FMO DATABASE

FMODB ID: Y1JG2

Calculation Name: 5DOC-B-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol | zinc ion

Ligand 3-letter code: GOL | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5DOC

Chain ID: B

ChEMBL ID:

UniProt ID: P16794

Base Structure: X-ray

Registration Date: 2025-10-04

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	202
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2420436.157329
FMO2-HF: Nuclear repulsion	2336826.891526
FMO2-HF: Total energy	-83609.265803
FMO2-MP2: Total energy	-83844.479914

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:17:LYS)

Summations of interaction energy for fragment #1(A:17:LYS)

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.
-323.829	-315.131	20.879	-15.381	-14.194	-0.181

Interaction energy analysis for fragmet #1(A:17:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.582 / q_NPA : 1.784

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	19	SER	0	0.076	0.042	3.843	2.485	4.354	-0.017	-0.870	-0.983	-0.001
14	A	30	ARG	1	0.938	0.996	2.989	98.101	99.334	0.409	-0.476	-1.166	-0.005
17	A	33	THR	0	-0.044	-0.020	4.039	-5.094	-4.922	0.000	-0.022	-0.150	0.000
27	A	43	GLU	-1	-0.856	-0.931	1.777	-169.844	-169.759	14.425	-8.851	-5.659	-0.109
28	A	44	GLN	0	0.018	0.021	3.312	5.669	6.424	0.013	-0.185	-0.582	-0.001
29	A	45	VAL	0	0.017	-0.018	2.144	-51.022	-46.818	5.981	-5.430	-4.755	-0.062
30	A	46	SER	0	0.003	0.003	3.143	15.600	15.875	0.068	0.479	-0.821	-0.003
31	A	47	ARG	1	0.922	0.924	4.363	45.417	45.522	0.000	-0.026	-0.078	0.000
4	A	20	ILE	0	-0.052	-0.023	6.242	2.327	2.327	0.000	0.000	0.000	0.000
5	A	21	CYS	0	-0.015	-0.006	8.833	3.737	3.737	0.000	0.000	0.000	0.000
6	A	22	LEU	0	-0.028	0.000	11.920	-0.739	-0.739	0.000	0.000	0.000	0.000
7	A	23	PRO	0	0.006	0.000	14.674	1.170	1.170	0.000	0.000	0.000	0.000
8	A	24	PHE	0	0.022	0.004	9.930	-0.989	-0.989	0.000	0.000	0.000	0.000
9	A	25	ASN	0	0.022	0.012	14.681	0.648	0.648	0.000	0.000	0.000	0.000
10	A	26	PHE	0	0.056	0.006	13.050	-2.243	-2.243	0.000	0.000	0.000	0.000
11	A	27	HIS	0	0.006	0.004	14.903	-2.088	-2.088	0.000	0.000	0.000	0.000
12	A	28	SER	0	-0.060	-0.027	12.275	0.483	0.483	0.000	0.000	0.000	0.000
13	A	29	HIS	0	-0.079	-0.048	9.712	-2.307	-2.307	0.000	0.000	0.000	0.000
15	A	31	GLN	0	0.062	0.024	8.311	-4.465	-4.465	0.000	0.000	0.000	0.000
16	A	32	HIS	0	-0.001	-0.018	7.326	-4.310	-4.310	0.000	0.000	0.000	0.000
18	A	34	CYS	0	-0.016	0.037	6.564	8.380	8.380	0.000	0.000	0.000	0.000
19	A	35	LEU	0	0.005	0.002	6.491	-10.084	-10.084	0.000	0.000	0.000	0.000
20	A	36	ASP	-1	-0.892	-0.924	5.523	-58.622	-58.622	0.000	0.000	0.000	0.000
