FMO DATABASE

FMODB ID: Q1Z8Y

Calculation Name: 2J85-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: 2J85

Chain ID: A

ChEMBL ID:
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UniProt ID: Q6Q0K9

Base Structure: X-ray

Registration Date: 2023-06-19

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-990524.316003
FMO2-HF: Nuclear repulsion	942651.972975
FMO2-HF: Total energy	-47872.343028
FMO2-MP2: Total energy	-48009.643422

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:GLY)

Summations of interaction energy for fragment #1(A:2: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.
-10.283	-5.282	1.297	-3.342	-2.956	-0.017

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : 0.002

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	4	VAL	0	0.051	0.025	3.797	-1.262	0.499	-0.011	-1.004	-0.746	0.005
4	A	5	PHE	0	-0.017	-0.010	6.774	0.667	0.667	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.040	0.041	9.720	0.090	0.090	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.020	-0.029	13.000	0.100	0.100	0.000	0.000	0.000	0.000
7	A	8	ASN	0	0.005	0.004	15.612	-0.002	-0.002	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.025	0.001	17.699	0.060	0.060	0.000	0.000	0.000	0.000
9	A	10	PHE	0	0.076	0.039	13.521	-0.071	-0.071	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.022	-0.014	16.461	0.067	0.067	0.000	0.000	0.000	0.000
11	A	12	ILE	0	0.104	0.046	16.269	-0.037	-0.037	0.000	0.000	0.000	0.000
12	A	13	ASN	0	-0.015	-0.013	16.858	0.038	0.038	0.000	0.000	0.000	0.000
13	A	14	MET	0	-0.036	-0.006	12.677	-0.006	-0.006	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.020	0.006	11.997	-0.060	-0.060	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.844	0.915	9.337	-0.094	-0.094	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.953	-0.974	12.593	0.357	0.357	0.000	0.000	0.000	0.000
17	A	18	PHE	0	-0.047	-0.003	14.873	-0.035	-0.035	0.000	0.000	0.000	0.000
18	A	19	PRO	0	-0.008	-0.019	17.516	0.018	0.018	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.010	0.002	12.427	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.029	-0.010	14.041	-0.025	-0.025	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.005	0.001	11.716	0.007	0.007	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.023	-0.002	13.089	0.077	0.077	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.023	-0.020	13.581	-0.109	-0.109	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.856	-0.915	15.620	-0.308	-0.308	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.854	0.915	17.235	0.260	0.260	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.003	0.005	14.575	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.887	-0.938	19.149	-0.339	-0.339	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.860	-0.978	20.375	-0.346	-0.346	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.941	-0.959	20.696	-0.353	-0.353	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.851	-0.935	17.237	-0.478	-0.478	0.000	0.000	0.000	0.000
31	A	32	PHE	0	-0.040	-0.037	16.184	-0.119	-0.119	0.000	0.000	0.000	0.000
32	A	33	CYS	0	-0.089	-0.046	15.885	-0.104	-0.104	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.066	0.050	16.648	-0.055	-0.055	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.862	0.941	11.790	0.835	0.835	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.003	-0.007	11.638	-0.226	-0.226	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.900	-0.966	12.915	-0.623	-0.623	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.035	-0.008	10.052	0.001	0.001	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.861	0.921	6.767	2.172	2.172	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.054	-0.022	9.455	-0.085	-0.085	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.952	-0.981	12.249	-0.440	-0.440	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.852	-0.874	7.281	-2.252	-2.252	0.000	0.000	0.000	0.000
42	A	43	GLY	0	-0.019	-0.007	8.393	0.006	0.006	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.090	-0.079	3.801	-0.496	-0.325	0.000	-0.047	-0.123	0.000
44	A	45	LEU	0	-0.036	-0.018	6.360	-0.588	-0.588	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.050	-0.018	7.898	0.408	0.408	0.000	0.000	0.000	0.000
46	A	47	ASN	0	0.052	0.017	10.364	-0.022	-0.022	0.000	0.000	0.000	0.000
47	A	48	ALA	0	-0.001	0.002	13.574	0.087	0.087	0.000	0.000	0.000	0.000
48	A	49	ILE	0	-0.002	0.016	15.380	0.085	0.085	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.003	-0.009	18.580	0.019	0.019	0.000	0.000	0.000	0.000
50	A	51	HIS	0	-0.040	-0.034	21.305	0.016	0.016	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.788	-0.913	23.861	-0.300	-0.300	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.042	-0.016	26.051	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	54	THR	0	-0.037	-0.021	21.604	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.000	0.007	19.505	-0.022	-0.022	0.000	0.000	0.000	0.000
