FMO DATABASE

FMODB ID: QKQ7Y

Calculation Name: 2BM3-A-Xray547

Preferred Name:

Target Type:

Ligand Name: isopropyl alcohol

Ligand 3-letter code: IPA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BM3

Chain ID: A

ChEMBL ID:

UniProt ID: P71143

Base Structure: X-ray

Registration Date: 2025-10-03

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	162
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1542437.386641
FMO2-HF: Nuclear repulsion	1481480.143254
FMO2-HF: Total energy	-60957.243387
FMO2-MP2: Total energy	-61138.339395

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:5:LYS)

Summations of interaction energy for fragment #1(A:5:LYS)

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.
-186.424	-185.242	9.23	-5.188	-5.225	-0.058

Interaction energy analysis for fragmet #1(A:5:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.789 / q_NPA : 1.882

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	7	SER	0	-0.019	-0.013	3.636	-9.339	-7.963	-0.004	-0.648	-0.725	-0.001
27	A	31	ASN	0	-0.009	-0.014	4.700	0.973	1.049	-0.001	-0.001	-0.074	0.000
28	A	32	ASN	0	0.013	0.000	1.928	-43.924	-44.363	9.237	-4.528	-4.271	-0.057
29	A	33	ILE	0	0.056	0.056	5.119	-4.171	-4.145	-0.001	-0.004	-0.021	0.000
30	A	34	LYS	1	0.880	0.930	4.316	90.098	90.241	-0.001	-0.007	-0.134	0.000
4	A	8	SER	0	0.023	0.025	6.255	4.042	4.042	0.000	0.000	0.000	0.000
5	A	9	ILE	0	0.010	0.014	8.287	-0.978	-0.978	0.000	0.000	0.000	0.000
6	A	10	GLU	-1	-0.907	-0.957	10.273	-45.572	-45.572	0.000	0.000	0.000	0.000
7	A	11	LEU	0	-0.031	-0.002	12.394	1.287	1.287	0.000	0.000	0.000	0.000
8	A	12	LYS	1	0.975	0.988	12.515	38.973	38.973	0.000	0.000	0.000	0.000
9	A	13	PHE	0	-0.017	-0.007	16.050	0.974	0.974	0.000	0.000	0.000	0.000
10	A	14	ASP	-1	-0.871	-0.925	18.549	-25.756	-25.756	0.000	0.000	0.000	0.000
11	A	15	ARG	1	0.803	0.866	20.350	20.875	20.875	0.000	0.000	0.000	0.000
12	A	16	ASN	0	0.019	-0.004	22.098	1.180	1.180	0.000	0.000	0.000	0.000
13	A	17	LYS	1	0.897	0.932	24.232	22.672	22.672	0.000	0.000	0.000	0.000
14	A	18	GLY	0	0.047	0.023	28.021	-0.305	-0.305	0.000	0.000	0.000	0.000
15	A	19	GLU	-1	-0.883	-0.930	30.807	-15.759	-15.759	0.000	0.000	0.000	0.000
16	A	20	VAL	0	-0.001	-0.016	33.775	-0.315	-0.315	0.000	0.000	0.000	0.000
17	A	21	GLY	0	-0.014	-0.003	35.346	0.337	0.337	0.000	0.000	0.000	0.000
18	A	22	ASP	-1	-0.822	-0.873	31.180	-18.999	-18.999	0.000	0.000	0.000	0.000
19	A	23	ILE	0	-0.015	-0.014	27.170	-0.054	-0.054	0.000	0.000	0.000	0.000
20	A	24	LEU	0	-0.032	0.006	24.811	-0.225	-0.225	0.000	0.000	0.000	0.000
