FMO DATABASE

FMODB ID: 5N21Z

Calculation Name: 5LSB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5LSB

Chain ID: A

ChEMBL ID:

UniProt ID: Q02554

Base Structure: X-ray

Registration Date: 2023-09-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
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	179
LigandResidueName
LigandFragmentNumber	0
LigandCharge	DGL=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1880463.250945
FMO2-HF: Nuclear repulsion	1808930.602266
FMO2-HF: Total energy	-71532.648679
FMO2-MP2: Total energy	-71746.362186

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:8:GLY)

Summations of interaction energy for fragment #1(A:8: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.
-2.793	1.39	0.463	-2.146	-2.497	-0.004

Interaction energy analysis for fragmet #1(A:8:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.013 / q_NPA : -0.022

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	10	THR	0	-0.019	0.012	2.682	-2.871	0.558	0.045	-1.712	-1.762	-0.002
4	A	11	VAL	0	-0.011	-0.004	3.882	-1.542	-1.379	0.001	-0.112	-0.051	-0.001
5	A	12	TYR	0	-0.015	-0.005	6.639	0.314	0.314	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.006	-0.001	9.325	-0.045	-0.045	0.000	0.000	0.000	0.000
7	A	14	GLY	0	0.037	0.006	12.763	0.051	0.051	0.000	0.000	0.000	0.000
8	A	15	ASN	0	-0.065	-0.052	15.755	0.008	0.008	0.000	0.000	0.000	0.000
9	A	16	ILE	0	-0.007	0.007	15.817	0.000	0.000	0.000	0.000	0.000	0.000
10	A	17	ASP	-1	-0.780	-0.872	20.264	-0.046	-0.046	0.000	0.000	0.000	0.000
11	A	18	PRO	0	0.060	0.017	23.348	0.001	0.001	0.000	0.000	0.000	0.000
12	A	19	ARG	1	0.820	0.884	24.519	0.055	0.055	0.000	0.000	0.000	0.000
13	A	20	ILE	0	-0.036	0.008	20.770	0.003	0.003	0.000	0.000	0.000	0.000
14	A	21	THR	0	0.072	0.039	22.754	0.004	0.004	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.936	0.948	16.709	-0.094	-0.094	0.000	0.000	0.000	0.000
16	A	23	GLU	-1	-0.928	-0.952	19.656	-0.013	-0.013	0.000	0.000	0.000	0.000
17	A	24	GLN	0	0.095	0.042	21.583	-0.010	-0.010	0.000	0.000	0.000	0.000
18	A	25	LEU	0	-0.036	-0.007	16.304	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	26	TYR	0	-0.009	-0.015	16.440	-0.029	-0.029	0.000	0.000	0.000	0.000
20	A	27	GLU	-1	-0.911	-0.956	18.243	-0.069	-0.069	0.000	0.000	0.000	0.000
21	A	28	LEU	0	-0.021	0.001	18.193	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	29	PHE	0	-0.001	-0.036	13.304	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	30	ILE	0	-0.014	0.001	15.684	-0.030	-0.030	0.000	0.000	0.000	0.000
24	A	31	GLN	0	-0.068	-0.028	17.750	0.003	0.003	0.000	0.000	0.000	0.000
25	A	32	ILE	0	-0.101	-0.033	14.151	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	33	ASN	0	0.031	0.003	11.962	0.013	0.013	0.000	0.000	0.000	0.000
27	A	34	PRO	0	0.037	0.044	13.898	0.020	0.020	0.000	0.000	0.000	0.000
