FMO DATABASE

FMODB ID: QVZQY

Calculation Name: 1R26-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1R26

Chain ID: A

ChEMBL ID:

UniProt ID: Q9NG23

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-946028.296648
FMO2-HF: Nuclear repulsion	899776.721075
FMO2-HF: Total energy	-46251.575573
FMO2-MP2: Total energy	-46382.707511

3D Structure

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:-7:ILE)

Summations of interaction energy for fragment #1(A:-7:ILE)

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.
-5.002	0.064999999999999	0.473	-2.626	-2.914	-0.001

Interaction energy analysis for fragmet #1(A:-7:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.069 / 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	-5	MET	0	-0.004	0.010	2.970	-2.545	1.243	0.215	-2.053	-1.950	0.000
4	A	-4	ARG	1	0.994	0.993	4.600	-0.063	0.056	-0.001	-0.004	-0.114	0.000
5	A	-3	ALA	0	0.002	-0.008	6.937	-0.082	-0.082	0.000	0.000	0.000	0.000
6	A	-2	ARG	1	0.895	0.947	9.591	0.670	0.670	0.000	0.000	0.000	0.000
7	A	-1	TYR	0	0.053	0.024	11.314	0.029	0.029	0.000	0.000	0.000	0.000
8	A	0	PRO	0	-0.007	0.006	13.723	-0.075	-0.075	0.000	0.000	0.000	0.000
9	A	1	SER	0	-0.009	-0.015	14.108	0.034	0.034	0.000	0.000	0.000	0.000
10	A	2	VAL	0	0.006	0.005	13.907	-0.081	-0.081	0.000	0.000	0.000	0.000
11	A	3	VAL	0	-0.037	-0.008	9.822	-0.039	-0.039	0.000	0.000	0.000	0.000
12	A	4	ASP	-1	-0.881	-0.932	13.060	-0.453	-0.453	0.000	0.000	0.000	0.000
13	A	5	VAL	0	-0.055	-0.021	14.087	-0.084	-0.084	0.000	0.000	0.000	0.000
14	A	6	TYR	0	0.051	0.028	15.677	0.072	0.072	0.000	0.000	0.000	0.000
15	A	7	SER	0	0.040	0.017	15.741	0.030	0.030	0.000	0.000	0.000	0.000
16	A	8	VAL	0	0.047	0.015	16.399	-0.053	-0.053	0.000	0.000	0.000	0.000
17	A	9	GLU	-1	-0.724	-0.818	13.526	-0.447	-0.447	0.000	0.000	0.000	0.000
18	A	10	GLN	0	-0.014	-0.004	11.774	0.013	0.013	0.000	0.000	0.000	0.000
19	A	11	PHE	0	0.037	0.001	11.393	-0.145	-0.145	0.000	0.000	0.000	0.000
20	A	12	ARG	1	0.828	0.883	11.847	0.357	0.357	0.000	0.000	0.000	0.000
21	A	13	ASN	0	-0.051	-0.021	8.384	0.075	0.075	0.000	0.000	0.000	0.000
22	A	14	ILE	0	0.012	0.007	7.979	-0.111	-0.111	0.000	0.000	0.000	0.000
23	A	15	MET	0	-0.039	-0.017	8.527	-0.083	-0.083	0.000	0.000	0.000	0.000
24	A	16	SER	0	-0.040	-0.040	9.357	0.183	0.183	0.000	0.000	0.000	0.000
25	A	17	GLU	-1	-0.768	-0.865	3.587	-5.978	-5.472	0.018	-0.300	-0.223	-0.002
26	A	18	ASP	-1	-0.780	-0.828	5.420	0.675	0.675	0.000	0.000	0.000	0.000
27	A	19	ILE	0	-0.077	-0.048	2.462	-0.393	0.211	0.242	-0.262	-0.585	0.001
28	A	20	LEU	0	0.003	0.023	6.605	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	21	THR	0	0.012	-0.014	8.573	-0.209	-0.209	0.000	0.000	0.000	0.000
30	A	22	VAL	0	-0.037	-0.025	10.987	0.120	0.120	0.000	0.000	0.000	0.000
31	A	23	ALA	0	0.036	0.022	14.499	-0.050	-0.050	0.000	0.000	0.000	0.000
32	A	24	TRP	0	-0.001	-0.012	16.199	0.054	0.054	0.000	0.000	0.000	0.000
33	A	25	PHE	0	0.029	0.008	18.993	-0.017	-0.017	0.000	0.000	0.000	0.000
