FMO DATABASE

FMODB ID: 5365Z

Calculation Name: 2OB9-A-Xray372

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: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	107
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-809076.693752
FMO2-HF: Nuclear repulsion	766194.294807
FMO2-HF: Total energy	-42882.398944
FMO2-MP2: Total energy	-43007.243078

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-13.119	-8.866	2.679	-3.136	-3.796	0.022

Interaction energy analysis for fragmet #1(A:2:SER)

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 : -0.009

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	4	THR	0	0.012	0.008	2.144	-10.743	-6.728	2.679	-3.095	-3.599	0.022
4	A	5	LEU	0	0.060	0.035	4.478	-1.657	-1.419	0.000	-0.041	-0.197	0.000
5	A	6	LYS	1	0.968	0.983	6.146	-0.610	-0.610	0.000	0.000	0.000	0.000
6	A	7	GLN	0	0.003	-0.005	7.441	0.203	0.203	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.017	-0.013	8.486	-0.155	-0.155	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.006	-0.001	10.430	-0.122	-0.122	0.000	0.000	0.000	0.000
9	A	10	MET	0	-0.034	-0.019	12.138	-0.077	-0.077	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.002	0.025	13.606	0.011	0.011	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.880	0.917	15.115	-0.301	-0.301	0.000	0.000	0.000	0.000
12	A	13	MET	0	-0.024	-0.017	18.732	0.005	0.005	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.007	0.010	15.487	-0.014	-0.014	0.000	0.000	0.000	0.000
14	A	15	GLY	0	-0.066	-0.021	17.255	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	16	PHE	0	0.003	0.003	20.079	-0.020	-0.020	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.881	0.939	21.474	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	18	HIS	0	0.014	-0.011	19.811	0.012	0.012	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.821	0.925	24.041	-0.064	-0.064	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.001	0.000	26.148	0.002	0.002	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.013	0.001	28.135	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	22	VAL	0	-0.005	0.000	31.820	0.005	0.005	0.000	0.000	0.000	0.000
22	A	23	VAL	0	-0.023	-0.017	34.702	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	24	PRO	0	-0.020	-0.009	37.817	0.000	0.000	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.791	-0.890	40.968	0.054	0.054	0.000	0.000	0.000	0.000
25	A	26	TRP	0	-0.045	-0.027	37.465	0.000	0.000	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.892	-0.957	40.208	0.071	0.071	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.038	0.000	38.934	0.002	0.002	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.011	0.009	35.212	0.007	0.007	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.933	0.953	29.800	-0.135	-0.135	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.036	0.025	31.680	0.003	0.003	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.046	-0.037	25.499	0.005	0.005	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.021	0.005	28.678	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.781	0.856	25.830	-0.088	-0.088	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.809	-0.910	24.018	0.056	0.056	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.008	-0.003	27.911	0.008	0.008	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.028	0.007	27.448	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.011	-0.016	27.796	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.887	-0.958	28.165	0.049	0.049	0.000	0.000	0.000	0.000
39	A	40	ALA	0	-0.008	0.010	31.547	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	41	TRP	0	-0.021	-0.035	30.317	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.054	-0.009	33.423	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.895	0.939	35.177	-0.039	-0.039	0.000	0.000	0.000	0.000
43	A	44	TRP	0	0.002	0.012	37.136	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.050	-0.040	37.858	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.925	-0.951	39.997	0.023	0.023	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.059	-0.025	41.634	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	48	VAL	0	-0.026	-0.001	42.545	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	56	ASN	0	-0.021	-0.032	57.152	0.000	0.000	0.000	0.000	0.000	0.000
49	A	57	VAL	0	-0.026	0.015	52.902	0.001	0.001	0.000	0.000	0.000	0.000
