FMO DATABASE

FMODB ID: 4KN3N

Calculation Name: 2OBB-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2OBB

Chain ID: A

ChEMBL ID:

UniProt ID: Q8A9J5

Base Structure: X-ray

Registration Date: 2025-10-12

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1106973.680998
FMO2-HF: Nuclear repulsion	1056263.850207
FMO2-HF: Total energy	-50709.830791
FMO2-MP2: Total energy	-50859.128366

3D Structure Molmil

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:ASN)

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

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.
-181.152	-178.888	10.938	-6.454	-6.747	-0.029

Interaction energy analysis for fragmet #1(A:-1:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.792 / q_NPA : 0.886

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	1	MET	0	-0.034	-0.023	2.080	-38.828	-35.776	5.670	-4.422	-4.300	-0.056
4	A	2	THR	0	0.005	-0.003	4.407	8.345	8.450	-0.001	-0.029	-0.075	0.000
115	A	113	LYS	1	0.821	0.912	1.942	29.264	28.371	5.269	-2.003	-2.372	0.027
5	A	3	ILE	0	-0.010	-0.008	7.854	0.061	0.061	0.000	0.000	0.000	0.000
6	A	4	ALA	0	-0.004	0.009	10.067	1.657	1.657	0.000	0.000	0.000	0.000
7	A	5	VAL	0	-0.027	-0.024	13.658	-0.324	-0.324	0.000	0.000	0.000	0.000
8	A	6	ASP	-1	-0.734	-0.845	16.155	-13.252	-13.252	0.000	0.000	0.000	0.000
9	A	7	PHE	0	-0.044	-0.039	19.856	-0.173	-0.173	0.000	0.000	0.000	0.000
10	A	8	ASP	-1	-0.775	-0.872	22.861	-11.176	-11.176	0.000	0.000	0.000	0.000
11	A	9	GLY	0	0.023	0.010	25.460	0.137	0.137	0.000	0.000	0.000	0.000
12	A	10	THR	0	-0.055	-0.025	18.772	-0.248	-0.248	0.000	0.000	0.000	0.000
13	A	11	ILE	0	-0.014	-0.016	18.833	-0.352	-0.352	0.000	0.000	0.000	0.000
14	A	12	VAL	0	-0.024	-0.008	22.305	0.357	0.357	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-0.848	-0.913	26.152	-10.224	-10.224	0.000	0.000	0.000	0.000
16	A	14	HIS	0	0.043	0.011	27.708	0.067	0.067	0.000	0.000	0.000	0.000
17	A	15	ARG	1	0.768	0.860	29.457	10.021	10.021	0.000	0.000	0.000	0.000
18	A	16	TYR	0	0.032	0.049	29.326	0.304	0.304	0.000	0.000	0.000	0.000
19	A	17	PRO	0	-0.026	-0.017	32.060	0.235	0.235	0.000	0.000	0.000	0.000
20	A	18	ARG	1	0.945	0.970	32.723	8.558	8.558	0.000	0.000	0.000	0.000
21	A	19	ILE	0	0.059	0.034	28.837	-0.211	-0.211	0.000	0.000	0.000	0.000
22	A	20	GLY	0	-0.052	-0.025	29.974	0.407	0.407	0.000	0.000	0.000	0.000
23	A	21	GLU	-1	-0.897	-0.951	30.285	-9.629	-9.629	0.000	0.000	0.000	0.000
24	A	22	GLU	-1	-0.873	-0.942	23.882	-13.197	-13.197	0.000	0.000	0.000	0.000
