FMO DATABASE

FMODB ID: N81JQ

Calculation Name: 2ZW2-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2ZW2

Chain ID: A

ChEMBL ID:

UniProt ID: F9VNF4

Base Structure: X-ray

Registration Date: 2025-10-04

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-551367.201643
FMO2-HF: Nuclear repulsion	516611.810141
FMO2-HF: Total energy	-34755.391503
FMO2-MP2: Total energy	-34857.567197

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:4:MET)

Summations of interaction energy for fragment #1(A:4:MET)

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.
-23.595	-15.568	3.845	-4.465	-7.407	-0.036

Interaction energy analysis for fragmet #1(A:4:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.816 / q_NPA : 0.904

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

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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	6	TYR	0	0.041	0.016	3.228	2.870	5.479	-0.002	-1.001	-1.605	-0.004
49	A	52	ASN	0	-0.007	-0.012	3.750	-18.484	-18.152	0.003	-0.214	-0.121	-0.001
50	A	53	SER	0	-0.020	-0.021	3.583	9.176	9.709	0.001	-0.154	-0.380	0.000
51	A	54	SER	0	-0.053	-0.066	2.458	-18.100	-16.213	2.453	-1.954	-2.387	-0.021
52	A	55	SER	0	0.008	0.003	3.254	-1.778	-0.429	0.254	-0.560	-1.042	-0.006
53	A	56	GLN	0	0.040	0.016	5.162	-0.218	-0.206	-0.001	-0.001	-0.010	0.000
83	A	86	ARG	1	0.949	0.975	2.396	44.823	46.128	1.137	-0.581	-1.862	-0.004
4	A	7	ARG	1	0.876	0.945	6.840	21.440	21.440	0.000	0.000	0.000	0.000
5	A	8	VAL	0	0.008	-0.011	9.884	0.520	0.520	0.000	0.000	0.000	0.000
6	A	9	GLU	-1	-0.809	-0.876	12.436	-16.755	-16.755	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.003	-0.007	16.240	-0.070	-0.070	0.000	0.000	0.000	0.000
8	A	11	ILE	0	0.000	0.002	18.864	0.434	0.434	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.009	0.001	22.404	0.220	0.220	0.000	0.000	0.000	0.000
10	A	13	THR	0	0.049	0.018	25.216	0.402	0.402	0.000	0.000	0.000	0.000
11	A	14	ASN	0	0.012	0.006	28.652	-0.329	-0.329	0.000	0.000	0.000	0.000
12	A	15	LYS	1	0.814	0.897	30.949	9.745	9.745	0.000	0.000	0.000	0.000
13	A	16	GLU	-1	-0.887	-0.948	32.973	-9.135	-9.135	0.000	0.000	0.000	0.000
14	A	17	GLY	0	-0.011	0.008	35.602	0.211	0.211	0.000	0.000	0.000	0.000
15	A	18	VAL	0	-0.058	-0.026	35.467	0.188	0.188	0.000	0.000	0.000	0.000
16	A	19	ARG	1	0.865	0.887	36.709	7.422	7.422	0.000	0.000	0.000	0.000
17	A	20	ASP	-1	-0.734	-0.858	34.912	-9.248	-9.248	0.000	0.000	0.000	0.000
18	A	21	PRO	0	-0.011	-0.024	36.865	0.152	0.152	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.920	-0.931	33.607	-9.599	-9.599	0.000	0.000	0.000	0.000
20	A	23	GLY	0	0.033	0.001	36.207	0.117	0.117	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.830	-0.872	36.940	-7.327	-7.327	0.000	0.000	0.000	0.000
22	A	25	THR	0	-0.033	-0.033	40.389	0.277	0.277	0.000	0.000	0.000	0.000
23	A	26	ILE	0	0.021	0.004	35.918	0.192	0.192	0.000	0.000	0.000	0.000
24	A	27	GLN	0	0.031	0.017	39.832	-0.053	-0.053	0.000	0.000	0.000	0.000
25	A	28	ARG	1	0.928	0.965	41.174	6.898	6.898	0.000	0.000	0.000	0.000
26	A	29	TYR	0	-0.034	-0.026	43.798	0.213	0.213	0.000	0.000	0.000	0.000
27	A	30	VAL	0	-0.014	0.001	40.340	0.092	0.092	0.000	0.000	0.000	0.000
28	A	31	VAL	0	0.010	0.002	38.374	0.105	0.105	0.000	0.000	0.000	0.000
29	A	32	SER	0	-0.041	-0.024	41.723	0.097	0.097	0.000	0.000	0.000	0.000
30	A	33	ARG	1	0.890	0.945	45.079	6.730	6.730	0.000	0.000	0.000	0.000
31	A	34	PHE	0	-0.032	0.005	40.038	0.083	0.083	0.000	0.000	0.000	0.000
32	A	35	SER	0	-0.002	-0.022	42.320	0.033	0.033	0.000	0.000	0.000	0.000
