FMO DATABASE

FMODB ID: 4386N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-753975.317471
FMO2-HF: Nuclear repulsion	713683.024227
FMO2-HF: Total energy	-40292.293244
FMO2-MP2: Total energy	-40406.220277

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.
-3.094	-0.952	-0.011	-1.051	-1.079	0.006

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 : 0.061 / q_NPA : 0.031

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	0.082	0.028	3.797	-1.289	0.383	-0.009	-0.960	-0.703	0.006
4	A	185	ASN	0	-0.004	0.021	6.525	0.276	0.276	0.000	0.000	0.000	0.000
5	A	186	ASN	0	-0.032	-0.029	4.337	0.606	0.713	-0.001	-0.008	-0.098	0.000
6	A	187	GLU	-1	-0.902	-0.929	3.934	-4.119	-3.851	0.000	-0.080	-0.187	0.000
7	A	188	CYS	0	-0.106	-0.036	7.197	0.401	0.401	0.000	0.000	0.000	0.000
8	A	189	LYS	1	0.905	0.938	10.704	0.737	0.737	0.000	0.000	0.000	0.000
9	A	190	MET	0	-0.004	-0.002	13.589	0.064	0.064	0.000	0.000	0.000	0.000
10	A	191	VAL	0	-0.020	-0.011	17.180	-0.021	-0.021	0.000	0.000	0.000	0.000
11	A	192	ASP	-1	-0.824	-0.908	19.727	-0.202	-0.202	0.000	0.000	0.000	0.000
12	A	193	LEU	0	-0.010	-0.008	23.500	-0.020	-0.020	0.000	0.000	0.000	0.000
13	A	194	ARG	1	0.845	0.919	25.408	0.174	0.174	0.000	0.000	0.000	0.000
14	A	195	GLY	0	0.043	0.032	28.141	0.015	0.015	0.000	0.000	0.000	0.000
15	A	196	ALA	0	-0.022	0.006	26.468	0.008	0.008	0.000	0.000	0.000	0.000
16	A	197	LYS	1	0.833	0.901	21.463	0.221	0.221	0.000	0.000	0.000	0.000
17	A	198	VAL	0	-0.003	-0.001	20.434	0.023	0.023	0.000	0.000	0.000	0.000
18	A	199	ALA	0	0.044	0.009	15.692	-0.040	-0.040	0.000	0.000	0.000	0.000
19	A	200	SER	0	-0.081	-0.059	15.162	0.020	0.020	0.000	0.000	0.000	0.000
20	A	201	PHE	0	0.070	0.021	9.344	0.006	0.006	0.000	0.000	0.000	0.000
21	A	202	THR	0	-0.023	-0.011	11.570	0.161	0.161	0.000	0.000	0.000	0.000
22	A	203	VAL	0	-0.001	-0.017	11.359	-0.233	-0.233	0.000	0.000	0.000	0.000
23	A	204	GLU	-1	-0.921	-0.956	13.021	-0.364	-0.364	0.000	0.000	0.000	0.000
24	A	205	GLY	0	-0.001	0.009	14.243	0.067	0.067	0.000	0.000	0.000	0.000
25	A	206	CYS	0	0.004	0.005	16.074	0.077	0.077	0.000	0.000	0.000	0.000
26	A	207	GLU	-1	-0.804	-0.874	16.047	-0.606	-0.606	0.000	0.000	0.000	0.000
27	A	208	LEU	0	-0.012	-0.016	15.724	0.096	0.096	0.000	0.000	0.000	0.000
28	A	209	ILE	0	0.007	0.019	16.668	-0.053	-0.053	0.000	0.000	0.000	0.000
29	A	210	CYS	0	-0.024	0.003	17.817	0.040	0.040	0.000	0.000	0.000	0.000
30	A	211	LEU	0	0.033	0.018	19.158	0.025	0.025	0.000	0.000	0.000	0.000
31	A	212	PRO	0	-0.012	-0.028	20.864	0.015	0.015	0.000	0.000	0.000	0.000
32	A	213	GLN	0	0.106	0.056	20.391	-0.017	-0.017	0.000	0.000	0.000	0.000
