FMO DATABASE

FMODB ID: 3JNML

Calculation Name: 3MJQ-A-Xray372

Preferred Name:
Warning: Undefined array key "pref_name" in /home/FMODBwui_src/fmodbwui/detail.php on line 446

Target Type:
Warning: Undefined array key "target_type" in /home/FMODBwui_src/fmodbwui/detail.php on line 447

Ligand Name:
Warning: Undefined variable $Ligand in /home/FMODBwui_src/fmodbwui/detail.php on line 448

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 448

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 448

ligand 3-letter code:
Warning: Undefined variable $Ligand in /home/FMODBwui_src/fmodbwui/detail.php on line 449

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 449

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 449

PDB ID: 3MJQ

Chain ID: A

ChEMBL ID:
Warning: Undefined array key "chembl_id" in /home/FMODBwui_src/fmodbwui/detail.php on line 452

Warning: Undefined array key "chembl_id" in /home/FMODBwui_src/fmodbwui/detail.php on line 452

UniProt ID: Q24QT8

Base Structure: X-ray

Registration Date: 2023-09-20

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	107
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-841169.816863
FMO2-HF: Nuclear repulsion	798747.189444
FMO2-HF: Total energy	-42422.62742
FMO2-MP2: Total energy	-42545.453816

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:LYS)

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

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.
3.129	9.247	6.579	-4.39	-8.307	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.958 / q_NPA : 0.988

