FMO DATABASE

FMODB ID: 9RM12

Calculation Name: 2CXY-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CXY

Chain ID: A

ChEMBL ID:

UniProt ID: Q8NFD5

Base Structure: X-ray

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-933973.662976
FMO2-HF: Nuclear repulsion	888820.915027
FMO2-HF: Total energy	-45152.74795
FMO2-MP2: Total energy	-45285.568957

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.
114.923	116.205	-0.019	-0.411	-0.853	-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 : 0.795 / q_NPA : 0.880

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	LYS	1	1.036	1.009	3.720	39.200	40.226	-0.016	-0.376	-0.635	-0.001
36	A	36	SER	0	-0.065	-0.046	4.240	-1.971	-1.941	-0.001	-0.010	-0.019	0.000
38	A	38	PRO	0	-0.005	0.014	4.579	-6.658	-6.539	-0.001	-0.007	-0.111	0.000
44	A	44	PRO	0	0.013	0.000	3.852	1.467	1.574	-0.001	-0.018	-0.088	0.000
4	A	4	ILE	0	0.045	0.030	6.969	0.008	0.008	0.000	0.000	0.000	0.000
5	A	5	THR	0	0.003	0.001	9.120	0.802	0.802	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.840	0.896	6.863	34.573	34.573	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.011	-0.006	9.920	1.169	1.169	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.052	-0.052	12.041	1.430	1.430	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.805	-0.889	11.782	-26.883	-26.883	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.070	-0.035	9.167	0.190	0.190	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.003	0.013	13.170	0.563	0.563	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.032	-0.017	17.024	-0.269	-0.269	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.750	-0.847	19.112	-16.205	-16.205	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.006	0.006	22.086	-0.393	-0.393	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.879	-0.949	23.580	-12.969	-12.969	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.706	0.812	14.553	19.211	19.211	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.851	0.897	19.621	14.728	14.728	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.046	0.020	20.734	-0.211	-0.211	0.000	0.000	0.000	0.000
19	A	19	TRP	0	-0.013	-0.010	15.482	-0.200	-0.200	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.015	-0.006	15.323	-0.227	-0.227	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.784	-0.838	17.917	-15.706	-15.706	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.940	0.979	20.273	12.374	12.374	0.000	0.000	0.000	0.000
23	A	23	TYR	0	-0.020	-0.025	13.309	-0.616	-0.616	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.038	-0.034	13.208	-0.324	-0.324	0.000	0.000	0.000	0.000
25	A	25	THR	0	0.033	0.020	16.888	-0.091	-0.091	0.000	0.000	0.000	0.000
26	A	26	PHE	0	0.022	0.009	19.702	0.212	0.212	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.085	-0.045	14.765	0.483	0.483	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.972	-0.986	17.698	-16.703	-16.703	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.914	-0.960	18.749	-12.169	-12.169	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.838	0.922	18.560	15.490	15.490	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.040	0.029	20.476	0.101	0.101	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.074	-0.034	16.319	-0.150	-0.150	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.083	0.047	14.673	-0.881	-0.881	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.027	-0.018	9.810	-1.612	-1.612	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.049	0.018	9.479	0.249	0.249	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.014	-0.002	5.077	3.775	3.775	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.011	0.003	4.896	-1.525	-1.525	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.014	0.008	6.930	3.814	3.814	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.012	0.012	9.614	-0.269	-0.269	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.958	0.966	6.222	30.400	30.400	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.880	0.954	6.249	21.086	21.086	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.030	-0.020	6.573	4.614	4.614	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.736	-0.851	9.809	-22.701	-22.701	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.022	-0.021	10.720	1.724	1.724	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.057	0.051	13.468	1.263	1.263	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.977	0.991	15.909	16.721	16.721	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.022	-0.003	14.172	0.917	0.917	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.005	-0.041	16.993	0.759	0.759	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.017	0.006	19.115	0.857	0.857	0.000	0.000	0.000	0.000
