FMO DATABASE

FMODB ID: 13NKZ

Calculation Name: 4FTF-A-Xray549

Preferred Name:

Target Type:

Ligand Name: acetate ion | zinc ion

Ligand 3-letter code: ACT | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4FTF

Chain ID: A

ChEMBL ID:

UniProt ID: Q9KRD9

Base Structure: X-ray

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-802439.368686
FMO2-HF: Nuclear repulsion	759367.152339
FMO2-HF: Total energy	-43072.216346
FMO2-MP2: Total energy	-43193.462409

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:3:GLY)

Summations of interaction energy for fragment #1(A:3: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.
20.266	21.448	-0.011	-0.534	-0.637	-0.003

Interaction energy analysis for fragmet #1(A:3:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.880 / q_NPA : 0.926

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	5	MET	0	0.045	0.026	3.851	7.885	9.067	-0.011	-0.534	-0.637	-0.003
4	A	6	ALA	0	0.047	0.020	5.788	4.997	4.997	0.000	0.000	0.000	0.000
5	A	7	GLU	-1	-0.931	-0.959	7.371	-33.036	-33.036	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.888	0.931	6.850	29.472	29.472	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.039	-0.029	8.723	1.737	1.737	0.000	0.000	0.000	0.000
8	A	10	ARG	1	1.004	1.006	11.288	20.093	20.093	0.000	0.000	0.000	0.000
9	A	11	ASN	0	0.017	-0.008	10.502	3.298	3.298	0.000	0.000	0.000	0.000
10	A	12	LEU	0	-0.046	-0.016	12.151	1.437	1.437	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.871	-0.924	14.770	-18.100	-18.100	0.000	0.000	0.000	0.000
12	A	14	LEU	0	-0.051	-0.023	16.092	1.229	1.229	0.000	0.000	0.000	0.000
13	A	15	LEU	0	-0.014	0.008	17.122	0.999	0.999	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.042	0.013	18.807	0.907	0.907	0.000	0.000	0.000	0.000
15	A	17	GLY	0	0.011	-0.006	20.754	0.786	0.786	0.000	0.000	0.000	0.000
16	A	18	ASN	0	-0.015	-0.009	22.062	1.095	1.095	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.932	0.963	22.218	12.769	12.769	0.000	0.000	0.000	0.000
18	A	20	ALA	0	0.033	0.011	24.757	0.500	0.500	0.000	0.000	0.000	0.000
19	A	21	SER	0	-0.024	0.007	26.482	0.633	0.633	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.023	0.006	26.293	0.361	0.361	0.000	0.000	0.000	0.000
21	A	23	LEU	0	-0.010	-0.006	27.717	0.336	0.336	0.000	0.000	0.000	0.000
22	A	24	SER	0	-0.048	-0.043	30.430	0.346	0.346	0.000	0.000	0.000	0.000
23	A	25	THR	0	-0.101	-0.053	32.664	0.246	0.246	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.952	-0.957	34.231	-8.416	-8.416	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.077	-0.011	34.032	-0.032	-0.032	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.045	-0.034	37.485	0.164	0.164	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.056	0.028	33.079	-0.040	-0.040	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.910	-0.947	36.984	-7.871	-7.871	0.000	0.000	0.000	0.000
29	A	31	PHE	0	-0.043	-0.034	31.314	-0.224	-0.224	0.000	0.000	0.000	0.000
30	A	32	GLY	0	0.029	0.014	36.535	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	33	PRO	0	-0.057	-0.036	38.202	0.173	0.173	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.022	-0.015	35.340	0.107	0.107	0.000	0.000	0.000	0.000
33	A	35	ASN	0	0.031	0.023	38.269	-0.107	-0.107	0.000	0.000	0.000	0.000
34	A	36	ILE	0	-0.016	-0.009	32.160	-0.075	-0.075	0.000	0.000	0.000	0.000
35	A	37	LEU	0	0.038	0.002	35.775	0.136	0.136	0.000	0.000	0.000	0.000
36	A	38	ARG	1	0.902	0.953	32.151	9.499	9.499	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.071	0.048	28.692	-0.137	-0.137	0.000	0.000	0.000	0.000
38	A	40	THR	0	-0.049	-0.038	27.511	0.270	0.270	0.000	0.000	0.000	0.000
39	A	41	ALA	0	0.012	0.028	22.573	-0.181	-0.181	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.925	0.961	22.759	12.100	12.100	0.000	0.000	0.000	0.000
41	A	43	GLY	0	0.058	0.033	18.777	-0.260	-0.260	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.017	-0.002	15.417	0.429	0.429	0.000	0.000	0.000	0.000
43	A	45	THR	0	-0.028	-0.015	17.559	0.058	0.058	0.000	0.000	0.000	0.000
44	A	46	VAL	0	-0.015	-0.005	21.123	0.190	0.190	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.890	-0.955	24.047	-11.408	-11.408	0.000	0.000	0.000	0.000
46	A	48	LEU	0	0.002	0.000	27.196	0.135	0.135	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.036	-0.006	30.257	0.102	0.102	0.000	0.000	0.000	0.000
48	A	50	MET	0	-0.009	-0.001	32.597	0.001	0.001	0.000	0.000	0.000	0.000
49	A	51	VAL	0	0.001	0.004	35.764	0.072	0.072	0.000	0.000	0.000	0.000
