FMO DATABASE

FMODB ID: 673GZ

Calculation Name: 2QR3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2QR3

Chain ID: A

ChEMBL ID:

UniProt ID: Q64UD2

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1082595.816299
FMO2-HF: Nuclear repulsion	1034710.186189
FMO2-HF: Total energy	-47885.63011
FMO2-MP2: Total energy	-48028.744942

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:0:SER)

Summations of interaction energy for fragment #1(A:0: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.
-141.993	-140.353	-0.005	-0.696	-0.937	-0.003

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.804 / q_NPA : 0.886

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	2	GLY	0	0.030	0.033	3.797	3.496	5.021	-0.002	-0.675	-0.848	-0.003
4	A	3	THR	0	-0.024	-0.028	5.384	2.261	2.332	-0.001	-0.001	-0.068	0.000
27	A	26	SER	0	-0.049	-0.033	4.095	2.993	3.107	-0.001	-0.008	-0.105	0.000
48	A	47	GLU	-1	-0.778	-0.898	5.558	-55.999	-56.069	-0.001	-0.012	0.084	0.000
5	A	4	ILE	0	-0.001	0.023	9.112	-0.144	-0.144	0.000	0.000	0.000	0.000
6	A	5	ILE	0	-0.022	-0.012	11.726	1.379	1.379	0.000	0.000	0.000	0.000
7	A	6	ILE	0	-0.006	-0.004	15.008	0.101	0.101	0.000	0.000	0.000	0.000
8	A	7	VAL	0	-0.002	-0.003	18.172	0.523	0.523	0.000	0.000	0.000	0.000
9	A	8	ASP	-1	-0.733	-0.882	21.710	-12.526	-12.526	0.000	0.000	0.000	0.000
10	A	9	ASP	-1	-0.789	-0.867	24.596	-10.690	-10.690	0.000	0.000	0.000	0.000
11	A	10	ASN	0	-0.042	-0.016	27.332	0.278	0.278	0.000	0.000	0.000	0.000
12	A	11	LYS	1	0.939	0.954	25.854	10.510	10.510	0.000	0.000	0.000	0.000
13	A	12	GLY	0	0.023	0.033	25.524	-0.328	-0.328	0.000	0.000	0.000	0.000
14	A	13	VAL	0	-0.005	0.004	23.344	-0.316	-0.316	0.000	0.000	0.000	0.000
15	A	14	LEU	0	-0.017	-0.002	21.054	-0.660	-0.660	0.000	0.000	0.000	0.000
16	A	15	THR	0	-0.030	-0.033	20.669	-0.729	-0.729	0.000	0.000	0.000	0.000
17	A	16	ALA	0	-0.007	-0.003	21.335	-0.432	-0.432	0.000	0.000	0.000	0.000
18	A	17	VAL	0	0.034	0.009	17.042	-0.547	-0.547	0.000	0.000	0.000	0.000
19	A	18	GLN	0	0.006	0.009	16.278	-1.549	-1.549	0.000	0.000	0.000	0.000
20	A	19	LEU	0	-0.072	-0.036	16.623	-0.662	-0.662	0.000	0.000	0.000	0.000
21	A	20	LEU	0	-0.028	-0.008	17.090	-0.493	-0.493	0.000	0.000	0.000	0.000
22	A	21	LEU	0	0.041	0.010	12.576	-0.886	-0.886	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.848	0.924	11.584	15.033	15.033	0.000	0.000	0.000	0.000
24	A	23	ASN	0	-0.042	-0.021	11.074	-0.405	-0.405	0.000	0.000	0.000	0.000
