FMO DATABASE

FMODB ID: ZYLRN

Calculation Name: 1TIG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TIG

Chain ID: A

ChEMBL ID:

UniProt ID: P03000

Base Structure: X-ray

Registration Date: 2023-03-13

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	88
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-620993.998486
FMO2-HF: Nuclear repulsion	585978.755924
FMO2-HF: Total energy	-35015.242562
FMO2-MP2: Total energy	-35117.453804

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:83:ILE)

Summations of interaction energy for fragment #1(A:83:ILE)

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.
-4.323	-6.986	14.286	-5.845	-5.777	-0.043

Interaction energy analysis for fragmet #1(A:83:ILE)

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 : 0.038

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

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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	85	VAL	0	0.028	0.010	3.701	-1.948	-0.023	-0.006	-0.936	-0.982	0.005
4	A	86	LYS	1	0.916	0.966	5.699	1.386	1.386	0.000	0.000	0.000	0.000
5	A	87	GLU	-1	-0.862	-0.914	8.488	-0.302	-0.302	0.000	0.000	0.000	0.000
6	A	88	VAL	0	-0.015	0.000	12.185	0.048	0.048	0.000	0.000	0.000	0.000
7	A	89	ARG	1	0.856	0.907	14.585	0.305	0.305	0.000	0.000	0.000	0.000
8	A	90	LEU	0	0.009	-0.006	17.717	0.015	0.015	0.000	0.000	0.000	0.000
9	A	91	SER	0	0.008	0.002	20.878	0.001	0.001	0.000	0.000	0.000	0.000
10	A	92	PRO	0	0.002	-0.022	24.625	0.000	0.000	0.000	0.000	0.000	0.000
11	A	93	THR	0	0.007	-0.014	26.945	0.004	0.004	0.000	0.000	0.000	0.000
12	A	94	ILE	0	-0.093	-0.008	22.470	0.002	0.002	0.000	0.000	0.000	0.000
13	A	95	GLU	-1	-0.852	-0.921	26.721	-0.076	-0.076	0.000	0.000	0.000	0.000
14	A	96	GLU	-1	-0.771	-0.875	26.473	-0.096	-0.096	0.000	0.000	0.000	0.000
15	A	97	HIS	0	0.045	0.016	25.687	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	98	ASP	-1	-0.819	-0.914	23.052	-0.163	-0.163	0.000	0.000	0.000	0.000
17	A	99	PHE	0	0.006	-0.003	21.047	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	100	ASN	0	0.059	0.026	20.738	-0.020	-0.020	0.000	0.000	0.000	0.000
19	A	101	THR	0	-0.076	-0.042	20.046	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	102	LYS	1	0.800	0.899	17.579	0.173	0.173	0.000	0.000	0.000	0.000
21	A	103	LEU	0	0.036	0.029	16.126	-0.041	-0.041	0.000	0.000	0.000	0.000
22	A	104	ARG	1	0.957	0.982	15.864	0.116	0.116	0.000	0.000	0.000	0.000
23	A	105	ASN	0	-0.035	-0.033	14.053	0.011	0.011	0.000	0.000	0.000	0.000
24	A	106	ALA	0	0.019	0.007	11.720	-0.065	-0.065	0.000	0.000	0.000	0.000
25	A	107	ARG	1	0.880	0.900	10.906	0.031	0.031	0.000	0.000	0.000	0.000
26	A	108	LYS	1	0.918	0.975	10.416	0.350	0.350	0.000	0.000	0.000	0.000
27	A	109	PHE	0	-0.020	-0.041	7.514	0.059	0.059	0.000	0.000	0.000	0.000
28	A	110	LEU	0	0.057	0.034	6.686	-0.146	-0.146	0.000	0.000	0.000	0.000
29	A	111	GLU	-1	-0.897	-0.954	7.618	0.131	0.131	0.000	0.000	0.000	0.000
30	A	112	LYS	1	0.717	0.875	6.588	0.227	0.227	0.000	0.000	0.000	0.000
31	A	113	GLY	0	0.090	0.058	4.664	0.276	0.353	-0.001	-0.019	-0.057	0.000
32	A	114	ASP	-1	-0.852	-0.922	1.864	-8.070	-12.874	14.285	-5.067	-4.414	-0.048
33	A	115	LYS	1	0.910	0.933	3.284	1.916	2.055	0.008	0.177	-0.324	0.000
34	A	116	VAL	0	-0.042	-0.020	5.477	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	117	LYS	1	0.952	0.994	8.906	0.507	0.507	0.000	0.000	0.000	0.000
36	A	118	ALA	0	-0.004	0.003	11.737	0.012	0.012	0.000	0.000	0.000	0.000
37	A	119	THR	0	0.002	-0.021	14.947	0.027	0.027	0.000	0.000	0.000	0.000
38	A	120	ILE	0	0.039	0.048	17.806	0.011	0.011	0.000	0.000	0.000	0.000
39	A	121	ARG	1	0.946	0.973	21.285	0.193	0.193	0.000	0.000	0.000	0.000
40	A	122	PHE	0	0.016	-0.005	23.774	0.008	0.008	0.000	0.000	0.000	0.000
