FMO DATABASE

FMODB ID: 43R4N

Calculation Name: 3UB0-A-Xray320

Preferred Name: Replicase polyprotein 1ab

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3UB0

Chain ID: A

ChEMBL ID: CHEMBL4295624

UniProt ID: Q98VG9

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:

Apendix: None

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	197
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1527863.229771
FMO2-HF: Nuclear repulsion	1452730.943295
FMO2-HF: Total energy	-75132.286476
FMO2-MP2: Total energy	-75350.411873

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:-3:ACE )

Summations of interaction energy for fragment #1(A:-3: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.
2.601	3.964	0.118	-0.526	-0.955	0

Interaction energy analysis for fragmet #1(A:-3:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.050 / q_NPA : 0.011

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].
3	A	-1	LEU	0	-0.019	-0.009	3.817	0.549	1.339	0.006	-0.322	-0.474
4	A	0	GLY	0	0.002	-0.003	3.027	0.865	1.303	0.108	-0.214	-0.332
5	A	1	SER	0	-0.003	-0.001	4.002	0.302	0.437	0.004	0.010	-0.149
6	A	2	VAL	0	-0.065	-0.024	6.767	0.259	0.259	0.000	0.000	0.000
7	A	3	ALA	0	0.037	0.029	9.347	0.075	0.075	0.000	0.000	0.000
8	A	4	SER	0	0.057	0.024	12.101	0.047	0.047	0.000	0.000	0.000
9	A	5	ALA	0	0.034	0.008	8.011	-0.041	-0.041	0.000	0.000	0.000
10	A	6	TYR	0	-0.002	-0.005	9.824	-0.010	-0.010	0.000	0.000	0.000
11	A	7	ALA	0	0.013	0.001	12.992	0.005	0.005	0.000	0.000	0.000
12	A	8	ALA	0	0.000	-0.007	10.841	0.003	0.003	0.000	0.000	0.000
13	A	9	LEU	0	0.002	0.012	10.256	-0.041	-0.041	0.000	0.000	0.000
14	A	10	PRO	0	0.016	0.006	12.470	-0.005	-0.005	0.000	0.000	0.000
15	A	11	SER	0	0.064	0.036	15.164	-0.021	-0.021	0.000	0.000	0.000
16	A	12	TRP	0	-0.002	-0.012	7.883	0.009	0.009	0.000	0.000	0.000
17	A	13	ILE	0	-0.006	0.005	12.404	0.001	0.001	0.000	0.000	0.000
18	A	14	ALA	0	0.001	0.011	13.710	0.025	0.025	0.000	0.000	0.000
19	A	15	TYR	0	-0.019	-0.015	12.210	0.053	0.053	0.000	0.000	0.000
20	A	16	GLU	-1	-0.894	-0.955	10.306	-0.496	-0.496	0.000	0.000	0.000
21	A	17	LYS	1	0.963	0.970	13.151	0.188	0.188	0.000	0.000	0.000
22	A	18	ALA	0	0.048	0.032	16.398	0.026	0.026	0.000	0.000	0.000
23	A	19	ARG	1	0.876	0.909	10.424	0.485	0.485	0.000	0.000	0.000
24	A	20	ALA	0	-0.028	-0.006	14.693	0.025	0.025	0.000	0.000	0.000
25	A	21	ASP	-1	-0.865	-0.923	16.244	-0.106	-0.106	0.000	0.000	0.000
26	A	22	LEU	0	-0.056	-0.029	19.101	0.017	0.017	0.000	0.000	0.000
27	A	23	GLU	-1	-0.927	-0.974	16.011	-0.094	-0.094	0.000	0.000	0.000
28	A	24	GLU	-1	-0.960	-0.980	18.810	-0.045	-0.045	0.000	0.000	0.000
29	A	25	ALA	0	-0.012	-0.014	21.050	0.012	0.012	0.000	0.000	0.000
30	A	26	LYS	1	0.907	0.956	19.529	0.139	0.139	0.000	0.000	0.000
