FMO DATABASE

FMODB ID: 4QM1N

Calculation Name: 2KFL-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KFL

Chain ID: A

ChEMBL ID:

UniProt ID: Q58YZ3

Base Structure: SolutionNMR

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	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-939947.785153
FMO2-HF: Nuclear repulsion	892306.037249
FMO2-HF: Total energy	-47641.747904
FMO2-MP2: Total energy	-47775.810778

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:119:GLY)

Summations of interaction energy for fragment #1(A:119: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.
-27.283	-25.176	0.114	-0.906	-1.314	-0.004

Interaction energy analysis for fragmet #1(A:119:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.895 / q_NPA : 0.937

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	121	VAL	0	0.043	0.013	3.864	1.082	2.165	-0.014	-0.510	-0.558	-0.001
67	A	185	LYS	1	0.810	0.923	2.969	44.530	45.141	0.128	-0.223	-0.516	-0.002
68	A	186	GLN	0	0.005	-0.006	4.940	0.881	0.876	-0.001	-0.001	0.007	0.000
70	A	188	THR	0	0.015	-0.026	3.686	-5.583	-5.232	0.002	-0.157	-0.196	-0.001
71	A	189	THR	0	-0.032	0.000	4.085	-7.652	-7.585	-0.001	-0.015	-0.051	0.000
4	A	122	VAL	0	0.051	0.028	7.285	0.143	0.143	0.000	0.000	0.000	0.000
5	A	123	GLY	0	0.022	0.023	10.859	1.556	1.556	0.000	0.000	0.000	0.000
6	A	124	GLY	0	0.010	-0.003	10.549	0.069	0.069	0.000	0.000	0.000	0.000
7	A	125	LEU	0	-0.021	-0.013	7.633	-0.724	-0.724	0.000	0.000	0.000	0.000
8	A	126	GLY	0	0.037	0.029	11.189	1.887	1.887	0.000	0.000	0.000	0.000
9	A	127	GLY	0	-0.003	-0.002	14.054	1.189	1.189	0.000	0.000	0.000	0.000
10	A	128	TYR	0	-0.087	-0.064	11.754	0.811	0.811	0.000	0.000	0.000	0.000
11	A	129	MET	0	0.000	0.017	15.140	0.361	0.361	0.000	0.000	0.000	0.000
12	A	130	LEU	0	0.016	-0.021	15.061	-0.783	-0.783	0.000	0.000	0.000	0.000
13	A	131	GLY	0	-0.021	-0.007	17.433	0.890	0.890	0.000	0.000	0.000	0.000
14	A	132	SER	0	-0.044	-0.017	19.457	1.046	1.046	0.000	0.000	0.000	0.000
15	A	133	ALA	0	-0.003	-0.013	20.383	-0.685	-0.685	0.000	0.000	0.000	0.000
16	A	134	MET	0	-0.003	0.010	20.086	0.351	0.351	0.000	0.000	0.000	0.000
17	A	135	SER	0	0.005	-0.004	23.063	0.092	0.092	0.000	0.000	0.000	0.000
18	A	136	ARG	1	0.845	0.902	18.530	15.354	15.354	0.000	0.000	0.000	0.000
19	A	137	PRO	0	-0.010	0.015	20.644	0.577	0.577	0.000	0.000	0.000	0.000
20	A	138	VAL	0	0.030	0.009	22.586	-0.309	-0.309	0.000	0.000	0.000	0.000
21	A	139	MET	0	-0.045	-0.010	18.191	-0.806	-0.806	0.000	0.000	0.000	0.000
22	A	140	HIS	0	-0.009	-0.012	21.655	0.337	0.337	0.000	0.000	0.000	0.000
23	A	141	PHE	0	-0.025	-0.026	16.767	-0.449	-0.449	0.000	0.000	0.000	0.000
24	A	142	GLY	0	-0.006	0.010	22.138	0.181	0.181	0.000	0.000	0.000	0.000
25	A	143	ASN	0	-0.086	-0.042	21.755	0.850	0.850	0.000	0.000	0.000	0.000
26	A	144	GLU	-1	-0.861	-0.930	25.225	-11.273	-11.273	0.000	0.000	0.000	0.000
27	A	145	TYR	0	-0.017	-0.019	17.473	-0.367	-0.367	0.000	0.000	0.000	0.000
