FMO DATABASE

FMODB ID: KVKQ3

Calculation Name: 2FE5-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | glycerol

Ligand 3-letter code: SO4 | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FE5

Chain ID: A

ChEMBL ID:

UniProt ID: Q92796

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	94
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-618695.60014
FMO2-HF: Nuclear repulsion	583659.98504
FMO2-HF: Total energy	-35035.6151
FMO2-MP2: Total energy	-35137.365171

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:221:SER)

Summations of interaction energy for fragment #1(A:221:SER)

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.
-11.975	-10.745	-0.006	-0.478	-0.746	-0.001

Interaction energy analysis for fragmet #1(A:221:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.867 / q_NPA : 0.918

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	223	THR	0	0.054	0.028	3.832	-2.905	-1.675	-0.006	-0.478	-0.746	-0.001
4	A	224	ILE	0	-0.015	-0.004	5.957	4.813	4.813	0.000	0.000	0.000	0.000
5	A	225	MET	0	-0.002	0.002	8.053	0.611	0.611	0.000	0.000	0.000	0.000
6	A	226	GLU	-1	-0.839	-0.892	11.623	-19.556	-19.556	0.000	0.000	0.000	0.000
7	A	227	VAL	0	-0.041	-0.031	14.555	0.469	0.469	0.000	0.000	0.000	0.000
8	A	228	ASN	0	-0.003	-0.003	18.100	0.561	0.561	0.000	0.000	0.000	0.000
9	A	229	LEU	0	-0.002	0.005	21.106	0.264	0.264	0.000	0.000	0.000	0.000
10	A	230	LEU	0	0.050	0.016	24.013	0.198	0.198	0.000	0.000	0.000	0.000
11	A	231	LYS	1	0.794	0.888	27.781	10.898	10.898	0.000	0.000	0.000	0.000
12	A	232	GLY	0	0.039	0.017	29.524	0.082	0.082	0.000	0.000	0.000	0.000
13	A	233	PRO	0	0.002	-0.022	32.825	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	234	LYS	1	0.924	0.972	32.603	8.891	8.891	0.000	0.000	0.000	0.000
15	A	235	GLY	0	0.017	0.031	30.668	-0.120	-0.120	0.000	0.000	0.000	0.000
16	A	236	LEU	0	0.033	-0.002	24.097	-0.035	-0.035	0.000	0.000	0.000	0.000
17	A	237	GLY	0	0.014	0.018	26.025	-0.293	-0.293	0.000	0.000	0.000	0.000
18	A	238	PHE	0	0.011	0.008	21.486	-0.191	-0.191	0.000	0.000	0.000	0.000
19	A	239	SER	0	-0.065	-0.029	25.119	0.572	0.572	0.000	0.000	0.000	0.000
20	A	240	ILE	0	0.023	0.009	21.352	-0.551	-0.551	0.000	0.000	0.000	0.000
21	A	241	ALA	0	-0.001	0.016	22.040	0.784	0.784	0.000	0.000	0.000	0.000
22	A	242	GLY	0	0.070	0.039	20.097	-0.780	-0.780	0.000	0.000	0.000	0.000
23	A	243	GLY	0	0.053	0.021	19.942	0.771	0.771	0.000	0.000	0.000	0.000
24	A	244	ILE	0	-0.032	-0.022	21.255	0.282	0.282	0.000	0.000	0.000	0.000
25	A	245	GLY	0	-0.035	-0.022	22.917	0.499	0.499	0.000	0.000	0.000	0.000
