FMO DATABASE

FMODB ID: PJQG9

Calculation Name: 3FMY-A-Xray22

Preferred Name:

Target Type:

Ligand Name: n5-methylglutamine

ligand 3-letter code: MEQ

PDB ID: 3FMY

Chain ID: A

ChEMBL ID:

UniProt ID: Q46864

Base Structure: X-ray

Registration Date: 2018-06-07

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	Apo structure with with a 3 angstrom solvent shell.
Procedure	Auto-FMO protocol ver. 1.20180227

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	117
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-481621.26937
FMO2-HF: Nuclear repulsion	452395.466052
FMO2-HF: Total energy	-29225.803318
FMO2-MP2: Total energy	-29312.148293

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:65:ACE)

Summations of interaction energy for fragment #1(A:65: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.
2.111	2.87	-0.011	-0.316	-0.432	0

Interaction energy analysis for fragmet #1(A:65:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / q_NPA : 0.003

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].
3	A	67	GLU	-1	-0.800	-0.832	3.844	0.511	1.270	-0.011	-0.316	-0.432
4	A	68	THR	0	0.047	0.013	6.859	-0.073	-0.073	0.000	0.000	0.000
5	A	69	VAL	0	0.019	0.011	9.086	0.060	0.060	0.000	0.000	0.000
6	A	70	ALA	0	0.049	0.036	12.816	0.012	0.012	0.000	0.000	0.000
7	A	71	PRO	0	0.071	0.034	15.641	-0.015	-0.015	0.000	0.000	0.000
8	A	72	GLU	-1	-0.860	-0.940	18.054	-0.100	-0.100	0.000	0.000	0.000
9	A	73	PHE	0	-0.029	-0.013	17.387	0.010	0.010	0.000	0.000	0.000
10	A	74	ILE	0	0.016	0.010	15.854	-0.002	-0.002	0.000	0.000	0.000
11	A	75	VAL	0	-0.011	0.002	19.711	0.010	0.010	0.000	0.000	0.000
12	A	76	LYS	1	0.840	0.926	22.246	0.123	0.123	0.000	0.000	0.000
13	A	77	VAL	0	0.021	0.016	20.646	0.011	0.011	0.000	0.000	0.000
14	A	78	ARG	1	0.799	0.867	23.337	0.128	0.128	0.000	0.000	0.000
15	A	79	LYS	1	0.864	0.922	24.945	0.093	0.093	0.000	0.000	0.000
16	A	80	LYS	1	0.809	0.906	25.285	0.115	0.115	0.000	0.000	0.000
17	A	81	LEU	0	0.001	0.011	24.253	0.004	0.004	0.000	0.000	0.000
18	A	82	SER	0	-0.062	-0.018	28.534	0.004	0.004	0.000	0.000	0.000
19	A	83	LEU	0	0.018	0.029	25.882	0.001	0.001	0.000	0.000	0.000
20	A	84	THR	0	0.007	0.014	28.828	-0.001	-0.001	0.000	0.000	0.000
21	A	85	GLN	0	-0.021	-0.047	25.015	-0.003	-0.003	0.000	0.000	0.000
22	A	86	LYS	1	0.902	0.952	25.883	0.083	0.083	0.000	0.000	0.000
23	A	87	GLU	-1	-0.792	-0.899	27.660	-0.101	-0.101	0.000	0.000	0.000
24	A	88	ALA	0	0.044	0.024	23.423	-0.006	-0.006	0.000	0.000	0.000
25	A	89	SER	0	0.009	-0.010	22.842	-0.021	-0.021	0.000	0.000	0.000
26	A	90	GLU	-1	-0.860	-0.890	23.724	-0.118	-0.118	0.000	0.000	0.000
27	A	91	ILE	0	0.006	0.021	24.028	-0.004	-0.004	0.000	0.000	0.000
28	A	92	PHE	0	-0.043	-0.030	19.689	-0.014	-0.014	0.000	0.000	0.000
29	A	93	GLY	0	0.011	0.027	19.895	-0.027	-0.027	0.000	0.000	0.000
30	A	94	GLY	0	0.000	-0.014	19.117	-0.014	-0.014	0.000	0.000	0.000
