FMO DATABASE

FMODB ID: 8GQVY

Calculation Name: 1C20-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1C20

Chain ID: A

ChEMBL ID:

UniProt ID: Q24573

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	128
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1144547.473824
FMO2-HF: Nuclear repulsion	1092420.683065
FMO2-HF: Total energy	-52126.790759
FMO2-MP2: Total energy	-52279.478589

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:3:GLY)

Summations of interaction energy for fragment #1(A:3: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.
30.157	31.062	-0.005	-0.338	-0.562	-0.001

Interaction energy analysis for fragmet #1(A:3:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / 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

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	5	SER	0	0.018	-0.021	3.829	-3.019	-2.114	-0.005	-0.338	-0.562	-0.001
4	A	6	PHE	0	0.030	-0.006	6.467	2.710	2.710	0.000	0.000	0.000	0.000
5	A	7	GLU	-1	-0.896	-0.937	9.676	-21.967	-21.967	0.000	0.000	0.000	0.000
6	A	8	GLU	-1	-0.861	-0.912	9.237	-29.120	-29.120	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.046	-0.026	10.278	2.015	2.015	0.000	0.000	0.000	0.000
8	A	10	PHE	0	0.016	0.012	12.899	1.814	1.814	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.923	0.955	13.606	23.304	23.304	0.000	0.000	0.000	0.000
10	A	12	GLN	0	0.010	-0.008	12.475	0.622	0.622	0.000	0.000	0.000	0.000
11	A	13	VAL	0	0.026	0.014	16.922	0.858	0.858	0.000	0.000	0.000	0.000
12	A	14	ARG	1	0.938	0.988	19.346	16.092	16.092	0.000	0.000	0.000	0.000
13	A	15	GLN	0	0.040	0.014	18.261	-0.171	-0.171	0.000	0.000	0.000	0.000
14	A	16	LEU	0	-0.035	-0.019	20.552	0.427	0.427	0.000	0.000	0.000	0.000
15	A	17	TYR	0	-0.069	-0.074	23.587	0.339	0.339	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.956	-0.986	23.419	-13.284	-13.284	0.000	0.000	0.000	0.000
17	A	19	ILE	0	-0.096	-0.018	24.598	0.218	0.218	0.000	0.000	0.000	0.000
18	A	20	ASN	0	-0.013	-0.019	27.952	0.227	0.227	0.000	0.000	0.000	0.000
19	A	21	ASP	-1	-0.868	-0.921	31.042	-9.742	-9.742	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.892	-0.939	33.213	-8.975	-8.975	0.000	0.000	0.000	0.000
21	A	23	PRO	0	0.027	0.007	33.642	-0.260	-0.260	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.944	0.967	34.474	8.356	8.356	0.000	0.000	0.000	0.000
23	A	25	ARG	1	0.861	0.910	27.376	11.145	11.145	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.924	0.955	29.969	9.580	9.580	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.853	-0.930	30.088	-9.624	-9.624	0.000	0.000	0.000	0.000
26	A	28	PHE	0	-0.045	-0.011	27.079	-0.134	-0.134	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.025	-0.012	24.578	-0.348	-0.348	0.000	0.000	0.000	0.000
28	A	30	ASP	-1	-0.793	-0.875	26.432	-11.653	-11.653	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.896	-0.931	28.008	-9.931	-9.931	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.074	-0.030	24.327	-0.198	-0.198	0.000	0.000	0.000	0.000
31	A	33	PHE	0	-0.027	-0.052	19.514	-0.699	-0.699	0.000	0.000	0.000	0.000
32	A	34	SER	0	-0.019	-0.023	23.646	-0.337	-0.337	0.000	0.000	0.000	0.000
33	A	35	PHE	0	-0.003	0.015	25.928	-0.205	-0.205	0.000	0.000	0.000	0.000
34	A	36	MET	0	-0.052	-0.013	19.643	-0.115	-0.115	0.000	0.000	0.000	0.000
35	A	37	GLN	0	0.001	0.017	21.354	-0.493	-0.493	0.000	0.000	0.000	0.000
36	A	38	LYS	1	0.981	0.996	22.401	11.731	11.731	0.000	0.000	0.000	0.000
37	A	39	ARG	1	0.853	0.912	15.481	17.395	17.395	0.000	0.000	0.000	0.000
