FMO DATABASE

FMODB ID: QK54Y

Calculation Name: 1F1G-A-Xray547

Preferred Name:

Target Type:

Ligand Name: phosphate ion | copper (ii) ion | zinc ion

Ligand 3-letter code: PO4 | CU | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1F1G

Chain ID: A

ChEMBL ID:

UniProt ID: P00445

Base Structure: X-ray

Registration Date: 2025-09-02

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	152
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1309053.211915
FMO2-HF: Nuclear repulsion	1253857.477525
FMO2-HF: Total energy	-55195.73439
FMO2-MP2: Total energy	-55357.53263

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:VAL)

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

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.
-137.09	-128.49	11.03	-8.908	-10.725	-0.09

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.814 / q_NPA : 0.898

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	3	ALA	0	0.021	0.009	3.462	2.260	4.297	0.008	-0.915	-1.131	-0.003
20	A	20	GLU	-1	-0.893	-0.954	3.040	-73.051	-70.709	0.072	-1.186	-1.228	-0.010
21	A	21	GLN	0	0.016	0.015	2.946	7.932	9.272	0.029	-0.467	-0.902	-0.001
22	A	22	ALA	0	0.011	0.016	1.813	-40.690	-41.082	9.439	-5.403	-3.644	-0.069
23	A	23	SER	0	0.019	-0.005	3.849	-1.959	-1.479	0.003	-0.140	-0.344	-0.001
106	A	106	LEU	0	0.011	0.001	2.747	0.508	1.539	0.443	-0.329	-1.145	-0.002
107	A	107	ILE	0	-0.051	-0.003	2.627	-1.361	-0.181	0.859	-0.354	-1.685	-0.003
108	A	108	GLY	0	0.101	0.056	5.245	2.297	2.307	-0.001	-0.002	-0.007	0.000
150	A	151	LEU	0	-0.008	-0.026	2.941	-2.683	-2.196	0.179	-0.108	-0.559	-0.001
152	A	153	ASN	-1	-0.893	-0.920	4.927	-41.420	-41.335	-0.001	-0.004	-0.080	0.000
4	A	4	VAL	0	-0.029	-0.019	5.497	0.994	0.994	0.000	0.000	0.000	0.000
5	A	5	ALA	0	0.040	0.033	9.340	0.730	0.730	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.044	-0.026	12.510	0.429	0.429	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.035	-0.008	15.867	0.456	0.456	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.947	0.952	18.572	14.445	14.445	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.096	0.037	21.873	-0.211	-0.211	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.916	-0.948	25.137	-10.483	-10.483	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.059	-0.023	28.193	0.323	0.323	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.005	0.002	29.107	0.058	0.058	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.026	-0.001	23.499	-0.190	-0.190	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.039	-0.016	22.339	-0.190	-0.190	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.049	0.013	19.779	0.168	0.168	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.079	-0.032	13.766	-0.373	-0.373	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.015	0.014	12.069	0.327	0.327	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.941	0.969	9.725	23.359	23.359	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.013	0.004	6.342	2.083	2.083	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.820	-0.927	5.640	-26.373	-26.373	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.025	0.007	7.645	1.539	1.539	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.957	-0.966	7.280	-26.890	-26.890	0.000	0.000	0.000	0.000
27	A	27	PRO	0	0.002	-0.011	8.869	-1.101	-1.101	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.047	-0.038	6.643	-5.935	-5.935	0.000	0.000	0.000	0.000
29	A	29	THR	0	-0.032	-0.023	7.366	6.067	6.067	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.020	0.014	8.688	-3.249	-3.249	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.027	-0.027	11.458	1.971	1.971	0.000	0.000	0.000	0.000
32	A	32	TYR	0	0.021	0.007	13.556	-0.581	-0.581	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.861	-0.923	16.317	-16.212	-16.212	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.008	-0.002	18.984	-0.304	-0.304	0.000	0.000	0.000	0.000
35	A	35	ALA	0	0.025	0.020	21.574	0.371	0.371	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.072	0.024	25.182	-0.099	-0.099	0.000	0.000	0.000	0.000
