FMO DATABASE

FMODB ID: 76N7K

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

Total energy (hartree)

FMO2-HF: Electronic energy	-902666.054245
FMO2-HF: Nuclear repulsion	857158.423381
FMO2-HF: Total energy	-45507.630863
FMO2-MP2: Total energy	-45642.74348

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.
-1.611	-0.27	-0.011	-0.55	-0.78	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 : -0.024

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

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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	0.017	0.009	3.806	-1.855	-0.514	-0.011	-0.550	-0.780	0.003
4	A	16	ALA	0	-0.004	0.006	6.390	0.753	0.753	0.000	0.000	0.000	0.000
5	A	17	TYR	0	0.005	-0.005	9.919	-0.123	-0.123	0.000	0.000	0.000	0.000
6	A	18	LYS	1	0.876	0.930	9.309	1.281	1.281	0.000	0.000	0.000	0.000
7	A	19	THR	0	-0.007	0.004	14.068	0.050	0.050	0.000	0.000	0.000	0.000
8	A	20	VAL	0	0.029	0.021	17.081	0.035	0.035	0.000	0.000	0.000	0.000
9	A	21	VAL	0	0.020	0.020	19.283	0.016	0.016	0.000	0.000	0.000	0.000
10	A	22	VAL	0	-0.009	-0.004	22.537	0.015	0.015	0.000	0.000	0.000	0.000
11	A	23	GLY	0	-0.021	0.006	24.836	0.002	0.002	0.000	0.000	0.000	0.000
12	A	24	THR	0	-0.047	-0.058	28.293	0.004	0.004	0.000	0.000	0.000	0.000
13	A	25	ASP	-1	-0.795	-0.872	31.339	-0.057	-0.057	0.000	0.000	0.000	0.000
14	A	26	GLY	0	0.032	0.009	34.127	0.004	0.004	0.000	0.000	0.000	0.000
15	A	27	SER	0	-0.090	-0.051	34.663	0.001	0.001	0.000	0.000	0.000	0.000
16	A	28	ASP	-1	-0.860	-0.945	34.599	-0.065	-0.065	0.000	0.000	0.000	0.000
17	A	29	SER	0	-0.089	-0.050	31.697	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	30	SER	0	0.016	0.021	30.218	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	31	MET	0	0.085	0.041	29.383	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	32	ARG	1	0.917	0.966	28.644	0.062	0.062	0.000	0.000	0.000	0.000
21	A	33	ALA	0	0.006	-0.002	25.675	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	34	VAL	0	0.014	0.014	24.818	-0.018	-0.018	0.000	0.000	0.000	0.000
23	A	35	ASP	-1	-0.788	-0.848	25.238	-0.144	-0.144	0.000	0.000	0.000	0.000
24	A	36	ARG	1	0.808	0.899	19.871	0.121	0.121	0.000	0.000	0.000	0.000
25	A	37	ALA	0	0.026	-0.001	20.823	-0.027	-0.027	0.000	0.000	0.000	0.000
26	A	38	ALA	0	0.010	0.010	20.714	-0.040	-0.040	0.000	0.000	0.000	0.000
27	A	39	GLN	0	-0.022	-0.010	17.585	0.002	0.002	0.000	0.000	0.000	0.000
28	A	40	ILE	0	-0.089	-0.042	15.365	-0.032	-0.032	0.000	0.000	0.000	0.000
29	A	41	ALA	0	-0.005	0.006	16.502	-0.074	-0.074	0.000	0.000	0.000	0.000
30	A	42	GLY	0	0.016	0.009	17.954	-0.056	-0.056	0.000	0.000	0.000	0.000
31	A	43	ALA	0	0.003	-0.033	18.691	0.045	0.045	0.000	0.000	0.000	0.000
32	A	44	ASP	-1	-0.936	-0.957	15.277	-0.611	-0.611	0.000	0.000	0.000	0.000
33	A	45	ALA	0	-0.031	0.012	15.841	-0.050	-0.050	0.000	0.000	0.000	0.000
34	A	46	LYS	1	0.766	0.866	17.240	0.336	0.336	0.000	0.000	0.000	0.000
35	A	47	LEU	0	-0.004	-0.002	19.694	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	48	ILE	0	-0.014	-0.015	22.335	0.020	0.020	0.000	0.000	0.000	0.000
37	A	49	ILE	0	-0.003	-0.004	24.752	0.007	0.007	0.000	0.000	0.000	0.000
38	A	50	ALA	0	0.007	-0.007	27.726	0.007	0.007	0.000	0.000	0.000	0.000
39	A	51	SER	0	-0.007	-0.020	29.655	0.006	0.006	0.000	0.000	0.000	0.000
40	A	52	ALA	0	0.001	0.004	32.957	0.000	0.000	0.000	0.000	0.000	0.000