26	A	246	ASN	0	-0.107	-0.053	24.075	0.776	0.776	0.000	0.000	0.000	0.000
27	A	247	GLN	0	0.000	0.005	20.706	-0.105	-0.105	0.000	0.000	0.000	0.000
28	A	248	HIS	0	-0.026	-0.008	17.716	1.118	1.118	0.000	0.000	0.000	0.000
29	A	249	ILE	0	0.022	0.013	15.036	0.211	0.211	0.000	0.000	0.000	0.000
30	A	250	PRO	0	-0.005	-0.010	18.893	-0.081	-0.081	0.000	0.000	0.000	0.000
31	A	251	GLY	0	0.008	0.006	18.411	-0.581	-0.581	0.000	0.000	0.000	0.000
32	A	252	ASP	-1	-0.822	-0.862	14.577	-22.321	-22.321	0.000	0.000	0.000	0.000
33	A	253	ASN	0	-0.003	-0.020	16.949	1.182	1.182	0.000	0.000	0.000	0.000
34	A	254	SER	0	-0.063	-0.042	13.726	-0.053	-0.053	0.000	0.000	0.000	0.000
35	A	255	ILE	0	-0.038	-0.008	16.035	0.935	0.935	0.000	0.000	0.000	0.000
36	A	256	TYR	0	0.004	-0.036	14.191	-1.617	-1.617	0.000	0.000	0.000	0.000
37	A	257	ILE	0	-0.023	-0.012	18.142	1.283	1.283	0.000	0.000	0.000	0.000
38	A	258	THR	0	0.012	-0.006	20.176	-0.270	-0.270	0.000	0.000	0.000	0.000
39	A	259	LYS	1	0.939	0.963	22.937	11.229	11.229	0.000	0.000	0.000	0.000
40	A	260	ILE	0	0.045	0.029	21.652	-0.155	-0.155	0.000	0.000	0.000	0.000
41	A	261	ILE	0	-0.075	-0.040	25.734	0.377	0.377	0.000	0.000	0.000	0.000
42	A	262	GLU	-1	-0.824	-0.906	29.358	-10.548	-10.548	0.000	0.000	0.000	0.000
43	A	263	GLY	0	-0.017	-0.013	31.633	0.266	0.266	0.000	0.000	0.000	0.000
44	A	264	GLY	0	-0.023	-0.018	29.432	0.161	0.161	0.000	0.000	0.000	0.000
45	A	265	ALA	0	-0.016	-0.007	26.862	-0.188	-0.188	0.000	0.000	0.000	0.000
46	A	266	ALA	0	0.014	-0.002	23.105	-0.239	-0.239	0.000	0.000	0.000	0.000
47	A	267	GLN	0	-0.024	-0.010	23.883	-0.215	-0.215	0.000	0.000	0.000	0.000
48	A	268	LYS	1	0.912	0.958	26.337	10.154	10.154	0.000	0.000	0.000	0.000
49	A	269	ASP	-1	-0.809	-0.872	21.204	-14.539	-14.539	0.000	0.000	0.000	0.000
50	A	270	GLY	0	0.025	0.018	22.436	-0.231	-0.231	0.000	0.000	0.000	0.000
51	A	271	ARG	1	0.799	0.870	17.215	14.982	14.982	0.000	0.000	0.000	0.000
52	A	272	LEU	0	-0.042	-0.011	17.073	-1.173	-1.173	0.000	0.000	0.000	0.000
53	A	273	GLN	0	0.029	0.013	16.340	-0.158	-0.158	0.000	0.000	0.000	0.000
54	A	274	ILE	0	-0.025	-0.012	18.604	-0.377	-0.377	0.000	0.000	0.000	0.000
55	A	275	GLY	0	0.030	0.015	17.011	-0.304	-0.304	0.000	0.000	0.000	0.000
56	A	276	ASP	-1	-0.794	-0.871	14.252	-22.593	-22.593	0.000	0.000	0.000	0.000
57	A	277	ARG	1	0.884	0.942	8.261	32.834	32.834	0.000	0.000	0.000	0.000
58	A	278	LEU	0	-0.021	-0.014	13.711	-1.008	-1.008	0.000	0.000	0.000	0.000
59	A	279	LEU	0	-0.001	-0.007	9.319	0.037	0.037	0.000	0.000	0.000	0.000
60	A	280	ALA	0	-0.021	-0.018	13.939	0.571	0.571	0.000	0.000	0.000	0.000