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	PHE	0	0.016	0.004	1.884	-1.980	1.704	6.066	-3.813	-5.937	-0.006
4	A	5	LEU	0	0.065	0.066	2.617	6.419	8.354	0.513	-0.467	-1.981	-0.003
5	A	6	GLU	-1	-0.815	-0.909	4.689	-25.279	-25.053	-0.001	-0.030	-0.195	0.000
6	A	7	THR	0	-0.127	-0.109	6.663	3.288	3.288	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.031	0.004	7.471	1.751	1.751	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.902	-0.958	10.000	-20.289	-20.289	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.970	-0.974	12.761	-17.054	-17.054	0.000	0.000	0.000	0.000
10	A	11	MET	0	-0.044	-0.020	11.172	-1.310	-1.310	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.007	-0.004	6.467	0.430	0.430	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.012	-0.003	8.785	-0.411	-0.411	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.037	-0.006	5.728	-0.270	-0.270	0.000	0.000	0.000	0.000
14	A	15	ILE	0	0.001	0.002	9.629	0.395	0.395	0.000	0.000	0.000	0.000
15	A	16	ASN	0	0.081	0.036	13.201	0.522	0.522	0.000	0.000	0.000	0.000
16	A	17	ARG	1	1.002	0.972	15.402	12.010	12.010	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.916	-0.963	18.730	-10.979	-10.979	0.000	0.000	0.000	0.000
18	A	19	GLY	0	-0.018	0.008	18.147	0.326	0.326	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.894	0.967	16.048	12.689	12.689	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.036	-0.007	12.617	-0.504	-0.504	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.035	0.003	9.519	-0.035	-0.035	0.000	0.000	0.000	0.000
22	A	23	TYR	0	-0.005	-0.008	4.199	-2.192	-1.919	0.001	-0.080	-0.194	0.000
23	A	24	ALA	0	0.037	0.010	7.591	1.417	1.417	0.000	0.000	0.000	0.000
24	A	25	ASN	0	0.027	0.032	6.805	0.467	0.467	0.000	0.000	0.000	0.000
25	A	26	THR	0	0.061	0.015	8.355	3.146	3.146	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.018	-0.011	10.969	1.818	1.818	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.012	-0.004	11.187	1.559	1.559	0.000	0.000	0.000	0.000
28	A	29	PRO	0	0.001	0.005	12.549	1.087	1.087	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.885	0.953	14.699	19.196	19.196	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.867	0.923	16.515	15.498	15.498	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.014	-0.010	16.709	0.722	0.722	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.015	0.015	19.405	0.663	0.663	0.000	0.000	0.000	0.000
33	A	34	TYR	0	-0.030	-0.010	18.277	0.487	0.487	0.000	0.000	0.000	0.000
34	A	35	THR	0	-0.002	-0.011	17.258	-0.640	-0.640	0.000	0.000	0.000	0.000
35	A	36	HIS	0	0.048	0.023	9.178	0.095	0.095	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.869	-0.947	14.345	-16.139	-16.139	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.800	-0.903	16.475	-12.418	-12.418	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.014	-0.022	12.926	0.240	0.240	0.000	0.000	0.000	0.000
39	A	40	MET	0	-0.063	-0.009	10.355	-0.336	-0.336	0.000	0.000	0.000	0.000
40	A	41	SER	0	-0.077	-0.036	14.548	0.487	0.487	0.000	0.000	0.000	0.000
41	A	42	MET	0	-0.016	-0.011	18.163	0.540	0.540	0.000	0.000	0.000	0.000
42	A	43	HIS	0	0.042	0.031	17.944	-0.527	-0.527	0.000	0.000	0.000	0.000
43	A	44	ILE	0	0.040	0.006	15.780	0.162	0.162	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.009	-0.014	18.644	0.052	0.052	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.067	-0.022	21.731	0.458	0.458	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.000	0.004	17.559	0.127	0.127	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.031	-0.018	19.788	0.235	0.235	0.000	0.000	0.000	0.000
48	A	49	SER	0	-0.041	-0.031	22.511	0.311	0.311	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.084	0.069	25.829	0.324	0.324	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.019	0.008	27.371	0.227	0.227	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.846	0.913	29.199	8.644	8.644	0.000	0.000	0.000	0.000
52	A	53	MET	0	0.084	0.041	26.033	-0.294	-0.294	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.049	0.037	27.802	-0.194	-0.194	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.901	-0.971	29.555	-8.613	-8.613	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.012	0.005	25.895	-0.218	-0.218	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.951	-0.987	24.639	-10.085	-10.085	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.958	0.977	25.806	8.797	8.797	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.004	0.006	23.113	-0.178	-0.178	0.000	0.000	0.000	0.000
59	A	60	LEU	0	0.029	0.019	18.635	-0.325	-0.325	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.020	0.001	21.825	-0.313	-0.313	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.958	-1.000	24.069	-10.032	-10.032	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.052	-0.034	18.909	-0.143	-0.143	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.025	0.016	16.815	-0.461	-0.461	0.000	0.000	0.000	0.000
64	A	65	ALA	0	-0.086	-0.035	20.758	-0.060	-0.060	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.061	0.044	21.898	0.101	0.101	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.825	0.939	22.945	9.570	9.570	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.916	0.949	23.023	10.579	10.579	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.833	-0.908	19.933	-13.388	-13.388	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.101	-0.058	19.016	-0.683	-0.683	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.018	-0.003	19.886	0.654	0.654	0.000	0.000	0.000	0.000
71	A	72	PRO	0	-0.015	-0.007	21.403	-0.505	-0.505	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.011	-0.021	18.769	0.045	0.045	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.020	0.012	22.990	0.209	0.209	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.039	-0.018	18.045	-0.052	-0.052	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.864	-0.933	21.938	-9.971	-9.971	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.904	0.938	22.268	11.183	11.183	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.894	0.959	22.612	12.006	12.006	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.960	-1.005	24.334	-9.905	-9.905	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.031	0.033	26.669	0.356	0.356	0.000	0.000	0.000	0.000
80	A	81	THR	0	-0.047	-0.002	26.570	0.244	0.244	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.015	-0.013	25.443	-0.428	-0.428	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.025	-0.008	20.436	0.183	0.183	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.016	0.026	23.634	-0.192	-0.192	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.045	0.015	19.504	-0.433	-0.433	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.937	0.970	20.100	12.886	12.886	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.005	0.019	16.657	-0.735	-0.735	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.928	0.961	15.725	15.642	15.642	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.011	-0.007	14.551	-0.879	-0.879	0.000	0.000	0.000	0.000
89	A	90	TRP	0	0.024	0.019	12.704	0.125	0.125	0.000	0.000	0.000	0.000
90	A	91	GLN	0	0.012	0.007	13.631	-0.243	-0.243	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.034	0.025	11.924	-0.393	-0.393	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.928	0.942	11.727	16.357	16.357	0.000	0.000	0.000	0.000
93	A	94	TRP	0	-0.008	0.011	5.684	-0.348	-0.348	0.000	0.000	0.000	0.000
94	A	95	HIS	0	0.029	0.023	7.812	-0.863	-0.863	0.000	0.000	0.000	0.000
95	A	96	ASN	0	0.045	-0.011	11.601	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.972	-0.960	14.712	-12.577	-12.577	0.000	0.000	0.000	0.000
97	A	98	PRO	0	-0.064	-0.042	14.646	-0.810	-0.810	0.000	0.000	0.000	0.000
98	A	99	CYS	0	-0.047	-0.029	11.034	0.123	0.123	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.019	0.002	13.817	-0.043	-0.043	0.000	0.000	0.000	0.000
100	A	101	PHE	0	-0.020	-0.003	6.642	-0.669	-0.669	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.027	0.003	10.691	0.817	0.817	0.000	0.000	0.000	0.000
102	A	103	ILE	0	0.020	0.021	10.097	-1.105	-1.105	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.034	-0.030	12.327	1.346	1.346	0.000	0.000	0.000	0.000
104	A	105	LYS	1	1.008	1.006	15.244	13.291	13.291	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.799	-0.901	17.836	-12.375	-12.375	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.142	-0.078	20.145	-0.040	-0.040	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.018	-0.002	23.399	0.746	0.746	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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