FMO DATABASE

FMODB ID: ZVK3N

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	OptH
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	-943634.836212
FMO2-HF: Nuclear repulsion	897383.8784
FMO2-HF: Total energy	-46250.957812
FMO2-MP2: Total energy	-46381.99856

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.
-4.65	-0.816	1.028	-2.013	-2.849	-0.01

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 : 0.035 / q_NPA : 0.009

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	-0.006	0.002	2.612	-1.495	1.155	1.003	-1.505	-2.148	-0.007
4	A	-4	ARG	1	1.002	1.002	3.977	0.110	0.299	-0.001	-0.017	-0.171	0.000
5	A	-3	ALA	0	-0.020	-0.016	6.387	-0.119	-0.119	0.000	0.000	0.000	0.000
6	A	-2	ARG	1	0.901	0.937	8.902	0.472	0.472	0.000	0.000	0.000	0.000
7	A	-1	TYR	0	0.056	0.030	10.950	0.076	0.076	0.000	0.000	0.000	0.000
8	A	0	PRO	0	0.004	0.003	13.318	-0.076	-0.076	0.000	0.000	0.000	0.000
9	A	1	SER	0	-0.007	-0.004	13.973	-0.004	-0.004	0.000	0.000	0.000	0.000
10	A	2	VAL	0	0.012	0.014	14.070	-0.048	-0.048	0.000	0.000	0.000	0.000
11	A	3	VAL	0	-0.045	-0.013	9.993	-0.054	-0.054	0.000	0.000	0.000	0.000
12	A	4	ASP	-1	-0.900	-0.940	13.198	-0.335	-0.335	0.000	0.000	0.000	0.000
13	A	5	VAL	0	-0.055	-0.032	13.979	-0.095	-0.095	0.000	0.000	0.000	0.000
14	A	6	TYR	0	0.024	0.003	15.723	0.070	0.070	0.000	0.000	0.000	0.000
15	A	7	SER	0	0.053	0.022	15.850	0.027	0.027	0.000	0.000	0.000	0.000
16	A	8	VAL	0	0.049	0.013	16.567	-0.042	-0.042	0.000	0.000	0.000	0.000
17	A	9	GLU	-1	-0.799	-0.889	13.888	-0.571	-0.571	0.000	0.000	0.000	0.000
18	A	10	GLN	0	0.006	0.005	11.512	0.020	0.020	0.000	0.000	0.000	0.000
19	A	11	PHE	0	0.031	0.002	11.650	-0.107	-0.107	0.000	0.000	0.000	0.000
20	A	12	ARG	1	0.883	0.942	12.646	0.499	0.499	0.000	0.000	0.000	0.000
21	A	13	ASN	0	-0.004	-0.003	8.834	0.108	0.108	0.000	0.000	0.000	0.000
22	A	14	ILE	0	-0.024	-0.008	7.984	-0.130	-0.130	0.000	0.000	0.000	0.000
23	A	15	MET	0	-0.053	-0.023	8.537	0.093	0.093	0.000	0.000	0.000	0.000
24	A	16	SER	0	-0.019	-0.015	9.762	0.211	0.211	0.000	0.000	0.000	0.000
25	A	17	GLU	-1	-0.892	-0.946	3.305	-5.939	-5.253	0.016	-0.408	-0.294	-0.003
26	A	18	ASP	-1	-0.834	-0.897	5.840	1.562	1.562	0.000	0.000	0.000	0.000
27	A	19	ILE	0	-0.066	-0.043	3.241	0.382	0.691	0.010	-0.083	-0.236	0.000
28	A	20	LEU	0	-0.033	0.002	7.510	-0.318	-0.318	0.000	0.000	0.000	0.000
29	A	21	THR	0	0.025	-0.005	9.448	-0.135	-0.135	0.000	0.000	0.000	0.000
30	A	22	VAL	0	-0.017	-0.007	11.781	0.039	0.039	0.000	0.000	0.000	0.000
31	A	23	ALA	0	0.014	0.014	14.970	-0.064	-0.064	0.000	0.000	0.000	0.000
32	A	24	TRP	0	0.025	-0.003	16.485	0.042	0.042	0.000	0.000	0.000	0.000
33	A	25	PHE	0	0.025	0.015	19.434	-0.028	-0.028	0.000	0.000	0.000	0.000
34	A	26	THR	0	-0.019	-0.044	22.183	0.031	0.031	0.000	0.000	0.000	0.000
35	A	27	ALA	0	0.129	0.058	24.659	-0.013	-0.013	0.000	0.000	0.000	0.000
