FMO DATABASE

FMODB ID: VQ9G1

Calculation Name: 1KNG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1KNG

Chain ID: A

ChEMBL ID:

UniProt ID: P30960

Base Structure: X-ray

Registration Date: 2023-09-23

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	143
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1308667.091095
FMO2-HF: Nuclear repulsion	1254462.044968
FMO2-HF: Total energy	-54205.046126
FMO2-MP2: Total energy	-54365.344338

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:50:ARG)

Summations of interaction energy for fragment #1(A:50:ARG)

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.
-87.705	-82.544	23.45	-11.974	-16.64	-0.134

Interaction energy analysis for fragmet #1(A:50:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.910 / q_NPA : 0.963

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	52	ALA	0	0.021	0.020	2.697	-15.164	-11.459	0.741	-2.204	-2.242	-0.011
4	A	53	PRO	0	-0.004	0.002	2.503	2.885	3.927	1.595	-0.605	-2.032	0.002
5	A	54	GLN	0	-0.038	-0.029	5.167	7.830	7.894	-0.001	-0.006	-0.057	0.000
6	A	55	THR	0	-0.018	-0.004	6.584	1.562	1.562	0.000	0.000	0.000	0.000
7	A	56	ALA	0	0.016	0.011	9.245	0.493	0.493	0.000	0.000	0.000	0.000
8	A	57	LEU	0	-0.063	-0.029	11.097	-0.569	-0.569	0.000	0.000	0.000	0.000
9	A	58	PRO	0	0.016	0.015	14.698	0.544	0.544	0.000	0.000	0.000	0.000
10	A	59	PRO	0	0.066	0.021	17.902	-0.722	-0.722	0.000	0.000	0.000	0.000
11	A	60	LEU	0	-0.026	-0.006	20.275	0.247	0.247	0.000	0.000	0.000	0.000
12	A	61	GLU	-1	-0.886	-0.936	21.774	-11.451	-11.451	0.000	0.000	0.000	0.000
13	A	62	GLY	0	0.012	0.012	25.219	0.103	0.103	0.000	0.000	0.000	0.000
14	A	63	LEU	0	-0.056	-0.015	22.343	0.307	0.307	0.000	0.000	0.000	0.000
15	A	64	GLN	0	0.002	-0.007	25.980	-0.057	-0.057	0.000	0.000	0.000	0.000
16	A	65	ALA	0	-0.014	-0.009	26.135	-0.124	-0.124	0.000	0.000	0.000	0.000
17	A	66	ASP	-1	-0.915	-0.952	28.154	-10.826	-10.826	0.000	0.000	0.000	0.000
18	A	67	ASN	0	-0.067	-0.030	31.331	0.377	0.377	0.000	0.000	0.000	0.000
19	A	68	VAL	0	0.003	0.006	28.367	0.174	0.174	0.000	0.000	0.000	0.000
20	A	69	GLN	0	-0.021	-0.024	23.726	0.214	0.214	0.000	0.000	0.000	0.000
21	A	70	VAL	0	-0.004	0.002	21.123	-0.206	-0.206	0.000	0.000	0.000	0.000
22	A	71	PRO	0	0.010	0.008	20.609	-0.202	-0.202	0.000	0.000	0.000	0.000
23	A	72	GLY	0	0.065	0.030	18.093	-0.425	-0.425	0.000	0.000	0.000	0.000
24	A	73	LEU	0	-0.021	0.000	10.161	0.094	0.094	0.000	0.000	0.000	0.000
25	A	74	ASP	-1	-0.783	-0.893	13.937	-18.991	-18.991	0.000	0.000	0.000	0.000
26	A	75	PRO	0	0.019	0.016	10.478	0.072	0.072	0.000	0.000	0.000	0.000
27	A	76	ALA	0	0.012	0.005	11.851	-0.537	-0.537	0.000	0.000	0.000	0.000
28	A	77	ALA	0	-0.011	0.000	14.194	0.713	0.713	0.000	0.000	0.000	0.000
29	A	78	PHE	0	0.021	0.004	9.526	0.328	0.328	0.000	0.000	0.000	0.000
