FMO DATABASE

FMODB ID: 2JVMR

Calculation Name: 2YT4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2YT4

Chain ID: A

ChEMBL ID:

UniProt ID: Q8WYQ5

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	205
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2298420.268166
FMO2-HF: Nuclear repulsion	2216382.515968
FMO2-HF: Total energy	-82037.752198
FMO2-MP2: Total energy	-82274.253408

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:489:GLY)

Summations of interaction energy for fragment #1(A:489: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.
-1.215	0.609	2.323	-2.169	-1.978	0.002

Interaction energy analysis for fragmet #1(A:489:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.005 / q_NPA : -0.018

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	491	HIS	0	-0.023	-0.027	3.798	-1.280	-0.480	-0.011	-0.485	-0.304	0.001
4	A	492	MET	0	0.006	0.020	6.245	0.359	0.359	0.000	0.000	0.000	0.000
5	A	493	SER	0	0.039	0.014	8.959	-0.123	-0.123	0.000	0.000	0.000	0.000
6	A	494	VAL	0	-0.010	0.008	12.150	0.040	0.040	0.000	0.000	0.000	0.000
7	A	495	GLN	0	0.038	0.023	14.332	-0.027	-0.027	0.000	0.000	0.000	0.000
8	A	496	ASP	-1	-0.850	-0.923	18.060	0.016	0.016	0.000	0.000	0.000	0.000
9	A	497	ALA	0	-0.024	-0.047	21.333	-0.010	-0.010	0.000	0.000	0.000	0.000
10	A	498	PRO	0	0.036	0.049	22.347	0.007	0.007	0.000	0.000	0.000	0.000
11	A	499	THR	0	0.051	0.018	23.773	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	500	LYS	1	0.897	0.938	23.796	0.009	0.009	0.000	0.000	0.000	0.000
13	A	501	LYS	1	0.842	0.931	21.322	0.007	0.007	0.000	0.000	0.000	0.000
14	A	502	GLU	-1	-0.836	-0.919	16.504	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	503	PHE	0	-0.092	-0.036	15.030	-0.027	-0.027	0.000	0.000	0.000	0.000
16	A	504	VAL	0	0.069	0.030	10.425	0.018	0.018	0.000	0.000	0.000	0.000
17	A	505	ILE	0	-0.042	-0.011	8.644	-0.030	-0.030	0.000	0.000	0.000	0.000
18	A	506	ASN	0	0.078	0.040	6.428	-0.401	-0.401	0.000	0.000	0.000	0.000
19	A	507	PRO	0	-0.010	0.004	2.702	-0.214	0.224	0.098	-0.127	-0.409	0.000
20	A	508	ASN	0	0.020	-0.001	2.150	0.593	0.960	2.233	-1.412	-1.188	0.001
21	A	509	GLY	0	0.056	0.030	4.136	0.065	0.174	0.003	-0.072	-0.040	0.000
22	A	510	LYS	1	0.783	0.886	6.867	0.679	0.679	0.000	0.000	0.000	0.000
23	A	511	SER	0	0.003	-0.003	7.639	0.022	0.022	0.000	0.000	0.000	0.000
24	A	512	GLU	-1	-0.763	-0.887	9.084	0.398	0.398	0.000	0.000	0.000	0.000
25	A	513	VAL	0	-0.022	-0.016	10.770	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	514	CYS	0	-0.044	-0.012	11.524	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	515	ILE	0	0.034	0.032	6.456	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	516	LEU	0	0.020	0.018	10.701	0.003	0.003	0.000	0.000	0.000	0.000
