FMO DATABASE

FMODB ID: 63JMZ

Calculation Name: 2OB9-A-Xray316

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OB9

Chain ID: A

ChEMBL ID:

UniProt ID: Q9MCS5

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-816925.749306
FMO2-HF: Nuclear repulsion	773702.476124
FMO2-HF: Total energy	-43223.273182
FMO2-MP2: Total energy	-43349.222412

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:ACE )

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

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.
1.396	2.406	-0.006	-0.506	-0.498	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.005

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].
3	A	3	GLN	0	0.039	0.013	3.855	0.816	1.826	-0.006	-0.506	-0.498
4	A	4	THR	0	0.021	0.018	7.056	0.221	0.221	0.000	0.000	0.000
5	A	5	LEU	0	0.054	0.031	8.692	0.142	0.142	0.000	0.000	0.000
6	A	6	LYS	1	0.979	0.985	9.081	0.051	0.051	0.000	0.000	0.000
7	A	7	GLN	0	0.002	-0.004	10.761	0.000	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.021	-0.016	12.684	0.044	0.044	0.000	0.000	0.000
9	A	9	ALA	0	-0.009	-0.001	13.678	0.037	0.037	0.000	0.000	0.000
10	A	10	MET	0	-0.030	-0.016	14.292	0.041	0.041	0.000	0.000	0.000
11	A	11	ALA	0	0.009	0.027	16.581	0.008	0.008	0.000	0.000	0.000
12	A	12	LYS	1	0.942	0.959	18.572	0.094	0.094	0.000	0.000	0.000
13	A	13	MET	0	-0.027	-0.021	22.267	-0.006	-0.006	0.000	0.000	0.000
14	A	14	ALA	0	-0.005	0.014	18.981	-0.001	-0.001	0.000	0.000	0.000
15	A	15	GLY	0	-0.065	-0.022	20.959	0.001	0.001	0.000	0.000	0.000
16	A	16	PHE	0	-0.003	0.007	23.261	0.006	0.006	0.000	0.000	0.000
17	A	17	ARG	1	0.913	0.956	25.640	0.052	0.052	0.000	0.000	0.000
18	A	18	HIS	0	-0.026	-0.043	24.331	0.004	0.004	0.000	0.000	0.000
19	A	19	LYS	1	0.874	0.954	28.981	0.048	0.048	0.000	0.000	0.000
20	A	20	THR	0	-0.004	0.000	31.000	0.004	0.004	0.000	0.000	0.000
21	A	21	VAL	0	-0.029	-0.009	33.333	-0.001	-0.001	0.000	0.000	0.000
22	A	22	VAL	0	0.007	0.005	37.044	0.000	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.016	-0.018	39.962	0.001	0.001	0.000	0.000	0.000
24	A	24	PRO	0	-0.012	-0.003	42.938	0.001	0.001	0.000	0.000	0.000
25	A	25	GLU	-1	-0.836	-0.914	46.209	-0.031	-0.031	0.000	0.000	0.000
26	A	26	TRP	0	-0.051	-0.032	41.718	0.001	0.001	0.000	0.000	0.000
27	A	27	GLU	-1	-0.895	-0.956	45.016	-0.030	-0.030	0.000	0.000	0.000
28	A	28	GLY	0	-0.037	-0.002	44.140	-0.001	-0.001	0.000	0.000	0.000
29	A	29	VAL	0	-0.009	0.017	39.880	-0.004	-0.004	0.000	0.000	0.000
30	A	30	LYS	1	0.939	0.949	34.917	0.061	0.061	0.000	0.000	0.000
31	A	31	VAL	0	0.037	0.027	36.301	0.001	0.001	0.000	0.000	0.000
32	A	32	VAL	0	-0.053	-0.043	30.096	-0.005	-0.005	0.000	0.000	0.000
