FMO DATABASE

FMODB ID: 3Q87L

Calculation Name: 1K4N-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1K4N

Chain ID: A

ChEMBL ID:

UniProt ID: P52007

Base Structure: X-ray

Registration Date: 2023-06-19

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	183
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2010684.202956
FMO2-HF: Nuclear repulsion	1937999.845687
FMO2-HF: Total energy	-72684.357269
FMO2-MP2: Total energy	-72897.01025

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:1:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-1.17	-0.389	-0.001	-0.28	-0.501	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / 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	3	MET	0	-0.003	-0.006	3.798	-0.457	0.324	-0.001	-0.280	-0.501	0.001
4	A	4	ILE	0	-0.009	-0.008	6.033	0.695	0.695	0.000	0.000	0.000	0.000
5	A	5	MET	0	-0.003	0.019	8.177	0.151	0.151	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.017	0.016	11.619	0.041	0.041	0.000	0.000	0.000	0.000
7	A	7	ASN	0	0.028	0.008	14.441	0.073	0.073	0.000	0.000	0.000	0.000
8	A	8	TRP	0	0.105	0.024	16.711	0.036	0.036	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.082	-0.045	20.132	0.024	0.024	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.089	-0.048	17.130	0.010	0.010	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.025	0.009	18.018	0.000	0.000	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.853	-0.919	20.932	-0.205	-0.205	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.932	-0.976	23.657	-0.228	-0.228	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.045	-0.025	22.583	0.017	0.017	0.000	0.000	0.000	0.000
15	A	15	GLN	0	0.035	0.019	24.788	0.014	0.014	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.786	-0.877	26.734	-0.141	-0.141	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.033	0.001	26.460	0.010	0.010	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.005	0.009	25.087	0.004	0.004	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.051	-0.031	26.982	0.011	0.011	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.747	-0.846	29.918	-0.098	-0.098	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.010	0.009	27.084	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	PRO	0	0.025	0.003	29.708	0.008	0.008	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.812	0.885	32.431	0.103	0.103	0.000	0.000	0.000	0.000
24	A	24	PHE	0	-0.011	-0.010	32.502	0.006	0.006	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.022	0.018	30.077	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	HIS	0	0.016	0.014	34.022	0.003	0.003	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.008	0.004	37.376	0.004	0.004	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.021	-0.017	33.977	0.004	0.004	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.846	-0.892	36.964	-0.056	-0.056	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.902	-0.968	38.600	-0.045	-0.045	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.044	-0.020	41.151	0.004	0.004	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.012	-0.026	39.331	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.824	0.924	40.401	0.052	0.052	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.901	0.950	44.023	0.051	0.051	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.010	-0.012	43.816	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.015	0.028	46.083	0.001	0.001	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.012	-0.004	40.892	0.001	0.001	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.015	-0.014	39.651	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.058	0.014	35.067	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.016	-0.004	34.389	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.036	-0.016	34.526	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.027	0.005	36.193	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.034	0.016	31.172	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.009	-0.005	29.784	0.001	0.001	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.774	-0.876	30.239	-0.135	-0.135	0.000	0.000	0.000	0.000
46	A	46	HIS	1	0.773	0.885	29.232	0.118	0.118	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.002	0.014	28.296	0.014	0.014	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.053	-0.080	30.834	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.017	0.030	29.325	0.008	0.008	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.806	0.888	33.711	0.106	0.106	0.000	0.000	0.000	0.000
