FMO DATABASE

FMODB ID: YZ852

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1136834.87506
FMO2-HF: Nuclear repulsion	1086069.541022
FMO2-HF: Total energy	-50765.334038
FMO2-MP2: Total energy	-50914.495323

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.
-19.511	-25.907	21.143	-6.849	-7.897	0.062

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 : 0.053 / q_NPA : 0.040

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

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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	-0.001	-0.002	3.856	0.724	2.714	-0.013	-0.836	-1.141	0.004
4	A	4	VAL	0	0.013	0.015	5.905	0.139	0.139	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.891	-0.935	8.787	-0.342	-0.342	0.000	0.000	0.000	0.000
6	A	6	GLN	0	0.001	-0.014	12.246	0.129	0.129	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.851	0.885	13.833	-0.095	-0.095	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.019	0.024	16.325	0.012	0.012	0.000	0.000	0.000	0.000
9	A	9	HIS	1	0.869	0.929	17.898	-0.224	-0.224	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.932	0.968	17.920	0.255	0.255	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.005	0.013	20.407	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.040	-0.012	20.079	0.010	0.010	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.031	0.018	21.280	-0.030	-0.030	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.910	0.937	17.236	0.102	0.102	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.004	-0.005	20.626	0.004	0.004	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.012	0.013	23.378	0.013	0.013	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.027	-0.004	19.944	0.024	0.024	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.081	0.032	17.619	0.046	0.046	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.863	0.913	15.107	0.112	0.112	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.031	-0.006	12.164	0.036	0.036	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.016	-0.002	8.914	-0.144	-0.144	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.025	-0.016	2.652	-1.055	-0.283	0.368	-0.174	-0.965	0.000
23	A	23	ILE	0	0.010	0.009	6.874	0.511	0.511	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.879	0.930	2.183	-21.633	-30.791	20.788	-5.839	-5.791	0.058
25	A	25	GLU	-1	-0.891	-0.947	5.198	1.054	1.054	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.023	0.017	6.720	0.910	0.910	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.107	-0.102	5.782	0.669	0.669	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.000	0.006	7.784	0.002	0.002	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.796	-0.859	6.832	1.621	1.621	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.001	0.007	9.570	-0.270	-0.270	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.816	-0.878	12.702	-0.098	-0.098	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.001	-0.019	14.542	-0.042	-0.042	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.846	-0.901	18.309	-0.039	-0.039	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.054	-0.047	20.828	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.022	-0.021	23.908	-0.016	-0.016	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.793	-0.905	27.179	0.042	0.042	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.901	-0.954	30.502	0.013	0.013	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.071	0.002	23.917	0.003	0.003	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.816	0.908	29.561	-0.022	-0.022	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.045	-0.021	31.968	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.844	-0.936	34.629	0.088	0.088	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.837	-0.914	35.804	0.052	0.052	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.813	0.905	35.296	-0.073	-0.073	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.005	0.001	32.339	0.001	0.001	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.027	0.000	29.968	0.007	0.007	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.024	0.003	25.512	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	47	HIS	0	0.025	0.010	28.816	0.023	0.023	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.045	0.012	26.720	0.009	0.009	0.000	0.000	0.000	0.000
49	A	49	GLY	0	-0.001	-0.007	26.054	0.025	0.025	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.031	0.014	24.559	0.010	0.010	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.020	0.017	21.394	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	PHE	0	-0.004	-0.003	21.140	0.051	0.051	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.029	0.021	21.946	0.031	0.031	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.013	-0.006	15.929	0.021	0.021	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.009	-0.020	17.398	0.061	0.061	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.905	-0.957	17.837	0.424	0.424	0.000	0.000	0.000	0.000
