FMO DATABASE

FMODB ID: 4QGGN

Calculation Name: 1EU3-A-Xray547

Preferred Name:

Target Type:

Ligand Name: phosphate ion | zinc ion | potassium ion

Ligand 3-letter code: PO4 | ZN | K

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EU3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9RQQ5

Base Structure: X-ray

Registration Date: 2025-09-02

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	210
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2559132.088762
FMO2-HF: Nuclear repulsion	2475902.733968
FMO2-HF: Total energy	-83229.354794
FMO2-MP2: Total energy	-83478.468926

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:2:GLY)

Summations of interaction energy for fragment #1(A:2: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.
-37.484	-33.913	0.74	-1.883	-2.428	-0.015

Interaction energy analysis for fragmet #1(A:2:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.843 / q_NPA : 0.912

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	2	GLU	-1	-0.810	-0.913	3.828	-34.357	-33.617	-0.006	-0.256	-0.479	0.000
5	A	4	ASP	-1	-0.869	-0.936	3.461	-45.630	-45.444	0.011	-0.070	-0.127	0.000
6	A	5	ASN	0	-0.004	-0.009	2.991	-7.249	-5.697	0.236	-0.873	-0.915	-0.008
178	A	177	VAL	0	-0.002	-0.009	4.214	-0.181	-0.116	-0.001	-0.009	-0.055	0.000
181	A	180	ARG	1	0.832	0.908	2.801	55.965	56.993	0.500	-0.675	-0.852	-0.007
4	A	3	VAL	0	0.031	0.017	6.855	2.408	2.408	0.000	0.000	0.000	0.000
7	A	6	ASN	0	0.071	0.044	5.486	4.453	4.453	0.000	0.000	0.000	0.000
8	A	7	SER	0	-0.023	-0.037	8.441	3.813	3.813	0.000	0.000	0.000	0.000
9	A	8	LEU	0	-0.055	-0.002	6.122	1.855	1.855	0.000	0.000	0.000	0.000
10	A	9	LEU	0	0.005	0.004	8.507	2.750	2.750	0.000	0.000	0.000	0.000
11	A	10	ARG	1	0.901	0.954	10.684	24.409	24.409	0.000	0.000	0.000	0.000
12	A	11	ASN	0	-0.019	-0.007	12.472	2.022	2.022	0.000	0.000	0.000	0.000
13	A	12	ILE	0	-0.018	0.016	10.987	1.455	1.455	0.000	0.000	0.000	0.000
14	A	13	TYR	0	0.005	-0.013	13.527	1.099	1.099	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.077	-0.031	16.390	1.191	1.191	0.000	0.000	0.000	0.000
16	A	15	THR	0	-0.081	-0.048	17.264	0.911	0.911	0.000	0.000	0.000	0.000
17	A	16	ILE	0	-0.015	-0.003	19.783	0.235	0.235	0.000	0.000	0.000	0.000
18	A	17	VAL	0	-0.004	-0.019	22.890	-0.254	-0.254	0.000	0.000	0.000	0.000
19	A	18	TYR	0	-0.003	0.005	25.062	0.319	0.319	0.000	0.000	0.000	0.000
20	A	19	GLU	-1	-0.874	-0.953	28.287	-10.083	-10.083	0.000	0.000	0.000	0.000
21	A	20	TYR	0	-0.032	-0.051	31.074	0.110	0.110	0.000	0.000	0.000	0.000
22	A	21	SER	0	0.006	0.002	34.499	-0.105	-0.105	0.000	0.000	0.000	0.000
23	A	22	ASP	-1	-0.842	-0.920	37.311	-7.449	-7.449	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.008	0.018	35.582	0.014	0.014	0.000	0.000	0.000	0.000
