FMO DATABASE

FMODB ID: R57G8

Calculation Name: 3VOQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3VOQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BPZ7

Base Structure: X-ray

Registration Date: 2023-06-20

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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-998723.600002
FMO2-HF: Nuclear repulsion	949927.982953
FMO2-HF: Total energy	-48795.617049
FMO2-MP2: Total energy	-48936.933849

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:369:GLY)

Summations of interaction energy for fragment #1(A:369: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.
-1.174	0.981	1.095	-1.338	-1.911	0

Interaction energy analysis for fragmet #1(A:369:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.053 / 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

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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	371	MET	0	0.044	0.009	3.863	-0.530	0.496	-0.003	-0.457	-0.565	0.002
4	A	372	ALA	0	-0.005	0.003	2.178	-1.001	-0.511	1.095	-0.626	-0.959	-0.002
5	A	373	THR	0	0.032	0.002	3.628	0.451	1.090	0.003	-0.255	-0.387	0.000
6	A	374	VAL	0	0.021	0.011	5.927	0.582	0.582	0.000	0.000	0.000	0.000
7	A	375	GLN	0	-0.017	-0.007	7.437	0.151	0.151	0.000	0.000	0.000	0.000
8	A	376	ASP	-1	-0.849	-0.918	7.797	-0.799	-0.799	0.000	0.000	0.000	0.000
9	A	377	MET	0	0.017	0.005	9.474	0.148	0.148	0.000	0.000	0.000	0.000
10	A	378	LEU	0	-0.061	-0.008	11.599	0.116	0.116	0.000	0.000	0.000	0.000
11	A	379	SER	0	-0.033	-0.027	12.246	0.081	0.081	0.000	0.000	0.000	0.000
12	A	380	SER	0	-0.011	0.002	13.957	0.050	0.050	0.000	0.000	0.000	0.000
13	A	381	HIS	0	0.049	0.034	15.147	0.050	0.050	0.000	0.000	0.000	0.000
14	A	382	HIS	0	0.018	0.031	16.022	0.025	0.025	0.000	0.000	0.000	0.000
15	A	383	TYR	0	0.017	0.009	18.728	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	384	LYS	1	0.796	0.891	13.959	0.344	0.344	0.000	0.000	0.000	0.000
17	A	385	SER	0	-0.050	-0.017	19.536	0.000	0.000	0.000	0.000	0.000	0.000
18	A	386	PHE	0	0.034	0.021	16.040	0.002	0.002	0.000	0.000	0.000	0.000
19	A	387	LYS	1	0.847	0.910	21.314	0.122	0.122	0.000	0.000	0.000	0.000
20	A	388	VAL	0	0.048	0.039	22.054	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	389	SER	0	0.022	-0.002	24.770	0.011	0.011	0.000	0.000	0.000	0.000
22	A	390	MET	0	-0.017	0.004	27.732	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	391	ILE	0	0.031	0.008	28.299	0.011	0.011	0.000	0.000	0.000	0.000
24	A	392	HIS	1	0.834	0.903	31.672	0.086	0.086	0.000	0.000	0.000	0.000
25	A	393	ARG	1	0.941	0.944	35.331	0.068	0.068	0.000	0.000	0.000	0.000
26	A	394	LEU	0	0.043	0.031	32.325	0.005	0.005	0.000	0.000	0.000	0.000
27	A	395	ARG	1	0.922	0.964	35.054	0.068	0.068	0.000	0.000	0.000	0.000
28	A	396	PHE	0	0.006	0.014	35.485	0.002	0.002	0.000	0.000	0.000	0.000
29	A	397	THR	0	0.055	0.028	30.194	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	398	THR	0	-0.044	-0.018	32.376	0.008	0.008	0.000	0.000	0.000	0.000
31	A	399	ASP	-1	-0.857	-0.899	29.264	-0.097	-0.097	0.000	0.000	0.000	0.000
32	A	400	VAL	0	-0.063	-0.040	27.123	0.009	0.009	0.000	0.000	0.000	0.000
33	A	401	GLN	0	-0.021	-0.006	25.576	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	402	LEU	0	0.014	0.012	22.692	0.008	0.008	0.000	0.000	0.000	0.000
