FMO DATABASE

FMODB ID: 17GKZ

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	OptAll
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	-1077975.177104
FMO2-HF: Nuclear repulsion	1027723.148547
FMO2-HF: Total energy	-50252.028557
FMO2-MP2: Total energy	-50398.957885

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.
-42.154	-43.092	28.95	-15.537	-12.474	-0.072

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 : 0.035 / q_NPA : -0.007

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	-0.804	-0.891	3.873	-0.367	1.972	-0.010	-1.257	-1.072	0.006
4	A	2434	VAL	0	0.013	-0.002	6.278	0.012	0.012	0.000	0.000	0.000	0.000
5	A	2435	ALA	0	0.001	0.008	3.940	-0.366	-0.258	0.000	-0.022	-0.085	0.000
6	A	2436	ARG	1	0.865	0.923	2.487	-7.416	-5.198	2.701	-1.801	-3.118	0.020
7	A	2437	ALA	0	0.031	0.011	4.972	-0.556	-0.482	-0.001	-0.005	-0.068	0.000
8	A	2438	ALA	0	-0.012	-0.009	8.657	-0.125	-0.125	0.000	0.000	0.000	0.000
9	A	2439	ARG	1	0.807	0.865	3.093	4.968	5.468	0.003	-0.251	-0.252	0.000
10	A	2440	LEU	0	0.014	0.011	8.011	0.001	0.001	0.000	0.000	0.000	0.000
11	A	2441	ALA	0	-0.006	-0.001	10.200	0.045	0.045	0.000	0.000	0.000	0.000
12	A	2442	GLN	0	-0.052	-0.036	12.307	0.056	0.056	0.000	0.000	0.000	0.000
13	A	2443	ILE	0	0.058	0.036	10.819	0.035	0.035	0.000	0.000	0.000	0.000
14	A	2444	PHE	0	-0.019	-0.026	12.613	0.042	0.042	0.000	0.000	0.000	0.000
15	A	2445	LYS	1	0.839	0.900	16.236	0.157	0.157	0.000	0.000	0.000	0.000
16	A	2446	GLU	-1	-0.859	-0.909	16.425	-0.301	-0.301	0.000	0.000	0.000	0.000
17	A	2447	ILE	0	-0.028	-0.015	17.031	0.026	0.026	0.000	0.000	0.000	0.000
18	A	2448	CYS	0	-0.097	-0.051	20.218	0.025	0.025	0.000	0.000	0.000	0.000
19	A	2449	ASP	-1	-0.803	-0.896	22.023	-0.114	-0.114	0.000	0.000	0.000	0.000
20	A	2450	GLY	0	0.007	0.033	23.098	0.013	0.013	0.000	0.000	0.000	0.000
21	A	2451	ILE	0	-0.082	-0.042	24.559	0.012	0.012	0.000	0.000	0.000	0.000
22	A	2452	ILE	0	0.003	-0.014	25.098	0.012	0.012	0.000	0.000	0.000	0.000
23	A	2453	SER	0	-0.081	-0.053	27.171	0.010	0.010	0.000	0.000	0.000	0.000
24	A	2454	TYR	0	0.035	0.030	29.071	0.010	0.010	0.000	0.000	0.000	0.000
25	A	2455	LYS	1	0.861	0.914	30.725	0.085	0.085	0.000	0.000	0.000	0.000
26	A	2456	ASP	-1	-0.836	-0.906	34.232	-0.067	-0.067	0.000	0.000	0.000	0.000
27	A	2457	SER	0	0.039	0.009	37.018	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	2458	SER	0	-0.055	-0.041	39.641	0.003	0.003	0.000	0.000	0.000	0.000
29	A	2459	ARG	1	0.892	0.950	38.117	0.054	0.054	0.000	0.000	0.000	0.000
30	A	2460	GLN	0	0.037	0.026	38.288	0.000	0.000	0.000	0.000	0.000	0.000
31	A	2461	ALA	0	0.028	0.006	34.394	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	2462	LEU	0	-0.028	-0.017	33.986	0.001	0.001	0.000	0.000	0.000	0.000
33	A	2463	ALA	0	0.053	0.029	30.547	0.001	0.001	0.000	0.000	0.000	0.000
34	A	2464	ALA	0	0.025	0.013	32.561	0.001	0.001	0.000	0.000	0.000	0.000
35	A	2465	PRO	0	-0.071	-0.044	35.041	0.002	0.002	0.000	0.000	0.000	0.000
36	A	2466	LEU	0	-0.044	-0.018	30.333	0.002	0.002	0.000	0.000	0.000	0.000
37	A	2467	LEU	0	0.017	0.017	30.113	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	2468	ASN	0	-0.016	-0.012	31.011	0.001	0.001	0.000	0.000	0.000	0.000
39	A	2469	LEU	0	0.002	0.004	32.149	0.001	0.001	0.000	0.000	0.000	0.000
40	A	2470	PRO	0	0.006	0.007	35.097	0.003	0.003	0.000	0.000	0.000	0.000
