FMO DATABASE

FMODB ID: 941L2

Calculation Name: 2PZH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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:

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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1236588.533028
FMO2-HF: Nuclear repulsion	1181708.199793
FMO2-HF: Total energy	-54880.333236
FMO2-MP2: Total energy	-55040.865809

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:-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.
2.19	3.199	-0.005	-0.483	-0.52	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 : -0.003 / q_NPA : -0.017

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	0.022	0.039	3.888	1.232	2.186	-0.004	-0.481	-0.469	0.003
4	A	2	ARG	1	0.941	0.969	5.576	2.549	2.549	0.000	0.000	0.000	0.000
5	A	3	CYS	0	-0.018	-0.008	8.983	0.317	0.317	0.000	0.000	0.000	0.000
6	A	4	ARG	1	0.875	0.950	12.698	0.512	0.512	0.000	0.000	0.000	0.000
7	A	5	VAL	0	-0.007	0.013	15.438	0.051	0.051	0.000	0.000	0.000	0.000
8	A	6	TYR	0	0.023	-0.002	16.839	-0.006	-0.006	0.000	0.000	0.000	0.000
9	A	7	TYR	0	0.073	0.011	21.380	0.002	0.002	0.000	0.000	0.000	0.000
10	A	8	GLU	-1	-0.914	-0.945	21.086	-0.166	-0.166	0.000	0.000	0.000	0.000
11	A	9	ASP	-1	-0.813	-0.901	19.460	-0.282	-0.282	0.000	0.000	0.000	0.000
12	A	10	THR	0	-0.069	-0.028	22.840	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	11	ASP	-1	-0.826	-0.924	25.443	-0.143	-0.143	0.000	0.000	0.000	0.000
14	A	12	SER	0	-0.011	-0.010	28.895	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-0.972	-0.976	28.548	-0.159	-0.159	0.000	0.000	0.000	0.000
16	A	14	GLY	0	-0.024	-0.009	28.134	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	15	VAL	0	-0.022	-0.016	24.191	-0.030	-0.030	0.000	0.000	0.000	0.000
18	A	16	VAL	0	-0.052	-0.034	19.644	0.010	0.010	0.000	0.000	0.000	0.000
19	A	17	TYR	0	0.047	0.030	22.773	0.008	0.008	0.000	0.000	0.000	0.000
20	A	18	HIS	0	0.016	-0.009	22.910	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	19	ALA	0	0.030	0.014	21.973	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	20	ASN	0	-0.017	-0.011	20.717	0.028	0.028	0.000	0.000	0.000	0.000
23	A	21	TYR	0	0.042	0.023	17.279	-0.037	-0.037	0.000	0.000	0.000	0.000
24	A	22	LEU	0	0.017	0.003	16.762	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	23	LYS	1	0.917	0.965	17.979	0.162	0.162	0.000	0.000	0.000	0.000
26	A	24	TYR	0	-0.072	-0.058	13.933	0.002	0.002	0.000	0.000	0.000	0.000
27	A	25	CYS	0	-0.009	-0.005	13.205	-0.039	-0.039	0.000	0.000	0.000	0.000
28	A	26	GLU	-1	-0.778	-0.852	13.701	0.176	0.176	0.000	0.000	0.000	0.000
29	A	27	ARG	1	0.883	0.937	13.357	0.273	0.273	0.000	0.000	0.000	0.000
30	A	28	ALA	0	0.015	-0.008	9.408	0.085	0.085	0.000	0.000	0.000	0.000
31	A	29	ARG	1	0.780	0.873	10.164	0.155	0.155	0.000	0.000	0.000	0.000
32	A	30	SER	0	0.025	-0.016	12.421	0.131	0.131	0.000	0.000	0.000	0.000
33	A	31	GLU	-1	-0.821	-0.889	8.640	0.825	0.825	0.000	0.000	0.000	0.000
34	A	32	PHE	0	-0.052	-0.028	5.273	0.257	0.257	0.000	0.000	0.000	0.000
35	A	33	PHE	0	-0.021	-0.003	9.858	0.093	0.093	0.000	0.000	0.000	0.000
36	A	34	PHE	0	0.037	0.023	12.475	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.832	0.900	5.019	-2.020	-1.965	-0.001	-0.002	-0.051	0.000
38	A	36	GLN	0	-0.074	-0.036	10.529	0.045	0.045	0.000	0.000	0.000	0.000
39	A	37	ASN	0	-0.060	-0.025	13.328	-0.127	-0.127	0.000	0.000	0.000	0.000
40	A	38	VAL	0	-0.015	0.003	15.872	-0.081	-0.081	0.000	0.000	0.000	0.000
41	A	39	LEU	0	0.062	0.026	16.755	0.020	0.020	0.000	0.000	0.000	0.000
