FMO DATABASE

FMODB ID: Q1MQY

Calculation Name: 2O49-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2O49

Chain ID: A

ChEMBL ID:

UniProt ID: Q01826

Base Structure: X-ray

Registration Date: 2023-03-13

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	84
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-610374.398505
FMO2-HF: Nuclear repulsion	576081.132482
FMO2-HF: Total energy	-34293.266024
FMO2-MP2: Total energy	-34394.99296

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:370:GLU)

Summations of interaction energy for fragment #1(A:370:GLU)

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.
-143.266	-150.104	32.613	-14.526	-11.248	0.163

Interaction energy analysis for fragmet #1(A:370:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.817 / q_NPA : -0.887

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	372	SER	0	0.019	0.016	3.873	-2.871	-1.367	-0.017	-0.731	-0.756	0.001
4	A	373	SER	0	0.026	-0.013	6.256	1.139	1.139	0.000	0.000	0.000	0.000
5	A	374	GLU	-1	-0.873	-0.912	8.902	17.943	17.943	0.000	0.000	0.000	0.000
6	A	375	ILE	0	-0.039	-0.005	8.817	-1.251	-1.251	0.000	0.000	0.000	0.000
7	A	376	TYR	0	0.003	-0.029	10.904	-0.588	-0.588	0.000	0.000	0.000	0.000
8	A	377	GLN	0	-0.017	-0.016	14.252	-0.952	-0.952	0.000	0.000	0.000	0.000
9	A	378	TRP	0	0.006	-0.017	8.821	0.439	0.439	0.000	0.000	0.000	0.000
10	A	379	VAL	0	0.006	0.004	13.012	-0.654	-0.654	0.000	0.000	0.000	0.000
11	A	380	ARG	1	0.770	0.862	15.689	-16.447	-16.447	0.000	0.000	0.000	0.000
12	A	381	ASP	-1	-0.851	-0.920	18.613	13.521	13.521	0.000	0.000	0.000	0.000
13	A	382	GLU	-1	-0.715	-0.768	16.752	15.333	15.333	0.000	0.000	0.000	0.000
14	A	383	LEU	0	-0.065	-0.045	18.971	-0.620	-0.620	0.000	0.000	0.000	0.000
15	A	384	LYS	1	0.929	0.966	21.146	-12.442	-12.442	0.000	0.000	0.000	0.000
16	A	385	ARG	1	0.655	0.784	19.875	-14.617	-14.617	0.000	0.000	0.000	0.000
17	A	386	ALA	0	0.033	0.023	22.441	-0.457	-0.457	0.000	0.000	0.000	0.000
18	A	387	GLY	0	0.005	0.018	24.190	-0.389	-0.389	0.000	0.000	0.000	0.000
19	A	388	ILE	0	-0.048	-0.005	20.495	-0.424	-0.424	0.000	0.000	0.000	0.000
20	A	389	SER	0	0.022	0.007	24.119	0.292	0.292	0.000	0.000	0.000	0.000
21	A	390	GLN	0	0.075	0.016	21.353	0.077	0.077	0.000	0.000	0.000	0.000
22	A	391	ALA	0	-0.016	-0.011	21.022	0.680	0.680	0.000	0.000	0.000	0.000
23	A	392	VAL	0	0.043	0.038	21.734	0.517	0.517	0.000	0.000	0.000	0.000
24	A	393	PHE	0	0.078	0.029	13.967	0.612	0.612	0.000	0.000	0.000	0.000
25	A	394	ALA	0	-0.006	-0.012	17.121	1.075	1.075	0.000	0.000	0.000	0.000
26	A	395	ARG	1	0.873	0.953	17.047	-14.160	-14.160	0.000	0.000	0.000	0.000
27	A	396	VAL	0	0.002	-0.011	17.675	0.641	0.641	0.000	0.000	0.000	0.000
28	A	397	ALA	0	0.008	0.022	13.582	0.868	0.868	0.000	0.000	0.000	0.000
29	A	398	PHE	0	-0.014	-0.030	11.817	2.038	2.038	0.000	0.000	0.000	0.000
30	A	399	ASN	0	-0.003	0.024	13.135	-0.624	-0.624	0.000	0.000	0.000	0.000
31	A	400	ARG	1	0.820	0.914	12.203	-23.438	-23.438	0.000	0.000	0.000	0.000
32	A	401	THR	0	0.011	-0.005	17.916	-0.587	-0.587	0.000	0.000	0.000	0.000
33	A	402	GLN	0	0.049	-0.002	20.348	0.480	0.480	0.000	0.000	0.000	0.000
34	A	403	GLY	0	0.039	0.030	22.083	0.257	0.257	0.000	0.000	0.000	0.000
35	A	404	LEU	0	0.005	0.005	16.279	0.096	0.096	0.000	0.000	0.000	0.000
36	A	405	LEU	0	0.030	0.021	16.149	0.627	0.627	0.000	0.000	0.000	0.000
37	A	406	SER	0	0.004	0.001	18.581	0.050	0.050	0.000	0.000	0.000	0.000
38	A	407	GLU	-1	-0.816	-0.888	19.825	14.241	14.241	0.000	0.000	0.000	0.000