21	A	37	ILE	0	0.005	0.008	7.311	-3.830	-3.830	0.000	0.000	0.000	0.000
22	A	38	SER	0	0.091	0.053	8.888	3.148	3.148	0.000	0.000	0.000	0.000
23	A	39	PRO	0	-0.002	-0.007	11.462	-0.609	-0.609	0.000	0.000	0.000	0.000
24	A	40	TYR	0	-0.035	-0.011	9.536	1.865	1.865	0.000	0.000	0.000	0.000
25	A	41	GLY	0	-0.018	-0.001	8.572	-1.743	-1.743	0.000	0.000	0.000	0.000
26	A	42	ASN	0	0.034	0.022	8.420	1.749	1.749	0.000	0.000	0.000	0.000
32	A	48	ILE	0	-0.065	-0.033	7.503	3.431	3.431	0.000	0.000	0.000	0.000
33	A	49	ALA	0	-0.020	-0.006	4.843	2.440	2.440	0.000	0.000	0.000	0.000
34	A	50	CYS	0	-0.056	-0.008	6.298	-4.834	-4.834	0.000	0.000	0.000	0.000
35	A	51	THR	0	0.114	0.057	7.844	2.668	2.668	0.000	0.000	0.000	0.000
36	A	52	SER	0	0.036	0.014	9.924	3.535	3.535	0.000	0.000	0.000	0.000
37	A	53	CYS	0	-0.106	-0.066	11.170	2.326	2.326	0.000	0.000	0.000	0.000
38	A	54	GLU	-1	-0.942	-0.953	11.387	-42.292	-42.292	0.000	0.000	0.000	0.000
39	A	55	ASP	-1	-0.915	-0.948	14.418	-32.258	-32.258	0.000	0.000	0.000	0.000
40	A	56	ASN	0	-0.098	-0.035	14.945	2.872	2.872	0.000	0.000	0.000	0.000
41	A	57	ARG	1	0.954	0.964	17.931	25.182	25.182	0.000	0.000	0.000	0.000
42	A	58	ILE	0	0.006	-0.004	19.171	-0.644	-0.644	0.000	0.000	0.000	0.000
43	A	59	LEU	0	0.027	0.021	16.762	1.200	1.200	0.000	0.000	0.000	0.000
44	A	60	PRO	0	-0.055	-0.017	20.636	0.439	0.439	0.000	0.000	0.000	0.000
45	A	61	THR	0	0.028	-0.026	21.916	-0.819	-0.819	0.000	0.000	0.000	0.000
46	A	62	ALA	0	0.049	0.003	23.085	0.668	0.668	0.000	0.000	0.000	0.000
47	A	63	SER	0	-0.018	-0.008	24.641	0.781	0.781	0.000	0.000	0.000	0.000
48	A	64	ASP	-1	-0.805	-0.872	25.926	-22.019	-22.019	0.000	0.000	0.000	0.000
49	A	65	ALA	0	-0.002	-0.001	25.596	0.648	0.648	0.000	0.000	0.000	0.000
50	A	66	MET	0	-0.011	0.011	27.716	0.683	0.683	0.000	0.000	0.000	0.000
51	A	67	VAL	0	-0.003	-0.005	30.562	0.763	0.763	0.000	0.000	0.000	0.000
52	A	68	ALA	0	-0.020	-0.004	29.926	0.649	0.649	0.000	0.000	0.000	0.000
53	A	69	PHE	0	0.018	0.006	31.522	0.407	0.407	0.000	0.000	0.000	0.000
54	A	70	ILE	0	-0.002	-0.009	33.081	0.576	0.576	0.000	0.000	0.000	0.000
55	A	71	ASN	0	-0.064	-0.037	35.402	0.931	0.931	0.000	0.000	0.000	0.000
56	A	72	GLN	0	0.063	0.057	33.885	0.029	0.029	0.000	0.000	0.000	0.000
57	A	73	THR	0	0.000	0.004	36.057	-0.027	-0.027	0.000	0.000	0.000	0.000
58	A	74	SER	0	-0.022	-0.009	38.529	0.537	0.537	0.000	0.000	0.000	0.000
59	A	75	ASN	0	-0.072	-0.046	33.680	-0.266	-0.266	0.000	0.000	0.000	0.000
60	A	76	ILE	0	0.025	0.021	34.326	-0.498	-0.498	0.000	0.000	0.000	0.000
61	A	77	MET	0	0.051	0.021	34.991	-0.346	-0.346	0.000	0.000	0.000	0.000
