FMO DATABASE

FMODB ID: MNQRZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1095212.582831
FMO2-HF: Nuclear repulsion	1044158.445059
FMO2-HF: Total energy	-51054.137772
FMO2-MP2: Total energy	-51204.089908

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.
-2.58	0.657	0.582	-1.637	-2.181	0.005

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 : -0.030 / q_NPA : -0.025

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	-0.066	-0.043	3.871	0.912	3.026	-0.020	-1.179	-0.914	0.001
4	A	5	HIS	0	-0.041	-0.023	6.908	-0.525	-0.525	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.016	-0.003	10.547	0.094	0.094	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.763	-0.852	13.458	0.317	0.317	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.020	-0.019	17.157	0.011	0.011	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.013	-0.017	19.688	-0.035	-0.035	0.000	0.000	0.000	0.000
9	A	10	SER	0	0.041	-0.004	23.347	0.008	0.008	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.014	-0.007	27.013	0.008	0.008	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.867	-0.914	29.677	0.102	0.102	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.072	-0.033	26.863	-0.019	-0.019	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.014	0.006	21.457	0.034	0.034	0.000	0.000	0.000	0.000
14	A	15	MET	0	-0.027	0.001	21.922	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	16	PHE	0	-0.004	-0.014	13.459	-0.060	-0.060	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.015	-0.021	16.778	0.031	0.031	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.001	0.005	13.829	-0.078	-0.078	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.012	-0.002	7.339	0.084	0.084	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.038	-0.010	8.515	-0.281	-0.281	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.803	-0.889	4.879	-1.627	-1.627	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.845	0.918	6.133	0.503	0.503	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.029	0.028	8.964	-0.142	-0.142	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.054	-0.037	12.690	0.017	0.017	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.044	0.023	15.749	-0.037	-0.037	0.000	0.000	0.000	0.000
25	A	26	THR	0	-0.001	0.006	18.876	0.002	0.002	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.078	0.043	21.630	0.001	0.001	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.022	-0.015	22.476	-0.036	-0.036	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.863	-0.919	22.403	0.305	0.305	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.008	0.007	23.528	-0.015	-0.015	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.958	-0.962	18.826	0.145	0.145	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.007	0.005	17.198	0.015	0.015	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.009	-0.003	13.936	-0.041	-0.041	0.000	0.000	0.000	0.000
33	A	34	ILE	0	-0.017	0.005	10.921	0.080	0.080	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.029	0.016	6.898	-0.306	-0.306	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.032	0.015	2.880	-1.404	-0.395	0.603	-0.454	-1.158	0.004
36	A	37	GLY	0	-0.022	-0.007	5.165	-0.624	-0.510	-0.001	-0.004	-0.109	0.000
37	A	38	HIS	0	-0.067	-0.030	7.449	-0.689	-0.689	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.009	0.008	10.491	0.009	0.009	0.000	0.000	0.000	0.000
39	A	40	PRO	0	0.001	-0.005	13.716	-0.019	-0.019	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.011	0.003	15.854	-0.063	-0.063	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.005	0.000	18.258	0.014	0.014	0.000	0.000	0.000	0.000
42	A	43	THR	0	-0.049	-0.038	20.466	-0.040	-0.040	0.000	0.000	0.000	0.000
43	A	44	ALA	0	0.026	0.019	23.053	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.007	0.001	20.834	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.832	0.919	24.635	-0.212	-0.212	0.000	0.000	0.000	0.000
46	A	47	PRO	0	-0.040	-0.022	26.348	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.002	-0.007	25.592	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	49	MET	0	-0.039	-0.021	20.301	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.027	0.019	16.038	0.031	0.031	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.804	0.899	15.054	-0.013	-0.013	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.030	0.003	13.810	0.053	0.053	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.014	-0.012	10.453	-0.052	-0.052	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.925	0.944	10.218	0.114	0.114	0.000	0.000	0.000	0.000
54	A	55	GLN	0	0.002	-0.007	6.261	-0.059	-0.059	0.000	0.000	0.000	0.000
55	A	56	HIS	0	-0.056	-0.039	7.699	0.112	0.112	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.014	0.019	9.172	0.146	0.146	0.000	0.000	0.000	0.000
57	A	58	HIS	0	-0.047	-0.009	10.975	0.187	0.187	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.827	-0.914	13.839	-0.093	-0.093	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.827	-0.891	15.875	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	61	PHE	0	-0.006	0.002	18.160	0.035	0.035	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.007	0.004	20.332	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	63	TYR	0	0.025	0.017	22.892	0.020	0.020	0.000	0.000	0.000	0.000
63	A	64	LEU	0	0.013	0.002	21.535	0.005	0.005	0.000	0.000	0.000	0.000
