FMO DATABASE

FMODB ID: Q1ZYY

Calculation Name: 2VSZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2VSZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q92556

Base Structure: X-ray

Registration Date: 2023-06-19

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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1319108.441851
FMO2-HF: Nuclear repulsion	1259728.251695
FMO2-HF: Total energy	-59380.190156
FMO2-MP2: Total energy	-59552.657523

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:527:GLY)

Summations of interaction energy for fragment #1(A:527: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.
6.03	1.799	1.22	4.13	-1.12	-0.007

Interaction energy analysis for fragmet #1(A:527:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.040 / q_NPA : 0.037

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	529	LEU	0	0.008	-0.011	2.844	7.260	2.898	1.218	4.182	-1.039	-0.007
4	A	530	GLY	0	0.040	0.028	3.928	-1.412	-1.434	0.003	-0.046	0.065	0.000
5	A	531	SER	0	0.003	-0.017	4.894	1.098	1.251	-0.001	-0.006	-0.146	0.000
6	A	532	PRO	0	0.083	0.038	5.676	-0.385	-0.385	0.000	0.000	0.000	0.000
7	A	533	ILE	0	-0.048	-0.014	8.683	-0.180	-0.180	0.000	0.000	0.000	0.000
8	A	534	LEU	0	0.004	0.009	9.358	-0.069	-0.069	0.000	0.000	0.000	0.000
9	A	535	GLU	-1	-0.861	-0.931	9.133	-0.024	-0.024	0.000	0.000	0.000	0.000
10	A	536	LEU	0	-0.009	0.009	12.528	-0.044	-0.044	0.000	0.000	0.000	0.000
11	A	537	LYS	1	0.873	0.921	15.452	0.007	0.007	0.000	0.000	0.000	0.000
12	A	538	GLU	-1	-0.932	-0.986	12.291	-0.263	-0.263	0.000	0.000	0.000	0.000
13	A	539	LYS	1	0.808	0.900	12.306	0.108	0.108	0.000	0.000	0.000	0.000
14	A	540	ILE	0	0.033	0.015	15.646	0.003	0.003	0.000	0.000	0.000	0.000
15	A	541	GLN	0	0.037	0.028	18.015	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	542	PRO	0	0.003	-0.002	18.349	0.001	0.001	0.000	0.000	0.000	0.000
17	A	543	GLU	-1	-0.797	-0.888	17.100	-0.121	-0.121	0.000	0.000	0.000	0.000
18	A	544	ILE	0	0.000	0.003	21.066	0.004	0.004	0.000	0.000	0.000	0.000
19	A	545	LEU	0	-0.029	-0.013	23.637	0.001	0.001	0.000	0.000	0.000	0.000
20	A	546	GLU	-1	-0.760	-0.851	24.023	-0.099	-0.099	0.000	0.000	0.000	0.000
21	A	547	LEU	0	-0.003	0.003	25.187	0.002	0.002	0.000	0.000	0.000	0.000
22	A	548	ILE	0	-0.004	-0.008	26.911	0.003	0.003	0.000	0.000	0.000	0.000
23	A	549	LYS	1	0.822	0.895	27.938	0.096	0.096	0.000	0.000	0.000	0.000
24	A	550	GLN	0	-0.011	-0.023	28.500	0.006	0.006	0.000	0.000	0.000	0.000
25	A	551	GLN	0	0.031	0.020	31.041	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	552	ARG	1	0.801	0.874	33.034	0.032	0.032	0.000	0.000	0.000	0.000
27	A	553	LEU	0	-0.001	0.005	32.600	0.001	0.001	0.000	0.000	0.000	0.000
28	A	554	ASN	0	-0.018	-0.025	32.569	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	555	ARG	1	0.878	0.936	36.533	0.019	0.019	0.000	0.000	0.000	0.000
30	A	556	LEU	0	0.024	0.030	39.392	0.001	0.001	0.000	0.000	0.000	0.000
