FMO DATABASE

FMODB ID: K3M83

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:

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. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	101
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-754246.58287
FMO2-HF: Nuclear repulsion	713954.73905
FMO2-HF: Total energy	-40291.84382
FMO2-MP2: Total energy	-40405.794509

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.
-3.488	-1.555	-0.012	-0.94	-0.982	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 : 0.058 / q_NPA : 0.025

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	0.104	0.036	3.797	-1.583	-0.070	-0.009	-0.881	-0.624	0.005
4	A	185	ASN	0	-0.004	0.016	6.525	0.141	0.141	0.000	0.000	0.000	0.000
5	A	186	ASN	0	-0.018	-0.007	4.042	1.011	1.132	-0.001	-0.012	-0.108	0.000
6	A	187	GLU	-1	-0.890	-0.919	4.125	-4.200	-3.986	-0.001	-0.045	-0.168	0.000
7	A	188	CYS	0	-0.094	-0.032	7.290	0.448	0.448	0.000	0.000	0.000	0.000
8	A	189	LYS	1	0.966	0.977	10.769	0.787	0.787	0.000	0.000	0.000	0.000
9	A	190	MET	0	-0.019	-0.004	13.680	0.069	0.069	0.000	0.000	0.000	0.000
10	A	191	VAL	0	-0.025	-0.011	17.312	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	192	ASP	-1	-0.913	-0.971	19.834	-0.224	-0.224	0.000	0.000	0.000	0.000
12	A	193	LEU	0	-0.005	0.002	23.606	-0.021	-0.021	0.000	0.000	0.000	0.000
13	A	194	ARG	1	0.892	0.952	25.503	0.188	0.188	0.000	0.000	0.000	0.000
14	A	195	GLY	0	0.032	0.030	28.279	0.015	0.015	0.000	0.000	0.000	0.000
15	A	196	ALA	0	-0.012	0.013	26.520	0.008	0.008	0.000	0.000	0.000	0.000
16	A	197	LYS	1	0.927	0.960	21.054	0.271	0.271	0.000	0.000	0.000	0.000
17	A	198	VAL	0	-0.013	-0.005	20.283	0.022	0.022	0.000	0.000	0.000	0.000
18	A	199	ALA	0	0.042	0.001	15.649	-0.042	-0.042	0.000	0.000	0.000	0.000
19	A	200	SER	0	-0.086	-0.054	15.256	0.019	0.019	0.000	0.000	0.000	0.000
20	A	201	PHE	0	0.062	0.022	9.342	0.008	0.008	0.000	0.000	0.000	0.000
21	A	202	THR	0	-0.019	-0.010	11.564	0.169	0.169	0.000	0.000	0.000	0.000
22	A	203	VAL	0	-0.002	-0.014	11.353	-0.240	-0.240	0.000	0.000	0.000	0.000
23	A	204	GLU	-1	-0.934	-0.964	13.018	-0.357	-0.357	0.000	0.000	0.000	0.000
24	A	205	GLY	0	0.001	0.010	14.243	0.068	0.068	0.000	0.000	0.000	0.000
25	A	206	CYS	0	-0.015	-0.002	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	-0.660	-0.660	0.000	0.000	0.000	0.000
27	A	208	LEU	0	-0.022	-0.024	15.596	0.100	0.100	0.000	0.000	0.000	0.000
28	A	209	ILE	0	0.008	0.020	16.662	-0.059	-0.059	0.000	0.000	0.000	0.000
29	A	210	CYS	0	-0.022	0.001	17.822	0.040	0.040	0.000	0.000	0.000	0.000
30	A	211	LEU	0	0.028	0.018	19.152	0.028	0.028	0.000	0.000	0.000	0.000
