FMO DATABASE

FMODB ID: 49L1N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1051185.963556
FMO2-HF: Nuclear repulsion	996575.805674
FMO2-HF: Total energy	-54610.157881
FMO2-MP2: Total energy	-54768.30548

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.
-7.702	-5.578	8.673617379884E-19	-1.214	-0.912	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 : -0.001 / q_NPA : 0.003

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	-0.070	-0.059	3.772	0.643	2.164	-0.015	-0.856	-0.651	0.005
4	A	2	LEU	0	0.002	0.001	6.751	0.076	0.076	0.000	0.000	0.000	0.000
5	A	3	SER	0	0.036	0.009	10.283	0.142	0.142	0.000	0.000	0.000	0.000
6	A	4	TYR	0	0.024	0.021	13.744	0.046	0.046	0.000	0.000	0.000	0.000
7	A	5	GLU	-1	-0.784	-0.877	15.876	-0.513	-0.513	0.000	0.000	0.000	0.000
8	A	6	THR	0	0.014	0.001	13.146	0.006	0.006	0.000	0.000	0.000	0.000
9	A	7	GLU	-1	-0.929	-0.967	16.036	-0.264	-0.264	0.000	0.000	0.000	0.000
10	A	8	ILE	0	-0.025	-0.015	13.100	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	9	LEU	0	-0.029	-0.012	16.720	0.043	0.043	0.000	0.000	0.000	0.000
12	A	10	THR	0	0.003	-0.022	18.294	0.020	0.020	0.000	0.000	0.000	0.000
13	A	11	VAL	0	-0.040	-0.031	20.512	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	12	GLU	-1	-0.835	-0.883	22.436	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	13	TYR	0	-0.037	-0.026	22.424	0.000	0.000	0.000	0.000	0.000	0.000
16	A	14	GLY	0	0.003	0.024	23.981	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	15	LEU	0	-0.053	-0.029	20.388	0.000	0.000	0.000	0.000	0.000	0.000
18	A	16	LEU	0	-0.002	0.008	19.697	0.023	0.023	0.000	0.000	0.000	0.000
19	A	17	PRO	0	0.054	0.049	18.080	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	18	ILE	0	0.069	0.017	10.477	0.060	0.060	0.000	0.000	0.000	0.000
21	A	19	GLY	0	0.033	0.006	14.625	0.037	0.037	0.000	0.000	0.000	0.000
22	A	20	LYS	1	0.903	0.967	15.802	0.203	0.203	0.000	0.000	0.000	0.000
23	A	21	ILE	0	-0.003	-0.005	15.324	0.042	0.042	0.000	0.000	0.000	0.000
24	A	22	VAL	0	-0.001	0.001	11.578	0.076	0.076	0.000	0.000	0.000	0.000
25	A	23	GLU	-1	-0.910	-0.952	14.778	-0.129	-0.129	0.000	0.000	0.000	0.000
26	A	24	LYS	1	0.806	0.899	17.463	0.132	0.132	0.000	0.000	0.000	0.000
27	A	25	ARG	1	0.881	0.945	13.377	-0.115	-0.115	0.000	0.000	0.000	0.000
28	A	26	ILE	0	-0.039	-0.002	18.027	0.017	0.017	0.000	0.000	0.000	0.000
29	A	27	GLU	-1	-0.883	-0.936	18.486	0.109	0.109	0.000	0.000	0.000	0.000
30	A	28	CYS	0	-0.095	-0.052	18.380	-0.030	-0.030	0.000	0.000	0.000	0.000
31	A	29	THR	0	-0.028	-0.040	18.774	0.033	0.033	0.000	0.000	0.000	0.000
32	A	30	VAL	0	0.023	0.016	13.932	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	31	TYR	0	-0.023	-0.032	16.811	0.043	0.043	0.000	0.000	0.000	0.000
34	A	32	SER	0	-0.011	-0.010	14.348	-0.060	-0.060	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.005	-0.009	14.804	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	34	ASP	-1	-0.792	-0.876	15.165	0.090	0.090	0.000	0.000	0.000	0.000
37	A	35	ASN	0	-0.038	-0.032	14.936	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	36	ASN	0	-0.076	-0.043	17.790	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	37	GLY	0	0.021	0.023	19.531	-0.011	-0.011	0.000	0.000	0.000	0.000
40	A	38	ASN	0	-0.078	-0.046	20.684	-0.024	-0.024	0.000	0.000	0.000	0.000
41	A	39	ILE	0	0.002	-0.006	19.647	0.007	0.007	0.000	0.000	0.000	0.000
42	A	40	TYR	0	-0.077	-0.035	15.306	0.012	0.012	0.000	0.000	0.000	0.000
43	A	41	THR	0	0.001	-0.001	19.104	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	42	GLN	0	0.026	0.027	14.329	0.008	0.008	0.000	0.000	0.000	0.000
