FMO DATABASE

FMODB ID: 49JZN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-935129.037766
FMO2-HF: Nuclear repulsion	887075.709211
FMO2-HF: Total energy	-48053.328554
FMO2-MP2: Total energy	-48190.503351

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.
-2.97	-0.384	0.065	-1.29	-1.361	0.005

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 : 0.003 / q_NPA : -0.021

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	0.835	0.925	3.411	-2.859	-0.273	0.065	-1.290	-1.361	0.005
4	A	91	LEU	0	0.067	0.053	5.831	-0.163	-0.163	0.000	0.000	0.000	0.000
5	A	92	ARG	1	0.911	0.952	7.674	0.163	0.163	0.000	0.000	0.000	0.000
6	A	93	ILE	0	0.038	0.047	10.171	0.031	0.031	0.000	0.000	0.000	0.000
7	A	94	GLU	-1	-0.773	-0.868	10.644	0.271	0.271	0.000	0.000	0.000	0.000
8	A	95	ASP	-1	-0.872	-0.953	8.006	0.467	0.467	0.000	0.000	0.000	0.000
9	A	96	ALA	0	-0.072	-0.013	11.317	-0.021	-0.021	0.000	0.000	0.000	0.000
10	A	97	SER	0	0.041	-0.008	14.454	-0.022	-0.022	0.000	0.000	0.000	0.000
11	A	98	HIS	0	-0.024	-0.002	11.698	-0.045	-0.045	0.000	0.000	0.000	0.000
12	A	99	ASN	0	-0.053	-0.044	12.156	0.010	0.010	0.000	0.000	0.000	0.000
13	A	100	ALA	0	0.077	0.043	16.108	-0.010	-0.010	0.000	0.000	0.000	0.000
14	A	101	ARG	1	0.779	0.863	17.666	-0.212	-0.212	0.000	0.000	0.000	0.000
15	A	102	LYS	1	0.800	0.892	14.008	-0.355	-0.355	0.000	0.000	0.000	0.000
16	A	103	LEU	0	-0.045	-0.013	19.702	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	104	GLY	0	-0.021	0.002	22.329	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	105	LEU	0	-0.022	-0.006	22.932	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	106	ALA	0	-0.030	-0.029	23.286	0.018	0.018	0.000	0.000	0.000	0.000
20	A	107	PRO	0	0.002	0.005	19.818	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	108	SER	0	0.054	0.026	22.732	0.017	0.017	0.000	0.000	0.000	0.000
22	A	109	SER	0	0.044	0.008	22.584	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	110	THR	0	0.006	-0.003	23.207	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	111	ASP	-1	-0.721	-0.801	22.604	0.056	0.056	0.000	0.000	0.000	0.000
25	A	112	GLU	-1	-0.770	-0.852	17.790	0.189	0.189	0.000	0.000	0.000	0.000
26	A	113	LYS	1	0.805	0.907	19.347	-0.065	-0.065	0.000	0.000	0.000	0.000
27	A	114	LYS	1	0.928	0.934	21.762	-0.031	-0.031	0.000	0.000	0.000	0.000
28	A	115	ILE	0	-0.011	-0.010	18.197	-0.017	-0.017	0.000	0.000	0.000	0.000
29	A	116	ARG	1	0.786	0.876	14.074	-0.133	-0.133	0.000	0.000	0.000	0.000
30	A	117	ASP	-1	-0.930	-0.970	19.251	-0.054	-0.054	0.000	0.000	0.000	0.000
31	A	118	LEU	0	-0.060	-0.014	22.306	-0.015	-0.015	0.000	0.000	0.000	0.000
32	A	119	TYR	0	-0.015	-0.025	18.686	-0.022	-0.022	0.000	0.000	0.000	0.000
33	A	120	GLY	0	0.014	0.029	17.191	-0.045	-0.045	0.000	0.000	0.000	0.000
34	A	121	ASP	-1	-0.867	-0.937	11.962	-0.341	-0.341	0.000	0.000	0.000	0.000
35	A	122	SER	0	-0.072	-0.074	11.166	0.046	0.046	0.000	0.000	0.000	0.000
36	A	123	LEU	0	0.029	0.020	13.077	0.020	0.020	0.000	0.000	0.000	0.000
37	A	124	THR	0	0.020	-0.003	14.059	-0.024	-0.024	0.000	0.000	0.000	0.000
