FMO DATABASE

FMODB ID: 3G51L

Calculation Name: 2B0L-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2B0L

Chain ID: A

ChEMBL ID:

UniProt ID: P39779

Base Structure: X-ray

Registration Date: 2025-10-11

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	98
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-697945.442324
FMO2-HF: Nuclear repulsion	659801.154868
FMO2-HF: Total energy	-38144.287456
FMO2-MP2: Total energy	-38255.772464

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:161:HIS)

Summations of interaction energy for fragment #1(A:161:HIS)

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.
20.568	23.801	-0.015	-1.599	-1.618	-0.003

Interaction energy analysis for fragmet #1(A:161:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.901 / q_NPA : 0.934

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	163	HIS	0	0.023	-0.002	3.835	7.405	10.638	-0.015	-1.599	-1.618	-0.003
4	A	164	HIS	0	0.027	0.024	5.850	5.710	5.710	0.000	0.000	0.000	0.000
5	A	165	HIS	0	0.062	0.027	6.175	4.848	4.848	0.000	0.000	0.000	0.000
6	A	166	HIS	0	0.031	0.028	8.619	3.714	3.714	0.000	0.000	0.000	0.000
7	A	167	MET	0	0.060	0.043	11.926	1.665	1.665	0.000	0.000	0.000	0.000
8	A	168	SER	0	-0.005	-0.002	12.858	1.027	1.027	0.000	0.000	0.000	0.000
9	A	169	LYS	1	0.963	0.978	9.997	26.244	26.244	0.000	0.000	0.000	0.000
10	A	170	ALA	0	0.011	0.015	15.106	1.009	1.009	0.000	0.000	0.000	0.000
11	A	171	VAL	0	0.030	0.010	17.696	0.813	0.813	0.000	0.000	0.000	0.000
12	A	172	VAL	0	0.011	0.016	18.001	0.821	0.821	0.000	0.000	0.000	0.000
13	A	173	GLN	0	-0.024	-0.016	17.807	1.332	1.332	0.000	0.000	0.000	0.000
14	A	174	MET	0	-0.047	-0.015	20.779	0.424	0.424	0.000	0.000	0.000	0.000
15	A	175	ALA	0	0.038	0.035	23.137	0.639	0.639	0.000	0.000	0.000	0.000
16	A	176	ILE	0	0.040	0.024	21.669	0.609	0.609	0.000	0.000	0.000	0.000
17	A	177	SER	0	-0.072	-0.042	24.928	0.516	0.516	0.000	0.000	0.000	0.000
18	A	178	SER	0	-0.052	-0.034	26.800	0.503	0.503	0.000	0.000	0.000	0.000
19	A	179	LEU	0	-0.052	-0.013	27.475	0.481	0.481	0.000	0.000	0.000	0.000
20	A	180	SER	0	-0.015	-0.040	30.718	0.080	0.080	0.000	0.000	0.000	0.000
21	A	181	TYR	0	0.052	0.010	32.708	-0.031	-0.031	0.000	0.000	0.000	0.000
22	A	182	SER	0	0.048	0.032	33.542	-0.064	-0.064	0.000	0.000	0.000	0.000
23	A	183	GLU	-1	-0.838	-0.896	32.470	-9.248	-9.248	0.000	0.000	0.000	0.000
24	A	184	LEU	0	0.020	0.006	27.150	-0.151	-0.151	0.000	0.000	0.000	0.000
25	A	185	GLU	-1	-0.858	-0.929	29.917	-8.801	-8.801	0.000	0.000	0.000	0.000
26	A	186	ALA	0	-0.044	-0.030	32.211	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	187	ILE	0	-0.042	-0.034	26.428	-0.055	-0.055	0.000	0.000	0.000	0.000
