FMO DATABASE

FMODB ID: N1JNQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-940513.890999
FMO2-HF: Nuclear repulsion	894619.408888
FMO2-HF: Total energy	-45894.48211
FMO2-MP2: Total energy	-46030.280737

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.
-6.199	0.351	1.699	-2.767	-5.486	-0.004

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 : 0.022 / 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	-0.024	0.002	3.426	0.549	2.440	0.009	-0.727	-1.173	0.002
4	A	13	PRO	0	0.071	0.046	5.303	-0.139	-0.094	-0.001	-0.004	-0.041	0.000
5	A	14	ALA	0	0.104	0.043	8.957	-0.487	-0.487	0.000	0.000	0.000	0.000
6	A	15	ASP	-1	-0.824	-0.894	10.674	-1.331	-1.331	0.000	0.000	0.000	0.000
7	A	16	GLN	0	-0.073	-0.041	8.480	0.437	0.437	0.000	0.000	0.000	0.000
8	A	17	ALA	0	-0.037	-0.006	6.955	-0.258	-0.258	0.000	0.000	0.000	0.000
9	A	18	PHE	0	-0.018	-0.004	8.529	0.031	0.031	0.000	0.000	0.000	0.000
10	A	19	ALA	0	0.020	0.012	12.161	0.255	0.255	0.000	0.000	0.000	0.000
11	A	20	PHE	0	-0.034	-0.015	14.645	0.082	0.082	0.000	0.000	0.000	0.000
12	A	21	ASP	-1	-0.880	-0.938	18.051	-0.657	-0.657	0.000	0.000	0.000	0.000
13	A	22	PHE	0	-0.044	-0.022	21.416	0.002	0.002	0.000	0.000	0.000	0.000
14	A	23	GLN	0	0.031	0.018	24.955	0.023	0.023	0.000	0.000	0.000	0.000
15	A	24	GLN	0	-0.004	-0.003	28.085	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	25	ASN	0	-0.031	-0.009	31.499	0.025	0.025	0.000	0.000	0.000	0.000
17	A	26	GLN	0	0.015	-0.001	34.686	0.019	0.019	0.000	0.000	0.000	0.000
18	A	27	HIS	1	0.905	0.930	35.947	0.247	0.247	0.000	0.000	0.000	0.000
19	A	28	ASP	-1	-0.911	-0.917	32.970	-0.336	-0.336	0.000	0.000	0.000	0.000
20	A	29	LEU	0	0.020	0.009	28.310	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	30	ASN	0	-0.034	-0.016	24.886	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	31	LEU	0	0.005	0.005	23.023	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	32	THR	0	-0.001	-0.007	18.871	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	33	TRP	0	0.008	0.002	15.427	0.022	0.022	0.000	0.000	0.000	0.000
25	A	34	GLN	0	-0.057	-0.042	14.045	0.020	0.020	0.000	0.000	0.000	0.000
26	A	35	ILE	0	-0.047	-0.023	9.860	-0.113	-0.113	0.000	0.000	0.000	0.000
27	A	36	LYS	1	0.912	0.978	4.937	6.488	6.488	0.000	0.000	0.000	0.000
28	A	37	ASP	-1	-0.872	-0.947	7.172	-3.579	-3.579	0.000	0.000	0.000	0.000
29	A	38	GLY	0	0.014	0.011	4.366	-2.375	-2.258	-0.001	-0.008	-0.109	0.000
30	A	39	TYR	0	-0.067	-0.045	2.757	-5.378	-2.829	0.434	-1.164	-1.819	-0.010
31	A	40	TYR	0	-0.025	-0.018	7.125	0.611	0.611	0.000	0.000	0.000	0.000
32	A	41	LEU	0	-0.014	0.001	10.875	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	42	TYR	0	0.018	-0.022	14.099	0.061	0.061	0.000	0.000	0.000	0.000
34	A	43	ARG	1	0.874	0.940	16.870	0.588	0.588	0.000	0.000	0.000	0.000
35	A	44	LYS	1	0.913	0.927	20.071	0.479	0.479	0.000	0.000	0.000	0.000
36	A	45	GLN	0	0.002	0.018	17.711	0.060	0.060	0.000	0.000	0.000	0.000