25	A	23	ILE	0	-0.019	0.009	23.327	0.363	0.363	0.000	0.000	0.000	0.000
26	A	24	PRO	0	-0.012	-0.020	23.998	-0.453	-0.453	0.000	0.000	0.000	0.000
27	A	25	PHE	0	0.036	0.011	21.279	-0.297	-0.297	0.000	0.000	0.000	0.000
28	A	26	ALA	0	0.048	0.054	19.907	-0.883	-0.883	0.000	0.000	0.000	0.000
29	A	27	VAL	0	-0.016	-0.021	19.009	-1.040	-1.040	0.000	0.000	0.000	0.000
30	A	28	GLU	-1	-0.964	-0.980	19.618	-14.380	-14.380	0.000	0.000	0.000	0.000
31	A	29	THR	0	0.001	-0.014	15.262	-0.858	-0.858	0.000	0.000	0.000	0.000
32	A	30	LEU	0	-0.028	-0.010	14.402	-1.751	-1.751	0.000	0.000	0.000	0.000
33	A	31	LYS	1	0.879	0.928	14.793	13.047	13.047	0.000	0.000	0.000	0.000
34	A	32	LEU	0	-0.013	0.009	13.202	-0.772	-0.772	0.000	0.000	0.000	0.000
35	A	33	LEU	0	0.011	-0.004	9.809	-1.809	-1.809	0.000	0.000	0.000	0.000
36	A	34	GLN	0	-0.003	-0.007	10.515	-2.174	-2.174	0.000	0.000	0.000	0.000
37	A	35	GLN	0	-0.030	-0.002	12.299	-0.880	-0.880	0.000	0.000	0.000	0.000
38	A	36	GLU	-1	-0.866	-0.903	8.011	-26.613	-26.613	0.000	0.000	0.000	0.000
39	A	37	LYS	1	0.835	0.910	7.068	21.354	21.354	0.000	0.000	0.000	0.000
40	A	38	HIS	0	0.049	0.032	4.957	-7.814	-7.814	0.000	0.000	0.000	0.000
41	A	39	ARG	1	0.887	0.957	7.888	32.976	32.976	0.000	0.000	0.000	0.000
42	A	40	LEU	0	0.021	0.025	9.948	-0.800	-0.800	0.000	0.000	0.000	0.000
43	A	41	ILE	0	-0.044	-0.023	12.775	0.860	0.860	0.000	0.000	0.000	0.000
44	A	42	LEU	0	0.017	0.031	15.051	-0.098	-0.098	0.000	0.000	0.000	0.000
45	A	43	TRP	0	0.003	-0.024	17.087	0.055	0.055	0.000	0.000	0.000	0.000
46	A	44	SER	0	0.053	0.024	19.080	0.322	0.322	0.000	0.000	0.000	0.000
47	A	45	VAL	0	-0.029	-0.019	22.662	0.150	0.150	0.000	0.000	0.000	0.000
48	A	46	ARG	1	0.681	0.814	25.841	11.458	11.458	0.000	0.000	0.000	0.000
49	A	47	GLU	-1	-0.843	-0.924	26.080	-12.584	-12.584	0.000	0.000	0.000	0.000
50	A	48	GLY	0	-0.030	-0.015	28.483	0.395	0.395	0.000	0.000	0.000	0.000
51	A	49	GLU	-1	-0.826	-0.920	29.881	-9.625	-9.625	0.000	0.000	0.000	0.000
52	A	50	LEU	0	-0.046	-0.008	30.700	-0.096	-0.096	0.000	0.000	0.000	0.000
53	A	51	LEU	0	-0.031	-0.012	23.400	-0.274	-0.274	0.000	0.000	0.000	0.000
54	A	52	ASP	-1	-0.870	-0.936	26.744	-11.377	-11.377	0.000	0.000	0.000	0.000
55	A	53	GLU	-1	-0.939	-0.978	28.636	-9.689	-9.689	0.000	0.000	0.000	0.000
56	A	54	ALA	0	-0.016	-0.010	25.297	-0.046	-0.046	0.000	0.000	0.000	0.000
57	A	55	ILE	0	-0.003	0.003	23.218	-0.512	-0.512	0.000	0.000	0.000	0.000
