FMO DATABASE

FMODB ID: 14LYZ

Calculation Name: 4EXW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4EXW

Chain ID: A

ChEMBL ID:

UniProt ID: Q1J1N6

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:

Apendix: None

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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1088336.669135
FMO2-HF: Nuclear repulsion	1036867.872098
FMO2-HF: Total energy	-51468.797037
FMO2-MP2: Total energy	-51620.945946

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:-5:GLY)

Summations of interaction energy for fragment #1(A:-5:GLY)

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.
1.083	2.024	-0.005	-0.333	-0.603	0

Interaction energy analysis for fragmet #1(A:-5:GLY)

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 : -0.022

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	-3	ASP	-1	-0.836	-0.896	3.799	0.215	1.156	-0.005	-0.333	-0.603
4	A	-2	PRO	0	-0.019	-0.022	6.460	0.148	0.148	0.000	0.000	0.000
5	A	-1	PHE	0	-0.053	-0.022	9.481	0.057	0.057	0.000	0.000	0.000
6	A	0	THR	0	-0.022	-0.021	9.770	-0.045	-0.045	0.000	0.000	0.000
7	A	1	MET	0	-0.016	0.002	12.145	-0.015	-0.015	0.000	0.000	0.000
8	A	2	LEU	0	-0.042	-0.014	10.944	-0.030	-0.030	0.000	0.000	0.000
9	A	3	HIS	1	0.802	0.871	15.200	0.260	0.260	0.000	0.000	0.000
10	A	4	ILE	0	0.009	0.022	18.330	-0.023	-0.023	0.000	0.000	0.000
11	A	5	GLU	-1	-0.809	-0.890	20.014	-0.114	-0.114	0.000	0.000	0.000
12	A	6	PHE	0	0.002	-0.001	22.001	-0.004	-0.004	0.000	0.000	0.000
13	A	7	ILE	0	-0.026	-0.010	25.949	0.002	0.002	0.000	0.000	0.000
14	A	8	THR	0	-0.004	-0.007	29.493	0.002	0.002	0.000	0.000	0.000
15	A	9	ASP	-1	-0.821	-0.915	31.396	-0.047	-0.047	0.000	0.000	0.000
16	A	10	LEU	0	-0.059	-0.030	34.367	0.003	0.003	0.000	0.000	0.000
17	A	11	GLY	0	-0.025	-0.005	34.338	0.001	0.001	0.000	0.000	0.000
18	A	12	ALA	0	-0.038	-0.005	33.436	-0.003	-0.003	0.000	0.000	0.000
19	A	13	LYS	1	0.853	0.908	27.195	0.114	0.114	0.000	0.000	0.000
20	A	14	VAL	0	0.002	0.004	27.362	0.002	0.002	0.000	0.000	0.000
21	A	15	THR	0	0.002	-0.003	22.511	-0.005	-0.005	0.000	0.000	0.000
22	A	16	VAL	0	-0.027	-0.007	21.690	0.010	0.010	0.000	0.000	0.000
23	A	17	ASP	-1	-0.811	-0.898	20.112	-0.165	-0.165	0.000	0.000	0.000
24	A	18	VAL	0	-0.032	-0.021	15.298	0.020	0.020	0.000	0.000	0.000
25	A	19	GLU	-1	-0.826	-0.892	15.542	0.003	0.003	0.000	0.000	0.000
