FMO DATABASE

FMODB ID: VV3V1

Calculation Name: 1WI8-A-Other547

Preferred Name: Eukaryotic translation initiation factor 4B

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1WI8

Chain ID: A

ChEMBL ID: CHEMBL3308928

UniProt ID: P23588

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

Total energy (hartree)

FMO2-HF: Electronic energy	-680049.490512
FMO2-HF: Nuclear repulsion	641195.748997
FMO2-HF: Total energy	-38853.741515
FMO2-MP2: Total energy	-38969.225277

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:81:GLY)

Summations of interaction energy for fragment #1(A:81: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.
-32.325	-31.276	-0.015	-0.45	-0.585	-0.002

Interaction energy analysis for fragmet #1(A:81:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.857 / q_NPA : 0.915

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	83	SER	0	0.018	0.017	3.840	2.246	3.295	-0.015	-0.450	-0.585	-0.002
4	A	84	GLY	0	0.039	0.009	7.181	-0.812	-0.812	0.000	0.000	0.000	0.000
5	A	85	SER	0	-0.039	-0.021	9.969	1.309	1.309	0.000	0.000	0.000	0.000
6	A	86	SER	0	0.025	0.009	13.766	-0.489	-0.489	0.000	0.000	0.000	0.000
7	A	87	GLY	0	0.003	0.000	16.975	0.139	0.139	0.000	0.000	0.000	0.000
8	A	88	SER	0	-0.028	-0.005	20.614	0.401	0.401	0.000	0.000	0.000	0.000
9	A	89	ARG	1	0.906	0.946	23.386	12.614	12.614	0.000	0.000	0.000	0.000
10	A	90	LEU	0	0.048	0.035	27.024	0.066	0.066	0.000	0.000	0.000	0.000
11	A	91	PRO	0	0.047	0.029	29.403	0.151	0.151	0.000	0.000	0.000	0.000
12	A	92	LYS	1	0.919	0.945	32.721	9.435	9.435	0.000	0.000	0.000	0.000
13	A	93	SER	0	-0.040	-0.028	35.072	0.253	0.253	0.000	0.000	0.000	0.000
14	A	94	PRO	0	0.018	0.042	36.735	-0.195	-0.195	0.000	0.000	0.000	0.000
15	A	95	PRO	0	0.050	0.020	36.794	0.164	0.164	0.000	0.000	0.000	0.000
16	A	96	TYR	0	-0.042	-0.031	33.293	-0.232	-0.232	0.000	0.000	0.000	0.000
17	A	97	THR	0	-0.001	-0.019	31.302	-0.091	-0.091	0.000	0.000	0.000	0.000
18	A	98	ALA	0	-0.006	0.004	27.983	-0.325	-0.325	0.000	0.000	0.000	0.000
19	A	99	PHE	0	-0.037	-0.028	21.237	0.097	0.097	0.000	0.000	0.000	0.000
20	A	100	LEU	0	0.020	0.014	24.195	-0.312	-0.312	0.000	0.000	0.000	0.000
21	A	101	GLY	0	0.034	0.004	21.392	0.179	0.179	0.000	0.000	0.000	0.000
22	A	102	ASN	0	-0.082	-0.052	17.940	-0.769	-0.769	0.000	0.000	0.000	0.000
23	A	103	LEU	0	0.045	0.042	20.493	0.055	0.055	0.000	0.000	0.000	0.000
24	A	104	PRO	0	-0.053	-0.032	23.805	-0.304	-0.304	0.000	0.000	0.000	0.000
25	A	105	TYR	0	-0.018	-0.034	25.477	0.192	0.192	0.000	0.000	0.000	0.000
26	A	106	ASP	-1	-0.940	-0.970	28.280	-10.006	-10.006	0.000	0.000	0.000	0.000
27	A	107	VAL	0	-0.004	0.018	28.189	0.282	0.282	0.000	0.000	0.000	0.000
28	A	108	THR	0	0.037	0.010	30.739	0.034	0.034	0.000	0.000	0.000	0.000
29	A	109	GLU	-1	-0.934	-0.988	33.893	-8.358	-8.358	0.000	0.000	0.000	0.000
