FMO DATABASE

FMODB ID: N64NQ

Calculation Name: 1RO5-A-Xray549

Preferred Name: Acyl-homoserine-lactone synthase

Target Type: SINGLE PROTEIN

Ligand Name: sulfate ion | zinc ion

Ligand 3-letter code: SO4 | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1RO5

Chain ID: A

ChEMBL ID: CHEMBL1795157

UniProt ID: P33883

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

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. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-2296748.349078
FMO2-HF: Nuclear repulsion	2217611.395809
FMO2-HF: Total energy	-79136.953269
FMO2-MP2: Total energy	-79363.70333

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:397:GLY)

Summations of interaction energy for fragment #1(A:397:GLY)

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.
-91.072	-88.809	7.435	-5.009	-4.687	-0.07

Interaction energy analysis for fragmet #1(A:397:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.776 / q_NPA : 0.872

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	399	HIS	0	0.062	0.040	2.066	-22.825	-20.776	7.438	-4.928	-4.558	-0.070
4	A	1	MET	0	0.041	0.028	4.101	-4.653	-4.530	-0.001	-0.060	-0.062	0.000
5	A	2	ILE	0	-0.049	-0.018	4.275	-1.250	-1.164	-0.001	-0.007	-0.077	0.000
62	A	59	ASP	-1	-0.899	-0.960	4.578	-48.707	-48.702	-0.001	-0.014	0.010	0.000
6	A	3	VAL	0	0.002	-0.001	7.494	2.273	2.273	0.000	0.000	0.000	0.000
7	A	4	GLN	0	-0.034	-0.015	11.178	1.250	1.250	0.000	0.000	0.000	0.000
8	A	5	ILE	0	-0.022	-0.027	13.678	0.717	0.717	0.000	0.000	0.000	0.000
9	A	6	GLY	0	0.051	0.048	17.504	0.003	0.003	0.000	0.000	0.000	0.000
10	A	7	ARG	1	0.976	0.972	20.154	12.226	12.226	0.000	0.000	0.000	0.000
11	A	8	ARG	1	0.865	0.915	21.903	12.238	12.238	0.000	0.000	0.000	0.000
12	A	9	GLU	-1	-0.989	-1.004	22.533	-11.962	-11.962	0.000	0.000	0.000	0.000
13	A	10	GLU	-1	-0.898	-0.930	19.320	-15.119	-15.119	0.000	0.000	0.000	0.000
14	A	11	PHE	0	-0.021	0.000	15.230	-1.143	-1.143	0.000	0.000	0.000	0.000
15	A	12	ASP	-1	-0.884	-0.940	15.352	-19.185	-19.185	0.000	0.000	0.000	0.000
16	A	13	LYS	1	0.948	0.948	18.037	13.308	13.308	0.000	0.000	0.000	0.000
17	A	14	LYS	1	0.964	0.987	15.957	18.505	18.505	0.000	0.000	0.000	0.000
18	A	15	LEU	0	0.070	0.044	11.835	-0.041	-0.041	0.000	0.000	0.000	0.000
19	A	16	LEU	0	-0.021	-0.003	15.894	0.304	0.304	0.000	0.000	0.000	0.000
20	A	17	GLY	0	0.032	0.017	19.343	0.540	0.540	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.842	-0.933	12.769	-23.723	-23.723	0.000	0.000	0.000	0.000
22	A	19	MET	0	-0.008	0.009	17.181	0.646	0.646	0.000	0.000	0.000	0.000
23	A	20	HIS	0	0.024	0.011	18.621	0.452	0.452	0.000	0.000	0.000	0.000
24	A	21	LYS	1	0.873	0.944	19.515	14.367	14.367	0.000	0.000	0.000	0.000
25	A	22	LEU	0	0.013	0.014	16.335	0.568	0.568	0.000	0.000	0.000	0.000
26	A	23	ARG	1	0.774	0.830	19.919	13.390	13.390	0.000	0.000	0.000	0.000
27	A	24	ALA	0	0.005	0.008	23.006	0.635	0.635	0.000	0.000	0.000	0.000
28	A	25	GLN	0	-0.066	-0.046	19.526	0.057	0.057	0.000	0.000	0.000	0.000
29	A	26	VAL	0	-0.041	0.001	22.102	0.280	0.280	0.000	0.000	0.000	0.000
30	A	27	PHE	0	-0.026	-0.034	24.864	0.653	0.653	0.000	0.000	0.000	0.000
31	A	28	LYS	1	1.001	1.013	26.999	12.079	12.079	0.000	0.000	0.000	0.000
