FMO DATABASE

FMODB ID: PGQN1

Calculation Name: 1KNG-A-Xray13

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: 2018-02-14

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	145
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1310349.654964
FMO2-HF: Nuclear repulsion	1255974.175132
FMO2-HF: Total energy	-54375.479831
FMO2-MP2: Total energy	-54536.161389

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:49:ACE)

Summations of interaction energy for fragment #1(A:49:ACE)

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.
1.473	3.456	0.2	-0.931	-1.251	-0.003

Interaction energy analysis for fragmet #1(A:49:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.014

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	51	PRO	0	0.006	0.000	3.851	0.802	1.694	-0.012	-0.425	-0.454	0.000
4	A	52	ALA	0	0.043	0.025	7.210	-0.057	-0.057	0.000	0.000	0.000	0.000
5	A	53	PRO	0	-0.017	-0.001	8.783	-0.009	-0.009	0.000	0.000	0.000	0.000
6	A	54	GLN	0	-0.031	-0.023	11.550	0.117	0.117	0.000	0.000	0.000	0.000
7	A	55	THR	0	-0.002	0.009	14.787	0.030	0.030	0.000	0.000	0.000	0.000
8	A	56	ALA	0	0.024	0.013	16.869	0.010	0.010	0.000	0.000	0.000	0.000
9	A	57	LEU	0	-0.076	-0.029	18.777	0.001	0.001	0.000	0.000	0.000	0.000
10	A	58	PRO	0	0.023	0.018	22.042	0.005	0.005	0.000	0.000	0.000	0.000
11	A	59	PRO	0	0.071	0.019	24.810	0.000	0.000	0.000	0.000	0.000	0.000
12	A	60	LEU	0	-0.008	0.007	26.643	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	61	GLU	-1	-0.941	-0.973	28.511	-0.021	-0.021	0.000	0.000	0.000	0.000
14	A	62	GLY	0	0.043	0.016	32.031	0.002	0.002	0.000	0.000	0.000	0.000
15	A	63	LEU	0	-0.054	-0.018	27.152	0.003	0.003	0.000	0.000	0.000	0.000
16	A	64	GLN	0	-0.015	-0.009	31.055	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	65	ALA	0	-0.007	-0.014	29.532	0.003	0.003	0.000	0.000	0.000	0.000
18	A	66	ASP	-1	-0.898	-0.937	31.534	0.012	0.012	0.000	0.000	0.000	0.000
19	A	67	ASN	0	-0.073	-0.041	34.141	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	68	VAL	0	0.026	0.021	31.641	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	69	GLN	0	-0.031	-0.024	29.282	0.003	0.003	0.000	0.000	0.000	0.000
22	A	70	VAL	0	-0.005	0.006	25.713	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	71	PRO	0	-0.019	-0.005	24.736	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	72	GLY	0	0.071	0.035	23.761	0.003	0.003	0.000	0.000	0.000	0.000
25	A	73	LEU	0	-0.035	-0.004	15.985	0.007	0.007	0.000	0.000	0.000	0.000
26	A	74	ASP	-1	-0.840	-0.927	19.922	-0.122	-0.122	0.000	0.000	0.000	0.000
27	A	75	PRO	0	0.022	0.010	15.260	0.015	0.015	0.000	0.000	0.000	0.000
28	A	76	ALA	0	0.016	0.001	15.394	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	77	ALA	0	-0.056	-0.028	17.516	0.016	0.016	0.000	0.000	0.000	0.000
30	A	78	PHE	0	0.013	-0.001	12.328	0.024	0.024	0.000	0.000	0.000	0.000
