FMO DATABASE

FMODB ID: 7KN5K

Calculation Name: 2KI3-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KI3

Chain ID: A

ChEMBL ID:

UniProt ID: A5K8X6

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1014215.042273
FMO2-HF: Nuclear repulsion	964726.016165
FMO2-HF: Total energy	-49489.026108
FMO2-MP2: Total energy	-49631.505744

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.
-61.621	-59.289	-0.017	-0.998	-1.318	-0.003

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 : 0.754 / q_NPA : 0.853

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	GLN	0	-0.019	-0.005	3.805	9.234	11.566	-0.017	-0.998	-1.318	-0.003
4	A	4	GLU	-1	-0.950	-0.969	5.478	-26.143	-26.143	0.000	0.000	0.000	0.000
5	A	5	THR	0	-0.052	-0.029	7.707	3.715	3.715	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.015	0.003	9.307	-1.199	-1.199	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.870	-0.932	9.847	-26.588	-26.588	0.000	0.000	0.000	0.000
8	A	8	GLN	0	-0.043	-0.027	13.588	0.812	0.812	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.002	-0.004	15.159	-0.052	-0.052	0.000	0.000	0.000	0.000
10	A	10	HIS	0	0.027	0.011	18.155	-0.121	-0.121	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.031	-0.027	19.976	-0.206	-0.206	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.044	-0.017	22.940	0.358	0.358	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.865	-0.932	26.419	-10.831	-10.831	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.944	-0.968	28.273	-9.230	-9.230	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.044	-0.020	27.153	0.139	0.139	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.016	-0.019	27.811	-0.134	-0.134	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.025	-0.002	23.644	0.024	0.024	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.026	0.005	20.891	-0.218	-0.218	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.928	0.974	14.289	17.895	17.895	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.031	-0.017	14.695	-0.129	-0.129	0.000	0.000	0.000	0.000
21	A	21	ILE	0	0.004	-0.022	9.459	0.274	0.274	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.022	-0.003	11.607	-0.114	-0.114	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.896	0.931	6.101	31.277	31.277	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.946	0.992	5.305	34.393	34.393	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.002	0.002	6.982	-1.645	-1.645	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.947	-0.964	6.622	-27.501	-27.501	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.019	0.017	6.900	-2.135	-2.135	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.032	0.015	9.194	0.149	0.149	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.932	-0.978	12.240	-13.177	-13.177	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.954	-0.973	13.299	-16.953	-16.953	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.063	-0.053	10.931	-0.160	-0.160	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.059	0.032	14.591	-0.432	-0.432	0.000	0.000	0.000	0.000
33	A	33	PRO	0	-0.005	0.002	16.914	0.502	0.502	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.933	0.963	20.228	11.697	11.697	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.956	0.977	23.634	10.299	10.299	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.018	-0.012	26.807	0.065	0.065	0.000	0.000	0.000	0.000
37	A	37	ASN	0	-0.017	-0.011	26.636	0.215	0.215	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.715	-0.819	27.922	-9.756	-9.756	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.025	-0.012	23.082	-0.365	-0.365	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.031	-0.022	23.135	0.463	0.463	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.020	-0.014	20.325	-0.718	-0.718	0.000	0.000	0.000	0.000
42	A	42	HIS	0	0.004	-0.009	18.716	1.102	1.102	0.000	0.000	0.000	0.000
43	A	43	TYR	0	0.025	0.013	20.301	-0.547	-0.547	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.028	-0.006	21.581	0.493	0.493	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.085	0.054	23.626	-0.345	-0.345	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.900	0.937	21.523	13.178	13.178	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.043	0.031	26.768	-0.112	-0.112	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.947	-0.981	26.616	-10.585	-10.585	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.021	0.014	28.193	0.049	0.049	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.027	-0.019	31.253	0.261	0.261	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.009	-0.001	27.759	0.067	0.067	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.899	0.957	27.709	9.002	9.002	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.004	-0.006	24.959	-0.121	-0.121	0.000	0.000	0.000	0.000
54	A	54	PHE	0	0.005	0.000	27.695	0.355	0.355	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.812	-0.897	28.193	-10.137	-10.137	0.000	0.000	0.000	0.000
56	A	56	SER	0	0.014	0.005	25.369	-0.561	-0.561	0.000	0.000	0.000	0.000