32	A	29	GLU	-1	-0.962	-0.984	29.569	-9.836	-9.836	0.000	0.000	0.000	0.000
33	A	30	ARG	1	0.828	0.926	29.409	11.061	11.061	0.000	0.000	0.000	0.000
34	A	31	LYS	1	0.986	0.984	33.369	8.167	8.167	0.000	0.000	0.000	0.000
35	A	32	GLY	0	-0.017	-0.015	36.327	-0.088	-0.088	0.000	0.000	0.000	0.000
36	A	33	TRP	0	-0.008	-0.019	31.065	-0.061	-0.061	0.000	0.000	0.000	0.000
37	A	34	ASP	-1	-0.838	-0.905	32.999	-9.123	-9.123	0.000	0.000	0.000	0.000
38	A	35	VAL	0	0.004	0.022	30.170	-0.264	-0.264	0.000	0.000	0.000	0.000
39	A	36	SER	0	-0.018	-0.009	31.315	0.442	0.442	0.000	0.000	0.000	0.000
40	A	37	VAL	0	-0.018	-0.015	27.969	-0.373	-0.373	0.000	0.000	0.000	0.000
41	A	38	ILE	0	0.004	0.002	29.213	0.407	0.407	0.000	0.000	0.000	0.000
42	A	39	ASP	-1	-0.897	-0.952	27.367	-11.891	-11.891	0.000	0.000	0.000	0.000
43	A	40	GLU	-1	-0.894	-0.937	24.864	-13.135	-13.135	0.000	0.000	0.000	0.000
44	A	41	MET	0	-0.041	-0.016	23.131	-0.831	-0.831	0.000	0.000	0.000	0.000
45	A	42	GLU	-1	-0.800	-0.878	24.969	-11.112	-11.112	0.000	0.000	0.000	0.000
46	A	43	ILE	0	-0.029	-0.006	25.860	-0.489	-0.489	0.000	0.000	0.000	0.000
47	A	44	ASP	-1	-0.732	-0.840	28.250	-10.328	-10.328	0.000	0.000	0.000	0.000
48	A	45	GLY	0	0.031	0.003	30.896	-0.135	-0.135	0.000	0.000	0.000	0.000
49	A	46	TYR	0	-0.001	-0.027	30.617	0.068	0.068	0.000	0.000	0.000	0.000
50	A	47	ASP	-1	-0.751	-0.832	26.392	-12.447	-12.447	0.000	0.000	0.000	0.000
51	A	48	ALA	0	-0.028	-0.011	28.201	-0.265	-0.265	0.000	0.000	0.000	0.000
52	A	49	LEU	0	-0.058	-0.022	30.996	0.188	0.188	0.000	0.000	0.000	0.000
53	A	50	SER	0	-0.041	-0.019	28.910	-0.028	-0.028	0.000	0.000	0.000	0.000
54	A	51	PRO	0	0.000	0.024	25.665	-0.067	-0.067	0.000	0.000	0.000	0.000
55	A	52	TYR	0	-0.040	-0.046	22.899	-0.489	-0.489	0.000	0.000	0.000	0.000
56	A	53	TYR	0	-0.056	-0.064	19.834	0.432	0.432	0.000	0.000	0.000	0.000
57	A	54	MET	0	-0.012	0.013	16.095	-0.289	-0.289	0.000	0.000	0.000	0.000
58	A	55	LEU	0	-0.043	-0.020	13.537	0.462	0.462	0.000	0.000	0.000	0.000
59	A	56	ILE	0	0.034	0.010	11.090	-0.756	-0.756	0.000	0.000	0.000	0.000
60	A	57	GLN	0	0.006	0.000	8.200	1.684	1.684	0.000	0.000	0.000	0.000
61	A	58	GLU	-1	-0.856	-0.944	6.245	-37.400	-37.400	0.000	0.000	0.000	0.000
63	A	60	GLY	0	-0.054	-0.024	5.514	3.483	3.483	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.026	-0.002	6.726	3.938	3.938	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.028	-0.024	9.785	-1.951	-1.951	0.000	0.000	0.000	0.000
66	A	66	PHE	0	-0.013	-0.012	9.867	2.097	2.097	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.009	0.003	13.473	1.656	1.656	0.000	0.000	0.000	0.000
68	A	68	CYS	0	-0.094	-0.024	15.273	-0.663	-0.663	0.000	0.000	0.000	0.000
69	A	69	TRP	0	0.075	0.028	17.974	0.571	0.571	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.787	0.848	20.999	11.029	11.029	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.022	-0.004	21.604	0.220	0.220	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.012	0.001	25.703	0.016	0.016	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.774	-0.864	29.257	-10.587	-10.587	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.018	-0.023	31.764	0.323	0.323	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.010	-0.023	34.806	0.235	0.235	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.030	0.032	35.148	0.230	0.230	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.025	-0.022	35.631	0.117	0.117	0.000	0.000	0.000	0.000
