FMO DATABASE

FMODB ID: YZK82

Calculation Name: 3MQM-A-Xray372

Preferred Name: Histone-lysine N-methyltransferase ASH1L

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3MQM

Chain ID: A

ChEMBL ID: CHEMBL3588739

UniProt ID: Q9NR48

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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1073654.178328
FMO2-HF: Nuclear repulsion	1023403.316937
FMO2-HF: Total energy	-50250.861392
FMO2-MP2: Total energy	-50397.821819

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:2431:SER)

Summations of interaction energy for fragment #1(A:2431:SER)

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.
-44.212	-50.233	34.497	-16.712	-11.762	-0.063

Interaction energy analysis for fragmet #1(A:2431:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.033 / q_NPA : -0.020

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	2433	GLU	-1	-0.897	-0.953	3.814	0.335	2.790	-0.013	-1.239	-1.203	0.006
4	A	2434	VAL	0	0.044	0.019	5.965	0.147	0.147	0.000	0.000	0.000	0.000
5	A	2435	ALA	0	-0.012	0.000	3.354	-0.482	-0.283	0.014	-0.054	-0.160	0.000
6	A	2436	ARG	1	0.920	0.968	2.405	-6.642	-5.434	4.853	-2.159	-3.902	0.025
7	A	2437	ALA	0	0.043	0.002	4.973	-0.928	-0.840	-0.001	-0.009	-0.078	0.000
8	A	2438	ALA	0	-0.002	0.006	8.280	-0.225	-0.225	0.000	0.000	0.000	0.000
9	A	2439	ARG	1	0.863	0.915	2.744	3.981	5.111	0.041	-0.561	-0.609	0.002
10	A	2440	LEU	0	-0.010	-0.002	8.220	-0.108	-0.108	0.000	0.000	0.000	0.000
11	A	2441	ALA	0	0.026	0.020	10.441	-0.040	-0.040	0.000	0.000	0.000	0.000
12	A	2442	GLN	0	-0.101	-0.054	12.450	0.013	0.013	0.000	0.000	0.000	0.000
13	A	2443	ILE	0	0.061	0.032	10.867	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	2444	PHE	0	-0.031	-0.041	13.174	0.012	0.012	0.000	0.000	0.000	0.000
15	A	2445	LYS	1	0.911	0.953	16.533	0.027	0.027	0.000	0.000	0.000	0.000
16	A	2446	GLU	-1	-0.870	-0.904	17.022	-0.157	-0.157	0.000	0.000	0.000	0.000
17	A	2447	ILE	0	-0.030	-0.011	17.299	0.008	0.008	0.000	0.000	0.000	0.000
18	A	2448	CYS	0	-0.035	-0.034	20.511	0.008	0.008	0.000	0.000	0.000	0.000
19	A	2449	ASP	-1	-0.766	-0.879	22.190	-0.032	-0.032	0.000	0.000	0.000	0.000
20	A	2450	GLY	0	-0.016	-0.004	23.486	0.005	0.005	0.000	0.000	0.000	0.000
21	A	2451	ILE	0	-0.094	-0.053	24.671	0.004	0.004	0.000	0.000	0.000	0.000
22	A	2452	ILE	0	-0.024	-0.012	26.186	0.005	0.005	0.000	0.000	0.000	0.000
23	A	2453	SER	0	-0.102	-0.040	27.754	0.005	0.005	0.000	0.000	0.000	0.000
24	A	2454	TYR	0	0.030	0.016	29.151	0.004	0.004	0.000	0.000	0.000	0.000
25	A	2455	LYS	1	0.896	0.940	30.853	0.043	0.043	0.000	0.000	0.000	0.000
26	A	2456	ASP	-1	-0.871	-0.937	34.490	-0.044	-0.044	0.000	0.000	0.000	0.000
27	A	2457	SER	0	0.062	0.011	37.101	0.001	0.001	0.000	0.000	0.000	0.000
28	A	2458	SER	0	-0.045	-0.014	39.294	0.002	0.002	0.000	0.000	0.000	0.000
29	A	2459	ARG	1	0.907	0.954	38.147	0.030	0.030	0.000	0.000	0.000	0.000
30	A	2460	GLN	0	-0.022	-0.002	38.857	0.002	0.002	0.000	0.000	0.000	0.000
31	A	2461	ALA	0	0.002	-0.002	34.226	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	2462	LEU	0	0.047	0.017	33.844	0.001	0.001	0.000	0.000	0.000	0.000
33	A	2463	ALA	0	0.028	0.022	30.687	0.001	0.001	0.000	0.000	0.000	0.000
34	A	2464	ALA	0	0.004	0.009	32.652	0.003	0.003	0.000	0.000	0.000	0.000
35	A	2465	PRO	0	-0.038	-0.033	35.209	0.003	0.003	0.000	0.000	0.000	0.000
36	A	2466	LEU	0	-0.057	-0.029	30.974	0.001	0.001	0.000	0.000	0.000	0.000
37	A	2467	LEU	0	0.020	0.026	30.232	0.001	0.001	0.000	0.000	0.000	0.000
