FMO DATABASE

FMODB ID: 7G14K

Calculation Name: 3TUF-A-Xray372

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: 2023-06-20

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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-843081.222678
FMO2-HF: Nuclear repulsion	798292.81369
FMO2-HF: Total energy	-44788.408988
FMO2-MP2: Total energy	-44919.895

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:103:ASP)

Summations of interaction energy for fragment #1(A:103:ASP)

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.
61.277	65.608	0.164	-1.794	-2.703	0.012

Interaction energy analysis for fragmet #1(A:103:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.964 / q_NPA : -1.006

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	105	LEU	0	0.045	0.019	3.078	-5.526	-1.661	0.164	-1.697	-2.332	0.012
4	A	106	PHE	0	-0.011	0.001	4.456	-7.538	-7.385	0.000	-0.032	-0.121	0.000
5	A	107	THR	0	-0.047	-0.049	6.764	-1.618	-1.618	0.000	0.000	0.000	0.000
6	A	108	THR	0	-0.008	0.004	3.823	-3.379	-3.066	0.000	-0.065	-0.250	0.000
7	A	109	TYR	0	0.041	0.037	6.499	-6.079	-6.079	0.000	0.000	0.000	0.000
8	A	110	ARG	1	0.833	0.922	8.953	-26.221	-26.221	0.000	0.000	0.000	0.000
9	A	111	LEU	0	-0.013	-0.001	9.222	-2.575	-2.575	0.000	0.000	0.000	0.000
10	A	112	ASP	-1	-0.846	-0.925	9.160	30.539	30.539	0.000	0.000	0.000	0.000
11	A	113	LEU	0	-0.075	-0.039	11.947	-2.197	-2.197	0.000	0.000	0.000	0.000
12	A	114	GLU	-1	-0.892	-0.956	14.426	16.193	16.193	0.000	0.000	0.000	0.000
13	A	115	ASP	-1	-0.914	-0.946	13.987	20.260	20.260	0.000	0.000	0.000	0.000
14	A	116	ALA	0	-0.078	-0.051	16.076	-1.507	-1.507	0.000	0.000	0.000	0.000
15	A	117	ARG	1	0.857	0.911	17.888	-17.553	-17.553	0.000	0.000	0.000	0.000
16	A	118	SER	0	-0.055	-0.033	19.753	-1.327	-1.327	0.000	0.000	0.000	0.000
17	A	119	LYS	1	0.932	0.972	16.874	-18.611	-18.611	0.000	0.000	0.000	0.000
18	A	120	GLH	0	0.007	-0.004	22.069	-1.062	-1.062	0.000	0.000	0.000	0.000
19	A	121	ARG	1	0.889	0.953	21.281	-14.795	-14.795	0.000	0.000	0.000	0.000
20	A	122	GLU	-1	-0.944	-0.970	25.490	11.564	11.564	0.000	0.000	0.000	0.000
21	A	123	GLU	-1	-0.922	-0.962	25.745	12.166	12.166	0.000	0.000	0.000	0.000
22	A	124	LEU	0	-0.060	-0.024	27.163	-0.557	-0.557	0.000	0.000	0.000	0.000
23	A	125	ASN	0	-0.006	-0.026	29.919	-0.714	-0.714	0.000	0.000	0.000	0.000
24	A	126	ALA	0	0.004	0.024	31.164	-0.431	-0.431	0.000	0.000	0.000	0.000
25	A	127	ILE	0	-0.021	-0.013	31.581	-0.384	-0.384	0.000	0.000	0.000	0.000
26	A	128	VAL	0	-0.026	-0.020	34.482	-0.369	-0.369	0.000	0.000	0.000	0.000
27	A	129	SER	0	-0.086	-0.056	35.194	-0.378	-0.378	0.000	0.000	0.000	0.000
28	A	130	SER	0	-0.014	0.011	37.352	-0.267	-0.267	0.000	0.000	0.000	0.000
29	A	131	ASP	-1	-0.922	-0.977	38.945	7.370	7.370	0.000	0.000	0.000	0.000
30	A	132	ASP	-1	-0.982	-0.992	40.354	7.528	7.528	0.000	0.000	0.000	0.000
31	A	133	ALA	0	-0.039	0.015	38.389	0.032	0.032	0.000	0.000	0.000	0.000
32	A	134	THR	0	-0.059	-0.062	40.360	-0.262	-0.262	0.000	0.000	0.000	0.000
33	A	135	ALA	0	0.011	-0.015	41.233	0.150	0.150	0.000	0.000	0.000	0.000