78	A	78	TYR	0	-0.070	-0.056	32.759	-0.312	-0.312	0.000	0.000	0.000	0.000
79	A	79	MET	0	0.005	0.017	31.222	0.114	0.114	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.030	-0.026	34.314	0.273	0.273	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.828	0.933	36.230	8.631	8.631	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.034	-0.035	37.462	0.128	0.128	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.015	0.009	35.485	0.050	0.050	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.034	-0.014	33.186	0.026	0.026	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.072	0.044	38.649	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.871	-0.952	40.972	-7.774	-7.774	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.065	-0.033	36.923	0.090	0.090	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.005	0.001	39.689	-0.114	-0.114	0.000	0.000	0.000	0.000
89	A	89	HIS	0	-0.091	-0.061	42.017	0.281	0.281	0.000	0.000	0.000	0.000
90	A	90	GLY	0	0.008	0.004	45.293	0.123	0.123	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.827	0.922	43.585	7.374	7.374	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.890	-0.946	43.322	-7.197	-7.197	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.003	0.000	39.627	-0.157	-0.157	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.003	-0.003	37.065	0.064	0.064	0.000	0.000	0.000	0.000
95	A	95	CYS	0	0.011	0.023	38.357	-0.201	-0.201	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.032	0.012	36.837	0.149	0.149	0.000	0.000	0.000	0.000
97	A	97	PRO	0	0.024	0.002	34.621	-0.218	-0.218	0.000	0.000	0.000	0.000
98	A	98	HIS	1	0.822	0.929	32.995	8.908	8.908	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.003	0.004	32.444	-0.087	-0.087	0.000	0.000	0.000	0.000
100	A	100	TRP	0	0.039	0.029	24.594	-0.127	-0.127	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.758	-0.888	29.710	-9.978	-9.978	0.000	0.000	0.000	0.000
102	A	102	LEU	0	0.009	0.016	24.410	-0.428	-0.428	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.016	-0.006	26.251	0.326	0.326	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.775	0.853	24.959	10.481	10.481	0.000	0.000	0.000	0.000
105	A	105	PHE	0	0.022	0.019	22.513	-0.464	-0.464	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.003	-0.008	21.016	0.530	0.530	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.025	0.007	16.916	-0.858	-0.858	0.000	0.000	0.000	0.000
108	A	108	ASN	0	-0.021	-0.004	14.907	1.940	1.940	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.007	-0.006	17.701	-0.637	-0.637	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.010	0.011	18.560	0.471	0.471	0.000	0.000	0.000	0.000
111	A	111	GLN	0	-0.029	-0.046	17.525	-0.653	-0.653	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.946	0.979	12.501	22.164	22.164	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.053	0.045	12.120	-1.970	-1.970	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.013	0.000	9.997	2.377	2.377	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.009	0.015	11.988	0.269	0.269	0.000	0.000	0.000	0.000
