FMO DATABASE

FMODB ID: 2RK5R

Calculation Name: 2RKQ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2RKQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9VS97

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	168
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1719992.712012
FMO2-HF: Nuclear repulsion	1655089.742722
FMO2-HF: Total energy	-64902.96929
FMO2-MP2: Total energy	-65091.605167

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:11:GLU)

Summations of interaction energy for fragment #1(A:11:GLU)

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.
-67.442	-57.702	7.644	-8.015	-9.372	0.009

Interaction energy analysis for fragmet #1(A:11:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.070 / q_NPA : -0.042

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	13	PRO	0	-0.020	-0.008	3.869	3.327	4.807	-0.016	-0.665	-0.800	0.000
120	A	130	GLU	-1	-0.883	-0.948	3.141	-16.632	-16.195	0.014	-0.106	-0.345	0.000
121	A	131	LEU	0	-0.026	-0.011	3.884	-2.814	-2.412	0.001	-0.145	-0.258	-0.001
123	A	133	GLU	-1	-0.847	-0.913	3.215	-5.609	-3.731	0.049	-1.009	-0.918	-0.008
124	A	134	GLN	0	-0.023	-0.019	2.351	-5.190	-2.939	3.731	-2.732	-3.250	-0.028
125	A	135	ALA	0	0.013	0.006	4.471	2.787	2.855	-0.001	-0.018	-0.050	0.000
127	A	137	LYS	1	0.830	0.900	2.130	-42.181	-39.030	3.867	-3.329	-3.690	0.046
128	A	138	GLN	0	-0.058	-0.027	4.267	-0.309	-0.236	-0.001	-0.011	-0.061	0.000
4	A	14	ILE	0	-0.010	-0.002	6.215	0.023	0.023	0.000	0.000	0.000	0.000
5	A	15	VAL	0	-0.023	0.000	8.989	0.676	0.676	0.000	0.000	0.000	0.000
6	A	16	THR	0	0.024	-0.038	12.324	0.203	0.203	0.000	0.000	0.000	0.000
7	A	17	ARG	1	0.768	0.808	14.161	1.047	1.047	0.000	0.000	0.000	0.000
8	A	18	ALA	0	-0.016	0.003	17.414	0.083	0.083	0.000	0.000	0.000	0.000
9	A	19	GLU	-1	-0.840	-0.884	13.525	-2.007	-2.007	0.000	0.000	0.000	0.000
10	A	20	TRP	0	-0.063	-0.032	16.387	0.100	0.100	0.000	0.000	0.000	0.000
11	A	21	ASN	0	-0.080	-0.032	19.307	0.121	0.121	0.000	0.000	0.000	0.000
12	A	22	ALA	0	0.028	0.027	20.543	0.048	0.048	0.000	0.000	0.000	0.000
13	A	23	LYS	1	0.901	0.950	22.546	0.724	0.724	0.000	0.000	0.000	0.000
14	A	24	PRO	0	0.050	0.027	24.056	-0.065	-0.065	0.000	0.000	0.000	0.000
15	A	25	PRO	0	0.028	-0.001	23.719	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	26	ASN	0	-0.044	-0.025	26.373	0.031	0.031	0.000	0.000	0.000	0.000
17	A	26	GLY	0	0.035	0.006	29.491	0.008	0.008	0.000	0.000	0.000	0.000
18	A	27	ALA	0	-0.008	0.005	28.771	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	28	ILE	0	-0.024	-0.009	23.658	-0.049	-0.049	0.000	0.000	0.000	0.000
