FMO DATABASE

FMODB ID: 2NRQR

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

Total energy (hartree)

FMO2-HF: Electronic energy	-904762.898191
FMO2-HF: Nuclear repulsion	859254.909751
FMO2-HF: Total energy	-45507.988439
FMO2-MP2: Total energy	-45643.048646

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.
-1.115	0.122	-0.007	-0.5	-0.73	0.002

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 : -0.017 / 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

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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	-0.012	-0.013	3.852	-1.181	0.056	-0.007	-0.500	-0.730	0.002
4	A	16	ALA	0	0.019	0.016	6.403	0.721	0.721	0.000	0.000	0.000	0.000
5	A	17	TYR	0	0.012	0.006	9.589	-0.207	-0.207	0.000	0.000	0.000	0.000
6	A	18	LYS	1	0.847	0.901	9.404	1.328	1.328	0.000	0.000	0.000	0.000
7	A	19	THR	0	-0.002	0.006	14.441	0.044	0.044	0.000	0.000	0.000	0.000
8	A	20	VAL	0	0.025	0.022	16.997	0.033	0.033	0.000	0.000	0.000	0.000
9	A	21	VAL	0	0.013	0.009	19.147	0.012	0.012	0.000	0.000	0.000	0.000
10	A	22	VAL	0	-0.018	-0.016	22.461	0.016	0.016	0.000	0.000	0.000	0.000
11	A	23	GLY	0	-0.010	0.013	24.887	0.001	0.001	0.000	0.000	0.000	0.000
12	A	24	THR	0	-0.037	-0.050	28.248	0.007	0.007	0.000	0.000	0.000	0.000
13	A	25	ASP	-1	-0.810	-0.850	31.293	-0.051	-0.051	0.000	0.000	0.000	0.000
14	A	26	GLY	0	0.047	0.031	34.295	0.003	0.003	0.000	0.000	0.000	0.000
15	A	27	SER	0	-0.076	-0.056	34.478	0.003	0.003	0.000	0.000	0.000	0.000
16	A	28	ASP	-1	-0.788	-0.900	33.978	-0.053	-0.053	0.000	0.000	0.000	0.000
17	A	29	SER	0	-0.056	-0.030	31.268	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	30	SER	0	0.004	-0.014	29.672	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	31	MET	0	0.056	0.033	29.153	-0.013	-0.013	0.000	0.000	0.000	0.000
20	A	32	ARG	1	0.821	0.907	28.493	0.040	0.040	0.000	0.000	0.000	0.000
21	A	33	ALA	0	0.002	0.003	25.382	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	34	VAL	0	0.009	0.007	24.537	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	35	ASP	-1	-0.790	-0.856	25.092	-0.119	-0.119	0.000	0.000	0.000	0.000
24	A	36	ARG	1	0.788	0.875	19.754	0.065	0.065	0.000	0.000	0.000	0.000
25	A	37	ALA	0	0.014	-0.006	20.530	-0.022	-0.022	0.000	0.000	0.000	0.000
26	A	38	ALA	0	0.012	0.009	20.403	-0.040	-0.040	0.000	0.000	0.000	0.000
27	A	39	GLN	0	-0.014	-0.009	17.629	0.005	0.005	0.000	0.000	0.000	0.000
28	A	40	ILE	0	-0.090	-0.040	15.073	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	41	ALA	0	0.006	0.012	16.273	-0.069	-0.069	0.000	0.000	0.000	0.000
30	A	42	GLY	0	0.024	0.022	18.269	-0.047	-0.047	0.000	0.000	0.000	0.000
31	A	43	ALA	0	-0.015	-0.042	18.763	0.043	0.043	0.000	0.000	0.000	0.000
32	A	44	ASP	-1	-0.924	-0.948	15.197	-0.545	-0.545	0.000	0.000	0.000	0.000
33	A	45	ALA	0	-0.012	0.016	15.350	-0.082	-0.082	0.000	0.000	0.000	0.000
34	A	46	LYS	1	0.774	0.871	17.159	0.353	0.353	0.000	0.000	0.000	0.000
35	A	47	LEU	0	-0.010	-0.009	19.866	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	48	ILE	0	-0.018	-0.007	22.520	0.017	0.017	0.000	0.000	0.000	0.000
37	A	49	ILE	0	0.011	0.005	25.053	0.011	0.011	0.000	0.000	0.000	0.000
38	A	50	ALA	0	0.014	0.007	27.744	0.006	0.006	0.000	0.000	0.000	0.000
39	A	51	SER	0	-0.026	-0.037	29.344	0.008	0.008	0.000	0.000	0.000	0.000
40	A	52	ALA	0	0.003	-0.001	32.838	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	53	TYR	0	0.003	-0.010	35.170	0.003	0.003	0.000	0.000	0.000	0.000
