FMO DATABASE

FMODB ID: 4L91N

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	OptH
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	-1877863.136129
FMO2-HF: Nuclear repulsion	1806331.642518
FMO2-HF: Total energy	-71531.493611
FMO2-MP2: Total energy	-71745.150478

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.
-3.076	1.289	0.453	-2.232	-2.587	-0.003

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 : -0.015 / 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	-0.001	0.025	2.734	-3.161	0.400	0.037	-1.788	-1.810	-0.002
4	A	11	VAL	0	-0.012	0.000	3.908	-1.522	-1.376	0.000	-0.102	-0.045	0.000
5	A	12	TYR	0	-0.022	-0.012	6.663	0.314	0.314	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.004	0.001	9.338	-0.049	-0.049	0.000	0.000	0.000	0.000
7	A	14	GLY	0	0.022	-0.001	12.781	0.050	0.050	0.000	0.000	0.000	0.000
8	A	15	ASN	0	-0.054	-0.048	15.765	0.008	0.008	0.000	0.000	0.000	0.000
9	A	16	ILE	0	-0.014	0.003	15.925	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	17	ASP	-1	-0.762	-0.856	20.286	-0.042	-0.042	0.000	0.000	0.000	0.000
11	A	18	PRO	0	0.066	0.021	23.376	0.002	0.002	0.000	0.000	0.000	0.000
12	A	19	ARG	1	0.808	0.869	24.545	0.051	0.051	0.000	0.000	0.000	0.000
13	A	20	ILE	0	-0.038	0.011	20.766	0.003	0.003	0.000	0.000	0.000	0.000
14	A	21	THR	0	0.075	0.046	22.789	0.005	0.005	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.958	0.961	16.880	-0.103	-0.103	0.000	0.000	0.000	0.000
16	A	23	GLU	-1	-0.936	-0.957	19.703	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	24	GLN	0	0.089	0.036	21.630	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	25	LEU	0	-0.028	-0.005	16.291	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	26	TYR	0	-0.011	-0.012	16.819	-0.026	-0.026	0.000	0.000	0.000	0.000
20	A	27	GLU	-1	-0.914	-0.961	18.291	-0.061	-0.061	0.000	0.000	0.000	0.000
21	A	28	LEU	0	-0.026	-0.006	18.032	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	29	PHE	0	0.004	-0.036	13.373	-0.023	-0.023	0.000	0.000	0.000	0.000
23	A	30	ILE	0	-0.018	-0.003	15.727	-0.028	-0.028	0.000	0.000	0.000	0.000
24	A	31	GLN	0	-0.062	-0.017	17.776	0.001	0.001	0.000	0.000	0.000	0.000
25	A	32	ILE	0	-0.102	-0.031	14.014	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	33	ASN	0	0.030	0.003	11.818	0.013	0.013	0.000	0.000	0.000	0.000
27	A	34	PRO	0	0.028	0.042	13.815	0.023	0.023	0.000	0.000	0.000	0.000
28	A	35	VAL	0	0.000	-0.017	12.381	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.055	-0.002	10.020	0.017	0.017	0.000	0.000	0.000	0.000
30	A	37	ARG	1	0.938	0.961	11.320	-0.454	-0.454	0.000	0.000	0.000	0.000
31	A	38	ILE	0	0.035	0.023	11.684	-0.015	-0.015	0.000	0.000	0.000	0.000
32	A	39	LYS	1	0.915	0.963	12.020	-0.141	-0.141	0.000	0.000	0.000	0.000