38	A	40	GLY	0	0.015	0.013	18.110	-0.707	-0.707	0.000	0.000	0.000	0.000
39	A	41	THR	0	-0.069	-0.032	13.650	-0.503	-0.503	0.000	0.000	0.000	0.000
40	A	42	PRO	0	0.030	0.016	14.823	0.803	0.803	0.000	0.000	0.000	0.000
41	A	43	ILE	0	0.016	0.011	16.706	-0.152	-0.152	0.000	0.000	0.000	0.000
42	A	44	ASN	0	-0.017	-0.024	14.166	-0.242	-0.242	0.000	0.000	0.000	0.000
43	A	45	ARG	1	0.967	0.964	9.950	23.409	23.409	0.000	0.000	0.000	0.000
44	A	46	LEU	0	0.045	0.036	13.558	1.346	1.346	0.000	0.000	0.000	0.000
45	A	47	PRO	0	-0.063	-0.024	14.275	-0.811	-0.811	0.000	0.000	0.000	0.000
46	A	48	ILE	0	0.030	0.022	15.472	0.956	0.956	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.008	-0.006	17.631	-0.393	-0.393	0.000	0.000	0.000	0.000
48	A	50	ALA	0	0.002	-0.003	19.984	0.809	0.809	0.000	0.000	0.000	0.000
49	A	51	LYS	1	0.945	0.965	21.277	11.754	11.754	0.000	0.000	0.000	0.000
50	A	52	SER	0	0.020	0.023	22.797	0.590	0.590	0.000	0.000	0.000	0.000
51	A	53	VAL	0	0.027	0.011	18.994	-0.831	-0.831	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.014	-0.009	18.598	0.607	0.607	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.751	-0.853	20.923	-12.506	-12.506	0.000	0.000	0.000	0.000
54	A	56	LEU	0	-0.001	-0.011	19.964	0.180	0.180	0.000	0.000	0.000	0.000
55	A	57	TYR	0	-0.014	-0.003	23.854	0.475	0.475	0.000	0.000	0.000	0.000
56	A	58	GLU	-1	-0.908	-0.945	26.381	-11.364	-11.364	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.018	-0.005	22.898	0.267	0.267	0.000	0.000	0.000	0.000
58	A	60	TYR	0	0.028	0.004	26.593	0.334	0.334	0.000	0.000	0.000	0.000
59	A	61	ASN	0	0.017	-0.007	28.844	0.174	0.174	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.031	-0.010	28.330	0.385	0.385	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.020	-0.009	28.135	0.244	0.244	0.000	0.000	0.000	0.000
62	A	64	ILE	0	-0.002	-0.002	31.229	0.361	0.361	0.000	0.000	0.000	0.000
63	A	65	ALA	0	-0.050	-0.022	34.270	0.302	0.302	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.795	0.897	32.536	9.465	9.465	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.004	0.016	36.344	0.205	0.205	0.000	0.000	0.000	0.000
66	A	68	GLY	0	0.051	0.029	34.337	0.098	0.098	0.000	0.000	0.000	0.000
67	A	69	LEU	0	-0.035	-0.026	27.729	-0.039	-0.039	0.000	0.000	0.000	0.000
68	A	70	VAL	0	0.022	0.007	31.716	-0.155	-0.155	0.000	0.000	0.000	0.000
69	A	71	ASP	-1	-0.796	-0.879	34.006	-8.131	-8.131	0.000	0.000	0.000	0.000
70	A	72	VAL	0	-0.037	-0.026	29.994	0.039	0.039	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.065	-0.028	28.686	-0.186	-0.186	0.000	0.000	0.000	0.000
72	A	74	ASN	0	0.042	0.034	31.790	0.093	0.093	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.851	0.899	35.340	8.111	8.111	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.876	0.945	31.986	8.891	8.891	0.000	0.000	0.000	0.000
75	A	77	LEU	0	0.002	0.009	32.480	-0.118	-0.118	0.000	0.000	0.000	0.000
76	A	78	TRP	0	0.054	0.008	25.449	-0.315	-0.315	0.000	0.000	0.000	0.000
77	A	79	GLN	0	0.017	0.005	28.449	-0.561	-0.561	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.859	-0.931	30.367	-9.168	-9.168	0.000	0.000	0.000	0.000
79	A	81	ILE	0	-0.032	0.000	26.095	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	82	ILE	0	-0.035	-0.031	24.650	-0.345	-0.345	0.000	0.000	0.000	0.000
81	A	83	LYS	1	0.943	0.980	26.649	8.902	8.902	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.004	0.018	28.893	0.163	0.163	0.000	0.000	0.000	0.000
83	A	85	LEU	0	-0.023	-0.018	22.406	-0.240	-0.240	0.000	0.000	0.000	0.000
