FMO DATABASE

FMODB ID: VV3N1

Calculation Name: 1WJS-A-Other547

Preferred Name: Lethal(3)malignant brain tumor-like protein 3

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1WJS

Chain ID: A

ChEMBL ID: CHEMBL1287623

UniProt ID: Q96JM7

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-974189.553726
FMO2-HF: Nuclear repulsion	924322.776669
FMO2-HF: Total energy	-49866.777057
FMO2-MP2: Total energy	-50009.858188

3D Structure

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:GLY)

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

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.
-3.353	-1.284	0.24	-1.134	-1.174	-0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / q_NPA : 0.920

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

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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	0.066	0.035	3.842	6.390	7.235	0.000	-0.362	-0.482	-0.001
4	A	4	GLY	0	0.013	0.002	2.938	-17.376	-16.316	0.243	-0.749	-0.555	-0.007
6	A	6	SER	0	-0.005	-0.004	4.433	-8.450	-8.413	-0.001	-0.016	-0.020	0.000
7	A	7	GLY	0	0.049	0.011	4.661	7.481	7.545	-0.001	-0.003	-0.059	0.000
8	A	8	PRO	0	-0.059	-0.005	4.789	-7.814	-7.751	-0.001	-0.004	-0.058	0.000
5	A	5	SER	0	-0.008	-0.009	5.165	4.007	4.007	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.010	0.002	5.723	3.331	3.331	0.000	0.000	0.000	0.000
10	A	10	ASN	0	0.004	-0.018	8.159	0.599	0.599	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.939	0.982	11.622	22.384	22.384	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.046	0.014	12.257	-1.408	-1.408	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.041	0.020	14.026	-0.852	-0.852	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.030	0.020	14.973	0.325	0.325	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.912	0.945	16.847	16.720	16.720	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.049	0.019	19.757	0.453	0.453	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.005	0.010	23.107	-0.137	-0.137	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.089	-0.008	19.915	0.247	0.247	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.836	0.933	25.346	9.942	9.942	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.012	-0.012	25.279	-0.405	-0.405	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.748	-0.889	28.759	-9.735	-9.735	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.028	0.004	29.684	-0.482	-0.482	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.020	0.007	31.467	0.309	0.309	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.808	-0.910	33.602	-8.477	-8.477	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.036	-0.032	35.397	0.016	0.016	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.953	-0.962	36.827	-7.414	-7.414	0.000	0.000	0.000	0.000
27	A	27	HIS	1	0.857	0.917	39.405	7.723	7.723	0.000	0.000	0.000	0.000
28	A	28	GLN	0	0.091	0.055	36.397	-0.082	-0.082	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.100	-0.068	37.650	0.080	0.080	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.031	0.014	39.234	0.117	0.117	0.000	0.000	0.000	0.000
31	A	31	TYR	0	0.033	0.013	33.438	-0.319	-0.319	0.000	0.000	0.000	0.000
32	A	32	CYS	0	0.001	0.000	35.312	0.317	0.317	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.005	0.007	32.915	-0.343	-0.343	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.018	0.011	30.085	0.123	0.123	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.025	-0.022	28.264	-0.173	-0.173	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.039	-0.004	22.279	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.071	0.029	25.751	-0.019	-0.019	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.896	-0.957	22.870	-12.758	-12.758	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.032	-0.014	17.481	-0.118	-0.118	0.000	0.000	0.000	0.000
40	A	40	CYS	0	-0.054	-0.028	17.739	-0.990	-0.990	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.036	0.022	15.709	0.393	0.393	0.000	0.000	0.000	0.000
42	A	42	TYR	0	-0.003	-0.009	14.214	-0.405	-0.405	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.941	0.973	17.323	14.244	14.244	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.005	0.000	19.896	-0.733	-0.733	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.879	0.954	22.303	11.832	11.832	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.014	-0.015	25.625	-0.210	-0.210	0.000	0.000	0.000	0.000
47	A	47	HIS	0	0.013	0.010	28.388	0.418	0.418	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.016	0.000	31.331	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.841	-0.919	34.500	-8.758	-8.758	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.049	0.024	35.734	0.269	0.269	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.055	-0.033	37.274	0.345	0.345	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.001	-0.003	37.740	-0.098	-0.098	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.805	-0.915	32.514	-9.654	-9.654	0.000	0.000	0.000	0.000
54	A	54	CYS	0	-0.112	-0.042	33.404	-0.132	-0.132	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.035	-0.026	35.782	0.127	0.127	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.804	-0.899	30.091	-10.301	-10.301	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.016	-0.005	29.089	-0.029	-0.029	0.000	0.000	0.000	0.000
