FMO DATABASE

FMODB ID: QLK5Y

Calculation Name: 2FEK-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FEK

Chain ID: A

ChEMBL ID:

UniProt ID: P0AAB2

Base Structure: SolutionNMR

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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1467636.602044
FMO2-HF: Nuclear repulsion	1407307.549498
FMO2-HF: Total energy	-60329.052547
FMO2-MP2: Total energy	-60499.027585

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:MET)

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

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.
-66.839	-56.51	7.298	-5.837	-11.79	-0.05

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.875 / q_NPA : 0.948

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	ASN	0	-0.012	-0.019	2.759	9.783	12.834	0.239	-0.980	-2.311	0.000
4	A	4	ASN	0	0.012	0.012	3.816	2.703	3.006	0.010	-0.031	-0.282	0.000
27	A	27	HIS	1	0.848	0.914	4.132	31.602	32.043	0.008	-0.077	-0.372	0.000
29	A	29	GLU	-1	-0.860	-0.905	4.340	-30.256	-30.099	-0.001	-0.009	-0.148	0.000
30	A	30	LEU	0	-0.007	0.018	3.029	-3.378	-2.904	0.132	-0.089	-0.517	0.000
31	A	31	LYS	1	0.933	0.979	5.297	24.561	24.603	-0.001	0.000	-0.041	0.000
142	A	142	LEU	0	-0.051	-0.030	2.291	-3.903	-3.814	3.324	-0.624	-2.789	-0.002
143	A	143	ASN	0	-0.058	-0.021	2.975	-8.370	-6.222	1.315	-1.557	-1.905	-0.020
144	A	144	ALA	0	0.011	0.017	5.324	0.192	0.241	-0.001	-0.007	-0.040	0.000
146	A	146	GLN	0	-0.109	-0.061	2.744	-28.379	-25.024	2.270	-2.382	-3.243	-0.027
147	A	147	VAL	-1	-0.958	-0.963	3.532	-43.399	-43.179	0.003	-0.081	-0.142	-0.001
5	A	5	ILE	0	0.012	0.002	5.994	0.060	0.060	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.017	-0.001	9.270	1.651	1.651	0.000	0.000	0.000	0.000
7	A	7	VAL	0	0.001	-0.005	12.295	0.146	0.146	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.006	-0.001	14.700	1.027	1.027	0.000	0.000	0.000	0.000
9	A	9	CYS	0	-0.057	0.000	18.463	0.214	0.214	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.059	0.027	21.726	0.061	0.061	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.052	0.030	25.460	-0.050	-0.050	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.029	0.005	20.438	0.105	0.105	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.014	0.000	21.961	-0.414	-0.414	0.000	0.000	0.000	0.000
14	A	14	CYS	0	-0.031	0.017	23.594	-0.127	-0.127	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.808	0.857	20.086	11.923	11.923	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.027	0.009	17.437	-0.405	-0.405	0.000	0.000	0.000	0.000
17	A	17	PRO	0	0.035	0.025	16.351	-0.847	-0.847	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.007	-0.022	16.873	-0.207	-0.207	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.017	0.001	14.071	-0.329	-0.329	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.766	-0.836	12.349	-16.995	-16.995	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.802	0.874	11.935	13.847	13.847	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.015	-0.008	13.213	-0.176	-0.176	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.001	-0.007	6.791	-0.444	-0.444	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.002	-0.003	8.223	-0.158	-0.158	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.802	0.907	9.921	14.005	14.005	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.068	-0.063	9.036	0.714	0.714	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.045	0.028	6.336	-0.424	-0.424	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.001	-0.002	7.898	-0.332	-0.332	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.871	-0.909	9.284	-15.934	-15.934	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.048	-0.057	13.064	0.055	0.055	0.000	0.000	0.000	0.000
35	A	35	ALA	0	0.028	0.009	16.270	0.522	0.522	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.028	-0.017	19.331	-0.041	-0.041	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.008	-0.001	22.281	0.054	0.054	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.010	0.021	24.484	0.311	0.311	0.000	0.000	0.000	0.000
