FMO DATABASE

FMODB ID: MVQLZ

Calculation Name: 2Z0U-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2Z0U

Chain ID: A

ChEMBL ID:

UniProt ID: Q8IX03

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1109193.583641
FMO2-HF: Nuclear repulsion	1057875.731147
FMO2-HF: Total energy	-51317.852495
FMO2-MP2: Total energy	-51465.539864

3D Structure Molmil

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:21:GLY)

Summations of interaction energy for fragment #1(A:21: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.
0.0049999999999998	1.272	0.034	-0.579	-0.722	0

Interaction energy analysis for fragmet #1(A:21:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : -0.008

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].
3	A	23	THR	0	0.006	0.008	3.855	2.445	3.381	-0.014	-0.447	-0.475
4	A	24	ARG	1	0.893	0.961	5.599	-2.301	-2.301	0.000	0.000	0.000
5	A	25	ILE	0	0.028	0.016	8.723	-0.138	-0.138	0.000	0.000	0.000
6	A	26	GLN	0	-0.003	0.008	12.450	0.049	0.049	0.000	0.000	0.000
7	A	27	ILE	0	0.024	0.002	14.712	-0.056	-0.056	0.000	0.000	0.000
8	A	28	ALA	0	-0.038	-0.021	17.909	0.014	0.014	0.000	0.000	0.000
9	A	29	LEU	0	-0.021	0.008	20.150	-0.017	-0.017	0.000	0.000	0.000
10	A	30	LYS	1	0.911	0.950	23.468	-0.088	-0.088	0.000	0.000	0.000
11	A	31	TYR	0	-0.028	-0.022	27.129	-0.006	-0.006	0.000	0.000	0.000
12	A	32	ASP	-1	-0.785	-0.881	30.377	0.064	0.064	0.000	0.000	0.000
13	A	33	GLU	-1	-0.756	-0.845	33.955	0.041	0.041	0.000	0.000	0.000
14	A	34	LYS	1	0.898	0.958	36.476	-0.057	-0.057	0.000	0.000	0.000
15	A	35	ASN	0	-0.038	-0.043	37.368	-0.006	-0.006	0.000	0.000	0.000
16	A	36	LYS	1	0.830	0.932	36.657	-0.040	-0.040	0.000	0.000	0.000
17	A	37	GLN	0	0.014	0.002	33.589	-0.004	-0.004	0.000	0.000	0.000
18	A	38	PHE	0	0.008	-0.014	24.370	0.004	0.004	0.000	0.000	0.000
19	A	39	ALA	0	0.009	0.013	27.931	-0.003	-0.003	0.000	0.000	0.000
20	A	40	ILE	0	0.010	-0.006	22.266	0.008	0.008	0.000	0.000	0.000
21	A	41	LEU	0	-0.012	0.005	22.179	-0.006	-0.006	0.000	0.000	0.000
22	A	42	ILE	0	0.035	0.006	18.298	0.027	0.027	0.000	0.000	0.000
23	A	43	ILE	0	-0.012	0.003	17.752	-0.006	-0.006	0.000	0.000	0.000
24	A	44	GLN	0	0.011	-0.013	14.250	-0.014	-0.014	0.000	0.000	0.000
25	A	45	LEU	0	0.024	0.023	12.475	0.038	0.038	0.000	0.000	0.000
26	A	46	SER	0	-0.023	-0.020	9.832	0.124	0.124	0.000	0.000	0.000
27	A	47	ASN	0	0.008	0.000	3.127	-0.319	0.012	0.048	-0.132	-0.247
28	A	48	LEU	0	0.003	0.010	7.165	-0.339	-0.339	0.000	0.000	0.000
29	A	49	SER	0	-0.018	-0.027	8.425	-0.197	-0.197	0.000	0.000	0.000
30	A	50	ALA	0	-0.040	-0.018	4.950	-0.162	-0.162	0.000	0.000	0.000
31	A	51	LEU	0	-0.053	-0.020	6.953	-0.171	-0.171	0.000	0.000	0.000
32	A	52	LEU	0	0.001	0.001	10.322	0.026	0.026	0.000	0.000	0.000
33	A	53	GLN	0	0.009	-0.004	9.984	0.126	0.126	0.000	0.000	0.000
34	A	54	GLN	0	-0.039	-0.013	13.048	0.024	0.024	0.000	0.000	0.000
35	A	55	GLN	0	-0.043	-0.038	13.139	0.049	0.049	0.000	0.000	0.000
36	A	56	ASP	-1	-0.927	-0.956	17.186	-0.012	-0.012	0.000	0.000	0.000
