FMO DATABASE

FMODB ID: 241MR

Calculation Name: 2FE1-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion | manganese (ii) ion | chloride ion

Ligand 3-letter code: CA | MN | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FE1

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZZP3

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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1101765.380933
FMO2-HF: Nuclear repulsion	1051525.350004
FMO2-HF: Total energy	-50240.030928
FMO2-MP2: Total energy	-50389.05624

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
-135.232	-120.193	5.758	-7.297	-13.497	-0.067

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.822 / q_NPA : 0.914

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	LEU	0	-0.016	-0.001	2.312	-1.006	2.045	2.568	-1.618	-4.000	-0.015
4	A	4	VAL	0	-0.009	-0.004	4.048	3.578	3.809	0.003	-0.064	-0.170	0.000
26	A	26	ALA	0	-0.034	-0.023	2.565	-5.063	-4.558	0.632	-0.338	-0.799	-0.001
27	A	27	VAL	0	0.023	-0.005	3.069	-10.257	-9.269	0.498	-0.479	-1.007	-0.009
29	A	29	GLN	0	0.004	0.014	3.313	-1.128	-0.647	0.014	-0.058	-0.437	0.000
30	A	30	ALA	0	-0.045	-0.009	2.848	-27.500	-23.108	0.367	-2.399	-2.360	-0.023
31	A	31	GLN	0	-0.087	-0.035	2.211	-4.717	-1.674	1.176	-1.779	-2.440	-0.018
32	A	32	GLU	-1	-0.861	-0.957	3.810	-20.447	-20.022	0.007	-0.099	-0.334	-0.001
112	A	112	GLY	0	-0.034	-0.016	3.572	-6.153	-5.950	0.005	-0.041	-0.167	0.000
113	A	113	LYS	1	0.796	0.896	3.620	34.236	35.343	0.267	-0.258	-1.115	0.001
114	A	114	LEU	0	-0.025	-0.008	5.280	-2.663	-2.678	-0.001	-0.005	0.022	0.000
130	A	130	THR	-1	-0.896	-0.931	2.957	-26.408	-25.780	0.222	-0.159	-0.690	-0.001
5	A	5	VAL	0	0.029	0.020	7.138	-0.316	-0.316	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.703	-0.795	9.250	-17.741	-17.741	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.036	0.001	12.698	-0.103	-0.103	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.073	-0.054	13.835	0.415	0.415	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.033	0.003	9.816	0.196	0.196	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.007	-0.007	11.958	-0.098	-0.098	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.031	-0.011	13.708	0.413	0.413	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.022	0.020	13.271	0.465	0.465	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.051	-0.027	9.460	-0.646	-0.646	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.016	-0.012	14.039	0.284	0.284	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.030	0.026	16.843	0.626	0.626	0.000	0.000	0.000	0.000
16	A	16	PRO	0	-0.072	-0.054	17.913	-0.653	-0.653	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.918	-0.945	17.284	-12.522	-12.522	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.937	-0.955	16.840	-15.036	-15.036	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.795	0.878	12.039	17.459	17.459	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.001	0.002	11.109	0.106	0.106	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.897	-0.959	10.865	-19.696	-19.696	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.075	-0.050	7.532	-0.560	-0.560	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.027	0.020	6.307	-2.978	-2.978	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.822	-0.907	6.595	-22.882	-22.882	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.855	0.918	5.143	31.784	31.784	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.026	-0.009	5.560	-2.927	-2.927	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.014	0.020	5.744	-5.001	-5.001	0.000	0.000	0.000	0.000
34	A	34	HIS	1	0.774	0.869	6.476	41.738	41.738	0.000	0.000	0.000	0.000
35	A	35	THR	0	0.053	0.012	9.633	0.494	0.494	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.012	0.001	12.547	0.150	0.150	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.771	-0.892	15.907	-14.602	-14.602	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.079	-0.036	18.366	0.574	0.574	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.056	0.028	15.802	0.660	0.660	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.014	0.016	17.871	0.311	0.311	0.000	0.000	0.000	0.000
41	A	41	TYR	0	-0.033	-0.018	20.414	0.797	0.797	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.856	-0.912	18.396	-14.394	-14.394	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.031	0.019	17.351	0.491	0.491	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.060	0.043	20.629	0.471	0.471	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.039	-0.021	24.090	0.562	0.562	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.858	-0.946	22.204	-11.615	-11.615	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.043	0.053	23.759	0.453	0.453	0.000	0.000	0.000	0.000
48	A	48	TRP	0	0.015	-0.001	25.396	0.463	0.463	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.841	0.909	26.021	11.214	11.214	0.000	0.000	0.000	0.000
50	A	50	HIS	1	0.856	0.916	23.621	11.760	11.760	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.066	0.044	28.502	0.274	0.274	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.910	0.959	31.231	8.998	8.998	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.874	0.939	27.826	9.928	9.928	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.006	0.010	33.429	0.113	0.113	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.081	-0.039	28.497	0.027	0.027	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.009	0.013	26.621	-0.213	-0.213	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.849	0.907	31.257	9.234	9.234	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.908	-0.960	32.271	-8.502	-8.502	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.868	-0.924	32.437	-8.744	-8.744	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.893	-0.921	29.391	-9.694	-9.694	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.051	0.005	27.866	-0.358	-0.358	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.034	-0.025	27.633	-0.325	-0.325	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.015	-0.013	28.338	-0.266	-0.266	0.000	0.000	0.000	0.000
