FMO DATABASE

FMODB ID: P4N1N

Calculation Name: 2QSB-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QSB

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HKJ8

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	87
LigandResidueName
LigandFragmentNumber	0
LigandCharge	SO4=-2
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-590647.918864
FMO2-HF: Nuclear repulsion	555713.032951
FMO2-HF: Total energy	-34934.885913
FMO2-MP2: Total energy	-35033.934579

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.
-0.163	1.048	0.006	-0.435	-0.782	-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 : 0.021 / q_NPA : 0.001

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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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	3	ARG	1	0.949	0.974	3.849	0.934	1.759	-0.011	-0.359	-0.455	-0.001
4	A	4	VAL	0	-0.015	-0.012	3.401	-0.146	0.069	0.018	-0.062	-0.171	0.000
5	A	5	ASP	-1	-0.755	-0.868	4.629	-1.074	-0.903	-0.001	-0.014	-0.156	0.000
6	A	6	GLN	0	-0.033	-0.032	6.304	0.239	0.239	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.049	-0.031	8.671	0.100	0.100	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.043	0.038	8.328	0.069	0.069	0.000	0.000	0.000	0.000
9	A	9	PHE	0	0.019	0.011	10.435	0.048	0.048	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.015	-0.020	12.313	0.038	0.038	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.886	-0.930	13.996	-0.070	-0.070	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.014	0.010	14.621	0.031	0.031	0.000	0.000	0.000	0.000
13	A	13	MET	0	-0.022	-0.005	16.401	0.029	0.029	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.021	0.000	18.437	0.020	0.020	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.012	-0.005	18.635	0.017	0.017	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.004	-0.001	19.541	0.013	0.013	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.912	-0.960	22.479	-0.100	-0.100	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.891	-0.940	24.276	-0.066	-0.066	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.012	0.013	25.309	0.008	0.008	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.112	-0.078	26.683	0.006	0.006	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.064	-0.034	28.543	0.009	0.009	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.775	-0.844	29.975	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.064	-0.057	31.868	0.002	0.002	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.102	-0.062	33.493	0.004	0.004	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.011	0.024	30.702	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.009	-0.010	33.640	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.963	0.968	33.830	0.041	0.041	0.000	0.000	0.000	0.000
28	A	28	ASN	0	0.007	-0.005	33.772	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.128	0.051	28.853	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.839	0.948	29.150	0.042	0.042	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.783	0.874	29.375	0.064	0.064	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.099	0.055	26.283	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.006	0.015	25.039	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	34	GLN	0	-0.058	-0.042	24.739	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.809	-0.887	25.792	-0.089	-0.089	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.023	-0.021	21.702	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.934	0.969	20.833	0.100	0.100	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.016	0.000	21.284	-0.018	-0.018	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.876	0.940	20.483	0.117	0.117	0.000	0.000	0.000	0.000
40	A	40	LEU	0	0.032	-0.006	15.780	-0.015	-0.015	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.027	-0.011	17.227	-0.046	-0.046	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.030	0.009	19.653	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.977	-0.994	17.250	-0.308	-0.308	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.057	-0.022	18.166	-0.024	-0.024	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.867	-0.935	19.178	-0.134	-0.134	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.002	-0.005	15.085	-0.035	-0.035	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.056	0.006	9.603	0.022	0.022	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.796	-0.887	11.594	-0.168	-0.168	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.083	-0.045	13.917	0.032	0.032	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.818	0.903	14.266	0.341	0.341	0.000	0.000	0.000	0.000
51	A	51	CYS	0	0.040	0.020	12.662	0.009	0.009	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.038	0.038	16.353	0.023	0.023	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.068	-0.037	18.790	0.015	0.015	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.019	-0.005	18.963	0.010	0.010	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.006	0.006	16.383	0.009	0.009	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.002	0.005	20.567	0.012	0.012	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.032	-0.009	23.928	0.002	0.002	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.028	-0.021	20.655	0.004	0.004	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.907	-0.945	24.021	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.939	-0.979	25.548	-0.036	-0.036	0.000	0.000	0.000	0.000
61	A	61	MET	0	-0.086	-0.026	27.726	0.002	0.002	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.012	-0.011	26.388	0.003	0.003	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.077	-0.033	28.506	0.008	0.008	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.838	-0.898	31.331	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	65	PRO	0	-0.029	-0.032	33.856	0.001	0.001	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.079	-0.048	36.564	0.003	0.003	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.008	0.016	30.749	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	68	PRO	0	-0.010	0.017	33.453	0.004	0.004	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.030	-0.004	32.574	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	70	HIS	0	0.009	-0.015	30.706	0.004	0.004	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.092	0.052	29.050	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.878	0.928	27.984	0.009	0.009	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.014	-0.001	25.804	0.002	0.002	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.894	-0.935	24.568	-0.038	-0.038	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.022	-0.017	23.242	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	76	TYR	0	0.031	0.005	22.336	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	77	THR	0	-0.057	-0.012	19.730	0.007	0.007	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.018	-0.019	18.476	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.024	0.009	17.458	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.004	-0.020	17.166	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.781	0.889	13.830	0.082	0.082	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.008	-0.005	12.614	-0.024	-0.024	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.953	-0.974	13.189	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.098	-0.040	10.818	0.034	0.034	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.108	-0.043	7.950	0.026	0.026	0.000	0.000	0.000	0.000
86	A	86	SER	-1	-0.942	-0.963	8.789	-0.095	-0.095	0.000	0.000	0.000	0.000
87	A	87	SO4	-2	-1.915	-1.958	33.771	-0.121	-0.121	0.000	0.000	0.000	0.000

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