FMO DATABASE

FMODB ID: N8Y3Q

Calculation Name: 6DKF-A-Other547

Preferred Name: ATP-dependent Clp protease proteolytic subunit

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6DKF

Chain ID: A

ChEMBL ID: CHEMBL1932910

UniProt ID: Q2G036

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	173
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1727219.541681
FMO2-HF: Nuclear repulsion	1660436.284425
FMO2-HF: Total energy	-66783.257256
FMO2-MP2: Total energy	-66977.402806

3D Structure Molmil

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:20:ILE)

Summations of interaction energy for fragment #1(A:20:ILE)

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.
-82.158	-79.277	0.026	-0.997	-1.909	-0.002

Interaction energy analysis for fragmet #1(A:20:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.872 / q_NPA : 0.918

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	22	SER	0	0.045	0.037	3.605	6.021	8.266	0.028	-0.902	-1.370	-0.002
4	A	23	ARG	1	0.947	0.963	4.216	41.530	41.920	-0.001	-0.076	-0.313	0.000
5	A	24	LEU	0	0.001	0.009	4.566	2.952	3.198	-0.001	-0.019	-0.226	0.000
6	A	25	LEU	0	0.066	0.039	6.564	2.980	2.980	0.000	0.000	0.000	0.000
7	A	26	LYS	1	0.919	0.958	8.891	27.814	27.814	0.000	0.000	0.000	0.000
8	A	27	ASP	-1	-0.948	-0.980	9.924	-21.288	-21.288	0.000	0.000	0.000	0.000
9	A	28	ARG	1	0.830	0.903	11.585	18.220	18.220	0.000	0.000	0.000	0.000
10	A	29	ILE	0	-0.008	0.010	8.438	0.831	0.831	0.000	0.000	0.000	0.000
11	A	30	ILE	0	-0.064	-0.032	9.232	-3.301	-3.301	0.000	0.000	0.000	0.000
12	A	31	MET	0	-0.043	-0.026	7.628	-0.481	-0.481	0.000	0.000	0.000	0.000
13	A	32	LEU	0	0.011	0.009	9.828	-0.836	-0.836	0.000	0.000	0.000	0.000
14	A	33	GLY	0	0.017	0.004	10.182	0.981	0.981	0.000	0.000	0.000	0.000
15	A	34	SER	0	0.003	-0.005	11.168	0.235	0.235	0.000	0.000	0.000	0.000
16	A	35	GLN	0	-0.009	0.014	13.626	1.151	1.151	0.000	0.000	0.000	0.000
17	A	36	ILE	0	-0.023	-0.006	15.760	-0.972	-0.972	0.000	0.000	0.000	0.000
18	A	37	ASP	-1	-0.841	-0.942	17.254	-14.272	-14.272	0.000	0.000	0.000	0.000
19	A	38	ASP	-1	-0.896	-0.949	17.884	-14.878	-14.878	0.000	0.000	0.000	0.000
20	A	39	ASN	0	-0.029	-0.007	14.541	-1.183	-1.183	0.000	0.000	0.000	0.000
21	A	40	VAL	0	-0.024	-0.014	11.921	-1.046	-1.046	0.000	0.000	0.000	0.000
22	A	41	ALA	0	0.045	0.020	14.116	-0.797	-0.797	0.000	0.000	0.000	0.000
23	A	42	ASN	0	0.012	0.004	16.846	-0.444	-0.444	0.000	0.000	0.000	0.000
24	A	43	SER	0	-0.041	-0.027	10.399	-0.822	-0.822	0.000	0.000	0.000	0.000
25	A	44	ILE	0	-0.005	-0.006	12.297	-0.950	-0.950	0.000	0.000	0.000	0.000
26	A	45	VAL	0	0.067	0.036	13.504	0.041	0.041	0.000	0.000	0.000	0.000
27	A	46	SER	0	-0.040	-0.008	14.674	0.277	0.277	0.000	0.000	0.000	0.000
