FMO DATABASE

FMODB ID: V51L1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1074200.422753
FMO2-HF: Nuclear repulsion	1023948.749287
FMO2-HF: Total energy	-50251.673467
FMO2-MP2: Total energy	-50398.642984

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.
-39.616	-41.719	27.812	-14.548	-11.159	-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 : 0.025 / 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

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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	-0.832	-0.904	3.814	-0.028	2.678	-0.013	-1.392	-1.301	0.007
4	A	2434	VAL	0	0.029	0.006	5.835	0.020	0.020	0.000	0.000	0.000	0.000
5	A	2435	ALA	0	0.005	0.006	3.558	-0.492	-0.325	0.005	-0.044	-0.128	0.000
6	A	2436	ARG	1	0.867	0.933	2.471	-5.263	-3.609	3.312	-1.802	-3.164	0.018
7	A	2437	ALA	0	0.025	-0.010	4.886	-0.884	-0.794	-0.001	-0.012	-0.077	0.000
8	A	2438	ALA	0	-0.007	0.004	8.149	-0.206	-0.206	0.000	0.000	0.000	0.000
9	A	2439	ARG	1	0.824	0.870	2.584	4.856	5.819	0.051	-0.508	-0.506	0.002
10	A	2440	LEU	0	-0.009	0.001	7.917	-0.065	-0.065	0.000	0.000	0.000	0.000
11	A	2441	ALA	0	0.021	0.014	10.232	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	2442	GLN	0	-0.081	-0.046	12.224	0.024	0.024	0.000	0.000	0.000	0.000
13	A	2443	ILE	0	0.055	0.031	10.866	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	2444	PHE	0	-0.034	-0.042	12.702	0.017	0.017	0.000	0.000	0.000	0.000
15	A	2445	LYS	1	0.823	0.882	16.335	0.045	0.045	0.000	0.000	0.000	0.000
16	A	2446	GLU	-1	-0.846	-0.895	16.756	-0.168	-0.168	0.000	0.000	0.000	0.000
17	A	2447	ILE	0	-0.032	-0.012	17.117	0.012	0.012	0.000	0.000	0.000	0.000
18	A	2448	CYS	0	-0.063	-0.048	20.319	0.012	0.012	0.000	0.000	0.000	0.000
19	A	2449	ASP	-1	-0.772	-0.867	21.994	-0.037	-0.037	0.000	0.000	0.000	0.000
20	A	2450	GLY	0	-0.002	0.025	23.316	0.007	0.007	0.000	0.000	0.000	0.000
21	A	2451	ILE	0	-0.091	-0.051	24.477	0.006	0.006	0.000	0.000	0.000	0.000
22	A	2452	ILE	0	-0.005	-0.009	25.475	0.007	0.007	0.000	0.000	0.000	0.000
23	A	2453	SER	0	-0.097	-0.058	27.240	0.005	0.005	0.000	0.000	0.000	0.000
24	A	2454	TYR	0	0.053	0.040	29.119	0.005	0.005	0.000	0.000	0.000	0.000
25	A	2455	LYS	1	0.872	0.917	30.696	0.047	0.047	0.000	0.000	0.000	0.000
26	A	2456	ASP	-1	-0.858	-0.907	34.339	-0.046	-0.046	0.000	0.000	0.000	0.000
27	A	2457	SER	0	0.063	0.015	36.965	0.001	0.001	0.000	0.000	0.000	0.000
28	A	2458	SER	0	-0.064	-0.050	39.174	0.003	0.003	0.000	0.000	0.000	0.000
29	A	2459	ARG	1	0.881	0.945	37.981	0.030	0.030	0.000	0.000	0.000	0.000
30	A	2460	GLN	0	0.025	0.023	38.691	0.003	0.003	0.000	0.000	0.000	0.000
31	A	2461	ALA	0	0.013	-0.004	34.066	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	2462	LEU	0	0.004	-0.003	33.725	0.001	0.001	0.000	0.000	0.000	0.000
33	A	2463	ALA	0	0.029	0.020	30.454	0.000	0.000	0.000	0.000	0.000	0.000
34	A	2464	ALA	0	0.016	0.014	32.459	0.002	0.002	0.000	0.000	0.000	0.000
35	A	2465	PRO	0	-0.047	-0.037	35.001	0.003	0.003	0.000	0.000	0.000	0.000
36	A	2466	LEU	0	-0.058	-0.022	30.233	0.001	0.001	0.000	0.000	0.000	0.000
37	A	2467	LEU	0	0.026	0.027	30.131	0.000	0.000	0.000	0.000	0.000	0.000
38	A	2468	ASN	0	-0.001	-0.009	31.212	0.004	0.004	0.000	0.000	0.000	0.000
39	A	2469	LEU	0	0.008	0.011	32.308	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	2470	PRO	0	-0.020	-0.004	35.055	0.003	0.003	0.000	0.000	0.000	0.000
