FMO DATABASE

FMODB ID: Y1KK2

Calculation Name: 1A70-A-Xray547

Preferred Name:

Target Type:

Ligand Name: fe2/s2 (inorganic) cluster

Ligand 3-letter code: FES

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1A70

Chain ID: A

ChEMBL ID:

UniProt ID: P00221

Base Structure: X-ray

Registration Date: 2025-10-05

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	97
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-676995.846581
FMO2-HF: Nuclear repulsion	639192.454765
FMO2-HF: Total energy	-37803.391815
FMO2-MP2: Total energy	-37910.54897

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:ALA)

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

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.
-372.308	-367.553	17.514	-13.02	-9.252	-0.15

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.713 / q_NPA : 0.837

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	TYR	0	-0.040	-0.004	2.834	-5.236	-2.002	0.178	-1.497	-1.916	-0.012
19	A	19	PRO	0	0.011	0.002	4.837	-7.311	-7.229	-0.001	-0.038	-0.043	0.000
20	A	20	ASP	-1	-0.823	-0.908	1.821	-140.040	-138.811	17.338	-11.456	-7.112	-0.138
21	A	21	ASP	-1	-0.929	-0.960	4.399	-38.981	-38.771	-0.001	-0.029	-0.181	0.000
4	A	4	LYS	1	0.842	0.915	6.330	24.647	24.647	0.000	0.000	0.000	0.000
5	A	5	VAL	0	0.013	0.010	10.068	0.221	0.221	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.017	-0.012	12.226	1.429	1.429	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.008	0.006	15.880	0.163	0.163	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.005	-0.011	18.497	0.594	0.594	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.023	-0.001	22.015	0.343	0.343	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.000	-0.014	24.223	0.338	0.338	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.032	-0.011	26.596	0.503	0.503	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.026	-0.004	26.142	0.213	0.213	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.026	-0.005	21.460	-0.159	-0.159	0.000	0.000	0.000	0.000
14	A	14	VAL	0	0.012	0.012	18.677	0.379	0.379	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.875	-0.925	15.668	-18.933	-18.933	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.033	0.017	12.291	0.801	0.801	0.000	0.000	0.000	0.000
17	A	17	GLN	0	-0.031	-0.024	7.653	1.258	1.258	0.000	0.000	0.000	0.000
18	A	18	CYS	0	0.013	0.012	8.098	3.055	3.055	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.007	-0.005	6.828	5.028	5.028	0.000	0.000	0.000	0.000
23	A	23	TYR	0	-0.068	-0.047	9.392	-1.081	-1.081	0.000	0.000	0.000	0.000
24	A	24	ILE	0	0.002	-0.018	11.416	0.427	0.427	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.050	-0.017	13.178	0.823	0.823	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.818	-0.907	13.955	-19.353	-19.353	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.064	0.016	11.482	0.468	0.468	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.039	-0.010	13.600	0.522	0.522	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.803	-0.876	16.543	-14.806	-14.806	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-1.011	-0.997	13.128	-22.198	-22.198	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.991	-0.993	14.404	-19.812	-19.812	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.069	-0.029	17.786	0.859	0.859	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.088	-0.047	17.757	0.903	0.903	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.963	-0.970	21.531	-12.491	-12.491	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.005	-0.014	18.666	0.018	0.018	0.000	0.000	0.000	0.000
36	A	36	PRO	0	-0.024	0.001	22.989	0.182	0.182	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.029	0.004	22.596	-0.385	-0.385	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.035	-0.049	24.613	0.508	0.508	0.000	0.000	0.000	0.000
39	A	39	CYS	0	-0.075	-0.021	25.192	-0.238	-0.238	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.753	0.829	18.455	16.022	16.022	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.040	0.014	20.536	-0.592	-0.592	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.083	0.037	20.690	0.210	0.210	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.029	0.018	21.277	0.158	0.158	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.063	-0.022	24.651	0.491	0.491	0.000	0.000	0.000	0.000
45	A	45	SER	0	0.098	0.049	24.763	-0.492	-0.492	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.048	-0.046	26.097	0.107	0.107	0.000	0.000	0.000	0.000
47	A	47	CYS	0	-0.027	0.043	20.981	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.035	0.035	21.342	-0.809	-0.809	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.009	-0.003	20.951	0.308	0.308	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.816	0.929	21.822	12.541	12.541	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.005	0.002	14.884	-0.263	-0.263	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.789	0.893	18.177	14.193	14.193	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.045	-0.041	15.494	0.641	0.641	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.062	0.041	12.777	-0.796	-0.796	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.051	-0.031	10.892	1.888	1.888	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.024	0.007	10.294	-2.453	-2.453	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.053	-0.016	10.237	1.927	1.927	0.000	0.000	0.000	0.000
58	A	58	GLN	0	0.053	-0.001	11.950	-0.021	-0.021	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.834	-0.908	14.108	-20.409	-20.409	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.858	-0.899	14.421	-20.430	-20.430	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.045	-0.023	17.171	1.205	1.205	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.063	-0.043	19.789	0.466	0.466	0.000	0.000	0.000	0.000
63	A	63	PHE	0	-0.072	-0.035	23.513	0.749	0.749	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.016	-0.002	21.449	0.432	0.432	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.854	-0.918	24.541	-11.599	-11.599	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.897	-0.971	23.692	-13.611	-13.611	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.902	-0.937	24.708	-11.144	-11.144	0.000	0.000	0.000	0.000
68	A	68	GLN	0	-0.019	-0.032	25.453	-0.441	-0.441	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.032	-0.020	19.493	-0.575	-0.575	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.930	-0.957	21.477	-13.899	-13.899	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.940	-0.974	23.619	-11.352	-11.352	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.032	-0.006	20.779	0.093	0.093	0.000	0.000	0.000	0.000
73	A	73	TRP	0	-0.069	-0.040	21.074	-0.474	-0.474	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.002	-0.008	16.465	-0.730	-0.730	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.003	-0.005	18.914	0.794	0.794	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.003	-0.030	16.711	-0.794	-0.794	0.000	0.000	0.000	0.000
77	A	77	CYS	0	-0.107	-0.071	16.193	-0.671	-0.671	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.037	0.029	16.056	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.011	0.010	13.589	-0.110	-0.110	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.006	0.017	7.910	-0.805	-0.805	0.000	0.000	0.000	0.000
81	A	81	PRO	0	-0.024	-0.009	6.418	2.185	2.185	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.013	-0.025	5.832	-6.084	-6.084	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.063	-0.042	6.515	-0.415	-0.415	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.841	-0.909	7.637	-33.160	-33.160	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.042	-0.008	9.561	1.755	1.755	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.028	-0.014	12.485	0.739	0.739	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.020	0.008	14.257	0.345	0.345	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.852	-0.908	18.155	-12.535	-12.535	0.000	0.000	0.000	0.000
89	A	89	THR	0	0.026	-0.013	19.859	-0.220	-0.220	0.000	0.000	0.000	0.000
90	A	90	HIS	0	0.015	0.006	22.461	0.311	0.311	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.819	0.913	24.697	12.230	12.230	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.911	0.982	26.705	10.678	10.678	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.907	-0.982	28.513	-10.008	-10.008	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.889	-0.924	29.120	-10.700	-10.700	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.043	-0.007	26.744	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.079	-0.043	29.846	0.443	0.443	0.000	0.000	0.000	0.000
97	A	97	ALA	-1	-0.888	-0.922	30.176	-10.261	-10.261	0.000	0.000	0.000	0.000

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