FMO DATABASE

FMODB ID: Q1M7Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-621901.776388
FMO2-HF: Nuclear repulsion	586885.754708
FMO2-HF: Total energy	-35016.021679
FMO2-MP2: Total energy	-35118.261001

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.
-8.549	-7.104	10.635	-5.647	-6.433	-0.035

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 : 0.060 / q_NPA : 0.029

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	0.027	0.015	3.763	-2.264	-0.213	-0.005	-1.126	-0.920	0.006
4	A	86	LYS	1	0.822	0.926	5.456	1.563	1.563	0.000	0.000	0.000	0.000
5	A	87	GLU	-1	-0.790	-0.863	8.825	-0.333	-0.333	0.000	0.000	0.000	0.000
6	A	88	VAL	0	-0.023	0.001	12.522	0.056	0.056	0.000	0.000	0.000	0.000
7	A	89	ARG	1	0.886	0.928	14.894	0.319	0.319	0.000	0.000	0.000	0.000
8	A	90	LEU	0	0.032	0.015	17.957	0.020	0.020	0.000	0.000	0.000	0.000
9	A	91	SER	0	0.002	-0.004	21.351	0.000	0.000	0.000	0.000	0.000	0.000
10	A	92	PRO	0	-0.010	-0.022	25.119	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	93	THR	0	0.009	0.002	27.362	0.004	0.004	0.000	0.000	0.000	0.000
12	A	94	ILE	0	-0.083	-0.019	22.494	0.002	0.002	0.000	0.000	0.000	0.000
13	A	95	GLU	-1	-0.833	-0.908	26.711	-0.078	-0.078	0.000	0.000	0.000	0.000
14	A	96	GLU	-1	-0.732	-0.831	26.340	-0.106	-0.106	0.000	0.000	0.000	0.000
15	A	97	HIS	0	0.052	0.028	25.549	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	98	ASP	-1	-0.792	-0.876	22.521	-0.172	-0.172	0.000	0.000	0.000	0.000
17	A	99	PHE	0	-0.001	-0.007	21.061	-0.020	-0.020	0.000	0.000	0.000	0.000
18	A	100	ASN	0	0.019	-0.017	20.665	-0.020	-0.020	0.000	0.000	0.000	0.000
19	A	101	THR	0	-0.030	-0.019	20.089	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	102	LYS	1	0.743	0.853	17.485	0.174	0.174	0.000	0.000	0.000	0.000
21	A	103	LEU	0	0.041	0.030	16.029	-0.046	-0.046	0.000	0.000	0.000	0.000
22	A	104	ARG	1	0.927	0.971	15.594	0.097	0.097	0.000	0.000	0.000	0.000
23	A	105	ASN	0	-0.037	-0.021	14.042	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	106	ALA	0	0.022	0.008	11.752	-0.062	-0.062	0.000	0.000	0.000	0.000
25	A	107	ARG	1	0.863	0.900	10.656	0.013	0.013	0.000	0.000	0.000	0.000
26	A	108	LYS	1	0.827	0.925	11.014	0.305	0.305	0.000	0.000	0.000	0.000
27	A	109	PHE	0	0.006	-0.016	7.188	0.107	0.107	0.000	0.000	0.000	0.000
28	A	110	LEU	0	0.079	0.044	6.652	-0.103	-0.103	0.000	0.000	0.000	0.000
29	A	111	GLU	-1	-0.833	-0.921	7.341	0.120	0.120	0.000	0.000	0.000	0.000
30	A	112	LYS	1	0.745	0.868	6.080	0.078	0.078	0.000	0.000	0.000	0.000
31	A	113	GLY	0	0.094	0.057	3.948	0.532	0.756	0.002	-0.086	-0.140	0.000
32	A	114	ASP	-1	-0.835	-0.892	1.972	-12.906	-13.662	10.609	-4.894	-4.960	-0.041
33	A	115	LYS	1	0.873	0.916	3.252	2.594	2.520	0.029	0.459	-0.413	0.000
34	A	116	VAL	0	-0.062	-0.029	5.458	0.075	0.075	0.000	0.000	0.000	0.000
35	A	117	LYS	1	0.901	0.967	9.029	0.541	0.541	0.000	0.000	0.000	0.000
36	A	118	ALA	0	0.004	0.002	11.867	0.018	0.018	0.000	0.000	0.000	0.000
37	A	119	THR	0	-0.033	-0.055	15.061	0.024	0.024	0.000	0.000	0.000	0.000
38	A	120	ILE	0	0.032	0.044	18.125	0.015	0.015	0.000	0.000	0.000	0.000
39	A	121	ARG	1	0.933	0.945	21.517	0.198	0.198	0.000	0.000	0.000	0.000
40	A	122	PHE	0	0.037	0.029	24.314	0.009	0.009	0.000	0.000	0.000	0.000
41	A	123	LYS	1	0.919	0.960	26.454	0.140	0.140	0.000	0.000	0.000	0.000
42	A	124	GLY	0	0.082	0.045	30.995	0.004	0.004	0.000	0.000	0.000	0.000
43	A	125	ARG	1	0.928	0.948	32.777	0.084	0.084	0.000	0.000	0.000	0.000
44	A	126	ALA	0	0.068	0.043	33.681	0.004	0.004	0.000	0.000	0.000	0.000