37	A	37	ASN	0	-0.049	-0.026	24.020	0.093	0.093	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.006	-0.003	27.937	0.263	0.263	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.034	0.039	30.045	-0.332	-0.332	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.061	-0.030	31.695	0.134	0.134	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.006	0.010	30.437	0.273	0.273	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.899	-0.956	27.436	-11.818	-11.818	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.834	0.914	25.273	10.885	10.885	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.057	0.035	23.885	-0.546	-0.546	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.021	-0.027	15.752	-0.275	-0.275	0.000	0.000	0.000	0.000
46	A	46	HIS	1	0.837	0.896	18.110	13.502	13.502	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.007	0.009	11.467	-0.240	-0.240	0.000	0.000	0.000	0.000
48	A	48	HIS	0	-0.049	-0.040	15.585	0.783	0.783	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.944	-0.978	15.828	-15.181	-15.181	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.044	0.024	15.910	-0.789	-0.789	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.018	0.038	14.953	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.851	-0.906	15.727	-12.558	-12.558	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.012	0.018	19.478	0.126	0.126	0.000	0.000	0.000	0.000
54	A	54	THR	0	-0.066	-0.056	21.397	0.581	0.581	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.032	-0.020	24.652	0.567	0.567	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.079	0.041	24.589	0.049	0.049	0.000	0.000	0.000	0.000
57	A	57	CYS	0	-0.005	-0.016	19.088	-0.630	-0.630	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.030	-0.007	23.172	-0.213	-0.213	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.007	-0.027	22.233	0.079	0.079	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.040	0.031	18.924	-0.191	-0.191	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.030	0.030	19.593	-0.491	-0.491	0.000	0.000	0.000	0.000
62	A	62	PRO	0	0.001	0.012	21.579	0.196	0.196	0.000	0.000	0.000	0.000
63	A	63	HIS	0	0.020	0.007	19.684	-0.406	-0.406	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.002	-0.011	12.700	0.456	0.456	0.000	0.000	0.000	0.000
65	A	65	ASN	0	0.017	-0.005	17.536	-0.714	-0.714	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.026	0.024	15.573	0.727	0.727	0.000	0.000	0.000	0.000
67	A	67	PHE	0	-0.025	-0.032	16.186	0.494	0.494	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.919	0.964	20.933	12.114	12.114	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.909	0.981	20.199	14.822	14.822	0.000	0.000	0.000	0.000
70	A	70	THR	0	0.035	0.011	24.734	0.099	0.099	0.000	0.000	0.000	0.000
71	A	71	HIS	1	0.723	0.849	23.029	12.158	12.158	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.023	0.006	23.759	0.508	0.508	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.005	-0.004	23.768	-0.271	-0.271	0.000	0.000	0.000	0.000
74	A	74	PRO	0	-0.012	-0.015	18.545	-0.133	-0.133	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.003	-0.005	19.644	-0.607	-0.607	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.806	-0.859	22.119	-11.539	-11.539	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.923	-0.969	21.735	-12.944	-12.944	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.081	-0.047	22.385	-0.354	-0.354	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.777	0.882	15.616	17.837	17.837	0.000	0.000	0.000	0.000
80	A	80	HIS	0	-0.025	-0.020	19.909	-0.515	-0.515	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.009	0.002	13.877	-0.351	-0.351	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.013	-0.012	15.261	-0.968	-0.968	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.760	-0.869	16.298	-13.817	-13.817	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.035	-0.010	14.527	-1.112	-1.112	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.024	0.020	18.176	0.148	0.148	0.000	0.000	0.000	0.000
86	A	86	ASN	0	-0.004	-0.004	22.028	0.249	0.249	0.000	0.000	0.000	0.000
87	A	87	VAL	0	-0.014	0.007	19.841	-0.425	-0.425	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.943	0.969	22.769	12.403	12.403	0.000	0.000	0.000	0.000
89	A	89	THR	0	-0.049	-0.054	25.044	-0.445	-0.445	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.782	-0.884	27.543	-10.927	-10.927	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.868	-0.947	29.905	-9.896	-9.896	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.099	-0.047	30.381	0.548	0.548	0.000	0.000	0.000	0.000
