FMO DATABASE

FMODB ID: XYK2X

Calculation Name: 3QPA-A-Xray13

Preferred Name: Cutinase 1

Target Type: SINGLE PROTEIN

Ligand Name: monoethylphosphorylserine

ligand 3-letter code: MIR

PDB ID: 3QPA

Chain ID: A

ChEMBL ID: CHEMBL2176862

UniProt ID: P00590

Base Structure: X-ray

Registration Date: 2017-11-21

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. 1.20171117

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	195
LigandCharge	MIR=-1
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-2086168.534685
FMO2-HF: Nuclear repulsion	2013731.839831
FMO2-HF: Total energy	-72436.694854
FMO2-MP2: Total energy	-72647.690978

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:16:GLY)

Summations of interaction energy for fragment #1(A:16: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.
-0.53899999999999	-8.017	8.136	2.398	-3.056	-0.024

Interaction energy analysis for fragmet #1(A:16:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.845 / q_NPA : 0.928

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	18	THR	0	0.043	0.013	2.228	3.910	-4.499	7.777	2.817	-2.185	-0.017
4	A	19	THR	0	0.013	0.019	3.311	5.727	5.745	0.076	-0.005	-0.089	-0.002
5	A	20	ARG	1	0.650	0.807	6.171	31.238	31.238	0.000	0.000	0.000	0.000
6	A	21	ASP	-1	-0.797	-0.900	8.625	-21.930	-21.930	0.000	0.000	0.000	0.000
7	A	22	ASP	-1	-0.771	-0.868	12.008	-24.050	-24.050	0.000	0.000	0.000	0.000
8	A	23	LEU	0	0.002	0.019	13.950	1.094	1.094	0.000	0.000	0.000	0.000
9	A	24	ILE	0	-0.071	-0.034	15.567	1.254	1.254	0.000	0.000	0.000	0.000
10	A	25	ASN	0	-0.077	-0.043	14.602	1.702	1.702	0.000	0.000	0.000	0.000
11	A	26	GLY	0	0.021	0.032	17.686	-0.130	-0.130	0.000	0.000	0.000	0.000
12	A	27	ASN	0	0.000	-0.008	19.276	1.008	1.008	0.000	0.000	0.000	0.000
13	A	28	SER	0	0.044	0.000	22.489	-0.073	-0.073	0.000	0.000	0.000	0.000
14	A	29	ALA	0	-0.038	-0.012	25.070	0.348	0.348	0.000	0.000	0.000	0.000
15	A	30	SER	0	-0.050	-0.029	23.137	0.375	0.375	0.000	0.000	0.000	0.000
16		109	CYS	0	-0.054	-0.021	22.507	-0.554	-0.554	0.000	0.000	0.000	0.000
17	A	32	ALA	0	-0.002	0.026	18.676	0.081	0.081	0.000	0.000	0.000	0.000
18	A	33	ASP	-1	-0.875	-0.936	20.737	-12.829	-12.829	0.000	0.000	0.000	0.000
19	A	34	VAL	0	-0.036	-0.015	17.825	0.305	0.305	0.000	0.000	0.000	0.000
20	A	35	ILE	0	-0.005	-0.007	17.022	-0.891	-0.891	0.000	0.000	0.000	0.000
21	A	36	PHE	0	0.005	-0.007	10.792	0.126	0.126	0.000	0.000	0.000	0.000
22	A	37	ILE	0	-0.005	0.000	13.912	-1.173	-1.173	0.000	0.000	0.000	0.000
23	A	38	TYR	0	-0.013	-0.001	9.839	-0.210	-0.210	0.000	0.000	0.000	0.000
