FMO DATABASE

FMODB ID: Z2QGN

Calculation Name: 1T38-A-Xray310

Preferred Name: 6-O-methylguanine-DNA methyltransferase

Target Type: SINGLE PROTEIN

Ligand Name: 6-o-methyl guanosine-5'-monophosphate

ligand 3-letter code: 6OG

PDB ID: 1T38

Chain ID: A

ChEMBL ID: CHEMBL2864

UniProt ID: P16455

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1414406.461461
FMO2-HF: Nuclear repulsion	1355970.335007
FMO2-HF: Total energy	-58436.126454
FMO2-MP2: Total energy	-58606.486

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:5:ACE )

Summations of interaction energy for fragment #1(A:5:ACE )

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.
2.337	4.616	0.671	-1.26	-1.688	-0.004

Interaction energy analysis for fragmet #1(A:5:ACE )

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 : 0.006

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	7	MET	0	-0.050	-0.019	3.844	1.222	2.025	-0.005	-0.372	-0.426	0.000
4	A	8	LYS	1	0.968	0.994	6.729	0.749	0.749	0.000	0.000	0.000	0.000
5	A	9	ARG	1	0.870	0.921	9.535	0.330	0.330	0.000	0.000	0.000	0.000
6	A	10	THR	0	0.030	0.028	13.115	-0.011	-0.011	0.000	0.000	0.000	0.000
7	A	11	THR	0	-0.040	-0.004	16.083	0.020	0.020	0.000	0.000	0.000	0.000
8	A	12	LEU	0	0.051	0.024	19.720	0.003	0.003	0.000	0.000	0.000	0.000
9	A	13	ASP	-1	-0.896	-0.942	22.210	-0.041	-0.041	0.000	0.000	0.000	0.000
10	A	14	SER	0	0.001	-0.014	25.334	0.008	0.008	0.000	0.000	0.000	0.000
11	A	15	PRO	0	0.022	0.017	27.404	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	16	LEU	0	0.002	0.005	26.705	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	17	GLY	0	-0.013	0.005	27.834	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	18	LYS	1	0.893	0.939	23.621	0.057	0.057	0.000	0.000	0.000	0.000
15	A	19	LEU	0	0.046	0.027	20.927	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.897	-0.958	16.333	-0.161	-0.161	0.000	0.000	0.000	0.000
17	A	21	LEU	0	-0.018	-0.017	15.057	0.004	0.004	0.000	0.000	0.000	0.000
18	A	22	SER	0	-0.021	-0.010	11.212	-0.029	-0.029	0.000	0.000	0.000	0.000
19	A	23	GLY	0	0.041	-0.012	8.323	0.077	0.077	0.000	0.000	0.000	0.000
20	A	24	CYS	0	-0.047	0.005	2.684	-0.126	0.125	0.387	-0.290	-0.348	0.001
21	A	25	GLU	-1	-0.904	-0.981	4.171	0.634	0.766	0.000	-0.019	-0.112	0.000
22	A	26	GLN	0	-0.033	-0.014	2.992	-0.047	1.015	0.289	-0.575	-0.775	-0.005
23	A	27	GLY	0	0.024	0.001	6.143	-0.239	-0.239	0.000	0.000	0.000	0.000
24	A	28	LEU	0	-0.059	-0.045	8.313	-0.056	-0.056	0.000	0.000	0.000	0.000
25	A	29	HIS	0	-0.032	-0.024	8.707	0.068	0.068	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.968	-1.000	10.516	-0.070	-0.070	0.000	0.000	0.000	0.000
27	A	31	ILE	0	-0.009	0.014	14.119	-0.025	-0.025	0.000	0.000	0.000	0.000
28	A	32	LYS	1	0.971	0.985	17.274	0.099	0.099	0.000	0.000	0.000	0.000
29	A	33	LEU	0	0.024	-0.007	19.385	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	34	LEU	0	-0.054	-0.020	20.849	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	35	GLY	0	-0.002	0.006	24.118	0.001	0.001	0.000	0.000	0.000	0.000
32	A	36	NME	0	-0.026	0.000	27.691	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	55	ACE	0	0.006	-0.009	11.762	-0.013	-0.013	0.000	0.000	0.000	0.000
