FMO DATABASE

FMODB ID: LZ659

Calculation Name: 5UW8-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5UW8

Chain ID: A

ChEMBL ID:

UniProt ID: P64604

Base Structure: X-ray

Registration Date: 2023-06-26

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	OptAll
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	105
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-736664.194231
FMO2-HF: Nuclear repulsion	697644.305466
FMO2-HF: Total energy	-39019.888765
FMO2-MP2: Total energy	-39136.519906

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:36:THR)

Summations of interaction energy for fragment #1(A:36:THR)

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.
-5.157	-2.497	0.57	-1.4	-1.83	-0.013

Interaction energy analysis for fragmet #1(A:36:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.061 / q_NPA : -0.047

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	38	PRO	0	-0.003	0.006	2.686	-3.875	-1.304	0.571	-1.396	-1.746	-0.013
4	A	39	THR	0	-0.046	-0.025	4.527	0.683	0.772	-0.001	-0.004	-0.084	0.000
5	A	40	TYR	0	-0.045	-0.029	6.663	0.018	0.018	0.000	0.000	0.000	0.000
6	A	41	THR	0	-0.019	-0.021	10.441	0.076	0.076	0.000	0.000	0.000	0.000
7	A	42	LEU	0	-0.004	0.011	12.941	0.024	0.024	0.000	0.000	0.000	0.000
8	A	43	TYR	0	-0.026	-0.012	15.919	0.025	0.025	0.000	0.000	0.000	0.000
9	A	44	ALA	0	0.035	0.023	18.752	0.003	0.003	0.000	0.000	0.000	0.000
10	A	45	THR	0	-0.010	-0.009	21.306	0.000	0.000	0.000	0.000	0.000	0.000
11	A	46	PHE	0	0.010	0.013	21.179	0.003	0.003	0.000	0.000	0.000	0.000
12	A	47	ASP	-1	-0.799	-0.860	26.527	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	48	ASN	0	-0.037	-0.035	28.328	0.008	0.008	0.000	0.000	0.000	0.000
14	A	49	ILE	0	0.052	0.019	22.800	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	50	GLY	0	0.007	0.004	23.839	0.014	0.014	0.000	0.000	0.000	0.000
16	A	51	GLY	0	-0.003	-0.004	23.840	0.000	0.000	0.000	0.000	0.000	0.000
17	A	52	LEU	0	-0.078	-0.021	17.915	0.027	0.027	0.000	0.000	0.000	0.000
18	A	53	LYS	1	0.911	0.942	17.054	-0.314	-0.314	0.000	0.000	0.000	0.000
19	A	54	ALA	0	0.089	0.048	14.419	0.003	0.003	0.000	0.000	0.000	0.000
20	A	55	ARG	1	0.901	0.936	9.437	-0.905	-0.905	0.000	0.000	0.000	0.000
21	A	56	SER	0	-0.016	-0.008	12.295	0.072	0.072	0.000	0.000	0.000	0.000
22	A	57	PRO	0	0.001	0.003	12.088	-0.041	-0.041	0.000	0.000	0.000	0.000
23	A	58	VAL	0	0.027	0.017	12.440	-0.039	-0.039	0.000	0.000	0.000	0.000
24	A	59	SER	0	-0.019	-0.015	13.202	0.010	0.010	0.000	0.000	0.000	0.000
25	A	60	ILE	0	0.061	0.043	15.734	-0.029	-0.029	0.000	0.000	0.000	0.000
26	A	61	GLY	0	0.000	-0.006	18.143	0.023	0.023	0.000	0.000	0.000	0.000
27	A	62	GLY	0	-0.033	-0.009	18.920	0.014	0.014	0.000	0.000	0.000	0.000
28	A	63	VAL	0	0.000	0.002	13.625	0.058	0.058	0.000	0.000	0.000	0.000
29	A	64	VAL	0	-0.035	-0.026	10.180	-0.058	-0.058	0.000	0.000	0.000	0.000