37	A	57	GLN	0	0.021	0.011	20.248	0.011	0.011	0.000	0.000	0.000
38	A	58	LYS	1	0.796	0.877	20.387	-0.036	-0.036	0.000	0.000	0.000
39	A	59	VAL	0	0.008	0.018	16.407	-0.018	-0.018	0.000	0.000	0.000
40	A	60	ASN	0	-0.054	-0.021	19.513	0.014	0.014	0.000	0.000	0.000
41	A	61	ILE	0	0.021	0.009	16.387	-0.003	-0.003	0.000	0.000	0.000
42	A	62	ARG	1	0.921	0.954	19.707	0.037	0.037	0.000	0.000	0.000
43	A	63	VAL	0	-0.008	-0.018	20.260	0.008	0.008	0.000	0.000	0.000
44	A	64	ALA	0	0.011	0.009	22.412	-0.008	-0.008	0.000	0.000	0.000
45	A	65	VAL	0	0.000	-0.002	23.647	0.003	0.003	0.000	0.000	0.000
46	A	66	LEU	0	0.003	0.021	23.414	-0.006	-0.006	0.000	0.000	0.000
47	A	67	PRO	0	0.046	-0.002	26.576	0.004	0.004	0.000	0.000	0.000
48	A	68	CYS	0	-0.092	-0.006	28.869	0.008	0.008	0.000	0.000	0.000
49	A	69	SER	0	0.019	0.003	30.588	-0.003	-0.003	0.000	0.000	0.000
50	A	70	GLU	-1	-0.803	-0.873	33.513	0.015	0.015	0.000	0.000	0.000
51	A	71	SER	0	0.017	-0.011	31.972	0.003	0.003	0.000	0.000	0.000
52	A	72	THR	0	-0.036	-0.040	32.101	0.002	0.002	0.000	0.000	0.000
53	A	73	THR	0	-0.017	-0.027	33.309	0.004	0.004	0.000	0.000	0.000
54	A	75	LEU	0	-0.023	-0.009	27.115	-0.002	-0.002	0.000	0.000	0.000
55	A	76	PHE	0	-0.004	-0.004	25.671	0.003	0.003	0.000	0.000	0.000
56	A	77	ARG	1	0.799	0.852	23.642	-0.014	-0.014	0.000	0.000	0.000
57	A	78	THR	0	-0.037	0.010	21.189	0.002	0.002	0.000	0.000	0.000
58	A	79	ARG	1	0.899	0.935	24.267	-0.086	-0.086	0.000	0.000	0.000
59	A	80	PRO	0	0.004	-0.006	23.472	0.008	0.008	0.000	0.000	0.000
60	A	81	LEU	0	-0.028	0.000	20.635	0.004	0.004	0.000	0.000	0.000
61	A	82	ASP	-1	-0.783	-0.887	21.307	0.048	0.048	0.000	0.000	0.000
62	A	83	ALA	0	0.005	0.011	16.600	0.022	0.022	0.000	0.000	0.000
63	A	84	SER	0	0.013	-0.002	15.643	-0.002	-0.002	0.000	0.000	0.000
64	A	85	ASP	-1	-0.787	-0.872	9.064	0.595	0.595	0.000	0.000	0.000
65	A	86	THR	0	-0.017	-0.017	11.126	0.172	0.172	0.000	0.000	0.000
66	A	87	LEU	0	-0.005	0.015	13.273	-0.061	-0.061	0.000	0.000	0.000
67	A	88	VAL	0	0.005	-0.003	16.400	0.018	0.018	0.000	0.000	0.000
68	A	89	PHE	0	0.000	-0.002	17.071	-0.027	-0.027	0.000	0.000	0.000
69	A	90	ASN	0	-0.039	-0.034	21.023	-0.003	-0.003	0.000	0.000	0.000
70	A	91	GLU	-1	-0.785	-0.871	22.975	0.077	0.077	0.000	0.000	0.000
71	A	92	VAL	0	-0.025	-0.029	23.877	0.012	0.012	0.000	0.000	0.000
72	A	93	PHE	0	-0.007	0.008	23.161	-0.011	-0.011	0.000	0.000	0.000
73	A	94	TRP	0	0.007	-0.014	27.761	0.007	0.007	0.000	0.000	0.000
74	A	95	VAL	0	0.019	0.011	29.173	-0.006	-0.006	0.000	0.000	0.000
75	A	96	SER	0	0.033	0.020	31.934	0.002	0.002	0.000	0.000	0.000
76	A	97	MET	0	-0.017	0.007	30.133	-0.002	-0.002	0.000	0.000	0.000
77	A	98	SER	0	0.032	0.027	35.052	0.003	0.003	0.000	0.000	0.000
78	A	99	TYR	0	0.049	0.003	30.164	-0.001	-0.001	0.000	0.000	0.000
79	A	100	PRO	0	0.023	-0.004	32.576	0.000	0.000	0.000	0.000	0.000
80	A	101	ALA	0	-0.005	0.006	33.359	-0.003	-0.003	0.000	0.000	0.000
81	A	102	LEU	0	0.000	-0.002	27.190	-0.002	-0.002	0.000	0.000	0.000
82	A	103	HIS	0	0.045	0.026	28.354	0.004	0.004	0.000	0.000	0.000
