FMO DATABASE

FMODB ID: 3M5RL

Calculation Name: 6AAF-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6AAF

Chain ID: A

ChEMBL ID:

UniProt ID: O94272

Base Structure: X-ray

Registration Date: 2025-10-06

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-948437.780369
FMO2-HF: Nuclear repulsion	903068.334811
FMO2-HF: Total energy	-45369.445558
FMO2-MP2: Total energy	-45503.859371

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:ARG)

Summations of interaction energy for fragment #1(A:2:ARG)

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.
-212.736	-217.434	34.019	-16.226	-13.094	-0.168

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.693 / q_NPA : 1.804

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	GLN	0	0.031	0.004	2.796	-17.484	-14.854	0.345	-1.245	-1.730	-0.010
4	A	5	PHE	0	-0.022	-0.021	5.107	4.160	4.282	-0.001	-0.004	-0.117	0.000
5	A	6	LYS	1	0.835	0.904	3.622	76.127	76.685	0.008	-0.078	-0.488	0.000
6	A	7	ASP	-1	-0.831	-0.874	1.693	-199.003	-207.347	33.660	-14.740	-10.575	-0.157
7	A	8	ASP	-1	-0.838	-0.905	3.550	-53.141	-52.805	0.007	-0.159	-0.184	-0.001
8	A	9	PHE	0	-0.027	-0.008	6.395	8.109	8.109	0.000	0.000	0.000	0.000
9	A	10	SER	0	0.061	0.028	6.420	-5.371	-5.371	0.000	0.000	0.000	0.000
10	A	11	PHE	0	0.037	0.003	7.959	1.759	1.759	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.880	-0.936	9.423	-33.465	-33.465	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.907	0.974	11.118	41.747	41.747	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.816	0.903	5.314	69.573	69.573	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.977	0.994	11.735	35.817	35.817	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.001	-0.008	14.361	2.452	2.452	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.874	-0.926	14.744	-29.920	-29.920	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.055	-0.063	15.012	2.427	2.427	0.000	0.000	0.000	0.000
18	A	19	GLN	0	-0.032	-0.013	16.951	0.280	0.280	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.894	0.935	19.673	29.561	29.561	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.062	-0.035	19.060	1.271	1.271	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.861	0.905	20.241	27.657	27.657	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.879	-0.927	22.734	-23.540	-23.540	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.872	0.953	24.687	23.707	23.707	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.024	-0.023	23.781	0.770	0.770	0.000	0.000	0.000	0.000
25	A	26	PRO	0	0.085	0.057	25.018	-0.884	-0.884	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.832	-0.901	26.284	-22.675	-22.675	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.787	0.889	22.977	23.148	23.148	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.029	0.030	17.700	-0.300	-0.300	0.000	0.000	0.000	0.000
29	A	30	PRO	0	-0.039	-0.009	16.363	-0.096	-0.096	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.010	0.001	13.982	-1.631	-1.631	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.045	-0.014	9.020	1.075	1.075	0.000	0.000	0.000	0.000
32	A	33	CYS	0	-0.031	-0.023	11.120	-1.013	-1.013	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.762	-0.866	6.657	-77.056	-77.056	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.835	0.916	8.922	41.909	41.909	0.000	0.000	0.000	0.000
35	A	36	VAL	0	-0.004	-0.011	6.610	-7.471	-7.471	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.903	-0.944	5.123	-67.164	-67.164	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.873	0.916	7.272	62.235	62.235	0.000	0.000	0.000	0.000
38	A	39	SER	0	0.042	0.028	10.219	3.685	3.685	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.865	-0.919	12.263	-30.195	-30.195	0.000	0.000	0.000	0.000
40	A	41	ILE	0	-0.024	-0.014	15.283	0.148	0.148	0.000	0.000	0.000	0.000
41	A	42	ALA	0	0.039	0.021	15.286	-1.891	-1.891	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.028	0.025	13.549	-1.494	-1.494	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.035	-0.014	15.185	2.168	2.168	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.769	-0.871	15.615	-32.312	-32.312	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.810	0.915	16.516	28.874	28.874	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.962	0.992	8.547	60.781	60.781	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.946	0.987	13.742	35.554	35.554	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.028	-0.032	15.528	3.825	3.825	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.038	0.030	18.333	-0.885	-0.885	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.014	0.021	18.960	1.532	1.532	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.017	-0.001	21.885	-0.407	-0.407	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.010	-0.015	23.662	-0.317	-0.317	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.872	-0.936	24.696	-21.672	-21.672	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.026	0.004	23.083	0.392	0.392	0.000	0.000	0.000	0.000
