FMO DATABASE

FMODB ID: ZVRJN

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	OptHSide
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	-1358046.662317
FMO2-HF: Nuclear repulsion	1300860.212376
FMO2-HF: Total energy	-57186.449941
FMO2-MP2: Total energy	-57353.28214

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.
-3.693	0.337	3.426	-2.84	-4.615	-0.009

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 : -0.035 / q_NPA : -0.024

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	0.053	0.011	2.969	-2.859	-0.317	0.183	-1.308	-1.416	-0.004
4	A	6	GLN	0	0.042	0.025	5.574	0.224	0.224	0.000	0.000	0.000	0.000
5	A	7	ASP	-1	-0.828	-0.893	2.400	-1.833	-0.556	1.284	-1.052	-1.509	-0.006
6	A	8	ILE	0	-0.038	-0.013	2.368	-0.149	-0.025	1.959	-0.457	-1.627	0.001
7	A	9	CYS	0	-0.037	-0.013	4.394	0.188	0.275	0.000	-0.023	-0.063	0.000
8	A	10	PHE	0	0.028	0.022	7.342	0.109	0.109	0.000	0.000	0.000	0.000
9	A	11	ALA	0	0.024	0.010	5.877	0.074	0.074	0.000	0.000	0.000	0.000
10	A	12	PHE	0	-0.012	-0.002	7.834	0.069	0.069	0.000	0.000	0.000	0.000
11	A	13	LEU	0	0.024	0.009	9.633	0.057	0.057	0.000	0.000	0.000	0.000
12	A	14	GLN	0	0.016	0.014	11.372	0.028	0.028	0.000	0.000	0.000	0.000
13	A	15	ASN	0	-0.033	-0.047	9.368	0.052	0.052	0.000	0.000	0.000	0.000
14	A	16	TYR	0	-0.093	-0.069	12.729	0.028	0.028	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.017	-0.024	15.176	0.018	0.018	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.836	-0.894	15.844	-0.095	-0.095	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.946	0.988	13.794	0.250	0.250	0.000	0.000	0.000	0.000
18	A	20	MET	0	-0.059	-0.013	18.349	0.014	0.014	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.838	0.917	18.140	0.110	0.110	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.016	-0.019	19.715	0.006	0.006	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.847	-0.909	21.897	-0.094	-0.094	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.035	0.020	22.398	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.063	-0.039	24.154	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.918	0.949	20.713	0.107	0.107	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.028	0.003	19.016	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.015	-0.002	19.321	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	29	TYR	0	-0.033	-0.012	15.712	0.005	0.005	0.000	0.000	0.000	0.000
28	A	30	PHE	0	-0.012	-0.008	13.240	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	31	TYR	0	-0.049	-0.028	16.051	-0.023	-0.023	0.000	0.000	0.000	0.000
30	A	32	ALA	0	0.089	0.058	18.347	0.009	0.009	0.000	0.000	0.000	0.000
31	A	33	SER	0	0.001	-0.015	19.501	0.010	0.010	0.000	0.000	0.000	0.000
32	A	34	THR	0	0.010	-0.004	22.818	0.010	0.010	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.035	0.007	20.829	0.003	0.003	0.000	0.000	0.000	0.000
34	A	36	GLU	-1	-0.874	-0.927	22.602	-0.104	-0.104	0.000	0.000	0.000	0.000
35	A	37	LEU	0	-0.044	-0.006	22.519	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	38	THR	0	-0.033	-0.025	24.542	0.014	0.014	0.000	0.000	0.000	0.000
37	A	39	HIS	0	0.074	0.018	22.540	0.004	0.004	0.000	0.000	0.000	0.000
38	A	40	THR	0	0.079	0.032	26.791	0.006	0.006	0.000	0.000	0.000	0.000
39	A	41	ASN	0	-0.015	-0.009	29.004	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	42	TYR	0	0.039	0.003	26.450	0.006	0.006	0.000	0.000	0.000	0.000
41	A	43	GLN	0	0.012	0.009	33.002	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.051	-0.009	35.866	0.004	0.004	0.000	0.000	0.000	0.000
43	A	45	LYS	1	0.915	0.967	37.859	0.046	0.046	0.000	0.000	0.000	0.000
