FMO DATABASE

FMODB ID: 7GKKK

Calculation Name: 3ENU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ENU

Chain ID: A

ChEMBL ID:

UniProt ID: Q2YAE2

Base Structure: X-ray

Registration Date: 2023-03-14

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	113
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-940679.387031
FMO2-HF: Nuclear repulsion	895359.53472
FMO2-HF: Total energy	-45319.852311
FMO2-MP2: Total energy	-45452.192956

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:27:THR)

Summations of interaction energy for fragment #1(A:27:THR)

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.
-4.119	-1.343	0.019	-1.235	-1.56	-0.002

Interaction energy analysis for fragmet #1(A:27:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.024 / 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].	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	29	GLU	-1	-0.924	-0.960	3.417	-4.992	-2.350	0.020	-1.217	-1.445	-0.002
4	A	30	VAL	0	0.012	-0.001	6.130	0.314	0.314	0.000	0.000	0.000	0.000
5	A	31	PRO	0	-0.013	0.011	9.478	-0.105	-0.105	0.000	0.000	0.000	0.000
6	A	32	VAL	0	0.001	-0.006	10.805	0.189	0.189	0.000	0.000	0.000	0.000
7	A	33	LEU	0	0.002	0.001	13.264	0.025	0.025	0.000	0.000	0.000	0.000
8	A	34	THR	0	-0.029	-0.021	15.846	0.038	0.038	0.000	0.000	0.000	0.000
9	A	35	PHE	0	0.008	0.012	18.418	0.011	0.011	0.000	0.000	0.000	0.000
10	A	36	VAL	0	-0.005	-0.004	17.862	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	37	PRO	0	0.030	0.011	21.305	0.018	0.018	0.000	0.000	0.000	0.000
12	A	38	VAL	0	0.064	0.029	22.297	-0.020	-0.020	0.000	0.000	0.000	0.000
13	A	39	GLN	0	0.049	0.011	23.063	-0.022	-0.022	0.000	0.000	0.000	0.000
14	A	40	VAL	0	0.010	0.012	17.419	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	41	SER	0	0.022	0.008	18.236	-0.031	-0.031	0.000	0.000	0.000	0.000
16	A	42	ALA	0	0.005	0.009	19.206	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	43	GLU	-1	-0.788	-0.871	16.667	-0.266	-0.266	0.000	0.000	0.000	0.000
18	A	44	LEU	0	-0.032	-0.022	12.947	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	45	GLU	-1	-0.820	-0.894	15.735	-0.274	-0.274	0.000	0.000	0.000	0.000
20	A	46	ASN	0	-0.047	-0.032	18.482	0.032	0.032	0.000	0.000	0.000	0.000
21	A	47	ARG	1	0.911	0.938	11.622	0.421	0.421	0.000	0.000	0.000	0.000
22	A	48	GLY	0	-0.001	0.015	14.842	0.011	0.011	0.000	0.000	0.000	0.000
23	A	49	CYS	0	-0.063	-0.022	8.720	-0.151	-0.151	0.000	0.000	0.000	0.000
24	A	50	TRP	0	0.008	0.021	12.515	-0.123	-0.123	0.000	0.000	0.000	0.000
25	A	51	VAL	0	0.023	0.003	14.775	0.074	0.074	0.000	0.000	0.000	0.000
26	A	52	LYS	1	0.786	0.878	17.436	0.237	0.237	0.000	0.000	0.000	0.000
27	A	53	PHE	0	0.034	0.005	17.733	0.032	0.032	0.000	0.000	0.000	0.000
28	A	54	PHE	0	0.008	-0.011	22.758	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	55	ASP	-1	-0.800	-0.887	26.473	-0.140	-0.140	0.000	0.000	0.000	0.000
30	A	56	LYS	1	0.913	0.967	29.278	0.123	0.123	0.000	0.000	0.000	0.000
31	A	57	LYS	1	0.955	0.989	30.269	0.072	0.072	0.000	0.000	0.000	0.000
