FMO DATABASE

FMODB ID: 1NMZZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1008072.945732
FMO2-HF: Nuclear repulsion	961202.527762
FMO2-HF: Total energy	-46870.41797
FMO2-MP2: Total energy	-47006.753005

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.
-14.674	-5.999	9.027	-6.744	-10.96	-0.052

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 : -0.038 / q_NPA : -0.030

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	0.013	0.003	3.825	-0.777	1.237	-0.020	-1.027	-0.967	0.001
4	A	5	GLU	-1	-0.887	-0.936	6.199	-0.035	-0.035	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.035	0.010	9.732	0.070	0.070	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.725	0.823	12.525	0.364	0.364	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.012	0.015	14.893	0.020	0.020	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.802	0.889	12.982	0.425	0.425	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.893	0.949	8.537	-0.104	-0.104	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.010	0.027	8.037	0.079	0.079	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.995	0.992	3.961	-0.252	-0.099	-0.001	-0.048	-0.105	0.000
12	A	13	LEU	0	-0.032	-0.017	2.451	-0.466	1.765	0.734	-0.920	-2.046	0.000
13	A	14	ASP	-1	-0.785	-0.889	2.072	-10.080	-9.113	5.097	-3.041	-3.024	-0.036
14	A	15	GLU	-1	-0.923	-0.973	2.411	-3.708	-1.748	2.743	-1.465	-3.238	-0.017
15	A	16	ASP	-1	-0.972	-0.967	3.780	-0.175	-0.145	0.010	0.118	-0.158	0.000
16	A	17	GLY	0	0.022	-0.002	4.066	0.501	0.610	-0.001	-0.024	-0.083	0.000
17	A	18	PHE	0	-0.082	-0.045	5.057	0.354	0.382	-0.001	-0.002	-0.025	0.000
18	A	19	LEU	0	0.014	0.022	6.145	-0.920	-0.920	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.090	-0.091	5.690	0.889	0.889	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.794	-0.871	8.197	-0.711	-0.711	0.000	0.000	0.000	0.000
21	A	22	TRP	0	-0.006	-0.020	10.210	0.078	0.078	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.912	-0.963	12.622	-0.523	-0.523	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.838	-0.907	12.396	-0.366	-0.366	0.000	0.000	0.000	0.000
24	A	25	TRP	0	-0.071	-0.025	13.288	0.037	0.037	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.758	-0.875	14.976	-0.353	-0.353	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.940	-0.975	16.335	-0.322	-0.322	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.821	-0.909	16.703	-0.311	-0.311	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.035	-0.011	11.005	-0.046	-0.046	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.037	-0.011	12.354	-0.087	-0.087	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.806	-0.891	14.105	-0.329	-0.329	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.015	-0.011	10.704	0.016	0.016	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.009	-0.002	8.016	-0.040	-0.040	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.059	-0.029	10.560	0.018	0.018	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.807	0.885	12.958	0.345	0.345	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.759	-0.864	6.159	-0.899	-0.899	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.040	-0.031	9.642	-0.026	-0.026	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.738	0.860	3.834	0.324	0.711	0.015	-0.100	-0.302	0.000
38	A	39	PHE	0	-0.025	0.007	2.711	-1.038	-0.242	0.451	-0.235	-1.012	0.000
39	A	40	SER	0	0.028	0.003	8.616	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.015	0.019	12.392	0.035	0.035	0.000	0.000	0.000	0.000
41	A	42	GLN	0	-0.049	-0.040	15.207	0.035	0.035	0.000	0.000	0.000	0.000
42	A	43	PRO	0	-0.007	0.009	14.496	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	44	ILE	0	0.000	0.002	15.860	0.035	0.035	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.929	-0.955	17.902	-0.190	-0.190	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.026	-0.020	16.931	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.043	0.000	21.081	0.018	0.018	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.897	-0.961	24.410	-0.167	-0.167	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.827	-0.891	26.592	-0.171	-0.171	0.000	0.000	0.000	0.000
49	A	50	HIS	0	0.013	0.024	20.586	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	51	TRP	0	0.058	0.028	18.877	-0.031	-0.031	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.860	0.938	23.247	0.154	0.154	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.038	-0.017	21.208	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.035	0.019	18.317	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.990	0.992	20.688	0.208	0.208	0.000	0.000	0.000	0.000
