FMO DATABASE

FMODB ID: P593Z

Calculation Name: 4JZ5-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JZ5

Chain ID: A

ChEMBL ID:

UniProt ID: B6D7J9

Base Structure: X-ray

Registration Date: 2018-02-14

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. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	207
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-2504496.239477
FMO2-HF: Nuclear repulsion	2422796.26247
FMO2-HF: Total energy	-81699.977006
FMO2-MP2: Total energy	-81937.64816

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:-4:ACE)

Summations of interaction energy for fragment #1(A:-4: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.
2.349	3.048	-0.012	-0.345	-0.343	0

Interaction energy analysis for fragmet #1(A:-4:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.026 / q_NPA : 0.003

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	-2	SER	0	0.006	0.006	3.836	1.069	1.768	-0.012	-0.345	-0.343
4	A	-1	HIS	0	0.048	0.024	7.288	-0.074	-0.074	0.000	0.000	0.000
5	A	0	MET	0	-0.035	-0.002	10.328	0.094	0.094	0.000	0.000	0.000
6	A	1	MET	0	-0.049	-0.024	10.259	-0.132	-0.132	0.000	0.000	0.000
7	A	2	VAL	0	0.034	0.020	8.844	0.058	0.058	0.000	0.000	0.000
8	A	3	LEU	0	0.031	0.031	11.392	0.062	0.062	0.000	0.000	0.000
9	A	4	VAL	0	0.008	0.005	14.399	0.021	0.021	0.000	0.000	0.000
10	A	5	LEU	0	-0.008	0.001	16.749	0.005	0.005	0.000	0.000	0.000
11	A	6	ASP	-1	-0.796	-0.887	20.440	-0.120	-0.120	0.000	0.000	0.000
12	A	7	ILE	0	0.017	0.008	23.497	0.002	0.002	0.000	0.000	0.000
13	A	8	SER	0	0.029	0.007	26.596	0.006	0.006	0.000	0.000	0.000
14	A	9	LYS	1	0.918	0.963	30.140	0.045	0.045	0.000	0.000	0.000
15	A	10	TRP	0	-0.034	-0.032	31.850	0.005	0.005	0.000	0.000	0.000
16	A	11	GLN	0	0.006	0.005	27.681	0.001	0.001	0.000	0.000	0.000
17	A	12	PRO	0	0.002	0.002	30.800	0.002	0.002	0.000	0.000	0.000
18	A	13	THR	0	-0.012	-0.008	31.533	0.005	0.005	0.000	0.000	0.000
19	A	14	VAL	0	0.035	0.023	25.424	-0.005	-0.005	0.000	0.000	0.000
20	A	15	ASN	0	-0.012	0.000	26.471	0.009	0.009	0.000	0.000	0.000
21	A	16	TYR	0	0.037	-0.034	24.121	-0.002	-0.002	0.000	0.000	0.000
22	A	17	SER	0	-0.010	0.001	22.345	-0.004	-0.004	0.000	0.000	0.000
23	A	18	GLY	0	-0.015	-0.011	21.528	-0.001	-0.001	0.000	0.000	0.000
24	A	19	LEU	0	-0.024	-0.020	19.737	-0.011	-0.011	0.000	0.000	0.000
25	A	20	LYS	1	0.849	0.919	16.948	-0.004	-0.004	0.000	0.000	0.000
26	A	21	GLU	-1	-0.980	-0.962	15.532	-0.107	-0.107	0.000	0.000	0.000
