FMO DATABASE

FMODB ID: 3Z2LL

Calculation Name: 1DOA-B-Xray547

Preferred Name: Cell division control protein 42 homolog

Target Type: SINGLE PROTEIN

Ligand Name: guanosine-5'-diphosphate | geran-8-yl geran | o-methylcysteine | magnesium ion

Ligand 3-letter code: GDP | GER | CMT | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1DOA

Chain ID: B

ChEMBL ID: CHEMBL6088

UniProt ID: P60953

Base Structure: X-ray

Registration Date: 2025-10-05

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	200
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2155016.944643
FMO2-HF: Nuclear repulsion	2074674.304567
FMO2-HF: Total energy	-80342.640076
FMO2-MP2: Total energy	-80577.77844

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:5:GLU)

Summations of interaction energy for fragment #1(A:5:GLU)

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.
-16.839	-10.241	1.986	-3.528	-5.056	0.02

Interaction energy analysis for fragmet #1(A:5:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.094 / q_NPA : -0.063

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	7	THR	0	0.023	0.008	2.244	-2.063	0.865	0.727	-1.573	-2.082	-0.005
4	A	8	ALA	0	0.078	0.065	2.580	-2.809	0.520	1.174	-1.767	-2.736	0.021
5	A	9	GLU	-1	-0.875	-0.951	3.594	0.355	0.696	0.085	-0.188	-0.238	0.004
6	A	10	GLN	0	-0.044	-0.024	6.368	0.292	0.292	0.000	0.000	0.000	0.000
7	A	11	LEU	0	-0.014	-0.007	8.026	-1.461	-1.461	0.000	0.000	0.000	0.000
8	A	12	ALA	0	0.080	0.035	10.520	-0.895	-0.895	0.000	0.000	0.000	0.000
9	A	13	GLN	0	-0.047	-0.016	11.465	0.158	0.158	0.000	0.000	0.000	0.000
10	A	14	ILE	0	-0.045	-0.029	9.799	-0.422	-0.422	0.000	0.000	0.000	0.000
11	A	15	ALA	0	0.039	0.052	13.660	-0.397	-0.397	0.000	0.000	0.000	0.000
12	A	16	ALA	0	-0.094	-0.054	16.963	-0.050	-0.050	0.000	0.000	0.000	0.000
13	A	17	GLU	-1	-0.896	-0.950	18.516	0.848	0.848	0.000	0.000	0.000	0.000
14	A	18	ASN	0	-0.052	-0.039	20.283	-0.046	-0.046	0.000	0.000	0.000	0.000
15	A	19	GLU	-1	-0.921	-0.968	22.178	0.874	0.874	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.867	-0.931	25.639	0.920	0.920	0.000	0.000	0.000	0.000
17	A	21	ASP	-1	-0.960	-0.980	26.412	0.545	0.545	0.000	0.000	0.000	0.000
18	A	22	GLU	-1	-0.946	-0.957	29.422	0.555	0.555	0.000	0.000	0.000	0.000
19	A	23	HIS	0	-0.097	-0.051	30.923	-0.105	-0.105	0.000	0.000	0.000	0.000
20	A	24	SER	0	-0.052	-0.023	34.589	-0.057	-0.057	0.000	0.000	0.000	0.000
21	A	25	VAL	0	-0.044	-0.028	37.735	0.018	0.018	0.000	0.000	0.000	0.000
22	A	26	ASN	0	0.004	0.001	37.095	-0.027	-0.027	0.000	0.000	0.000	0.000
23	A	27	TYR	0	-0.034	-0.020	40.478	-0.014	-0.014	0.000	0.000	0.000	0.000
