FMO DATABASE

FMODB ID: 9GRR2

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-939334.209523
FMO2-HF: Nuclear repulsion	894015.004063
FMO2-HF: Total energy	-45319.20546
FMO2-MP2: Total energy	-45451.570452

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.
-1.54	0.552	-0.021	-0.846	-1.225	0.001

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 : -0.018 / q_NPA : -0.022

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	-0.916	-0.956	3.600	-2.590	-0.620	-0.020	-0.828	-1.122	0.001
4	A	30	VAL	0	-0.011	-0.009	6.073	0.256	0.256	0.000	0.000	0.000	0.000
5	A	31	PRO	0	-0.020	0.000	9.489	-0.087	-0.087	0.000	0.000	0.000	0.000
6	A	32	VAL	0	0.020	0.006	10.748	0.163	0.163	0.000	0.000	0.000	0.000
7	A	33	LEU	0	-0.013	-0.002	13.399	0.017	0.017	0.000	0.000	0.000	0.000
8	A	34	THR	0	-0.032	-0.021	15.394	0.038	0.038	0.000	0.000	0.000	0.000
9	A	35	PHE	0	0.038	0.023	18.257	0.001	0.001	0.000	0.000	0.000	0.000
10	A	36	VAL	0	-0.025	-0.009	17.492	0.006	0.006	0.000	0.000	0.000	0.000
11	A	37	PRO	0	0.029	0.004	20.917	0.014	0.014	0.000	0.000	0.000	0.000
12	A	38	VAL	0	0.077	0.027	22.225	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	39	GLN	0	0.016	-0.002	23.258	-0.014	-0.014	0.000	0.000	0.000	0.000
14	A	40	VAL	0	0.027	0.019	17.536	0.000	0.000	0.000	0.000	0.000	0.000
15	A	41	SER	0	0.050	0.015	18.417	-0.024	-0.024	0.000	0.000	0.000	0.000
16	A	42	ALA	0	-0.014	0.003	19.337	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	43	GLU	-1	-0.895	-0.938	17.375	-0.179	-0.179	0.000	0.000	0.000	0.000
18	A	44	LEU	0	-0.043	-0.034	13.165	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	45	GLU	-1	-0.870	-0.920	15.977	-0.232	-0.232	0.000	0.000	0.000	0.000
20	A	46	ASN	0	-0.007	0.000	18.591	0.026	0.026	0.000	0.000	0.000	0.000
21	A	47	ARG	1	0.938	0.958	11.128	0.362	0.362	0.000	0.000	0.000	0.000
22	A	48	GLY	0	-0.017	-0.007	15.368	0.018	0.018	0.000	0.000	0.000	0.000
23	A	49	CYS	0	-0.052	-0.005	8.109	-0.116	-0.116	0.000	0.000	0.000	0.000
24	A	50	TRP	0	0.036	0.024	12.847	-0.113	-0.113	0.000	0.000	0.000	0.000
25	A	51	VAL	0	0.026	0.007	15.127	0.067	0.067	0.000	0.000	0.000	0.000
26	A	52	LYS	1	0.816	0.901	17.607	0.197	0.197	0.000	0.000	0.000	0.000
27	A	53	PHE	0	0.018	0.002	18.082	0.028	0.028	0.000	0.000	0.000	0.000
28	A	54	PHE	0	0.017	-0.006	22.583	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	55	ASP	-1	-0.832	-0.906	26.288	-0.146	-0.146	0.000	0.000	0.000	0.000
30	A	56	LYS	1	0.912	0.964	28.850	0.119	0.119	0.000	0.000	0.000	0.000
31	A	57	LYS	1	0.959	0.977	30.237	0.074	0.074	0.000	0.000	0.000	0.000
32	A	58	ASN	0	-0.055	-0.046	31.596	0.000	0.000	0.000	0.000	0.000	0.000
33	A	59	PHE	0	0.010	-0.003	26.561	0.007	0.007	0.000	0.000	0.000	0.000
34	A	60	GLN	0	-0.057	-0.003	29.334	0.003	0.003	0.000	0.000	0.000	0.000
35	A	61	GLY	0	0.001	-0.012	30.391	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	62	ASP	-1	-0.903	-0.940	27.975	-0.180	-0.180	0.000	0.000	0.000	0.000
