FMO DATABASE

FMODB ID: 1JQMZ

Calculation Name: 1U0S-A-Xray315

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U0S

Chain ID: A

ChEMBL ID:

UniProt ID: Q56310

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	86
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-620013.430211
FMO2-HF: Nuclear repulsion	585781.739135
FMO2-HF: Total energy	-34231.691077
FMO2-MP2: Total energy	-34333.906296

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:175:GLY )

Summations of interaction energy for fragment #1(A:175:GLY )

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.
-0.586	0.349	0.011	-0.543	-0.404	0.001

Interaction energy analysis for fragmet #1(A:175:GLY )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.020

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

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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	177	LYS	1	0.904	0.952	3.779	-0.216	0.719	0.011	-0.543	-0.404	0.001
4	A	178	THR	0	0.009	0.013	6.494	0.400	0.400	0.000	0.000	0.000	0.000
5	A	179	PHE	0	-0.027	-0.013	9.568	-0.085	-0.085	0.000	0.000	0.000	0.000
6	A	180	TYR	0	-0.077	-0.044	12.915	0.057	0.057	0.000	0.000	0.000	0.000
7	A	181	ILE	0	-0.007	-0.023	15.868	-0.036	-0.036	0.000	0.000	0.000	0.000
8	A	182	LYS	1	0.910	0.972	18.969	0.073	0.073	0.000	0.000	0.000	0.000
9	A	183	VAL	0	-0.023	-0.013	22.736	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	184	ILE	0	0.029	0.013	25.053	0.009	0.009	0.000	0.000	0.000	0.000
11	A	185	LEU	0	-0.039	-0.034	28.586	-0.006	-0.006	0.000	0.000	0.000	0.000
12	A	186	LYS	1	0.908	0.970	31.452	0.059	0.059	0.000	0.000	0.000	0.000
13	A	187	GLU	-1	-0.804	-0.901	34.920	-0.023	-0.023	0.000	0.000	0.000	0.000
14	A	188	GLY	0	-0.028	0.008	37.821	0.002	0.002	0.000	0.000	0.000	0.000
15	A	189	THR	0	-0.066	-0.037	33.140	0.000	0.000	0.000	0.000	0.000	0.000
16	A	190	GLN	0	0.013	0.005	36.535	0.002	0.002	0.000	0.000	0.000	0.000
17	A	191	LEU	0	-0.018	-0.008	35.757	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	192	LYS	1	0.938	0.984	32.686	0.010	0.010	0.000	0.000	0.000	0.000
19	A	193	SER	0	0.034	0.018	30.982	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	194	ALA	0	0.005	0.007	30.088	0.000	0.000	0.000	0.000	0.000	0.000
21	A	195	ARG	1	0.870	0.946	29.518	0.043	0.043	0.000	0.000	0.000	0.000
22	A	196	ILE	0	0.034	0.007	25.638	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	197	TYR	0	0.023	0.019	25.514	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	198	LEU	0	-0.012	-0.013	25.288	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	199	VAL	0	-0.008	-0.003	21.420	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	200	PHE	0	0.019	-0.004	21.046	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	201	HIS	0	-0.009	0.005	20.700	0.009	0.009	0.000	0.000	0.000	0.000
28	A	202	LYS	1	0.849	0.930	20.092	0.114	0.114	0.000	0.000	0.000	0.000
29	A	203	LEU	0	-0.013	-0.020	15.920	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	204	GLU	-1	-0.878	-0.931	16.035	0.041	0.041	0.000	0.000	0.000	0.000
31	A	205	GLU	-1	-0.916	-0.940	16.975	-0.115	-0.115	0.000	0.000	0.000	0.000
32	A	206	LEU	0	-0.114	-0.066	14.199	-0.026	-0.026	0.000	0.000	0.000	0.000
33	A	207	LYS	1	0.887	0.934	11.525	0.105	0.105	0.000	0.000	0.000	0.000
34	A	208	CYS	0	-0.077	-0.019	11.818	0.000	0.000	0.000	0.000	0.000	0.000
35	A	209	GLU	-1	-0.903	-0.939	12.372	0.518	0.518	0.000	0.000	0.000	0.000
36	A	210	VAL	0	-0.009	-0.016	13.740	-0.029	-0.029	0.000	0.000	0.000	0.000
37	A	211	VAL	0	-0.006	0.006	12.618	0.030	0.030	0.000	0.000	0.000	0.000
38	A	212	ARG	1	0.877	0.916	15.879	-0.130	-0.130	0.000	0.000	0.000	0.000
