FMO DATABASE

FMODB ID: 1Y2RZ

Calculation Name: 2P2E-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2P2E

Chain ID: A

ChEMBL ID:

UniProt ID: Q1WRG6

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	-1015003.797769
FMO2-HF: Nuclear repulsion	967064.531011
FMO2-HF: Total energy	-47939.266759
FMO2-MP2: Total energy	-48076.288115

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:LEU)

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

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.
-205.363	-192.154	16.16	-9.995	-19.378	-0.095

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.924

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	ILE	0	0.036	0.022	3.872	1.230	2.910	-0.017	-0.763	-0.900	0.000
26	A	28	LEU	0	-0.029	-0.011	4.674	0.755	0.811	-0.001	-0.003	-0.052	0.000
64	A	66	GLU	-1	-0.833	-0.871	4.950	-43.052	-42.917	-0.001	-0.003	-0.131	0.000
66	A	68	ILE	0	-0.023	0.003	2.311	-13.566	-12.331	1.548	-0.698	-2.085	-0.003
67	A	69	ASP	-1	-0.879	-0.933	4.326	-34.403	-34.169	0.000	-0.029	-0.205	0.000
75	A	77	TYR	0	-0.022	-0.041	2.858	-5.888	-3.687	0.898	-0.833	-2.267	-0.010
80	A	82	LYS	1	0.886	0.921	2.104	48.149	48.084	3.907	-0.780	-3.063	0.002
81	A	83	MET	0	-0.065	-0.021	3.809	-2.283	-2.013	-0.001	-0.054	-0.216	0.000
83	A	85	MET	0	-0.038	-0.011	2.317	-2.896	-3.344	3.779	-0.766	-2.565	-0.006
84	A	86	ASP	-1	-0.711	-0.847	4.078	-33.130	-32.810	0.000	-0.076	-0.245	0.000
85	A	87	ASP	-1	-0.905	-0.961	2.377	-82.204	-77.304	2.999	-3.522	-4.377	-0.044
86	A	88	ASN	0	-0.173	-0.113	2.383	-19.330	-17.566	2.483	-2.221	-2.026	-0.031
87	A	89	MET	0	0.040	0.044	2.712	5.604	6.531	0.566	-0.247	-1.246	-0.003
4	A	6	THR	0	-0.022	-0.007	6.367	2.952	2.952	0.000	0.000	0.000	0.000
5	A	7	VAL	0	0.010	-0.005	10.077	0.536	0.536	0.000	0.000	0.000	0.000
6	A	8	THR	0	0.021	0.002	12.501	0.526	0.526	0.000	0.000	0.000	0.000
7	A	9	ASP	-1	-0.852	-0.927	16.023	-15.587	-15.587	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.927	-0.964	19.129	-13.641	-13.641	0.000	0.000	0.000	0.000
9	A	11	ALA	0	-0.034	-0.016	15.230	0.312	0.312	0.000	0.000	0.000	0.000
10	A	12	ALA	0	0.026	0.009	16.128	-0.125	-0.125	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.866	0.929	17.182	12.708	12.708	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.834	0.918	18.810	14.379	14.379	0.000	0.000	0.000	0.000
13	A	15	LEU	0	0.043	0.009	13.716	0.298	0.298	0.000	0.000	0.000	0.000
14	A	16	GLN	0	0.042	0.051	17.975	0.338	0.338	0.000	0.000	0.000	0.000
15	A	17	ARG	1	0.928	0.957	20.508	11.695	11.695	0.000	0.000	0.000	0.000
16	A	18	TYR	0	-0.024	-0.005	18.311	0.392	0.392	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.028	-0.026	15.758	-0.215	-0.215	0.000	0.000	0.000	0.000
18	A	20	ASP	-1	-0.921	-0.961	18.770	-13.272	-13.272	0.000	0.000	0.000	0.000
19	A	21	ASP	-1	-0.845	-0.895	21.555	-12.499	-12.499	0.000	0.000	0.000	0.000
20	A	22	SER	0	0.018	-0.003	21.062	-0.735	-0.735	0.000	0.000	0.000	0.000
21	A	23	ASN	0	-0.044	-0.016	21.602	-0.499	-0.499	0.000	0.000	0.000	0.000
22	A	24	ALA	0	0.021	0.027	19.160	-0.122	-0.122	0.000	0.000	0.000	0.000
