FMO DATABASE

FMODB ID: 4N4GN

Calculation Name: 1L8R-A-Xray309

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1L8R

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UI36

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

Apendix: None

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. 1.20200116
Remarks	Structural optimization was performed under the unconstrained condition of hydrogen and heavy atoms fixed using MOE with Auto-FMO protocol as OptH.

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. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-754165.758673
FMO2-HF: Nuclear repulsion	713874.515454
FMO2-HF: Total energy	-40291.243219
FMO2-MP2: Total energy	-40405.197027

3D Structure Molmil

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.
-3.581	-1.713	-0.006	-0.911	-0.95	0.005

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 : 0.057 / q_NPA : 0.024

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	0.105	0.036	3.797	-1.531	-0.079	-0.006	-0.852	-0.594	0.005
4	A	185	ASN	0	0.000	0.018	6.525	0.165	0.165	0.000	0.000	0.000	0.000
5	A	186	ASN	0	-0.023	-0.008	4.042	1.008	1.127	0.000	-0.013	-0.106	0.000
6	A	187	GLU	-1	-0.887	-0.920	4.141	-4.265	-4.055	0.000	-0.043	-0.167	0.000
7	A	188	CYS	0	-0.098	-0.032	7.308	0.474	0.474	0.000	0.000	0.000	0.000
8	A	189	LYS	1	0.968	0.977	10.783	0.791	0.791	0.000	0.000	0.000	0.000
9	A	190	MET	0	-0.020	-0.004	13.698	0.074	0.074	0.000	0.000	0.000	0.000
10	A	191	VAL	0	-0.026	-0.012	17.332	0.000	0.000	0.000	0.000	0.000	0.000
11	A	192	ASP	-1	-0.914	-0.971	19.854	-0.225	-0.225	0.000	0.000	0.000	0.000
12	A	193	LEU	0	-0.005	0.002	23.625	-0.021	-0.021	0.000	0.000	0.000	0.000
13	A	194	ARG	1	0.899	0.956	25.521	0.190	0.190	0.000	0.000	0.000	0.000
14	A	195	GLY	0	0.030	0.030	28.297	0.015	0.015	0.000	0.000	0.000	0.000
15	A	196	ALA	0	-0.013	0.012	26.532	0.007	0.007	0.000	0.000	0.000	0.000
16	A	197	LYS	1	0.926	0.960	21.069	0.273	0.273	0.000	0.000	0.000	0.000
17	A	198	VAL	0	-0.013	-0.005	20.298	0.021	0.021	0.000	0.000	0.000	0.000
18	A	199	ALA	0	0.040	-0.001	15.659	-0.044	-0.044	0.000	0.000	0.000	0.000
19	A	200	SER	0	-0.081	-0.051	15.271	0.018	0.018	0.000	0.000	0.000	0.000
20	A	201	PHE	0	0.058	0.020	9.343	0.001	0.001	0.000	0.000	0.000	0.000
21	A	202	THR	0	-0.022	-0.010	11.564	0.169	0.169	0.000	0.000	0.000	0.000
22	A	203	VAL	0	-0.001	-0.015	11.353	-0.241	-0.241	0.000	0.000	0.000	0.000
23	A	204	GLU	-1	-0.935	-0.964	13.018	-0.350	-0.350	0.000	0.000	0.000	0.000
24	A	205	GLY	0	-0.002	0.010	14.243	0.068	0.068	0.000	0.000	0.000	0.000
25	A	206	CYS	0	-0.012	-0.001	16.074	0.069	0.069	0.000	0.000	0.000	0.000
26	A	207	GLU	-1	-0.911	-0.957	16.041	-0.662	-0.662	0.000	0.000	0.000	0.000
27	A	208	LEU	0	-0.023	-0.024	15.597	0.101	0.101	0.000	0.000	0.000	0.000