45	A	43	PRO	0	0.025	0.011	17.640	-0.027	-0.027	0.000	0.000	0.000	0.000
46	A	44	VAL	0	0.005	0.013	13.093	0.030	0.030	0.000	0.000	0.000	0.000
47	A	45	ALA	0	-0.005	-0.004	13.365	0.013	0.013	0.000	0.000	0.000	0.000
48	A	46	GLN	0	-0.019	-0.024	10.287	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	47	TRP	0	-0.015	0.007	11.266	-0.041	-0.041	0.000	0.000	0.000	0.000
50	A	48	HIS	0	-0.011	-0.018	7.226	0.117	0.117	0.000	0.000	0.000	0.000
51	A	49	ASP	-1	-0.826	-0.910	9.389	-0.444	-0.444	0.000	0.000	0.000	0.000
52	A	50	ARG	1	0.807	0.892	3.684	0.716	0.901	0.005	-0.070	-0.121	0.000
53	A	51	GLY	0	0.026	0.027	9.075	-0.036	-0.036	0.000	0.000	0.000	0.000
54	A	52	GLU	-1	-0.947	-0.973	12.021	-0.652	-0.652	0.000	0.000	0.000	0.000
55	A	53	GLN	0	-0.092	-0.057	8.662	-0.213	-0.213	0.000	0.000	0.000	0.000
56	A	54	GLU	-1	-0.929	-0.955	11.445	-0.664	-0.664	0.000	0.000	0.000	0.000
57	A	55	VAL	0	-0.044	-0.030	11.408	-0.252	-0.252	0.000	0.000	0.000	0.000
58	A	56	PHE	0	-0.011	-0.006	12.746	0.155	0.155	0.000	0.000	0.000	0.000
59	A	57	GLU	-1	-0.859	-0.932	14.906	-0.551	-0.551	0.000	0.000	0.000	0.000
60	A	58	TYR	0	-0.050	-0.055	12.763	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	59	CYS	0	-0.022	-0.016	17.780	0.024	0.024	0.000	0.000	0.000	0.000
62	A	60	LEU	0	0.003	0.011	17.868	0.009	0.009	0.000	0.000	0.000	0.000
63	A	61	GLU	-1	-0.836	-0.918	21.868	-0.254	-0.254	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-1.029	-1.004	23.976	-0.295	-0.295	0.000	0.000	0.000	0.000
65	A	63	GLY	0	-0.031	-0.031	25.334	0.016	0.016	0.000	0.000	0.000	0.000
66	A	64	SER	0	-0.084	-0.048	21.941	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	65	LEU	0	0.004	-0.006	19.826	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	66	ILE	0	0.006	0.018	13.431	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	67	ARG	1	0.782	0.862	14.878	0.503	0.503	0.000	0.000	0.000	0.000
70	A	68	ALA	0	0.001	-0.004	9.588	-0.040	-0.040	0.000	0.000	0.000	0.000
71	A	69	THR	0	0.019	0.000	6.322	0.222	0.222	0.000	0.000	0.000	0.000
72	A	70	LYS	1	0.848	0.904	9.045	0.714	0.714	0.000	0.000	0.000	0.000
73	A	71	ASP	-1	-0.844	-0.917	3.508	-7.247	-6.883	0.011	-0.254	-0.121	-0.002
74	A	72	HIS	0	-0.021	0.005	4.643	-1.264	-1.210	-0.001	-0.034	-0.019	0.000
75	A	73	LYS	1	0.888	0.943	4.981	1.861	1.861	0.000	0.000	0.000	0.000
76	A	74	PHE	0	0.003	-0.002	7.142	0.123	0.123	0.000	0.000	0.000	0.000
77	A	75	MET	0	0.025	-0.002	10.445	0.090	0.090	0.000	0.000	0.000	0.000
78	A	76	VAL	0	0.022	0.010	13.180	-0.009	-0.009	0.000	0.000	0.000	0.000
79	A	77	ASP	-1	-0.881	-0.966	16.027	-0.117	-0.117	0.000	0.000	0.000	0.000
80	A	78	GLY	0	-0.017	0.013	17.595	0.005	0.005	0.000	0.000	0.000	0.000
81	A	79	GLN	0	-0.037	-0.040	13.388	0.027	0.027	0.000	0.000	0.000	0.000
82	A	80	MET	0	-0.043	0.008	8.837	-0.109	-0.109	0.000	0.000	0.000	0.000
83	A	81	LEU	0	-0.012	-0.012	9.674	0.069	0.069	0.000	0.000	0.000	0.000
84	A	82	PRO	0	0.016	0.014	6.950	-0.225	-0.225	0.000	0.000	0.000	0.000
85	A	83	ILE	0	0.043	0.019	8.364	0.354	0.354	0.000	0.000	0.000	0.000
86	A	84	ASP	-1	-0.751	-0.830	10.458	-0.732	-0.732	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.804	-0.890	11.315	-0.433	-0.433	0.000	0.000	0.000	0.000
88	A	86	ILE	0	-0.055	-0.022	11.999	0.129	0.129	0.000	0.000	0.000	0.000
89	A	87	PHE	0	-0.037	-0.022	14.610	0.095	0.095	0.000	0.000	0.000	0.000
90	A	88	GLU	-1	-0.970	-0.992	15.459	-0.510	-0.510	0.000	0.000	0.000	0.000