51	A	51	CYS	0	0.006	0.018	35.488	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.069	-0.049	37.537	0.003	0.003	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.011	0.005	38.150	0.007	0.007	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.067	0.003	37.385	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.004	0.000	35.551	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	56	THR	0	-0.035	-0.031	33.545	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.062	0.028	32.285	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.915	-0.970	31.316	-0.163	-0.163	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.801	0.900	28.856	0.140	0.140	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.026	-0.018	27.670	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.786	0.895	26.645	0.173	0.173	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.891	0.945	25.443	0.194	0.194	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.050	0.025	23.235	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.037	-0.023	21.922	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.913	-0.953	21.703	-0.278	-0.278	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.067	-0.029	18.446	-0.049	-0.049	0.000	0.000	0.000	0.000
67	A	67	CYS	0	-0.090	-0.020	17.028	-0.040	-0.040	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.041	0.015	18.278	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.977	-0.967	18.221	-0.457	-0.457	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.056	-0.032	21.552	0.021	0.021	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.026	-0.013	24.617	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.005	-0.008	26.841	0.016	0.016	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.777	-0.884	30.332	-0.165	-0.165	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.008	0.018	32.711	0.007	0.007	0.000	0.000	0.000	0.000
75	A	75	MET	0	0.001	0.001	36.373	0.000	0.000	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.005	0.012	38.750	0.007	0.007	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.039	-0.039	41.404	0.000	0.000	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.015	0.005	44.125	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.859	0.927	39.187	0.099	0.099	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.032	0.022	35.377	0.002	0.002	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.036	-0.021	34.240	0.002	0.002	0.000	0.000	0.000	0.000
82	A	82	CYS	0	-0.018	0.007	29.593	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.005	0.015	29.297	0.003	0.003	0.000	0.000	0.000	0.000
84	A	84	PHE	0	0.043	0.013	24.142	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.990	0.992	20.837	0.285	0.285	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.014	-0.024	20.213	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	87	HIS	0	0.003	-0.003	14.802	-0.022	-0.022	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.886	-0.933	13.598	-0.618	-0.618	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.038	-0.018	17.739	0.020	0.020	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.004	0.020	21.436	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.025	-0.028	23.517	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.007	-0.014	25.325	0.008	0.008	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.020	0.020	29.125	0.006	0.006	0.000	0.000	0.000	0.000
94	A	94	HIS	0	0.012	-0.007	28.335	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	TRP	0	-0.026	-0.024	27.862	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	96	GLN	0	0.016	0.006	21.853	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	97	PHE	0	-0.008	0.000	25.211	0.000	0.000	0.000	0.000	0.000	0.000
98	A	98	SER	0	0.067	0.027	22.343	-0.024	-0.024	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.013	0.015	23.607	-0.020	-0.020	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.023	0.010	25.637	0.018	0.018	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.845	-0.892	28.107	-0.126	-0.126	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.008	-0.011	29.274	0.005	0.005	0.000	0.000	0.000	0.000
103	A	103	PRO	0	-0.062	-0.027	32.103	0.002	0.002	0.000	0.000	0.000	0.000
104	A	104	TRP	0	0.047	0.016	31.750	0.001	0.001	0.000	0.000	0.000	0.000
105	A	105	PRO	0	-0.021	0.006	37.416	0.005	0.005	0.000	0.000	0.000	0.000
106	A	106	GLY	0	-0.004	-0.005	40.608	0.000	0.000	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.939	-0.960	43.329	-0.064	-0.064	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.875	0.949	45.045	0.074	0.074	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.989	0.987	44.493	0.062	0.062	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.016	-0.010	41.179	0.004	0.004	0.000	0.000	0.000	0.000
111	A	111	PRO	0	-0.006	-0.023	42.171	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	112	HIS	0	-0.063	-0.013	35.950	0.005	0.005	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.755	-0.849	35.896	-0.110	-0.110	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.049	0.021	33.411	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	115	TRP	0	-0.047	-0.027	27.465	0.003	0.003	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.808	-0.872	34.025	-0.088	-0.088	0.000	0.000	0.000	0.000
117	A	117	HIS	1	0.713	0.812	35.735	0.113	0.113	0.000	0.000	0.000	0.000
118	A	118	ILE	0	0.039	0.044	32.714	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.891	-0.948	33.982	-0.095	-0.095	0.000	0.000	0.000	0.000
