FMO DATABASE

FMODB ID: J4ZK9

Calculation Name: 2FKI-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FKI

Chain ID: A

ChEMBL ID:

UniProt ID: P0AF50

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-976777.266711
FMO2-HF: Nuclear repulsion	929350.444292
FMO2-HF: Total energy	-47426.822419
FMO2-MP2: Total energy	-47564.931228

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.
-148.157	-140.571	24.63	-10.434	-21.781	-0.119

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 : 0.915

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	ILE	0	0.045	0.003	2.875	1.044	2.536	3.424	-1.224	-3.691	-0.011
4	A	4	SER	0	0.002	-0.002	4.345	2.176	2.114	0.001	0.223	-0.162	0.000
5	A	5	GLU	-1	-0.823	-0.887	3.156	-36.648	-36.227	0.029	-0.062	-0.387	0.000
6	A	6	LEU	0	-0.023	0.001	2.156	0.463	1.763	2.422	-1.041	-2.682	-0.002
7	A	7	LEU	0	0.025	0.011	3.541	3.131	3.356	0.027	-0.027	-0.224	0.000
83	A	83	LEU	0	0.044	0.004	4.670	-0.898	-0.704	-0.001	-0.013	-0.180	0.000
84	A	84	ASP	-1	-0.818	-0.894	4.488	-49.341	-49.245	-0.001	-0.008	-0.087	0.000
85	A	85	GLY	0	0.005	-0.003	3.124	5.574	5.929	0.039	-0.171	-0.224	-0.001
86	A	86	SER	0	-0.035	-0.031	1.918	-35.930	-37.150	8.584	-4.205	-3.159	-0.052
87	A	87	LEU	0	-0.005	0.015	4.102	2.606	2.988	0.001	-0.081	-0.302	0.000
88	A	88	PRO	0	-0.006	0.000	2.294	-34.456	-31.453	2.052	-2.511	-2.544	-0.030
89	A	89	ASP	-1	-0.850	-0.956	2.041	-54.549	-51.557	5.433	-3.737	-4.687	-0.014
90	A	90	SER	0	0.007	-0.001	2.643	10.111	6.946	0.260	3.360	-0.456	-0.001
92	A	92	ILE	0	0.007	-0.004	2.338	2.691	3.009	2.088	-0.506	-1.900	-0.003
93	A	93	TYR	0	0.047	0.011	3.128	0.556	1.811	0.272	-0.431	-1.096	-0.005
8	A	8	GLN	0	0.030	0.011	6.874	1.173	1.173	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.033	-0.032	5.722	1.813	1.813	0.000	0.000	0.000	0.000
10	A	10	CYS	0	-0.084	-0.052	7.245	1.490	1.490	0.000	0.000	0.000	0.000
11	A	11	MET	0	-0.020	-0.014	9.617	1.102	1.102	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.029	0.005	10.677	1.055	1.055	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.746	0.885	10.338	20.417	20.417	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.058	0.036	14.066	0.248	0.248	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.027	-0.007	17.807	0.171	0.171	0.000	0.000	0.000	0.000
16	A	16	ALA	0	-0.094	-0.037	14.564	0.259	0.259	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.808	-0.895	15.973	-14.643	-14.643	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.068	-0.052	13.500	-1.145	-1.145	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.022	-0.012	16.324	0.968	0.968	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.003	0.002	17.695	-0.316	-0.316	0.000	0.000	0.000	0.000
21	A	21	HIS	1	0.841	0.888	19.079	13.181	13.181	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.020	-0.017	20.877	-0.914	-0.914	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.820	-0.887	22.235	-12.038	-12.038	0.000	0.000	0.000	0.000
24	A	24	TRP	0	-0.012	-0.022	16.386	-0.166	-0.166	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.946	0.976	17.154	15.754	15.754	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.015	0.030	16.018	-0.900	-0.900	0.000	0.000	0.000	0.000
27	A	27	THR	0	0.019	0.001	13.594	1.239	1.239	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.039	-0.034	14.362	-0.668	-0.668	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.004	0.011	10.668	0.243	0.243	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.879	0.935	15.003	12.753	12.753	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.071	0.055	18.169	-0.014	-0.014	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.897	-0.950	20.786	-10.219	-10.219	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.922	-0.962	24.337	-10.807	-10.807	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.023	-0.007	21.723	-0.097	-0.097	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.039	-0.020	17.711	-0.464	-0.464	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.008	0.001	13.358	0.424	0.424	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.030	0.012	12.640	-0.440	-0.440	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.017	0.006	14.041	0.811	0.811	0.000	0.000	0.000	0.000
39	A	39	VAL	0	0.013	0.019	8.569	-0.632	-0.632	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.832	0.889	11.727	22.502	22.502	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.807	-0.877	10.263	-26.768	-26.768	0.000	0.000	0.000	0.000
42	A	42	VAL	0	-0.009	-0.012	12.700	2.169	2.169	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.837	-0.899	13.237	-22.143	-22.143	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.054	-0.024	12.799	0.149	0.149	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.813	0.877	9.448	24.036	24.036	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.014	-0.011	5.919	2.337	2.337	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.003	0.012	8.325	-1.037	-1.037	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.034	0.041	9.015	1.950	1.950	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.032	-0.019	10.946	0.470	0.470	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.031	0.020	11.660	0.300	0.300	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.957	0.976	15.578	12.936	12.936	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.044	-0.046	18.821	-0.284	-0.284	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.015	-0.012	17.841	-0.112	-0.112	0.000	0.000	0.000	0.000