29	A	517	HIS	0	-0.036	-0.019	13.622	0.009	0.009	0.000	0.000	0.000	0.000
30	A	518	GLU	-1	-0.806	-0.887	11.857	-0.315	-0.315	0.000	0.000	0.000	0.000
31	A	519	TYR	0	0.021	-0.001	12.925	0.007	0.007	0.000	0.000	0.000	0.000
32	A	520	MET	0	0.019	0.022	14.733	0.007	0.007	0.000	0.000	0.000	0.000
33	A	521	GLN	0	0.022	0.029	18.116	0.000	0.000	0.000	0.000	0.000	0.000
34	A	522	ARG	1	0.774	0.849	12.689	0.226	0.226	0.000	0.000	0.000	0.000
35	A	523	VAL	0	-0.041	-0.021	16.193	0.001	0.001	0.000	0.000	0.000	0.000
36	A	524	LEU	0	-0.041	-0.018	19.062	0.005	0.005	0.000	0.000	0.000	0.000
37	A	525	LYS	1	0.902	0.973	21.181	0.045	0.045	0.000	0.000	0.000	0.000
38	A	526	VAL	0	0.026	0.010	22.109	0.003	0.003	0.000	0.000	0.000	0.000
39	A	527	ARG	1	0.940	0.973	21.583	0.019	0.019	0.000	0.000	0.000	0.000
40	A	528	PRO	0	0.011	0.007	18.427	0.006	0.006	0.000	0.000	0.000	0.000
41	A	529	VAL	0	-0.018	-0.003	21.520	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	530	TYR	0	0.003	-0.017	17.155	0.010	0.010	0.000	0.000	0.000	0.000
43	A	531	ASN	0	0.000	0.004	23.598	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	532	PHE	0	-0.015	-0.037	22.644	0.004	0.004	0.000	0.000	0.000	0.000
45	A	533	PHE	0	0.021	0.017	25.121	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	534	GLU	-1	-0.938	-0.967	28.096	0.042	0.042	0.000	0.000	0.000	0.000
47	A	535	CYS	0	-0.025	-0.011	27.765	0.005	0.005	0.000	0.000	0.000	0.000
48	A	536	GLU	-1	-0.884	-0.932	30.137	0.048	0.048	0.000	0.000	0.000	0.000
49	A	537	ASN	0	0.011	-0.014	27.218	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	538	PRO	0	0.020	-0.008	29.342	0.002	0.002	0.000	0.000	0.000	0.000
51	A	539	SER	0	-0.005	0.014	25.645	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	540	GLU	-1	-0.973	-1.006	21.398	0.136	0.136	0.000	0.000	0.000	0.000
53	A	541	PRO	0	0.032	0.043	25.608	0.002	0.002	0.000	0.000	0.000	0.000
54	A	542	PHE	0	-0.015	-0.009	23.982	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	543	GLY	0	0.098	0.055	24.068	0.011	0.011	0.000	0.000	0.000	0.000
56	A	544	ALA	0	-0.095	-0.064	21.122	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	545	SER	0	0.041	0.027	22.272	0.014	0.014	0.000	0.000	0.000	0.000
58	A	546	VAL	0	0.004	0.008	18.625	-0.013	-0.013	0.000	0.000	0.000	0.000
59	A	547	THR	0	-0.005	-0.002	22.093	0.005	0.005	0.000	0.000	0.000	0.000
60	A	548	ILE	0	-0.013	-0.033	21.140	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	549	ASP	-1	-0.890	-0.946	25.329	0.026	0.026	0.000	0.000	0.000	0.000
62	A	550	GLY	0	0.011	0.009	29.005	0.001	0.001	0.000	0.000	0.000	0.000
63	A	551	VAL	0	-0.008	0.013	26.780	0.003	0.003	0.000	0.000	0.000	0.000
