FMO DATABASE

FMODB ID: 6NNRZ

Calculation Name: 4WFW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4WFW

Chain ID: A

ChEMBL ID:

UniProt ID: Q01563

Base Structure: X-ray

Registration Date: 2023-06-21

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

DOI:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-556821.409827
FMO2-HF: Nuclear repulsion	524370.86042
FMO2-HF: Total energy	-32450.549407
FMO2-MP2: Total energy	-32546.736813

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:115:LEU)

Summations of interaction energy for fragment #1(A:115:LEU)

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.
0.157	1.982	-0.01	-0.7	-1.115	0.001

Interaction energy analysis for fragmet #1(A:115:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.022 / q_NPA : -0.020

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	117	THR	0	-0.069	-0.045	3.882	1.107	2.501	-0.011	-0.642	-0.741	0.001
4	A	118	GLY	0	0.010	0.022	5.980	-0.346	-0.346	0.000	0.000	0.000	0.000
5	A	119	TRP	0	0.012	-0.012	9.374	-0.070	-0.070	0.000	0.000	0.000	0.000
6	A	120	GLN	0	0.004	-0.007	7.553	0.033	0.033	0.000	0.000	0.000	0.000
7	A	121	THR	0	0.003	0.000	11.731	0.045	0.045	0.000	0.000	0.000	0.000
8	A	122	ALA	0	0.011	0.014	14.457	-0.031	-0.031	0.000	0.000	0.000	0.000
9	A	123	LYS	1	0.874	0.928	16.227	0.133	0.133	0.000	0.000	0.000	0.000
10	A	124	PRO	0	0.010	-0.014	19.732	0.008	0.008	0.000	0.000	0.000	0.000
11	A	125	GLY	0	0.022	0.021	22.026	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	126	GLU	-1	-0.879	-0.936	16.972	-0.094	-0.094	0.000	0.000	0.000	0.000
13	A	127	LEU	0	0.024	0.026	13.939	0.007	0.007	0.000	0.000	0.000	0.000
14	A	128	PRO	0	-0.054	-0.022	10.615	-0.033	-0.033	0.000	0.000	0.000	0.000
15	A	129	TYR	0	-0.032	-0.043	4.579	-0.321	-0.094	-0.001	-0.018	-0.208	0.000
16	A	130	ILE	0	-0.044	-0.016	8.307	0.064	0.064	0.000	0.000	0.000	0.000
17	A	131	ALA	0	0.034	0.019	3.898	-0.230	-0.026	0.002	-0.040	-0.166	0.000
18	A	132	PHE	0	-0.034	-0.018	5.762	0.456	0.456	0.000	0.000	0.000	0.000
19	A	133	SER	0	-0.003	-0.008	5.805	-0.210	-0.210	0.000	0.000	0.000	0.000
20	A	134	ALA	0	-0.011	-0.013	7.594	-0.178	-0.178	0.000	0.000	0.000	0.000
21	A	135	HIS	0	0.019	0.016	11.404	0.009	0.009	0.000	0.000	0.000	0.000
22	A	136	VAL	0	-0.061	-0.022	14.938	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	137	TYR	0	-0.048	-0.032	18.402	-0.015	-0.015	0.000	0.000	0.000	0.000
24	A	138	THR	0	-0.008	-0.029	21.755	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	139	SER	0	0.015	0.012	25.281	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	140	ALA	0	0.002	-0.001	27.950	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	141	PRO	0	0.087	0.038	26.339	0.013	0.013	0.000	0.000	0.000	0.000
28	A	142	ASP	-1	-0.768	-0.867	24.813	0.150	0.150	0.000	0.000	0.000	0.000
29	A	143	LYS	1	0.727	0.843	23.541	-0.127	-0.127	0.000	0.000	0.000	0.000
30	A	144	ARG	1	0.771	0.905	21.441	-0.127	-0.127	0.000	0.000	0.000	0.000
31	A	145	SER	0	-0.059	-0.040	16.867	0.010	0.010	0.000	0.000	0.000	0.000
32	A	146	VAL	0	0.054	0.040	13.708	0.002	0.002	0.000	0.000	0.000	0.000
33	A	147	THR	0	-0.062	-0.035	8.872	-0.054	-0.054	0.000	0.000	0.000	0.000
34	A	148	LEU	0	0.019	0.014	9.201	0.094	0.094	0.000	0.000	0.000	0.000
35	A	149	ASN	0	0.002	-0.005	6.493	-0.049	-0.049	0.000	0.000	0.000	0.000
36	A	150	GLY	0	-0.005	-0.004	6.520	-0.170	-0.170	0.000	0.000	0.000	0.000
37	A	151	GLU	-1	-0.897	-0.898	6.985	0.080	0.080	0.000	0.000	0.000	0.000
38	A	152	ARG	1	0.886	0.937	10.833	-0.394	-0.394	0.000	0.000	0.000	0.000
