FMO DATABASE

FMODB ID: N1V5Q

Calculation Name: 3TUF-A-Xray320

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3TUF

Chain ID: A

ChEMBL ID:

UniProt ID: P71044

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	117
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-848044.590632
FMO2-HF: Nuclear repulsion	803085.243269
FMO2-HF: Total energy	-44959.347364
FMO2-MP2: Total energy	-45091.364613

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:102:ACE )

Summations of interaction energy for fragment #1(A:102:ACE )

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.
-0.542	0.939	-0.005	-0.739	-0.738	-0.003

Interaction energy analysis for fragmet #1(A:102:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.053 / q_NPA : -0.043

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	104	ASP	-1	-0.831	-0.891	3.869	-0.138	1.343	-0.005	-0.739	-0.738	-0.003
4	A	105	LEU	0	0.050	0.021	7.263	0.098	0.098	0.000	0.000	0.000	0.000
5	A	106	PHE	0	-0.013	0.000	10.271	0.121	0.121	0.000	0.000	0.000	0.000
6	A	107	THR	0	-0.048	-0.049	9.323	0.005	0.005	0.000	0.000	0.000	0.000
7	A	108	THR	0	-0.004	0.006	8.474	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	109	TYR	0	0.042	0.038	10.862	0.133	0.133	0.000	0.000	0.000	0.000
9	A	110	ARG	1	0.829	0.921	14.354	0.300	0.300	0.000	0.000	0.000	0.000
10	A	111	LEU	0	-0.009	0.001	11.470	0.058	0.058	0.000	0.000	0.000	0.000
11	A	112	ASP	-1	-0.846	-0.925	13.785	-0.475	-0.475	0.000	0.000	0.000	0.000
12	A	113	LEU	0	-0.074	-0.039	16.270	0.047	0.047	0.000	0.000	0.000	0.000
13	A	114	GLU	-1	-0.893	-0.957	18.393	-0.141	-0.141	0.000	0.000	0.000	0.000
14	A	115	ASP	-1	-0.910	-0.944	16.784	-0.230	-0.230	0.000	0.000	0.000	0.000
15	A	116	ALA	0	-0.080	-0.051	20.098	0.028	0.028	0.000	0.000	0.000	0.000
16	A	117	ARG	1	0.856	0.909	22.221	0.180	0.180	0.000	0.000	0.000	0.000
17	A	118	SER	0	-0.055	-0.033	22.837	0.023	0.023	0.000	0.000	0.000	0.000
18	A	119	LYS	1	0.931	0.972	20.500	0.204	0.204	0.000	0.000	0.000	0.000
19	A	120	GLH	0	0.009	-0.003	26.226	0.016	0.016	0.000	0.000	0.000	0.000
20	A	121	ARG	1	0.886	0.952	24.591	0.126	0.126	0.000	0.000	0.000	0.000
21	A	122	GLU	-1	-0.942	-0.968	28.742	-0.078	-0.078	0.000	0.000	0.000	0.000
22	A	123	GLU	-1	-0.923	-0.963	29.512	-0.098	-0.098	0.000	0.000	0.000	0.000
23	A	124	LEU	0	-0.061	-0.025	31.724	0.007	0.007	0.000	0.000	0.000	0.000
24	A	125	ASN	0	-0.005	-0.025	33.732	0.009	0.009	0.000	0.000	0.000	0.000
25	A	126	ALA	0	0.003	0.024	34.640	0.006	0.006	0.000	0.000	0.000	0.000
26	A	127	ILE	0	-0.022	-0.013	35.881	0.005	0.005	0.000	0.000	0.000	0.000
27	A	128	VAL	0	-0.029	-0.021	38.471	0.004	0.004	0.000	0.000	0.000	0.000
28	A	129	SER	0	-0.085	-0.054	38.551	0.005	0.005	0.000	0.000	0.000	0.000
29	A	130	SER	0	-0.011	0.011	40.808	0.004	0.004	0.000	0.000	0.000	0.000
30	A	131	ASP	-1	-0.924	-0.978	42.433	-0.035	-0.035	0.000	0.000	0.000	0.000
31	A	132	ASP	-1	-0.983	-0.992	43.985	-0.038	-0.038	0.000	0.000	0.000	0.000
32	A	133	ALA	0	-0.040	0.014	42.490	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	134	THR	0	-0.058	-0.063	44.517	0.003	0.003	0.000	0.000	0.000	0.000
34	A	135	ALA	0	0.011	-0.015	45.737	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	136	LYS	1	0.922	0.961	46.226	0.042	0.042	0.000	0.000	0.000	0.000
