FMO DATABASE

FMODB ID: R5G38

Calculation Name: 1U0S-A-Xray372

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: 2023-06-20

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	OptH
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	86
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-620188.285603
FMO2-HF: Nuclear repulsion	585955.926924
FMO2-HF: Total energy	-34232.358679
FMO2-MP2: Total energy	-34334.573524

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.
-0.335	0.584	0.008	-0.535	-0.393	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 : -0.013 / q_NPA : -0.017

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	0.907	0.954	3.779	-0.132	0.787	0.008	-0.535	-0.393	0.001
4	A	178	THR	0	0.022	0.027	6.494	0.383	0.383	0.000	0.000	0.000	0.000
5	A	179	PHE	0	-0.033	-0.021	9.568	-0.082	-0.082	0.000	0.000	0.000	0.000
6	A	180	TYR	0	-0.083	-0.047	12.915	0.051	0.051	0.000	0.000	0.000	0.000
7	A	181	ILE	0	-0.002	-0.021	15.867	-0.037	-0.037	0.000	0.000	0.000	0.000
8	A	182	LYS	1	0.914	0.974	18.969	0.070	0.070	0.000	0.000	0.000	0.000
9	A	183	VAL	0	-0.020	-0.012	22.736	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	184	ILE	0	0.028	0.013	25.053	0.009	0.009	0.000	0.000	0.000	0.000
11	A	185	LEU	0	-0.040	-0.034	28.586	-0.006	-0.006	0.000	0.000	0.000	0.000
12	A	186	LYS	1	0.913	0.973	31.452	0.059	0.059	0.000	0.000	0.000	0.000
13	A	187	GLU	-1	-0.806	-0.902	34.920	-0.023	-0.023	0.000	0.000	0.000	0.000
14	A	188	GLY	0	-0.025	0.009	37.821	0.002	0.002	0.000	0.000	0.000	0.000
15	A	189	THR	0	-0.067	-0.038	33.140	0.000	0.000	0.000	0.000	0.000	0.000
16	A	190	GLN	0	0.013	0.006	36.535	0.002	0.002	0.000	0.000	0.000	0.000
17	A	191	LEU	0	-0.016	-0.007	35.757	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	192	LYS	1	0.937	0.983	32.686	0.010	0.010	0.000	0.000	0.000	0.000
19	A	193	SER	0	0.032	0.017	30.982	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	194	ALA	0	0.005	0.008	30.088	0.000	0.000	0.000	0.000	0.000	0.000
21	A	195	ARG	1	0.872	0.947	29.518	0.044	0.044	0.000	0.000	0.000	0.000
22	A	196	ILE	0	0.033	0.005	25.638	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	197	TYR	0	0.024	0.020	25.514	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	198	LEU	0	-0.009	-0.011	25.288	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	199	VAL	0	-0.013	-0.005	21.419	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	200	PHE	0	0.020	-0.004	21.046	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	201	HIS	0	-0.006	0.007	20.699	0.009	0.009	0.000	0.000	0.000	0.000
28	A	202	LYS	1	0.851	0.932	20.092	0.117	0.117	0.000	0.000	0.000	0.000
29	A	203	LEU	0	-0.016	-0.021	15.920	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	204	GLU	-1	-0.882	-0.933	16.035	0.035	0.035	0.000	0.000	0.000	0.000
31	A	205	GLU	-1	-0.911	-0.938	16.975	-0.119	-0.119	0.000	0.000	0.000	0.000
32	A	206	LEU	0	-0.114	-0.066	14.200	-0.026	-0.026	0.000	0.000	0.000	0.000
33	A	207	LYS	1	0.891	0.936	11.525	0.113	0.113	0.000	0.000	0.000	0.000
34	A	208	CYS	0	-0.080	-0.021	11.817	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	209	GLU	-1	-0.900	-0.937	12.372	0.515	0.515	0.000	0.000	0.000	0.000
36	A	210	VAL	0	-0.007	-0.016	13.740	-0.027	-0.027	0.000	0.000	0.000	0.000
37	A	211	VAL	0	-0.009	0.004	12.617	0.028	0.028	0.000	0.000	0.000	0.000
38	A	212	ARG	1	0.880	0.916	15.879	-0.133	-0.133	0.000	0.000	0.000	0.000
39	A	213	THR	0	-0.027	-0.030	19.000	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	214	ILE	0	-0.036	0.029	21.877	0.011	0.011	0.000	0.000	0.000	0.000