83	A	104	GLN	0	0.000	0.004	28.124	-0.003	-0.003	0.000	0.000	0.000
84	A	105	LYS	1	0.792	0.913	26.579	-0.022	-0.022	0.000	0.000	0.000
85	A	106	THR	0	-0.009	-0.011	20.844	0.003	0.003	0.000	0.000	0.000
86	A	107	LEU	0	-0.007	-0.002	19.738	-0.006	-0.006	0.000	0.000	0.000
87	A	108	ARG	1	0.861	0.922	16.287	0.081	0.081	0.000	0.000	0.000
88	A	109	VAL	0	-0.006	-0.012	15.465	0.015	0.015	0.000	0.000	0.000
89	A	110	ASP	-1	-0.743	-0.860	16.319	-0.067	-0.067	0.000	0.000	0.000
90	A	111	VAL	0	-0.011	0.005	12.763	0.032	0.032	0.000	0.000	0.000
91	A	112	CYS	0	-0.135	-0.087	16.122	-0.025	-0.025	0.000	0.000	0.000
92	A	113	THR	0	0.016	-0.002	18.076	0.022	0.022	0.000	0.000	0.000
93	A	114	THR	0	-0.001	-0.008	20.080	-0.007	-0.007	0.000	0.000	0.000
94	A	115	ASP	-1	-0.732	-0.840	23.637	-0.033	-0.033	0.000	0.000	0.000
95	A	116	ARG	1	0.938	0.960	24.887	0.029	0.029	0.000	0.000	0.000
96	A	117	SER	0	-0.087	-0.060	28.030	0.005	0.005	0.000	0.000	0.000
97	A	118	HIS	0	-0.070	-0.036	28.441	0.002	0.002	0.000	0.000	0.000
98	A	119	LEU	0	0.006	0.017	25.288	0.002	0.002	0.000	0.000	0.000
99	A	120	GLU	-1	-0.846	-0.895	22.661	-0.009	-0.009	0.000	0.000	0.000
100	A	121	GLU	-1	-0.914	-0.952	18.915	-0.160	-0.160	0.000	0.000	0.000
101	A	123	LEU	0	0.065	0.044	13.734	-0.016	-0.016	0.000	0.000	0.000
102	A	124	GLY	0	0.050	0.028	12.617	-0.097	-0.097	0.000	0.000	0.000
103	A	125	GLY	0	-0.021	-0.016	13.347	0.078	0.078	0.000	0.000	0.000
104	A	126	ALA	0	-0.044	-0.006	12.560	-0.045	-0.045	0.000	0.000	0.000
105	A	127	GLN	0	-0.008	-0.014	14.448	-0.002	-0.002	0.000	0.000	0.000
106	A	128	ILE	0	-0.010	0.010	15.651	-0.001	-0.001	0.000	0.000	0.000
107	A	129	SER	0	0.021	0.010	18.342	-0.006	-0.006	0.000	0.000	0.000
108	A	130	LEU	0	0.021	-0.002	21.403	0.018	0.018	0.000	0.000	0.000
109	A	131	ALA	0	0.000	0.013	24.066	0.003	0.003	0.000	0.000	0.000
110	A	132	GLU	-1	-0.845	-0.897	20.128	0.105	0.105	0.000	0.000	0.000
111	A	133	VAL	0	-0.067	-0.025	24.176	0.011	0.011	0.000	0.000	0.000
112	A	134	CYS	0	-0.002	-0.002	25.916	-0.009	-0.009	0.000	0.000	0.000
113	A	135	ARG	1	0.835	0.883	28.682	-0.045	-0.045	0.000	0.000	0.000
114	A	136	SER	0	-0.026	-0.050	31.659	-0.004	-0.004	0.000	0.000	0.000
115	A	137	GLY	0	-0.018	0.008	30.478	0.000	0.000	0.000	0.000	0.000
116	A	138	GLU	-1	-0.834	-0.907	27.241	0.090	0.090	0.000	0.000	0.000
117	A	139	ARG	1	0.903	0.961	22.659	-0.178	-0.178	0.000	0.000	0.000
118	A	140	SER	0	0.004	0.008	21.356	0.018	0.018	0.000	0.000	0.000
119	A	141	THR	0	-0.006	-0.020	18.393	-0.006	-0.006	0.000	0.000	0.000
120	A	142	ARG	1	0.805	0.887	15.253	-0.171	-0.171	0.000	0.000	0.000
121	A	143	TRP	0	0.028	0.010	10.448	0.083	0.083	0.000	0.000	0.000
122	A	144	TYR	0	0.020	0.003	10.800	-0.058	-0.058	0.000	0.000	0.000
123	A	145	ASN	0	0.010	0.000	5.592	0.754	0.754	0.000	0.000	0.000
124	A	146	LEU	0	-0.051	-0.016	8.136	-0.153	-0.153	0.000	0.000	0.000
125	A	147	LEU	0	-0.018	-0.012	7.375	-0.200	-0.200	0.000	0.000	0.000
126	A	148	SER	0	0.017	0.009	10.386	0.088	0.088	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:21:GLY)