FMO DATABASE

FMODB ID: G5J91

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	OptHSide
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	-1009088.774251
FMO2-HF: Nuclear repulsion	962217.787665
FMO2-HF: Total energy	-46870.986586
FMO2-MP2: Total energy	-47007.370331

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.
-14.506	-6.26	10.127	-6.892	-11.481	-0.049

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 : -0.032 / q_NPA : -0.027

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	0.010	0.007	3.825	-1.007	1.178	-0.019	-1.137	-1.029	0.001
4	A	5	GLU	-1	-0.870	-0.915	6.174	-0.031	-0.031	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.027	0.004	9.657	0.068	0.068	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.747	0.838	12.512	0.374	0.374	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.013	0.015	14.811	0.019	0.019	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.774	0.872	12.878	0.420	0.420	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.778	0.862	8.607	-0.161	-0.161	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.005	0.022	8.070	0.064	0.064	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.976	0.976	4.085	-0.305	-0.168	-0.001	-0.045	-0.091	0.000
12	A	13	LEU	0	-0.030	-0.011	2.348	-0.243	1.796	0.908	-0.890	-2.056	0.002
13	A	14	ASP	-1	-0.796	-0.896	2.073	-10.374	-9.348	5.224	-3.073	-3.177	-0.037
14	A	15	GLU	-1	-0.925	-0.975	2.432	-3.293	-1.611	3.088	-1.470	-3.300	-0.015
15	A	16	ASP	-1	-0.896	-0.929	3.636	-0.046	-0.071	0.009	0.180	-0.164	0.000
16	A	17	GLY	0	0.019	0.011	4.101	0.478	0.588	-0.001	-0.025	-0.085	0.000
17	A	18	PHE	0	-0.066	-0.037	5.008	0.330	0.356	-0.001	-0.002	-0.023	0.000
18	A	19	LEU	0	0.008	0.024	5.917	-0.927	-0.927	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.069	-0.078	5.600	0.904	0.904	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.782	-0.863	8.194	-0.839	-0.839	0.000	0.000	0.000	0.000
21	A	22	TRP	0	0.007	-0.009	10.206	0.079	0.079	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.911	-0.962	12.623	-0.519	-0.519	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.798	-0.885	12.388	-0.355	-0.355	0.000	0.000	0.000	0.000
24	A	25	TRP	0	-0.068	-0.026	13.330	0.041	0.041	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.777	-0.887	15.126	-0.351	-0.351	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.934	-0.973	16.498	-0.327	-0.327	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.815	-0.900	16.628	-0.306	-0.306	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.042	-0.012	11.143	-0.043	-0.043	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.035	-0.011	12.462	-0.085	-0.085	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.803	-0.891	14.203	-0.328	-0.328	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.012	-0.008	10.733	0.017	0.017	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.007	-0.001	8.182	-0.041	-0.041	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.055	-0.027	10.642	0.018	0.018	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.816	0.888	12.931	0.351	0.351	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.756	-0.847	6.115	-0.891	-0.891	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.030	-0.027	9.573	-0.025	-0.025	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.719	0.828	3.667	0.410	0.799	0.014	-0.098	-0.305	0.000
38	A	39	PHE	0	-0.021	-0.001	2.466	-1.060	-0.383	0.906	-0.332	-1.251	0.000
39	A	40	SER	0	0.035	0.011	8.384	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.017	0.013	12.179	0.036	0.036	0.000	0.000	0.000	0.000
41	A	42	GLN	0	-0.052	-0.036	15.041	0.034	0.034	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.003	0.015	14.302	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.013	-0.008	15.806	0.035	0.035	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.922	-0.951	17.899	-0.189	-0.189	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.023	-0.012	17.004	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.048	-0.010	21.146	0.018	0.018	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.845	-0.932	24.516	-0.170	-0.170	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.776	-0.870	26.465	-0.171	-0.171	0.000	0.000	0.000	0.000
49	A	50	HIS	0	0.010	0.033	20.638	0.000	0.000	0.000	0.000	0.000	0.000
50	A	51	TRP	0	0.058	0.026	18.885	-0.032	-0.032	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.817	0.911	23.369	0.152	0.152	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.039	-0.026	21.254	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.039	0.025	18.101	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.988	0.994	20.505	0.212	0.212	0.000	0.000	0.000	0.000