62	A	78	LYS	1	0.909	0.975	28.559	20.679	20.679	0.000	0.000	0.000	0.000
63	A	79	ASN	0	0.041	0.006	30.086	-0.992	-0.992	0.000	0.000	0.000	0.000
64	A	80	ARG	1	0.915	0.959	31.170	18.542	18.542	0.000	0.000	0.000	0.000
65	A	81	ASN	0	0.081	0.027	27.558	0.962	0.962	0.000	0.000	0.000	0.000
66	A	82	PHE	0	0.019	0.011	28.575	0.014	0.014	0.000	0.000	0.000	0.000
67	A	83	TYR	0	-0.026	-0.047	30.525	0.202	0.202	0.000	0.000	0.000	0.000
68	A	84	TYR	0	-0.006	-0.015	32.435	0.248	0.248	0.000	0.000	0.000	0.000
69	A	85	GLY	0	0.069	0.047	30.900	0.245	0.245	0.000	0.000	0.000	0.000
70	A	86	PHE	0	-0.002	-0.009	31.767	-0.045	-0.045	0.000	0.000	0.000	0.000
71	A	87	CYS	0	-0.018	-0.006	33.962	0.433	0.433	0.000	0.000	0.000	0.000
72	A	88	LYS	1	0.954	0.971	36.551	15.301	15.301	0.000	0.000	0.000	0.000
73	A	89	SER	0	0.014	0.017	38.301	0.532	0.532	0.000	0.000	0.000	0.000
74	A	90	SER	0	0.054	0.018	39.164	-0.391	-0.391	0.000	0.000	0.000	0.000
75	A	91	GLU	-1	-0.969	-0.976	40.749	-14.883	-14.883	0.000	0.000	0.000	0.000
76	A	92	LEU	0	0.010	0.003	34.996	-0.214	-0.214	0.000	0.000	0.000	0.000
77	A	93	LEU	0	0.024	0.031	36.369	-0.403	-0.403	0.000	0.000	0.000	0.000
78	A	94	LYS	1	0.964	0.987	37.720	14.052	14.052	0.000	0.000	0.000	0.000
79	A	95	LEU	0	0.020	0.033	36.747	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	96	SER	0	-0.012	-0.018	33.486	-0.430	-0.430	0.000	0.000	0.000	0.000
81	A	97	THR	0	-0.135	-0.088	34.917	-0.105	-0.105	0.000	0.000	0.000	0.000
82	A	98	ASN	0	-0.054	-0.035	37.423	0.303	0.303	0.000	0.000	0.000	0.000
83	A	99	GLN	0	0.039	0.026	31.639	0.379	0.379	0.000	0.000	0.000	0.000
84	A	100	PRO	0	0.032	0.017	31.263	-0.479	-0.479	0.000	0.000	0.000	0.000
85	A	101	PRO	0	0.031	0.010	26.885	-0.386	-0.386	0.000	0.000	0.000	0.000
86	A	102	ILE	0	0.025	0.021	26.904	-0.904	-0.904	0.000	0.000	0.000	0.000
87	A	103	PHE	0	0.010	0.001	27.527	-0.484	-0.484	0.000	0.000	0.000	0.000
88	A	104	GLN	0	-0.043	-0.041	25.951	-0.382	-0.382	0.000	0.000	0.000	0.000
89	A	105	ILE	0	0.015	0.002	21.566	-0.920	-0.920	0.000	0.000	0.000	0.000
90	A	106	TYR	0	0.022	0.011	22.501	-0.633	-0.633	0.000	0.000	0.000	0.000
91	A	107	TYR	0	-0.018	-0.014	23.774	-0.337	-0.337	0.000	0.000	0.000	0.000
92	A	108	LEU	0	-0.054	-0.032	20.688	-0.270	-0.270	0.000	0.000	0.000	0.000
93	A	109	LEU	0	0.046	0.007	17.553	-1.174	-1.174	0.000	0.000	0.000	0.000
94	A	110	HIS	0	0.042	0.033	19.950	-0.806	-0.806	0.000	0.000	0.000	0.000
95	A	111	ALA	0	-0.086	-0.042	21.739	0.205	0.205	0.000	0.000	0.000	0.000
96	A	112	ALA	0	-0.047	-0.017	16.368	-0.422	-0.422	0.000	0.000	0.000	0.000
97	A	113	ASN	0	-0.031	-0.028	15.208	-1.140	-1.140	0.000	0.000	0.000	0.000