27	A	22	ASP	-1	-0.864	-0.935	14.117	-0.225	-0.225	0.000	0.000	0.000
28	A	23	VAL	0	-0.095	-0.045	14.124	-0.049	-0.049	0.000	0.000	0.000
29	A	24	GLY	0	-0.001	0.000	12.549	0.021	0.021	0.000	0.000	0.000
30	A	25	PHE	0	0.001	-0.022	13.377	0.029	0.029	0.000	0.000	0.000
31	A	26	VAL	0	0.000	0.001	16.325	-0.017	-0.017	0.000	0.000	0.000
32	A	27	VAL	0	-0.002	0.012	20.035	0.014	0.014	0.000	0.000	0.000
33	A	28	ILE	0	-0.008	-0.005	22.595	-0.002	-0.002	0.000	0.000	0.000
34	A	29	ARG	1	0.859	0.934	26.165	0.058	0.058	0.000	0.000	0.000
35	A	30	SER	0	0.004	-0.010	29.422	0.006	0.006	0.000	0.000	0.000
36	A	31	SER	0	-0.001	-0.009	31.477	0.004	0.004	0.000	0.000	0.000
37	A	32	ASN	0	-0.007	0.018	34.098	-0.006	-0.006	0.000	0.000	0.000
38	A	33	GLY	0	0.052	0.021	36.830	0.003	0.003	0.000	0.000	0.000
39	A	34	THR	0	0.033	-0.015	38.289	0.000	0.000	0.000	0.000	0.000
40	A	35	GLN	0	-0.048	0.009	40.873	0.000	0.000	0.000	0.000	0.000
41	A	36	LYS	1	0.840	0.898	37.898	0.039	0.039	0.000	0.000	0.000
42	A	37	TYR	0	0.033	0.005	35.347	-0.002	-0.002	0.000	0.000	0.000
43	A	38	ASP	-1	-0.763	-0.875	32.993	-0.049	-0.049	0.000	0.000	0.000
44	A	39	GLU	-1	-0.771	-0.890	35.051	-0.036	-0.036	0.000	0.000	0.000
45	A	40	ARG	1	0.858	0.931	32.096	0.039	0.039	0.000	0.000	0.000
46	A	41	LEU	0	0.015	0.028	29.967	-0.001	-0.001	0.000	0.000	0.000
47	A	42	GLU	-1	-0.881	-0.952	30.515	-0.018	-0.018	0.000	0.000	0.000
48	A	43	GLN	0	-0.088	-0.037	31.045	0.004	0.004	0.000	0.000	0.000
49	A	44	HIS	0	0.041	0.038	27.160	0.003	0.003	0.000	0.000	0.000
50	A	45	ALA	0	0.036	0.025	26.721	-0.001	-0.001	0.000	0.000	0.000
51	A	46	LYS	1	0.981	0.991	26.779	0.019	0.019	0.000	0.000	0.000
52	A	47	GLY	0	-0.044	-0.018	27.363	0.004	0.004	0.000	0.000	0.000
53	A	48	LEU	0	-0.020	-0.032	21.712	-0.001	-0.001	0.000	0.000	0.000
54	A	49	ASP	-1	-0.869	-0.934	22.750	0.004	0.004	0.000	0.000	0.000
55	A	50	LYS	1	0.909	0.975	24.253	0.028	0.028	0.000	0.000	0.000
56	A	51	VAL	0	-0.059	-0.033	21.210	0.005	0.005	0.000	0.000	0.000
57	A	52	GLY	0	0.055	0.031	20.100	0.002	0.002	0.000	0.000	0.000
58	A	53	MET	0	-0.128	-0.048	17.102	0.001	0.001	0.000	0.000	0.000
59	A	54	PRO	0	0.009	0.012	14.940	0.004	0.004	0.000	0.000	0.000
60	A	55	PHE	0	0.023	-0.014	18.216	-0.019	-0.019	0.000	0.000	0.000
61	A	56	GLY	0	0.072	0.044	20.610	0.011	0.011	0.000	0.000	0.000
62	A	57	LEU	0	-0.043	-0.017	22.612	-0.002	-0.002	0.000	0.000	0.000
63	A	58	TYR	0	0.079	0.021	25.866	0.001	0.001	0.000	0.000	0.000
