FMO DATABASE

FMODB ID: J37Q9

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-941053.994561
FMO2-HF: Nuclear repulsion	895159.054974
FMO2-HF: Total energy	-45894.939587
FMO2-MP2: Total energy	-46030.68368

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.
-9.422	-2.212	4.083	-3.614	-7.678	-0.015

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 : 0.008 / q_NPA : -0.011

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	-0.003	0.008	3.435	0.524	2.430	0.008	-0.730	-1.184	0.002
4	A	13	PRO	0	0.070	0.037	5.312	-0.207	-0.167	-0.001	-0.004	-0.035	0.000
5	A	14	ALA	0	0.089	0.036	9.087	-0.424	-0.424	0.000	0.000	0.000	0.000
6	A	15	ASP	-1	-0.789	-0.850	10.848	-1.217	-1.217	0.000	0.000	0.000	0.000
7	A	16	GLN	0	-0.077	-0.043	8.773	0.293	0.293	0.000	0.000	0.000	0.000
8	A	17	ALA	0	-0.037	-0.003	6.798	-0.160	-0.160	0.000	0.000	0.000	0.000
9	A	18	PHE	0	-0.015	-0.013	8.168	0.044	0.044	0.000	0.000	0.000	0.000
10	A	19	ALA	0	-0.002	0.011	11.560	0.227	0.227	0.000	0.000	0.000	0.000
11	A	20	PHE	0	-0.012	-0.013	14.311	0.081	0.081	0.000	0.000	0.000	0.000
12	A	21	ASP	-1	-0.877	-0.932	17.577	-0.550	-0.550	0.000	0.000	0.000	0.000
13	A	22	PHE	0	-0.032	-0.024	20.994	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	23	GLN	0	0.019	0.015	24.432	0.030	0.030	0.000	0.000	0.000	0.000
15	A	24	GLN	0	-0.002	0.001	27.605	-0.012	-0.012	0.000	0.000	0.000	0.000
16	A	25	ASN	0	-0.010	-0.005	30.986	0.024	0.024	0.000	0.000	0.000	0.000
17	A	26	GLN	0	0.010	-0.006	34.201	0.014	0.014	0.000	0.000	0.000	0.000
18	A	27	HIS	1	0.902	0.939	35.385	0.210	0.210	0.000	0.000	0.000	0.000
19	A	28	ASP	-1	-0.918	-0.922	32.543	-0.285	-0.285	0.000	0.000	0.000	0.000
20	A	29	LEU	0	0.023	0.011	27.517	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	30	ASN	0	-0.030	-0.012	24.406	-0.042	-0.042	0.000	0.000	0.000	0.000
22	A	31	LEU	0	0.019	0.012	22.412	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	32	THR	0	0.007	-0.012	18.737	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	33	TRP	0	0.019	0.008	14.833	0.020	0.020	0.000	0.000	0.000	0.000
25	A	34	GLN	0	-0.022	-0.019	13.931	0.090	0.090	0.000	0.000	0.000	0.000
26	A	35	ILE	0	-0.053	-0.021	9.402	-0.133	-0.133	0.000	0.000	0.000	0.000
27	A	36	LYS	1	0.895	0.966	3.733	6.075	6.306	-0.001	-0.069	-0.161	0.000
28	A	37	ASP	-1	-0.844	-0.935	6.538	-2.634	-2.634	0.000	0.000	0.000	0.000
29	A	38	GLY	0	0.003	0.010	3.634	-2.041	-1.842	0.000	-0.027	-0.172	0.000
30	A	39	TYR	0	-0.070	-0.045	2.235	-9.143	-6.449	2.971	-1.987	-3.677	-0.019
31	A	40	TYR	0	-0.031	-0.039	6.490	0.694	0.694	0.000	0.000	0.000	0.000
32	A	41	LEU	0	-0.010	0.004	10.215	-0.057	-0.057	0.000	0.000	0.000	0.000
33	A	42	TYR	0	0.018	-0.028	13.378	0.076	0.076	0.000	0.000	0.000	0.000
34	A	43	ARG	1	0.804	0.879	16.179	0.549	0.549	0.000	0.000	0.000	0.000
35	A	44	LYS	1	0.921	0.933	19.366	0.489	0.489	0.000	0.000	0.000	0.000
36	A	45	GLN	0	0.007	0.021	17.640	0.064	0.064	0.000	0.000	0.000	0.000