30	A	110	GLU	-1	-0.898	-0.957	35.930	-8.306	-8.306	0.000	0.000	0.000	0.000
31	A	111	SER	0	0.017	0.020	31.720	-0.176	-0.176	0.000	0.000	0.000	0.000
32	A	112	ILE	0	0.002	-0.009	30.911	-0.217	-0.217	0.000	0.000	0.000	0.000
33	A	113	LYS	1	0.923	0.960	32.852	7.991	7.991	0.000	0.000	0.000	0.000
34	A	114	GLU	-1	-0.975	-0.980	32.995	-9.343	-9.343	0.000	0.000	0.000	0.000
35	A	115	PHE	0	-0.006	0.000	25.146	-0.056	-0.056	0.000	0.000	0.000	0.000
36	A	116	PHE	0	0.017	0.002	28.600	-0.212	-0.212	0.000	0.000	0.000	0.000
37	A	117	ARG	1	0.974	0.986	32.957	8.361	8.361	0.000	0.000	0.000	0.000
38	A	118	GLY	0	-0.063	-0.035	35.260	-0.098	-0.098	0.000	0.000	0.000	0.000
39	A	119	LEU	0	-0.026	0.007	31.824	0.049	0.049	0.000	0.000	0.000	0.000
40	A	120	ASN	0	-0.014	-0.012	36.509	0.109	0.109	0.000	0.000	0.000	0.000
41	A	121	ILE	0	-0.070	-0.031	34.913	-0.084	-0.084	0.000	0.000	0.000	0.000
42	A	122	SER	0	-0.017	0.000	37.852	0.259	0.259	0.000	0.000	0.000	0.000
43	A	123	ALA	0	-0.009	-0.018	38.120	0.176	0.176	0.000	0.000	0.000	0.000
44	A	124	VAL	0	0.023	0.018	34.169	-0.297	-0.297	0.000	0.000	0.000	0.000
45	A	125	ARG	1	0.946	0.969	33.663	8.842	8.842	0.000	0.000	0.000	0.000
46	A	126	LEU	0	0.035	0.016	31.234	-0.380	-0.380	0.000	0.000	0.000	0.000
47	A	127	PRO	0	-0.017	0.001	30.314	0.304	0.304	0.000	0.000	0.000	0.000
48	A	128	ARG	1	0.952	0.980	31.709	9.122	9.122	0.000	0.000	0.000	0.000
49	A	129	GLU	-1	-0.874	-0.953	29.908	-10.887	-10.887	0.000	0.000	0.000	0.000
50	A	130	PRO	0	-0.062	-0.022	32.353	0.299	0.299	0.000	0.000	0.000	0.000
51	A	131	SER	0	-0.015	-0.002	33.508	0.234	0.234	0.000	0.000	0.000	0.000
52	A	132	ASN	0	0.004	-0.009	33.518	0.118	0.118	0.000	0.000	0.000	0.000
53	A	133	PRO	0	0.073	0.028	34.520	-0.256	-0.256	0.000	0.000	0.000	0.000
54	A	134	GLU	-1	-0.922	-0.959	35.987	-8.490	-8.490	0.000	0.000	0.000	0.000
55	A	135	ARG	1	0.884	0.948	29.092	10.497	10.497	0.000	0.000	0.000	0.000
56	A	136	LEU	0	0.011	0.001	29.025	0.156	0.156	0.000	0.000	0.000	0.000
57	A	137	LYS	1	0.906	0.957	27.970	10.078	10.078	0.000	0.000	0.000	0.000
58	A	138	GLY	0	0.009	0.016	24.493	-0.388	-0.388	0.000	0.000	0.000	0.000
59	A	139	PHE	0	-0.039	-0.023	23.977	-0.446	-0.446	0.000	0.000	0.000	0.000
60	A	140	GLY	0	-0.023	-0.019	25.756	0.498	0.498	0.000	0.000	0.000	0.000
61	A	141	TYR	0	-0.012	-0.009	27.847	-0.405	-0.405	0.000	0.000	0.000	0.000
62	A	142	ALA	0	-0.019	-0.004	30.481	0.270	0.270	0.000	0.000	0.000	0.000
63	A	143	GLU	-1	-0.833	-0.882	32.655	-9.156	-9.156	0.000	0.000	0.000	0.000
64	A	144	PHE	0	-0.009	-0.023	31.008	0.137	0.137	0.000	0.000	0.000	0.000
65	A	145	GLU	-1	-0.864	-0.933	36.388	-7.769	-7.769	0.000	0.000	0.000	0.000
66	A	146	ASP	-1	-0.881	-0.934	38.067	-7.843	-7.843	0.000	0.000	0.000	0.000
67	A	147	LEU	0	-0.009	-0.017	34.546	-0.253	-0.253	0.000	0.000	0.000	0.000
