FMO DATABASE

FMODB ID: 721KK

Calculation Name: 2YT4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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:

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. 2.20220422

FMO calculation

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2299134.134862
FMO2-HF: Nuclear repulsion	2217098.089376
FMO2-HF: Total energy	-82036.045486
FMO2-MP2: Total energy	-82272.764501

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: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.
-1.256	0.482	2.128	-2.01	-1.856	-0.001

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 : -0.007 / q_NPA : -0.019

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	-0.032	-0.033	3.798	-1.338	-0.543	-0.011	-0.487	-0.297	0.000
4	A	492	MET	0	0.000	0.021	5.691	0.355	0.355	0.000	0.000	0.000	0.000
5	A	493	SER	0	0.027	0.005	8.980	-0.124	-0.124	0.000	0.000	0.000	0.000
6	A	494	VAL	0	-0.003	0.015	12.203	0.042	0.042	0.000	0.000	0.000	0.000
7	A	495	GLN	0	0.055	0.040	14.351	-0.046	-0.046	0.000	0.000	0.000	0.000
8	A	496	ASP	-1	-0.885	-0.945	18.080	0.025	0.025	0.000	0.000	0.000	0.000
9	A	497	ALA	0	-0.038	-0.073	21.351	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	498	PRO	0	0.002	0.022	22.494	0.008	0.008	0.000	0.000	0.000	0.000
11	A	499	THR	0	0.101	0.038	24.380	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	500	LYS	1	0.873	0.934	23.830	0.008	0.008	0.000	0.000	0.000	0.000
13	A	501	LYS	1	0.917	0.977	21.001	0.021	0.021	0.000	0.000	0.000	0.000
14	A	502	GLU	-1	-0.873	-0.944	16.813	-0.032	-0.032	0.000	0.000	0.000	0.000
15	A	503	PHE	0	-0.080	-0.036	15.018	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	504	VAL	0	0.071	0.033	10.327	0.020	0.020	0.000	0.000	0.000	0.000
17	A	505	ILE	0	-0.053	-0.024	8.657	-0.033	-0.033	0.000	0.000	0.000	0.000
18	A	506	ASN	0	0.080	0.038	6.554	-0.382	-0.382	0.000	0.000	0.000	0.000
19	A	507	PRO	0	-0.007	-0.004	2.875	-0.239	0.121	0.054	-0.091	-0.324	0.000
20	A	508	ASN	0	0.038	0.009	2.144	0.696	1.140	2.084	-1.334	-1.194	-0.001
21	A	509	GLY	0	0.045	0.025	4.120	0.126	0.222	0.003	-0.063	-0.035	0.000
22	A	510	LYS	1	0.778	0.877	6.855	0.718	0.718	0.000	0.000	0.000	0.000
23	A	511	SER	0	0.000	0.001	7.621	0.005	0.005	0.000	0.000	0.000	0.000
24	A	512	GLU	-1	-0.763	-0.870	8.970	0.353	0.353	0.000	0.000	0.000	0.000
25	A	513	VAL	0	-0.017	-0.012	10.759	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	514	CYS	0	-0.026	-0.009	11.719	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	515	ILE	0	0.038	0.035	6.383	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	516	LEU	0	0.013	0.009	10.697	0.008	0.008	0.000	0.000	0.000	0.000
29	A	517	HIS	0	-0.019	-0.011	13.620	0.010	0.010	0.000	0.000	0.000	0.000
30	A	518	GLU	-1	-0.810	-0.893	11.789	-0.327	-0.327	0.000	0.000	0.000	0.000
31	A	519	TYR	0	-0.006	-0.010	12.983	0.008	0.008	0.000	0.000	0.000	0.000
32	A	520	MET	0	0.023	0.031	14.737	0.007	0.007	0.000	0.000	0.000	0.000
33	A	521	GLN	0	0.033	0.025	18.068	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	522	ARG	1	0.807	0.891	12.801	0.227	0.227	0.000	0.000	0.000	0.000
35	A	523	VAL	0	-0.048	-0.020	16.249	0.000	0.000	0.000	0.000	0.000	0.000