26	A	20	SER	0	0.082	0.029	10.879	-0.025	-0.025	0.000	0.000	0.000
27	A	21	ALA	0	0.033	0.001	8.079	0.026	0.026	0.000	0.000	0.000
28	A	22	ASP	-1	-0.925	-0.959	8.082	0.418	0.418	0.000	0.000	0.000
29	A	23	LYS	1	0.821	0.896	10.587	-0.020	-0.020	0.000	0.000	0.000
30	A	24	LEU	0	-0.014	0.002	12.993	-0.001	-0.001	0.000	0.000	0.000
31	A	25	LEU	0	0.008	-0.015	13.039	0.016	0.016	0.000	0.000	0.000
32	A	26	ASP	-1	-0.882	-0.941	15.941	0.025	0.025	0.000	0.000	0.000
33	A	27	VAL	0	-0.002	-0.001	17.885	0.005	0.005	0.000	0.000	0.000
34	A	28	GLN	0	-0.013	-0.021	16.406	-0.014	-0.014	0.000	0.000	0.000
35	A	29	ARG	1	0.839	0.912	17.641	0.032	0.032	0.000	0.000	0.000
36	A	30	GLN	0	-0.041	-0.004	22.171	0.010	0.010	0.000	0.000	0.000
37	A	31	TYR	0	0.015	-0.005	23.195	0.007	0.007	0.000	0.000	0.000
38	A	32	GLY	0	0.063	0.046	24.362	0.000	0.000	0.000	0.000	0.000
39	A	33	ARG	1	0.784	0.862	24.458	0.031	0.031	0.000	0.000	0.000
40	A	34	LEU	0	-0.040	-0.009	28.177	0.005	0.005	0.000	0.000	0.000
41	A	35	GLY	0	-0.032	-0.003	29.280	0.002	0.002	0.000	0.000	0.000
42	A	36	TRP	0	-0.047	-0.020	26.858	-0.004	-0.004	0.000	0.000	0.000
43	A	37	THR	0	-0.011	-0.003	26.035	0.000	0.000	0.000	0.000	0.000
44	A	38	SER	0	-0.039	-0.045	22.077	-0.007	-0.007	0.000	0.000	0.000
45	A	39	GLY	0	0.006	0.013	23.417	-0.008	-0.008	0.000	0.000	0.000
46	A	40	GLU	-1	-0.798	-0.886	24.574	-0.081	-0.081	0.000	0.000	0.000
47	A	41	VAL	0	-0.043	-0.009	25.502	-0.008	-0.008	0.000	0.000	0.000
48	A	42	PRO	0	-0.019	0.006	24.047	0.002	0.002	0.000	0.000	0.000
49	A	43	VAL	0	0.074	0.023	26.843	0.008	0.008	0.000	0.000	0.000
50	A	44	GLY	0	0.000	0.003	29.409	-0.001	-0.001	0.000	0.000	0.000
51	A	45	GLY	0	-0.036	-0.015	28.736	0.005	0.005	0.000	0.000	0.000
52	A	46	TYR	0	0.025	0.000	22.853	-0.002	-0.002	0.000	0.000	0.000
53	A	47	GLN	0	-0.024	-0.018	23.243	0.018	0.018	0.000	0.000	0.000
54	A	48	PHE	0	-0.001	0.005	20.718	-0.014	-0.014	0.000	0.000	0.000
55	A	49	PRO	0	0.023	0.001	19.505	0.004	0.004	0.000	0.000	0.000
56	A	50	LEU	0	0.012	-0.001	22.602	0.003	0.003	0.000	0.000	0.000
57	A	51	GLU	-1	-0.909	-0.964	23.503	-0.008	-0.008	0.000	0.000	0.000
58	A	52	ASN	0	-0.007	-0.026	20.288	-0.001	-0.001	0.000	0.000	0.000
59	A	53	GLU	-1	-0.781	-0.836	24.006	-0.027	-0.027	0.000	0.000	0.000
60	A	54	PRO	0	-0.006	0.003	27.231	0.000	0.000	0.000	0.000	0.000
