FMO DATABASE

FMODB ID: LG969

Calculation Name: 5CX3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5CX3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BQS8

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	-1064422.540357
FMO2-HF: Nuclear repulsion	1015330.782529
FMO2-HF: Total energy	-49091.757829
FMO2-MP2: Total energy	-49235.332022

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:SER)

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

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.
103.115	98.241	10.868	-1.358	-4.637	-0.042

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.787 / q_NPA : 0.884

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	ARG	1	0.948	0.978	2.137	37.264	32.189	10.869	-1.295	-4.500	-0.042
4	A	6	PRO	0	0.124	0.071	4.126	2.256	2.346	0.000	-0.056	-0.035	0.000
8	A	10	ARG	1	0.774	0.879	4.341	33.189	33.300	-0.001	-0.007	-0.102	0.000
5	A	7	PHE	0	0.014	-0.006	7.797	-1.642	-1.642	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.842	0.923	9.838	17.770	17.770	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.006	-0.013	7.158	-2.855	-2.855	0.000	0.000	0.000	0.000
9	A	11	ARG	1	0.936	0.979	7.861	22.515	22.515	0.000	0.000	0.000	0.000
10	A	12	SER	0	0.031	0.004	11.630	0.280	0.280	0.000	0.000	0.000	0.000
11	A	13	PHE	0	0.088	0.028	14.320	-0.136	-0.136	0.000	0.000	0.000	0.000
12	A	14	ALA	0	0.065	0.036	17.368	0.565	0.565	0.000	0.000	0.000	0.000
13	A	15	ASP	-1	-0.845	-0.906	15.768	-16.414	-16.414	0.000	0.000	0.000	0.000
14	A	16	ARG	1	0.756	0.871	13.717	19.565	19.565	0.000	0.000	0.000	0.000
15	A	17	CYS	0	0.018	0.031	17.769	0.549	0.549	0.000	0.000	0.000	0.000
16	A	18	LYS	1	0.885	0.951	19.604	14.738	14.738	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.789	-0.886	16.482	-16.904	-16.904	0.000	0.000	0.000	0.000
18	A	20	VAL	0	-0.001	-0.001	20.242	0.450	0.450	0.000	0.000	0.000	0.000
19	A	21	GLN	0	0.000	-0.012	22.446	0.574	0.574	0.000	0.000	0.000	0.000
20	A	22	GLN	0	0.008	0.003	22.804	-0.035	-0.035	0.000	0.000	0.000	0.000
21	A	23	ILE	0	-0.036	-0.020	20.942	0.266	0.266	0.000	0.000	0.000	0.000
22	A	24	ARG	1	0.886	0.940	24.953	11.017	11.017	0.000	0.000	0.000	0.000
23	A	25	ASP	-1	-0.913	-0.946	27.616	-9.555	-9.555	0.000	0.000	0.000	0.000
24	A	26	GLN	0	-0.030	-0.020	26.336	0.056	0.056	0.000	0.000	0.000	0.000
25	A	27	HIS	0	-0.068	-0.041	26.855	0.268	0.268	0.000	0.000	0.000	0.000
26	A	28	PRO	0	0.045	0.032	28.938	-0.211	-0.211	0.000	0.000	0.000	0.000
27	A	29	SER	0	-0.020	0.003	31.137	-0.161	-0.161	0.000	0.000	0.000	0.000
28	A	30	LYS	1	0.855	0.935	26.334	10.452	10.452	0.000	0.000	0.000	0.000
29	A	31	ILE	0	0.047	0.031	24.255	-0.034	-0.034	0.000	0.000	0.000	0.000
30	A	32	PRO	0	-0.031	0.003	21.277	-0.305	-0.305	0.000	0.000	0.000	0.000
31	A	33	VAL	0	0.015	-0.007	19.327	-0.195	-0.195	0.000	0.000	0.000	0.000
32	A	34	ILE	0	-0.045	-0.017	13.643	-0.621	-0.621	0.000	0.000	0.000	0.000
33	A	35	ILE	0	0.004	0.000	15.558	0.321	0.321	0.000	0.000	0.000	0.000
34	A	36	GLU	-1	-0.813	-0.916	9.864	-28.818	-28.818	0.000	0.000	0.000	0.000
35	A	37	ARG	1	0.880	0.951	9.591	28.099	28.099	0.000	0.000	0.000	0.000
36	A	38	TYR	0	0.073	0.044	11.742	-1.492	-1.492	0.000	0.000	0.000	0.000
