FMO DATABASE

FMODB ID: QYV6Y

Calculation Name: 2AUC-A-Xray372

Preferred Name:

Target Type:

Ligand Name: n-acetyl-serine

ligand 3-letter code: SAC

PDB ID: 2AUC

Chain ID: A

ChEMBL ID:

UniProt ID: Q7RQ71

Base Structure: X-ray

Registration Date: 2023-06-22

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-928834.815921
FMO2-HF: Nuclear repulsion	880782.338553
FMO2-HF: Total energy	-48052.477368
FMO2-MP2: Total energy	-48189.59645

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:88:ASN)

Summations of interaction energy for fragment #1(A:88:ASN)

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.
-0.064	2.676	-0.011	-1.276	-1.454	-0.002

Interaction energy analysis for fragmet #1(A:88:ASN)

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 : -0.032

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	90	LYS	1	0.848	0.933	3.414	1.312	4.052	-0.011	-1.276	-1.454	-0.002
4	A	91	LEU	0	0.050	0.040	5.808	0.143	0.143	0.000	0.000	0.000	0.000
5	A	92	ARG	1	0.963	1.005	8.329	0.635	0.635	0.000	0.000	0.000	0.000
6	A	93	ILE	0	0.021	0.029	10.186	0.082	0.082	0.000	0.000	0.000	0.000
7	A	94	GLU	-1	-0.842	-0.925	10.787	-0.515	-0.515	0.000	0.000	0.000	0.000
8	A	95	ASP	-1	-0.914	-0.959	7.763	-0.513	-0.513	0.000	0.000	0.000	0.000
9	A	96	ALA	0	-0.087	-0.042	11.260	0.063	0.063	0.000	0.000	0.000	0.000
10	A	97	SER	0	0.076	0.024	14.310	0.053	0.053	0.000	0.000	0.000	0.000
11	A	98	HIS	0	-0.034	-0.006	12.734	0.030	0.030	0.000	0.000	0.000	0.000
12	A	99	ASN	0	-0.043	-0.040	12.815	0.058	0.058	0.000	0.000	0.000	0.000
13	A	100	ALA	0	0.052	0.031	16.145	0.028	0.028	0.000	0.000	0.000	0.000
14	A	101	ARG	1	0.930	0.966	17.564	0.203	0.203	0.000	0.000	0.000	0.000
15	A	102	LYS	1	0.861	0.939	14.788	0.080	0.080	0.000	0.000	0.000	0.000
16	A	103	LEU	0	-0.059	-0.022	19.909	0.017	0.017	0.000	0.000	0.000	0.000
17	A	104	GLY	0	-0.007	0.014	22.270	0.008	0.008	0.000	0.000	0.000	0.000
18	A	105	LEU	0	-0.042	-0.019	22.842	0.002	0.002	0.000	0.000	0.000	0.000
19	A	106	ALA	0	-0.016	-0.025	23.140	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	107	PRO	0	-0.002	0.016	19.738	0.004	0.004	0.000	0.000	0.000	0.000
21	A	108	SER	0	0.039	0.048	22.631	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	109	SER	0	0.051	-0.002	22.704	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	110	THR	0	-0.012	-0.019	23.350	-0.020	-0.020	0.000	0.000	0.000	0.000
24	A	111	ASP	-1	-0.760	-0.893	23.045	-0.169	-0.169	0.000	0.000	0.000	0.000
25	A	112	GLU	-1	-0.935	-0.982	18.242	-0.269	-0.269	0.000	0.000	0.000	0.000
26	A	113	LYS	1	0.878	0.934	19.918	0.184	0.184	0.000	0.000	0.000	0.000
27	A	114	LYS	1	0.914	0.949	22.391	0.143	0.143	0.000	0.000	0.000	0.000
28	A	115	ILE	0	0.001	0.005	18.422	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	116	ARG	1	0.884	0.946	13.606	0.478	0.478	0.000	0.000	0.000	0.000
30	A	117	ASP	-1	-0.924	-0.954	19.332	-0.277	-0.277	0.000	0.000	0.000	0.000
31	A	118	LEU	0	-0.095	-0.027	22.297	0.006	0.006	0.000	0.000	0.000	0.000
32	A	119	TYR	0	-0.036	-0.037	18.548	0.012	0.012	0.000	0.000	0.000	0.000
33	A	120	GLY	0	0.013	0.029	16.894	-0.044	-0.044	0.000	0.000	0.000	0.000
34	A	121	ASP	-1	-0.878	-0.967	12.114	-0.772	-0.772	0.000	0.000	0.000	0.000