42	A	54	LEU	0	-0.025	-0.010	37.947	0.003	0.003	0.000	0.000	0.000	0.000
43	A	55	PRO	0	-0.025	0.002	40.848	0.004	0.004	0.000	0.000	0.000	0.000
44	A	76	THR	0	-0.003	-0.017	42.896	0.001	0.001	0.000	0.000	0.000	0.000
45	A	77	ALA	0	0.012	0.015	42.162	0.002	0.002	0.000	0.000	0.000	0.000
46	A	78	PRO	0	0.092	0.018	41.934	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	79	ILE	0	-0.015	0.008	35.699	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	80	TYR	0	0.016	-0.011	36.680	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	81	GLU	-1	-0.943	-0.948	37.852	-0.067	-0.067	0.000	0.000	0.000	0.000
50	A	82	ILE	0	0.006	-0.001	35.076	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	83	LEU	0	-0.051	-0.027	32.039	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	84	HIS	0	-0.038	-0.016	33.162	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	85	ASP	-1	-0.857	-0.930	34.340	-0.088	-0.088	0.000	0.000	0.000	0.000
54	A	86	ALA	0	-0.052	-0.032	30.671	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	87	LYS	1	0.856	0.916	29.812	0.142	0.142	0.000	0.000	0.000	0.000
56	A	88	GLU	-1	-0.840	-0.907	30.203	-0.128	-0.128	0.000	0.000	0.000	0.000
57	A	89	ARG	1	0.788	0.872	29.888	0.084	0.084	0.000	0.000	0.000	0.000
58	A	90	ALA	0	0.015	-0.005	26.156	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	91	HIS	0	-0.051	-0.037	26.474	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	92	ASN	0	-0.077	-0.048	28.096	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	93	ALA	0	-0.056	-0.015	25.588	0.002	0.002	0.000	0.000	0.000	0.000
62	A	94	GLY	0	-0.029	-0.014	24.269	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	95	ALA	0	-0.033	0.000	22.713	-0.025	-0.025	0.000	0.000	0.000	0.000
64	A	96	LYS	1	0.927	0.966	22.868	0.298	0.298	0.000	0.000	0.000	0.000
65	A	97	ASN	0	-0.063	-0.037	20.224	0.049	0.049	0.000	0.000	0.000	0.000
66	A	98	VAL	0	0.002	0.006	23.584	-0.013	-0.013	0.000	0.000	0.000	0.000
67	A	99	GLU	-1	-0.820	-0.888	25.298	-0.210	-0.210	0.000	0.000	0.000	0.000
68	A	100	GLU	-1	-0.863	-0.925	28.065	-0.128	-0.128	0.000	0.000	0.000	0.000
69	A	101	ARG	1	0.820	0.863	26.172	0.177	0.177	0.000	0.000	0.000	0.000
70	A	102	PRO	0	0.005	0.006	31.083	0.006	0.006	0.000	0.000	0.000	0.000
71	A	103	ILE	0	-0.020	0.010	29.444	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	104	VAL	0	0.016	-0.006	33.608	0.006	0.006	0.000	0.000	0.000	0.000
73	A	105	GLY	0	0.009	0.015	35.514	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	106	ALA	0	0.017	0.004	34.896	0.001	0.001	0.000	0.000	0.000	0.000
75	A	107	PRO	0	0.023	0.003	32.674	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	108	VAL	0	-0.009	-0.005	28.393	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	109	ASP	-1	-0.854	-0.933	28.641	-0.032	-0.032	0.000	0.000	0.000	0.000
78	A	110	ALA	0	0.012	0.011	29.341	-0.009	-0.009	0.000	0.000	0.000	0.000
79	A	111	LEU	0	-0.020	-0.006	25.081	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	112	VAL	0	-0.005	-0.002	24.334	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	113	ASN	0	0.007	-0.003	24.706	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	114	LEU	0	-0.032	-0.004	25.086	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	115	ALA	0	-0.012	-0.018	21.140	-0.025	-0.025	0.000	0.000	0.000	0.000
