FMO DATABASE

FMODB ID: 4JVGN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2258258.493775
FMO2-HF: Nuclear repulsion	2181324.801451
FMO2-HF: Total energy	-76933.692325
FMO2-MP2: Total energy	-77156.104818

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.
-11.721	-13.481	12.028	-4.755	-5.514	-0.046

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 : -0.033 / q_NPA : -0.029

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	0.035	0.008	1.926	-4.350	-7.341	9.472	-3.301	-3.181	-0.046
4	A	5	PRO	0	-0.052	-0.028	4.647	-0.245	-0.198	-0.001	-0.020	-0.026	0.000
5	A	6	THR	0	0.051	0.042	5.833	-0.225	-0.225	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.067	0.016	7.926	0.308	0.308	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.868	-0.944	9.931	0.405	0.405	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.783	-0.868	5.576	1.914	1.914	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.011	-0.015	9.677	0.142	0.142	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.829	0.903	11.786	0.100	0.100	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.815	0.919	8.892	-0.814	-0.814	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.876	-0.929	11.700	0.751	0.751	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.848	0.915	14.576	-0.272	-0.272	0.000	0.000	0.000	0.000
14	A	15	ILE	0	0.013	0.010	12.044	-0.027	-0.027	0.000	0.000	0.000	0.000
15	A	16	ILE	0	0.019	0.064	14.188	-0.043	-0.043	0.000	0.000	0.000	0.000
16	A	17	PRO	0	-0.024	-0.035	17.058	0.032	0.032	0.000	0.000	0.000	0.000
17	A	18	HIS	0	-0.061	-0.040	19.272	0.015	0.015	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.016	-0.005	16.149	0.006	0.006	0.000	0.000	0.000	0.000
19	A	20	PHE	0	0.025	0.008	12.635	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	21	PRO	0	0.012	-0.002	18.304	0.012	0.012	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.818	-0.906	20.027	-0.117	-0.117	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.837	-0.923	16.718	-0.122	-0.122	0.000	0.000	0.000	0.000
23	A	24	ASN	0	-0.068	-0.027	16.591	-0.067	-0.067	0.000	0.000	0.000	0.000
24	A	25	VAL	0	-0.025	-0.003	13.588	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.813	-0.891	14.294	-0.655	-0.655	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.076	-0.039	9.050	0.026	0.026	0.000	0.000	0.000	0.000
27	A	28	THR	0	0.055	0.019	9.635	-0.236	-0.236	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.035	0.004	9.560	-0.200	-0.200	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.886	-0.953	3.616	-5.051	-4.460	0.015	-0.350	-0.256	-0.002
30	A	31	MET	0	-0.039	-0.020	5.873	0.498	0.498	0.000	0.000	0.000	0.000
31	A	32	TYR	0	-0.050	-0.031	7.291	0.377	0.377	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.020	-0.004	8.148	-0.137	-0.137	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.039	0.024	11.043	0.196	0.196	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.008	-0.023	13.332	-0.102	-0.102	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.846	0.917	16.285	-0.388	-0.388	0.000	0.000	0.000	0.000
36	A	37	SER	0	0.040	0.030	16.166	0.072	0.072	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.069	0.038	14.849	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.760	0.881	14.818	-0.453	-0.453	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.802	-0.883	9.478	0.837	0.837	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.061	-0.022	9.600	0.076	0.076	0.000	0.000	0.000	0.000
41	A	42	ASN	0	0.000	-0.012	4.774	1.854	1.996	-0.001	-0.007	-0.134	0.000
42	A	43	HIS	1	0.871	0.928	2.030	-3.018	-2.567	2.543	-1.077	-1.917	0.002
43	A	44	GLY	0	-0.007	-0.001	7.143	-0.251	-0.251	0.000	0.000	0.000	0.000