25	A	24	VAL	0	-0.011	-0.001	38.976	0.014	0.014	0.000	0.000	0.000	0.000
26	A	25	ILE	0	-0.005	0.007	36.412	-0.139	-0.139	0.000	0.000	0.000	0.000
27	A	26	ASP	-1	-0.861	-0.926	37.956	-7.610	-7.610	0.000	0.000	0.000	0.000
28	A	27	PHE	0	-0.029	-0.020	36.724	0.170	0.170	0.000	0.000	0.000	0.000
29	A	28	LYS	1	0.895	0.975	35.306	8.635	8.635	0.000	0.000	0.000	0.000
30	A	29	THR	0	-0.027	-0.017	33.453	0.107	0.107	0.000	0.000	0.000	0.000
31	A	30	SER	0	0.036	0.009	33.085	-0.092	-0.092	0.000	0.000	0.000	0.000
32	A	31	HIS	1	0.885	0.918	27.302	11.173	11.173	0.000	0.000	0.000	0.000
33	A	32	ASN	0	-0.050	-0.016	27.538	-0.248	-0.248	0.000	0.000	0.000	0.000
34	A	33	LEU	0	0.018	0.020	30.889	0.461	0.461	0.000	0.000	0.000	0.000
35	A	34	VAL	0	-0.022	-0.015	31.666	-0.350	-0.350	0.000	0.000	0.000	0.000
36	A	35	THR	0	0.036	0.019	33.077	0.204	0.204	0.000	0.000	0.000	0.000
37	A	36	LYS	1	0.847	0.907	35.641	7.579	7.579	0.000	0.000	0.000	0.000
38	A	37	LYS	1	0.831	0.919	37.019	7.519	7.519	0.000	0.000	0.000	0.000
39	A	38	LEU	0	-0.034	-0.002	32.890	0.166	0.166	0.000	0.000	0.000	0.000
40	A	39	ASP	-1	-0.764	-0.872	34.854	-9.024	-9.024	0.000	0.000	0.000	0.000
41	A	40	VAL	0	-0.036	-0.022	37.319	0.057	0.057	0.000	0.000	0.000	0.000
42	A	41	ARG	1	0.867	0.938	30.509	9.849	9.849	0.000	0.000	0.000	0.000
43	A	42	ASP	-1	-0.867	-0.938	31.154	-9.832	-9.832	0.000	0.000	0.000	0.000
44	A	43	ALA	0	-0.060	-0.033	34.716	0.070	0.070	0.000	0.000	0.000	0.000
45	A	44	ARG	1	0.805	0.910	33.645	9.395	9.395	0.000	0.000	0.000	0.000
46	A	45	ASP	-1	-0.797	-0.901	36.263	-7.912	-7.912	0.000	0.000	0.000	0.000
47	A	46	PHE	0	-0.011	-0.013	29.285	-0.195	-0.195	0.000	0.000	0.000	0.000
48	A	47	PHE	0	-0.023	-0.014	32.988	0.306	0.306	0.000	0.000	0.000	0.000
49	A	48	ILE	0	0.036	0.019	28.496	-0.326	-0.326	0.000	0.000	0.000	0.000
50	A	49	ASN	0	-0.009	-0.001	28.324	0.127	0.127	0.000	0.000	0.000	0.000
51	A	50	SER	0	-0.011	-0.009	27.262	-0.405	-0.405	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.783	-0.871	23.737	-11.881	-11.881	0.000	0.000	0.000	0.000
53	A	52	MET	0	0.022	0.000	25.445	-0.342	-0.342	0.000	0.000	0.000	0.000
54	A	53	ASP	-1	-0.861	-0.932	24.755	-12.897	-12.897	0.000	0.000	0.000	0.000
55	A	54	GLU	-1	-0.926	-0.973	27.505	-9.408	-9.408	0.000	0.000	0.000	0.000
56	A	55	TYR	0	-0.037	-0.019	29.983	0.240	0.240	0.000	0.000	0.000	0.000
57	A	56	ALA	0	0.058	0.032	29.306	0.276	0.276	0.000	0.000	0.000	0.000
58	A	57	ALA	0	-0.011	-0.016	31.291	0.215	0.215	0.000	0.000	0.000	0.000
59	A	58	ASN	0	-0.072	-0.049	32.958	0.366	0.366	0.000	0.000	0.000	0.000
60	A	59	ASP	-1	-0.915	-0.931	35.066	-8.779	-8.779	0.000	0.000	0.000	0.000
61	A	60	PHE	0	-0.054	-0.024	32.956	0.195	0.195	0.000	0.000	0.000	0.000