36	A	28	VAL	0	0.056	0.041	26.870	0.011	0.011	0.000	0.000	0.000	0.000
37	A	29	TRP	0	-0.015	-0.012	28.978	0.010	0.010	0.000	0.000	0.000	0.000
38	A	30	CYS	0	0.031	0.050	29.830	0.009	0.009	0.000	0.000	0.000	0.000
39	A	31	GLY	0	-0.019	-0.012	31.233	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	32	PRO	0	0.093	0.019	31.144	0.000	0.000	0.000	0.000	0.000	0.000
41	A	33	CYS	0	-0.049	-0.018	26.776	0.004	0.004	0.000	0.000	0.000	0.000
42	A	34	LYS	1	1.007	1.021	27.613	0.083	0.083	0.000	0.000	0.000	0.000
43	A	35	THR	0	-0.091	-0.049	29.529	0.005	0.005	0.000	0.000	0.000	0.000
44	A	36	ILE	0	-0.025	-0.017	24.993	0.008	0.008	0.000	0.000	0.000	0.000
45	A	37	GLU	-1	-0.914	-0.955	24.896	-0.121	-0.121	0.000	0.000	0.000	0.000
46	A	38	ARG	1	1.027	1.009	24.370	0.050	0.050	0.000	0.000	0.000	0.000
47	A	39	PRO	0	-0.035	-0.024	25.172	0.007	0.007	0.000	0.000	0.000	0.000
48	A	40	MET	0	-0.012	0.005	19.826	0.021	0.021	0.000	0.000	0.000	0.000
49	A	41	GLU	-1	-0.930	-0.952	20.538	-0.101	-0.101	0.000	0.000	0.000	0.000
50	A	42	LYS	1	0.927	0.969	20.446	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	43	ILE	0	-0.042	-0.023	18.898	0.022	0.022	0.000	0.000	0.000	0.000
52	A	44	ALA	0	0.009	-0.001	16.198	0.026	0.026	0.000	0.000	0.000	0.000
53	A	45	TYR	0	-0.045	-0.027	15.967	0.025	0.025	0.000	0.000	0.000	0.000
54	A	46	GLU	-1	-0.843	-0.917	17.537	0.100	0.100	0.000	0.000	0.000	0.000
55	A	47	PHE	0	-0.054	-0.016	15.666	0.036	0.036	0.000	0.000	0.000	0.000
56	A	48	PRO	0	0.077	0.045	12.535	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	49	THR	0	-0.035	-0.024	9.960	-0.042	-0.042	0.000	0.000	0.000	0.000
58	A	50	VAL	0	-0.009	0.008	10.088	0.127	0.127	0.000	0.000	0.000	0.000
59	A	51	LYS	1	0.887	0.961	5.418	2.093	2.093	0.000	0.000	0.000	0.000
60	A	52	PHE	0	0.033	0.010	10.686	0.045	0.045	0.000	0.000	0.000	0.000
61	A	53	ALA	0	0.016	0.005	12.266	-0.073	-0.073	0.000	0.000	0.000	0.000
62	A	54	LYS	1	0.940	0.976	14.082	0.269	0.269	0.000	0.000	0.000	0.000
63	A	55	VAL	0	0.022	-0.001	17.364	-0.044	-0.044	0.000	0.000	0.000	0.000
64	A	56	ASP	-1	-0.815	-0.920	19.468	-0.161	-0.161	0.000	0.000	0.000	0.000
65	A	57	ALA	0	-0.008	-0.029	22.873	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	58	ASP	-1	-0.913	-0.946	25.189	-0.135	-0.135	0.000	0.000	0.000	0.000
67	A	59	ASN	0	-0.088	-0.048	23.769	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	60	ASN	0	-0.063	-0.023	20.422	-0.040	-0.040	0.000	0.000	0.000	0.000
69	A	61	SER	0	0.062	0.023	23.048	0.000	0.000	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.840	-0.928	23.334	-0.211	-0.211	0.000	0.000	0.000	0.000
71	A	63	ILE	0	-0.031	-0.015	17.767	0.007	0.007	0.000	0.000	0.000	0.000
72	A	64	VAL	0	0.001	0.000	21.502	0.015	0.015	0.000	0.000	0.000	0.000
73	A	65	SER	0	-0.042	-0.009	24.190	0.017	0.017	0.000	0.000	0.000	0.000
74	A	66	LYS	1	0.928	0.962	20.507	0.228	0.228	0.000	0.000	0.000	0.000