20	A	29	ASP	-1	-0.857	-0.900	26.440	-0.214	-0.214	0.000	0.000	0.000	0.000
21	A	30	SER	0	0.000	-0.006	23.385	-0.067	-0.067	0.000	0.000	0.000	0.000
22	A	31	MET	0	-0.085	-0.020	19.278	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	32	VAL	0	-0.001	-0.004	20.597	0.035	0.035	0.000	0.000	0.000	0.000
24	A	33	THR	0	-0.014	0.023	15.268	-0.114	-0.114	0.000	0.000	0.000	0.000
25	A	34	PRO	0	-0.019	-0.013	14.133	0.122	0.122	0.000	0.000	0.000	0.000
26	A	35	LEU	0	-0.022	-0.020	15.458	-0.013	-0.013	0.000	0.000	0.000	0.000
27	A	36	PRO	0	-0.013	-0.010	16.566	-0.037	-0.037	0.000	0.000	0.000	0.000
28	A	37	ARG	1	0.904	0.967	18.140	0.520	0.520	0.000	0.000	0.000	0.000
29	A	38	ALA	0	0.022	0.015	14.162	-0.056	-0.056	0.000	0.000	0.000	0.000
30	A	39	VAL	0	-0.019	-0.003	16.156	0.069	0.069	0.000	0.000	0.000	0.000
31	A	40	ILE	0	0.025	0.018	13.807	-0.159	-0.159	0.000	0.000	0.000	0.000
32	A	41	ALA	0	-0.009	-0.017	17.623	0.249	0.249	0.000	0.000	0.000	0.000
33	A	42	HIS	0	0.010	0.019	19.138	-0.269	-0.269	0.000	0.000	0.000	0.000
34	A	43	THR	0	0.022	0.006	20.819	0.106	0.106	0.000	0.000	0.000	0.000
35	A	44	ALA	0	-0.026	0.006	23.367	0.119	0.119	0.000	0.000	0.000	0.000
36	A	45	GLY	0	0.018	0.017	26.049	0.079	0.079	0.000	0.000	0.000	0.000
37	A	46	GLY	0	-0.002	-0.006	26.508	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	47	ALA	0	0.049	0.008	22.879	-0.068	-0.068	0.000	0.000	0.000	0.000
39	A	48	CYS	0	-0.132	-0.010	18.354	0.077	0.077	0.000	0.000	0.000	0.000
40	A	49	ALA	0	0.037	0.004	21.036	-0.155	-0.155	0.000	0.000	0.000	0.000
41	A	50	ASP	-1	-0.799	-0.867	20.208	-1.565	-1.565	0.000	0.000	0.000	0.000
42	A	51	ASP	-1	-0.780	-0.890	16.888	-2.497	-2.497	0.000	0.000	0.000	0.000
43	A	52	VAL	0	-0.029	-0.003	19.318	0.037	0.037	0.000	0.000	0.000	0.000
44	A	53	THR	0	0.000	-0.033	22.817	0.007	0.007	0.000	0.000	0.000	0.000
45	A	55	SER	0	0.081	0.049	19.451	0.069	0.069	0.000	0.000	0.000	0.000
46	A	56	GLN	0	-0.013	-0.011	20.515	0.095	0.095	0.000	0.000	0.000	0.000
47	A	57	HIS	0	-0.056	-0.034	22.188	0.149	0.149	0.000	0.000	0.000	0.000
48	A	58	MET	0	0.025	0.038	17.489	0.033	0.033	0.000	0.000	0.000	0.000
49	A	59	ARG	1	0.849	0.907	21.439	1.281	1.281	0.000	0.000	0.000	0.000
50	A	60	ASN	0	-0.046	-0.016	24.518	0.128	0.128	0.000	0.000	0.000	0.000
51	A	61	LEU	0	0.029	0.021	21.898	0.090	0.090	0.000	0.000	0.000	0.000
52	A	62	GLN	0	0.034	0.020	23.260	0.058	0.058	0.000	0.000	0.000	0.000
53	A	63	ASN	0	0.003	-0.005	25.070	0.106	0.106	0.000	0.000	0.000	0.000
54	A	64	PHE	0	0.000	0.007	28.331	0.082	0.082	0.000	0.000	0.000	0.000
55	A	65	GLN	0	0.029	-0.003	24.188	0.002	0.002	0.000	0.000	0.000	0.000