37	A	46	ILE	0	-0.045	-0.011	18.201	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	47	ARG	1	0.814	0.896	21.110	0.535	0.535	0.000	0.000	0.000	0.000
39	A	48	ILE	0	0.010	-0.005	23.876	-0.024	-0.024	0.000	0.000	0.000	0.000
40	A	49	THR	0	-0.015	-0.007	26.539	0.017	0.017	0.000	0.000	0.000	0.000
41	A	50	PRO	0	0.009	0.028	29.655	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	51	GLU	-1	-0.799	-0.855	30.744	-0.331	-0.331	0.000	0.000	0.000	0.000
43	A	52	HIS	0	-0.008	-0.009	34.489	0.005	0.005	0.000	0.000	0.000	0.000
44	A	53	ALA	0	0.065	0.019	34.854	0.005	0.005	0.000	0.000	0.000	0.000
45	A	54	LYS	1	0.900	0.957	36.640	0.190	0.190	0.000	0.000	0.000	0.000
46	A	55	ILE	0	0.010	-0.003	30.661	0.003	0.003	0.000	0.000	0.000	0.000
47	A	56	ALA	0	-0.028	-0.006	34.324	0.010	0.010	0.000	0.000	0.000	0.000
48	A	57	ASP	-1	-0.907	-0.950	32.959	-0.279	-0.279	0.000	0.000	0.000	0.000
49	A	58	VAL	0	0.000	-0.003	26.652	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	59	GLN	0	-0.025	-0.008	28.247	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	60	LEU	0	-0.006	0.003	22.391	-0.018	-0.018	0.000	0.000	0.000	0.000
52	A	61	PRO	0	0.049	0.030	21.530	0.038	0.038	0.000	0.000	0.000	0.000
53	A	62	GLN	0	-0.038	-0.011	22.475	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	63	GLY	0	0.025	0.021	19.267	-0.026	-0.026	0.000	0.000	0.000	0.000
55	A	64	VAL	0	-0.026	-0.011	15.305	0.083	0.083	0.000	0.000	0.000	0.000
56	A	65	TRP	0	-0.048	-0.027	17.731	-0.045	-0.045	0.000	0.000	0.000	0.000
57	A	66	HIS	0	0.027	0.014	10.753	0.025	0.025	0.000	0.000	0.000	0.000
58	A	67	GLU	-1	-0.953	-0.986	15.176	-0.202	-0.202	0.000	0.000	0.000	0.000
59	A	68	ASP	-1	-0.778	-0.845	13.178	-0.883	-0.883	0.000	0.000	0.000	0.000
60	A	69	GLU	-1	-0.876	-0.951	13.431	-0.225	-0.225	0.000	0.000	0.000	0.000
61	A	70	PHE	0	-0.080	-0.025	11.102	0.013	0.013	0.000	0.000	0.000	0.000
62	A	71	TYR	0	-0.061	-0.038	16.063	0.094	0.094	0.000	0.000	0.000	0.000
63	A	72	GLY	0	0.022	0.029	18.173	0.037	0.037	0.000	0.000	0.000	0.000
64	A	73	LYS	1	0.949	0.985	18.128	0.242	0.242	0.000	0.000	0.000	0.000
65	A	74	SER	0	-0.012	-0.020	17.426	0.010	0.010	0.000	0.000	0.000	0.000
66	A	75	GLU	-1	-0.839	-0.891	18.136	-0.537	-0.537	0.000	0.000	0.000	0.000
67	A	76	ILE	0	-0.012	-0.015	12.346	-0.040	-0.040	0.000	0.000	0.000	0.000
68	A	77	TYR	0	-0.035	-0.050	14.658	0.108	0.108	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.845	0.868	7.951	1.575	1.575	0.000	0.000	0.000	0.000
70	A	79	ASP	-1	-0.862	-0.918	11.321	-1.092	-1.092	0.000	0.000	0.000	0.000
71	A	80	ARG	1	0.868	0.912	12.907	0.829	0.829	0.000	0.000	0.000	0.000
72	A	81	LEU	0	-0.031	0.015	15.521	0.069	0.069	0.000	0.000	0.000	0.000
73	A	82	THR	0	-0.034	-0.022	17.971	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	83	LEU	0	-0.009	-0.014	21.504	0.022	0.022	0.000	0.000	0.000	0.000
75	A	84	PRO	0	-0.005	0.016	23.979	0.004	0.004	0.000	0.000	0.000	0.000
76	A	85	VAL	0	0.002	-0.015	26.954	0.002	0.002	0.000	0.000	0.000	0.000
