FMO DATABASE

FMODB ID: YNZ82

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:

IFIE MAP

IFIE Diagram

Modeling method

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1885704.543044
FMO2-HF: Nuclear repulsion	1814169.256954
FMO2-HF: Total energy	-71535.28609
FMO2-MP2: Total energy	-71748.93978

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.
-3.348	0.634	0.731	-2.127	-2.587	0.001

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 : 0.016 / q_NPA : -0.007

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	-0.005	-0.003	2.648	-2.395	0.025	0.248	-1.255	-1.413	0.005
4	A	11	VAL	0	-0.024	-0.016	3.224	-2.701	-1.845	0.042	-0.527	-0.372	-0.004
5	A	12	TYR	0	0.015	0.019	6.070	0.324	0.324	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.014	-0.003	8.942	-0.122	-0.122	0.000	0.000	0.000	0.000
7	A	14	GLY	0	0.037	0.006	12.377	0.059	0.059	0.000	0.000	0.000	0.000
8	A	15	ASN	0	-0.043	-0.035	15.554	-0.007	-0.007	0.000	0.000	0.000	0.000
9	A	16	ILE	0	0.018	0.021	15.599	-0.005	-0.005	0.000	0.000	0.000	0.000
10	A	17	ASP	-1	-0.769	-0.866	19.888	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	18	PRO	0	0.024	-0.004	23.153	0.002	0.002	0.000	0.000	0.000	0.000
12	A	19	ARG	1	0.836	0.899	24.144	0.022	0.022	0.000	0.000	0.000	0.000
13	A	20	ILE	0	-0.006	0.017	20.639	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	21	THR	0	0.054	0.029	22.792	0.010	0.010	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.921	0.941	16.641	-0.179	-0.179	0.000	0.000	0.000	0.000
16	A	23	GLU	-1	-0.917	-0.948	19.268	0.014	0.014	0.000	0.000	0.000	0.000
17	A	24	GLN	0	0.110	0.053	21.185	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	25	LEU	0	-0.049	-0.016	16.092	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	26	TYR	0	-0.024	-0.024	16.093	-0.026	-0.026	0.000	0.000	0.000	0.000
20	A	27	GLU	-1	-0.912	-0.954	17.880	-0.057	-0.057	0.000	0.000	0.000	0.000
21	A	28	LEU	0	-0.009	0.004	17.858	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	29	PHE	0	-0.003	-0.028	12.788	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	30	ILE	0	0.003	0.004	15.543	-0.040	-0.040	0.000	0.000	0.000	0.000
24	A	31	GLN	0	-0.075	-0.027	17.519	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	32	ILE	0	-0.089	-0.030	14.244	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	33	ASN	0	0.011	-0.014	11.905	0.001	0.001	0.000	0.000	0.000	0.000
27	A	34	PRO	0	0.016	0.028	13.470	0.038	0.038	0.000	0.000	0.000	0.000
28	A	35	VAL	0	0.005	-0.003	12.360	-0.027	-0.027	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.040	-0.008	9.969	0.022	0.022	0.000	0.000	0.000	0.000
30	A	37	ARG	1	0.847	0.900	10.698	-0.572	-0.572	0.000	0.000	0.000	0.000
31	A	38	ILE	0	0.049	0.030	11.735	0.002	0.002	0.000	0.000	0.000	0.000
32	A	39	LYS	1	0.910	0.955	11.904	-0.359	-0.359	0.000	0.000	0.000	0.000
