FMO DATABASE

FMODB ID: 1Y74Z

Calculation Name: 3CPT-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3CPT

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JHS3

Base Structure: X-ray

Registration Date: 2025-10-04

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	-962954.733913
FMO2-HF: Nuclear repulsion	917984.757511
FMO2-HF: Total energy	-44969.976402
FMO2-MP2: Total energy	-45104.382562

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:ASP)

Summations of interaction energy for fragment #1(A:3:ASP)

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.
9.681	13.495	0.465	-1.541	-2.737	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.044 / q_NPA : -0.027

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	5	LEU	0	0.115	0.061	3.856	0.514	2.381	-0.012	-0.693	-1.162	0.001
4	A	6	LYS	1	0.945	0.984	2.589	-0.510	0.917	0.477	-0.604	-1.300	0.000
5	A	7	ARG	1	0.972	0.976	4.003	6.518	7.038	0.000	-0.244	-0.275	0.001
6	A	8	PHE	0	0.018	0.006	5.781	2.110	2.110	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.045	0.014	7.169	1.325	1.325	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.022	-0.011	8.122	0.959	0.959	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.891	0.934	9.652	2.272	2.272	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.889	0.939	11.677	2.429	2.429	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.030	0.026	12.234	0.243	0.243	0.000	0.000	0.000	0.000
12	A	14	PRO	0	-0.025	-0.026	14.552	0.152	0.152	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.078	-0.042	17.068	0.078	0.078	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.014	-0.013	19.104	0.055	0.055	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.900	-0.946	20.789	-0.484	-0.484	0.000	0.000	0.000	0.000
16	A	18	GLY	0	0.008	0.002	22.760	0.005	0.005	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.041	-0.012	16.585	0.019	0.019	0.000	0.000	0.000	0.000
18	A	20	HIS	0	0.018	0.006	17.924	-0.038	-0.038	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.001	-0.019	14.259	0.044	0.044	0.000	0.000	0.000	0.000
20	A	22	ILE	0	-0.007	0.006	11.887	-0.031	-0.031	0.000	0.000	0.000	0.000
21	A	23	VAL	0	-0.024	-0.019	11.698	-0.140	-0.140	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.018	0.019	10.034	0.063	0.063	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.019	-0.016	11.352	-0.065	-0.065	0.000	0.000	0.000	0.000
24	A	26	ASP	-1	-0.719	-0.850	13.954	-0.779	-0.779	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.945	0.949	16.687	0.660	0.660	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.853	-0.918	19.600	-0.311	-0.311	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.047	-0.018	17.476	0.097	0.097	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.027	-0.031	14.160	0.098	0.098	0.000	0.000	0.000	0.000
29	A	31	PRO	0	-0.093	-0.048	10.617	-0.215	-0.215	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.058	0.030	8.068	0.325	0.325	0.000	0.000	0.000	0.000
31	A	33	ILE	0	-0.024	-0.021	5.176	-1.234	-1.234	0.000	0.000	0.000	0.000
32	A	34	LYS	1	0.869	0.937	7.683	0.936	0.936	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.058	-0.024	7.240	0.288	0.288	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.028	-0.002	9.811	0.007	0.007	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.003	0.007	12.654	0.228	0.228	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.872	-0.943	15.320	0.024	0.024	0.000	0.000	0.000	0.000
37	A	39	ASN	0	-0.020	-0.004	18.286	0.069	0.069	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.043	-0.015	17.211	-0.049	-0.049	0.000	0.000	0.000	0.000
39	A	41	PRO	0	0.000	-0.005	19.212	0.096	0.096	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.863	-0.939	19.388	0.363	0.363	0.000	0.000	0.000	0.000
41	A	43	HIS	0	-0.073	-0.050	20.105	0.051	0.051	0.000	0.000	0.000	0.000
42	A	44	ALA	0	0.013	-0.004	20.933	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	45	LEU	0	0.006	0.013	15.258	-0.126	-0.126	0.000	0.000	0.000	0.000
44	A	46	ARG	1	0.925	0.966	16.818	-0.158	-0.158	0.000	0.000	0.000	0.000
45	A	47	PRO	0	0.031	0.021	17.169	-0.067	-0.067	0.000	0.000	0.000	0.000
46	A	48	GLY	0	0.070	0.047	19.323	-0.073	-0.073	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.027	0.017	21.444	-0.018	-0.018	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.008	-0.009	16.605	-0.050	-0.050	0.000	0.000	0.000	0.000
49	A	51	SER	0	0.055	0.027	20.704	-0.047	-0.047	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.025	-0.009	22.403	0.009	0.009	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.028	-0.016	22.962	0.011	0.011	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.054	0.042	22.194	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.004	0.006	24.353	0.011	0.011	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.014	0.003	27.328	0.020	0.020	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.039	-0.032	26.291	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.894	-0.914	27.415	-0.430	-0.430	0.000	0.000	0.000	0.000
