FMO DATABASE

FMODB ID: KV8M3

Calculation Name: 2KFP-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KFP

Chain ID: A

ChEMBL ID:

UniProt ID: Q880Y4

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	125
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1113684.189356
FMO2-HF: Nuclear repulsion	1062340.841625
FMO2-HF: Total energy	-51343.347731
FMO2-MP2: Total energy	-51494.980164

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.
-83.201	-72.649	19.628	-10.112	-20.067	-0.111

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 : 0.788 / q_NPA : 0.904

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

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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	ARG	1	0.989	0.993	3.098	29.978	32.448	0.092	-1.204	-1.358	-0.006
4	A	4	GLN	0	-0.008	-0.010	5.220	0.732	0.854	-0.001	-0.005	-0.116	0.000
5	A	5	GLN	0	0.009	-0.008	2.563	-4.799	-3.477	3.265	-1.081	-3.507	-0.009
6	A	6	PHE	0	0.008	0.008	3.387	-1.150	0.070	0.100	-0.337	-0.982	-0.003
7	A	7	ILE	0	0.042	0.022	3.927	3.368	3.531	0.004	-0.030	-0.136	0.000
9	A	9	TYR	0	-0.053	-0.032	4.683	1.415	1.567	-0.001	-0.005	-0.146	0.000
96	A	96	LEU	0	0.023	0.021	2.431	-10.623	-8.806	1.316	-0.852	-2.281	-0.006
97	A	97	ASN	0	-0.044	-0.023	1.817	-37.185	-36.736	8.700	-5.193	-3.956	-0.072
98	A	98	GLY	0	0.038	0.026	3.876	9.930	10.122	-0.001	-0.036	-0.155	0.000
99	A	99	PRO	0	-0.046	-0.036	4.002	-11.499	-11.259	0.000	-0.063	-0.177	0.000
100	A	100	LEU	0	-0.007	0.016	4.497	1.878	2.040	-0.001	-0.016	-0.146	0.000
101	A	101	GLY	0	0.040	0.015	3.086	-19.046	-17.195	0.050	-0.945	-0.956	-0.008
102	A	102	ALA	0	0.006	-0.017	2.573	1.259	1.361	3.401	-1.101	-2.401	0.003
103	A	103	LYS	1	0.987	0.991	3.697	27.688	26.104	0.026	1.850	-0.292	0.000
105	A	105	ILE	0	0.003	-0.004	2.337	-0.037	0.883	2.193	-0.672	-2.441	-0.006
106	A	106	HIS	0	-0.008	-0.019	2.659	3.211	4.165	0.485	-0.422	-1.017	-0.004
8	A	8	ASP	-1	-0.818	-0.906	6.852	-21.528	-21.528	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.022	0.010	6.509	1.886	1.886	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.013	-0.014	8.863	2.605	2.605	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.902	0.955	9.219	19.999	19.999	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.777	0.901	9.735	19.908	19.908	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.019	-0.005	9.745	0.609	0.609	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.933	-0.953	13.083	-14.366	-14.366	0.000	0.000	0.000	0.000
16	A	16	THR	0	-0.004	0.011	12.562	0.746	0.746	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.933	0.957	13.513	12.471	12.471	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.005	-0.001	13.479	-0.176	-0.176	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.790	-0.882	15.200	-13.298	-13.298	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.021	-0.006	17.780	-0.797	-0.797	0.000	0.000	0.000	0.000
21	A	21	PRO	0	-0.045	-0.029	19.864	0.646	0.646	0.000	0.000	0.000	0.000
22	A	22	TRP	0	-0.013	-0.003	19.718	0.376	0.376	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.884	-0.941	22.575	-11.284	-11.284	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.902	0.944	24.025	11.858	11.858	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.049	-0.025	19.265	0.042	0.042	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.040	0.026	19.031	-0.504	-0.504	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.913	-0.951	15.019	-18.143	-18.143	0.000	0.000	0.000	0.000
28	A	28	TYR	0	-0.105	-0.055	13.946	-1.755	-1.755	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.007	0.006	12.153	0.825	0.825	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.044	-0.021	13.625	-1.021	-1.021	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.014	-0.002	10.645	-0.146	-0.146	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.835	0.913	14.889	13.510	13.510	0.000	0.000	0.000	0.000
33	A	33	HIS	0	0.069	0.043	16.236	-0.445	-0.445	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.020	-0.011	19.814	0.171	0.171	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.910	-0.943	23.152	-10.931	-10.931	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.084	-0.049	20.702	-0.197	-0.197	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.889	-0.935	23.407	-10.755	-10.755	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.839	0.915	21.480	12.930	12.930	0.000	0.000	0.000	0.000
39	A	39	TRP	0	0.024	-0.007	18.095	-0.547	-0.547	0.000	0.000	0.000	0.000
40	A	40	TYR	0	-0.016	-0.021	17.263	0.618	0.618	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.051	0.032	12.426	-0.771	-0.771	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.024	-0.009	12.816	0.920	0.920	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.023	0.000	7.110	-1.383	-1.383	0.000	0.000	0.000	0.000
