FMO DATABASE

FMODB ID: R8K38

Calculation Name: 2QW6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QW6

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptHSide
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	88
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-560715.283802
FMO2-HF: Nuclear repulsion	528205.121204
FMO2-HF: Total energy	-32510.162598
FMO2-MP2: Total energy	-32604.833315

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:241:TYR)

Summations of interaction energy for fragment #1(A:241:TYR)

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.
-19.309	-13.069	5.007	-3.968	-7.279	-0.009

Interaction energy analysis for fragmet #1(A:241:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.021

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	243	VAL	0	0.012	0.022	3.801	-0.715	2.510	0.012	-1.099	-2.139	0.008
4	A	244	ILE	0	0.031	0.020	5.029	-0.685	-0.555	-0.001	-0.008	-0.120	0.000
5	A	245	SER	0	-0.035	-0.044	4.111	-0.074	0.068	-0.001	-0.015	-0.127	0.000
6	A	246	ALA	0	-0.071	-0.023	2.750	-1.315	-0.310	0.771	-0.521	-1.254	0.004
7	A	247	PHE	0	0.020	0.018	4.663	-0.483	-0.356	-0.001	-0.015	-0.112	0.000
8	A	248	GLN	0	0.056	0.035	7.630	0.046	0.046	0.000	0.000	0.000	0.000
9	A	249	LYS	1	0.891	0.931	4.419	-2.872	-2.746	-0.001	-0.005	-0.119	0.000
10	A	250	SER	0	0.000	-0.009	6.818	-0.122	-0.122	0.000	0.000	0.000	0.000
11	A	251	ILE	0	0.028	0.013	9.058	0.110	0.110	0.000	0.000	0.000	0.000
12	A	252	ARG	1	0.732	0.838	11.553	-0.055	-0.055	0.000	0.000	0.000	0.000
13	A	253	GLY	0	-0.049	-0.013	11.693	0.060	0.060	0.000	0.000	0.000	0.000
14	A	254	SER	0	-0.026	-0.017	12.721	0.005	0.005	0.000	0.000	0.000	0.000
15	A	255	ASP	-1	-0.917	-0.952	10.536	-0.804	-0.804	0.000	0.000	0.000	0.000
16	A	256	VAL	0	0.060	0.004	11.583	-0.114	-0.114	0.000	0.000	0.000	0.000
17	A	257	ASP	-1	-0.895	-0.943	12.511	-0.418	-0.418	0.000	0.000	0.000	0.000
18	A	258	ALA	0	-0.034	-0.012	7.167	-0.077	-0.077	0.000	0.000	0.000	0.000
19	A	259	ALA	0	0.005	-0.012	7.908	-0.194	-0.194	0.000	0.000	0.000	0.000
20	A	260	LEU	0	0.015	-0.005	10.001	0.059	0.059	0.000	0.000	0.000	0.000
21	A	261	HIS	0	0.002	0.027	5.664	0.196	0.196	0.000	0.000	0.000	0.000
22	A	262	TYR	0	-0.001	-0.015	2.012	-10.790	-9.555	4.229	-2.250	-3.214	-0.021
23	A	263	LEU	0	0.003	0.021	7.567	0.187	0.187	0.000	0.000	0.000	0.000
24	A	264	ALA	0	-0.007	-0.001	11.209	0.066	0.066	0.000	0.000	0.000	0.000
25	A	265	ARG	1	0.931	0.958	3.967	-1.253	-1.003	-0.001	-0.055	-0.194	0.000
26	A	266	LEU	0	-0.048	-0.023	9.074	0.021	0.021	0.000	0.000	0.000	0.000
27	A	267	VAL	0	-0.017	-0.022	11.400	0.006	0.006	0.000	0.000	0.000	0.000
28	A	268	GLU	-1	-0.962	-0.971	12.114	-0.119	-0.119	0.000	0.000	0.000	0.000
29	A	269	ALA	0	-0.056	-0.029	11.549	0.004	0.004	0.000	0.000	0.000	0.000
30	A	270	GLY	0	-0.003	0.001	13.699	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	271	ASP	-1	-0.853	-0.897	13.633	-0.295	-0.295	0.000	0.000	0.000	0.000
32	A	272	LEU	0	0.020	-0.007	15.454	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	273	ALA	0	0.017	0.012	18.039	0.004	0.004	0.000	0.000	0.000	0.000
34	A	274	SER	0	-0.070	-0.070	13.330	0.016	0.016	0.000	0.000	0.000	0.000
35	A	275	ILE	0	0.031	0.022	13.052	0.006	0.006	0.000	0.000	0.000	0.000
36	A	276	CYS	0	0.010	0.014	14.876	0.005	0.005	0.000	0.000	0.000	0.000
37	A	277	ARG	1	0.948	0.966	16.473	0.174	0.174	0.000	0.000	0.000	0.000
38	A	278	ARG	1	0.885	0.937	10.665	0.145	0.145	0.000	0.000	0.000	0.000
39	A	279	LEU	0	0.042	0.025	14.877	0.020	0.020	0.000	0.000	0.000	0.000
40	A	280	MET	0	0.008	0.010	17.095	0.020	0.020	0.000	0.000	0.000	0.000
41	A	281	VAL	0	-0.059	-0.024	15.611	0.014	0.014	0.000	0.000	0.000	0.000
