FMO DATABASE

FMODB ID: P5NGZ

Calculation Name: 2PRX-A-Xray32

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PRX

Chain ID: A

ChEMBL ID:

UniProt ID: A3QJH3

Base Structure: X-ray

Registration Date: 2018-09-07

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	Apo structure with with a 3 angstrom solvent shell.
Procedure	Auto-FMO protocol ver. 1.20180227

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge	CYM=-1
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1011496.025775
FMO2-HF: Nuclear repulsion	963392.583489
FMO2-HF: Total energy	-48103.442286
FMO2-MP2: Total energy	-48241.286788

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:5:ACE)

Summations of interaction energy for fragment #1(A:5: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.
20.208	-7.138	52.683	-15.952	-9.384	-0.06

Interaction energy analysis for fragmet #1(A:5:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / q_NPA : -0.078

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	7	GLN	0	0.089	0.030	3.495	1.163	1.627	-0.054	0.359	-0.768	0.005
4	A	8	ASP	-1	-0.862	-0.897	6.128	-0.313	-0.313	0.000	0.000	0.000	0.000
5	A	9	ALA	0	-0.081	-0.030	4.812	0.152	0.152	0.000	0.000	0.000	0.000
6	A	10	TYR	0	0.012	-0.020	2.232	1.013	0.824	4.107	-2.150	-1.769	-0.012
7	A	11	PRO	0	0.037	0.025	6.811	0.038	0.038	0.000	0.000	0.000	0.000
8	A	12	ASP	-1	-0.878	-0.962	6.283	0.911	0.911	0.000	0.000	0.000	0.000
9	A	13	ASP	-1	-0.961	-0.997	5.730	0.351	0.351	0.000	0.000	0.000	0.000
10	A	14	LEU	0	-0.009	0.035	6.620	-0.118	-0.118	0.000	0.000	0.000	0.000
11	A	15	SER	0	0.013	0.019	10.309	0.041	0.041	0.000	0.000	0.000	0.000
12	A	16	HIS	0	-0.108	-0.101	11.718	-0.055	-0.055	0.000	0.000	0.000	0.000
13	A	17	CYM	-1	-0.803	-0.831	10.817	-0.036	-0.036	0.000	0.000	0.000	0.000
14	A	18	TYR	0	-0.100	-0.078	12.805	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	19	GLY	0	0.083	0.035	8.945	-0.047	-0.047	0.000	0.000	0.000	0.000
16	A	20	NME	0	-0.040	-0.009	9.373	-0.012	-0.012	0.000	0.000	0.000	0.000
17	A	29	ACE	0	-0.060	-0.065	13.480	0.012	0.012	0.000	0.000	0.000	0.000
18	A	30	LEU	0	-0.007	-0.023	9.487	0.026	0.026	0.000	0.000	0.000	0.000
19	A	31	LYS	1	0.820	0.907	8.822	0.522	0.522	0.000	0.000	0.000	0.000
20	A	32	SER	0	-0.019	-0.008	5.160	0.283	0.283	0.000	0.000	0.000	0.000
21	A	33	TYR	0	0.021	0.011	6.172	-0.547	-0.547	0.000	0.000	0.000	0.000
22	A	34	TRP	0	0.002	0.000	5.276	-0.086	-0.086	0.000	0.000	0.000	0.000
23	A	35	ARG	1	0.920	0.957	7.651	0.416	0.416	0.000	0.000	0.000	0.000
24	A	36	GLY	0	-0.008	-0.002	11.025	0.078	0.078	0.000	0.000	0.000	0.000
25	A	37	GLU	-1	-0.930	-0.969	10.620	-0.118	-0.118	0.000	0.000	0.000	0.000
26	A	38	GLN	0	0.000	0.011	10.143	0.028	0.028	0.000	0.000	0.000	0.000
27	A	39	THR	0	-0.034	-0.023	4.818	-0.037	-0.037	0.000	0.000	0.000	0.000
28	A	40	ILE	0	-0.042	-0.044	7.789	0.224	0.224	0.000	0.000	0.000	0.000
29	A	41	ALA	0	0.008	-0.002	8.895	-0.275	-0.275	0.000	0.000	0.000	0.000
30	A	42	HIS	0	0.034	0.006	10.978	0.061	0.061	0.000	0.000	0.000	0.000
31	A	43	PHE	0	-0.004	-0.007	14.263	-0.019	-0.019	0.000	0.000	0.000	0.000
32	A	44	MET	0	0.012	0.035	16.582	0.030	0.030	0.000	0.000	0.000	0.000
33	A	45	PRO	0	-0.004	0.001	20.207	0.007	0.007	0.000	0.000	0.000	0.000
34	A	46	LYS	1	0.975	0.997	21.391	0.136	0.136	0.000	0.000	0.000	0.000
35	A	47	PRO	0	0.052	0.016	24.223	0.004	0.004	0.000	0.000	0.000	0.000
36	A	48	PHE	0	0.019	0.001	24.357	0.004	0.004	0.000	0.000	0.000	0.000
37	A	49	HIS	0	-0.004	0.019	21.038	0.004	0.004	0.000	0.000	0.000	0.000
38	A	50	THR	0	-0.031	-0.053	25.146	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	51	ALA	0	-0.001	0.016	27.166	0.003	0.003	0.000	0.000	0.000	0.000
40	A	52	ILE	0	-0.004	-0.002	28.745	0.006	0.006	0.000	0.000	0.000	0.000
41	A	53	PRO	0	0.025	-0.019	31.083	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	54	GLY	0	0.033	0.026	31.655	0.002	0.002	0.000	0.000	0.000	0.000
43	A	55	PHE	0	0.003	0.002	28.002	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	56	VAL	0	0.004	-0.005	21.839	0.003	0.003	0.000	0.000	0.000	0.000
45	A	57	TYR	0	-0.041	-0.009	23.045	0.006	0.006	0.000	0.000	0.000	0.000
46	A	58	GLY	0	0.093	0.031	22.431	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	59	GLY	0	0.019	-0.004	21.066	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	60	LEU	0	0.021	0.049	17.739	0.004	0.004	0.000	0.000	0.000	0.000
49	A	61	ILE	0	0.008	0.007	17.385	-0.018	-0.018	0.000	0.000	0.000	0.000
50	A	62	ALA	0	-0.007	-0.014	16.637	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	63	SER	0	-0.037	-0.047	15.454	0.014	0.014	0.000	0.000	0.000	0.000
52	A	64	LEU	0	0.008	0.006	12.875	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	65	ILE	0	0.021	-0.004	11.663	-0.063	-0.063	0.000	0.000	0.000	0.000
54	A	66	ASP	-1	-0.868	-0.921	11.022	0.072	0.072	0.000	0.000	0.000	0.000
55	A	67	CYS	0	0.057	0.023	8.751	0.055	0.055	0.000	0.000	0.000	0.000
56	A	68	HIS	0	0.021	0.020	6.925	-0.227	-0.227	0.000	0.000	0.000	0.000
57	A	69	GLY	0	0.013	0.027	6.342	-0.153	-0.153	0.000	0.000	0.000	0.000
58	A	70	THR	0	0.012	-0.004	5.833	0.272	0.272	0.000	0.000	0.000	0.000
59	A	71	GLY	0	0.004	0.009	2.936	0.467	0.761	0.154	-0.160	-0.288	0.000
60	A	72	SER	0	-0.011	-0.018	2.097	8.421	-0.596	19.487	-7.326	-3.143	-0.037
61	A	73	ALA	0	-0.038	-0.007	4.048	0.426	0.626	0.001	-0.058	-0.143	0.000