41	A	2471	PRO	0	0.031	0.019	38.976	0.001	0.001	0.000	0.000	0.000	0.000
42	A	2472	LYS	1	0.832	0.923	39.980	0.031	0.031	0.000	0.000	0.000	0.000
43	A	2473	LYS	1	0.957	0.971	41.693	0.023	0.023	0.000	0.000	0.000	0.000
44	A	2474	LYS	1	0.901	0.950	44.532	0.033	0.033	0.000	0.000	0.000	0.000
45	A	2475	ASN	0	-0.033	-0.011	42.057	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	2476	ALA	0	0.048	0.026	42.650	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	2477	ASP	-1	-0.716	-0.860	43.358	-0.036	-0.036	0.000	0.000	0.000	0.000
48	A	2478	TYR	0	0.012	-0.004	35.184	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	2479	TYR	0	-0.024	-0.047	36.201	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	2480	GLU	-1	-0.781	-0.871	39.681	-0.031	-0.031	0.000	0.000	0.000	0.000
51	A	2481	LYS	1	0.807	0.925	40.775	0.042	0.042	0.000	0.000	0.000	0.000
52	A	2482	ILE	0	-0.138	-0.070	34.464	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	2483	SER	0	0.059	0.021	35.300	0.001	0.001	0.000	0.000	0.000	0.000
54	A	2484	ASP	-1	-0.831	-0.895	29.131	-0.065	-0.065	0.000	0.000	0.000	0.000
55	A	2485	PRO	0	-0.024	-0.013	31.611	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	2486	LEU	0	0.004	0.002	25.214	0.001	0.001	0.000	0.000	0.000	0.000
57	A	2487	ASP	-1	-0.798	-0.871	28.904	-0.059	-0.059	0.000	0.000	0.000	0.000
58	A	2488	LEU	0	0.058	0.007	25.970	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	2489	ILE	0	0.013	0.020	25.702	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	2490	THR	0	-0.082	-0.060	25.971	0.003	0.003	0.000	0.000	0.000	0.000
61	A	2491	ILE	0	0.009	0.003	21.493	0.002	0.002	0.000	0.000	0.000	0.000
62	A	2492	GLU	-1	-0.725	-0.855	21.530	-0.125	-0.125	0.000	0.000	0.000	0.000
63	A	2493	LYS	1	0.868	0.935	21.244	0.047	0.047	0.000	0.000	0.000	0.000
64	A	2494	GLN	0	-0.010	-0.003	20.358	0.016	0.016	0.000	0.000	0.000	0.000
65	A	2495	ILE	0	-0.012	-0.005	16.207	0.008	0.008	0.000	0.000	0.000	0.000
66	A	2496	LEU	0	-0.014	-0.001	16.465	0.002	0.002	0.000	0.000	0.000	0.000
67	A	2497	THR	0	-0.085	-0.037	17.870	0.017	0.017	0.000	0.000	0.000	0.000
68	A	2498	GLY	0	0.036	0.023	14.132	0.022	0.022	0.000	0.000	0.000	0.000
69	A	2499	TYR	0	-0.049	-0.020	14.284	0.011	0.011	0.000	0.000	0.000	0.000
70	A	2500	TYR	0	-0.108	-0.085	15.568	0.005	0.005	0.000	0.000	0.000	0.000
71	A	2501	LYS	1	0.931	0.959	11.911	0.049	0.049	0.000	0.000	0.000	0.000
72	A	2502	THR	0	0.006	-0.006	10.908	0.004	0.004	0.000	0.000	0.000	0.000
73	A	2503	VAL	0	0.051	0.026	12.832	0.027	0.027	0.000	0.000	0.000	0.000
74	A	2504	GLU	-1	-0.813	-0.895	14.835	-0.261	-0.261	0.000	0.000	0.000	0.000
75	A	2505	ALA	0	-0.036	-0.016	16.918	0.026	0.026	0.000	0.000	0.000	0.000
76	A	2506	PHE	0	0.029	0.011	17.044	0.022	0.022	0.000	0.000	0.000	0.000
77	A	2507	ASP	-1	-0.758	-0.831	18.819	-0.218	-0.218	0.000	0.000	0.000	0.000
78	A	2508	ALA	0	-0.030	-0.011	20.871	0.016	0.016	0.000	0.000	0.000	0.000
79	A	2509	ASP	-1	-0.758	-0.874	22.133	-0.080	-0.080	0.000	0.000	0.000	0.000
80	A	2510	MET	0	0.008	0.009	21.776	0.016	0.016	0.000	0.000	0.000	0.000
81	A	2511	LEU	0	-0.028	-0.023	24.148	0.012	0.012	0.000	0.000	0.000	0.000
82	A	2512	LYS	1	0.813	0.924	26.164	0.086	0.086	0.000	0.000	0.000	0.000
83	A	2513	VAL	0	0.005	0.013	27.344	0.008	0.008	0.000	0.000	0.000	0.000
84	A	2514	PHE	0	0.031	0.010	26.605	0.008	0.008	0.000	0.000	0.000	0.000
