FMO DATABASE

FMODB ID: V5L31

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1137685.856451
FMO2-HF: Nuclear repulsion	1086920.289476
FMO2-HF: Total energy	-50765.566974
FMO2-MP2: Total energy	-50914.729832

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.
-18.85	-25.995	22.847	-7.513	-8.19	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 : 0.056 / q_NPA : 0.047

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	0.002	0.001	3.880	0.485	2.575	-0.012	-0.923	-1.156	0.004
4	A	4	VAL	0	-0.008	-0.003	5.704	0.215	0.215	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.837	-0.895	8.936	-0.288	-0.288	0.000	0.000	0.000	0.000
6	A	6	GLN	0	0.043	0.019	12.397	0.129	0.129	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.812	0.868	13.606	-0.034	-0.034	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.019	0.031	16.165	0.014	0.014	0.000	0.000	0.000	0.000
9	A	9	HIS	1	0.879	0.928	17.925	-0.209	-0.209	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.879	0.932	17.751	0.289	0.289	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.008	0.009	20.121	-0.025	-0.025	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.027	-0.013	19.767	0.017	0.017	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.025	0.010	20.903	-0.031	-0.031	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.906	0.919	17.061	0.135	0.135	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.008	0.005	20.489	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.014	0.014	23.262	0.011	0.011	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.041	-0.015	20.086	0.023	0.023	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.065	0.025	17.598	0.051	0.051	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.782	0.862	15.499	0.130	0.130	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.026	-0.016	11.717	0.029	0.029	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.008	0.007	8.615	-0.143	-0.143	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.024	-0.011	2.451	-1.125	-0.392	0.845	-0.230	-1.348	-0.001
23	A	23	ILE	0	0.017	0.013	6.604	0.500	0.500	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.871	0.929	2.139	-21.251	-31.219	22.014	-6.360	-5.686	0.059
25	A	25	GLU	-1	-0.868	-0.931	5.273	0.978	0.978	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.008	0.005	6.561	1.001	1.001	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.103	-0.090	5.839	0.826	0.826	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.011	-0.002	7.512	0.113	0.113	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.807	-0.870	6.794	1.656	1.656	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.016	0.009	9.501	-0.277	-0.277	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.825	-0.879	12.579	-0.094	-0.094	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.005	-0.009	14.686	-0.046	-0.046	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.770	-0.860	18.327	-0.067	-0.067	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.045	-0.051	20.996	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.039	0.016	24.048	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.781	-0.897	26.965	0.036	0.036	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.907	-0.964	30.096	0.004	0.004	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.077	-0.014	23.486	0.004	0.004	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.803	0.899	29.252	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.040	-0.022	31.707	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.821	-0.918	34.481	0.082	0.082	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.837	-0.898	35.758	0.048	0.048	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.806	0.889	35.056	-0.070	-0.070	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.012	0.014	32.413	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.033	-0.014	29.938	0.006	0.006	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.004	-0.008	25.324	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	47	HIS	0	0.023	0.014	28.645	0.025	0.025	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.048	0.017	26.371	0.008	0.008	0.000	0.000	0.000	0.000
49	A	49	GLY	0	-0.002	-0.011	25.688	0.026	0.026	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.032	0.017	24.134	0.011	0.011	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.008	0.003	21.188	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	PHE	0	0.003	0.004	20.898	0.054	0.054	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.023	0.013	21.657	0.032	0.032	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.004	0.001	16.007	0.015	0.015	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.004	-0.007	17.180	0.066	0.066	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.915	-0.956	17.714	0.405	0.405	0.000	0.000	0.000	0.000