64	A	59	HIS	1	0.736	0.868	27.619	0.044	0.044	0.000	0.000	0.000
65	A	60	TYR	0	-0.048	-0.048	31.315	-0.004	-0.004	0.000	0.000	0.000
66	A	61	ALA	0	-0.036	-0.025	33.304	0.005	0.005	0.000	0.000	0.000
67	A	62	LEU	0	-0.076	-0.047	35.533	-0.001	-0.001	0.000	0.000	0.000
68	A	63	PHE	0	0.003	0.017	35.229	0.001	0.001	0.000	0.000	0.000
69	A	64	GLU	-1	-0.914	-0.985	40.526	-0.027	-0.027	0.000	0.000	0.000
70	A	65	GLY	0	0.017	0.017	42.278	0.000	0.000	0.000	0.000	0.000
71	A	66	GLY	0	0.011	0.004	43.231	0.001	0.001	0.000	0.000	0.000
72	A	67	GLN	0	0.027	-0.009	42.978	0.000	0.000	0.000	0.000	0.000
73	A	68	ASP	-1	-0.791	-0.883	43.095	-0.027	-0.027	0.000	0.000	0.000
74	A	69	THR	0	-0.029	-0.022	37.865	-0.001	-0.001	0.000	0.000	0.000
75	A	70	ILE	0	0.009	0.011	38.339	-0.001	-0.001	0.000	0.000	0.000
76	A	71	ASN	0	0.014	0.005	39.105	0.001	0.001	0.000	0.000	0.000
77	A	72	GLU	-1	-0.713	-0.861	37.109	-0.037	-0.037	0.000	0.000	0.000
78	A	73	ALA	0	-0.005	0.001	34.790	-0.001	-0.001	0.000	0.000	0.000
79	A	74	ASN	0	0.042	0.003	34.898	0.001	0.001	0.000	0.000	0.000
80	A	75	MET	0	-0.052	0.010	36.468	0.002	0.002	0.000	0.000	0.000
81	A	76	LEU	0	-0.006	0.008	28.940	0.000	0.000	0.000	0.000	0.000
82	A	77	VAL	0	0.026	0.011	31.962	0.001	0.001	0.000	0.000	0.000
83	A	78	SER	0	-0.031	-0.023	33.397	0.003	0.003	0.000	0.000	0.000
84	A	79	ALA	0	-0.022	-0.015	31.983	0.002	0.002	0.000	0.000	0.000
85	A	80	TYR	0	0.033	0.015	26.158	0.001	0.001	0.000	0.000	0.000
86	A	81	LYS	1	0.973	0.980	30.493	0.010	0.010	0.000	0.000	0.000
87	A	82	LYS	1	0.915	0.969	33.175	0.020	0.020	0.000	0.000	0.000
88	A	83	CYS	0	-0.037	-0.015	28.398	-0.001	-0.001	0.000	0.000	0.000
89	A	84	ARG	1	0.851	0.902	28.176	-0.007	-0.007	0.000	0.000	0.000
90	A	85	GLN	0	-0.070	-0.018	30.621	0.003	0.003	0.000	0.000	0.000
91	A	86	LEU	0	-0.111	-0.065	31.465	0.001	0.001	0.000	0.000	0.000
92	A	87	GLY	0	0.006	0.013	30.136	0.000	0.000	0.000	0.000	0.000
93	A	88	ALA	0	0.015	0.027	26.294	0.002	0.002	0.000	0.000	0.000
94	A	89	GLU	-1	-0.787	-0.883	23.530	0.013	0.013	0.000	0.000	0.000
95	A	90	PRO	0	-0.084	-0.030	22.798	-0.003	-0.003	0.000	0.000	0.000
96	A	91	THR	0	0.030	-0.012	18.572	0.005	0.005	0.000	0.000	0.000
97	A	92	PHE	0	-0.052	-0.027	18.387	-0.004	-0.004	0.000	0.000	0.000
98	A	93	LEU	0	-0.041	-0.006	22.002	-0.002	-0.002	0.000	0.000	0.000
99	A	94	PHE	0	0.027	0.014	20.137	-0.004	-0.004	0.000	0.000	0.000
100	A	95	LEU	0	-0.011	0.003	26.205	0.005	0.005	0.000	0.000	0.000
