FMO DATABASE

FMODB ID: GNZQ1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1079916.551857
FMO2-HF: Nuclear repulsion	1027499.766836
FMO2-HF: Total energy	-52416.785022
FMO2-MP2: Total energy	-52571.637035

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.
1.437	4.6	0.042	-1.814	-1.391	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 : 0.053 / q_NPA : 0.027

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	-0.018	-0.016	3.333	-2.660	0.503	0.042	-1.814	-1.391	0.008
4	A	4	LYS	1	1.013	0.994	4.916	1.068	1.068	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.940	0.964	7.199	0.634	0.634	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.963	0.996	10.783	0.281	0.281	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.019	0.002	12.926	0.100	0.100	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.009	0.018	15.642	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.002	-0.031	18.983	0.007	0.007	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.021	-0.033	21.983	0.013	0.013	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.935	0.968	25.305	0.194	0.194	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.795	-0.876	19.935	-0.337	-0.337	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.792	0.884	20.948	0.308	0.308	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.010	-0.023	24.786	0.016	0.016	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.943	0.977	26.827	0.157	0.157	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.030	-0.010	22.278	0.008	0.008	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.055	-0.038	26.883	0.011	0.011	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.032	-0.029	29.524	0.000	0.000	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.811	-0.899	29.179	-0.112	-0.112	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.068	-0.048	29.010	0.008	0.008	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.881	-0.925	31.829	-0.097	-0.097	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.849	-0.894	34.648	-0.092	-0.092	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.064	-0.033	33.296	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.004	-0.008	34.367	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.887	-0.931	36.201	-0.056	-0.056	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.002	0.017	31.701	0.002	0.002	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.968	0.970	29.782	0.044	0.044	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.984	0.984	27.695	0.080	0.080	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.004	-0.002	24.868	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.781	-0.880	24.828	-0.082	-0.082	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.039	0.016	26.297	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.037	-0.029	21.963	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.920	0.957	21.711	0.067	0.067	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.831	0.922	22.254	0.083	0.083	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.025	-0.008	21.962	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.060	-0.021	15.822	-0.013	-0.013	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.055	-0.026	17.361	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.045	0.017	15.415	0.027	0.027	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.099	0.040	18.268	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.005	0.011	18.842	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.030	-0.008	17.658	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.027	0.020	20.213	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.006	0.000	23.491	0.009	0.009	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.019	-0.005	21.102	0.007	0.007	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.002	0.010	21.250	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.033	0.007	25.019	0.006	0.006	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.959	0.983	27.693	0.122	0.122	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.085	-0.043	25.340	0.009	0.009	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.896	0.937	28.524	0.102	0.102	0.000	0.000	0.000	0.000
50	A	50	ARG	1	1.008	0.992	30.508	0.091	0.091	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.024	0.025	29.249	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.019	-0.014	25.234	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.099	0.047	28.680	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.036	-0.010	31.804	0.004	0.004	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.059	-0.038	28.121	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.812	-0.869	29.438	-0.170	-0.170	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.937	0.970	30.365	0.121	0.121	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.894	0.969	30.143	0.171	0.171	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.060	-0.067	27.817	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.110	0.075	30.565	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.044	0.004	30.916	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.052	0.036	27.160	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.057	-0.037	26.120	-0.028	-0.028	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.010	0.004	25.109	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	65	CYS	0	-0.011	-0.011	22.145	-0.016	-0.016	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.869	0.959	21.341	0.220	0.220	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.931	0.968	16.140	0.525	0.525	0.000	0.000	0.000	0.000
68	A	68	THR	0	0.027	0.007	19.361	0.011	0.011	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.071	0.052	22.247	0.005	0.005	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.952	0.982	22.121	0.256	0.256	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.012	0.007	25.003	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.064	-0.043	27.425	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.056	0.019	28.576	0.004	0.004	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.064	0.025	31.298	0.003	0.003	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.943	-0.978	32.342	-0.141	-0.141	0.000	0.000	0.000	0.000
76	A	76	LYS	1	1.017	1.010	34.155	0.091	0.091	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.043	0.030	36.641	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.773	-0.873	32.399	-0.157	-0.157	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.000	0.012	36.768	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.021	0.007	38.841	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.009	0.007	37.666	0.002	0.002	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.023	-0.022	35.409	0.000	0.000	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.004	0.002	39.984	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	TRP	0	0.060	0.026	42.619	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	PHE	0	0.018	-0.001	37.755	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.057	-0.039	40.127	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	87	GLN	0	0.029	0.017	43.555	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.002	0.006	46.140	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.911	0.950	41.116	0.101	0.101	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.026	0.007	45.923	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.003	0.003	48.171	0.002	0.002	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.016	0.014	48.290	0.002	0.002	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.005	0.010	48.293	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.025	-0.012	44.390	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.028	0.005	41.329	0.003	0.003	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.987	0.988	42.127	0.065	0.065	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.013	-0.016	39.762	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.079	0.024	40.446	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.064	0.028	42.739	0.001	0.001	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.043	-0.014	37.296	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.893	0.933	36.576	0.105	0.105	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.818	-0.880	40.344	-0.070	-0.070	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.935	0.971	43.605	0.077	0.077	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.024	-0.024	38.828	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.002	-0.010	39.836	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.910	0.957	42.233	0.070	0.070	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.042	-0.014	41.869	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.031	-0.033	40.195	0.000	0.000	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.873	-0.924	41.967	-0.067	-0.067	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.944	-0.975	45.282	-0.069	-0.069	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.116	-0.080	40.680	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.062	0.055	43.401	0.000	0.000	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.126	-0.062	38.276	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.828	-0.921	40.452	-0.074	-0.074	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.907	-0.940	35.792	-0.094	-0.094	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.129	-0.071	34.858	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	117	THR	0	0.067	0.023	35.297	0.004	0.004	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.013	-0.003	35.756	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.016	0.008	31.293	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.074	0.025	31.485	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.021	0.016	28.232	-0.007	-0.007	0.000	0.000	0.000	0.000
122	A	122	TRP	0	-0.037	-0.017	28.590	-0.012	-0.012	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.043	0.019	30.500	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.778	-0.859	26.861	-0.215	-0.215	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.941	0.957	24.624	0.213	0.213	0.000	0.000	0.000	0.000
126	A	126	PHE	0	-0.014	0.002	27.946	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.943	0.966	31.139	0.129	0.129	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.826	0.879	23.055	0.251	0.251	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.780	0.893	27.496	0.177	0.177	0.000	0.000	0.000	0.000
130	A	130	ARG	1	0.827	0.933	28.503	0.130	0.130	0.000	0.000	0.000	0.000
131	A	131	SER	0	-0.002	0.020	30.095	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)