32	A	58	ASN	0	-0.055	-0.053	31.901	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	59	PHE	0	-0.010	-0.001	27.114	0.007	0.007	0.000	0.000	0.000	0.000
34	A	60	GLN	0	-0.043	-0.003	29.574	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	61	GLY	0	0.010	-0.008	30.763	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	62	ASP	-1	-0.913	-0.948	28.024	-0.194	-0.194	0.000	0.000	0.000	0.000
37	A	63	SER	0	-0.009	-0.029	24.008	0.001	0.001	0.000	0.000	0.000	0.000
38	A	64	LEU	0	-0.002	0.031	19.190	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	65	PHE	0	-0.009	-0.022	16.342	0.010	0.010	0.000	0.000	0.000	0.000
40	A	66	LEU	0	-0.007	-0.001	13.910	-0.035	-0.035	0.000	0.000	0.000	0.000
41	A	67	SER	0	0.018	0.006	10.946	0.131	0.131	0.000	0.000	0.000	0.000
42	A	68	GLY	0	0.005	0.008	9.341	-0.066	-0.066	0.000	0.000	0.000	0.000
43	A	69	PRO	0	-0.022	-0.024	4.316	0.204	0.338	-0.001	-0.018	-0.115	0.000
44	A	70	ALA	0	-0.011	-0.011	6.579	-0.663	-0.663	0.000	0.000	0.000	0.000
45	A	71	THR	0	0.017	0.009	7.625	0.483	0.483	0.000	0.000	0.000	0.000
46	A	72	LEU	0	0.032	0.008	10.116	-0.094	-0.094	0.000	0.000	0.000	0.000
47	A	73	PRO	0	-0.012	0.014	12.759	0.108	0.108	0.000	0.000	0.000	0.000
48	A	74	ARG	1	0.963	0.950	15.313	0.280	0.280	0.000	0.000	0.000	0.000
49	A	75	LEU	0	0.005	0.032	17.665	-0.061	-0.061	0.000	0.000	0.000	0.000
50	A	76	ILE	0	0.017	0.010	18.904	0.031	0.031	0.000	0.000	0.000	0.000
51	A	77	GLY	0	-0.002	-0.006	18.677	-0.060	-0.060	0.000	0.000	0.000	0.000
52	A	78	PRO	0	0.003	0.000	18.359	0.035	0.035	0.000	0.000	0.000	0.000
53	A	79	PHE	0	-0.037	-0.037	21.225	0.012	0.012	0.000	0.000	0.000	0.000
54	A	80	GLY	0	0.026	0.026	24.246	0.018	0.018	0.000	0.000	0.000	0.000
55	A	81	TYR	0	-0.029	-0.001	20.997	0.010	0.010	0.000	0.000	0.000	0.000
56	A	82	ASP	-1	-0.861	-0.948	23.015	-0.238	-0.238	0.000	0.000	0.000	0.000
57	A	83	TRP	0	-0.037	-0.029	17.721	0.015	0.015	0.000	0.000	0.000	0.000
58	A	84	GLU	-1	-0.687	-0.795	23.578	-0.167	-0.167	0.000	0.000	0.000	0.000
59	A	85	ASN	0	-0.081	-0.058	25.257	0.017	0.017	0.000	0.000	0.000	0.000
60	A	86	LYS	1	0.835	0.910	26.344	0.176	0.176	0.000	0.000	0.000	0.000
61	A	87	VAL	0	-0.021	0.014	22.872	0.004	0.004	0.000	0.000	0.000	0.000
62	A	88	ARG	1	0.832	0.893	26.333	0.139	0.139	0.000	0.000	0.000	0.000
63	A	89	SER	0	-0.085	-0.041	27.441	0.014	0.014	0.000	0.000	0.000	0.000
64	A	90	VAL	0	0.030	0.019	21.454	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	91	LYS	1	0.880	0.934	22.324	0.180	0.180	0.000	0.000	0.000	0.000
66	A	92	VAL	0	0.014	0.020	16.972	-0.048	-0.048	0.000	0.000	0.000	0.000
67	A	93	GLY	0	0.036	0.024	17.401	0.033	0.033	0.000	0.000	0.000	0.000
68	A	94	PRO	0	-0.031	-0.032	17.813	0.016	0.016	0.000	0.000	0.000	0.000
69	A	95	ARG	1	0.846	0.908	13.971	0.240	0.240	0.000	0.000	0.000	0.000
70	A	96	ALA	0	0.012	0.015	13.125	-0.074	-0.074	0.000	0.000	0.000	0.000
71	A	97	ASN	0	-0.040	-0.034	12.926	0.146	0.146	0.000	0.000	0.000	0.000
72	A	98	LEU	0	-0.045	-0.001	13.165	-0.066	-0.066	0.000	0.000	0.000	0.000
73	A	99	THR	0	0.026	0.016	14.972	0.068	0.068	0.000	0.000	0.000	0.000