30	A	65	VAL	0	0.011	0.012	10.712	0.056	0.056	0.000	0.000	0.000	0.000
31	A	66	GLY	0	0.066	0.024	8.961	-0.216	-0.216	0.000	0.000	0.000	0.000
32	A	67	ARG	1	0.751	0.854	5.104	-0.194	-0.194	0.000	0.000	0.000	0.000
33	A	68	VAL	0	0.041	0.026	10.888	-0.111	-0.111	0.000	0.000	0.000	0.000
34	A	69	ALA	0	-0.044	-0.015	11.252	0.086	0.086	0.000	0.000	0.000	0.000
35	A	70	ASP	-1	-0.846	-0.939	12.508	0.007	0.007	0.000	0.000	0.000	0.000
36	A	71	ILE	0	-0.049	-0.015	16.184	-0.008	-0.008	0.000	0.000	0.000	0.000
37	A	72	THR	0	-0.016	-0.008	19.819	0.006	0.006	0.000	0.000	0.000	0.000
38	A	73	LEU	0	-0.020	-0.002	22.645	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	74	ASP	-1	-0.713	-0.830	26.382	-0.077	-0.077	0.000	0.000	0.000	0.000
40	A	75	PRO	0	-0.024	-0.020	26.863	0.007	0.007	0.000	0.000	0.000	0.000
41	A	76	LYS	1	0.861	0.920	29.875	0.064	0.064	0.000	0.000	0.000	0.000
42	A	77	THR	0	-0.020	-0.019	30.377	0.004	0.004	0.000	0.000	0.000	0.000
43	A	78	TYR	0	-0.053	-0.021	30.291	0.007	0.007	0.000	0.000	0.000	0.000
44	A	79	LEU	0	0.058	0.035	28.617	0.008	0.008	0.000	0.000	0.000	0.000
45	A	80	PRO	0	-0.021	-0.016	24.978	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	81	ARG	1	0.874	0.935	20.938	0.089	0.089	0.000	0.000	0.000	0.000
47	A	82	VAL	0	-0.031	-0.016	17.339	0.018	0.018	0.000	0.000	0.000	0.000
48	A	83	THR	0	0.009	0.008	14.247	-0.029	-0.029	0.000	0.000	0.000	0.000
49	A	84	LEU	0	-0.040	-0.025	13.462	0.062	0.062	0.000	0.000	0.000	0.000
50	A	85	GLU	-1	-0.768	-0.847	6.953	-0.544	-0.544	0.000	0.000	0.000	0.000
51	A	86	ILE	0	0.000	0.000	9.992	0.152	0.152	0.000	0.000	0.000	0.000
52	A	87	GLU	-1	-0.772	-0.883	5.996	-0.254	-0.254	0.000	0.000	0.000	0.000
53	A	88	GLN	0	-0.037	-0.046	7.590	0.313	0.313	0.000	0.000	0.000	0.000
54	A	89	ARG	1	0.753	0.858	7.581	0.011	0.011	0.000	0.000	0.000	0.000
55	A	90	TYR	0	-0.015	-0.010	10.909	0.153	0.153	0.000	0.000	0.000	0.000
56	A	91	ASN	0	0.011	0.023	13.287	0.090	0.090	0.000	0.000	0.000	0.000
57	A	92	HIS	0	-0.029	-0.028	14.682	0.050	0.050	0.000	0.000	0.000	0.000
58	A	93	ILE	0	-0.021	0.006	15.063	0.049	0.049	0.000	0.000	0.000	0.000
59	A	94	PRO	0	0.057	0.036	18.923	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	95	ASP	-1	-0.861	-0.936	21.993	-0.136	-0.136	0.000	0.000	0.000	0.000
61	A	96	THR	0	-0.026	-0.019	23.552	0.009	0.009	0.000	0.000	0.000	0.000
62	A	97	SER	0	-0.046	-0.042	21.490	0.022	0.022	0.000	0.000	0.000	0.000
63	A	98	SER	0	-0.012	0.002	23.332	0.005	0.005	0.000	0.000	0.000	0.000
64	A	99	LEU	0	-0.009	-0.009	18.247	0.007	0.007	0.000	0.000	0.000	0.000
65	A	100	SER	0	-0.066	-0.053	22.057	0.003	0.003	0.000	0.000	0.000	0.000
66	A	101	ILE	0	-0.018	0.030	21.947	0.013	0.013	0.000	0.000	0.000	0.000
67	A	102	ARG	1	0.834	0.921	21.999	-0.067	-0.067	0.000	0.000	0.000	0.000
68	A	103	THR	0	0.029	0.011	22.222	0.010	0.010	0.000	0.000	0.000	0.000
