FMO DATABASE

FMODB ID: LNKQ9

Calculation Name: 1AQT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AQT

Chain ID: A

ChEMBL ID:

UniProt ID: P0A6E6

Base Structure: X-ray

Registration Date: 2023-09-24

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	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1090187.645536
FMO2-HF: Nuclear repulsion	1039134.824239
FMO2-HF: Total energy	-51052.821297
FMO2-MP2: Total energy	-51202.750092

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:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-2.201	1.099	0.66	-1.794	-2.165	-0.001

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.024 / q_NPA : -0.022

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	TYR	0	-0.062	-0.020	3.819	0.168	2.491	-0.029	-1.310	-0.984	0.001
4	A	5	HIS	0	0.000	-0.001	6.671	-0.045	-0.045	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.012	0.003	10.451	-0.124	-0.124	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.819	-0.915	12.911	0.148	0.148	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.056	-0.030	16.655	-0.042	-0.042	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.005	-0.012	19.101	0.025	0.025	0.000	0.000	0.000	0.000
9	A	10	SER	0	0.027	0.021	22.512	-0.017	-0.017	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.012	0.002	25.996	0.011	0.011	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.952	-0.975	29.151	-0.023	-0.023	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.029	-0.016	26.589	0.010	0.010	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.022	0.011	20.593	0.008	0.008	0.000	0.000	0.000	0.000
14	A	15	MET	0	-0.043	-0.018	21.353	0.013	0.013	0.000	0.000	0.000	0.000
15	A	16	PHE	0	-0.014	-0.020	13.214	-0.015	-0.015	0.000	0.000	0.000	0.000
16	A	17	SER	0	0.036	0.028	16.377	0.016	0.016	0.000	0.000	0.000	0.000
17	A	18	GLY	0	-0.012	0.008	13.495	0.053	0.053	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.023	-0.010	7.221	-0.023	-0.023	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.043	-0.007	8.466	-0.036	-0.036	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.884	-0.955	5.301	-2.311	-2.311	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.863	0.932	6.127	0.632	0.632	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.022	0.022	8.913	0.226	0.226	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.069	-0.033	12.671	-0.098	-0.098	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.065	0.042	15.706	0.058	0.058	0.000	0.000	0.000	0.000
25	A	26	THR	0	0.001	-0.001	18.369	-0.011	-0.011	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.060	0.027	20.699	0.029	0.029	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.047	-0.022	21.604	0.020	0.020	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.941	-0.977	21.571	-0.260	-0.260	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.014	0.018	23.185	0.004	0.004	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.983	-0.991	18.892	-0.452	-0.452	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.027	0.008	15.394	-0.025	-0.025	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.005	0.005	13.726	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	34	ILE	0	-0.013	0.003	9.667	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.023	-0.007	6.399	-0.044	-0.044	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.022	0.000	2.552	-0.645	0.209	0.690	-0.474	-1.070	-0.002
36	A	37	GLY	0	-0.025	-0.011	4.376	-0.131	-0.008	-0.001	-0.010	-0.111	0.000
37	A	38	HIS	0	-0.054	-0.017	6.522	0.143	0.143	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.003	-0.001	9.515	0.131	0.131	0.000	0.000	0.000	0.000
39	A	40	PRO	0	-0.018	-0.009	12.880	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.005	0.007	15.052	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.034	0.012	17.298	0.018	0.018	0.000	0.000	0.000	0.000
42	A	43	THR	0	-0.018	-0.001	19.313	0.011	0.011	0.000	0.000	0.000	0.000
43	A	44	ALA	0	0.018	0.023	21.751	0.009	0.009	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.037	-0.032	20.069	-0.022	-0.022	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.933	0.965	23.734	0.186	0.186	0.000	0.000	0.000	0.000
46	A	47	PRO	0	-0.046	-0.025	25.446	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.010	-0.015	25.162	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	49	MET	0	-0.060	-0.022	20.022	0.024	0.024	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.029	0.022	15.478	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.826	0.921	14.896	0.572	0.572	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.020	0.001	13.367	-0.089	-0.089	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.022	-0.007	10.037	0.069	0.069	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.986	0.979	10.012	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	55	GLN	0	0.016	-0.004	6.074	0.117	0.117	0.000	0.000	0.000	0.000
55	A	56	HIS	0	-0.035	-0.019	7.827	0.097	0.097	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.022	0.031	9.381	0.069	0.069	0.000	0.000	0.000	0.000
57	A	58	HIS	0	-0.026	0.000	11.195	0.080	0.080	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.883	-0.950	13.825	-0.576	-0.576	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.899	-0.953	16.154	-0.092	-0.092	0.000	0.000	0.000	0.000
60	A	61	PHE	0	-0.003	-0.003	18.079	-0.049	-0.049	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.027	0.020	19.826	0.036	0.036	0.000	0.000	0.000	0.000
62	A	63	TYR	0	0.029	0.011	22.486	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	64	LEU	0	0.020	0.006	20.791	0.014	0.014	0.000	0.000	0.000	0.000
