FMO DATABASE

FMODB ID: R1318

Calculation Name: 3FB9-A-Xray312

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3FB9

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-628770.999273
FMO2-HF: Nuclear repulsion	592586.411144
FMO2-HF: Total energy	-36184.588129
FMO2-MP2: Total energy	-36289.994661

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:-1:ACE )

Summations of interaction energy for fragment #1(A:-1: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.
0.446	1.403	-0.004	-0.48	-0.473	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.002 / q_NPA : -0.012

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	1	MET	0	-0.033	0.008	3.876	0.882	1.839	-0.004	-0.480	-0.473	-0.001
4	A	2	SER	0	0.046	0.013	7.089	-0.014	-0.014	0.000	0.000	0.000	0.000
5	A	3	ASP	-1	-0.880	-0.964	9.261	-0.294	-0.294	0.000	0.000	0.000	0.000
6	A	4	ALA	0	0.004	0.010	12.485	0.032	0.032	0.000	0.000	0.000	0.000
7	A	5	PHE	0	-0.037	-0.031	10.888	0.037	0.037	0.000	0.000	0.000	0.000
8	A	6	THR	0	-0.031	-0.001	12.666	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	7	ASP	-1	-0.832	-0.923	14.353	-0.287	-0.287	0.000	0.000	0.000	0.000
10	A	8	VAL	0	-0.047	-0.026	17.625	0.037	0.037	0.000	0.000	0.000	0.000
11	A	9	ALA	0	0.000	0.014	16.575	0.034	0.034	0.000	0.000	0.000	0.000
12	A	10	LYS	1	0.972	0.988	15.514	0.309	0.309	0.000	0.000	0.000	0.000
13	A	11	MET	0	0.000	0.008	19.101	0.032	0.032	0.000	0.000	0.000	0.000
14	A	12	LYS	1	0.874	0.950	22.122	0.131	0.131	0.000	0.000	0.000	0.000
15	A	13	LYS	1	0.911	0.966	21.078	0.110	0.110	0.000	0.000	0.000	0.000
16	A	14	ILE	0	0.050	0.037	21.567	0.013	0.013	0.000	0.000	0.000	0.000
17	A	15	LYS	1	0.845	0.920	24.603	0.124	0.124	0.000	0.000	0.000	0.000
18	A	16	GLU	-1	-0.945	-0.978	25.604	-0.088	-0.088	0.000	0.000	0.000	0.000
19	A	17	GLU	-1	-0.900	-0.961	23.472	-0.099	-0.099	0.000	0.000	0.000	0.000
20	A	18	ILE	0	0.019	0.007	27.804	0.007	0.007	0.000	0.000	0.000	0.000
21	A	19	LYS	1	0.930	0.968	30.327	0.066	0.066	0.000	0.000	0.000	0.000
22	A	20	ALA	0	-0.075	-0.043	30.673	0.005	0.005	0.000	0.000	0.000	0.000
23	A	21	HIS	0	0.036	0.027	31.301	0.002	0.002	0.000	0.000	0.000	0.000
24	A	22	GLU	-1	-0.927	-0.959	33.380	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	23	GLY	0	-0.056	-0.034	36.353	0.003	0.003	0.000	0.000	0.000	0.000
26	A	24	GLN	0	-0.023	-0.012	35.117	0.002	0.002	0.000	0.000	0.000	0.000
27	A	25	VAL	0	0.023	0.007	34.848	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	26	VAL	0	-0.005	0.009	31.088	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	27	GLU	-1	-0.833	-0.901	29.875	-0.040	-0.040	0.000	0.000	0.000	0.000
30	A	28	MET	0	-0.046	-0.029	28.979	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	29	THR	0	-0.029	-0.018	26.749	0.006	0.006	0.000	0.000	0.000	0.000
32	A	30	LEU	0	-0.042	-0.023	27.379	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	31	GLU	-1	-0.927	-0.933	20.202	-0.155	-0.155	0.000	0.000	0.000	0.000
34	A	32	ASN	0	0.023	-0.011	24.402	0.002	0.002	0.000	0.000	0.000	0.000
35	A	33	GLY	0	-0.006	0.013	23.383	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	34	ARG	1	0.940	0.954	20.790	0.015	0.015	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.852	0.938	23.270	0.034	0.034	0.000	0.000	0.000	0.000
38	A	36	ARG	1	1.015	1.015	20.514	0.082	0.082	0.000	0.000	0.000	0.000
39	A	37	GLN	0	0.025	-0.007	27.557	0.009	0.009	0.000	0.000	0.000	0.000
40	A	38	LYS	1	0.919	0.952	31.015	0.033	0.033	0.000	0.000	0.000	0.000
41	A	39	ASN	0	-0.001	-0.010	28.763	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	40	ARG	1	0.810	0.925	32.237	0.062	0.062	0.000	0.000	0.000	0.000
43	A	41	LEU	0	0.024	0.008	33.441	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	42	GLY	0	0.013	-0.005	35.351	0.001	0.001	0.000	0.000	0.000	0.000