84	A	116	ASP	-1	-0.884	-0.939	20.874	-0.144	-0.144	0.000	0.000	0.000	0.000
85	A	117	GLU	-1	-0.929	-0.977	21.736	-0.194	-0.194	0.000	0.000	0.000	0.000
86	A	118	GLU	-1	-0.799	-0.873	21.723	-0.257	-0.257	0.000	0.000	0.000	0.000
87	A	119	LYS	1	0.738	0.878	17.024	0.194	0.194	0.000	0.000	0.000	0.000
88	A	120	ALA	0	-0.006	0.007	16.704	-0.069	-0.069	0.000	0.000	0.000	0.000
89	A	121	ASP	-1	-0.795	-0.887	12.644	-0.754	-0.754	0.000	0.000	0.000	0.000
90	A	122	LEU	0	-0.045	-0.019	14.596	0.043	0.043	0.000	0.000	0.000	0.000
91	A	123	LEU	0	0.015	0.016	17.003	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	124	VAL	0	-0.012	-0.004	20.076	0.027	0.027	0.000	0.000	0.000	0.000
93	A	125	VAL	0	0.036	0.011	22.612	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	126	GLY	0	0.054	0.032	25.979	0.005	0.005	0.000	0.000	0.000	0.000
95	A	127	ASN	0	-0.112	-0.070	28.262	0.005	0.005	0.000	0.000	0.000	0.000
96	A	128	VAL	0	0.042	0.015	29.710	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	129	GLY	0	0.020	0.009	33.225	0.005	0.005	0.000	0.000	0.000	0.000
98	A	130	LEU	0	0.020	0.013	35.885	0.000	0.000	0.000	0.000	0.000	0.000
99	A	131	SER	0	-0.006	-0.016	39.321	0.004	0.004	0.000	0.000	0.000	0.000
100	A	132	THR	0	0.026	0.023	41.498	0.003	0.003	0.000	0.000	0.000	0.000
101	A	133	ILE	0	0.065	0.021	42.159	0.001	0.001	0.000	0.000	0.000	0.000
102	A	134	ALA	0	0.037	0.016	41.819	0.003	0.003	0.000	0.000	0.000	0.000
103	A	135	GLY	0	0.009	0.007	39.836	0.001	0.001	0.000	0.000	0.000	0.000
104	A	136	ARG	1	0.846	0.925	37.512	-0.015	-0.015	0.000	0.000	0.000	0.000
105	A	137	LEU	0	-0.032	-0.013	36.879	0.004	0.004	0.000	0.000	0.000	0.000
106	A	138	LEU	0	0.004	0.001	37.189	0.004	0.004	0.000	0.000	0.000	0.000
107	A	139	GLY	0	0.013	0.030	34.258	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	140	SER	0	0.035	0.010	28.688	0.007	0.007	0.000	0.000	0.000	0.000
109	A	141	VAL	0	0.043	0.006	27.993	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	142	PRO	0	0.051	0.025	24.344	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	143	ALA	0	0.087	0.056	26.321	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	144	ASN	0	0.022	0.004	28.651	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	145	VAL	0	-0.011	-0.011	26.034	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	146	SER	0	0.019	0.011	25.709	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	147	ARG	1	0.901	0.944	27.246	-0.033	-0.033	0.000	0.000	0.000	0.000
116	A	148	ARG	1	0.844	0.919	30.830	-0.067	-0.067	0.000	0.000	0.000	0.000
117	A	149	ALA	0	0.007	-0.001	27.385	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	150	LYS	1	0.892	0.955	28.365	-0.016	-0.016	0.000	0.000	0.000	0.000
119	A	151	VAL	0	0.029	0.031	22.822	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	152	ASP	-1	-0.783	-0.862	21.420	-0.030	-0.030	0.000	0.000	0.000	0.000
121	A	153	VAL	0	-0.062	-0.048	21.047	0.022	0.022	0.000	0.000	0.000	0.000
122	A	154	LEU	0	0.018	0.018	14.223	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	155	ILE	0	-0.032	-0.025	17.630	0.042	0.042	0.000	0.000	0.000	0.000
124	A	156	VAL	0	0.002	0.012	10.933	-0.049	-0.049	0.000	0.000	0.000	0.000
125	A	157	HIS	0	0.027	0.026	12.790	0.094	0.094	0.000	0.000	0.000	0.000
126	A	158	THR	0	0.015	0.002	12.903	0.082	0.082	0.000	0.000	0.000	0.000
127	A	159	THR	0	-0.008	-0.005	11.295	-0.122	-0.122	0.000	0.000	0.000	0.000

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