FMO DATABASE

FMODB ID: 391KL

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1236696.804849
FMO2-HF: Nuclear repulsion	1181817.715487
FMO2-HF: Total energy	-54879.089361
FMO2-MP2: Total energy	-55039.640112

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.
-0.048	0.977	-0.003	-0.497	-0.524	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 : -0.008 / q_NPA : -0.024

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	-0.005	0.038	3.671	1.585	2.572	-0.002	-0.497	-0.488	0.003
4	A	2	ARG	1	0.932	0.965	6.209	0.938	0.938	0.000	0.000	0.000	0.000
5	A	3	CYS	0	-0.016	0.008	8.987	0.357	0.357	0.000	0.000	0.000	0.000
6	A	4	ARG	1	0.890	0.949	12.733	0.282	0.282	0.000	0.000	0.000	0.000
7	A	5	VAL	0	-0.011	0.019	15.557	0.049	0.049	0.000	0.000	0.000	0.000
8	A	6	TYR	0	0.037	0.003	17.314	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	7	TYR	0	0.071	0.006	21.591	-0.005	-0.005	0.000	0.000	0.000	0.000
10	A	8	GLU	-1	-0.969	-0.967	22.203	-0.055	-0.055	0.000	0.000	0.000	0.000
11	A	9	ASP	-1	-0.842	-0.916	19.949	-0.173	-0.173	0.000	0.000	0.000	0.000
12	A	10	THR	0	-0.096	-0.051	23.133	-0.018	-0.018	0.000	0.000	0.000	0.000
13	A	11	ASP	-1	-0.790	-0.913	25.318	-0.145	-0.145	0.000	0.000	0.000	0.000
14	A	12	SER	0	-0.022	-0.022	28.545	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-1.017	-0.995	28.696	-0.189	-0.189	0.000	0.000	0.000	0.000
16	A	14	GLY	0	-0.031	-0.006	28.084	-0.009	-0.009	0.000	0.000	0.000	0.000
17	A	15	VAL	0	-0.031	-0.018	23.828	-0.032	-0.032	0.000	0.000	0.000	0.000
18	A	16	VAL	0	-0.057	-0.026	19.370	0.020	0.020	0.000	0.000	0.000	0.000
19	A	17	TYR	0	0.042	0.026	22.677	0.002	0.002	0.000	0.000	0.000	0.000
20	A	18	HIS	0	0.041	0.011	22.963	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	19	ALA	0	0.013	-0.002	21.942	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	20	ASN	0	-0.013	-0.013	20.568	0.041	0.041	0.000	0.000	0.000	0.000
23	A	21	TYR	0	0.052	0.029	16.761	-0.022	-0.022	0.000	0.000	0.000	0.000
24	A	22	LEU	0	0.031	0.012	16.547	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	23	LYS	1	0.952	0.982	17.640	0.063	0.063	0.000	0.000	0.000	0.000
26	A	24	TYR	0	-0.012	-0.010	13.756	0.029	0.029	0.000	0.000	0.000	0.000
27	A	25	CYS	0	-0.017	-0.012	12.956	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	26	GLU	-1	-0.909	-0.941	13.536	0.306	0.306	0.000	0.000	0.000	0.000
29	A	27	ARG	1	1.018	1.008	13.526	0.118	0.118	0.000	0.000	0.000	0.000
30	A	28	ALA	0	-0.017	-0.027	9.283	0.144	0.144	0.000	0.000	0.000	0.000
31	A	29	ARG	1	0.874	0.943	9.838	0.156	0.156	0.000	0.000	0.000	0.000
32	A	30	SER	0	0.016	-0.021	12.270	0.160	0.160	0.000	0.000	0.000	0.000
33	A	31	GLU	-1	-0.895	-0.948	9.214	1.285	1.285	0.000	0.000	0.000	0.000
34	A	32	PHE	0	-0.055	-0.025	5.450	0.313	0.313	0.000	0.000	0.000	0.000
35	A	33	PHE	0	-0.035	-0.015	9.764	0.098	0.098	0.000	0.000	0.000	0.000
36	A	34	PHE	0	0.038	0.017	12.891	0.005	0.005	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.906	0.953	5.307	-4.268	-4.230	-0.001	0.000	-0.036	0.000
38	A	36	GLN	0	-0.066	-0.021	9.621	-0.058	-0.058	0.000	0.000	0.000	0.000
39	A	37	ASN	0	-0.046	-0.021	13.407	-0.113	-0.113	0.000	0.000	0.000	0.000
40	A	38	VAL	0	-0.024	-0.002	15.859	-0.130	-0.130	0.000	0.000	0.000	0.000
41	A	39	LEU	0	0.063	0.022	16.606	0.048	0.048	0.000	0.000	0.000	0.000
42	A	40	PRO	0	-0.011	0.007	16.551	0.013	0.013	0.000	0.000	0.000	0.000
43	A	41	GLU	-1	-0.963	-1.001	18.367	0.217	0.217	0.000	0.000	0.000	0.000
