FMO DATABASE

FMODB ID: KGLG3

Calculation Name: 1ZHV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ZHV

Chain ID: A

ChEMBL ID:

UniProt ID: A9CJY8

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1078584.212584
FMO2-HF: Nuclear repulsion	1028257.344905
FMO2-HF: Total energy	-50326.867678
FMO2-MP2: Total energy	-50476.179719

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:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-0.162	1.981	0.008	-0.988	-1.161	0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.026 / q_NPA : 0.014

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	4	ARG	1	0.912	0.985	3.817	1.473	3.244	-0.008	-0.901	-0.862	0.005
4	A	5	ILE	0	-0.033	-0.022	6.209	0.512	0.512	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.901	0.947	8.657	0.980	0.980	0.000	0.000	0.000	0.000
6	A	7	LEU	0	0.001	0.001	9.969	0.068	0.068	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.944	0.984	13.966	0.296	0.296	0.000	0.000	0.000	0.000
8	A	9	ILE	0	0.004	0.034	17.750	0.018	0.018	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.065	-0.039	19.858	0.001	0.001	0.000	0.000	0.000	0.000
10	A	11	ASN	0	0.047	0.031	23.057	0.005	0.005	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.013	0.002	26.401	0.003	0.003	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.007	0.005	26.507	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	14	TYR	0	0.009	-0.006	25.310	0.002	0.002	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.010	0.005	27.489	0.005	0.005	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.016	-0.003	24.507	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.017	0.007	28.573	0.007	0.007	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.833	0.896	31.540	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.032	-0.019	33.517	0.001	0.001	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.024	-0.024	36.066	0.004	0.004	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.080	0.041	36.407	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.038	-0.018	37.432	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.879	-0.923	39.273	-0.020	-0.020	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.014	0.014	39.194	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.018	0.002	34.975	0.001	0.001	0.000	0.000	0.000	0.000
25	A	26	PRO	0	0.018	0.022	36.483	0.000	0.000	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.008	-0.018	38.152	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	28	TRP	0	0.041	0.018	33.756	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.004	0.012	33.782	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.879	-0.936	33.131	-0.086	-0.086	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.006	-0.004	33.118	0.005	0.005	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.024	0.004	32.301	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.011	0.004	28.261	0.004	0.004	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.006	-0.005	22.204	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.033	0.005	26.237	0.010	0.010	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.034	-0.007	24.495	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	37	ILE	0	0.023	0.012	27.040	0.007	0.007	0.000	0.000	0.000	0.000
37	A	38	THR	0	-0.010	-0.005	26.770	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.806	0.886	29.348	0.024	0.024	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.004	-0.002	28.985	0.000	0.000	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.942	-0.974	32.105	0.019	0.019	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.875	-0.936	33.144	0.018	0.018	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.891	-0.921	29.349	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.022	0.012	33.115	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.015	-0.033	28.489	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.038	-0.027	30.007	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.016	0.021	24.516	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	CYS	0	0.007	-0.008	27.839	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.024	-0.004	28.866	0.002	0.002	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.046	0.001	29.541	0.007	0.007	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.939	-0.963	32.386	-0.070	-0.070	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.762	0.866	31.743	0.082	0.082	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.043	-0.010	31.332	0.003	0.003	0.000	0.000	0.000	0.000
53	A	54	PRO	0	-0.008	0.003	36.012	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.014	-0.022	38.397	0.003	0.003	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.946	-0.963	40.855	-0.023	-0.023	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.016	-0.005	36.034	0.002	0.002	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.920	0.967	35.371	0.006	0.006	0.000	0.000	0.000	0.000
58	A	59	VAL	0	0.036	0.001	31.655	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.800	-0.832	27.676	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	61	PRO	0	0.009	-0.015	28.637	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.016	0.012	27.987	0.004	0.004	0.000	0.000	0.000	0.000
62	A	63	TRP	0	-0.050	-0.018	20.591	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.038	0.015	21.178	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	65	CYS	0	-0.039	0.003	20.207	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.048	0.022	15.837	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.927	0.969	17.483	0.348	0.348	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.042	0.017	10.031	-0.062	-0.062	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.008	-0.033	14.138	0.096	0.096	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.014	0.000	14.482	-0.083	-0.083	0.000	0.000	0.000	0.000