33	A	40	TYR	0	-0.001	-0.024	13.454	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	41	PRO	0	-0.054	-0.017	14.956	0.003	0.003	0.000	0.000	0.000	0.000
35	A	42	LYS	1	0.926	0.961	18.039	-0.082	-0.082	0.000	0.000	0.000	0.000
36	A	43	ASP	-1	-0.726	-0.851	21.845	0.080	0.080	0.000	0.000	0.000	0.000
37	A	44	LYS	1	0.808	0.888	22.109	-0.123	-0.123	0.000	0.000	0.000	0.000
38	A	45	VAL	0	0.017	0.019	27.040	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	46	LEU	0	0.022	0.000	27.193	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	47	GLN	0	-0.045	-0.013	27.306	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	48	ALA	0	0.040	0.040	26.043	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	49	TYR	0	-0.028	-0.027	20.676	0.015	0.015	0.000	0.000	0.000	0.000
43	A	50	GLN	0	-0.069	-0.055	19.098	0.005	0.005	0.000	0.000	0.000	0.000
44	A	51	GLY	0	0.034	0.026	19.933	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	52	TYR	0	-0.086	-0.039	13.549	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	53	ALA	0	-0.011	-0.015	13.624	0.028	0.028	0.000	0.000	0.000	0.000
47	A	54	PHE	0	-0.014	-0.002	7.398	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	55	ILE	0	-0.005	0.003	8.776	0.054	0.054	0.000	0.000	0.000	0.000
49	A	56	GLU	-1	-0.786	-0.869	7.048	0.972	0.972	0.000	0.000	0.000	0.000
50	A	57	PHE	0	0.020	0.007	7.551	-0.090	-0.090	0.000	0.000	0.000	0.000
51	A	58	TYR	0	0.055	0.022	8.225	0.172	0.172	0.000	0.000	0.000	0.000
52	A	59	ASN	0	-0.028	-0.016	6.811	-0.040	-0.040	0.000	0.000	0.000	0.000
53	A	60	GLN	0	-0.001	-0.011	2.656	-0.685	-0.376	0.442	-0.281	-0.470	0.000
54	A	61	GLY	0	0.058	0.028	5.071	-0.032	0.024	-0.001	-0.007	-0.048	0.000
55	A	62	ASP	-1	-0.801	-0.903	8.440	-0.467	-0.467	0.000	0.000	0.000	0.000
56	A	63	ALA	0	0.030	0.020	5.366	0.159	0.196	-0.001	-0.010	-0.026	0.000
57	A	64	GLN	0	-0.036	-0.029	4.856	0.597	0.597	0.000	0.000	0.000	0.000
58	A	65	TYR	0	0.001	0.017	8.000	0.197	0.197	0.000	0.000	0.000	0.000
59	A	66	ALA	0	0.056	0.015	9.989	0.086	0.086	0.000	0.000	0.000	0.000
60	A	67	ILE	0	-0.053	-0.037	6.328	0.102	0.102	0.000	0.000	0.000	0.000
61	A	68	LYS	1	0.829	0.904	9.880	0.834	0.834	0.000	0.000	0.000	0.000
62	A	69	ILE	0	0.042	0.047	13.784	0.060	0.060	0.000	0.000	0.000	0.000
63	A	70	MET	0	0.025	0.026	13.790	0.060	0.060	0.000	0.000	0.000	0.000
64	A	71	ASN	0	-0.031	-0.005	13.392	0.058	0.058	0.000	0.000	0.000	0.000
65	A	72	ASN	0	-0.040	-0.016	15.355	0.021	0.021	0.000	0.000	0.000	0.000
66	A	73	THR	0	0.011	0.001	18.424	0.020	0.020	0.000	0.000	0.000	0.000
67	A	74	VAL	0	0.038	0.021	19.282	0.017	0.017	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.781	0.877	20.961	0.081	0.081	0.000	0.000	0.000	0.000
69	A	76	LEU	0	0.019	0.008	19.785	0.005	0.005	0.000	0.000	0.000	0.000