62	A	61	LYS	1	0.922	0.948	37.579	7.391	7.391	0.000	0.000	0.000	0.000
63	A	62	THR	0	0.007	-0.015	40.038	-0.134	-0.134	0.000	0.000	0.000	0.000
64	A	63	GLY	0	-0.026	-0.008	41.145	0.181	0.181	0.000	0.000	0.000	0.000
65	A	64	ASP	-1	-0.836	-0.908	39.854	-7.708	-7.708	0.000	0.000	0.000	0.000
66	A	65	LYS	1	0.814	0.884	40.384	7.200	7.200	0.000	0.000	0.000	0.000
67	A	66	ILE	0	-0.009	-0.011	34.310	-0.019	-0.019	0.000	0.000	0.000	0.000
68	A	67	ALA	0	-0.014	-0.002	35.305	0.127	0.127	0.000	0.000	0.000	0.000
69	A	68	VAL	0	-0.019	-0.013	29.713	-0.177	-0.177	0.000	0.000	0.000	0.000
70	A	69	PHE	0	-0.027	-0.018	25.521	0.093	0.093	0.000	0.000	0.000	0.000
71	A	70	SER	0	-0.010	0.009	24.979	-0.230	-0.230	0.000	0.000	0.000	0.000
72	A	71	VAL	0	0.022	0.020	19.449	0.276	0.276	0.000	0.000	0.000	0.000
73	A	72	PRO	0	-0.039	-0.010	22.053	-0.099	-0.099	0.000	0.000	0.000	0.000
74	A	73	PHE	0	0.017	-0.017	18.434	-0.744	-0.744	0.000	0.000	0.000	0.000
75	A	74	ASP	-1	-0.892	-0.945	19.416	-13.993	-13.993	0.000	0.000	0.000	0.000
76	A	75	TRP	0	-0.036	-0.036	20.744	0.226	0.226	0.000	0.000	0.000	0.000
77	A	76	ASN	0	0.017	0.023	25.713	0.206	0.206	0.000	0.000	0.000	0.000
78	A	77	TYR	0	0.073	0.017	26.508	0.449	0.449	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.004	0.000	30.181	0.333	0.333	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.036	-0.003	33.375	0.342	0.342	0.000	0.000	0.000	0.000
81	A	80	LYS	1	0.992	0.970	36.182	7.436	7.436	0.000	0.000	0.000	0.000
82	A	81	GLY	0	0.030	0.018	38.703	0.065	0.065	0.000	0.000	0.000	0.000
83	A	82	LYS	1	0.932	1.000	34.935	8.810	8.810	0.000	0.000	0.000	0.000
84	A	83	VAL	0	0.031	0.020	30.072	-0.139	-0.139	0.000	0.000	0.000	0.000
85	A	84	THR	0	-0.054	-0.029	29.838	0.291	0.291	0.000	0.000	0.000	0.000
86	A	85	ALA	0	0.036	0.033	26.130	-0.286	-0.286	0.000	0.000	0.000	0.000
87	A	86	TYR	0	-0.021	-0.013	24.172	0.535	0.535	0.000	0.000	0.000	0.000
88	A	87	THR	0	-0.007	-0.004	23.189	-0.538	-0.538	0.000	0.000	0.000	0.000
89	A	88	TYR	0	0.007	0.001	18.595	0.528	0.528	0.000	0.000	0.000	0.000
90	A	89	GLY	0	0.045	0.030	23.471	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.035	0.017	26.394	0.109	0.109	0.000	0.000	0.000	0.000
92	A	91	ILE	0	-0.070	-0.024	27.555	0.351	0.351	0.000	0.000	0.000	0.000
93	A	92	THR	0	-0.008	-0.004	31.240	-0.027	-0.027	0.000	0.000	0.000	0.000
94	A	93	PRO	0	0.078	0.021	34.105	0.106	0.106	0.000	0.000	0.000	0.000
95	A	94	TYR	0	-0.018	0.003	37.796	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	95	GLN	0	0.010	0.007	39.213	0.014	0.014	0.000	0.000	0.000	0.000
97	A	96	LYS	1	0.918	0.974	41.142	6.699	6.699	0.000	0.000	0.000	0.000
98	A	97	THR	0	0.003	-0.009	43.855	0.080	0.080	0.000	0.000	0.000	0.000
99	A	98	SER	0	0.008	0.022	40.176	-0.104	-0.104	0.000	0.000	0.000	0.000
100	A	99	ILE	0	0.001	-0.017	40.043	0.211	0.211	0.000	0.000	0.000	0.000
101	A	100	PRO	0	-0.020	-0.006	38.052	-0.191	-0.191	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.841	0.920	36.823	8.269	8.269	0.000	0.000	0.000	0.000
103	A	102	ASN	0	-0.002	-0.005	34.146	-0.270	-0.270	0.000	0.000	0.000	0.000
104	A	103	ILE	0	-0.013	-0.006	29.859	0.191	0.191	0.000	0.000	0.000	0.000
105	A	104	PRO	0	0.003	0.007	31.458	-0.201	-0.201	0.000	0.000	0.000	0.000
106	A	105	VAL	0	0.011	-0.006	26.300	-0.285	-0.285	0.000	0.000	0.000	0.000
107	A	106	ASN	0	-0.051	-0.012	27.594	0.427	0.427	0.000	0.000	0.000	0.000
108	A	107	LEU	0	0.009	0.000	21.856	-0.470	-0.470	0.000	0.000	0.000	0.000
109	A	108	TRP	0	-0.024	-0.016	22.918	0.481	0.481	0.000	0.000	0.000	0.000
110	A	109	ILE	0	0.006	-0.004	19.435	-0.675	-0.675	0.000	0.000	0.000	0.000
111	A	110	ASN	0	0.013	0.018	18.036	-0.161	-0.161	0.000	0.000	0.000	0.000
112	A	111	GLY	0	0.026	0.024	20.391	0.624	0.624	0.000	0.000	0.000	0.000
113	A	112	LYS	1	0.910	0.964	23.070	12.633	12.633	0.000	0.000	0.000	0.000
114	A	113	GLN	0	0.001	0.005	25.093	-0.270	-0.270	0.000	0.000	0.000	0.000
115	A	114	ILE	0	-0.056	-0.035	24.611	0.322	0.322	0.000	0.000	0.000	0.000
116	A	115	SER	0	-0.020	-0.008	27.710	0.064	0.064	0.000	0.000	0.000	0.000
117	A	116	VAL	0	0.041	0.016	27.104	-0.340	-0.340	0.000	0.000	0.000	0.000
118	A	117	PRO	0	-0.007	0.005	29.820	0.383	0.383	0.000	0.000	0.000	0.000
119	A	118	TYR	0	0.020	-0.002	32.089	-0.123	-0.123	0.000	0.000	0.000	0.000
120	A	119	ASN	0	-0.024	-0.028	34.176	0.021	0.021	0.000	0.000	0.000	0.000
121	A	120	GLU	-1	-0.911	-0.939	27.703	-11.153	-11.153	0.000	0.000	0.000	0.000
122	A	121	ILE	0	0.003	0.008	25.709	-0.278	-0.278	0.000	0.000	0.000	0.000
123	A	122	SER	0	0.025	0.017	29.594	0.238	0.238	0.000	0.000	0.000	0.000
124	A	123	THR	0	-0.016	-0.032	31.290	-0.181	-0.181	0.000	0.000	0.000	0.000
125	A	124	ASN	0	0.016	0.012	33.474	0.335	0.335	0.000	0.000	0.000	0.000
126	A	125	LYS	1	0.857	0.926	31.711	10.169	10.169	0.000	0.000	0.000	0.000
127	A	126	THR	0	0.010	-0.023	35.962	-0.089	-0.089	0.000	0.000	0.000	0.000
128	A	127	THR	0	-0.021	-0.004	33.904	0.003	0.003	0.000	0.000	0.000	0.000
129	A	128	VAL	0	-0.012	0.006	29.840	0.009	0.009	0.000	0.000	0.000	0.000
130	A	129	THR	0	0.061	0.017	27.071	-0.247	-0.247	0.000	0.000	0.000	0.000
131	A	130	ALA	0	0.028	0.010	23.896	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	131	GLN	0	0.042	0.007	22.379	-0.598	-0.598	0.000	0.000	0.000	0.000
133	A	132	GLU	-1	-0.777	-0.851	23.501	-10.574	-10.574	0.000	0.000	0.000	0.000
134	A	133	ILE	0	0.008	0.003	25.235	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	134	ASP	-1	-0.735	-0.829	18.843	-17.221	-17.221	0.000	0.000	0.000	0.000
136	A	135	LEU	0	-0.034	-0.016	19.901	-0.442	-0.442	0.000	0.000	0.000	0.000
137	A	136	LYS	1	0.769	0.886	21.975	10.766	10.766	0.000	0.000	0.000	0.000
138	A	137	VAL	0	0.049	0.018	20.602	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	138	ARG	1	0.837	0.899	13.994	19.586	19.586	0.000	0.000	0.000	0.000
140	A	139	LYS	1	0.926	0.974	19.387	12.807	12.807	0.000	0.000	0.000	0.000
141	A	140	PHE	0	0.059	0.026	21.589	-0.051	-0.051	0.000	0.000	0.000	0.000
142	A	141	LEU	0	-0.003	-0.006	19.108	0.041	0.041	0.000	0.000	0.000	0.000
143	A	142	ILE	0	-0.057	-0.023	16.460	-0.320	-0.320	0.000	0.000	0.000	0.000
144	A	143	ALA	0	-0.055	-0.021	19.081	0.084	0.084	0.000	0.000	0.000	0.000
145	A	144	GLN	0	-0.019	-0.008	22.664	0.322	0.322	0.000	0.000	0.000	0.000
146	A	145	HIS	0	0.015	0.012	21.243	0.051	0.051	0.000	0.000	0.000	0.000
147	A	146	GLN	0	0.014	0.018	18.428	-0.882	-0.882	0.000	0.000	0.000	0.000
148	A	147	LEU	0	0.058	0.043	14.175	-1.332	-1.332	0.000	0.000	0.000	0.000
149	A	148	TYR	0	-0.061	-0.057	11.535	1.151	1.151	0.000	0.000	0.000	0.000
150	A	149	SER	0	-0.025	-0.014	13.024	-0.427	-0.427	0.000	0.000	0.000	0.000
151	A	150	SER	0	-0.028	-0.028	13.493	-1.311	-1.311	0.000	0.000	0.000	0.000
152	A	151	GLY	0	0.012	-0.003	13.876	1.302	1.302	0.000	0.000	0.000	0.000
153	A	152	SER	0	-0.029	0.010	13.738	0.552	0.552	0.000	0.000	0.000	0.000
154	A	153	SER	0	-0.004	-0.018	12.948	-1.237	-1.237	0.000	0.000	0.000	0.000
155	A	154	TYR	0	-0.063	-0.034	13.064	-0.959	-0.959	0.000	0.000	0.000	0.000
156	A	155	LYS	1	0.835	0.902	8.560	23.651	23.651	0.000	0.000	0.000	0.000
157	A	156	SER	0	-0.069	-0.027	9.146	-2.132	-2.132	0.000	0.000	0.000	0.000
158	A	157	GLY	0	0.089	0.034	11.818	1.301	1.301	0.000	0.000	0.000	0.000
159	A	158	ARG	1	0.822	0.898	14.458	16.374	16.374	0.000	0.000	0.000	0.000
160	A	159	LEU	0	0.025	0.030	17.206	0.707	0.707	0.000	0.000	0.000	0.000
161	A	160	VAL	0	-0.002	-0.016	20.297	-0.200	-0.200	0.000	0.000	0.000	0.000
162	A	161	PHE	0	0.007	-0.007	22.703	0.429	0.429	0.000	0.000	0.000	0.000
163	A	162	HIS	0	-0.070	-0.038	26.282	0.257	0.257	0.000	0.000	0.000	0.000
164	A	163	THR	0	-0.002	-0.007	29.032	0.204	0.204	0.000	0.000	0.000	0.000
165	A	164	ASN	0	-0.062	-0.039	31.660	0.048	0.048	0.000	0.000	0.000	0.000
166	A	165	ASP	-1	-0.805	-0.884	33.754	-9.199	-9.199	0.000	0.000	0.000	0.000
167	A	166	ASN	0	-0.035	-0.031	34.646	-0.018	-0.018	0.000	0.000	0.000	0.000
168	A	167	SER	0	-0.102	-0.062	31.020	-0.191	-0.191	0.000	0.000	0.000	0.000
169	A	168	ASP	-1	-0.885	-0.945	27.095	-11.062	-11.062	0.000	0.000	0.000	0.000
170	A	169	LYS	1	0.891	0.950	25.987	11.247	11.247	0.000	0.000	0.000	0.000
171	A	170	TYR	0	-0.022	-0.034	22.303	-0.513	-0.513	0.000	0.000	0.000	0.000
172	A	171	SER	0	-0.018	-0.022	20.046	-0.070	-0.070	0.000	0.000	0.000	0.000
