FMO DATABASE

FMODB ID: K35V3

Calculation Name: 2OEB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OEB

Chain ID: A

ChEMBL ID:

UniProt ID: O28417

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:

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	152
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1495028.519299
FMO2-HF: Nuclear repulsion	1436155.68543
FMO2-HF: Total energy	-58872.833869
FMO2-MP2: Total energy	-59047.791772

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:ASP)

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

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.
-2.327	-4.077	15.755	-7.543	-6.465	-0.042

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.937 / q_NPA : -0.987

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	ARG	1	0.936	0.972	2.934	-44.209	-41.105	0.118	-1.549	-1.674	0.009
4	A	5	GLU	-1	-0.830	-0.915	1.806	33.565	28.150	15.638	-5.828	-4.396	-0.051
5	A	6	ILE	0	0.047	0.031	4.048	-6.001	-5.440	-0.001	-0.166	-0.395	0.000
6	A	7	GLU	-1	-0.824	-0.897	5.991	23.203	23.203	0.000	0.000	0.000	0.000
7	A	8	GLN	0	-0.062	-0.024	7.395	-3.589	-3.589	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.805	-0.898	8.115	22.491	22.491	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.763	0.841	8.069	-37.303	-37.303	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.030	-0.012	11.910	-2.296	-2.296	0.000	0.000	0.000	0.000
11	A	12	SER	0	0.018	0.013	13.064	-2.119	-2.119	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.002	0.002	14.127	-1.485	-1.485	0.000	0.000	0.000	0.000
13	A	14	ALA	0	0.011	-0.004	15.847	-1.268	-1.268	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.009	-0.002	17.588	-1.146	-1.146	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.895	0.967	16.888	-18.265	-18.265	0.000	0.000	0.000	0.000
16	A	17	VAL	0	0.000	-0.008	19.952	-0.786	-0.786	0.000	0.000	0.000	0.000
17	A	18	VAL	0	-0.013	-0.014	21.802	-0.720	-0.720	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.025	-0.030	22.884	-0.777	-0.777	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.881	-0.925	24.696	11.158	11.158	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.031	-0.009	26.311	-0.540	-0.540	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.848	0.908	27.883	-10.708	-10.708	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.932	-0.970	29.176	9.623	9.623	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.833	0.910	29.422	-10.973	-10.973	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.058	-0.070	31.680	-0.508	-0.508	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.012	0.040	33.894	-0.228	-0.228	0.000	0.000	0.000	0.000
26	A	27	GLN	0	-0.030	-0.025	34.739	-0.240	-0.240	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.030	-0.029	36.727	-0.313	-0.313	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.915	0.929	35.555	-8.301	-8.301	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.938	0.985	35.293	-7.648	-7.648	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.020	0.024	32.072	0.117	0.117	0.000	0.000	0.000	0.000
31	A	32	GLN	0	0.003	-0.004	30.874	0.514	0.514	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.049	0.031	30.575	0.336	0.336	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.829	0.905	31.523	-8.880	-8.880	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.016	-0.007	23.582	0.317	0.317	0.000	0.000	0.000	0.000
35	A	36	SER	0	0.013	-0.001	26.959	0.627	0.627	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.023	-0.042	27.002	0.330	0.330	0.000	0.000	0.000	0.000
37	A	38	TYR	0	-0.101	-0.062	27.656	0.036	0.036	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.068	0.036	22.857	0.326	0.326	0.000	0.000	0.000	0.000
39	A	40	GLH	0	-0.112	-0.098	23.087	0.540	0.540	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.887	0.940	24.960	-10.223	-10.223	0.000	0.000	0.000	0.000
41	A	42	ALA	0	0.052	0.032	23.298	-0.072	-0.072	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.018	0.001	20.215	0.059	0.059	0.000	0.000	0.000	0.000
43	A	44	THR	0	0.018	0.012	21.868	0.283	0.283	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.016	0.023	25.012	-0.213	-0.213	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.002	0.003	19.401	-0.084	-0.084	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.029	-0.018	19.589	0.052	0.052	0.000	0.000	0.000	0.000