55	A	56	TYR	0	0.004	0.018	23.165	0.001	0.001	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.032	-0.030	17.910	0.007	0.007	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.863	0.936	15.251	0.569	0.569	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.896	-0.949	20.215	-0.262	-0.262	0.000	0.000	0.000	0.000
59	A	60	TYR	0	-0.105	-0.056	22.774	0.024	0.024	0.000	0.000	0.000	0.000
60	A	61	PHE	0	0.013	0.009	16.104	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.005	0.004	19.188	0.008	0.008	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.851	0.935	22.107	0.235	0.235	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.038	-0.039	24.492	0.026	0.026	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.005	0.019	21.359	0.014	0.014	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.035	-0.009	19.324	-0.025	-0.025	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.051	0.023	17.475	0.009	0.009	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.000	0.010	19.537	0.033	0.033	0.000	0.000	0.000	0.000
68	A	69	PRO	0	0.012	0.005	21.784	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.119	0.031	22.004	0.006	0.006	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.934	0.970	24.293	0.179	0.179	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.063	-0.040	26.199	0.022	0.022	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.081	0.052	20.925	0.010	0.010	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.015	0.012	25.640	0.010	0.010	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.851	0.920	28.399	0.160	0.160	0.000	0.000	0.000	0.000
75	A	76	HIS	0	0.039	0.023	26.916	0.015	0.015	0.000	0.000	0.000	0.000
76	A	77	CYS	0	-0.023	0.018	27.341	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.910	0.951	29.267	0.137	0.137	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.895	0.947	32.686	0.130	0.130	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.866	-0.923	30.435	-0.143	-0.143	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.067	-0.025	27.800	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.883	0.888	31.206	0.132	0.132	0.000	0.000	0.000	0.000
82	A	83	PRO	0	0.022	0.022	33.471	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.847	-0.882	35.187	-0.116	-0.116	0.000	0.000	0.000	0.000
84	A	86	ASN	0	0.030	0.002	30.023	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	87	LEU	0	0.040	0.003	24.261	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	88	GLN	0	0.026	0.015	25.902	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	89	TYR	0	-0.078	-0.079	26.687	0.000	0.000	0.000	0.000	0.000	0.000
88	A	90	ILE	0	0.024	-0.007	22.449	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	91	TYR	0	0.016	0.012	20.341	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.904	0.973	22.448	0.138	0.138	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.064	-0.022	22.795	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	94	PHE	0	0.024	0.011	17.611	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.047	0.040	17.767	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	96	GLN	0	-0.089	-0.071	12.015	0.062	0.062	0.000	0.000	0.000	0.000
95	A	97	GLY	0	-0.004	-0.011	16.914	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.041	-0.032	17.190	-0.040	-0.040	0.000	0.000	0.000	0.000
97	A	99	ALA	0	0.027	0.003	15.582	-0.036	-0.036	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.921	0.952	8.442	0.764	0.764	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.720	-0.839	11.990	-0.562	-0.562	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.008	0.003	14.260	-0.045	-0.045	0.000	0.000	0.000	0.000
101	A	103	CYS	0	-0.061	-0.041	14.507	0.002	0.002	0.000	0.000	0.000	0.000
102	A	104	ARG	1	0.868	0.942	8.144	0.895	0.895	0.000	0.000	0.000	0.000
103	A	105	ILE	0	0.012	0.011	11.676	-0.072	-0.072	0.000	0.000	0.000	0.000
104	A	106	ALA	0	-0.014	0.000	13.641	0.023	0.023	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.037	0.008	12.152	0.052	0.052	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.037	-0.015	13.173	0.028	0.028	0.000	0.000	0.000	0.000
107	A	109	PRO	0	0.037	0.031	10.336	-0.146	-0.146	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.828	0.889	7.886	1.134	1.134	0.000	0.000	0.000	0.000
109	A	111	PRO	0	0.047	0.046	11.292	0.095	0.095	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.019	-0.007	14.280	0.063	0.063	0.000	0.000	0.000	0.000
111	A	113	GLY	0	0.040	0.016	16.767	0.009	0.009	0.000	0.000	0.000	0.000
112	A	114	CYS	0	-0.078	-0.007	17.825	0.039	0.039	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.006	-0.007	19.423	0.000	0.000	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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