FMO DATABASE

FMODB ID: QVGMY

Calculation Name: 2FHZ-A-Xray372

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: 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:

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. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	106
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-831684.843497
FMO2-HF: Nuclear repulsion	789667.795829
FMO2-HF: Total energy	-42017.047668
FMO2-MP2: Total energy	-42139.27894

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:4:LYS)

Summations of interaction energy for fragment #1(A:4:LYS)

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.
-108.45	-96.927	5.918	-6.072	-11.365	-0.046

Interaction energy analysis for fragmet #1(A:4:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.927 / q_NPA : 0.967

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	6	PHE	0	-0.007	0.002	2.227	-3.703	2.623	3.768	-3.645	-6.450	-0.021
4	A	7	GLU	-1	-0.876	-0.946	2.999	-38.437	-37.217	0.279	-0.673	-0.826	-0.006
5	A	8	HIS	0	0.006	-0.017	2.625	3.548	4.875	0.527	-0.480	-1.373	-0.002
6	A	9	THR	0	-0.026	-0.014	6.192	1.712	1.712	0.000	0.000	0.000	0.000
7	A	10	VAL	0	-0.003	0.006	8.702	2.564	2.564	0.000	0.000	0.000	0.000
8	A	11	LEU	0	-0.017	0.011	9.647	-2.077	-2.077	0.000	0.000	0.000	0.000
9	A	12	TYR	0	0.031	0.001	7.020	0.394	0.394	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.822	-0.910	11.732	-16.171	-16.171	0.000	0.000	0.000	0.000
11	A	14	SER	0	-0.020	-0.003	13.791	1.086	1.086	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.056	0.010	13.196	-1.696	-1.696	0.000	0.000	0.000	0.000
13	A	16	ASP	-1	-0.903	-0.951	13.194	-19.307	-19.307	0.000	0.000	0.000	0.000
14	A	17	ALA	0	0.017	0.008	9.531	-1.180	-1.180	0.000	0.000	0.000	0.000
15	A	18	PHE	0	0.019	0.008	8.400	-3.535	-3.535	0.000	0.000	0.000	0.000
16	A	19	PHE	0	-0.032	-0.026	8.478	-3.424	-3.424	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.978	-0.981	10.178	-22.908	-22.908	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.026	-0.016	5.522	-0.821	-0.821	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.888	0.940	5.054	23.150	23.287	-0.001	-0.003	-0.132	0.000
20	A	23	GLY	0	0.038	0.008	4.065	-12.187	-11.865	0.000	-0.092	-0.230	0.000
21	A	24	ASN	0	0.008	0.010	5.093	1.736	1.823	-0.001	-0.001	-0.084	0.000
22	A	25	ALA	0	-0.017	-0.007	4.071	-11.814	-11.668	-0.001	-0.042	-0.103	0.000
23	A	26	SER	0	-0.075	-0.035	2.490	-10.829	-9.026	1.348	-1.128	-2.022	-0.017
24	A	27	MET	0	-0.021	0.006	4.627	4.409	4.564	-0.001	-0.008	-0.145	0.000
25	A	28	LYS	1	0.900	0.966	6.290	40.000	40.000	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.024	-0.013	9.573	0.374	0.374	0.000	0.000	0.000	0.000
27	A	30	SER	0	0.051	0.007	12.645	0.722	0.722	0.000	0.000	0.000	0.000
28	A	31	PRO	0	0.071	0.013	16.109	-0.392	-0.392	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.839	0.924	18.665	15.876	15.876	0.000	0.000	0.000	0.000