36	A	524	LEU	0	-0.036	-0.007	19.071	0.005	0.005	0.000	0.000	0.000	0.000
37	A	525	LYS	1	0.896	0.967	21.186	0.043	0.043	0.000	0.000	0.000	0.000
38	A	526	VAL	0	0.024	0.007	21.912	0.003	0.003	0.000	0.000	0.000	0.000
39	A	527	ARG	1	0.948	0.970	21.584	0.020	0.020	0.000	0.000	0.000	0.000
40	A	528	PRO	0	-0.009	-0.013	18.578	0.006	0.006	0.000	0.000	0.000	0.000
41	A	529	VAL	0	-0.030	0.008	21.517	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	530	TYR	0	-0.006	-0.021	17.160	0.011	0.011	0.000	0.000	0.000	0.000
43	A	531	ASN	0	0.001	0.005	23.590	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	532	PHE	0	-0.020	-0.039	22.758	0.004	0.004	0.000	0.000	0.000	0.000
45	A	533	PHE	0	0.026	0.022	24.952	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	534	GLU	-1	-0.948	-0.973	28.102	0.041	0.041	0.000	0.000	0.000	0.000
47	A	535	CYS	0	-0.025	-0.011	27.276	0.005	0.005	0.000	0.000	0.000	0.000
48	A	536	GLU	-1	-0.891	-0.937	30.141	0.048	0.048	0.000	0.000	0.000	0.000
49	A	537	ASN	0	0.013	-0.014	27.613	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	538	PRO	0	0.018	-0.003	29.345	0.001	0.001	0.000	0.000	0.000	0.000
51	A	539	SER	0	-0.009	0.010	25.691	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	540	GLU	-1	-1.035	-1.032	21.969	0.131	0.131	0.000	0.000	0.000	0.000
53	A	541	PRO	0	0.035	0.044	25.611	0.002	0.002	0.000	0.000	0.000	0.000
54	A	542	PHE	0	-0.034	-0.014	23.928	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	543	GLY	0	0.092	0.047	24.078	0.011	0.011	0.000	0.000	0.000	0.000
56	A	544	ALA	0	-0.094	-0.058	21.117	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	545	SER	0	0.041	0.024	22.266	0.015	0.015	0.000	0.000	0.000	0.000
58	A	546	VAL	0	0.015	0.015	18.685	-0.014	-0.014	0.000	0.000	0.000	0.000
59	A	547	THR	0	-0.004	-0.009	22.089	0.005	0.005	0.000	0.000	0.000	0.000
60	A	548	ILE	0	-0.010	-0.035	21.512	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	549	ASP	-1	-0.929	-0.972	25.330	0.026	0.026	0.000	0.000	0.000	0.000
62	A	550	GLY	0	0.002	0.005	29.011	0.001	0.001	0.000	0.000	0.000	0.000
63	A	551	VAL	0	-0.013	0.015	26.783	0.003	0.003	0.000	0.000	0.000	0.000
64	A	552	THR	0	-0.023	-0.014	24.404	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	553	TYR	0	-0.046	-0.031	20.632	0.003	0.003	0.000	0.000	0.000	0.000
66	A	554	GLY	0	0.049	0.038	18.981	0.008	0.008	0.000	0.000	0.000	0.000
67	A	555	SER	0	-0.021	-0.031	20.053	-0.024	-0.024	0.000	0.000	0.000	0.000
68	A	556	GLY	0	-0.024	-0.029	19.628	0.021	0.021	0.000	0.000	0.000	0.000
69	A	557	THR	0	0.021	0.008	20.354	-0.017	-0.017	0.000	0.000	0.000	0.000
70	A	558	ALA	0	-0.003	-0.028	19.485	0.019	0.019	0.000	0.000	0.000	0.000
71	A	559	SER	0	0.112	0.074	21.356	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	560	SER	0	0.019	0.007	20.243	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	561	LYS	1	1.019	1.017	21.247	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	562	LYS	1	0.943	0.965	15.872	0.019	0.019	0.000	0.000	0.000	0.000
75	A	563	LEU	0	0.007	-0.003	16.206	0.001	0.001	0.000	0.000	0.000	0.000
76	A	564	ALA	0	0.031	0.029	16.949	0.021	0.021	0.000	0.000	0.000	0.000
77	A	565	LYS	1	0.934	0.977	17.863	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	566	ASN	0	-0.013	-0.021	12.829	-0.022	-0.022	0.000	0.000	0.000	0.000
