FMO DATABASE

FMODB ID: R86R8

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	OptHSide
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	-944136.335705
FMO2-HF: Nuclear repulsion	897884.807449
FMO2-HF: Total energy	-46251.528255
FMO2-MP2: Total energy	-46382.595653

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.
-4.343	0.245	0.985	-2.443	-3.13	-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 : 0.045 / q_NPA : 0.029

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	-0.002	0.004	2.633	-2.592	1.255	0.951	-2.214	-2.585	-0.001
4	A	-4	ARG	1	1.000	0.998	3.979	-0.332	-0.141	-0.001	-0.018	-0.172	0.000
5	A	-3	ALA	0	-0.018	-0.014	6.437	-0.096	-0.096	0.000	0.000	0.000	0.000
6	A	-2	ARG	1	0.899	0.924	9.081	0.699	0.699	0.000	0.000	0.000	0.000
7	A	-1	TYR	0	0.060	0.035	10.967	0.047	0.047	0.000	0.000	0.000	0.000
8	A	0	PRO	0	0.012	0.010	13.315	-0.084	-0.084	0.000	0.000	0.000	0.000
9	A	1	SER	0	-0.009	-0.012	13.957	0.036	0.036	0.000	0.000	0.000	0.000
10	A	2	VAL	0	0.018	0.016	14.076	-0.090	-0.090	0.000	0.000	0.000	0.000
11	A	3	VAL	0	-0.044	-0.005	10.017	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	4	ASP	-1	-0.878	-0.932	13.312	-0.437	-0.437	0.000	0.000	0.000	0.000
13	A	5	VAL	0	-0.055	-0.031	14.264	-0.086	-0.086	0.000	0.000	0.000	0.000
14	A	6	TYR	0	0.023	0.001	15.681	0.075	0.075	0.000	0.000	0.000	0.000
15	A	7	SER	0	0.048	0.022	15.845	0.039	0.039	0.000	0.000	0.000	0.000
16	A	8	VAL	0	0.034	0.005	16.724	-0.055	-0.055	0.000	0.000	0.000	0.000
17	A	9	GLU	-1	-0.755	-0.835	13.890	-0.495	-0.495	0.000	0.000	0.000	0.000
18	A	10	GLN	0	-0.002	0.003	11.697	0.023	0.023	0.000	0.000	0.000	0.000
19	A	11	PHE	0	0.034	0.004	11.826	-0.141	-0.141	0.000	0.000	0.000	0.000
20	A	12	ARG	1	0.861	0.908	12.698	0.396	0.396	0.000	0.000	0.000	0.000
21	A	13	ASN	0	-0.037	-0.023	8.888	0.050	0.050	0.000	0.000	0.000	0.000
22	A	14	ILE	0	0.000	0.001	8.330	-0.174	-0.174	0.000	0.000	0.000	0.000
23	A	15	MET	0	-0.058	-0.022	8.791	-0.094	-0.094	0.000	0.000	0.000	0.000
24	A	16	SER	0	-0.024	-0.026	9.796	0.172	0.172	0.000	0.000	0.000	0.000
25	A	17	GLU	-1	-0.784	-0.877	4.121	-5.001	-4.886	0.000	-0.070	-0.045	0.000
26	A	18	ASP	-1	-0.769	-0.835	5.534	0.488	0.488	0.000	0.000	0.000	0.000
27	A	19	ILE	0	-0.075	-0.048	2.923	-0.148	0.287	0.035	-0.141	-0.328	0.000
28	A	20	LEU	0	-0.028	0.003	6.924	0.023	0.023	0.000	0.000	0.000	0.000
29	A	21	THR	0	0.033	0.001	9.175	-0.191	-0.191	0.000	0.000	0.000	0.000
30	A	22	VAL	0	-0.022	-0.006	11.571	0.117	0.117	0.000	0.000	0.000	0.000
31	A	23	ALA	0	0.015	0.016	15.016	-0.060	-0.060	0.000	0.000	0.000	0.000
32	A	24	TRP	0	0.009	-0.011	16.617	0.054	0.054	0.000	0.000	0.000	0.000
33	A	25	PHE	0	0.025	0.012	19.581	-0.017	-0.017	0.000	0.000	0.000	0.000
34	A	26	THR	0	-0.006	-0.032	22.445	0.034	0.034	0.000	0.000	0.000	0.000
35	A	27	ALA	0	0.107	0.049	24.961	-0.007	-0.007	0.000	0.000	0.000	0.000
