FMO DATABASE

FMODB ID: G5JK1

Calculation Name: 1TZV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TZV

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X286

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1463114.483265
FMO2-HF: Nuclear repulsion	1404626.980891
FMO2-HF: Total energy	-58487.502373
FMO2-MP2: Total energy	-58660.467272

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:1:MET)

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

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.
-0.681	0.453	0	-0.469	-0.666	0.002

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.002 / q_NPA : -0.019

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].	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	3	THR	0	0.009	-0.029	3.857	-0.712	0.422	-0.469	-0.666	0.002
4	A	4	PRO	0	-0.038	-0.007	5.643	0.404	0.404	0.000	0.000	0.000
5	A	5	ARG	1	0.922	0.916	8.253	-0.336	-0.336	0.000	0.000	0.000
6	A	6	ARG	1	0.860	0.900	12.000	-0.245	-0.245	0.000	0.000	0.000
7	A	7	ARG	1	0.871	0.928	7.916	0.415	0.415	0.000	0.000	0.000
8	A	8	MET	0	-0.007	0.018	11.198	-0.032	-0.032	0.000	0.000	0.000
9	A	9	ARG	1	0.828	0.860	12.579	-0.073	-0.073	0.000	0.000	0.000
10	A	10	LEU	0	-0.011	-0.017	13.955	0.003	0.003	0.000	0.000	0.000
11	A	11	ALA	0	-0.034	-0.008	14.222	0.004	0.004	0.000	0.000	0.000
12	A	12	VAL	0	0.036	0.024	16.200	0.009	0.009	0.000	0.000	0.000
13	A	13	PHE	0	-0.003	-0.008	18.982	0.008	0.008	0.000	0.000	0.000
14	A	14	LYS	1	0.880	0.945	14.116	0.115	0.115	0.000	0.000	0.000
15	A	15	ALA	0	0.053	0.030	20.260	0.005	0.005	0.000	0.000	0.000
16	A	16	LEU	0	0.005	-0.002	21.962	0.005	0.005	0.000	0.000	0.000
17	A	17	PHE	0	-0.047	-0.028	23.552	0.005	0.005	0.000	0.000	0.000
18	A	18	GLN	0	0.036	0.005	21.697	0.002	0.002	0.000	0.000	0.000
19	A	19	HIS	0	0.011	0.018	25.646	0.004	0.004	0.000	0.000	0.000
20	A	20	GLU	-1	-0.783	-0.858	27.930	0.001	0.001	0.000	0.000	0.000
21	A	21	PHE	0	-0.068	-0.037	28.399	0.004	0.004	0.000	0.000	0.000
22	A	22	ARG	1	0.721	0.800	24.162	0.038	0.038	0.000	0.000	0.000
23	A	23	ARG	1	0.854	0.911	30.344	0.003	0.003	0.000	0.000	0.000
24	A	24	ASP	-1	-0.926	-0.950	32.751	-0.020	-0.020	0.000	0.000	0.000
25	A	25	GLU	-1	-0.808	-0.862	28.493	-0.036	-0.036	0.000	0.000	0.000
26	A	26	ASP	-1	-0.811	-0.900	27.628	-0.043	-0.043	0.000	0.000	0.000
27	A	27	LEU	0	0.048	0.010	24.835	-0.005	-0.005	0.000	0.000	0.000
28	A	28	GLU	-1	-0.828	-0.892	23.050	-0.069	-0.069	0.000	0.000	0.000
29	A	29	GLN	0	-0.011	-0.008	22.337	-0.014	-0.014	0.000	0.000	0.000