173	A	172	PHE	0	-0.016	0.000	17.042	-0.152	-0.152	0.000	0.000	0.000	0.000
174	A	173	ASP	-1	-0.828	-0.912	11.628	-25.722	-25.722	0.000	0.000	0.000	0.000
175	A	174	LEU	0	-0.034	-0.014	13.694	-0.182	-0.182	0.000	0.000	0.000	0.000
176	A	175	PHE	0	0.011	0.004	8.390	-0.589	-0.589	0.000	0.000	0.000	0.000
177	A	176	TYR	0	-0.022	0.005	7.817	-5.828	-5.828	0.000	0.000	0.000	0.000
179	A	178	GLY	0	0.031	0.026	7.700	0.682	0.682	0.000	0.000	0.000	0.000
180	A	179	TYR	0	-0.042	-0.040	7.418	-4.237	-4.237	0.000	0.000	0.000	0.000
182	A	181	ASP	-1	-0.784	-0.863	8.083	-21.263	-21.263	0.000	0.000	0.000	0.000
183	A	182	LYS	1	0.923	0.968	11.801	17.150	17.150	0.000	0.000	0.000	0.000
184	A	183	GLU	-1	-0.923	-0.945	14.974	-15.976	-15.976	0.000	0.000	0.000	0.000
185	A	184	SER	0	-0.037	-0.053	11.866	-0.228	-0.228	0.000	0.000	0.000	0.000
186	A	185	ILE	0	-0.021	-0.007	9.308	0.151	0.151	0.000	0.000	0.000	0.000
187	A	186	PHE	0	0.036	-0.005	13.219	0.592	0.592	0.000	0.000	0.000	0.000
188	A	187	LYS	1	0.927	0.976	16.391	17.831	17.831	0.000	0.000	0.000	0.000
189	A	188	VAL	0	-0.006	-0.003	15.205	0.749	0.749	0.000	0.000	0.000	0.000
190	A	189	TYR	0	-0.021	-0.029	18.067	0.505	0.505	0.000	0.000	0.000	0.000
191	A	190	LYS	1	0.810	0.918	21.148	13.750	13.750	0.000	0.000	0.000	0.000
192	A	191	ASP	-1	-0.747	-0.852	23.061	-12.950	-12.950	0.000	0.000	0.000	0.000
193	A	192	ASN	0	-0.038	-0.031	25.042	0.354	0.354	0.000	0.000	0.000	0.000
194	A	193	LYS	1	0.876	0.978	24.999	11.657	11.657	0.000	0.000	0.000	0.000
195	A	194	SER	0	-0.004	-0.008	26.960	-0.113	-0.113	0.000	0.000	0.000	0.000
196	A	195	PHE	0	0.030	0.006	26.443	-0.040	-0.040	0.000	0.000	0.000	0.000
197	A	196	ASN	0	0.041	0.025	32.047	0.108	0.108	0.000	0.000	0.000	0.000
198	A	197	ILE	0	0.046	0.009	33.609	-0.097	-0.097	0.000	0.000	0.000	0.000
199	A	198	ASP	-1	-0.858	-0.918	35.339	-8.171	-8.171	0.000	0.000	0.000	0.000
200	A	199	LYS	1	0.868	0.943	34.335	8.525	8.525	0.000	0.000	0.000	0.000
201	A	200	ILE	0	-0.020	0.000	29.674	-0.196	-0.196	0.000	0.000	0.000	0.000
202	A	201	GLY	0	-0.006	0.008	32.582	0.214	0.214	0.000	0.000	0.000	0.000
203	A	202	HIS	0	-0.073	-0.043	29.236	0.461	0.461	0.000	0.000	0.000	0.000
204	A	203	LEU	0	-0.032	-0.010	25.574	-0.225	-0.225	0.000	0.000	0.000	0.000
205	A	204	ASP	-1	-0.780	-0.872	25.133	-11.193	-11.193	0.000	0.000	0.000	0.000
206	A	205	ILE	0	-0.011	-0.011	20.301	-0.575	-0.575	0.000	0.000	0.000	0.000
207	A	206	GLU	-1	-0.841	-0.900	19.026	-14.929	-14.929	0.000	0.000	0.000	0.000
208	A	207	ILE	0	0.009	-0.007	15.744	-1.072	-1.072	0.000	0.000	0.000	0.000
209	A	208	ASP	-1	-0.870	-0.940	15.299	-16.177	-16.177	0.000	0.000	0.000	0.000
210	A	209	SER	-1	-0.811	-0.906	13.604	-24.875	-24.875	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:GLY)