37	A	63	SER	0	0.006	-0.024	23.877	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	64	LEU	0	-0.003	0.024	19.099	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	65	PHE	0	-0.011	-0.021	16.343	0.004	0.004	0.000	0.000	0.000	0.000
40	A	66	LEU	0	-0.004	0.000	14.020	-0.041	-0.041	0.000	0.000	0.000	0.000
41	A	67	SER	0	0.020	0.000	11.600	0.127	0.127	0.000	0.000	0.000	0.000
42	A	68	GLY	0	-0.023	0.011	9.191	-0.106	-0.106	0.000	0.000	0.000	0.000
43	A	69	PRO	0	-0.013	-0.033	4.413	0.216	0.338	-0.001	-0.018	-0.103	0.000
44	A	70	ALA	0	0.011	-0.005	6.759	-0.526	-0.526	0.000	0.000	0.000	0.000
45	A	71	THR	0	0.022	0.028	8.014	0.510	0.510	0.000	0.000	0.000	0.000
46	A	72	LEU	0	0.014	-0.002	10.171	-0.081	-0.081	0.000	0.000	0.000	0.000
47	A	73	PRO	0	-0.013	0.010	12.785	0.125	0.125	0.000	0.000	0.000	0.000
48	A	74	ARG	1	1.040	0.989	15.338	0.335	0.335	0.000	0.000	0.000	0.000
49	A	75	LEU	0	0.003	0.031	17.788	-0.064	-0.064	0.000	0.000	0.000	0.000
50	A	76	ILE	0	0.021	0.013	18.986	0.037	0.037	0.000	0.000	0.000	0.000
51	A	77	GLY	0	-0.015	-0.020	18.739	-0.062	-0.062	0.000	0.000	0.000	0.000
52	A	78	PRO	0	-0.009	-0.008	18.569	0.035	0.035	0.000	0.000	0.000	0.000
53	A	79	PHE	0	-0.025	-0.036	21.428	0.011	0.011	0.000	0.000	0.000	0.000
54	A	80	GLY	0	0.016	0.014	24.677	0.015	0.015	0.000	0.000	0.000	0.000
55	A	81	TYR	0	-0.037	0.014	20.969	0.022	0.022	0.000	0.000	0.000	0.000
56	A	82	ASP	-1	-0.855	-0.938	23.247	-0.239	-0.239	0.000	0.000	0.000	0.000
57	A	83	TRP	0	-0.058	-0.037	17.737	0.016	0.016	0.000	0.000	0.000	0.000
58	A	84	GLU	-1	-0.776	-0.876	23.633	-0.201	-0.201	0.000	0.000	0.000	0.000
59	A	85	ASN	0	-0.064	-0.052	25.404	0.017	0.017	0.000	0.000	0.000	0.000
60	A	86	LYS	1	0.895	0.954	26.148	0.171	0.171	0.000	0.000	0.000	0.000
61	A	87	VAL	0	-0.007	0.011	22.708	0.008	0.008	0.000	0.000	0.000	0.000
62	A	88	ARG	1	0.890	0.942	26.135	0.143	0.143	0.000	0.000	0.000	0.000
63	A	89	SER	0	-0.077	-0.030	27.112	0.013	0.013	0.000	0.000	0.000	0.000
64	A	90	VAL	0	0.028	0.018	20.899	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	91	LYS	1	0.855	0.924	22.415	0.162	0.162	0.000	0.000	0.000	0.000
66	A	92	VAL	0	0.021	0.014	16.820	-0.047	-0.047	0.000	0.000	0.000	0.000
67	A	93	GLY	0	0.010	0.014	17.468	0.031	0.031	0.000	0.000	0.000	0.000
68	A	94	PRO	0	-0.025	-0.026	17.719	0.021	0.021	0.000	0.000	0.000	0.000
69	A	95	ARG	1	0.905	0.947	13.701	0.172	0.172	0.000	0.000	0.000	0.000
70	A	96	ALA	0	0.025	0.016	12.716	-0.058	-0.058	0.000	0.000	0.000	0.000
71	A	97	ASN	0	-0.044	-0.010	12.774	0.133	0.133	0.000	0.000	0.000	0.000
72	A	98	LEU	0	-0.006	-0.005	13.197	-0.088	-0.088	0.000	0.000	0.000	0.000
73	A	99	THR	0	0.018	0.020	14.730	0.080	0.080	0.000	0.000	0.000	0.000
74	A	100	ILE	0	-0.060	-0.023	15.980	-0.065	-0.065	0.000	0.000	0.000	0.000
75	A	101	PHE	0	0.049	0.000	14.358	0.027	0.027	0.000	0.000	0.000	0.000