34	A	26	THR	0	-0.005	-0.026	21.741	0.033	0.033	0.000	0.000	0.000	0.000
35	A	27	ALA	0	0.099	0.038	24.281	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	28	VAL	0	0.039	0.045	26.241	0.012	0.012	0.000	0.000	0.000	0.000
37	A	29	TRP	0	0.086	0.031	28.419	0.009	0.009	0.000	0.000	0.000	0.000
38	A	30	CYS	0	-0.005	0.033	29.620	0.014	0.014	0.000	0.000	0.000	0.000
39	A	31	GLY	0	0.035	0.010	31.013	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	32	PRO	0	0.045	0.000	30.853	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	33	CYS	0	-0.041	0.001	26.860	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	34	LYS	1	0.897	0.943	27.111	0.132	0.132	0.000	0.000	0.000	0.000
43	A	35	THR	0	-0.100	-0.050	29.359	0.003	0.003	0.000	0.000	0.000	0.000
44	A	36	ILE	0	-0.012	-0.001	24.048	0.006	0.006	0.000	0.000	0.000	0.000
45	A	37	GLU	-1	-0.842	-0.903	24.162	-0.232	-0.232	0.000	0.000	0.000	0.000
46	A	38	ARG	1	1.035	1.022	23.708	0.120	0.120	0.000	0.000	0.000	0.000
47	A	39	PRO	0	-0.031	-0.022	24.564	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	40	MET	0	-0.012	0.009	18.827	0.007	0.007	0.000	0.000	0.000	0.000
49	A	41	GLU	-1	-0.918	-0.959	19.805	-0.214	-0.214	0.000	0.000	0.000	0.000
50	A	42	LYS	1	0.894	0.954	20.185	0.086	0.086	0.000	0.000	0.000	0.000
51	A	43	ILE	0	-0.041	-0.022	18.099	0.013	0.013	0.000	0.000	0.000	0.000
52	A	44	ALA	0	-0.006	-0.007	16.023	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	45	TYR	0	-0.029	-0.021	15.862	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	46	GLU	-1	-0.807	-0.896	17.804	-0.077	-0.077	0.000	0.000	0.000	0.000
55	A	47	PHE	0	-0.038	-0.008	15.454	0.037	0.037	0.000	0.000	0.000	0.000
56	A	48	PRO	0	0.057	0.031	12.618	-0.064	-0.064	0.000	0.000	0.000	0.000
57	A	49	THR	0	-0.013	-0.017	10.203	-0.119	-0.119	0.000	0.000	0.000	0.000
58	A	50	VAL	0	-0.039	-0.007	9.512	-0.060	-0.060	0.000	0.000	0.000	0.000
59	A	51	LYS	1	0.780	0.883	4.474	3.597	3.647	-0.001	-0.007	-0.042	0.000
60	A	52	PHE	0	0.032	0.006	10.070	0.068	0.068	0.000	0.000	0.000	0.000
61	A	53	ALA	0	0.034	0.023	12.124	-0.021	-0.021	0.000	0.000	0.000	0.000
62	A	54	LYS	1	0.849	0.929	13.791	0.374	0.374	0.000	0.000	0.000	0.000
63	A	55	VAL	0	0.019	-0.004	17.222	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	56	ASP	-1	-0.778	-0.893	19.408	-0.199	-0.199	0.000	0.000	0.000	0.000
65	A	57	ALA	0	0.015	-0.019	22.864	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	58	ASP	-1	-0.914	-0.953	24.928	-0.167	-0.167	0.000	0.000	0.000	0.000
67	A	59	ASN	0	-0.078	-0.055	23.336	0.008	0.008	0.000	0.000	0.000	0.000
68	A	60	ASN	0	-0.064	-0.042	19.786	-0.034	-0.034	0.000	0.000	0.000	0.000
69	A	61	SER	0	0.060	0.030	22.789	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.806	-0.892	23.140	-0.202	-0.202	0.000	0.000	0.000	0.000
71	A	63	ILE	0	0.006	0.009	17.715	0.011	0.011	0.000	0.000	0.000	0.000
72	A	64	VAL	0	0.000	0.009	21.421	0.005	0.005	0.000	0.000	0.000	0.000
73	A	65	SER	0	-0.047	-0.026	23.994	0.016	0.016	0.000	0.000	0.000	0.000