30	A	79	LYS	1	0.901	0.956	10.020	24.732	24.732	0.000	0.000	0.000	0.000
31	A	80	GLY	0	0.006	0.002	13.920	1.138	1.138	0.000	0.000	0.000	0.000
32	A	81	LYS	1	0.846	0.926	14.712	18.757	18.757	0.000	0.000	0.000	0.000
33	A	82	VAL	0	0.030	0.040	12.947	-1.311	-1.311	0.000	0.000	0.000	0.000
34	A	83	SER	0	-0.014	-0.003	11.685	1.360	1.360	0.000	0.000	0.000	0.000
35	A	84	LEU	0	-0.011	0.003	12.029	-1.378	-1.378	0.000	0.000	0.000	0.000
36	A	85	VAL	0	0.001	-0.001	9.120	1.012	1.012	0.000	0.000	0.000	0.000
37	A	86	ASN	0	-0.021	-0.025	10.462	-1.201	-1.201	0.000	0.000	0.000	0.000
38	A	87	VAL	0	-0.016	-0.008	8.763	0.281	0.281	0.000	0.000	0.000	0.000
39	A	88	TRP	0	0.056	0.008	12.208	1.185	1.185	0.000	0.000	0.000	0.000
40	A	89	ALA	0	0.008	-0.009	15.772	-0.225	-0.225	0.000	0.000	0.000	0.000
41	A	90	SER	0	-0.051	-0.064	18.749	0.532	0.532	0.000	0.000	0.000	0.000
42	A	91	TRP	0	-0.018	-0.020	16.735	0.452	0.452	0.000	0.000	0.000	0.000
43	A	92	CYS	0	-0.064	0.006	17.650	-0.459	-0.459	0.000	0.000	0.000	0.000
44	A	93	VAL	0	0.028	0.012	20.400	0.050	0.050	0.000	0.000	0.000	0.000
45	A	94	PRO	0	0.056	0.018	19.215	0.160	0.160	0.000	0.000	0.000	0.000
46	A	96	HIS	0	-0.018	0.003	19.775	0.431	0.431	0.000	0.000	0.000	0.000
47	A	97	ASP	-1	-0.896	-0.947	22.558	-12.388	-12.388	0.000	0.000	0.000	0.000
48	A	98	GLU	-1	-0.802	-0.890	16.965	-17.825	-17.825	0.000	0.000	0.000	0.000
49	A	99	ALA	0	-0.010	0.010	21.445	-0.062	-0.062	0.000	0.000	0.000	0.000
50	A	100	PRO	0	0.008	-0.002	22.541	0.063	0.063	0.000	0.000	0.000	0.000
51	A	101	LEU	0	0.005	0.003	22.248	0.184	0.184	0.000	0.000	0.000	0.000
52	A	102	LEU	0	-0.012	0.002	17.025	-0.205	-0.205	0.000	0.000	0.000	0.000
53	A	103	THR	0	-0.033	-0.035	21.140	-0.288	-0.288	0.000	0.000	0.000	0.000
54	A	104	GLU	-1	-0.859	-0.908	24.416	-10.632	-10.632	0.000	0.000	0.000	0.000
55	A	105	LEU	0	-0.003	0.000	18.480	0.091	0.091	0.000	0.000	0.000	0.000
56	A	106	GLY	0	0.035	0.018	22.226	-0.162	-0.162	0.000	0.000	0.000	0.000
57	A	107	LYS	1	0.753	0.864	23.045	11.123	11.123	0.000	0.000	0.000	0.000
58	A	108	ASP	-1	-0.801	-0.881	22.404	-12.786	-12.786	0.000	0.000	0.000	0.000
59	A	109	LYS	1	0.873	0.920	22.248	11.855	11.855	0.000	0.000	0.000	0.000
60	A	110	ARG	1	0.732	0.839	20.705	13.027	13.027	0.000	0.000	0.000	0.000
61	A	111	PHE	0	-0.031	-0.016	16.879	-0.695	-0.695	0.000	0.000	0.000	0.000
62	A	112	GLN	0	-0.051	-0.044	14.508	1.408	1.408	0.000	0.000	0.000	0.000
63	A	113	LEU	0	0.027	0.018	15.616	-1.581	-1.581	0.000	0.000	0.000	0.000
64	A	114	VAL	0	-0.031	-0.021	13.314	0.694	0.694	0.000	0.000	0.000	0.000
65	A	115	GLY	0	0.010	0.016	14.247	-0.682	-0.682	0.000	0.000	0.000	0.000
66	A	116	ILE	0	-0.029	-0.023	9.250	-0.154	-0.154	0.000	0.000	0.000	0.000
67	A	117	ASN	0	-0.037	-0.012	13.353	0.227	0.227	0.000	0.000	0.000	0.000
68	A	118	TYR	0	0.036	0.015	11.201	-0.019	-0.019	0.000	0.000	0.000	0.000
