FMO DATABASE

FMODB ID: JQ689

Calculation Name: 2ZKZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2ZKZ

Chain ID: A

ChEMBL ID:

UniProt ID: O31178

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	OptH
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	86
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-621837.522645
FMO2-HF: Nuclear repulsion	586429.908294
FMO2-HF: Total energy	-35407.614352
FMO2-MP2: Total energy	-35509.350657

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:11:TYR)

Summations of interaction energy for fragment #1(A:11:TYR)

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.
-8.175	-4.237	1.639	-1.71	-3.866	-0.004

Interaction energy analysis for fragmet #1(A:11:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : -0.022

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	13	SER	0	0.039	0.028	3.172	-2.508	1.080	1.640	-1.686	-3.542	-0.004
4	A	14	LEU	0	0.083	0.038	4.577	-0.353	-0.131	0.000	-0.016	-0.206	0.000
5	A	15	GLU	-1	-0.882	-0.956	6.406	-0.722	-0.722	0.000	0.000	0.000	0.000
6	A	16	ASP	-1	-0.870	-0.932	6.600	-1.273	-1.273	0.000	0.000	0.000	0.000
7	A	17	ASP	-1	-0.900	-0.961	5.491	-1.473	-1.473	0.000	0.000	0.000	0.000
8	A	18	ALA	0	-0.013	-0.009	8.833	0.172	0.172	0.000	0.000	0.000	0.000
9	A	19	GLU	-1	-0.814	-0.892	11.695	-0.107	-0.107	0.000	0.000	0.000	0.000
10	A	20	LEU	0	-0.038	-0.012	9.703	0.118	0.118	0.000	0.000	0.000	0.000
11	A	21	LEU	0	0.019	0.000	12.434	0.084	0.084	0.000	0.000	0.000	0.000
12	A	22	LYS	1	0.945	0.981	15.018	0.241	0.241	0.000	0.000	0.000	0.000
13	A	23	THR	0	-0.115	-0.063	15.792	0.037	0.037	0.000	0.000	0.000	0.000
14	A	24	MET	0	0.017	0.000	15.408	0.049	0.049	0.000	0.000	0.000	0.000
15	A	25	ALA	0	-0.007	0.032	18.490	0.012	0.012	0.000	0.000	0.000	0.000
16	A	26	HIS	0	-0.007	-0.019	20.957	0.002	0.002	0.000	0.000	0.000	0.000
17	A	27	PRO	0	0.083	0.037	23.958	0.018	0.018	0.000	0.000	0.000	0.000
18	A	28	MET	0	0.009	0.000	26.044	0.015	0.015	0.000	0.000	0.000	0.000
19	A	29	ARG	1	0.871	0.920	20.768	0.027	0.027	0.000	0.000	0.000	0.000
20	A	30	LEU	0	0.077	0.040	20.226	0.030	0.030	0.000	0.000	0.000	0.000
21	A	31	LYS	1	0.952	0.975	22.613	-0.037	-0.037	0.000	0.000	0.000	0.000
22	A	32	ILE	0	-0.023	-0.007	22.167	0.013	0.013	0.000	0.000	0.000	0.000
23	A	33	VAL	0	0.026	0.012	18.009	0.023	0.023	0.000	0.000	0.000	0.000
24	A	34	ASN	0	0.067	0.023	20.824	0.037	0.037	0.000	0.000	0.000	0.000
25	A	35	GLU	-1	-0.872	-0.956	23.053	0.121	0.121	0.000	0.000	0.000	0.000
26	A	36	LEU	0	-0.011	-0.001	20.364	0.009	0.009	0.000	0.000	0.000	0.000
27	A	37	TYR	0	-0.009	0.013	19.697	0.033	0.033	0.000	0.000	0.000	0.000
28	A	38	LYS	1	0.869	0.930	21.453	-0.103	-0.103	0.000	0.000	0.000	0.000
29	A	39	HIS	0	0.007	0.001	25.121	0.005	0.005	0.000	0.000	0.000	0.000
30	A	40	LYS	1	0.866	0.955	20.503	-0.309	-0.309	0.000	0.000	0.000	0.000
31	A	41	ALA	0	-0.040	-0.032	21.869	0.035	0.035	0.000	0.000	0.000	0.000
32	A	42	LEU	0	-0.014	0.004	24.191	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	43	ASN	0	0.020	0.018	25.113	0.001	0.001	0.000	0.000	0.000	0.000
34	A	44	VAL	0	0.049	-0.008	26.625	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	45	THR	0	0.027	0.016	28.509	-0.007	-0.007	0.000	0.000	0.000	0.000
36	A	46	GLN	0	0.095	0.055	29.335	0.000	0.000	0.000	0.000	0.000	0.000
