FMO DATABASE

FMODB ID: YY812

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

Total energy (hartree)

FMO2-HF: Electronic energy	-810796.354314
FMO2-HF: Nuclear repulsion	767913.393111
FMO2-HF: Total energy	-42882.961204
FMO2-MP2: Total energy	-43007.82182

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.
-13.23	-11.974	6.247	-3.605	-3.897	0.026

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 : 0.031 / q_NPA : 0.008

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	0.021	0.010	1.903	-10.719	-9.764	6.246	-3.539	-3.661	0.026
4	A	5	LEU	0	0.053	0.028	4.297	-1.761	-1.460	0.001	-0.066	-0.236	0.000
5	A	6	LYS	1	0.946	0.972	6.159	-0.701	-0.701	0.000	0.000	0.000	0.000
6	A	7	GLN	0	-0.010	-0.017	7.389	0.280	0.280	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.016	-0.010	7.956	-0.150	-0.150	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.001	-0.003	10.202	-0.101	-0.101	0.000	0.000	0.000	0.000
9	A	10	MET	0	-0.042	-0.021	12.030	-0.060	-0.060	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.004	0.023	13.533	0.026	0.026	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.844	0.903	15.038	-0.302	-0.302	0.000	0.000	0.000	0.000
12	A	13	MET	0	0.006	0.004	18.900	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.012	0.003	15.012	-0.019	-0.019	0.000	0.000	0.000	0.000
14	A	15	GLY	0	-0.039	-0.011	16.949	-0.034	-0.034	0.000	0.000	0.000	0.000
15	A	16	PHE	0	0.012	0.005	19.521	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.806	0.908	20.996	0.038	0.038	0.000	0.000	0.000	0.000
17	A	18	HIS	0	0.014	-0.005	19.669	0.020	0.020	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.795	0.917	23.403	-0.036	-0.036	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.007	-0.001	25.648	0.000	0.000	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.030	-0.011	27.629	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	22	VAL	0	-0.014	0.000	31.383	0.005	0.005	0.000	0.000	0.000	0.000
22	A	23	VAL	0	-0.005	0.001	34.465	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	24	PRO	0	-0.006	-0.013	37.647	0.001	0.001	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.799	-0.880	40.617	0.049	0.049	0.000	0.000	0.000	0.000
25	A	26	TRP	0	-0.023	-0.021	37.459	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.897	-0.954	40.252	0.072	0.072	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.037	-0.003	38.828	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.018	0.007	35.322	0.007	0.007	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.909	0.940	29.703	-0.141	-0.141	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.043	0.027	31.478	0.004	0.004	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.044	-0.031	25.347	0.005	0.005	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.004	0.017	28.347	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.789	0.855	25.450	-0.065	-0.065	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.763	-0.867	23.537	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.004	-0.008	27.396	0.008	0.008	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.030	-0.026	27.576	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	38	GLY	0	-0.014	-0.004	27.934	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.881	-0.958	28.333	0.017	0.017	0.000	0.000	0.000	0.000
39	A	40	ALA	0	0.022	0.020	31.613	0.000	0.000	0.000	0.000	0.000	0.000
40	A	41	TRP	0	-0.014	-0.025	30.165	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.056	-0.021	33.496	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.845	0.907	35.314	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	44	TRP	0	-0.014	-0.002	36.900	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.022	-0.022	37.729	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.911	-0.934	39.809	0.009	0.009	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.007	0.007	41.732	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	VAL	0	-0.090	-0.044	41.996	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	56	ASN	0	-0.044	-0.040	57.283	0.000	0.000	0.000	0.000	0.000	0.000
49	A	57	VAL	0	0.011	0.026	52.391	0.001	0.001	0.000	0.000	0.000	0.000
50	A	58	SER	0	0.033	0.022	55.540	0.000	0.000	0.000	0.000	0.000	0.000
51	A	59	VAL	0	0.021	-0.011	55.138	0.000	0.000	0.000	0.000	0.000	0.000