23	A	25	VAL	0	-0.066	-0.041	13.607	-0.758	-0.758	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.015	0.017	12.290	0.592	0.592	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.009	-0.014	10.546	-1.806	-1.806	0.000	0.000	0.000	0.000
27	A	29	ASP	-1	-0.768	-0.872	8.261	-20.166	-20.166	0.000	0.000	0.000	0.000
28	A	30	PHE	0	-0.005	-0.004	9.322	-0.564	-0.564	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.742	-0.859	11.253	-14.438	-14.438	0.000	0.000	0.000	0.000
30	A	32	ASP	-1	-0.688	-0.840	13.250	-17.710	-17.710	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.011	0.021	16.190	0.543	0.543	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.089	-0.048	14.866	0.703	0.703	0.000	0.000	0.000	0.000
33	A	35	GLY	0	0.021	0.008	15.775	-0.666	-0.666	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.001	-0.014	16.739	0.734	0.734	0.000	0.000	0.000	0.000
35	A	37	LEU	0	0.042	0.013	15.325	0.467	0.467	0.000	0.000	0.000	0.000
36	A	38	SER	0	-0.020	-0.002	17.884	0.340	0.340	0.000	0.000	0.000	0.000
37	A	39	LYS	1	0.810	0.895	19.191	13.978	13.978	0.000	0.000	0.000	0.000
38	A	40	VAL	0	0.002	0.009	21.127	0.563	0.563	0.000	0.000	0.000	0.000
39	A	41	GLY	0	0.027	0.022	21.454	-0.380	-0.380	0.000	0.000	0.000	0.000
40	A	42	VAL	0	-0.044	-0.021	22.448	0.102	0.102	0.000	0.000	0.000	0.000
41	A	43	CYS	0	-0.039	-0.011	18.588	-0.739	-0.739	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.045	-0.017	19.021	0.872	0.872	0.000	0.000	0.000	0.000
43	A	45	LEU	0	-0.025	0.008	18.590	-0.532	-0.532	0.000	0.000	0.000	0.000
44	A	46	ASN	0	-0.075	-0.059	17.811	0.477	0.477	0.000	0.000	0.000	0.000
45	A	47	SER	0	-0.079	-0.037	14.252	-0.136	-0.136	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.794	-0.887	13.364	-17.492	-17.492	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.029	-0.009	6.788	-0.733	-0.733	0.000	0.000	0.000	0.000
48	A	50	ARG	1	0.802	0.879	11.418	17.100	17.100	0.000	0.000	0.000	0.000
49	A	51	ILE	0	-0.019	-0.012	10.312	-1.434	-1.434	0.000	0.000	0.000	0.000
50	A	52	LEU	0	0.007	0.007	12.868	1.356	1.356	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.052	-0.019	14.284	-1.152	-1.152	0.000	0.000	0.000	0.000
52	A	54	VAL	0	0.028	0.016	16.248	0.666	0.666	0.000	0.000	0.000	0.000
53	A	55	SER	0	0.065	0.017	18.959	-0.542	-0.542	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.814	0.896	17.965	15.506	15.506	0.000	0.000	0.000	0.000
55	A	57	ASP	-1	-0.891	-0.944	20.449	-12.828	-12.828	0.000	0.000	0.000	0.000
56	A	58	MET	0	-0.002	0.035	19.935	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.895	-0.954	18.705	-15.864	-15.864	0.000	0.000	0.000	0.000
58	A	60	TYR	0	0.015	-0.003	13.318	-0.097	-0.097	0.000	0.000	0.000	0.000
59	A	61	LYS	1	0.890	0.949	13.010	20.232	20.232	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.905	0.958	14.208	14.176	14.176	0.000	0.000	0.000	0.000
61	A	63	ASP	-1	-0.838	-0.914	13.820	-16.685	-16.685	0.000	0.000	0.000	0.000
62	A	64	TYR	0	-0.063	-0.063	10.178	-1.034	-1.034	0.000	0.000	0.000	0.000
63	A	65	ASN	0	0.021	0.009	9.729	-0.872	-0.872	0.000	0.000	0.000	0.000
65	A	67	VAL	0	-0.007	-0.020	5.861	3.205	3.205	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.007	-0.021	6.459	-2.804	-2.804	0.000	0.000	0.000	0.000
69	A	71	ASN	0	-0.009	-0.008	9.018	0.020	0.020	0.000	0.000	0.000	0.000