61	A	55	ASP	-1	-0.857	-0.926	24.784	0.000	0.000	0.000	0.000	0.000
62	A	56	PHE	0	0.026	0.017	21.630	0.000	0.000	0.000	0.000	0.000
63	A	57	ASP	-1	-0.734	-0.844	22.358	-0.027	-0.027	0.000	0.000	0.000
64	A	58	TRP	0	0.038	-0.002	23.764	-0.013	-0.013	0.000	0.000	0.000
65	A	59	SER	0	-0.054	-0.030	24.359	-0.006	-0.006	0.000	0.000	0.000
66	A	60	LEU	0	-0.025	-0.008	18.875	-0.008	-0.008	0.000	0.000	0.000
67	A	61	ILE	0	-0.041	-0.019	21.958	-0.014	-0.014	0.000	0.000	0.000
68	A	62	GLY	0	0.021	0.018	24.546	0.002	0.002	0.000	0.000	0.000
69	A	63	ALA	0	-0.087	-0.035	27.334	0.003	0.003	0.000	0.000	0.000
70	A	64	ARG	1	0.928	0.960	29.244	0.031	0.031	0.000	0.000	0.000
71	A	65	LYS	1	0.978	0.997	31.127	0.016	0.016	0.000	0.000	0.000
72	A	66	TRP	0	-0.025	-0.034	34.026	0.000	0.000	0.000	0.000	0.000
73	A	67	THR	0	0.042	0.020	37.733	-0.001	-0.001	0.000	0.000	0.000
74	A	68	ASN	0	-0.065	-0.026	40.924	0.001	0.001	0.000	0.000	0.000
75	A	69	PRO	0	0.007	0.002	43.840	0.001	0.001	0.000	0.000	0.000
76	A	70	GLU	-1	-0.895	-0.944	47.394	-0.017	-0.017	0.000	0.000	0.000
77	A	71	GLY	0	-0.027	-0.006	46.001	0.001	0.001	0.000	0.000	0.000
78	A	72	GLU	-1	-0.958	-0.980	41.601	-0.022	-0.022	0.000	0.000	0.000
79	A	73	GLU	-1	-0.871	-0.934	36.175	-0.018	-0.018	0.000	0.000	0.000
80	A	74	MET	0	-0.063	-0.023	37.671	-0.003	-0.003	0.000	0.000	0.000
81	A	75	ILE	0	-0.017	-0.007	31.225	0.001	0.001	0.000	0.000	0.000
82	A	76	LEU	0	-0.036	-0.020	34.287	-0.002	-0.002	0.000	0.000	0.000
83	A	77	HIS	0	0.005	-0.017	28.231	-0.003	-0.003	0.000	0.000	0.000
84	A	78	ARG	1	0.852	0.900	30.388	0.080	0.080	0.000	0.000	0.000
85	A	79	GLY	0	0.043	0.034	34.405	0.001	0.001	0.000	0.000	0.000
86	A	80	HIS	0	-0.067	-0.034	36.084	0.000	0.000	0.000	0.000	0.000
87	A	81	ALA	0	0.044	0.019	36.629	0.000	0.000	0.000	0.000	0.000
88	A	82	TYR	0	-0.052	-0.023	33.908	-0.001	-0.001	0.000	0.000	0.000
89	A	83	ARG	1	1.019	1.012	36.649	0.032	0.032	0.000	0.000	0.000
90	A	84	ARG	1	0.759	0.831	33.063	0.020	0.020	0.000	0.000	0.000
91	A	85	ARG	1	0.886	0.938	35.759	0.039	0.039	0.000	0.000	0.000
92	A	86	GLU	-1	-0.794	-0.880	35.414	-0.021	-0.021	0.000	0.000	0.000
93	A	87	LEU	0	-0.064	-0.042	34.319	-0.001	-0.001	0.000	0.000	0.000
94	A	88	GLU	-1	-0.837	-0.900	35.504	-0.020	-0.020	0.000	0.000	0.000
95	A	89	ALA	0	-0.076	-0.041	35.701	-0.002	-0.002	0.000	0.000	0.000
96	A	99	ALA	0	0.001	0.002	32.010	-0.001	-0.001	0.000	0.000	0.000