53	A	53	CYS	0	-0.006	-0.003	20.221	0.631	0.631	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.055	-0.027	19.785	0.604	0.604	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.861	0.917	22.482	12.314	12.314	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.915	-0.966	24.167	-12.385	-12.385	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.082	-0.038	23.974	0.517	0.517	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.021	0.014	27.131	0.429	0.429	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.013	0.005	24.762	0.240	0.240	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.028	-0.024	21.936	0.155	0.155	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.010	-0.005	24.461	0.095	0.095	0.000	0.000	0.000	0.000
62	A	62	GLN	0	0.080	0.038	28.102	0.302	0.302	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.025	0.015	22.646	0.195	0.195	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.010	-0.007	24.863	-0.345	-0.345	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.911	0.966	27.005	9.329	9.329	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.045	-0.035	29.763	0.553	0.553	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.928	0.972	27.419	10.526	10.526	0.000	0.000	0.000	0.000
68	A	68	LYS	1	1.008	1.020	25.471	10.678	10.678	0.000	0.000	0.000	0.000
69	A	69	TRP	0	0.042	0.013	18.536	-0.551	-0.551	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.897	0.923	20.696	12.004	12.004	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.903	-0.927	22.545	-12.026	-12.026	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.030	0.011	19.438	-0.438	-0.438	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.018	-0.012	17.537	-0.761	-0.761	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.002	-0.007	17.860	-0.827	-0.827	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.030	0.004	19.483	-0.498	-0.498	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.004	0.007	15.496	-0.214	-0.214	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.045	-0.022	14.860	-1.521	-1.521	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.019	0.000	12.894	-1.926	-1.926	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.026	-0.001	14.500	-0.724	-0.724	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.060	0.038	17.290	0.268	0.268	0.000	0.000	0.000	0.000
81	A	81	SER	0	0.005	0.013	18.863	0.791	0.791	0.000	0.000	0.000	0.000
82	A	82	SER	0	0.061	0.015	20.782	-0.312	-0.312	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.055	0.035	18.089	-0.056	-0.056	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.028	0.036	16.011	-0.721	-0.721	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.037	0.018	16.589	-0.597	-0.597	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.026	-0.023	18.917	0.143	0.143	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.037	-0.028	13.579	-0.296	-0.296	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.005	0.003	14.177	-0.827	-0.827	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.916	0.967	15.507	12.946	12.946	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.853	0.923	12.311	22.021	22.021	0.000	0.000	0.000	0.000
91	A	91	GLN	0	0.019	-0.004	9.286	1.607	1.607	0.000	0.000	0.000	0.000
92	A	92	TYR	0	0.009	-0.029	13.782	-0.314	-0.314	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.012	-0.017	16.541	0.503	0.503	0.000	0.000	0.000	0.000
94	A	94	GLN	0	0.007	0.026	12.085	0.618	0.618	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.011	-0.006	9.534	-0.341	-0.341	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.017	0.020	14.835	0.134	0.134	0.000	0.000	0.000	0.000
97	A	97	PHE	0	0.009	0.002	17.616	0.743	0.743	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.058	0.026	20.360	0.644	0.644	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.029	0.024	19.711	0.367	0.367	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.718	-0.838	21.659	-12.098	-12.098	0.000	0.000	0.000	0.000
101	A	101	CYS	0	-0.017	0.014	23.577	0.608	0.608	0.000	0.000	0.000	0.000
102	A	102	LYS	1	1.005	1.021	24.510	11.806	11.806	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.109	-0.044	23.301	0.390	0.390	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.819	-0.882	25.688	-11.589	-11.589	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.773	0.839	26.291	11.473	11.473	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.008	0.026	29.817	0.302	0.302	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.985	-0.990	28.220	-9.795	-9.795	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.948	-0.985	28.446	-10.424	-10.424	0.000	0.000	0.000	0.000
109	A	109	PRO	0	-0.068	-0.041	25.996	0.197	0.197	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.016	0.009	29.253	0.027	0.027	0.000	0.000	0.000	0.000
111	A	111	PRO	0	0.011	0.003	31.297	-0.203	-0.203	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.971	-0.983	28.030	-10.767	-10.767	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.075	-0.039	31.724	0.100	0.100	0.000	0.000	0.000	0.000
114	A	114	PHE	-1	-0.947	-0.952	33.723	-8.228	-8.228	0.000	0.000	0.000	0.000

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