FMO DATABASE

FMODB ID: R8NZ8

Calculation Name: 2QIY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QIY

Chain ID: A

ChEMBL ID:

UniProt ID: P53741

Base Structure: X-ray

Registration Date: 2023-09-20

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1358571.181104
FMO2-HF: Nuclear repulsion	1301384.266414
FMO2-HF: Total energy	-57186.91469
FMO2-MP2: Total energy	-57353.669049

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:3:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
-3.991	0.543	3.711	-3.391	-4.853	-0.005

Interaction energy analysis for fragmet #1(A:3:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.015 / q_NPA : 0.015

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	5	VAL	0	0.027	-0.007	3.104	-2.433	0.846	0.101	-1.826	-1.554	0.000
4	A	6	GLN	0	0.028	0.024	5.852	0.482	0.482	0.000	0.000	0.000	0.000
5	A	7	ASP	-1	-0.814	-0.878	2.367	-2.647	-1.810	1.798	-1.091	-1.545	-0.004
6	A	8	ILE	0	-0.007	-0.003	2.361	-0.031	0.313	1.812	-0.452	-1.703	-0.001
7	A	9	CYS	0	-0.026	-0.002	4.432	0.134	0.208	0.000	-0.022	-0.051	0.000
8	A	10	PHE	0	0.026	0.017	7.344	0.123	0.123	0.000	0.000	0.000	0.000
9	A	11	ALA	0	0.023	0.013	5.780	0.069	0.069	0.000	0.000	0.000	0.000
10	A	12	PHE	0	-0.006	0.001	7.701	0.054	0.054	0.000	0.000	0.000	0.000
11	A	13	LEU	0	0.034	0.005	9.682	0.040	0.040	0.000	0.000	0.000	0.000
12	A	14	GLN	0	0.018	0.016	11.064	0.037	0.037	0.000	0.000	0.000	0.000
13	A	15	ASN	0	-0.029	-0.046	9.601	0.024	0.024	0.000	0.000	0.000	0.000
14	A	16	TYR	0	-0.080	-0.049	12.743	0.009	0.009	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.031	-0.017	15.315	0.006	0.006	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.831	-0.875	14.610	0.112	0.112	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.908	0.961	14.099	0.027	0.027	0.000	0.000	0.000	0.000
18	A	20	MET	0	-0.070	-0.015	18.313	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.857	0.902	18.363	-0.082	-0.082	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.017	-0.018	19.412	0.003	0.003	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.818	-0.886	21.657	0.047	0.047	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.036	0.020	22.383	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.053	-0.033	24.121	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.875	0.923	21.083	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.003	0.015	18.981	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.008	-0.007	19.380	-0.011	-0.011	0.000	0.000	0.000	0.000
27	A	29	TYR	0	-0.047	-0.014	16.016	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	30	PHE	0	0.015	0.004	13.684	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	31	TYR	0	-0.025	-0.021	16.187	-0.024	-0.024	0.000	0.000	0.000	0.000
30	A	32	ALA	0	0.041	0.031	18.924	0.014	0.014	0.000	0.000	0.000	0.000
31	A	33	SER	0	-0.003	-0.017	19.929	0.005	0.005	0.000	0.000	0.000	0.000
32	A	34	THR	0	0.002	-0.010	23.241	0.008	0.008	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.008	0.021	21.228	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	36	GLU	-1	-0.824	-0.895	23.039	-0.092	-0.092	0.000	0.000	0.000	0.000
35	A	37	LEU	0	-0.031	-0.003	22.548	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	38	THR	0	-0.030	-0.024	24.534	0.007	0.007	0.000	0.000	0.000	0.000
37	A	39	HIS	0	0.071	0.031	22.269	0.001	0.001	0.000	0.000	0.000	0.000
38	A	40	THR	0	0.068	0.026	26.674	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	41	ASN	0	0.000	0.000	29.005	0.007	0.007	0.000	0.000	0.000	0.000
40	A	42	TYR	0	0.034	0.001	26.492	0.003	0.003	0.000	0.000	0.000	0.000
41	A	43	GLN	0	-0.005	-0.002	33.090	0.001	0.001	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.035	-0.005	35.893	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	45	LYS	1	0.825	0.926	37.759	0.031	0.031	0.000	0.000	0.000	0.000
