FMO DATABASE

FMODB ID: MRGZZ

Calculation Name: 2CT2-A-Other547

Preferred Name:

Target Type:

Ligand Name: zinc ion

Ligand 3-letter code: ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CT2

Chain ID: A

ChEMBL ID:

UniProt ID: Q13049

Base Structure: SolutionNMR

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	88
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-535679.415066
FMO2-HF: Nuclear repulsion	500780.745197
FMO2-HF: Total energy	-34898.669869
FMO2-MP2: Total energy	-34994.432668

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:GLY)

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

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.
-15.278	-14.09	-0.015	-0.543	-0.631	-0.003

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.859 / q_NPA : 0.915

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	3	SER	0	0.046	0.021	3.842	2.092	3.280	-0.015	-0.543	-0.631	-0.003
4	A	4	GLY	0	0.041	0.022	6.620	-0.462	-0.462	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.039	-0.019	10.124	0.858	0.858	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.005	0.013	13.494	-0.152	-0.152	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.036	0.018	16.817	-0.203	-0.203	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.073	-0.052	17.829	0.059	0.059	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.021	0.022	20.742	0.564	0.564	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.912	-0.950	22.374	-13.776	-13.776	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.011	-0.013	24.815	0.505	0.505	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.025	-0.007	24.394	0.428	0.428	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.861	0.922	27.476	9.063	9.063	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.860	-0.932	29.840	-9.843	-9.843	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.014	-0.005	28.118	-0.358	-0.358	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.004	-0.018	25.903	0.139	0.139	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.911	-0.937	21.069	-14.647	-14.647	0.000	0.000	0.000	0.000
18	A	18	CYS	0	-0.108	-0.042	23.812	0.706	0.706	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.014	0.005	24.143	-0.439	-0.439	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.046	-0.045	24.554	0.241	0.241	0.000	0.000	0.000	0.000
21	A	21	CYS	0	-0.039	-0.037	20.680	-0.094	-0.094	0.000	0.000	0.000	0.000
22	A	22	MET	0	-0.019	0.004	19.549	-0.748	-0.748	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.813	-0.908	17.369	-17.602	-17.602	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.015	0.011	20.257	1.133	1.133	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.005	-0.017	22.274	0.039	0.039	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.001	0.004	21.891	0.259	0.259	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.893	-0.976	25.216	-9.671	-9.671	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.949	-0.965	22.880	-13.013	-13.013	0.000	0.000	0.000	0.000
29	A	29	GLN	0	-0.017	-0.026	22.210	0.516	0.516	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.015	0.005	21.087	0.579	0.579	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.974	0.991	25.741	9.643	9.643	0.000	0.000	0.000	0.000
32	A	32	PRO	0	0.028	0.037	29.169	0.035	0.035	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.780	0.880	30.542	9.197	9.197	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.002	0.009	33.278	-0.184	-0.184	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.031	0.007	34.437	0.231	0.231	0.000	0.000	0.000	0.000
36	A	36	HIS	0	0.031	0.000	37.737	-0.034	-0.034	0.000	0.000	0.000	0.000
37	A	37	CYS	0	-0.141	-0.060	37.837	0.117	0.117	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.060	0.035	38.583	0.080	0.080	0.000	0.000	0.000	0.000
39	A	39	HIS	0	0.030	-0.008	33.652	-0.284	-0.284	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.006	-0.009	30.435	0.124	0.124	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.034	-0.028	28.683	-0.246	-0.246	0.000	0.000	0.000	0.000
42	A	42	CYS	0	0.024	0.056	24.463	0.227	0.227	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.902	0.935	28.045	10.646	10.646	0.000	0.000	0.000	0.000
44	A	44	GLN	0	0.043	0.015	21.246	0.180	0.180	0.000	0.000	0.000	0.000
45	A	45	CYS	0	0.000	-0.018	25.196	-0.052	-0.052	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.017	0.004	27.689	0.259	0.259	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.784	-0.908	29.664	-9.392	-9.392	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.908	0.964	25.414	11.854	11.854	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.033	-0.007	30.560	0.227	0.227	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.028	-0.025	33.466	0.262	0.262	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.024	0.013	33.552	0.238	0.238	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.016	0.007	34.322	0.151	0.151	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.130	-0.053	36.895	0.267	0.267	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.092	0.038	39.409	0.015	0.015	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.020	-0.009	42.679	0.036	0.036	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.024	0.000	41.720	0.109	0.109	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.036	0.025	35.196	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.943	0.982	35.145	8.598	8.598	0.000	0.000	0.000	0.000
59	A	59	CYS	0	-0.034	0.028	34.975	-0.277	-0.277	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.023	0.002	30.970	0.213	0.213	0.000	0.000	0.000	0.000
61	A	61	PHE	0	0.064	0.023	28.740	0.065	0.065	0.000	0.000	0.000	0.000
62	A	62	CYS	0	-0.033	-0.018	34.305	0.201	0.201	0.000	0.000	0.000	0.000
63	A	63	SER	0	0.002	-0.004	37.461	0.204	0.204	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.967	0.976	39.236	7.331	7.331	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.021	-0.006	40.053	-0.178	-0.178	0.000	0.000	0.000	0.000
66	A	66	THR	0	0.006	0.010	38.892	0.163	0.163	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.897	0.934	41.222	6.616	6.616	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.019	-0.004	37.901	0.126	0.126	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.038	0.016	41.047	-0.077	-0.077	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.026	0.010	39.328	-0.144	-0.144	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.024	0.011	33.085	0.067	0.067	0.000	0.000	0.000	0.000
72	A	72	THR	0	-0.010	-0.021	36.898	-0.125	-0.125	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.025	0.003	39.232	0.139	0.139	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.077	-0.018	35.954	0.132	0.132	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.053	0.029	39.496	0.090	0.090	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.823	-0.909	36.875	-8.580	-8.580	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.011	-0.006	32.521	0.292	0.292	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.077	0.025	33.364	-0.313	-0.313	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.027	-0.021	33.975	-0.132	-0.132	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.013	-0.001	29.263	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.022	0.007	29.322	-0.276	-0.276	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.805	0.907	31.483	8.708	8.708	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.007	0.006	32.727	-0.311	-0.311	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.044	0.022	32.302	0.293	0.293	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.082	0.035	32.904	0.068	0.068	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.058	-0.021	34.918	0.100	0.100	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.038	-0.022	37.901	0.228	0.228	0.000	0.000	0.000	0.000
88	A	88	GLY	-1	-0.852	-0.901	37.717	-8.358	-8.358	0.000	0.000	0.000	0.000

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