FMO DATABASE

FMODB ID: P592Z

Calculation Name: 2FHZ-A-Xray13

Preferred Name:
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Target Type:
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Ligand Name:
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ligand 3-letter code:
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PDB ID: 2FHZ

Chain ID: A

ChEMBL ID:
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UniProt ID: P18000

Base Structure: X-ray

Registration Date: 2018-02-14

Reference:

DOI:

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	107
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-835647.136246
FMO2-HF: Nuclear repulsion	793478.845262
FMO2-HF: Total energy	-42168.290984
FMO2-MP2: Total energy	-42290.958976

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:3:ACE)

Summations of interaction energy for fragment #1(A:3: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.
-0.224	0.528	-0.01	-0.321	-0.421	0

Interaction energy analysis for fragmet #1(A:3:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.020 / q_NPA : 0.000

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].
3	A	5	LEU	0	0.026	0.026	3.874	0.776	1.528	-0.010	-0.321	-0.421
4	A	6	PHE	0	-0.004	0.006	7.022	0.243	0.243	0.000	0.000	0.000
5	A	7	GLU	-1	-0.881	-0.949	6.872	-0.484	-0.484	0.000	0.000	0.000
6	A	8	HIS	0	0.010	-0.015	6.060	0.172	0.172	0.000	0.000	0.000
7	A	9	THR	0	-0.030	-0.017	9.659	0.046	0.046	0.000	0.000	0.000
8	A	10	VAL	0	-0.005	0.005	12.311	0.055	0.055	0.000	0.000	0.000
9	A	11	LEU	0	-0.017	0.011	13.979	-0.050	-0.050	0.000	0.000	0.000
10	A	12	TYR	0	0.032	0.001	11.733	-0.005	-0.005	0.000	0.000	0.000
11	A	13	ASP	-1	-0.825	-0.912	16.915	-0.146	-0.146	0.000	0.000	0.000
12	A	14	SER	0	-0.022	-0.005	19.267	0.018	0.018	0.000	0.000	0.000
13	A	15	GLY	0	0.058	0.011	18.769	-0.034	-0.034	0.000	0.000	0.000
14	A	16	ASP	-1	-0.903	-0.951	18.659	-0.223	-0.223	0.000	0.000	0.000
15	A	17	ALA	0	0.013	0.006	14.948	-0.027	-0.027	0.000	0.000	0.000
16	A	18	PHE	0	0.020	0.009	14.056	-0.091	-0.091	0.000	0.000	0.000
17	A	19	PHE	0	-0.023	-0.020	13.934	-0.071	-0.071	0.000	0.000	0.000
18	A	20	GLU	-1	-0.982	-0.983	14.546	-0.298	-0.298	0.000	0.000	0.000
19	A	21	LEU	0	-0.033	-0.020	10.333	-0.027	-0.027	0.000	0.000	0.000
20	A	22	LYS	1	0.896	0.944	9.333	0.222	0.222	0.000	0.000	0.000
21	A	23	GLY	0	0.034	0.005	9.534	-0.239	-0.239	0.000	0.000	0.000
22	A	24	ASN	0	0.024	0.019	11.233	0.074	0.074	0.000	0.000	0.000
23	A	25	ALA	0	-0.013	-0.005	11.471	-0.118	-0.118	0.000	0.000	0.000
24	A	26	SER	0	-0.075	-0.036	8.827	-0.143	-0.143	0.000	0.000	0.000
25	A	27	MET	0	-0.025	0.004	11.116	0.053	0.053	0.000	0.000	0.000
26	A	28	LYS	1	0.896	0.964	10.626	0.546	0.546	0.000	0.000	0.000