41	A	123	LYS	1	0.920	0.964	25.970	0.137	0.137	0.000	0.000	0.000	0.000
42	A	124	GLY	0	0.066	0.029	30.367	0.003	0.003	0.000	0.000	0.000	0.000
43	A	125	ARG	1	0.946	0.959	32.212	0.080	0.080	0.000	0.000	0.000	0.000
44	A	126	ALA	0	0.065	0.046	33.308	0.004	0.004	0.000	0.000	0.000	0.000
45	A	127	ILE	0	0.039	0.007	33.757	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	128	THR	0	0.063	0.050	32.855	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	129	HIS	0	-0.041	-0.031	29.288	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	130	LYS	1	0.953	0.981	26.708	0.094	0.094	0.000	0.000	0.000	0.000
49	A	131	GLU	-1	-0.842	-0.930	27.461	-0.083	-0.083	0.000	0.000	0.000	0.000
50	A	132	ILE	0	0.002	0.013	27.084	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	133	GLY	0	-0.014	-0.015	24.737	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	134	GLN	0	-0.050	-0.033	23.401	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	135	ARG	1	0.975	0.991	23.706	0.075	0.075	0.000	0.000	0.000	0.000
54	A	136	VAL	0	-0.001	0.008	21.664	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	137	LEU	0	-0.029	-0.028	18.074	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	138	ASP	-1	-0.819	-0.918	19.431	-0.128	-0.128	0.000	0.000	0.000	0.000
57	A	139	ARG	1	0.829	0.908	21.352	0.103	0.103	0.000	0.000	0.000	0.000
58	A	140	LEU	0	-0.043	-0.029	15.244	0.001	0.001	0.000	0.000	0.000	0.000
59	A	141	SER	0	-0.003	-0.017	16.468	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	142	GLU	-1	-0.939	-0.962	17.425	-0.069	-0.069	0.000	0.000	0.000	0.000
61	A	143	ALA	0	-0.014	-0.004	19.071	0.011	0.011	0.000	0.000	0.000	0.000
62	A	144	CYS	0	-0.065	-0.036	13.829	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	145	ALA	0	0.055	0.039	14.880	0.002	0.002	0.000	0.000	0.000	0.000
64	A	146	ASP	-1	-0.801	-0.848	16.855	-0.046	-0.046	0.000	0.000	0.000	0.000
65	A	147	ILE	0	0.010	0.008	12.075	0.020	0.020	0.000	0.000	0.000	0.000
66	A	148	ALA	0	-0.013	-0.006	11.281	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	149	VAL	0	-0.017	-0.007	11.124	0.040	0.040	0.000	0.000	0.000	0.000
68	A	150	VAL	0	0.007	-0.007	12.121	-0.071	-0.071	0.000	0.000	0.000	0.000
69	A	151	GLU	-1	-0.854	-0.901	9.107	-0.419	-0.419	0.000	0.000	0.000	0.000
70	A	152	THR	0	-0.067	-0.045	13.071	0.022	0.022	0.000	0.000	0.000	0.000
71	A	153	ALA	0	0.058	0.024	15.442	-0.021	-0.021	0.000	0.000	0.000	0.000
72	A	154	PRO	0	-0.017	-0.011	18.389	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	155	LYS	1	0.955	1.001	18.375	0.201	0.201	0.000	0.000	0.000	0.000
74	A	156	MET	0	-0.022	-0.013	21.071	-0.017	-0.017	0.000	0.000	0.000	0.000
75	A	157	ASP	-1	-0.917	-0.962	19.859	-0.207	-0.207	0.000	0.000	0.000	0.000
76	A	158	GLY	0	0.041	0.025	22.515	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	159	ARG	1	0.815	0.893	25.587	0.116	0.116	0.000	0.000	0.000	0.000
78	A	160	ASN	0	0.007	-0.008	21.119	0.004	0.004	0.000	0.000	0.000	0.000
79	A	161	MET	0	0.005	0.021	21.512	0.011	0.011	0.000	0.000	0.000	0.000
80	A	162	PHE	0	-0.033	-0.026	15.177	-0.011	-0.011	0.000	0.000	0.000	0.000
81	A	163	LEU	0	0.067	0.044	14.620	0.030	0.030	0.000	0.000	0.000	0.000
82	A	164	VAL	0	-0.022	-0.020	9.764	-0.045	-0.045	0.000	0.000	0.000	0.000
83	A	165	LEU	0	0.011	0.011	10.639	0.079	0.079	0.000	0.000	0.000	0.000
84	A	166	ALA	0	0.024	0.005	7.326	-0.239	-0.239	0.000	0.000	0.000	0.000
85	A	167	PRO	0	0.013	0.018	5.035	0.041	0.041	0.000	0.000	0.000	0.000
86	A	168	LYS	1	0.834	0.905	8.193	0.095	0.095	0.000	0.000	0.000	0.000
87	A	169	ASN	0	-0.029	-0.006	10.139	0.038	0.038	0.000	0.000	0.000	0.000
88	A	170	ASP	-1	-0.930	-0.956	6.237	1.072	1.072	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:83:ILE)