24	A	28	LYS	1	0.917	0.958	42.285	-0.286	-0.286	0.000	0.000	0.000	0.000
25	A	29	PRO	0	0.043	0.028	42.033	-0.016	-0.016	0.000	0.000	0.000	0.000
26	A	30	PRO	0	-0.019	0.010	44.532	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	31	ALA	0	-0.028	-0.025	47.882	0.011	0.011	0.000	0.000	0.000	0.000
28	A	32	GLN	0	-0.058	-0.039	46.714	-0.021	-0.021	0.000	0.000	0.000	0.000
29	A	33	LYS	1	0.886	0.969	50.254	-0.147	-0.147	0.000	0.000	0.000	0.000
30	A	34	SER	0	-0.001	-0.026	52.170	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	35	ILE	0	-0.007	-0.030	51.861	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	36	GLN	0	-0.047	-0.019	55.485	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	37	GLU	-1	-0.778	-0.870	56.488	0.144	0.144	0.000	0.000	0.000	0.000
34	A	38	ILE	0	-0.026	-0.014	54.562	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	39	GLN	0	-0.046	-0.026	58.064	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	40	GLU	-1	-1.013	-1.008	60.878	0.093	0.093	0.000	0.000	0.000	0.000
37	A	41	LEU	0	-0.080	-0.030	58.225	0.001	0.001	0.000	0.000	0.000	0.000
38	A	42	ASP	-1	-0.862	-0.925	62.326	0.087	0.087	0.000	0.000	0.000	0.000
39	A	43	LYS	1	0.916	0.965	64.876	-0.057	-0.057	0.000	0.000	0.000	0.000
40	A	44	ASP	-1	-0.902	-0.959	66.908	0.056	0.056	0.000	0.000	0.000	0.000
41	A	45	ASP	-1	-0.779	-0.891	65.392	0.037	0.037	0.000	0.000	0.000	0.000
42	A	46	GLU	-1	-0.885	-0.953	65.767	0.009	0.009	0.000	0.000	0.000	0.000
43	A	47	SER	0	-0.035	-0.008	63.755	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	48	LEU	0	0.043	0.007	59.596	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	49	ARG	1	0.847	0.926	61.000	-0.031	-0.031	0.000	0.000	0.000	0.000
46	A	50	LYS	1	0.850	0.920	61.527	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	51	TYR	0	-0.003	0.001	54.040	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	52	LYS	1	0.916	0.961	56.997	-0.072	-0.072	0.000	0.000	0.000	0.000
49	A	53	GLU	-1	-0.883	-0.924	57.076	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	54	ALA	0	-0.050	-0.030	56.380	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	55	LEU	0	-0.038	-0.010	51.428	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	56	LEU	0	-0.023	-0.010	52.296	0.004	0.004	0.000	0.000	0.000	0.000
53	A	57	GLY	0	0.008	0.031	54.387	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	58	ARG	1	0.839	0.878	56.194	0.009	0.009	0.000	0.000	0.000	0.000
55	A	59	VAL	0	-0.047	-0.027	58.530	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	60	ALA	0	-0.014	-0.001	55.260	0.001	0.001	0.000	0.000	0.000	0.000
57	A	61	VAL	0	0.063	0.045	53.870	0.001	0.001	0.000	0.000	0.000	0.000
58	A	62	SER	0	-0.014	-0.015	51.871	0.002	0.002	0.000	0.000	0.000	0.000
