FMO DATABASE

FMODB ID: KK1N3

Calculation Name: 2KV3-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KV3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BYZ8

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	128
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1196186.412945
FMO2-HF: Nuclear repulsion	1141061.170956
FMO2-HF: Total energy	-55125.241989
FMO2-MP2: Total energy	-55281.025996

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:GLN)

Summations of interaction energy for fragment #1(A:1:GLN)

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.
53.787	55.8	0.01	-0.995	-1.029	-0.002

Interaction energy analysis for fragmet #1(A:1:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.867 / q_NPA : 0.924

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	3	CYS	0	0.022	0.018	3.447	-8.230	-6.612	-0.004	-0.889	-0.725	-0.001
5	A	5	PRO	0	-0.052	-0.021	3.206	3.126	3.521	0.014	-0.106	-0.304	-0.001
4	A	4	ALA	0	0.063	0.022	5.185	5.224	5.224	0.000	0.000	0.000	0.000
6	A	6	GLY	0	0.021	0.020	5.433	-2.841	-2.841	0.000	0.000	0.000	0.000
7	A	7	TRP	0	-0.081	-0.037	5.452	0.978	0.978	0.000	0.000	0.000	0.000
8	A	8	PHE	0	0.004	-0.002	8.348	1.212	1.212	0.000	0.000	0.000	0.000
9	A	9	TYR	0	0.013	0.014	11.837	0.165	0.165	0.000	0.000	0.000	0.000
10	A	10	HIS	0	0.038	0.014	13.047	1.199	1.199	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.784	0.875	16.295	13.604	13.604	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.006	0.013	16.451	0.329	0.329	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.001	0.004	14.278	0.535	0.535	0.000	0.000	0.000	0.000
14	A	15	TYR	0	0.010	0.002	11.562	1.130	1.130	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.079	0.038	11.621	-1.172	-1.172	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.006	0.005	12.619	0.924	0.924	0.000	0.000	0.000	0.000
17	A	18	PHE	0	0.011	0.008	10.225	-0.526	-0.526	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.950	0.973	15.492	17.996	17.996	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.934	0.954	13.534	20.162	20.162	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.035	0.021	18.377	0.017	0.017	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.801	0.885	13.414	18.458	18.458	0.000	0.000	0.000	0.000
22	A	23	ASN	0	-0.014	0.006	20.038	0.129	0.129	0.000	0.000	0.000	0.000
23	A	24	TRP	0	0.048	0.025	20.775	-0.433	-0.433	0.000	0.000	0.000	0.000
24	A	25	SER	0	0.016	0.006	20.572	-0.647	-0.647	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.855	-0.901	16.931	-16.825	-16.825	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.010	-0.009	16.420	-0.911	-0.911	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.894	-0.967	16.038	-15.401	-15.401	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.002	0.008	15.247	-0.831	-0.831	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.847	-0.923	10.814	-23.345	-23.345	0.000	0.000	0.000	0.000
30	A	31	CYS	0	-0.102	-0.016	11.210	-1.398	-1.398	0.000	0.000	0.000	0.000
31	A	32	GLN	0	0.037	0.012	12.214	-1.277	-1.277	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.049	-0.020	10.178	-0.843	-0.843	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.012	0.006	5.321	-3.052	-3.052	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.018	0.021	9.784	-0.747	-0.747	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.077	-0.050	9.719	0.241	0.241	0.000	0.000	0.000	0.000
36	A	37	GLY	0	-0.001	-0.010	12.829	0.194	0.194	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.039	0.002	12.113	0.796	0.796	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.002	-0.015	14.184	0.892	0.892	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.050	0.021	16.471	-0.587	-0.587	0.000	0.000	0.000	0.000
40	A	41	ALA	0	-0.029	-0.010	18.743	0.392	0.392	0.000	0.000	0.000	0.000
41	A	42	SER	0	0.025	0.012	20.183	0.565	0.565	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.046	-0.032	22.562	-0.082	-0.082	0.000	0.000	0.000	0.000
43	A	44	LEU	0	0.062	0.040	25.820	0.319	0.319	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.002	-0.016	28.297	0.476	0.476	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.039	0.001	28.682	-0.394	-0.394	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.999	1.008	29.085	10.188	10.188	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.827	-0.893	23.188	-13.615	-13.615	0.000	0.000	0.000	0.000
48	A	49	ALA	0	-0.014	-0.012	24.633	-0.360	-0.360	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.005	0.005	26.022	-0.275	-0.275	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.046	0.012	23.907	-0.368	-0.368	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.005	-0.002	20.157	-0.429	-0.429	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.005	0.004	22.419	-0.328	-0.328	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.897	-0.945	25.052	-10.860	-10.860	0.000	0.000	0.000	0.000
54	A	55	TYR	0	-0.061	-0.022	19.841	-0.097	-0.097	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.057	-0.049	19.494	-0.186	-0.186	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.031	-0.007	22.115	0.181	0.181	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.012	0.005	24.931	0.243	0.243	0.000	0.000	0.000	0.000
58	A	59	TYR	0	0.022	-0.013	25.706	0.184	0.184	0.000	0.000	0.000	0.000
59	A	60	GLN	0	0.011	0.025	27.466	0.467	0.467	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.862	0.916	25.535	11.429	11.429	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.067	0.061	26.169	-0.527	-0.527	0.000	0.000	0.000	0.000
