FMO DATABASE

FMODB ID: LRQG9

Calculation Name: 7MOQ-M-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: M

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-657239.358154
FMO2-HF: Nuclear repulsion	621049.567439
FMO2-HF: Total energy	-36189.790714
FMO2-MP2: Total energy	-36294.871705

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:ASN)

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

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.
-59.419	-56.38	9.002	-6.268	-5.77	-0.072

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.758 / q_NPA : 0.867

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	4	GLU	-1	-0.857	-0.924	2.670	-69.952	-65.936	0.587	-2.475	-2.127	-0.022
4	A	5	PRO	0	-0.045	-0.028	5.261	0.370	0.401	-0.001	-0.004	-0.026	0.000
24	A	25	ILE	0	-0.023	-0.018	3.823	-4.155	-4.048	-0.001	-0.024	-0.081	0.000
76	A	77	ILE	0	0.056	0.033	4.533	-1.622	-1.563	-0.001	-0.004	-0.053	0.000
77	A	78	ASN	0	-0.007	-0.012	1.839	-33.015	-34.274	8.419	-3.758	-3.402	-0.050
78	A	79	GLU	-1	-0.830	-0.897	5.146	-23.929	-23.844	-0.001	-0.003	-0.081	0.000
5	A	6	GLU	-1	-0.845	-0.900	7.340	-24.490	-24.490	0.000	0.000	0.000	0.000
6	A	7	VAL	0	-0.007	-0.016	10.561	0.136	0.136	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.794	0.885	12.836	23.154	23.154	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.029	0.020	16.232	1.146	1.146	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.017	-0.022	17.691	-0.984	-0.984	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.852	-0.915	19.693	-11.725	-11.725	0.000	0.000	0.000	0.000
11	A	12	MET	0	-0.057	-0.004	18.910	0.118	0.118	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.812	-0.912	21.513	-13.001	-13.001	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.812	-0.913	17.240	-18.624	-18.624	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.869	-0.943	18.118	-14.864	-14.864	0.000	0.000	0.000	0.000
15	A	16	MET	0	-0.031	-0.010	18.312	-0.840	-0.840	0.000	0.000	0.000	0.000
16	A	17	ILE	0	-0.019	-0.014	15.129	-1.447	-1.447	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.860	0.921	13.791	18.465	18.465	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.901	0.952	13.469	13.350	13.350	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.008	-0.001	13.152	-0.914	-0.914	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.818	0.907	9.536	22.416	22.416	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.895	-0.955	9.119	-25.439	-25.439	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.088	0.048	10.282	-2.070	-2.070	0.000	0.000	0.000	0.000
23	A	24	ALA	0	-0.023	-0.015	9.150	-0.304	-0.304	0.000	0.000	0.000	0.000
25	A	26	ASN	0	0.007	0.019	6.838	-1.178	-1.178	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.014	-0.001	9.916	0.155	0.155	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.027	-0.021	5.343	0.894	0.894	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.876	0.958	6.182	35.252	35.252	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.910	-0.939	7.949	-19.217	-19.217	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.013	-0.009	11.477	1.428	1.428	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.897	0.935	10.265	20.779	20.779	0.000	0.000	0.000	0.000
32	A	33	GLN	0	0.049	0.022	11.804	1.126	1.126	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.839	-0.921	13.058	-23.803	-23.803	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.962	0.974	14.865	14.622	14.622	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.039	-0.019	15.240	0.157	0.157	0.000	0.000	0.000	0.000
36	A	37	ILE	0	0.040	0.028	10.167	0.422	0.422	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.004	-0.004	13.796	0.264	0.264	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.044	-0.018	16.685	0.157	0.157	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.019	0.002	13.352	1.096	1.096	0.000	0.000	0.000	0.000
40	A	41	ILE	0	0.053	0.014	11.710	0.402	0.402	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.830	0.911	16.211	13.667	13.667	0.000	0.000	0.000	0.000
42	A	43	TYR	0	-0.024	-0.035	19.866	0.910	0.910	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.914	-0.952	16.760	-15.502	-15.502	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.036	-0.004	15.620	0.431	0.431	0.000	0.000	0.000	0.000
45	A	46	ASP	-1	-0.785	-0.895	20.728	-12.147	-12.147	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.841	0.940	22.593	14.152	14.152	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.039	-0.010	19.523	0.469	0.469	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.849	-0.911	22.197	-13.408	-13.408	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.012	0.004	25.232	0.339	0.339	0.000	0.000	0.000	0.000
50	A	51	TYR	0	0.003	-0.008	26.387	-0.297	-0.297	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.031	-0.016	26.825	0.274	0.274	0.000	0.000	0.000	0.000
52	A	53	TRP	0	-0.016	-0.011	20.894	-0.215	-0.215	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.021	-0.010	22.643	0.164	0.164	0.000	0.000	0.000	0.000
54	A	55	CYS	0	-0.048	-0.015	15.922	-0.654	-0.654	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.019	-0.004	18.012	0.476	0.476	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.029	0.015	12.625	-0.959	-0.959	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.036	0.015	13.920	1.278	1.278	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.841	0.914	11.885	22.312	22.312	0.000	0.000	0.000	0.000
59	A	60	ASN	0	0.001	-0.010	14.673	-0.541	-0.541	0.000	0.000	0.000	0.000
60	A	61	PHE	0	-0.009	0.002	15.753	0.720	0.720	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.037	0.027	20.515	-0.230	-0.230	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.049	-0.037	21.907	0.066	0.066	0.000	0.000	0.000	0.000
63	A	64	HIS	0	0.031	0.018	24.450	-0.241	-0.241	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.028	-0.001	23.056	0.252	0.252	0.000	0.000	0.000	0.000
65	A	66	ILE	0	0.014	0.014	27.265	0.146	0.146	0.000	0.000	0.000	0.000
66	A	67	HIS	1	0.851	0.904	25.280	11.783	11.783	0.000	0.000	0.000	0.000
67	A	68	GLN	0	0.029	0.025	27.281	0.459	0.459	0.000	0.000	0.000	0.000
68	A	69	THR	0	-0.004	-0.001	26.670	-0.586	-0.586	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.896	0.953	25.551	11.400	11.400	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.923	0.967	22.845	11.911	11.911	0.000	0.000	0.000	0.000
71	A	72	TYR	0	0.031	0.011	21.010	-0.159	-0.159	0.000	0.000	0.000	0.000
72	A	73	ILE	0	0.002	-0.001	14.701	-0.265	-0.265	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.014	0.012	15.001	-0.355	-0.355	0.000	0.000	0.000	0.000
74	A	75	PHE	0	0.017	-0.010	9.442	0.038	0.038	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.954	0.976	9.525	25.742	25.742	0.000	0.000	0.000	0.000
79	A	80	LEU	0	0.008	0.024	7.657	3.559	3.559	0.000	0.000	0.000	0.000
80	A	81	CYS	0	-0.076	-0.049	9.645	-1.278	-1.278	0.000	0.000	0.000	0.000
81	A	82	LEU	0	0.015	0.011	9.452	0.831	0.831	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.020	0.000	13.280	0.392	0.392	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.000	0.002	16.464	0.292	0.292	0.000	0.000	0.000	0.000
84	A	85	TRP	0	0.003	-0.011	18.349	0.426	0.426	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.891	0.968	22.045	11.520	11.520	0.000	0.000	0.000	0.000
86	A	87	ALA	-1	-0.828	-0.910	25.033	-10.927	-10.927	0.000	0.000	0.000	0.000

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