FMO DATABASE

FMODB ID: 55R8Z

Calculation Name: 2FQL-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FQL

Chain ID: A

ChEMBL ID:

UniProt ID: Q07540

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

Total energy (hartree)

FMO2-HF: Electronic energy	-826483.591869
FMO2-HF: Nuclear repulsion	782827.326411
FMO2-HF: Total energy	-43656.265457
FMO2-MP2: Total energy	-43785.023537

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:61:VAL)

Summations of interaction energy for fragment #1(A:61:VAL)

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.
-110.136	-109.393	0.07	-0.051	-0.763	-0.002

Interaction energy analysis for fragmet #1(A:61:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / q_NPA : 0.902

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	63	GLN	0	0.077	0.018	3.243	-2.179	-1.436	0.070	-0.051	-0.763	-0.002
4	A	64	GLU	-1	-0.995	-0.993	6.388	-23.793	-23.793	0.000	0.000	0.000	0.000
5	A	65	VAL	0	0.032	0.023	6.762	1.188	1.188	0.000	0.000	0.000	0.000
6	A	66	LEU	0	-0.021	-0.010	6.182	2.596	2.596	0.000	0.000	0.000	0.000
7	A	67	ASN	0	-0.015	-0.006	9.336	0.826	0.826	0.000	0.000	0.000	0.000
8	A	68	LEU	0	0.001	0.016	12.027	2.182	2.182	0.000	0.000	0.000	0.000
9	A	69	PRO	0	-0.019	-0.014	14.240	-0.350	-0.350	0.000	0.000	0.000	0.000
10	A	70	LEU	0	-0.037	-0.010	10.103	0.063	0.063	0.000	0.000	0.000	0.000
11	A	71	GLU	-1	-0.895	-0.946	14.744	-15.112	-15.112	0.000	0.000	0.000	0.000
12	A	72	LYS	1	0.881	0.922	15.261	15.271	15.271	0.000	0.000	0.000	0.000
13	A	73	ALA	0	0.005	-0.017	16.949	0.809	0.809	0.000	0.000	0.000	0.000
14	A	74	HIS	1	0.857	0.924	19.059	13.380	13.380	0.000	0.000	0.000	0.000
15	A	75	GLU	-1	-0.866	-0.908	22.040	-12.903	-12.903	0.000	0.000	0.000	0.000
16	A	76	GLU	-1	-0.862	-0.937	23.652	-12.787	-12.787	0.000	0.000	0.000	0.000
17	A	77	ALA	0	-0.040	-0.034	26.582	0.479	0.479	0.000	0.000	0.000	0.000
18	A	78	ASP	-1	-0.839	-0.909	26.376	-11.330	-11.330	0.000	0.000	0.000	0.000
19	A	79	ASP	-1	-0.788	-0.866	26.128	-11.745	-11.745	0.000	0.000	0.000	0.000
20	A	80	TYR	0	-0.048	-0.048	29.355	0.363	0.363	0.000	0.000	0.000	0.000
21	A	81	LEU	0	-0.004	-0.019	32.039	0.318	0.318	0.000	0.000	0.000	0.000
22	A	82	ASP	-1	-0.906	-0.944	30.305	-10.053	-10.053	0.000	0.000	0.000	0.000
23	A	83	HIS	0	-0.085	-0.052	30.348	0.173	0.173	0.000	0.000	0.000	0.000
24	A	84	LEU	0	-0.050	-0.010	35.135	0.252	0.252	0.000	0.000	0.000	0.000
25	A	85	LEU	0	0.039	0.004	36.521	0.201	0.201	0.000	0.000	0.000	0.000
26	A	86	ASP	-1	-0.866	-0.919	36.232	-8.507	-8.507	0.000	0.000	0.000	0.000
27	A	87	SER	0	-0.066	-0.049	39.046	0.242	0.242	0.000	0.000	0.000	0.000
28	A	88	LEU	0	-0.062	-0.024	41.034	0.211	0.211	0.000	0.000	0.000	0.000
29	A	89	GLU	-1	-0.897	-0.964	40.361	-7.703	-7.703	0.000	0.000	0.000	0.000
30	A	90	GLU	-1	-1.005	-0.991	43.248	-7.044	-7.044	0.000	0.000	0.000	0.000
31	A	91	LEU	0	-0.016	-0.022	44.928	0.181	0.181	0.000	0.000	0.000	0.000
32	A	92	SER	0	-0.045	-0.016	46.794	0.195	0.195	0.000	0.000	0.000	0.000