57	A	57	TYR	0	0.000	-0.005	16.631	0.020	0.020	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.031	0.005	13.459	0.019	0.019	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.015	-0.003	13.941	0.166	0.166	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.067	-0.031	15.537	0.015	0.015	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.039	-0.025	12.508	-0.075	-0.075	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.009	0.013	10.892	0.113	0.113	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.040	-0.023	11.707	0.079	0.079	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.020	-0.016	10.888	-0.122	-0.122	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.743	-0.842	13.767	0.052	0.052	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.024	-0.021	16.851	0.015	0.015	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.029	-0.031	19.882	0.005	0.005	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.085	-0.017	17.795	0.011	0.011	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.047	0.002	20.886	-0.027	-0.027	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.001	0.004	21.647	0.045	0.045	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.012	-0.001	23.650	-0.034	-0.034	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.804	0.889	25.395	-0.387	-0.387	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.025	0.010	23.845	0.040	0.040	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.816	-0.859	24.532	0.355	0.355	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.008	0.001	22.834	0.049	0.049	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.897	0.951	24.128	-0.452	-0.452	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.025	0.012	24.064	0.029	0.029	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.034	-0.023	22.667	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.870	0.928	23.082	-0.314	-0.314	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.004	0.019	25.517	0.006	0.006	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.041	0.018	23.101	0.008	0.008	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.862	0.928	25.838	-0.083	-0.083	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.013	0.011	26.135	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.014	0.003	25.761	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.806	-0.877	22.144	0.127	0.127	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.839	0.914	14.956	0.087	0.087	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.011	-0.009	17.720	0.037	0.037	0.000	0.000	0.000	0.000
88	A	88	VAL	0	0.011	-0.011	10.896	-0.052	-0.052	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.006	0.008	13.931	0.064	0.064	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.859	0.917	7.767	-1.048	-1.048	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.021	0.014	10.766	-0.148	-0.148	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.946	0.972	9.840	-1.654	-1.654	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.006	0.007	11.843	-0.300	-0.300	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.095	-0.053	13.381	0.209	0.209	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.907	-0.958	16.173	0.592	0.592	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.817	-0.897	15.511	0.665	0.665	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.001	-0.012	17.770	-0.049	-0.049	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.021	0.020	19.877	-0.063	-0.063	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.970	0.980	20.031	-0.252	-0.252	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.905	0.976	22.048	-0.466	-0.466	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.853	0.921	15.095	-0.621	-0.621	0.000	0.000	0.000	0.000
102	A	102	ILE	0	-0.016	-0.002	18.774	-0.045	-0.045	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.018	0.015	14.541	0.112	0.112	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.866	-0.919	15.795	0.750	0.750	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.008	-0.008	14.898	0.186	0.186	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.823	0.903	14.812	-0.943	-0.943	0.000	0.000	0.000	0.000
107	A	107	VAL	0	0.012	-0.003	14.672	0.072	0.072	0.000	0.000	0.000	0.000
108	A	108	TYR	0	-0.009	-0.003	13.474	0.050	0.050	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.777	0.861	16.600	-0.240	-0.240	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.931	-0.973	15.706	0.092	0.092	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.892	-0.939	13.976	0.542	0.542	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.873	-0.913	16.671	0.296	0.296	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.002	-0.002	17.238	0.002	0.002	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.029	-0.006	19.241	-0.041	-0.041	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.016	-0.010	19.997	-0.032	-0.032	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.860	-0.911	19.268	0.662	0.662	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.043	0.002	19.744	-0.079	-0.079	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.869	0.942	19.674	-0.632	-0.632	0.000	0.000	0.000	0.000
119	A	119	PHE	0	0.048	0.004	19.124	-0.072	-0.072	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.054	-0.051	20.031	0.060	0.060	0.000	0.000	0.000	0.000
121	A	121	CYS	0	0.002	0.003	18.968	-0.056	-0.056	0.000	0.000	0.000	0.000
122	A	122	TYR	0	-0.003	-0.013	21.043	0.025	0.025	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.018	0.012	18.768	-0.011	-0.011	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.027	-0.011	21.890	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.883	-0.927	24.658	0.098	0.098	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.812	0.895	27.038	-0.054	-0.054	0.000	0.000	0.000	0.000
127	A	127	HIS	0	0.047	0.011	25.417	0.023	0.023	0.000	0.000	0.000	0.000
128	A	128	VAL	0	0.039	0.014	27.090	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	129	LEU	0	-0.037	-0.010	28.833	0.000	0.000	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.886	-0.919	31.066	0.025	0.025	0.000	0.000	0.000	0.000

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