57	A	57	TYR	0	-0.006	-0.015	16.755	0.003	0.003	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.032	0.007	13.494	0.019	0.019	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.028	0.004	14.119	0.160	0.160	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.064	-0.025	15.646	0.014	0.014	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.037	-0.025	12.521	-0.073	-0.073	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.018	0.023	10.887	0.088	0.088	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.062	-0.028	11.560	0.073	0.073	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.006	0.006	11.243	-0.120	-0.120	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.769	-0.876	14.081	0.129	0.129	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.019	-0.024	17.009	0.014	0.014	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.046	-0.037	19.954	0.003	0.003	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.071	-0.008	17.751	0.009	0.009	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.039	0.005	20.807	-0.030	-0.030	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.008	0.004	21.917	0.046	0.046	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.036	-0.013	23.853	-0.033	-0.033	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.846	0.911	25.524	-0.397	-0.397	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.031	0.012	24.442	0.041	0.041	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.815	-0.848	24.864	0.377	0.377	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.004	-0.010	23.080	0.046	0.046	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.929	0.974	24.437	-0.435	-0.435	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.002	0.004	24.343	0.030	0.030	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.030	-0.039	23.000	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.859	0.921	23.269	-0.312	-0.312	0.000	0.000	0.000	0.000
80	A	80	PRO	0	-0.008	0.013	25.508	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.036	0.016	23.286	0.005	0.005	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.910	0.957	25.865	-0.092	-0.092	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.017	0.000	26.073	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.021	-0.004	25.575	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.810	-0.871	22.073	0.137	0.137	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.858	0.924	14.873	0.074	0.074	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.043	-0.041	17.580	0.035	0.035	0.000	0.000	0.000	0.000
88	A	88	VAL	0	0.008	-0.006	10.810	-0.045	-0.045	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.010	0.013	13.872	0.069	0.069	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.847	0.914	7.914	-1.078	-1.078	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.015	0.012	11.265	-0.100	-0.100	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.965	0.979	10.198	-1.797	-1.797	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.003	0.006	11.870	-0.299	-0.299	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.090	-0.054	13.482	0.184	0.184	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.906	-0.961	16.094	0.603	0.603	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.822	-0.900	15.965	0.686	0.686	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.021	-0.021	18.169	-0.052	-0.052	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.029	0.023	20.416	-0.064	-0.064	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.980	0.984	20.188	-0.250	-0.250	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.909	0.981	22.113	-0.447	-0.447	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.859	0.924	15.524	-0.631	-0.631	0.000	0.000	0.000	0.000
102	A	102	ILE	0	-0.012	0.001	18.880	-0.059	-0.059	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.001	0.001	14.606	0.120	0.120	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.854	-0.909	15.965	0.789	0.789	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.016	-0.016	15.056	0.164	0.164	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.854	0.933	14.978	-0.956	-0.956	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.002	-0.007	14.873	0.067	0.067	0.000	0.000	0.000	0.000
108	A	108	TYR	0	0.005	-0.012	13.465	0.055	0.055	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.810	0.887	16.479	-0.243	-0.243	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.961	-0.986	15.871	0.106	0.106	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.895	-0.953	14.372	0.523	0.523	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.867	-0.893	16.986	0.296	0.296	0.000	0.000	0.000	0.000
113	A	113	VAL	0	0.015	0.012	17.558	0.012	0.012	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.021	-0.006	19.562	-0.042	-0.042	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.004	-0.006	20.280	-0.032	-0.032	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.870	-0.926	19.512	0.664	0.664	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.013	-0.003	19.842	-0.075	-0.075	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.867	0.945	19.919	-0.647	-0.647	0.000	0.000	0.000	0.000
119	A	119	PHE	0	0.041	0.004	19.522	-0.071	-0.071	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.097	-0.078	20.407	0.062	0.062	0.000	0.000	0.000	0.000
121	A	121	CYS	0	0.015	0.004	19.298	-0.052	-0.052	0.000	0.000	0.000	0.000
122	A	122	TYR	0	-0.002	-0.010	21.408	0.025	0.025	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.032	0.021	18.722	-0.015	-0.015	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.044	-0.020	21.866	-0.007	-0.007	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.881	-0.920	24.600	0.108	0.108	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.892	0.931	26.805	-0.056	-0.056	0.000	0.000	0.000	0.000
127	A	127	HIS	0	0.007	-0.013	25.052	0.019	0.019	0.000	0.000	0.000	0.000
128	A	128	VAL	0	0.062	0.019	26.929	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	129	LEU	0	-0.048	-0.008	28.800	0.000	0.000	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.931	-0.945	31.204	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)