FMO DATABASE

FMODB ID: K9G53

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

Total energy (hartree)

FMO2-HF: Electronic energy	-930322.711784
FMO2-HF: Nuclear repulsion	882269.64286
FMO2-HF: Total energy	-48053.068924
FMO2-MP2: Total energy	-48190.230647

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.
-1.644	1.013	-0.025	-1.293	-1.339	-0.001

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 : -0.030

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	90	LYS	1	0.851	0.936	3.812	-1.358	1.299	-0.025	-1.293	-1.339	-0.001
4	A	91	LEU	0	0.054	0.041	5.903	0.018	0.018	0.000	0.000	0.000	0.000
5	A	92	ARG	1	0.946	0.985	8.357	0.376	0.376	0.000	0.000	0.000	0.000
6	A	93	ILE	0	0.036	0.035	10.212	0.088	0.088	0.000	0.000	0.000	0.000
7	A	94	GLU	-1	-0.756	-0.860	10.729	0.003	0.003	0.000	0.000	0.000	0.000
8	A	95	ASP	-1	-0.896	-0.953	7.729	0.255	0.255	0.000	0.000	0.000	0.000
9	A	96	ALA	0	-0.113	-0.053	11.280	0.002	0.002	0.000	0.000	0.000	0.000
10	A	97	SER	0	0.045	-0.015	14.331	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	98	HIS	0	-0.024	0.000	12.114	-0.020	-0.020	0.000	0.000	0.000	0.000
12	A	99	ASN	0	-0.036	-0.034	12.249	0.035	0.035	0.000	0.000	0.000	0.000
13	A	100	ALA	0	0.060	0.039	16.159	0.003	0.003	0.000	0.000	0.000	0.000
14	A	101	ARG	1	0.867	0.915	17.789	-0.074	-0.074	0.000	0.000	0.000	0.000
15	A	102	LYS	1	0.804	0.908	14.208	-0.188	-0.188	0.000	0.000	0.000	0.000
16	A	103	LEU	0	-0.052	-0.020	19.920	0.001	0.001	0.000	0.000	0.000	0.000
17	A	104	GLY	0	-0.011	0.011	22.281	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	105	LEU	0	-0.042	-0.017	23.052	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	106	ALA	0	-0.011	-0.021	23.154	0.012	0.012	0.000	0.000	0.000	0.000
20	A	107	PRO	0	-0.005	0.012	19.824	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	108	SER	0	0.014	0.006	22.654	0.008	0.008	0.000	0.000	0.000	0.000
22	A	109	SER	0	0.076	0.012	22.727	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	110	THR	0	0.011	-0.010	23.377	-0.012	-0.012	0.000	0.000	0.000	0.000
24	A	111	ASP	-1	-0.715	-0.828	23.076	-0.020	-0.020	0.000	0.000	0.000	0.000
25	A	112	GLU	-1	-0.820	-0.887	18.669	0.026	0.026	0.000	0.000	0.000	0.000
26	A	113	LYS	1	0.836	0.907	19.945	0.021	0.021	0.000	0.000	0.000	0.000
27	A	114	LYS	1	0.888	0.933	22.419	0.027	0.027	0.000	0.000	0.000	0.000
28	A	115	ILE	0	-0.010	-0.005	18.466	-0.013	-0.013	0.000	0.000	0.000	0.000
29	A	116	ARG	1	0.803	0.881	14.001	0.077	0.077	0.000	0.000	0.000	0.000
30	A	117	ASP	-1	-0.927	-0.955	19.361	-0.142	-0.142	0.000	0.000	0.000	0.000
31	A	118	LEU	0	-0.090	-0.021	22.303	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	119	TYR	0	-0.032	-0.044	18.558	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	120	GLY	0	0.019	0.033	17.088	-0.039	-0.039	0.000	0.000	0.000	0.000
34	A	121	ASP	-1	-0.863	-0.943	12.260	-0.519	-0.519	0.000	0.000	0.000	0.000
35	A	122	SER	0	-0.063	-0.058	10.803	0.002	0.002	0.000	0.000	0.000	0.000
36	A	123	LEU	0	0.029	0.023	12.794	0.037	0.037	0.000	0.000	0.000	0.000