34	A	56	PRO	0	-0.002	-0.001	7.889	0.035	0.035	0.000	0.000	0.000	0.000
35	A	57	GLU	-1	-0.841	-0.935	10.029	0.274	0.274	0.000	0.000	0.000	0.000
36	A	58	PRO	0	-0.016	0.006	9.114	-0.046	-0.046	0.000	0.000	0.000	0.000
37	A	59	LEU	0	0.025	0.003	10.458	-0.037	-0.037	0.000	0.000	0.000	0.000
38	A	60	MET	0	-0.003	0.017	13.554	-0.027	-0.027	0.000	0.000	0.000	0.000
39	A	61	GLN	0	0.033	0.031	14.156	-0.019	-0.019	0.000	0.000	0.000	0.000
40	A	62	CYS	0	0.004	0.006	15.668	-0.017	-0.017	0.000	0.000	0.000	0.000
41	A	63	THR	0	-0.075	-0.049	16.705	-0.018	-0.018	0.000	0.000	0.000	0.000
42	A	64	ALA	0	0.007	0.008	19.137	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	65	TRP	0	0.050	0.026	20.530	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	66	LEU	0	0.005	-0.003	19.849	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	67	ASN	0	-0.041	-0.027	23.077	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	68	ALA	0	0.035	0.034	24.837	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	69	TYR	0	-0.056	-0.079	25.750	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	70	PHE	0	-0.027	-0.035	24.912	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	71	HIS	0	-0.038	-0.026	27.772	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	72	GLN	0	-0.021	-0.003	29.825	0.003	0.003	0.000	0.000	0.000	0.000
51	A	73	PRO	0	0.004	0.009	30.366	0.004	0.004	0.000	0.000	0.000	0.000
52	A	74	GLU	-1	-0.958	-0.978	31.427	0.028	0.028	0.000	0.000	0.000	0.000
53	A	75	ALA	0	-0.015	0.003	31.161	0.002	0.002	0.000	0.000	0.000	0.000
54	A	76	ILE	0	0.012	0.006	25.259	0.002	0.002	0.000	0.000	0.000	0.000
55	A	77	GLU	-1	-0.925	-0.981	26.371	0.076	0.076	0.000	0.000	0.000	0.000
56	A	78	GLU	-1	-0.995	-0.981	26.892	0.060	0.060	0.000	0.000	0.000	0.000
57	A	79	PHE	0	-0.029	-0.010	22.778	0.007	0.007	0.000	0.000	0.000	0.000
58	A	80	PRO	0	-0.013	0.005	19.059	0.002	0.002	0.000	0.000	0.000	0.000
59	A	81	VAL	0	-0.001	-0.013	18.270	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	82	PRO	0	-0.011	-0.002	14.026	0.023	0.023	0.000	0.000	0.000	0.000
61	A	83	ALA	0	0.043	0.035	11.279	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	84	LEU	0	-0.021	-0.002	11.819	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	85	HIS	0	0.022	0.003	4.597	-0.005	0.026	0.000	-0.004	-0.027	0.000
64	A	86	HIS	0	0.037	0.019	9.281	0.016	0.016	0.000	0.000	0.000	0.000
65	A	87	PRO	0	-0.010	-0.008	10.052	0.033	0.033	0.000	0.000	0.000	0.000
66	A	88	VAL	0	-0.027	-0.003	12.134	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	89	PHE	0	-0.008	-0.023	12.712	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	90	GLN	0	0.003	0.015	8.249	-0.060	-0.060	0.000	0.000	0.000	0.000
69	A	91	GLN	0	-0.015	-0.012	13.818	-0.018	-0.018	0.000	0.000	0.000	0.000
70	A	92	GLU	-1	-0.855	-0.939	16.905	0.122	0.122	0.000	0.000	0.000	0.000
71	A	93	SER	0	-0.024	-0.017	20.136	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	94	PHE	0	0.027	0.014	22.641	0.003	0.003	0.000	0.000	0.000	0.000
73	A	95	THR	0	0.032	0.009	20.388	0.000	0.000	0.000	0.000	0.000	0.000
