FMO DATABASE

FMODB ID: 53MZZ

Calculation Name: 3ENC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ENC

Chain ID: A

ChEMBL ID:

UniProt ID: Q8TZI1

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	79
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-508319.468379
FMO2-HF: Nuclear repulsion	477217.397471
FMO2-HF: Total energy	-31102.070908
FMO2-MP2: Total energy	-31194.921283

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:2:LYS)

Summations of interaction energy for fragment #1(A:2:LYS)

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.
87.902	87.894	4.045	-1.02	-3.018	0.006

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.030 / q_NPA : 0.989

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	4	LYS	1	0.930	0.963	2.050	57.876	57.868	4.045	-1.020	-3.018	0.006
4	A	5	ARG	1	0.994	1.015	6.371	21.562	21.562	0.000	0.000	0.000	0.000
5	A	6	VAL	0	-0.034	-0.008	9.003	-0.315	-0.315	0.000	0.000	0.000	0.000
6	A	7	GLN	0	-0.009	-0.019	11.796	1.317	1.317	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.006	0.018	15.584	-0.395	-0.395	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.982	0.990	17.990	12.179	12.179	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.047	-0.021	20.729	-0.159	-0.159	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.822	-0.881	24.247	-10.161	-10.161	0.000	0.000	0.000	0.000
11	A	12	MET	0	-0.064	-0.027	27.941	-0.220	-0.220	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.808	-0.924	30.356	-8.820	-8.820	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.039	-0.026	31.620	-0.037	-0.037	0.000	0.000	0.000	0.000
14	A	15	PRO	0	-0.010	-0.007	36.835	0.090	0.090	0.000	0.000	0.000	0.000
15	A	16	SER	0	0.052	0.023	40.630	0.064	0.064	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.770	-0.900	40.201	-7.521	-7.521	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.932	-0.954	40.471	-6.931	-6.931	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.089	-0.065	38.604	0.069	0.069	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.045	0.011	36.136	-0.192	-0.192	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.954	0.967	36.353	7.326	7.326	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.014	0.024	37.620	-0.130	-0.130	0.000	0.000	0.000	0.000
22	A	23	VAL	0	-0.004	0.006	32.713	-0.116	-0.116	0.000	0.000	0.000	0.000
23	A	24	TYR	0	-0.017	-0.019	31.536	-0.333	-0.333	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.931	-0.986	33.219	-7.735	-7.735	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.003	0.014	35.164	0.048	0.048	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.016	-0.012	28.627	-0.135	-0.135	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.003	0.006	29.931	-0.327	-0.327	0.000	0.000	0.000	0.000
28	A	29	TYR	0	0.063	0.023	31.395	-0.083	-0.083	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.916	-0.955	29.635	-9.241	-9.241	0.000	0.000	0.000	0.000
30	A	31	HIS	0	-0.050	-0.025	25.605	-0.695	-0.695	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.038	-0.027	27.905	-0.219	-0.219	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.058	-0.026	30.600	0.110	0.110	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.037	-0.012	25.004	-0.068	-0.068	0.000	0.000	0.000	0.000
34	A	35	PRO	0	-0.013	-0.001	25.656	-0.424	-0.424	0.000	0.000	0.000	0.000
35	A	36	TYR	0	-0.040	-0.016	21.988	-0.239	-0.239	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.981	1.006	21.229	11.000	11.000	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.929	0.979	15.788	13.914	13.914	0.000	0.000	0.000	0.000
38	A	39	SER	0	0.075	0.006	14.515	-0.698	-0.698	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.990	-0.998	16.960	-14.178	-14.178	0.000	0.000	0.000	0.000
40	A	41	ILE	0	-0.045	-0.037	19.014	-0.232	-0.232	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.891	-0.935	22.217	-10.353	-10.353	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.007	-0.024	25.334	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.939	0.966	27.232	10.122	10.122	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.022	0.045	30.606	-0.161	-0.161	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.944	-0.971	33.592	-8.479	-8.479	0.000	0.000	0.000	0.000
46	A	47	GLY	0	-0.010	0.004	36.110	0.217	0.217	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.987	0.960	37.401	7.847	7.847	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.822	0.905	31.385	9.470	9.470	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.024	0.001	29.137	0.079	0.079	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.050	-0.027	26.853	-0.271	-0.271	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.041	-0.009	22.706	-0.132	-0.132	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.787	-0.881	21.998	-12.390	-12.390	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.040	-0.041	17.248	0.003	0.003	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.908	0.945	12.622	17.813	17.813	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.026	-0.011	11.469	0.481	0.481	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.013	-0.005	9.032	-0.654	-0.654	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.825	-0.929	5.954	-25.938	-25.938	0.000	0.000	0.000	0.000
58	A	59	SER	0	0.036	-0.008	5.339	1.614	1.614	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.039	-0.030	8.107	1.662	1.662	0.000	0.000	0.000	0.000
60	A	61	ALA	0	-0.091	0.000	9.862	1.368	1.368	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.043	0.016	11.761	0.993	0.993	0.000	0.000	0.000	0.000
62	A	63	ARG	1	1.019	1.016	12.148	19.040	19.040	0.000	0.000	0.000	0.000
63	A	64	GLY	0	-0.009	-0.008	14.466	0.815	0.815	0.000	0.000	0.000	0.000
64	A	65	THR	0	0.027	0.004	16.362	1.028	1.028	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.042	0.017	17.476	0.621	0.621	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.097	-0.048	18.543	0.857	0.857	0.000	0.000	0.000	0.000
67	A	68	SER	0	-0.014	-0.003	20.262	0.423	0.423	0.000	0.000	0.000	0.000
68	A	69	TYR	0	0.032	0.000	21.904	0.346	0.346	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.050	0.029	22.064	0.372	0.372	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.868	0.939	23.749	11.614	11.614	0.000	0.000	0.000	0.000
71	A	72	TRP	0	0.055	0.043	25.769	0.225	0.225	0.000	0.000	0.000	0.000
72	A	73	ILE	0	0.058	0.021	27.618	0.258	0.258	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.896	0.950	27.535	10.232	10.232	0.000	0.000	0.000	0.000
74	A	75	ALA	0	-0.036	-0.024	30.410	0.230	0.230	0.000	0.000	0.000	0.000
75	A	76	ALA	0	0.018	0.019	32.145	0.242	0.242	0.000	0.000	0.000	0.000
76	A	77	ILE	0	-0.055	-0.029	32.666	0.196	0.196	0.000	0.000	0.000	0.000
77	A	78	ASP	-1	-0.915	-0.966	34.210	-8.255	-8.255	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.085	-0.018	36.763	0.231	0.231	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.041	-0.013	38.481	0.195	0.195	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)