FMO DATABASE

FMODB ID: LJ149

Calculation Name: 2DOK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2DOK

Chain ID: A

ChEMBL ID:

UniProt ID: Q86US8

Base Structure: X-ray

Registration Date: 2023-06-20

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	177
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1859347.590154
FMO2-HF: Nuclear repulsion	1788884.473543
FMO2-HF: Total energy	-70463.116611
FMO2-MP2: Total energy	-70668.715744

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.
-1.498	0.322	0.14	-0.858	-1.102	-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 : 0.013 / q_NPA : 0.000

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	PRO	0	-0.032	-0.031	3.244	-1.734	0.086	0.140	-0.858	-1.102	-0.001
4	A	4	GLU	-1	-0.903	-0.939	4.896	-0.528	-0.528	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.058	-0.028	6.714	0.086	0.086	0.000	0.000	0.000	0.000
6	A	6	MET	0	-0.023	0.002	10.198	0.058	0.058	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.815	-0.888	11.151	0.095	0.095	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.023	-0.022	14.549	-0.001	-0.001	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.868	-0.927	18.089	0.077	0.077	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.017	-0.016	19.751	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.882	0.929	22.355	-0.025	-0.025	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.038	-0.021	26.142	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.031	0.031	29.224	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.018	0.006	30.751	0.000	0.000	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.014	-0.005	31.990	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.019	0.002	33.243	0.000	0.000	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.003	0.011	35.031	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.775	-0.870	37.376	-0.033	-0.033	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.016	-0.054	39.086	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.024	-0.021	41.200	0.001	0.001	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.020	0.012	40.727	0.002	0.002	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.005	-0.014	41.523	0.003	0.003	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.035	-0.006	44.789	0.002	0.002	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.883	-0.945	43.733	-0.016	-0.016	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.039	-0.021	40.501	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.043	0.035	43.979	0.001	0.001	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.015	0.003	45.919	0.001	0.001	0.000	0.000	0.000	0.000
28	A	28	SER	0	0.008	-0.006	41.483	0.002	0.002	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.006	0.010	39.754	0.001	0.001	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.001	0.013	42.491	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.958	0.982	43.564	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.033	-0.015	37.468	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.001	0.029	40.841	0.001	0.001	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.901	-0.961	42.640	0.002	0.002	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.100	-0.067	40.016	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.767	0.856	41.434	0.002	0.002	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.901	0.962	36.208	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.014	-0.017	32.692	0.002	0.002	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.001	