FMO DATABASE

FMODB ID: K9243

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1050315.003857
FMO2-HF: Nuclear repulsion	995705.518073
FMO2-HF: Total energy	-54609.485784
FMO2-MP2: Total energy	-54767.63613

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.
-7.409	-5.302	0.021	-1.146	-0.984	0.003

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 : -0.004 / q_NPA : 0.000

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	-0.052	-0.066	3.772	0.513	2.054	-0.015	-0.867	-0.660	0.004
4	A	2	LEU	0	0.012	0.003	6.754	0.060	0.060	0.000	0.000	0.000	0.000
5	A	3	SER	0	0.028	0.000	10.283	0.137	0.137	0.000	0.000	0.000	0.000
6	A	4	TYR	0	0.023	0.030	13.748	0.051	0.051	0.000	0.000	0.000	0.000
7	A	5	GLU	-1	-0.829	-0.902	15.879	-0.513	-0.513	0.000	0.000	0.000	0.000
8	A	6	THR	0	0.020	-0.002	13.119	0.001	0.001	0.000	0.000	0.000	0.000
9	A	7	GLU	-1	-0.961	-0.980	16.036	-0.261	-0.261	0.000	0.000	0.000	0.000
10	A	8	ILE	0	-0.016	-0.004	13.137	-0.026	-0.026	0.000	0.000	0.000	0.000
11	A	9	LEU	0	-0.030	-0.021	16.721	0.040	0.040	0.000	0.000	0.000	0.000
12	A	10	THR	0	-0.014	-0.030	18.295	0.021	0.021	0.000	0.000	0.000	0.000
13	A	11	VAL	0	-0.023	-0.018	20.514	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	12	GLU	-1	-0.845	-0.909	22.677	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	13	TYR	0	-0.032	-0.022	22.746	0.000	0.000	0.000	0.000	0.000	0.000
16	A	14	GLY	0	-0.001	0.021	23.980	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	15	LEU	0	-0.053	-0.027	20.226	0.000	0.000	0.000	0.000	0.000	0.000
18	A	16	LEU	0	0.002	0.011	19.638	0.021	0.021	0.000	0.000	0.000	0.000
19	A	17	PRO	0	0.061	0.050	18.119	-0.027	-0.027	0.000	0.000	0.000	0.000
20	A	18	ILE	0	0.066	0.017	10.583	0.060	0.060	0.000	0.000	0.000	0.000
21	A	19	GLY	0	0.033	0.001	14.626	0.036	0.036	0.000	0.000	0.000	0.000
22	A	20	LYS	1	0.908	0.963	15.804	0.195	0.195	0.000	0.000	0.000	0.000
23	A	21	ILE	0	0.012	-0.001	14.947	0.040	0.040	0.000	0.000	0.000	0.000
24	A	22	VAL	0	0.005	0.004	11.542	0.075	0.075	0.000	0.000	0.000	0.000
25	A	23	GLU	-1	-0.912	-0.955	14.779	-0.127	-0.127	0.000	0.000	0.000	0.000
26	A	24	LYS	1	0.812	0.907	17.465	0.136	0.136	0.000	0.000	0.000	0.000
27	A	25	ARG	1	0.893	0.948	13.426	-0.099	-0.099	0.000	0.000	0.000	0.000
28	A	26	ILE	0	-0.042	-0.005	18.026	0.016	0.016	0.000	0.000	0.000	0.000
29	A	27	GLU	-1	-0.896	-0.944	18.485	0.107	0.107	0.000	0.000	0.000	0.000
30	A	28	CYS	0	-0.089	-0.045	18.446	-0.029	-0.029	0.000	0.000	0.000	0.000
31	A	29	THR	0	-0.031	-0.027	18.778	0.033	0.033	0.000	0.000	0.000	0.000
32	A	30	VAL	0	0.017	0.014	13.916	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	31	TYR	0	-0.022	-0.032	16.798	0.039	0.039	0.000	0.000	0.000	0.000
34	A	32	SER	0	-0.017	-0.036	14.314	-0.060	-0.060	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.002	-0.001	14.805	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	34	ASP	-1	-0.797	-0.883	15.165	0.085	0.085	0.000	0.000	0.000	0.000
37	A	35	ASN	0	-0.044	-0.050	14.976	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	36	ASN	0	-0.063	-0.028	17.789	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	37	GLY	0	0.024	0.027	19.532	-0.011	-0.011	0.000	0.000	0.000	0.000
40	A	38	ASN	0	-0.076	-0.039	20.683	-0.030	-0.030	0.000	0.000	0.000	0.000
41	A	39	ILE	0	-0.001	-0.003	19.646	0.008	0.008	0.000	0.000	0.000	0.000
42	A	40	TYR	0	-0.063	-0.025	15.801	0.010	0.010	0.000	0.000	0.000	0.000
43	A	41	THR	0	-0.008	-0.001	19.106	-0.015	-0.015	0.000	0.000	0.000	0.000
44	A	42	GLN	0	0.023	0.031	14.577	0.003	0.003	0.000	0.000	0.000	0.000
45	A	43	PRO	0	0.025	0.012	17.643	-0.028	-0.028	0.000	0.000	0.000	0.000
46	A	44	VAL	0	0.013	0.018	13.200	0.031	0.031	0.000	0.000	0.000	0.000
47	A	45	ALA	0	-0.015	-0.010	13.419	0.012	0.012	0.000	0.000	0.000	0.000
48	A	46	GLN	0	-0.036	-0.027	10.268	0.001	0.001	0.000	0.000	0.000	0.000
49	A	47	TRP	0	0.000	0.019	11.264	-0.041	-0.041	0.000	0.000	0.000	0.000
50	A	48	HIS	0	-0.039	-0.038	6.169	0.036	0.036	0.000	0.000	0.000	0.000
51	A	49	ASP	-1	-0.834	-0.913	9.390	-0.450	-0.450	0.000	0.000	0.000	0.000
52	A	50	ARG	1	0.842	0.911	3.221	0.170	0.487	0.037	-0.155	-0.200	-0.001
53	A	51	GLY	0	0.023	0.025	9.079	-0.035	-0.035	0.000	0.000	0.000	0.000
54	A	52	GLU	-1	-0.942	-0.966	12.026	-0.652	-0.652	0.000	0.000	0.000	0.000
55	A	53	GLN	0	-0.075	-0.048	8.313	-0.179	-0.179	0.000	0.000	0.000	0.000
56	A	54	GLU	-1	-0.944	-0.959	11.465	-0.629	-0.629	0.000	0.000	0.000	0.000
57	A	55	VAL	0	-0.035	-0.024	11.440	-0.250	-0.250	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.002	-0.003	12.809	0.152	0.152	0.000	0.000	0.000	0.000
59	A	57	GLU	-1	-0.899	-0.965	14.906	-0.533	-0.533	0.000	0.000	0.000	0.000
60	A	58	TYR	0	-0.049	-0.054	12.722	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	59	CYS	0	-0.017	-0.014	17.769	0.025	0.025	0.000	0.000	0.000	0.000
62	A	60	LEU	0	-0.017	0.004	17.938	0.011	0.011	0.000	0.000	0.000	0.000
63	A	61	GLU	-1	-0.834	-0.920	21.863	-0.256	-0.256	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-1.056	-1.022	24.135	-0.286	-0.286	0.000	0.000	0.000	0.000
65	A	63	GLY	0	-0.029	-0.035	25.335	0.016	0.016	0.000	0.000	0.000	0.000
66	A	64	SER	0	-0.075	-0.025	21.641	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	65	LEU	0	0.006	-0.009	19.845	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	66	ILE	0	0.022	0.028	13.361	0.000	0.000	0.000	0.000	0.000	0.000
69	A	67	ARG	1	0.848	0.924	14.878	0.488	0.488	0.000	0.000	0.000	0.000
70	A	68	ALA	0	0.006	-0.004	9.531	-0.039	-0.039	0.000	0.000	0.000	0.000
71	A	69	THR	0	0.037	0.026	6.382	0.224	0.224	0.000	0.000	0.000	0.000
72	A	70	LYS	1	0.883	0.944	9.031	0.724	0.724	0.000	0.000	0.000	0.000
73	A	71	ASP	-1	-0.866	-0.937	4.021	-5.765	-5.576	0.000	-0.089	-0.100	0.000
74	A	72	HIS	0	-0.046	0.005	4.635	-1.413	-1.353	-0.001	-0.035	-0.024	0.000
75	A	73	LYS	1	0.894	0.946	4.941	1.516	1.516	0.000	0.000	0.000	0.000
76	A	74	PHE	0	0.012	0.001	7.137	0.111	0.111	0.000	0.000	0.000	0.000
77	A	75	MET	0	0.033	-0.001	10.441	0.089	0.089	0.000	0.000	0.000	0.000
78	A	76	VAL	0	0.017	0.014	13.176	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	77	ASP	-1	-0.905	-0.975	16.022	-0.116	-0.116	0.000	0.000	0.000	0.000
80	A	78	GLY	0	-0.011	0.008	17.592	0.006	0.006	0.000	0.000	0.000	0.000
81	A	79	GLN	0	-0.048	-0.045	13.267	0.054	0.054	0.000	0.000	0.000	0.000
82	A	80	MET	0	-0.040	0.008	8.870	-0.097	-0.097	0.000	0.000	0.000	0.000
83	A	81	LEU	0	0.008	-0.004	9.655	0.066	0.066	0.000	0.000	0.000	0.000
84	A	82	PRO	0	0.014	0.018	6.997	-0.229	-0.229	0.000	0.000	0.000	0.000
85	A	83	ILE	0	0.050	0.018	8.361	0.339	0.339	0.000	0.000	0.000	0.000
86	A	84	ASP	-1	-0.787	-0.870	10.450	-0.704	-0.704	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.809	-0.889	11.345	-0.413	-0.413	0.000	0.000	0.000	0.000
88	A	86	ILE	0	-0.082	-0.038	12.126	0.129	0.129	0.000	0.000	0.000	0.000
89	A	87	PHE	0	-0.042	-0.022	14.603	0.096	0.096	0.000	0.000	0.000	0.000
90	A	88	GLU	-1	-0.965	-0.993	15.202	-0.534	-0.534	0.000	0.000	0.000	0.000
