FMO DATABASE

FMODB ID: J36Y9

Calculation Name: 3W3C-A-Xray318

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3W3C

Chain ID: A

ChEMBL ID:

UniProt ID: P0A247

Base Structure: X-ray

Registration Date: 2021-09-07

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	118
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-926440.070899
FMO2-HF: Nuclear repulsion	880965.051002
FMO2-HF: Total energy	-45475.019897
FMO2-MP2: Total energy	-45610.993626

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:130:ACE )

Summations of interaction energy for fragment #1(A:130: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.
9.115	-2.208	10.285	3.101	-2.063	-0.021

Interaction energy analysis for fragmet #1(A:130:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.003 / q_NPA : -0.040

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

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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	132	HIS	0	-0.034	-0.013	3.709	1.676	2.533	-0.005	-0.272	-0.581	-0.002
4	A	133	SER	0	0.032	0.027	4.309	0.668	0.767	0.000	-0.010	-0.088	0.000
5	A	134	ILE	0	-0.042	-0.037	6.564	0.133	0.133	0.000	0.000	0.000	0.000
6	A	135	ARG	1	0.936	0.954	6.611	-0.797	-0.797	0.000	0.000	0.000	0.000
7	A	136	GLU	-1	-0.832	-0.881	2.406	6.536	-5.743	10.290	3.383	-1.394	-0.019
8	A	137	LEU	0	-0.006	0.009	7.034	0.008	0.008	0.000	0.000	0.000	0.000
9	A	138	GLY	0	-0.012	-0.017	10.397	0.043	0.043	0.000	0.000	0.000	0.000
10	A	139	ILE	0	-0.002	-0.008	7.110	0.027	0.027	0.000	0.000	0.000	0.000
11	A	140	GLY	0	0.021	0.022	10.398	0.003	0.003	0.000	0.000	0.000	0.000
12	A	141	LEU	0	-0.008	-0.015	11.882	0.017	0.017	0.000	0.000	0.000	0.000
13	A	142	ASN	0	-0.013	-0.008	14.170	0.014	0.014	0.000	0.000	0.000	0.000
14	A	143	PHE	0	0.064	0.026	15.882	0.013	0.013	0.000	0.000	0.000	0.000
15	A	144	LEU	0	-0.005	0.004	18.225	0.003	0.003	0.000	0.000	0.000	0.000
16	A	145	LYS	1	0.903	0.965	17.782	-0.052	-0.052	0.000	0.000	0.000	0.000
17	A	146	VAL	0	-0.026	-0.016	19.182	0.004	0.004	0.000	0.000	0.000	0.000
18	A	147	SER	0	-0.054	-0.024	21.755	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	148	GLY	0	0.022	0.016	24.002	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	149	MET	0	-0.034	0.006	23.966	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	150	SER	0	0.011	0.001	24.361	0.000	0.000	0.000	0.000	0.000	0.000
22	A	151	TYR	0	0.090	0.010	20.984	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	152	LYS	1	0.890	0.952	23.110	0.024	0.024	0.000	0.000	0.000	0.000
24	A	153	ASP	-1	-0.828	-0.920	25.633	-0.045	-0.045	0.000	0.000	0.000	0.000
25	A	154	ILE	0	0.001	0.002	19.440	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	155	ALA	0	-0.047	-0.027	20.963	-0.014	-0.014	0.000	0.000	0.000	0.000
27	A	156	LYS	1	0.952	0.985	22.027	0.060	0.060	0.000	0.000	0.000	0.000
28	A	157	LYS	1	0.925	0.968	22.709	0.063	0.063	0.000	0.000	0.000	0.000
29	A	158	GLU	-1	-0.870	-0.934	18.221	-0.157	-0.157	0.000	0.000	0.000	0.000
30	A	159	ASN	0	-0.057	-0.010	19.910	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	160	LEU	0	0.002	0.003	16.502	-0.017	-0.017	0.000	0.000	0.000	0.000
32	A	161	SER	0	0.026	0.002	19.914	0.020	0.020	0.000	0.000	0.000	0.000
33	A	162	ARG	1	1.046	0.988	20.382	0.040	0.040	0.000	0.000	0.000	0.000
34	A	163	ALA	0	-0.006	0.003	20.991	0.008	0.008	0.000	0.000	0.000	0.000
35	A	164	LYS	1	0.946	0.973	13.947	0.271	0.271	0.000	0.000	0.000	0.000
36	A	165	VAL	0	0.071	0.047	16.159	0.001	0.001	0.000	0.000	0.000	0.000
37	A	166	THR	0	-0.014	-0.001	17.158	0.018	0.018	0.000	0.000	0.000	0.000
38	A	167	ARG	1	0.938	0.955	15.476	0.093	0.093	0.000	0.000	0.000	0.000
39	A	168	ALA	0	0.030	0.031	12.797	0.022	0.022	0.000	0.000	0.000	0.000
40	A	169	PHE	0	0.019	-0.006	12.946	0.041	0.041	0.000	0.000	0.000	0.000
41	A	170	GLN	0	-0.042	-0.005	15.519	0.026	0.026	0.000	0.000	0.000	0.000
42	A	171	ALA	0	0.030	0.016	10.398	0.034	0.034	0.000	0.000	0.000	0.000
43	A	172	ALA	0	-0.033	-0.015	10.827	0.083	0.083	0.000	0.000	0.000	0.000
44	A	173	SER	0	-0.071	-0.035	11.820	0.031	0.031	0.000	0.000	0.000	0.000
45	A	174	VAL	0	-0.029	0.003	12.064	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	175	PRO	0	0.048	0.034	12.291	0.084	0.084	0.000	0.000	0.000	0.000
47	A	176	GLN	0	0.043	0.005	7.614	0.067	0.067	0.000	0.000	0.000	0.000
48	A	177	GLU	-1	-0.900	-0.958	11.626	0.343	0.343	0.000	0.000	0.000	0.000
49	A	178	ILE	0	0.015	0.007	14.597	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	179	ILE	0	-0.030	-0.020	7.960	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	180	SER	0	-0.044	-0.029	11.056	0.079	0.079	0.000	0.000	0.000	0.000
52	A	181	LEU	0	-0.059	-0.008	12.158	-0.046	-0.046	0.000	0.000	0.000	0.000
53	A	182	PHE	0	-0.051	-0.021	11.698	-0.070	-0.070	0.000	0.000	0.000	0.000
54	A	183	PRO	0	0.045	0.029	12.161	0.076	0.076	0.000	0.000	0.000	0.000
55	A	184	ILE	0	0.027	0.008	9.190	0.086	0.086	0.000	0.000	0.000	0.000
56	A	185	ALA	0	0.011	-0.003	5.612	-0.087	-0.087	0.000	0.000	0.000	0.000
57	A	186	SER	0	-0.006	0.006	6.576	-0.078	-0.078	0.000	0.000	0.000	0.000
58	A	187	GLU	-1	-0.845	-0.924	7.628	-0.024	-0.024	0.000	0.000	0.000	0.000
59	A	188	LEU	0	-0.108	-0.039	9.092	-0.056	-0.056	0.000	0.000	0.000	0.000
60	A	189	ASN	0	0.037	0.020	10.425	-0.054	-0.054	0.000	0.000	0.000	0.000
61	A	190	PHE	0	0.009	-0.043	11.427	0.031	0.031	0.000	0.000	0.000	0.000
62	A	191	ASN	0	-0.031	-0.020	14.212	0.013	0.013	0.000	0.000	0.000	0.000
63	A	192	ASP	-1	-0.744	-0.867	13.710	0.099	0.099	0.000	0.000	0.000	0.000
64	A	193	TYR	0	0.052	0.019	7.489	0.073	0.073	0.000	0.000	0.000	0.000
65	A	194	LYS	1	0.921	0.976	14.038	-0.025	-0.025	0.000	0.000	0.000	0.000
66	A	195	ILE	0	-0.054	-0.026	17.566	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	196	LEU	0	0.061	0.030	13.265	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	197	PHE	0	-0.014	-0.004	16.477	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	198	ASN	0	-0.073	-0.058	17.798	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	199	TYR	0	0.007	0.016	19.251	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	200	TYR	0	0.075	0.026	18.368	0.004	0.004	0.000	0.000	0.000	0.000
72	A	201	LYS	1	0.952	0.987	20.429	-0.077	-0.077	0.000	0.000	0.000	0.000
73	A	202	GLY	0	-0.056	-0.033	22.580	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	203	LEU	0	0.037	0.026	21.487	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	204	GLU	-1	-0.890	-0.948	21.721	0.124	0.124	0.000	0.000	0.000	0.000
76	A	205	LYS	1	0.852	0.932	25.159	-0.064	-0.064	0.000	0.000	0.000	0.000
