FMO DATABASE

FMODB ID: Z2MVN

Calculation Name: 3K63-A-Xray312

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3K63

Chain ID: A

ChEMBL ID:

UniProt ID: Q9PRA0

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	121
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1023590.951263
FMO2-HF: Nuclear repulsion	975281.817073
FMO2-HF: Total energy	-48309.13419
FMO2-MP2: Total energy	-48452.384846

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:132:MET )

Summations of interaction energy for fragment #1(A:132:MET )

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.
-5.713	-0.556	5.391	-2.924	-7.624	-0.01

Interaction energy analysis for fragmet #1(A:132:MET )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.043 / q_NPA : -0.027

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	134	ASP	-1	-0.939	-0.969	3.097	-2.299	-0.028	0.129	-1.174	-1.227	-0.006
4	A	135	PHE	0	0.116	0.040	5.203	0.097	0.097	0.000	0.000	0.000	0.000
5	A	136	LYS	1	0.920	0.941	6.210	0.516	0.516	0.000	0.000	0.000	0.000
6	A	137	LYS	1	0.931	0.966	8.683	1.228	1.228	0.000	0.000	0.000	0.000
7	A	138	ILE	0	0.050	0.048	5.412	0.135	0.135	0.000	0.000	0.000	0.000
8	A	139	VAL	0	0.012	0.013	9.183	0.193	0.193	0.000	0.000	0.000	0.000
9	A	140	ASN	0	-0.047	-0.030	11.159	0.147	0.147	0.000	0.000	0.000	0.000
10	A	141	ASN	0	-0.026	-0.015	12.481	0.027	0.027	0.000	0.000	0.000	0.000
11	A	142	ILE	0	-0.006	0.029	11.256	0.027	0.027	0.000	0.000	0.000	0.000
12	A	143	ARG	1	0.882	0.920	14.514	0.346	0.346	0.000	0.000	0.000	0.000
13	A	144	LEU	0	0.021	0.013	17.840	0.003	0.003	0.000	0.000	0.000	0.000
14	A	145	LYS	1	0.926	0.965	20.008	0.083	0.083	0.000	0.000	0.000	0.000
15	A	146	ASP	-1	-0.927	-0.944	16.205	-0.347	-0.347	0.000	0.000	0.000	0.000
16	A	147	THR	0	-0.065	-0.041	12.036	-0.009	-0.009	0.000	0.000	0.000	0.000
17	A	148	PHE	0	0.013	-0.013	14.257	0.047	0.047	0.000	0.000	0.000	0.000
18	A	149	ASP	-1	-0.762	-0.843	16.748	-0.096	-0.096	0.000	0.000	0.000	0.000
19	A	150	PHE	0	0.008	-0.004	19.580	0.022	0.022	0.000	0.000	0.000	0.000
20	A	151	LYS	1	0.971	1.001	21.968	-0.054	-0.054	0.000	0.000	0.000	0.000
21	A	152	LEU	0	0.001	0.001	24.708	0.010	0.010	0.000	0.000	0.000	0.000
22	A	153	ALA	0	0.000	0.002	27.249	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	154	ALA	0	-0.015	0.002	28.729	0.000	0.000	0.000	0.000	0.000	0.000
24	A	155	PHE	0	-0.032	-0.022	30.691	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	156	PRO	0	-0.015	0.000	29.388	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	157	ASN	0	-0.041	-0.043	29.881	0.000	0.000	0.000	0.000	0.000	0.000
27	A	158	GLN	0	0.028	0.021	31.429	0.000	0.000	0.000	0.000	0.000	0.000
28	A	159	ASN	0	0.040	0.029	29.526	0.007	0.007	0.000	0.000	0.000	0.000
29	A	160	TYR	0	0.011	-0.017	22.803	0.003	0.003	0.000	0.000	0.000	0.000
30	A	161	ASP	-1	-0.871	-0.930	29.560	-0.046	-0.046	0.000	0.000	0.000	0.000
31	A	162	GLN	0	-0.060	-0.028	32.704	0.005	0.005	0.000	0.000	0.000	0.000
32	A	163	LEU	0	-0.062	-0.032	30.428	0.005	0.005	0.000	0.000	0.000	0.000
33	A	164	LEU	0	0.004	-0.010	33.108	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	165	PRO	0	0.008	0.007	31.774	0.005	0.005	0.000	0.000	0.000	0.000
35	A	166	SER	0	-0.009	-0.021	32.485	0.003	0.003	0.000	0.000	0.000	0.000