28	A	35	VAL	0	0.006	-0.012	12.296	-0.029	-0.029	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.064	-0.009	10.003	0.025	0.025	0.000	0.000	0.000	0.000
30	A	37	ARG	1	0.873	0.916	10.983	-0.531	-0.531	0.000	0.000	0.000	0.000
31	A	38	ILE	0	0.044	0.027	11.631	-0.019	-0.019	0.000	0.000	0.000	0.000
32	A	39	LYS	1	0.919	0.963	11.970	-0.130	-0.130	0.000	0.000	0.000	0.000
33	A	40	TYR	0	-0.008	-0.039	13.553	-0.037	-0.037	0.000	0.000	0.000	0.000
34	A	41	PRO	0	-0.071	-0.027	15.069	0.016	0.016	0.000	0.000	0.000	0.000
35	A	42	LYS	1	0.872	0.943	18.141	-0.024	-0.024	0.000	0.000	0.000	0.000
36	A	43	ASP	-1	-0.751	-0.871	21.936	0.018	0.018	0.000	0.000	0.000	0.000
37	A	44	LYS	1	0.901	0.923	22.360	-0.056	-0.056	0.000	0.000	0.000	0.000
38	A	45	VAL	0	0.011	0.015	26.629	0.001	0.001	0.000	0.000	0.000	0.000
39	A	46	LEU	0	0.014	0.003	27.462	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	47	GLN	0	-0.036	-0.010	27.323	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	48	ALA	0	0.028	0.037	26.212	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	49	TYR	0	-0.047	-0.034	20.639	0.006	0.006	0.000	0.000	0.000	0.000
43	A	50	GLN	0	-0.034	-0.032	19.405	0.005	0.005	0.000	0.000	0.000	0.000
44	A	51	GLY	0	0.059	0.050	19.980	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	52	TYR	0	-0.080	-0.038	13.535	-0.018	-0.018	0.000	0.000	0.000	0.000
46	A	53	ALA	0	-0.007	-0.013	13.739	0.038	0.038	0.000	0.000	0.000	0.000
47	A	54	PHE	0	-0.013	-0.003	7.775	-0.036	-0.036	0.000	0.000	0.000	0.000
48	A	55	ILE	0	0.007	0.007	9.165	0.118	0.118	0.000	0.000	0.000	0.000
49	A	56	GLU	-1	-0.799	-0.877	6.864	0.893	0.893	0.000	0.000	0.000	0.000
50	A	57	PHE	0	0.046	0.006	7.308	-0.025	-0.025	0.000	0.000	0.000	0.000
51	A	58	TYR	0	0.062	0.013	8.072	0.294	0.294	0.000	0.000	0.000	0.000
52	A	59	ASN	0	-0.033	-0.016	6.378	0.060	0.060	0.000	0.000	0.000	0.000
53	A	60	GLN	0	0.002	-0.008	2.809	-0.929	-0.607	0.421	-0.290	-0.452	-0.001
54	A	61	GLY	0	0.051	0.028	4.750	-0.145	-0.097	-0.001	-0.007	-0.040	0.000
55	A	62	ASP	-1	-0.825	-0.913	8.440	-0.371	-0.371	0.000	0.000	0.000	0.000
56	A	63	ALA	0	0.002	0.004	5.192	0.067	0.102	-0.001	-0.010	-0.023	0.000
57	A	64	GLN	0	-0.052	-0.038	4.391	0.429	0.514	-0.001	-0.005	-0.079	0.000
58	A	65	TYR	0	-0.032	-0.011	7.853	0.179	0.179	0.000	0.000	0.000	0.000
59	A	66	ALA	0	0.052	0.016	10.111	0.096	0.096	0.000	0.000	0.000	0.000
60	A	67	ILE	0	-0.063	-0.030	6.747	0.091	0.091	0.000	0.000	0.000	0.000
61	A	68	LYS	1	0.908	0.950	10.899	0.586	0.586	0.000	0.000	0.000	0.000
62	A	69	ILE	0	0.018	0.028	13.558	0.052	0.052	0.000	0.000	0.000	0.000
63	A	70	MET	0	0.028	0.011	14.231	0.056	0.056	0.000	0.000	0.000	0.000
64	A	71	ASN	0	-0.049	-0.010	14.001	0.037	0.037	0.000	0.000	0.000	0.000
65	A	72	ASN	0	-0.060	-0.034	15.991	0.026	0.026	0.000	0.000	0.000	0.000
66	A	73	THR	0	0.052	0.029	18.957	0.018	0.018	0.000	0.000	0.000	0.000