42	A	282	ILE	0	0.028	0.024	13.020	0.019	0.019	0.000	0.000	0.000	0.000
43	A	283	GLY	0	0.015	0.013	17.077	0.011	0.011	0.000	0.000	0.000	0.000
44	A	284	TYR	0	-0.047	-0.051	20.554	0.013	0.013	0.000	0.000	0.000	0.000
45	A	285	GLU	-1	-0.939	-0.948	16.265	0.097	0.097	0.000	0.000	0.000	0.000
46	A	286	ASP	-1	-0.801	-0.884	15.767	0.029	0.029	0.000	0.000	0.000	0.000
47	A	287	ILE	0	0.020	0.034	19.103	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	288	GLY	0	-0.038	-0.031	22.176	0.002	0.002	0.000	0.000	0.000	0.000
49	A	289	LEU	0	-0.069	-0.030	23.161	0.006	0.006	0.000	0.000	0.000	0.000
50	A	290	GLY	0	-0.006	-0.008	26.534	0.005	0.005	0.000	0.000	0.000	0.000
51	A	291	ASN	0	-0.017	-0.004	25.014	0.002	0.002	0.000	0.000	0.000	0.000
52	A	292	PRO	0	0.067	0.028	26.309	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	293	ALA	0	0.004	-0.003	28.546	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	294	ALA	0	0.031	0.014	23.893	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	295	ALA	0	0.019	0.012	23.865	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	296	ALA	0	-0.012	-0.007	24.948	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	297	ARG	1	0.850	0.899	25.108	0.089	0.089	0.000	0.000	0.000	0.000
58	A	298	THR	0	0.005	0.008	20.227	-0.013	-0.013	0.000	0.000	0.000	0.000
59	A	299	VAL	0	0.003	0.003	23.188	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	300	ASN	0	-0.046	-0.023	25.596	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	301	ALA	0	0.042	0.031	22.331	0.000	0.000	0.000	0.000	0.000	0.000
62	A	302	VAL	0	0.045	0.015	20.735	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	303	LEU	0	0.004	0.004	23.211	0.000	0.000	0.000	0.000	0.000	0.000
64	A	304	ALA	0	-0.037	-0.018	25.621	0.002	0.002	0.000	0.000	0.000	0.000
65	A	305	ALA	0	0.009	-0.005	21.431	0.001	0.001	0.000	0.000	0.000	0.000
66	A	306	GLU	-1	-0.961	-0.988	23.545	-0.123	-0.123	0.000	0.000	0.000	0.000
67	A	307	LYS	1	0.863	0.926	25.246	0.084	0.084	0.000	0.000	0.000	0.000
68	A	308	LEU	0	-0.053	-0.009	25.470	0.004	0.004	0.000	0.000	0.000	0.000
69	A	309	GLY	0	0.042	0.033	24.282	0.002	0.002	0.000	0.000	0.000	0.000
70	A	310	LEU	0	-0.017	0.004	18.149	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	311	PRO	0	0.033	-0.002	21.214	0.006	0.006	0.000	0.000	0.000	0.000
72	A	312	GLU	-1	-0.835	-0.930	21.421	-0.123	-0.123	0.000	0.000	0.000	0.000
73	A	313	ALA	0	0.017	0.013	21.162	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	314	ARG	1	0.877	0.924	17.970	0.135	0.135	0.000	0.000	0.000	0.000
75	A	315	ILE	0	-0.023	-0.005	19.112	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	316	PRO	0	-0.002	0.007	21.395	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	317	LEU	0	-0.007	-0.009	17.045	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	318	ALA	0	0.007	-0.008	16.662	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	319	ASP	-1	-0.907	-0.952	17.722	-0.158	-0.158	0.000	0.000	0.000	0.000
80	A	320	VAL	0	-0.003	-0.004	18.451	0.003	0.003	0.000	0.000	0.000	0.000
81	A	321	VAL	0	-0.013	-0.006	13.375	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	322	VAL	0	0.020	0.013	16.328	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	323	ASP	-1	-0.848	-0.897	18.113	-0.106	-0.106	0.000	0.000	0.000	0.000
84	A	324	LEU	0	-0.034	-0.031	17.265	0.014	0.014	0.000	0.000	0.000	0.000
85	A	325	CYS	0	-0.077	-0.026	14.561	-0.017	-0.017	0.000	0.000	0.000	0.000
86	A	326	LEU	0	0.002	0.001	16.905	0.018	0.018	0.000	0.000	0.000	0.000
87	A	327	SER	0	0.013	0.026	20.317	0.028	0.028	0.000	0.000	0.000	0.000
88	A	328	PRO	0	-0.067	-0.025	20.482	0.013	0.013	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:241:TYR)