FMO DATABASE

FMODB ID: JQ389

Calculation Name: 2IAZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2IAZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q97Q59

Base Structure: X-ray

Registration Date: 2023-09-21

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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-737279.274502
FMO2-HF: Nuclear repulsion	693913.424412
FMO2-HF: Total energy	-43365.850089
FMO2-MP2: Total energy	-43492.521472

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:0:GLY)

Summations of interaction energy for fragment #1(A:0: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.
-6.228	-5.29	5.929	-3.315	-3.551	-0.023

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / q_NPA : 0.003

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	2	SER	0	0.012	0.008	3.350	-2.281	-0.662	0.009	-0.781	-0.847	0.001
4	A	3	ASN	0	0.065	0.036	2.031	-4.780	-5.709	5.920	-2.472	-2.518	-0.024
5	A	4	ILE	0	0.041	0.043	4.121	1.076	1.324	0.000	-0.062	-0.186	0.000
6	A	5	TYR	0	0.002	-0.005	6.431	0.627	0.627	0.000	0.000	0.000	0.000
7	A	6	ASP	-1	-0.902	-0.958	6.322	-1.337	-1.337	0.000	0.000	0.000	0.000
8	A	7	SER	0	0.011	-0.015	7.619	0.337	0.337	0.000	0.000	0.000	0.000
9	A	8	ALA	0	0.012	0.013	10.148	0.208	0.208	0.000	0.000	0.000	0.000
10	A	9	ASN	0	-0.031	-0.006	12.080	0.186	0.186	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.921	-0.964	12.468	-0.575	-0.575	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.040	0.026	14.210	0.085	0.085	0.000	0.000	0.000	0.000
13	A	12	SER	0	0.010	0.019	15.960	0.081	0.081	0.000	0.000	0.000	0.000
14	A	13	ARG	1	0.842	0.915	16.112	0.382	0.382	0.000	0.000	0.000	0.000
15	A	14	GLY	0	0.029	0.013	18.746	0.034	0.034	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.012	-0.002	19.583	0.034	0.034	0.000	0.000	0.000	0.000
17	A	16	ARG	1	0.870	0.916	19.533	0.262	0.262	0.000	0.000	0.000	0.000
18	A	17	GLY	0	-0.021	-0.007	23.333	0.021	0.021	0.000	0.000	0.000	0.000
19	A	18	LEU	0	0.015	0.026	24.713	0.014	0.014	0.000	0.000	0.000	0.000
20	A	19	PRO	0	-0.001	-0.007	26.389	0.009	0.009	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.755	-0.871	29.190	-0.136	-0.136	0.000	0.000	0.000	0.000
22	A	21	TYR	0	0.016	0.021	26.342	0.008	0.008	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.833	0.909	27.675	0.168	0.168	0.000	0.000	0.000	0.000
24	A	23	ALA	0	-0.001	0.011	31.068	0.009	0.009	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.024	0.020	31.316	0.008	0.008	0.000	0.000	0.000	0.000
26	A	25	LYS	1	0.840	0.896	31.054	0.100	0.100	0.000	0.000	0.000	0.000
27	A	26	ALA	0	0.022	0.008	33.210	0.007	0.007	0.000	0.000	0.000	0.000
28	A	27	ALA	0	0.029	0.022	36.302	0.006	0.006	0.000	0.000	0.000	0.000
29	A	28	LYS	1	0.893	0.950	35.131	0.073	0.073	0.000	0.000	0.000	0.000
30	A	29	ASP	-1	-0.854	-0.903	35.612	-0.080	-0.080	0.000	0.000	0.000	0.000
31	A	30	ALA	0	-0.002	-0.004	38.346	0.005	0.005	0.000	0.000	0.000	0.000
32	A	31	ILE	0	-0.020	-0.017	39.420	0.004	0.004	0.000	0.000	0.000	0.000
33	A	32	ALA	0	-0.065	-0.020	39.546	0.003	0.003	0.000	0.000	0.000	0.000
34	A	33	ALA	0	-0.030	0.001	41.651	0.003	0.003	0.000	0.000	0.000	0.000
35	A	34	ASP	-1	-0.788	-0.891	44.379	-0.043	-0.043	0.000	0.000	0.000	0.000
36	A	35	ALA	0	0.018	0.001	46.242	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.911	-0.937	48.543	-0.040	-0.040	0.000	0.000	0.000	0.000
38	A	37	ALA	0	0.011	-0.001	44.490	0.000	0.000	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.006	-0.028	43.736	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	39	LYS	1	0.772	0.891	44.787	0.034	0.034	0.000	0.000	0.000	0.000
41	A	40	ILE	0	0.042	0.021	46.075	0.000	0.000	0.000	0.000	0.000	0.000
42	A	41	PHE	0	-0.001	-0.007	37.026	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	42	THR	0	-0.035	-0.033	42.402	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	43	ASP	-1	-0.812	-0.883	43.858	-0.035	-0.035	0.000	0.000	0.000	0.000
45	A	44	TYR	0	-0.036	-0.015	40.603	0.001	0.001	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.014	-0.021	37.772	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	46	ALA	0	-0.011	0.007	41.171	0.001	0.001	0.000	0.000	0.000	0.000
48	A	47	PHE	0	-0.032	-0.020	43.927	0.001	0.001	0.000	0.000	0.000	0.000
49	A	48	GLN	0	0.034	0.012	37.096	0.002	0.002	0.000	0.000	0.000	0.000
50	A	49	GLU	-1	-0.833	-0.903	41.153	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.850	-0.927	42.732	-0.029	-0.029	0.000	0.000	0.000	0.000
52	A	51	ILE	0	-0.027	-0.012	38.666	0.001	0.001	0.000	0.000	0.000	0.000
53	A	52	GLN	0	-0.043	-0.010	38.321	0.002	0.002	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.837	0.900	42.015	0.029	0.029	0.000	0.000	0.000	0.000
