FMO DATABASE

FMODB ID: 89R3Y

Calculation Name: 1SAU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SAU

Chain ID: A

ChEMBL ID:

UniProt ID: O28055

Base Structure: X-ray

Registration Date: 2023-09-23

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	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1010888.496319
FMO2-HF: Nuclear repulsion	964017.328119
FMO2-HF: Total energy	-46871.1682
FMO2-MP2: Total energy	-47007.534271

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:2:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-10.271	-1.457	5.644	-4.674	-9.784	-0.032

Interaction energy analysis for fragmet #1(A:2:PRO)

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 : -0.012

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	4	LEU	0	0.002	-0.003	3.873	-0.655	1.221	-0.012	-0.968	-0.897	0.000
4	A	5	GLU	-1	-0.868	-0.915	6.263	-0.095	-0.095	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.005	-0.004	9.774	0.067	0.067	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.743	0.846	12.651	0.380	0.380	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.025	0.028	14.801	0.029	0.029	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.782	0.871	13.179	0.403	0.403	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.807	0.874	8.695	-0.084	-0.084	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.003	0.026	8.197	0.024	0.024	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.964	0.984	3.920	0.004	0.169	-0.001	-0.050	-0.115	0.000
12	A	13	LEU	0	-0.035	-0.018	2.373	-0.313	1.359	1.091	-0.759	-2.004	0.000
13	A	14	ASP	-1	-0.808	-0.906	2.521	-7.901	-5.130	1.371	-1.701	-2.441	-0.020
14	A	15	GLU	-1	-0.932	-0.986	2.505	-2.225	-0.836	2.818	-1.194	-3.013	-0.012
15	A	16	ASP	-1	-0.885	-0.923	3.441	-0.034	-0.191	0.008	0.265	-0.116	0.000
16	A	17	GLY	0	0.026	0.010	4.512	0.424	0.483	-0.001	-0.008	-0.049	0.000
17	A	18	PHE	0	-0.089	-0.052	5.393	0.289	0.309	-0.001	-0.001	-0.018	0.000
18	A	19	LEU	0	0.027	0.029	5.929	-0.744	-0.744	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.074	-0.063	5.585	0.861	0.861	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.814	-0.889	8.118	-0.884	-0.884	0.000	0.000	0.000	0.000
21	A	22	TRP	0	-0.016	-0.013	10.189	0.079	0.079	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.862	-0.942	12.770	-0.512	-0.512	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.825	-0.882	12.558	-0.335	-0.335	0.000	0.000	0.000	0.000
24	A	25	TRP	0	-0.040	-0.034	13.375	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.794	-0.901	15.415	-0.348	-0.348	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.908	-0.961	16.622	-0.322	-0.322	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.811	-0.907	17.065	-0.318	-0.318	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.041	-0.007	11.446	-0.037	-0.037	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.023	-0.002	12.576	-0.089	-0.089	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.811	-0.904	14.372	-0.340	-0.340	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.001	0.003	11.145	0.009	0.009	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.012	-0.008	8.246	-0.031	-0.031	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.032	-0.011	10.861	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.812	0.875	13.112	0.364	0.364	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.746	-0.840	6.308	-0.964	-0.964	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.021	-0.020	9.563	-0.056	-0.056	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.706	0.820	4.021	0.713	0.929	0.001	-0.031	-0.186	0.000
38	A	39	PHE	0	-0.027	0.003	2.786	-0.997	-0.194	0.370	-0.227	-0.945	0.000
39	A	40	SER	0	0.045	0.025	8.527	0.012	0.012	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.026	0.002	12.391	0.035	0.035	0.000	0.000	0.000	0.000
41	A	42	GLN	0	-0.039	-0.033	15.186	0.037	0.037	0.000	0.000	0.000	0.000
42	A	43	PRO	0	-0.001	0.021	14.732	-0.033	-0.033	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.016	-0.015	16.071	0.038	0.038	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.936	-0.959	18.109	-0.200	-0.200	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.017	-0.005	17.114	0.006	0.006	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.053	-0.002	21.320	0.019	0.019	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.841	-0.930	24.613	-0.170	-0.170	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.741	-0.848	26.434	-0.171	-0.171	0.000	0.000	0.000	0.000
49	A	50	HIS	0	0.017	0.044	20.706	0.002	0.002	0.000	0.000	0.000	0.000
50	A	51	TRP	0	0.043	0.020	18.942	-0.025	-0.025	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.813	0.900	23.570	0.151	0.151	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.038	-0.009	21.555	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.043	0.016	18.187	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.986	0.998	20.445	0.213	0.213	0.000	0.000	0.000	0.000