101	A	96	ASH	0	-0.104	-0.090	28.421	-0.007	-0.007	0.000	0.000	0.000
102	A	97	TYR	0	0.048	-0.004	29.874	0.006	0.006	0.000	0.000	0.000
103	A	98	GLU	-1	-0.813	-0.883	31.489	-0.081	-0.081	0.000	0.000	0.000
104	A	99	GLU	-1	-0.861	-0.901	33.703	-0.047	-0.047	0.000	0.000	0.000
105	A	100	VAL	0	-0.016	-0.016	37.502	0.001	0.001	0.000	0.000	0.000
106	A	101	LYS	1	0.930	0.971	40.011	0.038	0.038	0.000	0.000	0.000
107	A	102	LEU	0	-0.058	-0.013	40.031	0.002	0.002	0.000	0.000	0.000
108	A	103	LYS	1	0.949	0.977	43.527	0.026	0.026	0.000	0.000	0.000
109	A	104	SER	0	-0.030	-0.011	45.987	0.001	0.001	0.000	0.000	0.000
110	A	105	GLY	0	0.054	0.032	43.907	0.000	0.000	0.000	0.000	0.000
111	A	106	ASN	0	0.012	0.001	38.815	-0.002	-0.002	0.000	0.000	0.000
112	A	107	VAL	0	0.063	0.022	35.218	0.000	0.000	0.000	0.000	0.000
113	A	108	VAL	0	0.026	0.026	33.776	-0.001	-0.001	0.000	0.000	0.000
114	A	109	ASN	0	0.024	0.002	35.086	-0.001	-0.001	0.000	0.000	0.000
115	A	110	GLU	-1	-0.826	-0.902	37.202	-0.027	-0.027	0.000	0.000	0.000
116	A	111	CYS	0	-0.025	-0.012	32.262	-0.001	-0.001	0.000	0.000	0.000
117	A	112	GLN	0	-0.021	-0.009	30.430	-0.003	-0.003	0.000	0.000	0.000
118	A	113	ARG	1	0.851	0.920	33.754	0.026	0.026	0.000	0.000	0.000
119	A	114	PHE	0	-0.004	0.003	31.024	0.002	0.002	0.000	0.000	0.000
120	A	115	ILE	0	0.018	-0.008	28.417	0.002	0.002	0.000	0.000	0.000
121	A	116	ASP	-1	-0.863	-0.923	30.956	-0.024	-0.024	0.000	0.000	0.000
122	A	117	HIS	0	-0.047	-0.025	32.820	0.004	0.004	0.000	0.000	0.000
123	A	118	VAL	0	0.010	-0.004	29.574	0.003	0.003	0.000	0.000	0.000
124	A	119	LYS	1	0.845	0.919	25.465	0.029	0.029	0.000	0.000	0.000
125	A	120	GLY	0	-0.008	0.002	29.857	0.004	0.004	0.000	0.000	0.000
126	A	121	GLN	0	-0.072	-0.031	32.972	0.004	0.004	0.000	0.000	0.000
127	A	122	THR	0	-0.059	-0.037	29.147	0.002	0.002	0.000	0.000	0.000
128	A	123	GLY	0	0.014	0.020	28.292	0.004	0.004	0.000	0.000	0.000
129	A	124	VAL	0	-0.031	-0.004	23.699	0.003	0.003	0.000	0.000	0.000
130	A	125	LYS	1	0.925	0.961	18.882	0.015	0.015	0.000	0.000	0.000
131	A	126	VAL	0	0.013	-0.006	23.561	-0.003	-0.003	0.000	0.000	0.000
132	A	127	GLY	0	0.011	0.015	23.148	-0.001	-0.001	0.000	0.000	0.000
133	A	128	LEU	0	-0.040	-0.021	24.089	0.008	0.008	0.000	0.000	0.000
134	A	129	TYR	0	-0.023	-0.033	24.526	-0.007	-0.007	0.000	0.000	0.000
135	A	130	ALA	0	0.016	0.013	26.372	0.010	0.010	0.000	0.000	0.000
136	A	131	GLY	0	0.052	0.033	26.984	-0.011	-0.011	0.000	0.000	0.000