38	A	2468	ASN	0	0.023	0.001	31.445	0.004	0.004	0.000	0.000	0.000	0.000
39	A	2469	LEU	0	-0.005	0.011	32.075	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	2470	PRO	0	-0.008	0.010	35.230	0.002	0.002	0.000	0.000	0.000	0.000
41	A	2471	PRO	0	0.021	0.002	39.029	0.001	0.001	0.000	0.000	0.000	0.000
42	A	2472	LYS	1	0.955	1.003	39.885	0.009	0.009	0.000	0.000	0.000	0.000
43	A	2473	LYS	1	0.949	0.973	41.476	0.000	0.000	0.000	0.000	0.000	0.000
44	A	2474	LYS	1	0.924	0.954	44.656	0.011	0.011	0.000	0.000	0.000	0.000
45	A	2475	ASN	0	-0.027	-0.014	42.192	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	2476	ALA	0	0.017	0.005	42.866	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	2477	ASP	-1	-0.750	-0.878	44.125	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	2478	TYR	0	-0.005	-0.011	35.780	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	2479	TYR	0	-0.083	-0.075	36.258	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	2480	GLU	-1	-0.810	-0.883	40.176	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	2481	LYS	1	0.827	0.927	41.329	0.023	0.023	0.000	0.000	0.000	0.000
52	A	2482	ILE	0	-0.100	-0.054	34.875	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	2483	SER	0	0.006	0.008	34.908	0.001	0.001	0.000	0.000	0.000	0.000
54	A	2484	ASP	-1	-0.850	-0.928	29.526	-0.024	-0.024	0.000	0.000	0.000	0.000
55	A	2485	PRO	0	-0.049	-0.012	31.483	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	2486	LEU	0	0.010	-0.008	25.276	0.002	0.002	0.000	0.000	0.000	0.000
57	A	2487	ASP	-1	-0.793	-0.841	29.426	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	2488	LEU	0	0.045	0.000	26.209	0.001	0.001	0.000	0.000	0.000	0.000
59	A	2489	ILE	0	0.010	0.024	26.137	0.002	0.002	0.000	0.000	0.000	0.000
60	A	2490	THR	0	-0.073	-0.089	25.650	0.007	0.007	0.000	0.000	0.000	0.000
61	A	2491	ILE	0	-0.026	-0.004	21.808	0.007	0.007	0.000	0.000	0.000	0.000
62	A	2492	GLU	-1	-0.804	-0.927	21.664	-0.021	-0.021	0.000	0.000	0.000	0.000
63	A	2493	LYS	1	0.906	0.960	21.718	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	2494	GLN	0	-0.050	-0.045	20.452	0.015	0.015	0.000	0.000	0.000	0.000
65	A	2495	ILE	0	0.015	0.014	16.442	0.021	0.021	0.000	0.000	0.000	0.000
66	A	2496	LEU	0	-0.017	-0.009	16.438	0.025	0.025	0.000	0.000	0.000	0.000
67	A	2497	THR	0	-0.080	-0.023	17.066	0.019	0.019	0.000	0.000	0.000	0.000
68	A	2498	GLY	0	0.032	0.020	13.838	0.033	0.033	0.000	0.000	0.000	0.000
69	A	2499	TYR	0	-0.058	-0.021	14.338	0.010	0.010	0.000	0.000	0.000	0.000
70	A	2500	TYR	0	-0.144	-0.102	15.523	-0.017	-0.017	0.000	0.000	0.000	0.000
71	A	2501	LYS	1	0.977	0.992	11.802	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	2502	THR	0	0.047	0.015	10.957	0.011	0.011	0.000	0.000	0.000	0.000
73	A	2503	VAL	0	0.081	0.030	13.212	0.031	0.031	0.000	0.000	0.000	0.000
74	A	2504	GLU	-1	-0.881	-0.933	14.959	-0.225	-0.225	0.000	0.000	0.000	0.000
75	A	2505	ALA	0	-0.065	-0.027	16.919	0.020	0.020	0.000	0.000	0.000	0.000
76	A	2506	PHE	0	0.043	0.021	16.944	0.016	0.016	0.000	0.000	0.000	0.000
77	A	2507	ASP	-1	-0.780	-0.858	18.793	-0.162	-0.162	0.000	0.000	0.000	0.000
78	A	2508	ALA	0	-0.049	-0.012	20.829	0.010	0.010	0.000	0.000	0.000	0.000
79	A	2509	ASP	-1	-0.789	-0.881	22.049	-0.023	-0.023	0.000	0.000	0.000	0.000
80	A	2510	MET	0	0.014	0.002	21.878	0.009	0.009	0.000	0.000	0.000	0.000
81	A	2511	LEU	0	-0.014	-0.026	24.432	0.006	0.006	0.000	0.000	0.000	0.000
82	A	2512	LYS	1	0.889	0.968	26.065	0.039	0.039	0.000	0.000	0.000	0.000
