FMO DATABASE

FMODB ID: LL2G9

Calculation Name: 1HUF-A-Xray309

Preferred Name: Secreted effector protein

Target Type: SINGLE PROTEIN

Ligand Name:
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ligand 3-letter code:
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PDB ID: 1HUF

Chain ID: A

ChEMBL ID: CHEMBL3646

UniProt ID: O68720

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:

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	125
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1017333.588251
FMO2-HF: Nuclear repulsion	970454.032698
FMO2-HF: Total energy	-46879.555553
FMO2-MP2: Total energy	-47017.73985

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:2:ACE )

Summations of interaction energy for fragment #1(A:2: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.
1.402	2.641	0.073	-0.549	-0.764	0

Interaction energy analysis for fragmet #1(A:2:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / 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

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	4	SER	0	0.026	0.023	3.833	1.017	1.867	-0.006	-0.405	-0.439
4	A	5	LEU	0	0.121	0.067	6.977	-0.043	-0.043	0.000	0.000	0.000
5	A	6	SER	0	0.069	0.026	9.120	0.013	0.013	0.000	0.000	0.000
6	A	7	ASP	-1	-0.884	-0.928	8.995	-0.613	-0.613	0.000	0.000	0.000
7	A	8	LEU	0	-0.044	-0.012	5.597	0.029	0.029	0.000	0.000	0.000
8	A	9	HIS	0	0.004	-0.013	8.052	0.131	0.131	0.000	0.000	0.000
9	A	10	ARG	1	0.919	0.931	11.585	0.471	0.471	0.000	0.000	0.000
10	A	11	GLN	0	-0.033	0.009	7.924	0.225	0.225	0.000	0.000	0.000
11	A	12	VAL	0	0.039	0.021	10.096	0.074	0.074	0.000	0.000	0.000
12	A	13	SER	0	-0.043	-0.034	12.669	0.063	0.063	0.000	0.000	0.000
13	A	14	ARG	1	0.923	0.966	13.323	0.401	0.401	0.000	0.000	0.000
14	A	15	LEU	0	-0.005	0.006	12.840	0.030	0.030	0.000	0.000	0.000
15	A	16	VAL	0	-0.027	-0.018	16.533	0.028	0.028	0.000	0.000	0.000
16	A	17	GLN	0	-0.037	-0.029	18.670	0.004	0.004	0.000	0.000	0.000
17	A	18	GLN	0	-0.059	-0.020	18.335	0.014	0.014	0.000	0.000	0.000
18	A	19	GLU	-1	-0.917	-0.944	21.661	-0.052	-0.052	0.000	0.000	0.000
19	A	20	SER	0	-0.013	-0.014	18.338	0.009	0.009	0.000	0.000	0.000
20	A	21	GLY	0	0.005	-0.006	18.461	0.005	0.005	0.000	0.000	0.000
21	A	22	ASP	-1	-0.897	-0.951	18.862	-0.017	-0.017	0.000	0.000	0.000
22	A	23	CYS	0	-0.045	-0.002	17.929	0.012	0.012	0.000	0.000	0.000
23	A	24	THR	0	-0.028	-0.049	15.338	-0.010	-0.010	0.000	0.000	0.000
24	A	25	GLY	0	0.014	0.014	11.844	-0.029	-0.029	0.000	0.000	0.000
25	A	26	LYS	1	0.916	0.959	11.028	0.005	0.005	0.000	0.000	0.000
26	A	27	LEU	0	0.014	-0.009	2.991	-0.345	-0.150	0.070	-0.093	-0.173
27	A	28	ARG	1	0.958	0.961	6.532	0.032	0.032	0.000	0.000	0.000
28	A	29	GLY	0	-0.040	-0.003	5.152	0.040	0.040	0.000	0.000	0.000
29	A	30	ASN	0	0.005	0.009	6.085	-0.613	-0.613	0.000	0.000	0.000
30	A	31	VAL	0	-0.015	-0.023	7.555	0.133	0.133	0.000	0.000	0.000
31	A	32	ALA	0	-0.004	0.000	9.369	0.002	0.002	0.000	0.000	0.000
32	A	33	ALA	0	0.046	0.015	12.756	0.033	0.033	0.000	0.000	0.000
33	A	34	ASN	0	-0.090	-0.052	15.500	-0.007	-0.007	0.000	0.000	0.000