50	A	58	SER	0	0.052	0.029	56.077	0.000	0.000	0.000	0.000	0.000	0.000
51	A	59	VAL	0	0.005	-0.028	55.588	0.001	0.001	0.000	0.000	0.000	0.000
52	A	60	SER	0	0.037	0.011	54.618	0.000	0.000	0.000	0.000	0.000	0.000
53	A	61	GLU	-1	-0.836	-0.908	53.428	0.013	0.013	0.000	0.000	0.000	0.000
54	A	62	LYS	1	0.945	0.967	49.296	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	63	ALA	0	-0.021	-0.013	49.827	0.001	0.001	0.000	0.000	0.000	0.000
56	A	64	HIS	0	0.052	0.035	49.534	0.002	0.002	0.000	0.000	0.000	0.000
57	A	65	ARG	1	0.951	0.972	47.518	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	66	ASN	0	-0.063	-0.048	45.286	0.001	0.001	0.000	0.000	0.000	0.000
59	A	67	LEU	0	0.028	0.035	44.405	0.002	0.002	0.000	0.000	0.000	0.000
60	A	68	CYS	0	-0.036	-0.024	44.399	0.003	0.003	0.000	0.000	0.000	0.000
61	A	69	ALA	0	0.038	0.022	41.725	0.002	0.002	0.000	0.000	0.000	0.000
62	A	70	ASP	-1	-0.864	-0.935	40.292	0.035	0.035	0.000	0.000	0.000	0.000
63	A	71	VAL	0	-0.027	-0.033	39.658	0.004	0.004	0.000	0.000	0.000	0.000
64	A	72	VAL	0	0.015	0.026	37.589	0.004	0.004	0.000	0.000	0.000	0.000
65	A	73	LEU	0	0.011	0.007	34.332	0.004	0.004	0.000	0.000	0.000	0.000
66	A	74	PHE	0	-0.047	-0.031	34.878	0.006	0.006	0.000	0.000	0.000	0.000
67	A	75	ILE	0	0.000	0.005	35.351	0.006	0.006	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.739	-0.827	30.962	0.080	0.080	0.000	0.000	0.000	0.000
69	A	77	VAL	0	-0.052	-0.028	30.696	0.008	0.008	0.000	0.000	0.000	0.000
70	A	78	LEU	0	-0.023	-0.001	30.629	0.008	0.008	0.000	0.000	0.000	0.000
71	A	79	CYS	0	-0.026	-0.012	28.394	0.004	0.004	0.000	0.000	0.000	0.000
72	A	80	ASP	-1	-0.735	-0.882	29.092	0.147	0.147	0.000	0.000	0.000	0.000
73	A	81	THR	0	-0.028	-0.040	27.819	0.004	0.004	0.000	0.000	0.000	0.000
74	A	82	ASP	-1	-0.977	-0.965	25.558	0.216	0.216	0.000	0.000	0.000	0.000
75	A	83	LYS	1	0.810	0.881	20.572	-0.216	-0.216	0.000	0.000	0.000	0.000
76	A	84	GLN	0	0.036	0.029	25.665	0.020	0.020	0.000	0.000	0.000	0.000
77	A	85	PRO	0	0.013	0.021	28.350	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	86	VAL	0	-0.012	-0.006	31.236	0.002	0.002	0.000	0.000	0.000	0.000
79	A	87	PHE	0	-0.030	-0.004	34.506	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	88	SER	0	-0.043	-0.043	35.044	0.003	0.003	0.000	0.000	0.000	0.000
81	A	89	VAL	0	0.010	-0.025	36.012	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	90	ASP	-1	-0.918	-0.962	37.657	0.059	0.059	0.000	0.000	0.000	0.000
83	A	91	GLU	-1	-0.860	-0.890	39.114	0.071	0.071	0.000	0.000	0.000	0.000
84	A	92	GLU	-1	-0.757	-0.863	41.218	0.038	0.038	0.000	0.000	0.000	0.000
85	A	93	GLU	-1	-0.832	-0.914	42.382	0.037	0.037	0.000	0.000	0.000	0.000
86	A	94	GLN	0	0.010	0.006	44.373	0.000	0.000	0.000	0.000	0.000	0.000
87	A	95	VAL	0	-0.007	0.002	40.501	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	96	ARG	1	0.737	0.812	43.893	-0.038	-0.038	0.000	0.000	0.000	0.000
89	A	97	GLU	-1	-0.980	-0.979	46.191	0.039	0.039	0.000	0.000	0.000	0.000
90	A	98	ILE	0	-0.044	-0.014	43.847	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	99	TYR	0	-0.083	-0.039	40.677	0.002	0.002	0.000	0.000	0.000	0.000
92	A	100	GLY	0	0.053	0.013	44.868	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	101	PRO	0	-0.024	-0.033	44.400	0.001	0.001	0.000	0.000	0.000	0.000
94	A	102	VAL	0	0.014	0.019	40.489	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	103	HIS	0	0.088	0.049	39.906	0.001	0.001	0.000	0.000	0.000	0.000
96	A	104	SER	0	-0.016	0.011	39.422	0.000	0.000	0.000	0.000	0.000	0.000
97	A	105	ARG	1	0.809	0.890	37.412	-0.056	-0.056	0.000	0.000	0.000	0.000
98	A	106	LEU	0	-0.022	-0.013	35.267	0.001	0.001	0.000	0.000	0.000	0.000
99	A	107	LEU	0	0.025	0.021	35.170	0.003	0.003	0.000	0.000	0.000	0.000
100	A	108	LYS	1	0.931	0.957	35.287	-0.030	-0.030	0.000	0.000	0.000	0.000
101	A	109	GLN	0	0.072	0.047	32.863	0.000	0.000	0.000	0.000	0.000	0.000
102	A	110	ALA	0	-0.002	0.003	31.089	0.002	0.002	0.000	0.000	0.000	0.000
103	A	111	LEU	0	-0.006	-0.013	30.679	0.000	0.000	0.000	0.000	0.000	0.000
104	A	112	ASP	-1	-0.879	-0.941	32.052	0.035	0.035	0.000	0.000	0.000	0.000
105	A	113	LEU	0	-0.139	-0.051	26.029	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	114	ILE	0	0.032	0.032	27.216	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	115	ASN	0	-0.044	-0.013	28.906	-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:2:SER)