70	A	77	TYR	0	-0.011	-0.026	23.827	0.003	0.003	0.000	0.000	0.000	0.000
71	A	78	ASP	-1	-0.876	-0.942	27.125	-0.055	-0.055	0.000	0.000	0.000	0.000
72	A	79	ARG	1	0.743	0.856	22.679	0.029	0.029	0.000	0.000	0.000	0.000
73	A	80	LEU	0	0.027	0.022	21.026	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	81	ILE	0	0.010	0.027	15.963	0.000	0.000	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.804	0.887	14.937	0.133	0.133	0.000	0.000	0.000	0.000
76	A	83	VAL	0	0.022	0.006	9.902	0.026	0.026	0.000	0.000	0.000	0.000
77	A	84	ARG	1	0.944	0.968	9.072	0.271	0.271	0.000	0.000	0.000	0.000
78	A	85	GLN	0	0.069	0.044	4.193	-0.158	-0.092	-0.001	-0.009	-0.056	0.000
79	A	86	VAL	0	0.006	0.010	3.639	0.341	0.579	0.002	-0.038	-0.202	0.000
80	A	106	PRO	0	-0.024	-0.035	19.572	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	107	ILE	0	0.032	0.034	22.563	0.001	0.001	0.000	0.000	0.000	0.000
82	A	108	ALA	0	0.085	0.057	24.934	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	109	LYS	1	0.766	0.894	27.172	0.065	0.065	0.000	0.000	0.000	0.000
84	A	110	LEU	0	0.041	0.020	29.318	0.001	0.001	0.000	0.000	0.000	0.000
85	A	111	PHE	0	0.008	-0.015	32.813	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	112	ILE	0	-0.007	0.002	35.336	0.003	0.003	0.000	0.000	0.000	0.000
87	A	113	LYS	1	0.833	0.914	38.314	0.027	0.027	0.000	0.000	0.000	0.000
88	A	114	ASN	0	0.013	-0.011	41.210	0.001	0.001	0.000	0.000	0.000	0.000
89	A	115	LEU	0	-0.007	0.002	38.902	0.002	0.002	0.000	0.000	0.000	0.000
90	A	116	ALA	0	0.054	0.033	43.510	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	117	ASP	-1	-0.840	-0.935	44.373	-0.027	-0.027	0.000	0.000	0.000	0.000
92	A	118	SER	0	-0.023	-0.017	44.217	0.000	0.000	0.000	0.000	0.000	0.000
93	A	119	ILE	0	-0.049	-0.007	40.497	0.001	0.001	0.000	0.000	0.000	0.000
94	A	120	ASP	-1	-0.792	-0.888	38.236	-0.030	-0.030	0.000	0.000	0.000	0.000
95	A	121	SER	0	0.037	0.006	33.263	0.001	0.001	0.000	0.000	0.000	0.000
96	A	122	ASP	-1	-0.777	-0.889	35.923	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	123	GLN	0	-0.014	-0.015	37.331	0.003	0.003	0.000	0.000	0.000	0.000
98	A	124	LEU	0	0.000	0.005	36.093	0.002	0.002	0.000	0.000	0.000	0.000
99	A	125	VAL	0	0.020	0.010	32.995	0.001	0.001	0.000	0.000	0.000	0.000
100	A	126	LYS	1	0.816	0.896	35.654	0.017	0.017	0.000	0.000	0.000	0.000
101	A	127	ILE	0	-0.064	-0.028	39.068	0.002	0.002	0.000	0.000	0.000	0.000
102	A	128	PHE	0	0.037	-0.006	35.302	0.001	0.001	0.000	0.000	0.000	0.000
103	A	129	ASN	0	0.034	0.004	33.732	0.000	0.000	0.000	0.000	0.000	0.000
104	A	130	LYS	1	0.830	0.937	35.762	0.011	0.011	0.000	0.000	0.000	0.000
105	A	131	PHE	0	-0.001	0.005	36.870	0.001	0.001	0.000	0.000	0.000	0.000
106	A	132	GLY	0	0.019	0.005	33.584	0.002	0.002	0.000	0.000	0.000	0.000
107	A	133	LYS	1	0.818	0.900	26.111	0.008	0.008	0.000	0.000	0.000	0.000
108	A	134	LEU	0	0.031	0.017	29.188	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	135	ILE	0	-0.003	0.009	21.592	0.000	0.000	0.000	0.000	0.000	0.000
110	A	136	ARG	1	0.835	0.915	19.378	0.058	0.058	0.000	0.000	0.000	0.000
111	A	137	GLU	-1	-0.839	-0.919	26.204	-0.048	-0.048	0.000	0.000	0.000	0.000
112	A	138	PRO	0	-0.055	-0.030	29.081	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	139	GLU	-1	-0.812	-0.870	28.919	-0.069	-0.069	0.000	0.000	0.000	0.000
114	A	140	ILE	0	0.010	-0.007	31.524	0.001	0.001	0.000	0.000	0.000	0.000
115	A	141	PHE	0	-0.035	-0.016	34.188	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	142	TYR	0	0.025	0.012	36.394	0.003	0.003	0.000	0.000	0.000	0.000
117	A	143	LEU	0	0.040	0.029	37.622	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	144	SER	0	-0.021	-0.013	41.165	0.003	0.003	0.000	0.000	0.000	0.000
119	A	145	ASN	0	0.042	0.015	43.655	0.003	0.003	0.000	0.000	0.000	0.000
120	A	146	GLY	0	0.046	0.028	42.723	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	147	LYS	1	0.873	0.929	43.778	0.031	0.031	0.000	0.000	0.000	0.000
122	A	148	LEU	0	0.030	0.018	42.860	0.001	0.001	0.000	0.000	0.000	0.000
123	A	149	LYS	1	0.833	0.932	40.641	0.026	0.026	0.000	0.000	0.000	0.000
124	A	150	CYS	0	-0.080	-0.036	37.917	0.002	0.002	0.000	0.000	0.000	0.000
125	A	151	ALA	0	0.040	0.012	35.115	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	152	TYR	0	-0.019	-0.005	30.910	0.001	0.001	0.000	0.000	0.000	0.000
127	A	153	VAL	0	0.015	0.012	31.648	0.000	0.000	0.000	0.000	0.000	0.000
128	A	154	TYR	0	-0.004	-0.035	25.240	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	155	PHE	0	0.037	0.022	28.231	0.001	0.001	0.000	0.000	0.000	0.000
130	A	156	GLU	-1	-0.836	-0.924	24.974	-0.011	-0.011	0.000	0.000	0.000	0.000
131	A	157	ASP	-1	-0.772	-0.873	26.614	0.005	0.005	0.000	0.000	0.000	0.000
132	A	158	PHE	0	0.025	-0.014	27.056	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	159	GLU	-1	-0.857	-0.904	31.362	0.006	0.006	0.000	0.000	0.000	0.000
134	A	160	LYS	1	0.773	0.870	32.817	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	161	ALA	0	0.006	0.010	32.310	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	162	ASP	-1	-0.818	-0.887	34.366	-0.013	-0.013	0.000	0.000	0.000	0.000
137	A	163	LEU	0	-0.045	-0.020	37.199	0.000	0.000	0.000	0.000	0.000	0.000
138	A	164	ALA	0	-0.001	0.016	36.835	0.000	0.000	0.000	0.000	0.000	0.000
139	A	165	ILE	0	0.000	-0.009	36.257	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	166	LYS	1	0.922	0.955	39.873	0.004	0.004	0.000	0.000	0.000	0.000
141	A	167	SER	0	-0.041	-0.024	42.153	0.001	0.001	0.000	0.000	0.000	0.000
142	A	168	LEU	0	-0.041	-0.018	39.888	0.000	0.000	0.000	0.000	0.000	0.000
143	A	169	ASN	0	0.054	0.032	42.247	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	170	ASN	0	-0.025	-0.013	43.825	0.002	0.002	0.000	0.000	0.000	0.000