34	A	35	LYS	1	0.967	0.972	17.121	0.060	0.060	0.000	0.000	0.000
35	A	36	GLU	-1	-0.938	-0.947	20.124	0.049	0.049	0.000	0.000	0.000
36	A	37	THR	0	-0.001	0.007	19.996	0.000	0.000	0.000	0.000	0.000
37	A	38	THR	0	0.042	0.008	20.649	-0.001	-0.001	0.000	0.000	0.000
38	A	39	PHE	0	-0.006	-0.014	18.709	0.011	0.011	0.000	0.000	0.000
39	A	40	GLN	0	-0.041	-0.018	21.089	-0.007	-0.007	0.000	0.000	0.000
40	A	41	GLY	0	0.042	0.027	20.810	0.000	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.070	-0.017	19.813	0.006	0.006	0.000	0.000	0.000
42	A	43	THR	0	0.073	0.017	18.527	0.019	0.019	0.000	0.000	0.000
43	A	44	ILE	0	-0.017	-0.005	14.642	-0.013	-0.013	0.000	0.000	0.000
44	A	45	ALA	0	-0.030	-0.006	18.684	-0.018	-0.018	0.000	0.000	0.000
45	A	46	SER	0	-0.016	-0.007	21.886	-0.011	-0.011	0.000	0.000	0.000
46	A	47	GLY	0	0.037	0.015	21.740	-0.012	-0.012	0.000	0.000	0.000
47	A	48	ALA	0	-0.052	-0.015	16.562	-0.005	-0.005	0.000	0.000	0.000
48	A	49	ARG	1	0.859	0.898	14.923	-0.082	-0.082	0.000	0.000	0.000
49	A	50	GLU	-1	-0.830	-0.934	12.722	0.367	0.367	0.000	0.000	0.000
50	A	51	SER	0	-0.036	-0.023	10.007	0.081	0.081	0.000	0.000	0.000
51	A	52	GLU	-1	-0.741	-0.809	9.912	0.137	0.137	0.000	0.000	0.000
52	A	53	LYS	1	1.012	1.025	11.370	-0.362	-0.362	0.000	0.000	0.000
53	A	54	VAL	0	-0.035	-0.009	5.554	0.083	0.083	0.000	0.000	0.000
54	A	55	PHE	0	-0.002	0.025	6.960	0.141	0.141	0.000	0.000	0.000
55	A	56	ALA	0	0.057	0.022	8.150	-0.012	-0.012	0.000	0.000	0.000
56	A	57	GLN	0	0.025	-0.011	8.958	0.003	0.003	0.000	0.000	0.000
57	A	58	THR	0	-0.042	-0.028	3.490	0.190	0.384	0.009	-0.051	-0.152
58	A	59	VAL	0	-0.006	0.009	6.264	-0.166	-0.166	0.000	0.000	0.000
59	A	60	LEU	0	0.001	0.000	9.000	-0.048	-0.048	0.000	0.000	0.000
60	A	61	SER	0	-0.096	-0.057	7.261	0.047	0.047	0.000	0.000	0.000
61	A	62	HIS	0	0.008	-0.004	4.805	-0.040	-0.040	0.000	0.000	0.000
62	A	63	VAL	0	-0.019	-0.006	9.711	-0.080	-0.080	0.000	0.000	0.000
63	A	64	ALA	0	0.006	0.006	12.782	-0.016	-0.016	0.000	0.000	0.000
64	A	65	ASN	0	-0.085	-0.047	14.745	-0.026	-0.026	0.000	0.000	0.000
65	A	66	VAL	0	0.015	0.032	15.001	-0.020	-0.020	0.000	0.000	0.000
66	A	67	VAL	0	-0.079	-0.043	18.007	0.007	0.007	0.000	0.000	0.000
67	A	68	LEU	0	-0.026	-0.016	17.862	-0.010	-0.010	0.000	0.000	0.000
68	A	69	THR	0	0.048	0.004	21.770	0.003	0.003	0.000	0.000	0.000
69	A	70	GLN	0	0.055	0.008	24.818	0.004	0.004	0.000	0.000	0.000
70	A	71	GLU	-1	-0.935	-0.968	24.680	-0.025	-0.025	0.000	0.000	0.000
71	A	72	ASP	-1	-0.765	-0.845	21.123	-0.013	-0.013	0.000	0.000	0.000
72	A	73	THR	0	0.041	0.026	23.069	0.004	0.004	0.000	0.000	0.000
73	A	74	ALA	0	-0.027	-0.006	24.319	0.003	0.003	0.000	0.000	0.000
74	A	75	LYS	1	0.912	0.957	22.366	0.032	0.032	0.000	0.000	0.000
75	A	76	LEU	0	0.025	0.013	18.680	0.002	0.002	0.000	0.000	0.000
76	A	77	LEU	0	-0.013	-0.009	22.565	0.003	0.003	0.000	0.000	0.000
77	A	78	GLN	0	0.007	0.001	25.973	0.001	0.001	0.000	0.000	0.000
78	A	79	SER	0	-0.022	-0.004	20.895	0.001	0.001	0.000	0.000	0.000
79	A	80	THR	0	0.024	-0.006	23.797	0.005	0.005	0.000	0.000	0.000
80	A	81	VAL	0	-0.038	-0.015	25.315	0.001	0.001	0.000	0.000	0.000