31	A	27	LYS	1	0.895	0.954	17.682	0.066	0.066	0.000	0.000	0.000
32	A	28	ASN	0	-0.009	-0.005	23.461	0.013	0.013	0.000	0.000	0.000
33	A	29	ASP	-1	-0.982	-0.974	26.366	-0.040	-0.040	0.000	0.000	0.000
34	A	30	VAL	0	-0.007	0.012	27.081	0.002	0.002	0.000	0.000	0.000
35	A	31	SER	0	0.037	0.010	29.206	-0.003	-0.003	0.000	0.000	0.000
36	A	32	PRO	0	0.072	0.015	30.329	-0.006	-0.006	0.000	0.000	0.000
37	A	33	GLN	0	-0.068	-0.033	30.788	-0.007	-0.007	0.000	0.000	0.000
38	A	34	LEU	0	0.063	0.032	27.788	-0.005	-0.005	0.000	0.000	0.000
39	A	35	LEU	0	0.102	0.048	25.275	-0.010	-0.010	0.000	0.000	0.000
40	A	36	LYS	1	0.940	0.989	26.027	0.063	0.063	0.000	0.000	0.000
41	A	37	GLN	0	-0.058	-0.026	27.539	-0.010	-0.010	0.000	0.000	0.000
42	A	38	LEU	0	0.059	0.023	22.971	-0.010	-0.010	0.000	0.000	0.000
43	A	39	THR	0	-0.013	-0.016	22.544	-0.019	-0.019	0.000	0.000	0.000
44	A	40	LYS	1	0.916	0.963	22.964	0.088	0.088	0.000	0.000	0.000
45	A	41	ALA	0	0.023	0.012	23.058	-0.010	-0.010	0.000	0.000	0.000
46	A	42	CYS	0	-0.008	0.022	17.584	-0.026	-0.026	0.000	0.000	0.000
47	A	43	ASN	0	-0.004	-0.016	19.385	-0.038	-0.038	0.000	0.000	0.000
48	A	44	ILE	0	-0.011	-0.004	21.292	-0.010	-0.010	0.000	0.000	0.000
49	A	45	ALA	0	0.050	0.030	18.062	-0.008	-0.008	0.000	0.000	0.000
50	A	46	LYS	1	0.928	0.975	15.855	0.326	0.326	0.000	0.000	0.000
51	A	47	SER	0	-0.039	-0.024	17.342	-0.017	-0.017	0.000	0.000	0.000
52	A	48	GLU	-1	-0.813	-0.912	19.935	-0.199	-0.199	0.000	0.000	0.000
53	A	49	PHE	0	0.000	0.004	10.331	-0.033	-0.033	0.000	0.000	0.000
54	A	50	GLU	-1	-0.947	-0.983	15.935	-0.369	-0.369	0.000	0.000	0.000
55	A	51	ARG	1	0.864	0.935	17.152	0.202	0.202	0.000	0.000	0.000
56	A	52	GLU	-1	-0.886	-0.964	17.698	-0.236	-0.236	0.000	0.000	0.000
57	A	53	ALA	0	0.002	0.015	14.723	0.007	0.007	0.000	0.000	0.000
58	A	54	SER	0	-0.110	-0.056	16.277	0.030	0.030	0.000	0.000	0.000
59	A	55	VAL	0	-0.004	0.000	19.354	0.024	0.024	0.000	0.000	0.000
60	A	56	GLN	0	0.016	-0.001	15.938	0.038	0.038	0.000	0.000	0.000
61	A	57	LYS	1	0.976	0.990	14.684	0.350	0.350	0.000	0.000	0.000
62	A	58	LYS	1	0.888	0.946	19.066	0.200	0.200	0.000	0.000	0.000
63	A	59	LEU	0	0.005	-0.004	21.843	0.017	0.017	0.000	0.000	0.000
64	A	60	ASP	-1	-0.852	-0.914	17.612	-0.182	-0.182	0.000	0.000	0.000
65	A	61	LYS	1	0.948	0.978	21.207	0.133	0.133	0.000	0.000	0.000
66	A	62	MET	0	-0.007	-0.005	23.307	0.014	0.014	0.000	0.000	0.000
67	A	63	ALA	0	0.024	0.012	23.891	0.011	0.011	0.000	0.000	0.000
68	A	64	GLU	-1	-0.944	-0.964	21.697	-0.091	-0.091	0.000	0.000	0.000
69	A	65	GLN	0	-0.037	-0.036	25.088	0.007	0.007	0.000	0.000	0.000
70	A	66	ALA	0	-0.001	0.006	28.357	0.007	0.007	0.000	0.000	0.000
71	A	67	ALA	0	0.022	0.010	27.437	0.007	0.007	0.000	0.000	0.000
72	A	68	ALA	0	-0.010	-0.006	28.760	0.007	0.007	0.000	0.000	0.000
73	A	69	SER	0	-0.098	-0.043	30.468	0.005	0.005	0.000	0.000	0.000