44	A	42	ASN	0	0.018	-0.010	22.105	0.024	0.024	0.000	0.000	0.000	0.000
45	A	43	GLU	-1	-0.845	-0.932	24.611	0.241	0.241	0.000	0.000	0.000	0.000
46	A	44	GLU	-1	-0.977	-0.974	28.118	0.156	0.156	0.000	0.000	0.000	0.000
47	A	45	GLY	0	-0.047	-0.033	26.792	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	46	VAL	0	0.009	0.012	23.665	0.024	0.024	0.000	0.000	0.000	0.000
49	A	47	PHE	0	0.008	0.005	18.879	-0.022	-0.022	0.000	0.000	0.000	0.000
50	A	48	VAL	0	-0.019	-0.004	22.577	-0.013	-0.013	0.000	0.000	0.000	0.000
51	A	49	ILE	0	0.007	0.003	20.746	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	50	ARG	1	0.877	0.939	23.612	-0.089	-0.089	0.000	0.000	0.000	0.000
53	A	51	SER	0	0.041	0.002	23.867	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	52	ILE	0	0.007	0.007	19.539	0.005	0.005	0.000	0.000	0.000	0.000
55	A	53	LYS	1	0.931	0.997	21.132	0.175	0.175	0.000	0.000	0.000	0.000
56	A	54	ALA	0	0.007	-0.019	19.898	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	55	ASP	-1	-0.949	-0.956	19.644	-0.223	-0.223	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.008	-0.012	19.449	-0.034	-0.034	0.000	0.000	0.000	0.000
59	A	57	PHE	0	-0.013	-0.017	17.930	0.001	0.001	0.000	0.000	0.000	0.000
60	A	58	THR	0	0.003	0.002	19.431	0.038	0.038	0.000	0.000	0.000	0.000
61	A	59	PRO	0	0.046	0.033	19.474	-0.045	-0.045	0.000	0.000	0.000	0.000
62	A	60	ALA	0	-0.001	-0.002	17.726	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	61	SER	0	0.048	0.011	19.797	0.050	0.050	0.000	0.000	0.000	0.000
64	A	62	LEU	0	0.044	0.009	20.654	-0.035	-0.035	0.000	0.000	0.000	0.000
65	A	63	GLY	0	-0.011	-0.006	20.168	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	64	GLN	0	0.032	0.019	17.023	-0.052	-0.052	0.000	0.000	0.000	0.000
67	A	65	VAL	0	-0.028	-0.009	11.392	0.040	0.040	0.000	0.000	0.000	0.000
68	A	66	LEU	0	0.006	-0.002	12.361	-0.107	-0.107	0.000	0.000	0.000	0.000
69	A	67	GLU	-1	-0.837	-0.918	5.823	-4.025	-4.025	0.000	0.000	0.000	0.000
70	A	68	ILE	0	-0.027	-0.023	8.006	0.154	0.154	0.000	0.000	0.000	0.000
71	A	69	ARG	1	0.826	0.898	5.232	2.050	2.050	0.000	0.000	0.000	0.000
72	A	70	THR	0	0.046	0.015	6.331	0.361	0.361	0.000	0.000	0.000	0.000
73	A	71	GLN	0	-0.014	0.002	7.591	0.116	0.116	0.000	0.000	0.000	0.000
74	A	72	ILE	0	0.034	0.018	10.058	-0.010	-0.010	0.000	0.000	0.000	0.000
75	A	73	LYS	1	0.915	0.971	13.206	0.129	0.129	0.000	0.000	0.000	0.000
76	A	74	GLU	-1	-0.802	-0.905	16.034	0.043	0.043	0.000	0.000	0.000	0.000
77	A	75	LEU	0	0.015	0.017	16.604	0.010	0.010	0.000	0.000	0.000	0.000
78	A	76	ARG	1	0.829	0.910	19.233	-0.082	-0.082	0.000	0.000	0.000	0.000
79	A	77	LYS	1	0.909	0.941	22.627	-0.145	-0.145	0.000	0.000	0.000	0.000
80	A	78	VAL	0	0.052	0.019	25.089	0.015	0.015	0.000	0.000	0.000	0.000
81	A	79	PHE	0	-0.013	0.000	22.125	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	80	VAL	0	0.034	0.023	16.519	0.012	0.012	0.000	0.000	0.000	0.000
83	A	81	VAL	0	-0.009	-0.003	18.170	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	82	LEU	0	0.015	0.009	12.649	0.012	0.012	0.000	0.000	0.000	0.000
85	A	83	PHE	0	-0.022	-0.006	12.334	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	84	GLN	0	-0.010	-0.017	10.760	0.020	0.020	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.877	-0.942	10.341	-0.744	-0.744	0.000	0.000	0.000	0.000
88	A	86	ILE	0	-0.017	-0.008	9.964	-0.180	-0.180	0.000	0.000	0.000	0.000
89	A	87	TYR	0	-0.009	-0.006	9.909	0.097	0.097	0.000	0.000	0.000	0.000