55	A	56	THR	0	0.025	-0.009	24.412	-0.755	-0.755	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.026	0.010	18.786	-0.510	-0.510	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.002	-0.006	20.968	-0.631	-0.631	0.000	0.000	0.000	0.000
58	A	59	GLN	0	0.020	0.030	23.341	-0.342	-0.342	0.000	0.000	0.000	0.000
59	A	60	PHE	0	0.039	0.013	15.774	0.067	0.067	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.030	0.013	18.245	-0.566	-0.566	0.000	0.000	0.000	0.000
61	A	62	TYR	0	0.002	-0.001	20.317	0.155	0.155	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.008	-0.007	21.458	0.247	0.247	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.026	0.008	15.932	0.122	0.122	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.851	0.936	19.720	24.548	24.548	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.910	0.960	21.696	21.461	21.461	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.800	0.895	19.976	28.502	28.502	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.011	-0.026	17.242	0.354	0.354	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.906	0.961	20.684	22.406	22.406	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.005	0.015	19.472	0.329	0.329	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.041	-0.041	22.844	0.346	0.346	0.000	0.000	0.000	0.000
71	A	72	PRO	0	-0.019	-0.022	24.966	-0.626	-0.626	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.797	-0.878	26.705	-21.468	-21.468	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.947	0.994	20.954	25.211	25.211	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.036	0.023	20.280	0.256	0.256	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.033	-0.034	15.795	-0.439	-0.439	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.046	0.001	15.038	1.214	1.214	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.003	-0.009	13.289	-2.016	-2.016	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.014	-0.005	9.783	1.474	1.474	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.006	-0.019	10.778	-2.126	-2.126	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.822	-0.885	9.083	-45.006	-45.006	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.955	-0.985	6.524	-65.818	-65.818	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.016	0.013	10.004	3.160	3.160	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.021	0.005	13.667	-1.007	-1.007	0.000	0.000	0.000	0.000
84	A	85	PRO	0	-0.030	0.003	14.978	1.545	1.545	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.045	0.015	17.973	0.708	0.708	0.000	0.000	0.000	0.000
86	A	87	THR	0	0.030	-0.011	21.724	0.139	0.139	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.015	0.005	23.067	0.078	0.078	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.007	0.021	22.146	0.579	0.579	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.028	0.014	23.627	-0.466	-0.466	0.000	0.000	0.000	0.000
90	A	91	MET	0	0.014	-0.008	17.552	-1.071	-1.071	0.000	0.000	0.000	0.000
91	A	92	SER	0	0.021	-0.007	20.494	-1.162	-1.162	0.000	0.000	0.000	0.000
92	A	93	THR	0	-0.014	-0.002	22.000	-0.399	-0.399	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.019	-0.005	16.666	-0.734	-0.734	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.037	-0.042	16.812	-1.241	-1.241	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.889	-0.945	17.965	-28.546	-28.546	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.947	-0.962	17.968	-29.206	-29.206	0.000	0.000	0.000	0.000
97	A	98	HIS	1	0.840	0.899	13.522	35.570	35.570	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.775	0.902	13.187	27.376	27.376	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.023	-0.010	9.707	-2.629	-2.629	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.813	-0.885	10.507	-49.611	-49.611	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.819	-0.895	9.357	-53.033	-53.033	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.029	0.037	12.465	1.549	1.549	0.000	0.000	0.000	0.000
103	A	104	PHE	0	-0.021	-0.012	11.590	2.491	2.491	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.030	0.025	12.764	-0.773	-0.773	0.000	0.000	0.000	0.000
105	A	106	TYR	0	-0.067	-0.067	7.586	-2.706	-2.706	0.000	0.000	0.000	0.000
106	A	107	ILE	0	-0.009	-0.002	9.885	2.176	2.176	0.000	0.000	0.000	0.000
107	A	108	THR	0	0.032	0.024	5.964	-4.078	-4.078	0.000	0.000	0.000	0.000
108	A	109	TYR	0	-0.042	-0.041	8.722	4.017	4.017	0.000	0.000	0.000	0.000
109	A	110	SER	0	0.026	-0.003	10.515	-3.082	-3.082	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.028	-0.030	12.571	1.922	1.922	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.984	-0.981	14.752	-29.280	-29.280	0.000	0.000	0.000	0.000
112	A	113	ASN	-1	-0.883	-0.920	13.130	-32.767	-32.767	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:ARG)