44	A	46	SER	0	0.039	0.012	40.056	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	47	THR	0	-0.069	-0.046	38.234	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	48	ASN	0	0.015	-0.012	41.315	0.000	0.000	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.866	-0.934	43.188	-0.032	-0.032	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.902	0.968	36.625	0.045	0.045	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.951	-0.946	37.473	-0.044	-0.044	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.780	-0.866	34.687	-0.048	-0.048	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.037	-0.014	32.360	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.019	-0.009	30.671	0.002	0.002	0.000	0.000	0.000	0.000
53	A	55	PRO	0	0.005	0.012	32.244	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.014	-0.014	28.387	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	57	VAL	0	-0.049	-0.024	30.251	0.005	0.005	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.889	0.940	28.633	0.099	0.099	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.045	-0.016	27.685	0.006	0.006	0.000	0.000	0.000	0.000
58	A	60	THR	0	0.052	0.021	27.247	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.029	0.023	26.082	0.008	0.008	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.903	0.937	19.589	0.178	0.178	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.881	-0.941	24.867	-0.095	-0.095	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.069	-0.051	28.151	0.010	0.010	0.000	0.000	0.000	0.000
63	A	65	ILE	0	0.022	0.021	22.963	0.005	0.005	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.043	0.012	25.593	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.895	0.966	26.584	0.085	0.085	0.000	0.000	0.000	0.000
66	A	68	PHE	0	-0.028	-0.013	26.424	0.007	0.007	0.000	0.000	0.000	0.000
67	A	69	PHE	0	0.049	0.005	22.414	0.006	0.006	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.007	-0.007	27.097	0.004	0.004	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.843	0.923	29.135	0.076	0.076	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.044	-0.013	29.500	0.009	0.009	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.757	-0.845	28.195	-0.080	-0.080	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.061	0.019	28.616	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.931	0.968	30.203	0.060	0.060	0.000	0.000	0.000	0.000
74	A	76	VAL	0	0.015	0.026	24.378	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.833	0.892	25.356	0.079	0.079	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.146	-0.086	26.177	0.004	0.004	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.017	-0.011	22.188	0.005	0.005	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.886	0.948	23.647	0.059	0.059	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.023	-0.015	18.875	0.000	0.000	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.821	0.907	21.967	0.055	0.055	0.000	0.000	0.000	0.000
81	A	83	LEU	0	-0.015	-0.019	15.128	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	84	ASP	-1	-0.850	-0.912	19.045	-0.057	-0.057	0.000	0.000	0.000	0.000
83	A	85	THR	0	-0.009	0.013	17.703	0.008	0.008	0.000	0.000	0.000	0.000
84	A	86	ILE	0	-0.011	-0.023	11.693	-0.021	-0.021	0.000	0.000	0.000	0.000
85	A	87	ASP	-1	-0.905	-0.927	14.976	-0.129	-0.129	0.000	0.000	0.000	0.000
86	A	88	PHE	0	0.019	-0.018	10.211	-0.061	-0.061	0.000	0.000	0.000	0.000
87	A	89	GLN	0	-0.026	-0.007	13.281	0.033	0.033	0.000	0.000	0.000	0.000
88	A	90	TYR	0	0.003	0.013	6.752	-0.045	-0.045	0.000	0.000	0.000	0.000
89	A	91	THR	0	0.015	-0.002	13.223	0.065	0.065	0.000	0.000	0.000	0.000
90	A	92	GLY	0	0.034	0.020	15.157	-0.029	-0.029	0.000	0.000	0.000	0.000
91	A	93	HIS	0	0.047	0.013	17.371	0.007	0.007	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.013	-0.001	15.562	-0.034	-0.034	0.000	0.000	0.000	0.000