21	A	25	ILE	0	0.014	-0.007	21.373	0.141	0.141	0.000	0.000	0.000	0.000
22	A	26	GLY	0	0.032	0.033	20.018	-1.037	-1.037	0.000	0.000	0.000	0.000
23	A	27	THR	0	-0.062	-0.050	15.239	0.521	0.521	0.000	0.000	0.000	0.000
24	A	28	VAL	0	0.028	0.018	15.347	-1.143	-1.143	0.000	0.000	0.000	0.000
25	A	29	ARG	1	0.883	0.929	8.391	50.595	50.595	0.000	0.000	0.000	0.000
26	A	30	ILE	0	0.047	0.043	9.857	-0.687	-0.687	0.000	0.000	0.000	0.000
31	A	35	ASN	0	0.042	0.012	9.689	1.979	1.979	0.000	0.000	0.000	0.000
32	A	36	PHE	0	0.004	0.009	11.830	3.296	3.296	0.000	0.000	0.000	0.000
33	A	37	ALA	0	0.012	0.015	13.612	0.889	0.889	0.000	0.000	0.000	0.000
34	A	38	GLY	0	0.019	-0.003	16.933	2.125	2.125	0.000	0.000	0.000	0.000
35	A	39	PHE	0	-0.035	-0.011	16.632	-1.964	-1.964	0.000	0.000	0.000	0.000
36	A	40	GLN	0	0.018	-0.007	18.614	1.377	1.377	0.000	0.000	0.000	0.000
37	A	41	VAL	0	-0.050	-0.023	17.832	-1.500	-1.500	0.000	0.000	0.000	0.000
38	A	42	ASN	0	0.013	0.005	20.918	1.869	1.869	0.000	0.000	0.000	0.000
39	A	43	ILE	0	-0.022	-0.016	19.707	-0.732	-0.732	0.000	0.000	0.000	0.000
40	A	44	VAL	0	-0.017	-0.008	23.437	0.975	0.975	0.000	0.000	0.000	0.000
41	A	45	TYR	0	0.012	0.001	25.504	-0.547	-0.547	0.000	0.000	0.000	0.000
42	A	46	ASP	-1	-0.776	-0.885	28.073	-16.803	-16.803	0.000	0.000	0.000	0.000
43	A	47	PRO	0	0.048	0.028	31.648	-0.048	-0.048	0.000	0.000	0.000	0.000
44	A	48	LYS	1	0.819	0.902	33.512	16.935	16.935	0.000	0.000	0.000	0.000
45	A	49	VAL	0	-0.088	-0.049	32.113	0.354	0.354	0.000	0.000	0.000	0.000
46	A	50	LEU	0	0.003	0.005	27.101	-0.131	-0.131	0.000	0.000	0.000	0.000
47	A	51	MET	0	0.031	0.019	31.140	0.243	0.243	0.000	0.000	0.000	0.000
48	A	52	ALA	0	0.021	0.028	27.985	-0.309	-0.309	0.000	0.000	0.000	0.000
49	A	53	VAL	0	-0.029	-0.021	28.468	0.757	0.757	0.000	0.000	0.000	0.000
50	A	54	ASP	-1	-0.792	-0.886	27.780	-20.905	-20.905	0.000	0.000	0.000	0.000
51	A	55	PRO	0	-0.066	-0.037	24.273	0.415	0.415	0.000	0.000	0.000	0.000
52	A	56	GLU	-1	-0.916	-0.948	26.355	-21.616	-21.616	0.000	0.000	0.000	0.000
53	A	57	THR	0	-0.090	-0.078	29.578	0.756	0.756	0.000	0.000	0.000	0.000
54	A	58	GLY	0	0.000	0.009	31.284	0.562	0.562	0.000	0.000	0.000	0.000
55	A	59	LYS	1	0.829	0.913	32.608	16.872	16.872	0.000	0.000	0.000	0.000
56	A	60	GLU	-1	-0.905	-0.968	32.208	-16.541	-16.541	0.000	0.000	0.000	0.000
57	A	61	PHE	0	0.014	0.004	25.871	0.174	0.174	0.000	0.000	0.000	0.000
58	A	62	THR	0	0.001	-0.006	31.787	0.571	0.571	0.000	0.000	0.000	0.000
59	A	63	SER	0	0.057	0.027	31.820	-0.555	-0.555	0.000	0.000	0.000	0.000