37	A	124	THR	0	0.021	-0.002	13.610	-0.032	-0.032	0.000	0.000	0.000	0.000
38	A	125	TYR	0	-0.003	-0.025	15.935	0.023	0.023	0.000	0.000	0.000	0.000
39	A	126	GLU	-1	-0.896	-0.953	17.332	-0.078	-0.078	0.000	0.000	0.000	0.000
40	A	127	GLN	0	0.055	0.036	17.741	-0.012	-0.012	0.000	0.000	0.000	0.000
41	A	128	TYR	0	-0.051	-0.021	16.214	0.010	0.010	0.000	0.000	0.000	0.000
42	A	129	LEU	0	0.004	-0.002	18.315	0.020	0.020	0.000	0.000	0.000	0.000
43	A	130	GLU	-1	-0.902	-0.943	21.705	-0.050	-0.050	0.000	0.000	0.000	0.000
44	A	131	TYR	0	-0.038	-0.024	17.695	0.003	0.003	0.000	0.000	0.000	0.000
45	A	132	LEU	0	-0.029	-0.018	20.047	0.012	0.012	0.000	0.000	0.000	0.000
46	A	133	THR	0	0.006	-0.005	22.983	0.010	0.010	0.000	0.000	0.000	0.000
47	A	134	MET	0	-0.031	0.000	23.630	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	135	CYS	0	-0.075	-0.043	23.259	0.003	0.003	0.000	0.000	0.000	0.000
49	A	136	VAL	0	-0.036	-0.021	25.833	0.005	0.005	0.000	0.000	0.000	0.000
50	A	137	HIS	0	-0.007	-0.006	28.695	0.003	0.003	0.000	0.000	0.000	0.000
51	A	138	ASP	-1	-0.796	-0.887	28.156	-0.032	-0.032	0.000	0.000	0.000	0.000
52	A	139	ARG	1	0.917	0.964	28.053	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	140	ASP	-1	-0.900	-0.952	31.282	0.002	0.002	0.000	0.000	0.000	0.000
54	A	141	ASN	0	-0.001	0.001	33.556	0.001	0.001	0.000	0.000	0.000	0.000
55	A	142	MET	0	-0.021	-0.002	32.562	0.000	0.000	0.000	0.000	0.000	0.000
56	A	143	GLU	-1	-0.902	-0.966	35.105	0.011	0.011	0.000	0.000	0.000	0.000
57	A	144	GLU	-1	-0.788	-0.881	37.453	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	145	LEU	0	-0.021	-0.016	36.658	0.000	0.000	0.000	0.000	0.000	0.000
59	A	146	ILE	0	0.006	0.010	37.703	0.000	0.000	0.000	0.000	0.000	0.000
60	A	147	LYS	1	0.788	0.906	40.422	0.007	0.007	0.000	0.000	0.000	0.000
61	A	148	MET	0	-0.042	-0.016	43.065	0.000	0.000	0.000	0.000	0.000	0.000
62	A	149	PHE	0	-0.024	-0.036	38.674	0.000	0.000	0.000	0.000	0.000	0.000
63	A	150	SER	0	-0.028	-0.036	43.805	0.001	0.001	0.000	0.000	0.000	0.000
64	A	151	HIS	0	-0.070	-0.012	46.162	0.001	0.001	0.000	0.000	0.000	0.000
65	A	152	PHE	0	-0.028	-0.023	47.560	0.000	0.000	0.000	0.000	0.000	0.000
66	A	153	ASP	-1	-0.752	-0.826	47.449	0.001	0.001	0.000	0.000	0.000	0.000
67	A	154	ASN	0	0.012	-0.001	49.553	0.001	0.001	0.000	0.000	0.000	0.000
68	A	155	ASN	0	-0.094	-0.044	53.246	0.001	0.001	0.000	0.000	0.000	0.000
69	A	156	SER	0	-0.017	-0.015	49.678	0.001	0.001	0.000	0.000	0.000	0.000
70	A	157	SER	0	-0.047	-0.014	49.166	0.001	0.001	0.000	0.000	0.000	0.000
71	A	158	GLY	0	-0.008	-0.010	45.417	0.001	0.001	0.000	0.000	0.000	0.000
72	A	159	PHE	0	-0.061	-0.044	43.879	0.000	0.000	0.000	0.000	0.000	0.000
73	A	160	LEU	0	-0.007	0.005	44.993	0.000	0.000	0.000	0.000	0.000	0.000
74	A	161	THR	0	-0.012	-0.004	45.265	0.000	0.000	0.000	0.000	0.000	0.000
75	A	162	LYS	1	0.953	0.983	40.788	0.019	0.019	0.000	0.000	0.000	0.000
76	A	163	ASN	0	0.006	0.001	44.196	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	164	GLN	0	0.011	0.010	46.778	0.000	0.000	0.000	0.000	0.000	0.000