31	A	79	LYS	1	0.881	0.950	11.639	0.236	0.236	0.000	0.000	0.000	0.000
32	A	80	GLY	0	0.007	0.003	14.291	0.011	0.011	0.000	0.000	0.000	0.000
33	A	81	LYS	1	0.874	0.930	14.894	0.011	0.011	0.000	0.000	0.000	0.000
34	A	82	VAL	0	0.040	0.028	12.530	0.004	0.004	0.000	0.000	0.000	0.000
35	A	83	SER	0	-0.006	-0.005	12.797	-0.035	-0.035	0.000	0.000	0.000	0.000
36	A	84	LEU	0	0.026	0.024	12.619	0.043	0.043	0.000	0.000	0.000	0.000
37	A	85	VAL	0	-0.011	-0.004	12.463	-0.030	-0.030	0.000	0.000	0.000	0.000
38	A	86	ASN	0	-0.004	-0.017	13.937	0.011	0.011	0.000	0.000	0.000	0.000
39	A	87	VAL	0	-0.034	-0.010	14.910	-0.019	-0.019	0.000	0.000	0.000	0.000
40	A	88	TRP	0	0.067	0.023	17.774	0.009	0.009	0.000	0.000	0.000	0.000
41	A	89	ALA	0	0.019	-0.009	21.357	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	90	SER	0	-0.039	-0.045	24.817	0.007	0.007	0.000	0.000	0.000	0.000
43	A	91	TRP	0	-0.045	-0.025	24.321	0.006	0.006	0.000	0.000	0.000	0.000
44	A	95	CYS	0	-0.031	0.025	22.964	0.007	0.007	0.000	0.000	0.000	0.000
45	A	93	VAL	0	0.051	0.027	26.410	0.003	0.003	0.000	0.000	0.000	0.000
46	A	94	PRO	0	0.044	-0.006	22.946	0.002	0.002	0.000	0.000	0.000	0.000
47	A	96	HIS	0	-0.037	-0.003	24.290	0.004	0.004	0.000	0.000	0.000	0.000
48	A	97	ASP	-1	-0.896	-0.934	25.880	0.049	0.049	0.000	0.000	0.000	0.000
49	A	98	GLU	-1	-0.828	-0.926	20.146	0.080	0.080	0.000	0.000	0.000	0.000
50	A	99	ALA	0	-0.024	0.001	24.091	0.004	0.004	0.000	0.000	0.000	0.000
51	A	100	PRO	0	-0.016	-0.021	25.650	0.001	0.001	0.000	0.000	0.000	0.000
52	A	101	LEU	0	0.002	0.008	23.583	0.002	0.002	0.000	0.000	0.000	0.000
53	A	102	LEU	0	0.000	0.001	19.160	0.007	0.007	0.000	0.000	0.000	0.000
54	A	103	THR	0	-0.025	-0.017	23.063	0.000	0.000	0.000	0.000	0.000	0.000
55	A	104	GLU	-1	-0.864	-0.920	26.153	0.057	0.057	0.000	0.000	0.000	0.000
56	A	105	LEU	0	-0.001	0.013	18.532	0.003	0.003	0.000	0.000	0.000	0.000
57	A	106	GLY	0	0.038	0.022	23.122	0.002	0.002	0.000	0.000	0.000	0.000
58	A	107	LYS	1	0.786	0.880	24.112	-0.060	-0.060	0.000	0.000	0.000	0.000
59	A	108	ASP	-1	-0.811	-0.889	22.624	0.106	0.106	0.000	0.000	0.000	0.000
60	A	109	LYS	1	0.891	0.935	22.741	-0.045	-0.045	0.000	0.000	0.000	0.000
61	A	110	ARG	1	0.744	0.860	20.316	-0.134	-0.134	0.000	0.000	0.000	0.000
62	A	111	PHE	0	-0.053	-0.023	16.627	0.011	0.011	0.000	0.000	0.000	0.000
63	A	112	GLN	0	-0.077	-0.037	16.485	-0.022	-0.022	0.000	0.000	0.000	0.000
64	A	113	LEU	0	0.035	0.021	17.169	0.012	0.012	0.000	0.000	0.000	0.000
65	A	114	VAL	0	-0.021	-0.023	16.258	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	115	GLY	0	0.028	0.022	17.531	0.012	0.012	0.000	0.000	0.000	0.000
67	A	116	ILE	0	-0.010	-0.010	15.326	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	117	ASN	0	-0.043	-0.023	19.355	0.005	0.005	0.000	0.000	0.000	0.000
69	A	118	TYR	0	0.041	0.001	19.937	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	119	LYS	1	0.899	0.962	22.504	0.060	0.060	0.000	0.000	0.000	0.000