64	A	552	THR	0	0.009	0.000	24.600	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	553	TYR	0	-0.048	-0.039	20.753	0.003	0.003	0.000	0.000	0.000	0.000
66	A	554	GLY	0	0.047	0.043	18.982	0.008	0.008	0.000	0.000	0.000	0.000
67	A	555	SER	0	-0.020	-0.031	20.054	-0.023	-0.023	0.000	0.000	0.000	0.000
68	A	556	GLY	0	-0.021	-0.026	19.616	0.021	0.021	0.000	0.000	0.000	0.000
69	A	557	THR	0	0.022	0.005	20.342	-0.016	-0.016	0.000	0.000	0.000	0.000
70	A	558	ALA	0	0.008	-0.001	19.441	0.019	0.019	0.000	0.000	0.000	0.000
71	A	559	SER	0	0.085	0.053	21.480	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	560	SER	0	0.015	0.005	20.166	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	561	LYS	1	1.006	1.013	21.240	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	562	LYS	1	0.954	0.973	16.106	0.012	0.012	0.000	0.000	0.000	0.000
75	A	563	LEU	0	0.018	0.002	16.366	0.001	0.001	0.000	0.000	0.000	0.000
76	A	564	ALA	0	0.040	0.036	16.943	0.021	0.021	0.000	0.000	0.000	0.000
77	A	565	LYS	1	0.900	0.966	17.986	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	566	ASN	0	-0.012	-0.030	12.904	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	567	LYS	1	0.881	0.961	14.098	-0.134	-0.134	0.000	0.000	0.000	0.000
80	A	568	ALA	0	0.043	0.031	15.887	0.021	0.021	0.000	0.000	0.000	0.000
81	A	569	ALA	0	-0.013	0.003	14.190	0.004	0.004	0.000	0.000	0.000	0.000
82	A	570	ARG	1	0.831	0.906	7.852	-0.751	-0.751	0.000	0.000	0.000	0.000
83	A	571	ALA	0	0.019	0.018	12.880	0.034	0.034	0.000	0.000	0.000	0.000
84	A	572	THR	0	0.010	-0.018	16.052	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	573	LEU	0	-0.030	-0.017	10.552	-0.024	-0.024	0.000	0.000	0.000	0.000
86	A	574	GLU	-1	-0.887	-0.934	12.612	0.510	0.510	0.000	0.000	0.000	0.000
87	A	575	ILE	0	-0.034	-0.002	14.395	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	576	LEU	0	-0.041	-0.024	16.318	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	577	ILE	0	-0.075	-0.044	11.486	-0.030	-0.030	0.000	0.000	0.000	0.000
90	A	578	PRO	0	-0.023	-0.012	13.918	0.056	0.056	0.000	0.000	0.000	0.000
91	A	579	ASP	-1	-0.762	-0.860	12.772	0.412	0.412	0.000	0.000	0.000	0.000
92	A	580	PHE	0	-0.025	0.066	8.060	0.216	0.216	0.000	0.000	0.000	0.000
93	A	581	VAL	0	0.002	-0.049	9.331	0.153	0.153	0.000	0.000	0.000	0.000
94	A	582	LYS	1	0.818	0.904	4.245	-2.290	-2.098	0.001	-0.068	-0.124	0.000
95	A	583	GLN	0	0.027	-0.030	5.237	0.579	0.497	-0.001	-0.005	0.087	0.000
96	A	592	SER	0	-0.023	-0.008	20.065	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	593	GLU	-1	-0.934	-0.991	20.590	0.166	0.166	0.000	0.000	0.000	0.000
98	A	594	GLU	-1	-0.806	-0.894	22.466	0.107	0.107	0.000	0.000	0.000	0.000
