FMO DATABASE

FMODB ID: QLRRY

Calculation Name: 5FAR-B-Xray547

Preferred Name:

Target Type:

Ligand Name: 9-methylguanine

Ligand 3-letter code: 9MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5FAR | pdb_00005far

Chain ID: B

UniProt ID:

ChEMBL ID:

Base Structure: X-ray

Registration Date: 2025-10-05

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	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1008186.82165
FMO2-HF: Nuclear repulsion	959493.190824
FMO2-HF: Total energy	-48693.630826
FMO2-MP2: Total energy	-48835.615715

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.
-76.049	-67.663	10.711	-5.996	-13.101	-0.064

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 : 0.792 / q_NPA : 0.908

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	3	LYS	1	0.925	0.95	2.977	62.146	64.941	0.189	-1.367	-1.617	-0.008
35	A	35	GLU	-1	-0.86	-0.916	2.449	-73.250	-70.658	3.366	-2.334	-3.624	-0.018
36	A	36	LEU	0	0.071	0.012	2.757	5.021	6.508	2.556	-1.249	-2.794	-0.010
37	A	37	ASP	-1	-0.938	-0.972	2.439	-50.716	-50.689	2.119	0.113	-2.260	-0.026
38	A	38	LEU	0	0.003	-0.01	4.297	4.772	4.931	0.001	-0.020	-0.140	0.000
90	A	90	ILE	0	-0.035	-0.003	5.793	-2.793	-2.655	-0.001	-0.008	-0.129	0.000
91	A	91	SER	0	-0.006	-0.001	2.560	-1.890	-1.402	2.455	-0.977	-1.966	-0.002
92	A	92	ARG	1	0.777	0.866	3.162	47.206	47.906	0.026	-0.154	-0.571	0.000
4	A	4	ILE	0	0.019	0.032	5.737	3.285	3.285	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.005	-0.02	8.840	-2.598	-2.598	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.018	-0.012	11.751	1.124	1.124	0.000	0.000	0.000	0.000
7	A	7	HIS	0	-0.009	-0.004	13.358	0.080	0.080	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.837	-0.903	17.314	-12.677	-12.677	0.000	0.000	0.000	0.000
9	A	9	MET	0	-0.047	-0.002	17.118	0.739	0.739	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.931	-0.977	21.602	-10.845	-10.845	0.000	0.000	0.000	0.000
11	A	11	PHE	0	0.026	0.015	21.782	0.061	0.061	0.000	0.000	0.000	0.000
12	A	12	TYR	0	-0.049	-0.04	27.229	0.058	0.058	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.041	0.025	29.825	-0.043	-0.043	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.001	-0.004	30.826	0.161	0.161	0.000	0.000	0.000	0.000
15	A	15	HIS	0	0	0.005	27.449	0.259	0.259	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.002	-0.009	31.005	0.036	0.036	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.025	-0.007	32.144	0.094	0.094	0.000	0.000	0.000	0.000
18	A	18	PHE	0	-0.016	0.002	34.551	0.217	0.217	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.041	0.026	37.414	-0.132	-0.132	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.877	-0.959	39.783	-7.507	-7.507	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.789	-0.881	33.492	-9.397	-9.397	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.064	-0.035	34.430	0.051	0.051	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.91	0.97	36.754	7.375	7.375	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.056	-0.035	38.435	0.152	0.152	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.035	0.034	34.457	-0.027	-0.027	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.07	-0.05	30.766	0.041	0.041	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.88	0.926	28.863	9.706	9.706	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.049	-0.031	25.433	-0.046	-0.046	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.857	0.91	22.938	12.495	12.495	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.024	-0.016	17.711	-0.069	-0.069	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.84	-0.907	15.407	-17.139	-17.139	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.005	-0.007	11.612	-0.221	-0.221	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.003	-0.012	7.229	-1.093	-1.093	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.007	0	7.721	0.719	0.719	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.886	0.945	6.893	29.420	29.420	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.956	0.976	8.716	23.766	23.766	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.035	0.033	9.827	1.916	1.916	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.002	0	10.931	1.582	1.582	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.919	-0.955	12.812	-20.597	-20.597	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.08	-0.059	14.209	1.231	1.231	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.958	-0.963	15.742	-14.792	-14.792	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.835	-0.915	15.671	-14.541	-14.541	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.022	-0.018	14.472	-1.134	-1.134	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.856	-0.91	14.567	-15.415	-15.415	0.000	0.000	0.000	0.000
49	A	49	HIS	1	0.674	0.821	12.263	16.716	16.716	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.012	0.004	10.008	-2.685	-2.685	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.001	0.002	9.972	0.884	0.884	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.005	-0.003	12.098	-0.375	-0.375	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.065	0.014	14.251	0.266	0.266	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.023	0.013	15.545	0.360	0.360	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.858	-0.906	17.172	-14.561	-14.561	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.001	0.007	11.728	0.144	0.144	0.000	0.000	0.000	0.000
