FMO DATABASE

FMODB ID: K9753

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	OptAll
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	-1282861.827836
FMO2-HF: Nuclear repulsion	1228365.481661
FMO2-HF: Total energy	-54496.346175
FMO2-MP2: Total energy	-54659.008818

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.
-18.069	-6.889	9.27	-5.276	-15.174	-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 : -0.015 / q_NPA : -0.023

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	-0.768	-0.854	3.799	-2.679	-1.228	0.000	-0.700	-0.752	0.001
4	A	39	ALA	0	-0.038	-0.012	6.578	0.160	0.160	0.000	0.000	0.000	0.000
5	A	40	ILE	0	0.012	-0.008	2.827	-0.585	0.067	0.292	-0.167	-0.777	-0.001
6	A	41	THR	0	0.004	-0.001	3.616	-0.386	0.026	0.011	-0.103	-0.320	0.000
7	A	42	ARG	1	0.781	0.870	5.664	0.988	0.988	0.000	0.000	0.000	0.000
8	A	43	TYR	0	-0.037	-0.009	8.328	0.128	0.128	0.000	0.000	0.000	0.000
9	A	44	PHE	0	0.027	0.004	6.195	0.101	0.101	0.000	0.000	0.000	0.000
10	A	45	ALA	0	0.013	0.010	9.329	0.044	0.044	0.000	0.000	0.000	0.000
11	A	46	SER	0	0.005	0.003	11.186	0.109	0.109	0.000	0.000	0.000	0.000
12	A	47	GLN	0	-0.019	-0.011	11.672	0.106	0.106	0.000	0.000	0.000	0.000
13	A	48	TYR	0	-0.017	-0.005	12.878	0.050	0.050	0.000	0.000	0.000	0.000
14	A	49	VAL	0	0.026	0.005	14.816	0.040	0.040	0.000	0.000	0.000	0.000
15	A	50	ARG	1	0.880	0.926	15.120	0.287	0.287	0.000	0.000	0.000	0.000
16	A	51	ALA	0	0.008	0.020	17.936	0.028	0.028	0.000	0.000	0.000	0.000
17	A	52	ARG	1	0.805	0.890	18.237	0.454	0.454	0.000	0.000	0.000	0.000
18	A	53	GLU	-1	-0.775	-0.850	20.549	-0.307	-0.307	0.000	0.000	0.000	0.000
19	A	54	GLY	0	0.041	0.023	22.790	0.020	0.020	0.000	0.000	0.000	0.000
20	A	55	PHE	0	-0.008	-0.015	24.669	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	56	GLN	0	0.057	0.017	27.113	0.020	0.020	0.000	0.000	0.000	0.000
22	A	57	ALA	0	0.032	0.024	28.395	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	58	SER	0	-0.023	-0.009	29.729	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	59	GLU	-1	-0.841	-0.905	24.532	-0.110	-0.110	0.000	0.000	0.000	0.000
25	A	60	ALA	0	-0.006	0.017	24.837	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	61	GLU	-1	-0.853	-0.933	23.181	-0.215	-0.215	0.000	0.000	0.000	0.000
27	A	62	ASN	0	-0.036	-0.037	21.895	-0.026	-0.026	0.000	0.000	0.000	0.000
28	A	63	ASN	0	-0.019	-0.024	20.157	-0.036	-0.036	0.000	0.000	0.000	0.000
29	A	64	PHE	0	0.015	0.024	19.811	-0.046	-0.046	0.000	0.000	0.000	0.000
30	A	65	ARG	1	0.918	0.951	16.919	0.170	0.170	0.000	0.000	0.000	0.000
31	A	66	LEU	0	0.002	0.003	14.895	-0.050	-0.050	0.000	0.000	0.000	0.000
