FMO DATABASE

FMODB ID: 24Z3R

Calculation Name: 2K0S-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2K0S

Chain ID: A

ChEMBL ID:

UniProt ID: Q7SYL1

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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1198949.001118
FMO2-HF: Nuclear repulsion	1143757.699884
FMO2-HF: Total energy	-55191.301234
FMO2-MP2: Total energy	-55350.283626

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:GLY)

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

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.
-291.338	-289.097	0.074	-1.068	-1.247	-0.006

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.933 / q_NPA : 0.958

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	HIS	0	0.024	0.021	3.866	5.460	6.852	-0.014	-0.636	-0.741	-0.002
66	A	66	ILE	0	-0.139	-0.082	3.039	-8.988	-8.187	0.089	-0.430	-0.461	-0.004
70	A	70	HIS	0	-0.105	-0.066	4.448	5.246	5.294	-0.001	-0.002	-0.045	0.000
4	A	4	HIS	0	0.070	0.049	5.684	-5.852	-5.852	0.000	0.000	0.000	0.000
5	A	5	HIS	0	-0.057	-0.033	8.486	3.224	3.224	0.000	0.000	0.000	0.000
6	A	6	HIS	0	0.075	0.070	11.227	-1.251	-1.251	0.000	0.000	0.000	0.000
7	A	7	HIS	0	-0.067	-0.072	14.002	1.143	1.143	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.033	0.000	15.548	-0.619	-0.619	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.894	-0.953	17.762	-13.391	-13.391	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.982	-0.994	20.816	-13.342	-13.342	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.097	-0.028	19.344	0.346	0.346	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.751	-0.862	17.271	-16.912	-16.912	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.036	0.010	19.663	-0.314	-0.314	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.888	-0.969	18.557	-16.008	-16.008	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.038	0.022	12.973	-0.569	-0.569	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.923	-0.953	18.041	-14.934	-14.934	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.009	0.000	19.554	0.247	0.247	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.011	-0.013	17.624	0.343	0.343	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.022	-0.007	13.752	-0.339	-0.339	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.024	0.012	17.812	0.097	0.097	0.000	0.000	0.000	0.000
21	A	21	ASN	0	-0.080	-0.067	20.984	0.739	0.739	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.037	-0.019	16.031	0.201	0.201	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.965	-0.989	18.845	-13.959	-13.959	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.885	-0.937	20.040	-11.397	-11.397	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.042	-0.023	20.474	0.264	0.264	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.102	-0.046	18.387	-0.152	-0.152	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.064	-0.024	22.402	0.161	0.161	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.912	-0.958	25.981	-9.663	-9.663	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.785	-0.892	25.109	-12.474	-12.474	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.944	-0.986	26.682	-9.814	-9.814	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.011	0.017	27.278	0.191	0.191	0.000	0.000	0.000	0.000
32	A	32	GLN	0	0.034	0.009	20.457	-0.346	-0.346	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.044	-0.017	25.509	0.248	0.248	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.012	-0.018	28.126	0.151	0.151	0.000	0.000	0.000	0.000
35	A	35	GLN	0	-0.001	0.009	25.979	0.063	0.063	0.000	0.000	0.000	0.000
36	A	36	GLN	0	0.009	-0.009	22.700	0.277	0.277	0.000	0.000	0.000	0.000
37	A	37	SER	0	-0.017	0.005	25.285	0.063	0.063	0.000	0.000	0.000	0.000
38	A	38	PHE	0	-0.035	-0.024	28.566	0.280	0.280	0.000	0.000	0.000	0.000
39	A	39	MET	0	-0.002	0.010	23.918	0.048	0.048	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.818	-0.891	25.510	-11.672	-11.672	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.816	0.894	26.384	10.558	10.558	0.000	0.000	0.000	0.000
42	A	42	TYR	0	-0.007	-0.011	28.793	0.328	0.328	0.000	0.000	0.000	0.000
43	A	43	TYR	0	-0.005	0.005	21.195	0.015	0.015	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.037	0.007	24.928	0.173	0.173	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-1.078	-1.021	28.245	-8.778	-8.778	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.166	-0.083	29.113	0.518	0.518	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.937	-0.960	26.232	-10.826	-10.826	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.888	-0.938	22.370	-13.865	-13.865	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.010	-0.017	18.314	-0.679	-0.679	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-1.046	-1.033	18.367	-14.612	-14.612	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.809	-0.885	19.453	-12.427	-12.427	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.081	-0.081	17.896	-0.132	-0.132	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.875	0.929	19.826	13.967	13.967	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.053	0.009	18.688	-0.579	-0.579	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.066	-0.019	15.757	-0.382	-0.382	0.000	0.000	0.000	0.000
56	A	56	TYR	0	0.015	-0.008	14.352	-1.276	-1.276	0.000	0.000	0.000	0.000
57	A	57	THR	0	0.070	0.062	14.623	-1.151	-1.151	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.033	-0.006	12.256	-0.667	-0.667	0.000	0.000	0.000	0.000