36	A	167	GLN	0	0.050	0.057	34.448	0.000	0.000	0.000	0.000	0.000	0.000
37	A	168	ILE	0	0.036	0.033	27.984	0.006	0.006	0.000	0.000	0.000	0.000
38	A	169	TYR	0	-0.048	-0.029	30.436	0.007	0.007	0.000	0.000	0.000	0.000
39	A	170	LYS	1	0.928	0.962	31.539	0.008	0.008	0.000	0.000	0.000	0.000
40	A	171	ASN	0	-0.009	-0.026	32.281	0.007	0.007	0.000	0.000	0.000	0.000
41	A	172	TYR	0	0.036	0.032	26.441	0.005	0.005	0.000	0.000	0.000	0.000
42	A	173	TYR	0	-0.028	0.002	27.512	0.010	0.010	0.000	0.000	0.000	0.000
43	A	174	GLN	0	-0.009	-0.006	29.572	0.002	0.002	0.000	0.000	0.000	0.000
44	A	175	GLY	0	-0.001	0.005	25.839	0.009	0.009	0.000	0.000	0.000	0.000
45	A	176	ILE	0	-0.040	-0.022	21.518	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	177	GLU	-1	-0.912	-0.942	21.225	0.104	0.104	0.000	0.000	0.000	0.000
47	A	178	ILE	0	-0.029	-0.028	16.015	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	179	GLN	0	-0.043	-0.030	17.973	0.015	0.015	0.000	0.000	0.000	0.000
49	A	180	GLN	0	-0.049	-0.052	9.201	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	181	HIS	0	-0.025	-0.016	13.912	0.079	0.079	0.000	0.000	0.000	0.000
51	A	182	LYS	1	0.888	0.941	10.244	0.411	0.411	0.000	0.000	0.000	0.000
52	A	183	TYR	0	0.021	0.006	6.234	0.153	0.153	0.000	0.000	0.000	0.000
53	A	184	GLN	0	0.027	0.021	7.009	0.188	0.188	0.000	0.000	0.000	0.000
54	A	185	ASN	0	-0.027	0.000	3.948	-0.677	-0.297	0.059	-0.127	-0.312	0.001
55	A	186	GLU	-1	-0.842	-0.949	2.532	-2.175	-0.799	4.294	-1.613	-4.058	-0.005
56	A	187	LEU	0	-0.022	-0.020	3.378	-0.604	-0.902	0.006	0.501	-0.209	0.000
57	A	188	ASP	-1	-0.876	-0.915	6.711	0.436	0.436	0.000	0.000	0.000	0.000
58	A	189	ILE	0	0.010	0.007	9.848	-0.091	-0.091	0.000	0.000	0.000	0.000
59	A	190	LYS	1	0.902	0.957	13.191	-0.158	-0.158	0.000	0.000	0.000	0.000
60	A	191	ILE	0	0.012	0.011	16.399	-0.028	-0.028	0.000	0.000	0.000	0.000
61	A	192	ILE	0	-0.039	-0.024	18.936	0.015	0.015	0.000	0.000	0.000	0.000
62	A	193	ASN	0	-0.035	-0.028	21.549	0.004	0.004	0.000	0.000	0.000	0.000
63	A	194	PHE	0	0.042	0.033	24.185	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	195	LEU	0	-0.025	-0.025	26.544	0.005	0.005	0.000	0.000	0.000	0.000
65	A	196	TYR	0	0.057	0.035	28.948	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	197	PRO	0	-0.010	-0.021	29.548	0.001	0.001	0.000	0.000	0.000	0.000
67	A	198	ASP	-1	-0.801	-0.882	31.010	-0.059	-0.059	0.000	0.000	0.000	0.000
68	A	199	GLY	0	-0.043	-0.011	33.434	0.003	0.003	0.000	0.000	0.000	0.000
69	A	200	ASP	-1	-0.909	-0.974	34.896	-0.027	-0.027	0.000	0.000	0.000	0.000
70	A	201	PHE	0	0.032	-0.006	36.239	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	202	GLY	0	0.027	0.034	37.293	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	203	SER	0	-0.078	-0.056	36.806	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	204	ALA	0	-0.007	-0.007	33.244	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	205	ASN	0	-0.003	-0.023	34.848	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	206	LYS	1	0.914	0.969	37.012	0.037	0.037	0.000	0.000	0.000	0.000
76	A	207	ASN	0	0.025	0.019	34.109	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	208	GLY	0	0.025	0.047	33.499	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	209	THR	0	-0.101	-0.075	28.998	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	210	LEU	0	-0.024	-0.012	27.364	0.009	0.009	0.000	0.000	0.000	0.000
