FMO DATABASE

FMODB ID: 15M2Z

Calculation Name: 1N3K-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1N3K

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Z297

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1057498.682156
FMO2-HF: Nuclear repulsion	1004984.292872
FMO2-HF: Total energy	-52514.389285
FMO2-MP2: Total energy	-52668.408561

3D Structure

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.
-158.878	-151.618	4.284	-3.798	-7.749	-0.016

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 : 0.889 / q_NPA : 0.929

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	GLU	-1	-0.827	-0.913	3.028	-39.228	-37.222	0.035	-0.760	-1.281	-0.002
4	A	4	TYR	0	-0.019	0.020	2.752	3.444	5.625	0.314	-0.976	-1.519	-0.008
5	A	5	GLY	0	0.084	0.033	4.321	8.821	9.080	-0.001	-0.068	-0.190	0.000
57	A	57	LYS	1	0.889	0.912	1.964	41.472	42.422	3.916	-1.079	-3.788	0.001
58	A	58	ASP	-1	-0.932	-0.983	3.457	-59.204	-57.925	0.020	-0.670	-0.630	-0.005
82	A	82	TYR	0	0.000	-0.019	3.447	-6.037	-5.550	0.001	-0.226	-0.262	-0.002
86	A	86	VAL	0	-0.031	-0.028	3.837	-0.554	-0.456	-0.001	-0.019	-0.079	0.000
6	A	6	THR	0	-0.074	-0.034	6.379	6.811	6.811	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.034	0.026	7.062	3.556	3.556	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.005	0.004	7.172	3.842	3.842	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.008	0.017	10.140	4.154	4.154	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.911	-0.961	11.347	-23.767	-23.767	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.009	-0.003	12.102	1.965	1.965	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.063	-0.061	13.714	1.890	1.890	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.042	-0.023	15.297	1.680	1.680	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.087	-0.041	17.691	0.706	0.706	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.017	0.008	18.106	0.595	0.595	0.000	0.000	0.000	0.000
16	A	16	THR	0	0.020	0.016	20.197	0.311	0.311	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.034	0.003	23.097	-0.352	-0.352	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.911	-0.952	24.860	-10.530	-10.530	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.815	-0.917	22.842	-12.981	-12.981	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.023	-0.007	18.908	-0.289	-0.289	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.898	-0.957	22.370	-11.222	-11.222	0.000	0.000	0.000	0.000
22	A	22	GLN	0	0.002	0.023	24.936	0.242	0.242	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.011	-0.005	18.536	0.035	0.035	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.866	0.940	22.047	12.656	12.656	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.123	-0.080	23.385	0.466	0.466	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.008	0.005	23.586	0.340	0.340	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.039	-0.013	20.551	-0.306	-0.306	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.875	0.950	22.980	11.145	11.145	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.965	-0.966	25.573	-10.958	-10.958	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.898	-0.948	20.543	-14.270	-14.270	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.109	-0.061	19.638	-0.547	-0.547	0.000	0.000	0.000	0.000
32	A	32	PRO	0	0.011	0.009	22.187	0.564	0.564	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.061	-0.003	24.845	-0.256	-0.256	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.938	-0.969	26.715	-10.399	-10.399	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.842	0.930	21.760	13.399	13.399	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.008	0.001	23.015	-0.456	-0.456	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.963	-0.966	24.547	-10.326	-10.326	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.870	-0.934	21.559	-13.771	-13.771	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.054	-0.012	19.281	-0.569	-0.569	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.036	-0.002	21.511	0.488	0.488	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.012	-0.007	18.220	-0.139	-0.139	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.102	0.056	16.257	-0.075	-0.075	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.060	0.027	13.727	-0.556	-0.556	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.024	0.012	14.530	-0.656	-0.656	0.000	0.000	0.000	0.000
45	A	45	TRP	0	0.022	0.004	15.980	-0.176	-0.176	0.000	0.000	0.000	0.000
46	A	46	PHE	0	0.044	0.005	10.767	-0.128	-0.128	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.023	0.004	12.169	-0.828	-0.828	0.000	0.000	0.000	0.000
48	A	48	PHE	0	-0.005	0.003	13.676	0.233	0.233	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.030	-0.027	12.483	0.307	0.307	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.920	-0.962	7.986	-32.428	-32.428	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.109	-0.058	11.296	0.412	0.412	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.086	-0.045	14.277	2.275	2.275	0.000	0.000	0.000	0.000
53	A	53	ASN	0	-0.005	-0.007	13.702	-0.932	-0.932	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.852	0.935	14.472	16.768	16.768	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.019	0.024	8.348	0.006	0.006	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.870	-0.913	7.218	-27.456	-27.456	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.044	-0.004	6.242	2.054	2.054	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.062	0.023	7.944	1.161	1.161	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.006	0.005	10.914	1.429	1.429	0.000	0.000	0.000	0.000