0.008	35.578	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.024	-0.004	36.385	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.011	-0.004	35.755	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.012	-0.002	37.730	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.021	-0.005	37.022	0.000	0.000	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.003	0.003	39.574	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.048	0.019	39.464	0.001	0.001	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.004	0.006	39.920	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.016	-0.008	42.872	0.002	0.002	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.027	0.012	45.537	0.000	0.000	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.823	-0.859	43.063	-0.034	-0.034	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.052	-0.029	45.742	0.001	0.001	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.740	-0.844	48.644	-0.020	-0.020	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.011	0.014	50.378	0.001	0.001	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.061	-0.036	47.928	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.021	-0.005	52.167	0.001	0.001	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.858	0.940	54.569	0.020	0.020	0.000	0.000	0.000	0.000
56	A	63	ALA	0	0.033	-0.002	59.750	0.000	0.000	0.000	0.000	0.000	0.000
57	A	64	GLY	0	0.002	-0.002	61.626	0.000	0.000	0.000	0.000	0.000	0.000
58	A	65	GLY	0	0.039	0.018	59.695	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	66	TYR	0	0.061	0.017	49.241	0.000	0.000	0.000	0.000	0.000	0.000
60	A	67	ALA	0	0.061	0.034	54.980	0.000	0.000	0.000	0.000	0.000	0.000
61	A	68	ARG	1	0.937	0.974	56.139	0.011	0.011	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.027	-0.015	53.154	0.001	0.001	0.000	0.000	0.000	0.000
63	A	70	VAL	0	0.048	0.027	50.075	0.001	0.001	0.000	0.000	0.000	0.000
64	A	71	GLN	0	0.040	0.039	52.572	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	72	GLU	-1	-0.894	-0.944	54.834	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	73	LYS	1	0.885	0.938	48.630	0.014	0.014	0.000	0.000	0.000	0.000
67	A	74	ALA	0	0.027	0.021	50.332	0.000	0.000	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.863	0.921	51.380	0.014	0.014	0.000	0.000	0.000	0.000
69	A	76	LYS	1	0.878	0.943	52.644	0.009	0.009	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.040	-0.028	47.889	0.001	0.001	0.000	0.000	0.000	0.000
71	A	78	ILE	0	0.010	0.008	49.259	0.000	0.000	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.922	-0.961	51.283	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	80	PHE	0	-0.006	0.001	45.569	0.001	0.001	0.000	0.000	0.000	0.000
74	A	81	LEU	0	-0.017	-0.021	44.987	0.001	0.001	0.000	0.000	0.000	0.000
75	A	82	GLU	-1	-0.806	-0.902	48.888	-0.015	-0.015	0.000	0.000	0.000	0.000
76	A	83	GLN	0	0.036	0.025	51.938	0.001	0.001	0.000	0.000	0.000	0.000
77	A	84	ARG	1	0.807	0.901	47.695	0.006	0.006	0.000	0.000	0.000	0.000
78	A	85	PHE	0	0.039	0.003	44.133	0.000	0.000	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.983	-0.974	49.394	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	87	SER	0	-0.096	-0.052	51.153	0.001	0.001	0.000	0.000	0.000	0.000
81	A	88	ARG	1	0.883	0.940	48.996	0.013	0.013	0.000	0.000	0.000	0.000
82	A	89	ASP	-1	-0.734	-0.837	45.260	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	90	SER	0	0.042	0.012	43.514	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	91	CYS	0	-0.100	-0.034	40.838	0.000	0.000	0.000	0.000	0.000	0.000
85	A	92	LEU	0	-0.005	0.010	40.922	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	93	ARG	1	0.912	0.935	36.789	0.016	0.016	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.024	0.021	41.292	0.000	0.000	0.000	0.000	0.000	0.000
88	A	95	LEU	0	-0.058	0.001	34.787	0.000	0.000	0.000	0.000	0.000	0.000
89	A	96	THR	0	-0.030	-0.020	39.432	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	97	SER	0	-0.003	-0.044	37.354	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	98	ARG	1	0.867	0.916	36.298	0.033	0.033	0.000	0.000	0.000	0.000
92	A	99	GLY	0	0.029	0.018	35.865	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.067	-0.021	36.544	0.002	0.002	0.000	0.000	0.000	0.000
94	A	101	GLU	-1	-0.751	-0.848	36.680	-0.024	-0.024	0.000	0.000	0.000	0.000
95	A	102	LEU	0	-0.061	-0.026	40.574	0.001	0.001	0.000	0.000	0.000	0.000
96	A	103	GLU	-1	-0.878	-0.950	43.821	-0.013	-0.013	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.058	-0.041	46.145	0.002	0.002	0.000	0.000	0.000	0.000
98	A	105	ILE	0	0.036	0.019	46.709	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	106	ALA	0	0.030	0.027	49.424	0.000	0.000	0.000	0.000	0.000	0.000
100	A	107	PHE	0	-0.057	-0.043	52.375	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	108	ARG	1	0.687	0.815	48.684	0.018	0.018	0.000	0.000	0.000	0.000
102	A	109	SER	0	0.013	-0.001	48.419	0.000	0.000	0.000	0.000	0.000	0.000
103	A	110	GLU	-1	-0.898	-0.952	47.656	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	111	ASP	-1	-0.810	-0.887	41.185	-0.041	-0.041	0.000	0.000	0.000	0.000
105	A	112	ILE	0	0.006	0.016	42.093	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	113	THR	0	0.056	0.021	40.925	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	114	GLY	0	-0.063	-0.021	40.486	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	115	GLN	0	-0.014	-0.012	34.983	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	116	LEU	0	0.004	0.006	30.358	0.000	0.000	0.000	0.000	0.000	0.000
110	A	117	GLY	0	-0.001	0.002	34.978	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	118	ASN	0	-0.112	-0.059	36.059	0.007	0.007	0.000	0.000	0.000	0.000
112	A	119	ASN	0	0.066	0.004	38.128	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	120	ASP	-1	-0.820	-0.898	34.936	-0.054	-0.054	0.000	0.000	0.000	0.000
114	A	121	ASP	-1	-0.878	-0.949	33.152	-0.075	-0.075	0.000	0.000	0.000	0.000
115	A	122	LEU	0	0.033	0.025	33.859	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	123	ILE	0	0.037	0.022	34.314	0.001	0.001	0.000	0.000	0.000	0.000
117	A	124	LEU	0	-0.013	-0.009	28.686	0.000	0.000	0.000	0.000	0.000	0.000
118	A	125	SER	0	-0.005	-0.022	30.642	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	126	CYS	0	-0.043	-0.010	31.992	0.001	0.001	0.000	0.000	0.000	0.000
120	A	127	CYS	0	-0.050	-0.029	29.572	0.004	0.004	0.000	0.000	0.000	0.000
121	A	128	LEU	0	0.036	-0.006	25.724	0.001	0.001	0.000	0.000	0.000	0.000
122	A	129	HIS	0	-0.019	0.014	28.121	-0.008	-0.008	0.000	0.000	0.000	0.000
123	A	130	TYR	0	-0.027	-0.051	29.023	0.002	0.002	0.000	0.000	0.000	0.000
124	A	131	CYS	0	-0.053	-0.007	23.779	0.003	0.003	0.000	0.000	0.000	0.000
125	A	132	LYS	1	0.865	0.962	24.273	0.049	0.049	0.000	0.000	0.000	0.000
126	A	133	ASP	-1	-0.763	-0.834	19.816	-0.089	-0.089	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.748	0.842	21.302	0.058	0.058	0.000	0.000	0.000	0.000
128	A	135	ALA	0	0.045	0.008	18.618	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	136	LYS	1	0.958	0.963	17.046	0.045	0.045	0.000	0.000	0.000	0.000
130	A	137	ASP	-1	-0.772	-0.866	16.821	-0.062	-0.062	0.000	0.000	0.000	0.000
