FMO DATABASE

FMODB ID: 3N5YL

Calculation Name: 2O49-A-Xray311

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: 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:

Apendix: None

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-613720.90617
FMO2-HF: Nuclear repulsion	579257.429853
FMO2-HF: Total energy	-34463.476318
FMO2-MP2: Total energy	-34565.801543

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:369:ACE )

Summations of interaction energy for fragment #1(A:369: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.
1.77	3.003	-0.003	-0.575	-0.654	-0.001

Interaction energy analysis for fragmet #1(A:369:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / 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	371	VAL	0	-0.017	0.004	3.833	0.736	1.801	-0.003	-0.557	-0.505	-0.001
4	A	372	SER	0	0.014	0.012	4.977	0.604	0.708	0.000	-0.005	-0.100	0.000
5	A	373	SER	0	-0.019	-0.031	6.952	0.106	0.106	0.000	0.000	0.000	0.000
6	A	374	GLU	-1	-0.929	-0.956	8.580	0.061	0.061	0.000	0.000	0.000	0.000
7	A	375	ILE	0	-0.011	0.009	10.258	-0.042	-0.042	0.000	0.000	0.000	0.000
8	A	376	TYR	0	-0.013	-0.052	12.012	-0.059	-0.059	0.000	0.000	0.000	0.000
9	A	377	GLN	0	-0.029	-0.013	14.750	0.001	0.001	0.000	0.000	0.000	0.000
10	A	378	TRP	0	0.054	0.016	10.542	-0.037	-0.037	0.000	0.000	0.000	0.000
11	A	379	VAL	0	-0.010	-0.003	15.560	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	380	ARG	1	0.886	0.939	17.960	-0.050	-0.050	0.000	0.000	0.000	0.000
13	A	381	ASP	-1	-0.853	-0.920	19.701	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	382	GLU	-1	-0.700	-0.785	19.936	-0.091	-0.091	0.000	0.000	0.000	0.000
15	A	383	LEU	0	-0.060	-0.049	21.770	0.002	0.002	0.000	0.000	0.000	0.000
16	A	384	LYS	1	0.950	0.979	24.082	0.001	0.001	0.000	0.000	0.000	0.000
17	A	385	ARG	1	0.712	0.833	23.509	0.071	0.071	0.000	0.000	0.000	0.000
18	A	386	ALA	0	-0.001	-0.003	25.607	0.001	0.001	0.000	0.000	0.000	0.000
19	A	387	GLY	0	0.002	0.022	27.346	0.002	0.002	0.000	0.000	0.000	0.000
20	A	388	ILE	0	-0.083	-0.031	24.332	0.001	0.001	0.000	0.000	0.000	0.000
21	A	389	SER	0	0.018	0.006	27.416	0.003	0.003	0.000	0.000	0.000	0.000
22	A	390	GLN	0	0.095	0.017	24.169	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	391	ALA	0	-0.011	-0.007	24.479	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	392	VAL	0	0.043	0.036	26.125	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	393	PHE	0	0.068	0.024	17.902	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	394	ALA	0	0.001	-0.013	21.057	-0.013	-0.013	0.000	0.000	0.000	0.000
27	A	395	ARG	1	0.870	0.960	21.668	0.058	0.058	0.000	0.000	0.000	0.000
28	A	396	VAL	0	0.010	-0.014	22.729	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	397	ALA	0	-0.009	0.028	18.306	-0.016	-0.016	0.000	0.000	0.000	0.000
30	A	398	PHE	0	-0.009	-0.025	16.623	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	399	ASN	0	0.013	0.023	18.522	0.015	0.015	0.000	0.000	0.000	0.000
32	A	400	ARG	1	0.845	0.933	17.688	0.112	0.112	0.000	0.000	0.000	0.000
33	A	401	THR	0	0.021	-0.005	22.303	0.002	0.002	0.000	0.000	0.000	0.000
34	A	402	GLN	0	0.050	0.002	23.625	0.000	0.000	0.000	0.000	0.000	0.000
35	A	403	GLY	0	0.033	0.023	24.411	0.004	0.004	0.000	0.000	0.000	0.000
36	A	404	LEU	0	0.009	0.008	19.311	0.008	0.008	0.000	0.000	0.000	0.000
37	A	405	LEU	0	0.037	0.022	18.863	0.007	0.007	0.000	0.000	0.000	0.000
38	A	406	SER	0	-0.012	0.001	20.506	0.009	0.009	0.000	0.000	0.000	0.000
39	A	407	GLU	-1	-0.821	-0.901	21.267	0.056	0.056	0.000	0.000	0.000	0.000
