FMO DATABASE

FMODB ID: K3LN3

Calculation Name: 1S4K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1S4K

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZPR1

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1039090.06554
FMO2-HF: Nuclear repulsion	988633.394324
FMO2-HF: Total energy	-50456.671215
FMO2-MP2: Total energy	-50601.069152

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
-1.176	-0.025	-0.001	-0.529	-0.621	0.002

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.008

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	2	MET	0	0.004	0.020	3.812	-1.271	-0.120	-0.001	-0.529	-0.621	0.002
4	A	3	ASN	0	0.005	0.009	5.073	0.730	0.730	0.000	0.000	0.000	0.000
5	A	4	ALA	0	0.085	0.030	7.242	0.081	0.081	0.000	0.000	0.000	0.000
6	A	5	LEU	0	0.029	0.018	10.001	0.075	0.075	0.000	0.000	0.000	0.000
7	A	6	GLU	-1	-0.893	-0.963	5.986	-2.493	-2.493	0.000	0.000	0.000	0.000
8	A	7	LEU	0	-0.016	0.010	10.218	0.093	0.093	0.000	0.000	0.000	0.000
9	A	8	GLN	0	-0.014	-0.010	12.758	0.058	0.058	0.000	0.000	0.000	0.000
10	A	9	ALA	0	-0.010	-0.007	12.757	0.064	0.064	0.000	0.000	0.000	0.000
11	A	10	LEU	0	-0.007	-0.013	12.078	0.057	0.057	0.000	0.000	0.000	0.000
12	A	11	ARG	1	0.797	0.887	15.299	0.340	0.340	0.000	0.000	0.000	0.000
13	A	12	ARG	1	0.930	0.961	17.943	0.336	0.336	0.000	0.000	0.000	0.000
14	A	13	ILE	0	0.002	0.020	16.345	0.027	0.027	0.000	0.000	0.000	0.000
15	A	14	PHE	0	-0.056	-0.030	16.687	0.028	0.028	0.000	0.000	0.000	0.000
16	A	15	ASP	-1	-0.911	-0.950	21.151	-0.156	-0.156	0.000	0.000	0.000	0.000
17	A	16	MET	0	-0.022	0.005	21.626	0.016	0.016	0.000	0.000	0.000	0.000
18	A	17	THR	0	0.009	0.001	22.814	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	18	ILE	0	0.010	-0.009	20.793	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	19	GLU	-1	-0.853	-0.934	22.986	-0.150	-0.150	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.821	-0.914	25.157	-0.143	-0.143	0.000	0.000	0.000	0.000
22	A	21	CYS	0	-0.068	-0.022	20.442	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.037	-0.013	22.428	0.009	0.009	0.000	0.000	0.000	0.000
24	A	23	ILE	0	0.002	0.015	23.928	0.015	0.015	0.000	0.000	0.000	0.000
25	A	24	TYR	0	-0.008	-0.031	24.555	0.015	0.015	0.000	0.000	0.000	0.000
26	A	25	ILE	0	-0.049	-0.015	18.137	0.000	0.000	0.000	0.000	0.000	0.000
27	A	26	THR	0	-0.068	-0.069	19.314	0.001	0.001	0.000	0.000	0.000	0.000
28	A	27	GLN	0	-0.075	-0.017	21.666	0.016	0.016	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.791	-0.887	23.555	-0.092	-0.092	0.000	0.000	0.000	0.000
30	A	29	ASN	0	-0.060	-0.039	26.418	0.001	0.001	0.000	0.000	0.000	0.000
31	A	30	ASN	0	0.009	0.014	23.543	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	31	SER	0	0.056	0.002	22.980	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	32	ALA	0	0.006	0.015	22.675	-0.016	-0.016	0.000	0.000	0.000	0.000
34	A	33	THR	0	-0.011	-0.021	18.917	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	34	TRP	0	0.027	-0.012	17.336	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	35	GLN	0	0.003	-0.013	17.828	-0.033	-0.033	0.000	0.000	0.000	0.000
37	A	36	ARG	1	0.949	0.990	18.062	0.100	0.100	0.000	0.000	0.000	0.000