78	A	165	MET	0	0.024	0.025	41.509	0.000	0.000	0.000	0.000	0.000	0.000
79	A	166	LYS	1	0.885	0.957	42.147	0.024	0.024	0.000	0.000	0.000	0.000
80	A	167	ASN	0	-0.045	-0.018	43.211	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	168	ILE	0	0.009	0.016	42.368	0.000	0.000	0.000	0.000	0.000	0.000
82	A	169	LEU	0	0.015	-0.005	37.499	0.000	0.000	0.000	0.000	0.000	0.000
83	A	170	THR	0	-0.057	-0.031	40.174	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	171	THR	0	-0.072	-0.024	42.291	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	172	TRP	0	-0.029	-0.025	42.922	0.000	0.000	0.000	0.000	0.000	0.000
86	A	173	GLY	0	0.038	0.024	39.111	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	174	ASP	-1	-0.899	-0.938	34.668	-0.030	-0.030	0.000	0.000	0.000	0.000
88	A	175	ALA	0	-0.068	-0.022	36.804	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	176	LEU	0	0.020	0.016	34.300	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	177	THR	0	-0.023	-0.064	37.166	0.002	0.002	0.000	0.000	0.000	0.000
91	A	178	GLU	-1	-0.903	-0.982	39.163	-0.031	-0.031	0.000	0.000	0.000	0.000
92	A	179	GLN	0	-0.073	-0.033	36.201	0.002	0.002	0.000	0.000	0.000	0.000
93	A	180	GLU	-1	-0.775	-0.863	33.736	-0.052	-0.052	0.000	0.000	0.000	0.000
94	A	181	ALA	0	0.002	0.016	35.721	0.002	0.002	0.000	0.000	0.000	0.000
95	A	182	ASN	0	-0.047	-0.055	37.696	0.003	0.003	0.000	0.000	0.000	0.000
96	A	183	ASP	-1	-0.926	-0.936	33.651	-0.049	-0.049	0.000	0.000	0.000	0.000
97	A	184	ALA	0	0.068	0.032	33.719	0.001	0.001	0.000	0.000	0.000	0.000
98	A	185	LEU	0	-0.046	-0.027	34.657	0.004	0.004	0.000	0.000	0.000	0.000
99	A	186	ASN	0	-0.030	-0.035	37.654	0.006	0.006	0.000	0.000	0.000	0.000
100	A	187	ALA	0	-0.017	0.005	32.135	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	188	PHE	0	-0.034	-0.001	33.725	0.002	0.002	0.000	0.000	0.000	0.000
102	A	189	SER	0	-0.036	-0.015	35.300	0.002	0.002	0.000	0.000	0.000	0.000
103	A	190	SER	0	-0.024	-0.008	38.714	0.004	0.004	0.000	0.000	0.000	0.000
104	A	191	GLU	-1	-0.954	-0.967	40.703	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	192	ASP	-1	-0.899	-0.973	42.871	-0.015	-0.015	0.000	0.000	0.000	0.000
106	A	193	ARG	1	0.911	0.950	44.922	0.005	0.005	0.000	0.000	0.000	0.000
107	A	194	ILE	0	0.048	0.016	39.305	0.001	0.001	0.000	0.000	0.000	0.000
108	A	195	ASN	0	0.041	0.017	40.024	0.000	0.000	0.000	0.000	0.000	0.000
109	A	196	TYR	0	-0.010	-0.047	39.209	0.001	0.001	0.000	0.000	0.000	0.000
110	A	197	LYS	1	0.929	0.974	38.379	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	198	LEU	0	0.034	0.018	34.051	0.001	0.001	0.000	0.000	0.000	0.000
112	A	199	PHE	0	-0.022	-0.003	34.375	0.000	0.000	0.000	0.000	0.000	0.000
113	A	200	CYS	0	-0.073	-0.049	33.983	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	201	GLU	-1	-0.960	-0.975	32.067	0.021	0.021	0.000	0.000	0.000	0.000
115	A	202	ASP	-1	-0.869	-0.932	29.749	0.018	0.018	0.000	0.000	0.000	0.000
116	A	203	ILE	0	-0.133	-0.042	28.358	-0.002	-0.002	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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