36	A	28	VAL	0	0.063	0.051	26.996	0.008	0.008	0.000	0.000	0.000	0.000
37	A	29	TRP	0	0.011	0.001	29.065	0.009	0.009	0.000	0.000	0.000	0.000
38	A	30	CYS	0	0.028	0.019	30.124	0.013	0.013	0.000	0.000	0.000	0.000
39	A	31	GLY	0	0.008	0.005	31.476	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	32	PRO	0	0.072	0.012	31.270	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	33	CYS	0	-0.027	0.008	27.467	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	34	LYS	1	0.944	0.973	27.751	0.141	0.141	0.000	0.000	0.000	0.000
43	A	35	THR	0	-0.083	-0.034	29.638	0.001	0.001	0.000	0.000	0.000	0.000
44	A	36	ILE	0	-0.026	-0.013	24.695	0.005	0.005	0.000	0.000	0.000	0.000
45	A	37	GLU	-1	-0.849	-0.916	24.956	-0.244	-0.244	0.000	0.000	0.000	0.000
46	A	38	ARG	1	1.033	1.014	24.389	0.124	0.124	0.000	0.000	0.000	0.000
47	A	39	PRO	0	-0.034	-0.025	25.113	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	40	MET	0	-0.012	0.007	19.439	0.007	0.007	0.000	0.000	0.000	0.000
49	A	41	GLU	-1	-0.922	-0.952	20.409	-0.232	-0.232	0.000	0.000	0.000	0.000
50	A	42	LYS	1	0.897	0.959	20.453	0.098	0.098	0.000	0.000	0.000	0.000
51	A	43	ILE	0	-0.035	-0.021	18.571	0.010	0.010	0.000	0.000	0.000	0.000
52	A	44	ALA	0	-0.001	-0.001	16.209	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	45	TYR	0	-0.047	-0.028	15.972	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	46	GLU	-1	-0.797	-0.890	17.543	-0.094	-0.094	0.000	0.000	0.000	0.000
55	A	47	PHE	0	-0.054	-0.013	15.481	0.042	0.042	0.000	0.000	0.000	0.000
56	A	48	PRO	0	0.087	0.050	12.493	-0.072	-0.072	0.000	0.000	0.000	0.000
57	A	49	THR	0	-0.029	-0.016	9.960	-0.130	-0.130	0.000	0.000	0.000	0.000
58	A	50	VAL	0	-0.018	0.002	9.717	-0.067	-0.067	0.000	0.000	0.000	0.000
59	A	51	LYS	1	0.776	0.895	5.248	3.265	3.265	0.000	0.000	0.000	0.000
60	A	52	PHE	0	0.047	0.012	10.550	0.089	0.089	0.000	0.000	0.000	0.000
61	A	53	ALA	0	0.017	0.009	12.511	-0.045	-0.045	0.000	0.000	0.000	0.000
62	A	54	LYS	1	0.863	0.935	14.372	0.383	0.383	0.000	0.000	0.000	0.000
63	A	55	VAL	0	0.019	-0.005	17.748	-0.027	-0.027	0.000	0.000	0.000	0.000
64	A	56	ASP	-1	-0.800	-0.900	19.898	-0.218	-0.218	0.000	0.000	0.000	0.000
65	A	57	ALA	0	-0.008	-0.027	23.208	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	58	ASP	-1	-0.912	-0.949	25.586	-0.178	-0.178	0.000	0.000	0.000	0.000
67	A	59	ASN	0	-0.089	-0.060	23.804	0.010	0.010	0.000	0.000	0.000	0.000
68	A	60	ASN	0	-0.054	-0.022	20.212	-0.034	-0.034	0.000	0.000	0.000	0.000
69	A	61	SER	0	0.067	0.026	23.322	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.800	-0.903	23.436	-0.226	-0.226	0.000	0.000	0.000	0.000
71	A	63	ILE	0	-0.005	0.000	18.067	0.006	0.006	0.000	0.000	0.000	0.000
72	A	64	VAL	0	0.011	0.009	21.811	0.005	0.005	0.000	0.000	0.000	0.000
73	A	65	SER	0	-0.044	-0.009	24.574	0.016	0.016	0.000	0.000	0.000	0.000
74	A	66	LYS	1	0.868	0.925	20.831	0.245	0.245	0.000	0.000	0.000	0.000