44	A	45	ASN	0	0.029	0.008	9.964	-0.205	-0.205	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.009	-0.008	11.630	-0.187	-0.187	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.005	0.009	13.454	-0.032	-0.032	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.820	-0.899	16.449	0.361	0.361	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.047	0.026	19.813	0.000	0.000	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.019	0.028	22.053	-0.024	-0.024	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.030	0.001	21.506	0.036	0.036	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.014	-0.026	18.600	0.004	0.004	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.014	0.019	21.165	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.033	-0.012	22.865	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	55	VAL	0	0.032	0.029	19.776	0.032	0.032	0.000	0.000	0.000	0.000
55	A	56	PRO	0	-0.022	-0.009	15.600	0.003	0.003	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.946	0.985	17.767	-0.183	-0.183	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.013	-0.013	14.696	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	59	ILE	0	0.005	0.013	11.949	0.097	0.097	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.822	0.898	10.655	0.056	0.056	0.000	0.000	0.000	0.000
60	A	61	PHE	0	0.034	0.015	9.978	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.028	0.016	8.219	0.015	0.015	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.965	-0.983	10.266	-0.888	-0.888	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.921	-0.954	13.701	-0.277	-0.277	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.060	-0.002	16.892	-0.037	-0.037	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.039	0.006	18.157	0.015	0.015	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.914	-0.958	21.016	-0.187	-0.187	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.894	-0.947	24.491	-0.165	-0.165	0.000	0.000	0.000	0.000
68	A	69	TYR	0	-0.059	-0.020	21.651	0.017	0.017	0.000	0.000	0.000	0.000
69	A	70	CYS	0	-0.064	-0.005	20.902	0.002	0.002	0.000	0.000	0.000	0.000
70	A	71	TYR	0	0.005	-0.035	14.350	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.015	-0.007	18.461	0.036	0.036	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.031	-0.011	14.007	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.021	0.009	16.921	0.024	0.024	0.000	0.000	0.000	0.000
74	A	75	MET	0	-0.049	-0.010	16.441	0.018	0.018	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.018	-0.003	17.401	-0.020	-0.020	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.773	-0.881	18.145	0.337	0.337	0.000	0.000	0.000	0.000
77	A	78	PRO	0	0.041	0.044	17.987	-0.033	-0.033	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.799	-0.874	19.821	0.296	0.296	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.018	0.034	22.819	0.005	0.005	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.025	0.012	25.571	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.063	-0.057	26.359	0.017	0.017	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.942	0.971	18.192	-0.393	-0.393	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.919	0.949	24.742	-0.206	-0.206	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.991	1.001	27.762	-0.143	-0.143	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.012	0.033	25.270	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.867	-0.950	27.223	0.104	0.104	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.059	-0.051	28.598	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.823	0.930	22.567	-0.162	-0.162	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.796	-0.907	21.672	0.097	0.097	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.037	-0.035	23.546	-0.016	-0.016	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.017	0.013	22.136	0.023	0.023	0.000	0.000	0.000	0.000
92	A	93	HIS	0	-0.064	-0.046	20.619	0.008	0.008	0.000	0.000	0.000	0.000
93	A	94	TRP	0	-0.026	-0.024	16.503	0.010	0.010	0.000	0.000	0.000	0.000