38	A	37	TRP	0	-0.025	-0.010	14.034	-0.024	-0.024	0.000	0.000	0.000	0.000
39	A	38	GLU	-1	-0.768	-0.872	13.443	-0.409	-0.409	0.000	0.000	0.000	0.000
40	A	39	ALA	0	-0.009	0.015	15.105	-0.025	-0.025	0.000	0.000	0.000	0.000
41	A	40	GLY	0	-0.027	-0.016	12.564	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	41	ASP	-1	-0.913	-0.942	13.344	-0.170	-0.170	0.000	0.000	0.000	0.000
43	A	42	ILE	0	-0.087	-0.058	14.301	0.047	0.047	0.000	0.000	0.000	0.000
44	A	43	PRO	0	-0.007	0.000	10.286	-0.066	-0.066	0.000	0.000	0.000	0.000
45	A	44	ILE	0	0.029	0.011	9.865	0.071	0.071	0.000	0.000	0.000	0.000
46	A	45	SER	0	0.001	0.011	11.693	0.049	0.049	0.000	0.000	0.000	0.000
47	A	46	PRO	0	0.062	0.002	10.947	-0.061	-0.061	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.888	-0.936	12.255	0.038	0.038	0.000	0.000	0.000	0.000
49	A	48	ILE	0	-0.006	-0.005	14.883	-0.014	-0.014	0.000	0.000	0.000	0.000
50	A	49	ILE	0	0.000	0.002	8.160	-0.057	-0.057	0.000	0.000	0.000	0.000
51	A	50	ALA	0	-0.001	0.000	11.752	-0.050	-0.050	0.000	0.000	0.000	0.000
52	A	51	ARG	1	0.951	0.985	12.954	0.075	0.075	0.000	0.000	0.000	0.000
53	A	52	LEU	0	0.024	0.007	12.782	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.901	0.946	5.459	0.704	0.704	0.000	0.000	0.000	0.000
55	A	54	GLU	-1	-0.818	-0.898	12.263	-0.067	-0.067	0.000	0.000	0.000	0.000
56	A	55	MET	0	-0.023	-0.007	15.634	0.015	0.015	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.950	0.981	9.439	0.870	0.870	0.000	0.000	0.000	0.000
58	A	57	ALA	0	0.002	0.007	14.663	0.016	0.016	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.917	0.958	16.020	0.138	0.138	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.821	0.888	17.919	0.293	0.293	0.000	0.000	0.000	0.000
61	A	60	GLN	0	-0.022	-0.012	16.616	-0.020	-0.020	0.000	0.000	0.000	0.000
62	A	61	ARG	1	0.902	0.946	18.064	0.101	0.101	0.000	0.000	0.000	0.000
63	A	62	ARG	1	0.940	0.986	21.247	0.117	0.117	0.000	0.000	0.000	0.000
64	A	63	ILE	0	0.055	0.024	20.385	0.013	0.013	0.000	0.000	0.000	0.000
65	A	64	ASN	0	-0.003	-0.005	19.581	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	65	ALA	0	-0.018	-0.005	23.619	0.011	0.011	0.000	0.000	0.000	0.000
67	A	66	ILE	0	-0.014	-0.010	26.686	0.009	0.009	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.054	0.023	25.067	0.006	0.006	0.000	0.000	0.000	0.000
69	A	68	ASP	-1	-0.944	-0.968	27.463	-0.051	-0.051	0.000	0.000	0.000	0.000
70	A	69	LYS	1	0.882	0.936	28.990	0.064	0.064	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.018	0.003	29.976	0.005	0.005	0.000	0.000	0.000	0.000
72	A	71	ASN	0	-0.015	-0.013	30.675	0.000	0.000	0.000	0.000	0.000	0.000
73	A	72	ASN	0	-0.012	0.019	31.697	0.003	0.003	0.000	0.000	0.000	0.000
74	A	73	ARG	1	0.853	0.921	34.605	0.052	0.052	0.000	0.000	0.000	0.000
75	A	74	ILE	0	0.045	0.027	36.751	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	75	GLY	0	-0.010	-0.008	39.093	0.003	0.003	0.000	0.000	0.000	0.000
77	A	76	ASN	0	-0.059	-0.040	38.622	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	77	ASN	0	0.025	0.045	34.697	0.006	0.006	0.000	0.000	0.000	0.000
79	A	78	THR	0	-0.005	-0.021	36.270	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	79	MET	0	0.018	0.043	29.230	0.002	0.002	0.000	0.000	0.000	0.000