56	A	66	MET	0	-0.027	0.022	27.074	0.025	0.025	0.000	0.000	0.000	0.000
57	A	67	SER	0	-0.059	-0.039	29.760	0.068	0.068	0.000	0.000	0.000	0.000
58	A	68	LYS	1	0.848	0.917	32.158	0.577	0.577	0.000	0.000	0.000	0.000
59	A	69	GLN	0	0.022	0.008	28.394	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	70	LYS	1	0.880	0.967	31.960	0.456	0.456	0.000	0.000	0.000	0.000
61	A	71	PHE	0	0.025	0.014	26.177	0.032	0.032	0.000	0.000	0.000	0.000
62	A	72	SER	0	0.012	-0.008	27.278	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	73	ASP	-1	-0.717	-0.841	21.871	-0.892	-0.892	0.000	0.000	0.000	0.000
64	A	74	ILE	0	-0.018	0.005	20.182	0.018	0.018	0.000	0.000	0.000	0.000
65	A	75	GLY	0	0.016	0.010	21.936	0.016	0.016	0.000	0.000	0.000	0.000
66	A	76	TYR	0	-0.024	-0.007	17.579	0.085	0.085	0.000	0.000	0.000	0.000
67	A	77	HIS	0	0.020	0.019	14.702	-0.081	-0.081	0.000	0.000	0.000	0.000
68	A	78	TYR	0	-0.027	-0.027	9.773	-0.321	-0.321	0.000	0.000	0.000	0.000
69	A	79	LEU	0	-0.020	-0.013	13.881	0.304	0.304	0.000	0.000	0.000	0.000
70	A	80	ILE	0	-0.006	0.013	11.193	-0.363	-0.363	0.000	0.000	0.000	0.000
71	A	81	GLY	0	0.045	0.011	14.319	0.445	0.445	0.000	0.000	0.000	0.000
72	A	82	GLY	0	0.038	0.005	15.791	-0.312	-0.312	0.000	0.000	0.000	0.000
73	A	83	ASN	0	-0.043	-0.040	16.194	-0.157	-0.157	0.000	0.000	0.000	0.000
74	A	84	GLY	0	0.013	0.001	13.153	-0.154	-0.154	0.000	0.000	0.000	0.000
75	A	85	LYS	1	0.846	0.925	11.335	2.099	2.099	0.000	0.000	0.000	0.000
76	A	86	VAL	0	0.065	0.032	8.074	0.632	0.632	0.000	0.000	0.000	0.000
77	A	87	TYR	0	-0.013	-0.009	11.036	0.179	0.179	0.000	0.000	0.000	0.000
78	A	88	GLU	-1	-0.849	-0.921	13.207	-1.434	-1.434	0.000	0.000	0.000	0.000
79	A	89	GLY	0	-0.006	0.000	14.123	0.206	0.206	0.000	0.000	0.000	0.000
80	A	90	ARG	1	0.796	0.876	17.080	0.928	0.928	0.000	0.000	0.000	0.000
81	A	91	SER	0	0.077	0.030	15.721	-0.169	-0.169	0.000	0.000	0.000	0.000
82	A	92	PRO	0	0.042	0.005	12.655	0.072	0.072	0.000	0.000	0.000	0.000
83	A	93	SER	0	0.009	0.013	15.887	0.065	0.065	0.000	0.000	0.000	0.000
84	A	94	GLN	0	0.001	0.001	18.661	0.007	0.007	0.000	0.000	0.000	0.000
85	A	95	ARG	1	0.840	0.899	20.263	0.202	0.202	0.000	0.000	0.000	0.000
86	A	96	GLY	0	0.044	0.032	21.510	-0.052	-0.052	0.000	0.000	0.000	0.000
87	A	97	ALA	0	-0.088	-0.059	22.099	0.104	0.104	0.000	0.000	0.000	0.000
88	A	98	PHE	0	-0.011	-0.011	20.080	-0.058	-0.058	0.000	0.000	0.000	0.000
89	A	99	ALA	0	0.025	0.011	24.422	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	100	GLY	0	0.023	0.026	26.211	0.054	0.054	0.000	0.000	0.000	0.000
91	A	101	PRO	0	0.012	0.000	28.190	0.003	0.003	0.000	0.000	0.000	0.000