50	A	52	TYR	0	0.078	0.039	39.580	0.055	0.055	0.000	0.000	0.000	0.000
51	A	53	ASN	0	0.017	-0.010	41.585	0.092	0.092	0.000	0.000	0.000	0.000
52	A	54	THR	0	0.000	-0.018	44.201	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.792	-0.845	46.495	-6.379	-6.379	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.027	-0.002	48.058	0.129	0.129	0.000	0.000	0.000	0.000
55	A	57	ASN	0	0.031	0.006	50.006	0.008	0.008	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.045	-0.029	50.043	-0.023	-0.023	0.000	0.000	0.000	0.000
57	A	59	ALA	0	0.001	0.018	46.703	-0.142	-0.142	0.000	0.000	0.000	0.000
58	A	60	LYS	1	0.938	0.961	42.952	7.294	7.294	0.000	0.000	0.000	0.000
59	A	61	PRO	0	0.051	0.028	42.045	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	62	THR	0	0.035	0.007	37.149	-0.044	-0.044	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.859	-0.928	36.890	-8.143	-8.143	0.000	0.000	0.000	0.000
62	A	64	GLN	0	-0.010	-0.016	36.724	-0.046	-0.046	0.000	0.000	0.000	0.000
63	A	65	VAL	0	-0.038	-0.009	37.695	-0.098	-0.098	0.000	0.000	0.000	0.000
64	A	66	LEU	0	0.010	0.002	31.415	-0.169	-0.169	0.000	0.000	0.000	0.000
65	A	67	GLN	0	0.044	0.016	33.077	-0.088	-0.088	0.000	0.000	0.000	0.000
66	A	68	SER	0	-0.022	0.014	33.506	-0.242	-0.242	0.000	0.000	0.000	0.000
67	A	69	ALA	0	0.026	0.023	32.755	-0.141	-0.141	0.000	0.000	0.000	0.000
68	A	70	VAL	0	0.045	0.010	27.750	-0.251	-0.251	0.000	0.000	0.000	0.000
69	A	71	SER	0	0.016	-0.011	29.077	-0.321	-0.321	0.000	0.000	0.000	0.000
70	A	72	SER	0	-0.050	-0.032	30.597	-0.067	-0.067	0.000	0.000	0.000	0.000
71	A	73	PHE	0	-0.048	-0.041	26.589	-0.155	-0.155	0.000	0.000	0.000	0.000
72	A	111	CYS	-1	-0.922	-0.935	23.716	-11.813	-11.813	0.000	0.000	0.000	0.000
73	A	75	ALA	0	0.020	0.023	26.782	-0.208	-0.208	0.000	0.000	0.000	0.000
74	A	76	ASN	0	-0.015	-0.006	28.169	-0.232	-0.232	0.000	0.000	0.000	0.000
75	A	77	LYS	1	0.993	0.983	26.271	9.971	9.971	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.889	-0.932	24.548	-11.908	-11.908	0.000	0.000	0.000	0.000
77	A	79	ILE	0	-0.055	-0.027	23.404	-0.609	-0.609	0.000	0.000	0.000	0.000
78	A	80	ARG	1	0.894	0.953	22.059	12.398	12.398	0.000	0.000	0.000	0.000
79	A	81	SER	0	0.007	0.009	20.534	-0.956	-0.956	0.000	0.000	0.000	0.000
80	A	82	ASN	0	0.004	-0.014	18.820	-1.301	-1.301	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.000	0.010	18.063	-0.923	-0.923	0.000	0.000	0.000	0.000
82	A	84	ASP	-1	-0.842	-0.915	17.821	-15.675	-15.675	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.034	-0.007	14.107	-1.380	-1.380	0.000	0.000	0.000	0.000
84	A	86	GLY	0	0.003	0.006	13.270	-2.041	-2.041	0.000	0.000	0.000	0.000
85	A	87	ILE	0	-0.061	-0.020	14.981	-0.327	-0.327	0.000	0.000	0.000	0.000
86	A	88	SER	0	0.004	0.014	17.721	0.554	0.554	0.000	0.000	0.000	0.000
87	A	89	TYR	0	0.049	0.011	20.200	0.022	0.022	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.833	0.902	23.940	11.605	11.605	0.000	0.000	0.000	0.000
89	A	91	ILE	0	0.014	0.011	26.741	0.241	0.241	0.000	0.000	0.000	0.000
90	A	92	GLN	0	-0.021	-0.013	30.195	0.275	0.275	0.000	0.000	0.000	0.000
91	A	93	MET	0	-0.001	0.016	32.697	0.274	0.274	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.926	0.950	35.787	8.513	8.513	0.000	0.000	0.000	0.000
93	A	95	ASN	0	0.077	0.039	39.195	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	96	THR	0	0.019	0.004	42.831	-0.088	-0.088	0.000	0.000	0.000	0.000
95	A	97	ARG	1	0.767	0.849	45.408	6.561	6.561	0.000	0.000	0.000	0.000
96	A	98	GLY	0	0.022	0.019	41.916	0.011	0.011	0.000	0.000	0.000	0.000
97	A	99	GLN	0	-0.012	0.000	41.160	-0.299	-0.299	0.000	0.000	0.000	0.000
98	A	100	LEU	0	-0.041	-0.022	34.995	-0.044	-0.044	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.044	-0.015	38.228	0.159	0.159	0.000	0.000	0.000	0.000
100	A	102	ALA	0	0.028	0.001	33.683	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.845	-0.914	29.953	-10.548	-10.548	0.000	0.000	0.000	0.000
102	A	104	GLN	0	-0.031	-0.010	27.230	0.129	0.129	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.016	-0.005	21.326	-0.102	-0.102	0.000	0.000	0.000	0.000
104	A	106	VAL	0	0.009	0.010	24.398	0.198	0.198	0.000	0.000	0.000	0.000
105	A	107	THR	0	0.015	-0.016	19.174	-0.685	-0.685	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.877	0.922	15.512	18.264	18.264	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.921	-0.947	20.139	-13.992	-13.992	0.000	0.000	0.000	0.000
108	A	110	SER	0	-0.096	-0.055	21.734	0.399	0.399	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:GLY)