84	A	86	HIS	0	0.001	-0.002	23.983	-0.484	-0.484	0.000	0.000	0.000	0.000
85	A	87	LEU	0	-0.018	-0.009	20.387	-0.660	-0.660	0.000	0.000	0.000	0.000
86	A	88	PRO	0	-0.017	0.004	19.231	0.384	0.384	0.000	0.000	0.000	0.000
87	A	89	SER	0	0.041	-0.015	22.346	0.681	0.681	0.000	0.000	0.000	0.000
88	A	90	SER	0	-0.035	-0.010	19.728	0.134	0.134	0.000	0.000	0.000	0.000
89	A	91	ILE	0	-0.035	-0.010	21.776	-0.200	-0.200	0.000	0.000	0.000	0.000
90	A	92	THR	0	0.076	0.050	16.949	0.294	0.294	0.000	0.000	0.000	0.000
91	A	93	SER	0	0.067	0.042	17.816	0.882	0.882	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.000	0.014	19.661	-0.345	-0.345	0.000	0.000	0.000	0.000
93	A	95	ALA	0	0.070	0.025	21.135	-0.107	-0.107	0.000	0.000	0.000	0.000
94	A	96	PHE	0	0.003	-0.005	17.892	0.144	0.144	0.000	0.000	0.000	0.000
95	A	97	THR	0	-0.011	-0.036	16.240	-0.540	-0.540	0.000	0.000	0.000	0.000
96	A	98	LEU	0	-0.013	0.001	18.727	-0.348	-0.348	0.000	0.000	0.000	0.000
97	A	99	ARG	1	0.956	0.982	21.523	11.800	11.800	0.000	0.000	0.000	0.000
98	A	100	THR	0	-0.022	0.003	17.685	0.172	0.172	0.000	0.000	0.000	0.000
99	A	101	GLN	0	-0.044	-0.036	15.440	-1.111	-1.111	0.000	0.000	0.000	0.000
100	A	102	TYR	0	0.009	-0.020	19.099	-0.055	-0.055	0.000	0.000	0.000	0.000
101	A	103	MET	0	0.019	-0.002	22.786	0.365	0.365	0.000	0.000	0.000	0.000
102	A	104	LYS	1	0.839	0.941	17.183	16.430	16.430	0.000	0.000	0.000	0.000
103	A	105	TYR	0	-0.016	-0.028	16.269	-0.151	-0.151	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.041	0.037	22.684	0.308	0.308	0.000	0.000	0.000	0.000
105	A	107	TYR	0	0.018	0.013	25.373	0.465	0.465	0.000	0.000	0.000	0.000
106	A	108	PRO	0	-0.011	-0.016	26.012	0.404	0.404	0.000	0.000	0.000	0.000
107	A	109	TYR	0	0.087	0.057	27.771	0.435	0.435	0.000	0.000	0.000	0.000
108	A	110	GLU	-1	-0.774	-0.868	29.571	-9.831	-9.831	0.000	0.000	0.000	0.000
109	A	111	CYS	0	-0.081	-0.041	31.521	0.461	0.461	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.884	-0.949	31.513	-9.580	-9.580	0.000	0.000	0.000	0.000
111	A	113	LYS	1	0.877	0.942	32.274	9.847	9.847	0.000	0.000	0.000	0.000
112	A	114	LYS	1	0.880	0.931	35.297	8.640	8.640	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.016	0.011	36.468	0.080	0.080	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.021	-0.006	34.583	0.208	0.208	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.021	-0.003	35.908	0.101	0.101	0.000	0.000	0.000	0.000
116	A	118	THR	0	-0.016	-0.013	35.996	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	119	PRO	0	-0.019	-0.016	31.988	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	120	ALA	0	0.042	0.029	33.726	-0.114	-0.114	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.806	-0.920	36.398	-8.553	-8.553	0.000	0.000	0.000	0.000
120	A	122	LEU	0	0.009	0.011	29.564	-0.079	-0.079	0.000	0.000	0.000	0.000
121	A	123	GLN	0	-0.042	-0.018	32.204	-0.117	-0.117	0.000	0.000	0.000	0.000
122	A	124	ALA	0	0.084	0.053	33.778	-0.054	-0.054	0.000	0.000	0.000	0.000
123	A	125	ALA	0	-0.054	-0.024	34.125	0.075	0.075	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.062	-0.040	28.667	-0.188	-0.188	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.906	-0.962	32.015	-9.261	-9.261	0.000	0.000	0.000	0.000
126	A	128	GLY	0	-0.006	0.004	34.329	0.099	0.099	0.000	0.000	0.000	0.000
127	A	129	ASN	0	-0.148	-0.085	29.508	0.070	0.070	0.000	0.000	0.000	0.000
128	A	130	ARG	0	0.005	0.023	28.358	0.773	0.773	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:GLY)