FMO DATABASE

FMODB ID: KGV83

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	OptAll
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	-1180323.726977
FMO2-HF: Nuclear repulsion	1128411.538074
FMO2-HF: Total energy	-51912.188903
FMO2-MP2: Total energy	-52065.655802

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.
-34.608	-22.525	11.695	-8.545	-15.232	-0.061

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 : 0.032 / q_NPA : 0.030

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	-0.014	0.002	2.576	-1.630	0.111	0.902	-0.619	-2.024	0.002
4	A	5	ILE	0	-0.035	-0.028	4.678	-0.075	-0.015	-0.001	-0.009	-0.051	0.000
5	A	6	ILE	0	-0.003	-0.007	8.244	0.010	0.010	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.833	0.909	11.026	-0.054	-0.054	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.014	0.003	14.809	0.003	0.003	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.982	1.012	17.483	-0.037	-0.037	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.044	-0.024	21.202	0.010	0.010	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.880	0.935	23.992	-0.051	-0.051	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.066	0.038	27.467	0.006	0.006	0.000	0.000	0.000	0.000
12	A	13	THR	0	-0.012	0.001	29.946	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.855	-0.908	24.370	0.084	0.084	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.775	-0.876	26.559	0.105	0.105	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.954	0.978	23.666	-0.082	-0.082	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.042	0.008	22.234	0.017	0.017	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.822	0.910	22.202	-0.082	-0.082	0.000	0.000	0.000	0.000
18	A	19	VAL	0	0.044	0.023	19.097	0.013	0.013	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.910	0.974	17.649	-0.198	-0.198	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.962	0.971	17.142	-0.117	-0.117	0.000	0.000	0.000	0.000
21	A	22	ALA	0	0.026	0.022	17.489	0.018	0.018	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.005	0.008	12.233	0.017	0.017	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.039	-0.028	12.984	0.043	0.043	0.000	0.000	0.000	0.000
24	A	25	ASN	0	-0.043	-0.025	14.129	0.036	0.036	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.023	-0.003	10.420	0.001	0.001	0.000	0.000	0.000	0.000
26	A	27	PHE	0	-0.009	-0.014	6.335	0.080	0.080	0.000	0.000	0.000	0.000
27	A	28	PRO	0	0.034	0.015	9.978	0.015	0.015	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.852	0.920	8.623	-0.788	-0.788	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.029	0.000	9.508	0.036	0.036	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.877	0.943	10.415	-0.687	-0.687	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.033	-0.015	12.544	-0.018	-0.018	0.000	0.000	0.000	0.000
32	A	33	THR	0	0.004	0.002	15.017	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	34	PHE	0	-0.022	-0.037	17.939	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	ILE	0	0.006	0.013	20.065	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.831	-0.922	23.132	0.076	0.076	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.817	0.891	21.574	-0.046	-0.046	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.851	-0.923	27.960	0.023	0.023	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.060	-0.042	30.913	0.001	0.001	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.862	-0.936	31.572	0.043	0.043	0.000	0.000	0.000	0.000
40	A	41	PHE	0	-0.054	-0.021	26.585	0.005	0.005	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.038	0.018	25.021	0.000	0.000	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.930	-0.958	18.920	0.045	0.045	0.000	0.000	0.000	0.000
43	A	44	TRP	0	-0.035	-0.019	16.796	0.012	0.012	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.790	-0.897	14.879	0.046	0.046	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.032	0.001	12.221	0.015	0.015	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.918	0.976	7.514	-0.260	-0.260	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.003	-0.009	5.105	0.022	0.022	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.905	0.951	2.934	-10.002	-7.995	0.233	-0.931	-1.309	0.005
49	A	50	SER	0	-0.084	-0.054	3.098	-0.799	0.125	0.210	-0.426	-0.708	-0.004
50	A	51	VAL	0	0.089	0.020	2.751	-1.025	-0.156	0.378	-0.223	-1.023	0.001
51	A	52	GLU	-1	-0.763	-0.845	5.404	0.716	0.716	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.899	0.953	8.454	-0.370	-0.370	0.000	0.000	0.000	0.000
53	A	54	LEU	0	0.047	0.025	6.871	-0.069	-0.069	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.798	0.878	4.948	-0.440	-0.440	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.824	-0.911	10.053	0.259	0.259	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.005	0.023	13.214	-0.041	-0.041	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.004	-0.001	9.992	-0.037	-0.037	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.790	0.891	10.182	-0.197	-0.197	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.034	-0.032	15.757	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	61	GLN	0	-0.017	-0.015	17.298	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.025	-0.004	18.461	-0.014	-0.014	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.020	0.021	15.766	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	64	LEU	0	-0.007	-0.007	12.898	0.003	0.003	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.865	-0.933	14.445	0.014	0.014	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.049	0.019	16.586	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.019	0.009	11.966	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.783	0.884	11.709	0.115	0.115	0.000	0.000	0.000	0.000