116	A	116	GLY	0	0.005	0.015	13.465	1.573	1.573	0.000	0.000	0.000	0.000
117	A	117	PHE	0	-0.027	-0.028	16.474	-0.371	-0.371	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.011	-0.023	19.163	0.078	0.078	0.000	0.000	0.000	0.000
119	A	119	ASP	-1	-0.829	-0.917	16.859	-16.230	-16.230	0.000	0.000	0.000	0.000
120	A	120	CYS	0	-0.009	0.009	15.236	-0.741	-0.741	0.000	0.000	0.000	0.000
121	A	121	THR	0	-0.001	-0.018	16.191	0.004	0.004	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.032	-0.001	18.745	0.470	0.470	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.831	-0.925	13.759	-19.657	-19.657	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.015	0.000	16.287	-0.105	-0.105	0.000	0.000	0.000	0.000
125	A	125	MET	0	0.012	-0.007	17.489	0.435	0.435	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.839	0.915	17.159	17.229	17.229	0.000	0.000	0.000	0.000
127	A	127	ALA	0	0.023	0.021	15.589	0.509	0.509	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.018	0.007	17.720	0.497	0.497	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.019	0.021	20.495	0.621	0.621	0.000	0.000	0.000	0.000
130	A	130	ARG	1	0.950	0.978	16.273	17.486	17.486	0.000	0.000	0.000	0.000
131	A	131	TYR	0	0.013	0.000	19.760	0.593	0.593	0.000	0.000	0.000	0.000
132	A	132	SER	0	0.006	-0.018	21.877	0.543	0.543	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.017	-0.007	25.310	0.426	0.426	0.000	0.000	0.000	0.000
134	A	134	GLN	0	-0.023	-0.005	21.407	-0.109	-0.109	0.000	0.000	0.000	0.000
135	A	135	ASN	0	-0.097	-0.049	23.950	0.266	0.266	0.000	0.000	0.000	0.000
136	A	136	ASP	-1	-0.833	-0.912	27.555	-9.153	-9.153	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.011	0.015	28.138	0.408	0.408	0.000	0.000	0.000	0.000
138	A	138	GLN	0	-0.044	-0.032	29.571	0.063	0.063	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.065	-0.047	31.848	-0.014	-0.014	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.005	0.005	25.719	-0.104	-0.104	0.000	0.000	0.000	0.000
141	A	141	VAL	0	0.011	-0.002	30.008	0.169	0.169	0.000	0.000	0.000	0.000
142	A	142	THR	0	-0.031	-0.032	28.838	-0.388	-0.388	0.000	0.000	0.000	0.000
143	A	143	VAL	0	0.028	0.025	31.074	0.378	0.378	0.000	0.000	0.000	0.000
144	A	144	THR	0	0.018	0.014	27.809	-0.298	-0.298	0.000	0.000	0.000	0.000
145	A	145	THR	0	0.051	0.022	30.181	0.398	0.398	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.010	-0.006	31.692	-0.136	-0.136	0.000	0.000	0.000	0.000
147	A	147	GLY	0	-0.056	-0.029	31.027	0.078	0.078	0.000	0.000	0.000	0.000
148	A	148	VAL	0	0.040	0.015	26.369	-0.181	-0.181	0.000	0.000	0.000	0.000
149	A	149	GLU	-1	-0.723	-0.838	28.735	-9.090	-9.090	0.000	0.000	0.000	0.000
150	A	150	LYS	1	0.907	0.946	31.183	9.084	9.084	0.000	0.000	0.000	0.000
151	A	151	MET	0	-0.038	0.003	24.430	0.015	0.015	0.000	0.000	0.000	0.000
152	A	152	MET	0	0.049	0.015	26.316	-0.231	-0.231	0.000	0.000	0.000	0.000
153	A	153	ILE	0	-0.024	-0.009	28.329	0.029	0.029	0.000	0.000	0.000	0.000
154	A	154	ARG	1	0.903	0.950	28.908	10.648	10.648	0.000	0.000	0.000	0.000
155	A	155	ALA	0	-0.008	0.012	25.535	-0.018	-0.018	0.000	0.000	0.000	0.000