44	A	46	SER	0	0.066	0.027	39.568	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	47	THR	0	-0.052	-0.036	37.866	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	48	ASN	0	0.024	0.007	41.231	0.002	0.002	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.872	-0.929	43.407	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.846	0.928	36.888	0.025	0.025	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.830	-0.907	37.257	-0.033	-0.033	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.776	-0.854	34.946	-0.045	-0.045	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.020	-0.003	32.024	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.008	-0.011	30.683	0.005	0.005	0.000	0.000	0.000	0.000
53	A	55	PRO	0	0.001	0.009	32.159	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.022	-0.019	28.369	0.003	0.003	0.000	0.000	0.000	0.000
55	A	57	VAL	0	-0.054	-0.023	30.222	0.002	0.002	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.851	0.908	28.082	0.096	0.096	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.040	-0.015	27.647	0.007	0.007	0.000	0.000	0.000	0.000
58	A	60	THR	0	0.043	0.021	27.302	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.025	0.025	26.308	0.008	0.008	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.866	0.932	19.211	0.061	0.061	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.877	-0.945	24.909	-0.022	-0.022	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.073	-0.053	28.191	0.011	0.011	0.000	0.000	0.000	0.000
63	A	65	ILE	0	0.029	0.024	22.828	0.004	0.004	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.016	-0.006	24.633	0.002	0.002	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.904	0.970	26.483	0.034	0.034	0.000	0.000	0.000	0.000
66	A	68	PHE	0	-0.029	-0.010	26.331	0.004	0.004	0.000	0.000	0.000	0.000
67	A	69	PHE	0	0.056	0.014	22.443	0.004	0.004	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.010	-0.014	27.143	0.007	0.007	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.828	0.917	29.259	0.028	0.028	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.011	-0.006	29.401	0.002	0.002	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.771	-0.840	27.729	0.021	0.021	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.065	0.025	28.327	0.002	0.002	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.888	0.957	30.331	0.008	0.008	0.000	0.000	0.000	0.000
74	A	76	VAL	0	-0.002	0.013	24.075	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.836	0.880	25.289	-0.034	-0.034	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.097	-0.063	26.275	0.003	0.003	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.009	-0.006	22.185	0.000	0.000	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.824	0.905	23.334	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.025	-0.012	18.758	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.801	0.899	21.800	0.064	0.064	0.000	0.000	0.000	0.000
81	A	83	LEU	0	-0.018	-0.026	15.478	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	84	ASP	-1	-0.832	-0.900	18.875	-0.063	-0.063	0.000	0.000	0.000	0.000
83	A	85	THR	0	-0.037	-0.007	17.527	0.002	0.002	0.000	0.000	0.000	0.000
84	A	86	ILE	0	-0.001	-0.016	11.297	0.008	0.008	0.000	0.000	0.000	0.000
85	A	87	ASP	-1	-0.871	-0.910	14.301	-0.292	-0.292	0.000	0.000	0.000	0.000
86	A	88	PHE	0	0.009	-0.017	10.163	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	89	GLN	0	-0.014	-0.007	13.091	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	90	TYR	0	0.011	0.013	6.752	-0.082	-0.082	0.000	0.000	0.000	0.000
89	A	91	THR	0	0.025	0.001	13.131	0.085	0.085	0.000	0.000	0.000	0.000
90	A	92	GLY	0	0.028	0.017	15.267	-0.027	-0.027	0.000	0.000	0.000	0.000
91	A	93	HIS	0	0.056	0.020	17.488	-0.023	-0.023	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.008	-0.002	15.733	-0.044	-0.044	0.000	0.000	0.000	0.000
