FMO DATABASE

FMODB ID: 24GRR

Calculation Name: 1EGX-A-Other547

Preferred Name: Vasodilator-stimulated phosphoprotein

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EGX

Chain ID: A

ChEMBL ID: CHEMBL4295774

UniProt ID: P50552

Base Structure: SolutionNMR

Registration Date: 2025-09-02

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-914987.917178
FMO2-HF: Nuclear repulsion	869574.843005
FMO2-HF: Total energy	-45413.074173
FMO2-MP2: Total energy	-45543.120129

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:1:MET)

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

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.
8.703	13.22	2.617	-1.866	-5.268	-0.02

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.823 / q_NPA : 0.911

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	3	GLU	-1	-0.782	-0.888	3.388	-34.574	-33.062	1.689	-0.588	-2.613	-0.009
4	A	4	THR	0	-0.021	-0.010	3.015	-13.065	-11.263	0.219	-0.935	-1.085	-0.008
5	A	5	VAL	0	-0.030	-0.007	2.353	3.816	4.671	0.710	-0.304	-1.262	-0.003
6	A	6	ILE	0	-0.028	0.010	4.171	0.082	0.164	0.000	-0.017	-0.064	0.000
39	A	39	TYR	0	-0.045	-0.024	4.950	-1.926	-1.660	-0.001	-0.022	-0.244	0.000
7	A	7	CYS	0	-0.010	0.000	7.861	0.843	0.843	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.058	-0.027	8.295	-0.641	-0.641	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.001	0.012	10.058	0.980	0.980	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.929	0.974	13.609	12.022	12.022	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.044	-0.006	16.292	0.690	0.690	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.028	-0.014	17.720	-0.540	-0.540	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.016	-0.012	16.402	0.360	0.360	0.000	0.000	0.000	0.000
14	A	14	MET	0	-0.018	0.000	19.735	0.291	0.291	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.049	0.024	21.644	-0.329	-0.329	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.033	-0.028	24.131	0.454	0.454	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.866	-0.936	27.397	-9.248	-9.248	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.879	-0.963	30.198	-8.900	-8.900	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.047	-0.010	32.594	0.260	0.260	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.064	-0.046	34.041	0.415	0.415	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.895	0.957	33.793	7.774	7.774	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.930	0.985	31.732	8.539	8.539	0.000	0.000	0.000	0.000
23	A	23	TRP	0	0.045	0.015	24.674	-0.291	-0.291	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.014	0.004	27.066	0.319	0.319	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.030	-0.015	24.289	-0.341	-0.341	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.009	0.013	20.162	0.073	0.073	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.024	0.024	20.271	-0.232	-0.232	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.022	-0.026	21.000	0.446	0.446	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.026	0.018	23.835	0.046	0.046	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.019	0.000	24.768	0.111	0.111	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.043	-0.039	23.155	-0.470	-0.470	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.041	0.017	21.823	0.315	0.315	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.002	0.016	18.786	-0.539	-0.539	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.037	-0.042	15.142	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.959	0.989	10.788	17.636	17.636	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.006	-0.003	11.422	-0.920	-0.920	0.000	0.000	0.000	0.000
37	A	37	GLN	0	0.013	-0.009	5.112	0.225	0.225	0.000	0.000	0.000	0.000
38	A	38	ILE	0	0.021	0.027	8.049	0.668	0.668	0.000	0.000	0.000	0.000
40	A	40	HIS	0	0.089	0.027	6.893	1.957	1.957	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.036	-0.024	8.313	-3.510	-3.510	0.000	0.000	0.000	0.000
42	A	42	PRO	0	0.089	0.040	10.178	1.749	1.749	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.047	-0.024	10.901	1.905	1.905	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.011	0.007	13.517	1.002	1.002	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.030	-0.006	15.744	0.376	0.376	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.019	0.002	14.448	1.347	1.347	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.059	0.042	10.801	-2.104	-2.104	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.835	0.907	8.432	28.542	28.542	0.000	0.000	0.000	0.000
49	A	49	VAL	0	0.002	0.015	10.134	-1.408	-1.408	0.000	0.000	0.000	0.000
50	A	50	VAL	0	0.016	-0.002	8.270	0.679	0.679	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.014	0.004	9.631	-0.653	-0.653	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.930	0.986	9.621	21.135	21.135	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.898	0.963	13.573	13.122	13.122	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.077	-0.032	15.430	-1.231	-1.231	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.014	-0.018	17.408	0.523	0.523	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.054	0.011	17.930	-0.673	-0.673	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.841	-0.902	18.363	-13.113	-13.113	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.079	-0.041	13.388	-0.740	-0.740	0.000	0.000	0.000	0.000
