FMO DATABASE

FMODB ID: LZQ99

Calculation Name: 5V3N-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5V3N

Chain ID: A

ChEMBL ID:

UniProt ID: P25651

Base Structure: X-ray

Registration Date: 2023-06-22

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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-887899.81562
FMO2-HF: Nuclear repulsion	843177.494788
FMO2-HF: Total energy	-44722.320832
FMO2-MP2: Total energy	-44854.334313

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:70:ASN)

Summations of interaction energy for fragment #1(A:70:ASN)

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.
-3.867	0.626	0.858	-1.743	-3.609	0.005

Interaction energy analysis for fragmet #1(A:70:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.041 / q_NPA : -0.002

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	72	GLU	-1	-0.786	-0.875	3.013	-1.671	0.536	0.005	-0.928	-1.285	0.002
4	A	73	VAL	0	0.035	0.026	3.153	-0.465	0.462	0.070	-0.227	-0.770	0.000
5	A	74	ILE	0	0.002	0.002	2.491	-1.446	-0.087	0.783	-0.588	-1.554	0.003
6	A	75	LYS	1	0.822	0.887	5.979	-0.329	-0.329	0.000	0.000	0.000	0.000
7	A	76	ASP	-1	-0.787	-0.866	7.839	0.487	0.487	0.000	0.000	0.000	0.000
8	A	77	LEU	0	-0.016	-0.004	8.528	-0.068	-0.068	0.000	0.000	0.000	0.000
9	A	78	TYR	0	-0.025	-0.023	8.918	-0.132	-0.132	0.000	0.000	0.000	0.000
10	A	79	GLU	-1	-0.854	-0.899	12.184	0.210	0.210	0.000	0.000	0.000	0.000
11	A	80	TYR	0	-0.059	-0.047	11.479	-0.058	-0.058	0.000	0.000	0.000	0.000
12	A	81	LEU	0	-0.066	-0.021	13.226	-0.043	-0.043	0.000	0.000	0.000	0.000
13	A	82	CYS	0	-0.044	-0.021	15.538	-0.056	-0.056	0.000	0.000	0.000	0.000
14	A	83	ASN	0	0.002	0.033	17.379	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	84	VAL	0	-0.017	-0.029	16.398	-0.039	-0.039	0.000	0.000	0.000	0.000
16	A	85	ARG	1	0.832	0.893	10.001	-0.264	-0.264	0.000	0.000	0.000	0.000
17	A	86	VAL	0	-0.003	0.005	14.287	-0.020	-0.020	0.000	0.000	0.000	0.000
18	A	87	HIS	0	-0.025	-0.025	13.618	0.005	0.005	0.000	0.000	0.000	0.000
19	A	88	LYS	1	0.905	0.949	14.140	0.012	0.012	0.000	0.000	0.000	0.000
20	A	89	SER	0	-0.028	-0.017	15.941	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	90	TYR	0	-0.058	-0.015	17.971	0.009	0.009	0.000	0.000	0.000	0.000
22	A	91	GLU	-1	-0.913	-0.954	20.746	-0.147	-0.147	0.000	0.000	0.000	0.000
23	A	92	ASP	-1	-0.839	-0.918	23.480	-0.052	-0.052	0.000	0.000	0.000	0.000
24	A	93	ASP	-1	-0.957	-0.974	27.062	-0.056	-0.056	0.000	0.000	0.000	0.000
25	A	94	SER	0	-0.058	-0.035	29.354	0.000	0.000	0.000	0.000	0.000	0.000
26	A	95	GLY	0	0.002	-0.013	27.296	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	96	LEU	0	-0.016	0.019	19.605	0.000	0.000	0.000	0.000	0.000	0.000
28	A	97	TRP	0	-0.019	-0.014	22.577	0.010	0.010	0.000	0.000	0.000	0.000
29	A	98	PHE	0	-0.017	-0.015	16.491	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	99	ASP	-1	-0.841	-0.903	19.170	0.005	0.005	0.000	0.000	0.000	0.000
31	A	100	ILE	0	-0.016	-0.014	18.386	0.003	0.003	0.000	0.000	0.000	0.000
