FMO DATABASE

FMODB ID: 52N1Z

Calculation Name: 4KL6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4KL6

Chain ID: A

ChEMBL ID:

UniProt ID: B2J821

Base Structure: X-ray

Registration Date: 2023-06-22

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	136
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1050703.448101
FMO2-HF: Nuclear repulsion	996092.921334
FMO2-HF: Total energy	-54610.526767
FMO2-MP2: Total energy	-54768.715016

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:-1:GLY)

Summations of interaction energy for fragment #1(A:-1: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.
-15.363	-12.198	4.575	-4.147	-3.591	-0.039

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

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 : -0.011

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	1	ALA	0	-0.039	-0.035	3.824	0.720	2.109	-0.016	-0.786	-0.587	0.002
4	A	2	LEU	0	-0.001	-0.001	7.163	0.004	0.004	0.000	0.000	0.000	0.000
5	A	3	SER	0	0.013	-0.014	10.444	0.143	0.143	0.000	0.000	0.000	0.000
6	A	4	TYR	0	0.012	0.015	14.079	0.032	0.032	0.000	0.000	0.000	0.000
7	A	5	GLU	-1	-0.781	-0.862	16.425	-0.635	-0.635	0.000	0.000	0.000	0.000
8	A	6	THR	0	0.011	-0.007	13.275	0.028	0.028	0.000	0.000	0.000	0.000
9	A	7	GLU	-1	-0.900	-0.964	15.976	-0.394	-0.394	0.000	0.000	0.000	0.000
10	A	8	ILE	0	-0.011	0.000	13.324	-0.034	-0.034	0.000	0.000	0.000	0.000
11	A	9	LEU	0	-0.047	-0.015	16.966	0.050	0.050	0.000	0.000	0.000	0.000
12	A	10	THR	0	-0.003	-0.021	18.539	0.007	0.007	0.000	0.000	0.000	0.000
13	A	11	VAL	0	-0.041	-0.032	20.915	0.008	0.008	0.000	0.000	0.000	0.000
14	A	12	GLU	-1	-0.829	-0.888	22.973	-0.128	-0.128	0.000	0.000	0.000	0.000
15	A	13	TYR	0	-0.051	-0.031	23.002	0.009	0.009	0.000	0.000	0.000	0.000
16	A	14	GLY	0	0.004	0.021	24.494	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	15	LEU	0	-0.049	-0.020	20.552	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	16	LEU	0	0.006	-0.001	19.860	0.031	0.031	0.000	0.000	0.000	0.000
19	A	17	PRO	0	0.016	0.036	18.347	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	18	ILE	0	0.062	0.012	11.041	0.048	0.048	0.000	0.000	0.000	0.000
21	A	19	GLY	0	0.031	0.011	15.458	0.024	0.024	0.000	0.000	0.000	0.000
22	A	20	LYS	1	0.901	0.964	16.568	0.317	0.317	0.000	0.000	0.000	0.000
23	A	21	ILE	0	-0.008	-0.009	16.044	0.049	0.049	0.000	0.000	0.000	0.000
24	A	22	VAL	0	-0.007	-0.001	12.612	0.069	0.069	0.000	0.000	0.000	0.000
25	A	23	GLU	-1	-0.900	-0.958	15.878	-0.296	-0.296	0.000	0.000	0.000	0.000
26	A	24	LYS	1	0.822	0.907	18.721	0.265	0.265	0.000	0.000	0.000	0.000
27	A	25	ARG	1	0.860	0.940	14.351	0.197	0.197	0.000	0.000	0.000	0.000
28	A	26	ILE	0	-0.016	0.008	19.115	0.032	0.032	0.000	0.000	0.000	0.000
29	A	27	GLU	-1	-0.873	-0.926	19.504	-0.078	-0.078	0.000	0.000	0.000	0.000
30	A	28	CYS	0	-0.086	-0.044	18.917	-0.019	-0.019	0.000	0.000	0.000	0.000
31	A	29	THR	0	-0.025	-0.035	19.247	0.013	0.013	0.000	0.000	0.000	0.000
32	A	30	VAL	0	0.020	0.014	14.312	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	31	TYR	0	-0.013	-0.026	17.030	0.058	0.058	0.000	0.000	0.000	0.000
34	A	32	SER	0	-0.017	-0.012	14.780	-0.077	-0.077	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.003	-0.009	15.118	0.001	0.001	0.000	0.000	0.000	0.000
36	A	34	ASP	-1	-0.763	-0.856	15.466	0.104	0.104	0.000	0.000	0.000	0.000
37	A	35	ASN	0	-0.030	-0.020	14.606	-0.016	-0.016	0.000	0.000	0.000	0.000
38	A	36	ASN	0	-0.088	-0.053	17.699	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	37	GLY	0	0.021	0.020	19.680	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	38	ASN	0	-0.109	-0.065	20.738	-0.033	-0.033	0.000	0.000	0.000	0.000
41	A	39	ILE	0	0.014	0.000	19.776	0.005	0.005	0.000	0.000	0.000	0.000
42	A	40	TYR	0	-0.081	-0.038	15.472	0.021	0.021	0.000	0.000	0.000	0.000
43	A	41	THR	0	-0.007	-0.007	19.305	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	42	GLN	0	0.034	0.028	14.389	0.037	0.037	0.000	0.000	0.000	0.000
45	A	43	PRO	0	0.021	0.007	17.943	-0.034	-0.034	0.000	0.000	0.000	0.000
46	A	44	VAL	0	0.000	0.005	13.777	0.015	0.015	0.000	0.000	0.000	0.000
47	A	45	ALA	0	-0.008	0.004	13.767	0.018	0.018	0.000	0.000	0.000	0.000
48	A	46	GLN	0	-0.001	-0.020	11.739	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	47	TRP	0	-0.030	0.002	12.520	-0.075	-0.075	0.000	0.000	0.000	0.000
50	A	48	HIS	0	0.016	0.001	7.958	-0.022	-0.022	0.000	0.000	0.000	0.000
51	A	49	ASP	-1	-0.779	-0.874	10.358	-0.701	-0.701	0.000	0.000	0.000	0.000
52	A	50	ARG	1	0.762	0.850	4.607	1.757	1.798	-0.001	-0.006	-0.033	0.000
53	A	51	GLY	0	0.001	0.018	9.867	0.005	0.005	0.000	0.000	0.000	0.000
54	A	52	GLU	-1	-0.925	-0.960	12.566	-0.763	-0.763	0.000	0.000	0.000	0.000
55	A	53	GLN	0	-0.091	-0.062	8.712	-0.236	-0.236	0.000	0.000	0.000	0.000
56	A	54	GLU	-1	-0.917	-0.957	10.869	-0.646	-0.646	0.000	0.000	0.000	0.000
57	A	55	VAL	0	-0.055	-0.026	10.674	-0.265	-0.265	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.001	-0.002	11.542	0.219	0.219	0.000	0.000	0.000	0.000
59	A	57	GLU	-1	-0.851	-0.932	13.815	-0.645	-0.645	0.000	0.000	0.000	0.000
60	A	58	TYR	0	-0.046	-0.049	11.605	-0.012	-0.012	0.000	0.000	0.000	0.000
61	A	59	CYS	0	-0.028	-0.015	16.580	0.010	0.010	0.000	0.000	0.000	0.000
62	A	60	LEU	0	0.016	0.021	17.093	0.006	0.006	0.000	0.000	0.000	0.000
63	A	61	GLU	-1	-0.848	-0.928	20.855	-0.224	-0.224	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-0.936	-0.950	23.021	-0.308	-0.308	0.000	0.000	0.000	0.000
65	A	63	GLY	0	-0.044	-0.023	24.297	0.017	0.017	0.000	0.000	0.000	0.000
66	A	64	SER	0	-0.091	-0.057	21.101	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	65	LEU	0	0.002	-0.010	19.210	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	66	ILE	0	0.000	0.011	12.734	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	67	ARG	1	0.787	0.864	14.386	0.616	0.616	0.000	0.000	0.000	0.000
70	A	68	ALA	0	0.011	0.004	8.972	-0.051	-0.051	0.000	0.000	0.000	0.000
71	A	69	THR	0	-0.001	0.002	5.223	0.269	0.269	0.000	0.000	0.000	0.000
72	A	70	LYS	1	0.842	0.904	7.465	0.508	0.508	0.000	0.000	0.000	0.000
73	A	71	ASP	-1	-0.760	-0.887	2.098	-13.392	-13.116	4.521	-2.572	-2.225	-0.035
74	A	72	HIS	0	-0.024	0.004	3.123	-3.175	-1.970	0.071	-0.750	-0.526	-0.006
75	A	73	LYS	1	0.844	0.912	3.756	0.926	1.180	0.000	-0.033	-0.220	0.000
76	A	74	PHE	0	0.013	0.005	5.914	0.064	0.064	0.000	0.000	0.000	0.000
77	A	75	MET	0	0.017	-0.004	9.731	0.157	0.157	0.000	0.000	0.000	0.000
78	A	76	VAL	0	0.006	-0.005	12.691	-0.041	-0.041	0.000	0.000	0.000	0.000
79	A	77	ASP	-1	-0.823	-0.916	15.146	0.004	0.004	0.000	0.000	0.000	0.000
80	A	78	GLY	0	-0.048	-0.022	16.822	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	79	GLN	0	-0.043	-0.035	12.711	0.064	0.064	0.000	0.000	0.000	0.000
82	A	80	MET	0	0.003	0.012	8.788	-0.134	-0.134	0.000	0.000	0.000	0.000
83	A	81	LEU	0	-0.019	0.001	8.462	0.292	0.292	0.000	0.000	0.000	0.000
84	A	82	PRO	0	0.021	0.011	5.531	-0.263	-0.263	0.000	0.000	0.000	0.000
85	A	83	ILE	0	0.028	0.018	6.838	0.406	0.406	0.000	0.000	0.000	0.000
86	A	84	ASP	-1	-0.763	-0.836	9.016	-0.632	-0.632	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.805	-0.895	9.758	0.041	0.041	0.000	0.000	0.000	0.000
88	A	86	ILE	0	-0.053	-0.030	10.625	0.123	0.123	0.000	0.000	0.000	0.000
89	A	87	PHE	0	-0.030	-0.011	13.091	0.087	0.087	0.000	0.000	0.000	0.000
90	A	88	GLU	-1	-0.955	-0.981	13.770	-0.311	-0.311	0.000	0.000	0.000	0.000
91	A	89	ARG	1	0.766	0.882	13.332	0.183	0.183	0.000	0.000	0.000	0.000
92	A	90	GLU	-1	-0.971	-0.974	17.150	-0.180	-0.180	0.000	0.000	0.000	0.000
93	A	91	LEU	0	-0.064	-0.027	15.097	0.044	0.044	0.000	0.000	0.000	0.000
94	A	92	ASP	-1	-0.920	-0.962	17.200	-0.280	-0.280	0.000	0.000	0.000	0.000
95	A	93	LEU	0	-0.009	-0.008	12.918	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	94	MET	0	-0.053	-0.003	15.828	0.051	0.051	0.000	0.000	0.000	0.000
97	A	95	ARG	1	0.880	0.935	16.980	0.212	0.212	0.000	0.000	0.000	0.000
98	A	96	ASN	0	-0.020	-0.015	19.709	0.024	0.024	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.026	0.019	22.588	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	98	GLY	0	0.004	0.000	25.603	0.017	0.017	0.000	0.000	0.000	0.000
101	A	99	ILE	0	-0.008	-0.002	26.523	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.960	0.973	28.715	0.144	0.144	0.000	0.000	0.000	0.000
103	A	101	ILE	0	0.020	0.007	31.682	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.020	0.022	31.882	0.007	0.007	0.000	0.000	0.000	0.000
105	A	103	THR	0	-0.025	-0.014	33.937	0.008	0.008	0.000	0.000	0.000	0.000
106	A	104	ARG	1	0.992	0.995	37.418	0.085	0.085	0.000	0.000	0.000	0.000
107	A	105	LYS	1	0.967	0.979	39.411	0.129	0.129	0.000	0.000	0.000	0.000
108	A	106	TYR	0	0.002	-0.007	43.226	0.002	0.002	0.000	0.000	0.000	0.000
109	A	107	LEU	0	0.036	0.011	42.891	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	108	GLY	0	0.021	0.027	47.396	0.001	0.001	0.000	0.000	0.000	0.000
111	A	109	LYS	1	0.907	0.949	50.413	0.059	0.059	0.000	0.000	0.000	0.000
112	A	110	GLN	0	0.052	0.024	45.310	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	111	ASN	0	-0.022	0.003	50.669	0.002	0.002	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.002	-0.003	47.371	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	113	TYR	0	-0.028	-0.033	46.355	0.002	0.002	0.000	0.000	0.000	0.000
116	A	114	ASP	-1	-0.817	-0.892	45.892	-0.069	-0.069	0.000	0.000	0.000	0.000
117	A	115	ILE	0	-0.053	-0.020	42.128	0.002	0.002	0.000	0.000	0.000	0.000
118	A	116	GLY	0	0.033	0.033	46.027	0.000	0.000	0.000	0.000	0.000	0.000
119	A	117	VAL	0	-0.015	-0.013	43.898	0.000	0.000	0.000	0.000	0.000	0.000
120	A	118	GLU	-1	-0.859	-0.903	47.277	-0.033	-0.033	0.000	0.000	0.000	0.000
121	A	119	ARG	1	0.856	0.891	44.682	0.040	0.040	0.000	0.000	0.000	0.000
122	A	120	ASP	-1	-0.856	-0.935	42.611	-0.045	-0.045	0.000	0.000	0.000	0.000
123	A	121	HIS	0	-0.077	-0.014	43.904	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	122	ASN	0	-0.043	-0.020	39.357	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	123	PHE	0	0.030	0.017	39.307	0.001	0.001	0.000	0.000	0.000	0.000
126	A	124	ALA	0	0.039	0.024	33.965	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	125	LEU	0	-0.030	-0.008	34.519	0.002	0.002	0.000	0.000	0.000	0.000
128	A	126	LYS	1	0.950	0.950	28.135	0.206	0.206	0.000	0.000	0.000	0.000
129	A	127	ASN	0	-0.003	-0.002	26.773	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	128	GLY	0	0.049	0.036	28.218	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	129	PHE	0	-0.049	-0.020	30.313	0.005	0.005	0.000	0.000	0.000	0.000
132	A	130	ILE	0	0.022	0.008	33.120	0.002	0.002	0.000	0.000	0.000	0.000
133	A	131	ALA	0	-0.020	0.008	36.243	0.001	0.001	0.000	0.000	0.000	0.000
134	A	132	SER	0	-0.019	-0.050	39.783	0.004	0.004	0.000	0.000	0.000	0.000
135	A	133	ASN	0	-0.064	-0.053	42.862	0.000	0.000	0.000	0.000	0.000	0.000
136	A	134	ALA	0	-0.029	0.004	45.322	0.004	0.004	0.000	0.000	0.000	0.000

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