99	A	595	LEU	0	-0.068	-0.021	23.911	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	596	GLU	-1	-0.929	-0.981	20.242	0.185	0.185	0.000	0.000	0.000	0.000
101	A	597	TYR	0	0.039	0.016	22.598	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	598	PHE	0	-0.038	-0.027	25.284	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	599	ASN	0	0.048	0.007	20.304	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	600	HIS	0	-0.080	-0.051	20.523	0.001	0.001	0.000	0.000	0.000	0.000
105	A	601	ILE	0	-0.058	-0.014	24.864	-0.011	-0.011	0.000	0.000	0.000	0.000
106	A	602	SER	0	-0.017	-0.012	27.440	0.005	0.005	0.000	0.000	0.000	0.000
107	A	603	ILE	0	0.070	0.041	26.803	0.002	0.002	0.000	0.000	0.000	0.000
108	A	604	GLU	-1	-0.907	-0.961	30.204	0.030	0.030	0.000	0.000	0.000	0.000
109	A	605	ASP	-1	-0.818	-0.865	32.031	0.039	0.039	0.000	0.000	0.000	0.000
110	A	606	SER	0	0.005	-0.014	33.955	0.002	0.002	0.000	0.000	0.000	0.000
111	A	607	ARG	1	0.874	0.906	32.318	-0.044	-0.044	0.000	0.000	0.000	0.000
112	A	608	VAL	0	-0.001	0.011	31.145	0.002	0.002	0.000	0.000	0.000	0.000
113	A	609	TYR	0	0.051	0.029	33.877	0.002	0.002	0.000	0.000	0.000	0.000
114	A	610	GLU	-1	-0.922	-0.961	36.407	0.046	0.046	0.000	0.000	0.000	0.000
115	A	611	LEU	0	0.024	0.015	31.403	0.001	0.001	0.000	0.000	0.000	0.000
116	A	612	THR	0	0.021	0.009	31.127	0.002	0.002	0.000	0.000	0.000	0.000
117	A	613	SER	0	-0.059	-0.020	33.500	0.001	0.001	0.000	0.000	0.000	0.000
118	A	614	LYS	1	0.929	0.971	35.899	-0.055	-0.055	0.000	0.000	0.000	0.000
119	A	615	ALA	0	-0.042	-0.031	31.100	0.001	0.001	0.000	0.000	0.000	0.000
120	A	616	GLY	0	0.031	0.031	32.809	0.005	0.005	0.000	0.000	0.000	0.000
121	A	617	LEU	0	-0.056	-0.038	28.607	0.004	0.004	0.000	0.000	0.000	0.000
122	A	618	LEU	0	0.005	0.003	31.280	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	619	SER	0	-0.039	-0.033	33.134	0.000	0.000	0.000	0.000	0.000	0.000
124	A	620	PRO	0	0.034	0.003	33.875	0.001	0.001	0.000	0.000	0.000	0.000
125	A	621	TYR	0	0.010	-0.012	34.949	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	622	GLN	0	0.010	0.010	35.286	0.002	0.002	0.000	0.000	0.000	0.000
127	A	623	ILE	0	0.050	0.021	29.227	0.001	0.001	0.000	0.000	0.000	0.000
128	A	624	LEU	0	0.002	0.007	32.110	0.001	0.001	0.000	0.000	0.000	0.000
129	A	625	HIS	0	-0.017	-0.018	34.344	0.000	0.000	0.000	0.000	0.000	0.000
130	A	626	GLU	-1	-0.852	-0.906	30.770	0.078	0.078	0.000	0.000	0.000	0.000
131	A	627	CYS	0	-0.026	-0.009	30.550	0.001	0.001	0.000	0.000	0.000	0.000
132	A	628	LEU	0	-0.027	-0.020	31.547	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	629	LYS	1	0.846	0.920	33.815	-0.068	-0.068	0.000	0.000	0.000	0.000
134	A	630	ARG	1	0.802	0.889	24.615	-0.112	-0.112	0.000	0.000	0.000	0.000