28	A	47	GLN	0	0.015	-0.001	8.594	-0.246	-0.246	0.000	0.000	0.000	0.000
29	A	48	LEU	0	0.028	0.020	13.569	-0.114	-0.114	0.000	0.000	0.000	0.000
30	A	49	LEU	0	0.037	0.023	16.328	0.592	0.592	0.000	0.000	0.000	0.000
31	A	50	PHE	0	-0.061	-0.036	11.057	0.137	0.137	0.000	0.000	0.000	0.000
32	A	51	LEU	0	-0.001	-0.007	13.185	0.166	0.166	0.000	0.000	0.000	0.000
33	A	52	GLN	0	0.028	0.010	16.403	0.377	0.377	0.000	0.000	0.000	0.000
34	A	53	ALA	0	-0.073	-0.035	18.702	0.675	0.675	0.000	0.000	0.000	0.000
35	A	54	GLN	0	-0.116	-0.045	13.928	-0.591	-0.591	0.000	0.000	0.000	0.000
36	A	55	ASP	-1	-0.821	-0.923	17.959	-13.943	-13.943	0.000	0.000	0.000	0.000
37	A	56	SER	0	0.021	0.017	20.513	-0.233	-0.233	0.000	0.000	0.000	0.000
38	A	57	GLU	-1	-0.937	-0.959	22.845	-11.030	-11.030	0.000	0.000	0.000	0.000
39	A	58	LYS	0	-0.061	-0.026	14.869	0.267	0.267	0.000	0.000	0.000	0.000
40	A	59	ASP	-1	-0.801	-0.883	18.407	-15.149	-15.149	0.000	0.000	0.000	0.000
41	A	60	ILE	0	-0.032	-0.002	14.646	-1.006	-1.006	0.000	0.000	0.000	0.000
42	A	61	TYR	0	0.052	0.032	11.863	0.705	0.705	0.000	0.000	0.000	0.000
43	A	62	LEU	0	0.028	-0.004	12.792	-1.928	-1.928	0.000	0.000	0.000	0.000
44	A	63	TYR	0	-0.032	-0.016	9.486	1.188	1.188	0.000	0.000	0.000	0.000
45	A	64	ILE	0	-0.045	-0.001	12.690	-1.023	-1.023	0.000	0.000	0.000	0.000
46	A	65	ASN	0	-0.045	-0.024	12.745	0.048	0.048	0.000	0.000	0.000	0.000
47	A	66	SER	0	-0.002	-0.024	14.123	-0.455	-0.455	0.000	0.000	0.000	0.000
48	A	67	PRO	0	0.010	-0.019	16.786	0.649	0.649	0.000	0.000	0.000	0.000
49	A	68	GLY	0	0.055	0.056	19.070	0.743	0.743	0.000	0.000	0.000	0.000
50	A	69	GLY	0	-0.013	-0.023	19.595	-0.686	-0.686	0.000	0.000	0.000	0.000
51	A	70	SER	0	-0.022	-0.007	21.438	0.708	0.708	0.000	0.000	0.000	0.000
52	A	71	VAL	0	0.081	0.030	22.635	-0.403	-0.403	0.000	0.000	0.000	0.000
53	A	72	THR	0	-0.016	-0.005	25.291	-0.127	-0.127	0.000	0.000	0.000	0.000
54	A	73	ALA	0	0.021	0.013	20.170	-0.079	-0.079	0.000	0.000	0.000	0.000
55	A	74	GLY	0	0.052	-0.017	21.099	-0.475	-0.475	0.000	0.000	0.000	0.000
56	A	75	PHE	0	0.012	0.001	22.192	-0.107	-0.107	0.000	0.000	0.000	0.000
57	A	76	ALA	0	-0.011	0.012	21.865	0.023	0.023	0.000	0.000	0.000	0.000
58	A	77	ILE	0	-0.001	0.000	16.396	-0.317	-0.317	0.000	0.000	0.000	0.000
59	A	78	TYR	0	0.014	0.004	20.088	0.040	0.040	0.000	0.000	0.000	0.000
60	A	79	ASP	-1	-0.900	-0.950	22.822	-11.437	-11.437	0.000	0.000	0.000	0.000
61	A	80	THR	0	-0.018	-0.033	20.718	-0.198	-0.198	0.000	0.000	0.000	0.000
62	A	81	ILE	0	-0.062	-0.030	19.336	-0.438	-0.438	0.000	0.000	0.000	0.000
63	A	82	GLN	0	-0.026	0.000	21.947	0.147	0.147	0.000	0.000	0.000	0.000
64	A	83	HIS	0	-0.087	-0.048	25.080	0.434	0.434	0.000	0.000	0.000	0.000