67	A	74	VAL	0	0.050	0.027	19.906	0.019	0.019	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.804	0.882	21.473	0.098	0.098	0.000	0.000	0.000	0.000
69	A	76	LEU	0	0.033	0.021	20.253	0.007	0.007	0.000	0.000	0.000	0.000
70	A	77	TYR	0	0.005	-0.022	24.293	0.002	0.002	0.000	0.000	0.000	0.000
71	A	78	ASP	-1	-0.878	-0.940	27.567	-0.076	-0.076	0.000	0.000	0.000	0.000
72	A	79	ARG	1	0.752	0.876	23.253	0.083	0.083	0.000	0.000	0.000	0.000
73	A	80	LEU	0	0.000	0.004	21.156	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	81	ILE	0	0.042	0.040	16.432	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.786	0.891	15.366	0.181	0.181	0.000	0.000	0.000	0.000
76	A	83	VAL	0	0.032	0.016	10.433	0.009	0.009	0.000	0.000	0.000	0.000
77	A	84	ARG	1	0.944	0.972	10.006	0.339	0.339	0.000	0.000	0.000	0.000
78	A	85	GLN	0	0.076	0.049	4.812	-0.201	-0.201	0.000	0.000	0.000	0.000
79	A	86	VAL	0	0.015	0.014	4.291	0.286	0.387	-0.001	-0.010	-0.090	0.000
80	A	106	PRO	0	-0.018	-0.033	19.916	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	107	ILE	0	-0.035	0.006	22.914	0.005	0.005	0.000	0.000	0.000	0.000
82	A	108	ALA	0	0.070	0.044	25.474	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	109	LYS	1	0.791	0.911	27.930	0.087	0.087	0.000	0.000	0.000	0.000
84	A	110	LEU	0	0.039	0.021	30.155	0.001	0.001	0.000	0.000	0.000	0.000
85	A	111	PHE	0	-0.027	-0.027	33.790	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	112	ILE	0	0.006	0.004	35.970	0.003	0.003	0.000	0.000	0.000	0.000
87	A	113	LYS	1	0.948	0.976	38.880	0.039	0.039	0.000	0.000	0.000	0.000
88	A	114	ASN	0	-0.025	-0.033	41.799	0.002	0.002	0.000	0.000	0.000	0.000
89	A	115	LEU	0	-0.002	-0.005	39.327	0.002	0.002	0.000	0.000	0.000	0.000
90	A	116	ALA	0	0.044	0.028	43.958	0.000	0.000	0.000	0.000	0.000	0.000
91	A	117	ASP	-1	-0.841	-0.930	44.884	-0.034	-0.034	0.000	0.000	0.000	0.000
92	A	118	SER	0	-0.033	-0.026	45.055	0.000	0.000	0.000	0.000	0.000	0.000
93	A	119	ILE	0	-0.068	-0.017	40.975	0.000	0.000	0.000	0.000	0.000	0.000
94	A	120	ASP	-1	-0.811	-0.901	38.969	-0.041	-0.041	0.000	0.000	0.000	0.000
95	A	121	SER	0	0.067	0.021	34.475	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	122	ASP	-1	-0.825	-0.913	36.397	-0.033	-0.033	0.000	0.000	0.000	0.000
97	A	123	GLN	0	-0.004	-0.015	37.905	0.002	0.002	0.000	0.000	0.000	0.000
98	A	124	LEU	0	0.015	0.020	36.553	0.001	0.001	0.000	0.000	0.000	0.000
99	A	125	VAL	0	0.019	0.014	33.411	0.000	0.000	0.000	0.000	0.000	0.000
100	A	126	LYS	1	0.829	0.893	36.032	0.031	0.031	0.000	0.000	0.000	0.000
101	A	127	ILE	0	-0.075	-0.037	39.232	0.002	0.002	0.000	0.000	0.000	0.000
102	A	128	PHE	0	0.037	-0.006	35.645	0.001	0.001	0.000	0.000	0.000	0.000
103	A	129	ASN	0	0.032	0.009	34.281	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	130	LYS	1	0.862	0.955	36.311	0.026	0.026	0.000	0.000	0.000	0.000
105	A	131	PHE	0	-0.003	-0.001	37.409	0.002	0.002	0.000	0.000	0.000	0.000
