FMO DATABASE

FMODB ID: Q1G9Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-619966.08105
FMO2-HF: Nuclear repulsion	585732.119439
FMO2-HF: Total energy	-34233.961611
FMO2-MP2: Total energy	-34336.076228

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.
-0.324	0.609	0.008	-0.533	-0.407	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 : -0.014 / 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	0.827	0.894	3.779	-0.148	0.785	0.008	-0.533	-0.407	0.001
4	A	178	THR	0	0.034	0.030	6.494	0.393	0.393	0.000	0.000	0.000	0.000
5	A	179	PHE	0	-0.043	-0.026	9.568	-0.078	-0.078	0.000	0.000	0.000	0.000
6	A	180	TYR	0	-0.051	-0.036	12.915	0.052	0.052	0.000	0.000	0.000	0.000
7	A	181	ILE	0	-0.004	-0.024	15.777	-0.036	-0.036	0.000	0.000	0.000	0.000
8	A	182	LYS	1	0.798	0.893	18.969	0.064	0.064	0.000	0.000	0.000	0.000
9	A	183	VAL	0	-0.004	-0.004	22.736	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	184	ILE	0	0.017	0.004	25.053	0.009	0.009	0.000	0.000	0.000	0.000
11	A	185	LEU	0	-0.041	-0.028	28.586	-0.006	-0.006	0.000	0.000	0.000	0.000
12	A	186	LYS	1	0.939	0.981	31.452	0.059	0.059	0.000	0.000	0.000	0.000
13	A	187	GLU	-1	-0.839	-0.912	34.920	-0.023	-0.023	0.000	0.000	0.000	0.000
14	A	188	GLY	0	-0.031	-0.003	37.821	0.002	0.002	0.000	0.000	0.000	0.000
15	A	189	THR	0	-0.078	-0.056	33.074	0.000	0.000	0.000	0.000	0.000	0.000
16	A	190	GLN	0	0.010	0.004	36.535	0.002	0.002	0.000	0.000	0.000	0.000
17	A	191	LEU	0	-0.018	-0.007	35.823	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	192	LYS	1	0.959	0.985	32.673	0.010	0.010	0.000	0.000	0.000	0.000
19	A	193	SER	0	0.013	-0.019	30.999	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	194	ALA	0	-0.015	-0.006	30.088	0.000	0.000	0.000	0.000	0.000	0.000
21	A	195	ARG	1	0.813	0.909	29.505	0.039	0.039	0.000	0.000	0.000	0.000
22	A	196	ILE	0	0.030	-0.001	25.626	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	197	TYR	0	0.002	-0.002	25.514	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	198	LEU	0	-0.010	-0.009	25.288	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	199	VAL	0	-0.012	-0.007	21.291	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	200	PHE	0	0.024	0.001	21.045	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	201	HIS	0	0.017	0.032	20.717	0.010	0.010	0.000	0.000	0.000	0.000
28	A	202	LYS	1	0.808	0.889	20.084	0.118	0.118	0.000	0.000	0.000	0.000
29	A	203	LEU	0	-0.008	-0.020	15.884	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	204	GLU	-1	-0.875	-0.928	16.052	0.045	0.045	0.000	0.000	0.000	0.000
31	A	205	GLU	-1	-0.857	-0.895	16.991	-0.115	-0.115	0.000	0.000	0.000	0.000
32	A	206	LEU	0	-0.100	-0.056	14.198	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	207	LYS	1	0.837	0.907	11.784	0.121	0.121	0.000	0.000	0.000	0.000
34	A	208	CYS	0	-0.070	-0.016	11.835	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	209	GLU	-1	-0.888	-0.931	12.292	0.521	0.521	0.000	0.000	0.000	0.000
36	A	210	VAL	0	-0.003	-0.015	13.741	-0.026	-0.026	0.000	0.000	0.000	0.000
37	A	211	VAL	0	-0.011	-0.001	12.573	0.027	0.027	0.000	0.000	0.000	0.000
38	A	212	ARG	1	0.887	0.925	15.879	-0.140	-0.140	0.000	0.000	0.000	0.000
39	A	213	THR	0	-0.026	-0.023	19.000	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	214	ILE	0	-0.050	0.022	21.877	0.011	0.011	0.000	0.000	0.000	0.000
41	A	215	PRO	0	0.033	0.011	25.049	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	216	SER	0	0.008	-0.043	25.740	0.003	0.003	0.000	0.000	0.000	0.000
