FMO DATABASE

FMODB ID: 5261Z

Calculation Name: 1EP7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1EP7

Chain ID: A

ChEMBL ID:

UniProt ID: P80028

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptHSide
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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-814728.591624
FMO2-HF: Nuclear repulsion	773624.501543
FMO2-HF: Total energy	-41104.090081
FMO2-MP2: Total energy	-41223.737691

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:1:GLY)

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

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.
-0.839	1.069	-0.008	-0.837	-1.063	-0.001

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : -0.008

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	3	SER	0	-0.017	-0.008	3.457	-1.699	0.209	-0.008	-0.837	-1.063	-0.001
4	A	4	VAL	0	-0.035	-0.010	5.465	-0.152	-0.152	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.029	-0.008	5.914	1.083	1.083	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.019	-0.018	7.673	-0.403	-0.403	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.041	-0.011	9.850	-0.082	-0.082	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.835	-0.911	12.928	0.314	0.314	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.001	-0.019	14.769	-0.069	-0.069	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.867	0.903	17.144	-0.114	-0.114	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.017	0.019	18.372	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.021	0.018	13.289	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.011	-0.011	15.029	0.027	0.027	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.778	-0.884	16.821	0.137	0.137	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.032	-0.009	15.049	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	16	GLN	0	0.017	0.002	11.196	0.000	0.000	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.022	0.014	14.565	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.011	-0.002	17.889	-0.023	-0.023	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.914	0.968	9.589	-0.260	-0.260	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.014	0.005	16.091	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.833	0.904	17.145	-0.046	-0.046	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.836	-0.907	18.496	0.002	0.002	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.921	-0.963	13.419	-0.084	-0.084	0.000	0.000	0.000	0.000
24	A	24	HIS	0	-0.090	-0.035	18.235	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.841	0.926	13.851	0.104	0.104	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.031	-0.003	18.126	0.020	0.020	0.000	0.000	0.000	0.000
27	A	27	ILE	0	0.018	0.011	14.702	0.014	0.014	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.013	-0.010	15.175	-0.029	-0.029	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.033	-0.021	14.712	0.079	0.079	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.869	-0.945	14.696	0.373	0.373	0.000	0.000	0.000	0.000
31	A	31	PHE	0	-0.013	-0.006	16.292	0.047	0.047	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.040	-0.015	15.775	-0.044	-0.044	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.091	0.044	19.073	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.001	0.004	18.070	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	35	TRP	0	-0.046	-0.036	20.292	-0.012	-0.012	0.000	0.000	0.000	0.000
36	A	36	CYS	0	0.000	0.037	19.572	-0.020	-0.020	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.018	0.005	22.264	0.014	0.014	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.024	-0.013	23.017	0.009	0.009	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.921	0.964	18.479	-0.192	-0.192	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.027	-0.014	18.599	0.004	0.004	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.031	0.001	18.701	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.032	0.020	14.347	0.012	0.012	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.040	0.017	13.577	0.045	0.045	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.018	0.001	13.537	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.013	0.006	11.892	-0.035	-0.035	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.846	-0.927	9.074	0.790	0.790	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.034	0.004	9.800	-0.045	-0.045	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.006	-0.008	11.996	-0.065	-0.065	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.012	-0.031	8.564	0.044	0.044	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.004	-0.006	7.080	-0.148	-0.148	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.908	-0.948	9.461	-0.086	-0.086	0.000	0.000	0.000	0.000
52	A	53	TYR	0	-0.070	-0.052	12.440	-0.040	-0.040	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.091	0.063	8.959	0.019	0.019	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.051	-0.031	10.719	-0.037	-0.037	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.831	0.918	12.644	0.120	0.120	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.005	-0.004	13.916	0.015	0.015	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.009	0.016	10.849	0.013	0.013	0.000	0.000	0.000	0.000
58	A	59	PHE	0	0.028	0.016	10.043	-0.029	-0.029	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.004	0.000	9.941	0.247	0.247	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.888	0.948	11.248	-0.809	-0.809	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.011	-0.001	12.935	0.032	0.032	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.849	-0.922	15.876	0.278	0.278	0.000	0.000	0.000	0.000
63	A	64	VAL	0	0.007	-0.039	17.375	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.872	-0.917	20.987	0.173	0.173	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.063	-0.024	17.679	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.046	-0.022	16.960	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.079	0.035	20.292	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.008	0.005	23.221	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.014	-0.008	19.118	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.001	0.006	22.247	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.955	-0.982	23.495	0.102	0.102	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.024	-0.007	24.958	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.055	-0.020	23.060	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	75	GLY	0	-0.004	0.001	25.190	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.061	-0.025	23.097	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.001	-0.002	26.556	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.010	0.002	27.821	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	79	MET	0	-0.018	0.030	22.186	0.016	0.016	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.003	-0.034	20.787	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	81	THR	0	-0.008	-0.016	21.592	-0.028	-0.028	0.000	0.000	0.000	0.000
81	A	82	PHE	0	-0.020	-0.015	17.515	0.026	0.026	0.000	0.000	0.000	0.000
82	A	83	HIS	0	0.014	0.017	19.729	-0.024	-0.024	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.010	0.003	19.448	0.027	0.027	0.000	0.000	0.000	0.000
84	A	85	TYR	0	-0.036	-0.034	19.285	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.904	0.934	20.196	-0.062	-0.062	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.879	-0.938	22.322	0.046	0.046	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.009	-0.002	21.967	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.028	-0.003	22.955	0.007	0.007	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.864	0.922	24.015	-0.122	-0.122	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.028	-0.021	24.317	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.782	-0.869	24.523	0.079	0.079	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.916	-0.937	23.998	0.136	0.136	0.000	0.000	0.000	0.000
93	A	94	LEU	0	0.001	0.015	22.635	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.022	0.022	24.044	0.017	0.017	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.030	0.021	25.138	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.007	-0.015	23.189	0.012	0.012	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.035	-0.038	24.153	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	99	GLN	0	0.076	0.015	21.221	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.808	-0.872	22.372	0.091	0.091	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.878	0.916	24.915	-0.090	-0.090	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.037	0.026	17.398	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.912	0.960	19.873	-0.101	-0.101	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.005	0.010	21.108	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.009	0.015	21.247	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	106	VAL	0	0.023	0.003	16.518	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.008	0.006	19.722	-0.014	-0.014	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.831	0.898	21.586	-0.083	-0.083	0.000	0.000	0.000	0.000
108	A	109	HIS	0	-0.023	-0.044	21.266	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	110	ALA	0	-0.039	0.001	18.971	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.042	-0.009	20.396	-0.017	-0.017	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.008	0.005	23.905	0.002	0.002	0.000	0.000	0.000	0.000

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