FMO DATABASE

FMODB ID: Q1J4Y

Calculation Name: 1PXU-A-Xray372

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: 2023-06-19

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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1202262.194146
FMO2-HF: Nuclear repulsion	1148046.339188
FMO2-HF: Total energy	-54215.854958
FMO2-MP2: Total energy	-54370.209501

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.
-0.616	1.077	-0.019	-0.625	-1.049	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 : -0.025 / q_NPA : -0.029

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	-0.019	-0.003	3.801	-0.676	0.935	-0.018	-0.623	-0.970	0.002
4	A	4	GLU	-1	-0.731	-0.863	5.317	0.553	0.635	-0.001	-0.002	-0.079	0.000
5	A	5	ARG	1	0.754	0.869	8.030	0.126	0.126	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.886	-0.952	11.211	-0.612	-0.612	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.015	-0.019	12.851	0.072	0.072	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.049	0.012	15.078	0.019	0.019	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.892	0.931	15.026	0.549	0.549	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.859	0.925	12.313	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.818	-0.912	16.813	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.942	-0.968	20.003	-0.237	-0.237	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.825	-0.880	17.206	-0.331	-0.331	0.000	0.000	0.000	0.000
14	A	14	ALA	0	-0.024	0.000	20.216	0.026	0.026	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.021	-0.028	22.122	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.003	-0.002	24.832	0.006	0.006	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.025	0.022	21.511	0.013	0.013	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.022	0.003	23.454	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.038	0.027	23.133	0.034	0.034	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.032	0.000	24.021	-0.031	-0.031	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.049	-0.029	24.160	0.030	0.030	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.030	0.031	22.063	-0.039	-0.039	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.807	-0.874	25.401	0.238	0.238	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.902	-0.963	28.185	0.221	0.221	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.013	0.020	23.593	0.000	0.000	0.000	0.000	0.000	0.000
26	A	26	MET	0	-0.052	-0.021	26.806	-0.022	-0.022	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.013	-0.002	27.717	0.016	0.016	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.027	-0.003	24.498	0.012	0.012	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.804	-0.867	24.960	0.099	0.099	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.014	-0.038	25.114	0.009	0.009	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.032	-0.004	26.372	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	32	HIS	0	-0.071	-0.055	22.391	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.047	-0.006	20.523	0.036	0.036	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.004	0.019	19.187	0.028	0.028	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.024	-0.030	18.238	-0.030	-0.030	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.000	-0.024	22.595	0.010	0.010	0.000	0.000	0.000	0.000
37	A	37	CYS	0	-0.061	-0.012	23.440	0.032	0.032	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.913	0.965	25.894	-0.206	-0.206	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.014	-0.024	24.408	0.027	0.027	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.875	0.938	27.659	-0.284	-0.284	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.001	-0.011	28.343	0.021	0.021	0.000	0.000	0.000	0.000
42	A	42	TRP	0	-0.054	-0.018	27.588	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.939	0.956	28.558	-0.159	-0.159	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.018	0.002	27.764	0.018	0.018	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.023	-0.012	23.230	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.833	0.903	23.902	0.015	0.015	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.090	0.054	27.662	0.012	0.012	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.925	0.966	29.730	-0.083	-0.083	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.906	-0.951	32.238	0.030	0.030	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.042	0.024	29.536	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.009	-0.012	29.825	0.003	0.003	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.107	-0.071	32.830	0.004	0.004	0.000	0.000	0.000	0.000
53	A	53	HIS	0	-0.020	-0.008	36.303	0.002	0.002	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.939	-0.954	32.938	0.016	0.016	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.069	-0.029	31.314	0.005	0.005	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.039	-0.015	34.852	0.000	0.000	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.015	-0.014	33.657	0.009	0.009	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.837	-0.908	35.113	0.143	0.143	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.000	-0.017	36.165	0.009	0.009	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.032	-0.012	38.048	0.002	0.002	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.031	-0.023	33.860	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.853	0.914	31.694	-0.179	-0.179	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.021	0.020	27.929	