.911	0.250	0.250	0.000	0.000	0.000	0.000
87	A	178	GLU	-1	-0.893	-0.921	26.174	-9.872	-9.872	0.000	0.000	0.000	0.000
88	A	179	ARG	1	0.778	0.880	22.866	12.989	12.989	0.000	0.000	0.000	0.000
89	A	180	ASP	-1	-0.916	-0.955	26.350	-9.966	-9.966	0.000	0.000	0.000	0.000
90	A	181	VAL	0	-0.022	-0.003	23.462	0.038	0.038	0.000	0.000	0.000	0.000
91	A	182	ASP	-1	-0.850	-0.935	26.921	-9.657	-9.657	0.000	0.000	0.000	0.000
92	A	183	ILE	0	0.000	-0.008	27.768	-0.371	-0.371	0.000	0.000	0.000	0.000
93	A	184	ASN	0	-0.024	-0.022	29.203	0.042	0.042	0.000	0.000	0.000	0.000
94	A	185	ILE	0	-0.038	-0.008	25.038	0.070	0.070	0.000	0.000	0.000	0.000
95	A	186	TYR	0	-0.014	-0.032	27.292	-0.336	-0.336	0.000	0.000	0.000	0.000
96	A	187	ASP	-1	-0.816	-0.882	24.383	-12.088	-12.088	0.000	0.000	0.000	0.000
97	A	188	TRP	0	0.018	0.000	25.522	0.249	0.249	0.000	0.000	0.000	0.000
98	A	189	ASN	0	-0.079	-0.034	24.697	0.204	0.204	0.000	0.000	0.000	0.000
99	A	190	GLY	0	0.011	0.015	26.719	0.258	0.258	0.000	0.000	0.000	0.000
100	A	191	GLY	0	-0.017	-0.005	27.843	0.334	0.334	0.000	0.000	0.000	0.000
101	A	192	THR	0	0.065	0.022	27.686	-0.104	-0.104	0.000	0.000	0.000	0.000
102	A	193	PRO	0	0.007	-0.001	25.108	-0.048	-0.048	0.000	0.000	0.000	0.000
103	A	194	LEU	0	0.028	0.016	26.393	-0.105	-0.105	0.000	0.000	0.000	0.000
104	A	195	LEU	0	0.013	0.017	29.377	0.051	0.051	0.000	0.000	0.000	0.000
105	A	196	TYR	0	-0.063	-0.056	24.098	0.086	0.086	0.000	0.000	0.000	0.000
106	A	197	ALA	0	0.005	0.007	25.940	-0.072	-0.072	0.000	0.000	0.000	0.000
107	A	198	VAL	0	-0.019	-0.013	26.840	0.094	0.094	0.000	0.000	0.000	0.000
108	A	199	ARG	1	0.920	0.963	27.228	10.030	10.030	0.000	0.000	0.000	0.000
109	A	200	GLY	0	0.009	-0.002	25.248	0.049	0.049	0.000	0.000	0.000	0.000
110	A	201	ASN	0	-0.057	-0.030	26.156	0.137	0.137	0.000	0.000	0.000	0.000
111	A	202	HIS	0	0.011	0.028	22.605	0.391	0.391	0.000	0.000	0.000	0.000
112	A	203	VAL	0	-0.031	-0.031	27.244	0.060	0.060	0.000	0.000	0.000	0.000
113	A	204	LYS	1	0.992	0.994	27.444	10.213	10.213	0.000	0.000	0.000	0.000
114	A	205	CYS	0	-0.004	0.027	25.177	-0.125	-0.125	0.000	0.000	0.000	0.000
115	A	206	VAL	0	0.008	0.007	27.174	0.072	0.072	0.000	0.000	0.000	0.000
116	A	207	GLU	-1	-0.919	-0.973	30.444	-8.682	-8.682	0.000	0.000	0.000	0.000
117	A	208	ALA	0	-0.028	-0.014	28.087	0.166	0.166	0.000	0.000	0.000	0.000
118	A	209	LEU	0	0.001	0.000	26.661	0.031	0.031	0.000	0.000	0.000	0.000
119	A	210	LEU	0	-0.001	-0.003	30.333	0.163	0.163	0.000	0.000	0.000	0.000
120	A	211	ALA	0	-0.034	-0.017	33.155	0.206	0.206	0.000	0.000	0.000	0.000
121	A	212	ARG	1	0.805	0.891	28.602	10.341	10.341	0.000	0.000	0.000	0.000
122	A	213	GLY	0	-0.001	0.004	33.148	-0.046	-0.046	0.000	0.000	0.000	0.000
123	A	214	ALA	0	-0.031	-0.013	31.547	0.037	0.037	0.000	0.000	0.000	0.000
124	A	215	ASP	-1	-0.807	-0.869	33.525	-7.810	-7.810	0.000	0.000	0.000	0.000
