FMO DATABASE

FMODB ID: VYKL1

Calculation Name: 2CUG-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CUG

Chain ID: A

ChEMBL ID:

UniProt ID: Q80TN4

Base Structure: SolutionNMR

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	88
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-524229.723422
FMO2-HF: Nuclear repulsion	490738.69027
FMO2-HF: Total energy	-33491.033152
FMO2-MP2: Total energy	-33590.760866

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.
10.38	11.544	-0.002	-0.434	-0.726	-0.001

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 : 0.867 / 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	3	SER	0	0.048	0.024	3.853	5.535	6.534	-0.001	-0.418	-0.579	-0.001
4	A	4	GLY	0	0.048	0.013	4.485	-4.412	-4.247	-0.001	-0.016	-0.147	0.000
5	A	5	SER	0	-0.045	-0.021	6.609	1.421	1.421	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.011	-0.008	10.372	0.640	0.640	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.044	0.021	13.901	-0.075	-0.075	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.037	-0.003	17.487	0.660	0.660	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.013	0.005	19.989	0.397	0.397	0.000	0.000	0.000	0.000
10	A	10	GLN	0	0.027	0.011	23.350	0.055	0.055	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.026	-0.025	26.769	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.020	-0.008	29.332	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.009	0.006	33.016	-0.154	-0.154	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.008	0.018	35.232	0.104	0.104	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.028	-0.008	38.428	0.238	0.238	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.922	-0.957	37.828	-8.028	-8.028	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.023	-0.028	35.753	-0.289	-0.289	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.777	-0.890	34.196	-8.742	-8.742	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.000	-0.001	35.119	-0.254	-0.254	0.000	0.000	0.000	0.000
20	A	20	TYR	0	0.018	-0.015	33.686	-0.088	-0.088	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.937	0.975	29.446	10.383	10.383	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.023	0.004	30.917	-0.346	-0.346	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.040	-0.029	32.669	-0.142	-0.142	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.014	0.012	29.462	-0.123	-0.123	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.033	-0.011	29.489	-0.178	-0.178	0.000	0.000	0.000	0.000
26	A	26	SER	0	0.018	-0.010	29.763	-0.126	-0.126	0.000	0.000	0.000	0.000
27	A	27	ARG	1	1.007	0.987	32.243	9.536	9.536	0.000	0.000	0.000	0.000
28	A	28	THR	0	0.006	0.011	32.601	0.230	0.230	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.007	0.013	34.014	0.161	0.161	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.065	0.027	35.781	0.248	0.248	0.000	0.000	0.000	0.000
31	A	31	GLN	0	0.030	-0.001	39.239	-0.270	-0.270	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.034	-0.015	40.105	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.912	-0.956	33.774	-9.610	-9.610	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.053	0.032	36.309	-0.142	-0.142	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.960	0.995	37.744	7.489	7.489	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.916	0.957	33.272	9.540	9.540	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.016	0.008	33.721	-0.077	-0.077	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.066	0.032	34.974	-0.026	-0.026	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.927	0.955	37.810	7.469	7.469	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.935	0.973	31.216	10.131	10.131	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.017	0.015	31.104	-0.027	-0.027	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.023	0.001	34.871	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.897	0.941	37.555	8.129	8.129	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.953	-0.971	32.134	-9.804	-9.804	0.000	0.000	0.000	0.000
45	A	45	TRP	0	-0.038	-0.017	28.893	-0.113	-0.113	0.000	0.000	0.000	0.000
46	A	46	HIS	0	0.006	0.009	35.378	0.162	0.162	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.027	0.003	39.042	-0.080	-0.080	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.984	-0.965	40.835	-7.263	-7.263	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.897	0.948	37.326	8.234	8.234	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.029	-0.023	34.831	-0.147	-0.147	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.965	0.978	36.972	7.980	7.980	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.897	-0.944	33.545	-9.553	-9.553	0.000	0.000	0.000	0.000
53	A	53	PRO	0	-0.009	-0.004	35.511	0.095	0.095	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.044	0.014	35.450	-0.232	-0.232	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.007	0.002	35.392	-0.148	-0.148	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.882	-0.958	36.380	-8.200	-8.200	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.884	-0.918	36.038	-8.832	-8.832	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.993	0.997	30.451	10.323	10.323	0.000	0.000	0.000	0.000
59	A	59	PHE	0	-0.002	0.003	35.846	0.069	0.069	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.001	-0.005	38.600	0.145	0.145	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.042	-0.032	34.843	0.088	0.088	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.037	-0.019	34.133	0.034	0.034	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.030	-0.020	37.663	0.099	0.099	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.845	0.913	40.976	7.203	7.203	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.001	0.008	37.479	0.096	0.096	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.007	-0.006	39.520	0.087	0.087	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.825	-0.905	41.137	-7.000	-7.000	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.023	0.009	41.297	0.183	0.183	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.005	0.001	38.264	0.088	0.088	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.039	-0.032	42.760	0.158	0.158	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.036	-0.020	44.771	0.290	0.290	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.893	-0.942	47.466	-6.473	-6.473	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.865	-0.919	48.859	-6.131	-6.131	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.858	0.939	46.884	6.534	6.534	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.935	0.971	42.419	7.208	7.208	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.012	-0.020	45.305	-0.117	-0.117	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.027	-0.020	47.983	0.056	0.056	0.000	0.000	0.000	0.000
78	A	78	TYR	0	-0.065	-0.040	38.323	0.024	0.024	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.960	-0.982	44.114	-7.319	-7.319	0.000	0.000	0.000	0.000
80	A	80	HIS	0	0.012	0.006	45.083	-0.039	-0.039	0.000	0.000	0.000	0.000
81	A	81	TYR	0	-0.017	0.000	45.624	0.065	0.065	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.012	0.021	43.538	-0.067	-0.067	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.117	-0.069	38.951	-0.245	-0.245	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.005	0.009	40.826	-0.166	-0.166	0.000	0.000	0.000	0.000
85	A	85	PRO	0	-0.044	-0.025	43.489	-0.025	-0.025	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.000	-0.032	45.888	0.078	0.078	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.036	-0.036	48.849	-0.024	-0.024	0.000	0.000	0.000	0.000
88	A	88	GLY	-1	-0.928	-0.911	51.805	-6.163	-6.163	0.000	0.000	0.000	0.000

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