68	A	148	ASP	-1	-0.876	-0.944	33.112	-9.156	-9.156	0.000	0.000	0.000	0.000
69	A	149	SER	0	-0.003	0.015	32.906	-0.174	-0.174	0.000	0.000	0.000	0.000
70	A	150	LEU	0	0.020	0.010	28.805	-0.304	-0.304	0.000	0.000	0.000	0.000
71	A	151	LEU	0	-0.039	-0.024	27.995	-0.459	-0.459	0.000	0.000	0.000	0.000
72	A	152	SER	0	-0.009	-0.024	28.013	-0.369	-0.369	0.000	0.000	0.000	0.000
73	A	153	ALA	0	0.001	0.001	28.107	-0.309	-0.309	0.000	0.000	0.000	0.000
74	A	154	LEU	0	-0.029	-0.016	23.626	-0.476	-0.476	0.000	0.000	0.000	0.000
75	A	155	SER	0	-0.020	-0.005	23.267	-0.558	-0.558	0.000	0.000	0.000	0.000
76	A	156	LEU	0	0.013	0.016	24.206	-0.170	-0.170	0.000	0.000	0.000	0.000
77	A	157	ASN	0	-0.125	-0.055	18.165	0.141	0.141	0.000	0.000	0.000	0.000
78	A	158	GLU	-1	-0.922	-0.975	18.420	-16.947	-16.947	0.000	0.000	0.000	0.000
79	A	159	GLU	-1	-0.905	-0.943	19.749	-12.731	-12.731	0.000	0.000	0.000	0.000
80	A	160	SER	0	-0.082	-0.058	22.318	-0.342	-0.342	0.000	0.000	0.000	0.000
81	A	161	LEU	0	0.054	0.043	23.606	0.495	0.495	0.000	0.000	0.000	0.000
82	A	162	GLY	0	0.054	0.021	26.076	-0.184	-0.184	0.000	0.000	0.000	0.000
83	A	163	ASN	0	-0.054	-0.034	24.854	-0.457	-0.457	0.000	0.000	0.000	0.000
84	A	164	LYS	1	0.872	0.935	20.596	13.229	13.229	0.000	0.000	0.000	0.000
85	A	165	ARG	1	0.966	1.002	16.295	17.634	17.634	0.000	0.000	0.000	0.000
86	A	166	ILE	0	-0.001	0.020	20.018	-0.526	-0.526	0.000	0.000	0.000	0.000
87	A	167	ARG	1	0.942	0.977	13.871	19.459	19.459	0.000	0.000	0.000	0.000
88	A	168	VAL	0	0.013	0.005	20.008	0.368	0.368	0.000	0.000	0.000	0.000
89	A	169	ASP	-1	-0.866	-0.921	21.284	-14.976	-14.976	0.000	0.000	0.000	0.000
90	A	170	VAL	0	-0.024	-0.024	23.253	0.612	0.612	0.000	0.000	0.000	0.000
91	A	171	ALA	0	-0.046	-0.013	25.598	-0.391	-0.391	0.000	0.000	0.000	0.000
92	A	172	ASP	-1	-0.911	-0.957	27.988	-10.375	-10.375	0.000	0.000	0.000	0.000
93	A	173	GLN	0	-0.048	-0.023	29.908	0.004	0.004	0.000	0.000	0.000	0.000
94	A	174	ALA	0	-0.041	-0.020	32.170	0.221	0.221	0.000	0.000	0.000	0.000
95	A	175	GLN	0	-0.012	-0.003	34.134	0.210	0.210	0.000	0.000	0.000	0.000
96	A	176	ASP	-1	-0.905	-0.943	37.223	-8.771	-8.771	0.000	0.000	0.000	0.000
97	A	177	LYS	1	0.877	0.924	40.196	6.983	6.983	0.000	0.000	0.000	0.000
98	A	178	ASP	-1	-0.882	-0.924	44.005	-7.456	-7.456	0.000	0.000	0.000	0.000
99	A	179	SER	0	-0.089	-0.062	46.484	0.169	0.169	0.000	0.000	0.000	0.000
100	A	180	GLY	0	0.036	0.014	50.148	-0.092	-0.092	0.000	0.000	0.000	0.000
101	A	181	PRO	0	-0.026	-0.005	52.805	0.072	0.072	0.000	0.000	0.000	0.000
102	A	182	SER	0	-0.020	-0.021	56.521	-0.018	-0.018	0.000	0.000	0.000	0.000
103	A	183	SER	0	-0.044	-0.034	59.434	0.053	0.053	0.000	0.000	0.000	0.000
104	A	184	GLY	-1	-0.917	-0.929	63.062	-4.896	-4.896	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:81:GLY)