81	A	80	ARG	1	0.971	0.979	34.889	0.071	0.071	0.000	0.000	0.000	0.000
82	A	81	TYR	0	0.047	0.046	29.323	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	82	PHE	0	-0.057	-0.035	32.381	0.007	0.007	0.000	0.000	0.000	0.000
84	A	83	PRO	0	0.014	0.001	32.481	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	84	ASP	-1	-0.774	-0.874	33.182	-0.085	-0.085	0.000	0.000	0.000	0.000
86	A	85	LEU	0	0.049	0.026	31.312	0.001	0.001	0.000	0.000	0.000	0.000
87	A	86	SER	0	0.026	0.010	33.855	0.004	0.004	0.000	0.000	0.000	0.000
88	A	87	SER	0	-0.083	-0.054	36.263	0.003	0.003	0.000	0.000	0.000	0.000
89	A	88	PHE	0	-0.007	0.006	30.188	0.002	0.002	0.000	0.000	0.000	0.000
90	A	89	GLN	0	0.012	-0.018	34.193	0.004	0.004	0.000	0.000	0.000	0.000
91	A	90	SER	0	-0.095	-0.041	36.596	0.005	0.005	0.000	0.000	0.000	0.000
92	A	91	ILE	0	-0.067	-0.031	36.454	0.003	0.003	0.000	0.000	0.000	0.000
93	A	92	TYR	0	-0.046	-0.030	33.201	0.003	0.003	0.000	0.000	0.000	0.000
94	A	93	THR	0	0.004	-0.005	35.243	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	94	GLU	-1	-0.939	-0.960	34.555	-0.038	-0.038	0.000	0.000	0.000	0.000
96	A	95	GLY	0	-0.024	0.008	31.374	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.840	-0.921	27.691	-0.088	-0.088	0.000	0.000	0.000	0.000
98	A	97	PHE	0	0.029	-0.014	25.346	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	98	ILE	0	0.021	0.002	22.139	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	99	GLU	-1	-0.939	-0.978	24.548	-0.091	-0.091	0.000	0.000	0.000	0.000
101	A	100	TRP	0	-0.041	-0.012	26.539	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.913	0.966	23.909	0.150	0.150	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.048	-0.020	21.122	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	103	TYR	0	-0.077	-0.065	23.484	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	104	GLN	0	0.087	0.047	26.717	0.007	0.007	0.000	0.000	0.000	0.000
106	A	105	SER	0	-0.015	-0.006	21.359	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	106	VAL	0	-0.042	-0.023	22.738	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	107	ALA	0	0.015	-0.006	24.621	0.002	0.002	0.000	0.000	0.000	0.000
109	A	108	ALA	0	0.007	-0.003	25.535	0.005	0.005	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.848	-0.899	20.748	-0.262	-0.262	0.000	0.000	0.000	0.000
111	A	110	LEU	0	0.023	-0.007	24.856	0.004	0.004	0.000	0.000	0.000	0.000
112	A	111	PHE	0	-0.052	-0.015	27.560	0.009	0.009	0.000	0.000	0.000	0.000
113	A	112	ALA	0	-0.024	-0.010	25.786	0.004	0.004	0.000	0.000	0.000	0.000
114	A	113	HIS	0	-0.090	-0.039	22.431	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	114	ASP	-1	-0.928	-0.951	27.755	-0.108	-0.108	0.000	0.000	0.000	0.000
116	A	115	LEU	0	-0.071	-0.038	27.321	0.008	0.008	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.886	-0.959	30.703	-0.084	-0.084	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.937	0.974	33.061	0.080	0.080	0.000	0.000	0.000	0.000
119	A	118	LEU	0	0.021	0.004	31.380	0.001	0.001	0.000	0.000	0.000	0.000
120	A	119	CYS	0	-0.040	-0.009	35.615	0.002	0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)