24	A	39	ALA	0	0.020	0.009	12.295	-0.880	-0.880	0.000	0.000	0.000	0.000
25	A	40	ARG	1	0.835	0.933	10.122	23.247	23.247	0.000	0.000	0.000	0.000
26	A	41	GLY	0	0.048	0.030	11.832	2.145	2.145	0.000	0.000	0.000	0.000
27	A	42	SER	0	0.016	-0.041	13.651	-0.335	-0.335	0.000	0.000	0.000	0.000
28	A	43	THR	0	-0.070	-0.029	14.943	-0.163	-0.163	0.000	0.000	0.000	0.000
29	A	44	GLU	-1	-0.774	-0.858	9.661	-31.061	-31.061	0.000	0.000	0.000	0.000
30	A	45	THR	0	0.003	-0.010	6.923	-0.038	-0.038	0.000	0.000	0.000	0.000
31	A	46	GLY	0	-0.014	-0.010	6.968	-2.580	-2.580	0.000	0.000	0.000	0.000
32	A	47	ASN	0	0.035	0.000	7.670	-0.330	-0.330	0.000	0.000	0.000	0.000
33	A	48	LEU	0	-0.008	0.008	5.207	0.966	0.966	0.000	0.000	0.000	0.000
34	A	49	GLY	0	-0.023	-0.004	6.932	0.594	0.594	0.000	0.000	0.000	0.000
35	A	50	THR	0	-0.067	-0.058	5.430	-8.412	-8.412	0.000	0.000	0.000	0.000
36	A	51	LEU	0	0.001	0.002	6.324	-3.369	-3.369	0.000	0.000	0.000	0.000
37	A	52	GLY	0	0.059	0.032	7.649	0.060	0.060	0.000	0.000	0.000	0.000
38	A	53	PRO	0	-0.046	-0.036	2.844	-3.107	-2.209	0.284	-0.410	-0.772	-0.005
39	A	54	SER	0	-0.007	0.000	5.056	2.312	2.327	-0.001	-0.004	-0.010	0.000
40	A	55	ILE	0	0.029	0.028	6.880	3.272	3.272	0.000	0.000	0.000	0.000
41	A	56	ALA	0	0.002	-0.003	7.336	1.930	1.930	0.000	0.000	0.000	0.000
42	A	57	SER	0	-0.017	0.001	7.409	3.178	3.178	0.000	0.000	0.000	0.000
43	A	58	ASN	0	0.002	-0.012	9.224	3.851	3.851	0.000	0.000	0.000	0.000
44	A	59	LEU	0	0.001	0.007	12.131	2.011	2.011	0.000	0.000	0.000	0.000
45	A	60	GLU	-1	-0.815	-0.912	9.839	-31.533	-31.533	0.000	0.000	0.000	0.000
46	A	61	SER	0	-0.055	-0.024	13.078	1.552	1.552	0.000	0.000	0.000	0.000
47	A	62	ALA	0	-0.062	-0.015	15.388	1.264	1.264	0.000	0.000	0.000	0.000
48	A	63	PHE	0	0.007	-0.013	17.040	1.020	1.020	0.000	0.000	0.000	0.000
49	A	64	GLY	0	0.070	0.054	17.567	0.842	0.842	0.000	0.000	0.000	0.000
50	A	65	LYS	1	0.895	0.929	11.008	23.695	23.695	0.000	0.000	0.000	0.000
51	A	66	ASP	-1	-0.910	-0.968	15.425	-17.587	-17.587	0.000	0.000	0.000	0.000
52	A	67	GLY	0	0.035	0.040	18.261	0.710	0.710	0.000	0.000	0.000	0.000
53	A	68	VAL	0	-0.063	-0.034	14.022	0.172	0.172	0.000	0.000	0.000	0.000
54	A	69	TRP	0	-0.005	0.006	14.465	-0.769	-0.769	0.000	0.000	0.000	0.000
55	A	70	ILE	0	-0.035	-0.030	8.500	-0.344	-0.344	0.000	0.000	0.000	0.000
56	A	71	GLN	0	-0.021	-0.021	11.465	-0.173	-0.173	0.000	0.000	0.000	0.000
57	A	72	GLY	0	0.025	0.010	10.242	0.241	0.241	0.000	0.000	0.000	0.000
58	A	73	VAL	0	-0.012	-0.007	11.118	1.491	1.491	0.000	0.000	0.000	0.000