37	A	46	ILE	0	-0.026	-0.003	19.057	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	47	ARG	1	0.820	0.908	21.748	0.527	0.527	0.000	0.000	0.000	0.000
39	A	48	ILE	0	0.003	-0.008	24.744	-0.029	-0.029	0.000	0.000	0.000	0.000
40	A	49	THR	0	-0.024	-0.004	27.211	0.016	0.016	0.000	0.000	0.000	0.000
41	A	50	PRO	0	0.003	0.026	30.172	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	51	GLU	-1	-0.800	-0.901	31.396	-0.338	-0.338	0.000	0.000	0.000	0.000
43	A	52	HIS	0	-0.014	-0.012	34.948	0.003	0.003	0.000	0.000	0.000	0.000
44	A	53	ALA	0	0.070	0.021	35.551	0.003	0.003	0.000	0.000	0.000	0.000
45	A	54	LYS	1	0.895	0.954	37.353	0.209	0.209	0.000	0.000	0.000	0.000
46	A	55	ILE	0	0.018	0.001	31.481	0.001	0.001	0.000	0.000	0.000	0.000
47	A	56	ALA	0	-0.035	-0.009	34.914	0.012	0.012	0.000	0.000	0.000	0.000
48	A	57	ASP	-1	-0.904	-0.947	33.643	-0.302	-0.302	0.000	0.000	0.000	0.000
49	A	58	VAL	0	-0.004	-0.008	27.349	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	59	GLN	0	-0.039	-0.015	28.806	-0.013	-0.013	0.000	0.000	0.000	0.000
51	A	60	LEU	0	-0.027	-0.011	23.309	-0.022	-0.022	0.000	0.000	0.000	0.000
52	A	61	PRO	0	0.033	0.018	22.113	0.040	0.040	0.000	0.000	0.000	0.000
53	A	62	GLN	0	-0.047	-0.024	22.887	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	63	GLY	0	0.012	0.002	19.821	-0.039	-0.039	0.000	0.000	0.000	0.000
55	A	64	VAL	0	-0.014	0.001	15.984	0.088	0.088	0.000	0.000	0.000	0.000
56	A	65	TRP	0	-0.032	-0.022	18.423	-0.031	-0.031	0.000	0.000	0.000	0.000
57	A	66	HIS	0	0.018	0.003	11.477	-0.064	-0.064	0.000	0.000	0.000	0.000
58	A	67	GLU	-1	-0.967	-0.989	15.668	-0.114	-0.114	0.000	0.000	0.000	0.000
59	A	68	ASP	-1	-0.778	-0.859	13.240	-0.707	-0.707	0.000	0.000	0.000	0.000
60	A	69	GLU	-1	-0.870	-0.953	13.212	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	70	PHE	0	-0.085	-0.025	11.034	0.001	0.001	0.000	0.000	0.000	0.000
62	A	71	TYR	0	-0.066	-0.041	16.271	0.063	0.063	0.000	0.000	0.000	0.000
63	A	72	GLY	0	0.025	0.031	18.109	0.021	0.021	0.000	0.000	0.000	0.000
64	A	73	LYS	1	0.935	0.978	18.337	0.227	0.227	0.000	0.000	0.000	0.000
65	A	74	SER	0	-0.009	-0.016	17.803	0.014	0.014	0.000	0.000	0.000	0.000
66	A	75	GLU	-1	-0.824	-0.884	18.757	-0.594	-0.594	0.000	0.000	0.000	0.000
67	A	76	ILE	0	-0.008	-0.016	12.990	-0.037	-0.037	0.000	0.000	0.000	0.000
68	A	77	TYR	0	-0.059	-0.062	15.302	0.103	0.103	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.887	0.898	8.469	1.906	1.906	0.000	0.000	0.000	0.000
70	A	79	ASP	-1	-0.858	-0.910	11.719	-1.444	-1.444	0.000	0.000	0.000	0.000
71	A	80	ARG	1	0.908	0.930	13.245	1.004	1.004	0.000	0.000	0.000	0.000
72	A	81	LEU	0	-0.032	0.023	15.955	0.084	0.084	0.000	0.000	0.000	0.000
73	A	82	THR	0	-0.015	-0.020	18.509	-0.024	-0.024	0.000	0.000	0.000	0.000
74	A	83	LEU	0	-0.011	-0.014	22.020	0.029	0.029	0.000	0.000	0.000	0.000
75	A	84	PRO	0	-0.010	0.008	24.564	0.006	0.006	0.000	0.000	0.000	0.000
76	A	85	VAL	0	0.011	-0.006	27.629	0.006	0.006	0.000	0.000	0.000	0.000