28	A	188	GLU	-1	-0.846	-0.933	27.127	-11.057	-11.057	0.000	0.000	0.000	0.000
29	A	189	HIS	0	0.040	0.025	28.656	0.018	0.018	0.000	0.000	0.000	0.000
30	A	190	ILE	0	-0.035	-0.027	29.109	0.104	0.104	0.000	0.000	0.000	0.000
31	A	191	PHE	0	-0.073	-0.046	24.637	-0.067	-0.067	0.000	0.000	0.000	0.000
32	A	192	GLU	-1	-0.898	-0.929	25.824	-10.692	-10.692	0.000	0.000	0.000	0.000
33	A	193	GLU	-1	-0.984	-0.991	28.353	-8.554	-8.554	0.000	0.000	0.000	0.000
34	A	194	LEU	0	-0.089	-0.028	24.838	0.152	0.152	0.000	0.000	0.000	0.000
35	A	195	ASP	-1	-0.914	-0.950	26.931	-10.775	-10.775	0.000	0.000	0.000	0.000
36	A	196	GLY	0	-0.006	0.001	22.670	-0.288	-0.288	0.000	0.000	0.000	0.000
37	A	197	ASN	0	-0.019	-0.025	18.454	-0.242	-0.242	0.000	0.000	0.000	0.000
38	A	198	GLU	-1	-0.825	-0.874	22.402	-11.315	-11.315	0.000	0.000	0.000	0.000
39	A	199	GLY	0	0.070	0.037	26.085	0.075	0.075	0.000	0.000	0.000	0.000
40	A	200	LEU	0	-0.069	-0.025	29.633	0.127	0.127	0.000	0.000	0.000	0.000
41	A	201	LEU	0	0.079	0.055	32.366	0.080	0.080	0.000	0.000	0.000	0.000
42	A	202	VAL	0	0.012	-0.012	34.095	0.229	0.229	0.000	0.000	0.000	0.000
43	A	203	ALA	0	0.021	0.000	37.215	0.054	0.054	0.000	0.000	0.000	0.000
44	A	204	SER	0	-0.056	-0.023	38.143	0.024	0.024	0.000	0.000	0.000	0.000
45	A	205	LYS	1	1.033	1.019	38.226	7.718	7.718	0.000	0.000	0.000	0.000
46	A	206	ILE	0	0.035	0.028	34.120	0.027	0.027	0.000	0.000	0.000	0.000
47	A	207	ALA	0	-0.012	-0.006	37.460	0.029	0.029	0.000	0.000	0.000	0.000
48	A	208	ASP	-1	-0.940	-0.988	40.450	-7.058	-7.058	0.000	0.000	0.000	0.000
49	A	209	ARG	1	0.852	0.931	33.797	8.798	8.798	0.000	0.000	0.000	0.000
50	A	210	VAL	0	0.020	0.008	35.928	0.034	0.034	0.000	0.000	0.000	0.000
51	A	211	GLY	0	0.014	0.033	39.288	0.064	0.064	0.000	0.000	0.000	0.000
52	A	212	ILE	0	-0.024	0.001	36.871	0.082	0.082	0.000	0.000	0.000	0.000
53	A	213	THR	0	0.019	-0.010	41.324	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	214	ARG	1	1.008	0.979	39.845	6.987	6.987	0.000	0.000	0.000	0.000
55	A	215	SER	0	-0.008	-0.006	39.047	-0.167	-0.167	0.000	0.000	0.000	0.000
56	A	216	VAL	0	0.051	0.040	36.558	-0.142	-0.142	0.000	0.000	0.000	0.000
57	A	217	ILE	0	0.051	0.041	34.557	-0.255	-0.255	0.000	0.000	0.000	0.000
58	A	218	VAL	0	-0.036	-0.023	34.189	-0.239	-0.239	0.000	0.000	0.000	0.000
59	A	219	ASN	0	-0.089	-0.047	34.906	-0.210	-0.210	0.000	0.000	0.000	0.000
60	A	220	ALA	0	0.069	0.038	31.284	-0.237	-0.237	0.000	0.000	0.000	0.000
61	A	221	LEU	0	0.018	0.006	30.124	-0.365	-0.365	0.000	0.000	0.000	0.000
62	A	222	ARG	1	0.974	0.983	30.029	8.154	8.154	0.000	0.000	0.000	0.000
63	A	223	LYS	1	0.805	0.909	29.654	9.403	9.403	0.000	0.000	0.000	0.000