41	A	2471	PRO	0	0.028	0.011	38.901	0.001	0.001	0.000	0.000	0.000	0.000
42	A	2472	LYS	1	0.886	0.970	39.798	0.015	0.015	0.000	0.000	0.000	0.000
43	A	2473	LYS	1	0.941	0.970	41.388	0.004	0.004	0.000	0.000	0.000	0.000
44	A	2474	LYS	1	0.921	0.950	44.579	0.015	0.015	0.000	0.000	0.000	0.000
45	A	2475	ASN	0	-0.035	-0.014	42.043	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	2476	ALA	0	0.026	0.006	42.734	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	2477	ASP	-1	-0.725	-0.862	44.021	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	2478	TYR	0	0.000	-0.011	35.507	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	2479	TYR	0	-0.074	-0.068	36.173	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	2480	GLU	-1	-0.764	-0.864	40.069	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	2481	LYS	1	0.822	0.934	41.102	0.028	0.028	0.000	0.000	0.000	0.000
52	A	2482	ILE	0	-0.115	-0.061	34.700	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	2483	SER	0	0.022	0.016	34.961	0.001	0.001	0.000	0.000	0.000	0.000
54	A	2484	ASP	-1	-0.816	-0.905	29.156	-0.042	-0.042	0.000	0.000	0.000	0.000
55	A	2485	PRO	0	-0.020	-0.004	31.329	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	2486	LEU	0	0.007	0.003	25.117	0.002	0.002	0.000	0.000	0.000	0.000
57	A	2487	ASP	-1	-0.792	-0.871	29.275	-0.023	-0.023	0.000	0.000	0.000	0.000
58	A	2488	LEU	0	0.047	-0.002	25.882	0.000	0.000	0.000	0.000	0.000	0.000
59	A	2489	ILE	0	0.008	0.022	25.895	0.001	0.001	0.000	0.000	0.000	0.000
60	A	2490	THR	0	-0.063	-0.051	25.616	0.008	0.008	0.000	0.000	0.000	0.000
61	A	2491	ILE	0	-0.012	0.001	21.441	0.006	0.006	0.000	0.000	0.000	0.000
62	A	2492	GLU	-1	-0.748	-0.874	21.493	-0.036	-0.036	0.000	0.000	0.000	0.000
63	A	2493	LYS	1	0.859	0.938	21.567	0.001	0.001	0.000	0.000	0.000	0.000
64	A	2494	GLN	0	-0.002	-0.020	20.300	0.017	0.017	0.000	0.000	0.000	0.000
65	A	2495	ILE	0	0.000	0.006	16.168	0.018	0.018	0.000	0.000	0.000	0.000
66	A	2496	LEU	0	0.006	0.007	16.338	0.022	0.022	0.000	0.000	0.000	0.000
67	A	2497	THR	0	-0.096	-0.033	17.140	0.021	0.021	0.000	0.000	0.000	0.000
68	A	2498	GLY	0	0.045	0.027	13.716	0.036	0.036	0.000	0.000	0.000	0.000
69	A	2499	TYR	0	-0.060	-0.024	14.228	0.005	0.005	0.000	0.000	0.000	0.000
70	A	2500	TYR	0	-0.109	-0.079	15.439	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	2501	LYS	1	0.955	0.972	11.721	0.022	0.022	0.000	0.000	0.000	0.000
72	A	2502	THR	0	0.002	-0.025	10.865	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	2503	VAL	0	0.061	0.029	13.020	0.041	0.041	0.000	0.000	0.000	0.000
74	A	2504	GLU	-1	-0.821	-0.889	14.792	-0.271	-0.271	0.000	0.000	0.000	0.000
75	A	2505	ALA	0	-0.050	-0.018	16.741	0.027	0.027	0.000	0.000	0.000	0.000
76	A	2506	PHE	0	0.045	0.019	16.800	0.022	0.022	0.000	0.000	0.000	0.000
77	A	2507	ASP	-1	-0.773	-0.834	18.609	-0.191	-0.191	0.000	0.000	0.000	0.000
78	A	2508	ALA	0	-0.045	-0.009	20.659	0.015	0.015	0.000	0.000	0.000	0.000
79	A	2509	ASP	-1	-0.762	-0.883	21.854	-0.042	-0.042	0.000	0.000	0.000	0.000
80	A	2510	MET	0	0.001	0.003	21.643	0.013	0.013	0.000	0.000	0.000	0.000
81	A	2511	LEU	0	-0.018	-0.029	24.213	0.009	0.009	0.000	0.000	0.000	0.000
82	A	2512	LYS	1	0.815	0.928	26.228	0.056	0.056	0.000	0.000	0.000	0.000
83	A	2513	VAL	0	0.017	0.016	27.089	0.006	0.006	0.000	0.000	0.000	0.000
84	A	2514	PHE	0	0.016	0.005	26.625	0.005	0.005	0.000	0.000	0.000	0.000