68	A	69	MET	0	0.008	0.030	13.127	-0.031	-0.031	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.020	-0.015	12.869	-0.016	-0.016	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.005	-0.003	7.484	-0.023	-0.023	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.743	-0.850	11.090	-0.209	-0.209	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.866	0.928	13.283	0.028	0.028	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.009	0.004	13.079	0.002	0.002	0.000	0.000	0.000	0.000
74	A	75	MET	0	-0.073	-0.029	10.627	-0.034	-0.034	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.077	-0.052	11.156	0.028	0.028	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.853	-0.924	11.542	-0.557	-0.557	0.000	0.000	0.000	0.000
77	A	78	ASN	0	0.020	0.009	8.130	-0.155	-0.155	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.011	-0.005	6.966	-0.257	-0.257	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.021	-0.001	6.823	0.121	0.121	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.896	0.951	8.692	0.193	0.193	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.020	-0.001	7.793	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	83	TYR	0	0.024	0.009	13.042	0.004	0.004	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.006	0.004	11.484	0.010	0.010	0.000	0.000	0.000	0.000
84	A	85	ASN	0	-0.001	0.005	15.592	0.004	0.004	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.784	0.850	18.585	-0.073	-0.073	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.037	-0.028	19.555	0.011	0.011	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.014	-0.001	19.683	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.041	0.029	16.194	0.008	0.008	0.000	0.000	0.000	0.000
89	A	90	TYR	0	-0.034	-0.021	17.931	0.015	0.015	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.043	-0.019	20.717	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.013	0.007	18.242	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	ALA	0	-0.028	-0.011	18.022	0.009	0.009	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.024	-0.022	13.078	0.005	0.005	0.000	0.000	0.000	0.000
94	A	95	ASN	0	-0.004	-0.019	15.813	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	96	PHE	0	0.023	0.000	11.817	0.009	0.009	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.824	-0.864	17.127	0.054	0.054	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.014	-0.014	19.225	0.011	0.011	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.720	-0.851	21.087	0.075	0.075	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.034	0.008	23.442	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	101	HIS	0	0.026	0.015	24.388	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.026	-0.013	22.122	0.003	0.003	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.008	0.008	18.503	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.060	-0.019	12.864	0.002	0.002	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.010	-0.011	14.133	-0.015	-0.015	0.000	0.000	0.000	0.000
105	A	106	VAL	0	0.000	-0.003	7.954	0.039	0.039	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.907	0.955	8.539	0.047	0.047	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.016	-0.003	2.817	-0.796	0.073	0.529	-0.187	-1.211	0.000
108	A	109	LEU	0	0.009	0.002	4.176	-0.256	0.066	-0.001	-0.051	-0.269	0.000
109	A	110	ALA	0	0.016	0.003	2.562	-3.920	-1.240	1.732	-2.238	-2.175	-0.024
110	A	111	ASP	-1	-0.846	-0.932	2.143	-12.546	-10.233	3.452	-3.018	-2.747	-0.041
111	A	112	GLU	-1	-0.920	-0.971	4.575	-0.642	-0.597	-0.001	-0.006	-0.038	0.000
112	A	113	ASN	0	-0.066	-0.024	6.012	0.641	0.641	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.922	-0.962	2.917	-2.991	-2.360	0.050	-0.212	-0.469	-0.001
114	A	115	ASP	-1	-0.813	-0.892	6.093	-0.313	-0.313	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.024	0.016	5.640	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	117	MET	0	0.051	0.022	6.711	0.247	0.247	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.834	0.912	7.332	0.953	0.953	0.000	0.000	0.000	0.000
118	A	119	ILE	0	0.064	0.032	2.327	0.262	-0.624	4.115	-0.526	-2.703	0.000
119	A	120	ILE	0	-0.021	-0.016	4.651	0.352	0.396	-0.001	-0.005	-0.038	0.000
120	A	121	LYS	1	0.800	0.886	7.614	0.461	0.461	0.000	0.000	0.000	0.000
121	A	122	ASP	-1	-0.766	-0.858	4.987	0.151	0.210	-0.001	0.000	-0.057	0.000
122	A	123	ILE	0	-0.007	-0.008	2.836	-0.336	0.069	0.099	-0.094	-0.410	0.001
123	A	124	ALA	0	0.005	0.015	7.206	0.012	0.012	0.000	0.000	0.000	0.000
124	A	125	PRO	0	0.007	0.022	10.660	-0.052	-0.052	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.854	0.902	13.118	0.127	0.127	0.000	0.000	0.000	0.000
126	A	127	THR	0	0.009	0.000	16.502	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.928	0.961	19.533	0.039	0.039	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.061	0.045	23.389	0.001	0.001	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.024	0.019	21.052	0.004	0.004	0.000	0.000	0.000	0.000
130	A	131	VAL	0	0.002	-0.004	19.950	0.008	0.008	0.000	0.000	0.000	0.000
131	A	132	ILE	0	0.016	-0.006	14.526	-0.010	-0.010	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.032	-0.001	18.031	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	134	ASN	0	-0.012	-0.006	14.567	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:2:LEU)