59	A	59	ILE	0	-0.013	-0.014	9.739	-1.774	-1.774	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.047	0.031	9.887	-3.257	-3.257	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.048	0.027	11.464	-0.383	-0.383	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.984	-0.994	7.131	-34.009	-34.009	0.000	0.000	0.000	0.000
63	A	63	TYR	0	-0.111	-0.077	6.229	-5.759	-5.759	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.033	0.045	7.794	-2.320	-2.320	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.860	-0.922	8.119	-29.276	-29.276	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.036	-0.018	6.320	-1.349	-1.349	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.858	-0.929	8.285	-19.972	-19.972	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.930	0.970	7.658	32.673	32.673	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.018	0.005	9.797	1.750	1.750	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.899	-0.957	12.732	-18.520	-18.520	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.002	0.009	12.565	-0.605	-0.605	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.065	-0.035	11.853	2.195	2.195	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.007	0.009	15.568	1.189	1.189	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.076	-0.027	18.140	1.267	1.267	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-1.006	-1.014	17.368	-16.499	-16.499	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.807	0.919	17.988	17.108	17.108	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.035	-0.022	21.215	0.630	0.630	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.050	0.024	23.266	0.408	0.408	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.002	-0.005	25.552	0.368	0.368	0.000	0.000	0.000	0.000
82	A	82	PHE	0	-0.001	-0.027	28.780	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.044	-0.048	27.096	-0.129	-0.129	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.073	-0.001	19.460	-0.045	-0.045	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.759	-0.925	18.828	-16.198	-16.198	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.030	0.034	21.402	-0.104	-0.104	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.074	0.029	13.954	-0.032	-0.032	0.000	0.000	0.000	0.000
88	A	88	THR	0	-0.016	-0.018	19.090	-0.159	-0.159	0.000	0.000	0.000	0.000
89	A	89	HIS	0	0.007	0.011	20.715	0.718	0.718	0.000	0.000	0.000	0.000
90	A	90	SER	0	0.017	-0.006	19.326	0.327	0.327	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.048	0.026	15.582	-0.300	-0.300	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.908	0.966	18.437	14.343	14.343	0.000	0.000	0.000	0.000
93	A	93	GLN	0	-0.034	-0.037	21.308	0.813	0.813	0.000	0.000	0.000	0.000
94	A	94	HIS	1	0.852	0.933	24.648	10.905	10.905	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.830	0.919	24.596	12.239	12.239	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.802	-0.916	27.234	-10.216	-10.216	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.943	-0.965	30.333	-9.511	-9.511	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.083	-0.045	28.998	0.292	0.292	0.000	0.000	0.000	0.000
99	A	99	SER	0	0.099	0.045	28.797	-0.608	-0.608	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.007	0.008	29.511	0.168	0.168	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.858	-0.921	30.507	-8.785	-8.785	0.000	0.000	0.000	0.000
102	A	102	ILE	0	-0.044	-0.024	32.886	0.270	0.270	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.057	-0.018	28.136	0.062	0.062	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.873	-0.955	31.323	-9.340	-9.340	0.000	0.000	0.000	0.000
105	A	105	MET	0	-0.053	-0.007	32.488	0.202	0.202	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.073	-0.040	34.669	0.259	0.259	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.038	-0.013	28.676	0.148	0.148	0.000	0.000	0.000	0.000
108	A	108	THR	0	0.020	0.018	31.577	-0.169	-0.169	0.000	0.000	0.000	0.000
109	A	109	PHE	0	-0.130	-0.065	31.723	0.045	0.045	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.085	-0.055	27.757	-0.070	-0.070	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.783	-0.878	28.500	-10.685	-10.685	0.000	0.000	0.000	0.000
112	A	112	PHE	0	0.011	-0.005	25.585	-0.319	-0.319	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.005	0.018	25.970	-0.347	-0.347	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.000	-0.010	26.208	-0.222	-0.222	0.000	0.000	0.000	0.000
115	A	115	PHE	0	-0.035	-0.020	21.646	-0.607	-0.607	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.922	0.963	21.360	11.212	11.212	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.929	-0.961	22.094	-12.551	-12.551	0.000	0.000	0.000	0.000
118	A	118	MET	0	-0.008	-0.007	19.047	-0.403	-0.403	0.000	0.000	0.000	0.000
119	A	119	PHE	0	-0.009	-0.009	15.075	-1.254	-1.254	0.000	0.000	0.000	0.000
120	A	120	THR	0	0.006	-0.001	17.262	-0.791	-0.791	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.903	-0.930	18.867	-14.489	-14.489	0.000	0.000	0.000	0.000
122	A	122	TYR	0	-0.048	-0.032	13.851	-0.933	-0.933	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.748	0.866	11.720	20.098	20.098	0.000	0.000	0.000	0.000
124	A	124	ALA	0	0.079	0.031	15.238	-0.495	-0.495	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.966	-0.976	16.923	-16.151	-16.151	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.792	0.895	7.827	30.215	30.215	0.000	0.000	0.000	0.000
127	A	127	GLU	-1	-0.782	-0.890	13.762	-21.047	-21.047	0.000	0.000	0.000	0.000
128	A	128	GLY	0	-0.060	-0.018	15.695	0.307	0.307	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.889	0.954	18.384	13.311	13.311	0.000	0.000	0.000	0.000
130	A	130	GLY	-1	-0.946	-0.964	21.043	-12.145	-12.145	0.000	0.000	0.000	0.000

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