44	A	44	MET	0	-0.005	-0.006	10.773	2.578	2.578	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.859	-0.923	10.554	-29.855	-29.855	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.041	-0.027	12.189	2.481	2.481	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.016	-0.009	13.155	-1.451	-1.451	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.012	0.007	12.303	-0.035	-0.035	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.823	-0.912	14.043	-15.355	-15.355	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.843	0.919	16.343	16.455	16.455	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.043	-0.015	11.207	-0.222	-0.222	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.014	-0.001	15.341	-0.136	-0.136	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.063	-0.018	11.644	0.046	0.046	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.014	-0.011	15.834	0.067	0.067	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.038	-0.009	15.650	0.619	0.619	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.854	-0.941	16.099	-16.717	-16.717	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.905	0.973	9.599	29.058	29.058	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.974	0.975	13.229	17.459	17.459	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.042	-0.027	8.310	-1.636	-1.636	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.772	-0.888	6.357	-37.426	-37.426	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.062	-0.042	6.752	-5.153	-5.153	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.009	0.003	5.662	1.301	1.301	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.886	-0.945	9.203	-19.280	-19.280	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.055	-0.025	8.999	-1.110	-1.110	0.000	0.000	0.000	0.000
65	A	65	LYS	0	0.046	0.040	11.947	1.055	1.055	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.012	-0.014	14.722	-0.471	-0.471	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.031	0.006	17.199	0.347	0.347	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.010	-0.001	20.529	-0.530	-0.530	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.869	-0.927	22.892	-11.993	-11.993	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.015	0.003	18.065	-0.272	-0.272	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.001	0.014	17.917	-1.018	-1.018	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.002	0.000	18.294	-0.679	-0.679	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.029	-0.014	17.729	-0.511	-0.511	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.000	-0.007	11.677	-1.052	-1.052	0.000	0.000	0.000	0.000
75	A	75	ARG	1	1.001	0.982	13.796	14.699	14.699	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.952	0.994	15.829	16.210	16.210	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.843	0.942	10.798	24.148	24.148	0.000	0.000	0.000	0.000
78	A	78	PRO	0	0.056	0.024	11.751	-0.397	-0.397	0.000	0.000	0.000	0.000
79	A	79	GLY	0	-0.011	-0.015	9.289	-2.357	-2.357	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.030	-0.010	9.300	-2.143	-2.143	0.000	0.000	0.000	0.000
81	A	81	TYR	0	0.033	0.019	11.219	2.568	2.568	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.036	-0.026	13.803	0.034	0.034	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.047	0.039	16.045	-0.580	-0.580	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.023	-0.017	15.697	0.969	0.969	0.000	0.000	0.000	0.000
85	A	85	HIS	0	0.008	0.008	17.480	1.335	1.335	0.000	0.000	0.000	0.000
86	A	86	MET	0	0.006	-0.007	21.565	0.207	0.207	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.017	0.012	21.821	0.653	0.653	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.914	0.947	20.264	14.375	14.375	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.870	-0.946	19.392	-13.051	-13.051	0.000	0.000	0.000	0.000
90	A	90	HIS	0	-0.013	-0.006	19.473	-0.722	-0.722	0.000	0.000	0.000	0.000
91	A	91	TRP	0	-0.005	0.001	16.374	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.044	-0.028	12.671	0.560	0.560	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.010	0.012	10.940	-0.894	-0.894	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.010	-0.009	5.894	-0.488	-0.488	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.020	0.012	6.321	-1.273	-1.273	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.906	-0.943	6.634	-31.078	-31.078	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.018	0.009	6.002	2.358	2.358	0.000	0.000	0.000	0.000
108	A	108	LEU	0	0.031	-0.005	8.779	1.293	1.293	0.000	0.000	0.000	0.000
109	A	109	ILE	0	0.011	0.006	5.319	0.818	0.818	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.860	-0.913	9.247	-16.574	-16.574	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.913	-0.959	11.758	-16.775	-16.775	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.088	-0.058	11.668	0.583	0.583	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.009	-0.003	12.701	0.879	0.879	0.000	0.000	0.000	0.000
114	A	114	GLN	0	-0.014	-0.011	14.461	1.126	1.126	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.056	-0.025	17.226	0.789	0.789	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.064	-0.029	15.543	0.007	0.007	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.914	0.977	18.020	12.671	12.671	0.000	0.000	0.000	0.000
118	A	118	LEU	0	0.058	0.023	19.628	0.363	0.363	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.975	-0.987	22.576	-9.880	-9.880	0.000	0.000	0.000	0.000
120	A	120	HIS	0	0.014	0.014	25.157	0.258	0.258	0.000	0.000	0.000	0.000
121	A	121	HIS	1	0.874	0.918	26.380	9.647	9.647	0.000	0.000	0.000	0.000
122	A	122	HIS	0	0.002	0.011	30.179	0.008	0.008	0.000	0.000	0.000	0.000
123	A	123	HIS	0	0.026	0.017	32.763	-0.097	-0.097	0.000	0.000	0.000	0.000
124	A	124	HIS	0	-0.017	-0.010	35.958	-0.036	-0.036	0.000	0.000	0.000	0.000
125	A	125	HIS	-1	-0.952	-0.959	38.963	-7.160	-7.160	0.000	0.000	0.000	0.000

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