37	A	39	LYS	1	0.936	0.956	10.290	21.768	21.768	0.000	0.000	0.000	0.000
38	A	40	GLY	0	-0.007	-0.012	10.837	0.772	0.772	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.741	-0.816	11.715	-17.952	-17.952	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.870	0.908	7.132	34.049	34.049	0.000	0.000	0.000	0.000
41	A	43	GLN	0	0.038	0.044	13.485	-0.200	-0.200	0.000	0.000	0.000	0.000
42	A	44	LEU	0	0.002	0.014	16.707	0.854	0.854	0.000	0.000	0.000	0.000
43	A	45	PRO	0	0.023	0.024	15.269	-1.879	-1.879	0.000	0.000	0.000	0.000
44	A	46	VAL	0	-0.002	0.003	10.388	-0.575	-0.575	0.000	0.000	0.000	0.000
45	A	47	LEU	0	0.036	0.017	13.512	1.600	1.600	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.927	-0.962	13.580	-18.528	-18.528	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.890	0.935	14.367	15.845	15.845	0.000	0.000	0.000	0.000
48	A	50	THR	0	0.018	0.011	11.221	0.171	0.171	0.000	0.000	0.000	0.000
49	A	51	LYS	1	0.793	0.895	13.757	18.035	18.035	0.000	0.000	0.000	0.000
50	A	52	PHE	0	-0.018	-0.010	16.875	0.649	0.649	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.031	0.023	20.540	0.014	0.014	0.000	0.000	0.000	0.000
52	A	54	VAL	0	-0.014	-0.004	23.405	0.326	0.326	0.000	0.000	0.000	0.000
53	A	55	PRO	0	-0.020	-0.023	26.050	0.104	0.104	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.828	-0.929	29.857	-9.597	-9.597	0.000	0.000	0.000	0.000
55	A	57	HIS	0	0.012	0.010	31.026	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	58	VAL	0	-0.052	-0.009	29.392	0.205	0.205	0.000	0.000	0.000	0.000
57	A	59	ASN	0	0.070	0.031	31.381	-0.149	-0.149	0.000	0.000	0.000	0.000
58	A	60	MET	0	0.033	0.022	24.797	-0.377	-0.377	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.019	-0.037	27.991	-0.341	-0.341	0.000	0.000	0.000	0.000
60	A	62	GLU	-1	-0.835	-0.892	29.948	-9.632	-9.632	0.000	0.000	0.000	0.000
61	A	63	LEU	0	0.009	0.010	22.829	-0.230	-0.230	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.026	0.009	24.882	-0.496	-0.496	0.000	0.000	0.000	0.000
63	A	65	LYS	1	0.874	0.924	25.758	9.303	9.303	0.000	0.000	0.000	0.000
64	A	66	ILE	0	-0.062	-0.029	23.697	-0.130	-0.130	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.008	-0.001	19.716	-0.278	-0.278	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.865	0.927	22.142	11.203	11.203	0.000	0.000	0.000	0.000
67	A	69	ARG	1	0.946	0.974	24.379	10.711	10.711	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.890	0.945	20.422	13.391	13.391	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.004	-0.007	17.365	-0.449	-0.449	0.000	0.000	0.000	0.000
70	A	72	GLN	0	-0.055	-0.019	20.807	0.290	0.290	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.011	0.019	21.361	0.184	0.184	0.000	0.000	0.000	0.000
72	A	74	ASN	0	0.064	0.052	25.078	0.803	0.803	0.000	0.000	0.000	0.000
73	A	75	PRO	0	-0.006	-0.032	28.467	-0.194	-0.194	0.000	0.000	0.000	0.000
74	A	76	THR	0	-0.035	-0.026	29.933	0.018	0.018	0.000	0.000	0.000	0.000
75	A	77	GLN	0	0.045	0.043	23.210	0.174	0.174	0.000	0.000	0.000	0.000
76	A	78	ALA	0	0.035	0.026	26.849	0.059	0.059	0.000	0.000	0.000	0.000
77	A	79	PHE	0	-0.050	-0.041	21.102	-0.442	-0.442	0.000	0.000	0.000	0.000