47	A	48	ASN	0	-0.066	-0.030	22.998	-0.479	-0.479	0.000	0.000	0.000	0.000
48	A	49	ASN	0	-0.075	-0.037	25.944	-0.535	-0.535	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.066	0.048	22.936	-0.139	-0.139	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.010	0.005	17.782	-0.472	-0.472	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.059	0.026	21.783	-0.285	-0.285	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.035	0.018	24.370	-0.422	-0.422	0.000	0.000	0.000	0.000
53	A	54	THR	0	-0.012	-0.016	23.753	-0.420	-0.420	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.015	-0.002	21.298	-0.335	-0.335	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.044	0.014	25.556	-0.376	-0.376	0.000	0.000	0.000	0.000
56	A	57	PHE	0	-0.012	-0.002	28.668	-0.474	-0.474	0.000	0.000	0.000	0.000
57	A	58	PHE	0	-0.003	-0.004	23.723	-0.351	-0.351	0.000	0.000	0.000	0.000
58	A	59	LEU	0	0.065	0.041	28.634	-0.388	-0.388	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.100	-0.056	31.360	-0.488	-0.488	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.841	0.902	32.864	-9.548	-9.548	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.069	-0.005	31.438	-0.194	-0.194	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.877	-0.932	35.746	7.712	7.712	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.762	0.876	35.532	-8.774	-8.774	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.013	-0.009	39.882	-0.198	-0.198	0.000	0.000	0.000	0.000
65	A	66	ILE	0	-0.014	-0.024	33.757	0.049	0.049	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.927	-0.950	35.671	8.606	8.606	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.812	-0.890	30.826	10.542	10.542	0.000	0.000	0.000	0.000
68	A	69	VAL	0	-0.047	-0.038	29.939	0.015	0.015	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.812	-0.877	25.630	13.216	13.216	0.000	0.000	0.000	0.000
70	A	71	TYR	0	-0.063	-0.082	20.839	-0.277	-0.277	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.800	0.904	23.039	-13.472	-13.472	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.012	-0.035	26.009	-0.153	-0.153	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.027	0.013	28.140	-0.366	-0.366	0.000	0.000	0.000	0.000
74	A	75	ASN	0	0.079	0.035	29.481	0.477	0.477	0.000	0.000	0.000	0.000
75	A	76	PRO	0	-0.015	-0.010	28.610	-0.319	-0.319	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.788	-0.863	31.782	9.800	9.800	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.052	-0.024	34.384	-0.310	-0.310	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.023	0.019	33.091	-0.201	-0.201	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.045	0.018	37.688	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	81	ASN	0	-0.018	-0.019	38.160	0.020	0.020	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.044	0.006	36.379	0.199	0.199	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.759	-0.842	34.500	9.351	9.351	0.000	0.000	0.000	0.000
83	A	84	ASN	0	0.024	0.004	33.358	0.244	0.244	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.024	0.035	32.690	0.321	0.321	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.011	0.009	30.257	0.382	0.382	0.000	0.000	0.000	0.000
86	A	87	TYR	0	-0.011	-0.018	28.728	0.333	0.333	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.028	0.028	28.268	0.436	0.436	0.000	0.000	0.000	0.000
88	A	89	PHE	0	0.008	-0.005	27.047	0.331	0.331	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.031	-0.005	23.001	0.566	0.566	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.025	-0.023	23.379	0.724	0.724	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.830	0.910	23.344	-11.375	-11.375	0.000	0.000	0.000	0.000
92	A	93	HIS	0	0.017	0.029	21.384	0.776	0.776	0.000	0.000	0.000	0.000
93	A	94	LEU	0	0.007	0.009	17.752	0.900	0.900	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.030	-0.006	18.300	1.204	1.204	0.000	0.000	0.000	0.000
95	A	96	THR	0	-0.005	-0.023	18.631	0.263	0.263	0.000	0.000	0.000	0.000
96	A	97	TRP	0	-0.040	-0.031	10.275	-0.065	-0.065	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.020	-0.011	14.210	1.432	1.432	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.019	0.033	15.099	0.823	0.823	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.904	-0.940	15.701	15.510	15.510	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.029	0.008	12.547	0.592	0.592	0.000	0.000	0.000	0.000
