FMO DATABASE

FMODB ID: 3ZMQL

Calculation Name: 4F8K-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4F8K

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JIL4

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	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-808863.461379
FMO2-HF: Nuclear repulsion	766981.647243
FMO2-HF: Total energy	-41881.814136
FMO2-MP2: Total energy	-42004.84504

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:5:GLY)

Summations of interaction energy for fragment #1(A:5: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.
-169.675	-167.51	8.808	-5.603	-5.367	-0.057

Interaction energy analysis for fragmet #1(A:5:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.824 / q_NPA : 0.902

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	7	PRO	0	0.020	0.014	3.817	-0.961	-0.082	-0.008	-0.297	-0.574	0.000
83	A	87	LEU	0	0.000	0.010	4.033	-2.978	-2.879	-0.001	-0.040	-0.058	0.000
84	A	88	ASP	-1	-0.770	-0.846	2.939	-73.393	-71.102	0.173	-1.327	-1.137	-0.013
86	A	90	ASP	-1	-0.822	-0.879	5.084	-48.221	-48.180	-0.001	-0.003	-0.036	0.000
87	A	91	SER	0	-0.046	-0.067	1.926	-26.296	-27.712	8.644	-3.747	-3.480	-0.043
88	A	92	TYR	0	-0.044	-0.051	3.691	3.990	4.261	0.001	-0.189	-0.082	-0.001
4	A	8	ARG	1	0.798	0.856	5.952	36.136	36.136	0.000	0.000	0.000	0.000
5	A	9	GLU	-1	-0.834	-0.918	8.804	-17.418	-17.418	0.000	0.000	0.000	0.000
6	A	10	SER	0	-0.017	-0.014	12.528	-0.334	-0.334	0.000	0.000	0.000	0.000
7	A	11	LYS	1	0.817	0.907	14.235	17.629	17.629	0.000	0.000	0.000	0.000
8	A	12	LEU	0	0.010	0.016	16.581	0.274	0.274	0.000	0.000	0.000	0.000
9	A	13	SER	0	-0.036	-0.029	20.101	0.521	0.521	0.000	0.000	0.000	0.000
10	A	14	LYS	1	0.835	0.931	23.865	10.828	10.828	0.000	0.000	0.000	0.000
11	A	15	GLN	0	0.013	0.003	26.622	0.324	0.324	0.000	0.000	0.000	0.000
12	A	16	GLU	-1	-0.844	-0.923	30.242	-9.651	-9.651	0.000	0.000	0.000	0.000
13	A	17	GLY	0	-0.033	-0.019	32.930	0.098	0.098	0.000	0.000	0.000	0.000
14	A	18	GLN	0	-0.012	0.014	28.090	-0.279	-0.279	0.000	0.000	0.000	0.000
15	A	19	ASN	0	-0.039	-0.036	25.795	0.082	0.082	0.000	0.000	0.000	0.000
16	A	20	TYR	0	0.040	-0.022	21.320	-0.158	-0.158	0.000	0.000	0.000	0.000
17	A	21	GLY	0	0.028	0.019	21.523	-0.466	-0.466	0.000	0.000	0.000	0.000
18	A	22	PHE	0	-0.002	-0.002	17.979	-0.635	-0.635	0.000	0.000	0.000	0.000
19	A	23	PHE	0	-0.026	-0.003	20.043	0.765	0.765	0.000	0.000	0.000	0.000
20	A	24	LEU	0	0.034	0.022	17.598	-0.894	-0.894	0.000	0.000	0.000	0.000
21	A	25	ARG	1	0.840	0.912	18.913	15.600	15.600	0.000	0.000	0.000	0.000
22	A	26	ILE	0	0.071	0.046	18.969	-0.771	-0.771	0.000	0.000	0.000	0.000
23	A	27	GLU	-1	-0.787	-0.877	18.521	-16.123	-16.123	0.000	0.000	0.000	0.000
24	A	28	LYS	1	0.884	0.920	20.478	12.393	12.393	0.000	0.000	0.000	0.000
25	A	29	ASP	-1	-0.879	-0.935	21.002	-13.604	-13.604	0.000	0.000	0.000	0.000