93	A	95	HIS	0	0.020	0.014	14.252	-0.034	-0.034	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.880	0.937	10.356	0.315	0.315	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.003	0.011	10.483	-0.066	-0.066	0.000	0.000	0.000	0.000
96	A	98	ILE	0	-0.030	-0.017	7.300	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.008	0.003	11.895	0.032	0.032	0.000	0.000	0.000	0.000
98	A	100	ILE	0	0.007	-0.003	10.167	-0.021	-0.021	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.003	-0.006	14.199	0.029	0.029	0.000	0.000	0.000	0.000
100	A	102	ALA	0	0.034	0.022	16.032	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.030	-0.027	17.636	0.015	0.015	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.085	0.036	20.314	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.855	-0.893	22.664	-0.047	-0.047	0.000	0.000	0.000	0.000
104	A	106	MET	0	0.002	0.006	22.678	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	107	PHE	0	0.001	-0.008	25.897	0.007	0.007	0.000	0.000	0.000	0.000
106	A	108	TRP	0	-0.002	0.001	27.313	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	109	THR	0	-0.014	-0.034	29.609	0.004	0.004	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.003	0.006	31.443	0.000	0.000	0.000	0.000	0.000	0.000
109	A	111	THR	0	-0.045	-0.012	32.169	0.001	0.001	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.027	0.017	33.168	0.000	0.000	0.000	0.000	0.000	0.000
111	A	113	VAL	0	0.017	-0.001	29.016	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	114	TYR	0	0.023	0.017	29.198	0.003	0.003	0.000	0.000	0.000	0.000
113	A	115	LYS	1	0.906	0.951	27.240	0.048	0.048	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.033	-0.019	20.426	0.001	0.001	0.000	0.000	0.000	0.000
115	A	117	CYS	0	0.014	0.020	22.292	0.000	0.000	0.000	0.000	0.000	0.000
116	A	118	GLN	0	0.010	-0.021	19.465	0.011	0.011	0.000	0.000	0.000	0.000
117	A	119	THR	0	-0.027	-0.001	18.295	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	120	PHE	0	0.006	-0.009	14.818	0.007	0.007	0.000	0.000	0.000	0.000
119	A	121	ILE	0	-0.036	-0.005	15.471	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.009	0.008	9.876	0.016	0.016	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.025	-0.001	12.693	-0.023	-0.023	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.013	0.000	9.768	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	125	SER	0	0.043	0.017	11.121	0.036	0.036	0.000	0.000	0.000	0.000
124	A	126	SER	0	0.017	-0.012	13.015	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	127	ASN	0	-0.051	-0.030	13.980	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	128	GLY	0	0.018	0.037	10.022	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	129	SER	0	-0.043	-0.027	6.511	0.050	0.050	0.000	0.000	0.000	0.000
128	A	130	THR	0	0.026	0.013	6.388	-0.098	-0.098	0.000	0.000	0.000	0.000
129	A	131	PHE	0	-0.038	-0.029	5.780	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.879	-0.920	10.677	-0.255	-0.255	0.000	0.000	0.000	0.000
131	A	133	ILE	0	-0.041	-0.028	14.358	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	134	THR	0	0.018	-0.015	16.293	0.018	0.018	0.000	0.000	0.000	0.000
133	A	135	ASN	0	-0.020	-0.008	18.400	0.012	0.012	0.000	0.000	0.000	0.000
134	A	136	ASP	-1	-0.708	-0.801	18.568	-0.196	-0.196	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.002	0.004	20.563	0.017	0.017	0.000	0.000	0.000	0.000
136	A	138	ILE	0	0.007	0.021	22.255	-0.007	-0.007	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.919	0.954	24.316	0.087	0.087	0.000	0.000	0.000	0.000
138	A	140	PHE	0	0.003	-0.010	26.626	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	141	ILE	0	-0.052	-0.031	26.149	0.002	0.002	0.000	0.000	0.000	0.000
140	A	142	SER	0	-0.029	-0.028	30.366	0.002	0.002	0.000	0.000	0.000	0.000
141	A	143	ASN	0	-0.012	-0.022	32.532	-0.001	-0.001	0.000	0.000	0.000	0.000

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