91	A	89	ARG	1	0.780	0.876	14.907	0.440	0.440	0.000	0.000	0.000	0.000
92	A	90	GLU	-1	-0.983	-0.976	18.729	-0.242	-0.242	0.000	0.000	0.000	0.000
93	A	91	LEU	0	-0.066	-0.021	16.129	0.041	0.041	0.000	0.000	0.000	0.000
94	A	92	ASP	-1	-0.900	-0.946	19.078	-0.314	-0.314	0.000	0.000	0.000	0.000
95	A	93	LEU	0	-0.028	-0.024	14.211	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	94	MET	0	-0.039	0.002	16.701	0.061	0.061	0.000	0.000	0.000	0.000
97	A	95	ARG	1	0.896	0.939	17.504	0.222	0.222	0.000	0.000	0.000	0.000
98	A	96	ASN	0	-0.027	-0.019	19.986	0.021	0.021	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.028	0.022	22.719	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	98	GLY	0	0.006	0.007	25.729	0.013	0.013	0.000	0.000	0.000	0.000
101	A	99	ILE	0	0.000	-0.013	26.591	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.957	0.981	28.786	0.112	0.112	0.000	0.000	0.000	0.000
103	A	101	ILE	0	0.026	0.010	31.542	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.010	0.023	32.197	0.006	0.006	0.000	0.000	0.000	0.000
105	A	103	THR	0	-0.018	-0.017	34.145	0.009	0.009	0.000	0.000	0.000	0.000
106	A	104	ARG	1	0.997	0.990	37.610	0.071	0.071	0.000	0.000	0.000	0.000
107	A	105	LYS	1	0.969	0.981	39.717	0.111	0.111	0.000	0.000	0.000	0.000
108	A	106	TYR	0	-0.004	0.006	43.301	0.000	0.000	0.000	0.000	0.000	0.000
109	A	107	LEU	0	0.052	0.012	43.044	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	108	GLY	0	-0.004	0.014	47.465	0.001	0.001	0.000	0.000	0.000	0.000
111	A	109	LYS	1	0.914	0.956	50.249	0.055	0.055	0.000	0.000	0.000	0.000
112	A	110	GLN	0	0.057	0.020	45.747	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	111	ASN	0	-0.033	-0.005	51.134	0.001	0.001	0.000	0.000	0.000	0.000
114	A	112	VAL	0	0.001	-0.001	47.922	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	113	TYR	0	-0.027	-0.031	47.332	0.002	0.002	0.000	0.000	0.000	0.000
116	A	114	ASP	-1	-0.821	-0.898	46.893	-0.072	-0.072	0.000	0.000	0.000	0.000
117	A	115	ILE	0	-0.060	-0.021	43.368	0.001	0.001	0.000	0.000	0.000	0.000
118	A	116	GLY	0	0.032	0.025	47.305	0.000	0.000	0.000	0.000	0.000	0.000
119	A	117	VAL	0	-0.016	-0.011	44.714	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	118	GLU	-1	-0.864	-0.920	47.982	-0.046	-0.046	0.000	0.000	0.000	0.000
121	A	119	ARG	1	0.861	0.907	45.199	0.057	0.057	0.000	0.000	0.000	0.000
122	A	120	ASP	-1	-0.879	-0.936	43.418	-0.060	-0.060	0.000	0.000	0.000	0.000
123	A	121	HIS	0	-0.077	-0.029	45.063	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	122	ASN	0	-0.036	-0.018	40.206	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	123	PHE	0	0.036	0.011	40.087	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	124	ALA	0	0.027	0.017	34.769	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	125	LEU	0	-0.053	-0.014	35.606	0.001	0.001	0.000	0.000	0.000	0.000
128	A	126	LYS	1	1.070	1.010	30.460	0.197	0.197	0.000	0.000	0.000	0.000
129	A	127	ASN	0	-0.012	-0.011	27.607	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	128	GLY	0	0.028	0.033	29.314	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	129	PHE	0	-0.056	-0.021	30.731	0.006	0.006	0.000	0.000	0.000	0.000
132	A	130	ILE	0	0.038	0.016	33.811	0.001	0.001	0.000	0.000	0.000	0.000
133	A	131	ALA	0	-0.025	0.006	36.747	0.004	0.004	0.000	0.000	0.000	0.000
134	A	132	SER	0	-0.023	-0.038	40.162	0.003	0.003	0.000	0.000	0.000	0.000
135	A	133	ASN	0	-0.051	-0.038	43.137	0.001	0.001	0.000	0.000	0.000	0.000
136	A	134	ALA	0	-0.001	0.016	45.632	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)