26	A	30	THR	0	-0.040	-0.006	15.532	-0.807	-0.807	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.892	-0.932	14.177	-18.813	-18.813	0.000	0.000	0.000	0.000
28	A	32	GLY	0	0.060	0.024	14.173	-1.502	-1.502	0.000	0.000	0.000	0.000
29	A	33	HIS	0	-0.045	-0.027	15.254	0.678	0.678	0.000	0.000	0.000	0.000
30	A	34	LEU	0	-0.013	0.004	13.682	-1.159	-1.159	0.000	0.000	0.000	0.000
31	A	35	ILE	0	0.009	0.007	12.783	1.709	1.709	0.000	0.000	0.000	0.000
32	A	36	ARG	1	0.757	0.849	14.794	18.372	18.372	0.000	0.000	0.000	0.000
33	A	37	VAL	0	-0.038	-0.025	17.564	0.690	0.690	0.000	0.000	0.000	0.000
34	A	38	ILE	0	0.006	0.009	15.102	0.439	0.439	0.000	0.000	0.000	0.000
35	A	39	GLU	-1	-0.868	-0.921	18.814	-11.873	-11.873	0.000	0.000	0.000	0.000
36	A	40	GLU	-1	-0.906	-0.940	21.494	-12.490	-12.490	0.000	0.000	0.000	0.000
37	A	41	GLY	0	0.008	0.005	22.615	0.540	0.540	0.000	0.000	0.000	0.000
38	A	42	SER	0	-0.062	-0.037	20.875	0.141	0.141	0.000	0.000	0.000	0.000
39	A	43	PRO	0	-0.028	-0.030	21.210	-0.420	-0.420	0.000	0.000	0.000	0.000
40	A	44	ALA	0	0.016	0.012	17.471	-0.629	-0.629	0.000	0.000	0.000	0.000
41	A	45	GLU	-1	-0.857	-0.920	16.325	-15.499	-15.499	0.000	0.000	0.000	0.000
42	A	46	LYS	1	0.853	0.917	16.704	11.923	11.923	0.000	0.000	0.000	0.000
43	A	47	ALA	0	-0.020	0.006	16.286	-0.183	-0.183	0.000	0.000	0.000	0.000
44	A	48	GLY	0	0.003	0.015	12.780	-1.255	-1.255	0.000	0.000	0.000	0.000
45	A	49	LEU	0	-0.039	-0.017	11.264	-2.374	-2.374	0.000	0.000	0.000	0.000
46	A	50	LEU	0	-0.014	-0.014	7.917	0.762	0.762	0.000	0.000	0.000	0.000
47	A	51	ASP	-1	-0.838	-0.911	11.926	-18.446	-18.446	0.000	0.000	0.000	0.000
48	A	52	GLY	0	0.026	-0.003	11.988	-1.274	-1.274	0.000	0.000	0.000	0.000
49	A	53	ASP	-1	-0.750	-0.838	8.554	-33.479	-33.479	0.000	0.000	0.000	0.000
50	A	54	ARG	1	0.708	0.849	9.755	28.119	28.119	0.000	0.000	0.000	0.000
51	A	55	VAL	0	-0.013	-0.009	10.968	-1.721	-1.721	0.000	0.000	0.000	0.000
52	A	56	LEU	0	-0.009	0.000	9.207	0.464	0.464	0.000	0.000	0.000	0.000
53	A	57	ARG	1	0.851	0.892	13.603	20.859	20.859	0.000	0.000	0.000	0.000
54	A	58	ILE	0	0.019	0.023	16.060	-0.556	-0.556	0.000	0.000	0.000	0.000
55	A	59	ASN	0	-0.005	-0.024	18.922	0.164	0.164	0.000	0.000	0.000	0.000
56	A	60	GLY	0	0.033	0.026	18.603	0.567	0.567	0.000	0.000	0.000	0.000
57	A	61	VAL	0	-0.010	0.005	19.554	-0.279	-0.279	0.000	0.000	0.000	0.000
58	A	62	PHE	0	-0.004	-0.007	14.224	-0.382	-0.382	0.000	0.000	0.000	0.000
59	A	63	VAL	0	0.019	-0.002	16.892	0.907	0.907	0.000	0.000	0.000	0.000
60	A	64	ASP	-1	-0.790	-0.867	14.315	-20.868	-20.868	0.000	0.000	0.000	0.000
61	A	65	LYS	1	0.841	0.906	16.497	18.625	18.625	0.000	0.000	0.000	0.000
62	A	66	GLU	-1	-0.898	-0.931	20.105	-12.214	-12.214	0.000	0.000	0.000	0.000
63	A	67	GLU	-1	-0.893	-0.950	21.840	-13.065	-13.065	0.000	0.000	0.000	0.000
64	A	68	HIS	0	-0.036	-0.042	21.582	0.360	0.360	0.000	0.000	0.000	0.000
65	A	69	ALA	0	0.005	0.008	23.733	-0.053	-0.053	0.000	0.000	0.000	0.000
