FMO DATABASE

FMODB ID: GQK71

Calculation Name: 1PXU-A-Xray310

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1PXU

Chain ID: A

ChEMBL ID:

UniProt ID: P31696

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1200748.610577
FMO2-HF: Nuclear repulsion	1146534.119068
FMO2-HF: Total energy	-54214.49151
FMO2-MP2: Total energy	-54368.87263

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:ASN )

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

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.
-1.184	0.4	-0.013	-0.587	-0.984	0.002

Interaction energy analysis for fragmet #1(A:1:ASN )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.014 / 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	3	PRO	0	-0.032	-0.007	3.801	-1.135	0.364	-0.013	-0.585	-0.901	0.002
4	A	4	GLU	-1	-0.743	-0.863	5.285	0.747	0.832	0.000	-0.002	-0.083	0.000
5	A	5	ARG	1	0.782	0.885	8.039	0.218	0.218	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.880	-0.946	11.238	-1.082	-1.082	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.027	-0.023	12.876	0.137	0.137	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.087	0.029	15.121	0.016	0.016	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.915	0.962	14.534	0.845	0.845	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.895	0.942	12.607	0.354	0.354	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.845	-0.928	16.838	-0.143	-0.143	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.935	-0.960	20.067	-0.384	-0.384	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.860	-0.911	17.817	-0.463	-0.463	0.000	0.000	0.000	0.000
14	A	14	ALA	0	-0.028	-0.002	20.283	0.047	0.047	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.020	-0.024	22.146	-0.013	-0.013	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.007	-0.003	24.862	0.011	0.011	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.028	0.024	21.605	0.011	0.011	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.028	0.001	23.422	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.037	0.026	23.108	0.035	0.035	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.031	-0.001	23.996	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.061	-0.031	24.141	0.042	0.042	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.031	0.031	22.048	-0.043	-0.043	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.835	-0.911	25.383	0.251	0.251	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.930	-0.974	28.175	0.257	0.257	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.010	0.027	23.563	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	26	MET	0	-0.044	-0.013	26.788	-0.031	-0.031	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.008	-0.003	27.697	0.022	0.022	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.036	0.003	24.640	0.013	0.013	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.842	-0.901	24.910	0.135	0.135	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.020	-0.040	25.090	0.015	0.015	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.026	0.002	26.349	0.000	0.000	0.000	0.000	0.000	0.000
32	A	32	HIS	0	-0.049	-0.031	22.272	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.042	-0.003	20.401	0.051	0.051	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.003	0.020	19.368	0.035	0.035	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.011	-0.045	18.197	-0.043	-0.043	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.028	0.009	22.570	0.006	0.006	0.000	0.000	0.000	0.000
37	A	37	CYS	0	-0.048	-0.014	23.034	0.038	0.038	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.952	0.991	25.872	-0.229	-0.229	0.000	0.000	0.000	0.000
39	A	39	VAL	0	0.001	-0.013	24.396	0.029	0.029	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.876	0.929	27.637	-0.282	-0.282	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.000	-0.008	28.257	0.020	0.020	0.000	0.000	0.000	0.000
42	A	42	TRP	0	-0.059	-0.017	27.572	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.937	0.948	28.538	-0.105	-0.105	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.012	0.001	27.741	0.015	0.015	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.018	-0.012	23.252	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.870	0.924	24.063	0.126	0.126	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.087	0.056	27.712	0.017	0.017	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.929	0.964	29.771	-0.038	-0.038	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.889	-0.946	32.240	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.041	0.025	29.702	0.004	0.004	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.025	-0.015	29.957	0.009	0.009	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.109	-0.065	32.799	0.008	0.008	0.000	0.000	0.000	0.000
