FMO DATABASE

FMODB ID: R8948

Calculation Name: 2QZJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QZJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q180B0

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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1064401.082271
FMO2-HF: Nuclear repulsion	1015820.267392
FMO2-HF: Total energy	-48580.814878
FMO2-MP2: Total energy	-48720.813462

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:4:GLN)

Summations of interaction energy for fragment #1(A:4:GLN)

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.
-29.837	-25.109	11.046	-6.657	-9.112	-0.038

Interaction energy analysis for fragmet #1(A:4:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.049 / q_NPA : -0.043

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	6	LYS	1	0.938	0.970	2.470	-7.770	-5.145	1.320	-1.661	-2.283	-0.015
4	A	7	ILE	0	-0.012	0.000	4.951	0.262	0.333	-0.001	-0.006	-0.063	0.000
5	A	8	LEU	0	-0.009	0.013	8.141	0.273	0.273	0.000	0.000	0.000	0.000
6	A	9	ILE	0	-0.030	-0.024	11.331	-0.096	-0.096	0.000	0.000	0.000	0.000
7	A	10	ILE	0	-0.014	-0.011	14.087	0.083	0.083	0.000	0.000	0.000	0.000
8	A	11	ASP	-1	-0.754	-0.880	17.612	-0.277	-0.277	0.000	0.000	0.000	0.000
9	A	12	GLY	0	0.059	0.038	20.200	0.028	0.028	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.881	-0.934	22.393	-0.226	-0.226	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.960	0.964	20.196	0.002	0.002	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.875	-0.921	19.436	-0.241	-0.241	0.000	0.000	0.000	0.000
13	A	16	ASN	0	-0.116	-0.066	18.981	-0.090	-0.090	0.000	0.000	0.000	0.000
14	A	17	CYS	0	-0.039	-0.022	16.399	-0.075	-0.075	0.000	0.000	0.000	0.000
15	A	18	GLN	0	0.005	0.005	14.634	-0.120	-0.120	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.934	0.965	14.830	0.379	0.379	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.018	-0.027	13.380	-0.136	-0.136	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.894	0.969	10.314	-0.143	-0.143	0.000	0.000	0.000	0.000
19	A	22	GLY	0	0.063	0.038	10.142	-0.311	-0.311	0.000	0.000	0.000	0.000
20	A	23	PHE	0	-0.013	-0.018	10.700	-0.297	-0.297	0.000	0.000	0.000	0.000
21	A	24	LEU	0	-0.015	-0.017	8.685	-0.223	-0.223	0.000	0.000	0.000	0.000
22	A	25	GLU	-1	-0.869	-0.945	6.200	-1.620	-1.620	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.984	-0.988	6.099	-2.950	-2.950	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.835	0.939	7.583	1.728	1.728	0.000	0.000	0.000	0.000
25	A	28	GLY	0	-0.016	-0.003	3.601	0.219	0.570	0.002	-0.138	-0.215	-0.001
26	A	29	ILE	0	-0.066	-0.032	1.956	-16.271	-16.328	6.560	-2.995	-3.507	-0.041
27	A	30	SER	0	-0.017	0.008	2.309	-1.442	0.061	3.157	-1.764	-2.895	0.019
28	A	31	ILE	0	0.012	-0.011	4.231	-1.023	-0.788	0.008	-0.093	-0.149	0.000
29	A	32	ASP	-1	-0.838	-0.887	7.749	1.425	1.425	0.000	0.000	0.000	0.000
30	A	33	LEU	0	-0.053	-0.043	10.529	-0.239	-0.239	0.000	0.000	0.000	0.000
31	A	34	ALA	0	0.030	-0.003	14.146	0.093	0.093	0.000	0.000	0.000	0.000
32	A	35	TYR	0	-0.016	-0.016	17.460	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	36	ASN	0	0.032	0.023	20.874	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	37	CYS	0	0.007	0.011	21.310	0.007	0.007	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.959	-0.965	21.776	0.107	0.107	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.881	-0.961	19.368	0.116	0.116	0.000	0.000	0.000	0.000