33	A	33	LEU	0	-0.033	0.002	33.426	0.004	0.004	0.000	0.000	0.000
34	A	34	ARG	1	0.791	0.880	29.720	0.031	0.031	0.000	0.000	0.000
35	A	35	GLU	-1	-0.828	-0.915	27.815	-0.049	-0.049	0.000	0.000	0.000
36	A	36	PRO	0	0.032	0.006	31.509	-0.001	-0.001	0.000	0.000	0.000
37	A	37	SER	0	0.017	0.027	30.367	-0.001	-0.001	0.000	0.000	0.000
38	A	38	GLY	0	0.025	-0.012	30.473	0.001	0.001	0.000	0.000	0.000
39	A	39	GLU	-1	-0.928	-0.971	30.981	-0.008	-0.008	0.000	0.000	0.000
40	A	40	ALA	0	0.002	0.014	34.092	0.001	0.001	0.000	0.000	0.000
41	A	41	TRP	0	-0.013	-0.035	33.355	0.002	0.002	0.000	0.000	0.000
42	A	42	LEU	0	-0.059	-0.010	35.978	0.001	0.001	0.000	0.000	0.000
43	A	43	ARG	1	1.015	1.010	37.681	0.010	0.010	0.000	0.000	0.000
44	A	44	TRP	0	-0.006	0.012	39.933	0.000	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.054	-0.044	40.855	0.001	0.001	0.000	0.000	0.000
46	A	46	GLU	-1	-0.943	-0.953	42.412	-0.003	-0.003	0.000	0.000	0.000
47	A	47	VAL	0	-0.078	-0.042	44.146	0.001	0.001	0.000	0.000	0.000
48	A	48	VAL	0	-0.092	-0.040	44.756	0.001	0.001	0.000	0.000	0.000
49	A	49	NME	0	-0.013	0.004	46.332	0.001	0.001	0.000	0.000	0.000
50	A	55	ACE	0	0.054	0.023	59.609	0.000	0.000	0.000	0.000	0.000
51	A	56	ASN	0	-0.082	-0.051	59.821	0.000	0.000	0.000	0.000	0.000
52	A	57	VAL	0	0.032	0.033	56.030	0.000	0.000	0.000	0.000	0.000
53	A	58	SER	0	0.082	0.044	58.977	0.000	0.000	0.000	0.000	0.000
54	A	59	VAL	0	0.021	-0.018	58.697	0.000	0.000	0.000	0.000	0.000
55	A	60	SER	0	0.011	-0.002	57.914	-0.001	-0.001	0.000	0.000	0.000
56	A	61	GLU	-1	-0.894	-0.932	56.176	-0.006	-0.006	0.000	0.000	0.000
57	A	62	LYS	1	0.940	0.962	52.450	0.012	0.012	0.000	0.000	0.000
58	A	63	ALA	0	-0.027	-0.016	53.037	-0.001	-0.001	0.000	0.000	0.000
59	A	64	HIS	0	0.053	0.034	52.941	-0.001	-0.001	0.000	0.000	0.000
60	A	65	ARG	1	1.016	1.011	50.298	0.008	0.008	0.000	0.000	0.000
61	A	66	ASN	0	-0.050	-0.047	48.500	-0.001	-0.001	0.000	0.000	0.000
62	A	67	LEU	0	0.042	0.047	47.777	-0.001	-0.001	0.000	0.000	0.000
63	A	68	CYS	0	-0.048	-0.027	47.810	-0.001	-0.001	0.000	0.000	0.000
64	A	69	ALA	0	0.029	0.018	44.745	0.000	0.000	0.000	0.000	0.000
65	A	70	ASP	-1	-0.925	-0.971	43.477	-0.020	-0.020	0.000	0.000	0.000
66	A	71	VAL	0	-0.044	-0.037	43.204	-0.002	-0.002	0.000	0.000	0.000
67	A	72	VAL	0	0.033	0.030	40.537	-0.001	-0.001	0.000	0.000	0.000
68	A	73	LEU	0	0.002	0.000	37.538	-0.001	-0.001	0.000	0.000	0.000
69	A	74	PHE	0	-0.061	-0.037	38.421	-0.003	-0.003	0.000	0.000	0.000
70	A	75	ILE	0	0.000	0.004	38.957	-0.002	-0.002	0.000	0.000	0.000
71	A	76	ASP	-1	-0.757	-0.852	34.238	-0.029	-0.029	0.000	0.000	0.000
72	A	77	VAL	0	-0.071	-0.038	34.426	-0.003	-0.003	0.000	0.000	0.000
