FMO DATABASE

FMODB ID: MZ94Z

Calculation Name: 4V6X-A-Other547

Preferred Name: Elongation factor 2

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4V6X

Chain ID: A

ChEMBL ID: CHEMBL1795108

UniProt ID: P13639

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1168144.499565
FMO2-HF: Nuclear repulsion	1114170.275194
FMO2-HF: Total energy	-53974.224371
FMO2-MP2: Total energy	-54135.081588

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:2:LYS)

Summations of interaction energy for fragment #1(A:2:LYS)

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.
433.319	438.642	16.182	-8.784	-12.72	-0.104

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.703 / q_NPA : 1.846

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	4	ASN	0	0.068	0.042	3.656	1.147	4.715	-0.009	-1.659	-1.900	-0.010
4	A	5	PRO	0	0.065	0.032	1.964	-48.220	-47.416	5.571	-3.249	-3.126	-0.046
5	A	6	PHE	0	0.048	0.024	3.952	-3.168	-2.897	-0.001	-0.082	-0.188	-0.001
6	A	7	VAL	0	-0.029	-0.006	2.541	6.308	8.110	0.716	-0.636	-1.882	-0.002
7	A	8	THR	0	-0.008	-0.013	2.161	-31.117	-33.546	9.571	-2.998	-4.143	-0.042
8	A	9	SER	0	0.012	-0.004	2.628	-1.045	0.198	0.333	-0.129	-1.446	-0.003
9	A	10	ASP	-1	-0.791	-0.873	4.173	-44.252	-44.188	0.001	-0.031	-0.035	0.000
10	A	11	ARG	1	1.025	0.999	7.253	40.344	40.344	0.000	0.000	0.000	0.000
11	A	12	SER	0	-0.008	-0.015	10.525	3.203	3.203	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.974	0.987	7.885	57.676	57.676	0.000	0.000	0.000	0.000
13	A	14	ASN	0	-0.009	-0.007	6.730	2.189	2.189	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.979	0.985	10.472	35.406	35.406	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.999	1.011	13.875	34.756	34.756	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.955	0.971	9.444	50.567	50.567	0.000	0.000	0.000	0.000
17	A	18	HIS	0	0.018	0.023	13.998	0.001	0.001	0.000	0.000	0.000	0.000
18	A	19	PHE	0	0.012	0.002	15.730	1.536	1.536	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.003	-0.004	17.784	2.090	2.090	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.025	0.041	17.351	0.093	0.093	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.069	0.046	18.433	1.646	1.646	0.000	0.000	0.000	0.000
22	A	23	SER	0	0.039	0.005	21.508	-0.841	-0.841	0.000	0.000	0.000	0.000
23	A	24	HIS	0	0.058	0.026	20.365	-0.773	-0.773	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.041	0.018	16.011	-0.245	-0.245	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.819	0.895	19.068	26.049	26.049	0.000	0.000	0.000	0.000
26	A	27	ARG	0	0.088	0.073	21.023	-0.731	-0.731	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.868	0.909	17.604	28.218	28.218	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.016	-0.005	15.880	-0.545	-0.545	0.000	0.000	0.000	0.000
29	A	30	MET	0	-0.069	-0.015	18.321	0.316	0.316	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.001	0.003	18.810	0.957	0.957	0.000	0.000	0.000	0.000
31	A	32	SER	0	0.028	0.020	21.322	-0.233	-0.233	0.000	0.000	0.000	0.000
32	A	33	PRO	0	-0.081	-0.052	21.999	-0.328	-0.328	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.032	0.033	23.375	0.680	0.680	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.018	0.005	26.390	-0.366	-0.366	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.922	0.937	26.835	20.916	20.916	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.834	-0.897	29.682	-17.310	-17.310	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.041	0.015	30.275	-0.167	-0.167	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.845	0.914	23.402	23.192	23.192	0.000	0.000	0.000	0.000
39	A	40	GLN	0	0.020	-0.001	27.818	-0.255	-0.255	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.861	0.947	30.578	17.580	17.580	0.000	0.000	0.000	0.000
41	A	42	TYR	-1	-0.821	-0.913	28.632	-18.361	-18.361	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.040	-0.007	26.140	-0.336	-0.336	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.026	0.006	22.839	-1.114	-1.114	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.907	0.957	18.203	29.029	29.029	0.000	0.000	0.000	0.000
45	A	46	SER	0	0.023	-0.010	19.193	0.436	0.436	0.000	0.000	0.000	0.000
46	A	47	MET	0	0.041	0.028	22.014	-0.993	-0.993	0.000	0.000	0.000	0.000
47	A	48	PRO	0	-0.062	-0.032	21.353	-0.067	-0.067	0.000	0.000	0.000	0.000
48	A	49	ILE	0	-0.007	0.017	23.646	0.535	0.535	0.000	0.000	0.000	0.000
49	A	50	ARG	0	-0.035	0.004	26.838	-0.040	-0.040	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.880	0.930	30.160	16.343	16.343	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.805	-0.912	33.498	-15.909	-15.909	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.800	-0.898	30.752	-19.410	-19.410	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.818	-0.908	33.590	-16.184	-16.184	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.044	-0.032	30.336	-0.766	-0.766	0.000	0.000	0.000	0.000
55	A	56	GLN	0	0.045	0.029	31.692	0.517	0.517	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.022	0.002	30.562	-0.855	-0.855	0.000	0.000	0.000	0.000
57	A	58	VAL	0	-0.028	-0.012	26.931	0.285	0.285	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.869	0.919	24.433	22.340	22.340	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.059	0.029	29.137	0.184	0.184	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.039	0.010	31.432	-0.376	-0.376	0.000	0.000	0.000	0.000
61	A	62	TYR	0	0.039	0.022	34.273	0.329	0.329	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.892	0.957	30.750	18.585	18.585	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.051	0.023	32.862	-0.215	-0.215	0.000	0.000	0.000	0.000
64	A	65	GLN	0	0.048	0.016	34.913	0.384	0.384	0.000	0.000	0.000	0.000