28	A	209	ILE	0	0.012	0.021	16.662	-0.060	-0.060	0.000	0.000	0.000	0.000
29	A	210	CYS	0	-0.024	-0.001	17.823	0.041	0.041	0.000	0.000	0.000	0.000
30	A	211	LEU	0	0.028	0.019	19.153	0.029	0.029	0.000	0.000	0.000	0.000
31	A	212	PRO	0	-0.028	-0.038	20.874	0.018	0.018	0.000	0.000	0.000	0.000
32	A	213	GLN	0	0.156	0.083	20.328	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	214	ALA	0	0.018	0.012	23.350	0.013	0.013	0.000	0.000	0.000	0.000
34	A	215	PHE	0	-0.025	-0.013	25.183	0.018	0.018	0.000	0.000	0.000	0.000
35	A	216	ASP	-1	-0.867	-0.944	26.185	-0.124	-0.124	0.000	0.000	0.000	0.000
36	A	217	LEU	0	-0.038	-0.016	25.044	0.010	0.010	0.000	0.000	0.000	0.000
37	A	218	PHE	0	-0.020	-0.017	26.899	0.008	0.008	0.000	0.000	0.000	0.000
38	A	219	LEU	0	-0.007	-0.014	29.914	0.006	0.006	0.000	0.000	0.000	0.000
39	A	220	LYS	1	0.841	0.932	29.419	0.118	0.118	0.000	0.000	0.000	0.000
40	A	221	HIS	0	0.032	0.001	33.041	0.006	0.006	0.000	0.000	0.000	0.000
41	A	222	LEU	0	-0.027	-0.007	35.243	0.003	0.003	0.000	0.000	0.000	0.000
42	A	223	VAL	0	-0.013	0.003	33.017	0.001	0.001	0.000	0.000	0.000	0.000
43	A	224	GLY	0	0.038	0.035	34.883	0.006	0.006	0.000	0.000	0.000	0.000
44	A	225	GLY	0	0.019	0.006	32.978	0.005	0.005	0.000	0.000	0.000	0.000
45	A	226	LEU	0	0.005	-0.005	25.103	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	227	HIS	0	-0.001	-0.002	29.535	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	228	THR	0	0.089	0.034	31.551	0.000	0.000	0.000	0.000	0.000	0.000
48	A	229	VAL	0	0.019	0.028	27.778	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	230	TYR	0	-0.011	-0.016	23.822	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	231	THR	0	-0.026	-0.007	29.345	0.001	0.001	0.000	0.000	0.000	0.000
51	A	232	LYS	1	0.935	0.962	32.427	0.105	0.105	0.000	0.000	0.000	0.000
52	A	233	LEU	0	0.013	-0.005	25.640	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	234	LYS	1	0.916	0.967	29.856	0.091	0.091	0.000	0.000	0.000	0.000
54	A	235	ARG	1	0.903	0.963	31.065	0.106	0.106	0.000	0.000	0.000	0.000
55	A	236	LEU	0	-0.057	-0.026	31.213	0.001	0.001	0.000	0.000	0.000	0.000
56	A	237	GLU	-1	-0.904	-0.940	30.714	-0.133	-0.133	0.000	0.000	0.000	0.000
57	A	238	ILE	0	-0.040	-0.006	25.387	-0.016	-0.016	0.000	0.000	0.000	0.000
58	A	239	THR	0	-0.024	-0.024	22.879	0.018	0.018	0.000	0.000	0.000	0.000
59	A	240	PRO	0	-0.083	-0.058	21.780	-0.023	-0.023	0.000	0.000	0.000	0.000
60	A	241	VAL	0	0.068	0.050	15.117	0.019	0.019	0.000	0.000	0.000	0.000
61	A	242	VAL	0	-0.051	-0.035	16.529	0.012	0.012	0.000	0.000	0.000	0.000
62	A	243	CYS	0	-0.045	-0.002	13.732	-0.023	-0.023	0.000	0.000	0.000	0.000
63	A	244	ASN	0	0.012	0.003	8.402	0.179	0.179	0.000	0.000	0.000	0.000