106	A	132	GLY	0	0.015	0.006	34.011	0.001	0.001	0.000	0.000	0.000	0.000
107	A	133	LYS	1	0.821	0.911	26.617	0.049	0.049	0.000	0.000	0.000	0.000
108	A	134	LEU	0	0.034	0.022	29.711	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	135	ILE	0	-0.004	0.000	22.130	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	136	ARG	1	0.858	0.927	19.638	0.104	0.104	0.000	0.000	0.000	0.000
111	A	137	GLU	-1	-0.868	-0.926	26.526	-0.073	-0.073	0.000	0.000	0.000	0.000
112	A	138	PRO	0	-0.048	-0.035	29.349	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	139	GLU	-1	-0.863	-0.906	29.517	-0.089	-0.089	0.000	0.000	0.000	0.000
114	A	140	ILE	0	0.005	-0.005	32.036	0.002	0.002	0.000	0.000	0.000	0.000
115	A	141	PHE	0	-0.017	-0.014	34.371	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	142	TYR	0	0.047	0.020	36.782	0.002	0.002	0.000	0.000	0.000	0.000
117	A	143	LEU	0	0.029	0.025	37.937	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	144	SER	0	-0.021	-0.024	41.410	0.003	0.003	0.000	0.000	0.000	0.000
119	A	145	ASN	0	0.005	0.006	43.664	0.004	0.004	0.000	0.000	0.000	0.000
120	A	146	GLY	0	0.082	0.034	42.965	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	147	LYS	1	0.864	0.934	44.205	0.036	0.036	0.000	0.000	0.000	0.000
122	A	148	LEU	0	0.031	0.023	43.394	0.001	0.001	0.000	0.000	0.000	0.000
123	A	149	LYS	1	0.865	0.945	41.152	0.036	0.036	0.000	0.000	0.000	0.000
124	A	150	CYS	0	-0.069	-0.023	38.479	0.002	0.002	0.000	0.000	0.000	0.000
125	A	151	ALA	0	0.047	0.013	35.680	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	152	TYR	0	-0.036	-0.013	31.006	0.000	0.000	0.000	0.000	0.000	0.000
127	A	153	VAL	0	0.033	0.017	32.055	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	154	TYR	0	-0.022	-0.021	26.356	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	155	PHE	0	0.046	0.017	29.234	0.001	0.001	0.000	0.000	0.000	0.000
130	A	156	GLU	-1	-0.871	-0.945	25.421	-0.056	-0.056	0.000	0.000	0.000	0.000
131	A	157	ASP	-1	-0.731	-0.851	27.053	-0.034	-0.034	0.000	0.000	0.000	0.000
132	A	158	PHE	0	0.026	-0.011	27.516	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	159	GLU	-1	-0.913	-0.937	31.853	-0.023	-0.023	0.000	0.000	0.000	0.000
134	A	160	LYS	1	0.777	0.877	33.129	0.028	0.028	0.000	0.000	0.000	0.000
135	A	161	ALA	0	-0.001	-0.005	32.727	0.001	0.001	0.000	0.000	0.000	0.000
136	A	162	ASP	-1	-0.794	-0.872	34.765	-0.035	-0.035	0.000	0.000	0.000	0.000
137	A	163	LEU	0	-0.057	-0.018	37.649	0.002	0.002	0.000	0.000	0.000	0.000
138	A	164	ALA	0	0.007	0.009	37.381	0.001	0.001	0.000	0.000	0.000	0.000
139	A	165	ILE	0	0.009	0.012	36.762	0.001	0.001	0.000	0.000	0.000	0.000
140	A	166	LYS	1	0.926	0.966	40.444	0.022	0.022	0.000	0.000	0.000	0.000
141	A	167	SER	0	-0.058	-0.040	42.786	0.002	0.002	0.000	0.000	0.000	0.000
142	A	168	LEU	0	-0.036	-0.018	40.455	0.001	0.001	0.000	0.000	0.000	0.000