65	A	66	GLN	0	-0.006	-0.006	36.431	-0.333	-0.333	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.100	-0.043	36.520	0.068	0.068	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.053	0.034	36.188	0.521	0.521	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.995	1.028	35.431	14.615	14.615	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.036	-0.014	30.765	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.049	0.025	34.163	0.274	0.274	0.000	0.000	0.000	0.000
71	A	72	GLN	0	-0.001	-0.020	33.849	-0.199	-0.199	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.045	0.022	27.586	-0.435	-0.435	0.000	0.000	0.000	0.000
73	A	74	TYR	0	0.032	0.030	29.547	-0.341	-0.341	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.952	0.944	25.031	22.147	22.147	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.964	0.982	25.169	20.146	20.146	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.956	0.976	26.604	18.914	18.914	0.000	0.000	0.000	0.000
77	A	78	TYR	0	-0.093	-0.064	18.641	-0.301	-0.301	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.047	0.005	24.536	-0.536	-0.536	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.017	-0.012	26.973	0.115	0.115	0.000	0.000	0.000	0.000
80	A	81	TYR	0	0.011	-0.004	29.457	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.005	0.002	31.597	-0.080	-0.080	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.771	-0.889	34.933	-14.853	-14.853	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.919	0.974	37.946	14.414	14.414	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.049	-0.037	34.812	0.185	0.185	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.033	-0.030	37.319	-0.283	-0.283	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.903	0.964	37.115	15.984	15.984	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.882	-0.940	40.752	-13.466	-13.466	0.000	0.000	0.000	0.000
88	A	89	LYS	0	-0.077	-0.040	43.601	-0.333	-0.333	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.029	0.001	45.634	0.197	0.197	0.000	0.000	0.000	0.000
90	A	91	ASN	0	0.050	0.034	48.542	0.220	0.220	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.056	0.034	49.740	0.080	0.080	0.000	0.000	0.000	0.000
92	A	93	THR	0	-0.034	-0.006	45.806	-0.060	-0.060	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.027	0.010	43.249	-0.253	-0.253	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.018	0.003	38.191	-0.146	-0.146	0.000	0.000	0.000	0.000
95	A	96	HIS	0	-0.028	-0.014	36.054	-0.018	-0.018	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.052	-0.017	33.013	-0.287	-0.287	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.016	-0.022	31.124	-0.212	-0.212	0.000	0.000	0.000	0.000
98	A	99	ILE	0	0.032	0.016	28.256	-0.355	-0.355	0.000	0.000	0.000	0.000
99	A	100	HIS	0	0.079	0.058	20.166	-0.242	-0.242	0.000	0.000	0.000	0.000
100	A	101	PRO	0	0.055	0.035	22.175	0.319	0.319	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.014	-0.036	20.234	0.104	0.104	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.822	0.895	20.941	26.404	26.404	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.027	0.026	25.429	0.951	0.951	0.000	0.000	0.000	0.000
104	A	105	VAL	0	-0.053	-0.020	25.857	-1.007	-1.007	0.000	0.000	0.000	0.000
105	A	106	ILE	0	0.029	0.021	26.694	0.637	0.637	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.041	-0.049	29.631	0.003	0.003	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.958	0.961	32.965	16.354	16.354	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.064	-0.006	28.296	-0.304	-0.304	0.000	0.000	0.000	0.000
109	A	110	LYS	0	0.019	0.014	32.849	0.589	0.589	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.025	-0.026	32.507	-0.708	-0.708	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.772	-0.862	33.416	-17.444	-17.444	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.978	0.965	33.816	15.850	15.850	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.862	-0.931	30.183	-19.702	-19.702	0.000	0.000	0.000	0.000
114	A	115	ARG	0	-0.133	-0.076	29.219	-0.885	-0.885	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.926	0.966	29.267	17.589	17.589	0.000	0.000	0.000	0.000
116	A	117	LYS	1	1.029	1.028	27.621	21.061	21.061	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.043	-0.036	23.991	-1.006	-1.006	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.019	-0.002	24.987	-1.157	-1.157	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.843	-0.921	26.436	-19.525	-19.525	0.000	0.000	0.000	0.000
120	A	121	ARG	0	0.015	0.005	22.304	0.206	0.206	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.869	0.944	20.556	26.291	26.291	0.000	0.000	0.000	0.000
122	A	123	ALA	0	0.056	0.029	22.784	-0.799	-0.799	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.981	0.987	23.814	23.187	23.187	0.000	0.000	0.000	0.000
124	A	125	SER	0	-0.030	-0.033	18.892	-0.949	-0.949	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.902	0.957	19.976	23.921	23.921	0.000	0.000	0.000	0.000
126	A	127	GLN	0	-0.063	-0.028	21.651	-0.014	-0.014	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.081	0.043	19.189	-0.102	-0.102	0.000	0.000	0.000	0.000
128	A	129	GLY	0	-0.014	-0.006	18.064	-0.673	-0.673	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.883	0.928	18.886	21.803	21.803	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.931	-0.955	21.563	-22.501	-22.501	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.938	0.969	14.702	35.024	35.024	0.000	0.000	0.000	0.000
132	A	133	GLY	0	-0.081	-0.051	18.603	-1.154	-1.154	0.000	0.000	0.000	0.000
133	A	134	LYS	0	0.064	0.062	19.485	-3.778	-3.778	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)