35	A	122	SER	0	-0.070	-0.052	10.989	-0.069	-0.069	0.000	0.000	0.000	0.000
36	A	123	LEU	0	0.079	0.039	12.767	0.065	0.065	0.000	0.000	0.000	0.000
37	A	124	THR	0	0.019	0.005	13.590	-0.047	-0.047	0.000	0.000	0.000	0.000
38	A	125	TYR	0	-0.013	-0.031	16.000	0.001	0.001	0.000	0.000	0.000	0.000
39	A	126	GLU	-1	-0.885	-0.951	17.316	-0.117	-0.117	0.000	0.000	0.000	0.000
40	A	127	GLN	0	0.053	0.027	17.985	-0.026	-0.026	0.000	0.000	0.000	0.000
41	A	128	TYR	0	-0.050	-0.018	16.209	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	129	LEU	0	0.001	-0.006	18.295	0.015	0.015	0.000	0.000	0.000	0.000
43	A	130	GLU	-1	-0.900	-0.942	21.687	-0.125	-0.125	0.000	0.000	0.000	0.000
44	A	131	TYR	0	-0.027	-0.015	17.478	0.004	0.004	0.000	0.000	0.000	0.000
45	A	132	LEU	0	-0.035	-0.022	19.782	0.011	0.011	0.000	0.000	0.000	0.000
46	A	133	THR	0	0.005	-0.003	22.963	0.016	0.016	0.000	0.000	0.000	0.000
47	A	134	MET	0	-0.054	-0.008	24.035	0.003	0.003	0.000	0.000	0.000	0.000
48	A	135	CYS	0	-0.044	-0.012	22.919	0.003	0.003	0.000	0.000	0.000	0.000
49	A	136	VAL	0	-0.035	-0.022	25.811	0.008	0.008	0.000	0.000	0.000	0.000
50	A	137	HIS	0	-0.009	-0.001	28.674	0.008	0.008	0.000	0.000	0.000	0.000
51	A	138	ASP	-1	-0.770	-0.878	28.102	-0.138	-0.138	0.000	0.000	0.000	0.000
52	A	139	ARG	1	0.896	0.950	27.649	0.096	0.096	0.000	0.000	0.000	0.000
53	A	140	ASP	-1	-0.903	-0.952	31.260	-0.072	-0.072	0.000	0.000	0.000	0.000
54	A	141	ASN	0	0.014	0.008	33.489	0.009	0.009	0.000	0.000	0.000	0.000
55	A	142	MET	0	-0.048	-0.013	32.246	0.006	0.006	0.000	0.000	0.000	0.000
56	A	143	GLU	-1	-0.913	-0.971	35.085	-0.063	-0.063	0.000	0.000	0.000	0.000
57	A	144	GLU	-1	-0.899	-0.961	37.431	-0.060	-0.060	0.000	0.000	0.000	0.000
58	A	145	LEU	0	-0.016	-0.013	36.696	0.004	0.004	0.000	0.000	0.000	0.000
59	A	146	ILE	0	0.007	0.012	37.664	0.003	0.003	0.000	0.000	0.000	0.000
60	A	147	LYS	1	0.920	0.992	40.399	0.058	0.058	0.000	0.000	0.000	0.000
61	A	148	MET	0	-0.059	-0.024	43.049	0.005	0.005	0.000	0.000	0.000	0.000
62	A	149	PHE	0	-0.022	-0.036	38.750	0.002	0.002	0.000	0.000	0.000	0.000
63	A	150	SER	0	-0.027	-0.031	43.782	0.002	0.002	0.000	0.000	0.000	0.000
64	A	151	HIS	0	-0.077	-0.018	46.139	0.004	0.004	0.000	0.000	0.000	0.000
65	A	152	PHE	0	-0.038	-0.028	47.546	0.002	0.002	0.000	0.000	0.000	0.000
66	A	153	ASP	-1	-0.745	-0.826	47.425	-0.053	-0.053	0.000	0.000	0.000	0.000
67	A	154	ASN	0	0.006	-0.005	49.530	0.001	0.001	0.000	0.000	0.000	0.000
68	A	155	ASN	0	-0.105	-0.050	53.052	0.000	0.000	0.000	0.000	0.000	0.000
69	A	156	SER	0	-0.014	-0.009	49.242	0.001	0.001	0.000	0.000	0.000	0.000
70	A	157	SER	0	-0.040	-0.010	49.489	0.000	0.000	0.000	0.000	0.000	0.000
71	A	158	GLY	0	-0.013	-0.012	45.394	0.000	0.000	0.000	0.000	0.000	0.000
72	A	159	PHE	0	-0.058	-0.040	43.803	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	160	LEU	0	0.002	0.009	44.848	0.002	0.002	0.000	0.000	0.000	0.000
74	A	161	THR	0	-0.037	-0.015	45.240	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	162	LYS	1	0.962	0.972	40.781	0.093	0.093	0.000	0.000	0.000	0.000