59	A	74	GLY	0	0.001	-0.016	13.558	-0.884	-0.884	0.000	0.000	0.000	0.000
60	A	75	GLY	0	0.045	0.031	14.079	0.942	0.942	0.000	0.000	0.000	0.000
61	A	76	ALA	0	-0.046	-0.037	17.403	-0.184	-0.184	0.000	0.000	0.000	0.000
62	A	77	TYR	0	-0.043	-0.028	14.440	1.088	1.088	0.000	0.000	0.000	0.000
63	A	78	ARG	1	0.904	0.937	15.866	14.776	14.776	0.000	0.000	0.000	0.000
64	A	79	ALA	0	-0.009	0.032	14.769	-0.416	-0.416	0.000	0.000	0.000	0.000
65	A	80	THR	0	0.052	0.023	16.767	-0.658	-0.658	0.000	0.000	0.000	0.000
66	A	81	LEU	0	0.065	0.029	19.766	0.418	0.418	0.000	0.000	0.000	0.000
67	A	82	GLY	0	0.026	0.012	21.025	0.329	0.329	0.000	0.000	0.000	0.000
68	A	83	ASP	-1	-0.845	-0.939	22.139	-12.664	-12.664	0.000	0.000	0.000	0.000
69	A	84	ASN	0	-0.079	-0.052	20.306	0.038	0.038	0.000	0.000	0.000	0.000
70	A	85	ALA	0	-0.022	-0.015	23.914	0.294	0.294	0.000	0.000	0.000	0.000
71	A	86	LEU	0	-0.022	0.012	25.712	0.546	0.546	0.000	0.000	0.000	0.000
72	A	87	PRO	0	0.007	0.002	28.150	-0.222	-0.222	0.000	0.000	0.000	0.000
73	A	88	ARG	1	0.768	0.838	26.879	10.959	10.959	0.000	0.000	0.000	0.000
74	A	89	GLY	0	-0.044	-0.012	24.674	-0.378	-0.378	0.000	0.000	0.000	0.000
75	A	90	THR	0	0.026	-0.006	20.788	-0.742	-0.742	0.000	0.000	0.000	0.000
76	A	91	SER	0	0.013	0.023	22.459	0.685	0.685	0.000	0.000	0.000	0.000
77	A	92	SER	0	0.051	0.003	24.157	-0.254	-0.254	0.000	0.000	0.000	0.000
78	A	93	ALA	0	-0.022	-0.004	23.724	-0.023	-0.023	0.000	0.000	0.000	0.000
79	A	94	ALA	0	0.010	0.001	19.786	-0.315	-0.315	0.000	0.000	0.000	0.000
80	A	95	ILE	0	0.058	0.023	20.852	-0.429	-0.429	0.000	0.000	0.000	0.000
81	A	96	ARG	1	0.946	0.982	23.238	11.517	11.517	0.000	0.000	0.000	0.000
82	A	97	GLU	-1	-0.879	-0.933	17.917	-15.582	-15.582	0.000	0.000	0.000	0.000
83	A	98	MET	0	0.001	0.008	16.658	-0.266	-0.266	0.000	0.000	0.000	0.000
84	A	99	LEU	0	-0.001	0.002	19.866	-0.032	-0.032	0.000	0.000	0.000	0.000
85	A	100	GLY	0	0.014	0.014	22.841	0.237	0.237	0.000	0.000	0.000	0.000
86	A	101	LEU	0	-0.025	-0.014	15.989	-0.031	-0.031	0.000	0.000	0.000	0.000
87	A	102	PHE	0	0.060	0.012	20.048	-0.056	-0.056	0.000	0.000	0.000	0.000
88	A	103	GLN	0	-0.001	0.001	22.012	0.292	0.292	0.000	0.000	0.000	0.000
89	A	104	GLN	0	0.019	-0.003	20.278	0.104	0.104	0.000	0.000	0.000	0.000
90	A	105	ALA	0	0.015	0.008	20.384	0.155	0.155	0.000	0.000	0.000	0.000
91	A	106	ASN	0	-0.003	0.006	22.186	0.331	0.331	0.000	0.000	0.000	0.000
92	A	107	THR	0	-0.024	-0.012	25.780	0.489	0.489	0.000	0.000	0.000	0.000
93	A	108	LYS	1	0.857	0.937	20.545	14.566	14.566	0.000	0.000	0.000	0.000