27	A	29	LEU	0	-0.021	-0.012	14.744	-0.004	-0.004	0.000	0.000	0.000
28	A	30	SER	0	0.047	0.005	17.906	0.018	0.018	0.000	0.000	0.000
29	A	31	PRO	0	0.070	0.012	21.186	-0.009	-0.009	0.000	0.000	0.000
30	A	32	LYS	1	0.834	0.921	24.143	0.150	0.150	0.000	0.000	0.000
31	A	33	ALA	0	0.026	0.011	19.773	0.001	0.001	0.000	0.000	0.000
32	A	34	ALA	0	0.015	0.014	20.988	-0.013	-0.013	0.000	0.000	0.000
33	A	35	ILE	0	0.024	0.009	21.935	0.002	0.002	0.000	0.000	0.000
34	A	36	GLU	-1	-0.851	-0.915	22.955	-0.163	-0.163	0.000	0.000	0.000
35	A	37	VAL	0	-0.012	-0.003	18.458	0.003	0.003	0.000	0.000	0.000
36	A	38	CYS	0	-0.022	0.004	21.540	0.002	0.002	0.000	0.000	0.000
37	A	39	ASN	0	0.037	0.005	24.224	0.011	0.011	0.000	0.000	0.000
38	A	40	GLU	-1	-0.952	-0.971	21.958	-0.159	-0.159	0.000	0.000	0.000
39	A	41	ALA	0	0.011	0.000	22.236	0.002	0.002	0.000	0.000	0.000
40	A	42	ALA	0	0.016	0.010	23.533	0.008	0.008	0.000	0.000	0.000
41	A	43	LYS	1	0.894	0.951	26.648	0.133	0.133	0.000	0.000	0.000
42	A	44	LYS	1	0.861	0.947	20.635	0.210	0.210	0.000	0.000	0.000
43	A	45	GLY	0	-0.037	-0.005	25.363	0.001	0.001	0.000	0.000	0.000
44	A	46	LEU	0	-0.077	-0.046	20.052	0.000	0.000	0.000	0.000	0.000
45	A	47	TRP	0	-0.007	-0.018	23.939	0.008	0.008	0.000	0.000	0.000
46	A	48	ILE	0	0.010	-0.006	21.996	-0.022	-0.022	0.000	0.000	0.000
47	A	49	LEU	0	-0.019	-0.017	19.562	0.016	0.016	0.000	0.000	0.000
48	A	50	GLY	0	0.025	0.013	21.099	0.018	0.018	0.000	0.000	0.000
49	A	51	ILE	0	-0.043	-0.016	20.438	-0.028	-0.028	0.000	0.000	0.000
50	A	52	ASP	-1	-0.848	-0.903	17.922	-0.201	-0.201	0.000	0.000	0.000
51	A	53	GLY	0	0.069	0.028	20.217	-0.018	-0.018	0.000	0.000	0.000
52	A	54	GLY	0	0.015	-0.015	21.003	0.004	0.004	0.000	0.000	0.000
53	A	55	HIS	0	0.006	0.004	21.570	0.002	0.002	0.000	0.000	0.000
54	A	56	TRP	0	-0.001	-0.006	14.806	-0.012	-0.012	0.000	0.000	0.000
55	A	57	LEU	0	-0.049	-0.045	19.801	0.015	0.015	0.000	0.000	0.000
56	A	58	ASN	0	-0.080	-0.007	20.252	0.003	0.003	0.000	0.000	0.000
57	A	59	PRO	0	0.026	0.012	15.989	0.011	0.011	0.000	0.000	0.000
58	A	60	GLY	0	0.029	0.009	15.580	0.015	0.015	0.000	0.000	0.000
59	A	61	PHE	0	-0.002	-0.004	15.119	-0.007	-0.007	0.000	0.000	0.000
60	A	62	ARG	1	0.890	0.957	16.834	0.083	0.083	0.000	0.000	0.000
61	A	63	ILE	0	0.003	0.004	17.658	0.000	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.795	-0.874	20.020	-0.070	-0.070	0.000	0.000	0.000
63	A	65	SER	0	-0.017	-0.015	23.298	-0.005	-0.005	0.000	0.000	0.000
64	A	66	SER	0	-0.076	-0.044	24.143	-0.001	-0.001	0.000	0.000	0.000
65	A	67	ALA	0	0.027	0.017	24.564	0.003	0.003	0.000	0.000	0.000
66	A	68	SER	0	-0.096	-0.044	21.613	-0.007	-0.007	0.000	0.000	0.000
67	A	69	TRP	0	0.011	0.023	23.989	0.008	0.008	0.000	0.000	0.000
