FMO DATABASE

FMODB ID: 3Q6RL

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1857338.617331
FMO2-HF: Nuclear repulsion	1786876.453148
FMO2-HF: Total energy	-70462.164183
FMO2-MP2: Total energy	-70667.693214

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.
-1.509	0.431	0.139	-0.936	-1.141	-0.002

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 : 0.023 / q_NPA : 0.004

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	0.002	-0.019	3.243	-1.931	0.009	0.139	-0.936	-1.141	-0.002
4	A	4	GLU	-1	-0.891	-0.935	5.022	-0.421	-0.421	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.067	-0.028	6.713	0.082	0.082	0.000	0.000	0.000	0.000
6	A	6	MET	0	-0.018	0.004	10.197	0.062	0.062	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.871	-0.940	10.555	0.113	0.113	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.021	-0.020	14.550	-0.002	-0.002	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.932	-0.974	18.090	0.103	0.103	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.009	-0.009	19.752	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.948	0.975	22.588	-0.033	-0.033	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.044	-0.027	26.143	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.042	0.039	29.225	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.023	0.002	30.729	0.000	0.000	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.017	-0.006	31.991	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.025	0.006	33.411	0.000	0.000	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.012	0.008	35.032	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.773	-0.876	37.425	-0.032	-0.032	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.010	-0.059	39.087	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.019	-0.014	41.161	0.000	0.000	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.041	0.029	40.724	0.002	0.002	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.020	-0.019	41.524	0.003	0.003	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.070	-0.028	44.789	0.002	0.002	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.919	-0.966	43.512	-0.016	-0.016	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.040	-0.025	41.064	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.041	0.032	43.980	0.001	0.001	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.011	0.002	45.920	0.001	0.001	0.000	0.000	0.000	0.000
28	A	28	SER	0	0.003	-0.014	41.460	0.002	0.002	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.015	0.015	39.720	0.001	0.001	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.010	0.018	42.492	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.988	0.988	43.371	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.028	-0.011	37.312	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.002	0.028	40.842	0.002	0.002	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.945	-0.982	42.641	0.003	0.003	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.097	-0.060	40.011	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.798	0.885	41.435	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.921	0.968	35.999	-0.022	-0.022	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.012	-0.007	32.564	0.002	0.002	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.001	0.003	35.837	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.018	0.000	36.387	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.004	-0.006	35.745	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.020	-0.002	37.731	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.023	-0.007	37.071	0.000	0.000	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.005	0.001	39.573	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.041	0.018	39.554	0.001	0.001	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.005	0.012	39.927	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.009	-0.006	42.870	0.002	0.002	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.040	