41	A	215	PRO	0	0.044	0.015	25.049	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	216	SER	0	0.005	-0.011	25.740	0.002	0.002	0.000	0.000	0.000	0.000
43	A	217	VAL	0	0.052	-0.001	23.625	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	218	GLU	-1	-0.869	-0.935	26.477	0.035	0.035	0.000	0.000	0.000	0.000
45	A	219	GLU	-1	-0.832	-0.915	30.020	0.025	0.025	0.000	0.000	0.000	0.000
46	A	220	ILE	0	-0.084	-0.029	25.443	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	221	GLU	-1	-0.965	-0.990	28.383	0.030	0.030	0.000	0.000	0.000	0.000
48	A	222	GLU	-1	-0.893	-0.926	31.353	0.026	0.026	0.000	0.000	0.000	0.000
49	A	223	GLU	-1	-0.908	-0.977	33.150	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	224	LYS	1	0.837	0.923	33.527	-0.026	-0.026	0.000	0.000	0.000	0.000
51	A	225	PHE	0	-0.033	-0.032	31.012	0.001	0.001	0.000	0.000	0.000	0.000
52	A	226	GLU	-1	-0.924	-0.957	32.727	-0.013	-0.013	0.000	0.000	0.000	0.000
53	A	227	ASN	0	0.014	-0.012	32.650	0.001	0.001	0.000	0.000	0.000	0.000
54	A	228	GLU	-1	-0.911	-0.961	27.716	-0.043	-0.043	0.000	0.000	0.000	0.000
55	A	229	VAL	0	0.011	0.016	23.816	0.007	0.007	0.000	0.000	0.000	0.000
56	A	230	GLU	-1	-0.888	-0.923	22.035	-0.039	-0.039	0.000	0.000	0.000	0.000
57	A	231	LEU	0	-0.010	-0.013	18.688	0.015	0.015	0.000	0.000	0.000	0.000
58	A	232	PHE	0	-0.027	-0.005	12.035	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	233	VAL	0	0.026	0.007	12.768	0.042	0.042	0.000	0.000	0.000	0.000
60	A	234	ILE	0	0.043	0.026	7.544	-0.098	-0.098	0.000	0.000	0.000	0.000
61	A	235	SER	0	-0.026	-0.044	8.626	0.100	0.100	0.000	0.000	0.000	0.000
62	A	236	PRO	0	0.007	0.000	6.776	-0.489	-0.489	0.000	0.000	0.000	0.000
63	A	237	VAL	0	-0.025	0.003	7.828	-0.241	-0.241	0.000	0.000	0.000	0.000
64	A	238	ASH	0	-0.210	-0.185	9.713	-0.080	-0.080	0.000	0.000	0.000	0.000
65	A	239	LEU	0	0.064	0.022	10.941	0.104	0.104	0.000	0.000	0.000	0.000
66	A	240	GLU	-1	-0.731	-0.786	13.961	-0.464	-0.464	0.000	0.000	0.000	0.000
67	A	241	LYS	1	1.030	1.020	14.193	0.443	0.443	0.000	0.000	0.000	0.000
68	A	242	LEU	0	0.021	0.007	13.111	0.057	0.057	0.000	0.000	0.000	0.000
69	A	243	SER	0	0.016	-0.037	15.836	0.060	0.060	0.000	0.000	0.000	0.000
70	A	244	GLH	0	0.367	0.479	18.892	0.040	0.040	0.000	0.000	0.000	0.000
71	A	245	ALA	0	-0.361	-0.400	18.400	0.015	0.015	0.000	0.000	0.000	0.000
72	A	246	LEU	0	0.015	-0.032	18.255	0.027	0.027	0.000	0.000	0.000	0.000
73	A	247	SER	0	-0.097	-0.032	21.529	0.020	0.020	0.000	0.000	0.000	0.000
74	A	248	SER	0	-0.065	-0.052	23.530	0.014	0.014	0.000	0.000	0.000	0.000
75	A	249	ILE	0	-0.019	0.009	23.372	0.011	0.011	0.000	0.000	0.000	0.000
76	A	250	ALA	0	0.002	-0.002	27.031	0.000	0.000	0.000	0.000	0.000	0.000
77	A	251	ASP	-1	-0.870	-0.986	30.407	-0.042	-0.042	0.000	0.000	0.000	0.000
78	A	252	ILE	0	0.033	0.018	26.062	0.005	0.005	0.000	0.000	0.000	0.000
79	A	253	GLU	-1	-1.055	-1.012	29.869	-0.057	-0.057	0.000	0.000	0.000	0.000
80	A	254	ARG	1	0.952	0.965	26.219	0.087	0.087	0.000	0.000	0.000	0.000
81	A	255	VAL	0	0.059	0.043	21.215	0.007	0.007	0.000	0.000	0.000	0.000
82	A	256	ILE	0	-0.083	-0.036	21.274	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	257	ILE	0	0.037	0.023	15.952	0.005	0.005	0.000	0.000	0.000	0.000
84	A	258	LYS	1	0.931	0.952	16.683	0.118	0.118	0.000	0.000	0.000	0.000
85	A	259	GLU	-1	-0.879	-0.927	9.256	-0.755	-0.755	0.000	0.000	0.000	0.000
86	A	260	VAL	0	-0.013	0.000	10.243	0.020	0.020	0.000	0.000	0.000	0.000

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