FMO DATABASE

FMODB ID: LZKQ9

Calculation Name: 2PZH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PZH

Chain ID: A

ChEMBL ID:

UniProt ID: P94842

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	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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1236923.804108
FMO2-HF: Nuclear repulsion	1182043.836692
FMO2-HF: Total energy	-54879.967416
FMO2-MP2: Total energy	-55040.519824

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:-1:THR)

Summations of interaction energy for fragment #1(A:-1:THR)

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.
1.648	2.766	-0.007	-0.584	-0.527	0.003

Interaction energy analysis for fragmet #1(A:-1:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.013 / q_NPA : -0.021

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	1	MET	0	-0.001	0.029	3.820	0.958	2.076	-0.007	-0.584	-0.527	0.003
4	A	2	ARG	1	0.943	0.969	5.835	1.997	1.997	0.000	0.000	0.000	0.000
5	A	3	CYS	0	-0.005	0.013	9.054	0.316	0.316	0.000	0.000	0.000	0.000
6	A	4	ARG	1	0.885	0.949	12.802	0.460	0.460	0.000	0.000	0.000	0.000
7	A	5	VAL	0	-0.005	0.020	15.618	0.051	0.051	0.000	0.000	0.000	0.000
8	A	6	TYR	0	0.043	0.010	17.082	-0.017	-0.017	0.000	0.000	0.000	0.000
9	A	7	TYR	0	0.083	0.013	21.655	0.002	0.002	0.000	0.000	0.000	0.000
10	A	8	GLU	-1	-0.966	-0.966	22.229	-0.139	-0.139	0.000	0.000	0.000	0.000
11	A	9	ASP	-1	-0.843	-0.915	19.826	-0.242	-0.242	0.000	0.000	0.000	0.000
12	A	10	THR	0	-0.083	-0.045	23.335	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	11	ASP	-1	-0.802	-0.918	25.536	-0.138	-0.138	0.000	0.000	0.000	0.000
14	A	12	SER	0	-0.012	-0.012	28.756	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-1.006	-0.991	29.025	-0.154	-0.154	0.000	0.000	0.000	0.000
16	A	14	GLY	0	-0.026	-0.009	28.301	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	15	VAL	0	-0.036	-0.021	24.081	-0.029	-0.029	0.000	0.000	0.000	0.000
18	A	16	VAL	0	-0.054	-0.028	19.630	0.013	0.013	0.000	0.000	0.000	0.000
19	A	17	TYR	0	0.034	0.028	22.882	0.011	0.011	0.000	0.000	0.000	0.000
20	A	18	HIS	0	0.033	0.007	23.148	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	19	ALA	0	0.024	0.000	22.104	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	20	ASN	0	-0.006	0.002	20.741	0.034	0.034	0.000	0.000	0.000	0.000
23	A	21	TYR	0	0.058	0.033	17.139	-0.028	-0.028	0.000	0.000	0.000	0.000
24	A	22	LEU	0	0.023	0.006	16.701	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	23	LYS	1	0.910	0.959	17.775	0.128	0.128	0.000	0.000	0.000	0.000
26	A	24	TYR	0	-0.040	-0.043	13.963	0.011	0.011	0.000	0.000	0.000	0.000
27	A	25	CYS	0	-0.022	-0.012	13.087	-0.027	-0.027	0.000	0.000	0.000	0.000
28	A	26	GLU	-1	-0.784	-0.872	13.553	0.200	0.200	0.000	0.000	0.000	0.000
29	A	27	ARG	1	0.946	0.967	13.428	0.246	0.246	0.000	0.000	0.000	0.000
30	A	28	ALA	0	-0.009	-0.011	9.315	0.105	0.105	0.000	0.000	0.000	0.000
31	A	29	ARG	1	0.807	0.903	9.850	0.132	0.132	0.000	0.000	0.000	0.000
32	A	30	SER	0	0.027	-0.016	12.279	0.133	0.133	0.000	0.000	0.000	0.000
33	A	31	GLU	-1	-0.833	-0.897	8.922	0.886	0.886	0.000	0.000	0.000	0.000
34	A	32	PHE	0	-0.044	-0.023	5.277	0.235	0.235	0.000	0.000	0.000	0.000
35	A	33	PHE	0	-0.029	-0.008	9.767	0.081	0.081	0.000	0.000	0.000	0.000
36	A	34	PHE	0	0.035	0.014	12.899	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.828	0.897	5.685	-1.879	-1.879	0.000	0.000	0.000	0.000
38	A	36	GLN	0	-0.074	-0.025	9.634	-0.075	-0.075	0.000	0.000	0.000	0.000
39	A	37	ASN	0	-0.063	-0.031	13.399	-0.128	-0.128	0.000	0.000	0.000	0.000