85	A	2515	ARG	1	0.916	0.967	30.490	0.062	0.062	0.000	0.000	0.000	0.000
86	A	2516	ASN	0	0.001	-0.025	31.467	0.004	0.004	0.000	0.000	0.000	0.000
87	A	2517	ALA	0	0.030	0.033	33.555	0.004	0.004	0.000	0.000	0.000	0.000
88	A	2518	GLU	-1	-0.798	-0.891	34.166	-0.064	-0.064	0.000	0.000	0.000	0.000
89	A	2519	LYS	1	0.799	0.896	36.022	0.043	0.043	0.000	0.000	0.000	0.000
90	A	2520	TYR	0	-0.038	-0.020	38.045	0.002	0.002	0.000	0.000	0.000	0.000
91	A	2521	TYR	0	0.052	0.019	37.580	0.003	0.003	0.000	0.000	0.000	0.000
92	A	2522	GLY	0	-0.004	0.008	40.276	0.001	0.001	0.000	0.000	0.000	0.000
93	A	2523	ARG	1	0.847	0.887	34.362	0.065	0.065	0.000	0.000	0.000	0.000
94	A	2524	LYS	1	1.015	1.015	39.997	0.037	0.037	0.000	0.000	0.000	0.000
95	A	2525	SER	0	0.001	0.004	41.341	0.001	0.001	0.000	0.000	0.000	0.000
96	A	2526	PRO	0	0.039	0.000	41.694	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	2527	VAL	0	0.113	0.056	37.340	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	2528	GLY	0	-0.027	0.005	37.132	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	2529	ARG	1	0.878	0.922	37.166	0.036	0.036	0.000	0.000	0.000	0.000
100	A	2530	ASP	-1	-0.847	-0.911	35.869	-0.049	-0.049	0.000	0.000	0.000	0.000
101	A	2531	VAL	0	-0.010	-0.001	32.114	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	2532	CYS	0	-0.038	-0.022	32.347	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	2533	ARG	1	0.889	0.937	32.740	0.054	0.054	0.000	0.000	0.000	0.000
104	A	2534	LEU	0	0.035	0.017	29.732	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	2535	ARG	1	0.876	0.952	28.195	0.077	0.077	0.000	0.000	0.000	0.000
106	A	2536	LYS	1	0.886	0.954	27.490	0.070	0.070	0.000	0.000	0.000	0.000
107	A	2537	ALA	0	0.007	0.017	27.579	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	2538	TYR	0	-0.010	-0.042	20.391	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	2539	TYR	0	-0.009	-0.030	23.137	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	2540	ASN	0	-0.024	0.007	23.313	-0.016	-0.016	0.000	0.000	0.000	0.000
111	A	2541	ALA	0	0.090	0.052	21.369	-0.014	-0.014	0.000	0.000	0.000	0.000
112	A	2542	ARG	1	0.816	0.875	16.777	0.243	0.243	0.000	0.000	0.000	0.000
113	A	2543	HIS	0	-0.038	-0.019	18.509	-0.036	-0.036	0.000	0.000	0.000	0.000
114	A	2544	GLU	-1	-0.923	-0.960	19.122	-0.196	-0.196	0.000	0.000	0.000	0.000
115	A	2545	ALA	0	0.018	0.017	15.128	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	2546	SER	0	-0.095	-0.067	14.201	-0.083	-0.083	0.000	0.000	0.000	0.000
117	A	2547	ALA	0	0.064	0.040	13.702	-0.065	-0.065	0.000	0.000	0.000	0.000
118	A	2548	GLN	0	0.042	0.018	11.070	-0.071	-0.071	0.000	0.000	0.000	0.000
119	A	2549	ILE	0	-0.046	-0.039	9.341	-0.241	-0.241	0.000	0.000	0.000	0.000
120	A	2550	ASP	-1	-0.903	-0.944	9.255	-0.777	-0.777	0.000	0.000	0.000	0.000
121	A	2551	GLU	-1	-0.968	-0.983	8.204	-1.063	-1.063	0.000	0.000	0.000	0.000
122	A	2552	ILE	0	-0.078	-0.032	4.349	-0.835	-0.745	-0.001	-0.005	-0.084	0.000
123	A	2553	VAL	0	0.008	-0.008	4.606	-0.884	-0.865	-0.001	-0.005	-0.012	0.000
124	A	2554	GLY	0	-0.022	0.005	7.075	0.073	0.073	0.000	0.000	0.000	0.000
125	A	2555	GLU	-1	-0.759	-0.806	1.559	-32.446	-41.292	24.416	-10.246	-5.323	-0.086
126	A	2556	THR	0	-0.133	-0.071	3.248	-1.122	-0.068	0.044	-0.534	-0.564	-0.004

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