65	A	84	ILE	0	-0.050	-0.005	20.256	0.181	0.181	0.000	0.000	0.000	0.000
66	A	85	LYS	1	0.851	0.922	24.395	12.143	12.143	0.000	0.000	0.000	0.000
67	A	86	PRO	0	-0.082	-0.048	20.022	0.169	0.169	0.000	0.000	0.000	0.000
68	A	87	ASP	-1	-0.747	-0.857	21.915	-12.813	-12.813	0.000	0.000	0.000	0.000
69	A	88	VAL	0	0.031	0.007	17.855	-0.681	-0.681	0.000	0.000	0.000	0.000
70	A	89	GLN	0	-0.038	-0.015	17.416	0.110	0.110	0.000	0.000	0.000	0.000
71	A	90	THR	0	-0.012	-0.022	17.411	-0.860	-0.860	0.000	0.000	0.000	0.000
72	A	91	ILE	0	0.008	0.014	14.588	0.514	0.514	0.000	0.000	0.000	0.000
73	A	92	CYS	0	-0.005	0.003	16.107	-0.985	-0.985	0.000	0.000	0.000	0.000
74	A	93	ILE	0	-0.006	-0.013	12.151	0.323	0.323	0.000	0.000	0.000	0.000
75	A	94	GLY	0	-0.006	0.005	15.922	-0.369	-0.369	0.000	0.000	0.000	0.000
76	A	95	MET	0	0.012	0.015	17.315	0.875	0.875	0.000	0.000	0.000	0.000
77	A	96	ALA	0	0.030	0.012	17.858	-0.941	-0.941	0.000	0.000	0.000	0.000
78	A	97	ALA	0	0.043	0.020	20.168	0.641	0.641	0.000	0.000	0.000	0.000
79	A	98	SER	0	0.064	0.042	22.064	-0.584	-0.584	0.000	0.000	0.000	0.000
80	A	99	MET	0	-0.064	0.009	20.695	-0.328	-0.328	0.000	0.000	0.000	0.000
81	A	100	GLY	0	0.062	-0.003	19.510	-0.251	-0.251	0.000	0.000	0.000	0.000
82	A	101	SER	0	-0.016	-0.002	20.169	-0.082	-0.082	0.000	0.000	0.000	0.000
83	A	102	PHE	0	0.016	0.001	23.179	0.102	0.102	0.000	0.000	0.000	0.000
84	A	103	LEU	0	-0.002	-0.013	16.910	0.021	0.021	0.000	0.000	0.000	0.000
85	A	104	LEU	0	-0.029	-0.006	19.125	-0.197	-0.197	0.000	0.000	0.000	0.000
86	A	105	ALA	0	0.061	0.032	21.229	0.062	0.062	0.000	0.000	0.000	0.000
87	A	106	ALA	0	-0.030	-0.008	22.542	0.393	0.393	0.000	0.000	0.000	0.000
88	A	107	GLY	0	0.006	0.009	22.112	-0.028	-0.028	0.000	0.000	0.000	0.000
89	A	108	ALA	0	0.014	0.022	22.723	0.615	0.615	0.000	0.000	0.000	0.000
90	A	109	LYS	1	0.850	0.930	24.776	9.749	9.749	0.000	0.000	0.000	0.000
91	A	110	GLY	0	-0.025	-0.011	27.416	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	111	LYS	1	0.720	0.855	20.531	13.941	13.941	0.000	0.000	0.000	0.000
93	A	112	ARG	0	-0.016	0.036	21.625	-0.523	-0.523	0.000	0.000	0.000	0.000
94	A	113	PHE	0	-0.005	-0.011	17.576	0.388	0.388	0.000	0.000	0.000	0.000
95	A	114	ALA	0	0.005	-0.006	19.473	-0.468	-0.468	0.000	0.000	0.000	0.000
96	A	115	LEU	0	0.031	0.019	15.723	0.462	0.462	0.000	0.000	0.000	0.000
97	A	116	PRO	0	0.045	0.007	19.440	0.203	0.203	0.000	0.000	0.000	0.000
98	A	117	ASN	0	-0.093	-0.047	20.229	0.494	0.494	0.000	0.000	0.000	0.000
99	A	118	ALA	0	-0.051	-0.011	19.643	-0.088	-0.088	0.000	0.000	0.000	0.000
100	A	119	GLU	0	0.000	0.001	21.047	0.520	0.520	0.000	0.000	0.000	0.000
101	A	120	VAL	0	-0.068	-0.032	21.805	-0.663	-0.663	0.000	0.000	0.000	0.000
102	A	121	MET	0	-0.006	0.007	24.215	0.281	0.281	0.000	0.000	0.000	0.000
103	A	122	ILE	0	0.036	0.008	25.916	-0.439	-0.439	0.000	0.000	0.000	0.000
104	A	123	HIS	0	-0.018	0.011	28.194	-0.013	-0.013	0.000	0.000	0.000	0.000
105	A	124	GLN	0	0.005	-0.009	27.883	-0.318	-0.318	0.000	0.000	0.000	0.000
106	A	125	PRO	0	-0.010	-0.001	28.043	0.328	0.328	0.000	0.000	0.000	0.000
107	A	126	LEU	0	-0.011	-0.010	30.222	-0.180	-0.180	0.000	0.000	0.000	0.000
108	A	127	GLY	0	0.025	0.009	30.333	0.166	0.166	0.000	0.000	0.000	0.000
109	A	128	GLY	0	-0.030	-0.008	26.768	-0.252	-0.252	0.000	0.000	0.000	0.000
110	A	129	ALA	0	0.045	0.019	25.218	0.348	0.348	0.000	0.000	0.000	0.000
111	A	130	GLN	0	-0.036	-0.021	23.817	-0.182	-0.182	0.000	0.000	0.000	0.000
112	A	131	GLY	0	-0.017	-0.005	26.531	0.143	0.143	0.000	0.000	0.000	0.000
113	A	132	GLN	0	-0.089	-0.057	27.870	0.204	0.204	0.000	0.000	0.000	0.000
114	A	133	ALA	0	0.066	0.052	30.983	0.064	0.064	0.000	0.000	0.000	0.000
115	A	134	THR	0	-0.007	-0.011	32.124	0.368	0.368	0.000	0.000	0.000	0.000
116	A	135	GLU	-1	-0.842	-0.939	35.206	-8.043	-8.043	0.000	0.000	0.000	0.000
117	A	136	ILE	0	-0.026	-0.017	34.516	0.046	0.046	0.000	0.000	0.000	0.000
118	A	137	GLU	-1	-0.882	-0.932	29.491	-10.260	-10.260	0.000	0.000	0.000	0.000
119	A	138	ILE	0	0.045	0.025	33.100	-0.104	-0.104	0.000	0.000	0.000	0.000
120	A	139	ALA	0	-0.036	-0.011	35.117	0.073	0.073	0.000	0.000	0.000	0.000
121	A	140	ALA	0	0.007	-0.004	32.887	0.076	0.076	0.000	0.000	0.000	0.000
122	A	141	ASN	0	0.019	0.016	31.329	-0.131	-0.131	0.000	0.000	0.000	0.000
123	A	142	HIS	0	-0.012	0.000	33.181	-0.111	-0.111	0.000	0.000	0.000	0.000
124	A	143	ILE	0	-0.053	-0.022	36.355	0.135	0.135	0.000	0.000	0.000	0.000
125	A	144	LEU	0	-0.053	-0.024	29.908	0.032	0.032	0.000	0.000	0.000	0.000
126	A	145	LYS	0	0.015	0.024	34.319	-0.027	-0.027	0.000	0.000	0.000	0.000
127	A	146	THR	0	-0.009	-0.031	29.793	-0.018	-0.018	0.000	0.000	0.000	0.000
128	A	147	ARG	1	0.825	0.902	31.845	8.411	8.411	0.000	0.000	0.000	0.000
129	A	148	GLU	0	0.009	-0.009	33.372	0.051	0.051	0.000	0.000	0.000	0.000
130	A	149	LYS	0	-0.027	-0.011	30.138	0.100	0.100	0.000	0.000	0.000	0.000
131	A	150	LEU	0	0.003	0.003	27.790	-0.080	-0.080	0.000	0.000	0.000	0.000
132	A	151	ASN	0	-0.018	-0.034	30.924	0.052	0.052	0.000	0.000	0.000	0.000
133	A	152	ARG	1	0.838	0.914	33.974	8.617	8.617	0.000	0.000	0.000	0.000
134	A	153	ILE	0	-0.026	-0.002	28.122	0.030	0.030	0.000	0.000	0.000	0.000
135	A	154	LEU	0	0.043	0.019	28.070	-0.140	-0.140	0.000	0.000	0.000	0.000
136	A	155	SER	0	-0.029	0.002	30.995	0.053	0.053	0.000	0.000	0.000	0.000
137	A	156	GLU	-1	-0.865	-0.927	33.080	-8.800	-8.800	0.000	0.000	0.000	0.000
138	A	157	ARG	1	0.685	0.816	25.319	11.392	11.392	0.000	0.000	0.000	0.000