45	A	43	LYS	1	0.936	0.986	36.242	0.037	0.037	0.000	0.000	0.000	0.000
46	A	44	LEU	0	-0.012	-0.002	32.624	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	45	ILE	0	-0.067	-0.040	36.455	0.002	0.002	0.000	0.000	0.000	0.000
48	A	46	GLU	-1	-0.874	-0.929	38.217	-0.043	-0.043	0.000	0.000	0.000	0.000
49	A	47	VAL	0	0.013	0.007	33.617	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	48	TYR	0	0.013	0.011	35.471	0.003	0.003	0.000	0.000	0.000	0.000
51	A	49	PRO	0	-0.020	-0.014	34.074	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	50	SER	0	-0.066	-0.039	32.435	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	51	LEU	0	-0.020	-0.012	32.304	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	52	PHE	0	0.020	0.023	29.241	0.003	0.003	0.000	0.000	0.000	0.000
55	A	53	ILE	0	0.022	0.006	34.502	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	54	VAL	0	0.010	0.010	33.590	0.001	0.001	0.000	0.000	0.000	0.000
57	A	55	GLU	-1	-0.964	-0.976	36.999	-0.035	-0.035	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.021	-0.013	33.995	0.000	0.000	0.000	0.000	0.000	0.000
59	A	57	GLY	0	0.052	0.015	39.702	0.001	0.001	0.000	0.000	0.000	0.000
60	A	58	ASP	-1	-0.820	-0.919	42.196	-0.024	-0.024	0.000	0.000	0.000	0.000
61	A	59	VAL	0	-0.004	0.024	38.090	0.001	0.001	0.000	0.000	0.000	0.000
62	A	60	GLU	-1	-0.944	-0.981	41.378	-0.019	-0.019	0.000	0.000	0.000	0.000
63	A	61	GLY	0	-0.017	-0.012	40.469	0.000	0.000	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-0.866	-0.943	37.843	-0.035	-0.035	0.000	0.000	0.000	0.000
65	A	63	LYS	1	0.816	0.931	40.362	0.023	0.023	0.000	0.000	0.000	0.000
66	A	64	GLN	0	-0.082	-0.047	40.536	0.001	0.001	0.000	0.000	0.000	0.000
67	A	65	VAL	0	-0.041	-0.019	44.523	0.000	0.000	0.000	0.000	0.000	0.000
68	A	66	ASN	0	-0.047	-0.021	44.201	0.001	0.001	0.000	0.000	0.000	0.000
69	A	67	VAL	0	0.060	0.039	44.050	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	68	TYR	0	-0.075	-0.021	38.348	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	69	VAL	0	0.047	0.024	40.425	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	70	GLU	-1	-0.883	-0.944	34.761	-0.062	-0.062	0.000	0.000	0.000	0.000
73	A	71	SER	0	-0.055	-0.023	36.010	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	72	PHE	0	0.058	0.031	30.476	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	73	THR	0	-0.004	-0.003	29.406	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	74	TYR	0	0.052	-0.016	26.763	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	75	SER	0	0.000	-0.004	24.987	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	76	ASP	-1	-0.843	-0.905	24.567	-0.118	-0.118	0.000	0.000	0.000	0.000
79	A	77	ILE	0	0.002	0.006	23.349	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	78	LEU	0	-0.018	-0.025	19.261	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	79	THR	0	-0.115	-0.076	19.863	-0.022	-0.022	0.000	0.000	0.000	0.000
82	A	80	GLU	-1	-0.953	-0.973	17.479	-0.249	-0.249	0.000	0.000	0.000	0.000
83	A	81	LYS	1	1.001	1.025	21.765	0.111	0.111	0.000	0.000	0.000	0.000
84	A	82	ASN	0	-0.053	-0.049	25.089	0.009	0.009	0.000	0.000	0.000	0.000
85	A	83	LEU	0	-0.015	-0.006	21.772	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	84	ILE	0	-0.004	-0.014	24.708	0.009	0.009	0.000	0.000	0.000	0.000
87	A	85	HIS	0	-0.008	0.002	25.075	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	86	TYR	0	0.018	-0.004	25.426	0.003	0.003	0.000	0.000	0.000	0.000
89	A	87	LEU	0	-0.084	-0.029	29.468	0.002	0.002	0.000	0.000	0.000	0.000
90	A	88	ASP	-2	-1.855	-1.926	31.546	-0.063	-0.063	0.000	0.000	0.000	0.000

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