40	A	408	ILE	0	-0.065	-0.025	15.397	0.014	0.014	0.000	0.000	0.000	0.000
41	A	409	LEU	0	-0.014	-0.018	17.176	0.019	0.019	0.000	0.000	0.000	0.000
42	A	410	ARG	1	0.784	0.882	19.102	-0.053	-0.053	0.000	0.000	0.000	0.000
43	A	411	LYS	1	0.895	0.938	17.655	-0.069	-0.069	0.000	0.000	0.000	0.000
44	A	412	GLU	-1	-0.908	-0.931	15.449	0.139	0.139	0.000	0.000	0.000	0.000
45	A	413	GLU	-1	-0.930	-0.961	12.831	0.235	0.235	0.000	0.000	0.000	0.000
46	A	414	ASP	-1	-0.761	-0.875	8.910	0.868	0.868	0.000	0.000	0.000	0.000
47	A	415	PRO	0	0.002	-0.012	6.285	0.045	0.045	0.000	0.000	0.000	0.000
48	A	416	LYS	1	0.855	0.932	4.523	-1.467	-1.403	0.000	-0.013	-0.049	0.000
49	A	417	THR	0	-0.050	-0.018	6.407	-0.062	-0.062	0.000	0.000	0.000	0.000
50	A	418	ALA	0	0.003	0.022	8.289	-0.145	-0.145	0.000	0.000	0.000	0.000
51	A	419	SER	0	0.040	0.015	9.216	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	420	GLN	0	0.074	0.014	10.444	-0.069	-0.069	0.000	0.000	0.000	0.000
53	A	421	SER	0	-0.027	-0.015	11.498	-0.055	-0.055	0.000	0.000	0.000	0.000
54	A	422	LEU	0	0.014	0.017	11.244	-0.043	-0.043	0.000	0.000	0.000	0.000
55	A	423	LEU	0	0.058	0.027	5.862	-0.089	-0.089	0.000	0.000	0.000	0.000
56	A	424	VAL	0	-0.024	0.002	9.311	-0.116	-0.116	0.000	0.000	0.000	0.000
57	A	425	ASN	0	-0.007	-0.012	11.862	-0.045	-0.045	0.000	0.000	0.000	0.000
58	A	426	LEU	0	0.018	0.004	9.391	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	427	ARG	1	0.967	0.981	5.637	1.040	1.040	0.000	0.000	0.000	0.000
60	A	428	ALA	0	-0.037	0.003	10.351	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	429	MET	0	-0.012	-0.006	13.803	0.023	0.023	0.000	0.000	0.000	0.000
62	A	430	GLN	0	0.041	0.011	7.365	0.199	0.199	0.000	0.000	0.000	0.000
63	A	431	ASN	0	-0.003	-0.011	12.288	-0.045	-0.045	0.000	0.000	0.000	0.000
64	A	432	PHE	0	0.006	0.003	14.287	0.031	0.031	0.000	0.000	0.000	0.000
65	A	433	LEU	0	0.002	-0.017	14.734	0.024	0.024	0.000	0.000	0.000	0.000
66	A	434	GLN	0	-0.061	-0.017	12.196	-0.050	-0.050	0.000	0.000	0.000	0.000
67	A	435	LEU	0	-0.026	0.010	16.796	0.010	0.010	0.000	0.000	0.000	0.000
68	A	436	PRO	0	0.034	0.009	20.328	0.013	0.013	0.000	0.000	0.000	0.000
69	A	437	GLU	-1	-0.893	-0.949	23.288	-0.070	-0.070	0.000	0.000	0.000	0.000
70	A	438	ALA	0	0.022	0.008	24.626	0.005	0.005	0.000	0.000	0.000	0.000
71	A	439	GLU	-1	-0.967	-0.988	24.752	-0.130	-0.130	0.000	0.000	0.000	0.000
72	A	440	ARG	1	0.829	0.908	20.277	0.126	0.126	0.000	0.000	0.000	0.000
73	A	441	ASP	-1	-0.758	-0.869	24.593	-0.063	-0.063	0.000	0.000	0.000	0.000
74	A	442	ARG	1	0.917	0.964	27.858	0.097	0.097	0.000	0.000	0.000	0.000
75	A	443	ILE	0	0.002	0.001	24.379	0.004	0.004	0.000	0.000	0.000	0.000
76	A	444	TYR	0	-0.074	-0.085	22.508	0.002	0.002	0.000	0.000	0.000	0.000
77	A	445	GLN	0	-0.017	-0.009	28.314	0.009	0.009	0.000	0.000	0.000	0.000
78	A	446	ASP	-1	-0.838	-0.910	31.317	-0.063	-0.063	0.000	0.000	0.000	0.000
79	A	447	GLU	-1	-0.961	-0.993	27.748	-0.061	-0.061	0.000	0.000	0.000	0.000
80	A	448	ARG	1	0.913	0.955	30.761	0.044	0.044	0.000	0.000	0.000	0.000
81	A	449	GLU	-1	-0.927	-0.961	32.657	-0.041	-0.041	0.000	0.000	0.000	0.000
82	A	450	ARG	1	0.880	0.933	30.601	0.070	0.070	0.000	0.000	0.000	0.000
83	A	451	SER	0	-0.057	-0.031	31.825	0.003	0.003	0.000	0.000	0.000	0.000
84	A	452	LEU	0	-0.053	0.000	33.816	0.004	0.004	0.000	0.000	0.000	0.000
85	A	453	ARG	1	0.900	0.961	37.141	0.039	0.039	0.000	0.000	0.000	0.000
86	A	454	NME	0	0.009	0.009	37.571	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:369:ACE )