32	A	101	SER	0	-0.002	-0.009	18.882	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	102	GLN	0	-0.005	0.016	19.457	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	103	GLY	0	0.016	-0.004	21.280	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	104	THR	0	-0.014	-0.006	21.171	0.025	0.025	0.000	0.000	0.000	0.000
36	A	105	HIS	0	0.065	0.027	20.205	-0.024	-0.024	0.000	0.000	0.000	0.000
37	A	106	SER	0	-0.080	-0.055	23.681	0.008	0.008	0.000	0.000	0.000	0.000
38	A	107	GLY	0	0.035	0.008	25.228	0.017	0.017	0.000	0.000	0.000	0.000
39	A	108	GLY	0	-0.051	0.003	27.752	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	109	SER	0	-0.029	-0.023	30.564	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	110	SER	0	0.035	0.002	27.679	0.004	0.004	0.000	0.000	0.000	0.000
42	A	111	ASP	-1	-0.907	-0.947	27.801	0.105	0.105	0.000	0.000	0.000	0.000
43	A	112	ASP	-1	-0.969	-0.960	29.907	0.108	0.108	0.000	0.000	0.000	0.000
44	A	113	TYR	0	-0.005	-0.018	25.322	0.013	0.013	0.000	0.000	0.000	0.000
45	A	114	SER	0	-0.054	-0.017	26.220	-0.016	-0.016	0.000	0.000	0.000	0.000
46	A	115	ILE	0	0.037	0.014	21.922	0.006	0.006	0.000	0.000	0.000	0.000
47	A	116	MET	0	-0.028	0.003	24.861	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	117	ASP	-1	-0.756	-0.843	23.042	0.077	0.077	0.000	0.000	0.000	0.000
49	A	118	TYR	0	-0.069	-0.077	22.967	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	119	LYS	1	0.850	0.916	23.270	0.013	0.013	0.000	0.000	0.000	0.000
51	A	120	LEU	0	-0.041	-0.025	22.082	0.003	0.003	0.000	0.000	0.000	0.000
52	A	121	GLY	0	0.068	0.028	23.736	-0.008	-0.008	0.000	0.000	0.000	0.000
53	A	122	PHE	0	-0.051	-0.028	21.760	0.000	0.000	0.000	0.000	0.000	0.000
54	A	123	VAL	0	0.057	0.023	26.111	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	124	LYS	1	0.850	0.927	28.148	0.113	0.113	0.000	0.000	0.000	0.000
56	A	125	GLY	0	0.075	0.048	31.453	0.006	0.006	0.000	0.000	0.000	0.000
57	A	126	GLN	0	0.012	-0.011	34.571	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	127	ALA	0	0.003	-0.008	35.975	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	128	GLN	0	-0.010	0.002	32.525	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	129	VAL	0	0.005	0.009	31.396	-0.012	-0.012	0.000	0.000	0.000	0.000
61	A	130	THR	0	-0.047	-0.029	25.826	0.003	0.003	0.000	0.000	0.000	0.000
62	A	131	GLU	-1	-0.894	-0.933	29.230	-0.057	-0.057	0.000	0.000	0.000	0.000
63	A	132	VAL	0	-0.014	-0.017	26.097	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	133	ILE	0	-0.005	0.001	28.320	0.008	0.008	0.000	0.000	0.000	0.000
65	A	134	TYR	0	-0.035	-0.028	27.131	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	135	ALA	0	0.065	0.022	28.087	0.002	0.002	0.000	0.000	0.000	0.000
67	A	136	PRO	0	0.016	0.027	28.074	0.002	0.002	0.000	0.000	0.000	0.000
68	A	137	VAL	0	-0.063	-0.043	25.724	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	138	LEU	0	0.043	0.003	28.270	0.006	0.006	0.000	0.000	0.000	0.000
70	A	139	LYS	1	0.878	0.943	30.826	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	140	GLN	0	0.005	-0.003	27.253	0.004	0.004	0.000	0.000	0.000	0.000
72	A	141	ARG	1	0.750	0.874	26.607	-0.068	-0.068	0.000	0.000	0.000	0.000
