FMO DATABASE

FMODB ID: 9QL42

Calculation Name: 7MOQ-H-Other547

Preferred Name:

Target Type:

Ligand Name: guanosine-5'-triphosphate | adenosine-5'-triphosphate | guanosine-5'-diphosphate | adenosine-5'-diphosphate

Ligand 3-letter code: GTP | ATP | GDP | ADP

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7MOQ

Chain ID: H

ChEMBL ID:

UniProt ID:

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-629769.21479
FMO2-HF: Nuclear repulsion	594628.576159
FMO2-HF: Total energy	-35140.638631
FMO2-MP2: Total energy	-35242.347971

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:8:GLN)

Summations of interaction energy for fragment #1(A:8:GLN)

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.
-22.218	-17.51	0.624	-2.118	-3.214	-0.015

Interaction energy analysis for fragmet #1(A:8:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.854 / q_NPA : 0.917

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	10	VAL	0	0.001	0.010	2.969	-4.379	-1.609	0.246	-1.326	-1.690	-0.009
4	A	11	ILE	0	0.038	0.025	5.089	2.976	3.044	-0.001	-0.003	-0.063	0.000
74	A	81	VAL	0	0.043	0.022	3.567	-8.351	-8.061	0.001	-0.105	-0.187	-0.001
75	A	82	GLY	0	-0.019	-0.006	2.426	0.584	2.007	0.353	-0.768	-1.008	-0.004
76	A	83	GLN	0	-0.001	-0.010	3.169	8.060	8.217	0.025	0.084	-0.266	-0.001
5	A	12	LYS	1	0.835	0.927	8.770	25.358	25.358	0.000	0.000	0.000	0.000
6	A	13	ASN	0	0.001	-0.010	11.342	1.723	1.723	0.000	0.000	0.000	0.000
7	A	14	SER	0	-0.007	-0.009	13.549	-0.747	-0.747	0.000	0.000	0.000	0.000
8	A	15	ASP	-1	-0.789	-0.899	15.584	-13.729	-13.729	0.000	0.000	0.000	0.000
9	A	16	MET	0	-0.044	0.026	15.737	0.968	0.968	0.000	0.000	0.000	0.000
10	A	17	SER	0	0.047	0.026	17.760	-0.597	-0.597	0.000	0.000	0.000	0.000
11	A	18	VAL	0	0.049	-0.002	15.366	-0.564	-0.564	0.000	0.000	0.000	0.000
12	A	19	GLU	-1	-0.858	-0.911	14.841	-18.601	-18.601	0.000	0.000	0.000	0.000
13	A	20	MET	0	0.050	0.026	15.615	-0.824	-0.824	0.000	0.000	0.000	0.000
14	A	21	GLN	0	-0.081	-0.029	12.404	-1.648	-1.648	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.826	0.886	10.932	18.140	18.140	0.000	0.000	0.000	0.000
16	A	23	GLU	-1	-0.864	-0.910	11.452	-21.299	-21.299	0.000	0.000	0.000	0.000
17	A	24	VAL	0	-0.012	-0.002	10.742	-0.488	-0.488	0.000	0.000	0.000	0.000
18	A	25	GLU	-1	-0.904	-0.977	6.941	-33.882	-33.882	0.000	0.000	0.000	0.000
19	A	26	GLU	-1	-0.832	-0.913	7.445	-33.183	-33.183	0.000	0.000	0.000	0.000
20	A	27	VAL	0	-0.013	-0.003	9.649	0.164	0.164	0.000	0.000	0.000	0.000
21	A	28	ALA	0	-0.005	-0.011	8.007	0.656	0.656	0.000	0.000	0.000	0.000
22	A	29	LYS	1	0.802	0.905	5.736	31.184	31.184	0.000	0.000	0.000	0.000
23	A	30	LYS	1	0.946	0.984	7.127	23.421	23.421	0.000	0.000	0.000	0.000
24	A	31	ALA	0	-0.002	0.004	10.800	1.393	1.393	0.000	0.000	0.000	0.000
25	A	32	ILE	0	-0.061	-0.035	5.930	0.383	0.383	0.000	0.000	0.000	0.000
26	A	33	ASP	-1	-0.935	-0.971	8.637	-31.342	-31.342	0.000	0.000	0.000	0.000
27	A	34	TYR	0	-0.065	-0.033	10.590	2.046	2.046	0.000	0.000	0.000	0.000
28	A	35	CYS	0	-0.055	-0.015	13.080	2.070	2.070	0.000	0.000	0.000	0.000
29	A	36	ASN	0	0.032	0.005	13.053	-2.153	-2.153	0.000	0.000	0.000	0.000
30	A	37	THR	0	-0.083	-0.036	14.745	-0.433	-0.433	0.000	0.000	0.000	0.000
31	A	38	ASP	-1	-0.786	-0.884	14.569	-17.605	-17.605	0.000	0.000	0.000	0.000
32	A	39	LYS	1	0.878	0.925	15.637	14.989	14.989	0.000	0.000	0.000	0.000
33	A	40	GLU	-1	-0.800	-0.892	17.484	-15.489	-15.489	0.000	0.000	0.000	0.000
34	A	41	ILE	0	0.011	0.012	10.971	-0.251	-0.251	0.000	0.000	0.000	0.000