76	A	163	ASN	0	0.005	0.004	44.170	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	164	GLN	0	0.002	-0.002	46.751	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	165	MET	0	0.039	0.035	41.511	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	166	LYS	1	0.903	0.962	42.119	0.076	0.076	0.000	0.000	0.000	0.000
80	A	167	ASN	0	-0.057	-0.030	43.184	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	168	ILE	0	0.012	0.017	42.416	0.001	0.001	0.000	0.000	0.000	0.000
82	A	169	LEU	0	0.011	-0.010	37.411	0.000	0.000	0.000	0.000	0.000	0.000
83	A	170	THR	0	-0.055	-0.020	40.147	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	171	THR	0	-0.106	-0.033	42.264	0.001	0.001	0.000	0.000	0.000	0.000
85	A	172	TRP	0	-0.001	-0.016	42.897	0.002	0.002	0.000	0.000	0.000	0.000
86	A	173	GLY	0	0.047	0.026	39.084	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	174	ASP	-1	-0.903	-0.943	34.556	-0.097	-0.097	0.000	0.000	0.000	0.000
88	A	175	ALA	0	-0.084	-0.029	36.777	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	176	LEU	0	0.022	0.014	34.153	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	177	THR	0	-0.007	-0.018	37.097	0.007	0.007	0.000	0.000	0.000	0.000
91	A	178	GLU	-1	-0.933	-0.995	39.135	-0.086	-0.086	0.000	0.000	0.000	0.000
92	A	179	GLN	0	-0.054	-0.025	36.107	0.005	0.005	0.000	0.000	0.000	0.000
93	A	180	GLU	-1	-0.823	-0.918	33.613	-0.135	-0.135	0.000	0.000	0.000	0.000
94	A	181	ALA	0	0.008	0.016	35.693	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	182	ASN	0	-0.018	-0.037	37.668	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	183	ASP	-1	-0.912	-0.934	34.248	-0.142	-0.142	0.000	0.000	0.000	0.000
97	A	184	ALA	0	0.035	0.017	33.690	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	185	LEU	0	-0.052	-0.029	34.630	0.002	0.002	0.000	0.000	0.000	0.000
99	A	186	ASN	0	-0.026	-0.037	37.621	0.008	0.008	0.000	0.000	0.000	0.000
100	A	187	ALA	0	-0.011	0.007	32.106	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	188	PHE	0	-0.051	-0.009	33.496	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	189	SER	0	-0.032	0.005	35.275	0.005	0.005	0.000	0.000	0.000	0.000
103	A	190	SER	0	-0.018	-0.008	38.689	0.005	0.005	0.000	0.000	0.000	0.000
104	A	191	GLU	-1	-0.960	-0.971	40.678	-0.067	-0.067	0.000	0.000	0.000	0.000
105	A	192	ASP	-1	-0.927	-0.978	42.846	-0.074	-0.074	0.000	0.000	0.000	0.000
106	A	193	ARG	1	0.921	0.947	44.896	0.058	0.058	0.000	0.000	0.000	0.000
107	A	194	ILE	0	0.058	0.021	39.292	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	195	ASN	0	0.044	0.018	39.876	0.005	0.005	0.000	0.000	0.000	0.000
109	A	196	TYR	0	0.006	-0.038	39.186	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	197	LYS	1	0.941	0.972	38.355	0.056	0.056	0.000	0.000	0.000	0.000
111	A	198	LEU	0	0.044	0.018	34.120	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	199	PHE	0	-0.022	0.002	34.352	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	200	CYS	0	-0.067	-0.046	33.959	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	201	GLU	-1	-0.977	-0.980	32.047	-0.085	-0.085	0.000	0.000	0.000	0.000
115	A	202	ASP	-1	-0.848	-0.918	29.716	-0.116	-0.116	0.000	0.000	0.000	0.000
116	A	203	ILE	0	-0.133	-0.063	28.107	-0.012	-0.012	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:88:ASN)