73	A	142	SER	0	0.034	0.005	31.187	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	143	THR	0	0.032	-0.010	34.049	0.001	0.001	0.000	0.000	0.000	0.000
75	A	144	GLU	-1	-0.919	-0.954	35.445	0.059	0.059	0.000	0.000	0.000	0.000
76	A	145	GLU	-1	-0.735	-0.824	28.838	0.075	0.075	0.000	0.000	0.000	0.000
77	A	146	LEU	0	0.000	-0.007	32.924	0.000	0.000	0.000	0.000	0.000	0.000
78	A	147	TYR	0	0.005	0.019	34.649	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	148	SER	0	0.021	0.011	32.913	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	149	LEU	0	0.013	0.003	29.018	0.000	0.000	0.000	0.000	0.000	0.000
81	A	150	GLN	0	-0.035	-0.029	33.126	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	151	SER	0	-0.089	-0.026	35.966	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	152	LYS	1	0.876	0.932	30.354	-0.089	-0.089	0.000	0.000	0.000	0.000
84	A	153	LEU	0	-0.030	-0.004	29.696	0.000	0.000	0.000	0.000	0.000	0.000
85	A	154	PRO	0	-0.031	-0.013	33.085	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	155	GLU	-1	-0.806	-0.920	35.463	0.013	0.013	0.000	0.000	0.000	0.000
87	A	156	TYR	0	0.048	0.017	32.957	0.001	0.001	0.000	0.000	0.000	0.000
88	A	157	LEU	0	-0.068	-0.028	30.138	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	158	PHE	0	-0.029	-0.006	32.292	0.003	0.003	0.000	0.000	0.000	0.000
90	A	159	GLU	-1	-0.939	-0.961	34.704	0.000	0.000	0.000	0.000	0.000	0.000
91	A	160	THR	0	-0.045	-0.028	32.436	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	161	LEU	0	-0.037	-0.007	32.370	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	162	SER	0	0.005	0.001	32.390	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	163	PHE	0	-0.017	-0.015	27.128	0.004	0.004	0.000	0.000	0.000	0.000
95	A	164	PRO	0	0.085	0.049	30.858	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	165	LEU	0	0.066	0.021	23.797	0.002	0.002	0.000	0.000	0.000	0.000
97	A	166	SER	0	-0.041	-0.022	26.310	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	167	SER	0	-0.016	-0.016	28.015	0.002	0.002	0.000	0.000	0.000	0.000
99	A	168	LEU	0	0.013	0.018	21.624	0.010	0.010	0.000	0.000	0.000	0.000
100	A	169	ASN	0	0.020	0.005	21.775	0.012	0.012	0.000	0.000	0.000	0.000
101	A	170	GLN	0	0.026	0.014	24.078	0.013	0.013	0.000	0.000	0.000	0.000
102	A	171	PHE	0	0.028	0.023	26.285	0.011	0.011	0.000	0.000	0.000	0.000
103	A	172	TYR	0	-0.011	-0.018	19.938	0.002	0.002	0.000	0.000	0.000	0.000
104	A	173	ASN	0	0.012	-0.014	24.071	0.022	0.022	0.000	0.000	0.000	0.000
105	A	174	LYS	1	0.891	0.963	25.906	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	175	ILE	0	0.055	0.041	25.751	0.007	0.007	0.000	0.000	0.000	0.000
107	A	176	ALA	0	0.020	0.015	23.737	0.009	0.009	0.000	0.000	0.000	0.000
108	A	177	LYS	1	0.926	0.954	25.519	-0.046	-0.046	0.000	0.000	0.000	0.000
109	A	178	SER	0	-0.068	-0.057	28.459	0.001	0.001	0.000	0.000	0.000	0.000
110	A	179	LEU	0	-0.016	-0.006	25.204	0.002	0.002	0.000	0.000	0.000	0.000
111	A	180	ASN	0	-0.033	-0.011	23.962	0.013	0.013	0.000	0.000	0.000	0.000
112	A	181	LYS	1	0.850	0.943	28.020	-0.047	-0.047	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:70:ASN)