FMO DATABASE

FMODB ID: 3Q8JL

Calculation Name: 1JPE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JPE

Chain ID: A

ChEMBL ID:

UniProt ID: P36655

Base Structure: X-ray

Registration Date: 2023-06-19

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-942267.659277
FMO2-HF: Nuclear repulsion	896372.475232
FMO2-HF: Total energy	-45895.184045
FMO2-MP2: Total energy	-46030.963018

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:10:GLN)

Summations of interaction energy for fragment #1(A:10:GLN)

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.
-11.909	-4.925	7.548	-4.616	-9.918	-0.011

Interaction energy analysis for fragmet #1(A:10:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.037 / q_NPA : 0.002

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	12	VAL	0	0.009	0.013	3.634	0.406	2.278	-0.002	-0.792	-1.079	0.001
4	A	13	PRO	0	0.056	0.027	5.580	-0.011	-0.011	0.000	0.000	0.000	0.000
5	A	14	ALA	0	0.063	0.035	9.206	-0.440	-0.440	0.000	0.000	0.000	0.000
6	A	15	ASP	-1	-0.795	-0.865	10.500	-1.418	-1.418	0.000	0.000	0.000	0.000
7	A	16	GLN	0	-0.049	-0.037	8.703	0.286	0.286	0.000	0.000	0.000	0.000
8	A	17	ALA	0	-0.015	0.017	6.301	-0.322	-0.322	0.000	0.000	0.000	0.000
9	A	18	PHE	0	-0.033	-0.028	7.587	0.163	0.163	0.000	0.000	0.000	0.000
10	A	19	ALA	0	0.025	0.022	11.114	0.282	0.282	0.000	0.000	0.000	0.000
11	A	20	PHE	0	-0.037	-0.024	13.789	0.123	0.123	0.000	0.000	0.000	0.000
12	A	21	ASP	-1	-0.882	-0.937	16.938	-0.627	-0.627	0.000	0.000	0.000	0.000
13	A	22	PHE	0	-0.056	-0.036	20.306	0.005	0.005	0.000	0.000	0.000	0.000
14	A	23	GLN	0	0.019	0.014	23.855	0.040	0.040	0.000	0.000	0.000	0.000
15	A	24	GLN	0	0.015	0.016	27.211	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	25	ASN	0	0.007	0.003	30.741	0.022	0.022	0.000	0.000	0.000	0.000
17	A	26	GLN	0	0.000	-0.010	34.072	0.015	0.015	0.000	0.000	0.000	0.000
18	A	27	HIS	1	0.888	0.935	35.469	0.219	0.219	0.000	0.000	0.000	0.000
19	A	28	ASP	-1	-0.903	-0.927	32.375	-0.296	-0.296	0.000	0.000	0.000	0.000
20	A	29	LEU	0	0.009	-0.001	27.006	0.001	0.001	0.000	0.000	0.000	0.000
21	A	30	ASN	0	-0.044	-0.017	23.787	-0.042	-0.042	0.000	0.000	0.000	0.000
22	A	31	LEU	0	0.045	0.027	22.036	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	32	THR	0	0.017	-0.007	18.332	0.001	0.001	0.000	0.000	0.000	0.000
24	A	33	TRP	0	0.014	0.006	14.308	0.019	0.019	0.000	0.000	0.000	0.000
25	A	34	GLN	0	0.019	0.008	13.651	0.108	0.108	0.000	0.000	0.000	0.000
26	A	35	ILE	0	-0.068	-0.025	9.283	-0.166	-0.166	0.000	0.000	0.000	0.000
27	A	36	LYS	1	0.827	0.911	4.223	5.273	5.400	-0.001	-0.012	-0.114	0.000
28	A	37	ASP	-1	-0.790	-0.894	5.907	-3.128	-3.128	0.000	0.000	0.000	0.000
29	A	38	GLY	0	0.012	0.008	3.135	-2.192	-1.878	0.014	-0.071	-0.256	0.000
30	A	39	TYR	0	-0.058	-0.033	2.177	-9.075	-7.274	5.374	-2.329	-4.846	-0.018
31	A	40	TYR	0	-0.039	-0.047	5.989	0.876	0.876	0.000	0.000	0.000	0.000
32	A	41	LEU	0	-0.001	0.012	9.759	-0.096	-0.096	0.000	0.000	0.000	0.000
33	A	42	TYR	0	0.015	-0.034	12.925	0.082	0.082	0.000	0.000	0.000	0.000