94	A	95	ALA	0	0.037	0.024	20.815	0.002	0.002	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.034	-0.003	19.645	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.040	0.006	20.704	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.084	0.016	22.183	0.014	0.014	0.000	0.000	0.000	0.000
98	A	99	ILE	0	-0.058	-0.016	17.174	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.955	0.965	20.132	0.198	0.198	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.037	0.038	19.191	-0.035	-0.035	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.938	0.963	12.910	0.656	0.656	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.851	-0.907	14.287	-0.112	-0.112	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.007	0.008	16.076	0.011	0.011	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.025	-0.001	17.267	0.040	0.040	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.903	0.928	19.781	-0.087	-0.087	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.008	-0.001	19.841	0.000	0.000	0.000	0.000	0.000	0.000
107	A	108	THR	0	0.016	0.002	20.835	-0.013	-0.013	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.768	-0.879	22.868	-0.096	-0.096	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.956	0.978	24.850	0.098	0.098	0.000	0.000	0.000	0.000
110	A	111	ASN	0	-0.058	-0.032	23.842	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	CYS	0	-0.076	-0.020	22.524	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	113	ILE	0	0.052	0.028	24.997	0.012	0.012	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.036	-0.030	25.153	0.004	0.004	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.002	0.009	24.961	0.005	0.005	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.026	0.008	25.003	0.007	0.007	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.034	0.024	24.723	0.008	0.008	0.000	0.000	0.000	0.000
117	A	118	TYR	0	0.006	-0.024	19.120	0.019	0.019	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.002	0.014	23.877	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	120	GLY	0	0.021	0.013	22.421	0.014	0.014	0.000	0.000	0.000	0.000
120	A	121	PRO	0	-0.007	-0.010	19.991	-0.016	-0.016	0.000	0.000	0.000	0.000
121	A	122	SER	0	0.052	0.036	22.783	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	123	ILE	0	0.001	0.005	21.321	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.942	0.979	26.009	-0.173	-0.173	0.000	0.000	0.000	0.000
124	A	125	LYS	1	0.997	0.996	28.097	-0.174	-0.174	0.000	0.000	0.000	0.000
125	A	126	GLY	0	-0.022	-0.014	28.718	-0.014	-0.014	0.000	0.000	0.000	0.000
126	A	127	THR	0	-0.005	0.003	26.742	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	GLY	0	0.026	0.015	24.735	0.002	0.002	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.015	-0.005	18.517	-0.009	-0.009	0.000	0.000	0.000	0.000
129	A	130	HIS	1	0.772	0.857	19.968	-0.308	-0.308	0.000	0.000	0.000	0.000
130	A	131	ARG	1	0.796	0.862	15.432	-0.277	-0.277	0.000	0.000	0.000	0.000
131	A	132	ILE	0	-0.035	-0.002	15.986	-0.060	-0.060	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.012	-0.013	13.319	0.136	0.136	0.000	0.000	0.000	0.000
133	A	134	PHE	0	-0.019	-0.018	11.624	-0.049	-0.049	0.000	0.000	0.000	0.000
134	A	135	ILE	0	0.022	0.010	12.008	-0.011	-0.011	0.000	0.000	0.000	0.000
135	A	136	LEU	0	0.020	0.012	11.686	0.034	0.034	0.000	0.000	0.000	0.000
136	A	137	SER	0	0.034	0.012	14.205	-0.060	-0.060	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.017	0.003	17.005	0.007	0.007	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.028	0.003	19.394	0.019	0.019	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.908	0.951	22.997	0.119	0.119	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.790	-0.900	25.766	-0.116	-0.116	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.840	-0.922	26.994	-0.103	-0.103	0.000	0.000	0.000	0.000