33	A	36	ASP	-1	-0.881	-0.936	43.568	-6.918	-6.918	0.000	0.000	0.000	0.000
34	A	37	LYS	1	0.925	0.960	42.305	7.007	7.007	0.000	0.000	0.000	0.000
35	A	38	ILE	0	-0.026	0.003	37.695	-0.172	-0.172	0.000	0.000	0.000	0.000
36	A	39	ILE	0	0.027	0.014	40.204	0.063	0.063	0.000	0.000	0.000	0.000
37	A	40	GLU	-1	-0.934	-0.972	36.433	-8.509	-8.509	0.000	0.000	0.000	0.000
38	A	41	THR	0	-0.004	-0.003	35.099	-0.217	-0.217	0.000	0.000	0.000	0.000
39	A	42	ARG	1	0.782	0.897	32.539	8.880	8.880	0.000	0.000	0.000	0.000
40	A	43	ALA	0	0.037	0.026	31.777	-0.265	-0.265	0.000	0.000	0.000	0.000
41	A	44	GLY	0	0.000	-0.015	28.570	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.892	0.955	24.668	11.948	11.948	0.000	0.000	0.000	0.000
43	A	46	TYR	0	-0.020	-0.026	18.565	-0.321	-0.321	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.013	-0.011	19.539	0.284	0.284	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.003	-0.001	14.849	-0.321	-0.321	0.000	0.000	0.000	0.000
46	A	49	PHE	0	0.014	0.010	12.966	0.343	0.343	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.897	0.958	8.480	30.713	30.713	0.000	0.000	0.000	0.000
48	A	51	VAL	0	0.000	0.004	7.878	0.512	0.512	0.000	0.000	0.000	0.000
54	A	57	GLN	0	-0.027	0.000	7.665	1.118	1.118	0.000	0.000	0.000	0.000
55	A	58	GLU	-1	-0.773	-0.841	6.712	-36.042	-36.042	0.000	0.000	0.000	0.000
56	A	59	ALA	0	-0.005	-0.013	6.992	0.821	0.821	0.000	0.000	0.000	0.000
57	A	60	THR	0	-0.033	-0.036	9.015	2.175	2.175	0.000	0.000	0.000	0.000
58	A	61	GLU	-1	-0.856	-0.921	12.456	-18.245	-18.245	0.000	0.000	0.000	0.000
59	A	62	LEU	0	0.000	0.009	10.454	1.446	1.446	0.000	0.000	0.000	0.000
60	A	63	VAL	0	0.013	0.001	12.747	1.204	1.204	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.835	0.903	15.182	15.653	15.653	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.921	0.968	16.638	17.622	17.622	0.000	0.000	0.000	0.000
63	A	66	LEU	0	-0.005	0.003	16.135	0.897	0.897	0.000	0.000	0.000	0.000
64	A	67	ALA	0	0.001	-0.009	18.609	0.880	0.880	0.000	0.000	0.000	0.000
65	A	68	ASP	-1	-0.820	-0.882	21.183	-13.256	-13.256	0.000	0.000	0.000	0.000
66	A	69	GLU	-1	-0.912	-0.971	20.708	-14.401	-14.401	0.000	0.000	0.000	0.000
67	A	70	MET	0	-0.032	-0.017	20.597	0.564	0.564	0.000	0.000	0.000	0.000
68	A	71	ARG	1	0.891	0.960	23.403	11.759	11.759	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.022	0.022	20.102	0.281	0.281	0.000	0.000	0.000	0.000
70	A	73	TYR	0	-0.065	-0.058	23.706	0.422	0.422	0.000	0.000	0.000	0.000
71	A	74	ASN	0	0.043	0.019	26.901	-0.051	-0.051	0.000	0.000	0.000	0.000
72	A	75	PRO	0	0.051	0.029	27.466	0.249	0.249	0.000	0.000	0.000	0.000
73	A	76	ILE	0	0.012	0.009	29.260	0.178	0.178	0.000	0.000	0.000	0.000
74	A	77	VAL	0	-0.011	-0.008	32.369	0.224	0.224	0.000	0.000	0.000	0.000
75	A	78	HIS	0	0.020	0.013	28.286	-0.095	-0.095	0.000	0.000	0.000	0.000
76	A	79	LYS	1	0.901	0.952	27.109	10.752	10.752	0.000	0.000	0.000	0.000
77	A	80	ILE	0	-0.018	-0.015	20.925	-0.067	-0.067	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.816	-0.863	20.492	-13.878	-13.878	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.021	-0.017	15.125	-0.270	-0.270	0.000	0.000	0.000	0.000
80	A	83	ARG	1	0.840	0.903	15.682	15.164	15.164	0.000	0.000	0.000	0.000
81	A	84	ALA	0	0.002	-0.007	10.056	-0.926	-0.926	0.000	0.000	0.000	0.000
82	A	85	ASN	0	0.025	0.022	10.638	2.423	2.423	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.062	-0.035	6.153	5.176	5.176	0.000	0.000	0.000	0.000
85	A	88	GLU	-2	-1.788	-1.893	4.971	-79.722	-79.722	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:MET)