68	A	70	THR	0	-0.015	-0.036	23.683	-0.014	-0.014	0.000	0.000	0.000
69	A	71	TYR	0	-0.017	-0.003	25.030	0.016	0.016	0.000	0.000	0.000
70	A	72	ASP	-1	-0.887	-0.932	25.527	-0.120	-0.120	0.000	0.000	0.000
71	A	73	MET	0	-0.084	-0.041	25.581	0.000	0.000	0.000	0.000	0.000
72	A	74	PRO	0	-0.007	0.004	27.441	0.005	0.005	0.000	0.000	0.000
73	A	75	GLU	-1	-0.861	-0.952	30.096	-0.079	-0.079	0.000	0.000	0.000
74	A	76	GLU	-1	-0.989	-0.979	31.528	-0.064	-0.064	0.000	0.000	0.000
75	A	77	TYR	0	0.000	-0.010	27.463	0.000	0.000	0.000	0.000	0.000
76	A	78	LYS	1	0.987	0.979	29.050	0.101	0.101	0.000	0.000	0.000
77	A	79	SER	0	-0.002	-0.003	31.944	0.000	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.941	0.968	32.571	0.075	0.075	0.000	0.000	0.000
79	A	81	ILE	0	0.033	0.039	28.205	-0.002	-0.002	0.000	0.000	0.000
80	A	82	PRO	0	-0.023	-0.012	30.474	-0.005	-0.005	0.000	0.000	0.000
81	A	83	GLU	-1	-0.832	-0.910	32.685	-0.079	-0.079	0.000	0.000	0.000
82	A	84	ASN	0	-0.010	0.006	26.299	-0.008	-0.008	0.000	0.000	0.000
83	A	85	ASN	0	0.044	0.009	28.059	-0.012	-0.012	0.000	0.000	0.000
84	A	86	ARG	1	0.816	0.905	29.125	0.077	0.077	0.000	0.000	0.000
85	A	87	LEU	0	0.011	0.002	30.792	0.000	0.000	0.000	0.000	0.000
86	A	88	ALA	0	0.028	0.029	25.875	-0.001	-0.001	0.000	0.000	0.000
87	A	89	ILE	0	-0.043	-0.032	27.495	-0.002	-0.002	0.000	0.000	0.000
88	A	90	GLU	-1	-0.952	-0.977	28.932	-0.079	-0.079	0.000	0.000	0.000
89	A	91	ASN	0	0.080	0.041	25.895	0.008	0.008	0.000	0.000	0.000
90	A	92	ILE	0	-0.024	-0.008	23.821	-0.001	-0.001	0.000	0.000	0.000
91	A	93	LYS	1	0.879	0.922	27.452	0.103	0.103	0.000	0.000	0.000
92	A	94	ASP	-1	-0.846	-0.915	30.763	-0.078	-0.078	0.000	0.000	0.000
93	A	95	ASP	-1	-0.851	-0.941	26.274	-0.115	-0.115	0.000	0.000	0.000
94	A	96	ILE	0	-0.112	-0.061	27.685	0.001	0.001	0.000	0.000	0.000
95	A	97	GLU	-1	-0.964	-0.971	29.632	-0.066	-0.066	0.000	0.000	0.000
96	A	98	ASN	0	-0.059	-0.022	30.744	0.010	0.010	0.000	0.000	0.000
97	A	99	GLY	0	-0.025	-0.008	29.997	0.002	0.002	0.000	0.000	0.000
98	A	100	TYR	0	-0.105	-0.057	24.898	-0.002	-0.002	0.000	0.000	0.000
99	A	101	THR	0	-0.011	-0.025	23.882	-0.004	-0.004	0.000	0.000	0.000
100	A	102	ALA	0	-0.047	-0.028	18.843	-0.008	-0.008	0.000	0.000	0.000
101	A	103	PHE	0	-0.010	-0.002	19.533	0.010	0.010	0.000	0.000	0.000
102	A	104	ILE	0	-0.020	0.013	13.886	-0.035	-0.035	0.000	0.000	0.000
103	A	105	ILE	0	-0.007	0.008	16.564	0.031	0.031	0.000	0.000	0.000
104	A	106	THR	0	0.036	0.015	16.095	-0.076	-0.076	0.000	0.000	0.000
105	A	107	LEU	0	-0.024	-0.024	17.172	0.041	0.041	0.000	0.000	0.000
106	A	108	LYS	1	0.942	0.968	17.939	0.149	0.149	0.000	0.000	0.000
107	A	109	MET	-1	-0.961	-0.974	16.279	-0.260	-0.260	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ACE)