54	A	54	PRO	0	0.018	0.014	19.883	-0.101	-0.101	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.826	-0.923	16.142	-14.996	-14.996	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.028	-0.010	13.057	-0.705	-0.705	0.000	0.000	0.000	0.000
57	A	57	ALA	0	-0.017	-0.003	16.868	0.016	0.016	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.848	-0.914	19.964	-12.550	-12.550	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.004	0.014	13.518	0.129	0.129	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.029	-0.014	17.786	0.073	0.073	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.848	0.916	19.937	13.160	13.160	0.000	0.000	0.000	0.000
62	A	62	GLN	0	-0.024	-0.028	20.494	0.001	0.001	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.060	-0.024	15.950	-0.375	-0.375	0.000	0.000	0.000	0.000
64	A	64	HIS	0	-0.006	-0.007	19.506	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.060	-0.036	18.517	-0.095	-0.095	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.855	-0.926	12.537	-25.149	-25.149	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.007	0.008	10.523	0.184	0.184	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.891	0.948	12.719	17.413	17.413	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.086	0.043	15.831	0.078	0.078	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.018	-0.023	17.057	0.849	0.849	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.893	0.929	19.128	11.980	11.980	0.000	0.000	0.000	0.000
72	A	72	HIS	0	0.068	0.056	18.547	0.602	0.602	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.034	0.028	18.124	0.288	0.288	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.015	-0.027	20.945	0.613	0.613	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.965	0.983	20.642	12.706	12.706	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.000	0.013	21.868	-0.127	-0.127	0.000	0.000	0.000	0.000
77	A	77	HIS	0	0.027	0.008	23.729	-0.048	-0.048	0.000	0.000	0.000	0.000
78	A	78	TRP	0	-0.005	0.005	18.449	-0.073	-0.073	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.006	-0.003	16.554	0.412	0.412	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.050	-0.020	13.786	-0.638	-0.638	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.029	0.014	9.096	0.555	0.555	0.000	0.000	0.000	0.000
82	A	82	TYR	0	-0.039	-0.030	9.911	-0.961	-0.961	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.026	0.002	5.910	2.351	2.351	0.000	0.000	0.000	0.000
94	A	94	TYR	0	0.024	0.026	6.387	2.691	2.691	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.005	-0.002	8.556	1.984	1.984	0.000	0.000	0.000	0.000
96	A	96	VAL	0	0.008	0.013	7.021	1.808	1.808	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.749	-0.866	9.827	-18.858	-18.858	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.013	0.019	12.060	1.389	1.389	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.062	-0.049	12.607	1.208	1.208	0.000	0.000	0.000	0.000
100	A	100	TYR	0	0.022	0.009	13.740	0.850	0.850	0.000	0.000	0.000	0.000
101	A	101	GLN	0	0.015	0.001	15.440	1.141	1.141	0.000	0.000	0.000	0.000
102	A	102	GLN	0	0.004	0.005	17.904	0.837	0.837	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.006	0.004	18.608	0.698	0.698	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.004	0.004	19.158	0.663	0.663	0.000	0.000	0.000	0.000
105	A	105	ASN	0	-0.056	-0.033	21.685	0.761	0.761	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.054	-0.020	22.261	0.461	0.461	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.008	0.013	22.491	0.284	0.284	0.000	0.000	0.000	0.000
108	A	108	PRO	0	0.015	-0.005	26.368	0.186	0.186	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.850	-0.918	29.087	-9.197	-9.197	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.873	-0.926	30.372	-9.132	-9.132	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.862	0.904	25.999	9.594	9.594	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.922	0.971	25.454	10.203	10.203	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.847	0.907	26.662	8.736	8.736	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.011	0.000	26.560	0.002	0.002	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.002	-0.012	20.974	-0.146	-0.146	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.057	-0.022	22.841	-0.287	-0.287	0.000	0.000	0.000	0.000
117	A	117	GLN	0	-0.067	-0.030	25.272	0.069	0.069	0.000	0.000	0.000	0.000
118	A	118	LEU	-1	-0.958	-0.951	20.902	-12.358	-12.358	0.000	0.000	0.000	0.000

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