80	A	211	LYS	1	0.931	0.990	25.388	0.058	0.058	0.000	0.000	0.000	0.000
81	A	212	LEU	0	0.013	-0.006	20.739	0.013	0.013	0.000	0.000	0.000	0.000
82	A	213	SER	0	-0.016	0.000	21.508	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	214	LEU	0	0.008	-0.014	16.257	0.015	0.015	0.000	0.000	0.000	0.000
84	A	215	MET	0	-0.009	-0.004	14.818	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	216	LEU	0	-0.045	-0.026	11.000	0.012	0.012	0.000	0.000	0.000	0.000
86	A	217	THR	0	0.021	0.015	8.305	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	218	ASP	-1	-0.837	-0.904	5.058	-0.636	-0.597	0.000	-0.001	-0.038	0.000
88	A	219	LYS	1	0.930	0.940	3.485	-0.923	-0.676	0.006	-0.037	-0.216	0.000
89	A	220	LYS	1	0.930	0.992	2.347	-2.103	-1.123	0.885	-0.440	-1.424	0.000
90	A	221	ASN	0	-0.102	-0.080	3.928	0.121	0.283	0.012	-0.033	-0.140	0.000
91	A	222	ASN	0	0.030	0.023	6.990	0.064	0.064	0.000	0.000	0.000	0.000
92	A	223	GLN	0	-0.048	-0.021	8.768	0.008	0.008	0.000	0.000	0.000	0.000
93	A	224	VAL	0	0.018	0.013	10.221	-0.047	-0.047	0.000	0.000	0.000	0.000
94	A	225	TYR	0	-0.029	-0.019	9.768	-0.012	-0.012	0.000	0.000	0.000	0.000
95	A	226	TYR	0	0.040	0.019	14.213	0.009	0.009	0.000	0.000	0.000	0.000
96	A	227	LYS	1	0.922	0.955	15.485	0.207	0.207	0.000	0.000	0.000	0.000
97	A	228	LEU	0	0.014	0.028	18.145	0.013	0.013	0.000	0.000	0.000	0.000
98	A	229	LEU	0	-0.037	-0.023	18.378	-0.022	-0.022	0.000	0.000	0.000	0.000
99	A	230	GLU	-1	-0.923	-0.961	21.423	-0.079	-0.079	0.000	0.000	0.000	0.000
100	A	231	VAL	0	-0.032	-0.006	22.390	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	232	SER	0	0.062	0.021	25.408	0.011	0.011	0.000	0.000	0.000	0.000
102	A	233	GLY	0	-0.030	-0.019	27.730	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	234	PHE	0	-0.058	-0.021	25.921	0.005	0.005	0.000	0.000	0.000	0.000
104	A	235	LYS	1	0.970	0.996	31.445	0.022	0.022	0.000	0.000	0.000	0.000
105	A	236	SER	0	0.019	-0.011	35.122	0.001	0.001	0.000	0.000	0.000	0.000
106	A	237	ASN	0	-0.033	-0.027	37.568	0.002	0.002	0.000	0.000	0.000	0.000
107	A	238	PRO	0	0.031	0.016	41.259	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	239	TYR	0	0.017	0.004	43.244	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	240	GLY	0	-0.001	-0.015	40.556	0.001	0.001	0.000	0.000	0.000	0.000
110	A	241	VAL	0	-0.036	-0.005	41.326	0.001	0.001	0.000	0.000	0.000	0.000
111	A	242	ASP	-1	-0.886	-0.940	39.949	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	243	GLU	-1	-0.826	-0.939	38.391	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	244	ASN	0	-0.069	-0.027	41.423	0.002	0.002	0.000	0.000	0.000	0.000
114	A	245	GLY	0	-0.013	-0.006	44.309	0.001	0.001	0.000	0.000	0.000	0.000
115	A	246	THR	0	0.018	0.024	43.891	0.000	0.000	0.000	0.000	0.000	0.000
116	A	247	ILE	0	0.023	0.006	44.775	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	248	PRO	0	-0.066	-0.039	42.575	0.001	0.001	0.000	0.000	0.000	0.000
118	A	249	GLY	0	-0.009	-0.003	44.686	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	250	LEU	0	-0.041	-0.010	47.047	0.000	0.000	0.000	0.000	0.000	0.000
120	A	251	GLU	-1	-0.952	-0.971	49.414	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	1	NME	0	-0.018	0.002	47.700	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:132:MET )