101	A	102	ASN	0	-0.031	-0.052	12.368	-3.025	-3.025	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.016	0.010	13.888	-1.775	-1.775	0.000	0.000	0.000	0.000
103	A	104	LYS	1	0.915	0.948	13.838	-16.935	-16.935	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.935	-0.949	14.821	17.775	17.775	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.055	-0.020	11.514	0.554	0.554	0.000	0.000	0.000	0.000
106	A	107	ALA	0	-0.004	-0.015	5.835	0.628	0.628	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.005	-0.001	6.781	4.755	4.755	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.006	0.007	8.794	-2.505	-2.505	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.009	0.011	11.114	-2.081	-2.081	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.039	-0.025	9.579	1.734	1.734	0.000	0.000	0.000	0.000
111	A	112	THR	0	-0.051	-0.055	12.830	-0.495	-0.495	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.012	-0.017	15.361	-0.902	-0.902	0.000	0.000	0.000	0.000
113	A	114	GLY	0	0.025	0.024	16.786	-0.875	-0.875	0.000	0.000	0.000	0.000
114	A	115	GLH	0	-0.057	-0.060	19.786	-0.698	-0.698	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.753	-0.874	20.578	13.880	13.880	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.014	0.000	18.902	-0.164	-0.164	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.003	0.017	20.967	0.112	0.112	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.878	0.923	24.320	-12.412	-12.412	0.000	0.000	0.000	0.000
119	A	120	TYR	0	-0.021	-0.008	15.765	-0.313	-0.313	0.000	0.000	0.000	0.000
120	A	121	ILE	0	0.014	-0.018	20.093	0.166	0.166	0.000	0.000	0.000	0.000
121	A	122	MET	0	-0.075	-0.028	22.101	-0.262	-0.262	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.779	-0.829	23.279	12.818	12.818	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.788	0.916	18.908	-15.386	-15.386	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.021	-0.033	18.675	-0.509	-0.509	0.000	0.000	0.000	0.000
125	A	126	ALA	0	0.034	-0.005	19.637	0.512	0.512	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.024	0.016	14.790	0.365	0.365	0.000	0.000	0.000	0.000
127	A	128	ASP	-1	-0.767	-0.855	15.033	20.322	20.322	0.000	0.000	0.000	0.000
128	A	129	VAL	0	0.001	0.016	15.508	0.956	0.956	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.005	0.011	16.009	0.123	0.123	0.000	0.000	0.000	0.000
130	A	131	ILE	0	0.059	0.028	10.083	0.348	0.348	0.000	0.000	0.000	0.000
131	A	132	SER	0	-0.025	-0.039	12.278	1.129	1.129	0.000	0.000	0.000	0.000
132	A	133	THR	0	-0.063	-0.045	14.564	-0.786	-0.786	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.936	-0.963	9.206	30.729	30.729	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.737	-0.808	9.082	33.581	33.581	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.007	-0.004	11.985	-0.863	-0.863	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.020	-0.016	15.222	-1.058	-1.058	0.000	0.000	0.000	0.000
137	A	138	SER	0	-0.034	-0.020	11.295	-0.285	-0.285	0.000	0.000	0.000	0.000
138	A	139	ILE	0	-0.015	0.001	13.271	-0.839	-0.839	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.020	0.010	14.894	-1.329	-1.329	0.000	0.000	0.000	0.000
140	A	141	ASN	0	-0.012	-0.011	15.565	-2.002	-2.002	0.000	0.000	0.000	0.000
141	A	142	TRP	0	-0.026	-0.041	11.868	-2.382	-2.382	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.033	0.017	16.848	-0.868	-0.868	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.851	0.936	20.015	-14.786	-14.786	0.000	0.000	0.000	0.000
144	A	145	LYS	1	0.821	0.925	14.545	-21.391	-21.391	0.000	0.000	0.000	0.000
145	A	146	PHE	0	0.033	0.013	16.345	-0.608	-0.608	0.000	0.000	0.000	0.000
146	A	147	ALA	0	0.029	0.013	21.615	-0.647	-0.647	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.941	0.968	22.704	-13.931	-13.931	0.000	0.000	0.000	0.000
148	A	149	ALA	0	-0.037	-0.003	23.288	-0.347	-0.347	0.000	0.000	0.000	0.000
149	A	150	MET	0	-0.041	0.000	23.506	-0.048	-0.048	0.000	0.000	0.000	0.000
150	A	151	LEU	0	-0.043	-0.012	26.768	-0.464	-0.464	0.000	0.000	0.000	0.000
151	A	152	GLU	-1	-0.827	-0.896	29.347	8.867	8.867	0.000	0.000	0.000	0.000
152	A	153	GLU	-1	-0.821	-0.850	30.714	10.215	10.215	0.000	0.000	0.000	0.000

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