78	A	80	PHE	0	0.008	0.018	21.677	0.578	0.578	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.036	-0.031	19.699	-0.876	-0.876	0.000	0.000	0.000	0.000
80	A	82	LEU	0	-0.014	0.008	19.618	0.640	0.640	0.000	0.000	0.000	0.000
81	A	83	VAL	0	0.039	0.015	19.645	-0.825	-0.825	0.000	0.000	0.000	0.000
82	A	84	ASN	0	-0.030	-0.023	18.236	-0.539	-0.539	0.000	0.000	0.000	0.000
83	A	85	GLN	0	-0.040	-0.023	14.880	-1.794	-1.794	0.000	0.000	0.000	0.000
84	A	86	HIS	0	0.026	-0.011	17.614	-0.798	-0.798	0.000	0.000	0.000	0.000
85	A	87	SER	0	0.027	0.026	20.493	0.663	0.663	0.000	0.000	0.000	0.000
86	A	88	MET	0	0.016	0.009	23.586	-0.306	-0.306	0.000	0.000	0.000	0.000
87	A	89	VAL	0	0.028	0.014	25.614	0.284	0.284	0.000	0.000	0.000	0.000
88	A	90	SER	0	0.007	0.014	27.900	0.003	0.003	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.060	0.022	29.443	-0.068	-0.068	0.000	0.000	0.000	0.000
90	A	92	SER	0	-0.026	-0.023	31.266	-0.110	-0.110	0.000	0.000	0.000	0.000
91	A	93	THR	0	-0.003	-0.002	30.768	0.313	0.313	0.000	0.000	0.000	0.000
92	A	94	PRO	0	0.039	0.024	31.350	-0.339	-0.339	0.000	0.000	0.000	0.000
93	A	95	ILE	0	-0.036	-0.024	24.980	-0.269	-0.269	0.000	0.000	0.000	0.000
94	A	96	ALA	0	0.020	0.010	28.296	-0.323	-0.323	0.000	0.000	0.000	0.000
95	A	97	ASP	-1	-0.846	-0.924	30.377	-9.259	-9.259	0.000	0.000	0.000	0.000
96	A	98	ILE	0	0.001	-0.014	25.491	-0.200	-0.200	0.000	0.000	0.000	0.000
97	A	99	TYR	0	-0.092	-0.055	23.969	-0.244	-0.244	0.000	0.000	0.000	0.000
98	A	100	GLU	-1	-0.829	-0.926	26.892	-10.434	-10.434	0.000	0.000	0.000	0.000
99	A	101	GLN	0	-0.084	-0.020	28.828	0.311	0.311	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.907	-0.965	23.812	-11.990	-11.990	0.000	0.000	0.000	0.000
101	A	103	LYS	1	0.742	0.876	22.630	10.026	10.026	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.841	-0.925	18.585	-15.970	-15.970	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.907	-0.954	21.354	-12.198	-12.198	0.000	0.000	0.000	0.000
104	A	106	ASP	-1	-0.781	-0.872	17.259	-16.706	-16.706	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.054	0.026	20.849	0.137	0.137	0.000	0.000	0.000	0.000
106	A	108	PHE	0	-0.034	-0.020	17.416	0.160	0.160	0.000	0.000	0.000	0.000
107	A	109	LEU	0	0.027	0.027	20.447	0.076	0.076	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.070	-0.070	13.672	-1.428	-1.428	0.000	0.000	0.000	0.000
109	A	111	MET	0	-0.001	0.008	16.980	0.878	0.878	0.000	0.000	0.000	0.000
110	A	112	VAL	0	-0.021	-0.001	13.760	-1.449	-1.449	0.000	0.000	0.000	0.000
111	A	113	TYR	0	-0.036	-0.044	14.561	0.791	0.791	0.000	0.000	0.000	0.000
112	A	114	ALA	0	-0.011	-0.016	16.170	-1.447	-1.447	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.023	-0.037	18.491	1.014	1.014	0.000	0.000	0.000	0.000
114	A	116	GLN	0	0.000	-0.016	20.762	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.812	-0.910	21.423	-13.598	-13.598	0.000	0.000	0.000	0.000
116	A	118	THR	0	-0.118	-0.073	17.609	-0.301	-0.301	0.000	0.000	0.000	0.000
117	A	119	PHE	0	-0.086	-0.054	19.908	-0.337	-0.337	0.000	0.000	0.000	0.000
118	A	120	GLY	0	-0.028	0.000	22.984	0.464	0.464	0.000	0.000	0.000	0.000
119	A	121	PHE	-1	-0.886	-0.927	25.292	-11.281	-11.281	0.000	0.000	0.000	0.000

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