FMODB ID: KQLR3

Calculation Name: 1EF4-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EF4

Chain ID: A

ChEMBL ID:

UniProt ID: O26147

Base Structure: SolutionNMR

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	55
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

FMO2-HF: Electronic energy	-304075.690356
FMO2-HF: Nuclear repulsion	280354.233779
FMO2-HF: Total energy	-23721.456578
FMO2-MP2: Total energy	-23786.358994

Snapshot

Snapshot

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	PRO	0	0.070	0.032	2.571	-3.042	-0.884	1.593	-1.427	-2.324	-0.014
4	A	4	VAL	0	0.024	0.014	4.273	2.903	3.029	-0.001	0.005	-0.130	0.000
6	A	6	CYS	0	-0.002	0.000	4.058	-4.341	-4.190	0.002	-0.035	-0.117	0.000
7	A	7	LEU	0	0.030	0.015	2.165	1.989	3.094	1.873	-0.802	-2.176	0.001
8	A	8	SER	0	0.046	-0.026	2.481	-13.793	-11.160	0.732	-1.213	-2.153	-0.009
9	A	9	CYS	0	-0.105	-0.045	4.214	4.715	4.820	0.000	-0.014	-0.091	0.000
12	A	12	PRO	0	0.022	0.028	4.117	-3.948	-3.790	-0.001	-0.010	-0.147	0.000
13	A	13	VAL	0	0.087	0.046	2.368	0.976	1.371	2.229	-0.637	-1.987	-0.005
14	A	14	SER	0	-0.025	-0.007	1.852	-25.039	-26.242	10.310	-4.412	-4.696	-0.051
15	A	15	ALA	0	0.039	0.025	4.025	3.253	3.820	0.003	-0.359	-0.211	-0.002
17	A	17	PHE	0	0.005	-0.010	2.934	-3.103	-1.340	0.204	-0.919	-1.049	-0.009
48	A	48	LEU	0	-0.012	-0.006	4.753	-0.829	-0.755	-0.001	-0.003	-0.070	0.000
5	A	5	ARG	1	0.946	0.968	5.692	28.503	28.503	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.025	0.031	5.837	2.515	2.515	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.924	0.958	6.826	25.282	25.282	0.000	0.000	0.000	0.000
16	A	16	TYR	0	0.085	0.043	7.312	1.680	1.680	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.028	-0.008	7.249	3.335	3.335	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.875	-0.925	10.566	-18.628	-18.628	0.000	0.000	0.000	0.000
20	A	20	TYR	0	-0.015	-0.020	9.538	1.402	1.402	0.000	0.000	0.000	0.000
21	A	21	GLN	0	0.014	0.003	10.668	1.173	1.173	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.968	0.984	12.480	17.647	17.647	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.825	0.907	14.936	17.890	17.890	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.029	-0.020	14.211	1.004	1.004	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.058	-0.015	16.457	0.637	0.637	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.926	-0.960	18.024	-13.832	-13.832	0.000	0.000	0.000	0.000
27	A	27	GLY	0	-0.039	-0.011	19.778	0.779	0.779	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.870	-0.936	18.705	-14.767	-14.767	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.887	-0.948	18.483	-15.059	-15.059	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.035	0.009	14.345	-0.732	-0.732	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.872	0.912	14.493	14.008	14.008	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.855	-0.906	16.265	-14.915	-14.915	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.055	0.039	12.017	-0.639	-0.639	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.098	-0.071	9.880	-1.765	-1.765	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.964	-0.973	12.536	-17.392	-17.392	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.827	-0.915	13.874	-18.327	-18.327	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.100	-0.056	7.242	-1.627	-1.627	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.006	0.026	9.155	-2.337	-2.337	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.055	-0.030	6.547	-1.170	-1.170	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.947	0.974	8.926	20.146	20.146	0.000	0.000	0.000	0.000
41	A	41	ARG	1	1.002	0.973	9.638	16.808	16.808	0.000	0.000	0.000	0.000
42	A	42	TYR	0	0.073	0.034	11.254	-1.443	-1.443	0.000	0.000	0.000	0.000
43	A	43	CYS	0	-0.036	-0.016	9.615	-0.063	-0.063	0.000	0.000	0.000	0.000
44	A	44	CYS	0	0.019	0.007	6.969	-0.900	-0.900	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.923	0.963	8.537	19.414	19.414	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.972	0.987	10.736	18.531	18.531	0.000	0.000	0.000	0.000
47	A	47	MET	0	-0.043	-0.010	7.261	1.319	1.319	0.000	0.000	0.000	0.000
49	A	49	ILE	0	0.011	-0.013	8.912	0.395	0.395	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.058	-0.021	12.337	1.509	1.509	0.000	0.000	0.000	0.000
51	A	51	HIS	0	-0.054	-0.018	9.634	-0.075	-0.075	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.027	-0.021	5.845	-0.973	-0.973	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.918	-0.952	7.009	-28.187	-28.187	0.000	0.000	0.000	0.000
54	A	54	THR	0	-0.088	-0.049	5.645	-6.199	-6.199	0.000	0.000	0.000	0.000
55	A	55	TRP	-1	-0.940	-0.945	7.305	-32.542	-32.542	0.000	0.000	0.000	0.000