145	A	171	GLN	0	0.042	0.041	46.261	0.001	0.001	0.000	0.000	0.000	0.000
146	A	172	LEU	0	-0.027	-0.013	47.675	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	173	VAL	0	0.023	0.008	44.029	0.001	0.001	0.000	0.000	0.000	0.000
148	A	174	ALA	0	0.034	0.009	47.386	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	175	ASN	0	-0.006	-0.012	49.264	0.000	0.000	0.000	0.000	0.000	0.000
150	A	176	ASN	0	-0.016	0.007	47.756	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	177	ARG	1	0.859	0.922	48.192	0.013	0.013	0.000	0.000	0.000	0.000
152	A	178	ILE	0	0.022	0.027	42.427	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	179	THR	0	-0.090	-0.056	41.825	0.001	0.001	0.000	0.000	0.000	0.000
154	A	180	VAL	0	-0.003	-0.010	38.021	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	181	ASP	-1	-0.783	-0.880	38.190	-0.026	-0.026	0.000	0.000	0.000	0.000
156	A	182	TYR	0	-0.012	-0.049	32.318	-0.003	-0.003	0.000	0.000	0.000	0.000
157	A	183	ALA	0	-0.036	-0.005	30.756	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	184	PHE	0	0.016	-0.007	31.829	0.000	0.000	0.000	0.000	0.000	0.000
159	A	185	LYS	1	0.710	0.844	26.391	0.052	0.052	0.000	0.000	0.000	0.000
160	A	186	DGL	-1	-0.804	-0.862	26.740	-0.080	-0.080	0.000	0.000	0.000	0.000
161	A	187	ASN	0	0.105	0.052	29.738	0.001	0.001	0.000	0.000	0.000	0.000
162	A	188	GLY	0	0.077	0.030	32.471	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	189	LYS	1	0.794	0.907	24.908	0.053	0.053	0.000	0.000	0.000	0.000
164	A	190	GLY	0	0.081	0.041	30.321	0.002	0.002	0.000	0.000	0.000	0.000
165	A	191	ASN	0	-0.041	-0.010	28.113	0.002	0.002	0.000	0.000	0.000	0.000
166	A	192	ALA	0	0.083	0.022	30.462	0.000	0.000	0.000	0.000	0.000	0.000
167	A	193	LYS	1	0.890	0.953	27.217	0.034	0.034	0.000	0.000	0.000	0.000
168	A	194	TYR	0	-0.023	0.000	24.375	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	195	GLY	0	0.069	0.040	27.355	0.002	0.002	0.000	0.000	0.000	0.000
170	A	196	ASP	-1	-0.780	-0.879	21.910	-0.013	-0.013	0.000	0.000	0.000	0.000
171	A	197	ASP	-1	-0.856	-0.936	23.013	-0.008	-0.008	0.000	0.000	0.000	0.000
172	A	198	VAL	0	0.066	0.027	25.197	0.004	0.004	0.000	0.000	0.000	0.000
173	A	199	ASP	-1	-0.843	-0.908	22.023	0.062	0.062	0.000	0.000	0.000	0.000
174	A	200	ARG	1	0.802	0.876	19.651	0.009	0.009	0.000	0.000	0.000	0.000
175	A	201	LEU	0	-0.025	0.007	21.627	0.001	0.001	0.000	0.000	0.000	0.000
176	A	202	LEU	0	-0.011	0.003	24.640	0.005	0.005	0.000	0.000	0.000	0.000
177	A	203	ASN	0	-0.048	-0.040	19.790	0.023	0.023	0.000	0.000	0.000	0.000
178	A	204	LYS	1	0.854	0.942	20.515	-0.074	-0.074	0.000	0.000	0.000	0.000
179	A	205	GLU	-1	-0.922	-0.944	17.185	0.026	0.026	0.000	0.000	0.000	0.000

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