35	A	42	ALA	0	-0.027	-0.029	14.322	-0.224	-0.224	0.000	0.000	0.000	0.000
36	A	43	THR	0	-0.065	-0.065	16.185	0.484	0.484	0.000	0.000	0.000	0.000
37	A	44	PHE	0	0.055	0.039	13.763	0.420	0.420	0.000	0.000	0.000	0.000
38	A	45	ILE	0	0.036	0.006	11.477	0.237	0.237	0.000	0.000	0.000	0.000
39	A	46	LYS	1	0.830	0.921	15.618	14.239	14.239	0.000	0.000	0.000	0.000
40	A	47	ASP	-1	-0.934	-0.969	19.099	-12.933	-12.933	0.000	0.000	0.000	0.000
41	A	48	ASP	-1	-0.786	-0.878	16.580	-17.731	-17.731	0.000	0.000	0.000	0.000
42	A	49	PHE	0	-0.027	-0.044	14.266	0.377	0.377	0.000	0.000	0.000	0.000
43	A	50	ARG	1	0.798	0.908	19.601	13.244	13.244	0.000	0.000	0.000	0.000
44	A	51	SER	0	0.005	0.025	22.288	0.852	0.852	0.000	0.000	0.000	0.000
45	A	52	ARG	1	0.807	0.897	16.705	18.375	18.375	0.000	0.000	0.000	0.000
46	A	53	TYR	0	-0.046	-0.018	19.198	0.063	0.063	0.000	0.000	0.000	0.000
47	A	54	HIS	0	0.058	0.029	24.384	-0.128	-0.128	0.000	0.000	0.000	0.000
48	A	55	GLY	0	-0.032	-0.010	26.829	-0.168	-0.168	0.000	0.000	0.000	0.000
49	A	56	THR	0	-0.079	-0.087	25.954	-0.147	-0.147	0.000	0.000	0.000	0.000
50	A	57	TRP	0	0.061	0.032	18.597	-0.336	-0.336	0.000	0.000	0.000	0.000
51	A	58	HIS	0	0.007	-0.009	21.280	0.223	0.223	0.000	0.000	0.000	0.000
52	A	59	CYS	0	-0.020	0.011	14.828	-0.923	-0.923	0.000	0.000	0.000	0.000
53	A	60	ILE	0	-0.004	0.007	17.082	0.833	0.833	0.000	0.000	0.000	0.000
54	A	61	VAL	0	0.029	0.007	12.941	-1.347	-1.347	0.000	0.000	0.000	0.000
55	A	62	GLY	0	0.036	0.024	13.392	1.525	1.525	0.000	0.000	0.000	0.000
56	A	63	ARG	1	0.822	0.894	9.655	26.138	26.138	0.000	0.000	0.000	0.000
57	A	64	ASN	0	-0.004	0.004	14.306	-0.895	-0.895	0.000	0.000	0.000	0.000
58	A	65	PHE	0	0.028	0.013	16.961	0.822	0.822	0.000	0.000	0.000	0.000
59	A	66	GLY	0	0.034	0.021	17.984	-0.815	-0.815	0.000	0.000	0.000	0.000
60	A	67	SER	0	-0.046	-0.033	20.550	0.508	0.508	0.000	0.000	0.000	0.000
61	A	68	PHE	0	0.004	0.007	22.675	-0.280	-0.280	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.005	0.004	22.764	0.316	0.316	0.000	0.000	0.000	0.000
63	A	70	THR	0	0.001	0.007	25.257	-0.216	-0.216	0.000	0.000	0.000	0.000
64	A	71	PHE	0	0.021	-0.007	22.019	-0.302	-0.302	0.000	0.000	0.000	0.000
65	A	72	GLU	-1	-0.780	-0.876	25.313	-11.830	-11.830	0.000	0.000	0.000	0.000
66	A	73	ARG	1	0.814	0.910	24.052	12.142	12.142	0.000	0.000	0.000	0.000
67	A	74	SER	0	0.000	-0.022	21.204	0.123	0.123	0.000	0.000	0.000	0.000
68	A	75	TYR	0	-0.013	-0.008	20.855	-0.363	-0.363	0.000	0.000	0.000	0.000
69	A	76	TYR	0	0.031	-0.005	17.513	-0.044	-0.044	0.000	0.000	0.000	0.000
70	A	77	ILE	0	0.010	0.006	11.476	-0.361	-0.361	0.000	0.000	0.000	0.000
71	A	78	TYR	0	0.029	0.023	13.895	-0.193	-0.193	0.000	0.000	0.000	0.000
72	A	79	LEU	0	0.036	0.012	7.992	-0.823	-0.823	0.000	0.000	0.000	0.000
73	A	80	TYR	0	-0.011	-0.011	7.127	3.102	3.102	0.000	0.000	0.000	0.000
77	A	84	LEU	0	0.062	0.049	6.764	5.100	5.100	0.000	0.000	0.000	0.000
78	A	85	ALA	0	-0.087	-0.034	8.309	-3.013	-3.013	0.000	0.000	0.000	0.000
79	A	86	ILE	0	0.036	0.008	8.553	1.536	1.536	0.000	0.000	0.000	0.000
80	A	87	LEU	0	-0.014	-0.006	12.325	-0.319	-0.319	0.000	0.000	0.000	0.000
81	A	88	LEU	0	0.011	0.015	14.819	0.857	0.857	0.000	0.000	0.000	0.000
82	A	89	PHE	0	-0.025	-0.018	16.695	0.007	0.007	0.000	0.000	0.000	0.000
83	A	90	LYS	1	0.844	0.927	20.151	12.453	12.453	0.000	0.000	0.000	0.000
84	A	91	THR	0	-0.051	-0.038	23.361	0.072	0.072	0.000	0.000	0.000	0.000
85	A	92	GLY	-1	-0.770	-0.834	26.945	-11.425	-11.425	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:GLN)