79	A	567	LYS	1	0.933	0.990	14.104	-0.134	-0.134	0.000	0.000	0.000	0.000
80	A	568	ALA	0	0.048	0.033	15.892	0.021	0.021	0.000	0.000	0.000	0.000
81	A	569	ALA	0	-0.016	-0.006	14.148	0.005	0.005	0.000	0.000	0.000	0.000
82	A	570	ARG	1	0.881	0.910	7.544	-0.780	-0.780	0.000	0.000	0.000	0.000
83	A	571	ALA	0	0.041	0.031	12.876	0.033	0.033	0.000	0.000	0.000	0.000
84	A	572	THR	0	0.029	-0.001	16.051	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	573	LEU	0	-0.046	-0.027	10.646	-0.022	-0.022	0.000	0.000	0.000	0.000
86	A	574	GLU	-1	-0.944	-0.969	12.780	0.439	0.439	0.000	0.000	0.000	0.000
87	A	575	ILE	0	-0.032	-0.004	14.402	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	576	LEU	0	-0.038	-0.026	16.301	-0.025	-0.025	0.000	0.000	0.000	0.000
89	A	577	ILE	0	-0.064	-0.033	11.634	-0.031	-0.031	0.000	0.000	0.000	0.000
90	A	578	PRO	0	-0.028	-0.027	13.931	0.055	0.055	0.000	0.000	0.000	0.000
91	A	579	ASP	-1	-0.769	-0.864	12.570	0.414	0.414	0.000	0.000	0.000	0.000
92	A	580	PHE	0	-0.018	0.055	7.980	0.205	0.205	0.000	0.000	0.000	0.000
93	A	581	VAL	0	-0.014	-0.049	9.375	0.144	0.144	0.000	0.000	0.000	0.000
94	A	582	LYS	1	0.830	0.914	4.507	-2.413	-2.274	-0.001	-0.030	-0.108	0.000
95	A	583	GLN	0	0.043	-0.012	5.237	0.728	0.632	-0.001	-0.005	0.102	0.000
96	A	592	SER	0	-0.001	-0.013	20.068	0.004	0.004	0.000	0.000	0.000	0.000
97	A	593	GLU	-1	-0.916	-0.978	20.625	0.164	0.164	0.000	0.000	0.000	0.000
98	A	594	GLU	-1	-0.793	-0.880	22.466	0.114	0.114	0.000	0.000	0.000	0.000
99	A	595	LEU	0	-0.077	-0.045	24.065	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	596	GLU	-1	-0.971	-0.991	19.594	0.202	0.202	0.000	0.000	0.000	0.000
101	A	597	TYR	0	-0.001	0.012	22.618	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	598	PHE	0	-0.039	-0.040	25.236	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	599	ASN	0	0.102	0.032	19.326	-0.017	-0.017	0.000	0.000	0.000	0.000
104	A	600	HIS	0	-0.094	-0.055	20.676	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	601	ILE	0	-0.053	0.000	24.884	-0.011	-0.011	0.000	0.000	0.000	0.000
106	A	602	SER	0	-0.018	-0.011	27.457	0.006	0.006	0.000	0.000	0.000	0.000
107	A	603	ILE	0	0.074	0.032	26.892	0.002	0.002	0.000	0.000	0.000	0.000
108	A	604	GLU	-1	-0.908	-0.957	30.218	0.031	0.031	0.000	0.000	0.000	0.000
109	A	605	ASP	-1	-0.813	-0.861	31.994	0.041	0.041	0.000	0.000	0.000	0.000
110	A	606	SER	0	0.014	-0.018	33.972	0.002	0.002	0.000	0.000	0.000	0.000
111	A	607	ARG	1	0.858	0.905	32.211	-0.046	-0.046	0.000	0.000	0.000	0.000
112	A	608	VAL	0	-0.004	0.006	31.489	0.002	0.002	0.000	0.000	0.000	0.000
113	A	609	TYR	0	0.032	0.011	33.893	0.002	0.002	0.000	0.000	0.000	0.000
114	A	610	GLU	-1	-0.912	-0.948	36.423	0.048	0.048	0.000	0.000	0.000	0.000
115	A	611	LEU	0	0.018	0.013	31.519	0.002	0.002	0.000	0.000	0.000	0.000
116	A	612	THR	0	-0.001	-0.005	31.361	0.002	0.002	0.000	0.000	0.000	0.000
117	A	613	SER	0	-0.035	-0.007	33.516	0.001	0.001	0.000	0.000	0.000	0.000
118	A	614	LYS	1	0.927	0.970	35.841	-0.057	-0.057	0.000	0.000	0.000	0.000
119	A	615	ALA	0	-0.042	-0.032	31.124	0.001	0.001	0.000	0.000	0.000	0.000
120	A	616	GLY	0	0.032	0.029	32.825	0.005	0.005	0.000	0.000	0.000	0.000
