FMO DATABASE

FMODB ID: MN8YZ

Calculation Name: 1TQ8-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TQ8

Chain ID: A

ChEMBL ID:

UniProt ID: P9WFC9

Base Structure: X-ray

Registration Date: 2023-09-23

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-902190.46161
FMO2-HF: Nuclear repulsion	856683.445855
FMO2-HF: Total energy	-45507.015755
FMO2-MP2: Total energy	-45642.161424

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:13:SER)

Summations of interaction energy for fragment #1(A:13: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.
-1.218	0.126	-0.011	-0.547	-0.785	0.003

Interaction energy analysis for fragmet #1(A:13: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 : -0.027

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	15	SER	0	0.003	0.008	3.806	-1.928	-0.584	-0.011	-0.547	-0.785	0.003
4	A	16	ALA	0	-0.006	-0.006	6.157	0.738	0.738	0.000	0.000	0.000	0.000
5	A	17	TYR	0	-0.031	-0.015	9.914	-0.087	-0.087	0.000	0.000	0.000	0.000
6	A	18	LYS	1	0.959	0.964	8.419	1.501	1.501	0.000	0.000	0.000	0.000
7	A	19	THR	0	-0.016	0.007	13.810	0.050	0.050	0.000	0.000	0.000	0.000
8	A	20	VAL	0	0.043	0.029	16.983	0.032	0.032	0.000	0.000	0.000	0.000
9	A	21	VAL	0	0.027	0.024	19.053	0.017	0.017	0.000	0.000	0.000	0.000
10	A	22	VAL	0	-0.008	-0.006	22.418	0.013	0.013	0.000	0.000	0.000	0.000
11	A	23	GLY	0	-0.029	0.002	24.836	0.003	0.003	0.000	0.000	0.000	0.000
12	A	24	THR	0	-0.033	-0.039	28.293	0.006	0.006	0.000	0.000	0.000	0.000
13	A	25	ASP	-1	-0.829	-0.918	31.355	-0.057	-0.057	0.000	0.000	0.000	0.000
14	A	26	GLY	0	0.037	0.014	34.137	0.004	0.004	0.000	0.000	0.000	0.000
15	A	27	SER	0	-0.063	-0.010	34.679	0.001	0.001	0.000	0.000	0.000	0.000
16	A	28	ASP	-1	-0.858	-0.944	34.613	-0.066	-0.066	0.000	0.000	0.000	0.000
17	A	29	SER	0	-0.094	-0.054	31.858	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	30	SER	0	0.036	0.016	30.248	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	31	MET	0	0.062	0.032	29.397	-0.015	-0.015	0.000	0.000	0.000	0.000
20	A	32	ARG	1	0.907	0.961	28.617	0.067	0.067	0.000	0.000	0.000	0.000
21	A	33	ALA	0	0.013	0.001	25.690	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	34	VAL	0	0.006	0.013	24.830	-0.018	-0.018	0.000	0.000	0.000	0.000
23	A	35	ASP	-1	-0.797	-0.874	25.244	-0.150	-0.150	0.000	0.000	0.000	0.000
24	A	36	ARG	1	0.891	0.950	20.014	0.151	0.151	0.000	0.000	0.000	0.000
25	A	37	ALA	0	0.041	0.008	20.836	-0.028	-0.028	0.000	0.000	0.000	0.000
26	A	38	ALA	0	0.011	0.012	20.718	-0.040	-0.040	0.000	0.000	0.000	0.000
27	A	39	GLN	0	-0.038	-0.021	17.585	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	40	ILE	0	-0.084	-0.040	15.376	-0.030	-0.030	0.000	0.000	0.000	0.000
29	A	41	ALA	0	-0.007	0.005	16.498	-0.076	-0.076	0.000	0.000	0.000	0.000
30	A	42	GLY	0	0.014	0.007	17.938	-0.055	-0.055	0.000	0.000	0.000	0.000
31	A	43	ALA	0	0.002	-0.034	18.713	0.044	0.044	0.000	0.000	0.000	0.000
32	A	44	ASP	-1	-0.938	-0.955	15.269	-0.610	-0.610	0.000	0.000	0.000	0.000
33	A	45	ALA	0	-0.037	0.006	15.499	-0.048	-0.048	0.000	0.000	0.000	0.000
34	A	46	LYS	1	0.865	0.947	16.983	0.358	0.358	0.000	0.000	0.000	0.000
35	A	47	LEU	0	-0.006	-0.002	19.433	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	48	ILE	0	0.003	-0.005	22.071	0.021	0.021	0.000	0.000	0.000	0.000
37	A	49	ILE	0	-0.010	-0.008	24.492	0.006	0.006	0.000	0.000	0.000	0.000
38	A	50	ALA	0	0.002	-0.007	27.462	0.008	0.008	0.000	0.000	0.000	0.000