28	A	146	GLU	-1	-0.838	-0.918	17.884	-16.725	-16.725	0.000	0.000	0.000	0.000
29	A	147	ASP	-1	-0.714	-0.855	20.214	-13.598	-13.598	0.000	0.000	0.000	0.000
30	A	148	ARG	1	0.902	0.955	21.203	13.437	13.437	0.000	0.000	0.000	0.000
31	A	149	TYR	0	-0.023	-0.016	14.622	0.230	0.230	0.000	0.000	0.000	0.000
32	A	150	TYR	0	0.022	-0.003	17.740	-0.624	-0.624	0.000	0.000	0.000	0.000
33	A	151	ARG	1	0.829	0.897	19.656	12.528	12.528	0.000	0.000	0.000	0.000
34	A	152	GLU	-1	-0.885	-0.922	21.653	-12.656	-12.656	0.000	0.000	0.000	0.000
35	A	153	ASN	0	-0.029	-0.017	17.230	-0.158	-0.158	0.000	0.000	0.000	0.000
36	A	154	GLN	0	-0.055	-0.029	18.373	-0.639	-0.639	0.000	0.000	0.000	0.000
37	A	155	TYR	0	-0.012	-0.011	20.065	-0.137	-0.137	0.000	0.000	0.000	0.000
38	A	156	ARG	1	0.825	0.890	14.147	19.797	19.797	0.000	0.000	0.000	0.000
39	A	157	TYR	0	-0.058	-0.052	13.503	-0.801	-0.801	0.000	0.000	0.000	0.000
40	A	158	PRO	0	0.008	0.006	12.970	1.019	1.019	0.000	0.000	0.000	0.000
41	A	159	ASN	0	-0.012	-0.003	16.104	-0.191	-0.191	0.000	0.000	0.000	0.000
42	A	160	GLN	0	0.025	0.012	16.359	0.593	0.593	0.000	0.000	0.000	0.000
43	A	161	VAL	0	0.025	0.001	14.162	-1.253	-1.253	0.000	0.000	0.000	0.000
44	A	162	MET	0	-0.057	-0.023	12.084	1.228	1.228	0.000	0.000	0.000	0.000
45	A	163	TYR	0	0.016	-0.009	13.144	-1.298	-1.298	0.000	0.000	0.000	0.000
46	A	164	ARG	1	0.964	0.980	14.663	19.025	19.025	0.000	0.000	0.000	0.000
47	A	165	PRO	0	0.053	0.040	16.846	0.243	0.243	0.000	0.000	0.000	0.000
48	A	166	ILE	0	-0.028	-0.037	20.663	-0.251	-0.251	0.000	0.000	0.000	0.000
49	A	167	ASP	-1	-0.890	-0.937	22.693	-13.072	-13.072	0.000	0.000	0.000	0.000
50	A	168	GLN	0	-0.072	-0.039	18.508	-0.680	-0.680	0.000	0.000	0.000	0.000
51	A	169	TYR	0	-0.079	-0.053	16.124	-0.763	-0.763	0.000	0.000	0.000	0.000
52	A	170	GLY	0	0.030	0.029	21.717	0.566	0.566	0.000	0.000	0.000	0.000
53	A	171	SER	0	-0.029	-0.021	20.659	0.250	0.250	0.000	0.000	0.000	0.000
54	A	172	GLN	0	0.073	0.034	20.942	-0.934	-0.934	0.000	0.000	0.000	0.000
55	A	173	ASN	0	0.010	-0.004	18.925	-0.995	-0.995	0.000	0.000	0.000	0.000
56	A	174	SER	0	0.024	0.010	16.634	-0.552	-0.552	0.000	0.000	0.000	0.000
57	A	175	PHE	0	0.036	0.040	15.645	-1.256	-1.256	0.000	0.000	0.000	0.000
58	A	176	VAL	0	-0.011	-0.012	15.172	-1.338	-1.338	0.000	0.000	0.000	0.000
59	A	177	HIS	0	0.002	-0.003	12.720	-1.799	-1.799	0.000	0.000	0.000	0.000
60	A	178	ASP	-1	-0.790	-0.874	10.717	-27.816	-27.816	0.000	0.000	0.000	0.000
61	A	179	CYS	0	-0.038	-0.005	10.462	-1.846	-1.846	0.000	0.000	0.000	0.000
62	A	180	VAL	0	-0.015	0.026	9.578	-1.573	-1.573	0.000	0.000	0.000	0.000
63	A	181	ASN	0	0.021	0.003	6.449	-6.192	-6.192	0.000	0.000	0.000	0.000
64	A	182	ILE	0	-0.045	-0.010	5.919	-8.350	-8.350	0.000	0.000	0.000	0.000
65	A	183	THR	0	0.019	0.000	8.141	-1.560	-1.560	0.000	0.000	0.000	0.000
66	A	184	VAL	0	0.020	0.007	4.816	-0.815	-0.815	0.000	0.000	0.000	0.000
69	A	187	HIS	1	0.874	0.941	7.925	29.202	29.202	0.000	0.000	0.000	0.000