45	A	127	ILE	0	0.039	0.004	33.912	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	128	THR	0	0.033	0.011	33.323	0.001	0.001	0.000	0.000	0.000	0.000
47	A	129	HIS	0	-0.038	-0.039	29.406	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	130	LYS	1	0.919	0.968	27.028	0.109	0.109	0.000	0.000	0.000	0.000
49	A	131	GLU	-1	-0.802	-0.888	27.435	-0.099	-0.099	0.000	0.000	0.000	0.000
50	A	132	ILE	0	0.008	0.013	27.786	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	133	GLY	0	0.001	-0.013	25.054	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	134	GLN	0	-0.041	-0.043	23.507	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	135	ARG	1	0.975	0.992	23.484	0.088	0.088	0.000	0.000	0.000	0.000
54	A	136	VAL	0	-0.006	0.009	21.715	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	137	LEU	0	-0.032	-0.023	18.079	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	138	ASP	-1	-0.784	-0.896	19.182	-0.166	-0.166	0.000	0.000	0.000	0.000
57	A	139	ARG	1	0.831	0.891	20.865	0.109	0.109	0.000	0.000	0.000	0.000
58	A	140	LEU	0	-0.038	-0.024	15.708	0.002	0.002	0.000	0.000	0.000	0.000
59	A	141	SER	0	0.040	0.003	16.239	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	142	GLU	-1	-0.978	-0.980	17.272	-0.092	-0.092	0.000	0.000	0.000	0.000
61	A	143	ALA	0	-0.021	-0.013	19.068	0.012	0.012	0.000	0.000	0.000	0.000
62	A	144	CYS	0	-0.057	-0.032	13.594	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	145	ALA	0	0.026	0.022	14.700	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	146	ASP	-1	-0.769	-0.848	16.588	-0.064	-0.064	0.000	0.000	0.000	0.000
65	A	147	ILE	0	-0.014	0.001	11.305	0.016	0.016	0.000	0.000	0.000	0.000
66	A	148	ALA	0	-0.034	-0.004	11.012	0.005	0.005	0.000	0.000	0.000	0.000
67	A	149	VAL	0	0.011	0.014	11.043	0.064	0.064	0.000	0.000	0.000	0.000
68	A	150	VAL	0	0.008	-0.004	12.019	-0.084	-0.084	0.000	0.000	0.000	0.000
69	A	151	GLU	-1	-0.791	-0.860	8.910	-0.660	-0.660	0.000	0.000	0.000	0.000
70	A	152	THR	0	-0.069	-0.049	12.785	0.024	0.024	0.000	0.000	0.000	0.000
71	A	153	ALA	0	0.060	0.030	15.522	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	154	PRO	0	-0.025	-0.017	18.510	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	155	LYS	1	0.881	0.957	18.205	0.262	0.262	0.000	0.000	0.000	0.000
74	A	156	MET	0	-0.011	-0.011	21.393	-0.014	-0.014	0.000	0.000	0.000	0.000
75	A	157	ASP	-1	-0.851	-0.924	20.269	-0.248	-0.248	0.000	0.000	0.000	0.000
76	A	158	GLY	0	0.070	0.047	23.050	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	159	ARG	1	0.804	0.876	25.514	0.131	0.131	0.000	0.000	0.000	0.000
78	A	160	ASN	0	-0.032	-0.014	21.453	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	161	MET	0	-0.016	0.002	21.945	0.016	0.016	0.000	0.000	0.000	0.000
80	A	162	PHE	0	-0.011	-0.015	15.449	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	163	LEU	0	0.049	0.047	14.828	0.026	0.026	0.000	0.000	0.000	0.000
82	A	164	VAL	0	-0.020	-0.026	10.028	-0.044	-0.044	0.000	0.000	0.000	0.000
83	A	165	LEU	0	0.004	0.014	10.764	0.080	0.080	0.000	0.000	0.000	0.000
84	A	166	ALA	0	0.037	0.013	7.076	-0.287	-0.287	0.000	0.000	0.000	0.000
85	A	167	PRO	0	0.026	0.012	5.089	0.092	0.092	0.000	0.000	0.000	0.000
86	A	168	LYS	1	0.784	0.858	8.135	0.120	0.120	0.000	0.000	0.000	0.000
87	A	169	ASN	0	-0.036	-0.013	9.460	0.024	0.024	0.000	0.000	0.000	0.000
88	A	170	ASP	-1	-0.948	-0.958	5.491	1.188	1.188	0.000	0.000	0.000	0.000

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