74	A	96	ARG	1	0.915	0.995	16.943	-0.179	-0.179	0.000	0.000	0.000	0.000
75	A	97	GLN	0	0.067	0.048	20.622	0.010	0.010	0.000	0.000	0.000	0.000
76	A	98	VAL	0	-0.014	-0.022	23.758	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	99	LEU	0	-0.012	-0.016	19.205	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	100	TRP	0	0.026	0.022	16.949	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	101	LYS	1	0.858	0.920	22.289	-0.085	-0.085	0.000	0.000	0.000	0.000
80	A	102	LEU	0	-0.038	-0.019	24.589	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	103	LEU	0	0.021	0.006	20.149	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	104	LYS	1	0.900	0.962	24.091	-0.093	-0.093	0.000	0.000	0.000	0.000
83	A	105	VAL	0	-0.081	-0.055	25.830	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	106	VAL	0	0.018	0.021	28.155	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	107	LYS	1	0.896	0.944	27.512	-0.072	-0.072	0.000	0.000	0.000	0.000
86	A	108	PHE	0	0.048	0.004	29.722	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	109	GLY	0	0.063	0.052	31.464	0.000	0.000	0.000	0.000	0.000	0.000
88	A	110	GLU	-1	-0.940	-0.953	32.864	0.046	0.046	0.000	0.000	0.000	0.000
89	A	111	VAL	0	-0.022	-0.030	33.386	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	112	ILE	0	-0.032	-0.006	31.128	0.001	0.001	0.000	0.000	0.000	0.000
91	A	113	SER	0	0.004	-0.010	33.344	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	114	TYR	0	0.036	-0.003	30.813	0.002	0.002	0.000	0.000	0.000	0.000
93	A	115	GLN	0	-0.002	-0.020	33.219	0.003	0.003	0.000	0.000	0.000	0.000
94	A	116	GLN	0	0.041	0.042	35.446	0.001	0.001	0.000	0.000	0.000	0.000
95	A	117	LEU	0	0.031	0.022	27.594	0.003	0.003	0.000	0.000	0.000	0.000
96	A	118	ALA	0	-0.034	-0.008	30.656	0.004	0.004	0.000	0.000	0.000	0.000
97	A	119	ALA	0	-0.023	-0.032	32.229	0.003	0.003	0.000	0.000	0.000	0.000
98	A	120	LEU	0	-0.044	0.009	30.433	0.003	0.003	0.000	0.000	0.000	0.000
99	A	121	ALA	0	-0.019	-0.007	27.470	0.005	0.005	0.000	0.000	0.000	0.000
100	A	122	GLY	0	0.046	0.013	29.043	0.005	0.005	0.000	0.000	0.000	0.000
101	A	123	ASN	0	-0.012	-0.006	31.668	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	124	PRO	0	0.075	0.027	33.739	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	125	LYS	1	0.958	0.982	36.115	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	126	ALA	0	-0.055	-0.011	31.770	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	127	ALA	0	0.088	0.031	31.991	0.002	0.002	0.000	0.000	0.000	0.000
106	A	128	ARG	1	0.964	0.978	32.312	-0.010	-0.010	0.000	0.000	0.000	0.000
107	A	129	ALA	0	0.008	0.003	29.076	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	130	VAL	0	0.037	0.027	27.997	0.002	0.002	0.000	0.000	0.000	0.000
109	A	131	GLY	0	0.003	0.009	27.748	0.000	0.000	0.000	0.000	0.000	0.000
110	A	132	GLY	0	-0.006	-0.014	27.070	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	133	ALA	0	0.022	0.024	23.983	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	134	MET	0	0.011	0.004	23.149	0.002	0.002	0.000	0.000	0.000	0.000
113	A	135	ARG	1	0.841	0.930	24.286	0.007	0.007	0.000	0.000	0.000	0.000