74	A	70	MET	0	0.017	0.007	33.019	0.002	0.002	0.000	0.000	0.000
75	A	71	TYR	0	0.022	0.019	31.205	0.004	0.004	0.000	0.000	0.000
76	A	72	LYS	1	0.959	0.986	34.145	0.029	0.029	0.000	0.000	0.000
77	A	73	GLU	-1	-0.933	-0.966	37.575	-0.024	-0.024	0.000	0.000	0.000
78	A	74	ALA	0	0.007	0.000	38.467	0.001	0.001	0.000	0.000	0.000
79	A	75	ARG	1	0.792	0.892	40.158	0.018	0.018	0.000	0.000	0.000
80	A	76	ALA	0	0.017	0.006	44.582	-0.001	-0.001	0.000	0.000	0.000
81	A	77	VAL	0	-0.002	-0.020	40.681	-0.001	-0.001	0.000	0.000	0.000
82	A	78	ASP	-1	-0.808	-0.892	43.902	-0.014	-0.014	0.000	0.000	0.000
83	A	79	ARG	1	0.889	0.985	44.316	0.018	0.018	0.000	0.000	0.000
84	A	80	LYS	1	0.876	0.922	47.079	0.019	0.019	0.000	0.000	0.000
85	A	81	SER	0	0.153	0.075	50.331	0.000	0.000	0.000	0.000	0.000
86	A	82	LYS	1	0.984	0.971	52.936	0.016	0.016	0.000	0.000	0.000
87	A	83	ILE	0	0.030	0.009	46.887	0.000	0.000	0.000	0.000	0.000
88	A	84	VAL	0	0.081	0.053	50.618	0.000	0.000	0.000	0.000	0.000
89	A	85	SER	0	-0.014	-0.021	52.520	0.000	0.000	0.000	0.000	0.000
90	A	86	ALA	0	-0.052	-0.022	52.531	0.000	0.000	0.000	0.000	0.000
91	A	87	MET	0	0.015	0.005	48.913	-0.001	-0.001	0.000	0.000	0.000
92	A	88	HIS	0	0.040	0.022	53.336	0.000	0.000	0.000	0.000	0.000
93	A	89	SER	0	-0.032	-0.015	56.689	0.000	0.000	0.000	0.000	0.000
94	A	90	LEU	0	0.008	-0.004	52.414	0.000	0.000	0.000	0.000	0.000
95	A	91	LEU	0	0.008	0.012	54.985	0.000	0.000	0.000	0.000	0.000
96	A	92	PHE	0	0.037	0.001	56.645	0.000	0.000	0.000	0.000	0.000
97	A	93	GLY	0	0.011	0.020	59.887	0.000	0.000	0.000	0.000	0.000
98	A	94	MET	0	-0.061	-0.043	54.182	0.000	0.000	0.000	0.000	0.000
99	A	95	LEU	0	-0.005	-0.001	58.407	0.000	0.000	0.000	0.000	0.000
100	A	96	LYS	1	0.981	0.994	61.127	0.012	0.012	0.000	0.000	0.000
101	A	97	LYS	1	0.923	0.959	59.453	0.018	0.018	0.000	0.000	0.000
102	A	98	LEU	0	-0.044	-0.021	58.828	0.000	0.000	0.000	0.000	0.000
103	A	99	ASP	-1	-0.929	-0.953	62.752	-0.012	-0.012	0.000	0.000	0.000
104	A	100	MET	0	0.014	0.025	61.267	0.000	0.000	0.000	0.000	0.000
105	A	101	SER	0	0.034	0.007	66.117	0.000	0.000	0.000	0.000	0.000
106	A	102	SER	0	0.018	0.013	64.225	0.000	0.000	0.000	0.000	0.000
107	A	103	VAL	0	0.041	0.020	61.685	0.000	0.000	0.000	0.000	0.000
108	A	104	ASN	0	0.027	-0.002	64.312	0.000	0.000	0.000	0.000	0.000
109	A	105	THR	0	-0.056	-0.023	67.591	0.001	0.001	0.000	0.000	0.000
110	A	106	ILE	0	-0.016	-0.001	61.613	0.000	0.000	0.000	0.000	0.000
111	A	107	ILE	0	-0.014	-0.009	61.808	0.000	0.000	0.000	0.000	0.000
112	A	108	GLU	-1	-0.826	-0.913	65.802	-0.008	-0.008	0.000	0.000	0.000
113	A	109	GLN	0	-0.034	-0.034	67.805	0.000	0.000	0.000	0.000	0.000
114	A	110	ALA	0	0.031	0.026	64.748	0.000	0.000	0.000	0.000	0.000
115	A	111	ARG	1	0.833	0.930	66.696	0.008	0.008	0.000	0.000	0.000