64	A	64	MET	0	0.039	0.025	23.596	-0.147	-0.147	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.029	-0.014	23.450	-0.595	-0.595	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.920	-0.956	24.126	-11.445	-11.445	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.934	-0.973	21.703	-13.002	-13.002	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.037	-0.014	18.276	-0.863	-0.863	0.000	0.000	0.000	0.000
69	A	69	TRP	0	-0.026	-0.010	19.500	-0.949	-0.949	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.817	-0.907	20.992	-13.761	-13.761	0.000	0.000	0.000	0.000
71	A	71	PHE	0	0.011	0.012	12.204	-0.837	-0.837	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.014	-0.020	15.916	-1.384	-1.384	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.751	0.867	16.744	13.025	13.025	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.045	-0.012	13.895	-0.322	-0.322	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.046	-0.011	11.027	-2.497	-2.497	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.905	0.964	11.336	27.379	27.379	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.021	-0.012	12.764	-0.718	-0.718	0.000	0.000	0.000	0.000
78	A	78	HIS	0	-0.014	-0.012	11.864	-1.665	-1.665	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.011	-0.018	15.671	1.010	1.010	0.000	0.000	0.000	0.000
80	A	80	TYR	0	0.054	0.000	18.513	-0.283	-0.283	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.043	-0.021	20.603	0.063	0.063	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.860	-0.897	15.703	-19.389	-19.389	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.067	0.022	14.914	-0.434	-0.434	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.020	0.003	18.152	0.319	0.319	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.926	0.954	21.546	12.294	12.294	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.839	-0.917	17.760	-15.119	-15.119	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.011	0.013	18.679	0.117	0.117	0.000	0.000	0.000	0.000
88	A	88	PHE	0	-0.015	-0.014	19.599	0.412	0.412	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.001	0.001	21.502	0.366	0.366	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.011	0.000	15.843	0.496	0.496	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.009	-0.001	20.201	0.194	0.194	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.050	-0.028	22.510	0.397	0.397	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.854	0.936	20.148	13.500	13.500	0.000	0.000	0.000	0.000
94	A	94	HIS	0	0.027	0.011	18.440	0.140	0.140	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.016	0.022	22.239	0.061	0.061	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.048	-0.012	19.177	0.041	0.041	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.028	-0.037	21.345	0.312	0.312	0.000	0.000	0.000	0.000
98	A	98	VAL	0	0.018	-0.017	20.914	-0.449	-0.449	0.000	0.000	0.000	0.000
99	A	99	TYR	0	-0.007	-0.001	20.062	-0.339	-0.339	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.763	-0.867	17.146	-14.669	-14.669	0.000	0.000	0.000	0.000
101	A	101	ALA	0	-0.010	-0.004	15.945	-1.058	-1.058	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.010	-0.005	16.166	-0.665	-0.665	0.000	0.000	0.000	0.000
103	A	103	TYR	0	-0.030	-0.044	12.425	-1.320	-1.320	0.000	0.000	0.000	0.000
104	A	104	VAL	0	-0.010	0.002	11.379	-1.826	-1.826	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.043	0.013	11.836	-1.190	-1.190	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.033	-0.014	10.291	-0.587	-0.587	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.019	0.008	7.680	-1.945	-1.945	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.931	-0.974	8.064	-21.359	-21.359	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.799	0.903	10.471	19.040	19.040	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.075	-0.034	6.424	0.185	0.185	0.000	0.000	0.000	0.000
111	A	111	GLY	0	-0.013	0.003	6.926	-3.905	-3.905	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.027	0.019	5.733	0.895	0.895	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.019	-0.048	7.421	1.195	1.195	0.000	0.000	0.000	0.000
117	A	117	LEU	0	0.003	-0.005	11.155	-0.142	-0.142	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.869	-0.919	13.752	-13.139	-13.139	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.880	0.912	15.027	12.467	12.467	0.000	0.000	0.000	0.000
120	A	120	GLN	0	-0.001	0.004	16.601	0.112	0.112	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.004	-0.008	14.447	0.128	0.128	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.018	0.003	12.735	-0.437	-0.437	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.892	-0.942	13.857	-13.277	-13.277	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.813	0.916	16.847	12.634	12.634	0.000	0.000	0.000	0.000
125	A	125	PHE	0	-0.019	-0.008	13.075	0.315	0.315	0.000	0.000	0.000	0.000
126	A	126	PRO	0	0.053	0.032	11.858	-1.332	-1.332	0.000	0.000	0.000	0.000
127	A	127	ALA	0	-0.027	-0.011	10.702	-0.864	-0.864	0.000	0.000	0.000	0.000
128	A	128	LEU	0	-0.021	-0.012	8.148	-2.009	-2.009	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.003	0.017	7.956	-1.467	-1.467	0.000	0.000	0.000	0.000

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