FMO DATABASE

FMODB ID: 538YZ

Calculation Name: 1L8R-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1L8R

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UI36

Base Structure: X-ray

Registration Date: 2023-06-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	101
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-756292.03617
FMO2-HF: Nuclear repulsion	715999.628775
FMO2-HF: Total energy	-40292.407395
FMO2-MP2: Total energy	-40406.336225

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:182:GLY)

Summations of interaction energy for fragment #1(A:182:GLY)

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.
-6.008	-2.019	0.265	-2.068	-2.186	-0.01

Interaction energy analysis for fragmet #1(A:182:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.074 / q_NPA : 0.042

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	184	GLN	0	0.033	0.001	3.858	-0.576	1.056	-0.008	-0.887	-0.737	0.005
4	A	185	ASN	0	0.024	0.030	6.508	0.196	0.196	0.000	0.000	0.000	0.000
5	A	186	ASN	0	-0.041	-0.040	4.086	0.354	0.447	-0.001	-0.012	-0.080	0.000
6	A	187	GLU	-1	-0.884	-0.929	2.702	-8.008	-5.923	0.275	-1.159	-1.202	-0.015
7	A	188	CYS	0	-0.098	-0.030	6.173	0.392	0.392	0.000	0.000	0.000	0.000
8	A	189	LYS	1	0.880	0.928	9.747	0.660	0.660	0.000	0.000	0.000	0.000
9	A	190	MET	0	0.011	0.005	12.663	0.074	0.074	0.000	0.000	0.000	0.000
10	A	191	VAL	0	-0.021	-0.010	16.402	-0.041	-0.041	0.000	0.000	0.000	0.000
11	A	192	ASP	-1	-0.815	-0.896	18.925	-0.147	-0.147	0.000	0.000	0.000	0.000
12	A	193	LEU	0	-0.014	-0.009	22.732	-0.023	-0.023	0.000	0.000	0.000	0.000
13	A	194	ARG	1	0.838	0.917	24.631	0.140	0.140	0.000	0.000	0.000	0.000
14	A	195	GLY	0	0.043	0.032	27.255	0.015	0.015	0.000	0.000	0.000	0.000
15	A	196	ALA	0	-0.020	-0.002	25.992	0.005	0.005	0.000	0.000	0.000	0.000
16	A	197	LYS	1	0.814	0.883	20.973	0.148	0.148	0.000	0.000	0.000	0.000
17	A	198	VAL	0	-0.008	-0.001	19.530	0.024	0.024	0.000	0.000	0.000	0.000
18	A	199	ALA	0	0.054	0.018	15.045	-0.036	-0.036	0.000	0.000	0.000	0.000
19	A	200	SER	0	-0.091	-0.051	14.501	0.004	0.004	0.000	0.000	0.000	0.000
20	A	201	PHE	0	0.061	0.020	8.858	0.009	0.009	0.000	0.000	0.000	0.000
21	A	202	THR	0	-0.011	-0.011	10.820	0.153	0.153	0.000	0.000	0.000	0.000
22	A	203	VAL	0	0.000	-0.014	11.077	-0.221	-0.221	0.000	0.000	0.000	0.000
23	A	204	GLU	-1	-0.925	-0.961	13.047	-0.371	-0.371	0.000	0.000	0.000	0.000
24	A	205	GLY	0	0.012	0.020	14.467	0.061	0.061	0.000	0.000	0.000	0.000
25	A	206	CYS	0	-0.033	-0.012	16.263	0.056	0.056	0.000	0.000	0.000	0.000
26	A	207	GLU	-1	-0.771	-0.850	15.632	-0.529	-0.529	0.000	0.000	0.000	0.000
27	A	208	LEU	0	0.002	-0.009	15.360	0.086	0.086	0.000	0.000	0.000	0.000
28	A	209	ILE	0	-0.015	0.000	16.103	-0.043	-0.043	0.000	0.000	0.000	0.000
