FMO DATABASE

FMODB ID: V24J1

Calculation Name: 1S4K-A-Xray315

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	120
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1038883.642594
FMO2-HF: Nuclear repulsion	988427.556674
FMO2-HF: Total energy	-50456.08592
FMO2-MP2: Total energy	-50600.475524

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.
-1.282	-0.147	0.002	-0.527	-0.609	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

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	2	MET	0	0.003	0.020	3.812	-1.300	-0.165	0.002	-0.527	-0.609	0.002
4	A	3	ASN	0	0.005	0.010	5.075	0.752	0.752	0.000	0.000	0.000	0.000
5	A	4	ALA	0	0.083	0.029	7.244	0.091	0.091	0.000	0.000	0.000	0.000
6	A	5	LEU	0	0.031	0.018	10.003	0.075	0.075	0.000	0.000	0.000	0.000
7	A	6	GLU	-1	-0.891	-0.962	5.985	-2.514	-2.514	0.000	0.000	0.000	0.000
8	A	7	LEU	0	-0.020	0.008	10.216	0.098	0.098	0.000	0.000	0.000	0.000
9	A	8	GLN	0	-0.011	-0.009	12.756	0.060	0.060	0.000	0.000	0.000	0.000
10	A	9	ALA	0	-0.012	-0.008	12.755	0.063	0.063	0.000	0.000	0.000	0.000
11	A	10	LEU	0	-0.006	-0.013	12.076	0.057	0.057	0.000	0.000	0.000	0.000
12	A	11	ARG	1	0.795	0.886	15.297	0.342	0.342	0.000	0.000	0.000	0.000
13	A	12	ARG	1	0.929	0.961	17.941	0.338	0.338	0.000	0.000	0.000	0.000
14	A	13	ILE	0	0.004	0.021	16.344	0.026	0.026	0.000	0.000	0.000	0.000
15	A	14	PHE	0	-0.052	-0.028	16.688	0.028	0.028	0.000	0.000	0.000	0.000
16	A	15	ASP	-1	-0.908	-0.947	21.150	-0.156	-0.156	0.000	0.000	0.000	0.000
17	A	16	MET	0	-0.025	0.004	21.635	0.017	0.017	0.000	0.000	0.000	0.000
18	A	17	THR	0	0.012	0.000	22.810	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	18	ILE	0	0.004	-0.011	20.795	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	19	GLU	-1	-0.851	-0.933	22.988	-0.148	-0.148	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.816	-0.911	25.155	-0.143	-0.143	0.000	0.000	0.000	0.000
22	A	21	CYS	0	-0.068	-0.022	20.440	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.042	-0.015	22.426	0.010	0.010	0.000	0.000	0.000	0.000
24	A	23	ILE	0	0.006	0.017	23.930	0.016	0.016	0.000	0.000	0.000	0.000
25	A	24	TYR	0	-0.009	-0.030	24.557	0.015	0.015	0.000	0.000	0.000	0.000
26	A	25	ILE	0	-0.044	-0.015	18.139	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	26	THR	0	-0.075	-0.072	19.313	0.002	0.002	0.000	0.000	0.000	0.000
28	A	27	GLN	0	-0.075	-0.015	21.666	0.017	0.017	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.792	-0.888	23.555	-0.088	-0.088	0.000	0.000	0.000	0.000
30	A	29	ASN	0	-0.062	-0.040	26.420	0.000	0.000	0.000	0.000	0.000	0.000
31	A	30	ASN	0	0.010	0.014	23.545	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	31	SER	0	0.061	0.002	22.982	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	32	ALA	0	0.002	0.014	22.676	-0.016	-0.016	0.000	0.000	0.000	0.000
34	A	33	THR	0	-0.011	-0.021	18.919	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	34	TRP	0	0.026	-0.012	17.334	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	35	GLN	0	0.004	-0.012	17.829	-0.033	-0.033	0.000	0.000	0.000	0.000
37	A	36	ARG	1	0.949	0.990	18.063	0.097	0.097	0.000	0.000	0.000	0.000
38	A	37	TRP	0	-0.025	-0.010	14.035	-0.025	-0.025	0.000	0.000	0.000	0.000