75	A	67	CYS	0	-0.098	-0.048	20.579	0.000	0.000	0.000	0.000	0.000	0.000
76	A	68	ARG	1	0.936	0.977	23.136	0.154	0.154	0.000	0.000	0.000	0.000
77	A	69	VAL	0	-0.010	-0.002	23.319	0.009	0.009	0.000	0.000	0.000	0.000
78	A	70	LEU	0	0.000	0.001	26.481	0.005	0.005	0.000	0.000	0.000	0.000
79	A	71	GLN	0	0.007	0.004	28.789	0.003	0.003	0.000	0.000	0.000	0.000
80	A	72	LEU	0	-0.001	0.037	26.046	-0.016	-0.016	0.000	0.000	0.000	0.000
81	A	73	PRO	0	-0.010	-0.026	25.052	0.014	0.014	0.000	0.000	0.000	0.000
82	A	74	THR	0	-0.025	-0.025	23.198	0.021	0.021	0.000	0.000	0.000	0.000
83	A	75	PHE	0	-0.029	-0.017	20.096	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	76	ILE	0	-0.001	-0.001	18.135	0.033	0.033	0.000	0.000	0.000	0.000
85	A	77	ILE	0	-0.007	-0.004	15.609	-0.052	-0.052	0.000	0.000	0.000	0.000
86	A	78	ALA	0	0.019	0.003	13.676	0.051	0.051	0.000	0.000	0.000	0.000
87	A	79	ARG	1	0.854	0.887	8.400	-0.230	-0.230	0.000	0.000	0.000	0.000
88	A	80	SER	0	-0.006	0.003	9.610	0.091	0.091	0.000	0.000	0.000	0.000
89	A	81	GLY	0	0.002	0.007	10.657	0.078	0.078	0.000	0.000	0.000	0.000
90	A	82	LYS	1	0.906	0.969	13.487	0.069	0.069	0.000	0.000	0.000	0.000
91	A	83	MET	0	-0.011	-0.004	15.583	-0.044	-0.044	0.000	0.000	0.000	0.000
92	A	84	LEU	0	-0.021	-0.028	14.557	0.037	0.037	0.000	0.000	0.000	0.000
93	A	85	GLY	0	0.028	0.014	18.622	0.024	0.024	0.000	0.000	0.000	0.000
94	A	86	HIS	0	0.016	0.009	20.274	-0.031	-0.031	0.000	0.000	0.000	0.000
95	A	87	VAL	0	-0.021	-0.015	22.606	0.024	0.024	0.000	0.000	0.000	0.000
96	A	88	ILE	0	0.047	0.032	24.673	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	89	GLY	0	0.087	0.046	27.439	0.013	0.013	0.000	0.000	0.000	0.000
98	A	90	ALA	0	-0.007	-0.006	27.237	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	91	ASN	0	-0.043	-0.028	27.349	0.017	0.017	0.000	0.000	0.000	0.000
100	A	92	PRO	0	0.079	0.030	24.518	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	93	GLY	0	0.010	0.001	24.488	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	94	MET	0	0.040	0.018	25.865	0.003	0.003	0.000	0.000	0.000	0.000
103	A	95	LEU	0	0.006	0.008	18.999	0.003	0.003	0.000	0.000	0.000	0.000
104	A	96	ARG	1	0.830	0.900	21.277	0.126	0.126	0.000	0.000	0.000	0.000
105	A	97	GLN	0	-0.047	-0.032	21.985	0.005	0.005	0.000	0.000	0.000	0.000
106	A	98	LYS	1	0.920	0.963	20.967	0.137	0.137	0.000	0.000	0.000	0.000
107	A	99	LEU	0	0.008	0.000	15.783	0.004	0.004	0.000	0.000	0.000	0.000
108	A	100	ARG	1	0.897	0.926	18.461	0.084	0.084	0.000	0.000	0.000	0.000
109	A	101	ASP	-1	-0.775	-0.870	20.743	-0.029	-0.029	0.000	0.000	0.000	0.000
110	A	102	ILE	0	-0.014	0.005	16.041	0.008	0.008	0.000	0.000	0.000	0.000
111	A	103	ILE	0	-0.067	-0.045	14.974	0.018	0.018	0.000	0.000	0.000	0.000
112	A	104	LYS	1	0.816	0.917	17.368	0.049	0.049	0.000	0.000	0.000	0.000
113	A	105	ASP	-1	-0.973	-0.965	18.910	0.050	0.050	0.000	0.000	0.000	0.000

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