94	A	110	PRO	0	0.004	0.005	25.209	-0.252	-0.252	0.000	0.000	0.000	0.000
95	A	111	ASP	-1	-0.880	-0.935	27.674	-10.244	-10.244	0.000	0.000	0.000	0.000
96	A	112	ALA	0	-0.038	-0.006	22.113	-0.161	-0.161	0.000	0.000	0.000	0.000
97	A	113	THR	0	-0.039	-0.008	22.901	0.374	0.374	0.000	0.000	0.000	0.000
98	A	114	LEU	0	-0.012	-0.006	20.448	-0.815	-0.815	0.000	0.000	0.000	0.000
99	A	115	ILE	0	0.004	0.003	16.300	0.256	0.256	0.000	0.000	0.000	0.000
100	A	116	ALA	0	0.006	0.005	16.704	-0.650	-0.650	0.000	0.000	0.000	0.000
101	A	117	GLY	0	0.030	-0.002	15.232	0.043	0.043	0.000	0.000	0.000	0.000
102	A	118	GLY	0	0.010	0.006	14.253	-0.333	-0.333	0.000	0.000	0.000	0.000
103	A	119	TYR	0	-0.074	-0.037	12.391	0.644	0.644	0.000	0.000	0.000	0.000
104	A	120	MIR	-1	-0.790	-0.838	15.010	-17.978	-17.978	0.000	0.000	0.000	0.000
105	A	121	GLN	0	0.028	-0.001	17.666	0.889	0.889	0.000	0.000	0.000	0.000
106	A	122	GLY	0	0.038	0.020	15.506	0.627	0.627	0.000	0.000	0.000	0.000
107	A	123	ALA	0	-0.047	-0.024	16.572	0.265	0.265	0.000	0.000	0.000	0.000
108	A	124	ALA	0	-0.006	0.000	18.754	0.687	0.687	0.000	0.000	0.000	0.000
109	A	125	LEU	0	-0.034	-0.008	17.175	0.571	0.571	0.000	0.000	0.000	0.000
110	A	126	ALA	0	0.045	0.007	18.079	0.509	0.509	0.000	0.000	0.000	0.000
111	A	127	ALA	0	-0.017	-0.008	20.029	0.568	0.568	0.000	0.000	0.000	0.000
112	A	128	ALA	0	0.011	0.003	23.458	0.524	0.524	0.000	0.000	0.000	0.000
113	A	129	SER	0	0.004	-0.020	21.701	0.457	0.457	0.000	0.000	0.000	0.000
114	A	130	ILE	0	-0.007	-0.004	21.068	0.377	0.377	0.000	0.000	0.000	0.000
115	A	131	GLU	-1	-0.913	-0.940	24.863	-10.087	-10.087	0.000	0.000	0.000	0.000
116	A	132	ASP	-1	-0.781	-0.883	27.373	-10.445	-10.445	0.000	0.000	0.000	0.000
117	A	133	LEU	0	-0.114	-0.028	24.313	0.239	0.239	0.000	0.000	0.000	0.000
118	A	134	ASP	-1	-0.838	-0.921	27.959	-9.352	-9.352	0.000	0.000	0.000	0.000
119	A	135	SER	0	0.042	-0.002	29.627	-0.260	-0.260	0.000	0.000	0.000	0.000
120	A	136	ALA	0	0.040	0.036	30.824	-0.163	-0.163	0.000	0.000	0.000	0.000
121	A	137	ILE	0	-0.037	-0.019	25.289	-0.275	-0.275	0.000	0.000	0.000	0.000
122	A	138	ARG	1	0.859	0.919	26.129	10.112	10.112	0.000	0.000	0.000	0.000
123	A	139	ASP	-1	-0.901	-0.952	26.730	-10.358	-10.358	0.000	0.000	0.000	0.000
124	A	140	LYS	1	0.832	0.918	25.948	11.316	11.316	0.000	0.000	0.000	0.000
125	A	141	ILE	0	-0.061	-0.013	21.223	-0.541	-0.541	0.000	0.000	0.000	0.000
126	A	142	ALA	0	0.018	0.015	23.137	0.363	0.363	0.000	0.000	0.000	0.000
127	A	143	GLY	0	0.015	0.002	21.937	0.353	0.353	0.000	0.000	0.000	0.000