77	A	86	THR	0	0.041	0.024	29.685	0.007	0.007	0.000	0.000	0.000	0.000
78	A	87	ILE	0	0.026	0.015	31.938	0.004	0.004	0.000	0.000	0.000	0.000
79	A	88	ASN	0	0.001	-0.006	35.165	0.015	0.015	0.000	0.000	0.000	0.000
80	A	89	GLN	0	-0.028	-0.032	38.129	0.011	0.011	0.000	0.000	0.000	0.000
81	A	90	ALA	0	0.019	0.020	36.372	-0.013	-0.013	0.000	0.000	0.000	0.000
82	A	91	SER	0	-0.016	0.012	38.327	0.009	0.009	0.000	0.000	0.000	0.000
83	A	92	ALA	0	0.046	0.011	38.592	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	93	GLY	0	-0.020	-0.006	36.516	0.006	0.006	0.000	0.000	0.000	0.000
85	A	94	ALA	0	-0.030	0.004	35.574	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	95	THR	0	-0.040	-0.043	30.344	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	96	LEU	0	0.004	0.007	27.325	0.010	0.010	0.000	0.000	0.000	0.000
88	A	97	THR	0	-0.006	-0.025	25.560	-0.037	-0.037	0.000	0.000	0.000	0.000
89	A	98	VAL	0	-0.010	-0.011	21.187	0.005	0.005	0.000	0.000	0.000	0.000
90	A	99	THR	0	0.001	-0.003	20.516	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	100	TYR	0	0.011	0.017	14.506	0.071	0.071	0.000	0.000	0.000	0.000
92	A	101	GLN	0	0.044	0.001	14.036	0.080	0.080	0.000	0.000	0.000	0.000
93	A	102	GLY	0	0.053	0.026	11.283	0.092	0.092	0.000	0.000	0.000	0.000
94	A	103	CYS	0	-0.063	0.005	7.788	-0.433	-0.433	0.000	0.000	0.000	0.000
95	A	104	ALA	0	0.051	0.010	3.699	-0.902	-0.729	0.004	-0.056	-0.121	0.000
96	A	105	ASP	-1	-0.732	-0.849	4.865	-1.299	-1.299	0.000	0.000	0.000	0.000
97	A	106	ALA	0	-0.088	-0.039	2.828	-0.047	0.969	1.019	-0.538	-1.497	0.002
98	A	107	GLY	0	0.018	0.025	4.900	0.451	0.603	-0.001	-0.018	-0.133	0.000
99	A	108	PHE	0	-0.029	-0.021	2.943	-0.552	0.247	0.084	-0.185	-0.698	0.000
100	A	110	TYR	0	-0.053	-0.041	6.263	-0.348	-0.348	0.000	0.000	0.000	0.000
101	A	111	PRO	0	0.003	0.005	11.025	0.129	0.129	0.000	0.000	0.000	0.000
102	A	112	PRO	0	0.005	-0.014	14.671	-0.116	-0.116	0.000	0.000	0.000	0.000
103	A	113	GLH	0	-0.066	-0.054	15.099	-0.013	-0.013	0.000	0.000	0.000	0.000
104	A	114	THR	0	0.005	-0.012	17.813	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	115	LYS	1	0.836	0.924	17.123	0.899	0.899	0.000	0.000	0.000	0.000
106	A	116	THR	0	0.025	0.011	22.353	0.011	0.011	0.000	0.000	0.000	0.000
107	A	117	VAL	0	-0.018	-0.010	24.839	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	118	PRO	0	-0.008	0.004	27.193	0.022	0.022	0.000	0.000	0.000	0.000
109	A	119	LEU	0	-0.033	-0.012	30.442	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	120	SER	0	-0.038	-0.026	32.747	0.020	0.020	0.000	0.000	0.000	0.000
111	A	121	GLU	-1	-0.894	-0.969	35.513	-0.188	-0.188	0.000	0.000	0.000	0.000
112	A	122	VAL	0	-0.058	-0.025	36.972	0.001	0.001	0.000	0.000	0.000	0.000
113	A	123	VAL	0	0.010	0.000	39.963	0.002	0.002	0.000	0.000	0.000	0.000
114	A	124	ALA	0	-0.023	-0.022	42.664	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	125	ASN	0	-0.001	0.017	42.991	0.005	0.005	0.000	0.000	0.000	0.000

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