FMO DATABASE

FMODB ID: 89MLY

Calculation Name: 4G6T-A-Xray372

Preferred Name:
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Target Type:
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Ligand Name:
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ligand 3-letter code:
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PDB ID: 4G6T

Chain ID: A

ChEMBL ID:
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UniProt ID: Q87UE6

Base Structure: X-ray

Registration Date: 2023-09-23

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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1072123.654389
FMO2-HF: Nuclear repulsion	1020501.539683
FMO2-HF: Total energy	-51622.114706
FMO2-MP2: Total energy	-51769.040274

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:-2:PRO)

Summations of interaction energy for fragment #1(A:-2:PRO)

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.
-1.276	0.887	0.004	-0.958	-1.209	0.001

Interaction energy analysis for fragmet #1(A:-2:PRO)

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 : -0.016

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	0	ASP	-1	-0.801	-0.874	3.535	-3.514	-1.351	0.004	-0.958	-1.209	0.001
4	A	1	MET	0	0.021	-0.010	5.520	0.785	0.785	0.000	0.000	0.000	0.000
5	A	2	SER	0	-0.024	-0.012	7.589	0.404	0.404	0.000	0.000	0.000	0.000
6	A	3	ASN	0	0.015	0.004	8.727	0.449	0.449	0.000	0.000	0.000	0.000
7	A	4	LEU	0	-0.009	-0.017	10.322	0.160	0.160	0.000	0.000	0.000	0.000
8	A	5	PHE	0	-0.020	-0.007	12.800	0.094	0.094	0.000	0.000	0.000	0.000
9	A	6	TYR	0	0.039	0.019	14.963	0.046	0.046	0.000	0.000	0.000	0.000
10	A	7	LYS	1	0.899	0.939	15.939	0.231	0.231	0.000	0.000	0.000	0.000
11	A	8	THR	0	-0.005	-0.004	16.105	0.043	0.043	0.000	0.000	0.000	0.000
12	A	9	LEU	0	-0.003	0.009	18.682	0.033	0.033	0.000	0.000	0.000	0.000
13	A	10	LEU	0	0.008	0.001	20.818	0.026	0.026	0.000	0.000	0.000	0.000
14	A	11	ASP	-1	-0.808	-0.883	19.811	-0.157	-0.157	0.000	0.000	0.000	0.000
15	A	12	ASP	-1	-0.873	-0.938	22.951	-0.160	-0.160	0.000	0.000	0.000	0.000
16	A	13	PHE	0	-0.042	-0.033	24.941	0.014	0.014	0.000	0.000	0.000	0.000
17	A	14	SER	0	0.012	-0.003	25.409	0.015	0.015	0.000	0.000	0.000	0.000
18	A	15	ARG	1	0.889	0.931	23.104	0.150	0.150	0.000	0.000	0.000	0.000
19	A	16	SER	0	-0.051	-0.014	28.883	0.008	0.008	0.000	0.000	0.000	0.000
20	A	17	LEU	0	-0.056	-0.034	30.530	0.005	0.005	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.985	-0.967	32.148	-0.060	-0.060	0.000	0.000	0.000	0.000
22	A	19	MET	0	-0.025	0.002	29.750	0.005	0.005	0.000	0.000	0.000	0.000
23	A	20	GLN	0	-0.024	-0.020	28.100	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	21	PRO	0	-0.030	-0.032	24.347	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	22	LEU	0	0.021	0.016	25.394	0.009	0.009	0.000	0.000	0.000	0.000
26	A	23	VAL	0	-0.008	-0.019	20.846	-0.013	-0.013	0.000	0.000	0.000	0.000
27	A	24	PHE	0	-0.016	-0.012	18.090	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	25	ASP	-1	-0.776	-0.877	18.711	-0.096	-0.096	0.000	0.000	0.000	0.000
29	A	26	ASP	-1	-0.940	-0.978	15.814	-0.024	-0.024	0.000	0.000	0.000	0.000
30	A	27	HIS	0	-0.077	-0.036	16.154	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	28	GLY	0	-0.010	0.005	17.153	-0.032	-0.032	0.000	0.000	0.000	0.000
32	A	29	THR	0	-0.107	-0.074	17.743	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	30	CYS	0	0.002	0.005	21.539	0.014	0.014	0.000	0.000	0.000	0.000
34	A	31	ASN	0	-0.002	0.020	24.066	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	32	MET	0	0.003	-0.005	27.183	0.004	0.004	0.000	0.000	0.000	0.000