70	A	72	ILE	0	-0.010	0.002	11.930	1.920	1.920	0.000	0.000	0.000	0.000
71	A	73	GLY	0	0.026	0.025	12.422	1.241	1.241	0.000	0.000	0.000	0.000
72	A	74	LYS	1	0.839	0.923	8.957	28.184	28.184	0.000	0.000	0.000	0.000
73	A	75	PHE	0	0.056	0.036	7.003	2.691	2.691	0.000	0.000	0.000	0.000
74	A	76	TYR	0	-0.019	-0.017	7.248	-3.525	-3.525	0.000	0.000	0.000	0.000
76	A	78	LYS	1	0.848	0.945	7.172	19.334	19.334	0.000	0.000	0.000	0.000
77	A	79	GLY	0	0.019	0.021	6.378	-1.125	-1.125	0.000	0.000	0.000	0.000
78	A	80	TYR	0	-0.050	-0.076	6.419	-2.754	-2.754	0.000	0.000	0.000	0.000
79	A	81	SER	0	-0.020	-0.026	7.023	-0.726	-0.726	0.000	0.000	0.000	0.000
82	A	84	TYR	0	-0.019	-0.006	6.067	2.161	2.161	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.936	0.974	6.601	20.683	20.683	0.000	0.000	0.000	0.000
89	A	91	ILE	0	0.041	0.027	9.037	0.760	0.760	0.000	0.000	0.000	0.000
90	A	92	SER	0	-0.005	-0.007	11.753	0.410	0.410	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.008	0.003	15.559	-0.077	-0.077	0.000	0.000	0.000	0.000
92	A	94	ASN	0	-0.064	-0.028	18.439	0.170	0.170	0.000	0.000	0.000	0.000
93	A	95	THR	0	0.041	0.012	21.025	0.157	0.157	0.000	0.000	0.000	0.000
94	A	96	ASN	0	-0.010	-0.004	24.323	0.587	0.587	0.000	0.000	0.000	0.000
95	A	97	ASN	0	0.011	0.002	22.293	0.048	0.048	0.000	0.000	0.000	0.000
96	A	98	SER	0	0.033	0.018	23.331	-0.398	-0.398	0.000	0.000	0.000	0.000
97	A	99	LEU	0	0.024	0.021	18.884	-0.217	-0.217	0.000	0.000	0.000	0.000
98	A	100	LEU	0	0.015	0.009	14.489	0.220	0.220	0.000	0.000	0.000	0.000
99	A	101	ARG	1	0.827	0.923	14.183	16.643	16.643	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.018	0.003	6.913	-0.757	-0.757	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.030	-0.025	10.435	1.680	1.680	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.023	0.001	7.842	-3.007	-3.007	0.000	0.000	0.000	0.000
103	A	105	ASP	-1	-0.882	-0.927	8.264	-27.073	-27.073	0.000	0.000	0.000	0.000
104	A	106	ASN	0	-0.094	-0.063	7.748	4.309	4.309	0.000	0.000	0.000	0.000
105	A	107	SER	0	-0.023	-0.017	8.506	1.844	1.844	0.000	0.000	0.000	0.000
106	A	108	GLY	0	-0.015	0.013	11.101	1.765	1.765	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.885	-0.964	11.861	-17.733	-17.733	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.010	0.000	6.870	0.003	0.003	0.000	0.000	0.000	0.000
109	A	111	MET	0	-0.001	0.006	11.002	0.702	0.702	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.015	0.020	13.262	-0.231	-0.231	0.000	0.000	0.000	0.000
111	A	113	ALA	0	-0.028	-0.026	16.523	0.554	0.554	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.003	0.012	11.319	0.131	0.131	0.000	0.000	0.000	0.000
113	A	115	SER	0	0.006	-0.007	15.001	0.250	0.250	0.000	0.000	0.000	0.000
114	A	116	ILE	0	0.009	-0.013	15.246	-0.964	-0.964	0.000	0.000	0.000	0.000
115	A	117	GLN	0	-0.040	-0.010	17.003	0.635	0.635	0.000	0.000	0.000	0.000
116	A	118	ASP	-1	-0.790	-0.889	18.277	-13.849	-13.849	0.000	0.000	0.000	0.000
117	A	119	PHE	0	-0.045	-0.023	18.654	0.556	0.556	0.000	0.000	0.000	0.000
118	A	120	ARG	1	0.781	0.835	21.339	12.895	12.895	0.000	0.000	0.000	0.000
119	A	121	GLU	-2	-1.884	-1.926	23.367	-22.086	-22.086	0.000	0.000	0.000	0.000

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