30	A	30	ILE	0	0.016	0.019	22.619	-0.006	-0.006	0.000	0.000	0.000
31	A	31	LEU	0	-0.025	-0.018	17.463	-0.004	-0.004	0.000	0.000	0.000
32	A	32	GLU	-1	-0.800	-0.874	18.030	-0.179	-0.179	0.000	0.000	0.000
33	A	33	GLU	-1	-0.856	-0.881	17.815	-0.065	-0.065	0.000	0.000	0.000
34	A	34	ILE	0	-0.091	-0.041	16.086	0.006	0.006	0.000	0.000	0.000
35	A	35	LEU	0	-0.079	-0.025	13.254	-0.032	-0.032	0.000	0.000	0.000
36	A	36	ASP	-1	-0.692	-0.801	10.744	-0.249	-0.249	0.000	0.000	0.000
37	A	37	GLU	-1	-0.882	-0.955	9.778	-0.215	-0.215	0.000	0.000	0.000
38	A	38	THR	0	-0.096	-0.070	6.514	-0.145	-0.145	0.000	0.000	0.000
39	A	39	TYR	0	-0.067	-0.011	6.536	-0.346	-0.346	0.000	0.000	0.000
40	A	40	ASP	-1	-0.735	-0.848	6.235	-0.845	-0.845	0.000	0.000	0.000
41	A	41	LYS	1	0.926	0.943	8.130	0.414	0.414	0.000	0.000	0.000
42	A	42	LYS	1	0.853	0.920	10.488	0.103	0.103	0.000	0.000	0.000
43	A	43	ALA	0	0.010	-0.003	9.290	0.083	0.083	0.000	0.000	0.000
44	A	44	LYS	1	0.824	0.898	11.046	0.467	0.467	0.000	0.000	0.000
45	A	45	GLU	-1	-0.896	-0.941	13.801	-0.095	-0.095	0.000	0.000	0.000
46	A	46	ASP	-1	-0.788	-0.870	14.126	0.000	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.035	0.005	15.177	0.023	0.023	0.000	0.000	0.000
48	A	48	ARG	1	0.832	0.870	16.985	0.191	0.191	0.000	0.000	0.000
49	A	49	ARG	1	0.758	0.854	17.578	0.034	0.034	0.000	0.000	0.000
50	A	50	TYR	0	-0.014	-0.046	18.319	0.009	0.009	0.000	0.000	0.000
51	A	51	ILE	0	-0.026	0.001	20.815	0.008	0.008	0.000	0.000	0.000
52	A	52	ARG	1	0.856	0.912	23.087	0.064	0.064	0.000	0.000	0.000
53	A	53	GLY	0	0.032	0.023	24.712	0.005	0.005	0.000	0.000	0.000
54	A	54	ILE	0	0.005	-0.016	23.384	0.006	0.006	0.000	0.000	0.000
55	A	55	LYS	1	0.769	0.857	27.049	0.046	0.046	0.000	0.000	0.000
56	A	56	GLU	-1	-0.941	-0.962	29.055	-0.020	-0.020	0.000	0.000	0.000
57	A	57	ASN	0	-0.044	-0.032	29.428	0.005	0.005	0.000	0.000	0.000
58	A	58	LEU	0	0.011	0.025	29.963	0.004	0.004	0.000	0.000	0.000
59	A	59	SER	0	0.008	-0.012	32.230	0.002	0.002	0.000	0.000	0.000
60	A	60	MET	0	-0.026	0.002	32.347	0.003	0.003	0.000	0.000	0.000
61	A	61	ILE	0	0.023	0.012	28.568	0.003	0.003	0.000	0.000	0.000
62	A	62	ASP	-1	-0.765	-0.867	32.547	0.005	0.005	0.000	0.000	0.000
63	A	63	ASP	-1	-0.853	-0.891	34.588	0.011	0.011	0.000	0.000	0.000
64	A	64	LEU	0	-0.004	-0.002	32.960	0.002	0.002	0.000	0.000	0.000
65	A	65	ILE	0	0.000	-0.013	30.439	0.002	0.002	0.000	0.000	0.000
66	A	66	SER	0	-0.062	-0.055	34.702	0.002	0.002	0.000	0.000	0.000
67	A	67	ARG	1	0.817	0.907	38.168	-0.012	-0.012	0.000	0.000	0.000
68	A	68	TYR	0	-0.110	-0.077	35.852	0.001	0.001	0.000	0.000	0.000