38	A	125	TYR	0	-0.001	-0.019	16.367	0.038	0.038	0.000	0.000	0.000	0.000
39	A	126	GLU	-1	-0.914	-0.954	17.737	-0.098	-0.098	0.000	0.000	0.000	0.000
40	A	127	GLN	0	0.054	0.036	17.921	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	128	TYR	0	-0.020	-0.001	16.441	0.024	0.024	0.000	0.000	0.000	0.000
42	A	129	LEU	0	-0.004	-0.007	18.514	0.023	0.023	0.000	0.000	0.000	0.000
43	A	130	GLU	-1	-0.906	-0.941	22.028	-0.025	-0.025	0.000	0.000	0.000	0.000
44	A	131	TYR	0	-0.035	-0.034	17.649	0.004	0.004	0.000	0.000	0.000	0.000
45	A	132	LEU	0	-0.029	-0.021	20.185	0.014	0.014	0.000	0.000	0.000	0.000
46	A	133	THR	0	0.005	-0.012	22.884	0.008	0.008	0.000	0.000	0.000	0.000
47	A	134	MET	0	-0.026	0.000	23.123	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	135	CYS	0	-0.070	-0.044	23.010	0.005	0.005	0.000	0.000	0.000	0.000
49	A	136	VAL	0	-0.059	-0.019	25.633	0.007	0.007	0.000	0.000	0.000	0.000
50	A	137	HIS	0	-0.004	-0.007	28.632	0.001	0.001	0.000	0.000	0.000	0.000
51	A	138	ASP	-1	-0.788	-0.887	28.011	0.023	0.023	0.000	0.000	0.000	0.000
52	A	139	ARG	1	0.929	0.974	28.221	-0.077	-0.077	0.000	0.000	0.000	0.000
53	A	140	ASP	-1	-0.889	-0.951	30.992	0.042	0.042	0.000	0.000	0.000	0.000
54	A	141	ASN	0	0.012	0.008	33.429	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	142	MET	0	-0.038	0.000	32.557	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	143	GLU	-1	-0.894	-0.955	34.733	0.051	0.051	0.000	0.000	0.000	0.000
57	A	144	GLU	-1	-0.781	-0.882	37.215	0.020	0.020	0.000	0.000	0.000	0.000
58	A	145	LEU	0	-0.003	-0.004	36.040	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	146	ILE	0	0.020	0.012	37.430	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	147	LYS	1	0.755	0.893	39.946	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	148	MET	0	-0.039	-0.018	42.538	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	149	PHE	0	-0.017	-0.026	38.343	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	150	SER	0	-0.019	-0.041	43.334	0.001	0.001	0.000	0.000	0.000	0.000
64	A	151	HIS	0	-0.077	-0.020	45.721	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	152	PHE	0	-0.019	-0.009	47.428	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	153	ASP	-1	-0.758	-0.831	47.077	0.035	0.035	0.000	0.000	0.000	0.000
67	A	154	ASN	0	-0.025	-0.026	49.203	0.001	0.001	0.000	0.000	0.000	0.000
68	A	155	ASN	0	-0.063	-0.030	52.468	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	156	SER	0	-0.036	-0.018	49.170	0.001	0.001	0.000	0.000	0.000	0.000
70	A	157	SER	0	-0.048	-0.016	48.854	0.001	0.001	0.000	0.000	0.000	0.000
71	A	158	GLY	0	0.003	-0.003	45.023	0.002	0.002	0.000	0.000	0.000	0.000
72	A	159	PHE	0	-0.050	-0.038	43.371	0.002	0.002	0.000	0.000	0.000	0.000
73	A	160	LEU	0	-0.014	0.006	44.472	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	161	THR	0	-0.020	-0.013	44.717	0.001	0.001	0.000	0.000	0.000	0.000
75	A	162	LYS	1	0.901	0.956	40.069	-0.028	-0.028	0.000	0.000	0.000	0.000
76	A	163	ASN	0	-0.010	-0.008	43.581	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	164	GLN	0	0.002	0.006	46.275	0.000	0.000	0.000	0.000	0.000	0.000