40	A	38	VAL	0	-0.007	0.007	15.854	-0.084	-0.084	0.000	0.000	0.000	0.000
41	A	39	LEU	0	0.064	0.024	16.605	0.029	0.029	0.000	0.000	0.000	0.000
42	A	40	PRO	0	-0.023	0.000	16.494	0.018	0.018	0.000	0.000	0.000	0.000
43	A	41	GLU	-1	-0.923	-0.962	18.372	0.139	0.139	0.000	0.000	0.000	0.000
44	A	42	ASN	0	-0.014	-0.037	22.109	0.020	0.020	0.000	0.000	0.000	0.000
45	A	43	GLU	-1	-0.808	-0.897	24.613	0.191	0.191	0.000	0.000	0.000	0.000
46	A	44	GLU	-1	-0.917	-0.952	28.147	0.112	0.112	0.000	0.000	0.000	0.000
47	A	45	GLY	0	-0.038	-0.022	26.764	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	46	VAL	0	0.013	0.016	23.724	0.013	0.013	0.000	0.000	0.000	0.000
49	A	47	PHE	0	0.009	0.005	18.626	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	48	VAL	0	-0.022	-0.007	22.587	-0.015	-0.015	0.000	0.000	0.000	0.000
51	A	49	ILE	0	0.013	0.004	21.225	0.006	0.006	0.000	0.000	0.000	0.000
52	A	50	ARG	1	0.868	0.940	23.627	-0.097	-0.097	0.000	0.000	0.000	0.000
53	A	51	SER	0	0.035	0.006	23.871	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	52	ILE	0	0.003	-0.001	19.810	0.008	0.008	0.000	0.000	0.000	0.000
55	A	53	LYS	1	0.818	0.921	21.175	0.089	0.089	0.000	0.000	0.000	0.000
56	A	54	ALA	0	0.021	-0.009	19.964	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	55	ASP	-1	-0.859	-0.899	19.735	-0.103	-0.103	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.027	-0.001	19.560	-0.027	-0.027	0.000	0.000	0.000	0.000
59	A	57	PHE	0	-0.011	-0.014	18.187	0.012	0.012	0.000	0.000	0.000	0.000
60	A	58	THR	0	-0.001	0.002	19.512	0.026	0.026	0.000	0.000	0.000	0.000
61	A	59	PRO	0	0.043	0.032	19.647	-0.038	-0.038	0.000	0.000	0.000	0.000
62	A	60	ALA	0	-0.001	0.002	17.952	-0.021	-0.021	0.000	0.000	0.000	0.000
63	A	61	SER	0	0.043	0.006	20.002	0.042	0.042	0.000	0.000	0.000	0.000
64	A	62	LEU	0	0.041	0.010	20.759	-0.041	-0.041	0.000	0.000	0.000	0.000
65	A	63	GLY	0	0.003	0.001	20.219	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	64	GLN	0	0.042	0.033	17.023	-0.068	-0.068	0.000	0.000	0.000	0.000
67	A	65	VAL	0	-0.027	-0.007	11.384	0.013	0.013	0.000	0.000	0.000	0.000
68	A	66	LEU	0	0.006	-0.002	12.586	-0.058	-0.058	0.000	0.000	0.000	0.000
69	A	67	GLU	-1	-0.821	-0.912	5.804	-3.531	-3.531	0.000	0.000	0.000	0.000
70	A	68	ILE	0	-0.025	-0.017	8.223	0.215	0.215	0.000	0.000	0.000	0.000
71	A	69	ARG	1	0.801	0.893	5.383	1.467	1.467	0.000	0.000	0.000	0.000
72	A	70	THR	0	0.032	0.006	6.359	0.266	0.266	0.000	0.000	0.000	0.000
73	A	71	GLN	0	-0.007	0.005	7.556	0.162	0.162	0.000	0.000	0.000	0.000
74	A	72	ILE	0	0.033	0.012	10.119	-0.066	-0.066	0.000	0.000	0.000	0.000
75	A	73	LYS	1	0.814	0.904	13.329	-0.036	-0.036	0.000	0.000	0.000	0.000
76	A	74	GLU	-1	-0.786	-0.889	16.171	0.138	0.138	0.000	0.000	0.000	0.000
77	A	75	LEU	0	0.033	0.021	16.299	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	76	ARG	1	0.797	0.882	19.314	-0.165	-0.165	0.000	0.000	0.000	0.000
79	A	77	LYS	1	0.957	0.970	22.697	-0.162	-0.162	0.000	0.000	0.000	0.000
80	A	78	VAL	0	0.047	0.016	25.096	0.008	0.008	0.000	0.000	0.000	0.000
81	A	79	PHE	0	0.008	0.003	22.417	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	80	VAL	0	0.032	0.020	16.678	0.017	0.017	0.000	0.000	0.000	0.000
83	A	81	VAL	0	-0.022	-0.007	18.180	-0.023	-0.023	0.000	0.000	0.000	0.000
84	A	82	LEU	0	0.032	0.019	12.572	0.030	0.030	0.000	0.000	0.000	0.000
85	A	83	PHE	0	-0.019	-0.010	12.359	-0.038	-0.038	0.000	0.000	0.000	0.000
86	A	84	GLN	0	0.000	-0.010	11.003	0.034	0.034	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.776	-0.868	10.416	-0.364	-0.364	0.000	0.000	0.000	0.000