0.019	45.531	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.826	-0.864	43.090	-0.033	-0.033	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.048	-0.026	45.645	0.001	0.001	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.748	-0.855	48.643	-0.019	-0.019	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.005	0.009	50.380	0.001	0.001	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.064	-0.036	47.943	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.011	-0.002	52.166	0.001	0.001	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.851	0.933	54.568	0.019	0.019	0.000	0.000	0.000	0.000
56	A	63	ALA	0	0.038	0.003	59.727	0.000	0.000	0.000	0.000	0.000	0.000
57	A	64	GLY	0	-0.003	-0.007	61.626	0.000	0.000	0.000	0.000	0.000	0.000
58	A	65	GLY	0	0.037	0.016	59.696	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	66	TYR	0	0.063	0.018	49.254	0.000	0.000	0.000	0.000	0.000	0.000
60	A	67	ALA	0	0.070	0.037	54.981	0.000	0.000	0.000	0.000	0.000	0.000
61	A	68	ARG	1	0.941	0.979	56.140	0.011	0.011	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.032	-0.019	53.147	0.001	0.001	0.000	0.000	0.000	0.000
63	A	70	VAL	0	0.045	0.025	50.174	0.001	0.001	0.000	0.000	0.000	0.000
64	A	71	GLN	0	0.039	0.042	52.573	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	72	GLU	-1	-0.891	-0.949	54.835	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	73	LYS	1	0.952	0.980	50.028	0.013	0.013	0.000	0.000	0.000	0.000
67	A	74	ALA	0	0.044	0.028	50.334	0.000	0.000	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.878	0.927	51.381	0.014	0.014	0.000	0.000	0.000	0.000
69	A	76	LYS	1	0.890	0.953	52.601	0.009	0.009	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.033	-0.021	47.899	0.001	0.001	0.000	0.000	0.000	0.000
71	A	78	ILE	0	0.010	0.012	49.360	0.000	0.000	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.932	-0.965	51.284	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	80	PHE	0	-0.005	0.006	45.658	0.001	0.001	0.000	0.000	0.000	0.000
74	A	81	LEU	0	-0.021	-0.027	45.056	0.001	0.001	0.000	0.000	0.000	0.000
75	A	82	GLU	-1	-0.847	-0.936	48.889	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	83	GLN	0	0.038	0.026	51.939	0.001	0.001	0.000	0.000	0.000	0.000
77	A	84	ARG	1	0.822	0.914	47.841	0.004	0.004	0.000	0.000	0.000	0.000
78	A	85	PHE	0	0.018	-0.009	44.165	0.000	0.000	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.984	-0.983	49.395	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	87	SER	0	-0.088	-0.041	51.347	0.001	0.001	0.000	0.000	0.000	0.000
81	A	88	ARG	1	0.881	0.947	49.028	0.011	0.011	0.000	0.000	0.000	0.000
82	A	89	ASP	-1	-0.750	-0.869	45.351	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	90	SER	0	0.030	0.005	43.572	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	91	CYS	0	-0.096	-0.031	40.837	0.001	0.001	0.000	0.000	0.000	0.000
85	A	92	LEU	0	-0.002	0.012	40.923	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	93	ARG	1	0.925	0.958	36.626	0.013	0.013	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.029	0.025	41.322	0.000	0.000	0.000	0.000	0.000	0.000
88	A	95	LEU	0	-0.035	0.006	35.012	0.000	0.000	0.000	0.000	0.000	0.000
89	A	96	THR	0	-0.004	-0.029	39.431	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	97	SER	0	-0.012	-0.071	37.355	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	98	ARG	1	0.838	0.935	36.297	0.031	0.031	0.000	0.000	0.000	0.000
92	A	99	GLY	0	0.026	0.022	35.857	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.065	-0.034	36.543	0.000	0.000	0.000	0.000	0.000	0.000
94	A	101	GLU	-1	-0.804	-0.906	36.899	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	102	LEU	0	-0.072	-0.031	40.572	0.001	0.001	0.000	0.000	0.000	0.000
96	A	103	GLU	-1	-0.880	-0.951	43.819	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.054	-0.040	46.144	0.002	0.002	0.000	0.000	0.000	0.000
98	A	105	ILE	0	0.045	0.024	46.702	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	106	ALA	0	0.037	0.028	49.423	0.000	0.000	0.000	0.000	0.000	0.000