59	A	59	GLN	0	0.051	0.057	14.704	-0.553	-0.553	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.019	-0.006	12.564	-0.203	-0.203	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.028	-0.033	15.275	0.848	0.848	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.019	0.012	13.386	0.667	0.667	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.030	-0.017	13.142	-1.003	-1.003	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.015	0.023	14.170	0.670	0.670	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.026	0.007	14.310	-0.985	-0.985	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.003	-0.006	13.239	0.787	0.787	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.007	-0.009	16.206	-0.725	-0.725	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.900	0.959	18.766	13.047	13.047	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.102	0.055	21.564	0.435	0.435	0.000	0.000	0.000	0.000
70	A	70	VAL	0	-0.072	-0.012	18.975	0.406	0.406	0.000	0.000	0.000	0.000
71	A	71	LYS	1	1.009	0.989	21.198	10.456	10.456	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.049	-0.032	15.153	0.265	0.265	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.019	-0.016	21.735	0.296	0.296	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.065	-0.027	22.989	0.454	0.454	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.010	0.023	24.460	0.277	0.277	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.028	0.003	26.052	0.259	0.259	0.000	0.000	0.000	0.000
77	A	77	PRO	0	0.050	0.022	25.255	-0.362	-0.362	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.046	-0.013	23.206	-0.161	-0.161	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.009	0.013	22.857	-0.208	-0.208	0.000	0.000	0.000	0.000
80	A	80	HIS	0	0.003	0.010	18.814	0.278	0.278	0.000	0.000	0.000	0.000
81	A	81	GLN	0	0.023	0.008	21.271	-0.119	-0.119	0.000	0.000	0.000	0.000
82	A	82	TRP	0	0.020	0.012	16.744	0.092	0.092	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.934	0.960	22.820	9.509	9.509	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.824	-0.907	21.282	-13.026	-13.026	0.000	0.000	0.000	0.000
85	A	85	ALA	0	-0.024	0.000	23.405	0.403	0.403	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.934	0.947	25.857	9.917	9.917	0.000	0.000	0.000	0.000
87	A	87	GLN	0	0.004	0.022	23.524	0.134	0.134	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.004	-0.016	24.137	-0.070	-0.070	0.000	0.000	0.000	0.000
89	A	89	TRP	0	0.064	0.019	18.818	-0.073	-0.073	0.000	0.000	0.000	0.000
90	A	90	GLY	0	0.039	-0.015	21.392	0.069	0.069	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.055	-0.001	16.289	0.048	0.048	0.000	0.000	0.000	0.000
92	A	92	ASN	0	0.050	0.024	20.647	0.377	0.377	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.036	-0.031	16.521	-0.307	-0.307	0.000	0.000	0.000	0.000
94	A	94	GLY	0	-0.002	0.000	20.398	0.501	0.501	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.060	-0.041	21.053	0.537	0.537	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.993	0.982	21.222	9.620	9.620	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.889	-0.935	18.416	-13.238	-13.238	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.872	-0.932	16.646	-14.129	-14.129	0.000	0.000	0.000	0.000
99	A	99	ALA	0	0.042	0.009	16.727	-0.604	-0.604	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.005	0.008	18.769	-0.156	-0.156	0.000	0.000	0.000	0.000
101	A	101	GLN	0	0.056	0.019	13.037	-0.442	-0.442	0.000	0.000	0.000	0.000
102	A	102	PHE	0	0.021	-0.011	11.954	-0.758	-0.758	0.000	0.000	0.000	0.000
103	A	103	ALA	0	-0.013	-0.004	14.792	-0.351	-0.351	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.004	0.013	14.843	-0.045	-0.045	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.022	-0.007	11.813	-0.336	-0.336	0.000	0.000	0.000	0.000
106	A	106	MET	0	-0.008	-0.006	12.644	-0.705	-0.705	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.004	0.000	14.882	0.092	0.092	0.000	0.000	0.000	0.000
108	A	108	SER	0	0.033	0.024	13.791	0.122	0.122	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.004	-0.018	12.824	-0.166	-0.166	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.065	-0.043	14.633	0.275	0.275	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.895	-0.946	18.348	-12.947	-12.947	0.000	0.000	0.000	0.000
112	A	112	ALA	0	-0.013	-0.004	15.830	0.190	0.190	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.099	-0.043	16.111	-0.330	-0.330	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-1.018	-1.015	19.261	-11.369	-11.369	0.000	0.000	0.000	0.000
115	A	115	GLY	-1	-0.973	-0.960	22.203	-12.203	-12.203	0.000	0.000	0.000	0.000

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