77	A	206	ALA	0	-0.025	-0.005	27.979	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	207	ASN	0	-0.069	-0.036	28.060	0.002	0.002	0.000	0.000	0.000	0.000
79	A	208	GLU	-1	-0.887	-0.932	26.671	0.100	0.100	0.000	0.000	0.000	0.000
80	A	209	SER	0	-0.020	-0.014	24.577	0.009	0.009	0.000	0.000	0.000	0.000
81	A	210	LEU	0	0.064	0.004	18.046	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	211	SER	0	0.004	0.002	22.147	0.001	0.001	0.000	0.000	0.000	0.000
83	A	212	SER	0	-0.030	-0.014	24.004	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	213	THR	0	0.062	0.038	23.113	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	214	LEU	0	-0.057	-0.046	18.240	0.002	0.002	0.000	0.000	0.000	0.000
86	A	215	PRO	0	-0.067	-0.032	22.299	0.005	0.005	0.000	0.000	0.000	0.000
87	A	216	ILE	0	0.103	0.057	24.601	0.000	0.000	0.000	0.000	0.000	0.000
88	A	217	LEU	0	0.018	0.021	21.458	0.001	0.001	0.000	0.000	0.000	0.000
89	A	218	LYS	1	0.911	0.943	19.048	-0.254	-0.254	0.000	0.000	0.000	0.000
90	A	219	GLU	-1	-0.970	-0.994	21.818	0.122	0.122	0.000	0.000	0.000	0.000
91	A	220	GLU	-1	-0.857	-0.938	25.102	0.108	0.108	0.000	0.000	0.000	0.000
92	A	221	ILE	0	-0.071	-0.036	18.722	0.000	0.000	0.000	0.000	0.000	0.000
93	A	222	LYS	1	0.831	0.922	22.337	-0.181	-0.181	0.000	0.000	0.000	0.000
94	A	223	ASP	-1	-0.922	-0.949	24.244	0.099	0.099	0.000	0.000	0.000	0.000
95	A	224	LEU	0	-0.001	0.002	21.788	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	225	ASP	-1	-0.813	-0.914	24.811	0.088	0.088	0.000	0.000	0.000	0.000
97	A	226	THR	0	-0.061	-0.012	22.190	0.015	0.015	0.000	0.000	0.000	0.000
98	A	227	ASN	0	0.018	-0.027	19.822	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	228	LEU	0	-0.079	-0.026	22.936	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	229	PRO	0	-0.066	-0.009	21.698	-0.010	-0.010	0.000	0.000	0.000	0.000
101	A	230	PRO	0	-0.013	-0.006	19.826	0.007	0.007	0.000	0.000	0.000	0.000
102	A	231	ASP	-1	-0.821	-0.922	16.610	0.063	0.063	0.000	0.000	0.000	0.000
103	A	232	ILE	0	-0.076	-0.055	18.072	0.009	0.009	0.000	0.000	0.000	0.000
104	A	233	TYR	0	0.111	0.065	17.274	0.016	0.016	0.000	0.000	0.000	0.000
105	A	234	LYS	1	0.899	0.954	14.129	-0.087	-0.087	0.000	0.000	0.000	0.000
106	A	235	LYS	1	0.898	0.936	17.209	-0.050	-0.050	0.000	0.000	0.000	0.000
107	A	236	GLU	-1	-0.874	-0.935	20.069	0.087	0.087	0.000	0.000	0.000	0.000
108	A	237	ILE	0	0.048	0.035	16.846	0.000	0.000	0.000	0.000	0.000	0.000
109	A	238	LEU	0	-0.070	-0.045	16.425	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	239	ASN	0	-0.084	-0.042	19.768	-0.013	-0.013	0.000	0.000	0.000	0.000
111	A	240	ILE	0	0.016	0.003	22.196	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	241	ILE	0	0.003	0.013	17.871	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	242	LYS	1	0.867	0.928	22.317	-0.073	-0.073	0.000	0.000	0.000	0.000
114	A	243	LYS	1	0.933	0.963	24.811	-0.100	-0.100	0.000	0.000	0.000	0.000
115	A	244	SER	0	0.057	0.050	25.007	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	245	LYS	1	0.953	0.965	25.280	-0.078	-0.078	0.000	0.000	0.000	0.000
117	A	246	ASN	0	-0.128	-0.041	27.131	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	247	NME	0	0.054	0.040	30.155	-0.005	-0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:130:ACE )