90	A	88	CYS	0	-0.019	0.024	11.476	-0.111	-0.111	0.000	0.000	0.000	0.000
91	A	89	ILE	0	-0.050	-0.045	8.329	-0.024	-0.024	0.000	0.000	0.000	0.000
92	A	90	GLN	0	0.024	0.007	10.935	0.128	0.128	0.000	0.000	0.000	0.000
93	A	91	ASN	0	0.086	0.031	14.774	0.057	0.057	0.000	0.000	0.000	0.000
94	A	92	ALA	0	0.012	0.000	18.255	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	93	SER	0	-0.003	0.002	20.466	0.021	0.021	0.000	0.000	0.000	0.000
96	A	94	LEU	0	-0.060	-0.011	15.418	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	95	GLU	-1	-0.909	-0.948	18.925	-0.339	-0.339	0.000	0.000	0.000	0.000
98	A	96	PRO	0	-0.034	-0.020	17.760	-0.065	-0.065	0.000	0.000	0.000	0.000
99	A	97	MET	0	-0.017	-0.004	15.290	0.057	0.057	0.000	0.000	0.000	0.000
100	A	98	LYS	1	0.952	0.984	12.883	0.949	0.949	0.000	0.000	0.000	0.000
101	A	99	PRO	0	-0.019	-0.023	11.271	0.033	0.033	0.000	0.000	0.000	0.000
102	A	100	PHE	0	0.003	0.004	13.709	0.041	0.041	0.000	0.000	0.000	0.000
103	A	101	LYS	1	0.932	0.982	14.156	0.513	0.513	0.000	0.000	0.000	0.000
104	A	102	VAL	0	0.018	0.005	14.831	0.059	0.059	0.000	0.000	0.000	0.000
105	A	103	PHE	0	-0.011	-0.010	15.223	0.081	0.081	0.000	0.000	0.000	0.000
106	A	104	ALA	0	0.007	0.013	14.609	-0.102	-0.102	0.000	0.000	0.000	0.000
107	A	105	SER	0	-0.027	-0.013	15.200	0.079	0.079	0.000	0.000	0.000	0.000
108	A	106	GLU	-1	-0.891	-0.946	15.752	-0.144	-0.144	0.000	0.000	0.000	0.000
109	A	107	ILE	0	-0.014	-0.012	16.399	0.019	0.019	0.000	0.000	0.000	0.000
110	A	108	LYS	1	0.958	0.999	18.620	-0.026	-0.026	0.000	0.000	0.000	0.000
111	A	109	PHE	0	0.030	0.005	17.158	0.000	0.000	0.000	0.000	0.000	0.000
112	A	110	GLY	0	-0.045	-0.030	21.915	0.000	0.000	0.000	0.000	0.000	0.000
113	A	111	PHE	0	0.028	0.026	22.141	0.012	0.012	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.017	-0.003	25.082	-0.018	-0.018	0.000	0.000	0.000	0.000
115	A	113	ASN	0	0.083	0.036	28.083	0.007	0.007	0.000	0.000	0.000	0.000
116	A	114	ARG	1	0.842	0.914	26.148	-0.238	-0.238	0.000	0.000	0.000	0.000
117	A	115	SER	0	0.020	0.015	31.160	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	116	THR	0	-0.008	-0.006	34.945	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	117	TYR	0	0.035	0.019	28.858	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	118	SER	0	-0.003	0.001	32.297	-0.010	-0.010	0.000	0.000	0.000	0.000
121	A	119	PRO	0	-0.071	-0.041	29.746	0.012	0.012	0.000	0.000	0.000	0.000
122	A	120	ILE	0	0.018	0.018	27.638	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	121	ALA	0	-0.062	-0.040	26.719	0.001	0.001	0.000	0.000	0.000	0.000
124	A	122	ILE	0	0.013	0.009	20.070	0.006	0.006	0.000	0.000	0.000	0.000
125	A	123	PRO	0	0.030	0.031	21.888	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	124	LYS	1	0.952	0.952	21.489	-0.273	-0.273	0.000	0.000	0.000	0.000
127	A	125	LEU	0	0.096	0.046	19.750	0.013	0.013	0.000	0.000	0.000	0.000
128	A	126	PHE	0	0.048	0.029	17.369	0.060	0.060	0.000	0.000	0.000	0.000
129	A	127	LYS	1	0.878	0.947	16.718	-0.236	-0.236	0.000	0.000	0.000	0.000
130	A	128	GLU	-1	-0.908	-0.957	16.882	0.555	0.555	0.000	0.000	0.000	0.000
131	A	129	LEU	0	-0.001	0.005	13.310	0.062	0.062	0.000	0.000	0.000	0.000
132	A	130	LEU	0	-0.046	-0.026	12.137	0.101	0.101	0.000	0.000	0.000	0.000
133	A	131	ASN	0	-0.109	-0.067	12.470	-0.072	-0.072	0.000	0.000	0.000	0.000
134	A	132	ALA	0	-0.004	0.026	8.094	-0.035	-0.035	0.000	0.000	0.000	0.000

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