98	A	114	HIS	0	-0.027	-0.030	19.309	1.734	1.734	0.000	0.000	0.000	0.000
99	A	115	ASP	-1	-0.843	-0.886	20.745	-25.340	-25.340	0.000	0.000	0.000	0.000
100	A	116	ILE	0	-0.061	-0.036	20.519	-0.909	-0.909	0.000	0.000	0.000	0.000
101	A	117	VAL	0	0.007	0.006	23.170	1.064	1.064	0.000	0.000	0.000	0.000
102	A	118	PRO	0	-0.058	-0.020	25.493	-0.533	-0.533	0.000	0.000	0.000	0.000
103	A	119	PHE	0	0.045	0.009	26.677	0.825	0.825	0.000	0.000	0.000	0.000
104	A	120	MET	0	-0.046	-0.009	28.555	-0.761	-0.761	0.000	0.000	0.000	0.000
105	A	121	HIS	1	0.831	0.907	29.511	20.753	20.753	0.000	0.000	0.000	0.000
106	A	122	ALA	0	0.006	-0.006	33.002	-0.409	-0.409	0.000	0.000	0.000	0.000
107	A	123	GLU	-1	-0.874	-0.924	34.752	-18.003	-18.003	0.000	0.000	0.000	0.000
108	A	124	ASP	-1	-0.850	-0.920	36.911	-16.470	-16.470	0.000	0.000	0.000	0.000
109	A	125	GLY	0	-0.038	-0.017	39.109	0.160	0.160	0.000	0.000	0.000	0.000
110	A	126	ARG	1	0.796	0.897	33.604	17.870	17.870	0.000	0.000	0.000	0.000
111	A	127	LEU	0	-0.068	-0.037	31.990	0.021	0.021	0.000	0.000	0.000	0.000
112	A	128	HIS	0	0.089	0.048	29.037	-1.104	-1.104	0.000	0.000	0.000	0.000
113	A	129	MET	0	-0.052	-0.032	24.725	0.688	0.688	0.000	0.000	0.000	0.000
114	A	130	HIS	0	-0.004	-0.012	24.088	-0.159	-0.159	0.000	0.000	0.000	0.000
115	A	131	VAL	0	-0.007	-0.009	21.194	0.971	0.971	0.000	0.000	0.000	0.000
116	A	132	ILE	0	0.014	0.016	20.981	-1.532	-1.532	0.000	0.000	0.000	0.000
117	A	133	PHE	0	-0.001	-0.012	17.244	0.220	0.220	0.000	0.000	0.000	0.000
118	A	134	GLU	-1	-0.871	-0.945	20.211	-22.822	-22.822	0.000	0.000	0.000	0.000
119	A	135	ASN	0	-0.068	-0.040	18.123	1.317	1.317	0.000	0.000	0.000	0.000
120	A	136	PRO	0	-0.018	-0.011	16.603	-0.615	-0.615	0.000	0.000	0.000	0.000
121	A	137	ASP	-1	-0.885	-0.955	13.326	-40.609	-40.609	0.000	0.000	0.000	0.000
122	A	138	VAL	0	-0.042	-0.022	12.479	2.009	2.009	0.000	0.000	0.000	0.000
123	A	139	HIS	0	0.012	-0.025	7.739	-1.842	-1.842	0.000	0.000	0.000	0.000
124	A	140	ILE	0	-0.004	-0.001	10.558	4.110	4.110	0.000	0.000	0.000	0.000
125	A	141	PRO	0	0.063	0.007	10.951	-3.922	-3.922	0.000	0.000	0.000	0.000
126	A	142	CYS	0	-0.001	-0.022	9.660	1.512	1.512	0.000	0.000	0.000	0.000
127	A	143	ASP	-1	-0.883	-0.919	11.527	-37.168	-37.168	0.000	0.000	0.000	0.000
128	A	144	CYS	0	0.028	0.028	15.029	2.365	2.365	0.000	0.000	0.000	0.000
129	A	145	ILE	0	0.029	0.027	11.409	1.842	1.842	0.000	0.000	0.000	0.000
130	A	146	THR	0	-0.036	-0.021	14.057	2.280	2.280	0.000	0.000	0.000	0.000
131	A	147	GLN	0	-0.001	0.017	16.505	3.350	3.350	0.000	0.000	0.000	0.000
132	A	148	MET	0	0.040	0.015	17.804	1.194	1.194	0.000	0.000	0.000	0.000
133	A	149	LEU	0	0.009	0.008	15.586	1.377	1.377	0.000	0.000	0.000	0.000
134	A	150	THR	0	-0.083	-0.050	19.831	1.502	1.502	0.000	0.000	0.000	0.000
135	A	151	ALA	0	-0.042	-0.023	22.253	1.281	1.281	0.000	0.000	0.000	0.000
136	A	152	ALA	0	0.002	0.004	22.175	0.899	0.899	0.000	0.000	0.000	0.000
137	A	153	ARG	1	0.889	0.940	22.942	24.404	24.404	0.000	0.000	0.000	0.000
138	A	154	GLU	-1	-0.945	-0.966	24.333	-20.730	-20.730	0.000	0.000	0.000	0.000
139	A	155	ASP	-1	-0.794	-0.878	26.810	-20.045	-20.045	0.000	0.000	0.000	0.000
140	A	156	TYR	0	-0.004	-0.006	25.159	0.629	0.629	0.000	0.000	0.000	0.000
141	A	157	SER	0	-0.035	-0.001	22.674	-1.006	-1.006	0.000	0.000	0.000	0.000
142	A	158	VAL	0	0.035	0.021	19.001	0.452	0.452	0.000	0.000	0.000	0.000
143	A	159	THR	0	-0.066	-0.052	17.844	-1.270	-1.270	0.000	0.000	0.000	0.000
144	A	160	LEU	0	0.023	0.036	12.605	1.427	1.427	0.000	0.000	0.000	0.000
145	A	161	ASN	0	0.030	-0.005	15.980	-2.388	-2.388	0.000	0.000	0.000	0.000
146	A	162	ILE	0	0.023	0.023	13.702	0.081	0.081	0.000	0.000	0.000	0.000
147	A	163	VAL	0	-0.013	-0.008	17.563	0.618	0.618	0.000	0.000	0.000	0.000
148	A	164	ARG	1	0.854	0.914	21.405	21.297	21.297	0.000	0.000	0.000	0.000
149	A	165	ASP	-1	-0.912	-0.939	19.823	-26.676	-26.676	0.000	0.000	0.000	0.000
150	A	166	HIS	1	0.843	0.925	19.491	26.032	26.032	0.000	0.000	0.000	0.000
151	A	167	VAL	0	0.055	0.035	14.395	-0.254	-0.254	0.000	0.000	0.000	0.000
152	A	168	VAL	0	0.002	-0.001	17.280	1.575	1.575	0.000	0.000	0.000	0.000
153	A	169	ILE	0	-0.015	-0.005	15.671	-1.603	-1.603	0.000	0.000	0.000	0.000
154	A	170	SER	0	0.004	0.015	19.289	1.903	1.903	0.000	0.000	0.000	0.000
155	A	171	VAL	0	-0.027	-0.024	21.773	-1.292	-1.292	0.000	0.000	0.000	0.000
156	A	172	LEU	0	0.030	0.025	24.398	0.887	0.887	0.000	0.000	0.000	0.000
157	A	173	CYS	0	-0.042	-0.018	26.974	-0.317	-0.317	0.000	0.000	0.000	0.000
158	A	174	HIS	0	-0.011	-0.015	25.384	1.139	1.139	0.000	0.000	0.000	0.000
159	A	175	ALA	0	-0.025	-0.018	30.792	0.791	0.791	0.000	0.000	0.000	0.000
160	A	176	VAL	0	0.004	-0.006	32.156	-0.511	-0.511	0.000	0.000	0.000	0.000
161	A	177	SER	0	-0.035	-0.019	32.265	0.705	0.705	0.000	0.000	0.000	0.000
162	A	178	ALA	0	-0.037	-0.025	35.044	0.142	0.142	0.000	0.000	0.000	0.000
163	A	179	SER	0	0.019	0.003	35.939	-0.452	-0.452	0.000	0.000	0.000	0.000
164	A	180	SER	0	-0.031	-0.019	36.477	0.379	0.379	0.000	0.000	0.000	0.000
165	A	181	VAL	0	-0.026	-0.007	35.957	0.370	0.370	0.000	0.000	0.000	0.000
166	A	182	LYS	1	0.974	0.987	38.933	13.729	13.729	0.000	0.000	0.000	0.000
167	A	183	ILE	0	0.030	0.031	36.981	0.142	0.142	0.000	0.000	0.000	0.000
168	A	184	ASP	-1	-0.870	-0.936	40.881	-13.432	-13.432	0.000	0.000	0.000	0.000