55	A	56	ASN	0	0.011	-0.003	22.850	-0.023	-0.023	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.019	0.000	24.513	0.005	0.005	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.028	0.005	18.887	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	ASN	0	0.033	0.035	21.450	-0.056	-0.056	0.000	0.000	0.000	0.000
59	A	60	THR	0	-0.096	-0.039	23.288	0.017	0.017	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.030	-0.013	22.285	0.009	0.009	0.000	0.000	0.000	0.000
61	A	63	GLY	0	0.046	0.047	21.756	0.000	0.000	0.000	0.000	0.000	0.000
62	A	64	THR	0	-0.035	-0.031	17.805	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	65	GLN	0	-0.026	-0.032	20.116	0.049	0.049	0.000	0.000	0.000	0.000
64	A	66	LEU	0	-0.053	-0.017	16.099	0.002	0.002	0.000	0.000	0.000	0.000
65	A	67	GLN	0	0.053	0.020	19.904	0.067	0.067	0.000	0.000	0.000	0.000
66	A	68	LYS	1	0.931	0.975	19.729	0.210	0.210	0.000	0.000	0.000	0.000
67	A	69	ASN	0	-0.034	-0.038	15.327	0.090	0.090	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.915	0.957	18.181	0.218	0.218	0.000	0.000	0.000	0.000
69	A	71	VAL	0	0.022	0.016	12.717	0.023	0.023	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.977	-0.981	15.963	-0.209	-0.209	0.000	0.000	0.000	0.000
71	A	73	VAL	0	-0.008	-0.008	10.678	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	74	LYS	1	0.902	0.953	11.104	0.277	0.277	0.000	0.000	0.000	0.000
73	A	75	MET	0	-0.053	-0.013	7.650	0.000	0.000	0.000	0.000	0.000	0.000
74	A	76	ASN	0	-0.029	-0.021	5.480	0.163	0.163	0.000	0.000	0.000	0.000
75	A	77	GLU	-1	-0.769	-0.912	6.557	-0.018	-0.018	0.000	0.000	0.000	0.000
76	A	78	GLY	0	-0.025	-0.012	3.587	0.016	0.146	0.007	-0.064	-0.073	0.000
77	A	79	ASP	-1	-0.819	-0.894	2.628	-7.064	-4.229	1.299	-2.212	-1.922	-0.022
78	A	80	GLH	0	-0.063	-0.074	3.951	0.663	0.767	0.002	-0.015	-0.092	0.000
79	A	81	ALA	0	-0.042	-0.023	6.959	-0.213	-0.213	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.038	0.026	10.077	0.105	0.105	0.000	0.000	0.000	0.000
81	A	83	ILE	0	-0.036	-0.037	12.852	0.060	0.060	0.000	0.000	0.000	0.000
82	A	84	ILE	0	0.006	0.019	16.000	0.046	0.046	0.000	0.000	0.000	0.000
83	A	85	MET	0	-0.048	-0.030	19.554	0.023	0.023	0.000	0.000	0.000	0.000
84	A	86	ILE	0	0.014	0.000	22.245	0.017	0.017	0.000	0.000	0.000	0.000
85	A	87	SER	0	0.021	0.010	25.702	0.009	0.009	0.000	0.000	0.000	0.000
86	A	88	GLN	0	-0.045	-0.019	28.679	0.018	0.018	0.000	0.000	0.000	0.000
87	A	89	ARG	1	0.969	0.969	29.370	0.161	0.161	0.000	0.000	0.000	0.000
88	A	90	LEU	0	0.000	-0.001	26.832	0.016	0.016	0.000	0.000	0.000	0.000
89	A	91	GLU	-1	-0.867	-0.931	30.709	-0.149	-0.149	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.899	-0.950	29.156	-0.240	-0.240	0.000	0.000	0.000	0.000
91	A	93	GLY	0	0.015	0.002	32.648	0.012	0.012	0.000	0.000	0.000	0.000
92	A	94	LYS	1	0.827	0.925	34.320	0.159	0.159	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.010	0.007	32.851	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	96	LEU	0	-0.009	0.006	29.854	0.009	0.009	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.010	0.011	31.910	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.772	-0.927	28.638	-0.271	-0.271	0.000	0.000	0.000	0.000
97	A	99	LYS	1	0.908	0.961	31.178	0.141	0.141	0.000	0.000	0.000	0.000
98	A	100	GLU	-1	-0.890	-0.954	33.544	-0.174	-0.174	0.000	0.000	0.000	0.000
99	A	101	ILE	0	0.013	0.010	26.906	0.002	0.002	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.949	0.971	27.615	0.254	0.254	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.955	-0.954	30.572	-0.163	-0.163	0.000	0.000	0.000	0.000
102	A	104	MET	0	-0.084	-0.045	29.254	0.006	0.006	0.000	0.000	0.000	0.000
103	A	105	TYR	0	0.036	0.031	24.457	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	106	ARG	1	0.957	0.982	28.780	0.185	0.185	0.000	0.000	0.000	0.000
105	A	107	GLN	0	-0.071	-0.057	31.479	0.013	0.013	0.000	0.000	0.000	0.000
106	A	108	GLY	0	-0.005	0.013	29.166	0.009	0.009	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.840	0.926	29.322	0.176	0.176	0.000	0.000	0.000	0.000
108	A	110	ILE	0	-0.019	-0.003	23.848	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.047	-0.017	23.161	0.021	0.021	0.000	0.000	0.000	0.000
110	A	112	PHE	0	0.016	0.010	18.480	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	113	TYR	0	-0.009	-0.007	17.117	0.066	0.066	0.000	0.000	0.000	0.000
112	A	114	GLU	-1	-0.791	-0.847	10.158	-1.351	-1.351	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.038	-0.021	11.686	0.148	0.148	0.000	0.000	0.000	0.000
114	A	116	TRP	0	0.038	0.010	7.985	-0.372	-0.372	0.000	0.000	0.000	0.000
115	A	117	HIS	0	0.003	0.021	7.442	0.067	0.067	0.000	0.000	0.000	0.000
116	A	118	HIS	0	-0.018	-0.008	9.983	0.038	0.038	0.000	0.000	0.000	0.000

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