64	A	65	SER	0	0.019	0.004	25.391	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.010	-0.007	26.403	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.063	0.043	24.456	0.004	0.004	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.055	-0.020	21.761	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.012	-0.005	15.329	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.922	-0.971	17.068	-0.050	-0.050	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.007	0.004	11.602	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	72	GLN	0	0.016	-0.001	13.067	0.048	0.048	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.007	-0.009	10.826	-0.035	-0.035	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.018	0.000	8.220	0.109	0.109	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.041	-0.026	9.305	0.034	0.034	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.011	0.008	10.353	-0.082	-0.082	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.072	0.043	13.002	0.033	0.033	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.022	-0.011	16.622	-0.033	-0.033	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.004	0.005	18.998	0.020	0.020	0.000	0.000	0.000	0.000
79	A	80	ALA	0	-0.021	-0.027	22.626	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.923	-0.951	24.724	-0.083	-0.083	0.000	0.000	0.000	0.000
81	A	82	THR	0	-0.041	-0.036	28.421	0.013	0.013	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.002	-0.004	24.531	-0.016	-0.016	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.026	-0.007	26.442	0.015	0.015	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.933	0.969	21.591	0.060	0.060	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.056	0.017	24.096	0.008	0.008	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.037	-0.031	23.038	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.928	-0.961	27.563	-0.060	-0.060	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.091	-0.025	27.717	0.005	0.005	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.845	-0.927	31.110	-0.068	-0.068	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.881	-0.964	34.296	-0.107	-0.107	0.000	0.000	0.000	0.000
91	A	92	ALA	0	0.009	0.007	35.372	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.941	0.958	36.940	0.060	0.060	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.038	0.024	34.087	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	MET	0	-0.011	-0.011	36.096	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.990	-0.997	38.566	-0.060	-0.060	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.010	-0.011	37.492	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.902	0.947	36.462	0.104	0.104	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.943	0.996	39.273	0.064	0.064	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.918	0.949	42.370	0.061	0.061	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.047	0.035	40.126	0.002	0.002	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.889	-0.959	40.872	-0.092	-0.092	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.944	-0.972	43.312	-0.059	-0.059	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.011	-0.001	44.123	0.003	0.003	0.000	0.000	0.000	0.000
104	A	105	ILE	0	0.019	0.006	40.883	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.081	-0.012	45.312	0.002	0.002	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.023	-0.017	48.459	0.004	0.004	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.105	-0.064	46.500	0.001	0.001	0.000	0.000	0.000	0.000
108	A	109	HIS	0	-0.046	-0.010	48.759	0.002	0.002	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.052	-0.036	49.446	0.002	0.002	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.922	-0.967	45.301	-0.075	-0.075	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.012	0.003	44.210	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.815	-0.931	43.695	-0.067	-0.067	0.000	0.000	0.000	0.000
113	A	114	TYR	0	0.056	0.044	40.724	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.012	-0.002	39.545	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	116	GLN	0	-0.073	-0.046	38.838	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.079	0.045	39.775	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	118	SER	0	-0.063	-0.033	37.749	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.019	-0.009	35.276	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.933	-0.967	34.972	-0.083	-0.083	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.035	0.019	36.329	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.013	0.013	31.770	-0.007	-0.007	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.959	0.970	31.358	0.098	0.098	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.031	0.034	31.911	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.015	-0.015	30.798	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	126	ALA	0	-0.050	-0.031	27.924	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	127	GLN	0	-0.013	-0.015	28.111	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.061	0.024	29.458	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	129	ARG	1	0.920	0.978	25.206	0.220	0.220	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.019	0.007	24.163	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	131	ILE	0	0.009	0.015	25.767	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.838	-0.928	27.874	-0.142	-0.142	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.117	-0.071	21.766	-0.009	-0.009	0.000	0.000	0.000	0.000
133	A	134	THR	0	-0.028	-0.007	23.281	-0.016	-0.016	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.819	0.924	24.617	0.124	0.124	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.924	0.985	23.044	0.256	0.256	0.000	0.000	0.000	0.000

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