FMO DATABASE

FMODB ID: PZ26N

Calculation Name: 3S0A-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3S0A

Chain ID: A

ChEMBL ID:

UniProt ID: Q1W640

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	117
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1027023.310342
FMO2-HF: Nuclear repulsion	978256.379304
FMO2-HF: Total energy	-48766.931038
FMO2-MP2: Total energy	-48904.633107

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
-116.714	-107.286	7.396	-4.982	-11.843	-0.052

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.808 / q_NPA : 0.905

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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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	3	ILE	0	0.101	0.046	3.232	-2.578	-0.121	0.044	-0.964	-1.538	-0.003
4	A	4	GLU	-1	-0.810	-0.889	5.930	-23.761	-23.761	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.880	-0.945	2.228	-76.745	-72.936	2.939	-3.010	-3.738	-0.034
6	A	6	LEU	0	-0.001	-0.008	2.990	2.806	4.909	2.956	-1.665	-3.394	-0.007
7	A	7	LYS	1	0.788	0.877	3.741	28.571	27.152	0.106	1.590	-0.277	-0.001
8	A	8	THR	0	0.023	0.016	6.829	3.009	3.009	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.803	0.887	3.329	31.276	32.033	0.048	-0.157	-0.648	0.000
10	A	10	LEU	0	-0.008	-0.019	6.358	2.079	2.079	0.000	0.000	0.000	0.000
11	A	11	HIS	0	-0.009	0.008	7.989	1.311	1.311	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.037	-0.015	9.102	1.688	1.688	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.798	-0.902	7.501	-20.801	-20.801	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.001	-0.015	10.409	1.562	1.562	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.028	-0.004	13.038	1.387	1.387	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.022	0.002	12.647	0.990	0.990	0.000	0.000	0.000	0.000
17	A	49	CYS	0	0.030	0.037	13.568	-0.071	-0.071	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.928	0.978	15.690	12.756	12.756	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.082	-0.042	18.303	0.839	0.839	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.962	-0.969	17.304	-13.186	-13.186	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.051	-0.034	18.792	0.625	0.625	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.020	-0.017	21.433	0.521	0.521	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.075	-0.026	19.550	0.451	0.451	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.883	-0.934	22.888	-9.979	-9.979	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.023	-0.050	19.159	-0.136	-0.136	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.037	-0.008	22.014	-0.189	-0.189	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.937	0.958	23.085	9.620	9.620	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.007	0.000	18.076	-0.307	-0.307	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.049	0.015	18.251	-1.089	-1.089	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.842	-0.905	19.621	-11.478	-11.478	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.035	-0.036	15.837	-0.304	-0.304	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.048	-0.021	14.342	-0.589	-0.589	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.903	-0.960	15.889	-13.438	-13.438	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.014	-0.005	17.942	0.066	0.066	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.060	-0.019	18.700	0.465	0.465	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.028	-0.005	17.865	0.084	0.084	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.853	-0.923	21.692	-9.619	-9.619	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.028	-0.029	22.309	-0.060	-0.060	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.852	-0.926	24.222	-9.513	-9.513	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.801	-0.863	25.081	-9.935	-9.935	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.989	0.983	24.538	9.323	9.323	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.915	0.942	23.314	9.675	9.675	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.069	0.053	20.445	-0.558	-0.558	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.068	-0.044	19.694	-0.571	-0.571	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.070	-0.033	19.424	-0.357	-0.357	0.000	0.000	0.000	0.000
46	A	46	TYR	0	0.018	0.013	15.348	-0.607	-0.607	0.000	0.000	0.000	0.000
47	A	47	CYS	0	-0.021	-0.005	15.350	-0.797	-0.797	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.853	-0.941	14.566	-13.161	-13.161	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.059	0.026	9.689	-0.992	-0.992	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.042	-0.027	9.948	-1.387	-1.387	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.837	0.921	10.884	12.516	12.516	0.000	0.000	0.000	0.000
52	A	53	ASN	0	0.012	0.022	9.660	0.002	0.002	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.052	-0.026	3.080	-2.428	-2.060	0.024	-0.064	-0.329	0.000