34	A	43	ARG	1	0.790	0.875	15.955	0.538	0.538	0.000	0.000	0.000	0.000
35	A	44	LYS	1	0.850	0.903	19.264	0.517	0.517	0.000	0.000	0.000	0.000
36	A	45	GLN	0	0.013	0.024	17.406	0.063	0.063	0.000	0.000	0.000	0.000
37	A	46	ILE	0	-0.048	-0.013	17.466	-0.041	-0.041	0.000	0.000	0.000	0.000
38	A	47	ARG	1	0.799	0.882	20.569	0.564	0.564	0.000	0.000	0.000	0.000
39	A	48	ILE	0	0.022	-0.001	23.268	-0.028	-0.028	0.000	0.000	0.000	0.000
40	A	49	THR	0	-0.008	-0.012	26.057	0.024	0.024	0.000	0.000	0.000	0.000
41	A	50	PRO	0	0.001	0.019	29.366	-0.014	-0.014	0.000	0.000	0.000	0.000
42	A	51	GLU	-1	-0.781	-0.846	30.181	-0.353	-0.353	0.000	0.000	0.000	0.000
43	A	52	HIS	0	0.008	-0.001	34.099	0.004	0.004	0.000	0.000	0.000	0.000
44	A	53	ALA	0	0.038	0.028	34.500	0.008	0.008	0.000	0.000	0.000	0.000
45	A	54	LYS	1	0.910	0.955	36.283	0.201	0.201	0.000	0.000	0.000	0.000
46	A	55	ILE	0	0.007	0.002	30.336	0.003	0.003	0.000	0.000	0.000	0.000
47	A	56	ALA	0	-0.010	-0.004	33.678	0.014	0.014	0.000	0.000	0.000	0.000
48	A	57	ASP	-1	-0.913	-0.958	32.322	-0.290	-0.290	0.000	0.000	0.000	0.000
49	A	58	VAL	0	0.012	0.004	26.184	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	59	GLN	0	-0.029	-0.017	27.600	-0.035	-0.035	0.000	0.000	0.000	0.000
51	A	60	LEU	0	0.014	0.020	21.920	-0.016	-0.016	0.000	0.000	0.000	0.000
52	A	61	PRO	0	0.030	0.026	21.324	0.037	0.037	0.000	0.000	0.000	0.000
53	A	62	GLN	0	-0.031	-0.014	22.168	-0.025	-0.025	0.000	0.000	0.000	0.000
54	A	63	GLY	0	0.033	0.022	19.205	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	64	VAL	0	-0.037	-0.015	14.801	0.080	0.080	0.000	0.000	0.000	0.000
56	A	65	TRP	0	-0.037	-0.033	17.261	-0.047	-0.047	0.000	0.000	0.000	0.000
57	A	66	HIS	0	0.020	0.017	10.681	0.031	0.031	0.000	0.000	0.000	0.000
58	A	67	GLU	-1	-0.907	-0.967	14.870	-0.175	-0.175	0.000	0.000	0.000	0.000
59	A	68	ASP	-1	-0.761	-0.834	13.009	-0.843	-0.843	0.000	0.000	0.000	0.000
60	A	69	GLU	-1	-0.876	-0.951	13.325	-0.096	-0.096	0.000	0.000	0.000	0.000
61	A	70	PHE	0	-0.081	-0.028	11.032	0.000	0.000	0.000	0.000	0.000	0.000
62	A	71	TYR	0	-0.071	-0.058	15.680	0.072	0.072	0.000	0.000	0.000	0.000
63	A	72	GLY	0	0.041	0.041	17.969	0.041	0.041	0.000	0.000	0.000	0.000
64	A	73	LYS	1	0.892	0.950	18.303	0.194	0.194	0.000	0.000	0.000	0.000
65	A	74	SER	0	-0.030	-0.012	17.040	0.003	0.003	0.000	0.000	0.000	0.000
66	A	75	GLU	-1	-0.798	-0.873	18.301	-0.508	-0.508	0.000	0.000	0.000	0.000
67	A	76	ILE	0	-0.025	-0.012	12.338	-0.038	-0.038	0.000	0.000	0.000	0.000
68	A	77	TYR	0	-0.025	-0.041	14.442	0.119	0.119	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.821	0.860	7.687	1.568	1.568	0.000	0.000	0.000	0.000
70	A	79	ASP	-1	-0.854	-0.913	10.905	-1.146	-1.146	0.000	0.000	0.000	0.000
71	A	80	ARG	1	0.828	0.895	12.447	0.897	0.897	0.000	0.000	0.000	0.000
72	A	81	LEU	0	-0.028	0.020	15.307	0.082	0.082	0.000	0.000	0.000	0.000
73	A	82	THR	0	-0.022	-0.034	17.483	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	83	LEU	0	-0.018	-0.005	20.968	0.029	0.029	0.000	0.000	0.000	0.000
75	A	84	PRO	0	-0.005	0.010	23.746	0.002	0.002	0.000	0.000	0.000	0.000