135	A	631	ASN	0	-0.010	-0.027	29.046	0.002	0.002	0.000	0.000	0.000	0.000
136	A	632	HIS	0	0.035	0.023	32.355	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	633	GLY	0	0.009	0.014	34.627	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	634	MET	0	-0.008	-0.001	32.566	0.000	0.000	0.000	0.000	0.000	0.000
139	A	635	GLY	0	-0.023	-0.010	36.878	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	636	ASP	-1	-0.877	-0.927	40.588	0.029	0.029	0.000	0.000	0.000	0.000
141	A	637	THR	0	0.001	-0.012	39.626	0.000	0.000	0.000	0.000	0.000	0.000
142	A	638	SER	0	-0.059	-0.017	42.199	0.000	0.000	0.000	0.000	0.000	0.000
143	A	639	ILE	0	-0.005	-0.017	43.234	0.000	0.000	0.000	0.000	0.000	0.000
144	A	640	LYS	1	0.865	0.940	46.076	-0.018	-0.018	0.000	0.000	0.000	0.000
145	A	641	PHE	0	-0.031	-0.041	49.065	0.000	0.000	0.000	0.000	0.000	0.000
146	A	642	GLU	-1	-0.788	-0.895	50.983	0.017	0.017	0.000	0.000	0.000	0.000
147	A	643	VAL	0	-0.052	-0.029	53.709	0.000	0.000	0.000	0.000	0.000	0.000
148	A	644	VAL	0	0.130	0.063	55.953	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	645	PRO	0	0.019	0.016	58.505	0.001	0.001	0.000	0.000	0.000	0.000
150	A	646	GLY	0	0.021	-0.005	55.193	0.000	0.000	0.000	0.000	0.000	0.000
151	A	647	LYS	1	0.923	0.966	54.613	-0.016	-0.016	0.000	0.000	0.000	0.000
152	A	648	ASN	0	-0.029	-0.019	55.908	0.000	0.000	0.000	0.000	0.000	0.000
153	A	649	GLN	0	0.001	0.001	55.543	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	650	LYS	1	0.921	0.978	46.570	-0.018	-0.018	0.000	0.000	0.000	0.000
155	A	651	SER	0	0.056	0.034	50.824	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	652	GLU	-1	-0.829	-0.910	49.400	0.017	0.017	0.000	0.000	0.000	0.000
157	A	653	TYR	0	-0.027	-0.011	42.538	0.001	0.001	0.000	0.000	0.000	0.000
158	A	654	VAL	0	0.029	-0.011	46.122	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	655	MET	0	-0.034	-0.006	39.060	0.001	0.001	0.000	0.000	0.000	0.000
160	A	656	ALA	0	0.013	0.011	42.803	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	657	CYS	0	0.006	-0.019	37.912	0.002	0.002	0.000	0.000	0.000	0.000
162	A	658	GLY	0	0.097	0.069	38.978	0.000	0.000	0.000	0.000	0.000	0.000
163	A	659	LYS	1	0.821	0.918	33.616	-0.025	-0.025	0.000	0.000	0.000	0.000
164	A	660	HIS	0	-0.011	-0.003	35.099	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	661	THR	0	0.041	0.018	39.980	0.002	0.002	0.000	0.000	0.000	0.000
166	A	662	VAL	0	-0.006	-0.004	39.063	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	663	ARG	1	0.894	0.932	42.514	-0.015	-0.015	0.000	0.000	0.000	0.000
168	A	664	GLY	0	-0.025	-0.010	44.152	0.000	0.000	0.000	0.000	0.000	0.000
169	A	665	TRP	0	0.049	0.034	45.391	0.000	0.000	0.000	0.000	0.000	0.000
