FMO DATABASE

FMODB ID: 2R4JR

Calculation Name: 3RF4-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 5-(aminosulfonyl)-4-chloro-2-[(2-furylmethyl)amino]benzoic acid | imidazole | acetate ion

Ligand 3-letter code: FUN | IMD | ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3RF4

Chain ID: A

ChEMBL ID:

UniProt ID: A4GRE3

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-892671.299873
FMO2-HF: Nuclear repulsion	848147.036743
FMO2-HF: Total energy	-44524.263131
FMO2-MP2: Total energy	-44654.830045

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:PRO)

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

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.
-86.29	-79.895	26.887	-13.233	-20.048	-0.133

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.769 / q_NPA : 0.865

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	VAL	0	0.015	0.011	3.197	2.802	4.296	0.024	-0.498	-1.019	0.000
26	A	26	LEU	0	0.001	-0.010	3.559	-1.099	-0.677	0.010	-0.082	-0.349	0.000
27	A	27	ALA	0	-0.015	-0.007	4.539	-3.522	-3.369	-0.001	-0.016	-0.136	0.000
30	A	30	MET	0	-0.057	-0.038	2.967	-3.974	-4.591	3.664	-0.721	-2.326	-0.008
32	A	32	LYS	1	0.843	0.923	2.426	48.314	49.031	2.751	-0.737	-2.731	-0.003
33	A	33	PRO	0	0.032	0.011	4.362	2.190	2.307	-0.001	-0.014	-0.101	0.000
34	A	34	ARG	1	0.903	0.914	4.674	17.812	17.896	-0.001	-0.003	-0.080	0.000
36	A	36	ARG	1	0.893	0.940	3.742	39.892	40.391	0.003	-0.166	-0.336	-0.001
37	A	37	ILE	0	0.004	0.014	1.894	-41.835	-42.351	12.546	-5.462	-6.568	-0.065
38	A	38	ALA	0	-0.006	0.013	3.307	11.466	11.954	0.043	-0.004	-0.528	-0.001
39	A	39	ILE	0	-0.009	-0.017	5.102	-4.279	-4.276	-0.001	-0.016	0.015	0.000
61	A	61	VAL	0	0.034	0.011	3.601	-2.081	-1.914	0.003	-0.036	-0.134	0.000
62	A	62	GLU	-1	-0.860	-0.920	4.388	-34.358	-34.086	-0.001	-0.130	-0.142	0.000
63	A	63	SER	0	-0.038	-0.058	2.166	-33.919	-31.053	7.809	-5.416	-5.259	-0.054
64	A	64	ILE	0	0.028	0.052	3.298	9.004	9.133	0.040	0.072	-0.242	-0.001
66	A	66	ALA	0	-0.024	-0.005	4.786	-6.563	-6.446	-0.001	-0.004	-0.112	0.000
4	A	4	ARG	1	0.973	1.009	5.820	23.912	23.912	0.000	0.000	0.000	0.000
5	A	5	VAL	0	-0.002	-0.007	9.611	0.981	0.981	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.005	0.010	11.878	0.778	0.778	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.014	-0.034	15.586	0.314	0.314	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.020	-0.005	18.661	-0.127	-0.127	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.014	0.018	20.175	0.717	0.717	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.002	-0.011	21.997	-0.385	-0.385	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.863	-0.944	20.218	-14.854	-14.854	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.806	0.884	21.291	10.943	10.943	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.836	-0.900	22.677	-11.492	-11.492	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.003	0.004	15.931	-0.405	-0.405	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.033	0.002	17.651	0.210	0.210	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.070	0.013	17.342	-0.872	-0.872	0.000	0.000	0.000	0.000
17	A	17	ASN	0	0.002	0.002	16.101	-0.628	-0.628	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.027	0.006	11.604	-0.799	-0.799	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.810	-0.925	10.349	-22.288	-22.288	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.842	-0.861	9.828	-24.431	-24.431	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.943	0.957	10.995	15.805	15.805	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.012	0.010	7.366	-0.423	-0.423	0.000	0.000	0.000	0.000
23	A	23	THR	0	0.004	-0.026	6.205	-4.690	-4.690	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.883	-0.938	6.949	-27.182	-27.182	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.044	-0.008	8.679	-0.736	-0.736	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.847	-0.907	5.903	-20.841	-20.841	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.017	-0.029	7.177	2.441	2.441	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.002	0.016	5.488	-0.816	-0.816	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.011	-0.006	6.320	-4.380	-4.380	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.901	-0.943	7.590	-23.279	-23.279	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.038	0.007	10.857	-0.424	-0.424	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.068	-0.031	13.632	1.050	1.050	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.035	0.025	16.667	0.189	0.189	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.007	-0.002	19.324	0.265	0.265	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.011	0.003	17.738	0.352	0.352	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.936	0.945	22.129	11.149	11.149	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.009	0.025	18.492	-0.074	-0.074	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.083	-0.043	22.789	0.651	0.651	0.000	0.000	0.000	0.000