29	A	210	CYS	0	-0.008	0.008	17.156	0.035	0.035	0.000	0.000	0.000	0.000
30	A	211	LEU	0	0.030	0.024	18.466	0.022	0.022	0.000	0.000	0.000	0.000
31	A	212	PRO	0	-0.020	-0.034	20.207	0.012	0.012	0.000	0.000	0.000	0.000
32	A	213	GLN	0	0.114	0.054	19.809	-0.017	-0.017	0.000	0.000	0.000	0.000
33	A	214	ALA	0	0.034	0.019	22.615	0.005	0.005	0.000	0.000	0.000	0.000
34	A	215	PHE	0	-0.017	-0.012	24.397	0.008	0.008	0.000	0.000	0.000	0.000
35	A	216	ASP	-1	-0.801	-0.907	25.696	-0.027	-0.027	0.000	0.000	0.000	0.000
36	A	217	LEU	0	-0.035	-0.005	24.184	0.006	0.006	0.000	0.000	0.000	0.000
37	A	218	PHE	0	-0.016	-0.012	26.644	0.002	0.002	0.000	0.000	0.000	0.000
38	A	219	LEU	0	-0.011	-0.023	29.070	0.002	0.002	0.000	0.000	0.000	0.000
39	A	220	LYS	1	0.783	0.895	28.928	0.032	0.032	0.000	0.000	0.000	0.000
40	A	221	HIS	0	0.043	0.009	32.140	0.005	0.005	0.000	0.000	0.000	0.000
41	A	222	LEU	0	-0.030	-0.004	34.781	0.001	0.001	0.000	0.000	0.000	0.000
42	A	223	VAL	0	0.000	-0.003	32.232	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	224	GLY	0	0.021	0.020	34.821	0.003	0.003	0.000	0.000	0.000	0.000
44	A	225	GLY	0	0.023	0.003	32.036	0.007	0.007	0.000	0.000	0.000	0.000
45	A	226	LEU	0	0.010	0.004	24.316	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	227	HIS	0	0.015	0.012	28.720	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	228	THR	0	0.075	0.034	30.867	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	229	VAL	0	0.019	0.024	27.064	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	230	TYR	0	-0.010	-0.024	23.508	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	231	THR	0	-0.034	-0.013	28.685	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	232	LYS	1	0.820	0.880	31.832	0.073	0.073	0.000	0.000	0.000	0.000
52	A	233	LEU	0	-0.008	-0.011	25.077	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	234	LYS	1	0.968	0.980	29.278	0.061	0.061	0.000	0.000	0.000	0.000
54	A	235	ARG	1	0.823	0.893	30.767	0.081	0.081	0.000	0.000	0.000	0.000
55	A	236	LEU	0	-0.044	-0.021	30.798	0.001	0.001	0.000	0.000	0.000	0.000
56	A	237	GLU	-1	-0.891	-0.939	30.296	-0.117	-0.117	0.000	0.000	0.000	0.000
57	A	238	ILE	0	-0.056	-0.014	25.066	-0.014	-0.014	0.000	0.000	0.000	0.000
58	A	239	THR	0	0.002	-0.006	22.856	0.018	0.018	0.000	0.000	0.000	0.000
59	A	240	PRO	0	-0.075	-0.050	21.149	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	241	VAL	0	0.063	0.052	14.662	0.016	0.016	0.000	0.000	0.000	0.000
61	A	242	VAL	0	-0.045	-0.031	16.732	0.020	0.020	0.000	0.000	0.000	0.000
62	A	243	CYS	0	-0.035	0.001	13.530	-0.023	-0.023	0.000	0.000	0.000	0.000
63	A	244	ASN	0	0.012	-0.006	8.425	0.235	0.235	0.000	0.000	0.000	0.000
64	A	245	VAL	0	0.045	-0.003	11.601	0.006	0.006	0.000	0.000	0.000	0.000
65	A	246	GLU	-1	-0.877	-0.909	4.705	1.864	2.043	-0.001	-0.010	-0.167	0.000