81	A	82	LYS	1	0.869	0.940	25.074	0.003	0.003	0.000	0.000	0.000
82	A	83	HIS	0	-0.032	-0.027	22.150	0.000	0.000	0.000	0.000	0.000
83	A	84	ASN	0	-0.064	-0.016	26.172	0.004	0.004	0.000	0.000	0.000
84	A	85	LEU	0	0.017	0.017	22.473	0.005	0.005	0.000	0.000	0.000
85	A	86	ASN	0	-0.001	-0.004	23.956	0.000	0.000	0.000	0.000	0.000
86	A	87	ASN	0	0.033	0.018	16.824	0.013	0.013	0.000	0.000	0.000
87	A	88	TYR	0	-0.017	-0.043	16.403	0.025	0.025	0.000	0.000	0.000
88	A	89	ASP	-1	-0.831	-0.872	19.972	0.115	0.115	0.000	0.000	0.000
89	A	90	LEU	0	0.021	-0.001	20.423	0.008	0.008	0.000	0.000	0.000
90	A	91	ARG	1	0.963	0.980	21.908	-0.092	-0.092	0.000	0.000	0.000
91	A	92	SER	0	0.005	-0.016	24.905	-0.003	-0.003	0.000	0.000	0.000
92	A	93	VAL	0	-0.036	-0.012	25.103	0.001	0.001	0.000	0.000	0.000
93	A	94	GLY	0	0.025	0.022	27.557	-0.004	-0.004	0.000	0.000	0.000
94	A	95	ASN	0	-0.010	-0.024	29.760	-0.002	-0.002	0.000	0.000	0.000
95	A	96	GLY	0	0.007	0.012	30.235	-0.003	-0.003	0.000	0.000	0.000
96	A	97	ASN	0	0.053	0.027	25.734	-0.002	-0.002	0.000	0.000	0.000
97	A	98	SER	0	-0.097	-0.064	23.468	0.005	0.005	0.000	0.000	0.000
98	A	99	VAL	0	0.037	0.034	19.331	-0.005	-0.005	0.000	0.000	0.000
99	A	100	LEU	0	0.023	0.029	15.022	-0.001	-0.001	0.000	0.000	0.000
100	A	101	VAL	0	-0.065	-0.033	17.416	0.014	0.014	0.000	0.000	0.000
101	A	102	SER	0	-0.043	-0.059	16.663	0.026	0.026	0.000	0.000	0.000
102	A	103	LEU	0	-0.006	-0.006	13.120	-0.022	-0.022	0.000	0.000	0.000
103	A	104	ARG	1	0.860	0.937	17.437	-0.097	-0.097	0.000	0.000	0.000
104	A	105	SER	0	-0.035	-0.023	18.076	-0.009	-0.009	0.000	0.000	0.000
105	A	106	ASP	-1	-0.880	-0.938	14.859	0.301	0.301	0.000	0.000	0.000
106	A	107	GLN	0	-0.006	-0.025	14.511	0.006	0.006	0.000	0.000	0.000
107	A	108	MET	0	0.028	0.010	12.710	-0.008	-0.008	0.000	0.000	0.000
108	A	109	THR	0	0.012	0.020	14.426	-0.013	-0.013	0.000	0.000	0.000
109	A	110	LEU	0	0.038	0.010	12.675	-0.004	-0.004	0.000	0.000	0.000
110	A	111	GLN	0	-0.021	-0.023	15.224	-0.008	-0.008	0.000	0.000	0.000
111	A	112	ASP	-1	-0.763	-0.836	16.979	0.025	0.025	0.000	0.000	0.000
112	A	113	ALA	0	-0.019	-0.019	11.708	0.001	0.001	0.000	0.000	0.000
113	A	114	LYS	1	0.848	0.921	13.621	0.097	0.097	0.000	0.000	0.000
114	A	115	VAL	0	0.008	0.008	15.383	-0.008	-0.008	0.000	0.000	0.000
115	A	116	LEU	0	-0.009	-0.003	14.140	0.000	0.000	0.000	0.000	0.000
116	A	117	LEU	0	0.003	-0.008	9.391	-0.008	-0.008	0.000	0.000	0.000
117	A	118	GLU	-1	-0.825	-0.883	13.273	-0.137	-0.137	0.000	0.000	0.000
118	A	119	ALA	0	-0.004	0.011	16.617	0.000	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.008	-0.006	13.388	0.002	0.002	0.000	0.000	0.000
120	A	121	LEU	0	-0.027	-0.012	13.780	-0.017	-0.017	0.000	0.000	0.000
121	A	122	ARG	1	0.842	0.890	16.209	0.035	0.035	0.000	0.000	0.000
122	A	123	GLN	0	-0.018	-0.004	17.968	0.005	0.005	0.000	0.000	0.000
123	A	124	GLU	-1	-0.941	-0.965	14.079	-0.191	-0.191	0.000	0.000	0.000
124	A	125	SER	0	-0.122	-0.041	18.034	-0.001	-0.001	0.000	0.000	0.000
125	A	126	NME	0	0.003	-0.004	21.187	0.011	0.011	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ACE )