49	A	49	HIS	0	0.060	0.043	22.306	-0.397	-0.397	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.054	0.030	24.343	0.273	0.273	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.007	0.002	27.350	0.359	0.359	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.003	0.009	27.916	0.012	0.012	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.974	0.963	26.814	9.999	9.999	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.011	0.014	27.089	0.014	0.014	0.000	0.000	0.000	0.000
55	A	55	PRO	0	0.014	0.013	23.499	-0.299	-0.299	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.003	-0.007	19.361	0.131	0.131	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.022	0.034	15.176	-0.127	-0.127	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.045	-0.025	14.911	0.175	0.175	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.001	-0.007	8.960	-0.444	-0.444	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.875	0.940	9.091	22.285	22.285	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.059	0.028	5.866	-1.546	-1.546	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.004	0.006	4.970	-1.534	-1.534	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.012	-0.003	8.140	2.604	2.604	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.014	-0.004	11.798	-0.542	-0.542	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.853	-0.936	14.367	-16.870	-16.870	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.832	-0.880	8.994	-25.289	-25.289	0.000	0.000	0.000	0.000
72	A	72	ASN	0	0.025	-0.002	9.281	-2.533	-2.533	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.002	0.028	11.168	0.429	0.429	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.809	0.900	9.134	25.136	25.136	0.000	0.000	0.000	0.000
75	A	75	HIS	0	-0.011	0.005	7.019	0.944	0.944	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.026	0.004	10.197	0.255	0.255	0.000	0.000	0.000	0.000
77	A	77	GLN	0	-0.033	0.004	12.817	0.449	0.449	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.830	0.901	10.808	22.098	22.098	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.035	0.015	7.585	0.546	0.546	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.029	-0.028	12.096	0.853	0.853	0.000	0.000	0.000	0.000
81	A	81	GLN	0	-0.055	-0.031	15.527	0.922	0.922	0.000	0.000	0.000	0.000
82	A	82	PHE	0	0.049	0.025	12.366	0.749	0.749	0.000	0.000	0.000	0.000
83	A	83	CYS	0	-0.034	-0.009	13.846	0.267	0.267	0.000	0.000	0.000	0.000
84	A	84	GLN	0	-0.017	-0.006	16.519	0.491	0.491	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.847	-0.917	18.154	-14.304	-14.304	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.138	-0.079	16.170	0.617	0.617	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.019	0.007	15.696	0.628	0.628	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.843	0.922	19.677	13.506	13.506	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.016	0.010	17.870	0.556	0.556	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.012	-0.005	21.652	-0.125	-0.125	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.992	0.992	20.231	13.061	13.061	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.889	-0.940	20.039	-12.545	-12.545	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.796	0.888	20.861	12.406	12.406	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.043	0.014	14.378	-0.394	-0.394	0.000	0.000	0.000	0.000
95	A	95	ILE	0	-0.021	-0.005	15.869	0.060	0.060	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.024	0.015	9.609	-0.641	-0.641	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.069	-0.027	10.855	1.575	1.575	0.000	0.000	0.000	0.000
98	A	98	TYR	0	0.035	-0.004	6.861	-2.321	-2.321	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.014	-0.014	7.263	3.353	3.353	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.830	-0.920	6.707	-35.996	-35.996	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.031	-0.010	5.499	2.915	2.915	0.000	0.000	0.000	0.000
102	A	102	GLN	0	0.055	0.011	8.531	-1.397	-1.397	0.000	0.000	0.000	0.000
103	A	103	PRO	0	0.017	-0.002	9.051	-1.047	-1.047	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.010	-0.002	10.079	0.154	0.154	0.000	0.000	0.000	0.000
105	A	105	HIS	0	-0.011	-0.006	10.824	0.900	0.900	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.002	0.010	5.751	-1.347	-1.347	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.026	0.020	9.090	1.649	1.649	0.000	0.000	0.000	0.000
108	A	108	PHE	0	-0.035	-0.040	8.133	-3.184	-3.184	0.000	0.000	0.000	0.000
109	A	109	ASN	0	-0.032	-0.016	10.226	1.786	1.786	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.023	0.016	13.123	1.152	1.152	0.000	0.000	0.000	0.000
111	A	111	THR	0	0.016	0.025	13.911	1.362	1.362	0.000	0.000	0.000	0.000
112	A	112	THR	0	0.012	0.001	12.162	-1.677	-1.677	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.024	-0.018	6.940	0.087	0.087	0.000	0.000	0.000	0.000
114	A	114	ALA	0	-0.060	-0.038	10.268	0.427	0.427	0.000	0.000	0.000	0.000
115	A	115	ALA	0	-0.057	-0.023	13.093	1.311	1.311	0.000	0.000	0.000	0.000
116	A	116	ALA	-1	-0.939	-0.946	12.661	-18.708	-18.708	0.000	0.000	0.000	0.000

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