FMO DATABASE

FMODB ID: QY76Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1279335.176009
FMO2-HF: Nuclear repulsion	1224839.036878
FMO2-HF: Total energy	-54496.139131
FMO2-MP2: Total energy	-54658.762548

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.
-14.323	-4.241	7.596	-4.578	-13.101	-0.004

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 : -0.030 / q_NPA : -0.031

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	-0.755	-0.864	3.720	-3.069	-1.558	0.012	-0.717	-0.806	0.000
4	A	39	ALA	0	-0.033	-0.017	6.387	0.278	0.278	0.000	0.000	0.000	0.000
5	A	40	ILE	0	0.007	-0.002	2.476	-0.522	0.047	0.879	-0.359	-1.089	-0.001
6	A	41	THR	0	0.029	0.022	3.610	-0.278	0.070	0.004	-0.076	-0.277	0.000
7	A	42	ARG	1	0.793	0.890	5.666	1.200	1.200	0.000	0.000	0.000	0.000
8	A	43	TYR	0	-0.041	-0.013	8.296	0.152	0.152	0.000	0.000	0.000	0.000
9	A	44	PHE	0	0.031	-0.002	6.734	0.113	0.113	0.000	0.000	0.000	0.000
10	A	45	ALA	0	0.011	0.011	9.471	0.059	0.059	0.000	0.000	0.000	0.000
11	A	46	SER	0	0.010	-0.004	11.304	0.122	0.122	0.000	0.000	0.000	0.000
12	A	47	GLN	0	-0.013	-0.006	12.702	0.114	0.114	0.000	0.000	0.000	0.000
13	A	48	TYR	0	-0.013	0.004	13.144	0.061	0.061	0.000	0.000	0.000	0.000
14	A	49	VAL	0	0.028	0.002	15.043	0.046	0.046	0.000	0.000	0.000	0.000
15	A	50	ARG	1	0.891	0.942	15.888	0.334	0.334	0.000	0.000	0.000	0.000
16	A	51	ALA	0	-0.007	0.016	18.135	0.031	0.031	0.000	0.000	0.000	0.000
17	A	52	ARG	1	0.811	0.886	18.333	0.469	0.469	0.000	0.000	0.000	0.000
18	A	53	GLU	-1	-0.804	-0.877	20.878	-0.309	-0.309	0.000	0.000	0.000	0.000
19	A	54	GLY	0	-0.012	0.010	22.623	0.021	0.021	0.000	0.000	0.000	0.000
20	A	55	PHE	0	-0.016	-0.020	24.487	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	56	GLN	0	0.049	0.016	27.207	0.020	0.020	0.000	0.000	0.000	0.000
22	A	57	ALA	0	0.035	0.026	28.649	-0.004	-0.004	0.000	0.000	0.000	0.000
23	A	58	SER	0	-0.025	-0.014	29.928	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	59	GLU	-1	-0.811	-0.898	24.752	-0.128	-0.128	0.000	0.000	0.000	0.000
25	A	60	ALA	0	-0.027	0.007	24.753	-0.020	-0.020	0.000	0.000	0.000	0.000
26	A	61	GLU	-1	-0.893	-0.948	23.684	-0.201	-0.201	0.000	0.000	0.000	0.000
27	A	62	ASN	0	-0.034	-0.043	21.721	-0.018	-0.018	0.000	0.000	0.000	0.000
28	A	63	ASN	0	0.001	-0.010	20.350	-0.041	-0.041	0.000	0.000	0.000	0.000
29	A	64	PHE	0	0.008	0.013	20.057	-0.044	-0.044	0.000	0.000	0.000	0.000
30	A	65	ARG	1	0.926	0.961	17.247	0.161	0.161	0.000	0.000	0.000	0.000
31	A	66	LEU	0	-0.022	-0.002	15.044	-0.048	-0.048	0.000	0.000	0.000	0.000
32	A	67	VAL	0	0.028	0.003	15.287	-0.080	-0.080	0.000	0.000	0.000	0.000
33	A	68	SER	0	-0.041	-0.015	15.926	-0.071	-0.071	0.000	0.000	0.000	0.000
34	A	69	LEU	0	-0.008	-0.007	13.197	-0.067	-0.067	0.000	0.000	0.000	0.000
35	A	70	LEU	0	-0.057	-0.013	10.103	-0.136	-0.136	0.000	0.000	0.000	0.000
36	A	71	SER	0	0.004	-0.002	12.054	-0.132	-0.132	0.000	0.000	0.000	0.000
37	A	72	SER	0	0.021	0.025	13.477	0.038	0.038	0.000	0.000	0.000	0.000
38	A	73	PRO	0	0.071	0.026	14.347	0.070	0.070	0.000	0.000	0.000	0.000
39	A	74	LYS	1	0.829	0.904	16.399	0.650	0.650	0.000	0.000	0.000	0.000
40	A	75	GLU	-1	-0.760	-0.849	16.505	-0.429	-0.429	0.000	0.000	0.000	0.000
41	A	76	GLN	0	-0.044	-0.033	15.225	0.096	0.096	0.000	0.000	0.000	0.000
42	A	77	ASN	0	-0.011	0.003	19.208	0.055	0.055	0.000	0.000	0.000	0.000
43	A	78	ARG	1	0.788	0.867	19.313	0.483	0.483	0.000	0.000	0.000	0.000
44	A	79	PHE	0	0.031	0.023	20.531	0.024	0.024	0.000	0.000	0.000	0.000
45	A	80	GLY	0	0.053	0.026	22.549	0.025	0.025	0.000	0.000	0.000	0.000
46	A	81	LYS	1	0.858	0.917	24.725	0.269	0.269	0.000	0.000	0.000	0.000
47	A	82	TRP	0	-0.024	0.002	23.597	0.006	0.006	0.000	0.000	0.000	0.000
48	A	83	TYR	0	0.074	0.032	25.139	0.016	0.016	0.000	0.000	0.000	0.000
49	A	84	ALA	0	-0.004	0.028	27.254	0.018	0.018	0.000	0.000	0.000	0.000
50	A	85	GLY	0	0.074	0.029	30.009	0.003	0.003	0.000	0.000	0.000	0.000
51	A	86	ASN	0	-0.031	-0.011	33.090	0.005	0.005	0.000	0.000	0.000	0.000
52	A	87	ASN	0	-0.031	-0.017	30.026	0.014	0.014	0.000	0.000	0.000	0.000
53	A	88	PRO	0	0.009	0.009	33.430	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	89	GLU	-1	-0.902	-0.961	31.147	-0.173	-0.173	0.000	0.000	0.000	0.000
55	A	90	SER	0	-0.070	-0.034	29.290	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	91	PRO	0	0.028	0.001	26.057	0.013	0.013	0.000	0.000	0.000	0.000
57	A	92	GLN	0	-0.056	-0.032	29.340	0.019	0.019	0.000	0.000	0.000	0.000
58	A	93	ASN	0	-0.069	-0.044	31.489	0.018	0.018	0.000	0.000	0.000	0.000
59	A	94	ILE	0	-0.007	0.000	29.866	0.009	0.009	0.000	0.000	0.000	0.000
60	A	95	TYR	0	-0.017	-0.020	28.124	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	96	HIS	0	0.022	0.026	33.051	0.010	0.010	0.000	0.000	0.000	0.000
62	A	97	ASN	0	-0.107	-0.069	35.443	0.007	0.007	0.000	0.000	0.000	0.000
63	A	98	MET	0	-0.008	0.017	33.884	0.003	0.003	0.000	0.000	0.000	0.000
64	A	99	ILE	0	-0.024	-0.006	29.516	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	100	ALA	0	0.008	0.012	28.220	0.002	0.002	0.000	0.000	0.000	0.000
66	A	101	THR	0	-0.005	-0.002	25.541	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	102	VAL	0	0.000	-0.002	20.347	0.000	0.000	0.000	0.000	0.000	0.000
68	A	103	THR	0	-0.007	0.001	22.297	0.000	0.000	0.000	0.000	0.000	0.000
69	A	104	ILE	0	-0.033	-0.030	16.380	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	105	LYS	1	0.758	0.890	19.776	0.270	0.270	0.000	0.000	0.000	0.000
71	A	106	SER	0	0.018	-0.009	17.911	0.023	0.023	0.000	0.000	0.000	0.000
72	A	107	ILE	0	-0.021	-0.007	11.816	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	108	SER	0	-0.001	-0.006	14.331	0.001	0.001	0.000	0.000	0.000	0.000
74	A	109	PHE	0	-0.011	-0.003	7.739	-0.075	-0.075	0.000	0.000	0.000	0.000
75	A	110	ILE	0	-0.009	0.001	12.549	0.099	0.099	0.000	0.000	0.000	0.000
76	A	111	SER	0	0.001	-0.008	12.772	0.111	0.111	0.000	0.000	0.000	0.000
77	A	112	LYS	1	0.845	0.920	8.988	0.511	0.511	0.000	0.000	0.000	0.000
78	A	113	ASP	-1	-0.794	-0.889	8.080	-1.129	-1.129	0.000	0.000	0.000	0.000
79	A	114	LEU	0	-0.018	-0.021	10.252	0.054	0.054	0.000	0.000	0.000	0.000
80	A	115	ILE	0	-0.009	0.013	9.021	0.048	0.048	0.000	0.000	0.000	0.000
81	A	116	GLN	0	0.034	0.027	13.145	0.069	0.069	0.000	0.000	0.000	0.000
82	A	117	VAL	0	0.005	-0.017	14.412	-0.021	-0.021	0.000	0.000	0.000	0.000
83	A	118	ARG	1	0.866	0.927	17.028	0.322	0.322	0.000	0.000	0.000	0.000
84	A	119	TYR	0	0.000	-0.025	20.124	0.004	0.004	0.000	0.000	0.000	0.000
85	A	120	TYR	0	0.011	-0.001	22.092	0.008	0.008	0.000	0.000	0.000	0.000
86	A	121	LYS	1	0.884	0.959	24.852	0.248	0.248	0.000	0.000	0.000	0.000
87	A	122	THR	0	0.034	0.008	27.054	0.004	0.004	0.000	0.000	0.000	0.000
88	A	123	VAL	0	-0.040	-0.017	29.706	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	124	ARG	1	0.846	0.920	32.167	0.096	0.096	0.000	0.000	0.000	0.000
90	A	125	ASP	-1	-0.836	-0.924	34.886	-0.097	-0.097	0.000	0.000	0.000	0.000
91	A	126	PHE	0	0.032	0.004	37.842	0.002	0.002	0.000	0.000	0.000	0.000
92	A	127	ASN	0	-0.091	-0.042	40.265	0.009	0.009	0.000	0.000	0.000	0.000
93	A	128	GLU	-1	-0.848	-0.908	39.342	-0.085	-0.085	0.000	0.000	0.000	0.000
94	A	129	LYS	1	0.934	0.952	38.156	0.109	0.109	0.000	0.000	0.000	0.000
95	A	130	GLU	-1	-0.881	-0.932	33.904	-0.122	-0.122	0.000	0.000	0.000	0.000
96	A	131	ASN	0	-0.092	-0.045	34.060	0.009	0.009	0.000	0.000	0.000	0.000
97	A	132	ILE	0	0.024	0.017	29.752	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	133	SER	0	-0.026	-0.002	29.915	0.001	0.001	0.000	0.000	0.000	0.000
99	A	134	HIS	0	0.058	0.028	26.920	-0.025	-0.025	0.000	0.000	0.000	0.000
100	A	135	TRP	0	0.005	-0.004	24.308	0.005	0.005	0.000	0.000	0.000	0.000
101	A	136	ILE	0	-0.035	-0.016	20.836	-0.016	-0.016	0.000	0.000	0.000	0.000
102	A	137	SER	0	0.033	0.004	18.425	0.023	0.023	0.000	0.000	0.000	0.000
103	A	138	ILE	0	-0.052	-0.018	17.222	-0.034	-0.034	0.000	0.000	0.000	0.000
104	A	139	LEU	0	-0.002	0.000	12.398	0.016	0.016	0.000	0.000	0.000	0.000
105	A	140	ASN	0	0.009	0.027	13.305	-0.084	-0.084	0.000	0.000	0.000	0.000
106	A	141	PHE	0	-0.020	-0.016	5.485	0.099	0.099	0.000	0.000	0.000	0.000
107	A	142	SER	0	0.007	0.006	6.617	0.063	0.063	0.000	0.000	0.000	0.000
108	A	143	TYR	0	0.023	-0.017	2.358	-4.166	-0.981	4.790	-1.806	-6.169	-0.016
109	A	144	VAL	0	-0.024	-0.008	4.364	0.408	0.523	-0.001	-0.010	-0.104	0.000
110	A	145	ASN	0	-0.004	0.001	3.819	-1.966	-1.723	0.000	-0.064	-0.180	0.000
111	A	146	ALA	0	0.025	0.009	6.036	0.513	0.513	0.000	0.000	0.000	0.000
112	A	147	HIS	0	-0.003	-0.006	8.823	0.075	0.075	0.000	0.000	0.000	0.000
113	A	148	ILE	0	-0.007	-0.004	7.648	-0.081	-0.081	0.000	0.000	0.000	0.000
114	A	149	SER	0	-0.013	-0.032	11.357	0.122	0.122	0.000	0.000	0.000	0.000
115	A	150	THR	0	0.060	0.000	13.001	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	151	SER	0	0.062	0.035	14.037	0.042	0.042	0.000	0.000	0.000	0.000
117	A	152	ASP	-1	-0.787	-0.859	13.593	-0.216	-0.216	0.000	0.000	0.000	0.000
118	A	153	ARG	1	0.897	0.964	5.710	0.262	0.262	0.000	0.000	0.000	0.000
119	A	154	LEU	0	-0.037	-0.013	10.891	0.116	0.116	0.000	0.000	0.000	0.000
120	A	155	ILE	0	-0.028	-0.005	12.758	-0.011	-0.011	0.000	0.000	0.000	0.000
121	A	156	ASN	0	-0.043	-0.027	8.167	-0.097	-0.097	0.000	0.000	0.000	0.000
122	A	157	PRO	0	0.017	0.012	7.317	-0.171	-0.171	0.000	0.000	0.000	0.000
123	A	158	LEU	0	-0.026	-0.022	2.755	-3.656	-0.414	1.885	-1.186	-3.940	0.015
124	A	159	GLY	0	0.038	0.035	3.411	-4.526	-3.657	0.027	-0.360	-0.536	-0.002
125	A	160	PHE	0	-0.013	-0.003	5.857	-0.534	-0.534	0.000	0.000	0.000	0.000
126	A	161	GLN	0	-0.032	-0.022	6.725	0.534	0.534	0.000	0.000	0.000	0.000
127	A	162	VAL	0	0.022	0.012	9.526	-0.124	-0.124	0.000	0.000	0.000	0.000
128	A	163	SER	0	-0.085	-0.064	12.366	0.162	0.162	0.000	0.000	0.000	0.000
129	A	164	GLU	-1	-0.777	-0.884	14.610	-0.407	-0.407	0.000	0.000	0.000	0.000
130	A	165	TYR	0	-0.034	-0.052	16.058	-0.089	-0.089	0.000	0.000	0.000	0.000
131	A	166	ARG	1	0.800	0.877	18.430	0.360	0.360	0.000	0.000	0.000	0.000
132	A	167	SER	0	0.040	0.028	20.920	-0.025	-0.025	0.000	0.000	0.000	0.000
133	A	168	ASP	-1	-0.792	-0.851	23.155	-0.277	-0.277	0.000	0.000	0.000	0.000
134	A	169	PRO	0	0.046	0.016	25.726	-0.009	-0.009	0.000	0.000	0.000	0.000
135	A	170	GLU	-1	-0.802	-0.869	25.173	-0.252	-0.252	0.000	0.000	0.000	0.000

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