36	A	137	GLU	-1	-0.753	-0.859	42.164	-0.052	-0.052	0.000	0.000	0.000	0.000
37	A	138	LYS	1	0.871	0.956	41.558	0.040	0.040	0.000	0.000	0.000	0.000
38	A	139	SER	0	-0.011	-0.009	41.681	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	140	GLU	-1	-0.931	-0.961	40.494	-0.058	-0.058	0.000	0.000	0.000	0.000
40	A	141	ALA	0	-0.017	-0.005	37.528	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	142	TYR	0	-0.014	-0.018	37.196	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	143	ASP	-1	-0.882	-0.944	38.271	-0.058	-0.058	0.000	0.000	0.000	0.000
43	A	144	LYS	1	0.925	0.961	34.407	0.076	0.076	0.000	0.000	0.000	0.000
44	A	145	MET	0	-0.004	0.012	33.706	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	146	THR	0	-0.022	-0.022	33.798	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	147	ALA	0	0.004	0.001	34.871	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	148	LEU	0	0.037	0.021	27.723	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	149	SER	0	0.002	0.012	30.112	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	150	GLU	-1	-0.927	-0.954	31.332	-0.068	-0.068	0.000	0.000	0.000	0.000
50	A	151	VAL	0	-0.041	-0.004	27.750	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	152	GLU	-1	-0.880	-0.957	25.405	-0.138	-0.138	0.000	0.000	0.000	0.000
52	A	153	GLY	0	-0.030	-0.022	27.407	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	154	THR	0	-0.066	-0.045	29.375	0.003	0.003	0.000	0.000	0.000	0.000
54	A	155	GLU	-1	-0.762	-0.867	24.319	-0.154	-0.154	0.000	0.000	0.000	0.000
55	A	156	LYS	1	0.995	1.003	24.588	0.093	0.093	0.000	0.000	0.000	0.000
56	A	157	GLN	0	-0.009	-0.009	26.017	0.003	0.003	0.000	0.000	0.000	0.000
57	A	158	LEU	0	0.021	0.006	27.072	0.004	0.004	0.000	0.000	0.000	0.000
58	A	159	GLU	-1	-0.819	-0.924	21.106	-0.171	-0.171	0.000	0.000	0.000	0.000
59	A	160	THR	0	-0.084	-0.053	24.749	0.006	0.006	0.000	0.000	0.000	0.000
60	A	161	LEU	0	-0.006	-0.007	26.476	0.007	0.007	0.000	0.000	0.000	0.000
61	A	162	ILE	0	0.027	0.027	24.509	0.007	0.007	0.000	0.000	0.000	0.000
62	A	163	LYS	1	0.958	0.997	21.225	0.111	0.111	0.000	0.000	0.000	0.000
63	A	164	THR	0	-0.083	-0.040	25.035	0.010	0.010	0.000	0.000	0.000	0.000
64	A	165	GLN	0	-0.107	-0.063	28.020	0.008	0.008	0.000	0.000	0.000	0.000
65	A	166	GLY	0	-0.038	-0.006	26.752	0.002	0.002	0.000	0.000	0.000	0.000
66	A	167	TYR	0	-0.065	-0.034	22.574	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	168	GLU	-1	-0.909	-0.971	16.329	-0.115	-0.115	0.000	0.000	0.000	0.000
68	A	169	ASP	-1	-0.820	-0.913	16.096	-0.197	-0.197	0.000	0.000	0.000	0.000
69	A	170	ALA	0	-0.082	-0.059	19.151	0.002	0.002	0.000	0.000	0.000	0.000
70	A	171	LEU	0	0.017	0.027	16.159	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	172	VAL	0	-0.036	-0.005	19.970	0.006	0.006	0.000	0.000	0.000	0.000
72	A	173	ASN	0	0.019	0.022	21.773	0.018	0.018	0.000	0.000	0.000	0.000
73	A	174	ALA	0	-0.046	-0.056	23.962	0.005	0.005	0.000	0.000	0.000	0.000
74	A	175	GLU	-1	-0.864	-0.938	25.830	-0.139	-0.139	0.000	0.000	0.000	0.000
75	A	176	GLY	0	-0.028	-0.001	28.174	0.008	0.008	0.000	0.000	0.000	0.000