34	A	136	LYS	1	0.923	0.961	41.020	-7.374	-7.374	0.000	0.000	0.000	0.000
35	A	137	GLU	-1	-0.754	-0.860	37.507	8.419	8.419	0.000	0.000	0.000	0.000
36	A	138	LYS	1	0.872	0.956	36.833	-7.650	-7.650	0.000	0.000	0.000	0.000
37	A	139	SER	0	-0.012	-0.010	37.110	0.127	0.127	0.000	0.000	0.000	0.000
38	A	140	GLU	-1	-0.932	-0.961	35.264	8.811	8.811	0.000	0.000	0.000	0.000
39	A	141	ALA	0	-0.016	-0.004	32.708	0.328	0.328	0.000	0.000	0.000	0.000
40	A	142	TYR	0	-0.014	-0.018	32.514	0.294	0.294	0.000	0.000	0.000	0.000
41	A	143	ASP	-1	-0.884	-0.945	33.611	9.016	9.016	0.000	0.000	0.000	0.000
42	A	144	LYS	1	0.922	0.960	29.325	-10.203	-10.203	0.000	0.000	0.000	0.000
43	A	145	MET	0	0.001	0.014	28.961	0.394	0.394	0.000	0.000	0.000	0.000
44	A	146	THR	0	-0.017	-0.021	29.216	0.299	0.299	0.000	0.000	0.000	0.000
45	A	147	ALA	0	-0.003	-0.001	29.501	0.154	0.154	0.000	0.000	0.000	0.000
46	A	148	LEU	0	0.037	0.021	22.707	0.274	0.274	0.000	0.000	0.000	0.000
47	A	149	SER	0	0.002	0.012	25.282	0.497	0.497	0.000	0.000	0.000	0.000
48	A	150	GLU	-1	-0.927	-0.954	26.858	10.677	10.677	0.000	0.000	0.000	0.000
49	A	151	VAL	0	-0.042	-0.004	22.552	0.137	0.137	0.000	0.000	0.000	0.000
50	A	152	GLU	-1	-0.879	-0.957	21.080	15.571	15.571	0.000	0.000	0.000	0.000
51	A	153	GLY	0	-0.031	-0.023	22.940	0.366	0.366	0.000	0.000	0.000	0.000
52	A	154	THR	0	-0.065	-0.044	24.025	-0.066	-0.066	0.000	0.000	0.000	0.000
53	A	155	GLU	-1	-0.763	-0.868	19.256	16.380	16.380	0.000	0.000	0.000	0.000
54	A	156	LYS	1	0.997	1.004	20.836	-13.503	-13.503	0.000	0.000	0.000	0.000
55	A	157	GLN	0	-0.010	-0.009	21.874	0.088	0.088	0.000	0.000	0.000	0.000
56	A	158	LEU	0	0.023	0.007	22.051	-0.114	-0.114	0.000	0.000	0.000	0.000
57	A	159	GLU	-1	-0.824	-0.925	16.645	18.724	18.724	0.000	0.000	0.000	0.000
58	A	160	THR	0	-0.080	-0.051	20.428	0.079	0.079	0.000	0.000	0.000	0.000
59	A	161	LEU	0	-0.006	-0.007	22.881	-0.251	-0.251	0.000	0.000	0.000	0.000
60	A	162	ILE	0	0.027	0.027	19.942	-0.305	-0.305	0.000	0.000	0.000	0.000
61	A	163	LYS	1	0.956	0.996	18.076	-16.415	-16.415	0.000	0.000	0.000	0.000
62	A	164	THR	0	-0.079	-0.039	21.666	-0.443	-0.443	0.000	0.000	0.000	0.000
63	A	165	GLN	0	-0.107	-0.063	24.436	-0.642	-0.642	0.000	0.000	0.000	0.000
64	A	166	GLY	0	-0.036	-0.005	23.991	-0.152	-0.152	0.000	0.000	0.000	0.000
65	A	167	TYR	0	-0.065	-0.034	18.797	0.239	0.239	0.000	0.000	0.000	0.000
66	A	168	GLU	-1	-0.909	-0.972	14.121	21.138	21.138	0.000	0.000	0.000	0.000
67	A	169	ASP	-1	-0.820	-0.914	13.000	22.534	22.534	0.000	0.000	0.000	0.000
68	A	170	ALA	0	-0.082	-0.059	15.534	-0.319	-0.319	0.000	0.000	0.000	0.000
69	A	171	LEU	0	0.018	0.028	10.732	0.173	0.173	0.000	0.000	0.000	0.000
70	A	172	VAL	0	-0.038	-0.006	14.843	-0.357	-0.357	0.000	0.000	0.000	0.000
71	A	173	ASN	0	0.018	0.021	15.814	-1.146	-1.146	0.000	0.000	0.000	0.000
72	A	174	ALA	0	-0.045	-0.055	18.102	-0.289	-0.289	0.000	0.000	0.000	0.000
73	A	175	GLU	-1	-0.864	-0.939	20.204	14.624	14.624	0.000	0.000	0.000	0.000
74	A	176	GLY	0	-0.030	-0.002	22.065	-0.542	-0.542	0.000	0.000	0.000	0.000