116	A	112	ASN	0	-0.101	-0.048	68.907	0.000	0.000	0.000	0.000	0.000
117	A	113	GLY	0	0.037	0.015	68.762	0.000	0.000	0.000	0.000	0.000
118	A	114	VAL	0	-0.046	-0.019	68.679	0.000	0.000	0.000	0.000	0.000
119	A	115	LEU	0	-0.018	-0.010	62.966	-0.001	-0.001	0.000	0.000	0.000
120	A	116	PRO	0	-0.019	-0.017	60.515	0.000	0.000	0.000	0.000	0.000
121	A	117	LEU	0	0.016	0.017	62.034	0.000	0.000	0.000	0.000	0.000
122	A	118	SER	0	-0.025	-0.024	58.406	0.000	0.000	0.000	0.000	0.000
123	A	119	ILE	0	0.012	-0.002	56.413	0.000	0.000	0.000	0.000	0.000
124	A	120	ILE	0	0.005	0.013	54.086	0.000	0.000	0.000	0.000	0.000
125	A	121	PRO	0	0.005	0.004	51.410	0.000	0.000	0.000	0.000	0.000
126	A	122	ALA	0	0.030	0.008	50.937	0.001	0.001	0.000	0.000	0.000
127	A	123	ALA	0	0.057	0.027	52.726	0.000	0.000	0.000	0.000	0.000
128	A	124	SER	0	-0.104	-0.046	54.347	0.000	0.000	0.000	0.000	0.000
129	A	125	ALA	0	0.038	0.019	55.516	-0.001	-0.001	0.000	0.000	0.000
130	A	126	THR	0	-0.030	-0.011	56.154	0.000	0.000	0.000	0.000	0.000
131	A	127	ARG	1	0.908	0.940	57.902	0.003	0.003	0.000	0.000	0.000
132	A	128	LEU	0	-0.029	-0.006	59.402	0.000	0.000	0.000	0.000	0.000
133	A	129	ILE	0	0.019	0.012	61.916	0.000	0.000	0.000	0.000	0.000
134	A	130	VAL	0	0.002	-0.015	63.849	0.000	0.000	0.000	0.000	0.000
135	A	131	VAL	0	0.007	0.022	66.048	0.000	0.000	0.000	0.000	0.000
136	A	132	THR	0	-0.018	-0.021	68.515	0.000	0.000	0.000	0.000	0.000
137	A	133	PRO	0	0.012	-0.011	71.411	0.000	0.000	0.000	0.000	0.000
138	A	134	ASN	0	0.035	0.027	73.980	0.000	0.000	0.000	0.000	0.000
139	A	135	LEU	0	0.084	0.038	77.148	0.000	0.000	0.000	0.000	0.000
140	A	136	GLU	-1	-0.928	-0.946	79.696	-0.005	-0.005	0.000	0.000	0.000
141	A	137	VAL	0	-0.070	-0.059	74.265	0.000	0.000	0.000	0.000	0.000
142	A	138	LEU	0	0.006	0.007	74.700	0.000	0.000	0.000	0.000	0.000
143	A	139	SER	0	-0.012	-0.015	75.749	0.000	0.000	0.000	0.000	0.000
144	A	140	LYS	1	0.909	0.974	75.286	0.006	0.006	0.000	0.000	0.000
145	A	141	VAL	0	-0.003	-0.001	70.619	0.000	0.000	0.000	0.000	0.000
146	A	142	ARG	1	0.913	0.976	72.446	0.004	0.004	0.000	0.000	0.000
147	A	143	GLN	0	-0.057	-0.031	74.175	0.000	0.000	0.000	0.000	0.000
148	A	144	GLU	-1	-0.912	-0.960	75.378	-0.004	-0.004	0.000	0.000	0.000
149	A	145	ASN	0	-0.019	-0.012	73.876	0.000	0.000	0.000	0.000	0.000
150	A	146	ASN	0	0.017	0.015	71.124	0.000	0.000	0.000	0.000	0.000
151	A	147	VAL	0	0.023	0.016	68.173	0.000	0.000	0.000	0.000	0.000
152	A	148	HIS	0	0.041	0.026	68.865	0.000	0.000	0.000	0.000	0.000
153	A	149	TYR	0	0.047	-0.004	62.540	0.000	0.000	0.000	0.000	0.000
154	A	150	ALA	0	0.009	0.008	61.497	0.000	0.000	0.000	0.000	0.000
155	A	151	GLY	0	-0.034	-0.011	62.547	0.000	0.000	0.000	0.000	0.000
156	A	152	ALA	0	-0.052	-0.008	62.746	0.000	0.000	0.000	0.000	0.000
157	A	153	ILE	0	0.052	0.019	64.875	0.000	0.000	0.000	0.000	0.000
158	A	154	TRP	0	-0.066	-0.042	60.017	0.000	0.000	0.000	0.000	0.000
159	A	155	SER	0	0.058	0.032	66.667	0.000	0.000	0.000	0.000	0.000
160	A	156	ILE	0	-0.057	-0.045	67.708	0.000	0.000	0.000	0.000	0.000
161	A	157	VAL	0	-0.063	-0.016	65.500	0.000	0.000	0.000	0.000	0.000
162	A	158	GLU	-1	-0.874	-0.942	67.641	-0.001	-0.001	0.000	0.000	0.000
163	A	159	VAL	0	0.002	-0.003	69.930	0.000	0.000	0.000	0.000	0.000
164	A	160	LYS	1	0.884	0.955	66.790	0.002	0.002	0.000	0.000	0.000
165	A	161	ASP	-1	-0.818	-0.911	72.197	-0.002	-0.002	0.000	0.000	0.000
166	A	162	ALA	0	-0.008	0.008	71.504	0.000	0.000	0.000	0.000	0.000
167	A	163	ASN	0	-0.024	-0.026	71.520	0.000	0.000	0.000	0.000	0.000
168	A	164	GLY	0	-0.032	-0.017	70.441	0.000	0.000	0.000	0.000	0.000
169	A	165	ALA	0	-0.016	-0.003	71.118	0.000	0.000	0.000	0.000	0.000
170	A	166	GLN	0	-0.047	-0.043	70.734	0.000	0.000	0.000	0.000	0.000
171	A	167	VAL	0	0.043	0.027	74.766	0.000	0.000	0.000	0.000	0.000
172	A	168	HIS	0	0.016	0.010	76.065	0.000	0.000	0.000	0.000	0.000
173	A	169	LEU	0	0.050	-0.006	74.806	0.000	0.000	0.000	0.000	0.000
174	A	170	LYS	1	0.887	0.954	78.691	0.001	0.001	0.000	0.000	0.000
175	A	171	GLU	-1	-0.908	-0.955	81.794	-0.001	-0.001	0.000	0.000	0.000
176	A	172	VAL	0	0.004	0.028	78.416	0.000	0.000	0.000	0.000	0.000
177	A	173	THR	0	-0.016	-0.009	81.826	0.000	0.000	0.000	0.000	0.000
178	A	174	ALA	0	0.054	0.005	84.928	0.000	0.000	0.000	0.000	0.000
179	A	175	ALA	0	-0.036	-0.019	86.774	0.000	0.000	0.000	0.000	0.000
180	A	176	ASN	0	0.007	-0.003	84.183	0.000	0.000	0.000	0.000	0.000
181	A	177	GLU	-1	-0.907	-0.954	81.649	-0.004	-0.004	0.000	0.000	0.000
182	A	178	LEU	0	-0.007	-0.010	82.672	0.000	0.000	0.000	0.000	0.000
183	A	179	ASN	0	-0.060	-0.037	83.973	0.000	0.000	0.000	0.000	0.000
184	A	180	ILE	0	0.025	0.035	78.403	0.000	0.000	0.000	0.000	0.000
185	A	181	THR	0	-0.055	-0.011	76.243	0.000	0.000	0.000	0.000	0.000
186	A	182	TRP	0	0.013	0.025	75.586	0.000	0.000	0.000	0.000	0.000
187	A	183	PRO	0	-0.048	-0.039	70.614	0.000	0.000	0.000	0.000	0.000
188	A	184	LEU	0	0.038	0.019	72.670	0.000	0.000	0.000	0.000	0.000
189	A	185	SER	0	-0.035	-0.017	67.605	0.000	0.000	0.000	0.000	0.000
190	A	186	ILE	0	-0.009	-0.014	68.843	0.000	0.000	0.000	0.000	0.000
191	A	187	THR	0	0.007	0.010	64.250	-0.001	-0.001	0.000	0.000	0.000
192	A	188	CYS	0	-0.024	-0.005	65.157	0.000	0.000	0.000	0.000	0.000
193	A	189	GLU	-1	-0.803	-0.896	61.138	-0.003	-0.003	0.000	0.000	0.000
194	A	190	ARG	1	0.929	0.972	59.227	0.009	0.009	0.000	0.000	0.000
195	A	191	THR	0	-0.012	-0.015	62.466	0.000	0.000	0.000	0.000	0.000
196	A	192	THR	0	-0.089	-0.046	59.663	-0.001	-0.001	0.000	0.000	0.000
197	A	193	NME	0	0.047	0.036	60.440	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:ACE )