41	A	53	TYR	0	0.001	-0.006	35.048	0.001	0.001	0.000	0.000	0.000	0.000
42	A	54	LEU	0	-0.028	-0.017	38.062	0.004	0.004	0.000	0.000	0.000	0.000
43	A	55	PRO	0	-0.004	0.011	41.095	0.003	0.003	0.000	0.000	0.000	0.000
44	A	76	THR	0	0.022	0.009	42.653	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	77	ALA	0	-0.031	-0.019	41.910	0.002	0.002	0.000	0.000	0.000	0.000
46	A	78	PRO	0	0.111	0.026	42.117	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	79	ILE	0	-0.024	0.003	35.914	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	80	TYR	0	0.009	-0.016	36.626	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	81	GLU	-1	-0.926	-0.933	37.819	-0.072	-0.072	0.000	0.000	0.000	0.000
50	A	82	ILE	0	0.019	0.017	35.185	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	83	LEU	0	-0.062	-0.033	32.096	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	84	HIS	0	-0.040	-0.014	33.454	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	85	ASP	-1	-0.842	-0.932	34.711	-0.096	-0.096	0.000	0.000	0.000	0.000
54	A	86	ALA	0	-0.071	-0.041	30.849	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	87	LYS	1	0.855	0.914	29.994	0.137	0.137	0.000	0.000	0.000	0.000
56	A	88	GLU	-1	-0.860	-0.920	30.533	-0.136	-0.136	0.000	0.000	0.000	0.000
57	A	89	ARG	1	0.769	0.851	30.136	0.103	0.103	0.000	0.000	0.000	0.000
58	A	90	ALA	0	0.019	0.001	26.429	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	91	HIS	0	-0.033	-0.016	26.808	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	92	ASN	0	-0.102	-0.051	27.900	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	93	ALA	0	-0.023	-0.007	25.685	0.005	0.005	0.000	0.000	0.000	0.000
62	A	94	GLY	0	-0.066	-0.038	24.004	-0.017	-0.017	0.000	0.000	0.000	0.000
63	A	95	ALA	0	-0.009	0.008	22.690	-0.029	-0.029	0.000	0.000	0.000	0.000
64	A	96	LYS	1	0.925	0.967	22.756	0.321	0.321	0.000	0.000	0.000	0.000
65	A	97	ASN	0	-0.060	-0.035	20.464	0.046	0.046	0.000	0.000	0.000	0.000
66	A	98	VAL	0	0.022	0.013	23.335	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	99	GLU	-1	-0.843	-0.896	24.981	-0.202	-0.202	0.000	0.000	0.000	0.000
68	A	100	GLU	-1	-0.850	-0.909	27.712	-0.128	-0.128	0.000	0.000	0.000	0.000
69	A	101	ARG	1	0.836	0.872	26.145	0.163	0.163	0.000	0.000	0.000	0.000
70	A	102	PRO	0	0.011	0.016	31.026	0.003	0.003	0.000	0.000	0.000	0.000
71	A	103	ILE	0	-0.024	-0.006	29.254	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	104	VAL	0	0.025	-0.005	33.332	0.006	0.006	0.000	0.000	0.000	0.000
73	A	105	GLY	0	0.006	0.013	35.334	0.001	0.001	0.000	0.000	0.000	0.000
74	A	106	ALA	0	0.023	0.006	35.090	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	107	PRO	0	0.034	0.008	32.472	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	108	VAL	0	0.000	-0.004	28.041	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	109	ASP	-1	-0.868	-0.934	28.624	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	110	ALA	0	0.003	0.009	29.418	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	111	LEU	0	-0.031	-0.020	25.077	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	112	VAL	0	0.001	-0.002	24.304	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	113	ASN	0	0.022	0.018	24.616	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	114	LEU	0	-0.026	-0.003	24.914	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	115	ALA	0	-0.023	-0.020	21.000	-0.024	-0.024	0.000	0.000	0.000	0.000
84	A	116	ASP	-1	-0.870	-0.930	20.807	-0.099	-0.099	0.000	0.000	0.000	0.000
