FMO DATABASE

FMODB ID: KGL83

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	OptHSide
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	-832766.760272
FMO2-HF: Nuclear repulsion	790749.352932
FMO2-HF: Total energy	-42017.40734
FMO2-MP2: Total energy	-42139.698655

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.
-110.281	-98.09	7.192	-6.835	-12.545	-0.047

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 : 0.932 / q_NPA : 0.970

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	-0.011	0.001	2.208	-4.182	2.028	4.185	-3.655	-6.740	-0.019
4	A	7	GLU	-1	-0.807	-0.899	3.148	-35.628	-34.496	0.203	-0.586	-0.748	-0.005
5	A	8	HIS	0	0.018	-0.002	2.443	1.893	3.224	0.898	-0.616	-1.612	-0.003
6	A	9	THR	0	-0.063	-0.046	6.358	2.549	2.549	0.000	0.000	0.000	0.000
7	A	10	VAL	0	-0.022	-0.006	8.758	2.428	2.428	0.000	0.000	0.000	0.000
8	A	11	LEU	0	-0.011	0.013	9.634	-2.126	-2.126	0.000	0.000	0.000	0.000
9	A	12	TYR	0	0.029	-0.006	7.006	0.361	0.361	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.811	-0.890	11.720	-16.510	-16.510	0.000	0.000	0.000	0.000
11	A	14	SER	0	-0.004	-0.009	13.783	1.561	1.561	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.019	0.007	13.188	-1.817	-1.817	0.000	0.000	0.000	0.000
13	A	16	ASP	-1	-0.876	-0.929	12.723	-20.134	-20.134	0.000	0.000	0.000	0.000
14	A	17	ALA	0	0.039	0.020	9.556	-1.227	-1.227	0.000	0.000	0.000	0.000
15	A	18	PHE	0	0.034	0.017	7.941	-3.817	-3.817	0.000	0.000	0.000	0.000
16	A	19	PHE	0	-0.013	-0.013	7.758	-4.006	-4.006	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.961	-0.974	9.642	-24.151	-24.151	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.020	-0.013	5.556	-0.713	-0.713	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.826	0.907	4.766	23.592	23.761	-0.001	-0.008	-0.160	0.000
20	A	23	GLY	0	0.033	0.003	3.242	-17.827	-16.492	0.017	-0.698	-0.655	-0.006
21	A	24	ASN	0	-0.009	0.001	4.530	1.872	2.012	-0.001	-0.007	-0.131	0.000
22	A	25	ALA	0	-0.004	-0.001	3.659	-14.890	-14.496	0.002	-0.169	-0.227	-0.001
23	A	26	SER	0	-0.060	-0.033	2.454	-7.758	-6.466	1.890	-1.077	-2.104	-0.013
24	A	27	MET	0	-0.024	0.008	4.299	5.421	5.609	-0.001	-0.019	-0.168	0.000
25	A	28	LYS	1	0.859	0.946	5.821	41.803	41.803	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.026	-0.012	9.283	0.274	0.274	0.000	0.000	0.000	0.000
27	A	30	SER	0	0.042	-0.014	12.224	0.894	0.894	0.000	0.000	0.000	0.000
28	A	31	PRO	0	0.077	0.015	15.886	-0.479	-0.479	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.816	0.894	18.347	16.390	16.390	0.000	0.000	0.000	0.000
30	A	33	ALA	0	0.024	0.014	14.205	0.091	0.091	0.000	0.000	0.000	0.000
31	A	34	ALA	0	0.011	0.009	14.369	-0.757	-0.757	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.059	0.028	15.409	0.040	0.040	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.818	-0.893	16.831	-16.658	-16.658	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.035	-0.016	11.417	0.237	0.237	0.000	0.000	0.000	0.000