43	A	217	VAL	0	0.046	-0.006	23.560	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	218	GLU	-1	-0.879	-0.934	26.478	0.037	0.037	0.000	0.000	0.000	0.000
45	A	219	GLU	-1	-0.800	-0.887	29.967	0.027	0.027	0.000	0.000	0.000	0.000
46	A	220	ILE	0	-0.068	-0.019	25.470	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	221	GLU	-1	-0.958	-0.986	28.145	0.030	0.030	0.000	0.000	0.000	0.000
48	A	222	GLU	-1	-0.877	-0.937	31.353	0.025	0.025	0.000	0.000	0.000	0.000
49	A	223	GLU	-1	-0.872	-0.923	33.154	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	224	LYS	1	0.785	0.922	33.438	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	225	PHE	0	-0.041	-0.036	30.906	0.001	0.001	0.000	0.000	0.000	0.000
52	A	226	GLU	-1	-0.905	-0.949	32.726	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	227	ASN	0	-0.010	-0.002	32.650	0.000	0.000	0.000	0.000	0.000	0.000
54	A	228	GLU	-1	-0.861	-0.934	27.670	-0.043	-0.043	0.000	0.000	0.000	0.000
55	A	229	VAL	0	0.015	0.025	23.982	0.007	0.007	0.000	0.000	0.000	0.000
56	A	230	GLU	-1	-0.851	-0.893	22.191	-0.044	-0.044	0.000	0.000	0.000	0.000
57	A	231	LEU	0	-0.007	-0.007	18.711	0.015	0.015	0.000	0.000	0.000	0.000
58	A	232	PHE	0	-0.034	-0.010	12.211	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	233	VAL	0	0.028	0.007	12.799	0.041	0.041	0.000	0.000	0.000	0.000
60	A	234	ILE	0	0.040	0.029	7.542	-0.096	-0.096	0.000	0.000	0.000	0.000
61	A	235	SER	0	-0.028	-0.040	8.638	0.106	0.106	0.000	0.000	0.000	0.000
62	A	236	PRO	0	0.009	0.006	6.785	-0.470	-0.470	0.000	0.000	0.000	0.000
63	A	237	VAL	0	-0.022	-0.002	7.843	-0.233	-0.233	0.000	0.000	0.000	0.000
64	A	238	ASH	0	-0.038	-0.063	9.542	-0.040	-0.040	0.000	0.000	0.000	0.000
65	A	239	LEU	0	0.071	0.035	10.941	0.108	0.108	0.000	0.000	0.000	0.000
66	A	240	GLU	-1	-0.757	-0.821	13.961	-0.435	-0.435	0.000	0.000	0.000	0.000
67	A	241	LYS	1	0.891	0.922	14.164	0.449	0.449	0.000	0.000	0.000	0.000
68	A	242	LEU	0	0.015	0.021	13.141	0.054	0.054	0.000	0.000	0.000	0.000
69	A	243	SER	0	0.016	-0.027	15.836	0.060	0.060	0.000	0.000	0.000	0.000
70	A	244	GLH	0	-0.035	-0.007	18.888	0.037	0.037	0.000	0.000	0.000	0.000
71	A	245	ALA	0	0.003	0.015	18.357	0.028	0.028	0.000	0.000	0.000	0.000
72	A	246	LEU	0	0.031	0.016	18.489	0.028	0.028	0.000	0.000	0.000	0.000
73	A	247	SER	0	-0.083	-0.038	21.529	0.019	0.019	0.000	0.000	0.000	0.000
74	A	248	SER	0	-0.081	-0.050	23.497	0.014	0.014	0.000	0.000	0.000	0.000
75	A	249	ILE	0	-0.020	0.006	23.143	0.011	0.011	0.000	0.000	0.000	0.000
76	A	250	ALA	0	0.005	0.001	27.031	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	251	ASP	-1	-0.848	-0.954	30.407	-0.040	-0.040	0.000	0.000	0.000	0.000
78	A	252	ILE	0	0.063	0.031	26.314	0.004	0.004	0.000	0.000	0.000	0.000
79	A	253	GLU	-1	-1.021	-1.003	29.869	-0.056	-0.056	0.000	0.000	0.000	0.000
80	A	254	ARG	1	0.952	0.968	26.302	0.084	0.084	0.000	0.000	0.000	0.000
81	A	255	VAL	0	0.059	0.040	21.247	0.006	0.006	0.000	0.000	0.000	0.000
82	A	256	ILE	0	-0.085	-0.036	21.446	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	257	ILE	0	0.041	0.025	15.930	0.004	0.004	0.000	0.000	0.000	0.000
84	A	258	LYS	1	0.927	0.958	16.683	0.117	0.117	0.000	0.000	0.000	0.000
85	A	259	GLU	-1	-0.790	-0.865	9.112	-0.872	-0.872	0.000	0.000	0.000	0.000
86	A	260	VAL	0	-0.013	0.003	10.243	0.019	0.019	0.000	0.000	0.000	0.000

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