76	A	85	VAL	0	0.006	-0.011	26.733	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	86	THR	0	0.041	0.027	29.500	0.005	0.005	0.000	0.000	0.000	0.000
78	A	87	ILE	0	0.013	0.011	31.692	0.005	0.005	0.000	0.000	0.000	0.000
79	A	88	ASN	0	0.022	0.010	34.814	0.018	0.018	0.000	0.000	0.000	0.000
80	A	89	GLN	0	-0.049	-0.038	37.731	0.014	0.014	0.000	0.000	0.000	0.000
81	A	90	ALA	0	0.018	0.014	35.870	-0.015	-0.015	0.000	0.000	0.000	0.000
82	A	91	SER	0	-0.020	-0.020	37.871	0.013	0.013	0.000	0.000	0.000	0.000
83	A	92	ALA	0	0.019	-0.007	38.036	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	93	GLY	0	-0.001	0.008	36.351	0.008	0.008	0.000	0.000	0.000	0.000
85	A	94	ALA	0	-0.058	-0.018	35.204	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	95	THR	0	-0.064	-0.059	29.891	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	96	LEU	0	0.028	0.008	26.924	0.015	0.015	0.000	0.000	0.000	0.000
88	A	97	THR	0	0.007	-0.008	25.280	-0.047	-0.047	0.000	0.000	0.000	0.000
89	A	98	VAL	0	-0.038	-0.003	20.819	0.011	0.011	0.000	0.000	0.000	0.000
90	A	99	THR	0	-0.006	-0.017	20.130	0.007	0.007	0.000	0.000	0.000	0.000
91	A	100	TYR	0	0.026	0.021	13.970	0.086	0.086	0.000	0.000	0.000	0.000
92	A	101	GLN	0	0.041	0.015	13.827	0.076	0.076	0.000	0.000	0.000	0.000
93	A	102	GLY	0	0.045	0.016	10.967	0.087	0.087	0.000	0.000	0.000	0.000
94	A	103	CYS	0	-0.050	0.003	7.568	-0.448	-0.448	0.000	0.000	0.000	0.000
95	A	104	ALA	0	0.078	0.024	3.431	-1.304	-0.946	0.023	-0.147	-0.234	0.000
96	A	105	ASP	-1	-0.761	-0.862	5.120	-1.015	-1.015	0.000	0.000	0.000	0.000
97	A	106	ALA	0	-0.067	-0.026	2.742	-0.398	0.653	1.613	-0.839	-1.826	0.006
98	A	107	GLY	0	0.020	0.025	4.603	-0.042	0.116	-0.001	-0.023	-0.135	0.000
99	A	108	PHE	0	-0.045	-0.025	2.764	-1.010	0.293	0.528	-0.403	-1.428	0.000
100	A	110	TYR	0	-0.045	-0.034	5.977	-0.281	-0.281	0.000	0.000	0.000	0.000
101	A	111	PRO	0	0.007	0.003	10.866	0.153	0.153	0.000	0.000	0.000	0.000
102	A	112	PRO	0	-0.003	-0.016	14.395	-0.142	-0.142	0.000	0.000	0.000	0.000
103	A	113	GLH	0	-0.062	-0.036	14.465	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	114	THR	0	0.008	-0.004	17.105	0.022	0.022	0.000	0.000	0.000	0.000
105	A	115	LYS	1	0.831	0.913	16.685	0.979	0.979	0.000	0.000	0.000	0.000
106	A	116	THR	0	0.026	0.013	21.884	0.003	0.003	0.000	0.000	0.000	0.000
107	A	117	VAL	0	-0.005	0.010	24.241	0.001	0.001	0.000	0.000	0.000	0.000
108	A	118	PRO	0	0.001	0.000	26.529	0.028	0.028	0.000	0.000	0.000	0.000
109	A	119	LEU	0	-0.044	-0.016	30.042	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	120	SER	0	-0.020	-0.020	32.505	0.020	0.020	0.000	0.000	0.000	0.000
111	A	121	GLU	-1	-0.888	-0.946	35.412	-0.199	-0.199	0.000	0.000	0.000	0.000
112	A	122	VAL	0	-0.067	-0.032	36.458	0.001	0.001	0.000	0.000	0.000	0.000
113	A	123	VAL	0	0.035	0.011	39.635	0.002	0.002	0.000	0.000	0.000	0.000
114	A	124	ALA	0	-0.004	-0.004	42.228	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	125	ASN	0	-0.013	0.004	42.338	0.006	0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:GLN)