93	A	93	GLY	0	-0.001	0.013	29.491	-0.026	-0.026	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.061	-0.038	24.374	-0.456	-0.456	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.034	0.030	22.620	0.181	0.181	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.838	0.900	18.601	15.845	15.845	0.000	0.000	0.000	0.000
97	A	97	GLY	0	0.003	0.011	18.823	0.644	0.644	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.064	-0.036	13.876	-1.368	-1.368	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.015	0.008	14.129	1.200	1.200	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.925	0.955	10.669	25.028	25.028	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.750	-0.848	11.754	-18.919	-18.919	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.030	0.008	11.291	-2.339	-2.339	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.038	-0.017	12.688	-0.050	-0.050	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.003	-0.001	9.461	-0.562	-0.562	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.846	0.957	7.306	25.850	25.850	0.000	0.000	0.000	0.000
109	A	109	PRO	0	-0.048	-0.026	8.924	-0.061	-0.061	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.033	-0.026	11.349	1.070	1.070	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.032	-0.008	5.659	0.116	0.116	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.003	-0.014	8.035	2.663	2.663	0.000	0.000	0.000	0.000
113	A	113	VAL	0	0.018	0.000	4.813	0.670	0.670	0.000	0.000	0.000	0.000
114	A	114	GLY	0	-0.015	-0.003	7.908	1.461	1.461	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.825	0.924	11.083	21.244	21.244	0.000	0.000	0.000	0.000
116	A	116	SER	0	0.017	-0.021	12.920	-0.450	-0.450	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.033	-0.012	12.770	-0.217	-0.217	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.012	-0.015	15.437	0.602	0.602	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.002	0.012	19.233	-0.382	-0.382	0.000	0.000	0.000	0.000
120	A	120	HIS	0	-0.034	-0.024	21.523	-0.092	-0.092	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.004	-0.013	25.036	0.013	0.013	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.005	0.014	28.471	0.343	0.343	0.000	0.000	0.000	0.000
123	A	123	GLN	0	-0.021	-0.011	27.723	-0.212	-0.212	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.729	-0.846	24.258	-12.208	-12.208	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.733	-0.847	27.400	-10.258	-10.258	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.027	-0.029	24.681	0.018	0.018	0.000	0.000	0.000	0.000
127	A	127	GLY	0	-0.012	0.008	27.215	-0.204	-0.204	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.726	0.849	27.655	11.345	11.345	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.003	0.009	32.356	0.245	0.245	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.936	-0.971	34.340	-8.277	-8.277	0.000	0.000	0.000	0.000
131	A	131	THR	0	-0.003	0.012	34.818	0.040	0.040	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.876	-0.947	34.443	-8.525	-8.525	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.838	-0.896	30.270	-10.269	-10.269	0.000	0.000	0.000	0.000
134	A	134	SER	0	-0.007	0.004	30.243	-0.452	-0.452	0.000	0.000	0.000	0.000
135	A	135	LEU	0	0.025	-0.013	28.870	-0.474	-0.474	0.000	0.000	0.000	0.000
136	A	136	LYS	1	0.776	0.884	27.100	9.341	9.341	0.000	0.000	0.000	0.000
137	A	137	THR	0	-0.004	-0.054	25.591	-0.498	-0.498	0.000	0.000	0.000	0.000
138	A	138	GLY	0	-0.002	0.015	26.532	-0.242	-0.242	0.000	0.000	0.000	0.000
139	A	139	ASN	0	-0.041	-0.035	28.319	0.245	0.245	0.000	0.000	0.000	0.000
140	A	140	ALA	0	0.023	0.023	26.166	0.139	0.139	0.000	0.000	0.000	0.000
141	A	141	GLY	0	0.018	0.015	28.108	0.013	0.013	0.000	0.000	0.000	0.000
142	A	142	PRO	0	-0.015	-0.017	27.832	-0.353	-0.353	0.000	0.000	0.000	0.000
143	A	143	ARG	1	0.862	0.929	22.922	12.076	12.076	0.000	0.000	0.000	0.000
144	A	144	PRO	0	-0.014	0.004	25.419	0.065	0.065	0.000	0.000	0.000	0.000
145	A	145	ALA	0	0.036	0.016	22.027	0.081	0.081	0.000	0.000	0.000	0.000
146	A	147	GLY	0	0.035	0.022	16.081	0.323	0.323	0.000	0.000	0.000	0.000
147	A	148	VAL	0	-0.020	0.009	12.837	-0.595	-0.595	0.000	0.000	0.000	0.000
148	A	149	ILE	0	-0.028	-0.011	7.726	-0.621	-0.621	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.021	0.021	9.124	-0.061	-0.061	0.000	0.000	0.000	0.000
151	A	152	THR	0	-0.080	-0.050	5.202	5.855	5.855	0.000	0.000	0.000	0.000

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