59	A	63	ALA	0	-0.029	-0.016	51.469	0.006	0.006	0.000	0.000	0.000	0.000
60	A	64	ASP	-1	-0.847	-0.923	51.588	0.118	0.118	0.000	0.000	0.000	0.000
61	A	65	PRO	0	-0.035	-0.023	51.589	0.008	0.008	0.000	0.000	0.000	0.000
62	A	66	ASN	0	-0.012	-0.018	48.395	0.021	0.021	0.000	0.000	0.000	0.000
63	A	67	VAL	0	0.006	0.024	46.316	0.004	0.004	0.000	0.000	0.000	0.000
64	A	68	PRO	0	0.058	0.037	43.129	0.002	0.002	0.000	0.000	0.000	0.000
65	A	69	ASN	0	0.034	0.018	45.689	-0.029	-0.029	0.000	0.000	0.000	0.000
66	A	70	VAL	0	0.034	0.022	40.187	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	71	VAL	0	-0.009	-0.008	40.944	0.014	0.014	0.000	0.000	0.000	0.000
68	A	72	VAL	0	0.022	0.003	34.984	-0.024	-0.024	0.000	0.000	0.000	0.000
69	A	73	THR	0	-0.044	-0.011	37.901	0.004	0.004	0.000	0.000	0.000	0.000
70	A	74	ARG	1	0.799	0.870	34.353	0.186	0.186	0.000	0.000	0.000	0.000
71	A	75	LEU	0	0.007	0.022	28.024	0.011	0.011	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.021	-0.035	31.156	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	77	LEU	0	-0.024	-0.004	25.043	0.011	0.011	0.000	0.000	0.000	0.000
74	A	78	VAL	0	-0.032	-0.015	29.168	-0.040	-0.040	0.000	0.000	0.000	0.000
75	A	79	CYS	0	0.004	-0.009	26.512	-0.052	-0.052	0.000	0.000	0.000	0.000
76	A	80	SER	0	-0.004	0.001	29.005	-0.024	-0.024	0.000	0.000	0.000	0.000
77	A	81	THR	0	-0.024	-0.026	24.826	-0.048	-0.048	0.000	0.000	0.000	0.000
78	A	82	ALA	0	0.021	0.015	25.946	-0.110	-0.110	0.000	0.000	0.000	0.000
79	A	83	PRO	0	-0.038	-0.021	25.679	0.072	0.072	0.000	0.000	0.000	0.000
80	A	84	GLY	0	-0.024	-0.003	27.824	0.056	0.056	0.000	0.000	0.000	0.000
81	A	85	PRO	0	0.005	-0.006	28.693	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	86	LEU	0	-0.021	-0.001	24.075	-0.018	-0.018	0.000	0.000	0.000	0.000
83	A	87	GLU	-1	-0.826	-0.900	28.628	-0.244	-0.244	0.000	0.000	0.000	0.000
84	A	88	LEU	0	-0.018	-0.002	26.555	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	89	ASP	-1	-0.795	-0.887	30.727	-0.126	-0.126	0.000	0.000	0.000	0.000
86	A	90	LEU	0	-0.054	-0.028	30.864	0.027	0.027	0.000	0.000	0.000	0.000
87	A	91	THR	0	-0.025	-0.018	34.579	0.023	0.023	0.000	0.000	0.000	0.000
88	A	92	GLY	0	-0.009	0.001	37.370	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	93	ASP	-1	-0.929	-0.973	33.940	0.077	0.077	0.000	0.000	0.000	0.000
90	A	94	LEU	0	0.066	0.030	31.139	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	95	GLU	-1	-0.856	-0.927	29.395	0.424	0.424	0.000	0.000	0.000	0.000
92	A	96	SER	0	-0.035	-0.004	28.253	0.008	0.008	0.000	0.000	0.000	0.000
93	A	97	PHE	0	0.034	0.011	26.370	-0.043	-0.043	0.000	0.000	0.000	0.000