25	A	24	HIS	0	-0.004	0.013	8.256	-2.208	-2.208	0.000	0.000	0.000	0.000
26	A	25	PHE	0	0.025	0.005	6.610	-5.100	-5.100	0.000	0.000	0.000	0.000
28	A	27	LYS	1	0.782	0.874	6.773	24.549	24.549	0.000	0.000	0.000	0.000
29	A	28	VAL	0	0.027	0.025	10.096	-0.596	-0.596	0.000	0.000	0.000	0.000
30	A	29	ILE	0	0.012	0.009	12.933	1.663	1.663	0.000	0.000	0.000	0.000
31	A	30	THR	0	-0.005	0.003	15.775	-0.112	-0.112	0.000	0.000	0.000	0.000
32	A	31	LEU	0	-0.071	-0.029	19.202	0.649	0.649	0.000	0.000	0.000	0.000
33	A	32	SER	0	0.008	-0.032	22.335	0.030	0.030	0.000	0.000	0.000	0.000
34	A	33	SER	0	0.010	0.002	24.883	0.628	0.628	0.000	0.000	0.000	0.000
35	A	34	PRO	0	0.080	0.034	24.998	-0.506	-0.506	0.000	0.000	0.000	0.000
36	A	35	VAL	0	0.030	0.025	25.705	-0.318	-0.318	0.000	0.000	0.000	0.000
37	A	36	SER	0	0.018	0.005	22.942	-0.106	-0.106	0.000	0.000	0.000	0.000
38	A	37	LEU	0	0.031	0.020	20.071	-0.555	-0.555	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.054	-0.035	20.884	-0.542	-0.542	0.000	0.000	0.000	0.000
40	A	39	THR	0	-0.050	-0.011	20.896	0.045	0.045	0.000	0.000	0.000	0.000
41	A	40	VAL	0	0.014	-0.007	16.838	-0.507	-0.507	0.000	0.000	0.000	0.000
42	A	41	LEU	0	-0.014	-0.012	16.259	-1.104	-1.104	0.000	0.000	0.000	0.000
43	A	42	ARG	1	0.904	0.975	16.735	13.111	13.111	0.000	0.000	0.000	0.000
44	A	43	GLU	-1	-0.931	-0.975	16.426	-15.179	-15.179	0.000	0.000	0.000	0.000
45	A	44	GLU	-1	-0.829	-0.905	13.210	-21.011	-21.011	0.000	0.000	0.000	0.000
46	A	45	ASN	0	-0.080	-0.023	10.053	-1.853	-1.853	0.000	0.000	0.000	0.000
47	A	46	PRO	0	-0.023	-0.005	9.747	-2.541	-2.541	0.000	0.000	0.000	0.000
49	A	48	VAL	0	-0.014	-0.007	9.972	0.931	0.931	0.000	0.000	0.000	0.000
50	A	49	VAL	0	-0.023	-0.014	12.789	0.282	0.282	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.020	0.006	16.248	0.321	0.321	0.000	0.000	0.000	0.000
52	A	51	LEU	0	-0.016	-0.021	18.293	0.341	0.341	0.000	0.000	0.000	0.000
53	A	52	ASP	-1	-0.829	-0.925	21.887	-11.537	-11.537	0.000	0.000	0.000	0.000
54	A	53	MET	0	-0.024	0.011	25.026	-0.107	-0.107	0.000	0.000	0.000	0.000
55	A	54	ASN	0	-0.067	-0.053	27.647	0.198	0.198	0.000	0.000	0.000	0.000
56	A	55	PHE	0	-0.028	0.002	26.301	0.144	0.144	0.000	0.000	0.000	0.000
57	A	56	THR	0	-0.030	-0.018	28.411	0.421	0.421	0.000	0.000	0.000	0.000
58	A	57	SER	0	0.035	0.002	31.069	0.216	0.216	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.009	0.009	33.630	0.321	0.321	0.000	0.000	0.000	0.000
60	A	59	ILE	0	0.033	0.016	32.987	0.189	0.189	0.000	0.000	0.000	0.000