70	A	71	PRO	0	0.030	0.012	16.227	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	PHE	0	-0.010	-0.008	12.035	-0.106	-0.106	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.011	0.013	13.633	0.070	0.070	0.000	0.000	0.000	0.000
73	A	74	PHE	0	-0.050	-0.027	8.886	-0.184	-0.184	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.893	-0.952	9.164	-0.401	-0.401	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.908	-0.953	9.552	0.074	0.074	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.065	-0.019	4.974	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.051	0.004	6.075	-0.141	-0.141	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.030	0.019	6.382	-0.070	-0.070	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.086	0.048	7.745	-0.075	-0.075	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.007	0.003	6.943	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.040	-0.037	3.212	-0.269	-0.041	0.019	-0.076	-0.170	0.000
82	A	83	VAL	0	0.011	0.020	4.813	-0.144	-0.112	-0.001	-0.001	-0.029	0.000
83	A	84	ILE	0	0.053	0.008	7.775	0.075	0.075	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.027	0.019	6.776	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.032	0.026	6.590	0.050	0.050	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.024	0.029	9.383	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	88	SER	0	0.012	-0.014	12.364	0.008	0.008	0.000	0.000	0.000	0.000
88	A	89	THR	0	-0.107	-0.068	11.042	0.002	0.002	0.000	0.000	0.000	0.000
89	A	90	ASN	0	-0.076	-0.048	12.228	0.007	0.007	0.000	0.000	0.000	0.000
90	A	91	GLY	0	-0.003	0.006	15.491	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.055	-0.010	15.468	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.006	0.006	16.567	0.014	0.014	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.028	-0.023	13.915	-0.029	-0.029	0.000	0.000	0.000	0.000
94	A	95	PHE	0	0.048	0.025	17.293	0.019	0.019	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.006	-0.014	14.413	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.002	0.004	17.599	0.021	0.021	0.000	0.000	0.000	0.000
97	A	98	SER	0	0.005	-0.017	16.401	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	99	THR	0	-0.084	-0.053	18.627	0.012	0.012	0.000	0.000	0.000	0.000
99	A	100	PHE	0	-0.013	-0.010	19.861	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.912	-0.958	20.194	-0.220	-0.220	0.000	0.000	0.000	0.000
101	A	102	GLY	0	0.005	-0.009	16.592	-0.049	-0.049	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.863	-0.896	14.115	-0.194	-0.194	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.025	-0.024	16.409	-0.057	-0.057	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.023	-0.008	12.848	0.020	0.020	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.005	-0.007	16.627	-0.014	-0.014	0.000	0.000	0.000	0.000
106	A	107	VAL	0	0.020	0.009	16.234	0.015	0.015	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.901	0.922	19.412	0.015	0.015	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.023	-0.011	21.760	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	110	ASN	0	-0.066	-0.017	23.670	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.846	-0.935	19.347	-0.026	-0.026	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.003	0.013	18.888	-0.013	-0.013	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.862	-0.937	18.561	-0.164	-0.164	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.891	0.939	17.880	0.013	0.013	0.000	0.000	0.000	0.000
114	A	115	THR	0	0.005	-0.019	14.252	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	116	ALA	0	-0.012	-0.010	13.636	-0.050	-0.050	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.878	-0.931	13.946	-0.222	-0.222	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.052	-0.027	11.700	-0.030	-0.030	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.022	-0.014	9.184	-0.049	-0.049	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.020	0.016	8.882	-0.199	-0.199	0.000	0.000	0.000	0.000
120	A	121	ASN	0	-0.062	-0.041	9.459	-0.120	-0.120	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.049	-0.009	5.605	0.034	0.034	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.065	-0.037	4.546	-0.693	-0.626	-0.001	-0.006	-0.059	0.000
123	A	124	HIS	0	0.034	0.012	4.745	-0.560	-0.515	-0.001	-0.004	-0.041	0.000
124	A	125	SER	0	-0.061	-0.021	8.365	0.210	0.210	0.000	0.000	0.000	0.000
125	A	126	LEU	0	0.039	0.012	11.887	0.013	0.013	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.031	-0.010	14.803	0.028	0.028	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.036	-0.013	17.392	0.016	0.016	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.933	-0.946	20.475	-0.228	-0.228	0.000	0.000	0.000	0.000
129	A	130	HIS	0	-0.062	-0.060	23.789	-0.009	-0.009	0.000	0.000	0.000	0.000
130	A	131	HIS	0	-0.018	-0.011	26.181	0.010	0.010	0.000	0.000	0.000	0.000
131	A	132	HIS	0	0.016	0.009	28.635	0.000	0.000	0.000	0.000	0.000	0.000
132	A	133	HIS	0	-0.032	-0.010	30.493	0.005	0.005	0.000	0.000	0.000	0.000
133	A	134	HIS	0	-0.010	-0.005	33.966	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	HIS	0	0.034	0.024	35.654	0.003	0.003	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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