58	A	58	TRP	0	-0.046	-0.031	21.539	-0.584	-0.584	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.025	0.024	24.546	0.151	0.151	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.032	-0.035	22.364	-0.291	-0.291	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.022	-0.018	18.337	0.213	0.213	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.891	-0.952	19.515	-15.183	-15.183	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.033	-0.007	21.324	0.414	0.414	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.001	0.003	25.080	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.836	-0.932	27.729	-10.653	-10.653	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.003	-0.002	23.695	0.245	0.245	0.000	0.000	0.000	0.000
67	A	67	HIS	1	0.793	0.884	27.433	10.618	10.618	0.000	0.000	0.000	0.000
68	A	68	PRO	0	-0.021	0.008	25.663	0.067	0.067	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.002	-0.016	27.544	0.284	0.284	0.000	0.000	0.000	0.000
70	A	70	GLY	0	-0.028	0.003	30.620	-0.052	-0.052	0.000	0.000	0.000	0.000
71	A	71	TRP	0	-0.010	-0.008	30.558	0.087	0.087	0.000	0.000	0.000	0.000
72	A	72	CYS	0	-0.028	0.004	32.886	0.112	0.112	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.836	-0.925	36.346	-8.372	-8.372	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.898	0.971	32.019	9.806	9.806	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.106	-0.067	34.172	0.029	0.029	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.025	0.024	36.902	0.151	0.151	0.000	0.000	0.000	0.000
77	A	77	HIS	0	-0.037	-0.012	37.411	0.297	0.297	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.878	0.931	40.156	7.090	7.090	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.010	0.002	35.956	-0.056	-0.056	0.000	0.000	0.000	0.000
80	A	80	HIS	0	-0.063	-0.034	39.101	0.390	0.390	0.000	0.000	0.000	0.000
81	A	81	PRO	0	-0.030	-0.008	39.133	-0.225	-0.225	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.043	0.031	38.059	0.017	0.017	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.892	0.943	39.973	7.855	7.855	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.037	-0.029	42.713	-0.018	-0.018	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.024	0.003	41.732	0.053	0.053	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.862	0.920	44.468	6.458	6.458	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.853	-0.937	43.090	-7.150	-7.150	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.804	-0.893	43.624	-6.506	-6.506	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.932	-0.958	45.647	-6.693	-6.693	0.000	0.000	0.000	0.000
90	A	90	PHE	0	-0.045	-0.026	36.020	-0.137	-0.137	0.000	0.000	0.000	0.000
91	A	91	ASN	0	0.010	0.011	40.506	-0.185	-0.185	0.000	0.000	0.000	0.000
92	A	92	TRP	0	0.079	0.021	31.784	-0.138	-0.138	0.000	0.000	0.000	0.000
93	A	93	GLN	0	0.007	0.003	35.713	-0.289	-0.289	0.000	0.000	0.000	0.000
94	A	94	THR	0	0.019	0.002	36.717	-0.127	-0.127	0.000	0.000	0.000	0.000
95	A	95	TYR	0	0.087	0.005	34.114	-0.129	-0.129	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.034	-0.015	30.581	-0.192	-0.192	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.977	0.992	33.228	7.809	7.809	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.052	-0.030	35.617	0.040	0.040	0.000	0.000	0.000	0.000
99	A	99	CYS	0	-0.047	-0.007	32.397	0.035	0.035	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.900	0.954	31.443	9.474	9.474	0.000	0.000	0.000	0.000
101	A	101	ALA	0	-0.009	0.011	28.673	-0.366	-0.366	0.000	0.000	0.000	0.000
102	A	102	GLN	0	-0.017	-0.018	25.001	0.201	0.201	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.035	0.011	26.455	-0.206	-0.206	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.011	0.013	23.518	-0.420	-0.420	0.000	0.000	0.000	0.000
105	A	105	PRO	0	-0.011	-0.009	19.923	0.339	0.339	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.997	0.972	22.026	12.048	12.048	0.000	0.000	0.000	0.000
107	A	107	SER	0	0.058	0.032	17.626	0.315	0.315	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.085	-0.036	17.276	-0.860	-0.860	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.037	0.006	19.691	0.136	0.136	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.915	-0.949	19.433	-13.721	-13.721	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.017	-0.008	18.915	-0.364	-0.364	0.000	0.000	0.000	0.000
112	A	112	GLN	0	-0.030	0.005	22.102	0.185	0.185	0.000	0.000	0.000	0.000
113	A	113	ASN	0	-0.020	-0.014	23.740	0.538	0.538	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.021	-0.008	27.525	0.221	0.221	0.000	0.000	0.000	0.000
115	A	115	THR	0	-0.014	-0.003	29.721	-0.306	-0.306	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.002	-0.004	29.819	0.270	0.270	0.000	0.000	0.000	0.000
117	A	117	ILE	0	0.056	0.030	32.507	0.076	0.076	0.000	0.000	0.000	0.000
118	A	118	PRO	0	0.002	-0.010	35.987	-0.089	-0.089	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.047	-0.029	36.957	0.120	0.120	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.027	0.028	39.440	0.142	0.142	0.000	0.000	0.000	0.000
121	A	121	PHE	0	-0.003	-0.007	42.925	0.093	0.093	0.000	0.000	0.000	0.000
122	A	122	SER	0	-0.019	-0.021	42.602	-0.268	-0.268	0.000	0.000	0.000	0.000
123	A	123	GLY	0	-0.007	0.012	43.753	0.176	0.176	0.000	0.000	0.000	0.000
124	A	124	PRO	0	-0.005	-0.002	44.970	-0.102	-0.102	0.000	0.000	0.000	0.000
125	A	125	SER	0	-0.026	-0.020	43.491	-0.161	-0.161	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.042	-0.028	45.576	0.105	0.105	0.000	0.000	0.000	0.000
127	A	127	GLY	-1	-0.918	-0.938	46.293	-6.631	-6.631	0.000	0.000	0.000	0.000

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