FMO DATABASE

FMODB ID: KKNZ3

Calculation Name: 2CUJ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CUJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q8CHV6

Base Structure: SolutionNMR

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-714308.034385
FMO2-HF: Nuclear repulsion	673529.66096
FMO2-HF: Total energy	-40778.373425
FMO2-MP2: Total energy	-40897.314491

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.
36.069	37.081	0.002	-0.41	-0.603	-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 : 0.871 / q_NPA : 0.921

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	0.010	0.011	3.849	-0.112	0.794	0.003	-0.405	-0.504	-0.001
4	A	4	GLY	0	0.039	0.015	5.308	1.128	1.234	-0.001	-0.005	-0.099	0.000
5	A	5	SER	0	-0.036	-0.009	8.627	0.486	0.486	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.021	0.003	12.181	-0.125	-0.125	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.007	0.008	13.759	0.624	0.624	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.055	-0.024	17.302	-0.072	-0.072	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.913	-0.949	20.129	-12.839	-12.839	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.009	-0.006	23.900	0.084	0.084	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.035	0.025	26.854	0.249	0.249	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.031	-0.015	29.238	0.409	0.409	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.008	-0.008	31.642	-0.095	-0.095	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.019	0.004	31.331	0.286	0.286	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.018	0.007	34.576	0.016	0.016	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.019	-0.012	35.718	-0.197	-0.197	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.017	0.007	37.645	0.243	0.243	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.034	-0.021	38.974	-0.085	-0.085	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.029	0.013	39.292	0.097	0.097	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.023	-0.009	40.899	-0.012	-0.012	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.008	0.002	35.980	0.153	0.153	0.000	0.000	0.000	0.000
22	A	22	SER	0	0.013	0.011	39.444	0.136	0.136	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.023	0.021	36.353	-0.225	-0.225	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.962	0.976	32.893	9.106	9.106	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.980	0.983	35.730	7.876	7.876	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.007	-0.009	33.348	0.163	0.163	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.031	0.014	31.458	-0.286	-0.286	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.043	0.035	28.150	0.284	0.284	0.000	0.000	0.000	0.000
29	A	29	PRO	0	0.047	0.020	30.402	0.298	0.298	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.058	-0.015	31.433	-0.274	-0.274	0.000	0.000	0.000	0.000
31	A	31	ASN	0	0.014	-0.005	27.680	-0.101	-0.101	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.036	0.011	30.223	0.084	0.084	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.029	-0.004	25.873	0.251	0.251	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.073	0.037	28.608	-0.224	-0.224	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.023	0.001	29.888	0.270	0.270	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.047	0.032	33.388	0.047	0.047	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.037	-0.014	36.346	0.148	0.148	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.047	-0.045	32.682	0.192	0.192	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.934	-0.972	35.501	-8.598	-8.598	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.902	0.960	36.925	7.795	7.795	0.000	0.000	0.000	0.000
41	A	41	LEU	0	-0.029	-0.001	38.103	0.220	0.220	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.018	-0.017	38.706	-0.302	-0.302	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.920	-0.978	36.656	-8.024	-8.024	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.924	0.960	38.052	6.942	6.942	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.778	-0.893	40.884	-7.472	-7.472	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.950	0.981	33.272	9.037	9.037	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.895	-0.930	36.533	-8.070	-8.070	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.012	-0.010	38.194	-0.048	-0.048	0.000	0.000	0.000	0.000
49	A	49	CYS	0	-0.065	-0.033	37.167	0.013	0.013	0.000	0.000	0.000	0.000
50	A	50	GLN	0	-0.017	-0.002	32.258	-0.361	-0.361	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.003	-0.008	35.983	-0.027	-0.027	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.065	-0.026	38.559	0.137	0.137	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.843	0.929	34.215	8.987	8.987	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.052	-0.021	38.316	0.154	0.154	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.076	0.039	36.845	-0.161	-0.161	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.056	0.017	35.816	0.261	0.261	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.031	0.009	38.641	0.212	0.212	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.012	0.001	40.532	0.174	0.174	0.000	0.000	0.000	0.000
59	A	59	TYR	0	0.049	0.008	42.140	0.255	0.255	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.016	-0.005	41.272	0.186	0.186	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.858	-0.918	45.196	-6.491	-6.491	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.037	-0.042	44.779	0.159	0.159	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.818	0.928	46.183	6.911	6.911	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.084	0.041	49.746	0.137	0.137	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.011	0.009	52.073	0.136	0.136	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.051	-0.032	50.534	0.116	0.116	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.017	0.010	51.914	0.087	0.087	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.033	0.002	55.458	0.193	0.193	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.811	-0.906	57.885	-5.159	-5.159	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.061	-0.010	58.133	0.097	0.097	0.000	0.000	0.000	0.000
71	A	71	HIS	0	0.033	0.001	56.452	0.142	0.142	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.829	0.918	61.166	5.161	5.161	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.055	-0.022	63.475	0.071	0.071	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.056	0.037	62.740	0.072	0.072	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.006	0.005	62.073	-0.063	-0.063	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.007	0.006	56.541	0.013	0.013	0.000	0.000	0.000	0.000
77	A	77	ARG	1	1.000	1.015	58.693	5.082	5.082	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.030	0.013	52.641	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	79	ALA	0	-0.058	-0.036	55.960	-0.062	-0.062	0.000	0.000	0.000	0.000
80	A	80	GLN	0	0.086	0.037	58.593	0.023	0.023	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.058	0.026	53.613	-0.051	-0.051	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.891	0.933	52.668	5.527	5.527	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.019	-0.008	53.529	-0.071	-0.071	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.017	0.014	54.814	-0.022	-0.022	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.041	-0.016	49.228	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.904	0.964	50.754	5.860	5.860	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.002	0.011	46.164	-0.107	-0.107	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.824	-0.916	47.236	-6.506	-6.506	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.025	-0.004	48.722	-0.070	-0.070	0.000	0.000	0.000	0.000
90	A	90	ASN	0	-0.045	-0.032	47.127	0.092	0.092	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.884	0.935	41.033	7.533	7.533	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.043	0.021	46.179	-0.028	-0.028	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.950	0.958	48.968	6.064	6.064	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.932	0.983	44.421	6.918	6.918	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.010	0.015	45.342	-0.036	-0.036	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.006	-0.025	47.583	0.045	0.045	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.826	-0.920	50.386	-5.972	-5.972	0.000	0.000	0.000	0.000
98	A	98	PHE	0	-0.047	-0.015	45.233	0.043	0.043	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.022	-0.005	48.873	0.021	0.021	0.000	0.000	0.000	0.000
100	A	100	ILE	0	-0.039	-0.004	51.176	0.093	0.093	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.916	0.951	44.974	6.846	6.846	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.843	-0.911	47.509	-6.723	-6.723	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.005	0.021	51.534	0.036	0.036	0.000	0.000	0.000	0.000
104	A	104	TYR	0	-0.068	-0.030	48.382	0.066	0.066	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.031	-0.029	54.080	0.049	0.049	0.000	0.000	0.000	0.000
106	A	106	THR	0	0.032	0.008	56.905	-0.036	-0.036	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.825	0.903	55.270	5.688	5.688	0.000	0.000	0.000	0.000
108	A	108	ALA	-1	-0.887	-0.933	60.144	-5.026	-5.026	0.000	0.000	0.000	0.000

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