73	A	78	LEU	0	-0.024	0.001	34.720	-0.005	-0.005	0.000	0.000	0.000
74	A	79	CYS	0	-0.010	-0.010	32.363	0.001	0.001	0.000	0.000	0.000
75	A	80	ASP	-1	-0.727	-0.873	32.895	-0.049	-0.049	0.000	0.000	0.000
76	A	81	THR	0	-0.018	-0.036	32.311	-0.003	-0.003	0.000	0.000	0.000
77	A	82	ASP	-1	-1.000	-0.980	29.510	-0.070	-0.070	0.000	0.000	0.000
78	A	83	LYS	1	0.806	0.891	25.669	0.087	0.087	0.000	0.000	0.000
79	A	84	GLN	0	0.004	0.010	29.215	-0.002	-0.002	0.000	0.000	0.000
80	A	85	PRO	0	0.028	0.025	31.713	-0.001	-0.001	0.000	0.000	0.000
81	A	86	VAL	0	-0.014	-0.007	34.544	0.000	0.000	0.000	0.000	0.000
82	A	87	PHE	0	-0.005	0.004	38.007	0.001	0.001	0.000	0.000	0.000
83	A	88	SER	0	-0.035	-0.016	38.061	0.000	0.000	0.000	0.000	0.000
84	A	89	VAL	0	0.001	-0.025	37.628	0.000	0.000	0.000	0.000	0.000
85	A	90	ASP	-1	-0.919	-0.961	40.193	-0.008	-0.008	0.000	0.000	0.000
86	A	91	GLU	-1	-0.867	-0.920	41.920	-0.018	-0.018	0.000	0.000	0.000
87	A	92	GLU	-1	-0.818	-0.919	44.131	-0.013	-0.013	0.000	0.000	0.000
88	A	93	GLU	-1	-0.954	-0.989	45.354	-0.011	-0.011	0.000	0.000	0.000
89	A	94	GLN	0	0.021	0.011	47.299	0.000	0.000	0.000	0.000	0.000
90	A	95	VAL	0	-0.003	0.001	43.910	-0.001	-0.001	0.000	0.000	0.000
91	A	96	ARG	1	0.838	0.866	47.376	0.011	0.011	0.000	0.000	0.000
92	A	97	GLU	-1	-0.996	-0.979	49.665	-0.013	-0.013	0.000	0.000	0.000
93	A	98	ILE	0	-0.041	-0.003	47.419	0.000	0.000	0.000	0.000	0.000
94	A	99	TYR	0	-0.035	-0.006	44.397	-0.001	-0.001	0.000	0.000	0.000
95	A	100	GLY	0	0.059	0.018	49.091	0.001	0.001	0.000	0.000	0.000
96	A	101	PRO	0	-0.029	-0.033	48.734	-0.001	-0.001	0.000	0.000	0.000
97	A	102	VAL	0	0.013	0.017	45.246	-0.001	-0.001	0.000	0.000	0.000
98	A	103	HIS	0	0.097	0.050	44.281	-0.002	-0.002	0.000	0.000	0.000
99	A	104	SER	0	-0.017	0.009	43.730	-0.001	-0.001	0.000	0.000	0.000
100	A	105	ARG	1	0.834	0.908	42.486	0.034	0.034	0.000	0.000	0.000
101	A	106	LEU	0	-0.019	-0.009	39.926	-0.002	-0.002	0.000	0.000	0.000
102	A	107	LEU	0	0.033	0.020	39.441	-0.002	-0.002	0.000	0.000	0.000
103	A	108	LYS	1	0.947	0.966	39.496	0.024	0.024	0.000	0.000	0.000
104	A	109	GLN	0	0.070	0.035	38.174	0.000	0.000	0.000	0.000	0.000
105	A	110	ALA	0	-0.015	-0.009	35.541	-0.003	-0.003	0.000	0.000	0.000
106	A	111	LEU	0	-0.014	-0.018	34.912	-0.002	-0.002	0.000	0.000	0.000
107	A	112	ASP	-1	-0.884	-0.944	36.330	-0.039	-0.039	0.000	0.000	0.000
108	A	113	LEU	0	-0.152	-0.058	30.812	-0.003	-0.003	0.000	0.000	0.000
109	A	114	ILE	0	0.002	0.015	31.451	-0.004	-0.004	0.000	0.000	0.000
110	A	115	ASN	0	0.002	0.005	32.793	0.002	0.002	0.000	0.000	0.000
111	A	116	NME	0	-0.051	-0.016	33.119	-0.004	-0.004	0.000	0.000	0.000

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