61	A	281	VAL	0	0.026	0.021	16.628	-0.096	-0.096	0.000	0.000	0.000	0.000
62	A	282	ASN	0	0.005	-0.011	20.067	0.290	0.290	0.000	0.000	0.000	0.000
63	A	283	ASN	0	0.018	-0.001	18.972	-1.043	-1.043	0.000	0.000	0.000	0.000
64	A	284	THR	0	-0.029	0.002	20.025	0.013	0.013	0.000	0.000	0.000	0.000
65	A	285	ASN	0	-0.025	-0.031	14.113	-0.357	-0.357	0.000	0.000	0.000	0.000
66	A	286	LEU	0	-0.006	-0.017	16.802	0.996	0.996	0.000	0.000	0.000	0.000
67	A	287	GLN	0	0.000	0.000	10.663	0.164	0.164	0.000	0.000	0.000	0.000
68	A	288	ASP	-1	-0.854	-0.919	15.205	-16.423	-16.423	0.000	0.000	0.000	0.000
69	A	289	VAL	0	0.006	0.017	17.986	0.601	0.601	0.000	0.000	0.000	0.000
70	A	290	ARG	1	0.861	0.910	21.413	10.784	10.784	0.000	0.000	0.000	0.000
71	A	291	HIS	0	-0.013	-0.011	23.807	0.029	0.029	0.000	0.000	0.000	0.000
72	A	292	GLU	-1	-0.779	-0.880	24.946	-11.079	-11.079	0.000	0.000	0.000	0.000
73	A	293	GLU	-1	-0.857	-0.922	24.778	-12.051	-12.051	0.000	0.000	0.000	0.000
74	A	294	ALA	0	0.019	0.014	21.952	-0.045	-0.045	0.000	0.000	0.000	0.000
75	A	295	VAL	0	-0.032	-0.022	23.612	0.061	0.061	0.000	0.000	0.000	0.000
76	A	296	ALA	0	0.004	-0.004	26.707	0.205	0.205	0.000	0.000	0.000	0.000
77	A	297	SER	0	0.002	0.004	22.457	0.309	0.309	0.000	0.000	0.000	0.000
78	A	298	LEU	0	-0.007	-0.005	21.975	0.056	0.056	0.000	0.000	0.000	0.000
79	A	299	LYS	1	0.869	0.935	25.546	10.968	10.968	0.000	0.000	0.000	0.000
80	A	300	ASN	0	-0.012	0.009	28.003	0.533	0.533	0.000	0.000	0.000	0.000
81	A	301	THR	0	-0.017	-0.004	24.915	-0.030	-0.030	0.000	0.000	0.000	0.000
82	A	302	SER	0	0.033	0.016	28.276	0.273	0.273	0.000	0.000	0.000	0.000
83	A	303	ASP	-1	-0.858	-0.931	29.309	-10.195	-10.195	0.000	0.000	0.000	0.000
84	A	304	MET	0	-0.014	0.005	25.020	-0.209	-0.209	0.000	0.000	0.000	0.000
85	A	305	VAL	0	-0.045	-0.026	22.505	0.063	0.063	0.000	0.000	0.000	0.000
86	A	306	TYR	0	-0.039	-0.030	14.465	-0.292	-0.292	0.000	0.000	0.000	0.000
87	A	307	LEU	0	0.000	0.000	18.296	0.155	0.155	0.000	0.000	0.000	0.000
88	A	308	LYS	1	0.929	0.982	10.946	21.464	21.464	0.000	0.000	0.000	0.000
89	A	309	VAL	0	0.035	0.007	12.847	0.383	0.383	0.000	0.000	0.000	0.000
90	A	310	ALA	0	-0.014	-0.008	8.783	-2.127	-2.127	0.000	0.000	0.000	0.000
91	A	311	LYS	1	0.811	0.877	9.809	23.534	23.534	0.000	0.000	0.000	0.000
92	A	312	PRO	0	0.022	0.003	9.842	-2.993	-2.993	0.000	0.000	0.000	0.000
93	A	313	GLY	0	-0.047	-0.030	7.524	-2.230	-2.230	0.000	0.000	0.000	0.000
94	A	314	SER	-1	-0.945	-0.942	7.744	-28.306	-28.306	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:221:SER)