66	A	70	GLN	0	0.041	0.017	25.371	0.323	0.323	0.000	0.000	0.000	0.000
67	A	71	VAL	0	0.019	0.016	19.252	0.028	0.028	0.000	0.000	0.000	0.000
68	A	72	VAL	0	0.006	-0.008	22.577	-0.074	-0.074	0.000	0.000	0.000	0.000
69	A	73	GLU	-1	-0.912	-0.967	24.280	-10.485	-10.485	0.000	0.000	0.000	0.000
70	A	74	LEU	0	-0.047	-0.032	22.321	0.344	0.344	0.000	0.000	0.000	0.000
71	A	75	VAL	0	-0.003	0.005	21.163	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	76	ARG	1	0.882	0.955	23.888	11.736	11.736	0.000	0.000	0.000	0.000
73	A	77	LYS	1	0.928	0.959	27.548	11.466	11.466	0.000	0.000	0.000	0.000
74	A	78	SER	0	-0.002	0.008	24.183	0.005	0.005	0.000	0.000	0.000	0.000
75	A	79	GLY	0	0.008	0.011	26.207	0.091	0.091	0.000	0.000	0.000	0.000
76	A	80	ASN	0	-0.049	-0.040	27.131	-0.468	-0.468	0.000	0.000	0.000	0.000
77	A	81	SER	0	0.003	0.006	24.265	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	82	VAL	0	-0.001	0.021	19.845	0.193	0.193	0.000	0.000	0.000	0.000
79	A	83	THR	0	-0.021	-0.001	16.954	-0.474	-0.474	0.000	0.000	0.000	0.000
80	A	84	LEU	0	0.001	0.002	14.837	0.416	0.416	0.000	0.000	0.000	0.000
81	A	85	LEU	0	-0.006	0.011	10.959	-0.425	-0.425	0.000	0.000	0.000	0.000
82	A	86	VAL	0	0.019	-0.001	9.023	1.058	1.058	0.000	0.000	0.000	0.000
85	A	89	GLY	0	0.064	0.020	6.081	-2.591	-2.591	0.000	0.000	0.000	0.000
89	A	93	GLU	-1	-0.809	-0.894	7.186	-22.723	-22.723	0.000	0.000	0.000	0.000
90	A	94	LYS	1	0.784	0.861	5.372	48.419	48.419	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.003	0.004	6.568	2.794	2.794	0.000	0.000	0.000	0.000
92	A	96	VAL	0	0.021	0.013	7.944	3.055	3.055	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.867	0.941	10.597	22.943	22.943	0.000	0.000	0.000	0.000
94	A	98	ASN	0	-0.053	-0.039	8.619	3.870	3.870	0.000	0.000	0.000	0.000
95	A	99	GLN	0	-0.047	-0.015	11.692	0.866	0.866	0.000	0.000	0.000	0.000
96	A	100	VAL	0	-0.004	0.014	8.584	0.863	0.863	0.000	0.000	0.000	0.000
97	A	101	ASP	-1	-0.841	-0.927	11.819	-19.020	-19.020	0.000	0.000	0.000	0.000
98	A	102	LEU	0	0.006	-0.016	9.674	-1.485	-1.485	0.000	0.000	0.000	0.000
99	A	103	LYS	1	0.885	0.950	12.202	15.836	15.836	0.000	0.000	0.000	0.000
100	A	104	GLU	-1	-0.933	-0.956	14.035	-18.149	-18.149	0.000	0.000	0.000	0.000
101	A	105	LEU	0	-0.069	-0.015	7.593	-1.980	-1.980	0.000	0.000	0.000	0.000
102	A	106	ASP	-1	-0.845	-0.943	10.747	-20.739	-20.739	0.000	0.000	0.000	0.000
103	A	107	ILE	0	-0.038	-0.026	9.832	-3.009	-3.009	0.000	0.000	0.000	0.000
104	A	108	ALA	0	-0.058	-0.010	11.132	0.095	0.095	0.000	0.000	0.000	0.000
105	A	109	ALA	0	0.006	0.005	10.684	-1.063	-1.063	0.000	0.000	0.000	0.000
106	A	110	CYS	0	-0.044	-0.030	12.827	1.719	1.719	0.000	0.000	0.000	0.000
107	A	111	SER	0	-0.036	-0.030	14.241	-1.348	-1.348	0.000	0.000	0.000	0.000
108	A	112	LEU	0	-0.020	0.008	16.417	0.483	0.483	0.000	0.000	0.000	0.000
109	A	113	CYS	-1	-0.943	-0.966	18.170	-14.660	-14.660	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLY)