FMO DATABASE

FMODB ID: R9N28

Calculation Name: 4KZ1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4KZ1

Chain ID: A

ChEMBL ID:

UniProt ID: C6AER9

Base Structure: X-ray

Registration Date: 2023-06-21

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	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1278463.999899
FMO2-HF: Nuclear repulsion	1223968.412907
FMO2-HF: Total energy	-54495.586992
FMO2-MP2: Total energy	-54658.209101

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:36:TYR)

Summations of interaction energy for fragment #1(A:36:TYR)

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.
-12.435	-4.398	9.432	-4.493	-12.977	-0.006

Interaction energy analysis for fragmet #1(A:36:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.027 / 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	38	GLU	-1	-0.870	-0.938	3.673	-3.387	-1.917	0.012	-0.695	-0.788	0.000
4	A	39	ALA	0	-0.012	-0.008	6.328	0.380	0.380	0.000	0.000	0.000	0.000
5	A	40	ILE	0	0.024	0.006	2.453	-0.380	0.136	0.824	-0.324	-1.016	-0.001
6	A	41	THR	0	0.062	0.061	3.384	0.007	0.368	0.006	-0.074	-0.293	0.000
7	A	42	ARG	1	0.833	0.924	5.612	1.373	1.373	0.000	0.000	0.000	0.000
8	A	43	TYR	0	-0.035	0.002	8.270	0.167	0.167	0.000	0.000	0.000	0.000
9	A	44	PHE	0	0.039	0.002	6.545	0.145	0.145	0.000	0.000	0.000	0.000
10	A	45	ALA	0	0.015	0.013	9.426	0.077	0.077	0.000	0.000	0.000	0.000
11	A	46	SER	0	-0.009	-0.009	11.274	0.130	0.130	0.000	0.000	0.000	0.000
12	A	47	GLN	0	-0.011	-0.022	12.736	0.126	0.126	0.000	0.000	0.000	0.000
13	A	48	TYR	0	-0.037	0.003	13.136	0.059	0.059	0.000	0.000	0.000	0.000
14	A	49	VAL	0	0.033	0.006	15.015	0.048	0.048	0.000	0.000	0.000	0.000
15	A	50	ARG	1	0.921	0.954	16.626	0.337	0.337	0.000	0.000	0.000	0.000
16	A	51	ALA	0	-0.019	0.007	18.152	0.034	0.034	0.000	0.000	0.000	0.000
17	A	52	ARG	1	0.849	0.923	18.347	0.455	0.455	0.000	0.000	0.000	0.000
18	A	53	GLU	-1	-0.827	-0.876	20.884	-0.321	-0.321	0.000	0.000	0.000	0.000
19	A	54	GLY	0	-0.015	0.005	22.591	0.020	0.020	0.000	0.000	0.000	0.000
20	A	55	PHE	0	-0.037	-0.026	24.444	0.000	0.000	0.000	0.000	0.000	0.000
21	A	56	GLN	0	0.052	0.018	27.164	0.019	0.019	0.000	0.000	0.000	0.000
22	A	57	ALA	0	0.026	0.022	28.599	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	58	SER	0	-0.039	-0.030	29.546	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	59	GLU	-1	-0.830	-0.909	24.405	-0.112	-0.112	0.000	0.000	0.000	0.000
25	A	60	ALA	0	-0.032	0.000	24.939	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	61	GLU	-1	-0.891	-0.941	23.946	-0.162	-0.162	0.000	0.000	0.000	0.000
27	A	62	ASN	0	-0.007	-0.022	21.950	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	63	ASN	0	0.000	-0.007	20.547	-0.026	-0.026	0.000	0.000	0.000	0.000