62	A	63	GLN	0	-0.051	-0.047	21.564	0.147	0.147	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.008	0.026	25.779	0.085	0.085	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.018	-0.012	20.591	-0.546	-0.546	0.000	0.000	0.000	0.000
65	A	66	TRP	0	0.003	-0.005	21.998	0.268	0.268	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.021	-0.015	21.493	-0.614	-0.614	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.038	0.023	22.472	0.169	0.169	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.102	-0.049	23.049	0.422	0.422	0.000	0.000	0.000	0.000
69	A	70	HIS	1	0.941	0.976	25.681	11.414	11.414	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.829	-0.915	28.792	-9.426	-9.426	0.000	0.000	0.000	0.000
71	A	72	PRO	0	-0.057	-0.011	30.509	-0.208	-0.208	0.000	0.000	0.000	0.000
72	A	73	GLN	0	0.013	-0.020	31.897	0.088	0.088	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.951	0.982	34.592	9.010	9.010	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.965	0.995	36.656	8.244	8.244	0.000	0.000	0.000	0.000
75	A	76	GLN	0	-0.018	-0.019	38.574	0.048	0.048	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.055	0.044	34.985	-0.051	-0.051	0.000	0.000	0.000	0.000
77	A	78	TRP	0	-0.007	-0.005	32.641	-0.183	-0.183	0.000	0.000	0.000	0.000
78	A	79	GLN	0	-0.013	-0.020	30.342	-0.166	-0.166	0.000	0.000	0.000	0.000
79	A	80	TRP	0	-0.004	-0.017	24.688	0.097	0.097	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.012	-0.004	20.767	0.384	0.384	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.943	-0.964	23.589	-12.594	-12.594	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.029	0.028	25.137	0.355	0.355	0.000	0.000	0.000	0.000
83	A	84	ALA	0	-0.031	-0.009	26.928	0.417	0.417	0.000	0.000	0.000	0.000
84	A	85	MET	0	0.028	-0.006	28.906	0.227	0.227	0.000	0.000	0.000	0.000
85	A	86	TYR	0	0.003	0.006	30.883	-0.093	-0.093	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.009	0.007	33.234	0.253	0.253	0.000	0.000	0.000	0.000
87	A	88	TYR	0	0.009	-0.001	36.616	-0.070	-0.070	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.912	0.979	31.482	9.696	9.696	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.052	0.023	36.031	0.168	0.168	0.000	0.000	0.000	0.000
90	A	91	TRP	0	-0.045	-0.032	37.787	-0.211	-0.211	0.000	0.000	0.000	0.000
91	A	92	SER	0	0.068	0.037	40.320	0.174	0.174	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.041	0.021	40.825	-0.137	-0.137	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.864	0.940	35.445	8.523	8.523	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.030	0.013	39.609	0.149	0.149	0.000	0.000	0.000	0.000
95	A	96	MET	0	-0.004	-0.007	36.257	-0.238	-0.238	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.017	0.014	36.388	-0.216	-0.216	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.020	0.013	37.770	0.154	0.154	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.037	-0.027	31.907	0.149	0.149	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.915	0.959	32.389	8.198	8.198	0.000	0.000	0.000	0.000
100	A	101	HIS	0	0.083	0.043	30.183	-0.059	-0.059	0.000	0.000	0.000	0.000
101	A	102	CYS	0	-0.051	-0.032	25.615	-0.545	-0.545	0.000	0.000	0.000	0.000
102	A	103	ALA	0	-0.023	-0.006	28.477	0.254	0.254	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.887	-0.942	27.201	-11.165	-11.165	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.020	-0.005	26.350	0.250	0.250	0.000	0.000	0.000	0.000
105	A	106	SER	0	0.083	0.029	28.929	-0.184	-0.184	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.031	-0.025	29.137	0.227	0.227	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.021	-0.001	30.803	0.161	0.161	0.000	0.000	0.000	0.000
108	A	109	ASN	0	0.014	0.006	33.647	0.179	0.179	0.000	0.000	0.000	0.000
109	A	110	ASN	0	0.043	0.011	32.716	-0.493	-0.493	0.000	0.000	0.000	0.000
110	A	111	PHE	0	-0.020	-0.005	32.548	-0.176	-0.176	0.000	0.000	0.000	0.000
111	A	112	LEU	0	0.006	0.005	27.461	-0.063	-0.063	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.042	-0.010	30.643	-0.033	-0.033	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.028	-0.009	27.985	0.198	0.198	0.000	0.000	0.000	0.000
114	A	115	SER	0	-0.016	0.012	31.712	0.489	0.489	0.000	0.000	0.000	0.000
115	A	116	SER	0	-0.029	-0.022	31.958	-0.233	-0.233	0.000	0.000	0.000	0.000
116	A	117	ASN	0	-0.015	-0.006	29.569	0.120	0.120	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.802	-0.895	29.933	-9.538	-9.538	0.000	0.000	0.000	0.000
118	A	120	ASN	0	0.014	-0.018	25.232	-0.801	-0.801	0.000	0.000	0.000	0.000
119	A	121	LYS	1	0.895	0.956	26.557	10.860	10.860	0.000	0.000	0.000	0.000
120	A	122	ARG	1	0.957	0.971	22.387	12.325	12.325	0.000	0.000	0.000	0.000
121	A	123	GLN	0	-0.084	-0.050	22.865	0.424	0.424	0.000	0.000	0.000	0.000
122	A	124	HIS	0	0.058	0.044	20.126	-0.950	-0.950	0.000	0.000	0.000	0.000
123	A	125	PHE	0	0.032	0.015	14.295	0.707	0.707	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.019	0.001	16.363	-0.701	-0.701	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.900	0.937	14.281	16.829	16.829	0.000	0.000	0.000	0.000
126	A	129	TYR	0	0.015	-0.001	9.243	0.257	0.257	0.000	0.000	0.000	0.000
127	A	130	ARG	1	0.902	0.948	12.709	17.838	17.838	0.000	0.000	0.000	0.000
128	A	131	PRO	-1	-0.882	-0.926	12.871	-21.644	-21.644	0.000	0.000	0.000	0.000

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