36	A	33	ILE	0	0.013	0.009	30.516	0.001	0.001	0.000	0.000	0.000	0.000
37	A	34	ILE	0	-0.020	-0.008	32.533	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	35	ASP	-1	-0.867	-0.937	36.396	-0.057	-0.057	0.000	0.000	0.000	0.000
39	A	36	ASN	0	-0.094	-0.044	38.961	0.003	0.003	0.000	0.000	0.000	0.000
40	A	37	THR	0	-0.048	-0.026	39.411	0.004	0.004	0.000	0.000	0.000	0.000
41	A	38	PHE	0	0.029	0.018	36.721	0.000	0.000	0.000	0.000	0.000	0.000
42	A	39	ALA	0	0.010	0.007	33.522	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	40	LEU	0	0.016	0.006	29.157	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	41	THR	0	-0.014	-0.023	25.014	0.005	0.005	0.000	0.000	0.000	0.000
45	A	42	LEU	0	-0.024	-0.007	23.871	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	43	SER	0	0.001	-0.011	20.931	0.000	0.000	0.000	0.000	0.000	0.000
47	A	44	CYS	0	-0.018	0.001	16.807	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	45	ASP	-1	-0.780	-0.864	17.268	-0.353	-0.353	0.000	0.000	0.000	0.000
49	A	46	TYR	0	0.027	-0.015	12.251	-0.015	-0.015	0.000	0.000	0.000	0.000
50	A	47	ALA	0	0.010	0.015	13.178	-0.051	-0.051	0.000	0.000	0.000	0.000
51	A	48	ARG	1	0.846	0.900	14.092	0.302	0.302	0.000	0.000	0.000	0.000
52	A	49	GLU	-1	-0.834	-0.881	14.791	-0.637	-0.637	0.000	0.000	0.000	0.000
53	A	50	ARG	1	0.817	0.902	17.243	0.311	0.311	0.000	0.000	0.000	0.000
54	A	51	LEU	0	-0.004	0.005	19.646	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	52	LEU	0	-0.047	-0.022	21.950	0.019	0.019	0.000	0.000	0.000	0.000
56	A	53	LEU	0	0.029	0.020	24.463	0.001	0.001	0.000	0.000	0.000	0.000
57	A	54	ILE	0	0.004	-0.011	25.131	0.003	0.003	0.000	0.000	0.000	0.000
58	A	55	GLY	0	0.046	0.017	29.212	0.003	0.003	0.000	0.000	0.000	0.000
59	A	56	LEU	0	-0.011	0.006	32.672	0.000	0.000	0.000	0.000	0.000	0.000
60	A	57	LEU	0	-0.021	-0.010	35.053	0.001	0.001	0.000	0.000	0.000	0.000
61	A	58	GLU	-1	-0.859	-0.926	38.090	-0.039	-0.039	0.000	0.000	0.000	0.000
62	A	59	PRO	0	-0.006	0.009	40.910	0.001	0.001	0.000	0.000	0.000	0.000
63	A	60	HIS	0	0.074	0.032	43.931	0.002	0.002	0.000	0.000	0.000	0.000
64	A	61	LYS	1	0.943	0.973	46.821	0.027	0.027	0.000	0.000	0.000	0.000
65	A	62	ASP	-1	-0.907	-0.959	47.813	-0.028	-0.028	0.000	0.000	0.000	0.000
66	A	63	ILE	0	-0.064	-0.017	45.986	0.000	0.000	0.000	0.000	0.000	0.000
67	A	64	PRO	0	0.017	0.004	47.632	0.000	0.000	0.000	0.000	0.000	0.000
68	A	65	GLN	0	0.071	0.017	43.499	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	66	GLN	0	-0.012	-0.018	44.578	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	67	CYS	0	-0.004	0.012	45.994	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	68	LEU	0	0.040	0.028	41.437	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	69	LEU	0	-0.013	-0.014	40.323	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	70	ALA	0	-0.035	-0.013	41.631	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	71	GLY	0	0.043	0.020	41.449	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	72	ALA	0	-0.016	-0.011	37.425	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	73	LEU	0	-0.022	-0.004	37.099	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	74	ASN	0	-0.028	-0.015	37.404	0.001	0.001	0.000	0.000	0.000	0.000
78	A	75	PRO	0	0.003	0.008	33.393	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	76	LEU	0	-0.030	-0.006	35.560	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	77	LEU	0	-0.063	-0.031	37.285	0.000	0.000	0.000	0.000	0.000	0.000