39	A	38	GLU	-1	-0.772	-0.873	13.444	-0.410	-0.410	0.000	0.000	0.000	0.000
40	A	39	ALA	0	-0.005	0.016	15.106	-0.025	-0.025	0.000	0.000	0.000	0.000
41	A	40	GLY	0	-0.028	-0.017	12.565	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	41	ASP	-1	-0.913	-0.942	13.345	-0.166	-0.166	0.000	0.000	0.000	0.000
43	A	42	ILE	0	-0.088	-0.059	14.301	0.048	0.048	0.000	0.000	0.000	0.000
44	A	43	PRO	0	-0.006	0.000	10.286	-0.067	-0.067	0.000	0.000	0.000	0.000
45	A	44	ILE	0	0.026	0.010	9.869	0.070	0.070	0.000	0.000	0.000	0.000
46	A	45	SER	0	0.001	0.011	11.693	0.055	0.055	0.000	0.000	0.000	0.000
47	A	46	PRO	0	0.059	0.001	10.947	-0.060	-0.060	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.886	-0.935	12.255	0.045	0.045	0.000	0.000	0.000	0.000
49	A	48	ILE	0	-0.005	-0.005	14.883	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	49	ILE	0	-0.006	0.000	8.160	-0.059	-0.059	0.000	0.000	0.000	0.000
51	A	50	ALA	0	0.000	0.001	11.754	-0.048	-0.048	0.000	0.000	0.000	0.000
52	A	51	ARG	1	0.956	0.987	12.957	0.069	0.069	0.000	0.000	0.000	0.000
53	A	52	LEU	0	0.022	0.007	12.784	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.902	0.946	5.461	0.681	0.681	0.000	0.000	0.000	0.000
55	A	54	GLU	-1	-0.821	-0.899	12.265	-0.064	-0.064	0.000	0.000	0.000	0.000
56	A	55	MET	0	-0.019	-0.005	15.636	0.014	0.014	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.949	0.981	9.439	0.872	0.872	0.000	0.000	0.000	0.000
58	A	57	ALA	0	0.000	0.006	14.665	0.016	0.016	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.917	0.958	16.021	0.138	0.138	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.821	0.888	17.919	0.294	0.294	0.000	0.000	0.000	0.000
61	A	60	GLN	0	-0.021	-0.011	16.617	-0.020	-0.020	0.000	0.000	0.000	0.000
62	A	61	ARG	1	0.896	0.944	18.065	0.102	0.102	0.000	0.000	0.000	0.000
63	A	62	ARG	1	0.943	0.987	21.247	0.118	0.118	0.000	0.000	0.000	0.000
64	A	63	ILE	0	0.053	0.025	20.386	0.012	0.012	0.000	0.000	0.000	0.000
65	A	64	ASN	0	-0.001	-0.005	19.581	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	65	ALA	0	-0.020	-0.006	23.619	0.012	0.012	0.000	0.000	0.000	0.000
67	A	66	ILE	0	-0.009	-0.008	26.686	0.009	0.009	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.055	0.024	25.067	0.006	0.006	0.000	0.000	0.000	0.000
69	A	68	ASP	-1	-0.949	-0.970	27.463	-0.052	-0.052	0.000	0.000	0.000	0.000
70	A	69	LYS	1	0.882	0.935	28.990	0.065	0.065	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.014	0.006	29.975	0.005	0.005	0.000	0.000	0.000	0.000
72	A	71	ASN	0	-0.015	-0.012	30.674	0.000	0.000	0.000	0.000	0.000	0.000
73	A	72	ASN	0	-0.017	0.016	31.698	0.003	0.003	0.000	0.000	0.000	0.000
74	A	73	ARG	1	0.851	0.920	34.605	0.053	0.053	0.000	0.000	0.000	0.000
75	A	74	ILE	0	0.043	0.025	36.750	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	75	GLY	0	-0.013	-0.010	39.092	0.004	0.004	0.000	0.000	0.000	0.000
77	A	76	ASN	0	-0.061	-0.041	38.622	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	77	ASN	0	0.018	0.041	34.697	0.006	0.006	0.000	0.000	0.000	0.000
79	A	78	THR	0	-0.001	-0.018	36.269	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	79	MET	0	-0.003	0.027	29.217	0.001	0.001	0.000	0.000	0.000	0.000
