FMO DATABASE

FMODB ID: LVGY9

Calculation Name: 2KTS-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KTS

Chain ID: A

ChEMBL ID:

UniProt ID: P52644

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-926561.168243
FMO2-HF: Nuclear repulsion	879255.951686
FMO2-HF: Total energy	-47305.216557
FMO2-MP2: Total energy	-47434.91799

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.
-79.67	-75.151	2.959	-2.473	-5.006	-0.03

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 : 0.820 / q_NPA : 0.909

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	THR	0	-0.011	-0.012	2.662	-0.468	2.388	0.598	-1.536	-1.920	-0.015
4	A	4	PRO	0	0.072	0.013	5.363	2.179	2.263	-0.001	-0.006	-0.076	0.000
53	A	53	LEU	0	0.055	0.030	4.575	-0.508	-0.416	-0.001	-0.008	-0.083	0.000
55	A	55	ASN	0	0.016	-0.014	2.456	-2.018	-1.044	1.560	-0.912	-1.622	-0.006
56	A	56	GLY	0	0.041	0.025	2.781	-5.052	-4.623	0.804	-0.001	-1.232	-0.009
57	A	57	GLU	-1	-0.918	-0.945	4.741	-19.801	-19.717	-0.001	-0.010	-0.073	0.000
5	A	5	GLU	-1	-0.954	-0.974	8.901	-20.913	-20.913	0.000	0.000	0.000	0.000
6	A	6	GLN	0	0.058	0.025	5.601	-3.678	-3.678	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.001	0.006	8.363	-0.026	-0.026	0.000	0.000	0.000	0.000
8	A	8	GLN	0	-0.009	-0.019	11.845	2.901	2.901	0.000	0.000	0.000	0.000
9	A	9	HIS	1	0.845	0.919	14.584	20.146	20.146	0.000	0.000	0.000	0.000
10	A	10	HIS	0	-0.022	0.000	13.166	-0.412	-0.412	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.763	0.879	16.159	14.083	14.083	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.036	-0.005	11.819	-0.757	-0.757	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.005	0.000	17.533	0.809	0.809	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.019	-0.008	19.371	-0.677	-0.677	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.924	-0.957	19.464	-14.497	-14.497	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.032	-0.029	20.086	0.568	0.568	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.010	0.009	19.954	-0.742	-0.742	0.000	0.000	0.000	0.000
18	A	18	ASN	0	0.004	0.001	20.966	-0.163	-0.163	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.010	0.007	21.951	0.252	0.252	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.940	0.956	24.973	10.635	10.635	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.069	0.044	24.542	-0.432	-0.432	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.006	0.001	24.563	0.396	0.396	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.019	-0.005	27.078	0.006	0.006	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.009	-0.013	29.599	0.043	0.043	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.897	-0.944	31.339	-9.211	-9.211	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.899	0.951	31.043	9.902	9.902	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.041	-0.017	29.757	-0.148	-0.148	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.038	0.029	25.233	0.176	0.176	0.000	0.000	0.000	0.000
29	A	29	PRO	0	0.041	0.027	24.372	-0.096	-0.096	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.872	-0.921	21.798	-13.936	-13.936	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.038	-0.029	16.665	0.564	0.564	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.015	0.001	18.274	-0.767	-0.767	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.011	0.004	14.306	0.079	0.079	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.015	0.015	16.854	0.430	0.430	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.805	-0.897	16.428	-16.942	-16.942	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.805	0.876	15.814	15.219	15.219	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.041	-0.001	10.692	-0.715	-0.715	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.068	-0.004	14.156	0.241	0.241	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.029	0.016	15.426	-0.471	-0.471	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.059	-0.049	18.533	1.325	1.325	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.048	0.026	21.009	-0.609	-0.609	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.092	-0.052	22.588	0.725	0.725	0.000	0.000	0.000	0.000
43	A	43	MET	0	-0.010	0.024	21.186	0.233	0.233	0.000	0.000	0.000	0.000
44	A	44	CYS	0	0.039	0.017	26.067	0.488	0.488	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.034	-0.040	29.417	0.466	0.466	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.921	0.980	25.421	11.996	11.996	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.046	0.030	19.581	0.126	0.126	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.028	-0.016	21.959	-0.043	-0.043	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.087	0.036	20.147	0.375	0.375	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.815	-0.883	17.752	-14.131	-14.131	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.054	0.040	14.395	-0.016	-0.016	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.883	0.924	9.472	19.484	19.484	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.036	-0.014	5.462	0.163	0.163	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.045	-0.022	7.864	0.112	0.112	0.000	0.000	0.000	0.000