156	A	156	GLY	0	0.037	0.019	27.458	-0.181	-0.181	0.000	0.000	0.000	0.000
157	A	157	LEU	0	0.001	-0.004	25.571	0.208	0.208	0.000	0.000	0.000	0.000
158	A	158	ASP	-1	-0.843	-0.901	29.718	-8.689	-8.689	0.000	0.000	0.000	0.000
159	A	159	VAL	0	0.011	0.001	30.635	-0.178	-0.178	0.000	0.000	0.000	0.000
160	A	160	SER	0	-0.032	-0.005	33.551	0.355	0.355	0.000	0.000	0.000	0.000
161	A	161	ARG	1	0.795	0.859	36.076	8.209	8.209	0.000	0.000	0.000	0.000
162	A	162	PHE	0	-0.009	-0.002	36.092	0.232	0.232	0.000	0.000	0.000	0.000
163	A	163	GLY	0	0.023	0.002	40.171	0.283	0.283	0.000	0.000	0.000	0.000
164	A	164	PRO	0	-0.021	-0.013	40.765	-0.226	-0.226	0.000	0.000	0.000	0.000
165	A	165	HIS	0	0.047	0.046	38.578	-0.200	-0.200	0.000	0.000	0.000	0.000
166	A	166	LEU	0	0.025	0.010	39.397	0.232	0.232	0.000	0.000	0.000	0.000
167	A	167	LYS	1	0.870	0.931	39.068	7.551	7.551	0.000	0.000	0.000	0.000
168	A	168	ILE	0	0.053	0.038	36.200	0.161	0.161	0.000	0.000	0.000	0.000
169	A	169	GLY	0	0.062	0.032	36.536	-0.264	-0.264	0.000	0.000	0.000	0.000
170	A	170	ILE	0	-0.029	-0.028	33.488	0.324	0.324	0.000	0.000	0.000	0.000
171	A	171	GLU	-1	-0.861	-0.903	31.533	-10.173	-10.173	0.000	0.000	0.000	0.000
172	A	172	ARG	1	0.897	0.946	35.576	8.702	8.702	0.000	0.000	0.000	0.000
173	A	173	ALA	0	0.028	0.017	34.633	-0.279	-0.279	0.000	0.000	0.000	0.000
174	A	174	VAL	0	-0.007	-0.024	34.237	0.368	0.368	0.000	0.000	0.000	0.000
175	A	175	ALA	0	0.054	0.049	34.349	-0.301	-0.301	0.000	0.000	0.000	0.000
176	A	176	LEU	0	-0.064	-0.034	31.036	0.242	0.242	0.000	0.000	0.000	0.000
177	A	177	ARG	1	0.938	0.974	33.210	8.227	8.227	0.000	0.000	0.000	0.000
178	A	178	ILE	0	-0.007	-0.004	27.989	0.135	0.135	0.000	0.000	0.000	0.000
179	A	179	GLU	-1	-0.809	-0.878	31.042	-9.244	-9.244	0.000	0.000	0.000	0.000
180	A	180	LEU	0	-0.024	0.000	26.576	-0.210	-0.210	0.000	0.000	0.000	0.000
181	A	181	ASN	0	0.008	-0.020	29.735	-0.252	-0.252	0.000	0.000	0.000	0.000
182	A	182	ALA	0	0.060	0.014	30.595	-0.301	-0.301	0.000	0.000	0.000	0.000
183	A	183	LYS	1	0.846	0.936	30.875	9.067	9.067	0.000	0.000	0.000	0.000
184	A	184	THR	0	0.030	-0.005	27.206	-0.250	-0.250	0.000	0.000	0.000	0.000
185	A	185	GLN	0	-0.017	-0.003	26.314	-0.491	-0.491	0.000	0.000	0.000	0.000
186	A	186	ILE	0	-0.012	0.000	26.025	-0.424	-0.424	0.000	0.000	0.000	0.000
187	A	187	ALA	0	-0.048	-0.013	27.007	-0.261	-0.261	0.000	0.000	0.000	0.000
188	A	188	LEU	0	-0.032	-0.005	22.071	-0.425	-0.425	0.000	0.000	0.000	0.000
189	A	189	TYR	0	-0.059	-0.060	20.278	-0.574	-0.574	0.000	0.000	0.000	0.000
190	A	190	GLY	0	0.017	0.025	23.118	-0.200	-0.200	0.000	0.000	0.000	0.000
191	A	191	GLY	0	-0.027	-0.021	25.935	0.451	0.451	0.000	0.000	0.000	0.000
192	A	192	VAL	0	-0.019	-0.015	27.085	-0.168	-0.168	0.000	0.000	0.000	0.000
193	A	193	LEU	0	-0.015	-0.004	22.720	-0.286	-0.286	0.000	0.000	0.000	0.000
194	A	194	VAL	0	-0.023	-0.015	25.820	0.425	0.425	0.000	0.000	0.000	0.000
195	A	195	GLU	-1	-0.833	-0.904	24.990	-12.358	-12.358	0.000	0.000	0.000	0.000
196	A	196	GLN	0	-0.045	-0.032	24.891	0.634	0.634	0.000	0.000	0.000	0.000
197	A	197	ARG	0	-0.065	-0.032	26.142	0.191	0.191	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:397:GLY)