61	A	60	ASN	0	-0.040	-0.017	35.588	0.150	0.150	0.000	0.000	0.000	0.000
62	A	61	ASN	0	-0.090	-0.052	37.996	0.193	0.193	0.000	0.000	0.000	0.000
63	A	62	GLY	0	0.028	0.022	37.073	0.048	0.048	0.000	0.000	0.000	0.000
64	A	63	ASN	0	-0.072	-0.028	33.393	-0.161	-0.161	0.000	0.000	0.000	0.000
65	A	64	GLU	-1	-0.777	-0.901	30.816	-10.430	-10.430	0.000	0.000	0.000	0.000
66	A	65	GLY	0	-0.010	-0.009	27.226	-0.151	-0.151	0.000	0.000	0.000	0.000
67	A	66	LEU	0	-0.006	0.004	26.899	-0.391	-0.391	0.000	0.000	0.000	0.000
68	A	67	PHE	0	0.001	0.005	28.433	-0.115	-0.115	0.000	0.000	0.000	0.000
69	A	68	TRP	0	0.025	-0.009	25.463	-0.302	-0.302	0.000	0.000	0.000	0.000
70	A	69	LEU	0	0.023	0.017	22.291	-0.557	-0.557	0.000	0.000	0.000	0.000
71	A	70	HIS	0	0.011	0.021	24.095	-0.565	-0.565	0.000	0.000	0.000	0.000
72	A	71	GLU	-1	-0.783	-0.862	26.098	-11.143	-11.143	0.000	0.000	0.000	0.000
73	A	72	ILE	0	-0.031	-0.013	19.816	-0.275	-0.275	0.000	0.000	0.000	0.000
74	A	73	LYS	1	0.855	0.928	18.497	16.242	16.242	0.000	0.000	0.000	0.000
75	A	74	ARG	1	0.770	0.849	22.674	10.821	10.821	0.000	0.000	0.000	0.000
76	A	75	GLN	0	-0.075	-0.031	22.031	0.545	0.545	0.000	0.000	0.000	0.000
77	A	76	TYR	0	-0.011	-0.023	17.836	-0.238	-0.238	0.000	0.000	0.000	0.000
78	A	77	ARG	1	0.957	0.985	18.699	13.576	13.576	0.000	0.000	0.000	0.000
79	A	78	ASP	-1	-0.885	-0.949	15.565	-17.160	-17.160	0.000	0.000	0.000	0.000
80	A	79	LEU	0	-0.028	0.008	13.645	-1.243	-1.243	0.000	0.000	0.000	0.000
81	A	80	PRO	0	0.021	0.013	11.892	1.913	1.913	0.000	0.000	0.000	0.000
82	A	81	VAL	0	-0.018	-0.012	15.101	-0.193	-0.193	0.000	0.000	0.000	0.000
83	A	82	VAL	0	-0.003	0.011	16.010	0.571	0.571	0.000	0.000	0.000	0.000
84	A	83	LEU	0	0.007	0.007	18.761	0.225	0.225	0.000	0.000	0.000	0.000
85	A	84	PHE	0	0.009	-0.016	21.923	-0.179	-0.179	0.000	0.000	0.000	0.000
86	A	85	THR	0	0.066	0.014	23.721	0.451	0.451	0.000	0.000	0.000	0.000
87	A	86	ALA	0	0.037	0.032	27.317	-0.126	-0.126	0.000	0.000	0.000	0.000
88	A	87	TYR	0	-0.004	-0.027	28.994	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	88	ALA	0	-0.056	-0.019	32.085	0.180	0.180	0.000	0.000	0.000	0.000
90	A	89	ASP	-1	-0.784	-0.868	31.163	-9.645	-9.645	0.000	0.000	0.000	0.000
91	A	90	ILE	0	-0.002	-0.010	29.194	-0.314	-0.314	0.000	0.000	0.000	0.000
92	A	91	ASP	-1	-0.904	-0.949	30.342	-9.579	-9.579	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.002	0.004	31.511	-0.134	-0.134	0.000	0.000	0.000	0.000
94	A	93	ALA	0	0.048	0.016	26.384	-0.301	-0.301	0.000	0.000	0.000	0.000