30	A	33	ALA	0	0.026	0.011	14.189	0.169	0.169	0.000	0.000	0.000	0.000
31	A	34	ALA	0	0.013	0.013	14.712	-0.653	-0.653	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.027	0.010	15.745	0.122	0.122	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.849	-0.914	17.297	-16.271	-16.271	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.017	-0.006	11.956	0.222	0.222	0.000	0.000	0.000	0.000
35	A	38	CYS	0	-0.024	0.003	15.084	0.002	0.002	0.000	0.000	0.000	0.000
36	A	39	ASN	0	0.042	0.007	17.285	0.634	0.634	0.000	0.000	0.000	0.000
37	A	40	GLU	-1	-0.948	-0.969	16.061	-15.913	-15.913	0.000	0.000	0.000	0.000
38	A	41	ALA	0	0.003	-0.004	15.227	0.089	0.089	0.000	0.000	0.000	0.000
39	A	42	ALA	0	0.018	0.011	16.704	0.441	0.441	0.000	0.000	0.000	0.000
40	A	43	LYS	1	0.902	0.955	20.392	14.265	14.265	0.000	0.000	0.000	0.000
41	A	44	LYS	1	0.860	0.947	15.035	18.966	18.966	0.000	0.000	0.000	0.000
42	A	45	GLY	0	-0.033	-0.003	19.131	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	46	LEU	0	-0.095	-0.056	13.400	-0.223	-0.223	0.000	0.000	0.000	0.000
44	A	47	TRP	0	-0.001	-0.015	16.967	0.630	0.630	0.000	0.000	0.000	0.000
45	A	48	ILE	0	0.010	-0.007	14.600	-1.664	-1.664	0.000	0.000	0.000	0.000
46	A	49	LEU	0	-0.026	-0.021	12.646	0.996	0.996	0.000	0.000	0.000	0.000
47	A	50	GLY	0	0.029	0.015	13.894	1.055	1.055	0.000	0.000	0.000	0.000
48	A	51	ILE	0	-0.043	-0.015	13.271	-1.638	-1.638	0.000	0.000	0.000	0.000
49	A	52	ASP	-1	-0.848	-0.903	11.493	-23.054	-23.054	0.000	0.000	0.000	0.000
50	A	53	GLY	0	0.070	0.029	13.888	-0.928	-0.928	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.016	-0.014	15.614	-0.149	-0.149	0.000	0.000	0.000	0.000
52	A	55	HIS	0	0.007	0.005	16.544	0.181	0.181	0.000	0.000	0.000	0.000
53	A	56	TRP	0	-0.002	-0.007	10.976	-1.321	-1.321	0.000	0.000	0.000	0.000
54	A	57	LEU	0	-0.047	-0.044	15.948	1.126	1.126	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.079	-0.006	16.705	0.198	0.198	0.000	0.000	0.000	0.000
56	A	59	PRO	0	0.028	0.013	13.178	0.602	0.602	0.000	0.000	0.000	0.000
57	A	60	GLY	0	0.030	0.009	12.348	0.489	0.489	0.000	0.000	0.000	0.000
58	A	61	PHE	0	-0.005	-0.006	10.856	0.244	0.244	0.000	0.000	0.000	0.000
59	A	62	ARG	1	0.893	0.959	12.871	14.577	14.577	0.000	0.000	0.000	0.000
60	A	63	ILE	0	0.000	0.002	12.092	0.430	0.430	0.000	0.000	0.000	0.000
61	A	64	ASP	-1	-0.792	-0.872	14.822	-13.689	-13.689	0.000	0.000	0.000	0.000
62	A	65	SER	0	-0.018	-0.016	17.736	-0.052	-0.052	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.074	-0.043	18.712	0.173	0.173	0.000	0.000	0.000	0.000
64	A	67	ALA	0	0.029	0.018	18.531	0.419	0.419	0.000	0.000	0.000	0.000
65	A	68	SER	0	-0.097	-0.045	15.402	-0.435	-0.435	0.000	0.000	0.000	0.000
66	A	69	TRP	0	0.012	0.024	17.289	0.586	0.586	0.000	0.000	0.000	0.000
67	A	70	THR	0	-0.010	-0.034	16.727	-1.167	-1.167	0.000	0.000	0.000	0.000
68	A	71	TYR	0	-0.012	-0.002	17.909	1.281	1.281	0.000	0.000	0.000	0.000