32	A	67	VAL	0	0.023	0.004	15.066	-0.082	-0.082	0.000	0.000	0.000	0.000
33	A	68	SER	0	-0.027	-0.010	15.750	-0.081	-0.081	0.000	0.000	0.000	0.000
34	A	69	LEU	0	-0.022	-0.010	13.025	-0.079	-0.079	0.000	0.000	0.000	0.000
35	A	70	LEU	0	-0.048	-0.003	10.026	-0.160	-0.160	0.000	0.000	0.000	0.000
36	A	71	SER	0	-0.022	-0.018	11.840	-0.129	-0.129	0.000	0.000	0.000	0.000
37	A	72	SER	0	0.018	0.010	12.996	0.035	0.035	0.000	0.000	0.000	0.000
38	A	73	PRO	0	0.043	0.005	14.044	0.079	0.079	0.000	0.000	0.000	0.000
39	A	74	LYS	1	0.835	0.905	16.267	0.714	0.714	0.000	0.000	0.000	0.000
40	A	75	GLU	-1	-0.746	-0.839	16.573	-0.422	-0.422	0.000	0.000	0.000	0.000
41	A	76	GLN	0	-0.019	-0.015	14.812	0.101	0.101	0.000	0.000	0.000	0.000
42	A	77	ASN	0	-0.012	0.006	19.115	0.061	0.061	0.000	0.000	0.000	0.000
43	A	78	ARG	1	0.771	0.850	19.230	0.497	0.497	0.000	0.000	0.000	0.000
44	A	79	PHE	0	0.023	0.017	20.228	0.027	0.027	0.000	0.000	0.000	0.000
45	A	80	GLY	0	0.042	0.020	22.317	0.028	0.028	0.000	0.000	0.000	0.000
46	A	81	LYS	1	0.853	0.911	24.410	0.287	0.287	0.000	0.000	0.000	0.000
47	A	82	TRP	0	-0.042	0.000	23.194	0.006	0.006	0.000	0.000	0.000	0.000
48	A	83	TYR	0	0.048	0.010	24.822	0.019	0.019	0.000	0.000	0.000	0.000
49	A	84	ALA	0	0.003	0.025	26.948	0.018	0.018	0.000	0.000	0.000	0.000
50	A	85	GLY	0	0.063	0.030	29.744	0.004	0.004	0.000	0.000	0.000	0.000
51	A	86	ASN	0	-0.039	-0.022	32.995	0.004	0.004	0.000	0.000	0.000	0.000
52	A	87	ASN	0	-0.025	-0.012	29.674	0.013	0.013	0.000	0.000	0.000	0.000
53	A	88	PRO	0	0.012	0.008	33.133	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	89	GLU	-1	-0.893	-0.956	30.910	-0.166	-0.166	0.000	0.000	0.000	0.000
55	A	90	SER	0	-0.026	-0.009	28.981	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	91	PRO	0	0.010	-0.008	25.609	0.014	0.014	0.000	0.000	0.000	0.000
57	A	92	GLN	0	-0.063	-0.037	28.872	0.021	0.021	0.000	0.000	0.000	0.000
58	A	93	ASN	0	-0.097	-0.055	31.150	0.018	0.018	0.000	0.000	0.000	0.000
59	A	94	ILE	0	0.007	0.000	29.239	0.009	0.009	0.000	0.000	0.000	0.000
60	A	95	TYR	0	-0.020	-0.019	27.723	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	96	HIS	0	0.022	0.024	32.838	0.010	0.010	0.000	0.000	0.000	0.000
62	A	97	ASN	0	-0.088	-0.056	35.338	0.008	0.008	0.000	0.000	0.000	0.000
63	A	98	MET	0	-0.021	0.008	33.934	0.004	0.004	0.000	0.000	0.000	0.000
64	A	99	ILE	0	-0.026	-0.006	29.269	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	100	ALA	0	-0.001	0.005	28.217	0.002	0.002	0.000	0.000	0.000	0.000
66	A	101	THR	0	0.003	0.008	25.463	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	102	VAL	0	-0.015	-0.002	20.234	0.001	0.001	0.000	0.000	0.000	0.000
68	A	103	THR	0	-0.001	0.002	22.027	0.002	0.002	0.000	0.000	0.000	0.000
69	A	104	ILE	0	-0.029	-0.025	16.525	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	105	LYS	1	0.750	0.860	19.872	0.241	0.241	0.000	0.000	0.000	0.000
71	A	106	SER	0	0.016	-0.002	18.138	0.028	0.028	0.000	0.000	0.000	0.000
72	A	107	ILE	0	-0.023	0.000	11.977	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	108	SER	0	0.004	-0.007	14.196	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	109	PHE	0	-0.021	-0.005	7.715	-0.060	-0.060	0.000	0.000	0.000	0.000
75	A	110	ILE	0	-0.001	0.003	12.680	0.096	0.096	0.000	0.000	0.000	0.000
76	A	111	SER	0	-0.031	-0.040	13.072	0.112	0.112	0.000	0.000	0.000	0.000
77	A	112	LYS	1	0.854	0.916	8.897	0.531	0.531	0.000	0.000	0.000	0.000
78	A	113	ASP	-1	-0.756	-0.843	7.987	-1.140	-1.140	0.000	0.000	0.000	0.000
79	A	114	LEU	0	-0.019	-0.009	10.428	0.065	0.065	0.000	0.000	0.000	0.000
80	A	115	ILE	0	-0.005	0.006	8.989	0.037	0.037	0.000	0.000	0.000	0.000
81	A	116	GLN	0	0.044	0.034	13.065	0.064	0.064	0.000	0.000	0.000	0.000
82	A	117	VAL	0	0.015	-0.005	14.296	-0.035	-0.035	0.000	0.000	0.000	0.000
83	A	118	ARG	1	0.859	0.922	16.869	0.278	0.278	0.000	0.000	0.000	0.000
84	A	119	TYR	0	0.007	-0.022	19.958	0.006	0.006	0.000	0.000	0.000	0.000
85	A	120	TYR	0	0.005	0.005	22.005	0.011	0.011	0.000	0.000	0.000	0.000
86	A	121	LYS	1	0.875	0.944	24.530	0.237	0.237	0.000	0.000	0.000	0.000
87	A	122	THR	0	0.037	0.013	27.003	0.005	0.005	0.000	0.000	0.000	0.000
88	A	123	VAL	0	-0.030	-0.005	29.457	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	124	ARG	1	0.804	0.871	31.924	0.085	0.085	0.000	0.000	0.000	0.000
90	A	125	ASP	-1	-0.765	-0.889	34.440	-0.087	-0.087	0.000	0.000	0.000	0.000
91	A	126	PHE	0	-0.011	-0.005	37.505	0.002	0.002	0.000	0.000	0.000	0.000
92	A	127	ASN	0	-0.091	-0.043	39.723	0.009	0.009	0.000	0.000	0.000	0.000
93	A	128	GLU	-1	-0.834	-0.893	39.381	-0.068	-0.068	0.000	0.000	0.000	0.000
94	A	129	LYS	1	0.855	0.923	38.250	0.097	0.097	0.000	0.000	0.000	0.000
95	A	130	GLU	-1	-0.860	-0.928	33.749	-0.102	-0.102	0.000	0.000	0.000	0.000
96	A	131	ASN	0	-0.053	-0.037	34.085	0.011	0.011	0.000	0.000	0.000	0.000
97	A	132	ILE	0	0.014	0.023	29.962	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	133	SER	0	-0.022	0.007	29.912	0.000	0.000	0.000	0.000	0.000	0.000
99	A	134	HIS	0	0.063	0.032	27.103	-0.021	-0.021	0.000	0.000	0.000	0.000
100	A	135	TRP	0	-0.001	0.000	24.276	0.003	0.003	0.000	0.000	0.000	0.000
101	A	136	ILE	0	-0.019	-0.013	20.760	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	137	SER	0	0.020	0.010	18.338	0.022	0.022	0.000	0.000	0.000	0.000
103	A	138	ILE	0	-0.054	-0.027	17.127	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	139	LEU	0	0.019	0.007	12.429	0.013	0.013	0.000	0.000	0.000	0.000
105	A	140	ASN	0	-0.009	0.007	13.145	-0.051	-0.051	0.000	0.000	0.000	0.000
106	A	141	PHE	0	-0.029	-0.023	5.388	0.111	0.111	0.000	0.000	0.000	0.000
107	A	142	SER	0	0.005	0.008	6.870	0.059	0.059	0.000	0.000	0.000	0.000
108	A	143	TYR	0	0.026	-0.018	2.369	-4.722	-1.330	5.288	-1.975	-6.705	-0.017
109	A	144	VAL	0	-0.009	-0.001	4.479	0.405	0.524	-0.001	-0.011	-0.107	0.000
110	A	145	ASN	0	0.006	0.008	3.321	-3.460	-2.876	0.009	-0.213	-0.379	-0.002
111	A	146	ALA	0	0.012	0.009	5.721	0.806	0.806	0.000	0.000	0.000	0.000
112	A	147	HIS	0	0.013	-0.005	8.264	-0.036	-0.036	0.000	0.000	0.000	0.000
113	A	148	ILE	0	0.023	0.008	7.476	-0.080	-0.080	0.000	0.000	0.000	0.000
114	A	149	SER	0	-0.018	-0.027	11.126	0.122	0.122	0.000	0.000	0.000	0.000
115	A	150	THR	0	0.050	0.001	12.712	-0.011	-0.011	0.000	0.000	0.000	0.000
116	A	151	SER	0	0.045	0.016	13.838	0.049	0.049	0.000	0.000	0.000	0.000
117	A	152	ASP	-1	-0.796	-0.849	13.248	-0.254	-0.254	0.000	0.000	0.000	0.000
118	A	153	ARG	1	0.848	0.929	5.719	0.677	0.677	0.000	0.000	0.000	0.000
119	A	154	LEU	0	-0.013	-0.001	10.770	0.136	0.136	0.000	0.000	0.000	0.000
120	A	155	ILE	0	-0.026	-0.002	12.672	0.003	0.003	0.000	0.000	0.000	0.000
121	A	156	ASN	0	-0.050	-0.044	7.792	-0.041	-0.041	0.000	0.000	0.000	0.000
122	A	157	PRO	0	0.017	0.015	6.957	-0.198	-0.198	0.000	0.000	0.000	0.000
123	A	158	LEU	0	-0.018	-0.014	2.617	-4.499	-1.305	3.549	-1.509	-5.234	0.018
124	A	159	GLY	0	0.049	0.035	3.246	-5.872	-4.496	0.122	-0.598	-0.900	-0.005
125	A	160	PHE	0	-0.016	-0.005	5.688	-0.503	-0.503	0.000	0.000	0.000	0.000
126	A	161	GLN	0	-0.033	-0.026	6.496	0.520	0.520	0.000	0.000	0.000	0.000
127	A	162	VAL	0	0.005	0.013	9.441	-0.092	-0.092	0.000	0.000	0.000	0.000
128	A	163	SER	0	-0.051	-0.021	12.144	0.110	0.110	0.000	0.000	0.000	0.000
129	A	164	GLU	-1	-0.784	-0.882	14.294	-0.428	-0.428	0.000	0.000	0.000	0.000
130	A	165	TYR	0	-0.040	-0.049	16.104	-0.080	-0.080	0.000	0.000	0.000	0.000
131	A	166	ARG	1	0.799	0.867	18.381	0.350	0.350	0.000	0.000	0.000	0.000
132	A	167	SER	0	0.010	-0.012	20.392	-0.029	-0.029	0.000	0.000	0.000	0.000
133	A	168	ASP	-1	-0.773	-0.836	22.860	-0.272	-0.272	0.000	0.000	0.000	0.000
134	A	169	PRO	0	0.032	0.011	25.540	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	170	GLU	-1	-0.817	-0.873	25.402	-0.217	-0.217	0.000	0.000	0.000	0.000

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