31	A	212	PRO	0	-0.029	-0.038	20.873	0.017	0.017	0.000	0.000	0.000	0.000
32	A	213	GLN	0	0.157	0.084	20.320	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	214	ALA	0	0.021	0.014	23.349	0.013	0.013	0.000	0.000	0.000	0.000
34	A	215	PHE	0	-0.030	-0.016	25.183	0.018	0.018	0.000	0.000	0.000	0.000
35	A	216	ASP	-1	-0.875	-0.951	26.184	-0.120	-0.120	0.000	0.000	0.000	0.000
36	A	217	LEU	0	-0.036	-0.014	25.035	0.010	0.010	0.000	0.000	0.000	0.000
37	A	218	PHE	0	-0.013	-0.014	26.886	0.007	0.007	0.000	0.000	0.000	0.000
38	A	219	LEU	0	-0.018	-0.021	29.913	0.006	0.006	0.000	0.000	0.000	0.000
39	A	220	LYS	1	0.868	0.946	29.477	0.114	0.114	0.000	0.000	0.000	0.000
40	A	221	HIS	0	0.037	0.002	33.040	0.004	0.004	0.000	0.000	0.000	0.000
41	A	222	LEU	0	-0.047	-0.015	35.259	0.003	0.003	0.000	0.000	0.000	0.000
42	A	223	VAL	0	-0.015	0.000	33.016	0.001	0.001	0.000	0.000	0.000	0.000
43	A	224	GLY	0	0.042	0.038	34.882	0.006	0.006	0.000	0.000	0.000	0.000
44	A	225	GLY	0	0.022	0.007	32.978	0.005	0.005	0.000	0.000	0.000	0.000
45	A	226	LEU	0	0.007	-0.003	25.102	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	227	HIS	0	0.004	0.001	29.534	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	228	THR	0	0.083	0.032	31.551	0.000	0.000	0.000	0.000	0.000	0.000
48	A	229	VAL	0	0.016	0.026	27.778	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	230	TYR	0	-0.006	-0.013	23.822	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	231	THR	0	-0.021	-0.004	29.344	0.000	0.000	0.000	0.000	0.000	0.000
51	A	232	LYS	1	0.927	0.958	32.427	0.104	0.104	0.000	0.000	0.000	0.000
52	A	233	LEU	0	0.009	-0.006	25.639	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	234	LYS	1	0.925	0.971	29.855	0.090	0.090	0.000	0.000	0.000	0.000
54	A	235	ARG	1	0.900	0.960	31.065	0.105	0.105	0.000	0.000	0.000	0.000
55	A	236	LEU	0	-0.066	-0.032	31.213	0.002	0.002	0.000	0.000	0.000	0.000
56	A	237	GLU	-1	-0.899	-0.938	30.714	-0.133	-0.133	0.000	0.000	0.000	0.000
57	A	238	ILE	0	-0.041	-0.007	25.387	-0.015	-0.015	0.000	0.000	0.000	0.000
58	A	239	THR	0	-0.024	-0.023	22.879	0.018	0.018	0.000	0.000	0.000	0.000
59	A	240	PRO	0	-0.076	-0.055	21.780	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	241	VAL	0	0.070	0.051	15.117	0.021	0.021	0.000	0.000	0.000	0.000
61	A	242	VAL	0	-0.053	-0.037	16.528	0.013	0.013	0.000	0.000	0.000	0.000
62	A	243	CYS	0	-0.044	-0.001	13.732	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	244	ASN	0	0.011	0.004	8.402	0.180	0.180	0.000	0.000	0.000	0.000
64	A	245	VAL	0	0.040	-0.013	11.536	-0.021	-0.021	0.000	0.000	0.000	0.000
65	A	246	GLU	-1	-0.903	-0.953	5.061	-0.422	-0.337	-0.001	-0.002	-0.082	0.000