128	A	144	THR	0	-0.014	-0.016	19.306	-0.801	-0.801	0.000	0.000	0.000	0.000
129	A	145	VAL	0	-0.034	-0.003	15.310	0.488	0.488	0.000	0.000	0.000	0.000
130	A	146	LEU	0	-0.024	-0.005	17.288	-0.719	-0.719	0.000	0.000	0.000	0.000
131	A	147	PHE	0	0.042	0.021	13.414	0.163	0.163	0.000	0.000	0.000	0.000
132	A	148	GLY	0	0.020	0.007	17.116	-0.266	-0.266	0.000	0.000	0.000	0.000
133	A	149	TYR	0	-0.012	-0.037	19.126	-0.040	-0.040	0.000	0.000	0.000	0.000
134	A	150	THR	0	0.073	0.029	21.005	0.723	0.723	0.000	0.000	0.000	0.000
135	A	151	LYS	1	0.941	0.984	23.406	11.992	11.992	0.000	0.000	0.000	0.000
136	A	152	ASN	0	0.006	0.009	24.678	0.272	0.272	0.000	0.000	0.000	0.000
137	A	153	LEU	0	0.026	0.020	26.505	0.382	0.382	0.000	0.000	0.000	0.000
138	A	154	GLN	0	-0.015	-0.021	28.818	0.188	0.188	0.000	0.000	0.000	0.000
139	A	155	ASN	0	0.035	0.020	27.013	0.668	0.668	0.000	0.000	0.000	0.000
140	A	156	ARG	1	0.859	0.919	30.288	9.300	9.300	0.000	0.000	0.000	0.000
141	A	157	GLY	0	0.019	0.015	27.250	0.128	0.128	0.000	0.000	0.000	0.000
142	A	158	ARG	1	0.846	0.933	27.122	10.009	10.009	0.000	0.000	0.000	0.000
143	A	159	ILE	0	0.034	0.035	22.602	-0.239	-0.239	0.000	0.000	0.000	0.000
144	A	160	PRO	0	0.024	0.007	26.903	0.257	0.257	0.000	0.000	0.000	0.000
145	A	161	ASN	0	-0.022	-0.006	29.187	0.024	0.024	0.000	0.000	0.000	0.000
146	A	162	TYR	0	0.012	-0.005	23.919	-0.100	-0.100	0.000	0.000	0.000	0.000
147	A	163	PRO	0	0.021	0.022	28.544	0.123	0.123	0.000	0.000	0.000	0.000
148	A	164	ALA	0	0.016	-0.009	28.220	-0.398	-0.398	0.000	0.000	0.000	0.000
149	A	165	ASP	-1	-0.830	-0.901	27.737	-11.270	-11.270	0.000	0.000	0.000	0.000
150	A	166	ARG	1	0.906	0.972	25.357	10.989	10.989	0.000	0.000	0.000	0.000
151	A	167	THR	0	-0.034	-0.025	23.647	-0.689	-0.689	0.000	0.000	0.000	0.000
152	A	168	LYS	1	0.939	0.988	20.468	14.387	14.387	0.000	0.000	0.000	0.000
153	A	169	VAL	0	-0.027	-0.015	20.571	-0.811	-0.811	0.000	0.000	0.000	0.000
154	A	170	PHE	0	-0.010	0.003	17.824	0.340	0.340	0.000	0.000	0.000	0.000
155		178	CYS	0	-0.065	-0.033	19.606	-0.609	-0.609	0.000	0.000	0.000	0.000
156	A	172	ASN	0	0.002	0.006	18.126	0.861	0.861	0.000	0.000	0.000	0.000
157	A	173	THR	0	0.038	0.002	22.167	0.252	0.252	0.000	0.000	0.000	0.000
158	A	174	GLY	0	0.022	0.007	24.535	-0.244	-0.244	0.000	0.000	0.000	0.000
159	A	175	ASP	-1	-0.758	-0.845	20.292	-15.567	-15.567	0.000	0.000	0.000	0.000
160	A	176	LEU	0	0.033	-0.003	23.318	0.305	0.305	0.000	0.000	0.000	0.000
161	A	177	VAL	0	-0.005	0.003	21.097	0.387	0.387	0.000	0.000	0.000	0.000