72	A	190	THR	0	-0.036	-0.015	5.609	4.568	4.568	0.000	0.000	0.000	0.000
73	A	191	THR	0	-0.004	-0.007	9.397	2.058	2.058	0.000	0.000	0.000	0.000
74	A	192	THR	0	0.023	0.018	6.816	3.133	3.133	0.000	0.000	0.000	0.000
75	A	193	THR	0	-0.010	0.002	9.893	2.235	2.235	0.000	0.000	0.000	0.000
76	A	194	LYS	1	0.897	0.957	11.785	19.621	19.621	0.000	0.000	0.000	0.000
77	A	195	GLY	0	0.007	-0.002	13.588	1.621	1.621	0.000	0.000	0.000	0.000
78	A	196	GLU	-1	-0.828	-0.863	11.584	-21.293	-21.293	0.000	0.000	0.000	0.000
79	A	197	ASN	0	-0.065	-0.045	11.000	-1.494	-1.494	0.000	0.000	0.000	0.000
80	A	198	PHE	0	0.038	0.025	8.168	0.751	0.751	0.000	0.000	0.000	0.000
81	A	199	THR	0	0.046	0.020	8.693	-2.760	-2.760	0.000	0.000	0.000	0.000
82	A	200	GLU	-1	-0.844	-0.935	6.627	-38.451	-38.451	0.000	0.000	0.000	0.000
83	A	201	THR	0	0.003	-0.006	8.622	0.081	0.081	0.000	0.000	0.000	0.000
84	A	202	ASP	-1	-0.809	-0.885	10.810	-22.152	-22.152	0.000	0.000	0.000	0.000
85	A	203	ILE	0	-0.017	-0.008	5.834	-0.026	-0.026	0.000	0.000	0.000	0.000
86	A	204	LYS	1	0.873	0.937	8.910	30.982	30.982	0.000	0.000	0.000	0.000
87	A	205	ILE	0	0.023	0.029	11.915	1.384	1.384	0.000	0.000	0.000	0.000
88	A	206	MET	0	-0.016	-0.002	8.993	0.158	0.158	0.000	0.000	0.000	0.000
89	A	207	GLU	-1	-0.943	-1.002	7.736	-33.484	-33.484	0.000	0.000	0.000	0.000
90	A	208	ARG	1	0.981	0.999	11.282	21.130	21.130	0.000	0.000	0.000	0.000
91	A	209	VAL	0	0.025	0.006	15.126	0.989	0.989	0.000	0.000	0.000	0.000
92	A	210	VAL	0	-0.049	-0.036	11.240	0.733	0.733	0.000	0.000	0.000	0.000
93	A	211	GLU	-1	-0.875	-0.930	14.677	-17.207	-17.207	0.000	0.000	0.000	0.000
94	A	212	GLN	0	-0.008	-0.007	15.691	1.347	1.347	0.000	0.000	0.000	0.000
95	A	213	MET	0	-0.034	0.006	16.415	0.951	0.951	0.000	0.000	0.000	0.000
96	A	215	ILE	0	0.025	0.016	17.384	0.621	0.621	0.000	0.000	0.000	0.000
97	A	216	THR	0	-0.021	0.000	20.432	0.937	0.937	0.000	0.000	0.000	0.000
98	A	217	GLN	0	0.027	0.019	18.920	0.705	0.705	0.000	0.000	0.000	0.000
99	A	218	TYR	0	0.000	0.009	20.422	0.414	0.414	0.000	0.000	0.000	0.000
100	A	219	GLN	0	-0.051	-0.037	21.765	0.913	0.913	0.000	0.000	0.000	0.000
101	A	220	ASN	0	0.008	-0.007	23.213	0.800	0.800	0.000	0.000	0.000	0.000
102	A	221	GLU	-1	-0.861	-0.934	22.449	-13.149	-13.149	0.000	0.000	0.000	0.000
103	A	222	TYR	0	0.051	0.017	24.765	0.539	0.539	0.000	0.000	0.000	0.000
104	A	223	GLN	0	-0.019	-0.019	26.878	0.298	0.298	0.000	0.000	0.000	0.000
105	A	224	ALA	0	-0.042	-0.026	27.273	0.409	0.409	0.000	0.000	0.000	0.000
106	A	225	ALA	0	0.059	0.040	27.837	0.189	0.189	0.000	0.000	0.000	0.000
107	A	226	GLN	0	-0.008	-0.029	29.835	0.129	0.129	0.000	0.000	0.000	0.000
108	A	227	ARG	1	0.834	0.939	30.659	10.391	10.391	0.000	0.000	0.000	0.000
109	A	228	TYR	0	-0.079	-0.039	29.951	0.232	0.232	0.000	0.000	0.000	0.000
110	A	229	TYR	0	-0.079	-0.023	33.260	0.301	0.301	0.000	0.000	0.000	0.000
111	A	230	ASN	-1	-0.899	-0.935	30.551	-9.689	-9.689	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:119:GLY)