125	A	216	LEU	0	-0.038	-0.033	35.269	-0.145	-0.145	0.000	0.000	0.000	0.000
126	A	217	THR	0	-0.120	-0.082	37.438	0.110	0.110	0.000	0.000	0.000	0.000
127	A	218	THR	0	-0.019	-0.018	33.854	0.045	0.045	0.000	0.000	0.000	0.000
128	A	219	GLU	-1	-0.946	-0.980	35.465	-7.760	-7.760	0.000	0.000	0.000	0.000
129	A	220	ALA	0	-0.007	-0.007	32.287	-0.219	-0.219	0.000	0.000	0.000	0.000
130	A	221	ASP	-1	-0.820	-0.892	32.447	-9.027	-9.027	0.000	0.000	0.000	0.000
131	A	222	SER	0	-0.110	-0.058	33.777	0.158	0.158	0.000	0.000	0.000	0.000
132	A	223	GLY	0	0.016	0.011	35.527	0.181	0.181	0.000	0.000	0.000	0.000
133	A	224	TYR	0	-0.082	-0.030	35.225	0.166	0.166	0.000	0.000	0.000	0.000
134	A	225	THR	0	0.061	0.005	35.704	-0.246	-0.246	0.000	0.000	0.000	0.000
135	A	226	PRO	0	0.013	-0.009	33.611	-0.078	-0.078	0.000	0.000	0.000	0.000
136	A	227	MET	0	-0.010	-0.001	34.990	-0.107	-0.107	0.000	0.000	0.000	0.000
137	A	228	ASP	-1	-0.798	-0.860	38.049	-7.476	-7.476	0.000	0.000	0.000	0.000
138	A	229	LEU	0	-0.030	-0.013	31.388	-0.027	-0.027	0.000	0.000	0.000	0.000
139	A	230	ALA	0	-0.005	-0.007	34.879	-0.035	-0.035	0.000	0.000	0.000	0.000
140	A	231	VAL	0	-0.042	-0.022	35.775	0.061	0.061	0.000	0.000	0.000	0.000
141	A	232	ALA	0	-0.012	-0.005	37.440	0.072	0.072	0.000	0.000	0.000	0.000
142	A	233	LEU	0	-0.048	-0.016	31.545	-0.046	-0.046	0.000	0.000	0.000	0.000
143	A	234	GLY	0	-0.002	0.009	35.324	-0.067	-0.067	0.000	0.000	0.000	0.000
144	A	235	TYR	0	-0.032	0.000	29.371	0.069	0.069	0.000	0.000	0.000	0.000
145	A	236	ARG	1	0.896	0.924	35.240	7.094	7.094	0.000	0.000	0.000	0.000
146	A	237	LYS	1	0.893	0.955	34.657	8.198	8.198	0.000	0.000	0.000	0.000
147	A	238	VAL	0	0.049	0.023	31.641	0.018	0.018	0.000	0.000	0.000	0.000
148	A	239	GLN	0	0.015	-0.001	34.745	-0.009	-0.009	0.000	0.000	0.000	0.000
149	A	240	GLN	0	0.032	0.019	38.252	-0.080	-0.080	0.000	0.000	0.000	0.000
150	A	241	VAL	0	-0.035	-0.011	33.875	0.115	0.115	0.000	0.000	0.000	0.000
151	A	242	ILE	0	0.043	0.023	34.997	0.045	0.045	0.000	0.000	0.000	0.000
152	A	243	GLU	-1	-0.871	-0.934	38.229	-6.920	-6.920	0.000	0.000	0.000	0.000
153	A	244	ASN	0	-0.025	-0.030	39.911	0.274	0.274	0.000	0.000	0.000	0.000
154	A	245	HIS	0	0.025	0.021	37.998	0.137	0.137	0.000	0.000	0.000	0.000
155	A	246	ILE	0	0.019	0.003	40.273	0.110	0.110	0.000	0.000	0.000	0.000
156	A	247	LEU	0	-0.032	-0.018	43.076	0.139	0.139	0.000	0.000	0.000	0.000
157	A	248	LYS	1	0.771	0.872	42.117	6.797	6.797	0.000	0.000	0.000	0.000
158	A	249	LEU	0	0.003	0.009	40.446	0.023	0.023	0.000	0.000	0.000	0.000
159	A	250	PHE	0	-0.057	-0.022	44.232	0.092	0.092	0.000	0.000	0.000	0.000
160	A	251	GLN	0	-0.049	-0.019	47.457	0.139	0.139	0.000	0.000	0.000	0.000
161	A	252	SER	-1	-0.845	-0.896	47.600	-6.526	-6.526	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:92:LEU)