114	A	136	GLY	0	-0.005	-0.024	21.797	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	137	ASN	0	0.023	0.027	19.757	0.001	0.001	0.000	0.000	0.000	0.000
116	A	138	PRO	0	0.032	0.027	15.379	-0.010	-0.010	0.000	0.000	0.000	0.000
117	A	139	VAL	0	-0.010	-0.015	15.498	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	140	PRO	0	0.057	0.038	18.286	0.008	0.008	0.000	0.000	0.000	0.000
119	A	141	ILE	0	0.000	0.006	21.530	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	142	LEU	0	0.003	-0.008	17.273	0.005	0.005	0.000	0.000	0.000	0.000
121	A	143	ILE	0	-0.038	0.002	18.902	0.006	0.006	0.000	0.000	0.000	0.000
122	A	144	PRO	0	0.007	-0.008	22.102	-0.009	-0.009	0.000	0.000	0.000	0.000
123	A	145	SER	0	0.022	-0.009	23.917	0.000	0.000	0.000	0.000	0.000	0.000
124	A	146	HIS	0	-0.081	-0.066	26.495	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	147	ARG	1	0.848	0.910	27.531	-0.046	-0.046	0.000	0.000	0.000	0.000
126	A	148	VAL	0	-0.017	0.008	28.616	0.001	0.001	0.000	0.000	0.000	0.000
127	A	149	VAL	0	0.003	0.008	31.562	-0.004	-0.004	0.000	0.000	0.000	0.000
128	A	150	CYS	0	-0.082	-0.060	34.937	0.001	0.001	0.000	0.000	0.000	0.000
129	A	151	SER	0	0.064	0.009	37.686	0.001	0.001	0.000	0.000	0.000	0.000
130	A	152	SER	0	-0.074	-0.021	39.877	0.001	0.001	0.000	0.000	0.000	0.000
131	A	153	GLY	0	0.055	0.037	41.047	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	154	ALA	0	-0.016	-0.003	40.576	0.000	0.000	0.000	0.000	0.000	0.000
133	A	155	VAL	0	0.177	0.081	35.597	0.002	0.002	0.000	0.000	0.000	0.000
134	A	156	GLY	0	0.022	0.025	35.419	0.002	0.002	0.000	0.000	0.000	0.000
135	A	157	ASN	0	0.006	0.002	33.281	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	158	TYR	0	0.054	-0.005	25.972	0.006	0.006	0.000	0.000	0.000	0.000
137	A	159	SER	0	0.003	0.004	24.517	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	160	GLY	0	0.005	0.017	26.545	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	161	GLY	0	0.014	0.005	27.131	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	162	LEU	0	-0.064	-0.047	30.921	0.001	0.001	0.000	0.000	0.000	0.000
141	A	163	ALA	0	0.060	0.046	33.433	0.002	0.002	0.000	0.000	0.000	0.000
142	A	164	VAL	0	0.020	0.014	27.858	0.002	0.002	0.000	0.000	0.000	0.000
143	A	165	LYS	1	0.762	0.875	30.968	-0.012	-0.012	0.000	0.000	0.000	0.000
144	A	166	GLU	-1	-0.891	-0.948	31.760	0.005	0.005	0.000	0.000	0.000	0.000
145	A	167	TRP	0	0.035	0.015	30.674	0.002	0.002	0.000	0.000	0.000	0.000
146	A	168	LEU	0	-0.009	-0.018	27.627	0.001	0.001	0.000	0.000	0.000	0.000
147	A	169	LEU	0	-0.002	0.003	32.037	0.002	0.002	0.000	0.000	0.000	0.000
148	A	170	ALA	0	-0.002	0.008	34.547	0.001	0.001	0.000	0.000	0.000	0.000
149	A	171	HIS	0	-0.028	-0.013	31.214	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	172	GLU	-1	-0.803	-0.798	30.114	0.035	0.035	0.000	0.000	0.000	0.000
151	A	173	GLY	0	0.018	0.000	34.726	0.002	0.002	0.000	0.000	0.000	0.000
152	A	174	HIS	0	-0.067	-0.021	35.776	-0.002	-0.002	0.000	0.000	0.000	0.000
153	A	175	ARG	1	0.908	0.947	39.395	-0.012	-0.012	0.000	0.000	0.000	0.000
154	A	176	LEU	-1	-0.943	-0.966	38.419	0.007	0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ACE )