55	A	54	LEU	0	-0.044	-0.020	43.931	0.002	0.002	0.000	0.000	0.000	0.000
56	A	55	ALA	0	-0.006	0.007	43.339	0.000	0.000	0.000	0.000	0.000	0.000
57	A	56	GLN	0	-0.087	-0.059	44.931	0.002	0.002	0.000	0.000	0.000	0.000
58	A	57	THR	0	0.010	0.017	45.716	0.000	0.000	0.000	0.000	0.000	0.000
59	A	58	GLY	0	-0.006	-0.009	48.458	0.002	0.002	0.000	0.000	0.000	0.000
60	A	59	GLN	0	-0.070	-0.032	51.275	0.000	0.000	0.000	0.000	0.000	0.000
61	A	60	MET	0	0.034	0.023	52.172	0.001	0.001	0.000	0.000	0.000	0.000
62	A	61	PRO	0	-0.005	-0.009	50.978	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	62	ASP	-1	-0.748	-0.856	50.070	-0.027	-0.027	0.000	0.000	0.000	0.000
64	A	63	ALA	0	0.029	0.000	51.518	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	64	SER	0	0.009	0.007	53.458	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	65	PHE	0	0.018	0.011	44.033	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	66	GLN	0	-0.017	-0.023	49.344	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	67	ALA	0	0.006	0.005	50.391	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.793	0.889	49.614	0.029	0.029	0.000	0.000	0.000	0.000
70	A	69	MET	0	-0.005	0.009	42.280	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.840	-0.903	47.507	-0.037	-0.037	0.000	0.000	0.000	0.000
72	A	71	GLY	0	-0.002	-0.003	49.943	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	72	PHE	0	-0.007	-0.018	45.787	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	73	GLY	0	0.027	0.021	45.934	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	74	LYS	1	0.841	0.899	46.960	0.035	0.035	0.000	0.000	0.000	0.000
76	A	75	GLN	0	0.006	0.006	48.514	0.000	0.000	0.000	0.000	0.000	0.000
77	A	76	ILE	0	-0.028	-0.004	42.577	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	77	GLN	0	-0.029	-0.014	44.892	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	78	GLY	0	-0.003	0.018	47.751	0.001	0.001	0.000	0.000	0.000	0.000
80	A	79	ASN	0	-0.013	-0.028	46.551	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	80	SER	0	0.031	-0.003	46.304	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	81	LEU	0	-0.015	0.001	43.188	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.013	0.005	41.753	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	83	SER	0	0.027	-0.005	41.395	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.832	-0.871	38.900	-0.085	-0.085	0.000	0.000	0.000	0.000
86	A	85	PHE	0	0.002	-0.004	34.616	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	86	PHE	0	0.016	-0.010	36.629	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	87	THR	0	-0.037	-0.018	37.000	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.819	0.877	34.607	0.081	0.081	0.000	0.000	0.000	0.000
90	A	89	GLN	0	0.007	0.000	32.116	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	90	GLN	0	-0.036	-0.011	31.997	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	91	GLN	0	-0.002	-0.014	32.272	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.008	0.001	26.666	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	93	ALA	0	0.002	0.000	27.629	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	94	ILE	0	-0.005	0.008	27.516	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	95	TYR	0	-0.038	-0.040	25.018	-0.012	-0.012	0.000	0.000	0.000	0.000
97	A	96	LEU	0	-0.044	-0.026	23.181	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	97	SER	0	0.054	0.035	22.506	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	98	ASP	-1	-0.877	-0.939	22.981	-0.178	-0.178	0.000	0.000	0.000	0.000
100	A	99	ILE	0	-0.038	-0.022	17.972	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	100	GLU	-1	-0.955	-0.976	18.274	-0.218	-0.218	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.878	0.925	18.683	0.151	0.151	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.033	-0.013	15.831	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	103	VAL	0	-0.074	-0.036	13.379	-0.042	-0.042	0.000	0.000	0.000	0.000
105	A	104	PHE	0	-0.029	-0.022	13.976	-0.046	-0.046	0.000	0.000	0.000	0.000
106	A	105	GLU	-1	-0.811	-0.870	16.477	-0.153	-0.153	0.000	0.000	0.000	0.000
107	A	106	PRO	0	-0.030	-0.026	12.385	0.025	0.025	0.000	0.000	0.000	0.000
108	A	107	VAL	0	-0.065	-0.033	15.000	0.028	0.028	0.000	0.000	0.000	0.000
109	A	108	SER	0	-0.002	-0.021	17.178	0.030	0.030	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.961	-0.980	16.218	-0.148	-0.148	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.101	-0.034	15.127	0.025	0.025	0.000	0.000	0.000	0.000
112	A	111	LEU	0	-0.086	-0.029	19.587	0.021	0.021	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)