31	A	557	VAL	0	-0.054	-0.013	37.198	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	558	GLU	-1	-0.949	-0.950	40.401	-0.021	-0.021	0.000	0.000	0.000	0.000
33	A	559	GLY	0	-0.004	-0.001	42.322	0.000	0.000	0.000	0.000	0.000	0.000
34	A	560	THR	0	-0.031	-0.014	45.016	0.001	0.001	0.000	0.000	0.000	0.000
35	A	561	CYS	0	-0.023	-0.009	48.257	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	562	PHE	0	0.026	-0.002	49.256	0.002	0.002	0.000	0.000	0.000	0.000
37	A	563	ARG	1	0.886	0.932	54.545	0.009	0.009	0.000	0.000	0.000	0.000
38	A	564	LYS	1	0.820	0.877	58.306	0.021	0.021	0.000	0.000	0.000	0.000
39	A	565	LEU	0	-0.032	-0.018	58.914	0.001	0.001	0.000	0.000	0.000	0.000
40	A	566	ASN	0	0.031	0.023	62.199	0.001	0.001	0.000	0.000	0.000	0.000
41	A	567	ALA	0	-0.005	0.011	63.639	0.000	0.000	0.000	0.000	0.000	0.000
42	A	568	ARG	1	0.866	0.918	65.502	0.013	0.013	0.000	0.000	0.000	0.000
43	A	569	ARG	1	0.911	0.950	65.344	0.016	0.016	0.000	0.000	0.000	0.000
44	A	570	ARG	1	0.945	0.968	69.229	0.011	0.011	0.000	0.000	0.000	0.000
45	A	571	GLN	0	-0.071	-0.048	64.781	0.000	0.000	0.000	0.000	0.000	0.000
46	A	572	ASP	-1	-0.813	-0.881	62.123	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	573	LYS	1	0.754	0.853	61.640	0.015	0.015	0.000	0.000	0.000	0.000
48	A	574	PHE	0	0.025	0.004	56.515	0.001	0.001	0.000	0.000	0.000	0.000
49	A	575	TRP	0	0.001	0.010	52.051	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	576	TYR	0	0.011	-0.008	46.384	0.002	0.002	0.000	0.000	0.000	0.000
51	A	577	CYS	0	-0.055	-0.008	48.131	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	578	ARG	1	0.794	0.866	42.433	0.040	0.040	0.000	0.000	0.000	0.000
53	A	579	LEU	0	-0.035	-0.005	38.139	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	580	SER	0	0.027	-0.002	40.081	0.002	0.002	0.000	0.000	0.000	0.000
55	A	581	PRO	0	0.078	0.029	38.318	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	582	ASN	0	-0.036	-0.006	35.704	0.000	0.000	0.000	0.000	0.000	0.000
57	A	583	HIS	1	0.866	0.913	32.919	0.063	0.063	0.000	0.000	0.000	0.000
58	A	584	LYS	1	0.986	0.998	34.305	0.104	0.104	0.000	0.000	0.000	0.000
59	A	585	VAL	0	0.002	0.007	39.072	0.000	0.000	0.000	0.000	0.000	0.000
60	A	586	LEU	0	0.023	0.023	42.784	0.001	0.001	0.000	0.000	0.000	0.000
61	A	587	HIS	0	-0.043	-0.042	44.750	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	588	TYR	0	0.056	-0.005	47.643	0.001	0.001	0.000	0.000	0.000	0.000
63	A	589	GLY	0	0.030	0.004	50.852	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	590	ASP	-1	-0.783	-0.869	54.432	-0.021	-0.021	0.000	0.000	0.000	0.000
65	A	591	LEU	0	-0.003	0.004	52.825	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	592	GLU	-1	-0.792	-0.880	57.404	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	593	GLU	-1	-0.841	-0.910	58.824	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	594	SER	0	-0.003	0.007	55.217	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	595	PRO	0	-0.004	0.009	51.416	0.000	0.000	0.000	0.000	0.000	0.000
70	A	596	GLN	0	-0.027	-0.029	52.065	0.001	0.001	0.000	0.000	0.000	0.000