55	A	56	TYR	0	0.011	0.016	22.786	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.042	-0.030	17.727	0.009	0.009	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.853	0.930	15.049	0.551	0.551	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.843	-0.923	20.086	-0.231	-0.231	0.000	0.000	0.000	0.000
59	A	60	TYR	0	-0.070	-0.026	22.331	0.030	0.030	0.000	0.000	0.000	0.000
60	A	61	PHE	0	0.002	-0.003	15.722	0.009	0.009	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.015	-0.009	19.067	0.009	0.009	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.791	0.894	21.881	0.243	0.243	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.060	-0.039	23.809	0.024	0.024	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.031	0.034	20.847	0.011	0.011	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.060	-0.023	19.131	-0.024	-0.024	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.069	0.029	17.187	0.002	0.002	0.000	0.000	0.000	0.000
67	A	68	PRO	0	-0.017	0.000	19.215	0.034	0.034	0.000	0.000	0.000	0.000
68	A	69	PRO	0	0.024	0.016	21.717	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.078	0.023	22.298	0.009	0.009	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.938	0.967	24.577	0.174	0.174	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.063	-0.034	26.130	0.022	0.022	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.068	0.041	21.037	0.009	0.009	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.025	0.009	25.691	0.008	0.008	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.881	0.943	28.601	0.151	0.151	0.000	0.000	0.000	0.000
75	A	76	HIS	0	0.007	0.001	26.388	0.019	0.019	0.000	0.000	0.000	0.000
76	A	77	CYS	0	-0.004	0.026	27.621	0.004	0.004	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.868	0.941	29.514	0.131	0.131	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.858	0.930	32.515	0.127	0.127	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.844	-0.925	30.338	-0.146	-0.146	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.045	-0.008	28.117	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.878	0.895	31.577	0.132	0.132	0.000	0.000	0.000	0.000
82	A	83	PRO	0	0.029	0.025	33.832	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.819	-0.883	35.671	-0.115	-0.115	0.000	0.000	0.000	0.000
84	A	86	ASN	0	-0.004	-0.026	30.106	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	87	LEU	0	0.058	0.018	23.965	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	88	GLN	0	0.031	0.016	25.923	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	89	TYR	0	-0.059	-0.067	26.920	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	90	ILE	0	0.015	-0.003	22.363	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	91	TYR	0	-0.020	-0.007	19.638	-0.013	-0.013	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.808	0.922	22.681	0.163	0.163	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.076	-0.020	22.821	0.003	0.003	0.000	0.000	0.000	0.000
92	A	94	PHE	0	0.012	-0.006	17.763	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.040	0.040	17.646	0.000	0.000	0.000	0.000	0.000	0.000
94	A	96	GLN	0	-0.034	-0.042	12.044	0.046	0.046	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.007	-0.004	17.048	0.003	0.003	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.047	-0.035	17.151	-0.040	-0.040	0.000	0.000	0.000	0.000
97	A	99	ALA	0	0.038	0.009	15.799	-0.035	-0.035	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.875	0.920	8.735	0.739	0.739	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.748	-0.856	12.203	-0.578	-0.578	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.010	0.003	14.367	-0.037	-0.037	0.000	0.000	0.000	0.000
101	A	103	CYS	0	-0.051	-0.036	14.414	0.009	0.009	0.000	0.000	0.000	0.000
102	A	104	ARG	1	0.833	0.917	8.347	0.886	0.886	0.000	0.000	0.000	0.000
103	A	105	ILE	0	0.021	0.015	11.487	-0.078	-0.078	0.000	0.000	0.000	0.000
104	A	106	ALA	0	-0.027	-0.011	13.742	0.018	0.018	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.036	0.015	11.789	0.042	0.042	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.032	-0.014	12.819	0.040	0.040	0.000	0.000	0.000	0.000
107	A	109	PRO	0	0.039	0.033	9.842	-0.143	-0.143	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.807	0.884	7.934	1.139	1.139	0.000	0.000	0.000	0.000
109	A	111	PRO	0	0.036	0.034	11.419	0.080	0.080	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.000	-0.016	14.338	0.060	0.060	0.000	0.000	0.000	0.000
111	A	113	GLY	0	0.071	0.034	16.821	0.009	0.009	0.000	0.000	0.000	0.000
112	A	114	CYS	0	-0.067	-0.013	18.091	0.037	0.037	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.014	-0.016	19.937	0.009	0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)