58	A	56	GLU	-1	-0.834	-0.911	25.224	-11.201	-11.201	0.000	0.000	0.000	0.000
59	A	57	TRP	0	-0.019	-0.013	24.087	-0.079	-0.079	0.000	0.000	0.000	0.000
60	A	58	CYS	0	-0.048	-0.014	22.242	-0.196	-0.196	0.000	0.000	0.000	0.000
61	A	59	ARG	1	0.839	0.910	24.338	12.095	12.095	0.000	0.000	0.000	0.000
62	A	60	ALA	0	-0.023	-0.013	25.420	0.005	0.005	0.000	0.000	0.000	0.000
63	A	61	ARG	1	0.880	0.947	25.094	11.566	11.566	0.000	0.000	0.000	0.000
64	A	62	GLY	0	-0.026	-0.004	23.831	-0.365	-0.365	0.000	0.000	0.000	0.000
65	A	63	LEU	0	-0.030	-0.017	17.363	-0.717	-0.717	0.000	0.000	0.000	0.000
66	A	64	GLU	-1	-0.856	-0.925	19.254	-13.133	-13.133	0.000	0.000	0.000	0.000
67	A	65	PHE	0	0.016	0.000	16.449	-1.057	-1.057	0.000	0.000	0.000	0.000
68	A	66	TYR	0	-0.033	-0.020	13.237	-0.227	-0.227	0.000	0.000	0.000	0.000
69	A	67	ALA	0	0.016	0.001	15.548	0.532	0.532	0.000	0.000	0.000	0.000
70	A	68	ALA	0	0.027	0.008	17.773	-0.422	-0.422	0.000	0.000	0.000	0.000
71	A	69	ASN	0	0.013	0.005	19.853	-0.190	-0.190	0.000	0.000	0.000	0.000
72	A	70	LYS	0	0.013	0.042	18.845	0.649	0.649	0.000	0.000	0.000	0.000
73	A	71	ASP	-1	-0.804	-0.906	15.157	-20.948	-20.948	0.000	0.000	0.000	0.000
74	A	72	TYR	0	-0.113	-0.088	14.300	-2.123	-2.123	0.000	0.000	0.000	0.000
75	A	73	PRO	0	-0.008	0.001	16.558	0.686	0.686	0.000	0.000	0.000	0.000
76	A	74	GLU	-1	-0.841	-0.911	19.332	-15.209	-15.209	0.000	0.000	0.000	0.000
77	A	75	GLU	-1	-0.889	-0.950	21.754	-12.081	-12.081	0.000	0.000	0.000	0.000
78	A	76	GLU	0	-0.083	-0.054	20.883	0.599	0.599	0.000	0.000	0.000	0.000
79	A	77	ARG	1	0.789	0.871	21.939	12.248	12.248	0.000	0.000	0.000	0.000
80	A	78	ASP	-1	-0.846	-0.907	25.092	-11.144	-11.144	0.000	0.000	0.000	0.000
81	A	79	HIS	0	-0.019	-0.015	25.422	-0.508	-0.508	0.000	0.000	0.000	0.000
82	A	80	GLN	0	0.002	0.006	21.472	-0.518	-0.518	0.000	0.000	0.000	0.000
83	A	81	GLY	0	0.002	0.013	20.106	0.205	0.205	0.000	0.000	0.000	0.000
84	A	82	PHE	0	0.012	-0.006	19.435	-0.905	-0.905	0.000	0.000	0.000	0.000
85	A	83	SER	0	-0.030	-0.032	18.186	-0.150	-0.150	0.000	0.000	0.000	0.000
86	A	84	ARG	1	0.965	0.993	20.315	11.628	11.628	0.000	0.000	0.000	0.000
87	A	85	LYS	1	0.919	0.976	15.915	18.450	18.450	0.000	0.000	0.000	0.000
88	A	86	LEU	0	0.056	0.045	14.760	-0.159	-0.159	0.000	0.000	0.000	0.000
89	A	87	LYS	1	0.792	0.872	12.770	18.705	18.705	0.000	0.000	0.000	0.000
90	A	88	ALA	0	-0.019	0.003	10.085	-2.211	-2.211	0.000	0.000	0.000	0.000
91	A	89	ASP	-1	-0.869	-0.929	5.559	-48.732	-48.732	0.000	0.000	0.000	0.000
