FMO DATABASE

FMODB ID: YZ882

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

Total energy (hartree)

FMO2-HF: Electronic energy	-819393.735985
FMO2-HF: Nuclear repulsion	778289.504423
FMO2-HF: Total energy	-41104.231562
FMO2-MP2: Total energy	-41223.932052

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.
-0.015	1.728	-0.015	-0.834	-0.894	-0.002

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 : 0.005 / q_NPA : -0.013

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	-0.034	-0.007	3.621	-0.737	1.006	-0.015	-0.834	-0.894	-0.002
4	A	4	VAL	0	0.004	-0.007	5.391	-0.359	-0.359	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.047	-0.015	5.992	1.215	1.215	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.012	-0.013	7.866	-0.394	-0.394	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.043	-0.018	9.929	-0.053	-0.053	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.823	-0.897	13.158	0.371	0.371	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.013	-0.029	14.922	-0.078	-0.078	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.860	0.893	17.380	-0.128	-0.128	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.013	0.016	18.363	-0.006	-0.006	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.027	0.021	13.262	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.048	0.015	14.941	0.030	0.030	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.762	-0.866	16.886	0.143	0.143	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.022	-0.010	15.405	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.023	-0.011	11.690	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.026	0.011	14.998	-0.031	-0.031	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.026	-0.006	18.555	-0.025	-0.025	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.900	0.957	10.041	-0.242	-0.242	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.016	0.002	16.440	-0.028	-0.028	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.840	0.915	17.688	-0.039	-0.039	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.830	-0.907	19.063	-0.004	-0.004	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.922	-0.968	13.580	-0.109	-0.109	0.000	0.000	0.000	0.000
24	A	24	HIS	0	-0.086	-0.037	18.423	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.798	0.907	14.582	0.124	0.124	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.032	-0.007	17.849	0.021	0.021	0.000	0.000	0.000	0.000
27	A	27	ILE	0	0.024	0.015	15.279	0.007	0.007	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.017	-0.013	15.525	-0.028	-0.028	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.010	-0.005	14.947	0.074	0.074	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.841	-0.932	14.661	0.391	0.391	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.004	0.004	16.426	0.050	0.050	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.011	-0.015	15.685	-0.046	-0.046	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.067	0.027	19.125	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.016	0.001	18.454	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	35	TRP	0	-0.042	-0.044	20.267	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	36	CYS	0	0.007	0.048	19.149	-0.026	-0.026	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.001	-0.003	21.887	0.016	0.016	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.012	-0.019	22.586	0.008	0.008	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.925	0.968	17.901	-0.226	-0.226	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.032	-0.002	18.227	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.065	-0.023	18.369	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.036	0.022	13.867	0.006	0.006	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.072	0.032	12.998	0.043	0.043	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.036	0.009	13.315	-0.022	-0.022	0.000	0.000	0.000	0.000
45	A	46	PHE	0	-0.003	-0.007	11.922	-0.044	-0.044	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.830	-0.918	8.777	0.781	0.781	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.064	-0.022	9.510	-0.062	-0.062	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.011	-0.009	11.569	-0.065	-0.065	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.038	-0.041	8.439	0.010	0.010	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.001	0.003	6.916	-0.266	-0.266	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.883	-0.931	9.505	-0.082	-0.082	0.000	0.000	0.000	0.000
52	A	53	TYR	0	-0.049	-0.038	12.622	-0.035	-0.035	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.092	0.056	8.949	0.025	0.025	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.039	-0.017	10.659	-0.037	-0.037	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.834	0.902	12.547	0.169	0.169	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.010	-0.002	13.968	0.019	0.019	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.014	0.012	11.480	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	59	PHE	0	0.017	0.016	10.123	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.009	-0.003	10.268	0.223	0.223	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.854	0.921	11.231	-0.797	-0.797	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.015	0.003	13.061	0.053	0.053	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.816	-0.914	15.785	0.299	0.299	0.000	0.000	0.000	0.000
63	A	64	VAL	0	0.017	-0.025	17.473	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.837	-0.890	20.825	0.202	0.202	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.049	-0.024	17.667	-0.016	-0.016	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.029	-0.014	16.769	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.055	0.033	20.131	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.032	0.010	23.777	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.028	-0.015	19.127	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.001	0.000	22.229	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.953	-0.973	23.387	0.114	0.114	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.029	-0.012	24.888	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.041	-0.009	23.016	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	75	GLY	0	-0.001	-0.001	25.146	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.070	-0.034	22.929	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.001	-0.005	26.377	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.018	-0.005	27.395	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	79	MET	0	0.010	0.032	22.348	0.019	0.019	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.007	-0.033	20.537	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	81	THR	0	-0.034	-0.025	21.646	-0.032	-0.032	0.000	0.000	0.000	0.000
81	A	82	PHE	0	-0.019	-0.013	17.358	0.023	0.023	0.000	0.000	0.000	0.000
82	A	83	HIS	0	0.025	0.012	20.149	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.007	-0.004	19.726	0.025	0.025	0.000	0.000	0.000	0.000
84	A	85	TYR	0	-0.018	-0.024	19.709	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.899	0.946	20.592	-0.052	-0.052	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.881	-0.941	22.837	0.043	0.043	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.011	0.013	22.155	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.044	-0.019	23.170	0.010	0.010	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.852	0.912	24.062	-0.127	-0.127	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.023	-0.020	24.559	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.776	-0.861	24.538	0.074	0.074	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.906	-0.928	24.213	0.139	0.139	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.010	0.012	22.632	-0.015	-0.015	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.027	0.016	24.432	0.016	0.016	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.044	0.032	25.105	-0.013	-0.013	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.010	-0.006	22.616	0.007	0.007	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.048	-0.044	23.600	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	99	GLN	0	0.084	0.015	20.809	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.806	-0.856	21.968	0.090	0.090	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.873	0.910	24.338	-0.091	-0.091	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.037	0.025	16.995	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.885	0.946	19.782	-0.102	-0.102	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.005	0.000	20.883	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.012	0.001	21.027	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	106	VAL	0	0.026	0.007	16.340	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.006	0.004	19.366	-0.015	-0.015	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.797	0.875	21.641	-0.081	-0.081	0.000	0.000	0.000	0.000
108	A	109	HIS	0	-0.041	-0.036	21.241	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	110	ALA	0	0.024	0.022	18.736	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.044	-0.001	20.422	-0.018	-0.018	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.006	-0.006	24.130	0.010	0.010	0.000	0.000	0.000	0.000

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