FMO DATABASE

FMODB ID: 148JZ

Calculation Name: 1HLV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1HLV

Chain ID: A

ChEMBL ID:

UniProt ID: P07199

Base Structure: X-ray

Registration Date: 2023-06-19

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1079796.188576
FMO2-HF: Nuclear repulsion	1027380.490397
FMO2-HF: Total energy	-52415.698179
FMO2-MP2: Total energy	-52570.638808

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:MET)

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

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.
1.716	4.877	0.063	-1.821	-1.403	0.008

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.055 / q_NPA : 0.029

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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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	3	PRO	0	-0.026	-0.018	3.292	-2.551	0.610	0.063	-1.821	-1.403	0.008
4	A	4	LYS	1	1.020	0.996	5.034	1.170	1.170	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.943	0.963	7.173	0.629	0.629	0.000	0.000	0.000	0.000
6	A	6	ARG	1	1.013	1.022	10.755	0.293	0.293	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.028	-0.019	12.882	0.100	0.100	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.017	0.012	15.609	-0.014	-0.014	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.026	-0.032	18.942	0.008	0.008	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.047	-0.051	21.946	0.012	0.012	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.976	0.997	25.270	0.182	0.182	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.858	-0.917	20.410	-0.322	-0.322	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.858	0.923	21.176	0.291	0.291	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.015	-0.007	24.742	0.015	0.015	0.000	0.000	0.000	0.000
15	A	15	ARG	1	1.023	1.021	26.411	0.162	0.162	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.033	-0.012	22.228	0.008	0.008	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.061	-0.043	26.828	0.010	0.010	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.015	-0.008	29.476	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.874	-0.940	28.965	-0.101	-0.101	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.104	-0.068	29.043	0.008	0.008	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.989	-1.000	31.774	-0.097	-0.097	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.862	-0.917	34.601	-0.090	-0.090	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.058	-0.026	33.349	0.009	0.009	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.016	-0.017	34.549	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.892	-0.926	36.435	-0.054	-0.054	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.031	-0.002	31.976	0.002	0.002	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.959	0.976	29.957	0.046	0.046	0.000	0.000	0.000	0.000
28	A	28	LYS	1	1.016	0.996	27.597	0.085	0.085	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.000	-0.007	25.068	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.811	-0.907	25.072	-0.078	-0.078	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.046	0.020	26.475	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.040	-0.033	22.171	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.941	0.975	21.975	0.061	0.061	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.875	0.957	22.523	0.080	0.080	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.019	-0.004	21.911	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.050	-0.016	15.988	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.072	-0.031	17.405	-0.041	-0.041	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.046	0.015	15.633	0.026	0.026	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.107	0.040	18.464	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.001	0.005	18.911	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.042	-0.007	17.697	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.030	0.024	20.280	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.009	0.004	23.541	0.009	0.009	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.051	-0.012	21.089	0.005	0.005	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.017	0.008	21.540	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.024	0.000	24.986	0.007	0.007	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.955	0.981	27.685	0.121	0.121	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.062	-0.023	24.836	0.012	0.012	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.982	1.001	28.502	0.102	0.102	0.000	0.000	0.000	0.000
50	A	50	ARG	1	1.014	0.992	30.477	0.091	0.091	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.020	0.024	29.202	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.026	-0.023	25.227	-0.008	-0.008	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.082	0.038	28.654	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.044	-0.014	31.772	0.003	0.003	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.046	-0.032	27.964	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.825	-0.905	29.446	-0.163	-0.163	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.966	0.986	30.292	0.120	0.120	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.880	0.961	29.477	0.173	0.173	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.048	-0.049	27.443	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.097	0.067	30.552	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.036	0.004	30.836	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.060	0.039	27.163	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.050	-0.029	26.104	-0.025	-0.025	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.020	0.006	24.936	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	65	CYS	0	-0.031	-0.019	22.131	-0.020	-0.020	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.859	0.948	21.325	0.218	0.218	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.996	0.998	15.963	0.548	0.548	0.000	0.000	0.000	0.000
68	A	68	THR	0	0.032	0.017	19.462	0.014	0.014	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.056	0.034	22.113	0.002	0.002	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.955	0.984	21.837	0.259	0.259	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.017	0.009	24.891	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.046	-0.010	27.333	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.059	0.020	28.480	0.004	0.004	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.069	0.024	31.221	0.007	0.007	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.958	-0.985	32.227	-0.133	-0.133	0.000	0.000	0.000	0.000
76	A	76	LYS	1	1.035	1.019	34.059	0.090	0.090	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.041	0.019	36.960	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.783	-0.894	32.306	-0.154	-0.154	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.003	0.015	36.760	0.001	0.001	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.031	0.013	38.732	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.004	0.000	37.516	0.003	0.003	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.026	-0.022	35.495	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.009	0.000	39.973	0.003	0.003	0.000	0.000	0.000	0.000
84	A	84	TRP	0	0.061	0.026	42.538	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	PHE	0	0.016	-0.001	37.705	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.058	-0.044	39.834	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	87	GLN	0	0.021	0.016	43.541	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.005	0.009	45.980	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.903	0.944	40.520	0.099	0.099	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.021	0.008	45.907	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.004	0.005	48.156	0.002	0.002	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.017	0.013	48.272	0.002	0.002	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.009	0.005	48.284	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.030	-0.012	44.374	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.034	0.008	41.302	0.003	0.003	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.993	0.989	42.111	0.063	0.063	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.004	-0.011	39.748	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.072	0.026	40.430	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.059	0.030	42.724	0.001	0.001	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.047	-0.021	37.201	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.948	0.963	37.513	0.096	0.096	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.876	-0.918	40.332	-0.069	-0.069	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.936	0.964	43.202	0.075	0.075	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.012	-0.019	38.841	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.002	-0.005	39.780	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.971	0.995	42.225	0.068	0.068	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.029	-0.009	42.015	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.011	-0.040	40.185	0.000	0.000	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.911	-0.934	41.962	-0.065	-0.065	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.976	-0.982	45.277	-0.063	-0.063	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.124	-0.086	40.339	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.057	0.051	43.332	0.000	0.000	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.161	-0.054	38.369	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.831	-0.927	40.449	-0.073	-0.073	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.896	-0.934	35.777	-0.091	-0.091	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.125	-0.061	34.565	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	117	THR	0	0.057	0.021	35.111	0.004	0.004	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.034	-0.022	35.796	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.007	0.002	31.060	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.106	0.028	31.291	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.014	0.010	28.221	-0.007	-0.007	0.000	0.000	0.000	0.000
122	A	122	TRP	0	-0.049	-0.014	28.578	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.043	0.018	30.490	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.893	-0.946	27.217	-0.195	-0.195	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.908	0.942	24.390	0.204	0.204	0.000	0.000	0.000	0.000
126	A	126	PHE	0	0.002	0.013	27.933	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.966	0.970	31.126	0.127	0.127	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.964	0.979	22.695	0.254	0.254	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.737	0.862	27.549	0.171	0.171	0.000	0.000	0.000	0.000
130	A	130	ARG	1	0.874	0.959	28.490	0.130	0.130	0.000	0.000	0.000	0.000
131	A	131	SER	0	-0.003	0.012	30.025	0.007	0.007	0.000	0.000	0.000	0.000

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