39	A	408	ILE	0	-0.038	-0.013	13.898	0.172	0.172	0.000	0.000	0.000	0.000
40	A	409	LEU	0	0.011	-0.002	16.415	0.133	0.133	0.000	0.000	0.000	0.000
41	A	410	ARG	1	0.812	0.901	18.254	-14.177	-14.177	0.000	0.000	0.000	0.000
42	A	411	LYS	1	0.837	0.918	17.019	-16.929	-16.929	0.000	0.000	0.000	0.000
43	A	412	GLU	-1	-0.813	-0.895	14.886	16.457	16.457	0.000	0.000	0.000	0.000
44	A	413	GLU	-1	-0.884	-0.945	12.879	22.091	22.091	0.000	0.000	0.000	0.000
45	A	414	ASP	-1	-0.726	-0.833	9.697	27.324	27.324	0.000	0.000	0.000	0.000
46	A	415	PRO	0	0.016	-0.007	5.954	0.572	0.572	0.000	0.000	0.000	0.000
47	A	416	LYS	1	0.784	0.867	6.002	-25.759	-25.759	0.000	0.000	0.000	0.000
48	A	417	THR	0	-0.053	-0.028	8.559	-1.291	-1.291	0.000	0.000	0.000	0.000
49	A	418	ALA	0	-0.042	0.009	8.499	-1.038	-1.038	0.000	0.000	0.000	0.000
50	A	419	SER	0	0.054	0.033	9.637	2.257	2.257	0.000	0.000	0.000	0.000
51	A	420	GLN	0	0.078	0.016	7.272	6.625	6.625	0.000	0.000	0.000	0.000
52	A	421	SER	0	-0.047	-0.016	9.050	2.215	2.215	0.000	0.000	0.000	0.000
53	A	422	LEU	0	-0.009	0.004	10.314	0.556	0.556	0.000	0.000	0.000	0.000
54	A	423	LEU	0	0.061	0.026	4.574	1.259	1.339	-0.001	-0.005	-0.073	0.000
55	A	424	VAL	0	-0.023	-0.012	6.200	5.252	5.252	0.000	0.000	0.000	0.000
56	A	425	ASN	0	0.008	0.002	7.462	-0.676	-0.676	0.000	0.000	0.000	0.000
57	A	426	LEU	0	0.024	0.007	7.236	-1.122	-1.122	0.000	0.000	0.000	0.000
58	A	427	ARG	1	0.827	0.890	1.683	-138.585	-147.342	32.634	-13.670	-10.208	0.162
59	A	428	ALA	0	-0.043	0.004	5.392	-2.829	-2.760	-0.001	0.000	-0.067	0.000
60	A	429	MET	0	0.015	0.007	8.487	-2.682	-2.682	0.000	0.000	0.000	0.000
61	A	430	GLN	0	0.022	0.014	4.127	-3.982	-3.788	-0.001	-0.120	-0.073	0.000
62	A	431	ASN	0	-0.019	-0.027	5.062	-4.924	-4.852	-0.001	0.000	-0.071	0.000
63	A	432	PHE	0	0.011	0.009	8.595	-2.300	-2.300	0.000	0.000	0.000	0.000
64	A	433	LEU	0	-0.006	-0.023	11.074	-1.696	-1.696	0.000	0.000	0.000	0.000
65	A	434	GLN	0	-0.043	-0.019	7.149	0.506	0.506	0.000	0.000	0.000	0.000
66	A	435	LEU	0	-0.023	0.015	11.912	-1.043	-1.043	0.000	0.000	0.000	0.000
67	A	436	PRO	0	0.027	0.001	15.017	-0.530	-0.530	0.000	0.000	0.000	0.000
68	A	437	GLU	-1	-0.783	-0.880	18.483	14.083	14.083	0.000	0.000	0.000	0.000
69	A	438	ALA	0	0.018	-0.002	20.499	-0.025	-0.025	0.000	0.000	0.000	0.000
70	A	439	GLU	-1	-0.853	-0.888	19.072	13.605	13.605	0.000	0.000	0.000	0.000
71	A	440	ARG	1	0.769	0.860	15.511	-16.689	-16.689	0.000	0.000	0.000	0.000
72	A	441	ASP	-1	-0.745	-0.857	19.406	13.002	13.002	0.000	0.000	0.000	0.000
73	A	442	ARG	1	0.831	0.898	23.026	-13.199	-13.199	0.000	0.000	0.000	0.000
74	A	443	ILE	0	0.021	0.011	18.630	-0.243	-0.243	0.000	0.000	0.000	0.000
75	A	444	TYR	0	-0.060	-0.082	17.915	0.157	0.157	0.000	0.000	0.000	0.000
76	A	445	GLN	0	-0.007	-0.005	23.163	-0.598	-0.598	0.000	0.000	0.000	0.000
77	A	446	ASP	-1	-0.821	-0.908	25.219	11.741	11.741	0.000	0.000	0.000	0.000
78	A	447	GLU	-1	-0.916	-0.952	22.547	13.197	13.197	0.000	0.000	0.000	0.000
79	A	448	ARG	1	0.822	0.892	25.333	-11.354	-11.354	0.000	0.000	0.000	0.000
80	A	449	GLU	-1	-0.928	-0.962	28.027	9.459	9.459	0.000	0.000	0.000	0.000
81	A	450	ARG	1	0.782	0.875	23.491	-12.928	-12.928	0.000	0.000	0.000	0.000
82	A	451	SER	0	-0.055	-0.039	26.786	-0.097	-0.097	0.000	0.000	0.000	0.000
83	A	452	LEU	0	-0.046	0.005	28.795	-0.133	-0.133	0.000	0.000	0.000	0.000
84	A	453	ARG	1	0.932	0.977	31.940	-9.505	-9.505	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:370:GLU)