91	A	89	ARG	1	0.785	0.880	15.230	0.418	0.418	0.000	0.000	0.000	0.000
92	A	90	GLU	-1	-0.979	-0.975	18.725	-0.236	-0.236	0.000	0.000	0.000	0.000
93	A	91	LEU	0	-0.075	-0.023	16.371	0.041	0.041	0.000	0.000	0.000	0.000
94	A	92	ASP	-1	-0.893	-0.943	19.077	-0.309	-0.309	0.000	0.000	0.000	0.000
95	A	93	LEU	0	-0.028	-0.026	14.112	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	94	MET	0	-0.038	0.005	16.727	0.062	0.062	0.000	0.000	0.000	0.000
97	A	95	ARG	1	0.912	0.937	17.501	0.211	0.211	0.000	0.000	0.000	0.000
98	A	96	ASN	0	-0.035	-0.022	19.983	0.024	0.024	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.020	0.020	22.717	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	98	GLY	0	0.008	0.008	25.726	0.013	0.013	0.000	0.000	0.000	0.000
101	A	99	ILE	0	0.004	-0.013	26.589	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.965	0.984	28.784	0.111	0.111	0.000	0.000	0.000	0.000
103	A	101	ILE	0	0.022	0.009	31.541	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.008	0.021	32.225	0.006	0.006	0.000	0.000	0.000	0.000
105	A	103	THR	0	-0.019	-0.015	34.143	0.009	0.009	0.000	0.000	0.000	0.000
106	A	104	ARG	1	1.007	0.992	37.608	0.070	0.070	0.000	0.000	0.000	0.000
107	A	105	LYS	1	0.969	0.980	39.928	0.108	0.108	0.000	0.000	0.000	0.000
108	A	106	TYR	0	-0.004	0.014	43.299	0.000	0.000	0.000	0.000	0.000	0.000
109	A	107	LEU	0	0.052	0.014	43.182	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	108	GLY	0	-0.008	0.004	47.463	0.001	0.001	0.000	0.000	0.000	0.000
111	A	109	LYS	1	0.909	0.949	50.246	0.054	0.054	0.000	0.000	0.000	0.000
112	A	110	GLN	0	0.058	0.023	45.953	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	111	ASN	0	-0.045	-0.020	51.131	0.001	0.001	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.015	-0.005	48.006	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	113	TYR	0	0.004	-0.012	47.468	0.002	0.002	0.000	0.000	0.000	0.000
116	A	114	ASP	-1	-0.863	-0.934	46.732	-0.071	-0.071	0.000	0.000	0.000	0.000
117	A	115	ILE	0	-0.069	-0.019	43.377	0.001	0.001	0.000	0.000	0.000	0.000
118	A	116	GLY	0	0.035	0.028	47.301	0.000	0.000	0.000	0.000	0.000	0.000
119	A	117	VAL	0	-0.016	-0.009	44.686	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	118	GLU	-1	-0.907	-0.946	47.978	-0.044	-0.044	0.000	0.000	0.000	0.000
121	A	119	ARG	1	0.893	0.921	45.164	0.055	0.055	0.000	0.000	0.000	0.000
122	A	120	ASP	-1	-0.886	-0.933	43.222	-0.058	-0.058	0.000	0.000	0.000	0.000
123	A	121	HIS	0	-0.082	-0.037	45.059	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	122	ASN	0	-0.026	-0.020	40.163	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	123	PHE	0	0.037	0.012	40.066	0.000	0.000	0.000	0.000	0.000	0.000
126	A	124	ALA	0	0.031	0.020	34.747	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	125	LEU	0	-0.052	-0.016	35.463	0.001	0.001	0.000	0.000	0.000	0.000
128	A	126	LYS	1	1.066	1.012	30.967	0.182	0.182	0.000	0.000	0.000	0.000
129	A	127	ASN	0	-0.006	-0.003	27.676	-0.007	-0.007	0.000	0.000	0.000	0.000
130	A	128	GLY	0	0.033	0.034	29.310	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	129	PHE	0	-0.053	-0.016	30.753	0.006	0.006	0.000	0.000	0.000	0.000
132	A	130	ILE	0	0.039	0.015	33.808	0.001	0.001	0.000	0.000	0.000	0.000
133	A	131	ALA	0	-0.020	0.006	36.744	0.004	0.004	0.000	0.000	0.000	0.000
134	A	132	SER	0	-0.009	-0.023	40.158	0.003	0.003	0.000	0.000	0.000	0.000
135	A	133	ASN	0	-0.017	-0.006	43.134	0.001	0.001	0.000	0.000	0.000	0.000
136	A	134	ALA	0	0.000	0.014	45.691	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)