60	A	64	SER	0	0.012	0.013	31.240	-0.525	-0.525	0.000	0.000	0.000	0.000
61	A	65	THR	0	-0.024	-0.001	28.729	-0.035	-0.035	0.000	0.000	0.000	0.000
62	A	66	PHE	0	0.047	0.016	21.633	-0.535	-0.535	0.000	0.000	0.000	0.000
63	A	67	PRO	0	-0.025	0.003	22.335	0.509	0.509	0.000	0.000	0.000	0.000
64	A	68	PRO	0	0.033	0.024	23.707	-0.609	-0.609	0.000	0.000	0.000	0.000
65	A	69	GLY	0	0.006	-0.016	21.422	-0.954	-0.954	0.000	0.000	0.000	0.000
66	A	70	ARG	1	0.794	0.911	18.110	25.330	25.330	0.000	0.000	0.000	0.000
67	A	71	THR	0	-0.027	-0.040	14.485	0.879	0.879	0.000	0.000	0.000	0.000
68	A	72	VAL	0	-0.005	0.020	13.115	-0.114	-0.114	0.000	0.000	0.000	0.000
69	A	73	LEU	0	-0.001	0.011	16.477	1.480	1.480	0.000	0.000	0.000	0.000
70	A	74	LYS	1	0.893	0.945	18.988	28.403	28.403	0.000	0.000	0.000	0.000
71	A	75	ASN	0	0.037	0.028	21.347	2.251	2.251	0.000	0.000	0.000	0.000
72	A	76	ASN	0	0.049	-0.001	23.019	-0.405	-0.405	0.000	0.000	0.000	0.000
73	A	77	ALA	0	-0.019	0.009	25.141	0.638	0.638	0.000	0.000	0.000	0.000
74	A	78	TYR	0	0.012	-0.008	20.400	0.048	0.048	0.000	0.000	0.000	0.000
75	A	79	GLY	0	0.007	0.010	24.668	-0.087	-0.087	0.000	0.000	0.000	0.000
76	A	80	PRO	0	-0.032	-0.009	23.187	-0.177	-0.177	0.000	0.000	0.000	0.000
77	A	81	ILE	0	0.002	0.001	24.981	1.022	1.022	0.000	0.000	0.000	0.000
78	A	82	GLN	0	0.008	0.009	24.582	-1.369	-1.369	0.000	0.000	0.000	0.000
79	A	83	ILE	0	0.019	0.005	26.006	0.922	0.922	0.000	0.000	0.000	0.000
80	A	84	ALA	0	-0.039	-0.029	26.350	-1.017	-1.017	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.920	-0.950	28.455	-17.926	-17.926	0.000	0.000	0.000	0.000
82	A	86	ASN	0	-0.069	-0.037	27.792	-0.774	-0.774	0.000	0.000	0.000	0.000
83	A	87	ASP	-1	-0.763	-0.884	30.429	-16.299	-16.299	0.000	0.000	0.000	0.000
84	A	88	PRO	0	-0.015	-0.021	31.568	-0.144	-0.144	0.000	0.000	0.000	0.000
85	A	89	GLU	-1	-0.916	-0.932	32.840	-15.437	-15.437	0.000	0.000	0.000	0.000
86	A	90	LYS	1	0.807	0.877	34.092	16.364	16.364	0.000	0.000	0.000	0.000
87	A	91	GLY	0	-0.028	0.003	31.241	-0.280	-0.280	0.000	0.000	0.000	0.000
88	A	92	ILE	0	-0.023	-0.016	28.206	-0.814	-0.814	0.000	0.000	0.000	0.000
89	A	93	LEU	0	-0.042	-0.027	24.678	0.460	0.460	0.000	0.000	0.000	0.000
90	A	94	ASN	0	0.021	0.005	25.229	-0.996	-0.996	0.000	0.000	0.000	0.000
91	A	95	PHE	0	0.030	0.014	20.318	0.528	0.528	0.000	0.000	0.000	0.000
92	A	96	ALA	0	0.029	0.013	22.308	-1.135	-1.135	0.000	0.000	0.000	0.000
93	A	97	LEU	0	-0.072	-0.028	20.215	1.034	1.034	0.000	0.000	0.000	0.000
94	A	98	ALA	0	0.046	0.028	20.481	-1.618	-1.618	0.000	0.000	0.000	0.000