33	A	40	TYR	0	-0.012	-0.044	13.589	-0.036	-0.036	0.000	0.000	0.000	0.000
34	A	41	PRO	0	-0.057	-0.027	15.085	0.014	0.014	0.000	0.000	0.000	0.000
35	A	42	LYS	1	0.922	0.971	18.171	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	43	ASP	-1	-0.736	-0.871	21.966	0.018	0.018	0.000	0.000	0.000	0.000
37	A	44	LYS	1	0.890	0.922	22.842	-0.054	-0.054	0.000	0.000	0.000	0.000
38	A	45	VAL	0	0.002	0.015	26.654	0.000	0.000	0.000	0.000	0.000	0.000
39	A	46	LEU	0	0.015	0.008	27.265	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	47	GLN	0	-0.072	-0.028	27.388	0.000	0.000	0.000	0.000	0.000	0.000
41	A	48	ALA	0	0.024	0.028	26.240	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	49	TYR	0	-0.070	-0.048	20.453	0.007	0.007	0.000	0.000	0.000	0.000
43	A	50	GLN	0	0.019	0.005	19.412	0.008	0.008	0.000	0.000	0.000	0.000
44	A	51	GLY	0	0.104	0.075	19.997	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	52	TYR	0	-0.099	-0.048	13.395	-0.016	-0.016	0.000	0.000	0.000	0.000
46	A	53	ALA	0	-0.009	-0.016	13.767	0.037	0.037	0.000	0.000	0.000	0.000
47	A	54	PHE	0	-0.017	-0.003	8.155	-0.039	-0.039	0.000	0.000	0.000	0.000
48	A	55	ILE	0	0.010	0.004	9.194	0.114	0.114	0.000	0.000	0.000	0.000
49	A	56	GLU	-1	-0.883	-0.940	6.878	1.016	1.016	0.000	0.000	0.000	0.000
50	A	57	PHE	0	0.043	0.003	7.353	-0.053	-0.053	0.000	0.000	0.000	0.000
51	A	58	TYR	0	0.067	0.014	8.072	0.284	0.284	0.000	0.000	0.000	0.000
52	A	59	ASN	0	-0.012	-0.001	6.371	0.058	0.058	0.000	0.000	0.000	0.000
53	A	60	GLN	0	0.007	-0.005	2.773	-0.953	-0.654	0.421	-0.302	-0.419	-0.001
54	A	61	GLY	0	0.039	0.021	4.750	-0.140	-0.092	-0.001	-0.006	-0.040	0.000
55	A	62	ASP	-1	-0.831	-0.924	8.440	-0.364	-0.364	0.000	0.000	0.000	0.000
56	A	63	ALA	0	-0.008	0.003	5.212	0.059	0.093	-0.001	-0.010	-0.023	0.000
57	A	64	GLN	0	-0.047	-0.035	4.067	0.392	0.505	-0.001	-0.010	-0.102	0.000
58	A	65	TYR	0	-0.036	-0.011	7.853	0.181	0.181	0.000	0.000	0.000	0.000
59	A	66	ALA	0	0.052	0.014	10.071	0.093	0.093	0.000	0.000	0.000	0.000
60	A	67	ILE	0	-0.065	-0.030	6.745	0.093	0.093	0.000	0.000	0.000	0.000
61	A	68	LYS	1	0.910	0.950	10.992	0.560	0.560	0.000	0.000	0.000	0.000
62	A	69	ILE	0	0.012	0.029	13.558	0.050	0.050	0.000	0.000	0.000	0.000
63	A	70	MET	0	0.038	0.026	14.191	0.055	0.055	0.000	0.000	0.000	0.000
64	A	71	ASN	0	-0.042	-0.002	14.043	0.037	0.037	0.000	0.000	0.000	0.000
65	A	72	ASN	0	-0.057	-0.045	15.991	0.028	0.028	0.000	0.000	0.000	0.000
66	A	73	THR	0	0.047	0.021	18.890	0.016	0.016	0.000	0.000	0.000	0.000
67	A	74	VAL	0	0.037	0.020	19.900	0.018	0.018	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.820	0.893	21.490	0.095	0.095	0.000	0.000	0.000	0.000
69	A	76	LEU	0	0.037	0.021	20.185	0.007	0.007	0.000	0.000	0.000	0.000
70	A	77	TYR	0	0.002	-0.019	24.318	0.002	0.002	0.000	0.000	0.000	0.000
