FMO DATABASE

FMODB ID: 874VY

Calculation Name: 5DS2-F-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5DS2

Chain ID: F

ChEMBL ID:

UniProt ID: P19243

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

Total energy (hartree)

FMO2-HF: Electronic energy	-646647.391694
FMO2-HF: Nuclear repulsion	608559.014506
FMO2-HF: Total energy	-38088.377187
FMO2-MP2: Total energy	-38200.238536

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:2:SER)

Summations of interaction energy for fragment #1(A:2: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.
26.586	28.72	0.136	-0.706	-1.565	0.004

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.858 / q_NPA : 0.915

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	4	ARG	1	0.967	0.991	3.852	48.335	49.514	-0.004	-0.382	-0.793	0.001
66	A	67	ARG	1	0.834	0.927	3.032	32.747	33.702	0.140	-0.324	-0.772	0.003
4	A	5	VAL	0	-0.001	-0.025	6.050	1.686	1.686	0.000	0.000	0.000	0.000
5	A	6	ASP	-1	-0.877	-0.903	8.303	-22.985	-22.985	0.000	0.000	0.000	0.000
6	A	7	TRP	0	-0.066	-0.059	11.637	-0.231	-0.231	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.941	0.979	13.598	14.879	14.879	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.761	-0.856	17.332	-12.804	-12.804	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.070	-0.038	20.392	0.270	0.270	0.000	0.000	0.000	0.000
10	A	11	PRO	0	0.025	0.004	23.806	-0.061	-0.061	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.851	-0.929	26.501	-10.725	-10.725	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.019	-0.014	22.365	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	14	HIS	0	0.035	0.042	17.847	-0.804	-0.804	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.052	-0.038	17.736	0.095	0.095	0.000	0.000	0.000	0.000
15	A	16	PHE	0	0.047	0.011	11.841	-0.458	-0.458	0.000	0.000	0.000	0.000
16	A	17	LYS	1	0.898	0.936	12.930	18.065	18.065	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.017	0.008	9.152	-1.548	-1.548	0.000	0.000	0.000	0.000
18	A	19	ASP	-1	-0.880	-0.929	8.631	-26.887	-26.887	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.058	-0.034	7.599	-5.218	-5.218	0.000	0.000	0.000	0.000
20	A	21	PRO	0	0.062	0.026	9.090	2.563	2.563	0.000	0.000	0.000	0.000
21	A	22	GLY	0	-0.023	-0.020	11.588	-1.180	-1.180	0.000	0.000	0.000	0.000
22	A	23	LEU	0	-0.029	0.019	10.011	-0.246	-0.246	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.875	0.927	14.115	15.855	15.855	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.924	0.930	16.287	13.737	13.737	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.875	-0.925	17.459	-14.669	-14.669	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.828	-0.914	14.622	-18.723	-18.723	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.075	-0.040	11.644	-1.721	-1.721	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.863	0.933	13.459	18.348	18.348	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.028	-0.025	13.468	-1.366	-1.366	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.819	-0.894	15.285	-16.478	-16.478	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.013	-0.018	16.120	-0.847	-0.847	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.905	-0.937	16.369	-17.021	-17.021	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.877	-0.947	18.854	-12.299	-12.299	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.889	-0.946	19.084	-13.919	-13.919	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.793	0.881	19.042	12.121	12.121	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.008	0.003	13.306	-0.780	-0.780	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.000	0.018	13.577	0.348	0.348	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.043	-0.037	11.390	-2.411	-2.411	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.004	-0.001	9.481	0.973	0.973	0.000	0.000	0.000	0.000
40	A	41	SER	0	-0.040	-0.027	9.015	-2.558	-2.558	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.082	0.032	9.752	1.803	1.803	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.944	-0.983	9.846	-25.850	-25.850	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.794	0.900	9.074	30.370	30.370	0.000	0.000	0.000	0.000
44	A	45	SER	0	0.024	0.013	11.175	-0.508	-0.508	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.004	-0.015	13.344	-1.077	-1.077	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.970	-0.975	15.653	-14.052	-14.052	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.805	0.884	18.989	12.155	12.155	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.798	-0.879	20.743	-14.377	-14.377	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.892	-0.936	23.069	-11.200	-11.200	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.860	0.909	26.781	9.848	9.848	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.055	-0.037	28.821	0.338	0.338	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.807	-0.873	24.144	-12.337	-12.337	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.946	-0.978	25.199	-11.212	-11.212	0.000	0.000	0.000	0.000
54	A	55	TRP	0	-0.104	-0.057	18.449	-0.594	-0.594	0.000	0.000	0.000	0.000
55	A	56	HIS	0	0.049	0.027	22.051	-0.166	-0.166	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.849	0.914	17.460	15.006	15.006	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.032	0.018	13.896	0.062	0.062	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.894	-0.946	12.426	-20.663	-20.663	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.895	0.951	10.173	18.276	18.276	0.000	0.000	0.000	0.000
60	A	61	SER	0	0.013	0.008	5.607	2.661	2.661	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.001	0.002	7.643	2.738	2.738	0.000	0.000	0.000	0.000
62	A	63	GLY	0	0.085	0.053	7.890	-3.186	-3.186	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.945	0.970	8.668	22.884	22.884	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.031	-0.009	4.922	-7.019	-7.019	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.000	-0.011	4.834	4.976	4.976	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.923	0.951	6.679	23.219	23.219	0.000	0.000	0.000	0.000
68	A	69	PHE	0	0.001	-0.006	7.868	-1.721	-1.721	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.866	0.958	11.777	14.364	14.364	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.002	-0.002	15.127	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	PRO	0	0.021	0.013	17.519	0.471	0.471	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.799	-0.923	20.537	-11.867	-11.867	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.030	-0.018	23.140	-0.068	-0.068	0.000	0.000	0.000	0.000
74	A	75	ALA	0	-0.004	0.020	21.091	0.191	0.191	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.843	0.899	23.042	10.321	10.321	0.000	0.000	0.000	0.000
76	A	77	MET	0	0.016	0.005	18.088	-0.171	-0.171	0.000	0.000	0.000	0.000
77	A	78	ASP	-1	-0.805	-0.887	22.521	-11.052	-11.052	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.799	0.888	24.602	10.466	10.466	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.010	0.004	18.420	-0.169	-0.169	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.954	0.988	21.096	12.966	12.966	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.056	0.020	17.344	-0.668	-0.668	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.072	-0.030	18.305	0.975	0.975	0.000	0.000	0.000	0.000
83	A	84	MET	0	0.018	0.002	13.865	-0.815	-0.815	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.874	-0.927	17.936	-12.862	-12.862	0.000	0.000	0.000	0.000
85	A	86	ASN	0	-0.034	-0.017	17.928	-0.716	-0.716	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.004	0.008	14.721	-0.618	-0.618	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.006	0.006	13.149	-1.945	-1.945	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.005	0.002	12.034	1.672	1.672	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.016	-0.006	14.086	-0.561	-0.561	0.000	0.000	0.000	0.000
90	A	91	VAL	0	0.013	0.003	14.357	0.798	0.798	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.067	-0.042	16.788	0.220	0.220	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.042	0.019	17.996	0.153	0.153	0.000	0.000	0.000	0.000
93	A	94	PRO	0	0.003	0.001	20.844	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	95	LYS	0	0.002	0.027	23.286	1.060	1.060	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)