29	A	64	PHE	0	0.009	0.015	20.203	-0.041	-0.041	0.000	0.000	0.000	0.000
30	A	65	ARG	1	0.935	0.958	17.820	0.098	0.098	0.000	0.000	0.000	0.000
31	A	66	LEU	0	-0.027	-0.001	14.944	-0.038	-0.038	0.000	0.000	0.000	0.000
32	A	67	VAL	0	0.037	0.007	15.436	-0.068	-0.068	0.000	0.000	0.000	0.000
33	A	68	SER	0	-0.041	-0.017	16.011	-0.066	-0.066	0.000	0.000	0.000	0.000
34	A	69	LEU	0	-0.005	-0.004	13.359	-0.062	-0.062	0.000	0.000	0.000	0.000
35	A	70	LEU	0	-0.063	-0.015	10.604	-0.099	-0.099	0.000	0.000	0.000	0.000
36	A	71	SER	0	-0.015	-0.012	12.086	-0.142	-0.142	0.000	0.000	0.000	0.000
37	A	72	SER	0	0.012	0.020	13.494	0.043	0.043	0.000	0.000	0.000	0.000
38	A	73	PRO	0	0.084	0.033	14.318	0.063	0.063	0.000	0.000	0.000	0.000
39	A	74	LYS	1	0.829	0.915	16.475	0.604	0.604	0.000	0.000	0.000	0.000
40	A	75	GLU	-1	-0.786	-0.896	16.505	-0.437	-0.437	0.000	0.000	0.000	0.000
41	A	76	GLN	0	-0.018	-0.015	15.482	0.081	0.081	0.000	0.000	0.000	0.000
42	A	77	ASN	0	-0.019	0.000	19.233	0.045	0.045	0.000	0.000	0.000	0.000
43	A	78	ARG	1	0.873	0.927	19.256	0.455	0.455	0.000	0.000	0.000	0.000
44	A	79	PHE	0	0.026	0.022	20.551	0.019	0.019	0.000	0.000	0.000	0.000
45	A	80	GLY	0	0.061	0.029	22.562	0.023	0.023	0.000	0.000	0.000	0.000
46	A	81	LYS	1	0.866	0.925	24.771	0.250	0.250	0.000	0.000	0.000	0.000
47	A	82	TRP	0	-0.030	-0.012	24.082	0.009	0.009	0.000	0.000	0.000	0.000
48	A	83	TYR	0	0.084	0.025	25.223	0.017	0.017	0.000	0.000	0.000	0.000
49	A	84	ALA	0	0.002	0.014	27.311	0.017	0.017	0.000	0.000	0.000	0.000
50	A	85	GLY	0	0.064	0.025	30.074	0.001	0.001	0.000	0.000	0.000	0.000
51	A	86	ASN	0	-0.014	0.002	33.173	0.006	0.006	0.000	0.000	0.000	0.000
52	A	87	ASN	0	-0.025	-0.001	30.134	0.012	0.012	0.000	0.000	0.000	0.000
53	A	88	PRO	0	0.006	0.011	33.442	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	89	GLU	-1	-0.902	-0.965	31.130	-0.175	-0.175	0.000	0.000	0.000	0.000
55	A	90	SER	0	-0.062	-0.011	29.302	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	91	PRO	0	0.033	-0.001	26.085	0.012	0.012	0.000	0.000	0.000	0.000
57	A	92	GLN	0	-0.052	-0.028	29.349	0.018	0.018	0.000	0.000	0.000	0.000
58	A	93	ASN	0	-0.086	-0.061	31.512	0.017	0.017	0.000	0.000	0.000	0.000
59	A	94	ILE	0	-0.006	0.005	30.123	0.008	0.008	0.000	0.000	0.000	0.000
60	A	95	TYR	0	-0.005	-0.012	28.283	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	96	HIS	0	0.029	0.023	33.018	0.010	0.010	0.000	0.000	0.000	0.000
62	A	97	ASN	0	-0.113	-0.068	35.409	0.007	0.007	0.000	0.000	0.000	0.000
63	A	98	MET	0	0.003	0.018	33.985	0.002	0.002	0.000	0.000	0.000	0.000