39	A	51	SER	0	-0.004	-0.016	29.437	0.006	0.006	0.000	0.000	0.000	0.000
40	A	52	ALA	0	-0.005	0.004	32.873	0.000	0.000	0.000	0.000	0.000	0.000
41	A	53	TYR	0	0.006	0.001	34.990	0.001	0.001	0.000	0.000	0.000	0.000
42	A	54	LEU	0	-0.034	-0.019	38.253	0.004	0.004	0.000	0.000	0.000	0.000
43	A	55	PRO	0	-0.011	0.005	41.062	0.003	0.003	0.000	0.000	0.000	0.000
44	A	76	THR	0	0.025	0.010	42.425	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	77	ALA	0	-0.043	-0.025	41.609	0.001	0.001	0.000	0.000	0.000	0.000
46	A	78	PRO	0	0.101	0.021	41.857	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	79	ILE	0	-0.008	0.007	35.593	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	80	TYR	0	0.002	-0.015	36.460	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	81	GLU	-1	-0.927	-0.932	37.555	-0.072	-0.072	0.000	0.000	0.000	0.000
50	A	82	ILE	0	0.016	0.015	35.083	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	83	LEU	0	-0.068	-0.037	31.931	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	84	HIS	0	0.010	0.013	33.187	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	85	ASP	-1	-0.841	-0.933	34.444	-0.095	-0.095	0.000	0.000	0.000	0.000
54	A	86	ALA	0	-0.071	-0.038	30.809	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	87	LYS	1	0.936	0.957	29.691	0.137	0.137	0.000	0.000	0.000	0.000
56	A	88	GLU	-1	-0.902	-0.947	30.352	-0.137	-0.137	0.000	0.000	0.000	0.000
57	A	89	ARG	1	0.757	0.854	30.052	0.106	0.106	0.000	0.000	0.000	0.000
58	A	90	ALA	0	0.010	-0.002	26.311	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	91	HIS	0	-0.022	-0.007	26.802	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	92	ASN	0	-0.053	-0.016	27.912	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	93	ALA	0	-0.035	-0.013	25.551	0.004	0.004	0.000	0.000	0.000	0.000
62	A	94	GLY	0	-0.070	-0.041	24.014	-0.017	-0.017	0.000	0.000	0.000	0.000
63	A	95	ALA	0	-0.011	0.006	22.702	-0.029	-0.029	0.000	0.000	0.000	0.000
64	A	96	LYS	1	0.916	0.961	22.670	0.319	0.319	0.000	0.000	0.000	0.000
65	A	97	ASN	0	-0.050	-0.031	20.059	0.049	0.049	0.000	0.000	0.000	0.000
66	A	98	VAL	0	0.020	0.016	23.077	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	99	GLU	-1	-0.952	-0.973	24.775	-0.198	-0.198	0.000	0.000	0.000	0.000
68	A	100	GLU	-1	-0.903	-0.948	27.452	-0.115	-0.115	0.000	0.000	0.000	0.000
69	A	101	ARG	1	0.904	0.936	26.406	0.151	0.151	0.000	0.000	0.000	0.000
70	A	102	PRO	0	0.014	0.015	30.775	0.003	0.003	0.000	0.000	0.000	0.000
71	A	103	ILE	0	-0.015	0.001	29.134	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	104	VAL	0	0.027	-0.004	33.092	0.005	0.005	0.000	0.000	0.000	0.000
73	A	105	GLY	0	0.000	0.010	35.164	0.001	0.001	0.000	0.000	0.000	0.000
74	A	106	ALA	0	0.018	-0.002	35.043	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	107	PRO	0	0.034	0.008	32.547	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	108	VAL	0	0.010	0.002	28.030	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	109	ASP	-1	-0.861	-0.925	28.607	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	110	ALA	0	-0.025	-0.003	29.402	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	111	LEU	0	-0.032	-0.025	25.219	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	112	VAL	0	-0.001	-0.001	24.369	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	113	ASN	0	0.044	0.032	24.600	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	114	LEU	0	-0.040	-0.012	24.624	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	115	ALA	0	-0.024	-0.020	20.869	-0.023	-0.023	0.000	0.000	0.000	0.000
