FMO DATABASE

FMODB ID: KZ7Z3

Calculation Name: 2JOX-A-Other549

Preferred Name:

Target Type:

Ligand Name: zinc ion

Ligand 3-letter code: ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2JOX

Chain ID: A

ChEMBL ID:

UniProt ID: Q8WUH1

Base Structure: SolutionNMR

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-798276.075898
FMO2-HF: Nuclear repulsion	752958.119166
FMO2-HF: Total energy	-45317.956732
FMO2-MP2: Total energy	-45440.811668

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:2:CYS)

Summations of interaction energy for fragment #1(A:2:CYS)

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.
-163.492	-168.938	41.402	-15.687	-20.271	-0.145

Interaction energy analysis for fragmet #1(A:2:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.745 / q_NPA : 0.853

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	4	ASP	-1	-0.844	-0.933	2.404	-48.742	-45.965	0.577	-1.248	-2.105	-0.008
4	A	5	CYS	0	-0.144	-0.023	2.340	-4.872	-13.994	19.537	-5.467	-4.948	-0.039
5	A	6	VAL	0	-0.028	-0.014	4.427	5.198	5.416	0.007	-0.077	-0.149	0.000
29	A	30	CYS	0	-0.071	-0.028	4.439	-7.243	-6.841	0.039	-0.128	-0.313	0.000
30	A	31	ALA	0	0.098	0.035	2.201	4.388	3.419	4.127	-1.012	-2.147	-0.007
31	A	32	VAL	0	-0.003	-0.017	2.758	2.276	2.156	2.408	-0.065	-2.223	-0.003
32	A	33	CYS	0	-0.094	-0.059	5.020	3.871	3.935	0.004	-0.026	-0.042	0.000
65	A	66	HIS	0	0.093	0.041	1.961	-33.579	-36.862	14.089	-4.973	-5.834	-0.058
66	A	67	VAL	0	-0.009	-0.007	5.065	-0.564	-0.472	-0.001	-0.012	-0.079	0.000
67	A	68	ILE	0	-0.037	-0.026	2.823	-23.095	-20.705	0.364	-1.318	-1.436	-0.014
68	A	69	ALA	0	0.000	-0.011	2.758	-15.640	-13.651	0.253	-1.343	-0.899	-0.016
69	A	70	ARG	1	0.903	0.940	5.311	37.222	37.256	-0.001	0.000	-0.033	0.000
88	A	89	LEU	0	-0.009	0.005	4.295	-0.255	-0.173	-0.001	-0.018	-0.063	0.000
6	A	7	GLU	-1	-0.903	-0.940	7.499	-23.090	-23.090	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.923	0.951	10.929	20.414	20.414	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.904	-0.946	8.078	-34.327	-34.327	0.000	0.000	0.000	0.000
9	A	10	TYR	0	-0.044	-0.018	8.979	2.104	2.104	0.000	0.000	0.000	0.000
10	A	11	PRO	0	-0.027	0.001	11.958	2.008	2.008	0.000	0.000	0.000	0.000
11	A	12	ASN	0	-0.014	-0.010	14.810	0.201	0.201	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.874	0.928	15.852	17.902	17.902	0.000	0.000	0.000	0.000
13	A	14	GLY	0	-0.034	-0.007	19.665	0.408	0.408	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.009	-0.009	22.786	0.083	0.083	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.032	-0.016	20.588	-0.053	-0.053	0.000	0.000	0.000	0.000
16	A	17	CYS	0	-0.011	0.030	19.839	-1.092	-1.092	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.019	-0.017	18.290	0.419	0.419	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.761	-0.867	17.860	-15.402	-15.402	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.068	-0.047	17.707	-0.819	-0.819	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.037	0.029	16.350	-0.208	-0.208	0.000	0.000	0.000	0.000
21	A	22	SER	0	0.032	-0.015	11.572	-2.358	-2.358	0.000	0.000	0.000	0.000
22	A	23	PHE	0	0.037	0.022	12.343	1.259	1.259	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.031	-0.001	12.417	-1.406	-1.406	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.025	-0.006	13.259	-0.488	-0.488	0.000	0.000	0.000	0.000
25	A	26	ASN	0	-0.004	-0.004	10.388	0.473	0.473	0.000	0.000	0.000	0.000
26	A	27	PHE	0	-0.002	-0.006	5.795	-1.817	-1.817	0.000	0.000	0.000	0.000
27	A	28	THR	0	0.064	0.041	7.707	1.853	1.853	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.000	-0.001	7.925	3.066	3.066	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.033	0.024	7.029	2.485	2.485	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.893	0.955	8.670	22.577	22.577	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.943	0.971	8.934	19.103	19.103	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.906	-0.958	11.352	-18.762	-18.762	0.000	0.000	0.000	0.000
37	A	38	PHE	0	0.005	-0.006	11.676	0.896	0.896	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.076	-0.037	8.577	-2.268	-2.268	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.007	0.001	10.905	2.529	2.529	0.000	0.000	0.000	0.000
40	A	41	ILE	0	0.000	0.010	11.312	-2.282	-2.282	0.000	0.000	0.000	0.000