81	A	78	ASN	0	-0.028	-0.036	38.508	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	79	ALA	0	-0.043	-0.002	33.301	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	80	GLY	0	0.045	0.036	33.693	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	81	PRO	0	-0.002	-0.003	33.478	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	82	GLY	0	0.050	0.025	33.366	0.006	0.006	0.000	0.000	0.000	0.000
86	A	83	LEU	0	-0.032	-0.018	34.697	0.002	0.002	0.000	0.000	0.000	0.000
87	A	84	GLY	0	-0.007	-0.010	34.355	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	85	LEU	0	-0.022	0.002	35.210	0.001	0.001	0.000	0.000	0.000	0.000
89	A	86	ASP	-1	-0.791	-0.871	30.578	-0.066	-0.066	0.000	0.000	0.000	0.000
90	A	87	GLU	-1	-0.946	-0.985	32.993	-0.044	-0.044	0.000	0.000	0.000	0.000
91	A	88	LYS	1	0.836	0.934	26.667	0.075	0.075	0.000	0.000	0.000	0.000
92	A	89	SER	0	-0.017	-0.047	32.621	0.005	0.005	0.000	0.000	0.000	0.000
93	A	90	GLY	0	-0.013	0.004	34.414	0.004	0.004	0.000	0.000	0.000	0.000
94	A	91	LEU	0	-0.016	0.001	34.724	0.001	0.001	0.000	0.000	0.000	0.000
95	A	92	TYR	0	0.029	0.003	35.212	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	93	HIS	0	-0.021	-0.012	30.715	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	94	ALA	0	0.022	0.011	33.821	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	95	TYR	0	-0.029	-0.015	29.026	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	96	GLN	0	0.027	-0.003	29.305	0.001	0.001	0.000	0.000	0.000	0.000
100	A	97	SER	0	-0.027	-0.010	24.923	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	98	ILE	0	-0.009	-0.007	24.893	0.009	0.009	0.000	0.000	0.000	0.000
102	A	99	PRO	0	-0.029	-0.011	22.194	-0.021	-0.021	0.000	0.000	0.000	0.000
103	A	100	ARG	1	0.882	0.926	12.418	0.769	0.769	0.000	0.000	0.000	0.000
104	A	101	GLU	-1	-0.840	-0.955	20.118	-0.309	-0.309	0.000	0.000	0.000	0.000
105	A	102	LYS	1	0.826	0.921	21.928	0.290	0.290	0.000	0.000	0.000	0.000
106	A	103	LEU	0	-0.040	0.010	20.449	0.023	0.023	0.000	0.000	0.000	0.000
107	A	104	SER	0	0.027	0.001	23.997	0.001	0.001	0.000	0.000	0.000	0.000
108	A	105	VAL	0	0.074	0.040	25.755	0.005	0.005	0.000	0.000	0.000	0.000
109	A	106	PRO	0	0.002	-0.011	27.575	0.007	0.007	0.000	0.000	0.000	0.000
110	A	107	THR	0	0.004	0.007	27.744	0.015	0.015	0.000	0.000	0.000	0.000
111	A	108	LEU	0	0.047	0.030	24.959	0.004	0.004	0.000	0.000	0.000	0.000
112	A	109	LYS	1	0.926	0.959	28.471	0.117	0.117	0.000	0.000	0.000	0.000
113	A	110	ARG	1	0.831	0.919	31.032	0.150	0.150	0.000	0.000	0.000	0.000
114	A	111	GLU	-1	-0.802	-0.900	29.946	-0.134	-0.134	0.000	0.000	0.000	0.000
115	A	112	MET	0	-0.041	-0.009	29.556	0.001	0.001	0.000	0.000	0.000	0.000
116	A	113	ALA	0	0.021	0.014	32.441	0.007	0.007	0.000	0.000	0.000	0.000
117	A	114	GLY	0	0.033	0.018	35.443	0.006	0.006	0.000	0.000	0.000	0.000
118	A	115	LEU	0	-0.025	-0.025	31.316	0.005	0.005	0.000	0.000	0.000	0.000
119	A	116	LEU	0	0.030	0.009	35.056	0.005	0.005	0.000	0.000	0.000	0.000
120	A	117	GLU	-1	-0.800	-0.868	37.439	-0.061	-0.061	0.000	0.000	0.000	0.000
121	A	118	TRP	0	-0.039	-0.015	36.498	0.006	0.006	0.000	0.000	0.000	0.000
122	A	119	MET	0	-0.080	-0.037	35.277	0.001	0.001	0.000	0.000	0.000	0.000
123	A	120	ARG	1	0.839	0.889	39.350	0.065	0.065	0.000	0.000	0.000	0.000
124	A	121	GLY	0	0.038	0.026	42.611	0.004	0.004	0.000	0.000	0.000	0.000
125	A	122	TRP	0	-0.040	-0.046	40.213	0.006	0.006	0.000	0.000	0.000	0.000
126	A	123	ARG	1	0.751	0.880	42.334	0.045	0.045	0.000	0.000	0.000	0.000
127	A	124	GLU	-1	-1.008	-1.003	44.305	-0.042	-0.042	0.000	0.000	0.000	0.000
128	A	125	ALA	0	-0.033	0.003	46.818	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:PRO)