33	A	214	ALA	0	0.039	0.022	23.355	0.011	0.011	0.000	0.000	0.000	0.000
34	A	215	PHE	0	-0.025	-0.017	25.189	0.014	0.014	0.000	0.000	0.000	0.000
35	A	216	ASP	-1	-0.813	-0.914	26.623	-0.080	-0.080	0.000	0.000	0.000	0.000
36	A	217	LEU	0	-0.034	-0.007	24.954	0.008	0.008	0.000	0.000	0.000	0.000
37	A	218	PHE	0	-0.014	-0.016	27.001	0.006	0.006	0.000	0.000	0.000	0.000
38	A	219	LEU	0	-0.016	-0.021	29.854	0.005	0.005	0.000	0.000	0.000	0.000
39	A	220	LYS	1	0.807	0.912	29.783	0.085	0.085	0.000	0.000	0.000	0.000
40	A	221	HIS	0	0.042	0.006	33.046	0.005	0.005	0.000	0.000	0.000	0.000
41	A	222	LEU	0	-0.056	-0.022	35.285	0.003	0.003	0.000	0.000	0.000	0.000
42	A	223	VAL	0	-0.014	-0.002	33.148	0.000	0.000	0.000	0.000	0.000	0.000
43	A	224	GLY	0	0.043	0.044	34.886	0.005	0.005	0.000	0.000	0.000	0.000
44	A	225	GLY	0	0.025	0.010	32.983	0.005	0.005	0.000	0.000	0.000	0.000
45	A	226	LEU	0	-0.004	-0.009	25.084	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	227	HIS	0	0.008	0.003	29.538	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	228	THR	0	0.087	0.032	31.554	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	229	VAL	0	0.016	0.024	27.813	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	230	TYR	0	-0.004	-0.012	24.359	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	231	THR	0	-0.021	-0.002	29.348	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	232	LYS	1	0.831	0.884	32.515	0.097	0.097	0.000	0.000	0.000	0.000
52	A	233	LEU	0	-0.005	-0.012	25.664	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	234	LYS	1	0.945	0.976	29.830	0.076	0.076	0.000	0.000	0.000	0.000
54	A	235	ARG	1	0.841	0.896	31.068	0.096	0.096	0.000	0.000	0.000	0.000
55	A	236	LEU	0	-0.065	-0.031	31.207	0.001	0.001	0.000	0.000	0.000	0.000
56	A	237	GLU	-1	-0.915	-0.946	30.708	-0.125	-0.125	0.000	0.000	0.000	0.000
57	A	238	ILE	0	-0.042	-0.010	25.488	-0.016	-0.016	0.000	0.000	0.000	0.000
58	A	239	THR	0	-0.009	-0.014	22.865	0.018	0.018	0.000	0.000	0.000	0.000
59	A	240	PRO	0	-0.073	-0.053	21.785	-0.020	-0.020	0.000	0.000	0.000	0.000
60	A	241	VAL	0	0.061	0.045	15.230	0.019	0.019	0.000	0.000	0.000	0.000
61	A	242	VAL	0	-0.044	-0.031	16.702	0.015	0.015	0.000	0.000	0.000	0.000
62	A	243	CYS	0	-0.040	0.002	13.731	-0.024	-0.024	0.000	0.000	0.000	0.000
63	A	244	ASN	0	0.003	-0.008	8.375	0.218	0.218	0.000	0.000	0.000	0.000
64	A	245	VAL	0	0.041	-0.012	11.487	-0.015	-0.015	0.000	0.000	0.000	0.000
65	A	246	GLU	-1	-0.872	-0.925	4.995	0.391	0.486	-0.001	-0.003	-0.091	0.000
66	A	247	GLN	0	0.036	0.017	9.179	0.121	0.121	0.000	0.000	0.000	0.000