41	A	42	THR	0	-0.020	-0.015	12.097	1.795	1.795	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.048	-0.052	12.684	-0.485	-0.485	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.870	0.959	15.855	16.722	16.722	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.013	0.001	17.206	1.087	1.087	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.012	-0.007	19.616	-0.544	-0.544	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.783	0.877	22.435	12.506	12.506	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.888	-0.937	24.788	-10.845	-10.845	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.900	-0.944	26.679	-11.460	-11.460	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.955	-0.980	30.031	-8.978	-8.978	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.002	0.009	31.690	0.289	0.289	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.957	-0.963	25.010	-12.355	-12.355	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.959	-0.978	25.714	-11.263	-11.263	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.003	-0.003	20.298	-0.601	-0.601	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.030	-0.025	18.147	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	56	THR	0	0.016	0.010	15.252	-0.745	-0.745	0.000	0.000	0.000	0.000
56	A	57	TYR	0	-0.037	-0.036	12.476	0.489	0.489	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.774	-0.860	9.232	-32.228	-32.228	0.000	0.000	0.000	0.000
58	A	59	HIS	1	0.816	0.891	7.487	30.480	30.480	0.000	0.000	0.000	0.000
59	A	60	LEU	0	0.029	0.007	6.959	-5.970	-5.970	0.000	0.000	0.000	0.000
60	A	61	CYS	0	-0.038	-0.010	6.477	3.390	3.390	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.971	0.987	8.291	19.605	19.605	0.000	0.000	0.000	0.000
62	A	63	ASN	0	0.009	-0.003	10.509	3.234	3.234	0.000	0.000	0.000	0.000
63	A	64	CYS	0	-0.013	-0.013	7.006	0.091	0.091	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.004	0.010	9.511	-1.203	-1.203	0.000	0.000	0.000	0.000
70	A	71	HIS	0	-0.004	-0.014	8.580	-2.859	-2.859	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.890	-0.938	11.848	-17.504	-17.504	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.025	-0.015	15.320	-0.606	-0.606	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.001	0.002	18.628	0.203	0.203	0.000	0.000	0.000	0.000
74	A	75	PHE	0	0.008	0.010	22.019	-0.053	-0.053	0.000	0.000	0.000	0.000
75	A	76	SER	0	0.111	0.056	25.533	0.123	0.123	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.001	0.001	28.636	0.112	0.112	0.000	0.000	0.000	0.000
77	A	78	MET	0	-0.048	-0.010	31.544	0.147	0.147	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.938	-0.975	34.756	-8.185	-8.185	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.940	-0.954	38.523	-7.546	-7.546	0.000	0.000	0.000	0.000
80	A	81	PHE	0	-0.063	-0.056	34.226	0.052	0.052	0.000	0.000	0.000	0.000
81	A	82	GLN	0	0.028	0.036	30.642	-0.243	-0.243	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.888	-0.950	27.414	-10.840	-10.840	0.000	0.000	0.000	0.000
83	A	84	TYR	0	-0.010	-0.017	24.147	-0.333	-0.333	0.000	0.000	0.000	0.000
84	A	85	THR	0	0.062	0.019	21.022	-0.390	-0.390	0.000	0.000	0.000	0.000
85	A	86	MET	0	-0.063	-0.002	15.652	-0.431	-0.431	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.023	0.012	13.376	-0.356	-0.356	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.082	-0.022	9.830	-2.017	-2.017	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.010	-0.008	7.366	-0.097	-0.097	0.000	0.000	0.000	0.000
90	A	91	CYS	0	-0.017	-0.035	8.964	1.534	1.534	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.049	0.029	12.153	1.797	1.797	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.956	0.986	13.933	17.998	17.998	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.091	-0.050	16.198	0.501	0.501	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.882	-0.952	19.696	-13.282	-13.282	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.859	-0.921	23.089	-11.138	-11.138	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.022	-0.018	26.460	0.013	0.013	0.000	0.000	0.000	0.000
97	A	98	ILE	0	0.003	0.027	29.739	0.220	0.220	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.008	0.005	32.762	0.050	0.050	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.030	-0.012	35.298	0.036	0.036	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.023	0.008	38.104	0.203	0.203	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.036	0.005	40.625	-0.144	-0.144	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.989	-0.994	42.651	-7.043	-7.043	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.858	-0.897	36.607	-8.833	-8.833	0.000	0.000	0.000	0.000
104	A	105	PRO	0	-0.023	-0.019	38.620	-0.096	-0.096	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.764	0.844	32.399	9.223	9.223	0.000	0.000	0.000	0.000
106	A	107	GLN	-1	-0.982	-0.963	34.260	-9.069	-9.069	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:CYS)