35	A	403	GLY	0	0.008	-0.010	23.060	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	404	ILE	0	-0.001	-0.007	19.696	0.005	0.005	0.000	0.000	0.000	0.000
37	A	405	SER	0	-0.029	-0.053	20.686	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	406	GLY	0	0.062	0.023	21.850	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	407	ASP	-1	-0.865	-0.878	22.847	-0.117	-0.117	0.000	0.000	0.000	0.000
40	A	408	LYS	1	0.808	0.895	25.437	0.105	0.105	0.000	0.000	0.000	0.000
41	A	409	VAL	0	0.016	0.015	23.742	-0.014	-0.014	0.000	0.000	0.000	0.000
42	A	410	GLU	-1	-0.828	-0.871	26.235	-0.081	-0.081	0.000	0.000	0.000	0.000
43	A	411	ILE	0	-0.001	-0.003	27.036	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	412	ASP	-1	-0.845	-0.909	29.360	-0.081	-0.081	0.000	0.000	0.000	0.000
45	A	413	PRO	0	-0.072	-0.043	30.740	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	414	VAL	0	0.018	0.013	29.667	0.004	0.004	0.000	0.000	0.000	0.000
47	A	415	THR	0	-0.020	-0.022	32.296	0.003	0.003	0.000	0.000	0.000	0.000
48	A	416	ASN	0	0.055	0.037	34.031	0.004	0.004	0.000	0.000	0.000	0.000
49	A	417	GLN	0	0.064	0.034	36.066	0.002	0.002	0.000	0.000	0.000	0.000
50	A	418	LYS	1	0.837	0.907	38.340	0.051	0.051	0.000	0.000	0.000	0.000
51	A	419	ALA	0	0.025	0.017	41.711	0.002	0.002	0.000	0.000	0.000	0.000
52	A	420	SER	0	0.001	0.004	44.756	0.002	0.002	0.000	0.000	0.000	0.000
53	A	421	THR	0	0.029	0.009	44.596	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	422	LYS	1	0.939	0.981	46.764	0.031	0.031	0.000	0.000	0.000	0.000
55	A	423	PHE	0	0.040	-0.001	48.845	0.001	0.001	0.000	0.000	0.000	0.000
56	A	424	TRP	0	0.054	0.038	38.715	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	425	ILE	0	0.038	0.016	42.025	0.000	0.000	0.000	0.000	0.000	0.000
58	A	426	LYS	1	0.933	0.976	40.528	0.051	0.051	0.000	0.000	0.000	0.000
59	A	427	GLN	0	-0.025	-0.006	36.500	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	428	LYS	1	0.851	0.906	37.514	0.065	0.065	0.000	0.000	0.000	0.000
61	A	429	PRO	0	0.066	0.029	33.892	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	430	ILE	0	-0.050	-0.011	32.008	0.005	0.005	0.000	0.000	0.000	0.000
63	A	431	SER	0	-0.042	-0.059	31.201	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	432	ILE	0	-0.044	-0.019	28.947	0.006	0.006	0.000	0.000	0.000	0.000
65	A	433	ASP	-1	-0.825	-0.908	29.116	-0.110	-0.110	0.000	0.000	0.000	0.000
66	A	434	SER	0	0.029	-0.012	25.444	0.000	0.000	0.000	0.000	0.000	0.000
67	A	435	ASP	-1	-0.818	-0.905	27.129	-0.139	-0.139	0.000	0.000	0.000	0.000
68	A	436	LEU	0	-0.112	-0.042	29.498	0.005	0.005	0.000	0.000	0.000	0.000
69	A	437	LEU	0	-0.041	-0.005	24.612	0.002	0.002	0.000	0.000	0.000	0.000
70	A	438	CYS	0	-0.046	-0.023	27.751	0.002	0.002	0.000	0.000	0.000	0.000
71	A	439	ALA	0	0.028	0.014	24.717	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	440	CYS	0	0.008	0.008	21.004	0.010	0.010	0.000	0.000	0.000	0.000
73	A	441	ASP	-1	-0.806	-0.882	21.117	-0.204	-0.204	0.000	0.000	0.000	0.000
74	A	442	LEU	0	0.015	0.005	17.730	0.013	0.013	0.000	0.000	0.000	0.000
75	A	443	ALA	0	-0.056	-0.029	21.141	0.010	0.010	0.000	0.000	0.000	0.000
76	A	444	GLU	-1	-0.921	-0.976	23.688	-0.113	-0.113	0.000	0.000	0.000	0.000
77	A	445	GLU	-1	-0.875	-0.947	17.141	-0.290	-0.290	0.000	0.000	0.000	0.000
78	A	446	LYS	1	0.893	0.975	21.654	0.119	0.119	0.000	0.000	0.000	0.000