42	A	40	PRO	0	-0.018	-0.001	16.960	0.023	0.023	0.000	0.000	0.000	0.000
43	A	41	GLU	-1	-0.888	-0.948	18.608	0.123	0.123	0.000	0.000	0.000	0.000
44	A	42	ASN	0	-0.007	-0.027	22.352	0.019	0.019	0.000	0.000	0.000	0.000
45	A	43	GLU	-1	-0.800	-0.889	24.677	0.183	0.183	0.000	0.000	0.000	0.000
46	A	44	GLU	-1	-0.878	-0.938	28.444	0.105	0.105	0.000	0.000	0.000	0.000
47	A	45	GLY	0	-0.045	-0.031	27.211	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	46	VAL	0	0.018	0.019	23.273	0.013	0.013	0.000	0.000	0.000	0.000
49	A	47	PHE	0	0.001	0.006	18.463	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	48	VAL	0	-0.015	-0.005	22.356	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	49	ILE	0	0.011	0.004	21.705	0.007	0.007	0.000	0.000	0.000	0.000
52	A	50	ARG	1	0.839	0.927	23.616	-0.087	-0.087	0.000	0.000	0.000	0.000
53	A	51	SER	0	0.027	0.007	24.388	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	52	ILE	0	-0.010	-0.007	20.145	0.008	0.008	0.000	0.000	0.000	0.000
55	A	53	LYS	1	0.822	0.919	21.682	0.088	0.088	0.000	0.000	0.000	0.000
56	A	54	ALA	0	0.017	-0.009	20.237	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	55	ASP	-1	-0.847	-0.902	19.765	-0.098	-0.098	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.032	0.004	19.589	-0.028	-0.028	0.000	0.000	0.000	0.000
59	A	57	PHE	0	-0.003	-0.004	18.374	0.013	0.013	0.000	0.000	0.000	0.000
60	A	58	THR	0	0.017	0.008	19.642	0.024	0.024	0.000	0.000	0.000	0.000
61	A	59	PRO	0	0.042	0.031	19.652	-0.041	-0.041	0.000	0.000	0.000	0.000
62	A	60	ALA	0	0.004	0.005	17.809	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	61	SER	0	0.026	0.003	19.818	0.043	0.043	0.000	0.000	0.000	0.000
64	A	62	LEU	0	0.049	0.013	20.745	-0.043	-0.043	0.000	0.000	0.000	0.000
65	A	63	GLY	0	0.003	0.011	20.369	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	64	GLN	0	0.040	0.032	17.044	-0.068	-0.068	0.000	0.000	0.000	0.000
67	A	65	VAL	0	-0.032	-0.010	11.446	0.007	0.007	0.000	0.000	0.000	0.000
68	A	66	LEU	0	0.020	0.012	12.481	-0.027	-0.027	0.000	0.000	0.000	0.000
69	A	67	GLU	-1	-0.830	-0.918	5.576	-3.582	-3.582	0.000	0.000	0.000	0.000
70	A	68	ILE	0	-0.023	-0.003	8.269	0.203	0.203	0.000	0.000	0.000	0.000
71	A	69	ARG	1	0.806	0.900	5.520	1.564	1.564	0.000	0.000	0.000	0.000
72	A	70	THR	0	0.021	0.004	6.601	0.266	0.266	0.000	0.000	0.000	0.000
73	A	71	GLN	0	-0.010	0.003	7.741	0.156	0.156	0.000	0.000	0.000	0.000
74	A	72	ILE	0	0.026	0.007	10.414	-0.053	-0.053	0.000	0.000	0.000	0.000
75	A	73	LYS	1	0.825	0.905	13.858	-0.030	-0.030	0.000	0.000	0.000	0.000
76	A	74	GLU	-1	-0.789	-0.892	16.747	0.130	0.130	0.000	0.000	0.000	0.000
77	A	75	LEU	0	0.025	0.019	16.714	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	76	ARG	1	0.831	0.905	19.835	-0.151	-0.151	0.000	0.000	0.000	0.000
79	A	77	LYS	1	0.988	0.987	22.800	-0.150	-0.150	0.000	0.000	0.000	0.000
80	A	78	VAL	0	0.026	0.019	25.220	0.008	0.008	0.000	0.000	0.000	0.000
81	A	79	PHE	0	0.002	-0.007	22.991	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	80	VAL	0	0.005	0.007	16.866	0.017	0.017	0.000	0.000	0.000	0.000
83	A	81	VAL	0	-0.023	-0.004	18.518	-0.025	-0.025	0.000	0.000	0.000	0.000
84	A	82	LEU	0	0.044	0.024	12.868	0.031	0.031	0.000	0.000	0.000	0.000
85	A	83	PHE	0	-0.014	-0.011	12.674	-0.032	-0.032	0.000	0.000	0.000	0.000
86	A	84	GLN	0	-0.004	-0.013	11.118	0.046	0.046	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.767	-0.860	10.764	-0.311	-0.311	0.000	0.000	0.000	0.000
88	A	86	ILE	0	-0.012	-0.006	10.369	-0.146	-0.146	0.000	0.000	0.000	0.000