31	A	95	GLY	0	-0.012	0.008	19.870	0.008	0.008	0.000	0.000	0.000
32	A	96	VAL	0	0.090	0.032	23.307	-0.005	-0.005	0.000	0.000	0.000
33	A	97	ASN	0	-0.014	0.013	24.289	0.006	0.006	0.000	0.000	0.000
34	A	98	ALA	0	-0.047	0.000	19.779	0.000	0.000	0.000	0.000	0.000
35	A	99	PHE	0	0.082	0.019	20.137	-0.009	-0.009	0.000	0.000	0.000
36	A	100	SER	0	-0.028	0.018	21.739	0.005	0.005	0.000	0.000	0.000
37	A	101	ARG	1	0.903	0.929	18.400	0.199	0.199	0.000	0.000	0.000
38	A	102	TYR	0	-0.013	-0.007	16.118	-0.003	-0.003	0.000	0.000	0.000
39	A	103	GLU	-1	-0.712	-0.816	17.953	-0.134	-0.134	0.000	0.000	0.000
40	A	104	LYS	1	0.868	0.949	20.584	0.105	0.105	0.000	0.000	0.000
41	A	105	GLY	0	0.022	0.017	16.488	0.015	0.015	0.000	0.000	0.000
42	A	106	ASN	0	-0.038	-0.014	15.954	0.004	0.004	0.000	0.000	0.000
43	A	107	ALA	0	-0.038	-0.024	14.667	0.005	0.005	0.000	0.000	0.000
44	A	108	MEQ	0	0.001	0.009	7.803	0.155	0.155	0.000	0.000	0.000
45	A	109	PRO	0	0.028	0.022	12.325	-0.011	-0.011	0.000	0.000	0.000
46	A	110	HIS	0	0.055	0.023	11.529	-0.181	-0.181	0.000	0.000	0.000
47	A	111	PRO	0	0.027	0.008	8.240	0.064	0.064	0.000	0.000	0.000
48	A	112	SER	0	0.035	-0.007	10.672	0.054	0.054	0.000	0.000	0.000
49	A	113	THR	0	0.026	0.031	14.160	0.053	0.053	0.000	0.000	0.000
50	A	114	ILE	0	-0.033	0.002	10.153	0.044	0.044	0.000	0.000	0.000
51	A	115	LYS	1	0.874	0.927	8.935	0.952	0.952	0.000	0.000	0.000
52	A	116	LEU	0	0.053	0.040	14.759	0.044	0.044	0.000	0.000	0.000
53	A	117	LEU	0	0.024	0.011	17.063	0.036	0.036	0.000	0.000	0.000
54	A	118	ARG	1	0.787	0.867	12.124	0.397	0.397	0.000	0.000	0.000
55	A	119	VAL	0	0.011	0.008	18.109	0.028	0.028	0.000	0.000	0.000
56	A	120	LEU	0	0.042	0.011	20.438	0.020	0.020	0.000	0.000	0.000
57	A	121	ASP	-1	-0.757	-0.816	21.308	-0.114	-0.114	0.000	0.000	0.000
58	A	122	LYS	1	0.843	0.913	19.222	0.159	0.159	0.000	0.000	0.000
59	A	123	HIS	0	0.033	0.053	23.361	0.015	0.015	0.000	0.000	0.000
60	A	124	PRO	0	0.022	0.018	26.278	-0.006	-0.006	0.000	0.000	0.000
61	A	125	GLU	-1	-0.772	-0.870	27.500	-0.098	-0.098	0.000	0.000	0.000
62	A	126	LEU	0	-0.019	-0.004	24.813	0.000	0.000	0.000	0.000	0.000
63	A	127	LEU	0	-0.034	-0.015	26.596	-0.007	-0.007	0.000	0.000	0.000
64	A	128	ASN	0	-0.034	-0.028	28.113	-0.002	-0.002	0.000	0.000	0.000
65	A	129	GLU	-1	-0.890	-0.934	28.119	-0.109	-0.109	0.000	0.000	0.000
66	A	130	ILE	0	-0.099	-0.049	23.911	-0.007	-0.007	0.000	0.000	0.000
67	A	131	ARG	0	-0.050	-0.019	27.483	-0.014	-0.014	0.000	0.000	0.000
68	A	1	HOH	0	-0.010	-0.019	31.927	0.001	0.001	0.000	0.000	0.000
69	A	2	HOH	0	-0.031	-0.025	24.956	0.004	0.004	0.000	0.000	0.000
70	A	3	HOH	0	0.007	0.004	24.093	0.004	0.004	0.000	0.000	0.000
71	A	4	HOH	0	-0.008	-0.007	23.773	-0.002	-0.002	0.000	0.000	0.000
72	A	5	HOH	0	0.010	0.002	24.910	-0.001	-0.001	0.000	0.000	0.000
73	A	7	HOH	0	-0.039	-0.040	14.608	0.006	0.006	0.000	0.000	0.000
74	A	8	HOH	0	0.036	0.024	29.731	-0.003	-0.003	0.000	0.000	0.000