55	A	56	TYR	0	0.007	0.015	22.962	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.035	-0.029	17.612	0.007	0.007	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.851	0.925	14.930	0.579	0.579	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.886	-0.942	19.991	-0.259	-0.259	0.000	0.000	0.000	0.000
59	A	60	TYR	0	-0.106	-0.056	22.556	0.029	0.029	0.000	0.000	0.000	0.000
60	A	61	PHE	0	0.016	0.005	16.023	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.001	0.006	19.184	0.007	0.007	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.829	0.925	22.063	0.246	0.246	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.029	-0.029	24.279	0.022	0.022	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.005	0.018	21.359	0.014	0.014	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.043	-0.017	19.176	-0.025	-0.025	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.063	0.030	17.355	0.010	0.010	0.000	0.000	0.000	0.000
67	A	68	PRO	0	-0.006	0.008	19.410	0.032	0.032	0.000	0.000	0.000	0.000
68	A	69	PRO	0	0.025	0.008	21.701	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.106	0.028	21.973	0.006	0.006	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.942	0.973	24.252	0.179	0.179	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.046	-0.030	26.130	0.021	0.021	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.072	0.049	20.862	0.009	0.009	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.011	0.007	25.544	0.010	0.010	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.871	0.934	28.330	0.157	0.157	0.000	0.000	0.000	0.000
75	A	76	HIS	0	0.020	0.009	26.508	0.017	0.017	0.000	0.000	0.000	0.000
76	A	77	CYS	0	-0.007	0.023	27.289	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.883	0.940	29.162	0.134	0.134	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.897	0.948	32.584	0.128	0.128	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.869	-0.925	30.334	-0.146	-0.146	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.063	-0.019	27.637	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.873	0.898	31.086	0.133	0.133	0.000	0.000	0.000	0.000
82	A	83	PRO	0	0.040	0.029	33.388	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.842	-0.895	35.199	-0.117	-0.117	0.000	0.000	0.000	0.000
84	A	86	ASN	0	0.001	-0.016	29.955	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	87	LEU	0	0.050	0.010	24.101	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	88	GLN	0	0.029	0.014	25.919	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	89	TYR	0	-0.062	-0.067	26.705	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	90	ILE	0	0.018	-0.008	22.266	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	91	TYR	0	0.014	0.021	20.087	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.862	0.957	22.471	0.161	0.161	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.095	-0.041	22.762	0.000	0.000	0.000	0.000	0.000	0.000
92	A	94	PHE	0	0.033	0.013	17.505	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.049	0.046	17.694	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	96	GLN	0	-0.076	-0.063	11.890	0.056	0.056	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.000	-0.014	16.983	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.042	-0.033	17.182	-0.039	-0.039	0.000	0.000	0.000	0.000
97	A	99	ALA	0	0.023	0.004	15.611	-0.036	-0.036	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.855	0.900	8.504	0.780	0.780	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.720	-0.839	11.978	-0.569	-0.569	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.014	0.003	14.167	-0.044	-0.044	0.000	0.000	0.000	0.000
101	A	103	CYS	0	-0.063	-0.046	14.289	0.004	0.004	0.000	0.000	0.000	0.000
102	A	104	ARG	1	0.857	0.930	8.097	0.877	0.877	0.000	0.000	0.000	0.000
103	A	105	ILE	0	0.008	0.010	11.504	-0.072	-0.072	0.000	0.000	0.000	0.000
104	A	106	ALA	0	-0.014	0.002	13.540	0.022	0.022	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.036	0.010	11.899	0.051	0.051	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.036	-0.013	12.924	0.024	0.024	0.000	0.000	0.000	0.000
107	A	109	PRO	0	0.031	0.026	10.123	-0.142	-0.142	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.807	0.879	7.890	1.211	1.211	0.000	0.000	0.000	0.000
109	A	111	PRO	0	0.034	0.040	11.255	0.092	0.092	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.018	-0.006	14.228	0.064	0.064	0.000	0.000	0.000	0.000
111	A	113	GLY	0	0.035	0.013	16.729	0.008	0.008	0.000	0.000	0.000	0.000
112	A	114	CYS	0	-0.083	-0.014	17.862	0.039	0.039	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.007	-0.004	19.423	0.000	0.000	0.000	0.000	0.000	0.000

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