69	A	69	LEU	0	-0.088	-0.034	35.488	0.002	0.002	0.000	0.000	0.000
70	A	70	GLU	-1	-0.843	-0.931	39.440	0.018	0.018	0.000	0.000	0.000
71	A	71	LYS	1	0.946	0.995	42.278	-0.023	-0.023	0.000	0.000	0.000
72	A	72	TRP	0	-0.060	-0.018	37.987	-0.001	-0.001	0.000	0.000	0.000
73	A	73	SER	0	0.095	0.026	39.586	0.000	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.071	0.044	32.596	0.000	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.032	0.018	35.254	0.001	0.001	0.000	0.000	0.000
76	A	76	ARG	1	0.851	0.914	37.462	-0.014	-0.014	0.000	0.000	0.000
77	A	77	LEU	0	-0.017	0.016	33.394	0.001	0.001	0.000	0.000	0.000
78	A	78	SER	0	-0.012	-0.033	30.758	-0.003	-0.003	0.000	0.000	0.000
79	A	79	VAL	0	0.028	0.008	28.632	0.000	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.030	0.030	25.208	-0.003	-0.003	0.000	0.000	0.000
81	A	81	ASP	-1	-0.844	-0.898	27.206	0.026	0.026	0.000	0.000	0.000
82	A	82	ARG	1	0.776	0.857	29.131	-0.004	-0.004	0.000	0.000	0.000
83	A	83	ASN	0	-0.017	-0.026	25.684	-0.003	-0.003	0.000	0.000	0.000
84	A	84	VAL	0	-0.006	-0.001	23.581	-0.002	-0.002	0.000	0.000	0.000
85	A	85	LEU	0	0.005	0.008	25.351	0.003	0.003	0.000	0.000	0.000
86	A	86	ARG	1	0.786	0.849	27.448	0.002	0.002	0.000	0.000	0.000
87	A	87	LEU	0	-0.024	-0.002	20.140	0.000	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.023	0.004	23.746	0.001	0.001	0.000	0.000	0.000
89	A	89	THR	0	-0.004	-0.014	24.687	0.004	0.004	0.000	0.000	0.000
90	A	90	TYR	0	-0.034	-0.033	22.280	-0.001	-0.001	0.000	0.000	0.000
91	A	91	GLU	-1	-0.726	-0.800	19.379	0.064	0.064	0.000	0.000	0.000
92	A	92	LEU	0	-0.026	-0.025	23.566	0.007	0.007	0.000	0.000	0.000
93	A	93	LEU	0	-0.015	-0.009	26.446	0.002	0.002	0.000	0.000	0.000
94	A	94	PHE	0	-0.001	-0.001	25.758	-0.001	-0.001	0.000	0.000	0.000
95	A	95	GLU	-1	-0.785	-0.834	20.424	0.000	0.000	0.000	0.000	0.000
96	A	96	LYN	0	-0.050	-0.032	22.842	0.015	0.015	0.000	0.000	0.000
97	A	97	ASP	-1	-0.916	-0.962	18.398	0.111	0.111	0.000	0.000	0.000
98	A	98	ILE	0	-0.054	-0.019	17.312	0.021	0.021	0.000	0.000	0.000
99	A	99	PRO	0	0.039	0.026	20.296	-0.015	-0.015	0.000	0.000	0.000
100	A	100	ILE	0	0.051	0.000	22.956	0.002	0.002	0.000	0.000	0.000
101	A	101	GLU	-1	-0.919	-0.953	23.598	0.119	0.119	0.000	0.000	0.000
102	A	102	VAL	0	0.004	0.003	18.050	0.003	0.003	0.000	0.000	0.000
103	A	103	THR	0	-0.030	-0.038	20.480	-0.001	-0.001	0.000	0.000	0.000
104	A	104	ILE	0	-0.021	-0.002	22.207	-0.010	-0.010	0.000	0.000	0.000
105	A	105	ASP	-1	-0.850	-0.930	21.373	0.102	0.102	0.000	0.000	0.000