76	A	177	ASP	-1	-0.904	-0.959	29.836	-0.091	-0.091	0.000	0.000	0.000	0.000
77	A	178	LYS	1	0.858	0.930	25.953	0.152	0.152	0.000	0.000	0.000	0.000
78	A	179	ILE	0	-0.013	0.009	27.316	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	180	ASN	0	-0.046	-0.027	22.700	0.002	0.002	0.000	0.000	0.000	0.000
80	A	181	ILE	0	0.030	0.025	23.227	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	182	THR	0	-0.027	-0.015	17.723	0.001	0.001	0.000	0.000	0.000	0.000
82	A	183	VAL	0	-0.011	-0.001	20.284	0.003	0.003	0.000	0.000	0.000	0.000
83	A	184	LYS	1	0.944	1.007	12.979	0.210	0.210	0.000	0.000	0.000	0.000
84	A	185	SER	0	-0.070	-0.085	18.477	0.032	0.032	0.000	0.000	0.000	0.000
85	A	186	ASP	-1	-0.840	-0.898	18.827	-0.090	-0.090	0.000	0.000	0.000	0.000
86	A	187	LYS	1	0.876	0.932	21.120	0.047	0.047	0.000	0.000	0.000	0.000
87	A	188	HIS	0	0.093	0.075	24.163	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	189	SER	0	-0.016	-0.032	25.998	0.007	0.007	0.000	0.000	0.000	0.000
89	A	190	LYS	1	1.032	0.999	29.700	0.058	0.058	0.000	0.000	0.000	0.000
90	A	191	SER	0	0.014	0.002	32.380	0.000	0.000	0.000	0.000	0.000	0.000
91	A	192	LYS	1	0.949	0.978	26.812	0.064	0.064	0.000	0.000	0.000	0.000
92	A	193	ALA	0	0.028	0.023	28.808	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	194	THR	0	0.027	0.018	29.724	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	195	ALA	0	0.000	0.012	31.794	0.001	0.001	0.000	0.000	0.000	0.000
95	A	196	ILE	0	0.004	0.001	25.997	0.001	0.001	0.000	0.000	0.000	0.000
96	A	197	ILE	0	-0.002	0.002	30.053	0.000	0.000	0.000	0.000	0.000	0.000
97	A	198	ASP	-1	-0.935	-0.980	32.063	-0.058	-0.058	0.000	0.000	0.000	0.000
98	A	199	LEU	0	-0.078	-0.038	29.613	0.003	0.003	0.000	0.000	0.000	0.000
99	A	200	VAL	0	-0.026	0.015	30.638	0.000	0.000	0.000	0.000	0.000	0.000
100	A	201	ALA	0	0.076	0.031	33.165	0.005	0.005	0.000	0.000	0.000	0.000
101	A	202	LYS	1	0.962	0.960	36.230	0.048	0.048	0.000	0.000	0.000	0.000
102	A	203	GLU	-1	-0.858	-0.936	38.852	-0.060	-0.060	0.000	0.000	0.000	0.000
103	A	204	ILE	0	0.007	0.018	32.585	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	205	LYS	1	0.864	0.928	34.754	0.067	0.067	0.000	0.000	0.000	0.000
105	A	206	THR	0	-0.086	-0.044	36.460	0.002	0.002	0.000	0.000	0.000	0.000
106	A	207	MET	0	-0.084	-0.031	37.691	0.003	0.003	0.000	0.000	0.000	0.000
107	A	208	LYS	1	0.941	0.992	32.631	0.092	0.092	0.000	0.000	0.000	0.000
108	A	209	ASP	-1	-0.899	-0.929	31.699	-0.099	-0.099	0.000	0.000	0.000	0.000
109	A	210	VAL	0	-0.025	-0.039	29.546	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	211	ALA	0	-0.037	-0.012	26.378	0.004	0.004	0.000	0.000	0.000	0.000
111	A	212	VAL	0	0.010	-0.007	25.078	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	213	THR	0	-0.032	-0.018	20.073	0.018	0.018	0.000	0.000	0.000	0.000
113	A	214	PHE	0	-0.044	-0.039	21.147	0.000	0.000	0.000	0.000	0.000	0.000
114	A	215	GLU	-1	-0.869	-0.934	15.524	-0.345	-0.345	0.000	0.000	0.000	0.000
115	A	216	PRO	0	0.003	0.005	14.618	0.030	0.030	0.000	0.000	0.000	0.000
116	A	217	SER	0	-0.052	-0.034	14.703	-0.030	-0.030	0.000	0.000	0.000	0.000
117	A	218	NME	0	-0.019	0.001	13.792	-0.005	-0.005	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:102:ACE )