37	A	40	ALA	0	-0.050	-0.028	17.681	0.041	0.041	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.013	-0.026	17.685	0.015	0.015	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.032	0.034	19.271	0.022	0.022	0.000	0.000	0.000	0.000
40	A	43	LYS	1	0.909	0.967	12.966	-0.331	-0.331	0.000	0.000	0.000	0.000
41	A	44	ILE	0	-0.018	-0.011	14.336	0.037	0.037	0.000	0.000	0.000	0.000
42	A	45	PHE	0	-0.051	-0.027	15.961	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	46	SER	0	-0.074	-0.043	14.919	0.023	0.023	0.000	0.000	0.000	0.000
44	A	47	ASN	0	-0.064	-0.017	10.118	0.327	0.327	0.000	0.000	0.000	0.000
45	A	48	LYS	1	0.947	0.978	9.002	-0.303	-0.303	0.000	0.000	0.000	0.000
46	A	49	TYR	0	-0.050	-0.055	8.385	-0.081	-0.081	0.000	0.000	0.000	0.000
47	A	50	ASP	-1	-0.831	-0.911	6.061	-2.192	-2.192	0.000	0.000	0.000	0.000
48	A	51	LEU	0	-0.040	-0.036	9.338	0.138	0.138	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.011	0.005	10.858	-0.038	-0.038	0.000	0.000	0.000	0.000
50	A	53	PHE	0	-0.005	-0.004	11.815	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	54	LEU	0	-0.025	-0.021	15.624	0.051	0.051	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.761	-0.860	18.980	-0.230	-0.230	0.000	0.000	0.000	0.000
53	A	56	ILE	0	-0.024	-0.015	22.054	0.020	0.020	0.000	0.000	0.000	0.000
54	A	57	ILE	0	-0.008	0.002	25.482	0.022	0.022	0.000	0.000	0.000	0.000
55	A	58	LEU	0	0.007	0.000	22.291	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	59	SER	0	-0.005	-0.018	26.213	0.007	0.007	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.797	-0.902	25.934	0.001	0.001	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.014	0.008	28.057	0.011	0.011	0.000	0.000	0.000	0.000
59	A	62	ASP	-1	-0.792	-0.868	27.541	-0.079	-0.079	0.000	0.000	0.000	0.000
60	A	63	GLY	0	0.023	-0.015	23.983	0.006	0.006	0.000	0.000	0.000	0.000
61	A	64	TRP	0	-0.018	-0.012	24.225	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	65	THR	0	-0.083	-0.077	26.572	0.007	0.007	0.000	0.000	0.000	0.000
63	A	66	LEU	0	0.005	0.007	20.937	0.013	0.013	0.000	0.000	0.000	0.000
64	A	67	CYS	0	-0.024	0.014	21.790	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	68	LYS	1	0.951	0.968	22.686	0.077	0.077	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.939	0.978	23.805	-0.025	-0.025	0.000	0.000	0.000	0.000
67	A	70	ILE	0	0.021	0.018	17.742	0.021	0.021	0.000	0.000	0.000	0.000
68	A	71	ARG	1	0.791	0.886	17.653	0.186	0.186	0.000	0.000	0.000	0.000
69	A	72	ASN	0	-0.081	-0.020	21.568	0.002	0.002	0.000	0.000	0.000	0.000
70	A	73	VAL	0	-0.059	-0.030	17.385	0.023	0.023	0.000	0.000	0.000	0.000
71	A	74	THR	0	-0.006	-0.002	14.213	0.003	0.003	0.000	0.000	0.000	0.000
72	A	75	THR	0	0.017	0.007	16.726	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	76	CYS	0	-0.016	-0.001	13.025	-0.046	-0.046	0.000	0.000	0.000	0.000
74	A	77	PRO	0	0.021	0.027	13.240	0.027	0.027	0.000	0.000	0.000	0.000
75	A	78	ILE	0	-0.004	-0.005	14.830	-0.056	-0.056	0.000	0.000	0.000	0.000
76	A	79	VAL	0	-0.032	-0.026	16.072	0.017	0.017	0.000	0.000	0.000	0.000
77	A	80	TYR	0	0.061	0.010	18.037	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	81	MET	0	-0.057	-0.011	17.687	-0.062	-0.062	0.000	0.000	0.000	0.000