66	A	247	GLN	0	0.038	0.015	8.809	0.113	0.113	0.000	0.000	0.000	0.000
67	A	248	VAL	0	-0.040	-0.021	10.298	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	249	ARG	1	0.942	0.968	10.629	-0.825	-0.825	0.000	0.000	0.000	0.000
69	A	250	ILE	0	0.041	0.025	7.046	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	251	LEU	0	0.019	-0.014	11.717	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	252	ARG	1	0.823	0.905	14.850	-0.207	-0.207	0.000	0.000	0.000	0.000
72	A	253	GLY	0	-0.013	0.007	14.972	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	254	LEU	0	-0.024	-0.018	12.954	-0.019	-0.019	0.000	0.000	0.000	0.000
74	A	255	GLY	0	-0.006	0.008	16.773	-0.024	-0.024	0.000	0.000	0.000	0.000
75	A	256	ALA	0	-0.041	-0.015	17.420	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	257	ILE	0	-0.048	-0.036	16.979	-0.014	-0.014	0.000	0.000	0.000	0.000
77	A	258	GLN	0	0.068	0.026	20.368	0.032	0.032	0.000	0.000	0.000	0.000
78	A	259	PRO	0	0.068	0.020	21.224	0.007	0.007	0.000	0.000	0.000	0.000
79	A	260	GLY	0	0.028	0.022	21.491	0.020	0.020	0.000	0.000	0.000	0.000
80	A	261	VAL	0	-0.047	-0.016	20.170	0.000	0.000	0.000	0.000	0.000	0.000
81	A	262	ASN	0	0.017	0.003	18.563	0.043	0.043	0.000	0.000	0.000	0.000
82	A	263	ARG	1	0.960	0.983	18.330	-0.029	-0.029	0.000	0.000	0.000	0.000
83	A	264	CYS	0	-0.015	0.023	16.604	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	265	LYS	1	0.911	0.957	17.917	0.086	0.086	0.000	0.000	0.000	0.000
85	A	266	LEU	0	0.028	0.013	13.324	0.005	0.005	0.000	0.000	0.000	0.000
86	A	267	ILE	0	0.023	0.020	18.067	0.008	0.008	0.000	0.000	0.000	0.000
87	A	268	SER	0	0.048	0.003	19.972	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	269	ARG	1	0.860	0.892	20.334	0.353	0.353	0.000	0.000	0.000	0.000
89	A	270	LYS	1	0.948	0.979	23.410	0.229	0.229	0.000	0.000	0.000	0.000
90	A	271	ASP	-1	-0.809	-0.859	23.565	-0.219	-0.219	0.000	0.000	0.000	0.000
91	A	272	PHE	0	0.003	-0.002	24.354	0.019	0.019	0.000	0.000	0.000	0.000
92	A	273	GLU	-1	-0.769	-0.890	26.274	-0.141	-0.141	0.000	0.000	0.000	0.000
93	A	274	THR	0	-0.068	-0.039	28.886	0.012	0.012	0.000	0.000	0.000	0.000
94	A	275	LEU	0	0.011	0.004	27.448	0.012	0.012	0.000	0.000	0.000	0.000
95	A	276	TYR	0	0.019	0.009	30.239	0.012	0.012	0.000	0.000	0.000	0.000
96	A	277	ASN	0	0.052	0.030	31.897	0.013	0.013	0.000	0.000	0.000	0.000
97	A	278	ASP	-1	-0.746	-0.828	33.589	-0.077	-0.077	0.000	0.000	0.000	0.000
98	A	279	CYS	0	-0.126	-0.060	32.611	0.009	0.009	0.000	0.000	0.000	0.000
99	A	280	THR	0	-0.054	-0.032	35.462	0.005	0.005	0.000	0.000	0.000	0.000
100	A	281	ASN	0	-0.029	-0.015	37.957	0.006	0.006	0.000	0.000	0.000	0.000
101	A	282	ALA	0	-0.005	0.024	38.474	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:182:GLY)