57	A	57	PHE	0	0.047	0.022	16.237	0.169	0.169	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.783	-0.859	19.241	-11.236	-11.236	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.038	-0.004	16.194	0.504	0.504	0.000	0.000	0.000	0.000
60	A	60	CYS	0	-0.03	-0.027	17.669	0.050	0.050	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.734	0.82	20.436	11.503	11.503	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.863	0.92	22.949	12.172	12.172	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.081	-0.032	20.847	0.407	0.407	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.037	-0.02	22.905	0.318	0.318	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.837	-0.906	25.630	-10.360	-10.360	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.843	-0.894	27.699	-10.205	-10.205	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.82	0.914	22.394	12.304	12.304	0.000	0.000	0.000	0.000
68	A	68	THR	0	-0.032	-0.027	29.087	0.110	0.110	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.006	0.004	24.533	0.286	0.286	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.966	0.968	29.944	8.879	8.879	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.025	-0.002	26.745	0.127	0.127	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.057	0.021	23.666	-0.046	-0.046	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.832	-0.926	21.926	-12.548	-12.548	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.017	-0.011	21.751	-0.336	-0.336	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.021	0.026	21.427	-0.146	-0.146	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.037	0.015	17.920	-0.381	-0.381	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.78	-0.86	17.668	-16.570	-16.570	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.071	-0.036	18.313	-0.102	-0.102	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.043	0.025	15.783	-0.234	-0.234	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.024	-0.002	13.901	-0.670	-0.670	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.024	-0.019	13.895	-0.609	-0.609	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.856	-0.932	15.799	-13.798	-13.798	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.019	-0.014	10.983	-0.178	-0.178	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.018	-0.009	9.329	-0.488	-0.488	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.921	0.969	12.213	13.309	13.309	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.059	-0.025	15.109	0.971	0.971	0.000	0.000	0.000	0.000
87	A	87	TYR	0	-0.034	-0.039	10.877	0.181	0.181	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.916	-0.964	10.181	-19.075	-19.075	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.024	-0.01	8.171	-1.306	-1.306	0.000	0.000	0.000	0.000
93	A	93	CYS	0	-0.041	0.007	6.566	-0.962	-0.962	0.000	0.000	0.000	0.000
94	A	94	THR	0	0.025	0.008	8.763	0.383	0.383	0.000	0.000	0.000	0.000
95	A	95	ILE	0	-0.023	0.003	10.800	-0.123	-0.123	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.867	0.923	14.264	18.235	18.235	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.002	0.001	17.113	0.277	0.277	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.031	-0.021	20.178	0.288	0.288	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.871	0.932	23.536	10.468	10.468	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.013	-0.014	26.854	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.818	-0.896	28.884	-9.669	-9.669	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.007	0.013	30.539	0.206	0.206	0.000	0.000	0.000	0.000
103	A	103	PRO	0	0.013	0.009	32.885	0.186	0.186	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.021	-0.013	32.170	0.107	0.107	0.000	0.000	0.000	0.000
105	A	105	PRO	0	-0.011	-0.003	36.532	-0.025	-0.025	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.003	0.001	36.998	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	107	HIS	0	-0.014	0	35.819	-0.065	-0.065	0.000	0.000	0.000	0.000
108	A	108	TYR	0	-0.019	-0.027	30.528	-0.255	-0.255	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.943	0.971	23.045	12.829	12.829	0.000	0.000	0.000	0.000
110	A	110	ALA	0	0.019	0.006	25.806	-0.058	-0.058	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.024	0.009	26.522	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	112	ALA	0	-0.008	-0.014	21.412	-0.083	-0.083	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.009	0.011	20.582	0.129	0.129	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.852	-0.921	14.686	-20.363	-20.363	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.039	-0.006	15.425	0.358	0.358	0.000	0.000	0.000	0.000
116	A	116	THR	0	0	-0.004	9.293	-0.373	-0.373	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.749	0.827	10.992	19.358	19.358	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.835	-0.934	7.838	-31.556	-31.556	0.000	0.000	0.000	0.000
119	A	119	ARG	0	-0.093	-0.03	7.513	4.155	4.155	0.000	0.000	0.000	0.000

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