95	A	99	TYR	0	-0.058	-0.049	18.389	1.830	1.830	0.000	0.000	0.000	0.000
96	A	100	SER	0	-0.010	0.009	22.732	-0.119	-0.119	0.000	0.000	0.000	0.000
97	A	101	TYR	0	-0.027	-0.009	25.700	0.147	0.147	0.000	0.000	0.000	0.000
98	A	102	ILE	0	0.009	-0.009	21.325	-0.508	-0.508	0.000	0.000	0.000	0.000
99	A	103	ALA	0	0.012	0.016	21.949	-0.949	-0.949	0.000	0.000	0.000	0.000
100	A	104	GLY	0	0.079	0.034	23.280	-0.493	-0.493	0.000	0.000	0.000	0.000
101	A	105	TYR	0	-0.065	-0.046	15.314	-0.744	-0.744	0.000	0.000	0.000	0.000
102	A	106	LYS	1	0.829	0.894	18.118	30.351	30.351	0.000	0.000	0.000	0.000
103	A	107	GLU	-1	-0.981	-0.979	19.342	-24.181	-24.181	0.000	0.000	0.000	0.000
104	A	108	THR	0	-0.082	-0.047	20.442	-0.013	-0.013	0.000	0.000	0.000	0.000
105	A	109	GLY	0	0.000	0.010	17.009	-0.565	-0.565	0.000	0.000	0.000	0.000
106	A	110	VAL	0	-0.048	-0.027	14.612	-2.668	-2.668	0.000	0.000	0.000	0.000
107	A	111	ALA	0	0.051	0.026	12.103	1.367	1.367	0.000	0.000	0.000	0.000
108	A	112	GLU	-1	-0.795	-0.885	12.114	-36.279	-36.279	0.000	0.000	0.000	0.000
109	A	113	GLU	-1	-0.846	-0.926	7.530	-66.025	-66.025	0.000	0.000	0.000	0.000
110	A	114	SER	0	-0.090	-0.067	6.599	-11.182	-11.182	0.000	0.000	0.000	0.000
111	A	115	GLY	0	-0.012	0.003	8.883	2.674	2.674	0.000	0.000	0.000	0.000
112	A	116	ILE	0	-0.033	-0.006	11.622	-0.937	-0.937	0.000	0.000	0.000	0.000
113	A	117	ILE	0	0.026	0.005	14.245	0.935	0.935	0.000	0.000	0.000	0.000
114	A	118	ALA	0	0.025	0.008	16.493	1.701	1.701	0.000	0.000	0.000	0.000
115	A	119	LYS	1	0.890	0.962	18.281	26.981	26.981	0.000	0.000	0.000	0.000
116	A	120	ILE	0	0.030	0.011	20.890	0.866	0.866	0.000	0.000	0.000	0.000
117	A	121	GLY	0	0.016	0.021	23.477	-0.576	-0.576	0.000	0.000	0.000	0.000
118	A	122	PHE	0	0.016	-0.009	22.822	0.356	0.356	0.000	0.000	0.000	0.000
119	A	123	LYS	1	0.955	0.986	27.475	16.606	16.606	0.000	0.000	0.000	0.000
120	A	124	ILE	0	-0.012	0.003	29.830	0.170	0.170	0.000	0.000	0.000	0.000
121	A	125	LEU	0	-0.014	-0.001	32.617	0.537	0.537	0.000	0.000	0.000	0.000
122	A	126	GLN	0	-0.004	-0.016	35.037	0.319	0.319	0.000	0.000	0.000	0.000
123	A	127	LYS	1	0.862	0.935	34.589	16.310	16.310	0.000	0.000	0.000	0.000
124	A	128	LYS	1	0.887	0.951	34.111	17.492	17.492	0.000	0.000	0.000	0.000
125	A	129	SER	0	0.009	0.010	30.502	-0.620	-0.620	0.000	0.000	0.000	0.000
126	A	130	THR	0	-0.016	-0.030	28.547	0.414	0.414	0.000	0.000	0.000	0.000
127	A	131	ALA	0	0.035	0.025	24.613	-0.422	-0.422	0.000	0.000	0.000	0.000
128	A	132	VAL	0	-0.015	-0.003	22.740	0.713	0.713	0.000	0.000	0.000	0.000