59	A	59	THR	0	0.022	0.010	10.761	1.244	1.244	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.038	-0.019	13.460	-0.226	-0.226	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.773	0.882	16.652	14.000	14.000	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.016	-0.017	18.250	0.557	0.557	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.017	-0.016	20.020	-0.542	-0.542	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.022	-0.009	22.630	0.549	0.549	0.000	0.000	0.000	0.000
65	A	65	MET	0	-0.026	-0.011	24.473	-0.278	-0.278	0.000	0.000	0.000	0.000
66	A	66	THR	0	-0.062	-0.042	28.231	0.446	0.446	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.948	0.961	31.864	8.538	8.538	0.000	0.000	0.000	0.000
68	A	68	MET	0	-0.057	-0.015	32.310	0.351	0.351	0.000	0.000	0.000	0.000
69	A	69	MET	0	0.017	0.002	35.122	0.043	0.043	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.008	0.010	35.008	-0.070	-0.070	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.015	0.018	31.634	0.027	0.027	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.006	-0.002	33.891	-0.102	-0.102	0.000	0.000	0.000	0.000
73	A	74	GLN	0	0.011	-0.006	26.968	0.127	0.127	0.000	0.000	0.000	0.000
74	A	75	LEU	0	0.034	0.000	27.929	-0.329	-0.329	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.004	-0.011	28.784	-0.315	-0.315	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.955	-0.959	28.785	-10.831	-10.831	0.000	0.000	0.000	0.000
77	A	78	LEU	0	0.012	-0.017	24.030	-0.323	-0.323	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.710	-0.841	24.416	-12.031	-12.031	0.000	0.000	0.000	0.000
79	A	80	ASN	0	0.021	0.014	24.783	-0.324	-0.324	0.000	0.000	0.000	0.000
80	A	81	THR	0	-0.007	0.004	21.310	-0.171	-0.171	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.015	0.006	18.087	-0.620	-0.620	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.017	-0.029	19.694	-0.534	-0.534	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.899	-0.938	20.742	-12.550	-12.550	0.000	0.000	0.000	0.000
84	A	85	MET	0	-0.016	0.003	16.241	-0.075	-0.075	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.008	-0.014	15.166	-0.881	-0.881	0.000	0.000	0.000	0.000
86	A	87	LYS	1	0.908	0.966	16.557	12.326	12.326	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.850	-0.939	16.182	-15.342	-15.342	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.015	0.006	12.968	-0.197	-0.197	0.000	0.000	0.000	0.000
89	A	90	ALA	0	-0.023	-0.008	12.322	-0.644	-0.644	0.000	0.000	0.000	0.000
90	A	91	GLN	0	-0.009	-0.002	8.258	-3.594	-3.594	0.000	0.000	0.000	0.000
91	A	92	VAL	0	-0.035	-0.027	7.883	1.380	1.380	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.919	-0.954	6.296	-45.049	-45.049	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.071	-0.029	6.428	3.984	3.984	0.000	0.000	0.000	0.000
94	A	95	THR	0	0.045	0.015	5.479	-8.727	-8.727	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.017	-0.027	7.103	1.855	1.855	0.000	0.000	0.000	0.000
96	A	97	ASN	0	0.014	0.008	8.772	0.811	0.811	0.000	0.000	0.000	0.000
97	A	98	GLN	0	-0.034	-0.021	10.671	3.586	3.586	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.003	0.014	10.223	-3.102	-3.102	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.020	0.012	10.471	3.249	3.249	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.005	0.007	10.779	-1.833	-1.833	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.019	0.017	12.644	1.399	1.399	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.059	-0.028	13.172	-1.020	-1.020	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.003	0.016	15.508	0.463	0.463	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.828	0.912	18.616	13.006	13.006	0.000	0.000	0.000	0.000
105	A	106	GLN	0	0.013	-0.012	19.150	0.558	0.558	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.023	-0.012	15.519	-0.722	-0.722	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.005	-0.017	16.219	1.170	1.170	0.000	0.000	0.000	0.000
108	A	109	THR	0	0.020	0.019	15.040	-1.926	-1.926	0.000	0.000	0.000	0.000
109	A	110	TYR	0	0.032	0.004	15.271	1.665	1.665	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.896	0.947	14.972	15.626	15.626	0.000	0.000	0.000	0.000
111	A	112	LEU	0	0.059	0.041	12.501	0.403	0.403	0.000	0.000	0.000	0.000
112	A	113	ALA	0	-0.016	-0.006	15.763	0.558	0.558	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.778	-0.896	17.357	-17.597	-17.597	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.066	-0.033	19.411	0.451	0.451	0.000	0.000	0.000	0.000
115	A	116	MET	0	-0.045	-0.001	19.643	0.874	0.874	0.000	0.000	0.000	0.000
116	A	117	ASN	-1	-0.927	-0.961	19.987	-15.854	-15.854	0.000	0.000	0.000	0.000

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