77	A	86	THR	0	0.039	0.024	30.305	0.005	0.005	0.000	0.000	0.000	0.000
78	A	87	ILE	0	0.028	0.016	32.619	0.008	0.008	0.000	0.000	0.000	0.000
79	A	88	ASN	0	0.004	-0.001	35.798	0.012	0.012	0.000	0.000	0.000	0.000
80	A	89	GLN	0	-0.027	-0.037	38.790	0.011	0.011	0.000	0.000	0.000	0.000
81	A	90	ALA	0	0.032	0.030	37.030	-0.013	-0.013	0.000	0.000	0.000	0.000
82	A	91	SER	0	-0.002	0.015	38.979	0.010	0.010	0.000	0.000	0.000	0.000
83	A	92	ALA	0	0.054	0.012	38.980	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	93	GLY	0	-0.010	-0.004	36.583	0.008	0.008	0.000	0.000	0.000	0.000
85	A	94	ALA	0	-0.022	0.009	35.808	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	95	THR	0	-0.016	-0.013	30.643	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	96	LEU	0	-0.004	0.007	27.910	0.012	0.012	0.000	0.000	0.000	0.000
88	A	97	THR	0	0.012	0.006	25.792	-0.036	-0.036	0.000	0.000	0.000	0.000
89	A	98	VAL	0	-0.003	-0.011	21.848	0.007	0.007	0.000	0.000	0.000	0.000
90	A	99	THR	0	-0.015	0.000	20.692	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	100	TYR	0	0.036	0.028	15.170	0.072	0.072	0.000	0.000	0.000	0.000
92	A	101	GLN	0	0.047	0.005	14.218	0.071	0.071	0.000	0.000	0.000	0.000
93	A	102	GLY	0	0.049	0.019	11.872	0.068	0.068	0.000	0.000	0.000	0.000
94	A	103	CYS	0	-0.058	0.006	7.797	-0.428	-0.428	0.000	0.000	0.000	0.000
95	A	104	ALA	0	0.042	0.007	3.694	-0.845	-0.760	0.002	-0.032	-0.056	0.000
96	A	105	ASP	-1	-0.737	-0.857	5.265	-1.615	-1.615	0.000	0.000	0.000	0.000
97	A	106	ALA	0	-0.090	-0.043	2.843	0.104	1.178	1.220	-0.684	-1.610	0.004
98	A	107	GLY	0	0.015	0.024	4.759	0.570	0.746	-0.001	-0.025	-0.151	0.000
99	A	108	PHE	0	-0.028	-0.019	3.110	-0.458	0.155	0.037	-0.123	-0.527	0.000
100	A	110	TYR	0	-0.049	-0.047	6.479	-0.317	-0.317	0.000	0.000	0.000	0.000
101	A	111	PRO	0	-0.009	-0.001	11.101	0.121	0.121	0.000	0.000	0.000	0.000
102	A	112	PRO	0	0.009	-0.012	14.757	-0.129	-0.129	0.000	0.000	0.000	0.000
103	A	113	GLH	0	-0.053	-0.029	14.984	-0.020	-0.020	0.000	0.000	0.000	0.000
104	A	114	THR	0	-0.020	-0.042	17.912	0.011	0.011	0.000	0.000	0.000	0.000
105	A	115	LYS	1	0.836	0.923	17.225	0.951	0.951	0.000	0.000	0.000	0.000
106	A	116	THR	0	0.020	0.005	22.563	0.011	0.011	0.000	0.000	0.000	0.000
107	A	117	VAL	0	-0.016	-0.007	25.264	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	118	PRO	0	-0.017	0.000	27.495	0.027	0.027	0.000	0.000	0.000	0.000
109	A	119	LEU	0	-0.019	-0.011	30.838	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	120	SER	0	-0.042	-0.025	33.162	0.022	0.022	0.000	0.000	0.000	0.000
111	A	121	GLU	-1	-0.935	-0.980	35.880	-0.211	-0.211	0.000	0.000	0.000	0.000
112	A	122	VAL	0	-0.061	-0.025	37.558	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	123	VAL	0	0.020	0.003	40.564	0.004	0.004	0.000	0.000	0.000	0.000
114	A	124	ALA	0	-0.027	-0.026	43.290	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	125	ASN	0	-0.002	0.017	43.601	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:10:GLN)