39	A	39	ALA	0	-0.037	-0.003	24.245	0.222	0.222	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.020	-0.009	26.196	0.385	0.385	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.022	-0.031	25.958	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.019	0.011	26.380	0.371	0.371	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.921	0.975	27.820	9.350	9.350	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.070	0.044	25.206	-0.388	-0.388	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.002	-0.007	22.286	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.767	-0.851	24.319	-9.372	-9.372	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.074	0.030	26.420	-0.196	-0.196	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.060	-0.025	28.544	0.183	0.183	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.000	-0.006	22.982	-0.070	-0.070	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.038	0.012	23.737	-0.277	-0.277	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.060	-0.032	24.990	0.082	0.082	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.007	-0.009	23.370	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.010	-0.003	20.838	-0.252	-0.252	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.035	0.029	22.253	-0.160	-0.160	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.860	-0.925	24.779	-9.395	-9.395	0.000	0.000	0.000	0.000
56	A	56	HIS	1	0.855	0.937	20.875	11.321	11.321	0.000	0.000	0.000	0.000
57	A	57	GLN	0	0.009	0.006	20.783	-0.710	-0.710	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.029	-0.008	15.660	-0.388	-0.388	0.000	0.000	0.000	0.000
59	A	59	SER	0	0.029	0.010	19.057	0.613	0.613	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.043	-0.021	18.813	-0.542	-0.542	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.874	-0.939	20.469	-10.817	-10.817	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.028	0.014	20.394	-0.569	-0.569	0.000	0.000	0.000	0.000
63	A	63	HIS	0	-0.034	-0.004	18.783	0.142	0.142	0.000	0.000	0.000	0.000
64	A	64	CYS	0	0.005	0.002	20.971	0.768	0.768	0.000	0.000	0.000	0.000
65	A	65	ALA	0	-0.045	-0.002	21.608	-0.545	-0.545	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.831	0.877	16.879	15.323	15.323	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.007	-0.009	22.181	-0.124	-0.124	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.004	0.006	18.323	-0.206	-0.206	0.000	0.000	0.000	0.000
69	A	69	SER	0	0.053	0.009	21.623	0.542	0.542	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.933	0.941	21.176	12.652	12.652	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.962	0.971	20.486	12.344	12.344	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.009	0.006	18.309	-0.532	-0.532	0.000	0.000	0.000	0.000
73	A	73	CYS	0	-0.035	-0.017	16.568	-0.903	-0.903	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.884	0.917	15.612	13.903	13.903	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.046	-0.001	14.108	-0.018	-0.018	0.000	0.000	0.000	0.000
76	A	76	TYR	0	-0.045	-0.030	10.646	-0.186	-0.186	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.841	-0.908	6.270	-40.003	-40.003	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.027	-0.002	8.079	-0.243	-0.243	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.019	-0.008	10.175	1.364	1.364	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.032	0.020	10.479	0.337	0.337	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.008	-0.026	14.111	1.399	1.399	0.000	0.000	0.000	0.000
82	A	82	MET	0	0.002	-0.001	16.504	-0.297	-0.297	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.748	-0.831	19.470	-11.258	-11.258	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.970	0.982	21.749	12.460	12.460	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.855	0.900	22.947	11.007	11.007	0.000	0.000	0.000	0.000
86	A	86	HIS	0	-0.042	-0.038	21.819	0.386	0.386	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.076	0.029	18.352	-0.024	-0.024	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.882	-0.923	20.907	-12.503	-12.503	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.907	0.948	23.920	11.254	11.254	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.002	-0.007	18.645	0.052	0.052	0.000	0.000	0.000	0.000