62	A	74	SER	0	-0.058	-0.103	2.479	-0.893	-0.613	0.531	-0.424	-0.387	-0.001
63	A	75	ALA	0	0.022	0.068	1.985	8.083	-5.876	27.695	-10.864	-2.872	-0.009
64	A	76	ALA	0	-0.031	-0.017	2.861	3.179	-2.240	0.762	4.671	-0.014	-0.006
65	A	77	ALA	0	-0.065	-0.037	6.049	-0.409	-0.409	0.000	0.000	0.000	0.000
66	A	78	GLN	0	-0.090	-0.031	5.410	-0.318	-0.318	0.000	0.000	0.000	0.000
67	A	79	NME	0	-0.007	0.009	7.207	-0.280	-0.280	0.000	0.000	0.000	0.000
68	A	91	ACE	0	-0.004	-0.006	6.291	-0.030	-0.030	0.000	0.000	0.000	0.000
69	A	92	PRO	0	-0.048	0.002	5.303	-0.303	-0.303	0.000	0.000	0.000	0.000
70	A	93	ARG	1	1.029	1.075	5.944	0.113	0.113	0.000	0.000	0.000	0.000
71	A	94	PHE	0	-0.056	-0.017	6.445	-0.121	-0.121	0.000	0.000	0.000	0.000
72	A	95	VAL	0	0.044	0.017	8.359	-0.082	-0.082	0.000	0.000	0.000	0.000
73	A	96	THR	0	0.038	0.006	11.032	0.048	0.048	0.000	0.000	0.000	0.000
74	A	97	ALA	0	-0.088	-0.041	12.788	-0.020	-0.020	0.000	0.000	0.000	0.000
75	A	98	ALA	0	-0.022	-0.022	15.616	-0.029	-0.029	0.000	0.000	0.000	0.000
76	A	99	LEU	0	0.024	0.005	13.939	0.019	0.019	0.000	0.000	0.000	0.000
77	A	100	ASN	0	-0.055	-0.009	16.818	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	101	ILE	0	0.030	0.005	17.116	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	102	ASP	-1	-0.914	-0.929	20.190	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	103	TYR	0	-0.025	-0.035	20.993	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	104	LEU	0	-0.028	-0.017	22.246	0.005	0.005	0.000	0.000	0.000	0.000
82	A	105	ALA	0	0.009	0.000	25.235	0.003	0.003	0.000	0.000	0.000	0.000
83	A	106	PRO	0	-0.031	-0.006	25.672	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	107	THR	0	0.054	0.012	21.858	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	108	PRO	0	0.003	0.004	25.128	0.002	0.002	0.000	0.000	0.000	0.000
86	A	109	MET	0	-0.051	-0.018	25.329	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	110	GLY	0	-0.029	-0.009	25.962	0.005	0.005	0.000	0.000	0.000	0.000
88	A	111	VAL	0	-0.020	-0.014	23.162	0.001	0.001	0.000	0.000	0.000	0.000
89	A	112	GLU	-1	-0.967	-0.981	18.735	-0.261	-0.261	0.000	0.000	0.000	0.000
90	A	113	LEU	0	-0.033	-0.038	17.576	0.010	0.010	0.000	0.000	0.000	0.000
91	A	114	GLU	-1	-0.854	-0.905	14.993	-0.329	-0.329	0.000	0.000	0.000	0.000
92	A	115	LEU	0	-0.051	-0.034	11.683	0.054	0.054	0.000	0.000	0.000	0.000
93	A	116	VAL	0	0.041	0.026	11.349	-0.115	-0.115	0.000	0.000	0.000	0.000
94	A	117	GLY	0	-0.022	-0.004	9.223	0.069	0.069	0.000	0.000	0.000	0.000
95	A	118	GLU	-1	-0.868	-0.960	10.259	-0.049	-0.049	0.000	0.000	0.000	0.000
96	A	119	ILE	0	0.014	0.006	6.791	0.075	0.075	0.000	0.000	0.000	0.000
97	A	120	LYS	1	0.903	0.955	10.868	-0.032	-0.032	0.000	0.000	0.000	0.000