121	A	617	LEU	0	-0.065	-0.042	28.801	0.004	0.004	0.000	0.000	0.000	0.000
122	A	618	LEU	0	0.013	-0.004	30.985	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	619	SER	0	-0.040	-0.017	33.146	0.000	0.000	0.000	0.000	0.000	0.000
124	A	620	PRO	0	0.042	0.006	33.885	0.001	0.001	0.000	0.000	0.000	0.000
125	A	621	TYR	0	-0.021	-0.029	34.961	0.000	0.000	0.000	0.000	0.000	0.000
126	A	622	GLN	0	0.019	0.027	35.196	0.003	0.003	0.000	0.000	0.000	0.000
127	A	623	ILE	0	0.044	0.023	29.208	0.001	0.001	0.000	0.000	0.000	0.000
128	A	624	LEU	0	0.003	0.001	32.117	0.001	0.001	0.000	0.000	0.000	0.000
129	A	625	HIS	0	-0.009	-0.009	34.352	0.001	0.001	0.000	0.000	0.000	0.000
130	A	626	GLU	-1	-0.853	-0.909	30.736	0.081	0.081	0.000	0.000	0.000	0.000
131	A	627	CYS	0	-0.064	-0.021	30.117	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	628	LEU	0	-0.010	-0.023	31.552	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	629	LYS	1	0.861	0.926	33.797	-0.070	-0.070	0.000	0.000	0.000	0.000
134	A	630	ARG	1	0.825	0.918	24.884	-0.111	-0.111	0.000	0.000	0.000	0.000
135	A	631	ASN	0	-0.003	-0.021	29.110	0.000	0.000	0.000	0.000	0.000	0.000
136	A	632	HIS	0	0.042	0.024	32.355	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	633	GLY	0	0.002	0.011	34.624	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	634	MET	0	-0.001	0.000	32.259	0.000	0.000	0.000	0.000	0.000	0.000
139	A	635	GLY	0	-0.036	-0.016	36.879	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	636	ASP	-1	-0.885	-0.930	40.589	0.029	0.029	0.000	0.000	0.000	0.000
141	A	637	THR	0	-0.007	-0.027	39.029	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	638	SER	0	-0.059	-0.013	42.204	0.001	0.001	0.000	0.000	0.000	0.000
143	A	639	ILE	0	0.009	-0.010	43.286	0.000	0.000	0.000	0.000	0.000	0.000
144	A	640	LYS	1	0.975	0.998	46.084	-0.019	-0.019	0.000	0.000	0.000	0.000
145	A	641	PHE	0	-0.041	-0.038	49.075	0.000	0.000	0.000	0.000	0.000	0.000
146	A	642	GLU	-1	-0.893	-0.952	50.994	0.017	0.017	0.000	0.000	0.000	0.000
147	A	643	VAL	0	-0.058	-0.038	53.722	0.000	0.000	0.000	0.000	0.000	0.000
148	A	644	VAL	0	0.124	0.064	56.002	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	645	PRO	0	0.018	0.011	58.641	0.001	0.001	0.000	0.000	0.000	0.000
150	A	646	GLY	0	0.021	-0.005	55.307	0.000	0.000	0.000	0.000	0.000	0.000
151	A	647	LYS	1	0.925	0.968	54.731	-0.016	-0.016	0.000	0.000	0.000	0.000
152	A	648	ASN	0	-0.027	-0.018	56.092	0.000	0.000	0.000	0.000	0.000	0.000
153	A	649	GLN	0	0.007	0.007	55.583	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	650	LYS	1	0.917	0.976	46.886	-0.018	-0.018	0.000	0.000	0.000	0.000
155	A	651	SER	0	0.046	0.018	51.562	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	652	GLU	-1	-0.878	-0.940	49.419	0.017	0.017	0.000	0.000	0.000	0.000
157	A	653	TYR	0	-0.032	-0.013	42.592	0.001	0.001	0.000	0.000	0.000	0.000
158	A	654	VAL	0	0.013	-0.015	46.121	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	655	MET	0	-0.043	-0.008	39.288	0.001	0.001	0.000	0.000	0.000	0.000
160	A	656	ALA	0	0.016	0.011	42.811	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	657	CYS	0	0.024	-0.002	37.988	0.003	0.003	0.000	0.000	0.000	0.000
162	A	658	GLY	0	0.094	0.071	38.981	0.000	0.000	0.000	0.000	0.000	0.000