92	A	102	ASN	0	0.016	0.000	25.938	0.067	0.067	0.000	0.000	0.000	0.000
93	A	103	ASN	0	-0.013	-0.002	23.541	-0.139	-0.139	0.000	0.000	0.000	0.000
94	A	104	ASP	-1	-0.760	-0.864	22.543	-0.340	-0.340	0.000	0.000	0.000	0.000
95	A	105	GLY	0	0.010	0.011	20.965	-0.024	-0.024	0.000	0.000	0.000	0.000
96	A	106	SER	0	-0.023	-0.031	18.976	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	107	LEU	0	0.033	0.014	11.400	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	108	GLY	0	0.003	0.000	15.987	-0.151	-0.151	0.000	0.000	0.000	0.000
99	A	109	ILE	0	0.012	-0.006	11.360	-0.126	-0.126	0.000	0.000	0.000	0.000
100	A	110	ALA	0	-0.006	-0.003	15.260	0.083	0.083	0.000	0.000	0.000	0.000
101	A	111	PHE	0	0.033	0.012	13.696	-0.176	-0.176	0.000	0.000	0.000	0.000
102	A	112	ILE	0	-0.027	-0.037	17.828	0.316	0.316	0.000	0.000	0.000	0.000
103	A	113	GLY	0	0.009	-0.009	20.132	-0.069	-0.069	0.000	0.000	0.000	0.000
104	A	114	ASN	0	-0.081	-0.043	23.252	0.018	0.018	0.000	0.000	0.000	0.000
105	A	115	PHE	0	0.019	-0.005	20.570	-0.051	-0.051	0.000	0.000	0.000	0.000
106	A	116	GLU	-1	-0.781	-0.864	23.916	-0.946	-0.946	0.000	0.000	0.000	0.000
107	A	117	GLU	-1	-0.931	-0.962	27.030	-0.858	-0.858	0.000	0.000	0.000	0.000
108	A	118	ARG	1	0.908	0.957	23.432	1.464	1.464	0.000	0.000	0.000	0.000
109	A	119	ALA	0	0.062	0.031	19.729	-0.024	-0.024	0.000	0.000	0.000	0.000
110	A	120	PRO	0	-0.027	-0.015	16.983	0.082	0.082	0.000	0.000	0.000	0.000
111	A	121	ASN	0	-0.024	-0.017	17.278	0.193	0.193	0.000	0.000	0.000	0.000
112	A	122	LYS	1	0.923	0.950	12.429	3.840	3.840	0.000	0.000	0.000	0.000
113	A	123	GLU	-1	-0.856	-0.936	12.153	-3.715	-3.715	0.000	0.000	0.000	0.000
114	A	124	ALA	0	-0.007	0.001	11.138	-0.908	-0.908	0.000	0.000	0.000	0.000
115	A	125	LEU	0	-0.011	-0.019	11.874	-0.301	-0.301	0.000	0.000	0.000	0.000
116	A	126	ASP	-1	-0.873	-0.918	8.748	-4.874	-4.874	0.000	0.000	0.000	0.000
117	A	127	ALA	0	0.080	0.044	7.130	-1.442	-1.442	0.000	0.000	0.000	0.000
118	A	128	ALA	0	-0.008	-0.014	7.409	-0.991	-0.991	0.000	0.000	0.000	0.000
119	A	129	LYS	1	0.873	0.950	7.832	4.856	4.856	0.000	0.000	0.000	0.000
122	A	132	LEU	0	-0.040	-0.015	6.297	1.780	1.780	0.000	0.000	0.000	0.000
126	A	136	VAL	0	-0.006	0.006	8.191	0.943	0.943	0.000	0.000	0.000	0.000
129	A	139	ALA	0	-0.008	0.003	7.893	-0.626	-0.626	0.000	0.000	0.000	0.000
130	A	140	GLN	0	0.054	0.040	9.124	-0.850	-0.850	0.000	0.000	0.000	0.000
131	A	141	LEU	0	-0.049	-0.009	11.134	-0.272	-0.272	0.000	0.000	0.000	0.000
132	A	142	VAL	0	-0.014	-0.005	12.819	0.442	0.442	0.000	0.000	0.000	0.000
133	A	143	GLU	-1	-0.878	-0.951	12.896	1.517	1.517	0.000	0.000	0.000	0.000