170	A	666	CYS	0	-0.114	-0.041	45.818	0.002	0.002	0.000	0.000	0.000	0.000
171	A	667	LYS	1	1.020	0.999	47.488	-0.023	-0.023	0.000	0.000	0.000	0.000
172	A	668	ASN	0	0.067	0.020	47.681	0.001	0.001	0.000	0.000	0.000	0.000
173	A	669	LYS	1	1.027	1.024	47.435	-0.026	-0.026	0.000	0.000	0.000	0.000
174	A	670	ARG	1	0.917	0.961	42.985	-0.039	-0.039	0.000	0.000	0.000	0.000
175	A	671	VAL	0	0.030	0.007	42.185	0.002	0.002	0.000	0.000	0.000	0.000
176	A	672	GLY	0	0.011	0.004	42.359	0.001	0.001	0.000	0.000	0.000	0.000
177	A	673	LYS	1	0.932	0.990	41.697	-0.037	-0.037	0.000	0.000	0.000	0.000
178	A	674	GLN	0	0.033	0.045	38.342	0.004	0.004	0.000	0.000	0.000	0.000
179	A	675	LEU	0	0.040	0.024	37.932	0.001	0.001	0.000	0.000	0.000	0.000
180	A	676	ALA	0	-0.011	-0.005	38.242	0.000	0.000	0.000	0.000	0.000	0.000
181	A	677	SER	0	0.025	-0.018	36.700	0.000	0.000	0.000	0.000	0.000	0.000
182	A	678	GLN	0	-0.060	-0.036	33.957	0.001	0.001	0.000	0.000	0.000	0.000
183	A	679	LYS	1	0.941	0.985	33.881	-0.025	-0.025	0.000	0.000	0.000	0.000
184	A	680	ILE	0	0.012	0.013	34.789	0.000	0.000	0.000	0.000	0.000	0.000
185	A	681	LEU	0	0.019	0.013	30.326	0.001	0.001	0.000	0.000	0.000	0.000
186	A	682	GLN	0	-0.025	-0.012	28.141	0.003	0.003	0.000	0.000	0.000	0.000
187	A	683	LEU	0	-0.038	-0.042	30.753	-0.002	-0.002	0.000	0.000	0.000	0.000
188	A	684	LEU	0	-0.012	-0.001	31.234	-0.001	-0.001	0.000	0.000	0.000	0.000
189	A	685	HIS	1	0.778	0.883	26.021	-0.064	-0.064	0.000	0.000	0.000	0.000
190	A	686	PRO	0	0.015	0.005	27.376	0.002	0.002	0.000	0.000	0.000	0.000
191	A	687	HIS	0	0.011	0.012	23.886	-0.005	-0.005	0.000	0.000	0.000	0.000
192	A	688	VAL	0	0.012	0.014	22.784	0.005	0.005	0.000	0.000	0.000	0.000
193	A	689	LYS	1	0.962	0.986	23.639	-0.046	-0.046	0.000	0.000	0.000	0.000
194	A	690	ASN	0	-0.032	-0.020	20.725	0.003	0.003	0.000	0.000	0.000	0.000
195	A	691	TRP	0	0.089	0.028	24.752	0.001	0.001	0.000	0.000	0.000	0.000
196	A	692	GLY	0	0.053	0.030	22.718	0.003	0.003	0.000	0.000	0.000	0.000
197	A	693	SER	0	-0.009	-0.014	21.122	0.017	0.017	0.000	0.000	0.000	0.000
198	A	694	LEU	0	-0.005	-0.009	22.080	0.003	0.003	0.000	0.000	0.000	0.000
199	A	695	LEU	0	0.014	0.017	24.365	0.001	0.001	0.000	0.000	0.000	0.000
200	A	696	ARG	1	0.841	0.938	17.037	-0.205	-0.205	0.000	0.000	0.000	0.000
201	A	697	MET	0	-0.048	-0.001	21.860	0.004	0.004	0.000	0.000	0.000	0.000
202	A	698	TYR	0	0.026	-0.007	23.814	-0.006	-0.006	0.000	0.000	0.000	0.000
203	A	699	GLY	0	0.025	0.015	25.657	-0.008	-0.008	0.000	0.000	0.000	0.000
204	A	700	ARG	1	0.924	0.971	17.373	-0.270	-0.270	0.000	0.000	0.000	0.000
205	A	701	GLU	-1	-0.868	-0.905	21.298	0.144	0.144	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:489:GLY)