79	A	447	SER	0	-0.015	-0.021	21.968	0.010	0.010	0.000	0.000	0.000	0.000
80	A	448	PRO	0	0.072	0.021	17.640	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	449	SER	0	-0.041	-0.015	19.120	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	450	HIS	0	-0.026	-0.008	21.933	0.011	0.011	0.000	0.000	0.000	0.000
83	A	451	ALA	0	0.041	0.038	19.836	0.001	0.001	0.000	0.000	0.000	0.000
84	A	452	ILE	0	0.005	-0.008	21.835	0.007	0.007	0.000	0.000	0.000	0.000
85	A	453	PHE	0	0.025	0.009	21.431	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	454	LYS	1	0.827	0.903	23.550	0.165	0.165	0.000	0.000	0.000	0.000
87	A	455	LEU	0	0.037	0.021	24.027	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	456	THR	0	-0.039	-0.033	26.385	0.012	0.012	0.000	0.000	0.000	0.000
89	A	457	TYR	0	0.031	0.011	28.344	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	458	LEU	0	0.032	0.025	30.876	0.007	0.007	0.000	0.000	0.000	0.000
91	A	459	SER	0	-0.008	-0.016	34.237	0.002	0.002	0.000	0.000	0.000	0.000
92	A	460	ASN	0	-0.028	-0.030	36.913	0.003	0.003	0.000	0.000	0.000	0.000
93	A	461	HIS	0	0.035	0.011	39.274	0.001	0.001	0.000	0.000	0.000	0.000
94	A	462	ASP	-1	-0.851	-0.895	38.796	-0.070	-0.070	0.000	0.000	0.000	0.000
95	A	463	TYR	0	0.016	-0.003	33.259	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	464	LYS	1	0.769	0.892	34.335	0.080	0.080	0.000	0.000	0.000	0.000
97	A	465	HIS	0	0.052	0.022	31.010	-0.013	-0.013	0.000	0.000	0.000	0.000
98	A	466	LEU	0	-0.072	-0.022	28.952	0.009	0.009	0.000	0.000	0.000	0.000
99	A	467	TYR	0	0.035	0.009	27.760	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	468	PHE	0	-0.010	-0.008	24.823	0.013	0.013	0.000	0.000	0.000	0.000
101	A	469	GLU	-1	-0.912	-0.951	24.103	-0.124	-0.124	0.000	0.000	0.000	0.000
102	A	470	SER	0	-0.001	-0.021	20.373	0.012	0.012	0.000	0.000	0.000	0.000
103	A	471	ASP	-1	-0.789	-0.845	17.247	-0.240	-0.240	0.000	0.000	0.000	0.000
104	A	472	ALA	0	0.057	0.012	16.528	-0.012	-0.012	0.000	0.000	0.000	0.000
105	A	473	ALA	0	-0.019	0.012	13.059	-0.038	-0.038	0.000	0.000	0.000	0.000
106	A	474	THR	0	-0.036	-0.051	14.339	-0.051	-0.051	0.000	0.000	0.000	0.000
107	A	475	VAL	0	-0.047	-0.016	16.623	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	476	ASN	0	-0.045	-0.042	13.275	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	477	GLU	-1	-0.785	-0.865	11.841	-0.448	-0.448	0.000	0.000	0.000	0.000
110	A	478	ILE	0	-0.030	-0.011	13.900	0.009	0.009	0.000	0.000	0.000	0.000
111	A	479	VAL	0	-0.008	-0.020	16.987	0.012	0.012	0.000	0.000	0.000	0.000
112	A	480	LEU	0	-0.004	0.018	10.101	0.027	0.027	0.000	0.000	0.000	0.000
113	A	481	LYS	1	0.825	0.893	14.709	0.318	0.318	0.000	0.000	0.000	0.000
114	A	482	VAL	0	0.012	-0.013	16.018	0.030	0.030	0.000	0.000	0.000	0.000
115	A	483	ASN	0	-0.066	-0.049	17.106	0.042	0.042	0.000	0.000	0.000	0.000
116	A	484	TYR	0	0.011	-0.013	10.189	0.016	0.016	0.000	0.000	0.000	0.000
117	A	485	ILE	0	-0.069	-0.032	17.196	0.028	0.028	0.000	0.000	0.000	0.000
118	A	486	LEU	0	-0.080	-0.031	20.655	0.026	0.026	0.000	0.000	0.000	0.000
119	A	487	GLU	-1	-0.960	-0.981	16.469	-0.365	-0.365	0.000	0.000	0.000	0.000
120	A	488	SER	0	-0.052	-0.038	20.231	0.017	0.017	0.000	0.000	0.000	0.000
121	A	489	ARG	1	0.817	0.916	21.617	0.172	0.172	0.000	0.000	0.000	0.000
122	A	490	ALA	0	-0.046	-0.026	24.078	0.014	0.014	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:369:GLY)