69	A	119	LYS	1	0.872	0.939	13.617	21.501	21.501	0.000	0.000	0.000	0.000
70	A	120	ASP	-1	-0.725	-0.811	17.202	-13.583	-13.583	0.000	0.000	0.000	0.000
71	A	121	ALA	0	0.012	0.019	20.185	0.009	0.009	0.000	0.000	0.000	0.000
72	A	122	ALA	0	0.055	0.014	23.098	0.037	0.037	0.000	0.000	0.000	0.000
73	A	123	ASP	-1	-0.797	-0.886	24.025	-10.914	-10.914	0.000	0.000	0.000	0.000
74	A	124	ASN	0	-0.027	-0.011	24.555	0.558	0.558	0.000	0.000	0.000	0.000
75	A	125	ALA	0	0.021	0.013	21.460	0.044	0.044	0.000	0.000	0.000	0.000
76	A	126	ARG	1	0.833	0.883	23.255	11.489	11.489	0.000	0.000	0.000	0.000
77	A	127	ARG	1	0.932	0.972	26.112	10.523	10.523	0.000	0.000	0.000	0.000
78	A	128	PHE	0	-0.037	-0.028	20.776	0.369	0.369	0.000	0.000	0.000	0.000
79	A	129	LEU	0	0.019	0.007	21.013	0.104	0.104	0.000	0.000	0.000	0.000
80	A	130	GLY	0	-0.007	0.003	25.051	0.270	0.270	0.000	0.000	0.000	0.000
81	A	131	ARG	1	0.831	0.921	27.952	10.767	10.767	0.000	0.000	0.000	0.000
82	A	132	TYR	0	-0.023	-0.036	24.607	0.544	0.544	0.000	0.000	0.000	0.000
83	A	133	GLY	0	0.035	0.049	26.848	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	134	ASN	0	0.026	-0.012	22.150	-0.895	-0.895	0.000	0.000	0.000	0.000
85	A	135	PRO	0	-0.008	0.009	19.994	0.279	0.279	0.000	0.000	0.000	0.000
86	A	136	PHE	0	-0.022	-0.012	16.549	-0.534	-0.534	0.000	0.000	0.000	0.000
87	A	137	GLY	0	0.034	0.018	19.546	0.705	0.705	0.000	0.000	0.000	0.000
88	A	138	ARG	1	0.765	0.855	16.698	18.457	18.457	0.000	0.000	0.000	0.000
89	A	139	VAL	0	0.025	0.008	16.918	-0.693	-0.693	0.000	0.000	0.000	0.000
90	A	140	GLY	0	-0.010	0.005	14.497	0.627	0.627	0.000	0.000	0.000	0.000
91	A	141	VAL	0	0.012	0.000	15.463	-0.264	-0.264	0.000	0.000	0.000	0.000
92	A	142	ASP	-1	-0.731	-0.852	10.562	-26.502	-26.502	0.000	0.000	0.000	0.000
93	A	143	ALA	0	0.010	-0.009	13.848	-0.014	-0.014	0.000	0.000	0.000	0.000
94	A	144	ASN	0	-0.020	-0.015	13.810	-0.495	-0.495	0.000	0.000	0.000	0.000
95	A	145	GLY	0	0.021	-0.004	11.727	0.369	0.369	0.000	0.000	0.000	0.000
96	A	146	ARG	1	0.900	0.944	9.704	23.436	23.436	0.000	0.000	0.000	0.000
97	A	147	ALA	0	0.046	0.026	7.789	-3.335	-3.335	0.000	0.000	0.000	0.000
98	A	148	SER	0	0.016	-0.033	5.974	-6.393	-6.393	0.000	0.000	0.000	0.000
99	A	149	ILE	0	-0.028	-0.008	5.573	-4.858	-4.858	0.000	0.000	0.000	0.000
100	A	150	GLU	-1	-0.869	-0.915	3.934	-42.675	-41.717	0.000	-0.539	-0.419	-0.002
101	A	151	TRP	0	-0.009	-0.022	1.855	-50.399	-53.544	15.989	-6.786	-6.059	-0.091
102	A	152	GLY	0	-0.048	-0.011	2.246	-12.230	-13.033	4.078	-0.615	-2.661	-0.033
103	A	153	VAL	0	-0.068	-0.034	3.977	5.226	5.348	0.003	-0.017	-0.108	0.000
104	A	154	TYR	0	-0.030	-0.022	7.143	1.062	1.062	0.000	0.000	0.000	0.000
105	A	155	GLY	0	-0.019	-0.011	10.234	2.159	2.159	0.000	0.000	0.000	0.000
106	A	156	VAL	0	-0.042	0.005	11.720	-1.499	-1.499	0.000	0.000	0.000	0.000