143	A	169	ASN	0	0.032	0.023	42.901	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	170	ASN	0	-0.017	-0.011	44.420	0.002	0.002	0.000	0.000	0.000	0.000
145	A	171	GLN	0	0.048	0.032	46.859	0.002	0.002	0.000	0.000	0.000	0.000
146	A	172	LEU	0	-0.049	-0.010	48.031	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	173	VAL	0	0.035	0.008	44.553	0.001	0.001	0.000	0.000	0.000	0.000
148	A	174	ALA	0	0.031	0.006	47.731	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	175	ASN	0	-0.007	-0.018	49.508	0.000	0.000	0.000	0.000	0.000	0.000
150	A	176	ASN	0	-0.012	0.017	48.215	0.000	0.000	0.000	0.000	0.000	0.000
151	A	177	ARG	1	0.872	0.938	48.877	0.023	0.023	0.000	0.000	0.000	0.000
152	A	178	ILE	0	0.022	0.025	42.693	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	179	THR	0	-0.023	-0.021	42.285	0.001	0.001	0.000	0.000	0.000	0.000
154	A	180	VAL	0	-0.034	-0.024	38.480	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	181	ASP	-1	-0.872	-0.931	38.541	-0.041	-0.041	0.000	0.000	0.000	0.000
156	A	182	TYR	0	-0.020	-0.048	32.723	-0.005	-0.005	0.000	0.000	0.000	0.000
157	A	183	ALA	0	-0.019	-0.002	31.494	0.000	0.000	0.000	0.000	0.000	0.000
158	A	184	PHE	0	0.095	0.064	32.763	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	185	LYS	1	1.018	1.124	27.261	0.075	0.075	0.000	0.000	0.000	0.000
160	A	186	DGL	0	-1.351	-0.456	27.415	-0.007	-0.007	0.000	0.000	0.000	0.000
161	A	187	ASN	-1	-0.163	-0.833	33.044	-0.071	-0.071	0.000	0.000	0.000	0.000
162	A	188	GLY	0	0.512	0.178	32.601	-0.003	-0.003	0.000	0.000	0.000	0.000
163	A	189	LYS	1	0.834	0.902	25.795	0.091	0.091	0.000	0.000	0.000	0.000
164	A	190	GLY	0	0.102	0.045	30.565	0.003	0.003	0.000	0.000	0.000	0.000
165	A	191	ASN	0	-0.037	-0.015	28.568	0.004	0.004	0.000	0.000	0.000	0.000
166	A	192	ALA	0	0.101	0.043	31.246	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	193	LYS	1	0.883	0.942	27.333	0.058	0.058	0.000	0.000	0.000	0.000
168	A	194	TYR	0	-0.060	-0.023	25.063	-0.006	-0.006	0.000	0.000	0.000	0.000
169	A	195	GLY	0	0.104	0.068	28.026	0.004	0.004	0.000	0.000	0.000	0.000
170	A	196	ASP	-1	-0.810	-0.904	22.685	-0.068	-0.068	0.000	0.000	0.000	0.000
171	A	197	ASP	-1	-0.864	-0.943	23.433	-0.057	-0.057	0.000	0.000	0.000	0.000
172	A	198	VAL	0	0.057	0.024	25.444	0.002	0.002	0.000	0.000	0.000	0.000
173	A	199	ASP	-1	-0.797	-0.897	22.638	-0.014	-0.014	0.000	0.000	0.000	0.000
174	A	200	ARG	1	0.802	0.894	20.114	0.065	0.065	0.000	0.000	0.000	0.000
175	A	201	LEU	0	-0.026	-0.001	21.967	0.001	0.001	0.000	0.000	0.000	0.000
176	A	202	LEU	0	-0.028	0.004	24.914	0.004	0.004	0.000	0.000	0.000	0.000
177	A	203	ASN	0	-0.070	-0.054	19.936	0.017	0.017	0.000	0.000	0.000	0.000
178	A	204	LYS	1	0.882	0.961	20.089	-0.002	-0.002	0.000	0.000	0.000	0.000
179	A	205	GLU	-1	-0.917	-0.950	17.374	-0.066	-0.066	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:GLY)