74	A	100	ILE	0	-0.044	-0.015	15.933	-0.065	-0.065	0.000	0.000	0.000	0.000
75	A	101	PHE	0	0.049	0.002	14.564	0.037	0.037	0.000	0.000	0.000	0.000
76	A	102	ASP	-1	-0.876	-0.936	20.050	-0.099	-0.099	0.000	0.000	0.000	0.000
77	A	103	ASN	0	-0.014	-0.023	21.858	-0.023	-0.023	0.000	0.000	0.000	0.000
78	A	104	HIS	0	0.052	0.050	19.602	-0.024	-0.024	0.000	0.000	0.000	0.000
79	A	105	ASN	0	-0.108	-0.088	15.933	0.021	0.021	0.000	0.000	0.000	0.000
80	A	106	TYR	0	-0.018	-0.018	11.032	0.052	0.052	0.000	0.000	0.000	0.000
81	A	107	ARG	1	0.853	0.911	16.360	0.076	0.076	0.000	0.000	0.000	0.000
82	A	108	ASP	-1	-0.813	-0.872	19.908	-0.040	-0.040	0.000	0.000	0.000	0.000
83	A	109	GLU	-1	-0.840	-0.908	22.039	0.005	0.005	0.000	0.000	0.000	0.000
84	A	110	ASP	-1	-0.900	-0.967	19.101	0.019	0.019	0.000	0.000	0.000	0.000
85	A	111	LYS	1	0.792	0.908	20.508	0.023	0.023	0.000	0.000	0.000	0.000
86	A	112	PHE	0	0.028	0.022	15.849	-0.026	-0.026	0.000	0.000	0.000	0.000
87	A	113	LEU	0	-0.061	-0.036	18.579	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	114	ASP	-1	-0.758	-0.872	18.056	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	115	ALA	0	-0.009	-0.014	17.190	-0.036	-0.036	0.000	0.000	0.000	0.000
90	A	116	GLY	0	-0.054	-0.024	18.630	0.025	0.025	0.000	0.000	0.000	0.000
91	A	117	ALA	0	-0.021	0.007	21.115	0.011	0.011	0.000	0.000	0.000	0.000
92	A	118	ASN	0	-0.015	-0.015	22.956	-0.037	-0.037	0.000	0.000	0.000	0.000
93	A	119	VAL	0	0.020	0.018	24.935	0.016	0.016	0.000	0.000	0.000	0.000
94	A	120	ALA	0	0.022	0.008	27.243	-0.012	-0.012	0.000	0.000	0.000	0.000
95	A	121	ASN	0	0.033	-0.007	30.212	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	122	LEU	0	0.019	0.031	24.230	0.010	0.010	0.000	0.000	0.000	0.000
97	A	123	SER	0	0.043	0.014	28.311	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	124	LYS	1	0.912	0.939	30.156	0.056	0.056	0.000	0.000	0.000	0.000
99	A	125	GLU	-1	-0.978	-0.985	31.199	-0.047	-0.047	0.000	0.000	0.000	0.000
100	A	126	MET	0	-0.084	-0.031	31.041	0.006	0.006	0.000	0.000	0.000	0.000
101	A	127	GLY	0	0.019	0.016	30.410	0.001	0.001	0.000	0.000	0.000	0.000
102	A	128	PHE	0	-0.034	-0.034	23.987	0.002	0.002	0.000	0.000	0.000	0.000
103	A	129	PHE	0	0.031	0.014	22.139	0.006	0.006	0.000	0.000	0.000	0.000
104	A	130	ASP	-1	-0.799	-0.888	27.337	-0.078	-0.078	0.000	0.000	0.000	0.000
105	A	131	ASN	0	-0.022	-0.020	26.001	-0.021	-0.021	0.000	0.000	0.000	0.000
106	A	132	PHE	0	0.009	0.026	18.938	0.010	0.010	0.000	0.000	0.000	0.000
107	A	133	ARG	1	0.792	0.859	21.513	0.124	0.124	0.000	0.000	0.000	0.000
108	A	134	SER	0	-0.068	-0.031	16.094	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	135	MET	0	-0.011	0.002	14.021	0.047	0.047	0.000	0.000	0.000	0.000
110	A	136	VAL	0	-0.004	0.001	9.540	-0.098	-0.098	0.000	0.000	0.000	0.000
111	A	137	LEU	0	-0.021	0.004	10.659	0.126	0.126	0.000	0.000	0.000	0.000
112	A	138	ASN	0	0.052	0.016	8.605	-0.286	-0.286	0.000	0.000	0.000	0.000
113	A	140	ILE	0	-0.009	0.008	10.031	0.146	0.146	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:27:THR)