64	A	99	ILE	0	-0.016	-0.001	29.415	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	100	ALA	0	0.002	0.008	28.132	0.001	0.001	0.000	0.000	0.000	0.000
66	A	101	THR	0	-0.043	-0.018	25.477	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	102	VAL	0	0.038	0.016	20.354	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	103	THR	0	-0.016	-0.001	22.224	0.004	0.004	0.000	0.000	0.000	0.000
69	A	104	ILE	0	-0.025	-0.026	16.382	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	105	LYS	1	0.864	0.945	19.715	0.299	0.299	0.000	0.000	0.000	0.000
71	A	106	SER	0	0.004	-0.002	17.883	0.024	0.024	0.000	0.000	0.000	0.000
72	A	107	ILE	0	-0.009	0.007	11.713	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	108	SER	0	0.006	0.006	14.298	-0.018	-0.018	0.000	0.000	0.000	0.000
74	A	109	PHE	0	0.021	0.011	7.800	-0.027	-0.027	0.000	0.000	0.000	0.000
75	A	110	ILE	0	-0.009	0.003	12.543	0.103	0.103	0.000	0.000	0.000	0.000
76	A	111	SER	0	-0.004	-0.016	12.777	0.094	0.094	0.000	0.000	0.000	0.000
77	A	112	LYS	1	0.834	0.917	8.937	0.599	0.599	0.000	0.000	0.000	0.000
78	A	113	ASP	-1	-0.784	-0.883	8.120	-1.257	-1.257	0.000	0.000	0.000	0.000
79	A	114	LEU	0	-0.005	-0.007	10.333	0.084	0.084	0.000	0.000	0.000	0.000
80	A	115	ILE	0	-0.007	0.012	8.842	0.036	0.036	0.000	0.000	0.000	0.000
81	A	116	GLN	0	0.021	0.011	13.171	0.076	0.076	0.000	0.000	0.000	0.000
82	A	117	VAL	0	-0.008	-0.017	14.406	-0.030	-0.030	0.000	0.000	0.000	0.000
83	A	118	ARG	1	0.927	0.973	17.012	0.388	0.388	0.000	0.000	0.000	0.000
84	A	119	TYR	0	-0.027	-0.043	20.084	0.002	0.002	0.000	0.000	0.000	0.000
85	A	120	TYR	0	0.007	0.000	22.052	0.008	0.008	0.000	0.000	0.000	0.000
86	A	121	LYS	1	0.915	0.982	24.924	0.247	0.247	0.000	0.000	0.000	0.000
87	A	122	THR	0	0.028	0.008	27.008	0.004	0.004	0.000	0.000	0.000	0.000
88	A	123	VAL	0	-0.031	-0.016	29.649	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	124	ARG	1	0.840	0.913	32.114	0.100	0.100	0.000	0.000	0.000	0.000
90	A	125	ASP	-1	-0.848	-0.931	34.826	-0.101	-0.101	0.000	0.000	0.000	0.000
91	A	126	PHE	0	0.037	0.005	37.786	0.001	0.001	0.000	0.000	0.000	0.000
92	A	127	ASN	0	-0.088	-0.038	40.205	0.009	0.009	0.000	0.000	0.000	0.000
93	A	128	GLU	-1	-0.837	-0.897	39.167	-0.092	-0.092	0.000	0.000	0.000	0.000
94	A	129	LYS	1	0.944	0.963	38.283	0.115	0.115	0.000	0.000	0.000	0.000
95	A	130	GLU	-1	-0.893	-0.936	33.803	-0.131	-0.131	0.000	0.000	0.000	0.000
96	A	131	ASN	0	-0.098	-0.057	34.194	0.005	0.005	0.000	0.000	0.000	0.000
97	A	132	ILE	0	0.031	0.024	29.760	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	133	SER	0	-0.021	0.011	29.877	0.000	0.000	0.000	0.000	0.000	0.000
99	A	134	HIS	0	0.052	0.008	26.891	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	135	TRP	0	-0.003	-0.012	24.252	0.008	0.008	0.000	0.000	0.000	0.000
