FMO DATABASE

FMODB ID: 53VMZ

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	OptAll
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	-1043792.873704
FMO2-HF: Nuclear repulsion	993335.366622
FMO2-HF: Total energy	-50457.507083
FMO2-MP2: Total energy	-50601.829888

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.
-0.929	0.528	0.018	-0.721	-0.754	0.001

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 : 0.007 / q_NPA : -0.006

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	-0.016	0.012	3.498	-1.590	-0.133	0.018	-0.721	-0.754	0.001
4	A	3	ASN	0	-0.006	-0.018	5.281	0.669	0.669	0.000	0.000	0.000	0.000
5	A	4	ALA	0	0.078	0.038	7.101	0.063	0.063	0.000	0.000	0.000	0.000
6	A	5	LEU	0	0.025	0.008	9.830	0.062	0.062	0.000	0.000	0.000	0.000
7	A	6	GLU	-1	-0.866	-0.933	5.812	-1.983	-1.983	0.000	0.000	0.000	0.000
8	A	7	LEU	0	-0.020	0.002	10.109	0.070	0.070	0.000	0.000	0.000	0.000
9	A	8	GLN	0	0.002	0.009	12.504	0.072	0.072	0.000	0.000	0.000	0.000
10	A	9	ALA	0	-0.023	-0.007	12.576	0.045	0.045	0.000	0.000	0.000	0.000
11	A	10	LEU	0	-0.011	-0.022	10.786	0.030	0.030	0.000	0.000	0.000	0.000
12	A	11	ARG	1	0.797	0.853	14.828	0.276	0.276	0.000	0.000	0.000	0.000
13	A	12	ARG	1	0.882	0.936	17.693	0.300	0.300	0.000	0.000	0.000	0.000
14	A	13	ILE	0	-0.003	0.010	15.906	0.024	0.024	0.000	0.000	0.000	0.000
15	A	14	PHE	0	-0.035	-0.010	15.901	0.018	0.018	0.000	0.000	0.000	0.000
16	A	15	ASP	-1	-0.837	-0.908	20.588	-0.134	-0.134	0.000	0.000	0.000	0.000
17	A	16	MET	0	-0.028	0.010	21.371	0.014	0.014	0.000	0.000	0.000	0.000
18	A	17	THR	0	0.015	-0.022	22.359	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	18	ILE	0	-0.016	-0.015	20.318	-0.011	-0.011	0.000	0.000	0.000	0.000
20	A	19	GLU	-1	-0.781	-0.872	22.460	-0.127	-0.127	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.761	-0.858	24.822	-0.131	-0.131	0.000	0.000	0.000	0.000
22	A	21	CYS	0	-0.072	-0.025	19.786	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.004	-0.003	21.451	0.005	0.005	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.012	0.012	23.312	0.013	0.013	0.000	0.000	0.000	0.000
25	A	24	TYR	0	-0.026	-0.023	24.171	0.012	0.012	0.000	0.000	0.000	0.000
26	A	25	ILE	0	-0.063	-0.028	17.671	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	26	THR	0	-0.042	-0.072	19.128	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	27	GLN	0	-0.058	-0.007	21.301	0.015	0.015	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.760	-0.863	23.454	-0.075	-0.075	0.000	0.000	0.000	0.000
30	A	29	ASN	0	-0.035	-0.029	25.833	0.004	0.004	0.000	0.000	0.000	0.000
31	A	30	ASN	0	0.006	0.038	23.138	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	31	SER	0	-0.017	-0.064	22.658	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	32	ALA	0	0.019	0.021	22.225	-0.014	-0.014	0.000	0.000	0.000	0.000
34	A	33	THR	0	-0.022	-0.030	18.615	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	34	TRP	0	0.035	-0.006	16.806	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	35	GLN	0	-0.005	-0.012	17.438	-0.025	-0.025	0.000	0.000	0.000	0.000
37	A	36	ARG	1	0.850	0.912	18.127	0.063	0.063	0.000	0.000	0.000	0.000
38	A	37	TRP	0	-0.011	-0.002	13.600	-0.021	-0.021	0.000	0.000	0.000	0.000