53	A	53	HIS	0	-0.022	-0.011	36.274	0.006	0.006	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.952	-0.958	33.288	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.059	-0.023	31.328	0.008	0.008	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.043	-0.018	34.821	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.013	-0.015	33.373	0.012	0.012	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.870	-0.940	35.121	0.149	0.149	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.011	-0.019	36.141	0.008	0.008	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.035	-0.010	38.023	0.001	0.001	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.011	-0.010	33.765	-0.006	-0.006	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.873	0.949	31.669	-0.180	-0.180	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.028	0.021	27.910	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.007	0.010	28.094	0.026	0.026	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.029	-0.003	22.299	-0.023	-0.023	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.097	0.033	23.814	0.035	0.035	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.011	-0.008	20.641	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.031	-0.008	17.936	0.015	0.015	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.015	-0.021	15.907	-0.029	-0.029	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.851	-0.928	16.065	0.170	0.170	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.024	-0.007	13.029	0.073	0.073	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.040	-0.013	11.715	-0.047	-0.047	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.051	-0.005	11.855	-0.186	-0.186	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.851	-0.896	8.636	1.999	1.999	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.028	-0.018	10.626	-0.058	-0.058	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.055	0.050	13.800	-0.209	-0.209	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.039	-0.014	15.752	0.029	0.029	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.006	-0.001	18.744	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	80	THR	0	0.001	-0.017	21.727	-0.020	-0.020	0.000	0.000	0.000	0.000
80	A	81	GLY	0	-0.030	-0.018	24.878	0.022	0.022	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.865	-0.916	19.362	0.782	0.782	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.039	-0.021	21.565	-0.060	-0.060	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.860	0.924	15.896	-0.760	-0.760	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.031	0.022	18.624	-0.060	-0.060	0.000	0.000	0.000	0.000
85	A	86	PHE	0	0.002	-0.028	18.474	0.044	0.044	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.043	0.028	17.842	-0.039	-0.039	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.008	-0.017	19.806	0.017	0.017	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.036	0.017	22.528	-0.032	-0.032	0.000	0.000	0.000	0.000
89	A	90	PRO	0	0.045	0.030	25.344	0.027	0.027	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.012	0.010	27.487	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.047	0.018	27.212	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	93	GLN	0	0.070	0.017	30.365	0.017	0.017	0.000	0.000	0.000	0.000
93	A	94	TYR	0	-0.032	-0.009	26.911	0.012	0.012	0.000	0.000	0.000	0.000
94	A	95	MET	0	0.007	0.014	25.180	0.013	0.013	0.000	0.000	0.000	0.000
95	A	96	TRP	0	-0.070	-0.008	30.346	0.023	0.023	0.000	0.000	0.000	0.000
96	A	97	PRO	0	-0.022	-0.042	33.523	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.001	-0.002	30.397	0.008	0.008	0.000	0.000	0.000	0.000
98	A	99	HIS	1	0.831	0.884	26.141	-0.147	-0.147	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.965	0.986	30.112	-0.067	-0.067	0.000	0.000	0.000	0.000
100	A	101	ASN	0	-0.032	-0.011	33.157	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.808	-0.880	27.771	0.188	0.188	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.018	-0.006	25.809	-0.023	-0.023	0.000	0.000	0.000	0.000
103	A	104	MET	0	0.000	-0.011	22.934	0.037	0.037	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.003	-0.004	16.406	-0.034	-0.034	0.000	0.000	0.000	0.000
105	A	106	ASN	0	-0.004	-0.003	18.440	-0.055	-0.055	0.000	0.000	0.000	0.000
106	A	107	SER	0	0.006	-0.009	14.106	-0.087	-0.087	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.028	-0.048	10.150	0.198	0.198	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.026	0.019	12.883	-0.110	-0.110	0.000	0.000	0.000	0.000
109	A	110	MET	0	-0.003	0.004	13.395	0.106	0.106	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.806	0.876	12.108	-1.363	-1.363	0.000	0.000	0.000	0.000
111	A	112	ILE	0	0.042	0.023	17.106	-0.083	-0.083	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.005	-0.004	17.909	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.075	0.017	20.804	-0.025	-0.025	0.000	0.000	0.000	0.000
114	A	115	ARG	1	1.007	1.019	16.318	-0.110	-0.110	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.013	-0.009	15.540	-0.118	-0.118	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.046	-0.029	18.930	-0.042	-0.042	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.905	-0.953	22.369	-0.019	-0.019	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.946	-0.974	16.406	-0.211	-0.211	0.000	0.000	0.000	0.000
119	A	120	VAL	0	-0.041	-0.025	18.790	-0.045	-0.045	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.947	-0.978	21.047	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	122	HIS	0	-0.036	-0.003	22.979	-0.023	-0.023	0.000	0.000	0.000	0.000
122	A	123	CYS	0	-0.011	-0.002	20.288	-0.043	-0.043	0.000	0.000	0.000	0.000
123	A	124	VAL	0	0.007	0.009	22.561	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.958	-0.992	24.977	-0.108	-0.108	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.867	-0.957	24.829	-0.251	-0.251	0.000	0.000	0.000	0.000
126	A	127	HIS	0	0.001	0.010	24.478	-0.017	-0.017	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.868	0.942	26.488	0.111	0.111	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.834	0.920	29.188	0.225	0.225	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.112	-0.030	26.753	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	131	LEU	-1	-0.965	-0.969	31.089	-0.151	-0.151	0.000	0.000	0.000	0.000

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