35	A	38	CYS	0	-0.024	0.004	14.552	-0.085	-0.085	0.000	0.000	0.000	0.000
36	A	39	ASN	0	0.000	-0.018	16.840	1.016	1.016	0.000	0.000	0.000	0.000
37	A	40	GLU	-1	-0.854	-0.897	15.506	-16.287	-16.287	0.000	0.000	0.000	0.000
38	A	41	ALA	0	0.012	0.002	14.612	0.094	0.094	0.000	0.000	0.000	0.000
39	A	42	ALA	0	0.022	0.013	16.147	0.451	0.451	0.000	0.000	0.000	0.000
40	A	43	LYS	1	0.845	0.917	19.824	15.741	15.741	0.000	0.000	0.000	0.000
41	A	44	LYS	1	0.813	0.907	14.407	19.317	19.317	0.000	0.000	0.000	0.000
42	A	45	GLY	0	-0.025	0.001	18.486	-0.013	-0.013	0.000	0.000	0.000	0.000
43	A	46	LEU	0	-0.103	-0.060	12.806	-0.210	-0.210	0.000	0.000	0.000	0.000
44	A	47	TRP	0	0.000	-0.016	16.500	0.661	0.661	0.000	0.000	0.000	0.000
45	A	48	ILE	0	0.006	-0.010	14.215	-1.845	-1.845	0.000	0.000	0.000	0.000
46	A	49	LEU	0	-0.022	-0.015	12.208	1.047	1.047	0.000	0.000	0.000	0.000
47	A	50	GLY	0	0.032	0.016	13.307	1.140	1.140	0.000	0.000	0.000	0.000
48	A	51	ILE	0	-0.041	-0.016	12.750	-1.855	-1.855	0.000	0.000	0.000	0.000
49	A	52	ASP	-1	-0.826	-0.880	11.633	-22.413	-22.413	0.000	0.000	0.000	0.000
50	A	53	GLY	0	0.068	0.027	13.646	-0.955	-0.955	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.026	-0.009	15.562	-0.094	-0.094	0.000	0.000	0.000	0.000
52	A	55	HIS	0	0.022	0.028	16.466	0.198	0.198	0.000	0.000	0.000	0.000
53	A	56	TRP	0	0.007	0.001	11.039	-1.247	-1.247	0.000	0.000	0.000	0.000
54	A	57	LEU	0	-0.053	-0.046	16.020	1.123	1.123	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.080	-0.006	16.787	0.211	0.211	0.000	0.000	0.000	0.000
56	A	59	PRO	0	0.034	0.017	13.279	0.619	0.619	0.000	0.000	0.000	0.000
57	A	60	GLY	0	0.029	0.007	12.488	0.529	0.529	0.000	0.000	0.000	0.000
58	A	61	PHE	0	-0.006	-0.011	10.797	0.248	0.248	0.000	0.000	0.000	0.000
59	A	62	ARG	1	0.867	0.937	12.920	14.513	14.513	0.000	0.000	0.000	0.000
60	A	63	ILE	0	-0.003	-0.001	12.100	0.394	0.394	0.000	0.000	0.000	0.000
61	A	64	ASP	-1	-0.781	-0.851	14.893	-13.592	-13.592	0.000	0.000	0.000	0.000
62	A	65	SER	0	0.012	-0.005	17.766	-0.142	-0.142	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.123	-0.074	18.755	0.206	0.206	0.000	0.000	0.000	0.000
64	A	67	ALA	0	0.041	0.022	18.431	0.406	0.406	0.000	0.000	0.000	0.000
65	A	68	SER	0	-0.097	-0.059	15.322	-0.416	-0.416	0.000	0.000	0.000	0.000
66	A	69	TRP	0	0.007	0.022	16.698	0.537	0.537	0.000	0.000	0.000	0.000
67	A	70	THR	0	-0.023	-0.043	16.291	-1.252	-1.252	0.000	0.000	0.000	0.000
68	A	71	TYR	0	-0.006	0.004	17.429	1.291	1.291	0.000	0.000	0.000	0.000
69	A	72	ASP	-1	-0.877	-0.929	18.280	-16.577	-16.577	0.000	0.000	0.000	0.000