33	A	93	GLU	-1	-0.947	-0.971	48.427	-6.408	-6.408	0.000	0.000	0.000	0.000
34	A	94	ALA	0	-0.069	-0.049	50.925	0.145	0.145	0.000	0.000	0.000	0.000
35	A	95	HIS	0	0.027	0.032	51.489	0.120	0.120	0.000	0.000	0.000	0.000
36	A	96	PRO	0	-0.038	-0.019	53.383	0.062	0.062	0.000	0.000	0.000	0.000
37	A	97	ASP	-1	-0.961	-0.991	55.869	-5.468	-5.468	0.000	0.000	0.000	0.000
38	A	98	CYS	0	-0.113	-0.044	54.431	-0.072	-0.072	0.000	0.000	0.000	0.000
39	A	99	ILE	0	-0.023	-0.035	48.329	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	100	PRO	0	-0.052	-0.028	49.954	-0.088	-0.088	0.000	0.000	0.000	0.000
41	A	101	ASP	-1	-0.868	-0.930	46.377	-6.935	-6.935	0.000	0.000	0.000	0.000
42	A	102	VAL	0	-0.031	-0.023	42.034	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	103	GLU	-1	-0.883	-0.913	41.340	-7.755	-7.755	0.000	0.000	0.000	0.000
44	A	104	LEU	0	-0.029	-0.026	34.112	-0.085	-0.085	0.000	0.000	0.000	0.000
45	A	105	SER	0	-0.018	0.005	36.637	-0.120	-0.120	0.000	0.000	0.000	0.000
46	A	106	HIS	0	0.003	-0.034	31.730	-0.331	-0.331	0.000	0.000	0.000	0.000
47	A	107	GLY	0	-0.014	0.010	31.591	-0.076	-0.076	0.000	0.000	0.000	0.000
48	A	108	VAL	0	-0.053	-0.025	32.389	0.019	0.019	0.000	0.000	0.000	0.000
49	A	109	MET	0	0.033	0.020	36.119	0.072	0.072	0.000	0.000	0.000	0.000
50	A	110	THR	0	-0.068	-0.036	38.670	0.124	0.124	0.000	0.000	0.000	0.000
51	A	111	LEU	0	0.041	0.024	42.470	-0.038	-0.038	0.000	0.000	0.000	0.000
52	A	112	GLU	-1	-0.869	-0.931	45.517	-6.541	-6.541	0.000	0.000	0.000	0.000
53	A	113	ILE	0	0.015	0.001	48.086	0.040	0.040	0.000	0.000	0.000	0.000
54	A	114	PRO	0	0.009	0.000	51.363	0.066	0.066	0.000	0.000	0.000	0.000
55	A	115	ALA	0	-0.033	-0.001	54.631	0.099	0.099	0.000	0.000	0.000	0.000
56	A	116	PHE	0	-0.042	-0.035	51.453	0.090	0.090	0.000	0.000	0.000	0.000
57	A	117	GLY	0	-0.048	-0.019	52.343	0.034	0.034	0.000	0.000	0.000	0.000
58	A	118	THR	0	-0.030	-0.006	47.916	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	119	TYR	0	-0.023	-0.035	43.980	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	120	VAL	0	-0.022	-0.011	40.026	-0.065	-0.065	0.000	0.000	0.000	0.000
61	A	121	ILE	0	-0.017	-0.005	36.798	0.008	0.008	0.000	0.000	0.000	0.000
62	A	122	ASN	0	-0.023	-0.013	34.953	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	123	LYS	1	0.835	0.909	26.318	11.607	11.607	0.000	0.000	0.000	0.000
64	A	124	GLN	0	-0.036	-0.021	31.669	0.304	0.304	0.000	0.000	0.000	0.000
65	A	125	PRO	0	0.016	-0.004	28.729	-0.242	-0.242	0.000	0.000	0.000	0.000
66	A	126	PRO	0	0.051	0.011	26.461	0.355	0.355	0.000	0.000	0.000	0.000
67	A	127	ASN	0	-0.065	-0.017	29.751	0.270	0.270	0.000	0.000	0.000	0.000
68	A	128	LYS	1	0.889	0.933	31.710	8.609	8.609	0.000	0.000	0.000	0.000
69	A	129	GLN	0	0.016	0.030	25.896	0.191	0.191	0.000	0.000	0.000	0.000
70	A	130	ILE	0	0.069	0.054	31.250	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	131	TRP	0	-0.041	-0.038	33.690	0.201	0.201	0.000	0.000	0.000	0.000
72	A	132	LEU	0	0.054	0.023	37.008	-0.044	-0.044	0.000	0.000	0.000	0.000