64	A	245	VAL	0	0.043	-0.012	11.537	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	246	GLU	-1	-0.905	-0.954	5.062	-0.505	-0.418	0.000	-0.003	-0.083	0.000
66	A	247	GLN	0	0.045	0.015	9.144	0.150	0.150	0.000	0.000	0.000	0.000
67	A	248	VAL	0	-0.040	-0.012	10.865	0.027	0.027	0.000	0.000	0.000	0.000
68	A	249	ARG	1	0.940	0.958	11.780	-0.283	-0.283	0.000	0.000	0.000	0.000
69	A	250	ILE	0	0.050	0.038	8.054	0.047	0.047	0.000	0.000	0.000	0.000
70	A	251	LEU	0	0.012	-0.009	12.615	0.020	0.020	0.000	0.000	0.000	0.000
71	A	252	ARG	1	0.835	0.902	15.631	0.031	0.031	0.000	0.000	0.000	0.000
72	A	253	GLY	0	-0.033	-0.004	15.789	0.021	0.021	0.000	0.000	0.000	0.000
73	A	254	LEU	0	-0.028	-0.019	13.829	0.004	0.004	0.000	0.000	0.000	0.000
74	A	255	GLY	0	0.001	0.017	17.395	0.003	0.003	0.000	0.000	0.000	0.000
75	A	256	ALA	0	-0.060	-0.021	18.199	0.003	0.003	0.000	0.000	0.000	0.000
76	A	257	ILE	0	-0.027	-0.012	17.366	0.013	0.013	0.000	0.000	0.000	0.000
77	A	258	GLN	0	0.039	0.000	21.198	0.024	0.024	0.000	0.000	0.000	0.000
78	A	259	PRO	0	0.072	0.018	21.675	0.001	0.001	0.000	0.000	0.000	0.000
79	A	260	GLY	0	0.010	0.017	22.057	0.014	0.014	0.000	0.000	0.000	0.000
80	A	261	VAL	0	-0.043	0.001	20.380	0.007	0.007	0.000	0.000	0.000	0.000
81	A	262	ASN	0	0.024	0.004	19.074	0.009	0.009	0.000	0.000	0.000	0.000
82	A	263	ARG	1	0.962	0.979	18.454	0.063	0.063	0.000	0.000	0.000	0.000
83	A	264	CYS	0	0.009	0.012	17.007	0.003	0.003	0.000	0.000	0.000	0.000
84	A	265	LYS	1	0.935	0.979	17.797	0.146	0.146	0.000	0.000	0.000	0.000
85	A	266	LEU	0	0.037	0.014	13.854	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	267	ILE	0	0.035	0.030	18.593	0.018	0.018	0.000	0.000	0.000	0.000
87	A	268	SER	0	0.088	0.050	20.777	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	269	ARG	1	0.966	0.953	21.742	0.422	0.422	0.000	0.000	0.000	0.000
89	A	270	LYS	1	0.986	1.005	24.001	0.255	0.255	0.000	0.000	0.000	0.000
90	A	271	ASP	-1	-0.826	-0.922	24.544	-0.238	-0.238	0.000	0.000	0.000	0.000
91	A	272	PHE	0	-0.024	-0.025	24.919	0.020	0.020	0.000	0.000	0.000	0.000
92	A	273	GLU	-1	-0.821	-0.917	26.779	-0.194	-0.194	0.000	0.000	0.000	0.000
93	A	274	THR	0	-0.058	-0.009	29.506	0.018	0.018	0.000	0.000	0.000	0.000
94	A	275	LEU	0	-0.008	-0.008	27.957	0.014	0.014	0.000	0.000	0.000	0.000
95	A	276	TYR	0	-0.026	-0.023	30.641	0.014	0.014	0.000	0.000	0.000	0.000
96	A	277	ASN	0	0.015	-0.010	32.268	0.012	0.012	0.000	0.000	0.000	0.000
97	A	278	ASP	-1	-0.825	-0.904	34.194	-0.108	-0.108	0.000	0.000	0.000	0.000
98	A	279	CYS	0	-0.156	-0.083	33.254	0.009	0.009	0.000	0.000	0.000	0.000
99	A	280	THR	0	-0.089	-0.059	35.958	0.006	0.006	0.000	0.000	0.000	0.000
100	A	281	ASN	0	-0.076	-0.034	38.305	0.010	0.010	0.000	0.000	0.000	0.000
101	A	282	ALA	-1	-0.916	-0.928	39.112	-0.099	-0.099	0.000	0.000	0.000	0.000

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