94	A	98	LYS	1	0.823	0.909	23.980	-0.499	-0.499	0.000	0.000	0.000	0.000
95	A	99	LYS	1	0.874	0.933	23.065	0.010	0.010	0.000	0.000	0.000	0.000
96	A	100	GLN	0	0.017	0.017	23.714	-0.124	-0.124	0.000	0.000	0.000	0.000
97	A	101	SER	0	-0.026	-0.021	19.979	0.068	0.068	0.000	0.000	0.000	0.000
98	A	102	PHE	0	0.017	0.020	21.072	-0.174	-0.174	0.000	0.000	0.000	0.000
99	A	103	VAL	0	-0.028	-0.015	18.233	-0.041	-0.041	0.000	0.000	0.000	0.000
100	A	104	LEU	0	0.048	0.021	18.860	0.093	0.093	0.000	0.000	0.000	0.000
101	A	105	LYS	1	0.868	0.957	18.075	1.921	1.921	0.000	0.000	0.000	0.000
102	A	106	GLU	-1	-0.750	-0.872	13.106	-4.453	-4.453	0.000	0.000	0.000	0.000
103	A	107	GLY	0	-0.058	-0.036	17.026	-0.057	-0.057	0.000	0.000	0.000	0.000
104	A	108	VAL	0	-0.053	-0.011	19.208	0.094	0.094	0.000	0.000	0.000	0.000
105	A	109	GLU	-1	-0.861	-0.928	22.540	-0.720	-0.720	0.000	0.000	0.000	0.000
106	A	110	TYR	0	-0.092	-0.049	22.494	-0.073	-0.073	0.000	0.000	0.000	0.000
107	A	111	ARG	1	0.916	0.943	27.156	0.338	0.338	0.000	0.000	0.000	0.000
108	A	112	ILE	0	0.043	0.017	26.336	-0.043	-0.043	0.000	0.000	0.000	0.000
109	A	113	LYS	1	0.826	0.902	30.150	0.270	0.270	0.000	0.000	0.000	0.000
110	A	114	ILE	0	0.006	0.011	32.133	0.008	0.008	0.000	0.000	0.000	0.000
111	A	115	SER	0	0.034	0.018	34.701	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	116	PHE	0	-0.018	-0.003	37.724	0.024	0.024	0.000	0.000	0.000	0.000
113	A	117	ARG	1	0.917	0.959	40.068	0.006	0.006	0.000	0.000	0.000	0.000
114	A	118	VAL	0	0.028	0.025	43.556	0.019	0.019	0.000	0.000	0.000	0.000
115	A	119	ASN	0	-0.073	-0.045	45.645	-0.029	-0.029	0.000	0.000	0.000	0.000
116	A	120	ARG	1	0.828	0.898	48.906	-0.126	-0.126	0.000	0.000	0.000	0.000
117	A	121	GLU	-1	-0.774	-0.901	49.605	0.114	0.114	0.000	0.000	0.000	0.000
118	A	122	ILE	0	-0.007	0.000	47.574	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	123	VAL	0	-0.010	0.007	41.797	0.016	0.016	0.000	0.000	0.000	0.000
120	A	124	SER	0	-0.027	-0.047	44.009	-0.024	-0.024	0.000	0.000	0.000	0.000
121	A	125	GLY	0	0.040	0.011	40.741	0.020	0.020	0.000	0.000	0.000	0.000
122	A	126	MET	0	-0.041	-0.015	37.600	0.029	0.029	0.000	0.000	0.000	0.000
123	A	127	LYS	1	0.972	0.972	33.752	-0.364	-0.364	0.000	0.000	0.000	0.000
124	A	128	TYR	0	-0.039	-0.016	26.169	0.027	0.027	0.000	0.000	0.000	0.000
125	A	129	ILE	0	-0.011	-0.002	27.602	-0.018	-0.018	0.000	0.000	0.000	0.000
126	A	130	GLN	0	0.022	0.015	23.315	-0.081	-0.081	0.000	0.000	0.000	0.000
127	A	131	HIS	-1	-0.857	-0.910	22.521	0.936	0.936	0.000	0.000	0.000	0.000
128	A	132	THR	0	-0.038	-0.032	16.830	-0.072	-0.072	0.000	0.000	0.000	0.000
129	A	133	TYR	-1	-0.853	-0.936	16.522	1.749	1.749	0.000	0.000	0.000	0.000