137	A	132	ASP	-1	-0.759	-0.858	27.091	-0.113	-0.113	0.000	0.000	0.000
138	A	133	SER	0	-0.019	-0.014	28.331	0.006	0.006	0.000	0.000	0.000
139	A	134	PHE	0	0.054	0.032	32.002	0.005	0.005	0.000	0.000	0.000
140	A	135	TRP	0	0.026	-0.014	24.938	0.004	0.004	0.000	0.000	0.000
141	A	136	LYS	1	0.875	0.931	29.789	0.098	0.098	0.000	0.000	0.000
142	A	137	THR	0	-0.038	-0.020	32.000	0.005	0.005	0.000	0.000	0.000
143	A	138	HIS	1	0.844	0.929	34.209	0.062	0.062	0.000	0.000	0.000
144	A	139	ASP	-1	-0.855	-0.919	33.512	-0.049	-0.049	0.000	0.000	0.000
145	A	140	LEU	0	0.016	-0.010	29.641	0.002	0.002	0.000	0.000	0.000
146	A	141	ASP	-1	-0.841	-0.892	27.373	-0.090	-0.090	0.000	0.000	0.000
147	A	142	LYS	1	0.865	0.932	28.980	0.047	0.047	0.000	0.000	0.000
148	A	143	VAL	0	-0.042	-0.005	29.287	0.005	0.005	0.000	0.000	0.000
149	A	144	LYS	1	0.910	0.956	27.673	0.031	0.031	0.000	0.000	0.000
150	A	145	HIS	0	0.038	0.003	23.444	0.005	0.005	0.000	0.000	0.000
151	A	146	ASP	-1	-0.816	-0.898	21.297	-0.041	-0.041	0.000	0.000	0.000
152	A	147	LEU	0	-0.042	-0.033	16.874	-0.007	-0.007	0.000	0.000	0.000
153	A	148	ARG	1	0.796	0.889	20.224	0.127	0.127	0.000	0.000	0.000
154	A	149	TRP	0	-0.023	-0.007	20.226	-0.017	-0.017	0.000	0.000	0.000
155	A	150	VAL	0	0.017	0.005	21.700	0.014	0.014	0.000	0.000	0.000
156	A	151	ALA	0	0.045	0.031	22.767	-0.018	-0.018	0.000	0.000	0.000
157	A	152	ARG	1	0.839	0.906	24.665	0.132	0.132	0.000	0.000	0.000
158	A	153	TYR	0	0.059	0.007	24.735	-0.010	-0.010	0.000	0.000	0.000
159	A	154	GLY	0	-0.035	-0.002	26.886	-0.005	-0.005	0.000	0.000	0.000
160	A	155	VAL	0	-0.032	-0.028	27.894	0.007	0.007	0.000	0.000	0.000
161	A	156	ASP	-1	-0.770	-0.841	27.696	-0.111	-0.111	0.000	0.000	0.000
162	A	157	ASN	0	0.016	-0.001	26.273	-0.001	-0.001	0.000	0.000	0.000
163	A	158	GLY	0	0.035	0.019	25.281	0.001	0.001	0.000	0.000	0.000
164	A	159	LYS	1	0.887	0.936	20.638	0.185	0.185	0.000	0.000	0.000
165	A	160	PRO	0	0.008	0.006	18.118	0.012	0.012	0.000	0.000	0.000
166	A	161	SER	0	0.064	0.041	21.205	0.012	0.012	0.000	0.000	0.000
167	A	162	THR	0	-0.056	-0.039	22.967	-0.010	-0.010	0.000	0.000	0.000
168	A	163	LYS	1	0.996	1.005	16.932	0.316	0.316	0.000	0.000	0.000
169	A	164	PRO	0	-0.022	-0.017	21.290	0.018	0.018	0.000	0.000	0.000
170	A	165	SER	0	-0.087	-0.067	23.890	-0.002	-0.002	0.000	0.000	0.000
171	A	166	ILE	0	0.006	0.014	24.435	0.007	0.007	0.000	0.000	0.000
172	A	167	PRO	0	0.040	0.009	20.596	-0.015	-0.015	0.000	0.000	0.000
