FMO DATABASE

FMODB ID: 8921Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-734062.232699
FMO2-HF: Nuclear repulsion	690697.638409
FMO2-HF: Total energy	-43364.59429
FMO2-MP2: Total energy	-43491.278846

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.
-3.024	0.469	0.291	-1.471	-2.311	-0.003

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 : 0.016 / 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	0.048	0.014	3.656	-2.141	-0.623	0.006	-0.729	-0.794	0.002
4	A	3	ASN	0	0.058	0.033	2.959	-1.558	0.028	0.283	-0.608	-1.260	-0.005
5	A	4	ILE	0	0.024	0.031	4.071	0.572	0.961	0.002	-0.134	-0.257	0.000
6	A	5	TYR	0	-0.032	-0.038	6.277	0.574	0.574	0.000	0.000	0.000	0.000
7	A	6	ASP	-1	-0.887	-0.944	7.502	-0.327	-0.327	0.000	0.000	0.000	0.000
8	A	7	SER	0	-0.008	-0.002	8.108	0.170	0.170	0.000	0.000	0.000	0.000
9	A	8	ALA	0	-0.001	0.006	10.141	0.165	0.165	0.000	0.000	0.000	0.000
10	A	9	ASN	0	-0.032	-0.015	11.937	0.133	0.133	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.923	-0.972	11.875	-0.446	-0.446	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.033	0.030	14.351	0.060	0.060	0.000	0.000	0.000	0.000
13	A	12	SER	0	-0.004	0.005	16.021	0.069	0.069	0.000	0.000	0.000	0.000
14	A	13	ARG	1	0.848	0.902	16.636	0.211	0.211	0.000	0.000	0.000	0.000
15	A	14	GLY	0	0.024	0.017	18.734	0.026	0.026	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.007	-0.005	19.646	0.025	0.025	0.000	0.000	0.000	0.000
17	A	16	ARG	1	0.899	0.942	19.255	0.188	0.188	0.000	0.000	0.000	0.000
18	A	17	GLY	0	-0.060	-0.026	23.466	0.018	0.018	0.000	0.000	0.000	0.000
19	A	18	LEU	0	0.004	0.019	24.370	0.007	0.007	0.000	0.000	0.000	0.000
20	A	19	PRO	0	0.002	-0.011	26.664	0.008	0.008	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.804	-0.908	28.950	-0.113	-0.113	0.000	0.000	0.000	0.000
22	A	21	TYR	0	0.020	0.019	26.665	0.007	0.007	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.927	0.953	28.457	0.107	0.107	0.000	0.000	0.000	0.000
24	A	23	ALA	0	-0.024	-0.004	31.177	0.007	0.007	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.032	0.023	31.495	0.006	0.006	0.000	0.000	0.000	0.000
26	A	25	LYS	1	0.864	0.937	30.827	0.075	0.075	0.000	0.000	0.000	0.000
27	A	26	ALA	0	0.028	0.008	33.146	0.005	0.005	0.000	0.000	0.000	0.000
28	A	27	ALA	0	0.045	0.025	36.261	0.005	0.005	0.000	0.000	0.000	0.000
29	A	28	LYS	1	0.928	0.969	35.073	0.057	0.057	0.000	0.000	0.000	0.000
30	A	29	ASP	-1	-0.898	-0.955	35.781	-0.055	-0.055	0.000	0.000	0.000	0.000
31	A	30	ALA	0	-0.013	-0.012	38.385	0.004	0.004	0.000	0.000	0.000	0.000
32	A	31	ILE	0	-0.012	0.002	39.415	0.003	0.003	0.000	0.000	0.000	0.000
33	A	32	ALA	0	-0.076	-0.035	39.552	0.003	0.003	0.000	0.000	0.000	0.000
34	A	33	ALA	0	-0.032	-0.005	41.664	0.003	0.003	0.000	0.000	0.000	0.000
35	A	34	ASP	-1	-0.842	-0.917	44.310	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	35	ALA	0	-0.004	-0.023	46.675	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.957	-0.966	48.757	-0.030	-0.030	0.000	0.000	0.000	0.000
38	A	37	ALA	0	0.009	0.004	44.845	0.000	0.000	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.010	-0.021	43.771	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	39	LYS	1	0.853	0.964	44.502	0.027	0.027	0.000	0.000	0.000	0.000
41	A	40	ILE	0	0.038	0.026	45.765	0.000	0.000	0.000	0.000	0.000	0.000
42	A	41	PHE	0	0.001	-0.005	37.204	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	42	THR	0	-0.040	-0.055	42.164	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	43	ASP	-1	-0.860	-0.926	43.464	-0.030	-0.030	0.000	0.000	0.000	0.000
45	A	44	TYR	0	-0.054	-0.030	40.471	0.000	0.000	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.017	-0.030	37.781	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	46	ALA	0	-0.003	0.010	40.872	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	47	PHE	0	-0.011	0.004	43.512	0.001	0.001	0.000	0.000	0.000	0.000
49	A	48	GLN	0	0.003	-0.010	37.293	0.000	0.000	0.000	0.000	0.000	0.000
50	A	49	GLU	-1	-0.901	-0.944	40.743	-0.032	-0.032	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.939	-1.001	42.202	-0.029	-0.029	0.000	0.000	0.000	0.000
52	A	51	ILE	0	-0.034	-0.013	38.620	0.001	0.001	0.000	0.000	0.000	0.000
53	A	52	GLN	0	-0.051	-0.010	37.933	0.000	0.000	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.932	0.954	41.607	0.026	0.026	0.000	0.000	0.000	0.000
55	A	54	LEU	0	-0.021	0.007	43.502	0.002	0.002	0.000	0.000	0.000	0.000