74	A	66	LYS	1	0.860	0.917	20.644	0.214	0.214	0.000	0.000	0.000	0.000
75	A	67	CYS	0	-0.085	-0.043	20.123	0.005	0.005	0.000	0.000	0.000	0.000
76	A	68	ARG	1	0.909	0.967	22.631	0.134	0.134	0.000	0.000	0.000	0.000
77	A	69	VAL	0	-0.011	0.004	22.913	0.010	0.010	0.000	0.000	0.000	0.000
78	A	70	LEU	0	0.012	0.004	26.130	0.002	0.002	0.000	0.000	0.000	0.000
79	A	71	GLN	0	-0.002	0.001	28.550	0.002	0.002	0.000	0.000	0.000	0.000
80	A	72	LEU	0	0.021	0.033	25.433	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	73	PRO	0	-0.007	-0.023	24.801	0.011	0.011	0.000	0.000	0.000	0.000
82	A	74	THR	0	-0.051	-0.036	22.922	0.021	0.021	0.000	0.000	0.000	0.000
83	A	75	PHE	0	-0.020	-0.013	19.670	-0.027	-0.027	0.000	0.000	0.000	0.000
84	A	76	ILE	0	-0.006	-0.002	17.831	0.033	0.033	0.000	0.000	0.000	0.000
85	A	77	ILE	0	-0.007	-0.001	15.214	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	78	ALA	0	0.019	0.001	13.098	0.051	0.051	0.000	0.000	0.000	0.000
87	A	79	ARG	1	0.868	0.896	8.631	-0.476	-0.476	0.000	0.000	0.000	0.000
88	A	80	SER	0	-0.003	-0.015	9.130	0.101	0.101	0.000	0.000	0.000	0.000
89	A	81	GLY	0	-0.003	0.012	10.367	0.057	0.057	0.000	0.000	0.000	0.000
90	A	82	LYS	1	0.900	0.969	13.046	-0.014	-0.014	0.000	0.000	0.000	0.000
91	A	83	MET	0	-0.004	0.004	14.911	-0.040	-0.040	0.000	0.000	0.000	0.000
92	A	84	LEU	0	-0.032	-0.029	13.984	0.039	0.039	0.000	0.000	0.000	0.000
93	A	85	GLY	0	0.029	0.012	18.098	0.021	0.021	0.000	0.000	0.000	0.000
94	A	86	HIS	0	0.022	0.012	19.707	-0.030	-0.030	0.000	0.000	0.000	0.000
95	A	87	VAL	0	-0.018	-0.017	22.062	0.022	0.022	0.000	0.000	0.000	0.000
96	A	88	ILE	0	0.049	0.034	24.173	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	89	GLY	0	0.077	0.046	26.992	0.011	0.011	0.000	0.000	0.000	0.000
98	A	90	ALA	0	0.016	0.005	26.983	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	91	ASN	0	-0.037	-0.023	27.117	0.014	0.014	0.000	0.000	0.000	0.000
100	A	92	PRO	0	0.057	0.017	23.931	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	93	GLY	0	0.013	0.001	23.956	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	94	MET	0	0.027	0.016	25.408	0.004	0.004	0.000	0.000	0.000	0.000
103	A	95	LEU	0	0.005	0.011	18.269	0.005	0.005	0.000	0.000	0.000	0.000
104	A	96	ARG	1	0.841	0.900	20.789	0.114	0.114	0.000	0.000	0.000	0.000
105	A	97	GLN	0	-0.039	-0.024	21.761	0.005	0.005	0.000	0.000	0.000	0.000
106	A	98	LYS	1	0.921	0.956	20.457	0.110	0.110	0.000	0.000	0.000	0.000
107	A	99	LEU	0	0.012	0.004	15.452	0.006	0.006	0.000	0.000	0.000	0.000
108	A	100	ARG	1	0.892	0.932	18.224	0.065	0.065	0.000	0.000	0.000	0.000
109	A	101	ASP	-1	-0.797	-0.870	20.562	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	102	ILE	0	-0.002	-0.006	15.762	0.011	0.011	0.000	0.000	0.000	0.000
111	A	103	ILE	0	-0.064	-0.039	14.924	0.021	0.021	0.000	0.000	0.000	0.000
112	A	104	LYS	1	0.810	0.916	17.314	0.022	0.022	0.000	0.000	0.000	0.000
113	A	105	ASP	-1	-0.968	-0.971	18.662	0.082	0.082	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-7:ILE)