75	A	67	CYS	0	-0.081	-0.034	20.163	0.011	0.011	0.000	0.000	0.000	0.000
76	A	68	ARG	1	0.939	0.980	22.874	0.083	0.083	0.000	0.000	0.000	0.000
77	A	69	VAL	0	-0.014	-0.006	23.061	0.013	0.013	0.000	0.000	0.000	0.000
78	A	70	LEU	0	0.006	0.004	26.257	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	71	GLN	0	-0.003	-0.001	28.605	0.003	0.003	0.000	0.000	0.000	0.000
80	A	72	LEU	0	0.010	0.041	25.759	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	73	PRO	0	-0.035	-0.036	25.025	0.007	0.007	0.000	0.000	0.000	0.000
82	A	74	THR	0	0.001	-0.016	23.027	0.019	0.019	0.000	0.000	0.000	0.000
83	A	75	PHE	0	-0.038	-0.022	20.037	-0.021	-0.021	0.000	0.000	0.000	0.000
84	A	76	ILE	0	0.009	0.003	18.103	0.024	0.024	0.000	0.000	0.000	0.000
85	A	77	ILE	0	-0.009	-0.004	15.951	-0.029	-0.029	0.000	0.000	0.000	0.000
86	A	78	ALA	0	0.017	0.001	13.721	0.005	0.005	0.000	0.000	0.000	0.000
87	A	79	ARG	1	0.900	0.933	8.939	-1.209	-1.209	0.000	0.000	0.000	0.000
88	A	80	SER	0	0.013	0.020	9.905	0.034	0.034	0.000	0.000	0.000	0.000
89	A	81	GLY	0	0.009	0.013	10.919	-0.029	-0.029	0.000	0.000	0.000	0.000
90	A	82	LYS	1	0.914	0.971	13.525	-0.221	-0.221	0.000	0.000	0.000	0.000
91	A	83	MET	0	-0.011	-0.006	15.847	0.000	0.000	0.000	0.000	0.000	0.000
92	A	84	LEU	0	-0.030	-0.032	15.035	0.030	0.030	0.000	0.000	0.000	0.000
93	A	85	GLY	0	0.025	0.013	19.013	0.011	0.011	0.000	0.000	0.000	0.000
94	A	86	HIS	0	-0.014	-0.008	20.495	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	87	VAL	0	-0.022	-0.008	22.809	0.017	0.017	0.000	0.000	0.000	0.000
96	A	88	ILE	0	0.044	0.029	24.791	-0.015	-0.015	0.000	0.000	0.000	0.000
97	A	89	GLY	0	0.085	0.043	27.526	0.009	0.009	0.000	0.000	0.000	0.000
98	A	90	ALA	0	-0.007	-0.007	27.314	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	91	ASN	0	-0.041	-0.027	27.496	0.011	0.011	0.000	0.000	0.000	0.000
100	A	92	PRO	0	0.081	0.030	24.744	0.008	0.008	0.000	0.000	0.000	0.000
101	A	93	GLY	0	0.005	0.000	24.829	0.011	0.011	0.000	0.000	0.000	0.000
102	A	94	MET	0	0.035	0.018	26.177	0.011	0.011	0.000	0.000	0.000	0.000
103	A	95	LEU	0	0.006	0.009	19.366	0.013	0.013	0.000	0.000	0.000	0.000
104	A	96	ARG	1	0.853	0.916	21.727	-0.043	-0.043	0.000	0.000	0.000	0.000
105	A	97	GLN	0	-0.029	-0.015	22.560	0.015	0.015	0.000	0.000	0.000	0.000
106	A	98	LYS	1	0.989	0.998	21.304	-0.040	-0.040	0.000	0.000	0.000	0.000
107	A	99	LEU	0	0.004	-0.004	16.346	0.019	0.019	0.000	0.000	0.000	0.000
108	A	100	ARG	1	0.863	0.916	19.158	-0.074	-0.074	0.000	0.000	0.000	0.000
109	A	101	ASP	-1	-0.848	-0.929	21.384	0.159	0.159	0.000	0.000	0.000	0.000
110	A	102	ILE	0	-0.035	-0.001	16.728	0.011	0.011	0.000	0.000	0.000	0.000
111	A	103	ILE	0	-0.083	-0.049	15.600	0.038	0.038	0.000	0.000	0.000	0.000
112	A	104	LYS	1	0.907	0.966	18.063	-0.144	-0.144	0.000	0.000	0.000	0.000
113	A	105	ASP	-1	-0.945	-0.952	19.444	0.222	0.222	0.000	0.000	0.000	0.000

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