81	A	80	ARG	1	0.974	0.986	34.877	0.070	0.070	0.000	0.000	0.000	0.000
82	A	81	TYR	0	0.035	0.044	29.322	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	82	PHE	0	-0.041	-0.028	32.382	0.006	0.006	0.000	0.000	0.000	0.000
84	A	83	PRO	0	0.009	-0.002	32.479	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	84	ASP	-1	-0.787	-0.882	33.180	-0.085	-0.085	0.000	0.000	0.000	0.000
86	A	85	LEU	0	0.044	0.023	31.313	0.001	0.001	0.000	0.000	0.000	0.000
87	A	86	SER	0	0.025	0.008	33.856	0.004	0.004	0.000	0.000	0.000	0.000
88	A	87	SER	0	-0.076	-0.050	36.263	0.003	0.003	0.000	0.000	0.000	0.000
89	A	88	PHE	0	0.000	0.011	30.189	0.002	0.002	0.000	0.000	0.000	0.000
90	A	89	GLN	0	-0.007	-0.025	34.194	0.004	0.004	0.000	0.000	0.000	0.000
91	A	90	SER	0	-0.089	-0.040	36.597	0.006	0.006	0.000	0.000	0.000	0.000
92	A	91	ILE	0	-0.058	-0.025	36.460	0.003	0.003	0.000	0.000	0.000	0.000
93	A	92	TYR	0	-0.048	-0.032	33.202	0.003	0.003	0.000	0.000	0.000	0.000
94	A	93	THR	0	-0.001	-0.006	35.245	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	94	GLU	-1	-0.943	-0.963	34.556	-0.037	-0.037	0.000	0.000	0.000	0.000
96	A	95	GLY	0	-0.024	0.008	31.376	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.843	-0.922	27.692	-0.087	-0.087	0.000	0.000	0.000	0.000
98	A	97	PHE	0	0.030	-0.014	25.345	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	98	ILE	0	0.015	-0.001	22.141	-0.013	-0.013	0.000	0.000	0.000	0.000
100	A	99	GLU	-1	-0.940	-0.979	24.549	-0.090	-0.090	0.000	0.000	0.000	0.000
101	A	100	TRP	0	-0.035	-0.010	26.540	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.904	0.963	23.909	0.149	0.149	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.047	-0.022	21.122	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	103	TYR	0	-0.083	-0.068	23.485	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	104	GLN	0	0.090	0.049	26.718	0.006	0.006	0.000	0.000	0.000	0.000
106	A	105	SER	0	-0.020	-0.008	21.358	-0.009	-0.009	0.000	0.000	0.000	0.000
107	A	106	VAL	0	-0.045	-0.026	22.738	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	107	ALA	0	0.021	-0.001	24.621	0.002	0.002	0.000	0.000	0.000	0.000
109	A	108	ALA	0	0.009	-0.001	25.533	0.004	0.004	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.852	-0.902	20.747	-0.265	-0.265	0.000	0.000	0.000	0.000
111	A	110	LEU	0	0.020	-0.009	24.855	0.004	0.004	0.000	0.000	0.000	0.000
112	A	111	PHE	0	-0.042	-0.008	27.559	0.009	0.009	0.000	0.000	0.000	0.000
113	A	112	ALA	0	-0.028	-0.011	25.786	0.004	0.004	0.000	0.000	0.000	0.000
114	A	113	HIS	0	-0.096	-0.043	22.431	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	114	ASP	-1	-0.932	-0.953	27.755	-0.109	-0.109	0.000	0.000	0.000	0.000
116	A	115	LEU	0	-0.076	-0.042	27.319	0.008	0.008	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.888	-0.961	30.703	-0.085	-0.085	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.923	0.964	33.060	0.081	0.081	0.000	0.000	0.000	0.000
119	A	118	LEU	0	-0.002	-0.013	31.379	0.000	0.000	0.000	0.000	0.000	0.000
120	A	119	CYS	-1	-0.914	-0.945	35.614	-0.076	-0.076	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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