173	A	168	TYR	0	-0.022	-0.009	15.718	0.023	0.023	0.000	0.000	0.000
174	A	169	ASP	-1	-0.798	-0.884	16.285	-0.188	-0.188	0.000	0.000	0.000
175	A	170	LEU	0	-0.054	-0.033	15.518	-0.051	-0.051	0.000	0.000	0.000
176	A	171	TRP	0	-0.060	-0.030	17.614	0.016	0.016	0.000	0.000	0.000
177	A	172	GLN	0	0.067	0.059	19.413	-0.013	-0.013	0.000	0.000	0.000
178	A	173	TYR	0	0.009	-0.017	17.832	0.003	0.003	0.000	0.000	0.000
179	A	174	THR	0	-0.066	-0.040	22.536	0.010	0.010	0.000	0.000	0.000
180	A	175	SER	0	0.030	0.001	24.967	-0.001	-0.001	0.000	0.000	0.000
181	A	176	LYS	1	0.852	0.924	27.205	0.095	0.095	0.000	0.000	0.000
182	A	177	GLY	0	0.031	0.019	24.375	-0.003	-0.003	0.000	0.000	0.000
183	A	178	ARG	1	0.947	0.964	24.497	0.121	0.121	0.000	0.000	0.000
184	A	179	ILE	0	0.047	0.015	21.174	-0.010	-0.010	0.000	0.000	0.000
185	A	180	LYS	1	0.984	0.985	23.994	0.075	0.075	0.000	0.000	0.000
186	A	181	ALA	0	-0.024	-0.004	23.914	0.009	0.009	0.000	0.000	0.000
187	A	182	ILE	0	0.013	0.006	24.561	0.008	0.008	0.000	0.000	0.000
188	A	183	ALA	0	-0.005	0.008	27.799	-0.004	-0.004	0.000	0.000	0.000
189	A	184	SER	0	-0.027	-0.017	30.667	-0.001	-0.001	0.000	0.000	0.000
190	A	185	PRO	0	0.007	0.015	28.974	-0.005	-0.005	0.000	0.000	0.000
191	A	186	VAL	0	-0.018	-0.010	24.015	0.007	0.007	0.000	0.000	0.000
192	A	187	ASP	-1	-0.791	-0.879	24.459	-0.118	-0.118	0.000	0.000	0.000
193	A	188	MET	0	-0.121	-0.051	19.308	0.001	0.001	0.000	0.000	0.000
194	A	189	ASN	0	0.002	-0.019	18.347	0.009	0.009	0.000	0.000	0.000
195	A	190	THR	0	-0.036	-0.026	13.692	-0.044	-0.044	0.000	0.000	0.000
196	A	191	CYS	0	0.011	0.000	11.764	0.080	0.080	0.000	0.000	0.000
197	A	192	SER	0	0.025	0.029	8.934	-0.100	-0.100	0.000	0.000	0.000
198	A	193	SER	0	0.066	0.003	4.843	0.423	0.423	0.000	0.000	0.000
199	A	194	ASP	-1	-0.908	-0.939	7.256	0.061	0.061	0.000	0.000	0.000
200	A	195	ILE	0	0.023	0.012	8.894	0.103	0.103	0.000	0.000	0.000
201	A	196	LEU	0	-0.023	-0.012	8.910	0.066	0.066	0.000	0.000	0.000
202	A	197	ASN	0	-0.034	-0.026	9.168	0.072	0.072	0.000	0.000	0.000
203	A	198	LYS	1	0.982	1.004	11.114	0.124	0.124	0.000	0.000	0.000
204	A	199	LEU	0	-0.051	-0.024	14.234	0.022	0.022	0.000	0.000	0.000
205	A	200	LYS	1	0.888	0.939	10.265	0.049	0.049	0.000	0.000	0.000
206	A	201	GLY	0	-0.003	0.010	15.422	0.019	0.019	0.000	0.000	0.000
207	A	202	SER	-1	-0.972	-0.962	13.902	0.109	0.109	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-4:ACE)