54	A	55	ASN	0	-0.092	-0.041	7.413	0.111	0.111	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.023	-0.004	8.086	0.513	0.513	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.038	-0.004	11.356	1.125	1.125	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.829	-0.920	13.954	-14.201	-14.201	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.989	0.969	16.091	12.684	12.684	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.053	-0.025	18.331	0.576	0.576	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.036	-0.030	18.423	0.539	0.539	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.022	0.023	18.894	0.139	0.139	0.000	0.000	0.000	0.000
62	A	63	PHE	0	0.024	0.015	14.397	-0.732	-0.732	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.908	0.961	13.049	16.727	16.727	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.067	0.020	12.961	-1.262	-1.262	0.000	0.000	0.000	0.000
65	A	66	GLN	0	0.001	-0.006	10.686	0.874	0.874	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.030	0.014	8.768	-1.896	-1.896	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.039	0.014	7.893	-1.809	-1.809	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.931	0.968	9.357	18.192	18.192	0.000	0.000	0.000	0.000
69	A	70	ALA	0	-0.018	0.000	5.699	-1.355	-1.355	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.022	0.016	3.736	-5.109	-4.876	0.001	-0.030	-0.204	0.000
71	A	72	MET	0	0.006	-0.010	5.906	-1.446	-1.446	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.918	-0.961	8.562	-26.113	-26.113	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.078	-0.032	2.333	-4.516	-3.396	1.278	-0.682	-1.715	-0.007
74	A	75	LEU	0	-0.062	-0.032	6.540	1.385	1.385	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.044	-0.015	9.670	2.333	2.333	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.790	-0.865	11.987	-19.184	-19.184	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.862	-0.938	13.680	-19.286	-19.286	0.000	0.000	0.000	0.000
78	A	79	ASN	0	-0.039	-0.036	14.492	0.330	0.330	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.003	-0.031	16.170	1.092	1.092	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.007	0.019	11.593	0.570	0.570	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.894	0.945	14.902	17.069	17.069	0.000	0.000	0.000	0.000
82	A	83	GLN	0	-0.018	-0.009	17.805	0.913	0.913	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.058	0.047	13.624	0.505	0.505	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.052	-0.034	14.765	0.428	0.428	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.057	-0.044	17.241	0.719	0.719	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.828	-0.862	20.088	-12.395	-12.395	0.000	0.000	0.000	0.000
87	A	106	CYS	0	-0.086	-0.033	17.285	0.388	0.388	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.049	-0.035	18.415	0.171	0.171	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.040	-0.031	19.423	0.273	0.273	0.000	0.000	0.000	0.000
90	A	91	ILE	0	0.028	0.028	19.960	0.463	0.463	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.017	-0.021	23.589	0.020	0.020	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.831	-0.925	24.508	-9.644	-9.644	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.876	-0.938	25.588	-9.956	-9.956	0.000	0.000	0.000	0.000
94	A	95	ASN	0	-0.026	0.008	26.197	-0.333	-0.333	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.036	0.002	22.389	-0.279	-0.279	0.000	0.000	0.000	0.000
96	A	97	HIS	1	0.872	0.928	21.473	10.676	10.676	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.059	0.044	21.892	-0.370	-0.370	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.936	0.977	20.225	11.674	11.674	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.016	-0.001	17.603	-0.496	-0.496	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.015	-0.017	17.689	-0.584	-0.584	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.921	0.954	19.513	10.007	10.007	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.020	-0.006	15.938	-0.222	-0.222	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.020	0.010	13.767	-0.576	-0.576	0.000	0.000	0.000	0.000
104	A	105	GLN	0	0.018	0.006	15.882	-0.263	-0.263	0.000	0.000	0.000	0.000
105	A	107	VAL	0	0.045	0.006	11.867	-0.174	-0.174	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.043	-0.031	15.147	-0.732	-0.732	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.799	0.903	16.155	13.105	13.105	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.085	-0.055	15.246	0.109	0.109	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.936	0.958	12.233	19.790	19.790	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.038	0.046	13.686	-0.500	-0.500	0.000	0.000	0.000	0.000
111	A	113	MET	0	0.036	0.027	10.463	-1.233	-1.233	0.000	0.000	0.000	0.000
112	A	114	LYS	1	0.915	0.957	12.141	12.888	12.888	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.091	-0.061	13.973	-0.378	-0.378	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.020	0.000	7.702	-0.453	-0.453	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.813	-0.916	11.038	-21.598	-21.598	0.000	0.000	0.000	0.000
116	A	118	PHE	0	-0.155	-0.066	12.654	0.586	0.586	0.000	0.000	0.000	0.000
117	A	119	LEU	-1	-0.903	-0.918	10.693	-23.579	-23.579	0.000	0.000	0.000	0.000

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