39	A	153	TYR	0	0.002	-0.030	12.507	-0.062	-0.062	0.000	0.000	0.000	0.000
40	A	154	ARG	1	0.819	0.882	16.764	-0.210	-0.210	0.000	0.000	0.000	0.000
41	A	155	GLU	-1	-0.737	-0.854	20.286	0.148	0.148	0.000	0.000	0.000	0.000
42	A	156	GLY	0	-0.008	-0.005	22.724	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	157	ASP	-1	-0.846	-0.905	19.308	0.201	0.201	0.000	0.000	0.000	0.000
44	A	158	SER	0	-0.059	-0.050	20.284	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	159	PRO	0	-0.016	-0.003	14.836	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	160	TYR	0	0.005	0.007	15.654	-0.023	-0.023	0.000	0.000	0.000	0.000
47	A	161	GLN	0	-0.003	0.023	17.820	0.006	0.006	0.000	0.000	0.000	0.000
48	A	162	GLY	0	-0.005	-0.008	20.412	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	163	LEU	0	-0.044	-0.022	15.790	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	164	VAL	0	0.017	0.015	20.210	0.009	0.009	0.000	0.000	0.000	0.000
51	A	165	ILE	0	0.005	0.003	16.622	0.002	0.002	0.000	0.000	0.000	0.000
52	A	166	GLU	-1	-0.864	-0.903	20.615	0.088	0.088	0.000	0.000	0.000	0.000
53	A	167	GLN	0	-0.090	-0.076	22.638	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	168	ILE	0	-0.039	-0.007	18.504	0.009	0.009	0.000	0.000	0.000	0.000
55	A	169	GLU	-1	-0.724	-0.846	20.921	0.125	0.125	0.000	0.000	0.000	0.000
56	A	170	GLN	0	-0.072	-0.048	20.880	0.020	0.020	0.000	0.000	0.000	0.000
57	A	171	ASP	-1	-0.894	-0.948	19.830	0.152	0.152	0.000	0.000	0.000	0.000
58	A	172	MET	0	0.011	0.021	18.027	0.004	0.004	0.000	0.000	0.000	0.000
59	A	173	VAL	0	-0.065	-0.029	15.330	0.009	0.009	0.000	0.000	0.000	0.000
60	A	174	ILE	0	-0.024	-0.005	18.616	-0.017	-0.017	0.000	0.000	0.000	0.000
61	A	175	PHE	0	0.014	-0.018	14.750	0.014	0.014	0.000	0.000	0.000	0.000
62	A	176	SER	0	-0.026	-0.017	21.004	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	177	PHE	0	-0.009	-0.034	19.300	0.007	0.007	0.000	0.000	0.000	0.000
64	A	178	ASN	0	-0.078	-0.044	21.850	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	179	GLY	0	-0.009	0.005	25.058	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	180	GLU	-1	-0.896	-0.944	25.144	0.028	0.028	0.000	0.000	0.000	0.000
67	A	181	PRO	0	-0.022	-0.006	24.347	0.007	0.007	0.000	0.000	0.000	0.000
68	A	182	PHE	0	-0.013	-0.019	14.742	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	183	ILE	0	-0.012	-0.009	19.396	0.012	0.012	0.000	0.000	0.000	0.000
70	A	184	LEU	0	-0.032	0.008	12.547	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	185	ASP	-1	-0.814	-0.908	15.716	0.134	0.134	0.000	0.000	0.000	0.000
72	A	186	SER	0	-0.041	-0.051	14.322	0.045	0.045	0.000	0.000	0.000	0.000
73	A	187	LEU	0	-0.078	-0.031	10.191	-0.019	-0.019	0.000	0.000	0.000	0.000
74	A	188	GLN	0	-0.053	-0.014	9.866	-0.031	-0.031	0.000	0.000	0.000	0.000
75	A	189	ASP	-1	-0.757	-0.868	5.253	0.057	0.057	0.000	0.000	0.000	0.000
76	A	190	TRP	0	-0.006	0.007	8.960	-0.044	-0.044	0.000	0.000	0.000	0.000
77	A	191	PRO	0	-0.005	-0.008	8.607	-0.056	-0.056	0.000	0.000	0.000	0.000
78	A	192	GLY	0	-0.002	-0.004	9.678	-0.069	-0.069	0.000	0.000	0.000	0.000
79	A	193	GLY	0	-0.007	0.002	11.934	0.009	0.009	0.000	0.000	0.000	0.000
80	A	194	LYS	1	0.886	0.940	15.732	0.049	0.049	0.000	0.000	0.000	0.000
81	A	195	PRO	0	-0.009	0.004	17.208	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	196	GLY	0	0.017	0.008	19.286	0.003	0.003	0.000	0.000	0.000	0.000
83	A	197	ASP	-1	-1.005	-1.015	20.696	-0.045	-0.045	0.000	0.000	0.000	0.000
84	A	198	ASP	-1	-0.964	-0.963	18.501	-0.029	-0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:115:LEU)