79	A	82	THR	0	0.045	0.025	21.249	0.027	0.027	0.000	0.000	0.000	0.000
80	A	83	TYR	0	0.050	0.007	24.909	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.019	0.003	28.071	0.008	0.008	0.000	0.000	0.000	0.000
82	A	85	ASN	0	-0.010	0.010	29.002	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.855	-0.935	30.952	-0.127	-0.127	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.876	-0.940	32.091	-0.141	-0.141	0.000	0.000	0.000	0.000
85	A	88	GLN	0	-0.028	-0.028	32.865	0.003	0.003	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.005	-0.004	29.115	0.008	0.008	0.000	0.000	0.000	0.000
87	A	90	ILE	0	0.034	0.011	27.182	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	91	LEU	0	0.007	0.006	28.346	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	92	ASN	0	0.017	0.017	30.127	0.009	0.009	0.000	0.000	0.000	0.000
90	A	93	ALA	0	-0.015	-0.003	24.976	0.005	0.005	0.000	0.000	0.000	0.000
91	A	94	LEU	0	-0.016	-0.016	24.267	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	95	ASN	0	-0.042	-0.022	26.124	0.015	0.015	0.000	0.000	0.000	0.000
93	A	96	SER	0	-0.111	-0.043	26.116	0.018	0.018	0.000	0.000	0.000	0.000
94	A	97	GLY	0	0.004	0.001	23.769	0.010	0.010	0.000	0.000	0.000	0.000
95	A	98	GLY	0	-0.012	0.005	21.447	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.859	-0.916	18.710	-0.255	-0.255	0.000	0.000	0.000	0.000
97	A	100	ASP	-1	-0.842	-0.928	19.677	-0.373	-0.373	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.042	-0.050	21.235	0.009	0.009	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.040	-0.022	18.090	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	103	ILE	0	0.039	0.012	22.489	0.014	0.014	0.000	0.000	0.000	0.000
101	A	104	LYS	1	0.732	0.879	21.747	0.249	0.249	0.000	0.000	0.000	0.000
102	A	105	PRO	0	-0.006	-0.018	24.599	0.023	0.023	0.000	0.000	0.000	0.000
103	A	106	LEU	0	0.049	0.011	18.243	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	107	ASN	0	0.025	0.028	21.561	-0.052	-0.052	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.039	-0.008	16.184	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.871	-0.925	16.494	-0.929	-0.929	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.020	-0.022	17.829	-0.043	-0.043	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.019	0.012	14.021	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	112	TYR	0	0.106	0.029	9.135	0.169	0.169	0.000	0.000	0.000	0.000
110	A	113	ALA	0	-0.042	-0.017	13.996	-0.057	-0.057	0.000	0.000	0.000	0.000
111	A	114	LYS	1	0.893	0.947	16.244	0.434	0.434	0.000	0.000	0.000	0.000
112	A	115	VAL	0	0.034	0.027	10.208	0.041	0.041	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.922	0.969	11.496	1.029	1.029	0.000	0.000	0.000	0.000
114	A	117	ALA	0	-0.075	-0.037	12.743	0.126	0.126	0.000	0.000	0.000	0.000
115	A	118	ILE	0	0.019	0.000	13.416	0.098	0.098	0.000	0.000	0.000	0.000
116	A	119	LEU	0	0.042	0.028	7.528	0.094	0.094	0.000	0.000	0.000	0.000
117	A	120	ARG	1	0.947	0.989	11.257	0.579	0.579	0.000	0.000	0.000	0.000
118	A	121	ARG	1	0.905	0.962	13.209	0.297	0.297	0.000	0.000	0.000	0.000
119	A	122	MET	0	-0.011	-0.005	11.659	0.078	0.078	0.000	0.000	0.000	0.000
120	A	123	ASN	0	-0.008	0.001	7.961	0.100	0.100	0.000	0.000	0.000	0.000
121	A	124	SER	0	-0.082	-0.041	12.185	0.029	0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:GLN)