FMO DATABASE

FMODB ID: 5267Z

Calculation Name: 1IXL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1IXL

Chain ID: A

ChEMBL ID:

UniProt ID: O58863

Base Structure: X-ray

Registration Date: 2023-09-20

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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1136545.115192
FMO2-HF: Nuclear repulsion	1085780.670683
FMO2-HF: Total energy	-50764.444509
FMO2-MP2: Total energy	-50913.626463

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:1:MET)

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

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.
-16.835	-23.773	19.493	-5.237	-7.317	0.043

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : -0.003

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	3	PRO	0	0.004	-0.001	3.844	0.767	2.051	-0.012	-0.398	-0.873	0.001
4	A	4	VAL	0	0.013	0.014	5.868	0.483	0.483	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.926	-0.950	8.909	-0.498	-0.498	0.000	0.000	0.000	0.000
6	A	6	GLN	0	-0.004	-0.020	12.312	0.094	0.094	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.906	0.938	14.188	-0.038	-0.038	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.013	0.015	16.430	0.021	0.021	0.000	0.000	0.000	0.000
9	A	9	HIS	1	0.881	0.935	18.021	-0.108	-0.108	0.000	0.000	0.000	0.000
10	A	10	LYS	1	1.002	1.001	18.583	0.185	0.185	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.000	0.010	20.344	-0.030	-0.030	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.033	-0.005	19.945	0.016	0.016	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.039	0.021	21.189	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.919	0.953	17.305	0.290	0.290	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.005	-0.003	20.551	-0.013	-0.013	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.013	0.012	23.316	0.008	0.008	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.026	-0.001	19.875	0.021	0.021	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.089	0.033	17.668	0.025	0.025	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.916	0.953	15.418	0.361	0.361	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.014	-0.002	12.126	0.002	0.002	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.012	0.001	8.496	-0.095	-0.095	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.013	-0.009	2.661	-1.120	-0.526	0.484	-0.156	-0.922	-0.001
23	A	23	ILE	0	0.008	0.007	6.780	0.621	0.621	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.894	0.940	2.251	-18.630	-27.446	19.021	-4.683	-5.522	0.043
25	A	25	GLU	-1	-0.894	-0.951	5.198	1.202	1.202	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.020	0.017	6.656	0.813	0.813	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.135	-0.139	5.500	0.595	0.595	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.006	0.009	7.858	-0.086	-0.086	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.851	-0.875	6.335	0.348	0.348	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.002	0.006	9.512	-0.245	-0.245	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.880	-0.910	12.730	-0.467	-0.467	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.013	-0.026	14.615	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.881	-0.927	18.386	-0.236	-0.236	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.065	-0.051	20.939	0.015	0.015	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.030	-0.014	23.973	-0.012	-0.012	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.808	-0.922	27.278	-0.053	-0.053	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.915	-0.964	30.605	-0.082	-0.082	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.093	-0.014	23.968	0.004	0.004	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.862	0.946	29.598	0.062	0.062	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.049	-0.023	31.971	0.002	0.002	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.842	-0.929	34.595	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.886	-0.971	35.802	-0.023	-0.023	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.826	0.928	35.244	0.008	0.008	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.006	0.005	32.346	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.029	0.003	29.812	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.017	0.001	25.660	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	47	HIS	0	0.031	0.013	28.736	0.014	0.014	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.038	0.008	26.600	0.000	0.000	0.000	0.000	0.000	0.000
49	A	49	GLY	0	-0.006	-0.009	25.928	0.015	0.015	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.029	0.009	24.595	0.006	0.006	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.029	0.020	21.195	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	52	PHE	0	-0.005	-0.001	21.018	0.029	0.029	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.022	0.017	21.811	0.023	0.023	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.007	-0.003	15.777	0.013	0.013	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.007	-0.021	17.242	0.031	0.031	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.915	-0.958	17.669	0.237	0.237	0.000	0.000	0.000	0.000