107	A	157	PRO	0	0.043	0.008	14.224	1.119	1.119	0.000	0.000	0.000	0.000
108	A	158	GLU	-1	-0.759	-0.888	7.898	-33.854	-33.854	0.000	0.000	0.000	0.000
109	A	159	THR	0	-0.006	-0.003	10.954	0.712	0.712	0.000	0.000	0.000	0.000
110	A	160	PHE	0	-0.007	0.000	3.855	-1.334	-1.157	-0.001	-0.020	-0.157	0.000
111	A	161	VAL	0	0.018	0.001	8.791	2.758	2.758	0.000	0.000	0.000	0.000
112	A	162	VAL	0	-0.042	-0.023	7.128	-3.432	-3.432	0.000	0.000	0.000	0.000
113	A	163	GLY	0	0.084	0.042	7.823	3.071	3.071	0.000	0.000	0.000	0.000
114	A	164	ARG	1	0.900	0.942	9.543	15.064	15.064	0.000	0.000	0.000	0.000
115	A	165	GLU	-1	-0.813	-0.907	7.981	-23.629	-23.629	0.000	0.000	0.000	0.000
116	A	166	GLY	0	-0.042	-0.004	8.773	-0.247	-0.247	0.000	0.000	0.000	0.000
117	A	167	THR	0	-0.037	-0.026	4.287	-4.485	-4.272	-0.001	-0.061	-0.151	0.000
118	A	168	ILE	0	-0.008	-0.011	2.477	1.493	3.736	1.038	-0.882	-2.400	0.002
119	A	169	VAL	0	-0.004	0.006	3.630	-1.530	-0.945	0.009	-0.239	-0.354	-0.001
120	A	170	TYR	0	-0.015	-0.014	6.346	2.762	2.762	0.000	0.000	0.000	0.000
121	A	171	LYS	1	0.788	0.897	5.658	35.366	35.366	0.000	0.000	0.000	0.000
122	A	172	LEU	0	-0.033	0.008	9.112	1.925	1.925	0.000	0.000	0.000	0.000
123	A	173	VAL	0	0.016	-0.007	9.936	-1.547	-1.547	0.000	0.000	0.000	0.000
124	A	174	GLY	0	0.023	0.025	12.462	1.363	1.363	0.000	0.000	0.000	0.000
125	A	175	PRO	0	-0.002	-0.003	15.187	-0.812	-0.812	0.000	0.000	0.000	0.000
126	A	176	ILE	0	0.014	0.000	16.264	0.162	0.162	0.000	0.000	0.000	0.000
127	A	177	THR	0	0.003	-0.007	18.699	0.661	0.661	0.000	0.000	0.000	0.000
128	A	178	PRO	0	0.067	0.012	22.178	-0.269	-0.269	0.000	0.000	0.000	0.000
129	A	179	ASP	-1	-0.850	-0.902	24.157	-11.581	-11.581	0.000	0.000	0.000	0.000
130	A	180	ASN	0	-0.002	-0.002	18.461	-0.118	-0.118	0.000	0.000	0.000	0.000
131	A	181	LEU	0	0.044	0.026	18.983	-0.692	-0.692	0.000	0.000	0.000	0.000
132	A	182	ARG	1	0.854	0.896	20.393	11.085	11.085	0.000	0.000	0.000	0.000
133	A	183	SER	0	0.000	-0.004	21.592	0.187	0.187	0.000	0.000	0.000	0.000
134	A	184	VAL	0	-0.042	-0.010	15.220	-0.128	-0.128	0.000	0.000	0.000	0.000
135	A	185	LEU	0	0.005	-0.003	14.050	-0.586	-0.586	0.000	0.000	0.000	0.000
136	A	186	LEU	0	0.050	0.029	15.832	-0.539	-0.539	0.000	0.000	0.000	0.000
137	A	187	PRO	0	0.037	0.021	17.758	-0.244	-0.244	0.000	0.000	0.000	0.000
138	A	188	GLN	0	-0.024	-0.015	11.512	0.895	0.895	0.000	0.000	0.000	0.000
139	A	189	MET	0	-0.035	-0.010	13.452	-0.755	-0.755	0.000	0.000	0.000	0.000
140	A	190	GLU	-1	-0.809	-0.902	14.850	-13.093	-13.093	0.000	0.000	0.000	0.000
141	A	191	LYS	1	0.882	0.953	14.129	15.323	15.323	0.000	0.000	0.000	0.000
142	A	192	ALA	0	0.007	0.012	11.568	0.136	0.136	0.000	0.000	0.000	0.000
143	A	193	LEU	0	-0.075	-0.008	13.084	0.459	0.459	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:50:ARG)