57	A	59	GLN	0	0.011	-0.013	29.260	0.013	0.013	0.000	0.000	0.000	0.000
58	A	60	GLY	0	0.037	0.019	31.897	0.021	0.021	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.059	-0.051	30.725	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.821	0.900	31.060	0.368	0.368	0.000	0.000	0.000	0.000
61	A	63	LEU	0	-0.033	-0.005	35.359	0.023	0.023	0.000	0.000	0.000	0.000
62	A	64	GLY	0	0.004	0.013	36.951	0.016	0.016	0.000	0.000	0.000	0.000
63	A	65	LEU	0	-0.061	-0.014	33.157	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	66	SER	0	0.006	0.001	34.379	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.971	0.976	25.771	0.737	0.737	0.000	0.000	0.000	0.000
66	A	68	ASN	0	0.014	0.000	26.658	-0.072	-0.072	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.975	0.979	25.454	0.702	0.702	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.045	0.019	23.784	-0.114	-0.114	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.023	0.011	24.431	0.074	0.074	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.021	0.016	24.621	-0.061	-0.061	0.000	0.000	0.000	0.000
71	A	73	CYS	0	-0.058	-0.025	26.114	0.060	0.060	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.037	0.000	26.897	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	75	TYR	0	0.008	0.005	26.656	0.051	0.051	0.000	0.000	0.000	0.000
74	A	76	ASN	0	0.018	0.001	30.152	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	77	THR	0	0.013	0.011	28.243	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	78	TYR	0	0.013	0.018	23.969	0.003	0.003	0.000	0.000	0.000	0.000
77	A	79	GLN	0	0.003	0.003	24.054	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.011	-0.003	21.193	-0.043	-0.043	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.009	0.003	21.152	0.045	0.045	0.000	0.000	0.000	0.000
80	A	82	GLN	0	-0.037	-0.030	19.815	-0.088	-0.088	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.003	-0.009	18.928	0.095	0.095	0.000	0.000	0.000	0.000
82	A	84	ASN	0	-0.021	-0.019	19.550	-0.125	-0.125	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.777	0.860	17.509	1.418	1.418	0.000	0.000	0.000	0.000
84	A	86	LEU	0	0.016	0.023	18.361	-0.086	-0.086	0.000	0.000	0.000	0.000
85	A	87	PRO	0	0.029	0.010	17.102	0.001	0.001	0.000	0.000	0.000	0.000
86	A	88	LEU	0	0.005	0.022	12.827	0.107	0.107	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.035	-0.018	16.153	0.162	0.162	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.015	0.021	14.025	-0.169	-0.169	0.000	0.000	0.000	0.000
89	A	91	SER	0	0.002	-0.008	15.394	0.281	0.281	0.000	0.000	0.000	0.000
90	A	92	PHE	0	0.025	0.013	15.826	-0.139	-0.139	0.000	0.000	0.000	0.000
91	A	93	ILE	0	-0.031	-0.013	17.167	0.156	0.156	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.034	0.028	18.945	-0.065	-0.065	0.000	0.000	0.000	0.000
93	A	95	SER	0	0.055	0.021	21.671	0.053	0.053	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.069	-0.036	25.054	-0.051	-0.051	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.030	0.013	28.298	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.019	0.036	24.163	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	99	ASN	0	0.050	0.016	26.258	-0.018	-0.018	0.000	0.000	0.000	0.000
98	A	100	THR	0	0.061	0.009	24.977	-0.053	-0.053	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.007	0.017	24.919	-0.070	-0.070	0.000	0.000	0.000	0.000
100	A	102	LEU	0	-0.006	-0.013	23.632	-0.059	-0.059	0.000	0.000	0.000	0.000
101	A	103	ILE	0	0.021	0.020	19.696	-0.118	-0.118	0.000	0.000	0.000	0.000
102	A	104	VAL	0	0.007	-0.001	20.453	-0.134	-0.134	0.000	0.000	0.000	0.000
103	A	105	SER	0	-0.085	-0.036	22.054	-0.093	-0.093	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.070	0.027	15.935	-0.078	-0.078	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.844	-0.902	17.290	-1.830	-1.830	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.903	0.957	17.843	1.092	1.092	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.880	-0.926	17.535	-1.871	-1.871	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.014	-0.013	12.301	-0.212	-0.212	0.000	0.000	0.000	0.000
109	A	111	ALA	0	0.000	0.009	13.965	-0.333	-0.333	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.004	-0.002	15.557	-0.064	-0.064	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.054	0.032	10.216	-0.155	-0.155	0.000	0.000	0.000	0.000
112	A	114	PHE	0	-0.047	-0.043	10.865	-0.480	-0.480	0.000	0.000	0.000	0.000
113	A	115	GLU	-1	-0.838	-0.890	12.746	-1.668	-1.668	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.892	-0.951	11.822	-3.477	-3.477	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.060	-0.030	7.404	-0.238	-0.238	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.751	0.844	10.679	1.851	1.851	0.000	0.000	0.000	0.000
117	A	119	GLN	0	-0.059	-0.022	13.605	0.285	0.285	0.000	0.000	0.000	0.000
118	A	120	VAL	0	-0.086	-0.037	10.007	-0.196	-0.196	0.000	0.000	0.000	0.000
119	A	121	VAL	-1	-0.948	-0.964	13.111	-0.892	-0.892	0.000	0.000	0.000	0.000

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