FMO DATABASE

FMODB ID: Z753N

Calculation Name: 1SQL-A-Xray547

Preferred Name:

Target Type:

Ligand Name: guanine

Ligand 3-letter code: GUN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1SQL

Chain ID: A

ChEMBL ID:

UniProt ID: Q9SF23

Base Structure: X-ray

Registration Date: 2025-10-03

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-956163.96608
FMO2-HF: Nuclear repulsion	910126.230886
FMO2-HF: Total energy	-46037.735194
FMO2-MP2: Total energy	-46175.301466

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:GLY)

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

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.
21.523	22.947	0.121	-0.687	-0.857	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.828 / q_NPA : 0.901

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	0.869	0.917	3.812	33.706	34.363	-0.009	-0.369	-0.279	-0.001
35	A	35	TRP	0	-0.023	-0.026	2.807	3.140	3.907	0.130	-0.318	-0.578	-0.003
4	A	4	LEU	0	0.036	0.044	6.593	3.083	3.083	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.025	-0.025	9.265	-1.162	-1.162	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.009	0.010	12.261	1.520	1.520	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.864	0.900	15.365	17.922	17.922	0.000	0.000	0.000	0.000
8	A	8	GLY	0	-0.004	-0.006	17.511	0.710	0.710	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.012	0.001	18.982	0.823	0.823	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.942	0.965	22.219	12.021	12.021	0.000	0.000	0.000	0.000
11	A	11	PHE	0	0.043	0.028	22.283	0.082	0.082	0.000	0.000	0.000	0.000
12	A	12	TYR	0	-0.026	-0.034	27.672	-0.033	-0.033	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.053	0.035	30.164	-0.027	-0.027	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.017	-0.002	31.097	0.206	0.206	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.013	-0.002	28.779	0.331	0.331	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.066	0.023	31.608	-0.086	-0.086	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.032	-0.005	33.689	0.053	0.053	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.022	0.003	35.815	0.243	0.243	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.025	0.011	38.316	-0.147	-0.147	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.841	-0.937	40.448	-7.612	-7.612	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.825	-0.918	34.405	-9.457	-9.457	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.845	0.918	34.338	8.996	8.996	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.081	-0.033	37.563	0.068	0.068	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.004	0.005	39.228	0.067	0.067	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.043	0.032	35.139	-0.062	-0.062	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.058	-0.034	31.310	0.168	0.168	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.007	-0.001	29.809	-0.331	-0.331	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.050	-0.016	25.787	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.037	-0.016	22.285	0.016	0.016	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.005	-0.009	18.773	-0.134	-0.134	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.818	-0.874	15.498	-18.264	-18.264	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.008	-0.010	13.132	0.019	0.019	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.848	-0.902	8.737	-29.908	-29.908	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.034	0.007	9.376	0.080	0.080	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.024	0.007	5.391	4.174	4.174	0.000	0.000	0.000	0.000
37	A	37	SER	0	-0.054	-0.020	5.314	-5.866	-5.866	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.032	0.004	6.190	4.837	4.837	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.934	0.976	7.134	30.324	30.324	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.853	0.911	8.883	22.616	22.616	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.080	0.036	11.813	1.375	1.375	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.061	-0.022	11.673	1.202	1.202	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.966	-0.990	12.646	-20.780	-20.780	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.074	-0.070	15.056	0.953	0.953	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.952	-0.963	16.577	-14.827	-14.827	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.034	-0.025	17.655	0.690	0.690	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.006	-0.014	16.989	-1.173	-1.173	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.927	-0.947	17.435	-15.250	-15.250	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.835	-0.862	14.362	-18.779	-18.779	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.010	-0.016	12.008	-2.610	-2.610	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.030	-0.004	11.607	1.111	1.111	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.059	0.042	15.000	-0.662	-0.662	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.050	0.003	15.210	0.233	0.233	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.014	0.005	16.825	0.375	0.375	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.841	-0.906	19.009	-14.672	-14.672	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.027	-0.018	13.565	0.253	0.253	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.018	