97	A	100	ALA	0	-0.052	-0.044	30.869	-0.004	-0.004	0.000	0.000	0.000
98	A	101	VAL	0	0.019	0.028	30.733	0.003	0.003	0.000	0.000	0.000
99	A	102	LYS	1	0.889	0.953	30.891	0.048	0.048	0.000	0.000	0.000
100	A	103	TYR	0	0.051	0.012	30.672	0.004	0.004	0.000	0.000	0.000
101	A	104	SER	0	-0.047	-0.032	33.205	-0.004	-0.004	0.000	0.000	0.000
102	A	105	ARG	1	0.893	0.951	35.605	0.054	0.054	0.000	0.000	0.000
103	A	106	GLY	0	0.017	0.006	39.081	-0.002	-0.002	0.000	0.000	0.000
104	A	107	ALA	0	0.000	0.010	40.976	-0.001	-0.001	0.000	0.000	0.000
105	A	108	LYS	1	0.845	0.918	39.800	0.049	0.049	0.000	0.000	0.000
106	A	109	ASN	0	0.009	0.003	44.378	-0.001	-0.001	0.000	0.000	0.000
107	A	110	THR	0	0.000	-0.005	42.994	-0.001	-0.001	0.000	0.000	0.000
108	A	111	ASP	-1	-0.802	-0.905	38.775	-0.052	-0.052	0.000	0.000	0.000
109	A	112	PRO	0	-0.044	0.009	38.299	0.002	0.002	0.000	0.000	0.000
110	A	113	GLU	-1	-0.938	-0.967	36.323	-0.060	-0.060	0.000	0.000	0.000
111	A	124	GLU	-1	-0.913	-0.949	42.550	-0.035	-0.035	0.000	0.000	0.000
112	A	125	TYR	0	-0.047	-0.044	38.931	0.002	0.002	0.000	0.000	0.000
113	A	126	VAL	0	0.088	0.052	34.701	-0.002	-0.002	0.000	0.000	0.000
114	A	127	THR	0	-0.107	-0.078	31.429	0.003	0.003	0.000	0.000	0.000
115	A	128	LEU	0	0.015	0.025	29.334	-0.004	-0.004	0.000	0.000	0.000
116	A	129	ALA	0	0.005	-0.011	27.102	-0.008	-0.008	0.000	0.000	0.000
117	A	130	ILE	0	-0.040	-0.020	27.453	0.009	0.009	0.000	0.000	0.000
118	A	131	PHE	0	0.001	0.011	24.771	-0.007	-0.007	0.000	0.000	0.000
119	A	132	ARG	1	0.970	0.970	26.055	0.070	0.070	0.000	0.000	0.000
120	A	133	GLY	0	0.030	0.030	25.332	-0.007	-0.007	0.000	0.000	0.000
121	A	134	GLY	0	0.006	0.007	21.690	-0.001	-0.001	0.000	0.000	0.000
122	A	135	LYS	1	0.988	0.997	14.560	0.075	0.075	0.000	0.000	0.000
123	A	136	ARG	1	0.828	0.911	19.231	-0.020	-0.020	0.000	0.000	0.000
124	A	137	GLN	0	-0.063	-0.029	13.814	-0.037	-0.037	0.000	0.000	0.000
125	A	138	GLU	-1	-0.775	-0.898	16.275	0.021	0.021	0.000	0.000	0.000
126	A	139	ARG	1	0.892	0.949	12.363	0.178	0.178	0.000	0.000	0.000
127	A	140	TYR	0	-0.030	-0.024	16.111	-0.022	-0.022	0.000	0.000	0.000
128	A	141	ALA	0	0.051	0.046	19.093	-0.002	-0.002	0.000	0.000	0.000
129	A	142	VAL	0	-0.019	-0.002	21.023	-0.001	-0.001	0.000	0.000	0.000
130	A	143	PRO	0	-0.002	0.014	20.698	0.006	0.006	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-5:GLY)