84	A	116	ASP	-1	-0.881	-0.942	20.600	-0.093	-0.093	0.000	0.000	0.000	0.000
85	A	117	GLU	-1	-1.006	-1.008	21.773	-0.121	-0.121	0.000	0.000	0.000	0.000
86	A	118	GLU	-1	-0.925	-0.977	21.330	-0.239	-0.239	0.000	0.000	0.000	0.000
87	A	119	LYS	1	0.852	0.934	16.711	0.215	0.215	0.000	0.000	0.000	0.000
88	A	120	ALA	0	-0.019	-0.008	16.546	-0.062	-0.062	0.000	0.000	0.000	0.000
89	A	121	ASP	-1	-0.844	-0.919	12.944	-0.637	-0.637	0.000	0.000	0.000	0.000
90	A	122	LEU	0	-0.025	-0.010	14.934	0.048	0.048	0.000	0.000	0.000	0.000
91	A	123	LEU	0	-0.003	0.007	17.147	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	124	VAL	0	-0.010	-0.008	20.255	0.019	0.019	0.000	0.000	0.000	0.000
93	A	125	VAL	0	0.025	0.003	22.635	0.002	0.002	0.000	0.000	0.000	0.000
94	A	126	GLY	0	0.034	0.027	25.828	0.002	0.002	0.000	0.000	0.000	0.000
95	A	127	ASN	0	-0.084	-0.057	28.329	0.008	0.008	0.000	0.000	0.000	0.000
96	A	128	VAL	0	0.040	0.010	29.700	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	129	GLY	0	-0.017	-0.005	33.247	0.006	0.006	0.000	0.000	0.000	0.000
98	A	130	LEU	0	0.051	0.042	35.949	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	131	SER	0	-0.019	-0.043	39.165	0.003	0.003	0.000	0.000	0.000	0.000
100	A	132	THR	0	0.032	0.033	41.354	0.002	0.002	0.000	0.000	0.000	0.000
101	A	133	ILE	0	0.064	0.020	42.260	0.001	0.001	0.000	0.000	0.000	0.000
102	A	134	ALA	0	0.040	0.020	42.090	0.002	0.002	0.000	0.000	0.000	0.000
103	A	135	GLY	0	0.003	-0.001	40.102	0.002	0.002	0.000	0.000	0.000	0.000
104	A	136	ARG	1	0.875	0.934	37.173	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	137	LEU	0	-0.032	-0.021	37.213	0.003	0.003	0.000	0.000	0.000	0.000
106	A	138	LEU	0	-0.016	-0.006	37.542	0.004	0.004	0.000	0.000	0.000	0.000
107	A	139	GLY	0	0.009	0.035	34.329	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	140	SER	0	0.058	0.027	28.987	0.007	0.007	0.000	0.000	0.000	0.000
109	A	141	VAL	0	0.054	0.001	28.010	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	142	PRO	0	0.026	0.017	24.676	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	143	ALA	0	0.096	0.054	26.514	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	144	ASN	0	0.000	0.001	28.805	-0.012	-0.012	0.000	0.000	0.000	0.000
113	A	145	VAL	0	-0.013	-0.015	25.929	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	146	SER	0	0.026	0.038	26.193	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	147	ARG	1	0.923	0.958	27.474	-0.013	-0.013	0.000	0.000	0.000	0.000
116	A	148	ARG	1	0.839	0.912	30.665	-0.043	-0.043	0.000	0.000	0.000	0.000
117	A	149	ALA	0	-0.011	-0.007	27.489	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	150	LYS	1	0.910	0.962	28.222	0.015	0.015	0.000	0.000	0.000	0.000
119	A	151	VAL	0	0.012	0.019	22.856	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	152	ASP	-1	-0.872	-0.929	21.517	-0.073	-0.073	0.000	0.000	0.000	0.000
121	A	153	VAL	0	-0.063	-0.051	21.041	0.017	0.017	0.000	0.000	0.000	0.000
122	A	154	LEU	0	0.019	0.012	13.816	-0.018	-0.018	0.000	0.000	0.000	0.000
123	A	155	ILE	0	-0.034	-0.018	17.657	0.043	0.043	0.000	0.000	0.000	0.000
124	A	156	VAL	0	0.003	0.009	11.337	-0.041	-0.041	0.000	0.000	0.000	0.000
125	A	157	HIS	0	0.010	0.017	11.987	0.065	0.065	0.000	0.000	0.000	0.000
126	A	158	THR	0	0.052	0.012	13.049	0.083	0.083	0.000	0.000	0.000	0.000
127	A	159	THR	0	-0.035	-0.011	11.380	-0.078	-0.078	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:13:SER)