139	A	158	THR	0	-0.005	-0.020	30.758	0.174	0.174	0.000	0.000	0.000	0.000
140	A	159	GLY	0	-0.028	-0.008	32.765	0.129	0.129	0.000	0.000	0.000	0.000
141	A	160	GLN	0	-0.031	-0.020	35.634	0.343	0.343	0.000	0.000	0.000	0.000
142	A	161	SER	-1	-0.809	-0.890	37.656	-7.454	-7.454	0.000	0.000	0.000	0.000
143	A	162	ILE	0	-0.033	-0.028	38.222	-0.159	-0.159	0.000	0.000	0.000	0.000
144	A	163	GLU	-1	-0.919	-0.965	38.855	-7.013	-7.013	0.000	0.000	0.000	0.000
145	A	164	LYS	0	-0.022	-0.006	37.446	0.049	0.049	0.000	0.000	0.000	0.000
146	A	165	ILE	0	0.018	0.031	32.259	-0.109	-0.109	0.000	0.000	0.000	0.000
147	A	166	GLN	0	-0.046	0.004	35.276	-0.124	-0.124	0.000	0.000	0.000	0.000
148	A	167	LYS	0	-0.012	-0.003	37.566	-0.016	-0.016	0.000	0.000	0.000	0.000
149	A	168	ASP	-1	-0.838	-0.921	32.021	-9.280	-9.280	0.000	0.000	0.000	0.000
150	A	169	THR	0	-0.030	-0.045	31.281	-0.119	-0.119	0.000	0.000	0.000	0.000
151	A	170	ASP	-1	-0.897	-0.926	33.095	-8.153	-8.153	0.000	0.000	0.000	0.000
152	A	171	ARG	1	0.870	0.942	34.387	8.406	8.406	0.000	0.000	0.000	0.000
153	A	172	ASP	-1	-0.932	-0.965	30.557	-9.946	-9.946	0.000	0.000	0.000	0.000
154	A	173	ASN	0	-0.029	-0.047	30.739	0.338	0.338	0.000	0.000	0.000	0.000
155	A	174	PHE	0	-0.081	-0.038	25.450	-0.436	-0.436	0.000	0.000	0.000	0.000
156	A	175	LEU	0	0.050	0.060	27.824	0.176	0.176	0.000	0.000	0.000	0.000
157	A	176	THR	0	-0.035	-0.048	26.471	-0.542	-0.542	0.000	0.000	0.000	0.000
158	A	177	ALA	0	0.027	0.002	23.694	0.063	0.063	0.000	0.000	0.000	0.000
159	A	178	GLU	-1	-0.957	-0.979	25.594	-9.174	-9.174	0.000	0.000	0.000	0.000
160	A	179	GLU	-1	-0.794	-0.887	28.952	-9.261	-9.261	0.000	0.000	0.000	0.000
161	A	180	ALA	0	0.006	-0.010	26.757	0.141	0.141	0.000	0.000	0.000	0.000
162	A	181	LYS	1	0.843	0.911	28.409	9.903	9.903	0.000	0.000	0.000	0.000
163	A	182	GLU	-1	-0.996	-0.988	29.833	-8.059	-8.059	0.000	0.000	0.000	0.000
164	A	183	TYR	-1	-0.876	-0.943	31.366	-8.923	-8.923	0.000	0.000	0.000	0.000
165	A	184	GLY	0	0.005	-0.006	31.676	-0.136	-0.136	0.000	0.000	0.000	0.000
166	A	185	LEU	0	0.010	0.003	26.212	-0.266	-0.266	0.000	0.000	0.000	0.000
167	A	186	ILE	0	-0.059	-0.020	23.593	-0.275	-0.275	0.000	0.000	0.000	0.000
168	A	187	ASP	-1	-0.756	-0.875	25.701	-10.568	-10.568	0.000	0.000	0.000	0.000
169	A	188	GLU	-1	-0.962	-0.994	24.332	-11.081	-11.081	0.000	0.000	0.000	0.000
170	A	189	VAL	0	0.033	0.022	23.463	-0.482	-0.482	0.000	0.000	0.000	0.000
171	A	190	MET	0	-0.025	-0.005	18.701	0.034	0.034	0.000	0.000	0.000	0.000
172	A	191	VAL	0	-0.042	-0.025	22.343	-0.034	-0.034	0.000	0.000	0.000	0.000
173	A	192	PRO	-1	-0.936	-0.970	20.296	-12.894	-12.894	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:20:ILE)