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.005	0.007	28.059	0.021	0.021	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.030	-0.006	22.379	-0.017	-0.017	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.115	0.046	23.841	0.026	0.026	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.000	-0.018	20.672	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.023	-0.008	17.958	0.013	0.013	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.010	-0.021	15.913	-0.033	-0.033	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.837	-0.910	16.092	0.087	0.087	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.031	-0.018	13.050	0.058	0.058	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.049	-0.018	11.744	-0.069	-0.069	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.056	-0.008	11.874	-0.132	-0.132	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.835	-0.880	8.667	1.817	1.817	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.042	-0.007	10.649	-0.068	-0.068	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.040	0.033	13.790	-0.173	-0.173	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.031	-0.014	15.770	0.047	0.047	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.013	-0.006	18.759	-0.023	-0.023	0.000	0.000	0.000	0.000
79	A	80	THR	0	0.008	-0.015	21.738	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	81	GLY	0	-0.018	-0.011	24.887	0.018	0.018	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.789	-0.866	19.424	0.746	0.746	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.059	-0.031	21.506	-0.047	-0.047	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.779	0.881	15.982	-0.708	-0.708	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.012	0.007	18.730	-0.062	-0.062	0.000	0.000	0.000	0.000
85	A	86	PHE	0	0.000	-0.022	18.499	0.048	0.048	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.052	0.027	17.486	-0.034	-0.034	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.000	-0.017	19.838	0.008	0.008	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.023	0.014	22.462	-0.025	-0.025	0.000	0.000	0.000	0.000
89	A	90	PRO	0	0.050	0.036	25.355	0.020	0.020	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.010	0.011	27.525	-0.016	-0.016	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.047	0.015	27.368	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	93	GLN	0	0.062	0.015	30.400	0.012	0.012	0.000	0.000	0.000	0.000
93	A	94	TYR	0	-0.031	-0.006	26.446	0.006	0.006	0.000	0.000	0.000	0.000
94	A	95	MET	0	0.001	0.015	24.763	0.008	0.008	0.000	0.000	0.000	0.000
95	A	96	TRP	0	-0.067	-0.017	30.379	0.018	0.018	0.000	0.000	0.000	0.000
96	A	97	PRO	0	-0.007	-0.030	33.556	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.005	-0.006	30.447	0.007	0.007	0.000	0.000	0.000	0.000
98	A	99	HIS	1	0.840	0.883	25.832	-0.123	-0.123	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.946	0.976	30.143	-0.061	-0.061	0.000	0.000	0.000	0.000
100	A	101	ASN	0	-0.029	-0.004	33.188	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.744	-0.830	27.508	0.178	0.178	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.024	-0.006	25.885	-0.019	-0.019	0.000	0.000	0.000	0.000
103	A	104	MET	0	-0.001	-0.006	22.739	0.029	0.029	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.010	-0.004	16.221	-0.020	-0.020	0.000	0.000	0.000	0.000
105	A	106	ASN	0	0.007	0.005	18.222	-0.038	-0.038	0.000	0.000	0.000	0.000
106	A	107	SER	0	0.023	0.005	14.100	-0.069	-0.069	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.014	-0.029	10.616	0.147	0.147	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.031	0.013	12.913	-0.080	-0.080	0.000	0.000	0.000	0.000
109	A	110	MET	0	-0.007	0.006	13.417	0.105	0.105	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.821	0.876	12.279	-1.349	-1.349	0.000	0.000	0.000	0.000
111	A	112	ILE	0	0.051	0.029	17.120	-0.058	-0.058	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.010	-0.003	17.735	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.061	0.013	20.705	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	115	ARG	1	1.009	1.030	17.027	-0.339	-0.339	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.038	-0.030	15.661	-0.039	-0.039	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.034	-0.025	18.901	-0.041	-0.041	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.896	-0.950	22.511	0.141	0.141	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.925	-0.971	16.882	0.178	0.178	0.000	0.000	0.000	0.000
119	A	120	VAL	0	-0.038	-0.023	18.729	-0.042	-0.042	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.936	-0.974	20.980	0.090	0.090	0.000	0.000	0.000	0.000
121	A	122	HIS	0	-0.064	-0.026	23.128	-0.018	-0.018	0.000	0.000	0.000	0.000
122	A	123	CYS	0	0.003	0.003	20.431	-0.041	-0.041	0.000	0.000	0.000	0.000
123	A	124	VAL	0	-0.038	-0.013	22.508	-0.020	-0.020	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.895	-0.933	24.928	-0.021	-0.021	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.832	-0.911	24.781	-0.102	-0.102	0.000	0.000	0.000	0.000
126	A	127	HIS	0	0.008	0.010	24.421	-0.017	-0.017	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.856	0.915	26.454	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.823	0.895	29.069	0.081	0.081	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.085	-0.012	26.554	-0.004	-0.004	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.044	-0.011	31.063	-0.002	-0.002	0.000	0.000	0.000	0.000

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