62	A	62	TYR	0	0.019	0.007	14.452	1.012	1.012	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.019	0.008	10.716	0.931	0.931	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.930	-0.972	14.064	-20.740	-20.740	0.000	0.000	0.000	0.000
65	A	65	HIS	0	0.080	0.038	15.806	0.867	0.867	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.024	-0.011	17.961	0.889	0.889	0.000	0.000	0.000	0.000
67	A	67	PHE	0	-0.004	-0.010	13.921	0.652	0.652	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.963	-0.958	19.354	-14.126	-14.126	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.040	-0.015	21.519	0.866	0.866	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.051	-0.031	21.789	0.695	0.695	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.836	0.900	24.161	11.374	11.374	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.831	0.904	21.592	14.056	14.056	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.079	0.039	20.629	-0.761	-0.761	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.847	-0.899	19.740	-14.548	-14.548	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.014	-0.006	16.635	-0.888	-0.888	0.000	0.000	0.000	0.000
76	A	76	LEU	0	0.017	0.011	15.330	-1.483	-1.483	0.000	0.000	0.000	0.000
77	A	77	THR	0	-0.036	-0.023	15.541	-0.839	-0.839	0.000	0.000	0.000	0.000
78	A	78	MET	0	-0.004	0.008	12.895	-1.285	-1.285	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.010	0.003	11.103	-2.373	-2.373	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.028	0.017	11.285	-1.985	-1.985	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.889	-0.949	13.214	-19.770	-19.770	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.942	0.964	8.734	19.401	19.401	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.043	-0.014	9.856	0.075	0.075	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.871	0.928	8.202	33.052	33.052	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.024	0.029	7.322	-1.222	-1.222	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.816	0.897	9.463	21.852	21.852	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.059	-0.023	7.724	1.571	1.571	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.046	-0.028	5.596	-0.674	-0.674	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.856	-0.907	8.051	-20.457	-20.457	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.981	-0.994	6.386	-40.078	-40.078	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.883	-0.937	11.149	-18.667	-18.667	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.992	-0.985	11.207	-17.619	-17.619	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.039	0.042	8.564	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.867	-0.937	10.656	-17.086	-17.086	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.030	-0.039	13.633	0.628	0.628	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.816	0.901	11.791	19.477	19.477	0.000	0.000	0.000	0.000
99	A	99	LEU	0	-0.011	-0.009	13.588	0.755	0.755	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.035	-0.001	10.962	-0.791	-0.791	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.927	0.957	12.436	15.380	15.380	0.000	0.000	0.000	0.000
102	A	102	ILE	0	0.044	0.025	14.667	0.828	0.828	0.000	0.000	0.000	0.000
103	A	103	PRO	0	0.025	0.004	16.286	-0.360	-0.360	0.000	0.000	0.000	0.000
104	A	104	SER	0	-0.039	-0.010	17.670	-0.111	-0.111	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.022	0.014	16.229	0.233	0.233	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.906	0.982	9.742	21.364	21.364	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.938	0.957	11.727	17.392	17.392	0.000	0.000	0.000	0.000
108	A	108	TYR	0	0.002	0.003	11.692	-0.852	-0.852	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.938	0.945	8.289	20.572	20.572	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.848	-0.909	13.466	-13.545	-13.545	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.045	-0.012	15.583	0.407	0.407	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.042	0.010	14.323	-0.984	-0.984	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.887	0.946	10.875	19.200	19.200	0.000	0.000	0.000	0.000
114	A	114	GLN	0	0.034	0.011	11.228	-0.632	-0.632	0.000	0.000	0.000	0.000
115	A	115	PRO	0	0.003	0.006	9.185	-0.425	-0.425	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.004	-0.003	10.831	-1.365	-1.365	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.881	-0.939	11.981	-22.054	-22.054	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.974	-1.010	13.967	-14.657	-14.657	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.980	-0.969	17.362	-14.717	-14.717	0.000	0.000	0.000	0.000
120	A	120	ILE	0	0.006	-0.015	12.422	0.889	0.889	0.000	0.000	0.000	0.000
121	A	121	ILE	0	0.003	0.011	14.375	-0.263	-0.263	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.912	0.953	16.482	13.798	13.798	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.012	0.006	15.597	0.724	0.724	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.005	0.004	15.276	-0.331	-0.331	0.000	0.000	0.000	0.000
125	A	125	PRO	0	-0.008	0.002	16.858	0.907	0.907	0.000	0.000	0.000	0.000
126	A	126	PRO	0	-0.003	0.002	19.015	-0.183	-0.183	0.000	0.000	0.000	0.000
127	A	127	PRO	0	0.036	0.020	19.820	0.645	0.645	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.873	0.928	22.802	12.937	12.937	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.923	0.963	24.825	9.381	9.381	0.000	0.000	0.000	0.000
130	A	130	ALA	-1	-0.876	-0.935	28.586	-9.647	-9.647	0.000	0.000	0.000	0.000

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