FMO DATABASE

FMODB ID: QVLMY

Calculation Name: 2PZZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PZZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q58959

Base Structure: X-ray

Registration Date: 2023-09-23

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	133
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1182313.044085
FMO2-HF: Nuclear repulsion	1130401.225486
FMO2-HF: Total energy	-51911.818599
FMO2-MP2: Total energy	-52065.360345

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-29.809	-17.46	10.956	-7.583	-15.721	-0.043

Interaction energy analysis for fragmet #1(A:2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.028

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	4	VAL	0	-0.015	0.007	2.552	-1.100	0.253	1.087	-0.259	-2.181	0.002
4	A	5	ILE	0	-0.049	-0.034	4.710	-0.229	-0.159	-0.001	-0.012	-0.057	0.000
5	A	6	ILE	0	-0.006	-0.009	7.996	0.011	0.011	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.885	0.927	10.797	-0.110	-0.110	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.011	0.006	14.536	0.004	0.004	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.990	1.015	17.194	-0.076	-0.076	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.044	-0.029	20.903	0.012	0.012	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.848	0.920	23.410	-0.079	-0.079	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.071	0.045	26.711	0.005	0.005	0.000	0.000	0.000	0.000
12	A	13	THR	0	0.003	0.007	29.912	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.877	-0.910	23.729	0.118	0.118	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.767	-0.866	26.385	0.118	0.118	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.977	0.983	23.203	-0.098	-0.098	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.045	0.005	21.920	0.021	0.021	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.852	0.920	21.870	-0.096	-0.096	0.000	0.000	0.000	0.000
18	A	19	VAL	0	0.018	0.018	18.703	0.013	0.013	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.926	0.974	17.673	-0.214	-0.214	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.963	0.968	16.938	-0.132	-0.132	0.000	0.000	0.000	0.000
21	A	22	ALA	0	0.039	0.036	17.426	0.017	0.017	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.013	-0.001	12.109	0.025	0.025	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.042	-0.021	12.753	0.049	0.049	0.000	0.000	0.000	0.000
24	A	25	ASN	0	-0.044	-0.019	13.715	0.036	0.036	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.035	-0.008	10.016	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	27	PHE	0	-0.025	-0.029	6.095	0.104	0.104	0.000	0.000	0.000	0.000
27	A	28	PRO	0	0.045	0.021	9.767	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.807	0.900	8.426	-0.805	-0.805	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.028	-0.002	9.468	0.034	0.034	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.892	0.956	10.254	-0.732	-0.732	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.041	-0.024	12.609	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	33	THR	0	0.011	0.007	15.030	-0.015	-0.015	0.000	0.000	0.000	0.000
33	A	34	PHE	0	-0.018	-0.033	17.940	0.002	0.002	0.000	0.000	0.000	0.000
34	A	35	ILE	0	0.007	0.011	19.531	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.878	-0.950	22.849	0.088	0.088	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.809	0.881	21.267	-0.075	-0.075	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.858	-0.916	27.400	0.036	0.036	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.053	-0.045	30.392	0.001	0.001	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.865	-0.941	31.081	0.058	0.058	0.000	0.000	0.000	0.000
40	A	41	PHE	0	-0.065	-0.024	26.142	0.008	0.008	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.045	0.025	24.709	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.925	-0.955	18.655	0.088	0.088	0.000	0.000	0.000	0.000
43	A	44	TRP	0	-0.040	-0.014	16.672	0.007	0.007	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.801	-0.898	14.609	0.102	0.102	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.037	-0.001	12.043	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.913	0.972	7.299	-0.235	-0.235	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.032	0.013	5.062	-0.041	-0.041	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.921	0.958	2.636	-7.857	-5.923	0.363	-0.935	-1.361	0.006
49	A	50	SER	0	-0.094	-0.073	2.667	-1.027	-0.151	0.997	-0.576	-1.297	-0.009
50	A	51	VAL	0	0.084	0.022	2.402	-1.164	-0.253	1.088	-0.351	-1.649	0.002
51	A	52	GLU	-1	-0.772	-0.840	5.031	0.530	0.574	-0.001	-0.003	-0.040	0.000
52	A	53	LYS	1	0.922	0.960	7.873	-0.406	-0.406	0.000	0.000	0.000	0.000
53	A	54	LEU	0	0.029	0.011	6.672	-0.068	-0.068	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.812	0.882	5.133	-0.331	-0.331	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.819	-0.895	9.626	0.275	0.275	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.012	0.021	12.872	-0.045	-0.045	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.002	0.010	9.826	-0.039	-0.039	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.809	0.893	10.132	-0.213	-0.213	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.023	-0.024	15.584	-0.023	-0.023	0.000	0.000	0.000	0.000