92	A	90	LEU	0	-0.034	-0.019	7.831	1.022	1.022	0.000	0.000	0.000	0.000
93	A	91	PHE	0	-0.025	-0.017	9.721	0.795	0.795	0.000	0.000	0.000	0.000
94	A	92	ILE	0	-0.022	0.000	12.205	0.355	0.355	0.000	0.000	0.000	0.000
95	A	93	ASP	-1	-0.825	-0.927	15.383	-14.303	-14.303	0.000	0.000	0.000	0.000
96	A	94	ASP	-1	-0.881	-0.946	19.032	-12.757	-12.757	0.000	0.000	0.000	0.000
97	A	95	ARG	1	0.884	0.938	22.096	12.190	12.190	0.000	0.000	0.000	0.000
98	A	96	ASN	0	-0.040	-0.011	16.334	0.326	0.326	0.000	0.000	0.000	0.000
99	A	97	VAL	0	-0.028	-0.023	20.604	0.574	0.574	0.000	0.000	0.000	0.000
100	A	98	GLY	0	-0.036	-0.023	21.221	-0.483	-0.483	0.000	0.000	0.000	0.000
101	A	99	GLY	0	0.002	0.025	22.707	0.329	0.329	0.000	0.000	0.000	0.000
102	A	100	ILE	0	-0.041	-0.019	18.333	-0.749	-0.749	0.000	0.000	0.000	0.000
103	A	101	PRO	0	-0.019	0.001	18.617	0.693	0.693	0.000	0.000	0.000	0.000
104	A	102	ASP	-1	-0.830	-0.930	20.750	-14.027	-14.027	0.000	0.000	0.000	0.000
105	A	103	TRP	0	0.053	-0.006	15.094	-1.281	-1.281	0.000	0.000	0.000	0.000
106	A	104	GLY	0	0.017	0.027	17.229	-0.934	-0.934	0.000	0.000	0.000	0.000
107	A	105	ILE	0	0.030	0.009	16.676	-0.882	-0.882	0.000	0.000	0.000	0.000
108	A	106	ILE	0	-0.034	-0.011	14.073	-1.274	-1.274	0.000	0.000	0.000	0.000
109	A	107	TYR	0	-0.039	-0.043	11.548	-1.596	-1.596	0.000	0.000	0.000	0.000
110	A	108	GLU	-1	-0.837	-0.914	11.731	-18.428	-18.428	0.000	0.000	0.000	0.000
111	A	109	MET	0	-0.043	-0.015	11.720	-0.785	-0.785	0.000	0.000	0.000	0.000
112	A	110	ILE	0	-0.037	-0.016	7.628	-2.393	-2.393	0.000	0.000	0.000	0.000
113	A	111	LYS	1	0.753	0.869	7.207	20.444	20.444	0.000	0.000	0.000	0.000
114	A	112	GLU	-1	-0.943	-0.986	7.242	-22.644	-22.644	0.000	0.000	0.000	0.000
116	A	114	LYS	1	0.874	0.952	8.690	18.308	18.308	0.000	0.000	0.000	0.000
117	A	115	THR	0	-0.036	-0.050	12.388	-0.063	-0.063	0.000	0.000	0.000	0.000
118	A	116	PHE	0	0.075	0.003	14.638	0.400	0.400	0.000	0.000	0.000	0.000
119	A	117	ALA	0	-0.023	-0.004	18.040	0.734	0.734	0.000	0.000	0.000	0.000
120	A	118	ASP	-1	-0.806	-0.868	14.767	-17.963	-17.963	0.000	0.000	0.000	0.000
121	A	119	ILE	0	-0.062	-0.018	15.571	0.382	0.382	0.000	0.000	0.000	0.000
122	A	120	TYR	0	-0.023	-0.015	18.708	0.501	0.501	0.000	0.000	0.000	0.000
123	A	121	SER	0	-0.098	-0.053	20.457	0.623	0.623	0.000	0.000	0.000	0.000
124	A	122	GLN	-1	-0.984	-0.983	21.932	-11.313	-11.313	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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