85	A	2515	ARG	1	0.900	0.956	30.482	0.075	0.075	0.000	0.000	0.000	0.000
86	A	2516	ASN	0	0.025	-0.010	31.598	0.007	0.007	0.000	0.000	0.000	0.000
87	A	2517	ALA	0	0.037	0.028	33.683	0.005	0.005	0.000	0.000	0.000	0.000
88	A	2518	GLU	-1	-0.834	-0.909	33.931	-0.078	-0.078	0.000	0.000	0.000	0.000
89	A	2519	LYS	1	0.819	0.916	35.775	0.057	0.057	0.000	0.000	0.000	0.000
90	A	2520	TYR	0	-0.059	-0.028	38.039	0.003	0.003	0.000	0.000	0.000	0.000
91	A	2521	TYR	0	0.060	0.026	37.607	0.004	0.004	0.000	0.000	0.000	0.000
92	A	2522	GLY	0	-0.006	0.008	40.244	0.002	0.002	0.000	0.000	0.000	0.000
93	A	2523	ARG	1	0.872	0.898	34.194	0.076	0.076	0.000	0.000	0.000	0.000
94	A	2524	LYS	1	1.011	1.015	39.863	0.045	0.045	0.000	0.000	0.000	0.000
95	A	2525	SER	0	-0.001	0.006	41.217	0.001	0.001	0.000	0.000	0.000	0.000
96	A	2526	PRO	0	0.038	0.007	41.703	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	2527	VAL	0	0.110	0.053	37.129	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	2528	GLY	0	-0.018	0.001	37.132	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	2529	ARG	1	0.861	0.926	37.127	0.048	0.048	0.000	0.000	0.000	0.000
100	A	2530	ASP	-1	-0.845	-0.921	35.964	-0.069	-0.069	0.000	0.000	0.000	0.000
101	A	2531	VAL	0	-0.001	0.001	32.262	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	2532	CYS	0	-0.037	-0.019	32.303	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	2533	ARG	1	0.880	0.945	32.903	0.077	0.077	0.000	0.000	0.000	0.000
104	A	2534	LEU	0	0.043	0.022	29.608	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	2535	ARG	1	0.815	0.910	28.246	0.093	0.093	0.000	0.000	0.000	0.000
106	A	2536	LYS	1	0.883	0.936	27.424	0.086	0.086	0.000	0.000	0.000	0.000
107	A	2537	ALA	0	0.012	0.018	27.461	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	2538	TYR	0	-0.006	-0.031	20.206	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	2539	TYR	0	-0.008	-0.020	22.874	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	2540	ASN	0	-0.027	-0.001	23.143	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	2541	ALA	0	0.089	0.050	21.336	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	2542	ARG	1	0.812	0.869	16.639	0.266	0.266	0.000	0.000	0.000	0.000
113	A	2543	HIS	0	-0.033	-0.006	18.340	-0.032	-0.032	0.000	0.000	0.000	0.000
114	A	2544	GLU	-1	-0.918	-0.957	19.226	-0.224	-0.224	0.000	0.000	0.000	0.000
115	A	2545	ALA	0	0.022	0.014	15.402	-0.024	-0.024	0.000	0.000	0.000	0.000
116	A	2546	SER	0	-0.078	-0.054	14.376	-0.078	-0.078	0.000	0.000	0.000	0.000
117	A	2547	ALA	0	0.059	0.029	13.543	-0.066	-0.066	0.000	0.000	0.000	0.000
118	A	2548	GLN	0	0.054	0.026	11.060	-0.055	-0.055	0.000	0.000	0.000	0.000
119	A	2549	ILE	0	-0.039	-0.025	9.370	-0.245	-0.245	0.000	0.000	0.000	0.000
120	A	2550	ASP	-1	-0.909	-0.958	9.181	-0.698	-0.698	0.000	0.000	0.000	0.000
121	A	2551	GLU	-1	-0.959	-0.982	8.134	-1.027	-1.027	0.000	0.000	0.000	0.000
122	A	2552	ILE	0	-0.072	-0.030	4.485	-0.765	-0.696	-0.001	-0.003	-0.065	0.000
123	A	2553	VAL	0	-0.013	-0.012	4.424	-0.521	-0.503	-0.001	-0.011	-0.006	0.000
124	A	2554	GLY	0	0.015	0.018	6.915	0.120	0.120	0.000	0.000	0.000	0.000
125	A	2555	GLU	-1	-0.818	-0.834	1.594	-29.609	-38.023	24.341	-10.216	-5.711	-0.070
126	A	2556	THR	0	-0.112	-0.061	2.281	-5.448	-3.298	1.918	-1.971	-2.097	-0.028

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