76	A	102	ASP	-1	-0.875	-0.945	19.727	-0.119	-0.119	0.000	0.000	0.000	0.000
77	A	103	ASN	0	-0.002	0.031	21.944	-0.027	-0.027	0.000	0.000	0.000	0.000
78	A	104	HIS	0	-0.020	-0.018	19.640	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	105	ASN	0	-0.127	-0.102	16.210	0.054	0.054	0.000	0.000	0.000	0.000
80	A	106	TYR	0	0.008	-0.012	11.452	0.022	0.022	0.000	0.000	0.000	0.000
81	A	107	ARG	1	0.892	0.964	16.374	0.148	0.148	0.000	0.000	0.000	0.000
82	A	108	ASP	-1	-0.872	-0.950	19.742	-0.074	-0.074	0.000	0.000	0.000	0.000
83	A	109	GLU	-1	-0.910	-0.946	21.337	-0.026	-0.026	0.000	0.000	0.000	0.000
84	A	110	ASP	-1	-0.913	-0.960	18.994	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	111	LYS	1	0.878	0.952	20.290	0.048	0.048	0.000	0.000	0.000	0.000
86	A	112	PHE	0	0.011	0.012	15.285	-0.029	-0.029	0.000	0.000	0.000	0.000
87	A	113	LEU	0	-0.054	-0.030	18.544	0.004	0.004	0.000	0.000	0.000	0.000
88	A	114	ASP	-1	-0.774	-0.890	17.918	0.013	0.013	0.000	0.000	0.000	0.000
89	A	115	ALA	0	-0.007	-0.017	17.016	-0.033	-0.033	0.000	0.000	0.000	0.000
90	A	116	GLY	0	-0.071	-0.034	18.448	0.020	0.020	0.000	0.000	0.000	0.000
91	A	117	ALA	0	-0.038	0.000	20.875	0.004	0.004	0.000	0.000	0.000	0.000
92	A	118	ASN	0	0.036	0.025	22.647	-0.036	-0.036	0.000	0.000	0.000	0.000
93	A	119	VAL	0	0.025	0.028	24.333	0.015	0.015	0.000	0.000	0.000	0.000
94	A	120	ALA	0	0.013	-0.007	26.747	-0.012	-0.012	0.000	0.000	0.000	0.000
95	A	121	ASN	0	0.014	-0.005	29.901	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	122	LEU	0	0.002	0.011	24.061	0.008	0.008	0.000	0.000	0.000	0.000
97	A	123	SER	0	0.047	0.018	28.238	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	124	LYS	1	1.001	1.000	30.192	0.060	0.060	0.000	0.000	0.000	0.000
99	A	125	GLU	-1	-0.998	-0.994	31.090	-0.048	-0.048	0.000	0.000	0.000	0.000
100	A	126	MET	0	-0.075	-0.033	31.137	0.007	0.007	0.000	0.000	0.000	0.000
101	A	127	GLY	0	0.010	0.014	30.106	0.002	0.002	0.000	0.000	0.000	0.000
102	A	128	PHE	0	-0.065	-0.050	24.251	0.001	0.001	0.000	0.000	0.000	0.000
103	A	129	PHE	0	0.042	0.019	22.125	0.004	0.004	0.000	0.000	0.000	0.000
104	A	130	ASP	-1	-0.860	-0.938	27.245	-0.088	-0.088	0.000	0.000	0.000	0.000
105	A	131	ASN	0	-0.046	-0.038	26.354	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	132	PHE	0	-0.004	0.028	19.141	0.003	0.003	0.000	0.000	0.000	0.000
107	A	133	ARG	1	0.895	0.946	21.454	0.157	0.157	0.000	0.000	0.000	0.000
108	A	134	SER	0	-0.072	-0.032	16.137	-0.025	-0.025	0.000	0.000	0.000	0.000
109	A	135	MET	0	-0.014	-0.001	13.888	0.060	0.060	0.000	0.000	0.000	0.000
110	A	136	VAL	0	0.032	0.020	9.465	-0.127	-0.127	0.000	0.000	0.000	0.000
111	A	137	LEU	0	-0.022	-0.001	10.844	0.150	0.150	0.000	0.000	0.000	0.000
112	A	138	ASN	0	0.027	-0.001	8.206	-0.269	-0.269	0.000	0.000	0.000	0.000
113	A	140	ILE	0	-0.012	0.007	9.219	0.151	0.151	0.000	0.000	0.000	0.000

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