70	A	73	MET	0	-0.093	-0.045	18.105	0.178	0.178	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.000	0.007	20.037	0.220	0.220	0.000	0.000	0.000	0.000
72	A	75	GLU	-1	-0.862	-0.949	22.945	-12.705	-12.705	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.975	-0.974	24.633	-10.543	-10.543	0.000	0.000	0.000	0.000
74	A	77	TYR	0	0.010	-0.005	19.495	0.345	0.345	0.000	0.000	0.000	0.000
75	A	78	LYS	1	0.967	0.964	21.942	13.869	13.869	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.006	0.002	24.678	0.066	0.066	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.937	0.968	24.922	11.314	11.314	0.000	0.000	0.000	0.000
78	A	81	ILE	0	0.014	0.030	20.696	-0.203	-0.203	0.000	0.000	0.000	0.000
79	A	82	PRO	0	-0.022	-0.012	22.794	-0.347	-0.347	0.000	0.000	0.000	0.000
80	A	83	GLU	-1	-0.777	-0.873	25.012	-11.468	-11.468	0.000	0.000	0.000	0.000
81	A	84	ASN	0	-0.026	-0.002	18.495	-0.589	-0.589	0.000	0.000	0.000	0.000
82	A	85	ASN	0	0.030	-0.002	20.421	-0.966	-0.966	0.000	0.000	0.000	0.000
83	A	86	ARG	1	0.717	0.829	21.475	11.170	11.170	0.000	0.000	0.000	0.000
84	A	87	LEU	0	0.009	0.005	22.964	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	88	ALA	0	0.009	0.016	18.340	-0.143	-0.143	0.000	0.000	0.000	0.000
86	A	89	ILE	0	-0.030	-0.031	20.157	-0.215	-0.215	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.843	-0.904	21.694	-11.311	-11.311	0.000	0.000	0.000	0.000
88	A	91	ASN	0	0.057	0.034	19.330	0.556	0.556	0.000	0.000	0.000	0.000
89	A	92	ILE	0	-0.015	-0.010	16.846	-0.098	-0.098	0.000	0.000	0.000	0.000
90	A	93	LYS	1	0.886	0.930	20.673	12.777	12.777	0.000	0.000	0.000	0.000
91	A	94	ASP	-1	-0.844	-0.912	24.134	-11.408	-11.408	0.000	0.000	0.000	0.000
92	A	95	ASP	-1	-0.868	-0.940	19.832	-15.146	-15.146	0.000	0.000	0.000	0.000
93	A	96	ILE	0	-0.096	-0.053	21.448	0.008	0.008	0.000	0.000	0.000	0.000
94	A	97	GLU	-1	-0.959	-0.968	23.499	-10.580	-10.580	0.000	0.000	0.000	0.000
95	A	98	ASN	0	-0.110	-0.058	24.626	0.698	0.698	0.000	0.000	0.000	0.000
96	A	99	GLY	0	-0.016	0.002	24.469	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	100	TYR	0	-0.105	-0.065	18.978	-0.374	-0.374	0.000	0.000	0.000	0.000
98	A	101	THR	0	-0.017	-0.028	18.959	-0.135	-0.135	0.000	0.000	0.000	0.000
99	A	102	ALA	0	-0.044	-0.025	13.521	-0.430	-0.430	0.000	0.000	0.000	0.000
100	A	103	PHE	0	0.001	0.002	13.377	0.416	0.416	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.028	0.009	7.436	-2.038	-2.038	0.000	0.000	0.000	0.000
102	A	105	ILE	0	-0.003	0.011	9.578	1.665	1.665	0.000	0.000	0.000	0.000
103	A	106	THR	0	0.048	0.020	8.450	-5.887	-5.887	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.008	-0.009	9.388	2.989	2.989	0.000	0.000	0.000	0.000
105	A	108	LYS	1	0.971	0.990	10.426	18.536	18.536	0.000	0.000	0.000	0.000
106	A	109	MET	0	-0.037	-0.018	9.604	0.028	0.028	0.000	0.000	0.000	0.000

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