85	A	117	GLU	-1	-0.975	-0.995	21.957	-0.137	-0.137	0.000	0.000	0.000	0.000
86	A	118	GLU	-1	-0.835	-0.896	21.641	-0.243	-0.243	0.000	0.000	0.000	0.000
87	A	119	LYS	1	0.798	0.910	16.870	0.177	0.177	0.000	0.000	0.000	0.000
88	A	120	ALA	0	-0.018	-0.004	16.764	-0.061	-0.061	0.000	0.000	0.000	0.000
89	A	121	ASP	-1	-0.811	-0.907	12.708	-0.707	-0.707	0.000	0.000	0.000	0.000
90	A	122	LEU	0	-0.039	-0.019	14.934	0.049	0.049	0.000	0.000	0.000	0.000
91	A	123	LEU	0	-0.002	0.011	17.147	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	124	VAL	0	-0.013	-0.013	20.113	0.020	0.020	0.000	0.000	0.000	0.000
93	A	125	VAL	0	0.031	0.009	22.614	0.000	0.000	0.000	0.000	0.000	0.000
94	A	126	GLY	0	0.037	0.029	25.804	0.003	0.003	0.000	0.000	0.000	0.000
95	A	127	ASN	0	-0.103	-0.066	28.307	0.008	0.008	0.000	0.000	0.000	0.000
96	A	128	VAL	0	0.048	0.017	29.673	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	129	GLY	0	-0.006	-0.002	33.216	0.006	0.006	0.000	0.000	0.000	0.000
98	A	130	LEU	0	0.046	0.035	35.917	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	131	SER	0	-0.030	-0.032	39.131	0.003	0.003	0.000	0.000	0.000	0.000
100	A	132	THR	0	0.035	0.029	41.321	0.002	0.002	0.000	0.000	0.000	0.000
101	A	133	ILE	0	0.065	0.019	42.223	0.001	0.001	0.000	0.000	0.000	0.000
102	A	134	ALA	0	0.046	0.022	42.078	0.002	0.002	0.000	0.000	0.000	0.000
103	A	135	GLY	0	0.004	0.001	40.071	0.002	0.002	0.000	0.000	0.000	0.000
104	A	136	ARG	1	0.876	0.933	37.409	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	137	LEU	0	-0.041	-0.024	37.210	0.003	0.003	0.000	0.000	0.000	0.000
106	A	138	LEU	0	-0.007	-0.005	37.562	0.004	0.004	0.000	0.000	0.000	0.000
107	A	139	GLY	0	0.012	0.036	34.329	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	140	SER	0	0.049	0.022	28.885	0.007	0.007	0.000	0.000	0.000	0.000
109	A	141	VAL	0	0.049	-0.002	28.301	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	142	PRO	0	0.039	0.021	24.543	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	143	ALA	0	0.085	0.052	26.475	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	144	ASN	0	0.010	0.002	28.769	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	145	VAL	0	-0.003	-0.007	25.849	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	146	SER	0	0.028	0.034	25.919	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	147	ARG	1	0.906	0.947	27.442	-0.019	-0.019	0.000	0.000	0.000	0.000
116	A	148	ARG	1	0.847	0.920	30.691	-0.049	-0.049	0.000	0.000	0.000	0.000
117	A	149	ALA	0	-0.013	-0.009	27.469	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	150	LYS	1	0.917	0.966	28.195	0.008	0.008	0.000	0.000	0.000	0.000
119	A	151	VAL	0	0.022	0.024	22.827	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	152	ASP	-1	-0.816	-0.896	21.405	-0.070	-0.070	0.000	0.000	0.000	0.000
121	A	153	VAL	0	-0.061	-0.050	20.998	0.018	0.018	0.000	0.000	0.000	0.000
122	A	154	LEU	0	0.020	0.016	13.917	-0.016	-0.016	0.000	0.000	0.000	0.000
123	A	155	ILE	0	-0.031	-0.017	17.619	0.044	0.044	0.000	0.000	0.000	0.000
124	A	156	VAL	0	-0.004	0.004	11.287	-0.043	-0.043	0.000	0.000	0.000	0.000
125	A	157	HIS	0	0.016	0.023	12.445	0.071	0.071	0.000	0.000	0.000	0.000
126	A	158	THR	0	0.021	-0.004	13.048	0.091	0.091	0.000	0.000	0.000	0.000
127	A	159	THR	0	-0.002	0.004	11.345	-0.125	-0.125	0.000	0.000	0.000	0.000

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