130	A	134	ARG	1	0.815	0.893	7.319	-1.884	-1.884	0.000	0.000	0.000	0.000
131	A	135	LYS	1	0.779	0.864	5.381	-13.397	-13.397	0.000	0.000	0.000	0.000
132	A	136	GLY	0	0.021	0.016	12.403	0.236	0.236	0.000	0.000	0.000	0.000
133	A	137	VAL	0	-0.017	0.000	12.352	-0.131	-0.131	0.000	0.000	0.000	0.000
134	A	138	LYS	0	0.003	0.005	14.962	-0.013	-0.013	0.000	0.000	0.000	0.000
135	A	139	ILE	0	-0.095	-0.071	12.713	0.294	0.294	0.000	0.000	0.000	0.000
136	A	140	ASP	-1	-0.797	-0.890	16.127	0.562	0.562	0.000	0.000	0.000	0.000
137	A	141	LYS	1	0.927	0.985	19.469	-1.006	-1.006	0.000	0.000	0.000	0.000
138	A	142	THR	0	-0.009	-0.001	23.287	-0.083	-0.083	0.000	0.000	0.000	0.000
139	A	143	ASP	-1	-0.885	-0.939	25.766	0.481	0.481	0.000	0.000	0.000	0.000
140	A	144	TYR	0	-0.064	-0.066	25.710	-0.034	-0.034	0.000	0.000	0.000	0.000
141	A	145	MET	0	-0.055	-0.018	31.481	0.003	0.003	0.000	0.000	0.000	0.000
142	A	146	VAL	0	-0.015	-0.006	35.197	-0.036	-0.036	0.000	0.000	0.000	0.000
143	A	147	GLY	0	0.010	0.012	37.313	-0.029	-0.029	0.000	0.000	0.000	0.000
144	A	148	SER	0	-0.015	-0.013	40.667	0.019	0.019	0.000	0.000	0.000	0.000
145	A	149	TYR	0	-0.051	-0.024	40.460	-0.029	-0.029	0.000	0.000	0.000	0.000
146	A	150	GLY	0	0.063	0.033	45.751	0.017	0.017	0.000	0.000	0.000	0.000
147	A	151	PRO	0	-0.013	0.000	48.020	-0.011	-0.011	0.000	0.000	0.000	0.000
148	A	152	ARG	1	0.832	0.920	46.217	0.039	0.039	0.000	0.000	0.000	0.000
149	A	153	ALA	0	0.017	0.011	49.084	0.002	0.002	0.000	0.000	0.000	0.000
150	A	154	GLU	-1	-0.928	-0.964	47.112	-0.093	-0.093	0.000	0.000	0.000	0.000
151	A	155	GLU	-1	-0.928	-0.960	42.125	-0.082	-0.082	0.000	0.000	0.000	0.000
152	A	156	TYR	0	-0.032	-0.030	42.042	-0.016	-0.016	0.000	0.000	0.000	0.000
153	A	157	GLU	-1	-0.822	-0.897	38.871	-0.201	-0.201	0.000	0.000	0.000	0.000
154	A	158	PHE	0	0.007	0.002	34.238	-0.008	-0.008	0.000	0.000	0.000	0.000
155	A	159	LEU	0	-0.039	-0.023	34.432	-0.017	-0.017	0.000	0.000	0.000	0.000
156	A	160	THR	0	0.066	0.047	30.078	0.006	0.006	0.000	0.000	0.000	0.000
157	A	161	PRO	0	0.006	-0.003	30.553	-0.053	-0.053	0.000	0.000	0.000	0.000
158	A	162	MET	0	-0.057	-0.010	28.300	0.003	0.003	0.000	0.000	0.000	0.000
159	A	163	GLU	-1	-0.801	-0.867	24.459	-0.065	-0.065	0.000	0.000	0.000	0.000
160	A	164	GLU	-1	-0.929	-0.967	21.648	-0.995	-0.995	0.000	0.000	0.000	0.000
161	A	165	ALA	0	-0.010	-0.001	19.353	0.080	0.080	0.000	0.000	0.000	0.000
162	A	166	PRO	0	0.042	0.016	15.141	-0.250	-0.250	0.000	0.000	0.000	0.000
163	A	167	LYS	1	0.977	0.975	13.715	1.765	1.765	0.000	0.000	0.000	0.000
164	A	168	GLY	0	0.004	0.000	11.340	0.102	0.102	0.000	0.000	0.000	0.000
165	A	169	MET	0	-0.083	-0.067	8.750	-1.436	-1.436	0.000	0.000	0.000	0.000