75	A	9	HOH	0	-0.023	-0.016	17.470	0.001	0.001	0.000	0.000	0.000
76	A	10	HOH	0	-0.031	-0.037	19.253	-0.007	-0.007	0.000	0.000	0.000
77	A	11	HOH	0	-0.013	-0.015	23.117	0.004	0.004	0.000	0.000	0.000
78	A	12	HOH	0	0.030	0.019	20.310	-0.001	-0.001	0.000	0.000	0.000
79	A	13	HOH	0	0.004	0.000	31.353	0.001	0.001	0.000	0.000	0.000
80	A	14	HOH	0	-0.022	-0.017	27.779	0.000	0.000	0.000	0.000	0.000
81	A	16	HOH	0	0.012	0.009	22.098	-0.001	-0.001	0.000	0.000	0.000
82	A	18	HOH	0	-0.043	-0.028	28.096	-0.001	-0.001	0.000	0.000	0.000
83	A	19	HOH	0	-0.035	-0.028	23.604	0.002	0.002	0.000	0.000	0.000
84	A	20	HOH	0	-0.033	-0.030	8.667	-0.072	-0.072	0.000	0.000	0.000
85	A	21	HOH	0	-0.072	-0.076	28.135	0.003	0.003	0.000	0.000	0.000
86	A	24	HOH	0	0.022	-0.003	24.344	0.001	0.001	0.000	0.000	0.000
87	A	27	HOH	0	0.004	0.008	32.445	-0.001	-0.001	0.000	0.000	0.000
88	A	29	HOH	0	-0.043	-0.032	27.079	0.002	0.002	0.000	0.000	0.000
89	A	34	HOH	0	0.036	0.023	16.154	-0.010	-0.010	0.000	0.000	0.000
90	A	35	HOH	0	0.008	0.006	17.189	0.000	0.000	0.000	0.000	0.000
91	A	36	HOH	0	0.024	0.014	14.342	-0.020	-0.020	0.000	0.000	0.000
92	A	38	HOH	0	0.026	0.006	7.842	-0.129	-0.129	0.000	0.000	0.000
93	A	43	HOH	0	0.043	0.036	9.895	-0.112	-0.112	0.000	0.000	0.000
94	A	44	HOH	0	-0.003	0.019	30.764	0.001	0.001	0.000	0.000	0.000
95	A	50	HOH	0	0.058	0.033	25.914	-0.004	-0.004	0.000	0.000	0.000
96	A	51	HOH	0	-0.032	-0.026	30.211	0.000	0.000	0.000	0.000	0.000
97	A	53	HOH	0	-0.031	-0.016	10.636	0.011	0.011	0.000	0.000	0.000
98	A	134	HOH	0	-0.043	-0.042	27.663	-0.003	-0.003	0.000	0.000	0.000
99	A	135	HOH	0	-0.005	-0.011	6.150	0.107	0.107	0.000	0.000	0.000
100	A	136	HOH	0	-0.063	-0.055	12.036	0.030	0.030	0.000	0.000	0.000
101	A	138	HOH	0	0.027	0.017	14.921	-0.001	-0.001	0.000	0.000	0.000
102	A	146	HOH	0	0.035	0.026	27.900	-0.001	-0.001	0.000	0.000	0.000
103	A	147	HOH	0	-0.033	-0.024	29.851	0.002	0.002	0.000	0.000	0.000
104	A	149	HOH	0	-0.038	-0.025	33.838	0.002	0.002	0.000	0.000	0.000
105	A	151	HOH	0	0.036	0.021	12.815	-0.003	-0.003	0.000	0.000	0.000
106	A	153	HOH	0	-0.050	-0.057	31.113	0.002	0.002	0.000	0.000	0.000
107	A	154	HOH	0	0.058	0.037	27.581	0.000	0.000	0.000	0.000	0.000
108	A	156	HOH	0	-0.035	-0.056	27.208	0.001	0.001	0.000	0.000	0.000
109	A	158	HOH	0	0.002	-0.001	30.317	0.002	0.002	0.000	0.000	0.000
110	A	162	HOH	0	0.013	0.018	29.116	0.002	0.002	0.000	0.000	0.000
111	A	163	HOH	0	-0.066	-0.068	20.860	-0.007	-0.007	0.000	0.000	0.000
112	A	165	HOH	0	0.013	0.005	31.263	-0.001	-0.001	0.000	0.000	0.000
113	A	167	HOH	0	-0.012	-0.022	7.990	-0.054	-0.054	0.000	0.000	0.000
114	A	169	HOH	0	-0.013	-0.012	29.765	-0.001	-0.001	0.000	0.000	0.000
115	A	170	HOH	0	0.001	0.007	12.794	0.016	0.016	0.000	0.000	0.000
116	A	171	HOH	0	0.019	0.010	27.791	0.000	0.000	0.000	0.000	0.000
117	A	173	HOH	0	0.021	0.012	21.211	0.007	0.007	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:65:ACE)