57	A	57	SER	0	0.034	0.005	23.945	0.269	0.269	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.953	0.968	20.776	13.287	13.287	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-1.015	-0.996	24.483	-10.257	-10.257	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.838	0.910	27.563	10.161	10.161	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.075	-0.027	26.281	-0.158	-0.158	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.024	0.012	27.249	0.126	0.126	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.020	-0.003	23.706	-0.185	-0.185	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.039	0.015	24.916	0.459	0.459	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.848	0.913	25.302	9.361	9.361	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.004	-0.004	24.085	0.306	0.306	0.000	0.000	0.000	0.000
67	A	67	HIS	0	0.070	0.037	27.849	-0.323	-0.323	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.042	0.018	22.985	0.156	0.156	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.004	-0.012	27.346	0.165	0.165	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.041	-0.007	29.569	0.340	0.340	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.022	-0.020	31.910	-0.186	-0.186	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.902	-0.944	33.003	-8.608	-8.608	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.051	-0.015	28.290	-0.058	-0.058	0.000	0.000	0.000	0.000
74	A	74	ILE	0	0.036	0.033	29.138	0.098	0.098	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.920	0.933	28.994	9.537	9.537	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.051	0.019	26.449	-0.325	-0.325	0.000	0.000	0.000	0.000
77	A	77	TRP	0	-0.003	-0.014	24.665	-0.680	-0.680	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.869	-0.922	24.170	-10.991	-10.991	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.011	0.000	23.044	-0.333	-0.333	0.000	0.000	0.000	0.000
80	A	80	CYS	0	-0.031	-0.006	20.045	-0.790	-0.790	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.011	-0.011	19.465	-0.735	-0.735	0.000	0.000	0.000	0.000
82	A	82	ALA	0	-0.027	-0.005	20.035	-0.393	-0.393	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.047	-0.015	17.566	-0.106	-0.106	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.071	-0.016	15.054	-0.673	-0.673	0.000	0.000	0.000	0.000
85	A	85	THR	0	0.032	0.029	11.091	0.763	0.763	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.923	0.949	13.394	16.788	16.788	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.074	-0.047	10.370	-0.740	-0.740	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.866	-0.914	9.734	-27.385	-27.385	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.826	0.905	11.497	19.447	19.447	0.000	0.000	0.000	0.000
90	A	90	CYS	0	-0.027	-0.009	12.503	-1.423	-1.423	0.000	0.000	0.000	0.000
91	A	91	SER	0	0.012	0.015	15.051	1.263	1.263	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.006	-0.009	18.119	-0.290	-0.290	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.931	0.965	21.013	13.111	13.111	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.024	0.001	24.040	-0.036	-0.036	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.792	-0.886	27.412	-9.502	-9.502	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.072	-0.036	30.592	0.127	0.127	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.942	0.962	33.038	8.910	8.910	0.000	0.000	0.000	0.000
98	A	98	TYR	0	0.005	-0.008	29.755	0.112	0.112	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.014	0.013	31.083	-0.176	-0.176	0.000	0.000	0.000	0.000
100	A	100	TYR	0	-0.026	-0.020	31.879	-0.033	-0.033	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.012	0.022	35.222	0.225	0.225	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.937	-0.976	36.840	-7.770	-7.770	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.997	-0.993	39.677	-7.183	-7.183	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.004	0.005	37.030	-0.148	-0.148	0.000	0.000	0.000	0.000
105	A	105	CYS	0	-0.012	-0.011	35.804	0.242	0.242	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.053	0.031	37.782	-0.062	-0.062	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.936	-0.985	39.995	-7.305	-7.305	0.000	0.000	0.000	0.000
108	A	108	SER	0	-0.119	-0.052	35.890	-0.168	-0.168	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.035	-0.024	32.677	-0.311	-0.311	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.016	0.023	36.260	0.156	0.156	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.085	0.036	36.995	-0.210	-0.210	0.000	0.000	0.000	0.000
112	A	112	ASN	0	-0.081	-0.055	36.991	0.093	0.093	0.000	0.000	0.000	0.000
113	A	113	SER	0	0.010	0.011	34.256	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.005	0.008	27.899	-0.123	-0.123	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.000	-0.003	28.408	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.045	-0.029	21.959	-0.368	-0.368	0.000	0.000	0.000	0.000
117	A	117	PHE	0	0.035	0.029	23.321	0.303	0.303	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.942	-0.971	17.226	-16.926	-16.926	0.000	0.000	0.000	0.000
119	A	119	ILE	0	0.008	-0.007	18.448	0.505	0.505	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.802	-0.904	14.669	-19.031	-19.031	0.000	0.000	0.000	0.000
121	A	121	LEU	0	0.009	0.014	15.746	1.041	1.041	0.000	0.000	0.000	0.000
122	A	122	ILE	0	0.004	0.010	15.629	-0.909	-0.909	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.039	-0.045	17.316	-0.665	-0.665	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.007	0.013	17.647	0.560	0.560	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.768	0.880	22.371	9.937	9.937	0.000	0.000	0.000	0.000
126	A	126	GLU	-2	-1.843	-1.913	25.195	-19.699	-19.699	0.000	0.000	0.000	0.000

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