142	A	143	ASN	0	0.007	-0.011	28.004	0.019	0.019	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.804	0.919	25.449	0.107	0.107	0.000	0.000	0.000	0.000
144	A	145	GLY	0	-0.007	-0.012	26.815	0.009	0.009	0.000	0.000	0.000	0.000
145	A	146	ASN	0	-0.091	-0.044	29.304	0.016	0.016	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.045	0.037	25.674	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	148	THR	0	0.067	0.028	28.674	0.014	0.014	0.000	0.000	0.000	0.000
148	A	149	GLY	0	0.028	0.001	29.023	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.068	-0.044	25.727	0.014	0.014	0.000	0.000	0.000	0.000
150	A	151	PRO	0	0.002	0.011	29.089	-0.006	-0.006	0.000	0.000	0.000	0.000
151	A	152	LEU	0	0.049	0.027	30.612	0.005	0.005	0.000	0.000	0.000	0.000
152	A	153	TYR	0	-0.054	-0.054	30.138	0.004	0.004	0.000	0.000	0.000	0.000
153	A	154	ARG	1	0.946	0.967	32.166	-0.011	-0.011	0.000	0.000	0.000	0.000
154	A	155	GLY	0	0.035	0.014	33.810	0.001	0.001	0.000	0.000	0.000	0.000
155	A	156	GLU	-1	-0.765	-0.850	30.786	0.071	0.071	0.000	0.000	0.000	0.000
156	A	157	HIS	0	-0.033	-0.003	34.111	0.002	0.002	0.000	0.000	0.000	0.000
157	A	158	TYR	0	-0.050	-0.030	35.929	-0.003	-0.003	0.000	0.000	0.000	0.000
158	A	159	ILE	0	-0.022	0.012	30.292	-0.005	-0.005	0.000	0.000	0.000	0.000
159	A	160	THR	0	0.006	0.006	31.503	0.009	0.009	0.000	0.000	0.000	0.000
160	A	161	ARG	1	0.786	0.859	25.638	-0.096	-0.096	0.000	0.000	0.000	0.000
161	A	162	VAL	0	-0.023	-0.009	27.042	0.011	0.011	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.949	0.990	27.630	-0.080	-0.080	0.000	0.000	0.000	0.000
163	A	164	PHE	0	0.018	-0.003	21.484	-0.011	-0.011	0.000	0.000	0.000	0.000
164	A	165	ASN	0	0.037	0.016	26.677	-0.007	-0.007	0.000	0.000	0.000	0.000
165	A	166	ASN	0	-0.027	-0.010	29.923	-0.003	-0.003	0.000	0.000	0.000	0.000
166	A	167	CYS	0	-0.008	0.024	28.044	-0.010	-0.010	0.000	0.000	0.000	0.000
167	A	168	GLN	0	-0.028	-0.007	28.076	0.001	0.001	0.000	0.000	0.000	0.000
168	A	169	SER	0	0.027	-0.005	22.876	0.010	0.010	0.000	0.000	0.000	0.000
169	A	170	ALA	0	0.031	0.011	19.778	-0.013	-0.013	0.000	0.000	0.000	0.000
170	A	171	TYR	0	0.007	-0.006	19.047	-0.015	-0.015	0.000	0.000	0.000	0.000
171	A	172	ASN	0	-0.024	-0.017	21.362	-0.027	-0.027	0.000	0.000	0.000	0.000
172	A	173	VAL	0	0.019	0.005	23.943	-0.010	-0.010	0.000	0.000	0.000	0.000
173	A	174	ILE	0	0.014	0.004	18.414	-0.007	-0.007	0.000	0.000	0.000	0.000
174	A	175	GLN	0	-0.014	0.000	22.696	-0.020	-0.020	0.000	0.000	0.000	0.000
175	A	176	MET	0	-0.053	-0.016	24.545	0.000	0.000	0.000	0.000	0.000	0.000
176	A	177	ASN	0	-0.107	-0.075	25.614	0.007	0.007	0.000	0.000	0.000	0.000
177	A	178	ASP	-1	-0.889	-0.921	25.739	-0.118	-0.118	0.000	0.000	0.000	0.000
178	A	179	MET	0	-0.095	-0.027	21.207	-0.012	-0.012	0.000	0.000	0.000	0.000
179	A	180	LYS	1	0.870	0.917	16.989	0.433	0.433	0.000	0.000	0.000	0.000
180	A	181	ILE	0	-0.030	-0.018	13.849	-0.013	-0.013	0.000	0.000	0.000	0.000
181	A	182	VAL	0	0.015	-0.006	13.365	-0.025	-0.025	0.000	0.000	0.000	0.000
182	A	183	GLY	0	0.065	0.041	9.638	-0.214	-0.214	0.000	0.000	0.000	0.000
183	A	184	PHE	0	-0.002	-0.018	8.501	0.213	0.213	0.000	0.000	0.000	0.000
184	A	185	ASN	0	-0.003	-0.003	6.810	0.464	0.464	0.000	0.000	0.000	0.000
185	A	186	TRP	0	0.025	0.026	7.552	-0.185	-0.185	0.000	0.000	0.000	0.000
186	A	187	CYS	0	-0.024	0.019	9.894	0.305	0.305	0.000	0.000	0.000	0.000
187	A	188	GLN	0	-0.014	-0.015	12.576	-0.299	-0.299	0.000	0.000	0.000	0.000
188	A	189	MET	0	0.002	0.019	15.848	-0.004	-0.004	0.000	0.000	0.000	0.000
189	A	190	ARG	1	0.969	0.970	18.944	-0.384	-0.384	0.000	0.000	0.000	0.000
190	A	191	ARG	1	0.935	0.960	22.502	-0.224	-0.224	0.000	0.000	0.000	0.000
191	A	192	LYS	1	0.873	0.915	22.350	-0.430	-0.430	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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