71	A	597	GLY	0	0.008	-0.003	48.260	0.001	0.001	0.000	0.000	0.000	0.000
72	A	598	GLU	-1	-0.791	-0.872	44.044	-0.036	-0.036	0.000	0.000	0.000	0.000
73	A	599	VAL	0	0.006	0.005	46.993	0.001	0.001	0.000	0.000	0.000	0.000
74	A	600	PRO	0	-0.014	0.001	46.691	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	601	HIS	0	0.063	0.027	43.848	0.003	0.003	0.000	0.000	0.000	0.000
76	A	602	ASP	-1	-0.852	-0.935	45.888	-0.053	-0.053	0.000	0.000	0.000	0.000
77	A	603	SER	0	-0.076	-0.028	48.518	0.000	0.000	0.000	0.000	0.000	0.000
78	A	604	LEU	0	-0.066	-0.012	48.656	0.002	0.002	0.000	0.000	0.000	0.000
79	A	605	GLN	0	-0.078	-0.039	52.130	0.000	0.000	0.000	0.000	0.000	0.000
80	A	606	ASP	-1	-0.863	-0.913	52.935	-0.034	-0.034	0.000	0.000	0.000	0.000
81	A	607	LYS	1	0.876	0.922	47.478	0.050	0.050	0.000	0.000	0.000	0.000
82	A	608	LEU	0	-0.005	0.020	46.897	0.000	0.000	0.000	0.000	0.000	0.000
83	A	609	PRO	0	0.002	-0.002	43.920	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	610	VAL	0	0.011	-0.007	39.220	0.002	0.002	0.000	0.000	0.000	0.000
85	A	611	ALA	0	-0.050	-0.024	41.112	0.001	0.001	0.000	0.000	0.000	0.000
86	A	612	ASP	-1	-0.846	-0.918	42.231	-0.057	-0.057	0.000	0.000	0.000	0.000
87	A	613	ILE	0	-0.083	-0.043	43.146	0.004	0.004	0.000	0.000	0.000	0.000
88	A	614	LYS	1	0.795	0.907	44.183	0.037	0.037	0.000	0.000	0.000	0.000
89	A	615	ALA	0	-0.009	-0.008	45.423	0.000	0.000	0.000	0.000	0.000	0.000
90	A	616	VAL	0	0.008	0.007	44.509	0.000	0.000	0.000	0.000	0.000	0.000
91	A	617	VAL	0	-0.040	-0.012	46.991	0.001	0.001	0.000	0.000	0.000	0.000
92	A	618	THR	0	0.079	0.010	48.777	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	619	GLY	0	0.069	0.031	50.890	0.001	0.001	0.000	0.000	0.000	0.000
94	A	620	LYS	1	0.799	0.873	53.429	0.012	0.012	0.000	0.000	0.000	0.000
95	A	621	ASP	-1	-0.812	-0.891	52.607	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	622	CYS	0	-0.021	0.036	53.108	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	623	PRO	0	0.002	0.004	55.219	0.001	0.001	0.000	0.000	0.000	0.000
98	A	624	HIS	0	-0.025	-0.032	54.705	0.001	0.001	0.000	0.000	0.000	0.000
99	A	625	MET	0	-0.008	0.011	56.754	0.002	0.002	0.000	0.000	0.000	0.000
100	A	626	LYS	1	0.768	0.892	56.895	0.018	0.018	0.000	0.000	0.000	0.000
101	A	627	GLU	-1	-0.761	-0.880	62.105	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	628	LYS	1	0.773	0.889	60.895	0.006	0.006	0.000	0.000	0.000	0.000
103	A	629	GLY	0	0.103	0.064	64.719	0.001	0.001	0.000	0.000	0.000	0.000
104	A	630	ALA	0	0.016	0.012	65.782	0.001	0.001	0.000	0.000	0.000	0.000
105	A	631	LEU	0	-0.016	-0.007	65.705	0.000	0.000	0.000	0.000	0.000	0.000
106	A	632	LYS	1	0.949	0.962	64.988	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	633	GLN	0	-0.034	-0.022	63.982	0.001	0.001	0.000	0.000	0.000	0.000
108	A	634	ASN	0	0.014	-0.003	61.457	0.001	0.001	0.000	0.000	0.000	0.000