64	A	224	LEU	0	0.034	0.019	24.571	-0.382	-0.382	0.000	0.000	0.000	0.000
65	A	225	GLU	-1	-0.834	-0.886	25.784	-10.592	-10.592	0.000	0.000	0.000	0.000
66	A	226	SER	0	-0.085	-0.054	27.563	-0.208	-0.208	0.000	0.000	0.000	0.000
67	A	227	ALA	0	-0.015	0.001	24.296	-0.127	-0.127	0.000	0.000	0.000	0.000
68	A	228	GLY	0	-0.003	-0.004	23.367	-0.661	-0.661	0.000	0.000	0.000	0.000
69	A	229	VAL	0	-0.066	-0.031	20.902	-0.689	-0.689	0.000	0.000	0.000	0.000
70	A	230	ILE	0	-0.034	-0.025	21.990	-0.403	-0.403	0.000	0.000	0.000	0.000
71	A	231	GLU	-1	-0.930	-0.950	24.778	-10.799	-10.799	0.000	0.000	0.000	0.000
72	A	232	SER	0	-0.111	-0.083	27.686	0.092	0.092	0.000	0.000	0.000	0.000
73	A	233	ARG	1	0.973	0.979	30.900	9.704	9.704	0.000	0.000	0.000	0.000
74	A	234	SER	0	-0.001	0.000	33.904	0.045	0.045	0.000	0.000	0.000	0.000
75	A	235	LEU	0	0.018	0.013	35.283	0.087	0.087	0.000	0.000	0.000	0.000
76	A	236	GLY	0	-0.011	-0.019	38.646	0.121	0.121	0.000	0.000	0.000	0.000
77	A	237	MET	0	-0.046	-0.021	41.636	0.040	0.040	0.000	0.000	0.000	0.000
78	A	238	LYS	1	0.923	0.968	40.447	7.329	7.329	0.000	0.000	0.000	0.000
79	A	239	GLY	0	0.076	0.038	37.463	0.057	0.057	0.000	0.000	0.000	0.000
80	A	240	THR	0	-0.079	-0.040	34.193	0.032	0.032	0.000	0.000	0.000	0.000
81	A	241	TYR	0	-0.051	-0.054	28.319	-0.066	-0.066	0.000	0.000	0.000	0.000
82	A	242	ILE	0	0.026	0.008	26.988	0.014	0.014	0.000	0.000	0.000	0.000
83	A	243	LYS	1	0.883	0.930	23.485	12.048	12.048	0.000	0.000	0.000	0.000
84	A	244	VAL	0	0.022	0.008	19.732	-0.038	-0.038	0.000	0.000	0.000	0.000
85	A	245	LEU	0	-0.043	-0.013	20.706	-0.339	-0.339	0.000	0.000	0.000	0.000
86	A	246	ASN	0	-0.049	-0.031	16.540	-1.682	-1.682	0.000	0.000	0.000	0.000
87	A	247	ASN	0	0.035	-0.004	11.558	0.391	0.391	0.000	0.000	0.000	0.000
88	A	248	LYS	1	0.878	0.927	9.367	25.523	25.523	0.000	0.000	0.000	0.000
89	A	249	PHE	0	0.036	0.019	14.717	0.141	0.141	0.000	0.000	0.000	0.000
90	A	250	LEU	0	0.057	0.019	18.245	0.316	0.316	0.000	0.000	0.000	0.000
91	A	251	ILE	0	-0.036	0.001	13.370	-0.079	-0.079	0.000	0.000	0.000	0.000
92	A	252	GLU	-1	-0.911	-0.970	15.524	-17.998	-17.998	0.000	0.000	0.000	0.000
93	A	253	LEU	0	-0.023	-0.021	18.694	0.577	0.577	0.000	0.000	0.000	0.000
94	A	254	GLU	-1	-0.979	-0.983	18.912	-14.580	-14.580	0.000	0.000	0.000	0.000
95	A	255	ASN	0	-0.058	-0.031	17.476	0.804	0.804	0.000	0.000	0.000	0.000
96	A	256	LEU	0	-0.050	-0.027	20.457	0.306	0.306	0.000	0.000	0.000	0.000
97	A	257	LYS	1	0.817	0.920	23.526	11.524	11.524	0.000	0.000	0.000	0.000
98	A	258	SER	-1	-0.980	-0.969	26.246	-9.917	-9.917	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:161:HIS)