69	A	72	ASP	-1	-0.888	-0.932	18.750	-16.354	-16.354	0.000	0.000	0.000	0.000
70	A	73	MET	0	-0.092	-0.045	18.761	0.238	0.238	0.000	0.000	0.000	0.000
71	A	74	PRO	0	-0.001	0.007	20.595	0.206	0.206	0.000	0.000	0.000	0.000
72	A	75	GLU	-1	-0.861	-0.952	23.527	-12.584	-12.584	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.985	-0.977	25.206	-10.356	-10.356	0.000	0.000	0.000	0.000
74	A	77	TYR	0	-0.006	-0.013	20.829	0.110	0.110	0.000	0.000	0.000	0.000
75	A	78	LYS	1	0.984	0.977	22.661	13.314	13.314	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.004	0.001	25.055	0.075	0.075	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.944	0.970	25.424	11.159	11.159	0.000	0.000	0.000	0.000
78	A	81	ILE	0	0.027	0.035	21.238	-0.176	-0.176	0.000	0.000	0.000	0.000
79	A	82	PRO	0	-0.020	-0.011	23.159	-0.329	-0.329	0.000	0.000	0.000	0.000
80	A	83	GLU	-1	-0.828	-0.908	25.368	-11.078	-11.078	0.000	0.000	0.000	0.000
81	A	84	ASN	0	-0.012	0.004	18.963	-0.492	-0.492	0.000	0.000	0.000	0.000
82	A	85	ASN	0	0.040	0.007	20.755	-0.875	-0.875	0.000	0.000	0.000	0.000
83	A	86	ARG	1	0.821	0.907	21.817	10.901	10.901	0.000	0.000	0.000	0.000
84	A	87	LEU	0	0.013	0.003	23.439	0.000	0.000	0.000	0.000	0.000	0.000
85	A	88	ALA	0	0.024	0.026	18.633	-0.146	-0.146	0.000	0.000	0.000	0.000
86	A	89	ILE	0	-0.044	-0.033	20.457	-0.193	-0.193	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.949	-0.976	21.957	-11.213	-11.213	0.000	0.000	0.000	0.000
88	A	91	ASN	0	0.080	0.041	19.188	0.451	0.451	0.000	0.000	0.000	0.000
89	A	92	ILE	0	-0.027	-0.009	17.018	-0.127	-0.127	0.000	0.000	0.000	0.000
90	A	93	LYS	1	0.880	0.923	20.905	12.724	12.724	0.000	0.000	0.000	0.000
91	A	94	ASP	-1	-0.844	-0.913	24.404	-11.439	-11.439	0.000	0.000	0.000	0.000
92	A	95	ASP	-1	-0.852	-0.942	19.922	-15.073	-15.073	0.000	0.000	0.000	0.000
93	A	96	ILE	0	-0.113	-0.061	21.860	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	97	GLU	-1	-0.962	-0.970	23.814	-10.545	-10.545	0.000	0.000	0.000	0.000
95	A	98	ASN	0	-0.058	-0.021	24.790	0.734	0.734	0.000	0.000	0.000	0.000
96	A	99	GLY	0	-0.023	-0.007	24.650	-0.023	-0.023	0.000	0.000	0.000	0.000
97	A	100	TYR	0	-0.106	-0.057	19.196	-0.351	-0.351	0.000	0.000	0.000	0.000
98	A	101	THR	0	-0.009	-0.024	19.136	-0.151	-0.151	0.000	0.000	0.000	0.000
99	A	102	ALA	0	-0.046	-0.027	13.705	-0.427	-0.427	0.000	0.000	0.000	0.000
100	A	103	PHE	0	-0.009	-0.001	13.695	0.374	0.374	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.021	0.013	7.781	-1.865	-1.865	0.000	0.000	0.000	0.000
102	A	105	ILE	0	-0.003	0.010	9.761	1.608	1.608	0.000	0.000	0.000	0.000
103	A	106	THR	0	0.037	0.016	8.791	-5.288	-5.288	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.009	-0.015	9.825	2.796	2.796	0.000	0.000	0.000	0.000
105	A	108	LYS	1	0.965	0.985	10.949	18.075	18.075	0.000	0.000	0.000	0.000
106	A	109	MET	0	-0.033	-0.013	9.928	0.058	0.058	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LYS)