71	A	120	ASP	-1	-0.725	-0.825	25.621	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	121	ALA	0	-0.004	0.013	28.001	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	122	ALA	0	0.059	0.006	30.710	0.003	0.003	0.000	0.000	0.000	0.000
74	A	123	ASP	-1	-0.838	-0.911	31.739	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	124	ASN	0	-0.036	-0.015	31.737	0.004	0.004	0.000	0.000	0.000	0.000
76	A	125	ALA	0	0.026	0.017	27.892	0.004	0.004	0.000	0.000	0.000	0.000
77	A	126	ARG	1	0.863	0.910	29.584	0.018	0.018	0.000	0.000	0.000	0.000
78	A	127	ARG	1	0.952	0.991	31.971	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	128	PHE	0	-0.016	-0.019	25.763	0.002	0.002	0.000	0.000	0.000	0.000
80	A	129	LEU	0	0.017	-0.003	25.684	0.004	0.004	0.000	0.000	0.000	0.000
81	A	130	GLY	0	-0.012	0.012	29.716	0.002	0.002	0.000	0.000	0.000	0.000
82	A	131	ARG	1	0.816	0.917	32.593	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	132	TYR	0	-0.007	-0.049	29.028	0.002	0.002	0.000	0.000	0.000	0.000
84	A	133	GLY	0	0.012	0.030	30.118	0.005	0.005	0.000	0.000	0.000	0.000
85	A	134	ASN	0	0.033	-0.006	25.985	0.002	0.002	0.000	0.000	0.000	0.000
86	A	135	PRO	0	-0.020	0.010	23.157	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	136	PHE	0	-0.020	-0.016	19.605	0.004	0.004	0.000	0.000	0.000	0.000
88	A	137	GLY	0	0.012	0.008	22.100	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	138	ARG	1	0.875	0.925	19.962	0.037	0.037	0.000	0.000	0.000	0.000
90	A	139	VAL	0	0.036	0.013	21.341	0.006	0.006	0.000	0.000	0.000	0.000
91	A	140	GLY	0	-0.027	-0.002	21.167	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	141	VAL	0	0.012	0.002	21.938	0.004	0.004	0.000	0.000	0.000	0.000
93	A	142	ASP	-1	-0.736	-0.872	19.617	-0.108	-0.108	0.000	0.000	0.000	0.000
94	A	143	ALA	0	0.017	0.000	22.453	0.004	0.004	0.000	0.000	0.000	0.000
95	A	144	ASN	0	0.014	-0.008	23.637	0.000	0.000	0.000	0.000	0.000	0.000
96	A	145	GLY	0	-0.004	0.004	21.024	0.000	0.000	0.000	0.000	0.000	0.000
97	A	146	ARG	1	0.949	0.966	19.578	0.125	0.125	0.000	0.000	0.000	0.000
98	A	147	ALA	0	0.036	0.025	17.255	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	148	SER	0	0.006	-0.027	15.535	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	149	ILE	0	-0.002	0.017	14.722	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	150	GLU	-1	-0.921	-0.954	13.547	-0.317	-0.317	0.000	0.000	0.000	0.000
102	A	151	TRP	0	-0.033	-0.033	9.786	-0.124	-0.124	0.000	0.000	0.000	0.000
103	A	152	GLY	0	-0.066	-0.027	10.256	0.001	0.001	0.000	0.000	0.000	0.000
104	A	153	VAL	0	-0.072	-0.041	11.878	0.043	0.043	0.000	0.000	0.000	0.000
105	A	154	TYR	0	-0.037	-0.015	11.349	0.008	0.008	0.000	0.000	0.000	0.000
106	A	155	GLY	0	-0.024	-0.011	16.705	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	156	VAL	0	-0.066	0.006	17.776	0.005	0.005	0.000	0.000	0.000	0.000