162	A	179	THR	0	-0.057	-0.037	25.247	0.474	0.474	0.000	0.000	0.000	0.000
163	A	180	GLY	0	0.032	0.014	28.073	0.403	0.403	0.000	0.000	0.000	0.000
164	A	181	SER	0	-0.022	0.012	27.730	0.175	0.175	0.000	0.000	0.000	0.000
165	A	182	LEU	0	0.038	0.001	24.199	-0.379	-0.379	0.000	0.000	0.000	0.000
166	A	183	ILE	0	-0.038	-0.012	24.494	-0.393	-0.393	0.000	0.000	0.000	0.000
167	A	184	VAL	0	0.023	0.014	19.045	-0.211	-0.211	0.000	0.000	0.000	0.000
168	A	185	ALA	0	0.028	0.015	22.205	0.312	0.312	0.000	0.000	0.000	0.000
169	A	186	ALA	0	0.047	0.008	20.107	-0.619	-0.619	0.000	0.000	0.000	0.000
170	A	187	PRO	0	0.041	0.019	19.093	-0.925	-0.925	0.000	0.000	0.000	0.000
171	A	188	HIS	1	0.783	0.869	17.809	16.476	16.476	0.000	0.000	0.000	0.000
172	A	189	LEU	0	-0.004	0.005	14.871	-0.913	-0.913	0.000	0.000	0.000	0.000
173	A	190	ALA	0	-0.035	-0.007	14.343	-1.336	-1.336	0.000	0.000	0.000	0.000
174	A	191	TYR	0	0.027	-0.001	13.636	0.803	0.803	0.000	0.000	0.000	0.000
175	A	192	GLY	0	-0.002	0.004	10.589	-0.934	-0.934	0.000	0.000	0.000	0.000
176	A	193	PRO	0	-0.018	-0.034	11.468	-1.044	-1.044	0.000	0.000	0.000	0.000
177	A	194	ASP	-1	-0.775	-0.901	13.983	-17.719	-17.719	0.000	0.000	0.000	0.000
178	A	195	ALA	0	-0.049	-0.030	9.892	0.184	0.184	0.000	0.000	0.000	0.000
179	A	196	ARG	1	0.922	0.953	9.314	26.565	26.565	0.000	0.000	0.000	0.000
180	A	197	GLY	0	0.042	0.035	11.487	0.275	0.275	0.000	0.000	0.000	0.000
181	A	198	PRO	0	0.036	0.023	15.204	0.145	0.145	0.000	0.000	0.000	0.000
182	A	199	ALA	0	-0.012	-0.008	14.147	0.683	0.683	0.000	0.000	0.000	0.000
183	A	200	PRO	0	-0.002	-0.006	12.532	0.639	0.639	0.000	0.000	0.000	0.000
184	A	201	GLU	-1	-0.941	-0.955	15.159	-14.306	-14.306	0.000	0.000	0.000	0.000
185	A	202	PHE	0	0.009	0.001	18.426	0.638	0.638	0.000	0.000	0.000	0.000
186	A	203	LEU	0	-0.031	-0.019	15.155	0.512	0.512	0.000	0.000	0.000	0.000
187	A	204	ILE	0	-0.009	-0.006	16.014	0.595	0.595	0.000	0.000	0.000	0.000
188	A	205	GLU	-1	-0.945	-0.963	19.825	-12.129	-12.129	0.000	0.000	0.000	0.000
189	A	206	LYS	1	0.833	0.898	22.554	12.559	12.559	0.000	0.000	0.000	0.000
190	A	207	VAL	0	-0.012	-0.009	20.195	0.478	0.478	0.000	0.000	0.000	0.000
191	A	208	ARG	1	0.953	0.974	21.102	14.867	14.867	0.000	0.000	0.000	0.000
192	A	209	ALA	0	-0.058	-0.008	25.409	0.488	0.488	0.000	0.000	0.000	0.000
193	A	210	VAL	0	-0.072	-0.042	26.349	0.429	0.429	0.000	0.000	0.000	0.000
194	A	211	ARG	1	0.853	0.921	24.012	12.818	12.818	0.000	0.000	0.000	0.000
195	A	212	GLY	-1	-0.927	-0.949	26.949	-11.724	-11.724	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:GLY)