39	A	38	GLU	-1	-0.756	-0.851	13.283	-0.334	-0.334	0.000	0.000	0.000	0.000
40	A	39	ALA	0	-0.012	0.003	15.073	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	40	GLY	0	-0.030	-0.020	12.365	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	41	ASP	-1	-0.871	-0.901	13.141	-0.073	-0.073	0.000	0.000	0.000	0.000
43	A	42	ILE	0	-0.016	-0.014	14.500	0.043	0.043	0.000	0.000	0.000	0.000
44	A	43	PRO	0	-0.010	0.003	10.059	-0.067	-0.067	0.000	0.000	0.000	0.000
45	A	44	ILE	0	0.025	0.002	9.414	0.059	0.059	0.000	0.000	0.000	0.000
46	A	45	SER	0	0.019	0.019	11.346	0.050	0.050	0.000	0.000	0.000	0.000
47	A	46	PRO	0	0.038	-0.002	10.751	-0.067	-0.067	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.806	-0.877	12.027	-0.044	-0.044	0.000	0.000	0.000	0.000
49	A	48	ILE	0	-0.004	-0.005	14.568	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	49	ILE	0	0.002	-0.004	7.733	-0.085	-0.085	0.000	0.000	0.000	0.000
51	A	50	ALA	0	-0.020	-0.006	11.352	-0.064	-0.064	0.000	0.000	0.000	0.000
52	A	51	ARG	1	0.824	0.909	13.035	0.061	0.061	0.000	0.000	0.000	0.000
53	A	52	LEU	0	0.047	0.016	12.592	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.904	0.956	5.476	0.835	0.835	0.000	0.000	0.000	0.000
55	A	54	GLU	-1	-0.719	-0.825	12.191	-0.125	-0.125	0.000	0.000	0.000	0.000
56	A	55	MET	0	-0.033	-0.002	15.684	0.016	0.016	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.941	0.973	8.674	0.980	0.980	0.000	0.000	0.000	0.000
58	A	57	ALA	0	-0.005	0.007	14.805	0.019	0.019	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.888	0.945	16.271	0.150	0.150	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.802	0.878	17.612	0.288	0.288	0.000	0.000	0.000	0.000
61	A	60	GLN	0	-0.003	-0.007	16.802	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	61	ARG	1	0.803	0.856	18.151	0.150	0.150	0.000	0.000	0.000	0.000
63	A	62	ARG	1	0.943	0.983	21.213	0.126	0.126	0.000	0.000	0.000	0.000
64	A	63	ILE	0	0.053	0.029	19.790	0.012	0.012	0.000	0.000	0.000	0.000
65	A	64	ASN	0	-0.002	0.001	20.046	0.000	0.000	0.000	0.000	0.000	0.000
66	A	65	ALA	0	-0.003	0.006	23.768	0.012	0.012	0.000	0.000	0.000	0.000
67	A	66	ILE	0	0.025	0.018	26.653	0.012	0.012	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.047	0.014	25.129	0.008	0.008	0.000	0.000	0.000	0.000
69	A	68	ASP	-1	-0.849	-0.904	27.721	-0.067	-0.067	0.000	0.000	0.000	0.000
70	A	69	LYS	1	0.757	0.849	29.358	0.084	0.084	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.022	0.005	29.669	0.005	0.005	0.000	0.000	0.000	0.000
72	A	71	ASN	0	-0.002	-0.017	29.964	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	72	ASN	0	-0.086	-0.018	31.520	0.007	0.007	0.000	0.000	0.000	0.000
74	A	73	ARG	1	0.904	0.944	34.779	0.059	0.059	0.000	0.000	0.000	0.000
75	A	74	ILE	0	0.038	0.019	37.020	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	75	GLY	0	0.000	-0.003	39.115	0.004	0.004	0.000	0.000	0.000	0.000
77	A	76	ASN	0	-0.031	-0.014	38.751	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	77	ASN	0	0.005	0.020	34.010	0.006	0.006	0.000	0.000	0.000	0.000
79	A	78	THR	0	-0.048	-0.041	36.038	0.000	0.000	0.000	0.000	0.000	0.000