93	A	95	HIS	0	0.026	0.033	15.004	-0.049	-0.049	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.838	0.902	10.836	0.571	0.571	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.009	0.016	11.043	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	98	ILE	0	-0.021	-0.017	7.670	-0.074	-0.074	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.004	0.012	12.274	0.074	0.074	0.000	0.000	0.000	0.000
98	A	100	ILE	0	-0.010	-0.009	10.209	-0.060	-0.060	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.003	-0.009	14.017	0.044	0.044	0.000	0.000	0.000	0.000
100	A	102	ALA	0	0.040	0.025	15.593	-0.022	-0.022	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.015	-0.023	17.579	0.019	0.019	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.063	0.033	20.154	0.001	0.001	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.822	-0.886	22.602	-0.050	-0.050	0.000	0.000	0.000	0.000
104	A	106	MET	0	0.008	0.025	22.559	0.009	0.009	0.000	0.000	0.000	0.000
105	A	107	PHE	0	-0.005	-0.012	25.469	0.002	0.002	0.000	0.000	0.000	0.000
106	A	108	TRP	0	-0.001	-0.004	26.989	0.001	0.001	0.000	0.000	0.000	0.000
107	A	109	THR	0	-0.016	-0.028	29.232	0.002	0.002	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.014	0.017	31.308	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	111	THR	0	-0.044	-0.015	31.671	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.032	0.021	32.960	0.002	0.002	0.000	0.000	0.000	0.000
111	A	113	VAL	0	0.008	0.000	28.699	0.000	0.000	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.020	-0.020	28.925	0.001	0.001	0.000	0.000	0.000	0.000
113	A	115	LYS	1	0.909	0.949	27.184	0.062	0.062	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.062	-0.030	20.543	0.001	0.001	0.000	0.000	0.000	0.000
115	A	117	CYS	0	0.005	0.023	22.167	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	118	GLN	0	-0.009	-0.027	19.309	0.022	0.022	0.000	0.000	0.000	0.000
117	A	119	THR	0	-0.003	0.007	18.384	-0.023	-0.023	0.000	0.000	0.000	0.000
118	A	120	PHE	0	-0.003	-0.012	14.980	0.023	0.023	0.000	0.000	0.000	0.000
119	A	121	ILE	0	-0.030	-0.008	15.772	-0.035	-0.035	0.000	0.000	0.000	0.000
120	A	122	LEU	0	0.000	0.010	10.023	0.041	0.041	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.015	0.000	13.263	-0.057	-0.057	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.007	-0.004	10.346	0.027	0.027	0.000	0.000	0.000	0.000
123	A	125	SER	0	0.017	0.005	11.598	0.027	0.027	0.000	0.000	0.000	0.000
124	A	126	SER	0	0.034	-0.006	13.477	-0.029	-0.029	0.000	0.000	0.000	0.000
125	A	127	ASN	0	-0.063	-0.030	14.237	0.011	0.011	0.000	0.000	0.000	0.000
126	A	128	GLY	0	0.023	0.039	10.535	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	129	SER	0	-0.029	-0.020	7.283	0.092	0.092	0.000	0.000	0.000	0.000
128	A	130	THR	0	0.004	0.003	7.095	0.026	0.026	0.000	0.000	0.000	0.000
129	A	131	PHE	0	-0.010	-0.018	6.333	-0.085	-0.085	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.858	-0.910	11.355	-0.059	-0.059	0.000	0.000	0.000	0.000
131	A	133	ILE	0	-0.029	-0.026	15.033	-0.034	-0.034	0.000	0.000	0.000	0.000
132	A	134	THR	0	0.016	-0.006	16.651	0.020	0.020	0.000	0.000	0.000	0.000
133	A	135	ASN	0	-0.014	-0.006	18.734	0.004	0.004	0.000	0.000	0.000	0.000
134	A	136	ASP	-1	-0.723	-0.805	18.751	-0.129	-0.129	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.006	-0.004	20.627	0.017	0.017	0.000	0.000	0.000	0.000
136	A	138	ILE	0	0.000	0.021	22.310	-0.011	-0.011	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.911	0.944	24.181	0.090	0.090	0.000	0.000	0.000	0.000
138	A	140	PHE	0	0.029	0.007	26.475	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	141	ILE	0	-0.051	-0.035	26.231	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	142	SER	0	-0.038	-0.030	30.252	0.003	0.003	0.000	0.000	0.000	0.000
141	A	143	ASN	0	-0.013	-0.018	32.594	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:VAL)