-0.013	17.917	0.382	0.382	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.012	-0.019	20.352	0.766	0.766	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.037	-0.015	19.067	0.545	0.545	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.010	-0.015	19.485	0.365	0.365	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.914	0.976	21.491	11.579	11.579	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.924	-0.965	24.999	-10.813	-10.813	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.085	-0.032	21.879	0.401	0.401	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.058	-0.032	23.741	0.334	0.334	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.864	-0.947	26.573	-10.555	-10.555	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.028	0.039	28.877	0.424	0.424	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.072	-0.043	30.494	0.107	0.107	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.038	0.019	31.104	-0.331	-0.331	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.882	0.930	28.195	10.911	10.911	0.000	0.000	0.000	0.000
70	A	70	ASN	0	0.024	0.013	31.182	0.215	0.215	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.004	0.010	27.787	0.119	0.119	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.025	0.015	24.515	-0.080	-0.080	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.811	-0.919	22.661	-12.784	-12.784	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.019	-0.015	22.733	-0.338	-0.338	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.022	0.017	23.994	-0.196	-0.196	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.037	0.012	19.326	-0.400	-0.400	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.815	-0.874	19.208	-17.017	-17.017	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.028	-0.018	20.081	-0.367	-0.367	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.023	0.016	17.504	-0.303	-0.303	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.003	0.009	15.546	-0.776	-0.776	0.000	0.000	0.000	0.000
81	A	81	SER	0	0.001	0.005	16.154	-0.720	-0.720	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.945	0.970	18.424	13.033	13.033	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.002	-0.010	13.765	0.089	0.089	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.011	-0.002	11.852	-0.727	-0.727	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.891	-0.935	15.222	-13.632	-13.632	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.813	0.890	18.562	14.018	14.018	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.039	0.020	14.471	0.192	0.192	0.000	0.000	0.000	0.000
88	A	88	HIS	0	0.052	0.021	14.041	-1.723	-1.723	0.000	0.000	0.000	0.000
89	A	89	GLN	0	-0.027	-0.017	11.331	-1.706	-1.706	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.044	-0.002	9.285	-3.354	-3.354	0.000	0.000	0.000	0.000
91	A	91	ASN	0	-0.002	-0.003	6.296	4.371	4.371	0.000	0.000	0.000	0.000
92	A	92	ALA	0	0.026	0.010	7.257	1.021	1.021	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.003	0.004	8.832	-1.773	-1.773	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.770	0.858	10.531	24.908	24.908	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.010	0.008	12.048	-0.118	-0.118	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.852	0.939	12.726	23.011	23.011	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.000	0.005	17.814	0.154	0.154	0.000	0.000	0.000	0.000
98	A	98	SER	0	0.008	-0.006	21.458	0.208	0.208	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.826	0.919	24.400	10.342	10.342	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.021	0.000	26.931	0.073	0.073	0.000	0.000	0.000	0.000
101	A	101	ASN	0	-0.003	0.005	29.071	0.397	0.397	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.026	0.008	30.857	-0.043	-0.043	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.067	0.030	33.518	0.248	0.248	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.003	-0.007	37.046	-0.014	-0.014	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.016	0.019	34.468	0.220	0.220	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.885	0.926	37.552	7.663	7.663	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.008	-0.008	36.041	0.181	0.181	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.005	0.015	33.793	0.028	0.028	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.030	-0.018	30.030	-0.024	-0.024	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.885	-0.920	26.384	-11.517	-11.517	0.000	0.000	0.000	0.000
111	A	111	TYR	0	-0.029	-0.046	20.738	-0.127	-0.127	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.003	0.021	26.794	-0.043	-0.043	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.002	-0.018	23.637	0.056	0.056	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.047	0.005	20.962	0.073	0.073	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.761	-0.864	15.136	-21.224	-21.224	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.016	0.008	16.342	0.282	0.282	0.000	0.000	0.000	0.000
117	A	117	PHE	0	-0.002	-0.003	7.761	-0.580	-0.580	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.800	0.859	12.611	19.436	19.436	0.000	0.000	0.000	0.000
119	A	119	GLN	0	-0.023	-0.017	9.115	-4.662	-4.662	0.000	0.000	0.000	0.000
120	A	120	ARG	0	-0.035	-0.019	10.867	1.765	1.765	0.000	0.000	0.000	0.000

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