88	A	86	ILE	0	-0.003	-0.003	10.089	-0.158	-0.158	0.000	0.000	0.000	0.000
89	A	87	TYR	0	-0.036	-0.037	10.072	0.090	0.090	0.000	0.000	0.000	0.000
90	A	88	CYS	0	-0.024	0.011	11.677	-0.151	-0.151	0.000	0.000	0.000	0.000
91	A	89	ILE	0	-0.051	-0.040	8.330	0.005	0.005	0.000	0.000	0.000	0.000
92	A	90	GLN	0	0.010	0.001	11.024	0.091	0.091	0.000	0.000	0.000	0.000
93	A	91	ASN	0	0.078	0.021	14.701	0.055	0.055	0.000	0.000	0.000	0.000
94	A	92	ALA	0	0.005	-0.006	18.192	-0.031	-0.031	0.000	0.000	0.000	0.000
95	A	93	SER	0	-0.008	0.006	20.402	0.007	0.007	0.000	0.000	0.000	0.000
96	A	94	LEU	0	-0.078	-0.024	15.324	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	95	GLU	-1	-0.878	-0.936	18.879	-0.330	-0.330	0.000	0.000	0.000	0.000
98	A	96	PRO	0	-0.018	-0.012	17.711	-0.055	-0.055	0.000	0.000	0.000	0.000
99	A	97	MET	0	-0.012	0.003	15.043	0.058	0.058	0.000	0.000	0.000	0.000
100	A	98	LYS	1	0.943	0.982	13.385	0.504	0.504	0.000	0.000	0.000	0.000
101	A	99	PRO	0	-0.017	-0.020	11.288	0.029	0.029	0.000	0.000	0.000	0.000
102	A	100	PHE	0	0.012	0.006	13.860	0.064	0.064	0.000	0.000	0.000	0.000
103	A	101	LYS	1	0.844	0.929	14.101	0.267	0.267	0.000	0.000	0.000	0.000
104	A	102	VAL	0	0.012	0.005	14.985	0.040	0.040	0.000	0.000	0.000	0.000
105	A	103	PHE	0	-0.009	-0.010	15.440	0.062	0.062	0.000	0.000	0.000	0.000
106	A	104	ALA	0	0.001	0.012	14.727	-0.066	-0.066	0.000	0.000	0.000	0.000
107	A	105	SER	0	-0.020	-0.012	15.267	0.040	0.040	0.000	0.000	0.000	0.000
108	A	106	GLU	-1	-0.799	-0.882	15.789	0.016	0.016	0.000	0.000	0.000	0.000
109	A	107	ILE	0	-0.016	-0.011	16.674	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	108	LYS	1	0.907	0.987	18.616	-0.072	-0.072	0.000	0.000	0.000	0.000
111	A	109	PHE	0	0.050	0.016	17.321	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	110	GLY	0	-0.035	-0.025	21.928	0.008	0.008	0.000	0.000	0.000	0.000
113	A	111	PHE	0	0.018	0.017	21.871	0.007	0.007	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.019	-0.009	25.091	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	113	ASN	0	0.026	0.010	28.091	0.001	0.001	0.000	0.000	0.000	0.000
116	A	114	ARG	1	0.806	0.871	25.963	-0.167	-0.167	0.000	0.000	0.000	0.000
117	A	115	SER	0	0.016	0.014	31.168	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	116	THR	0	-0.001	-0.003	34.952	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	117	TYR	0	0.057	0.026	28.883	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	118	SER	0	-0.008	-0.002	32.307	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	119	PRO	0	-0.061	-0.038	29.771	0.009	0.009	0.000	0.000	0.000	0.000
122	A	120	ILE	0	0.003	0.014	27.726	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	121	ALA	0	-0.052	-0.035	26.777	0.004	0.004	0.000	0.000	0.000	0.000
124	A	122	ILE	0	0.007	0.007	20.061	0.000	0.000	0.000	0.000	0.000	0.000
125	A	123	PRO	0	0.037	0.034	21.934	0.003	0.003	0.000	0.000	0.000	0.000
126	A	124	LYS	1	0.957	0.955	21.491	-0.238	-0.238	0.000	0.000	0.000	0.000
127	A	125	LEU	0	0.102	0.051	19.794	0.019	0.019	0.000	0.000	0.000	0.000
128	A	126	PHE	0	0.030	0.019	17.400	0.057	0.057	0.000	0.000	0.000	0.000
129	A	127	LYS	1	0.860	0.942	16.720	-0.267	-0.267	0.000	0.000	0.000	0.000
130	A	128	GLU	-1	-0.923	-0.955	16.884	0.486	0.486	0.000	0.000	0.000	0.000
131	A	129	LEU	0	0.009	0.009	12.961	0.070	0.070	0.000	0.000	0.000	0.000
132	A	130	LEU	0	-0.051	-0.033	12.138	0.096	0.096	0.000	0.000	0.000	0.000
133	A	131	ASN	0	-0.115	-0.078	12.507	-0.012	-0.012	0.000	0.000	0.000	0.000
134	A	132	ALA	0	-0.010	0.026	8.073	0.004	0.004	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:-1:THR)