64	A	65	SER	0	-0.025	-0.041	26.151	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.015	-0.011	27.827	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.062	0.030	25.270	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.085	-0.036	22.898	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.000	0.011	16.313	0.002	0.002	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.882	-0.938	17.773	0.459	0.459	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.016	-0.004	12.543	0.046	0.046	0.000	0.000	0.000	0.000
71	A	72	GLN	0	0.044	0.009	13.873	-0.038	-0.038	0.000	0.000	0.000	0.000
72	A	73	PRO	0	-0.011	-0.023	11.406	0.209	0.209	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.008	0.012	8.523	-0.103	-0.103	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.030	-0.021	9.609	0.061	0.061	0.000	0.000	0.000	0.000
75	A	76	VAL	0	-0.002	0.004	11.459	0.023	0.023	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.014	0.002	14.025	-0.061	-0.061	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.030	-0.028	17.508	0.003	0.003	0.000	0.000	0.000	0.000
78	A	79	LEU	0	0.010	0.025	19.982	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.003	-0.015	23.630	0.003	0.003	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.837	-0.899	25.894	0.139	0.139	0.000	0.000	0.000	0.000
81	A	82	THR	0	-0.025	-0.028	28.840	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	83	ALA	0	-0.001	0.008	24.792	0.008	0.008	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.017	-0.004	26.677	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.868	0.923	21.671	-0.026	-0.026	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.034	0.000	24.380	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.027	-0.023	23.320	0.004	0.004	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.909	-0.952	27.753	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.083	-0.027	28.051	0.008	0.008	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.782	-0.903	31.292	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.849	-0.911	34.165	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.007	-0.003	35.497	0.003	0.003	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.891	0.936	36.827	-0.017	-0.017	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.051	0.031	34.086	0.004	0.004	0.000	0.000	0.000	0.000
94	A	95	MET	0	0.012	0.003	36.053	0.005	0.005	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.816	-0.869	38.758	0.022	0.022	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.020	-0.011	37.410	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.808	0.880	36.983	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.732	0.830	39.132	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.874	0.930	42.413	-0.028	-0.028	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.042	0.028	39.937	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.810	-0.894	40.929	0.026	0.026	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.829	-0.901	43.436	0.024	0.024	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.020	0.006	43.949	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	105	ILE	0	0.041	0.015	40.690	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.098	-0.040	45.330	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.061	-0.040	48.501	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.092	-0.047	46.849	0.002	0.002	0.000	0.000	0.000	0.000
108	A	109	HIS	0	-0.067	-0.039	49.150	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.043	-0.028	49.849	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.880	-0.935	45.733	0.061	0.061	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.001	-0.011	44.643	0.003	0.003	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.799	-0.897	44.233	0.052	0.052	0.000	0.000	0.000	0.000
113	A	114	TYR	0	0.025	0.021	40.991	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	ALA	0	-0.018	-0.015	40.465	0.001	0.001	0.000	0.000	0.000	0.000
115	A	116	GLN	0	-0.085	-0.052	39.558	0.008	0.008	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.055	0.031	39.887	0.002	0.002	0.000	0.000	0.000	0.000
117	A	118	SER	0	-0.001	-0.006	37.290	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.040	-0.016	35.616	0.003	0.003	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.869	-0.930	35.308	0.057	0.057	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.009	0.003	36.360	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.021	-0.005	32.202	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.933	0.961	31.805	-0.099	-0.099	0.000	0.000	0.000	0.000
123	A	124	ALA	0	-0.006	0.027	32.279	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.005	-0.016	30.893	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	126	ALA	0	-0.034	-0.003	28.095	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	127	GLN	0	-0.033	-0.027	28.112	-0.008	-0.008	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.029	0.010	29.565	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	129	ARG	1	0.929	0.972	24.363	-0.077	-0.077	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.027	0.012	24.112	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	131	ILE	0	0.018	0.029	25.828	-0.014	-0.014	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.836	-0.932	27.947	-0.045	-0.045	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.085	-0.040	21.904	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	134	THR	0	0.003	-0.013	23.745	-0.018	-0.018	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.754	0.873	24.859	0.014	0.014	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.827	0.936	22.685	0.045	0.045	0.000	0.000	0.000	0.000

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