108	A	157	PRO	0	0.027	-0.010	18.864	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	158	GLU	-1	-0.772	-0.908	13.168	0.021	0.021	0.000	0.000	0.000	0.000
110	A	159	THR	0	0.030	0.022	13.384	-0.027	-0.027	0.000	0.000	0.000	0.000
111	A	160	PHE	0	-0.031	-0.015	7.802	0.048	0.048	0.000	0.000	0.000	0.000
112	A	161	VAL	0	0.026	0.019	8.906	-0.055	-0.055	0.000	0.000	0.000	0.000
113	A	162	VAL	0	-0.032	-0.015	7.852	0.135	0.135	0.000	0.000	0.000	0.000
114	A	163	GLY	0	0.071	0.036	8.039	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	164	ARG	1	1.005	1.011	9.615	-0.189	-0.189	0.000	0.000	0.000	0.000
116	A	165	GLU	-1	-0.936	-0.964	8.030	0.111	0.111	0.000	0.000	0.000	0.000
117	A	166	GLY	0	-0.019	-0.012	9.794	-0.106	-0.106	0.000	0.000	0.000	0.000
118	A	167	THR	0	-0.012	-0.001	4.103	-0.130	-0.064	-0.001	-0.014	-0.052	0.000
119	A	168	ILE	0	-0.031	-0.015	4.039	0.180	0.306	0.000	-0.029	-0.097	0.000
120	A	169	VAL	0	-0.005	-0.008	3.144	0.806	1.642	0.214	-0.459	-0.591	-0.003
121	A	170	TYR	0	0.000	-0.009	5.312	0.102	0.165	-0.001	-0.004	-0.057	0.000
122	A	171	LYS	1	0.845	0.939	7.112	-0.209	-0.209	0.000	0.000	0.000	0.000
123	A	172	LEU	0	-0.035	-0.011	8.873	0.049	0.049	0.000	0.000	0.000	0.000
124	A	173	VAL	0	0.025	0.011	12.404	-0.044	-0.044	0.000	0.000	0.000	0.000
125	A	174	GLY	0	0.024	0.015	14.658	0.007	0.007	0.000	0.000	0.000	0.000
126	A	175	PRO	0	-0.014	0.003	17.631	0.008	0.008	0.000	0.000	0.000	0.000
127	A	176	ILE	0	-0.008	-0.019	17.580	0.019	0.019	0.000	0.000	0.000	0.000
128	A	177	THR	0	0.002	-0.002	19.880	-0.012	-0.012	0.000	0.000	0.000	0.000
129	A	178	PRO	0	0.081	0.020	22.049	0.011	0.011	0.000	0.000	0.000	0.000
130	A	179	ASP	-1	-0.847	-0.910	23.124	0.124	0.124	0.000	0.000	0.000	0.000
131	A	180	ASN	0	-0.015	0.001	17.723	0.012	0.012	0.000	0.000	0.000	0.000
132	A	181	LEU	0	0.049	0.019	18.155	0.029	0.029	0.000	0.000	0.000	0.000
133	A	182	ARG	1	0.879	0.921	19.402	-0.099	-0.099	0.000	0.000	0.000	0.000
134	A	183	SER	0	0.018	0.012	20.232	0.004	0.004	0.000	0.000	0.000	0.000
135	A	184	VAL	0	-0.051	-0.016	14.149	0.019	0.019	0.000	0.000	0.000	0.000
136	A	185	LEU	0	-0.011	-0.024	13.046	0.048	0.048	0.000	0.000	0.000	0.000
137	A	186	LEU	0	0.040	0.023	14.973	0.025	0.025	0.000	0.000	0.000	0.000
138	A	187	PRO	0	0.020	0.009	16.471	0.011	0.011	0.000	0.000	0.000	0.000
139	A	188	GLN	0	-0.006	-0.003	11.222	0.037	0.037	0.000	0.000	0.000	0.000
140	A	189	MET	0	-0.050	-0.017	12.439	0.030	0.030	0.000	0.000	0.000	0.000
141	A	190	GLU	-1	-0.858	-0.947	14.184	0.162	0.162	0.000	0.000	0.000	0.000
142	A	191	LYS	1	0.922	0.966	12.983	-0.386	-0.386	0.000	0.000	0.000	0.000
143	A	192	ALA	0	-0.014	0.006	10.830	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	193	LEU	0	-0.079	-0.039	12.245	-0.047	-0.047	0.000	0.000	0.000	0.000
145	A	194	NME	0	-0.037	0.007	15.117	-0.034	-0.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:49:ACE)