80	A	79	MET	0	-0.010	0.039	29.071	0.001	0.001	0.000	0.000	0.000	0.000
81	A	80	ARG	1	0.919	0.947	34.749	0.072	0.072	0.000	0.000	0.000	0.000
82	A	81	TYR	0	0.035	0.030	28.947	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	82	PHE	0	-0.031	-0.017	31.713	0.007	0.007	0.000	0.000	0.000	0.000
84	A	83	PRO	0	0.031	0.016	32.014	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	84	ASP	-1	-0.801	-0.864	32.989	-0.077	-0.077	0.000	0.000	0.000	0.000
86	A	85	LEU	0	0.042	0.036	30.784	0.000	0.000	0.000	0.000	0.000	0.000
87	A	86	SER	0	0.031	-0.010	33.310	0.003	0.003	0.000	0.000	0.000	0.000
88	A	87	SER	0	-0.066	-0.050	35.281	0.002	0.002	0.000	0.000	0.000	0.000
89	A	88	PHE	0	-0.005	0.005	29.896	0.001	0.001	0.000	0.000	0.000	0.000
90	A	89	GLN	0	0.023	-0.006	33.818	0.004	0.004	0.000	0.000	0.000	0.000
91	A	90	SER	0	-0.086	-0.055	36.372	0.005	0.005	0.000	0.000	0.000	0.000
92	A	91	ILE	0	-0.077	-0.037	36.352	0.003	0.003	0.000	0.000	0.000	0.000
93	A	92	TYR	0	-0.031	-0.025	32.192	0.001	0.001	0.000	0.000	0.000	0.000
94	A	93	THR	0	-0.021	-0.035	34.953	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	94	GLU	-1	-0.899	-0.920	34.646	-0.043	-0.043	0.000	0.000	0.000	0.000
96	A	95	GLY	0	-0.011	0.012	31.586	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.849	-0.930	26.968	-0.100	-0.100	0.000	0.000	0.000	0.000
98	A	97	PHE	0	0.035	-0.009	24.575	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	98	ILE	0	0.010	0.000	21.780	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	99	GLU	-1	-0.951	-0.980	24.243	-0.101	-0.101	0.000	0.000	0.000	0.000
101	A	100	TRP	0	-0.038	-0.005	26.391	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.836	0.910	23.622	0.139	0.139	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.048	-0.025	20.731	-0.015	-0.015	0.000	0.000	0.000	0.000
104	A	103	TYR	0	-0.061	-0.054	23.170	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	104	GLN	0	0.051	0.024	26.411	0.004	0.004	0.000	0.000	0.000	0.000
106	A	105	SER	0	-0.011	-0.019	20.796	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	106	VAL	0	-0.041	-0.021	22.239	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	107	ALA	0	0.016	-0.003	24.127	0.002	0.002	0.000	0.000	0.000	0.000
109	A	108	ALA	0	0.022	0.004	25.316	0.005	0.005	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.835	-0.883	20.008	-0.263	-0.263	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.001	-0.004	24.328	0.003	0.003	0.000	0.000	0.000	0.000
112	A	111	PHE	0	-0.011	-0.007	26.952	0.007	0.007	0.000	0.000	0.000	0.000
113	A	112	ALA	0	-0.029	-0.010	25.321	0.005	0.005	0.000	0.000	0.000	0.000
114	A	113	HIS	0	-0.094	-0.052	22.269	-0.012	-0.012	0.000	0.000	0.000	0.000
115	A	114	ASP	-1	-0.940	-0.967	27.674	-0.100	-0.100	0.000	0.000	0.000	0.000
116	A	115	LEU	0	-0.058	-0.021	26.729	0.007	0.007	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.833	-0.946	30.468	-0.085	-0.085	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.898	0.954	32.489	0.081	0.081	0.000	0.000	0.000	0.000
119	A	118	LEU	0	0.019	0.026	30.709	0.002	0.002	0.000	0.000	0.000	0.000
120	A	119	CYS	0	-0.023	0.002	34.803	0.003	0.003	0.000	0.000	0.000	0.000

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