66	A	247	GLN	0	0.046	0.015	9.143	0.156	0.156	0.000	0.000	0.000	0.000
67	A	248	VAL	0	-0.038	-0.011	10.864	0.022	0.022	0.000	0.000	0.000	0.000
68	A	249	ARG	1	0.940	0.958	11.779	-0.310	-0.310	0.000	0.000	0.000	0.000
69	A	250	ILE	0	0.048	0.038	8.055	0.046	0.046	0.000	0.000	0.000	0.000
70	A	251	LEU	0	0.012	-0.008	12.614	0.017	0.017	0.000	0.000	0.000	0.000
71	A	252	ARG	1	0.837	0.901	15.631	0.016	0.016	0.000	0.000	0.000	0.000
72	A	253	GLY	0	-0.033	-0.004	15.797	0.020	0.020	0.000	0.000	0.000	0.000
73	A	254	LEU	0	-0.030	-0.019	13.825	0.004	0.004	0.000	0.000	0.000	0.000
74	A	255	GLY	0	0.005	0.018	17.396	0.001	0.001	0.000	0.000	0.000	0.000
75	A	256	ALA	0	-0.059	-0.021	18.199	0.003	0.003	0.000	0.000	0.000	0.000
76	A	257	ILE	0	-0.028	-0.013	17.366	0.011	0.011	0.000	0.000	0.000	0.000
77	A	258	GLN	0	0.037	0.000	21.197	0.023	0.023	0.000	0.000	0.000	0.000
78	A	259	PRO	0	0.074	0.018	21.674	0.000	0.000	0.000	0.000	0.000	0.000
79	A	260	GLY	0	0.011	0.017	22.056	0.015	0.015	0.000	0.000	0.000	0.000
80	A	261	VAL	0	-0.044	0.000	20.379	0.007	0.007	0.000	0.000	0.000	0.000
81	A	262	ASN	0	0.027	0.005	19.073	0.010	0.010	0.000	0.000	0.000	0.000
82	A	263	ARG	1	0.961	0.978	18.453	0.060	0.060	0.000	0.000	0.000	0.000
83	A	264	CYS	0	0.008	0.013	17.006	0.004	0.004	0.000	0.000	0.000	0.000
84	A	265	LYS	1	0.935	0.979	17.797	0.145	0.145	0.000	0.000	0.000	0.000
85	A	266	LEU	0	0.037	0.015	13.853	0.001	0.001	0.000	0.000	0.000	0.000
86	A	267	ILE	0	0.034	0.029	18.593	0.018	0.018	0.000	0.000	0.000	0.000
87	A	268	SER	0	0.091	0.053	20.777	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	269	ARG	1	0.968	0.955	21.741	0.421	0.421	0.000	0.000	0.000	0.000
89	A	270	LYS	1	0.985	1.004	24.001	0.255	0.255	0.000	0.000	0.000	0.000
90	A	271	ASP	-1	-0.826	-0.923	24.544	-0.238	-0.238	0.000	0.000	0.000	0.000
91	A	272	PHE	0	-0.018	-0.021	24.919	0.020	0.020	0.000	0.000	0.000	0.000
92	A	273	GLU	-1	-0.819	-0.915	26.779	-0.192	-0.192	0.000	0.000	0.000	0.000
93	A	274	THR	0	-0.065	-0.012	29.506	0.018	0.018	0.000	0.000	0.000	0.000
94	A	275	LEU	0	-0.003	-0.006	27.956	0.015	0.015	0.000	0.000	0.000	0.000
95	A	276	TYR	0	-0.019	-0.018	30.641	0.014	0.014	0.000	0.000	0.000	0.000
96	A	277	ASN	0	0.018	-0.008	32.267	0.012	0.012	0.000	0.000	0.000	0.000
97	A	278	ASP	-1	-0.854	-0.921	34.193	-0.107	-0.107	0.000	0.000	0.000	0.000
98	A	279	CYS	0	-0.139	-0.075	33.248	0.009	0.009	0.000	0.000	0.000	0.000
99	A	280	THR	0	-0.068	-0.042	35.953	0.006	0.006	0.000	0.000	0.000	0.000
100	A	281	ASN	0	-0.040	-0.013	38.299	0.010	0.010	0.000	0.000	0.000	0.000
101	A	282	ALA	0	0.005	0.026	39.117	0.000	0.000	0.000	0.000	0.000	0.000

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