169	A	185	VAL	0	0.043	0.002	42.079	-0.118	-0.118	0.000	0.000	0.000	0.000
170	A	186	THR	0	-0.006	0.011	43.443	-0.085	-0.085	0.000	0.000	0.000	0.000
171	A	187	ILE	0	-0.038	-0.029	43.858	0.038	0.038	0.000	0.000	0.000	0.000
172	A	188	LEU	0	-0.014	-0.010	37.606	-0.070	-0.070	0.000	0.000	0.000	0.000
173	A	189	GLN	0	-0.009	-0.022	41.689	-0.371	-0.371	0.000	0.000	0.000	0.000
174	A	190	ARG	1	0.863	0.917	43.201	13.218	13.218	0.000	0.000	0.000	0.000
175	A	191	LYS	1	0.874	0.928	41.215	14.705	14.705	0.000	0.000	0.000	0.000
176	A	192	ILE	0	-0.014	-0.008	37.769	-0.233	-0.233	0.000	0.000	0.000	0.000
177	A	193	ASP	-1	-0.878	-0.930	40.949	-14.041	-14.041	0.000	0.000	0.000	0.000
178	A	194	GLU	-1	-0.912	-0.939	44.202	-13.121	-13.121	0.000	0.000	0.000	0.000
179	A	195	MET	0	-0.114	-0.039	35.791	-0.187	-0.187	0.000	0.000	0.000	0.000
180	A	196	ASP	-1	-0.875	-0.919	41.245	-14.149	-14.149	0.000	0.000	0.000	0.000
181	A	197	ILE	0	-0.053	-0.041	36.276	-0.460	-0.460	0.000	0.000	0.000	0.000
182	A	198	PRO	0	-0.013	0.002	35.690	0.306	0.306	0.000	0.000	0.000	0.000
183	A	199	ASN	0	0.016	0.011	37.250	-0.058	-0.058	0.000	0.000	0.000	0.000
184	A	200	ASP	-1	-0.789	-0.899	32.728	-18.147	-18.147	0.000	0.000	0.000	0.000
185	A	201	VAL	0	0.004	0.007	32.225	-0.510	-0.510	0.000	0.000	0.000	0.000
186	A	202	SER	0	-0.029	-0.014	33.259	-0.249	-0.249	0.000	0.000	0.000	0.000
187	A	203	GLU	-1	-0.933	-0.978	34.319	-16.857	-16.857	0.000	0.000	0.000	0.000
188	A	204	SER	0	-0.139	-0.065	29.240	-0.590	-0.590	0.000	0.000	0.000	0.000
189	A	205	PHE	0	0.026	0.006	30.439	-0.462	-0.462	0.000	0.000	0.000	0.000
190	A	206	GLU	-1	-0.859	-0.918	32.429	-16.700	-16.700	0.000	0.000	0.000	0.000
191	A	207	ARG	1	0.877	0.925	27.156	20.850	20.850	0.000	0.000	0.000	0.000
192	A	208	TYR	0	-0.044	-0.027	25.353	-0.665	-0.665	0.000	0.000	0.000	0.000
193	A	209	LYS	1	0.911	0.965	29.199	16.350	16.350	0.000	0.000	0.000	0.000
194	A	210	GLU	-1	-0.886	-0.955	30.143	-18.655	-18.655	0.000	0.000	0.000	0.000
195	A	211	LEU	0	-0.003	-0.001	23.731	-0.143	-0.143	0.000	0.000	0.000	0.000
196	A	212	ILE	0	0.016	0.009	27.712	-0.360	-0.360	0.000	0.000	0.000	0.000
197	A	213	GLN	0	-0.001	0.003	29.645	0.375	0.375	0.000	0.000	0.000	0.000
198	A	214	GLU	-1	-0.892	-0.934	25.900	-22.740	-22.740	0.000	0.000	0.000	0.000
199	A	215	LEU	0	-0.030	-0.025	23.544	-0.368	-0.368	0.000	0.000	0.000	0.000
200	A	216	CYS	0	-0.089	-0.052	27.615	0.127	0.127	0.000	0.000	0.000	0.000
201	A	217	GLN	0	-0.091	-0.041	30.344	0.889	0.889	0.000	0.000	0.000	0.000
202	A	218	SER	-1	-0.846	-0.895	27.637	-21.053	-21.053	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:17:LYS)