91	A	91	CYS	0	-0.058	-0.023	19.814	-0.628	-0.628	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.913	-0.952	21.179	-11.427	-11.427	0.000	0.000	0.000	0.000
93	A	93	MET	0	-0.084	-0.040	23.004	0.190	0.190	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.031	-0.032	19.185	0.063	0.063	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.062	0.052	19.357	-0.887	-0.887	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.776	-0.852	17.997	-15.091	-15.091	0.000	0.000	0.000	0.000
97	A	97	MET	0	-0.024	-0.011	12.120	-0.939	-0.939	0.000	0.000	0.000	0.000
98	A	98	ARG	1	0.938	0.961	15.251	14.525	14.525	0.000	0.000	0.000	0.000
99	A	99	GLY	0	-0.007	-0.003	14.523	0.167	0.167	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.850	0.918	9.193	28.738	28.738	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.003	0.010	12.389	-0.609	-0.609	0.000	0.000	0.000	0.000
102	A	102	MET	0	0.002	0.010	10.434	0.592	0.592	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.011	-0.006	15.150	0.104	0.104	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.014	-0.015	12.198	-0.592	-0.592	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.078	0.036	14.980	-0.592	-0.592	0.000	0.000	0.000	0.000
106	A	106	HIS	1	0.807	0.896	13.153	20.457	20.457	0.000	0.000	0.000	0.000
107	A	107	TRP	0	0.033	-0.005	9.938	0.274	0.274	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.838	-0.897	16.149	-13.141	-13.141	0.000	0.000	0.000	0.000
109	A	109	ASN	0	0.025	0.012	19.493	0.369	0.369	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.836	-0.882	18.272	-15.899	-15.899	0.000	0.000	0.000	0.000
111	A	111	CYS	0	-0.044	-0.012	20.862	0.744	0.744	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.873	-0.945	20.862	-12.807	-12.807	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.029	-0.011	18.757	0.461	0.461	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.038	0.008	23.233	-0.028	-0.028	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.761	-0.889	24.755	-11.637	-11.637	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.030	-0.007	25.137	0.347	0.347	0.000	0.000	0.000	0.000
117	A	117	TYR	0	-0.002	-0.018	27.935	0.482	0.482	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.841	0.897	29.692	9.165	9.165	0.000	0.000	0.000	0.000
119	A	119	LYS	1	0.935	0.980	31.358	9.078	9.078	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.088	0.028	32.234	-0.101	-0.101	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.916	0.946	29.389	8.766	8.766	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.874	-0.925	29.166	-8.796	-8.796	0.000	0.000	0.000	0.000
123	A	123	THR	0	-0.020	-0.011	28.396	-0.186	-0.186	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.014	0.000	25.505	-0.417	-0.417	0.000	0.000	0.000	0.000
125	A	125	ALA	0	0.044	0.022	24.640	-0.473	-0.473	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.013	0.025	24.613	-0.365	-0.365	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.020	-0.021	22.904	-0.377	-0.377	0.000	0.000	0.000	0.000
128	A	128	TYR	0	0.024	0.014	19.056	-0.632	-0.632	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.007	-0.020	19.736	-0.544	-0.544	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.019	-0.006	19.923	-0.362	-0.362	0.000	0.000	0.000	0.000
131	A	131	LEU	0	-0.030	-0.022	17.094	-0.690	-0.690	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.790	-0.845	15.472	-15.819	-15.819	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.859	0.913	15.017	12.371	12.371	0.000	0.000	0.000	0.000
134	A	134	SER	0	0.002	-0.005	14.555	-0.779	-0.779	0.000	0.000	0.000	0.000
135	A	135	ALA	0	-0.010	-0.001	11.397	-1.343	-1.343	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.873	0.911	10.039	13.689	13.689	0.000	0.000	0.000	0.000
137	A	137	GLN	0	-0.044	-0.015	10.479	-0.702	-0.702	0.000	0.000	0.000	0.000
138	A	138	TRP	0	0.004	-0.006	8.229	-1.953	-1.953	0.000	0.000	0.000	0.000
139	A	139	ALA	0	-0.006	0.002	5.906	-2.942	-2.942	0.000	0.000	0.000	0.000
140	A	140	GLN	0	0.006	-0.004	5.832	-3.446	-3.446	0.000	0.000	0.000	0.000
141	A	141	ALA	0	-0.016	-0.009	7.573	-1.506	-1.506	0.000	0.000	0.000	0.000
145	A	145	GLU	-1	-0.929	-0.971	5.510	-37.118	-37.118	0.000	0.000	0.000	0.000

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