37	A	47	ILE	0	0.008	0.011	24.903	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	48	ILE	0	-0.034	-0.015	29.265	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	49	GLN	0	-0.003	0.000	32.069	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	50	ILE	0	-0.003	0.014	29.193	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	51	LEU	0	-0.103	-0.069	27.490	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	52	LYS	1	0.870	0.954	31.815	-0.063	-0.063	0.000	0.000	0.000	0.000
43	A	53	LEU	0	0.000	0.004	30.407	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	54	PRO	0	0.072	0.029	34.157	0.005	0.005	0.000	0.000	0.000	0.000
45	A	55	GLN	0	0.086	0.027	31.706	0.005	0.005	0.000	0.000	0.000	0.000
46	A	56	SER	0	-0.016	0.000	30.964	0.004	0.004	0.000	0.000	0.000	0.000
47	A	57	THR	0	0.057	0.021	29.912	0.000	0.000	0.000	0.000	0.000	0.000
48	A	58	VAL	0	0.010	0.006	27.468	0.000	0.000	0.000	0.000	0.000	0.000
49	A	59	SER	0	0.007	-0.009	26.366	0.012	0.012	0.000	0.000	0.000	0.000
50	A	60	GLN	0	-0.002	0.013	25.412	0.009	0.009	0.000	0.000	0.000	0.000
51	A	61	HIS	0	0.034	0.020	23.886	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	62	LEU	0	0.010	0.005	21.874	0.007	0.007	0.000	0.000	0.000	0.000
53	A	63	CYS	0	-0.115	-0.051	20.644	0.016	0.016	0.000	0.000	0.000	0.000
54	A	64	LYS	1	0.960	0.977	19.936	0.056	0.056	0.000	0.000	0.000	0.000
55	A	65	MET	0	0.046	0.033	17.539	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	66	ARG	1	0.923	0.970	16.154	-0.061	-0.061	0.000	0.000	0.000	0.000
57	A	67	GLY	0	-0.052	-0.019	13.300	-0.050	-0.050	0.000	0.000	0.000	0.000
58	A	68	LYS	1	0.845	0.919	11.463	0.164	0.164	0.000	0.000	0.000	0.000
59	A	69	VAL	0	0.019	0.003	11.800	0.097	0.097	0.000	0.000	0.000	0.000
60	A	70	LEU	0	-0.010	-0.010	14.404	0.063	0.063	0.000	0.000	0.000	0.000
61	A	71	LYS	1	0.955	0.995	13.726	-0.563	-0.563	0.000	0.000	0.000	0.000
62	A	72	ARG	1	0.936	0.962	16.055	-0.199	-0.199	0.000	0.000	0.000	0.000
63	A	73	ASN	0	-0.075	-0.039	18.582	0.058	0.058	0.000	0.000	0.000	0.000
64	A	74	ARG	1	0.924	0.962	20.863	-0.167	-0.167	0.000	0.000	0.000	0.000
65	A	75	GLN	0	0.021	0.020	24.016	0.030	0.030	0.000	0.000	0.000	0.000
66	A	76	GLY	0	0.055	0.038	26.748	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	77	LEU	0	0.048	-0.003	29.229	0.001	0.001	0.000	0.000	0.000	0.000
68	A	78	GLU	-1	-0.875	-0.929	27.709	0.155	0.155	0.000	0.000	0.000	0.000
69	A	79	ILE	0	-0.051	-0.022	23.666	0.013	0.013	0.000	0.000	0.000	0.000
70	A	80	TYR	0	0.024	-0.003	22.029	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	81	TYR	0	-0.022	-0.035	19.709	0.017	0.017	0.000	0.000	0.000	0.000
72	A	82	SER	0	0.089	0.045	18.172	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	83	ILE	0	0.022	0.014	14.523	0.003	0.003	0.000	0.000	0.000	0.000
74	A	84	ASN	0	0.014	-0.008	10.855	-0.075	-0.075	0.000	0.000	0.000	0.000
75	A	85	ASN	0	0.037	0.030	7.986	0.372	0.372	0.000	0.000	0.000	0.000
76	A	86	PRO	0	0.086	0.022	8.078	-0.266	-0.266	0.000	0.000	0.000	0.000
77	A	87	LYS	1	0.941	0.964	4.430	-1.622	-1.494	-0.001	-0.008	-0.118	0.000
78	A	88	VAL	0	-0.006	0.008	10.350	-0.199	-0.199	0.000	0.000	0.000	0.000
79	A	89	GLU	-1	-0.961	-0.977	13.297	0.409	0.409	0.000	0.000	0.000	0.000
80	A	90	GLY	0	0.014	-0.005	13.582	-0.076	-0.076	0.000	0.000	0.000	0.000
81	A	91	ILE	0	0.017	-0.001	12.267	-0.072	-0.072	0.000	0.000	0.000	0.000
82	A	92	ILE	0	-0.033	-0.018	15.779	-0.036	-0.036	0.000	0.000	0.000	0.000
83	A	93	LYS	1	0.892	0.946	18.245	-0.251	-0.251	0.000	0.000	0.000	0.000
84	A	94	LEU	0	-0.009	-0.004	16.172	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	95	LEU	0	-0.041	-0.003	19.114	-0.020	-0.020	0.000	0.000	0.000	0.000
86	A	96	ASN	0	-0.049	0.004	21.523	-0.018	-0.018	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:TYR)