67	A	248	VAL	0	-0.035	-0.011	10.868	0.010	0.010	0.000	0.000	0.000	0.000
68	A	249	ARG	1	0.940	0.964	11.680	-0.496	-0.496	0.000	0.000	0.000	0.000
69	A	250	ILE	0	0.043	0.033	7.978	0.025	0.025	0.000	0.000	0.000	0.000
70	A	251	LEU	0	0.026	-0.007	12.618	0.000	0.000	0.000	0.000	0.000	0.000
71	A	252	ARG	1	0.832	0.900	15.635	-0.068	-0.068	0.000	0.000	0.000	0.000
72	A	253	GLY	0	-0.036	-0.008	15.884	0.013	0.013	0.000	0.000	0.000	0.000
73	A	254	LEU	0	-0.029	-0.017	13.512	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	255	GLY	0	0.005	0.019	17.436	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	256	ALA	0	-0.055	-0.022	18.180	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	257	ILE	0	-0.037	-0.026	17.582	0.004	0.004	0.000	0.000	0.000	0.000
77	A	258	GLN	0	0.055	0.013	21.201	0.024	0.024	0.000	0.000	0.000	0.000
78	A	259	PRO	0	0.083	0.024	21.674	0.003	0.003	0.000	0.000	0.000	0.000
79	A	260	GLY	0	0.009	0.013	22.058	0.017	0.017	0.000	0.000	0.000	0.000
80	A	261	VAL	0	-0.047	-0.008	20.442	0.005	0.005	0.000	0.000	0.000	0.000
81	A	262	ASN	0	0.023	0.009	19.056	0.026	0.026	0.000	0.000	0.000	0.000
82	A	263	ARG	1	0.962	0.986	18.455	0.024	0.024	0.000	0.000	0.000	0.000
83	A	264	CYS	0	0.004	0.012	17.011	0.000	0.000	0.000	0.000	0.000	0.000
84	A	265	LYS	1	0.930	0.979	17.800	0.117	0.117	0.000	0.000	0.000	0.000
85	A	266	LEU	0	0.033	0.012	13.879	0.002	0.002	0.000	0.000	0.000	0.000
86	A	267	ILE	0	0.014	0.019	18.598	0.015	0.015	0.000	0.000	0.000	0.000
87	A	268	SER	0	0.057	0.004	20.782	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	269	ARG	1	0.888	0.918	20.935	0.410	0.410	0.000	0.000	0.000	0.000
89	A	270	LYS	1	0.951	0.980	24.008	0.253	0.253	0.000	0.000	0.000	0.000
90	A	271	ASP	-1	-0.800	-0.867	24.240	-0.239	-0.239	0.000	0.000	0.000	0.000
91	A	272	PHE	0	0.004	-0.006	24.902	0.021	0.021	0.000	0.000	0.000	0.000
92	A	273	GLU	-1	-0.782	-0.885	26.785	-0.175	-0.175	0.000	0.000	0.000	0.000
93	A	274	THR	0	-0.058	-0.020	29.505	0.016	0.016	0.000	0.000	0.000	0.000
94	A	275	LEU	0	0.011	0.000	27.772	0.014	0.014	0.000	0.000	0.000	0.000
95	A	276	TYR	0	-0.001	-0.010	30.638	0.013	0.013	0.000	0.000	0.000	0.000
96	A	277	ASN	0	0.031	0.002	32.273	0.013	0.013	0.000	0.000	0.000	0.000
97	A	278	ASP	-1	-0.733	-0.811	34.180	-0.095	-0.095	0.000	0.000	0.000	0.000
98	A	279	CYS	0	-0.140	-0.067	33.228	0.010	0.010	0.000	0.000	0.000	0.000
99	A	280	THR	0	-0.051	-0.030	35.839	0.006	0.006	0.000	0.000	0.000	0.000
100	A	281	ASN	0	-0.035	-0.007	38.299	0.009	0.009	0.000	0.000	0.000	0.000
101	A	282	ALA	0	0.007	0.022	39.132	-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)