75	A	177	ASP	-1	-0.902	-0.958	23.715	11.425	11.425	0.000	0.000	0.000	0.000
76	A	178	LYS	1	0.856	0.929	19.617	-16.073	-16.073	0.000	0.000	0.000	0.000
77	A	179	ILE	0	-0.011	0.010	21.315	0.211	0.211	0.000	0.000	0.000	0.000
78	A	180	ASN	0	-0.047	-0.029	16.454	0.044	0.044	0.000	0.000	0.000	0.000
79	A	181	ILE	0	0.032	0.026	17.405	0.243	0.243	0.000	0.000	0.000	0.000
80	A	182	THR	0	-0.030	-0.016	11.930	-0.073	-0.073	0.000	0.000	0.000	0.000
81	A	183	VAL	0	-0.009	0.000	14.951	-0.114	-0.114	0.000	0.000	0.000	0.000
82	A	184	LYS	1	0.948	0.995	10.205	-26.372	-26.372	0.000	0.000	0.000	0.000
83	A	185	SER	0	-0.074	-0.085	14.528	-1.888	-1.888	0.000	0.000	0.000	0.000
84	A	186	ASP	-1	-0.851	-0.903	15.782	19.127	19.127	0.000	0.000	0.000	0.000
85	A	187	LYS	1	0.871	0.930	17.756	-13.440	-13.440	0.000	0.000	0.000	0.000
86	A	188	HIS	0	0.092	0.074	19.943	0.277	0.277	0.000	0.000	0.000	0.000
87	A	189	SER	0	-0.018	-0.032	21.977	-0.545	-0.545	0.000	0.000	0.000	0.000
88	A	190	LYS	1	1.032	0.999	25.298	-10.570	-10.570	0.000	0.000	0.000	0.000
89	A	191	SER	0	0.012	0.001	27.618	-0.158	-0.158	0.000	0.000	0.000	0.000
90	A	192	LYS	1	0.950	0.978	23.376	-13.404	-13.404	0.000	0.000	0.000	0.000
91	A	193	ALA	0	0.027	0.023	23.704	0.136	0.136	0.000	0.000	0.000	0.000
92	A	194	THR	0	0.029	0.018	24.640	0.030	0.030	0.000	0.000	0.000	0.000
93	A	195	ALA	0	-0.002	0.011	27.180	-0.169	-0.169	0.000	0.000	0.000	0.000
94	A	196	ILE	0	0.002	0.001	20.945	-0.085	-0.085	0.000	0.000	0.000	0.000
95	A	197	ILE	0	0.000	0.003	24.896	-0.088	-0.088	0.000	0.000	0.000	0.000
96	A	198	ASP	-1	-0.935	-0.981	26.475	10.112	10.112	0.000	0.000	0.000	0.000
97	A	199	LEU	0	-0.078	-0.038	24.827	-0.301	-0.301	0.000	0.000	0.000	0.000
98	A	200	VAL	0	-0.027	0.015	25.052	-0.024	-0.024	0.000	0.000	0.000	0.000
99	A	201	ALA	0	0.076	0.031	27.679	-0.394	-0.394	0.000	0.000	0.000	0.000
100	A	202	LYS	1	0.961	0.960	30.705	-8.829	-8.829	0.000	0.000	0.000	0.000
101	A	203	GLU	-1	-0.858	-0.936	33.257	9.548	9.548	0.000	0.000	0.000	0.000
102	A	204	ILE	0	0.009	0.018	26.647	0.029	0.029	0.000	0.000	0.000	0.000
103	A	205	LYS	1	0.869	0.929	28.812	-10.578	-10.578	0.000	0.000	0.000	0.000
104	A	206	THR	0	-0.088	-0.045	30.382	-0.186	-0.186	0.000	0.000	0.000	0.000
105	A	207	MET	0	-0.088	-0.033	31.525	-0.269	-0.269	0.000	0.000	0.000	0.000
106	A	208	LYS	1	0.943	0.994	26.530	-11.764	-11.764	0.000	0.000	0.000	0.000
107	A	209	ASP	-1	-0.899	-0.929	25.399	12.568	12.568	0.000	0.000	0.000	0.000
108	A	210	VAL	0	-0.028	-0.040	23.532	0.249	0.249	0.000	0.000	0.000	0.000
109	A	211	ALA	0	-0.035	-0.011	20.136	-0.215	-0.215	0.000	0.000	0.000	0.000
110	A	212	VAL	0	0.010	-0.007	19.235	0.304	0.304	0.000	0.000	0.000	0.000
111	A	213	THR	0	-0.032	-0.018	14.259	-1.120	-1.120	0.000	0.000	0.000	0.000
112	A	214	PHE	0	-0.041	-0.039	16.131	-0.019	-0.019	0.000	0.000	0.000	0.000
113	A	215	GLU	-1	-0.873	-0.935	10.077	30.790	30.790	0.000	0.000	0.000	0.000
114	A	216	PRO	0	0.008	0.009	10.655	-1.475	-1.475	0.000	0.000	0.000	0.000
115	A	217	SER	0	-0.049	-0.013	11.201	2.313	2.313	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:103:ASP)