73	A	133	ALA	0	-0.069	-0.038	40.418	0.097	0.097	0.000	0.000	0.000	0.000
74	A	134	SER	0	0.034	-0.006	43.617	0.051	0.051	0.000	0.000	0.000	0.000
75	A	135	PRO	0	-0.047	-0.013	46.386	0.053	0.053	0.000	0.000	0.000	0.000
76	A	136	LEU	0	-0.026	0.001	49.495	0.175	0.175	0.000	0.000	0.000	0.000
77	A	137	SER	0	-0.084	-0.079	47.235	0.018	0.018	0.000	0.000	0.000	0.000
78	A	138	GLY	0	-0.009	0.008	47.758	-0.034	-0.034	0.000	0.000	0.000	0.000
79	A	139	PRO	0	-0.035	-0.001	43.626	-0.151	-0.151	0.000	0.000	0.000	0.000
80	A	140	ASN	0	-0.017	-0.010	41.260	-0.050	-0.050	0.000	0.000	0.000	0.000
81	A	141	ARG	1	0.840	0.923	33.443	9.020	9.020	0.000	0.000	0.000	0.000
82	A	142	PHE	0	0.007	0.005	35.474	0.172	0.172	0.000	0.000	0.000	0.000
83	A	143	ASP	-1	-0.839	-0.915	29.735	-10.703	-10.703	0.000	0.000	0.000	0.000
84	A	144	LEU	0	0.010	0.028	27.802	0.280	0.280	0.000	0.000	0.000	0.000
85	A	145	LEU	0	-0.010	0.000	31.154	-0.016	-0.016	0.000	0.000	0.000	0.000
86	A	146	ASN	0	-0.067	-0.047	30.949	-0.571	-0.571	0.000	0.000	0.000	0.000
87	A	147	GLY	0	0.010	0.003	30.118	0.164	0.164	0.000	0.000	0.000	0.000
88	A	148	GLU	-1	-0.759	-0.850	31.109	-8.695	-8.695	0.000	0.000	0.000	0.000
89	A	149	TRP	0	0.036	0.022	28.993	-0.027	-0.027	0.000	0.000	0.000	0.000
90	A	150	VAL	0	-0.016	-0.008	34.717	0.348	0.348	0.000	0.000	0.000	0.000
91	A	151	SER	0	-0.021	-0.006	36.461	-0.109	-0.109	0.000	0.000	0.000	0.000
92	A	152	LEU	0	-0.002	-0.022	33.886	0.100	0.100	0.000	0.000	0.000	0.000
93	A	153	ARG	1	0.796	0.882	38.453	7.231	7.231	0.000	0.000	0.000	0.000
94	A	154	ASN	0	-0.019	-0.035	42.241	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	155	GLY	0	0.039	0.027	39.771	0.095	0.095	0.000	0.000	0.000	0.000
96	A	156	THR	0	-0.022	-0.004	40.609	-0.112	-0.112	0.000	0.000	0.000	0.000
97	A	157	LYS	1	0.903	0.938	38.291	8.037	8.037	0.000	0.000	0.000	0.000
98	A	158	LEU	0	0.029	0.009	36.569	0.179	0.179	0.000	0.000	0.000	0.000
99	A	159	THR	0	0.023	0.015	38.058	0.104	0.104	0.000	0.000	0.000	0.000
100	A	160	ASP	-1	-0.860	-0.923	40.604	-7.381	-7.381	0.000	0.000	0.000	0.000
101	A	161	ILE	0	-0.014	-0.009	42.522	0.141	0.141	0.000	0.000	0.000	0.000
102	A	162	LEU	0	0.012	0.004	39.985	0.152	0.152	0.000	0.000	0.000	0.000
103	A	163	THR	0	0.014	0.005	43.761	0.143	0.143	0.000	0.000	0.000	0.000
104	A	164	GLU	-1	-0.983	-1.005	46.066	-6.366	-6.366	0.000	0.000	0.000	0.000
105	A	165	GLU	-1	-0.747	-0.820	47.879	-6.562	-6.562	0.000	0.000	0.000	0.000
106	A	166	VAL	0	0.042	0.019	46.395	0.142	0.142	0.000	0.000	0.000	0.000
107	A	167	GLU	-1	-0.809	-0.889	49.041	-6.240	-6.240	0.000	0.000	0.000	0.000
108	A	168	LYS	1	0.696	0.832	51.301	6.380	6.380	0.000	0.000	0.000	0.000
109	A	169	ALA	0	0.010	0.013	52.102	0.127	0.127	0.000	0.000	0.000	0.000
110	A	170	ILE	0	0.023	0.032	51.142	0.072	0.072	0.000	0.000	0.000	0.000
111	A	171	SER	0	-0.126	-0.059	55.303	0.115	0.115	0.000	0.000	0.000	0.000
112	A	172	LYS	0	0.004	0.024	57.406	-0.022	-0.022	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:61:VAL)