131	A	138	PHE	0	-0.017	-0.010	13.497	0.012	0.012	0.000	0.000	0.000	0.000
132	A	139	MET	0	-0.035	-0.005	11.225	-0.040	-0.040	0.000	0.000	0.000	0.000
133	A	140	PRO	0	-0.003	0.022	8.835	0.027	0.027	0.000	0.000	0.000	0.000
134	A	141	ALA	0	-0.037	-0.036	12.054	-0.033	-0.033	0.000	0.000	0.000	0.000
135	A	142	SER	0	-0.116	-0.075	11.792	0.043	0.043	0.000	0.000	0.000	0.000
136	A	143	LYS	1	0.819	0.870	9.076	-0.748	-0.748	0.000	0.000	0.000	0.000
137	A	144	GLU	-1	-0.873	-0.920	4.884	0.954	0.954	0.000	0.000	0.000	0.000
138	A	145	GLU	-1	-0.782	-0.846	6.363	0.444	0.444	0.000	0.000	0.000	0.000
139	A	146	PRO	0	-0.028	-0.017	7.837	-0.066	-0.066	0.000	0.000	0.000	0.000
140	A	147	ILE	0	0.057	0.045	8.174	0.000	0.000	0.000	0.000	0.000	0.000
141	A	148	ARG	1	0.810	0.878	11.217	-0.116	-0.116	0.000	0.000	0.000	0.000
142	A	149	LEU	0	-0.005	0.008	14.545	0.000	0.000	0.000	0.000	0.000	0.000
143	A	150	LEU	0	-0.038	-0.006	18.024	0.009	0.009	0.000	0.000	0.000	0.000
144	A	151	ARG	1	0.744	0.827	20.599	0.069	0.069	0.000	0.000	0.000	0.000
145	A	152	GLU	-1	-0.833	-0.926	23.808	0.001	0.001	0.000	0.000	0.000	0.000
146	A	153	VAL	0	-0.043	-0.007	27.121	0.003	0.003	0.000	0.000	0.000	0.000
147	A	154	VAL	0	-0.026	-0.017	27.529	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	155	LEU	0	-0.020	-0.003	29.663	0.001	0.001	0.000	0.000	0.000	0.000
149	A	156	LEU	0	-0.034	-0.031	31.627	0.002	0.002	0.000	0.000	0.000	0.000
150	A	157	THR	0	0.016	-0.032	32.734	-0.002	-0.002	0.000	0.000	0.000	0.000
151	A	158	ASP	-1	-0.851	-0.921	34.420	-0.018	-0.018	0.000	0.000	0.000	0.000
152	A	159	ASP	-1	-0.765	-0.869	35.979	-0.046	-0.046	0.000	0.000	0.000	0.000
153	A	160	ARG	1	0.824	0.884	33.070	0.028	0.028	0.000	0.000	0.000	0.000
154	A	161	ASN	0	-0.010	-0.032	32.005	-0.010	-0.010	0.000	0.000	0.000	0.000
155	A	162	LEU	0	0.037	0.018	31.719	-0.007	-0.007	0.000	0.000	0.000	0.000
156	A	163	ARG	1	0.969	0.996	27.182	0.043	0.043	0.000	0.000	0.000	0.000
157	A	164	VAL	0	-0.012	-0.006	27.044	-0.004	-0.004	0.000	0.000	0.000	0.000
158	A	165	LYS	1	0.864	0.941	26.670	0.057	0.057	0.000	0.000	0.000	0.000
159	A	166	ALA	0	0.038	0.013	26.610	-0.008	-0.008	0.000	0.000	0.000	0.000
160	A	167	LEU	0	-0.032	-0.016	23.478	-0.004	-0.004	0.000	0.000	0.000	0.000
161	A	168	THR	0	-0.054	-0.041	22.162	-0.009	-0.009	0.000	0.000	0.000	0.000
162	A	169	ARG	1	0.899	0.964	21.869	0.085	0.085	0.000	0.000	0.000	0.000
163	A	170	ASN	0	0.002	0.007	18.596	0.008	0.008	0.000	0.000	0.000	0.000
164	A	171	VAL	0	0.032	0.015	21.903	0.009	0.009	0.000	0.000	0.000	0.000
165	A	172	PRO	0	0.011	0.010	23.574	0.000	0.000	0.000	0.000	0.000	0.000
166	A	173	VAL	0	-0.012	-0.007	25.595	0.000	0.000	0.000	0.000	0.000	0.000
167	A	174	ARG	1	0.788	0.892	28.394	0.013	0.013	0.000	0.000	0.000	0.000
168	A	175	ASP	-1	-0.721	-0.838	31.114	-0.013	-0.013	0.000	0.000	0.000	0.000
169	A	176	ILE	0	0.031	0.010	34.730	0.003	0.003	0.000	0.000	0.000	0.000
170	A	177	PRO	0	0.030	0.015	37.287	0.003	0.003	0.000	0.000	0.000	0.000
171	A	178	ALA	0	0.014	0.010	33.300	0.003	0.003	0.000	0.000	0.000	0.000
172	A	179	PHE	0	0.001	0.000	30.852	0.004	0.004	0.000	0.000	0.000	0.000
173	A	180	LEU	0	0.004	0.001	34.214	0.003	0.003	0.000	0.000	0.000	0.000
174	A	181	THR	0	-0.023	-0.022	36.039	0.003	0.003	0.000	0.000	0.000	0.000
175	A	182	TRP	0	-0.029	-0.005	28.108	0.002	0.002	0.000	0.000	0.000	0.000
176	A	183	ALA	0	-0.002	0.013	33.433	0.004	0.004	0.000	0.000	0.000	0.000
177	A	184	GLN	0	-0.115	-0.048	34.911	0.004	0.004	0.000	0.000	0.000	0.000

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