129	A	133	LYS	1	0.916	0.967	20.812	21.941	21.941	0.000	0.000	0.000	0.000
130	A	134	PHE	0	0.028	0.015	15.290	1.264	1.264	0.000	0.000	0.000	0.000
131	A	135	GLN	0	0.014	0.000	20.663	0.092	0.092	0.000	0.000	0.000	0.000
132	A	136	ASP	-1	-0.780	-0.881	22.922	-26.440	-26.440	0.000	0.000	0.000	0.000
133	A	137	THR	0	0.006	-0.003	24.783	1.089	1.089	0.000	0.000	0.000	0.000
134	A	138	LEU	0	0.004	-0.003	27.823	-0.393	-0.393	0.000	0.000	0.000	0.000
135	A	139	SER	0	-0.024	-0.013	29.045	0.051	0.051	0.000	0.000	0.000	0.000
136	A	140	MET	0	-0.038	0.001	21.666	0.021	0.021	0.000	0.000	0.000	0.000
137	A	141	PRO	0	0.009	0.009	25.490	-0.655	-0.655	0.000	0.000	0.000	0.000
138	A	142	GLY	0	0.017	-0.001	23.916	-0.291	-0.291	0.000	0.000	0.000	0.000
139	A	143	ALA	0	-0.024	0.006	21.212	-1.187	-1.187	0.000	0.000	0.000	0.000
140	A	144	ILE	0	0.011	0.007	16.013	0.216	0.216	0.000	0.000	0.000	0.000
141	A	145	SER	0	-0.020	-0.006	18.345	-1.279	-1.279	0.000	0.000	0.000	0.000
142	A	146	GLY	0	0.010	-0.002	20.021	-0.108	-0.108	0.000	0.000	0.000	0.000
143	A	147	THR	0	-0.054	-0.028	16.334	-0.752	-0.752	0.000	0.000	0.000	0.000
144	A	148	GLN	0	0.031	0.013	18.388	0.591	0.591	0.000	0.000	0.000	0.000
145	A	149	LEU	0	-0.022	-0.010	12.286	-0.215	-0.215	0.000	0.000	0.000	0.000
146	A	150	PHE	0	0.040	0.024	16.368	0.107	0.107	0.000	0.000	0.000	0.000
147	A	151	ASP	-1	-0.782	-0.897	15.151	-36.920	-36.920	0.000	0.000	0.000	0.000
148	A	152	TRP	0	-0.052	-0.038	14.425	1.808	1.808	0.000	0.000	0.000	0.000
149	A	153	ASP	-1	-0.828	-0.894	17.942	-30.580	-30.580	0.000	0.000	0.000	0.000
150	A	154	GLY	0	-0.044	-0.008	20.030	1.550	1.550	0.000	0.000	0.000	0.000
151	A	155	GLU	-1	-0.968	-0.970	18.659	-28.701	-28.701	0.000	0.000	0.000	0.000
152	A	156	VAL	0	-0.031	-0.026	18.442	-1.094	-1.094	0.000	0.000	0.000	0.000
153	A	157	ILE	0	-0.016	-0.002	12.014	-1.246	-1.246	0.000	0.000	0.000	0.000
154	A	158	THR	0	-0.009	-0.017	13.846	0.872	0.872	0.000	0.000	0.000	0.000
155	A	159	GLY	0	-0.017	-0.017	11.674	-2.794	-2.794	0.000	0.000	0.000	0.000
156	A	160	TYR	0	-0.104	-0.053	9.861	-5.148	-5.148	0.000	0.000	0.000	0.000
157	A	161	GLU	-1	-0.916	-0.966	9.710	-47.180	-47.180	0.000	0.000	0.000	0.000
158	A	162	VAL	0	-0.019	-0.020	11.246	-1.153	-1.153	0.000	0.000	0.000	0.000
159	A	163	ILE	0	0.009	0.005	8.880	1.242	1.242	0.000	0.000	0.000	0.000
160	A	164	GLN	0	0.012	-0.011	13.326	1.344	1.344	0.000	0.000	0.000	0.000
161	A	165	PRO	0	-0.038	-0.024	16.401	-0.887	-0.887	0.000	0.000	0.000	0.000
162	A	166	ASP	-2	-1.853	-1.895	17.405	-56.597	-56.597	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LYS)