71	A	78	ASP	-1	-0.875	-0.940	27.591	-0.072	-0.072	0.000	0.000	0.000	0.000
72	A	79	ARG	1	0.859	0.951	23.564	0.079	0.079	0.000	0.000	0.000	0.000
73	A	80	LEU	0	-0.033	-0.001	21.040	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	81	ILE	0	0.035	0.030	16.565	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.819	0.916	15.339	0.178	0.178	0.000	0.000	0.000	0.000
76	A	83	VAL	0	0.042	0.016	10.423	0.012	0.012	0.000	0.000	0.000	0.000
77	A	84	ARG	1	0.943	0.967	10.000	0.345	0.345	0.000	0.000	0.000	0.000
78	A	85	GLN	0	0.073	0.045	4.797	-0.275	-0.212	-0.001	-0.004	-0.058	0.000
79	A	86	VAL	0	0.006	0.010	4.257	0.285	0.386	-0.001	-0.010	-0.090	0.000
80	A	106	PRO	0	-0.040	-0.023	19.899	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	107	ILE	0	-0.013	-0.005	22.911	0.003	0.003	0.000	0.000	0.000	0.000
82	A	108	ALA	0	0.073	0.050	25.464	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	109	LYS	1	0.836	0.936	27.749	0.087	0.087	0.000	0.000	0.000	0.000
84	A	110	LEU	0	0.030	0.016	30.141	0.001	0.001	0.000	0.000	0.000	0.000
85	A	111	PHE	0	-0.023	-0.024	33.772	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	112	ILE	0	0.006	0.009	35.954	0.003	0.003	0.000	0.000	0.000	0.000
87	A	113	LYS	1	0.952	0.973	38.860	0.038	0.038	0.000	0.000	0.000	0.000
88	A	114	ASN	0	-0.041	-0.055	41.779	0.002	0.002	0.000	0.000	0.000	0.000
89	A	115	LEU	0	-0.013	-0.008	39.292	0.002	0.002	0.000	0.000	0.000	0.000
90	A	116	ALA	0	0.042	0.025	43.931	0.000	0.000	0.000	0.000	0.000	0.000
91	A	117	ASP	-1	-0.857	-0.946	44.853	-0.034	-0.034	0.000	0.000	0.000	0.000
92	A	118	SER	0	-0.059	-0.043	45.021	0.000	0.000	0.000	0.000	0.000	0.000
93	A	119	ILE	0	-0.081	-0.022	40.966	0.000	0.000	0.000	0.000	0.000	0.000
94	A	120	ASP	-1	-0.868	-0.938	39.973	-0.040	-0.040	0.000	0.000	0.000	0.000
95	A	121	SER	0	0.012	-0.002	34.170	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	122	ASP	-1	-0.802	-0.912	36.363	-0.040	-0.040	0.000	0.000	0.000	0.000
97	A	123	GLN	0	-0.036	-0.037	37.869	0.002	0.002	0.000	0.000	0.000	0.000
98	A	124	LEU	0	0.014	0.019	36.392	0.001	0.001	0.000	0.000	0.000	0.000
99	A	125	VAL	0	0.036	0.026	33.399	0.001	0.001	0.000	0.000	0.000	0.000
100	A	126	LYS	1	0.929	0.958	36.001	0.029	0.029	0.000	0.000	0.000	0.000
101	A	127	ILE	0	-0.072	-0.030	39.201	0.002	0.002	0.000	0.000	0.000	0.000
102	A	128	PHE	0	0.044	-0.006	35.651	0.001	0.001	0.000	0.000	0.000	0.000
103	A	129	ASN	0	0.026	0.010	34.469	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	130	LYS	1	0.867	0.950	36.285	0.026	0.026	0.000	0.000	0.000	0.000
105	A	131	PHE	0	-0.008	0.002	37.335	0.002	0.002	0.000	0.000	0.000	0.000
106	A	132	GLY	0	0.017	0.002	33.994	0.001	0.001	0.000	0.000	0.000	0.000
107	A	133	LYS	1	0.957	0.997	28.432	0.039	0.039	0.000	0.000	0.000	0.000
108	A	134	LEU	0	0.011	0.005	29.686	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	135	ILE	0	-0.016	-0.003	22.522	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	136	ARG	1	0.870	0.926	18.969	0.112	0.112	0.000	0.000	0.000	0.000
111	A	137	GLU	-1	-0.868	-0.922	26.496	-0.074	-0.074	0.000	0.000	0.000	0.000
112	A	138	PRO	0	-0.052	-0.036	29.319	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	139	GLU	-1	-0.926	-0.950	29.599	-0.087	-0.087	0.000	0.000	0.000	0.000
114	A	140	ILE	0	0.000	-0.004	32.006	0.002	0.002	0.000	0.000	0.000	0.000
115	A	141	PHE	0	-0.012	-0.012	34.141	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	142	TYR	0	0.038	0.017	36.782	0.003	0.003	0.000	0.000	0.000	0.000
117	A	143	LEU	0	0.005	0.009	37.890	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	144	SER	0	-0.003	-0.012	41.410	0.002	0.002	0.000	0.000	0.000	0.000
119	A	145	ASN	0	-0.019	-0.019	43.920	0.004	0.004	0.000	0.000	0.000	0.000
120	A	146	GLY	0	0.069	0.028	43.135	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	147	LYS	1	0.919	0.971	44.218	0.035	0.035	0.000	0.000	0.000	0.000
122	A	148	LEU	0	0.031	0.027	43.325	0.001	0.001	0.000	0.000	0.000	0.000
123	A	149	LYS	1	0.933	0.992	40.880	0.037	0.037	0.000	0.000	0.000	0.000
124	A	150	CYS	0	-0.067	-0.023	38.396	0.002	0.002	0.000	0.000	0.000	0.000
125	A	151	ALA	0	0.046	0.013	35.627	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	152	TYR	0	-0.031	-0.011	30.844	0.001	0.001	0.000	0.000	0.000	0.000
127	A	153	VAL	0	0.030	0.013	32.028	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	154	TYR	0	-0.032	-0.020	26.636	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	155	PHE	0	0.037	0.005	29.212	0.001	0.001	0.000	0.000	0.000	0.000
130	A	156	GLU	-1	-0.963	-1.004	25.666	-0.055	-0.055	0.000	0.000	0.000	0.000
131	A	157	ASP	-1	-0.818	-0.908	27.042	-0.033	-0.033	0.000	0.000	0.000	0.000
132	A	158	PHE	0	-0.001	-0.026	27.495	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	159	GLU	-1	-0.871	-0.910	31.847	-0.023	-0.023	0.000	0.000	0.000	0.000
134	A	160	LYS	1	0.827	0.913	33.090	0.026	0.026	0.000	0.000	0.000	0.000
135	A	161	ALA	0	-0.004	-0.004	32.764	0.000	0.000	0.000	0.000	0.000	0.000
136	A	162	ASP	-1	-0.814	-0.891	34.754	-0.034	-0.034	0.000	0.000	0.000	0.000
137	A	163	LEU	0	-0.072	-0.030	37.641	0.002	0.002	0.000	0.000	0.000	0.000
138	A	164	ALA	0	0.008	-0.001	37.389	0.001	0.001	0.000	0.000	0.000	0.000
139	A	165	ILE	0	0.010	0.012	36.761	0.000	0.000	0.000	0.000	0.000	0.000
140	A	166	LYS	1	0.921	0.965	40.431	0.021	0.021	0.000	0.000	0.000	0.000
141	A	167	SER	0	-0.045	-0.028	42.844	0.002	0.002	0.000	0.000	0.000	0.000
142	A	168	LEU	0	-0.031	-0.013	40.522	0.001	0.001	0.000	0.000	0.000	0.000
143	A	169	ASN	0	0.032	0.023	42.968	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	170	ASN	0	-0.029	-0.020	44.405	0.001	0.001	0.000	0.000	0.000	0.000