98	A	121	GLU	-1	-0.793	-0.922	12.692	0.228	0.228	0.000	0.000	0.000	0.000
99	A	122	VAL	0	0.024	0.029	9.793	0.054	0.054	0.000	0.000	0.000	0.000
100	A	123	LYS	1	0.826	0.924	12.243	-0.340	-0.340	0.000	0.000	0.000	0.000
101	A	124	PRO	0	0.050	0.016	12.213	0.080	0.080	0.000	0.000	0.000	0.000
102	A	125	ARG	1	0.871	0.934	12.342	-0.293	-0.293	0.000	0.000	0.000	0.000
103	A	126	LYS	1	0.876	0.937	12.364	-0.310	-0.310	0.000	0.000	0.000	0.000
104	A	127	VAL	0	0.031	0.039	7.729	-0.033	-0.033	0.000	0.000	0.000	0.000
105	A	128	VAL	0	-0.048	-0.013	10.855	-0.034	-0.034	0.000	0.000	0.000	0.000
106	A	129	VAL	0	-0.003	-0.005	8.257	0.004	0.004	0.000	0.000	0.000	0.000
107	A	130	GLU	-1	-0.968	-0.976	11.419	-0.036	-0.036	0.000	0.000	0.000	0.000
108	A	131	ILE	0	0.002	0.009	10.669	-0.043	-0.043	0.000	0.000	0.000	0.000
109	A	132	ALA	0	-0.015	-0.008	13.165	0.039	0.039	0.000	0.000	0.000	0.000
110	A	133	LEU	0	0.023	0.022	15.297	-0.040	-0.040	0.000	0.000	0.000	0.000
111	A	134	SER	0	-0.007	-0.006	17.005	0.042	0.042	0.000	0.000	0.000	0.000
112	A	135	ALA	0	0.065	0.019	19.470	-0.020	-0.020	0.000	0.000	0.000	0.000
113	A	136	ASP	-1	-0.798	-0.868	22.518	-0.080	-0.080	0.000	0.000	0.000	0.000
114	A	137	GLY	0	0.014	-0.002	22.708	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	138	LYS	1	0.760	0.855	23.136	0.081	0.081	0.000	0.000	0.000	0.000
116	A	139	LEU	0	-0.029	0.009	19.407	0.008	0.008	0.000	0.000	0.000	0.000
117	A	140	CYS	0	-0.006	-0.002	21.051	0.007	0.007	0.000	0.000	0.000	0.000
118	A	141	ALA	0	0.000	-0.009	19.541	0.014	0.014	0.000	0.000	0.000	0.000
119	A	142	ARG	1	0.949	0.990	17.723	0.049	0.049	0.000	0.000	0.000	0.000
120	A	143	GLY	0	0.047	0.025	16.005	0.010	0.010	0.000	0.000	0.000	0.000
121	A	144	HIS	0	-0.029	-0.022	15.540	-0.005	-0.005	0.000	0.000	0.000	0.000
122	A	145	MET	0	0.023	0.040	10.329	0.031	0.031	0.000	0.000	0.000	0.000
123	A	146	VAL	0	-0.041	-0.016	13.715	0.026	0.026	0.000	0.000	0.000	0.000
124	A	147	ALA	0	0.056	0.036	9.526	-0.024	-0.024	0.000	0.000	0.000	0.000
125	A	148	VAL	0	0.004	-0.016	11.470	0.032	0.032	0.000	0.000	0.000	0.000
126	A	149	LYS	1	0.960	0.991	10.507	-0.506	-0.506	0.000	0.000	0.000	0.000
127	A	150	MET	0	-0.006	-0.012	10.603	-0.090	-0.090	0.000	0.000	0.000	0.000
128	A	151	PRO	0	-0.052	-0.023	12.563	0.002	0.002	0.000	0.000	0.000	0.000
129	A	152	NME	0	-0.005	0.008	15.645	-0.037	-0.037	0.000	0.000	0.000	0.000
130	A	161	HOH	0	0.028	0.037	30.916	0.001	0.001	0.000	0.000	0.000	0.000
131	A	162	HOH	0	-0.015	-0.017	24.812	0.002	0.002	0.000	0.000	0.000	0.000
132	B	164	HOH	0	-0.004	0.002	14.360	-0.006	-0.006	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:5:ACE)