163	A	659	LYS	1	0.887	0.948	34.403	-0.022	-0.022	0.000	0.000	0.000	0.000
164	A	660	HIS	0	-0.018	-0.005	34.913	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	661	THR	0	0.026	0.014	39.986	0.002	0.002	0.000	0.000	0.000	0.000
166	A	662	VAL	0	0.007	0.001	39.150	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	663	ARG	1	0.980	0.989	42.523	-0.016	-0.016	0.000	0.000	0.000	0.000
168	A	664	GLY	0	-0.050	-0.027	44.164	0.000	0.000	0.000	0.000	0.000	0.000
169	A	665	TRP	0	0.059	0.045	45.404	0.000	0.000	0.000	0.000	0.000	0.000
170	A	666	CYS	0	-0.116	-0.050	45.832	0.002	0.002	0.000	0.000	0.000	0.000
171	A	667	LYS	1	1.006	0.993	47.170	-0.023	-0.023	0.000	0.000	0.000	0.000
172	A	668	ASN	0	0.081	0.037	47.319	0.000	0.000	0.000	0.000	0.000	0.000
173	A	669	LYS	1	1.065	1.029	47.449	-0.027	-0.027	0.000	0.000	0.000	0.000
174	A	670	ARG	1	0.902	0.959	43.381	-0.039	-0.039	0.000	0.000	0.000	0.000
175	A	671	VAL	0	0.014	0.000	42.104	0.002	0.002	0.000	0.000	0.000	0.000
176	A	672	GLY	0	0.026	0.010	42.373	0.001	0.001	0.000	0.000	0.000	0.000
177	A	673	LYS	1	0.969	0.999	42.026	-0.038	-0.038	0.000	0.000	0.000	0.000
178	A	674	GLN	0	0.051	0.062	38.404	0.003	0.003	0.000	0.000	0.000	0.000
179	A	675	LEU	0	0.036	0.025	37.945	0.001	0.001	0.000	0.000	0.000	0.000
180	A	676	ALA	0	-0.011	-0.003	38.255	0.000	0.000	0.000	0.000	0.000	0.000
181	A	677	SER	0	0.007	-0.043	36.761	0.000	0.000	0.000	0.000	0.000	0.000
182	A	678	GLN	0	-0.059	-0.036	33.699	-0.001	-0.001	0.000	0.000	0.000	0.000
183	A	679	LYS	1	0.948	0.987	33.893	-0.025	-0.025	0.000	0.000	0.000	0.000
184	A	680	ILE	0	0.015	0.016	34.799	-0.001	-0.001	0.000	0.000	0.000	0.000
185	A	681	LEU	0	0.033	0.011	30.804	0.000	0.000	0.000	0.000	0.000	0.000
186	A	682	GLN	0	-0.023	0.009	28.192	0.003	0.003	0.000	0.000	0.000	0.000
187	A	683	LEU	0	-0.047	-0.046	30.762	-0.002	-0.002	0.000	0.000	0.000	0.000
188	A	684	LEU	0	-0.003	0.002	31.239	-0.001	-0.001	0.000	0.000	0.000	0.000
189	A	685	HIS	1	0.773	0.870	26.223	-0.062	-0.062	0.000	0.000	0.000	0.000
190	A	686	PRO	0	0.005	0.001	27.385	0.003	0.003	0.000	0.000	0.000	0.000
191	A	687	HIS	0	0.017	0.018	23.930	-0.005	-0.005	0.000	0.000	0.000	0.000
192	A	688	VAL	0	0.012	0.017	22.679	0.005	0.005	0.000	0.000	0.000	0.000
193	A	689	LYS	1	0.961	0.999	23.656	-0.056	-0.056	0.000	0.000	0.000	0.000
194	A	690	ASN	0	-0.074	-0.048	20.897	0.003	0.003	0.000	0.000	0.000	0.000
195	A	691	TRP	0	0.073	0.030	24.766	0.000	0.000	0.000	0.000	0.000	0.000
196	A	692	GLY	0	0.065	0.038	22.725	0.003	0.003	0.000	0.000	0.000	0.000
197	A	693	SER	0	-0.005	-0.014	21.075	0.019	0.019	0.000	0.000	0.000	0.000
198	A	694	LEU	0	-0.004	-0.014	22.092	0.003	0.003	0.000	0.000	0.000	0.000
199	A	695	LEU	0	-0.017	0.008	24.339	0.001	0.001	0.000	0.000	0.000	0.000
200	A	696	ARG	1	0.869	0.967	18.278	-0.203	-0.203	0.000	0.000	0.000	0.000
201	A	697	MET	0	-0.022	0.021	21.867	0.004	0.004	0.000	0.000	0.000	0.000
202	A	698	TYR	0	0.021	-0.008	23.821	-0.006	-0.006	0.000	0.000	0.000	0.000
203	A	699	GLY	0	0.027	0.013	25.666	-0.008	-0.008	0.000	0.000	0.000	0.000
204	A	700	ARG	1	0.940	0.976	17.363	-0.279	-0.279	0.000	0.000	0.000	0.000
205	A	701	GLU	-1	-0.917	-0.947	21.344	0.143	0.143	0.000	0.000	0.000	0.000

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