101	A	136	ILE	0	-0.005	-0.001	20.793	-0.024	-0.024	0.000	0.000	0.000	0.000
102	A	137	SER	0	0.007	-0.007	18.432	0.028	0.028	0.000	0.000	0.000	0.000
103	A	138	ILE	0	-0.036	-0.010	17.264	-0.041	-0.041	0.000	0.000	0.000	0.000
104	A	139	LEU	0	-0.018	-0.013	12.315	0.028	0.028	0.000	0.000	0.000	0.000
105	A	140	ASN	0	0.000	0.008	13.259	-0.157	-0.157	0.000	0.000	0.000	0.000
106	A	141	PHE	0	-0.018	-0.010	5.364	0.094	0.094	0.000	0.000	0.000	0.000
107	A	142	SER	0	-0.001	0.001	6.569	0.010	0.010	0.000	0.000	0.000	0.000
108	A	143	TYR	0	0.012	-0.043	2.323	-3.544	-1.662	7.372	-2.121	-7.133	-0.015
109	A	144	VAL	0	-0.034	-0.011	4.229	0.225	0.358	-0.001	-0.015	-0.117	0.000
110	A	145	ASN	0	0.005	0.004	3.545	-2.189	-1.842	0.002	-0.114	-0.235	-0.001
111	A	146	ALA	0	0.025	0.009	5.829	0.443	0.443	0.000	0.000	0.000	0.000
112	A	147	HIS	0	-0.010	-0.007	8.860	0.144	0.144	0.000	0.000	0.000	0.000
113	A	148	ILE	0	0.000	-0.004	7.685	-0.083	-0.083	0.000	0.000	0.000	0.000
114	A	149	SER	0	0.016	0.018	11.568	0.117	0.117	0.000	0.000	0.000	0.000
115	A	150	THR	0	0.057	0.001	13.341	0.012	0.012	0.000	0.000	0.000	0.000
116	A	151	SER	0	0.023	0.011	14.459	0.031	0.031	0.000	0.000	0.000	0.000
117	A	152	ASP	-1	-0.783	-0.880	13.575	-0.145	-0.145	0.000	0.000	0.000	0.000
118	A	153	ARG	1	0.873	0.940	5.860	-0.254	-0.254	0.000	0.000	0.000	0.000
119	A	154	LEU	0	-0.039	-0.016	11.274	0.110	0.110	0.000	0.000	0.000	0.000
120	A	155	ILE	0	-0.032	0.000	13.178	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	156	ASN	0	-0.046	-0.040	8.499	-0.029	-0.029	0.000	0.000	0.000	0.000
122	A	157	PRO	0	0.016	0.021	7.510	-0.083	-0.083	0.000	0.000	0.000	0.000
123	A	158	LEU	0	-0.013	-0.020	2.992	-3.008	-0.263	1.204	-0.954	-2.995	0.012
124	A	159	GLY	0	0.040	0.039	3.561	-3.321	-2.738	0.013	-0.196	-0.400	-0.001
125	A	160	PHE	0	-0.003	0.004	5.825	-0.639	-0.639	0.000	0.000	0.000	0.000
126	A	161	GLN	0	-0.041	-0.023	6.794	0.507	0.507	0.000	0.000	0.000	0.000
127	A	162	VAL	0	0.029	0.015	9.503	-0.148	-0.148	0.000	0.000	0.000	0.000
128	A	163	SER	0	-0.066	-0.050	12.360	0.142	0.142	0.000	0.000	0.000	0.000
129	A	164	GLU	-1	-0.841	-0.929	14.487	-0.415	-0.415	0.000	0.000	0.000	0.000
130	A	165	TYR	0	-0.062	-0.087	16.016	-0.092	-0.092	0.000	0.000	0.000	0.000
131	A	166	ARG	1	0.817	0.911	18.391	0.383	0.383	0.000	0.000	0.000	0.000
132	A	167	SER	0	0.057	0.042	20.940	-0.022	-0.022	0.000	0.000	0.000	0.000
133	A	168	ASP	-1	-0.816	-0.885	23.166	-0.290	-0.290	0.000	0.000	0.000	0.000
134	A	169	PRO	0	0.038	0.013	25.726	-0.011	-0.011	0.000	0.000	0.000	0.000
135	A	170	GLU	-1	-0.943	-0.975	25.234	-0.289	-0.289	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:36:TYR)