166	A	170	LEU	0	0.016	0.016	5.427	-3.336	-3.336	0.000	0.000	0.000	0.000
167	A	171	ALA	0	0.040	0.029	7.444	-0.451	-0.451	0.000	0.000	0.000	0.000
168	A	172	ARG	1	0.799	0.893	8.776	7.497	7.497	0.000	0.000	0.000	0.000
169	A	173	GLY	0	-0.034	-0.012	9.920	-0.261	-0.261	0.000	0.000	0.000	0.000
170	A	174	SER	0	-0.011	-0.023	10.590	-0.185	-0.185	0.000	0.000	0.000	0.000
171	A	175	TYR	0	-0.044	-0.039	12.236	0.771	0.771	0.000	0.000	0.000	0.000
172	A	176	ASN	0	-0.059	-0.028	15.221	-0.126	-0.126	0.000	0.000	0.000	0.000
173	A	177	ILE	0	0.036	0.016	18.310	0.119	0.119	0.000	0.000	0.000	0.000
174	A	178	LYS	1	0.861	0.940	21.165	-1.034	-1.034	0.000	0.000	0.000	0.000
175	A	179	SER	0	0.053	0.031	24.319	-0.001	-0.001	0.000	0.000	0.000	0.000
176	A	180	ARG	1	0.878	0.929	27.359	-0.529	-0.529	0.000	0.000	0.000	0.000
177	A	181	PHE	0	0.009	0.012	30.995	-0.022	-0.022	0.000	0.000	0.000	0.000
178	A	182	THR	0	-0.035	-0.039	34.091	0.024	0.024	0.000	0.000	0.000	0.000
179	A	183	ASP	-1	-0.743	-0.871	36.415	0.239	0.239	0.000	0.000	0.000	0.000
180	A	184	ASP	-1	-0.833	-0.910	38.861	0.275	0.275	0.000	0.000	0.000	0.000
181	A	185	ASP	-1	-0.894	-0.928	41.029	0.264	0.264	0.000	0.000	0.000	0.000
182	A	186	ARG	1	0.851	0.922	37.369	-0.450	-0.450	0.000	0.000	0.000	0.000
183	A	187	THR	0	-0.013	0.000	38.743	0.026	0.026	0.000	0.000	0.000	0.000
184	A	188	ASP	-1	-0.861	-0.913	34.136	0.435	0.435	0.000	0.000	0.000	0.000
185	A	189	HIS	0	-0.081	-0.059	37.266	-0.021	-0.021	0.000	0.000	0.000	0.000
186	A	190	LEU	0	-0.028	-0.014	33.400	-0.024	-0.024	0.000	0.000	0.000	0.000
187	A	191	SER	0	0.020	0.020	30.562	0.015	0.015	0.000	0.000	0.000	0.000
188	A	192	TRP	0	0.000	-0.008	27.436	-0.010	-0.010	0.000	0.000	0.000	0.000
189	A	193	GLU	-1	-0.856	-0.923	23.612	0.709	0.709	0.000	0.000	0.000	0.000
190	A	194	TRP	0	-0.037	-0.027	23.184	-0.136	-0.136	0.000	0.000	0.000	0.000
191	A	195	ASN	0	-0.003	0.013	18.795	0.255	0.255	0.000	0.000	0.000	0.000
192	A	196	LEU	0	0.040	0.036	18.349	-0.170	-0.170	0.000	0.000	0.000	0.000
193	A	197	THR	0	-0.052	-0.030	13.963	0.129	0.129	0.000	0.000	0.000	0.000
194	A	198	ILE	0	0.030	0.037	13.607	-0.132	-0.132	0.000	0.000	0.000	0.000
195	A	199	LYS	1	0.857	0.903	13.798	1.984	1.984	0.000	0.000	0.000	0.000
196	A	200	LYS	1	0.972	0.978	12.491	4.803	4.803	0.000	0.000	0.000	0.000
197	A	201	GLU	-1	-0.919	-0.960	14.615	-2.139	-2.139	0.000	0.000	0.000	0.000
198	A	202	TRP	0	0.023	-0.003	18.102	0.026	0.026	0.000	0.000	0.000	0.000
199	A	203	LYS	1	0.885	0.942	20.872	1.160	1.160	0.000	0.000	0.000	0.000
200	A	204	ASP	-2	-1.774	-1.855	15.634	-5.270	-5.270	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLU)