FMO DATABASE

FMODB ID: KGLQ3

Calculation Name: 2GZQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2GZQ

Chain ID: A

ChEMBL ID:

UniProt ID: A5K000

Base Structure: X-ray

Registration Date: 2023-09-23

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	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	191
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2256846.309938
FMO2-HF: Nuclear repulsion	2179913.405695
FMO2-HF: Total energy	-76932.904243
FMO2-MP2: Total energy	-77155.222621

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:2:GLY)

Summations of interaction energy for fragment #1(A:2: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.
-12.047	-13.29	9.991	-4.019	-4.728	-0.045

Interaction energy analysis for fragmet #1(A:2:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.028 / q_NPA : -0.027

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	4	PRO	0	0.030	0.003	1.932	-4.588	-7.466	9.167	-3.163	-3.126	-0.044
4	A	5	PRO	0	-0.062	-0.031	4.650	-0.206	-0.158	-0.001	-0.020	-0.026	0.000
5	A	6	THR	0	0.077	0.056	5.796	-0.197	-0.197	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.060	0.012	7.933	0.300	0.300	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.938	-0.968	9.880	0.323	0.323	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.776	-0.873	5.427	1.804	1.804	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.015	-0.019	9.678	0.143	0.143	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.864	0.915	11.791	0.112	0.112	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.847	0.937	9.096	-0.881	-0.881	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.893	-0.940	11.662	0.734	0.734	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.885	0.931	14.577	-0.234	-0.234	0.000	0.000	0.000	0.000
14	A	15	ILE	0	0.013	0.013	12.274	-0.024	-0.024	0.000	0.000	0.000	0.000
15	A	16	ILE	0	0.024	0.068	14.275	-0.042	-0.042	0.000	0.000	0.000	0.000
16	A	17	PRO	0	-0.027	-0.039	17.064	0.031	0.031	0.000	0.000	0.000	0.000
17	A	18	HIS	0	-0.064	-0.043	19.297	0.016	0.016	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.018	-0.003	15.997	0.006	0.006	0.000	0.000	0.000	0.000
19	A	20	PHE	0	0.027	0.011	12.678	-0.026	-0.026	0.000	0.000	0.000	0.000
20	A	21	PRO	0	0.009	-0.007	18.293	0.014	0.014	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.881	-0.942	19.959	-0.119	-0.119	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.888	-0.935	16.707	-0.128	-0.128	0.000	0.000	0.000	0.000
23	A	24	ASN	0	-0.033	-0.006	16.599	-0.068	-0.068	0.000	0.000	0.000	0.000
24	A	25	VAL	0	-0.042	-0.014	13.545	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.813	-0.902	14.338	-0.656	-0.656	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.079	-0.041	9.027	0.020	0.020	0.000	0.000	0.000	0.000
27	A	28	THR	0	0.042	0.012	9.643	-0.246	-0.246	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.018	0.012	9.565	-0.202	-0.202	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.898	-0.965	3.727	-5.042	-4.612	0.005	-0.247	-0.188	-0.002
30	A	31	MET	0	-0.033	-0.017	5.874	0.522	0.522	0.000	0.000	0.000	0.000
31	A	32	TYR	0	-0.038	0.000	7.221	0.354	0.354	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.022	-0.004	8.146	-0.122	-0.122	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.035	0.024	11.031	0.190	0.190	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.018	-0.028	13.320	-0.094	-0.094	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.875	0.942	16.266	-0.361	-0.361	0.000	0.000	0.000	0.000
36	A	37	SER	0	0.020	0.017	16.151	0.072	0.072	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.079	0.041	14.829	-0.020	-0.020	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.780	0.894	14.789	-0.438	-0.438	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.825	-0.918	9.311	0.879	0.879	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.072	-0.028	9.489	0.080	0.080	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.011	-0.023	4.739	1.612	1.744	-0.001	-0.007	-0.124	0.000
42	A	43	HIS	1	0.874	0.928	2.378	-2.954	-1.929	0.821	-0.582	-1.264	0.001
43	A	44	GLY	0	-0.002	0.008	7.120	-0.222	-0.222	0.000	0.000	0.000	0.000
44	A	45	ASN	0	0.037	0.032	9.986	-0.146	-0.146	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.015	-0.015	11.630	-0.187	-0.187	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.004	0.004	13.499	-0.024	-0.024	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.922	-0.962	16.449	0.392	0.392	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.035	0.003	19.813	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.015	0.032	22.053	-0.024	-0.024	0.000	0.000	0.000	0.000
50	A	51	GLY	0	-0.002	-0.018	21.487	0.034	0.034	0.000	0.000	0.000	0.000
51	A	52	THR	0	0.002	-0.024	18.841	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.010	0.015	21.142	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.031	-0.013	22.811	-0.021	-0.021	0.000	0.000	0.000	0.000
54	A	55	VAL	0	0.032	0.028	19.754	0.031	0.031	0.000	0.000	0.000	0.000
55	A	56	PRO	0	-0.012	-0.004	15.579	0.003	0.003	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.947	0.986	17.748	-0.176	-0.176	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.009	-0.013	14.793	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	59	ILE	0	0.017	0.013	11.975	0.091	0.091	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.920	0.966	10.575	0.078	0.078	0.000	0.000	0.000	0.000
60	A	61	PHE	0	0.029	0.013	9.971	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.012	0.004	8.245	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.976	-0.987	10.273	-0.806	-0.806	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.959	-0.971	13.709	-0.289	-0.289	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.059	-0.001	16.898	-0.035	-0.035	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.040	0.007	18.147	0.017	0.017	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.899	-0.950	21.022	-0.185	-0.185	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.903	-0.950	24.497	-0.170	-0.170	0.000	0.000	0.000	0.000
68	A	69	TYR	0	-0.049	-0.015	21.577	0.018	0.018	0.000	0.000	0.000	0.000
69	A	70	CYS	0	-0.077	-0.019	20.879	0.003	0.003	0.000	0.000	0.000	0.000
70	A	71	TYR	0	0.002	-0.031	14.295	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.011	-0.006	18.442	0.036	0.036	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.032	-0.012	13.977	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.025	0.012	16.905	0.026	0.026	0.000	0.000	0.000	0.000
74	A	75	MET	0	-0.055	-0.017	16.424	0.016	0.016	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.020	-0.001	17.379	-0.017	-0.017	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.775	-0.875	18.123	0.321	0.321	0.000	0.000	0.000	0.000
77	A	78	PRO	0	0.044	0.044	17.949	-0.033	-0.033	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.799	-0.877	19.797	0.286	0.286	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.013	0.031	22.797	0.006	0.006	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.036	0.016	25.548	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.066	-0.057	26.326	0.017	0.017	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.957	0.981	18.552	-0.369	-0.369	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.912	0.945	24.721	-0.200	-0.200	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.989	0.998	27.763	-0.142	-0.142	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.014	0.030	25.245	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.871	-0.945	27.202	0.094	0.094	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.076	-0.054	28.561	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.838	0.943	22.879	-0.146	-0.146	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.794	-0.912	21.627	0.086	0.086	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.045	-0.036	23.510	-0.015	-0.015	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.022	0.015	22.069	0.021	0.021	0.000	0.000	0.000	0.000
92	A	93	HIS	0	-0.049	-0.032	20.582	0.010	0.010	0.000	0.000	0.000	0.000
93	A	94	TRP	0	-0.030	-0.025	16.596	0.010	0.010	0.000	0.000	0.000	0.000
94	A	95	ALA	0	0.048	0.030	20.797	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.039	-0.002	19.641	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.036	0.001	20.693	-0.024	-0.024	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.094	0.020	22.179	0.014	0.014	0.000	0.000	0.000	0.000
98	A	99	ILE	0	-0.050	-0.009	17.158	0.001	0.001	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.963	0.973	20.129	0.192	0.192	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.049	0.047	19.190	-0.036	-0.036	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.995	0.992	13.567	0.577	0.577	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.951	-0.977	14.285	-0.118	-0.118	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.014	0.004	16.072	0.013	0.013	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.022	-0.002	17.257	0.039	0.039	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.899	0.925	19.776	-0.083	-0.083	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.008	0.000	19.827	0.000	0.000	0.000	0.000	0.000	0.000
107	A	108	THR	0	0.029	0.007	20.820	-0.010	-0.010	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.826	-0.908	22.413	-0.099	-0.099	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.953	0.967	24.841	0.098	0.098	0.000	0.000	0.000	0.000
110	A	111	ASN	0	-0.012	0.003	24.046	0.009	0.009	0.000	0.000	0.000	0.000
111	A	112	CYS	0	-0.084	-0.022	22.488	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	113	ILE	0	0.052	0.031	24.988	0.012	0.012	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.026	-0.025	25.123	0.002	0.002	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.005	0.006	24.833	0.005	0.005	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.027	0.008	25.003	0.007	0.007	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.032	0.025	24.705	0.006	0.006	0.000	0.000	0.000	0.000
117	A	118	TYR	0	0.002	-0.024	19.176	0.020	0.020	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.008	0.012	23.855	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	120	GLY	0	0.020	0.009	22.398	0.013	0.013	0.000	0.000	0.000	0.000
120	A	121	PRO	0	-0.012	-0.017	20.008	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	122	SER	0	0.024	0.028	22.759	-0.008	-0.008	0.000	0.000	0.000	0.000
122	A	123	ILE	0	0.027	0.018	21.331	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.979	1.004	25.984	-0.168	-0.168	0.000	0.000	0.000	0.000
124	A	125	LYS	1	1.011	0.995	28.072	-0.177	-0.177	0.000	0.000	0.000	0.000
125	A	126	GLY	0	-0.056	-0.026	28.695	-0.014	-0.014	0.000	0.000	0.000	0.000
126	A	127	THR	0	0.004	0.010	26.714	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	GLY	0	0.017	0.011	24.734	0.001	0.001	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.020	-0.009	18.672	-0.013	-0.013	0.000	0.000	0.000	0.000
129	A	130	HIS	1	0.771	0.850	19.945	-0.297	-0.297	0.000	0.000	0.000	0.000
130	A	131	ARG	1	0.789	0.863	15.415	-0.265	-0.265	0.000	0.000	0.000	0.000
131	A	132	ILE	0	-0.031	0.000	15.886	-0.059	-0.059	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.012	-0.012	13.297	0.126	0.126	0.000	0.000	0.000	0.000
133	A	134	PHE	0	-0.026	-0.017	11.567	-0.042	-0.042	0.000	0.000	0.000	0.000
134	A	135	ILE	0	0.026	0.009	11.991	-0.017	-0.017	0.000	0.000	0.000	0.000
135	A	136	LEU	0	0.019	0.016	11.716	0.037	0.037	0.000	0.000	0.000	0.000
136	A	137	SER	0	0.022	0.006	14.195	-0.059	-0.059	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.006	0.009	16.999	0.007	0.007	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.011	-0.004	19.391	0.019	0.019	0.000	0.000	0.000	0.000
139	A	140	LYS	1	1.025	1.012	22.993	0.131	0.131	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.819	-0.928	25.920	-0.118	-0.118	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.973	-0.989	26.992	-0.102	-0.102	0.000	0.000	0.000	0.000
142	A	143	ASN	0	0.000	-0.008	27.734	0.016	0.016	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.828	0.932	25.512	0.106	0.106	0.000	0.000	0.000	0.000
144	A	145	GLY	0	-0.006	-0.012	26.806	0.009	0.009	0.000	0.000	0.000	0.000
145	A	146	ASN	0	-0.075	-0.034	29.293	0.015	0.015	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.044	0.038	25.719	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	148	THR	0	0.056	0.021	28.664	0.014	0.014	0.000	0.000	0.000	0.000
148	A	149	GLY	0	0.033	0.000	29.011	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.063	-0.039	25.753	0.013	0.013	0.000	0.000	0.000	0.000
150	A	151	PRO	0	-0.001	0.009	29.075	-0.006	-0.006	0.000	0.000	0.000	0.000
151	A	152	LEU	0	0.055	0.026	30.665	0.005	0.005	0.000	0.000	0.000	0.000
152	A	153	TYR	0	-0.056	-0.052	30.133	0.005	0.005	0.000	0.000	0.000	0.000
153	A	154	ARG	1	0.952	0.972	32.151	-0.007	-0.007	0.000	0.000	0.000	0.000
154	A	155	GLY	0	0.033	0.011	33.793	0.001	0.001	0.000	0.000	0.000	0.000
155	A	156	GLU	-1	-0.767	-0.866	30.725	0.063	0.063	0.000	0.000	0.000	0.000
156	A	157	HIS	0	-0.034	0.000	34.091	0.002	0.002	0.000	0.000	0.000	0.000
157	A	158	TYR	0	-0.054	-0.029	35.906	-0.003	-0.003	0.000	0.000	0.000	0.000
158	A	159	ILE	0	-0.024	0.012	30.248	-0.005	-0.005	0.000	0.000	0.000	0.000
159	A	160	THR	0	0.016	0.010	31.435	0.009	0.009	0.000	0.000	0.000	0.000
160	A	161	ARG	1	0.784	0.859	25.355	-0.088	-0.088	0.000	0.000	0.000	0.000
161	A	162	VAL	0	-0.023	-0.008	27.022	0.011	0.011	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.961	0.991	27.629	-0.071	-0.071	0.000	0.000	0.000	0.000
163	A	164	PHE	0	0.022	-0.001	21.537	-0.010	-0.010	0.000	0.000	0.000	0.000
164	A	165	ASN	0	0.031	0.008	26.659	-0.006	-0.006	0.000	0.000	0.000	0.000
165	A	166	ASN	0	-0.033	-0.009	29.905	-0.003	-0.003	0.000	0.000	0.000	0.000
166	A	167	CYS	0	-0.018	0.019	28.000	-0.010	-0.010	0.000	0.000	0.000	0.000
167	A	168	GLN	0	-0.026	-0.009	28.059	0.000	0.000	0.000	0.000	0.000	0.000
168	A	169	SER	0	0.032	0.001	22.879	0.010	0.010	0.000	0.000	0.000	0.000
169	A	170	ALA	0	0.036	0.010	19.804	-0.013	-0.013	0.000	0.000	0.000	0.000
170	A	171	TYR	0	0.031	0.013	19.252	-0.009	-0.009	0.000	0.000	0.000	0.000
171	A	172	ASN	0	-0.021	-0.016	21.351	-0.026	-0.026	0.000	0.000	0.000	0.000
172	A	173	VAL	0	0.021	0.005	23.923	-0.009	-0.009	0.000	0.000	0.000	0.000
173	A	174	ILE	0	0.016	0.003	18.461	-0.007	-0.007	0.000	0.000	0.000	0.000
174	A	175	GLN	0	-0.014	0.002	22.687	-0.020	-0.020	0.000	0.000	0.000	0.000
175	A	176	MET	0	-0.048	-0.016	24.538	0.000	0.000	0.000	0.000	0.000	0.000
176	A	177	ASN	0	-0.096	-0.066	25.564	0.007	0.007	0.000	0.000	0.000	0.000
177	A	178	ASP	-1	-0.891	-0.920	25.769	-0.121	-0.121	0.000	0.000	0.000	0.000
178	A	179	MET	0	-0.098	-0.035	21.219	-0.013	-0.013	0.000	0.000	0.000	0.000
179	A	180	LYS	1	0.876	0.935	16.856	0.421	0.421	0.000	0.000	0.000	0.000
180	A	181	ILE	0	-0.033	-0.021	13.936	-0.013	-0.013	0.000	0.000	0.000	0.000
181	A	182	VAL	0	0.018	-0.006	13.186	-0.022	-0.022	0.000	0.000	0.000	0.000
182	A	183	GLY	0	0.069	0.044	9.633	-0.212	-0.212	0.000	0.000	0.000	0.000
183	A	184	PHE	0	0.002	-0.016	8.493	0.217	0.217	0.000	0.000	0.000	0.000
184	A	185	ASN	0	0.030	0.020	6.015	0.397	0.397	0.000	0.000	0.000	0.000
185	A	186	TRP	0	0.027	0.015	7.607	-0.158	-0.158	0.000	0.000	0.000	0.000
186	A	187	CYS	0	-0.021	0.019	9.869	0.305	0.305	0.000	0.000	0.000	0.000
187	A	188	GLN	0	-0.021	-0.034	12.552	-0.295	-0.295	0.000	0.000	0.000	0.000
188	A	189	MET	0	0.009	0.024	15.830	-0.007	-0.007	0.000	0.000	0.000	0.000
189	A	190	ARG	1	1.002	0.990	18.936	-0.386	-0.386	0.000	0.000	0.000	0.000
190	A	191	ARG	1	0.898	0.930	22.502	-0.215	-0.215	0.000	0.000	0.000	0.000
191	A	192	LYS	1	0.984	0.994	23.144	-0.389	-0.389	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:GLY)