89	A	87	TYR	0	-0.023	-0.039	10.035	0.100	0.100	0.000	0.000	0.000	0.000
90	A	88	CYS	0	0.010	0.020	11.617	-0.154	-0.154	0.000	0.000	0.000	0.000
91	A	89	ILE	0	-0.059	-0.044	8.463	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	90	GLN	0	0.012	0.000	11.599	0.056	0.056	0.000	0.000	0.000	0.000
93	A	91	ASN	0	0.067	0.019	14.794	0.044	0.044	0.000	0.000	0.000	0.000
94	A	92	ALA	0	0.009	-0.006	18.183	-0.034	-0.034	0.000	0.000	0.000	0.000
95	A	93	SER	0	-0.022	-0.022	20.519	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	94	LEU	0	-0.083	-0.026	14.767	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	95	GLU	-1	-0.844	-0.901	18.521	-0.334	-0.334	0.000	0.000	0.000	0.000
98	A	96	PRO	0	-0.025	-0.007	17.722	-0.056	-0.056	0.000	0.000	0.000	0.000
99	A	97	MET	0	-0.008	0.006	15.135	0.056	0.056	0.000	0.000	0.000	0.000
100	A	98	LYS	1	0.949	0.982	13.520	0.433	0.433	0.000	0.000	0.000	0.000
101	A	99	PRO	0	-0.022	-0.021	11.311	0.026	0.026	0.000	0.000	0.000	0.000
102	A	100	PHE	0	-0.006	0.000	13.780	0.055	0.055	0.000	0.000	0.000	0.000
103	A	101	LYS	1	0.793	0.898	13.949	0.258	0.258	0.000	0.000	0.000	0.000
104	A	102	VAL	0	0.007	0.011	15.124	0.037	0.037	0.000	0.000	0.000	0.000
105	A	103	PHE	0	-0.010	-0.016	15.551	0.060	0.060	0.000	0.000	0.000	0.000
106	A	104	ALA	0	0.010	0.008	14.880	-0.062	-0.062	0.000	0.000	0.000	0.000
107	A	105	SER	0	-0.016	-0.008	15.428	0.035	0.035	0.000	0.000	0.000	0.000
108	A	106	GLU	-1	-0.796	-0.877	15.999	0.016	0.016	0.000	0.000	0.000	0.000
109	A	107	ILE	0	-0.011	-0.007	16.673	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	108	LYS	1	0.886	0.976	18.958	-0.068	-0.068	0.000	0.000	0.000	0.000
111	A	109	PHE	0	0.063	0.013	17.806	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	110	GLY	0	-0.016	-0.019	22.065	0.009	0.009	0.000	0.000	0.000	0.000
113	A	111	PHE	0	0.007	0.015	21.582	0.004	0.004	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.020	-0.011	25.043	-0.012	-0.012	0.000	0.000	0.000	0.000
115	A	113	ASN	0	0.021	0.005	27.959	0.000	0.000	0.000	0.000	0.000	0.000
116	A	114	ARG	1	0.769	0.849	25.934	-0.159	-0.159	0.000	0.000	0.000	0.000
117	A	115	SER	0	0.012	0.019	30.935	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	116	THR	0	0.006	-0.003	34.570	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	117	TYR	0	0.036	0.023	28.919	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	118	SER	0	0.004	-0.008	31.913	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	119	PRO	0	-0.058	-0.029	29.551	0.008	0.008	0.000	0.000	0.000	0.000
122	A	120	ILE	0	0.013	0.011	27.678	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	121	ALA	0	-0.038	-0.034	26.937	0.005	0.005	0.000	0.000	0.000	0.000
124	A	122	ILE	0	0.005	0.005	20.109	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	123	PRO	0	0.027	0.030	22.364	0.008	0.008	0.000	0.000	0.000	0.000
126	A	124	LYS	1	0.876	0.924	21.473	-0.281	-0.281	0.000	0.000	0.000	0.000
127	A	125	LEU	0	0.086	0.050	19.571	0.025	0.025	0.000	0.000	0.000	0.000
128	A	126	PHE	0	0.038	0.025	17.266	0.061	0.061	0.000	0.000	0.000	0.000
129	A	127	LYS	1	0.844	0.928	16.816	-0.268	-0.268	0.000	0.000	0.000	0.000
130	A	128	GLU	-1	-0.877	-0.942	17.318	0.414	0.414	0.000	0.000	0.000	0.000
131	A	129	LEU	0	0.033	0.020	12.731	0.056	0.056	0.000	0.000	0.000	0.000
132	A	130	LEU	0	-0.028	-0.021	12.375	0.100	0.100	0.000	0.000	0.000	0.000
133	A	131	ASN	0	-0.121	-0.069	13.786	-0.078	-0.078	0.000	0.000	0.000	0.000
134	A	132	ALA	0	-0.027	0.006	7.738	-0.004	-0.004	0.000	0.000	0.000	0.000

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