57	A	57	TYR	0	-0.007	-0.030	17.185	0.019	0.019	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.035	0.009	13.351	0.007	0.007	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.026	0.002	14.127	0.126	0.126	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.074	-0.030	15.691	0.035	0.035	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.028	-0.022	12.593	-0.035	-0.035	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.021	0.023	10.934	0.059	0.059	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.063	-0.028	11.570	0.099	0.099	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.009	0.004	11.267	-0.089	-0.089	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.828	-0.925	14.141	0.243	0.243	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.048	-0.038	17.048	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.056	-0.058	20.019	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.058	0.001	17.892	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.036	0.006	20.847	-0.033	-0.033	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.004	-0.003	21.981	0.041	0.041	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.033	-0.012	23.891	-0.023	-0.023	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.912	0.957	25.533	-0.279	-0.279	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.018	0.007	24.276	0.030	0.030	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.904	-0.930	24.710	0.259	0.259	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.009	-0.012	22.803	0.031	0.031	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.923	0.973	24.151	-0.257	-0.257	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.002	-0.001	24.078	0.014	0.014	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.026	-0.035	22.803	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.903	0.961	22.957	-0.115	-0.115	0.000	0.000	0.000	0.000
80	A	80	PRO	0	-0.014	0.013	25.343	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.042	0.015	23.122	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.952	0.978	25.784	0.048	0.048	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.013	-0.001	26.078	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.025	-0.008	25.670	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.811	-0.871	22.064	-0.059	-0.059	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.912	0.959	14.313	0.381	0.381	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.049	-0.049	17.547	0.024	0.024	0.000	0.000	0.000	0.000
88	A	88	VAL	0	0.004	-0.004	10.731	-0.054	-0.054	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.013	0.008	13.796	0.071	0.071	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.942	0.975	8.743	-0.261	-0.261	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.014	0.011	11.030	-0.033	-0.033	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.969	0.978	9.875	-1.489	-1.489	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.006	0.008	11.827	-0.250	-0.250	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.072	-0.045	13.399	0.159	0.159	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.902	-0.962	16.008	0.479	0.479	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.862	-0.927	16.053	0.599	0.599	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.032	-0.027	18.072	-0.038	-0.038	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.028	0.019	20.306	-0.059	-0.059	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.980	0.980	20.124	-0.234	-0.234	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.902	0.977	22.081	-0.353	-0.353	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.907	0.963	15.786	-0.492	-0.492	0.000	0.000	0.000	0.000
102	A	102	ILE	0	-0.019	0.005	18.814	-0.061	-0.061	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.005	0.000	14.713	0.098	0.098	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.968	-0.971	15.804	0.613	0.613	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.018	-0.015	14.947	0.114	0.114	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.937	0.977	14.642	-0.679	-0.679	0.000	0.000	0.000	0.000
107	A	107	VAL	0	0.004	-0.004	14.641	0.022	0.022	0.000	0.000	0.000	0.000
108	A	108	TYR	0	-0.008	-0.016	12.990	0.074	0.074	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.814	0.905	16.325	-0.036	-0.036	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.960	-0.985	15.881	-0.125	-0.125	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.878	-0.946	14.331	0.054	0.054	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.916	-0.949	16.827	0.078	0.078	0.000	0.000	0.000	0.000
113	A	113	VAL	0	0.000	0.005	17.284	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.015	-0.006	19.328	-0.016	-0.016	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.005	-0.002	19.932	-0.011	-0.011	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.902	-0.947	19.255	0.349	0.349	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.014	-0.007	19.530	-0.046	-0.046	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.924	0.981	19.629	-0.411	-0.411	0.000	0.000	0.000	0.000
119	A	119	PHE	0	0.043	0.006	19.463	-0.056	-0.056	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.068	-0.043	20.398	0.058	0.058	0.000	0.000	0.000	0.000
121	A	121	CYS	0	0.023	0.006	19.325	-0.046	-0.046	0.000	0.000	0.000	0.000
122	A	122	TYR	0	0.002	-0.005	21.410	0.032	0.032	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.023	0.013	18.683	-0.019	-0.019	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.047	-0.015	21.866	0.001	0.001	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.884	-0.913	24.611	0.121	0.121	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.900	0.952	26.821	-0.048	-0.048	0.000	0.000	0.000	0.000
127	A	127	HIS	0	-0.027	-0.044	25.344	0.015	0.015	0.000	0.000	0.000	0.000
128	A	128	VAL	0	0.069	0.018	26.982	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	129	LEU	0	-0.050	-0.012	28.853	0.000	0.000	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.912	-0.931	31.370	0.043	0.043	0.000	0.000	0.000	0.000

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