109	A	635	LYS	1	0.944	0.963	58.225	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	636	GLU	-1	-0.875	-0.930	57.277	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	637	VAL	0	0.013	0.007	56.601	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	638	LEU	0	-0.054	-0.040	56.139	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	639	GLU	-1	-0.972	-0.993	52.809	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	640	LEU	0	0.011	0.021	51.819	0.000	0.000	0.000	0.000	0.000	0.000
115	A	641	ALA	0	-0.019	0.006	52.796	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	642	PHE	0	0.023	-0.003	47.941	0.001	0.001	0.000	0.000	0.000	0.000
117	A	643	SER	0	-0.022	-0.036	50.477	0.001	0.001	0.000	0.000	0.000	0.000
118	A	644	ILE	0	0.019	0.026	46.195	0.000	0.000	0.000	0.000	0.000	0.000
119	A	645	LEU	0	-0.037	-0.021	48.717	0.001	0.001	0.000	0.000	0.000	0.000
120	A	646	TYR	0	0.051	0.007	48.629	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	647	ASP	-1	-0.794	-0.902	50.187	-0.041	-0.041	0.000	0.000	0.000	0.000
122	A	648	SER	0	0.012	0.017	52.025	0.000	0.000	0.000	0.000	0.000	0.000
123	A	649	ASN	0	-0.061	-0.053	54.518	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	650	CYS	0	0.023	0.051	53.771	0.002	0.002	0.000	0.000	0.000	0.000
125	A	651	GLN	0	-0.033	-0.034	53.285	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	652	LEU	0	0.007	0.030	49.748	0.001	0.001	0.000	0.000	0.000	0.000
127	A	653	ASN	0	0.020	0.006	52.091	0.000	0.000	0.000	0.000	0.000	0.000
128	A	654	PHE	0	0.057	0.027	49.297	0.000	0.000	0.000	0.000	0.000	0.000
129	A	655	ILE	0	-0.030	-0.027	53.625	0.001	0.001	0.000	0.000	0.000	0.000
130	A	656	ALA	0	-0.005	0.011	50.491	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	657	PRO	0	-0.004	0.000	51.321	0.001	0.001	0.000	0.000	0.000	0.000
132	A	658	ASP	-1	-0.769	-0.887	50.172	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	659	LYS	1	1.016	0.997	49.203	-0.007	-0.007	0.000	0.000	0.000	0.000
134	A	660	HIS	0	-0.020	-0.009	46.204	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	661	GLU	-1	-0.790	-0.886	45.638	-0.016	-0.016	0.000	0.000	0.000	0.000
136	A	662	TYR	0	-0.039	-0.016	46.660	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	663	CYS	0	-0.060	-0.018	43.221	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	664	ILE	0	-0.005	0.002	41.937	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	665	TRP	0	0.023	-0.010	41.878	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	666	THR	0	-0.025	-0.023	43.189	-0.003	-0.003	0.000	0.000	0.000	0.000
141	A	667	ASP	-1	-0.764	-0.839	37.585	-0.022	-0.022	0.000	0.000	0.000	0.000
142	A	668	GLY	0	0.032	0.020	38.436	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	669	LEU	0	0.005	-0.013	38.754	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	670	ASN	0	-0.059	-0.042	38.288	-0.004	-0.004	0.000	0.000	0.000	0.000
145	A	671	ALA	0	-0.090	-0.041	34.593	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	672	LEU	0	-0.042	-0.016	34.928	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	673	LEU	0	-0.075	-0.019	36.757	-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:527:GLY)