FMO DATABASE

FMODB ID: 824JY

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	OptAll
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	-1081908.411576
FMO2-HF: Nuclear repulsion	1029491.081882
FMO2-HF: Total energy	-52417.329694
FMO2-MP2: Total energy	-52572.092614

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.
1.934	4.692	0.029	-1.557	-1.23	0.006

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 : 0.068 / q_NPA : 0.033

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	3	PRO	0	-0.013	-0.008	3.382	-2.404	0.354	0.029	-1.557	-1.230	0.006
4	A	4	LYS	1	1.016	0.992	4.923	1.252	1.252	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.933	0.957	7.214	0.708	0.708	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.916	0.970	10.850	0.277	0.277	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.038	0.016	13.247	0.102	0.102	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.012	0.019	15.429	-0.015	-0.015	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.014	-0.033	18.877	0.013	0.013	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.027	-0.028	21.846	0.011	0.011	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.894	0.933	25.236	0.199	0.199	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.790	-0.864	19.570	-0.355	-0.355	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.809	0.888	20.857	0.324	0.324	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.021	-0.024	24.878	0.016	0.016	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.925	0.956	26.916	0.158	0.158	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.048	-0.020	22.269	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.049	-0.035	26.865	0.010	0.010	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.025	-0.021	29.761	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.756	-0.865	29.187	-0.117	-0.117	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.049	-0.038	28.706	0.008	0.008	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.879	-0.920	31.584	-0.101	-0.101	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.837	-0.900	34.675	-0.096	-0.096	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.050	-0.023	32.809	0.009	0.009	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.015	0.011	34.030	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.830	-0.919	35.546	-0.061	-0.061	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.029	0.007	31.786	0.003	0.003	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.995	0.987	29.967	0.045	0.045	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.877	0.920	27.828	0.085	0.085	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.002	-0.001	24.739	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.762	-0.859	24.625	-0.088	-0.088	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.041	0.021	25.978	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.045	-0.029	21.717	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.900	0.940	21.435	0.074	0.074	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.776	0.890	22.539	0.096	0.096	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.005	-0.004	21.890	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.022	-0.003	15.536	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.046	-0.022	17.024	-0.050	-0.050	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.058	0.023	15.446	0.029	0.029	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.092	0.036	18.259	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.012	0.027	19.244	0.003	0.003	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.027	-0.004	17.590	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.026	0.018	20.191	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.010	-0.006	23.399	0.010	0.010	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.021	-0.012	21.404	0.010	0.010	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.007	0.005	21.369	0.000	0.000	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.023	0.003	25.233	0.007	0.007	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.964	0.992	27.850	0.136	0.136	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.073	-0.051	25.588	0.008	0.008	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.884	0.933	28.477	0.111	0.111	0.000	0.000	0.000	0.000
50	A	50	ARG	1	1.010	1.000	30.546	0.097	0.097	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.043	0.028	29.227	0.001	0.001	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.028	-0.001	25.423	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.104	0.046	28.693	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.052	-0.005	31.983	0.006	0.006	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.038	-0.033	28.019	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.823	-0.884	29.447	-0.177	-0.177	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.932	0.961	30.351	0.125	0.125	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.864	0.947	31.014	0.168	0.168	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.026	-0.040	27.929	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.075	0.045	30.224	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.073	0.040	30.980	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.083	0.045	26.867	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.050	-0.036	25.790	-0.029	-0.029	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.016	0.011	25.376	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	CYS	0	-0.022	-0.013	21.778	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.849	0.934	20.995	0.219	0.219	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.925	0.951	16.296	0.524	0.524	0.000	0.000	0.000	0.000
68	A	68	THR	0	0.013	0.001	19.466	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.059	0.051	22.433	0.004	0.004	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.883	0.947	22.429	0.251	0.251	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.022	0.019	25.116	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.058	-0.055	27.423	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.007	-0.007	28.523	0.003	0.003	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.116	0.052	31.262	0.004	0.004	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.823	-0.921	31.555	-0.158	-0.158	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.979	0.994	34.240	0.095	0.095	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.052	0.040	36.721	0.004	0.004	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.750	-0.839	32.401	-0.160	-0.160	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.004	-0.001	36.742	0.001	0.001	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.023	0.017	38.741	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.013	0.011	37.652	0.003	0.003	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.073	-0.039	35.274	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.007	0.001	39.858	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	TRP	0	0.067	0.035	42.841	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	PHE	0	0.014	-0.011	37.527	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.033	-0.022	40.045	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	87	GLN	0	0.025	0.016	43.322	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.001	0.002	45.977	0.002	0.002	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.908	0.944	41.384	0.101	0.101	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.033	-0.001	45.723	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.001	0.012	47.968	0.002	0.002	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.021	0.014	48.293	0.002	0.002	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.016	0.003	48.229	0.000	0.000	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.019	-0.013	44.101	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.018	0.003	40.998	0.002	0.002	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.994	0.991	42.116	0.065	0.065	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.030	-0.027	39.919	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.075	0.029	40.131	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.082	0.034	42.505	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.035	-0.006	37.491	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.898	0.941	36.615	0.104	0.104	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.816	-0.883	40.275	-0.071	-0.071	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.828	0.901	43.920	0.079	0.079	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.039	-0.025	38.704	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.006	-0.012	39.969	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.891	0.946	42.096	0.070	0.070	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.026	-0.011	41.659	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.019	-0.021	40.134	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.866	-0.924	42.050	-0.069	-0.069	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.849	-0.920	45.582	-0.073	-0.073	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.112	-0.066	40.956	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.042	0.044	43.214	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.101	-0.058	38.266	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.821	-0.915	39.980	-0.079	-0.079	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.918	-0.945	35.771	-0.099	-0.099	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.076	-0.051	34.868	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	117	THR	0	0.006	-0.004	35.253	0.003	0.003	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.002	0.008	35.855	0.000	0.000	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.028	0.020	31.374	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.054	0.009	31.879	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.020	0.015	28.324	-0.006	-0.006	0.000	0.000	0.000	0.000
122	A	122	TRP	0	-0.025	-0.023	28.231	-0.014	-0.014	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.028	0.014	30.502	-0.006	-0.006	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.784	-0.870	26.516	-0.219	-0.219	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.929	0.968	24.652	0.218	0.218	0.000	0.000	0.000	0.000
126	A	126	PHE	0	0.001	0.001	27.818	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.931	0.968	31.127	0.128	0.128	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.832	0.873	22.739	0.253	0.253	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.785	0.900	27.177	0.183	0.183	0.000	0.000	0.000	0.000
130	A	130	ARG	1	0.898	0.935	28.480	0.130	0.130	0.000	0.000	0.000	0.000
131	A	131	SER	0	-0.018	0.020	29.942	0.011	0.011	0.000	0.000	0.000	0.000

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