78	A	165	MET	0	0.008	0.015	40.968	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	166	LYS	1	0.895	0.960	41.697	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	167	ASN	0	-0.016	-0.001	42.757	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	168	ILE	0	0.013	0.013	41.923	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	169	LEU	0	0.014	-0.003	37.093	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	170	THR	0	-0.050	-0.024	39.677	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	171	THR	0	-0.077	-0.035	42.145	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	172	TRP	0	-0.039	-0.025	42.491	0.000	0.000	0.000	0.000	0.000	0.000
86	A	173	GLY	0	0.067	0.036	38.637	0.001	0.001	0.000	0.000	0.000	0.000
87	A	174	ASP	-1	-0.911	-0.950	34.192	0.004	0.004	0.000	0.000	0.000	0.000
88	A	175	ALA	0	-0.080	-0.030	36.551	0.001	0.001	0.000	0.000	0.000	0.000
89	A	176	LEU	0	0.019	0.017	34.067	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	177	THR	0	-0.036	-0.070	36.749	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	178	GLU	-1	-0.895	-0.975	38.896	0.001	0.001	0.000	0.000	0.000	0.000
92	A	179	GLN	0	-0.075	-0.029	36.075	0.001	0.001	0.000	0.000	0.000	0.000
93	A	180	GLU	-1	-0.785	-0.865	33.377	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	181	ALA	0	0.014	0.018	35.496	0.005	0.005	0.000	0.000	0.000	0.000
95	A	182	ASN	0	-0.045	-0.049	37.892	0.006	0.006	0.000	0.000	0.000	0.000
96	A	183	ASP	-1	-0.919	-0.939	33.248	0.011	0.011	0.000	0.000	0.000	0.000
97	A	184	ALA	0	0.068	0.026	33.232	0.005	0.005	0.000	0.000	0.000	0.000
98	A	185	LEU	0	-0.019	-0.007	34.182	0.006	0.006	0.000	0.000	0.000	0.000
99	A	186	ASN	0	-0.036	-0.025	37.135	0.005	0.005	0.000	0.000	0.000	0.000
100	A	187	ALA	0	-0.015	0.007	31.679	0.001	0.001	0.000	0.000	0.000	0.000
101	A	188	PHE	0	-0.030	-0.011	33.388	0.003	0.003	0.000	0.000	0.000	0.000
102	A	189	SER	0	-0.024	-0.016	34.793	0.001	0.001	0.000	0.000	0.000	0.000
103	A	190	SER	0	-0.044	-0.014	38.112	0.004	0.004	0.000	0.000	0.000	0.000
104	A	191	GLU	-1	-0.938	-0.961	40.189	0.034	0.034	0.000	0.000	0.000	0.000
105	A	192	ASP	-1	-0.860	-0.959	42.308	0.022	0.022	0.000	0.000	0.000	0.000
106	A	193	ARG	1	0.917	0.955	44.168	-0.029	-0.029	0.000	0.000	0.000	0.000
107	A	194	ILE	0	0.042	0.024	38.773	0.002	0.002	0.000	0.000	0.000	0.000
108	A	195	ASN	0	0.028	0.014	39.629	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	196	TYR	0	-0.014	-0.049	38.999	0.003	0.003	0.000	0.000	0.000	0.000
110	A	197	LYS	1	0.897	0.956	38.466	-0.045	-0.045	0.000	0.000	0.000	0.000
111	A	198	LEU	0	0.053	0.024	33.887	0.001	0.001	0.000	0.000	0.000	0.000
112	A	199	PHE	0	-0.024	-0.019	34.219	0.003	0.003	0.000	0.000	0.000	0.000
113	A	200	CYS	0	-0.071	-0.038	33.905	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	201	GLU	-1	-0.940	-0.965	31.873	0.083	0.083	0.000	0.000	0.000	0.000
115	A	202	ASP	-1	-0.898	-0.946	29.427	0.101	0.101	0.000	0.000	0.000	0.000
116	A	203	ILE	0	-0.143	-0.067	27.831	0.002	0.002	0.000	0.000	0.000	0.000

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