95	A	94	VAL	0	-0.036	-0.020	26.806	-0.355	-0.355	0.000	0.000	0.000	0.000
96	A	95	ARG	1	0.771	0.862	28.677	9.736	9.736	0.000	0.000	0.000	0.000
97	A	96	GLY	0	0.076	0.019	26.613	-0.050	-0.050	0.000	0.000	0.000	0.000
98	A	97	ILE	0	-0.035	0.000	22.396	-0.307	-0.307	0.000	0.000	0.000	0.000
99	A	98	LYS	1	0.878	0.943	25.091	9.913	9.913	0.000	0.000	0.000	0.000
100	A	99	GLU	-1	-0.851	-0.902	27.520	-10.252	-10.252	0.000	0.000	0.000	0.000
101	A	100	GLY	0	0.007	0.012	23.561	-0.085	-0.085	0.000	0.000	0.000	0.000
102	A	101	ALA	0	-0.067	-0.033	21.180	-0.729	-0.729	0.000	0.000	0.000	0.000
103	A	102	SER	0	-0.020	-0.023	16.553	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	103	ASP	-1	-0.819	-0.913	17.833	-16.373	-16.373	0.000	0.000	0.000	0.000
105	A	104	PHE	0	-0.086	-0.056	19.762	0.355	0.355	0.000	0.000	0.000	0.000
106	A	105	VAL	0	-0.006	0.010	19.241	0.035	0.035	0.000	0.000	0.000	0.000
107	A	106	VAL	0	-0.029	-0.014	22.372	0.299	0.299	0.000	0.000	0.000	0.000
108	A	107	LYS	1	0.787	0.903	25.277	12.059	12.059	0.000	0.000	0.000	0.000
109	A	108	PRO	0	-0.026	-0.035	27.277	0.404	0.404	0.000	0.000	0.000	0.000
110	A	109	TRP	0	0.022	0.008	21.905	0.265	0.265	0.000	0.000	0.000	0.000
111	A	110	ASP	-1	-0.834	-0.916	21.659	-13.916	-13.916	0.000	0.000	0.000	0.000
112	A	111	ASN	0	-0.016	-0.026	19.992	-0.616	-0.616	0.000	0.000	0.000	0.000
113	A	112	GLN	0	-0.003	0.001	15.094	-0.606	-0.606	0.000	0.000	0.000	0.000
114	A	113	LYS	1	0.999	0.989	16.964	12.769	12.769	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.017	0.008	17.390	-0.602	-0.602	0.000	0.000	0.000	0.000
116	A	115	LEU	0	-0.013	0.001	11.343	-0.784	-0.784	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.853	-0.927	13.257	-20.374	-20.374	0.000	0.000	0.000	0.000
118	A	117	THR	0	-0.049	-0.034	13.658	-0.703	-0.703	0.000	0.000	0.000	0.000
119	A	118	LEU	0	-0.019	-0.014	12.875	-0.515	-0.515	0.000	0.000	0.000	0.000
120	A	119	LEU	0	-0.013	-0.003	8.065	-2.048	-2.048	0.000	0.000	0.000	0.000
121	A	120	ASN	0	0.009	0.006	9.152	-3.909	-3.909	0.000	0.000	0.000	0.000
122	A	121	ALA	0	-0.021	-0.003	11.333	-0.380	-0.380	0.000	0.000	0.000	0.000
123	A	122	ALA	0	-0.010	-0.007	7.821	0.567	0.567	0.000	0.000	0.000	0.000
124	A	123	SER	0	-0.088	-0.041	6.941	-5.461	-5.461	0.000	0.000	0.000	0.000
125	A	124	GLN	0	-0.099	-0.058	7.922	3.701	3.701	0.000	0.000	0.000	0.000
126	A	125	ALA	-1	-0.945	-0.959	9.524	-26.094	-26.094	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)