56	A	55	ALA	0	-0.014	0.001	43.585	0.000	0.000	0.000	0.000	0.000	0.000
57	A	56	GLN	0	-0.092	-0.058	44.781	0.002	0.002	0.000	0.000	0.000	0.000
58	A	57	THR	0	-0.026	-0.006	45.020	0.000	0.000	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.041	0.010	47.813	0.002	0.002	0.000	0.000	0.000	0.000
60	A	59	GLN	0	-0.080	-0.031	50.094	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	60	MET	0	0.021	0.009	51.268	0.001	0.001	0.000	0.000	0.000	0.000
62	A	61	PRO	0	0.009	0.004	50.841	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	62	ASP	-1	-0.764	-0.847	49.863	-0.027	-0.027	0.000	0.000	0.000	0.000
64	A	63	ALA	0	0.046	-0.001	51.419	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	64	SER	0	-0.019	-0.013	52.950	0.000	0.000	0.000	0.000	0.000	0.000
66	A	65	PHE	0	0.030	-0.001	43.900	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	66	GLN	0	-0.034	-0.007	49.121	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	67	ALA	0	0.022	0.015	50.300	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.925	0.970	49.316	0.027	0.027	0.000	0.000	0.000	0.000
70	A	69	MET	0	-0.027	0.000	42.271	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.940	-0.981	47.433	-0.034	-0.034	0.000	0.000	0.000	0.000
72	A	71	GLY	0	-0.020	-0.013	49.772	0.000	0.000	0.000	0.000	0.000	0.000
73	A	72	PHE	0	0.025	-0.008	45.873	0.000	0.000	0.000	0.000	0.000	0.000
74	A	73	GLY	0	0.040	0.038	46.002	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	74	LYS	1	0.932	0.957	47.039	0.034	0.034	0.000	0.000	0.000	0.000
76	A	75	GLN	0	0.000	0.000	48.628	0.000	0.000	0.000	0.000	0.000	0.000
77	A	76	ILE	0	-0.018	0.004	42.893	0.000	0.000	0.000	0.000	0.000	0.000
78	A	77	GLN	0	-0.053	-0.045	45.080	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	78	GLY	0	-0.016	0.005	47.858	0.000	0.000	0.000	0.000	0.000	0.000
80	A	79	ASN	0	0.055	0.031	46.688	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	80	SER	0	0.027	0.008	46.375	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	81	LEU	0	0.026	0.021	43.526	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.019	-0.001	42.072	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	83	SER	0	-0.013	-0.021	41.646	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.909	-0.954	39.556	-0.066	-0.066	0.000	0.000	0.000	0.000
86	A	85	PHE	0	0.001	-0.005	34.687	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	86	PHE	0	0.002	-0.017	36.672	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	87	THR	0	-0.005	0.011	36.958	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.891	0.949	34.909	0.068	0.068	0.000	0.000	0.000	0.000
90	A	89	GLN	0	0.035	0.011	32.243	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	90	GLN	0	-0.051	-0.021	31.955	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	91	GLN	0	0.003	-0.013	32.100	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.024	0.020	26.457	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	93	ALA	0	-0.023	-0.014	27.616	-0.012	-0.012	0.000	0.000	0.000	0.000
95	A	94	ILE	0	0.018	0.018	27.651	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	95	TYR	0	0.002	0.008	25.075	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	96	LEU	0	-0.044	-0.029	22.787	-0.017	-0.017	0.000	0.000	0.000	0.000
98	A	97	SER	0	0.022	0.019	22.453	-0.016	-0.016	0.000	0.000	0.000	0.000
99	A	98	ASP	-1	-0.941	-0.978	23.205	-0.178	-0.178	0.000	0.000	0.000	0.000
100	A	99	ILE	0	-0.009	-0.010	17.963	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	100	GLU	-1	-0.954	-0.978	18.324	-0.225	-0.225	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.914	0.948	18.494	0.145	0.145	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.011	0.009	15.489	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	103	VAL	0	-0.059	-0.031	13.031	-0.038	-0.038	0.000	0.000	0.000	0.000
105	A	104	PHE	0	-0.034	-0.031	13.599	-0.062	-0.062	0.000	0.000	0.000	0.000
106	A	105	GLU	-1	-0.877	-0.911	16.021	-0.199	-0.199	0.000	0.000	0.000	0.000
107	A	106	PRO	0	0.012	-0.006	11.954	0.019	0.019	0.000	0.000	0.000	0.000
108	A	107	VAL	0	-0.039	-0.018	14.604	0.025	0.025	0.000	0.000	0.000	0.000
109	A	108	SER	0	-0.007	-0.021	16.427	0.037	0.037	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.954	-0.960	16.665	-0.206	-0.206	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.113	-0.047	15.006	0.022	0.022	0.000	0.000	0.000	0.000
112	A	111	LEU	0	-0.088	-0.029	19.215	0.026	0.026	0.000	0.000	0.000	0.000

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