52	A	60	SER	0	0.036	0.016	54.104	0.000	0.000	0.000	0.000	0.000	0.000
53	A	61	GLU	-1	-0.812	-0.899	52.754	0.002	0.002	0.000	0.000	0.000	0.000
54	A	62	LYS	1	0.918	0.953	48.282	0.002	0.002	0.000	0.000	0.000	0.000
55	A	63	ALA	0	-0.027	-0.015	49.392	0.000	0.000	0.000	0.000	0.000	0.000
56	A	64	HIS	0	0.052	0.028	49.001	0.001	0.001	0.000	0.000	0.000	0.000
57	A	65	ARG	1	0.913	0.948	47.604	0.003	0.003	0.000	0.000	0.000	0.000
58	A	66	ASN	0	-0.017	-0.012	45.121	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	67	LEU	0	0.024	0.024	44.157	0.001	0.001	0.000	0.000	0.000	0.000
60	A	68	CYS	0	-0.045	-0.021	43.970	0.003	0.003	0.000	0.000	0.000	0.000
61	A	69	ALA	0	0.044	0.024	41.386	0.002	0.002	0.000	0.000	0.000	0.000
62	A	70	ASP	-1	-0.809	-0.897	39.840	0.021	0.021	0.000	0.000	0.000	0.000
63	A	71	VAL	0	0.013	-0.012	39.262	0.003	0.003	0.000	0.000	0.000	0.000
64	A	72	VAL	0	0.007	0.017	37.337	0.004	0.004	0.000	0.000	0.000	0.000
65	A	73	LEU	0	-0.012	-0.001	34.065	0.003	0.003	0.000	0.000	0.000	0.000
66	A	74	PHE	0	-0.040	-0.024	34.497	0.006	0.006	0.000	0.000	0.000	0.000
67	A	75	ILE	0	0.012	0.011	35.129	0.006	0.006	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.736	-0.801	30.607	0.056	0.056	0.000	0.000	0.000	0.000
69	A	77	VAL	0	-0.039	-0.028	30.157	0.008	0.008	0.000	0.000	0.000	0.000
70	A	78	LEU	0	-0.007	0.007	30.149	0.008	0.008	0.000	0.000	0.000	0.000
71	A	79	CYS	0	-0.018	-0.007	27.958	0.004	0.004	0.000	0.000	0.000	0.000
72	A	80	ASP	-1	-0.750	-0.880	28.551	0.149	0.149	0.000	0.000	0.000	0.000
73	A	81	THR	0	-0.065	-0.066	27.612	0.000	0.000	0.000	0.000	0.000	0.000
74	A	82	ASP	-1	-0.928	-0.937	25.101	0.221	0.221	0.000	0.000	0.000	0.000
75	A	83	LYS	1	0.825	0.896	20.254	-0.200	-0.200	0.000	0.000	0.000	0.000
76	A	84	GLN	0	0.027	0.024	25.461	0.020	0.020	0.000	0.000	0.000	0.000
77	A	85	PRO	0	0.012	0.008	28.087	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	86	VAL	0	-0.031	-0.024	30.774	0.003	0.003	0.000	0.000	0.000	0.000
79	A	87	PHE	0	-0.028	-0.006	34.085	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	88	SER	0	-0.063	-0.054	34.591	0.001	0.001	0.000	0.000	0.000	0.000
81	A	89	VAL	0	0.013	-0.016	36.084	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	90	ASP	-1	-0.908	-0.965	37.680	0.050	0.050	0.000	0.000	0.000	0.000
83	A	91	GLU	-1	-0.825	-0.872	38.949	0.065	0.065	0.000	0.000	0.000	0.000
84	A	92	GLU	-1	-0.774	-0.867	41.151	0.026	0.026	0.000	0.000	0.000	0.000
85	A	93	GLU	-1	-0.827	-0.889	42.260	0.027	0.027	0.000	0.000	0.000	0.000
86	A	94	GLN	0	-0.010	-0.011	44.364	0.000	0.000	0.000	0.000	0.000	0.000
87	A	95	VAL	0	-0.017	-0.009	39.951	0.000	0.000	0.000	0.000	0.000	0.000
88	A	96	ARG	1	0.707	0.794	43.251	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	97	GLU	-1	-0.935	-0.957	45.735	0.035	0.035	0.000	0.000	0.000	0.000
90	A	98	ILE	0	-0.041	-0.011	43.768	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	99	TYR	0	-0.044	-0.038	40.496	0.002	0.002	0.000	0.000	0.000	0.000
92	A	100	GLY	0	0.036	0.007	44.416	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	101	PRO	0	-0.032	-0.026	44.015	0.001	0.001	0.000	0.000	0.000	0.000
94	A	102	VAL	0	0.032	0.030	40.368	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	103	HIS	0	0.073	0.049	39.684	0.000	0.000	0.000	0.000	0.000	0.000
96	A	104	SER	0	-0.024	-0.010	38.990	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	105	ARG	1	0.804	0.881	36.697	-0.050	-0.050	0.000	0.000	0.000	0.000
98	A	106	LEU	0	-0.009	-0.007	35.008	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	107	LEU	0	0.021	0.019	34.603	0.001	0.001	0.000	0.000	0.000	0.000
100	A	108	LYS	1	0.817	0.900	34.715	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	109	GLN	0	0.039	0.020	32.690	0.000	0.000	0.000	0.000	0.000	0.000
102	A	110	ALA	0	0.008	0.002	30.760	0.002	0.002	0.000	0.000	0.000	0.000
103	A	111	LEU	0	-0.009	-0.012	30.256	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	112	ASP	-1	-0.841	-0.921	30.773	0.017	0.017	0.000	0.000	0.000	0.000
105	A	113	LEU	0	-0.125	-0.052	25.342	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	114	ILE	0	0.008	0.008	26.340	-0.006	-0.006	0.000	0.000	0.000	0.000
107	A	115	ASN	0	-0.036	-0.008	27.837	-0.008	-0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)