134	A	144	GLY	0	-0.019	-0.006	14.323	-0.286	-0.286	0.000	0.000	0.000	0.000
135	A	145	TYR	0	-0.041	-0.019	11.821	-0.129	-0.129	0.000	0.000	0.000	0.000
136	A	146	LYS	1	0.939	0.971	16.933	0.248	0.248	0.000	0.000	0.000	0.000
137	A	147	LEU	0	0.013	0.003	14.181	-0.120	-0.120	0.000	0.000	0.000	0.000
138	A	148	LEU	0	-0.002	0.001	17.281	0.116	0.116	0.000	0.000	0.000	0.000
139	A	149	GLY	0	0.022	0.007	19.102	-0.208	-0.208	0.000	0.000	0.000	0.000
140	A	150	HIS	0	-0.038	-0.046	21.401	0.046	0.046	0.000	0.000	0.000	0.000
141	A	151	ARG	1	0.775	0.842	23.184	1.043	1.043	0.000	0.000	0.000	0.000
142	A	152	GLN	0	0.028	0.011	22.776	-0.063	-0.063	0.000	0.000	0.000	0.000
143	A	153	VAL	0	0.011	0.014	23.307	0.061	0.061	0.000	0.000	0.000	0.000
144	A	154	SER	0	-0.030	-0.014	26.335	0.068	0.068	0.000	0.000	0.000	0.000
145	A	155	ALA	0	0.043	0.032	28.331	-0.026	-0.026	0.000	0.000	0.000	0.000
146	A	156	THR	0	-0.045	-0.026	26.493	-0.016	-0.016	0.000	0.000	0.000	0.000
147	A	157	LYS	1	0.889	0.908	28.569	0.835	0.835	0.000	0.000	0.000	0.000
148	A	158	SER	0	-0.015	0.016	23.478	-0.115	-0.115	0.000	0.000	0.000	0.000
149	A	159	PRO	0	-0.004	-0.009	20.343	0.083	0.083	0.000	0.000	0.000	0.000
150	A	160	GLY	0	0.038	0.013	22.439	-0.075	-0.075	0.000	0.000	0.000	0.000
151	A	161	GLU	-1	-0.751	-0.853	24.022	-0.958	-0.958	0.000	0.000	0.000	0.000
152	A	162	ALA	0	-0.041	-0.005	24.063	-0.033	-0.033	0.000	0.000	0.000	0.000
153	A	163	LEU	0	-0.031	-0.010	17.024	-0.105	-0.105	0.000	0.000	0.000	0.000
154	A	164	TYR	0	-0.016	-0.013	19.795	-0.122	-0.122	0.000	0.000	0.000	0.000
155	A	165	ALA	0	0.054	0.015	21.427	-0.017	-0.017	0.000	0.000	0.000	0.000
156	A	166	LEU	0	-0.045	-0.018	17.685	-0.011	-0.011	0.000	0.000	0.000	0.000
157	A	167	ILE	0	-0.006	-0.010	15.848	-0.065	-0.065	0.000	0.000	0.000	0.000
158	A	168	GLN	0	-0.020	-0.016	17.731	0.030	0.030	0.000	0.000	0.000	0.000
159	A	169	GLN	0	-0.068	-0.023	18.243	0.028	0.028	0.000	0.000	0.000	0.000
160	A	170	TRP	0	-0.057	-0.020	12.435	-0.326	-0.326	0.000	0.000	0.000	0.000
161	A	171	PRO	0	0.024	-0.004	12.001	0.226	0.226	0.000	0.000	0.000	0.000
162	A	172	ASN	0	-0.024	-0.017	14.346	-0.104	-0.104	0.000	0.000	0.000	0.000
163	A	173	TRP	0	-0.024	0.016	16.787	0.065	0.065	0.000	0.000	0.000	0.000
164	A	174	SER	0	-0.058	-0.045	18.981	0.164	0.164	0.000	0.000	0.000	0.000
165	A	175	GLU	-1	-0.927	-0.968	22.220	-0.505	-0.505	0.000	0.000	0.000	0.000
166	A	176	GLU	-1	-0.880	-0.919	23.750	-0.451	-0.451	0.000	0.000	0.000	0.000
167	A	177	MET	0	-0.058	-0.031	26.480	-0.105	-0.105	0.000	0.000	0.000	0.000
168	A	178	LEU	-1	-0.969	-0.964	25.780	-0.396	-0.396	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:GLU)