83	A	2513	VAL	0	0.035	0.026	27.315	0.004	0.004	0.000	0.000	0.000	0.000
84	A	2514	PHE	0	0.026	0.008	26.704	0.003	0.003	0.000	0.000	0.000	0.000
85	A	2515	ARG	1	0.911	0.960	30.673	0.051	0.051	0.000	0.000	0.000	0.000
86	A	2516	ASN	0	-0.009	-0.027	32.032	0.001	0.001	0.000	0.000	0.000	0.000
87	A	2517	ALA	0	0.032	0.035	33.749	0.003	0.003	0.000	0.000	0.000	0.000
88	A	2518	GLU	-1	-0.818	-0.913	34.503	-0.055	-0.055	0.000	0.000	0.000	0.000
89	A	2519	LYS	1	0.795	0.898	36.195	0.033	0.033	0.000	0.000	0.000	0.000
90	A	2520	TYR	0	-0.033	-0.014	38.243	0.001	0.001	0.000	0.000	0.000	0.000
91	A	2521	TYR	0	0.054	0.025	37.968	0.002	0.002	0.000	0.000	0.000	0.000
92	A	2522	GLY	0	-0.008	-0.018	40.460	0.001	0.001	0.000	0.000	0.000	0.000
93	A	2523	ARG	1	0.903	0.945	34.672	0.056	0.056	0.000	0.000	0.000	0.000
94	A	2524	LYS	1	0.992	1.033	40.154	0.034	0.034	0.000	0.000	0.000	0.000
95	A	2525	SER	0	-0.002	-0.016	41.815	0.001	0.001	0.000	0.000	0.000	0.000
96	A	2526	PRO	0	0.024	0.000	41.860	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	2527	VAL	0	0.138	0.062	37.400	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	2528	GLY	0	-0.031	0.005	37.310	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	2529	ARG	1	0.879	0.922	37.322	0.033	0.033	0.000	0.000	0.000	0.000
100	A	2530	ASP	-1	-0.846	-0.912	35.960	-0.044	-0.044	0.000	0.000	0.000	0.000
101	A	2531	VAL	0	-0.008	0.001	32.213	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	2532	CYS	0	-0.040	-0.026	32.500	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	2533	ARG	1	0.887	0.939	32.870	0.052	0.052	0.000	0.000	0.000	0.000
104	A	2534	LEU	0	0.036	0.017	29.871	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	2535	ARG	1	0.859	0.938	28.348	0.065	0.065	0.000	0.000	0.000	0.000
106	A	2536	LYS	1	0.914	0.970	27.610	0.064	0.064	0.000	0.000	0.000	0.000
107	A	2537	ALA	0	-0.001	0.008	27.675	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	2538	TYR	0	0.008	-0.014	20.503	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	2539	TYR	0	-0.009	-0.030	23.252	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	2540	ASN	0	-0.019	0.009	23.387	-0.017	-0.017	0.000	0.000	0.000	0.000
111	A	2541	ALA	0	0.081	0.048	21.390	-0.014	-0.014	0.000	0.000	0.000	0.000
112	A	2542	ARG	1	0.815	0.879	17.129	0.210	0.210	0.000	0.000	0.000	0.000
113	A	2543	HIS	0	-0.043	-0.023	18.576	-0.037	-0.037	0.000	0.000	0.000	0.000
114	A	2544	GLU	-1	-0.921	-0.966	19.144	-0.197	-0.197	0.000	0.000	0.000	0.000
115	A	2545	ALA	0	0.016	0.015	15.141	-0.027	-0.027	0.000	0.000	0.000	0.000
116	A	2546	SER	0	-0.100	-0.058	14.242	-0.080	-0.080	0.000	0.000	0.000	0.000
117	A	2547	ALA	0	0.080	0.048	13.702	-0.060	-0.060	0.000	0.000	0.000	0.000
118	A	2548	GLN	0	0.039	0.014	11.043	-0.057	-0.057	0.000	0.000	0.000	0.000
119	A	2549	ILE	0	-0.051	-0.035	9.352	-0.220	-0.220	0.000	0.000	0.000	0.000
120	A	2550	ASP	-1	-0.902	-0.948	9.296	-0.717	-0.717	0.000	0.000	0.000	0.000
121	A	2551	GLU	-1	-0.967	-0.981	8.076	-1.145	-1.145	0.000	0.000	0.000	0.000
122	A	2552	ILE	0	-0.070	-0.028	4.596	-0.928	-0.845	-0.001	-0.003	-0.078	0.000
123	A	2553	VAL	0	-0.003	-0.016	4.614	-0.737	-0.710	-0.001	-0.005	-0.020	0.000
124	A	2554	GLY	0	-0.027	0.000	7.062	0.095	0.095	0.000	0.000	0.000	0.000
125	A	2555	GLU	-1	-0.793	-0.846	1.496	-35.384	-47.562	29.570	-12.218	-5.174	-0.092
126	A	2556	THR	0	-0.142	-0.070	3.322	-0.914	0.053	0.035	-0.464	-0.538	-0.004

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Interactive mode: IFIE and PIEDA for fragment #1(A:2431:SER)