69	A	104	SER	0	0.004	0.011	20.776	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	105	GLY	0	0.021	-0.011	22.908	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	106	LEU	0	-0.016	-0.007	23.311	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	107	LEU	0	-0.001	-0.002	21.846	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	108	GLY	0	-0.007	0.009	25.313	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	109	GLU	-1	-0.877	-0.925	19.686	0.320	0.320	0.000	0.000	0.000	0.000
75	A	110	GLN	0	-0.004	-0.020	20.921	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	111	TYR	0	-0.045	-0.019	16.890	0.026	0.026	0.000	0.000	0.000	0.000
77	A	112	LEU	0	0.029	0.014	16.912	-0.022	-0.022	0.000	0.000	0.000	0.000
78	A	113	ALA	0	-0.013	-0.004	17.541	0.005	0.005	0.000	0.000	0.000	0.000
79	A	114	LEU	0	0.031	0.012	16.349	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	115	ASN	0	-0.059	-0.032	19.589	0.025	0.025	0.000	0.000	0.000	0.000
81	A	116	VAL	0	0.036	0.004	19.637	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	117	GLY	0	0.029	0.026	22.221	0.015	0.015	0.000	0.000	0.000	0.000
83	A	118	PHE	0	-0.045	-0.016	25.105	0.002	0.002	0.000	0.000	0.000	0.000
84	A	119	GLU	-1	-0.867	-0.945	25.197	-0.138	-0.138	0.000	0.000	0.000	0.000
85	A	120	ASP	-1	-0.853	-0.935	28.873	-0.049	-0.049	0.000	0.000	0.000	0.000
86	A	121	PRO	0	-0.036	-0.030	32.154	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	122	GLU	-1	-0.951	-0.965	33.276	-0.062	-0.062	0.000	0.000	0.000	0.000
88	A	123	LEU	0	-0.106	-0.048	32.680	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	124	GLY	0	-0.026	-0.001	30.489	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	125	THR	0	-0.028	-0.013	24.912	0.004	0.004	0.000	0.000	0.000	0.000
91	A	126	ALA	0	0.015	0.018	25.556	-0.020	-0.020	0.000	0.000	0.000	0.000
92	A	127	ILE	0	-0.057	-0.017	19.476	0.002	0.002	0.000	0.000	0.000	0.000
93	A	128	LEU	0	-0.045	-0.016	18.270	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	129	LYS	1	0.818	0.889	17.296	0.223	0.223	0.000	0.000	0.000	0.000
95	A	130	ASP	-1	-0.840	-0.919	13.566	-0.638	-0.638	0.000	0.000	0.000	0.000
96	A	131	GLY	0	-0.019	-0.003	15.589	0.027	0.027	0.000	0.000	0.000	0.000
97	A	132	ASP	-1	-0.798	-0.876	17.780	-0.222	-0.222	0.000	0.000	0.000	0.000
98	A	133	THR	0	-0.059	-0.053	19.137	0.003	0.003	0.000	0.000	0.000	0.000
99	A	134	ILE	0	0.007	0.014	18.657	0.007	0.007	0.000	0.000	0.000	0.000
100	A	135	GLN	0	-0.032	-0.021	22.267	0.009	0.009	0.000	0.000	0.000	0.000
101	A	136	ASP	-1	-0.868	-0.923	25.811	-0.038	-0.038	0.000	0.000	0.000	0.000
102	A	137	THR	0	-0.039	-0.030	23.265	0.007	0.007	0.000	0.000	0.000	0.000
103	A	138	LYS	1	0.907	0.945	25.329	0.011	0.011	0.000	0.000	0.000	0.000
104	A	139	SER	0	0.002	-0.044	25.739	0.007	0.007	0.000	0.000	0.000	0.000
105	A	140	ALA	0	-0.035	0.002	26.037	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:36:THR)