120	A	120	ILE	0	0.034	0.015	34.021	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	121	VAL	0	0.046	0.018	33.299	0.004	0.004	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.045	-0.020	36.287	0.003	0.003	0.000	0.000	0.000	0.000
123	A	123	PRO	0	0.036	0.011	36.510	0.003	0.003	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.006	0.000	39.203	0.004	0.004	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.827	-0.922	42.600	-0.051	-0.051	0.000	0.000	0.000	0.000
126	A	126	PRO	0	-0.015	-0.005	42.606	0.000	0.000	0.000	0.000	0.000	0.000
127	A	127	GLU	-1	-0.913	-0.947	44.951	-0.051	-0.051	0.000	0.000	0.000	0.000
128	A	128	THR	0	-0.024	-0.001	47.673	0.001	0.001	0.000	0.000	0.000	0.000
129	A	129	LEU	0	-0.053	-0.004	41.906	0.001	0.001	0.000	0.000	0.000	0.000
130	A	130	ASN	0	0.035	-0.012	45.722	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.009	0.004	47.890	0.000	0.000	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.845	0.900	42.435	0.057	0.057	0.000	0.000	0.000	0.000
133	A	133	ALA	0	0.010	0.005	44.278	0.000	0.000	0.000	0.000	0.000	0.000
134	A	134	LEU	0	-0.022	-0.024	45.557	0.000	0.000	0.000	0.000	0.000	0.000
135	A	135	ALA	0	-0.014	0.003	48.479	0.001	0.001	0.000	0.000	0.000	0.000
136	A	136	LEU	0	-0.056	-0.019	42.197	0.001	0.001	0.000	0.000	0.000	0.000
137	A	137	LEU	0	-0.065	-0.021	44.818	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	138	SER	0	0.014	0.014	47.837	0.003	0.003	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.875	-0.953	50.456	-0.034	-0.034	0.000	0.000	0.000	0.000
140	A	140	GLU	-1	-0.953	-0.968	52.634	-0.033	-0.033	0.000	0.000	0.000	0.000
141	A	141	GLY	0	0.049	0.013	49.832	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	142	LEU	0	-0.062	-0.037	49.941	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	143	SER	0	-0.080	-0.041	52.120	0.000	0.000	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.034	0.008	50.277	0.001	0.001	0.000	0.000	0.000	0.000
145	A	145	PRO	0	0.023	0.013	53.479	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	146	GLY	0	-0.060	-0.042	51.636	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	147	ILE	0	-0.012	0.005	47.374	-0.003	-0.003	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.058	-0.022	49.023	0.001	0.001	0.000	0.000	0.000	0.000
149	A	149	VAL	0	0.051	0.013	48.039	-0.003	-0.003	0.000	0.000	0.000	0.000
150	A	150	LYS	1	0.903	0.958	46.604	0.065	0.065	0.000	0.000	0.000	0.000
151	A	151	THR	0	0.039	0.026	47.477	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	152	SER	0	-0.007	0.007	44.612	0.000	0.000	0.000	0.000	0.000	0.000
153	A	160	ARG	1	1.003	1.014	40.154	0.067	0.067	0.000	0.000	0.000	0.000
154	A	161	LEU	0	0.045	0.011	37.534	0.005	0.005	0.000	0.000	0.000	0.000
155	A	162	PRO	0	-0.056	-0.041	41.516	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	163	ASN	0	0.103	0.059	39.086	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	164	PRO	0	-0.027	0.013	42.046	-0.002	-0.002	0.000	0.000	0.000	0.000
158	A	165	THR	0	0.039	-0.014	40.811	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	166	LEU	0	-0.034	0.001	43.225	0.002	0.002	0.000	0.000	0.000	0.000
160	A	167	ALA	0	-0.046	-0.037	43.176	-0.004	-0.004	0.000	0.000	0.000	0.000
161	A	168	VAL	0	0.065	0.039	43.349	0.004	0.004	0.000	0.000	0.000	0.000
162	A	169	THR	0	-0.028	-0.018	43.604	-0.003	-0.003	0.000	0.000	0.000	0.000
163	A	170	ASP	-1	-0.717	-0.866	44.381	-0.061	-0.061	0.000	0.000	0.000	0.000
164	A	171	GLY	0	-0.059	-0.022	46.185	0.002	0.002	0.000	0.000	0.000	0.000
165	A	172	LYS	1	0.809	0.885	42.567	0.061	0.061	0.000	0.000	0.000	0.000
166	A	173	THR	0	0.017	0.025	38.846	-0.007	-0.007	0.000	0.000	0.000	0.000
167	A	174	THR	0	-0.062	-0.033	39.847	0.006	0.006	0.000	0.000	0.000	0.000
168	A	175	ILE	0	0.039	0.031	38.390	-0.006	-0.006	0.000	0.000	0.000	0.000
169	A	176	LYS	1	0.892	0.943	38.702	0.093	0.093	0.000	0.000	0.000	0.000
170	A	177	PHE	0	0.050	0.034	38.725	-0.004	-0.004	0.000	0.000	0.000	0.000
171	A	178	HIS	1	0.821	0.891	35.088	0.104	0.104	0.000	0.000	0.000	0.000
172	A	179	PRO	0	-0.018	-0.022	38.858	-0.001	-0.001	0.000	0.000	0.000	0.000
173	A	180	TRP	0	-0.005	0.028	35.906	0.003	0.003	0.000	0.000	0.000	0.000
174	A	181	SER	0	0.032	0.030	30.847	-0.001	-0.001	0.000	0.000	0.000	0.000
175	A	182	ILE	0	0.007	-0.012	29.602	0.004	0.004	0.000	0.000	0.000	0.000
176	A	183	GLU	-1	-0.876	-0.956	26.158	-0.173	-0.173	0.000	0.000	0.000	0.000
177	A	184	GLU	-1	-0.893	-0.948	29.371	-0.097	-0.097	0.000	0.000	0.000	0.000
178	A	185	ILE	0	-0.025	-0.011	32.599	0.006	0.006	0.000	0.000	0.000	0.000
179	A	186	VAL	0	0.008	0.030	29.005	0.003	0.003	0.000	0.000	0.000	0.000
180	A	187	ALA	0	0.009	0.000	30.982	0.003	0.003	0.000	0.000	0.000	0.000
181	A	188	SER	0	-0.172	-0.108	32.391	0.008	0.008	0.000	0.000	0.000	0.000
182	A	189	GLU	-1	-1.008	-0.998	34.861	-0.101	-0.101	0.000	0.000	0.000	0.000
183	A	190	GLN	0	-0.027	-0.002	30.249	-0.011	-0.011	0.000	0.000	0.000	0.000

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