39	A	213	THR	0	-0.029	-0.031	19.000	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	214	ILE	0	-0.037	0.028	21.877	0.011	0.011	0.000	0.000	0.000	0.000
41	A	215	PRO	0	0.041	0.011	25.049	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	216	SER	0	0.006	-0.009	25.740	0.003	0.003	0.000	0.000	0.000	0.000
43	A	217	VAL	0	0.057	0.001	23.625	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	218	GLU	-1	-0.874	-0.937	26.477	0.034	0.034	0.000	0.000	0.000	0.000
45	A	219	GLU	-1	-0.833	-0.916	30.020	0.024	0.024	0.000	0.000	0.000	0.000
46	A	220	ILE	0	-0.080	-0.025	25.444	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	221	GLU	-1	-0.965	-0.989	28.383	0.030	0.030	0.000	0.000	0.000	0.000
48	A	222	GLU	-1	-0.898	-0.928	31.353	0.026	0.026	0.000	0.000	0.000	0.000
49	A	223	GLU	-1	-0.910	-0.978	33.150	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	224	LYS	1	0.836	0.923	33.527	-0.025	-0.025	0.000	0.000	0.000	0.000
51	A	225	PHE	0	-0.030	-0.031	31.012	0.001	0.001	0.000	0.000	0.000	0.000
52	A	226	GLU	-1	-0.928	-0.959	32.727	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	227	ASN	0	0.012	-0.013	32.650	0.001	0.001	0.000	0.000	0.000	0.000
54	A	228	GLU	-1	-0.912	-0.961	27.716	-0.045	-0.045	0.000	0.000	0.000	0.000
55	A	229	VAL	0	0.010	0.014	23.816	0.007	0.007	0.000	0.000	0.000	0.000
56	A	230	GLU	-1	-0.893	-0.924	22.035	-0.041	-0.041	0.000	0.000	0.000	0.000
57	A	231	LEU	0	-0.012	-0.016	18.688	0.016	0.016	0.000	0.000	0.000	0.000
58	A	232	PHE	0	-0.016	0.003	12.035	-0.021	-0.021	0.000	0.000	0.000	0.000
59	A	233	VAL	0	0.015	0.001	12.769	0.044	0.044	0.000	0.000	0.000	0.000
60	A	234	ILE	0	0.051	0.033	7.544	-0.094	-0.094	0.000	0.000	0.000	0.000
61	A	235	SER	0	-0.025	-0.045	8.627	0.100	0.100	0.000	0.000	0.000	0.000
62	A	236	PRO	0	0.001	-0.003	6.776	-0.491	-0.491	0.000	0.000	0.000	0.000
63	A	237	VAL	0	-0.035	-0.002	7.828	-0.240	-0.240	0.000	0.000	0.000	0.000
64	A	238	ASH	0	-0.202	-0.182	9.713	-0.079	-0.079	0.000	0.000	0.000	0.000
65	A	239	LEU	0	0.070	0.026	10.941	0.111	0.111	0.000	0.000	0.000	0.000
66	A	240	GLU	-1	-0.734	-0.788	13.961	-0.457	-0.457	0.000	0.000	0.000	0.000
67	A	241	LYS	1	1.024	1.017	14.193	0.441	0.441	0.000	0.000	0.000	0.000
68	A	242	LEU	0	0.024	0.009	13.111	0.059	0.059	0.000	0.000	0.000	0.000
69	A	243	SER	0	0.018	-0.037	15.836	0.062	0.062	0.000	0.000	0.000	0.000
70	A	244	GLH	0	0.362	0.477	18.892	0.041	0.041	0.000	0.000	0.000	0.000
71	A	245	ALA	0	-0.362	-0.407	18.402	0.016	0.016	0.000	0.000	0.000	0.000
72	A	246	LEU	0	0.017	-0.023	18.236	0.028	0.028	0.000	0.000	0.000	0.000
73	A	247	SER	0	-0.096	-0.031	21.529	0.021	0.021	0.000	0.000	0.000	0.000
74	A	248	SER	0	-0.068	-0.054	23.529	0.015	0.015	0.000	0.000	0.000	0.000
75	A	249	ILE	0	-0.022	0.009	23.373	0.012	0.012	0.000	0.000	0.000	0.000
76	A	250	ALA	0	0.001	-0.003	27.031	0.000	0.000	0.000	0.000	0.000	0.000
77	A	251	ASP	-1	-0.872	-0.988	30.407	-0.042	-0.042	0.000	0.000	0.000	0.000
78	A	252	ILE	0	0.034	0.019	26.062	0.005	0.005	0.000	0.000	0.000	0.000
79	A	253	GLU	-1	-1.056	-1.014	29.869	-0.058	-0.058	0.000	0.000	0.000	0.000
80	A	254	ARG	1	0.948	0.964	26.219	0.089	0.089	0.000	0.000	0.000	0.000
81	A	255	VAL	0	0.060	0.043	21.215	0.007	0.007	0.000	0.000	0.000	0.000
82	A	256	ILE	0	-0.087	-0.038	21.274	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	257	ILE	0	0.032	0.019	15.952	0.005	0.005	0.000	0.000	0.000	0.000
84	A	258	LYS	1	0.920	0.945	16.683	0.123	0.123	0.000	0.000	0.000	0.000
85	A	259	GLU	-1	-0.896	-0.939	9.256	-0.778	-0.778	0.000	0.000	0.000	0.000
86	A	260	VAL	-1	-0.902	-0.936	10.243	-0.190	-0.190	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:175:GLY )