60	A	61	GLN	0	-0.023	-0.006	17.033	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.004	0.004	18.137	-0.016	-0.016	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.001	0.010	15.453	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	64	LEU	0	-0.010	-0.016	12.874	0.009	0.009	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.911	-0.954	14.551	0.047	0.047	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.049	0.024	16.912	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.011	0.001	11.351	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.777	0.887	11.784	0.089	0.089	0.000	0.000	0.000	0.000
68	A	69	MET	0	0.035	0.037	13.082	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.026	-0.027	12.849	-0.019	-0.019	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.008	0.006	7.549	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.750	-0.850	11.047	-0.165	-0.165	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.895	0.948	13.270	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.001	0.015	13.259	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	75	MET	0	-0.076	-0.031	10.564	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.074	-0.039	11.417	0.010	0.010	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.858	-0.931	11.965	-0.497	-0.497	0.000	0.000	0.000	0.000
77	A	78	ASN	0	0.023	0.011	7.950	-0.127	-0.127	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.005	-0.019	6.913	-0.187	-0.187	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.008	-0.016	6.870	0.072	0.072	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.899	0.954	8.510	0.137	0.137	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.027	0.002	7.641	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	83	TYR	0	0.021	0.005	12.508	0.022	0.022	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.007	0.011	10.917	0.009	0.009	0.000	0.000	0.000	0.000
84	A	85	ASN	0	0.011	0.003	15.073	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.801	0.855	17.912	-0.109	-0.109	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.042	-0.035	19.222	0.007	0.007	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.005	0.001	19.145	0.000	0.000	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.038	0.031	16.055	0.006	0.006	0.000	0.000	0.000	0.000
89	A	90	TYR	0	-0.028	-0.014	17.681	0.013	0.013	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.053	-0.025	20.472	0.000	0.000	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.022	-0.002	17.782	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	93	ALA	0	-0.020	-0.001	17.906	0.006	0.006	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.041	-0.038	12.970	0.014	0.014	0.000	0.000	0.000	0.000
94	A	95	ASN	0	0.010	-0.025	15.901	-0.020	-0.020	0.000	0.000	0.000	0.000
95	A	96	PHE	0	0.008	0.002	11.698	0.011	0.011	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.835	-0.865	16.890	0.093	0.093	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.015	-0.018	18.788	0.013	0.013	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.709	-0.847	20.569	0.111	0.111	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.035	0.002	22.940	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	101	HIS	0	0.022	-0.001	23.847	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.032	-0.011	21.501	0.004	0.004	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.034	0.029	18.302	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.067	-0.023	12.430	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.030	-0.015	13.680	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.008	-0.010	7.428	0.044	0.044	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.919	0.964	8.441	-0.047	-0.047	0.000	0.000	0.000	0.000
107	A	108	ILE	0	0.007	0.013	2.585	-0.846	-0.042	0.928	-0.238	-1.494	-0.001
108	A	109	LEU	0	-0.023	-0.027	4.103	-0.448	-0.073	0.000	-0.073	-0.301	0.000
109	A	110	ALA	0	0.009	0.000	2.451	-3.193	-1.206	2.381	-2.374	-1.994	-0.022
110	A	111	ASP	-1	-0.844	-0.927	2.699	-9.019	-5.891	0.628	-1.865	-1.891	-0.020
111	A	112	GLU	-1	-0.913	-0.966	4.386	-0.588	-0.522	-0.001	-0.015	-0.050	0.000
112	A	113	ASN	0	-0.071	-0.029	6.304	0.589	0.589	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.961	-0.981	2.717	-3.508	-2.731	0.106	-0.301	-0.582	-0.001
114	A	115	ASP	-1	-0.817	-0.884	5.999	-0.299	-0.299	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.052	0.020	5.949	-0.075	-0.075	0.000	0.000	0.000	0.000
116	A	117	MET	0	0.027	0.012	6.832	0.199	0.199	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.847	0.908	7.754	0.875	0.875	0.000	0.000	0.000	0.000
118	A	119	ILE	0	0.056	0.042	2.273	-0.064	-0.482	3.281	-0.483	-2.380	-0.001
119	A	120	ILE	0	0.000	-0.006	4.691	0.366	0.419	-0.001	-0.003	-0.049	0.000
120	A	121	LYS	1	0.790	0.892	7.439	0.432	0.432	0.000	0.000	0.000	0.000
121	A	122	ASP	-1	-0.769	-0.864	5.263	0.049	0.049	0.000	0.000	0.000	0.000
122	A	123	ILE	0	-0.023	-0.009	2.844	-0.297	0.092	0.101	-0.095	-0.395	0.001
123	A	124	ALA	0	0.003	0.012	7.325	0.020	0.020	0.000	0.000	0.000	0.000
124	A	125	PRO	0	0.007	0.011	10.693	-0.051	-0.051	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.858	0.909	13.142	0.097	0.097	0.000	0.000	0.000	0.000
126	A	127	THR	0	0.016	-0.004	16.562	0.003	0.003	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.953	0.974	19.495	0.033	0.033	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.051	0.032	23.293	0.000	0.000	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.020	0.020	21.257	0.004	0.004	0.000	0.000	0.000	0.000
130	A	131	VAL	0	0.014	0.015	20.756	0.010	0.010	0.000	0.000	0.000	0.000
131	A	132	ILE	0	0.003	-0.019	14.608	-0.010	-0.010	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.031	-0.007	17.522	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	134	ASN	0	-0.011	0.006	14.645	0.011	0.011	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)