106	A	106	GLU	-1	-0.803	-0.872	15.716	0.170	0.170	0.000	0.000	0.000
107	A	107	ALA	0	0.006	0.013	19.544	-0.013	-0.013	0.000	0.000	0.000
108	A	108	ILE	0	-0.020	-0.017	22.368	-0.008	-0.008	0.000	0.000	0.000
109	A	109	GLU	-1	-0.831	-0.873	17.333	0.135	0.135	0.000	0.000	0.000
110	A	110	ILE	0	-0.045	-0.022	18.499	-0.006	-0.006	0.000	0.000	0.000
111	A	111	ALA	0	0.007	0.000	21.374	-0.005	-0.005	0.000	0.000	0.000
112	A	112	LYS	1	0.784	0.890	23.890	-0.073	-0.073	0.000	0.000	0.000
113	A	113	ARG	1	0.884	0.949	16.037	-0.044	-0.044	0.000	0.000	0.000
114	A	114	TYR	0	-0.013	-0.003	18.807	-0.001	-0.001	0.000	0.000	0.000
115	A	115	GLY	0	0.065	0.035	24.710	-0.005	-0.005	0.000	0.000	0.000
116	A	116	THR	0	-0.009	-0.003	28.036	0.002	0.002	0.000	0.000	0.000
117	A	117	GLU	-1	-0.760	-0.882	28.607	0.065	0.065	0.000	0.000	0.000
118	A	118	ASN	0	0.019	-0.009	29.761	0.003	0.003	0.000	0.000	0.000
119	A	119	SER	0	0.040	0.034	28.887	0.000	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.040	0.020	27.444	-0.001	-0.001	0.000	0.000	0.000
121	A	121	LYS	1	0.875	0.940	28.209	-0.049	-0.049	0.000	0.000	0.000
122	A	122	PHE	0	-0.016	-0.007	31.409	-0.001	-0.001	0.000	0.000	0.000
123	A	123	VAL	0	0.030	0.009	26.378	-0.001	-0.001	0.000	0.000	0.000
124	A	124	ASN	0	0.028	0.011	28.977	0.001	0.001	0.000	0.000	0.000
125	A	125	GLY	0	0.004	0.009	29.846	0.000	0.000	0.000	0.000	0.000
126	A	126	ILE	0	-0.034	-0.019	32.227	-0.002	-0.002	0.000	0.000	0.000
127	A	127	LEU	0	0.029	0.005	26.244	-0.002	-0.002	0.000	0.000	0.000
128	A	128	ASP	-1	-0.800	-0.882	30.349	0.048	0.048	0.000	0.000	0.000
129	A	129	ARG	1	0.848	0.929	31.996	-0.029	-0.029	0.000	0.000	0.000
130	A	130	ILE	0	0.022	0.012	31.206	-0.001	-0.001	0.000	0.000	0.000
131	A	131	ALA	0	0.008	0.001	29.676	-0.001	-0.001	0.000	0.000	0.000
132	A	132	LYS	1	0.807	0.887	31.547	-0.045	-0.045	0.000	0.000	0.000
133	A	133	GLU	-1	-0.808	-0.871	34.625	0.024	0.024	0.000	0.000	0.000
134	A	134	HIS	1	0.757	0.872	33.723	-0.027	-0.027	0.000	0.000	0.000
135	A	135	ALA	0	0.044	0.034	29.871	-0.001	-0.001	0.000	0.000	0.000
136	A	136	PRO	0	-0.041	-0.003	28.741	-0.001	-0.001	0.000	0.000	0.000
137	A	137	LYS	1	0.969	0.977	30.632	-0.022	-0.022	0.000	0.000	0.000
138	A	138	GLU	-1	-0.866	-0.940	28.779	0.037	0.037	0.000	0.000	0.000
139	A	139	LYS	1	0.787	0.907	23.687	-0.053	-0.053	0.000	0.000	0.000
140	A	140	PHE	0	-0.054	-0.011	28.189	0.002	0.002	0.000	0.000	0.000
141	A	141	GLU	-1	-0.994	-0.990	27.821	0.074	0.074	0.000	0.000	0.000

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