145	A	171	GLN	0	-0.003	0.007	46.783	0.002	0.002	0.000	0.000	0.000	0.000
146	A	172	LEU	0	-0.037	-0.009	48.011	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	173	VAL	0	0.026	0.008	44.643	0.001	0.001	0.000	0.000	0.000	0.000
148	A	174	ALA	0	0.035	0.008	47.757	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	175	ASN	0	-0.018	-0.031	49.479	0.000	0.000	0.000	0.000	0.000	0.000
150	A	176	ASN	0	-0.005	0.027	48.186	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	177	ARG	1	0.908	0.958	48.854	0.023	0.023	0.000	0.000	0.000	0.000
152	A	178	ILE	0	0.026	0.037	42.528	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	179	THR	0	-0.007	-0.007	42.259	0.001	0.001	0.000	0.000	0.000	0.000
154	A	180	VAL	0	-0.036	-0.027	38.463	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	181	ASP	-1	-0.853	-0.920	38.531	-0.040	-0.040	0.000	0.000	0.000	0.000
156	A	182	TYR	0	-0.025	-0.030	32.690	-0.005	-0.005	0.000	0.000	0.000	0.000
157	A	183	ALA	0	-0.017	-0.005	31.476	0.000	0.000	0.000	0.000	0.000	0.000
158	A	184	PHE	0	0.081	0.048	32.757	0.000	0.000	0.000	0.000	0.000	0.000
159	A	185	LYS	1	0.908	1.058	26.749	0.071	0.071	0.000	0.000	0.000	0.000
160	A	186	DGL	0	-1.250	-0.450	27.512	-0.011	-0.011	0.000	0.000	0.000	0.000
161	A	187	ASN	-1	-0.123	-0.765	32.924	-0.069	-0.069	0.000	0.000	0.000	0.000
162	A	188	GLY	0	0.481	0.178	32.601	-0.003	-0.003	0.000	0.000	0.000	0.000
163	A	189	LYS	1	0.863	0.905	25.916	0.090	0.090	0.000	0.000	0.000	0.000
164	A	190	GLY	0	0.133	0.064	30.567	0.003	0.003	0.000	0.000	0.000	0.000
165	A	191	ASN	0	-0.097	-0.041	28.949	0.004	0.004	0.000	0.000	0.000	0.000
166	A	192	ALA	0	0.104	0.041	31.253	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	193	LYS	1	0.905	0.952	27.307	0.051	0.051	0.000	0.000	0.000	0.000
168	A	194	TYR	0	-0.066	-0.027	25.437	-0.007	-0.007	0.000	0.000	0.000	0.000
169	A	195	GLY	0	0.097	0.064	28.018	0.003	0.003	0.000	0.000	0.000	0.000
170	A	196	ASP	-1	-0.896	-0.960	22.774	-0.064	-0.064	0.000	0.000	0.000	0.000
171	A	197	ASP	-1	-0.926	-0.971	23.437	-0.055	-0.055	0.000	0.000	0.000	0.000
172	A	198	VAL	0	0.046	0.023	25.444	0.002	0.002	0.000	0.000	0.000	0.000
173	A	199	ASP	-1	-0.847	-0.926	22.506	-0.015	-0.015	0.000	0.000	0.000	0.000
174	A	200	ARG	1	0.882	0.932	20.363	0.073	0.073	0.000	0.000	0.000	0.000
175	A	201	LEU	0	-0.006	0.010	21.968	0.001	0.001	0.000	0.000	0.000	0.000
176	A	202	LEU	0	-0.029	-0.003	24.774	0.004	0.004	0.000	0.000	0.000	0.000
177	A	203	ASN	0	-0.113	-0.074	20.002	0.016	0.016	0.000	0.000	0.000	0.000
178	A	204	LYS	1	0.882	0.959	20.086	-0.001	-0.001	0.000	0.000	0.000	0.000
179	A	205	GLU	-1	-0.905	-0.948	16.460	-0.063	-0.063	0.000	0.000	0.000	0.000

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