FMO DATABASE

FMODB ID: NLJGQ

Calculation Name: 3N3E-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3N3E

Chain ID: B

ChEMBL ID:

UniProt ID: Q8UUZ6

Base Structure: X-ray

Registration Date: 2025-10-05

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	104
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-761928.983179
FMO2-HF: Nuclear repulsion	720706.53962
FMO2-HF: Total energy	-41222.443559
FMO2-MP2: Total energy	-41343.292794

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:62:VAL)

Summations of interaction energy for fragment #1(A:62:VAL)

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.
-62.61	-56.298	0.856	-2.99	-4.178	-0.016

Interaction energy analysis for fragmet #1(A:62:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.890 / q_NPA : 0.933

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	64	GLU	-1	-0.816	-0.889	3.700	-35.247	-32.797	-0.015	-1.232	-1.203	-0.002
15	A	76	LEU	0	-0.021	-0.024	2.901	-7.937	-7.190	0.155	-0.225	-0.678	-0.002
16	A	77	ASP	-1	-0.847	-0.905	2.604	-45.972	-43.893	0.701	-1.011	-1.768	-0.008
17	A	78	VAL	0	-0.020	-0.017	3.468	-4.743	-3.707	0.015	-0.522	-0.529	-0.004
4	A	65	VAL	0	-0.007	-0.006	6.828	1.883	1.883	0.000	0.000	0.000	0.000
5	A	66	ARG	1	0.885	0.939	10.188	24.214	24.214	0.000	0.000	0.000	0.000
6	A	67	SER	0	-0.005	-0.004	13.552	0.860	0.860	0.000	0.000	0.000	0.000
7	A	68	ASP	-1	-0.827	-0.906	16.997	-15.533	-15.533	0.000	0.000	0.000	0.000
8	A	69	ARG	1	0.923	0.946	20.093	11.201	11.201	0.000	0.000	0.000	0.000
9	A	70	GLU	-1	-0.880	-0.936	22.832	-11.766	-11.766	0.000	0.000	0.000	0.000
10	A	71	LYS	1	0.954	0.984	18.274	16.920	16.920	0.000	0.000	0.000	0.000
11	A	72	PHE	0	-0.016	-0.008	12.762	-0.360	-0.360	0.000	0.000	0.000	0.000
12	A	73	THR	0	0.028	0.005	12.801	0.850	0.850	0.000	0.000	0.000	0.000
13	A	74	VAL	0	-0.019	-0.002	7.985	-0.964	-0.964	0.000	0.000	0.000	0.000
14	A	75	TYR	0	0.031	0.031	7.266	1.770	1.770	0.000	0.000	0.000	0.000
18	A	79	LYS	1	0.894	0.928	5.984	40.905	40.905	0.000	0.000	0.000	0.000
19	A	80	HIS	0	-0.034	0.002	6.443	3.825	3.825	0.000	0.000	0.000	0.000
20	A	81	PHE	0	-0.065	-0.036	7.708	1.909	1.909	0.000	0.000	0.000	0.000
21	A	82	SER	0	0.030	0.001	11.737	-0.809	-0.809	0.000	0.000	0.000	0.000
22	A	83	PRO	0	-0.008	-0.035	13.937	-0.483	-0.483	0.000	0.000	0.000	0.000
23	A	84	ASP	-1	-0.883	-0.918	15.301	-15.402	-15.402	0.000	0.000	0.000	0.000
24	A	85	GLU	-1	-0.764	-0.861	14.480	-18.093	-18.093	0.000	0.000	0.000	0.000
25	A	86	LEU	0	-0.037	-0.018	9.711	-1.142	-1.142	0.000	0.000	0.000	0.000
26	A	87	SER	0	-0.013	-0.010	13.559	1.733	1.733	0.000	0.000	0.000	0.000
27	A	88	VAL	0	-0.008	-0.002	12.372	-1.182	-1.182	0.000	0.000	0.000	0.000
28	A	89	LYS	1	0.936	0.968	14.978	15.759	15.759	0.000	0.000	0.000	0.000
29	A	90	VAL	0	-0.027	-0.007	16.171	-1.087	-1.087	0.000	0.000	0.000	0.000
30	A	91	THR	0	0.016	-0.007	18.400	0.686	0.686	0.000	0.000	0.000	0.000
31	A	92	ASP	-1	-0.885	-0.931	19.236	-13.057	-13.057	0.000	0.000	0.000	0.000
32	A	93	ASP	-1	-0.840	-0.898	20.516	-13.069	-13.069	0.000	0.000	0.000	0.000
33	A	94	TYR	0	-0.076	-0.059	14.396	-1.119	-1.119	0.000	0.000	0.000	0.000
34	A	95	VAL	0	0.020	0.019	12.239	0.436	0.436	0.000	0.000	0.000	0.000
35	A	96	GLU	-1	-0.869	-0.927	12.648	-18.307	-18.307	0.000	0.000	0.000	0.000
36	A	97	ILE	0	0.016	0.006	8.487	0.372	0.372	0.000	0.000	0.000	0.000
37	A	98	GLN	0	-0.015	-0.009	10.495	-0.452	-0.452	0.000	0.000	0.000	0.000
38	A	99	GLY	0	0.046	0.030	10.619	0.097	0.097	0.000	0.000	0.000	0.000
39	A	100	LYS	1	0.822	0.888	11.503	15.653	15.653	0.000	0.000	0.000	0.000
40	A	101	HIS	0	0.007	0.030	12.177	-0.489	-0.489	0.000	0.000	0.000	0.000
41	A	102	GLY	0	0.017	0.000	15.492	0.110	0.110	0.000	0.000	0.000	0.000
42	A	103	GLU	-1	-0.969	-0.987	17.509	-13.914	-13.914	0.000	0.000	0.000	0.000
43	A	104	ARG	1	0.778	0.878	13.175	19.172	19.172	0.000	0.000	0.000	0.000
44	A	105	GLN	0	0.028	0.008	19.281	-0.053	-0.053	0.000	0.000	0.000	0.000
45	A	106	ASP	-1	-0.908	-0.958	17.186	-16.145	-16.145	0.000	0.000	0.000	0.000
46	A	107	ASP	-1	-0.927	-0.968	19.577	-13.475	-13.475	0.000	0.000	0.000	0.000
47	A	108	HIS	0	-0.080	-0.039	18.836	0.950	0.950	0.000	0.000	0.000	0.000
48	A	109	GLY	0	-0.025	-0.014	21.186	0.535	0.535	0.000	0.000	0.000	0.000
49	A	110	TYR	0	-0.009	0.004	20.115	0.227	0.227	0.000	0.000	0.000	0.000
50	A	111	ILE	0	0.012	0.017	13.157	-0.591	-0.591	0.000	0.000	0.000	0.000
51	A	112	SER	0	-0.004	0.007	15.829	0.029	0.029	0.000	0.000	0.000	0.000
52	A	113	ARG	1	0.907	0.943	9.284	21.775	21.775	0.000	0.000	0.000	0.000
53	A	114	GLU	-1	-0.786	-0.875	11.835	-16.509	-16.509	0.000	0.000	0.000	0.000
54	A	115	PHE	0	-0.040	0.002	7.440	-1.623	-1.623	0.000	0.000	0.000	0.000
55	A	116	HIS	1	0.872	0.903	9.478	20.369	20.369	0.000	0.000	0.000	0.000
56	A	117	ARG	1	0.865	0.943	4.978	32.961	32.961	0.000	0.000	0.000	0.000
57	A	118	ARG	1	0.928	0.964	8.788	18.162	18.162	0.000	0.000	0.000	0.000
58	A	119	TYR	0	-0.006	-0.028	5.526	-1.556	-1.556	0.000	0.000	0.000	0.000
59	A	120	ARG	1	0.941	0.992	11.805	16.926	16.926	0.000	0.000	0.000	0.000
60	A	121	LEU	0	0.016	0.019	15.287	-0.735	-0.735	0.000	0.000	0.000	0.000
61	A	122	PRO	0	-0.050	-0.028	16.687	0.657	0.657	0.000	0.000	0.000	0.000
62	A	123	SER	0	0.031	0.010	19.828	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	124	ASN	0	0.033	0.013	22.879	-0.173	-0.173	0.000	0.000	0.000	0.000
64	A	125	VAL	0	-0.008	-0.001	18.727	0.014	0.014	0.000	0.000	0.000	0.000
65	A	126	ASP	-1	-0.794	-0.861	22.001	-11.646	-11.646	0.000	0.000	0.000	0.000
66	A	127	GLN	0	0.012	-0.025	20.651	-0.213	-0.213	0.000	0.000	0.000	0.000
67	A	128	SER	0	-0.081	-0.044	22.023	-0.308	-0.308	0.000	0.000	0.000	0.000
68	A	129	ALA	0	0.010	-0.004	23.674	-0.089	-0.089	0.000	0.000	0.000	0.000
69	A	130	ILE	0	-0.068	-0.024	16.986	-0.525	-0.525	0.000	0.000	0.000	0.000
70	A	131	THR	0	-0.030	-0.006	18.462	0.377	0.377	0.000	0.000	0.000	0.000
71	A	132	CYS	0	-0.058	-0.047	12.961	-1.307	-1.307	0.000	0.000	0.000	0.000
72	A	133	THR	0	-0.028	-0.026	14.214	1.195	1.195	0.000	0.000	0.000	0.000
73	A	134	LEU	0	-0.006	-0.006	10.335	-2.081	-2.081	0.000	0.000	0.000	0.000
74	A	135	SER	0	0.084	0.050	11.185	1.019	1.019	0.000	0.000	0.000	0.000
75	A	136	ALA	0	0.058	0.026	12.931	-0.815	-0.815	0.000	0.000	0.000	0.000
76	A	137	ASP	-1	-0.927	-0.947	10.700	-22.360	-22.360	0.000	0.000	0.000	0.000
77	A	138	GLY	0	-0.013	-0.022	9.538	-2.951	-2.951	0.000	0.000	0.000	0.000
78	A	139	LEU	0	-0.051	-0.025	5.957	-5.006	-5.006	0.000	0.000	0.000	0.000
79	A	140	LEU	0	0.013	0.012	7.480	3.293	3.293	0.000	0.000	0.000	0.000
80	A	141	THR	0	0.026	-0.001	8.658	-4.007	-4.007	0.000	0.000	0.000	0.000
81	A	142	LEU	0	0.000	0.008	11.467	1.743	1.743	0.000	0.000	0.000	0.000
82	A	143	CYS	0	-0.052	-0.034	13.384	-0.461	-0.461	0.000	0.000	0.000	0.000
83	A	144	GLY	0	0.070	0.041	16.327	0.716	0.716	0.000	0.000	0.000	0.000
84	A	145	PRO	0	0.017	0.019	19.196	-0.388	-0.388	0.000	0.000	0.000	0.000
85	A	146	LYS	1	0.792	0.888	19.117	15.604	15.604	0.000	0.000	0.000	0.000
86	A	147	THR	0	0.020	0.010	23.848	0.508	0.508	0.000	0.000	0.000	0.000
87	A	148	SER	0	-0.031	-0.025	27.395	-0.180	-0.180	0.000	0.000	0.000	0.000
88	A	149	GLY	0	-0.014	0.005	30.127	0.240	0.240	0.000	0.000	0.000	0.000
89	A	150	ILE	0	0.015	-0.001	29.439	-0.354	-0.354	0.000	0.000	0.000	0.000
90	A	151	ASP	-1	-0.846	-0.926	28.300	-10.257	-10.257	0.000	0.000	0.000	0.000
91	A	152	ALA	0	-0.024	-0.002	29.033	0.062	0.062	0.000	0.000	0.000	0.000
92	A	153	GLY	0	0.036	0.019	27.107	-0.365	-0.365	0.000	0.000	0.000	0.000
93	A	154	ARG	1	0.711	0.837	23.197	11.593	11.593	0.000	0.000	0.000	0.000
94	A	155	GLY	0	0.017	-0.010	24.577	0.501	0.501	0.000	0.000	0.000	0.000
95	A	156	ASP	-1	-0.850	-0.910	22.549	-13.316	-13.316	0.000	0.000	0.000	0.000
96	A	157	ARG	1	0.802	0.888	21.009	14.238	14.238	0.000	0.000	0.000	0.000
97	A	158	THR	0	-0.018	-0.016	19.442	-0.726	-0.726	0.000	0.000	0.000	0.000
98	A	159	ILE	0	-0.044	-0.024	16.769	0.574	0.574	0.000	0.000	0.000	0.000
99	A	160	PRO	0	-0.001	-0.011	17.633	-0.683	-0.683	0.000	0.000	0.000	0.000
100	A	161	VAL	0	0.018	0.012	13.472	-0.395	-0.395	0.000	0.000	0.000	0.000
101	A	162	THR	0	-0.044	-0.012	16.200	0.822	0.822	0.000	0.000	0.000	0.000
102	A	163	ARG	1	0.916	0.944	16.577	14.239	14.239	0.000	0.000	0.000	0.000
103	A	164	GLU	-1	-0.861	-0.932	14.269	-20.688	-20.688	0.000	0.000	0.000	0.000
104	A	165	ASP	-2	-1.904	-1.922	18.154	-29.177	-29.177	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:62:VAL)