100	A	107	PHE	0	-0.062	-0.044	52.374	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	108	ARG	1	0.717	0.857	48.651	0.017	0.017	0.000	0.000	0.000	0.000
102	A	109	SER	0	0.019	0.001	48.367	0.001	0.001	0.000	0.000	0.000	0.000
103	A	110	GLU	-1	-0.929	-0.969	47.633	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	111	ASP	-1	-0.805	-0.856	41.177	-0.042	-0.042	0.000	0.000	0.000	0.000
105	A	112	ILE	0	0.004	0.017	42.045	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	113	THR	0	0.074	0.025	40.950	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	114	GLY	0	-0.066	-0.022	40.447	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	115	GLN	0	-0.024	-0.017	34.994	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	116	LEU	0	-0.011	0.003	30.405	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	117	GLY	0	0.012	0.004	35.023	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	118	ASN	0	-0.099	-0.036	36.128	0.008	0.008	0.000	0.000	0.000	0.000
112	A	119	ASN	0	0.083	0.013	38.127	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	120	ASP	-1	-0.910	-0.956	35.109	-0.051	-0.051	0.000	0.000	0.000	0.000
114	A	121	ASP	-1	-0.903	-0.972	33.332	-0.077	-0.077	0.000	0.000	0.000	0.000
115	A	122	LEU	0	0.024	0.016	33.858	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	123	ILE	0	0.033	0.020	34.229	0.002	0.002	0.000	0.000	0.000	0.000
117	A	124	LEU	0	-0.019	-0.017	28.686	0.000	0.000	0.000	0.000	0.000	0.000
118	A	125	SER	0	-0.007	-0.025	30.641	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	126	CYS	0	-0.032	0.005	31.991	0.002	0.002	0.000	0.000	0.000	0.000
120	A	127	CYS	0	-0.037	-0.016	29.429	0.004	0.004	0.000	0.000	0.000	0.000
121	A	128	LEU	0	0.023	-0.007	25.670	0.001	0.001	0.000	0.000	0.000	0.000
122	A	129	HIS	0	-0.068	-0.015	28.120	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	130	TYR	0	-0.044	-0.030	29.022	0.002	0.002	0.000	0.000	0.000	0.000
124	A	131	CYS	0	-0.051	-0.015	23.925	0.004	0.004	0.000	0.000	0.000	0.000
125	A	132	LYS	1	0.937	0.989	24.272	0.053	0.053	0.000	0.000	0.000	0.000
126	A	133	ASP	-1	-0.760	-0.841	19.821	-0.084	-0.084	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.819	0.894	21.315	0.049	0.049	0.000	0.000	0.000	0.000
128	A	135	ALA	0	0.050	0.010	18.616	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	136	LYS	1	0.953	0.958	17.045	0.042	0.042	0.000	0.000	0.000	0.000
130	A	137	ASP	-1	-0.826	-0.905	16.820	-0.051	-0.051	0.000	0.000	0.000	0.000
131	A	138	PHE	0	-0.038	-0.022	13.497	0.014	0.014	0.000	0.000	0.000	0.000
132	A	139	MET	0	-0.032	-0.010	11.647	-0.049	-0.049	0.000	0.000	0.000	0.000
133	A	140	PRO	0	0.001	0.031	8.799	0.028	0.028	0.000	0.000	0.000	0.000
134	A	141	ALA	0	-0.034	-0.036	12.053	-0.037	-0.037	0.000	0.000	0.000	0.000
135	A	142	SER	0	-0.119	-0.074	11.813	0.049	0.049	0.000	0.000	0.000	0.000
136	A	143	LYS	1	0.825	0.874	9.201	-0.847	-0.847	0.000	0.000	0.000	0.000
137	A	144	GLU	-1	-0.881	-0.925	4.931	1.057	1.057	0.000	0.000	0.000	0.000
138	A	145	GLU	-1	-0.786	-0.848	6.398	0.526	0.526	0.000	0.000	0.000	0.000
139	A	146	PRO	0	-0.028	-0.024	7.838	-0.065	-0.065	0.000	0.000	0.000	0.000
140	A	147	ILE	0	0.054	0.046	8.447	-0.009	-0.009	0.000	0.000	0.000	0.000
141	A	148	ARG	1	0.878	0.937	11.215	-0.159	-0.159	0.000	0.000	0.000	0.000
142	A	149	LEU	0	-0.003	0.009	14.547	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	150	LEU	0	-0.024	0.002	18.022	0.010	0.010	0.000	0.000	0.000	0.000
144	A	151	ARG	1	0.746	0.838	20.721	0.062	0.062	0.000	0.000	0.000	0.000
145	A	152	GLU	-1	-0.864	-0.939	23.809	0.006	0.006	0.000	0.000	0.000	0.000
146	A	153	VAL	0	-0.038	-0.005	27.082	0.003	0.003	0.000	0.000	0.000	0.000
147	A	154	VAL	0	-0.017	-0.015	27.530	0.000	0.000	0.000	0.000	0.000	0.000
148	A	155	LEU	0	-0.019	-0.006	29.666	0.001	0.001	0.000	0.000	0.000	0.000
149	A	156	LEU	0	-0.046	-0.035	31.628	0.002	0.002	0.000	0.000	0.000	0.000
150	A	157	THR	0	0.018	-0.032	32.773	-0.002	-0.002	0.000	0.000	0.000	0.000
151	A	158	ASP	-1	-0.851	-0.919	34.420	-0.016	-0.016	0.000	0.000	0.000	0.000
152	A	159	ASP	-1	-0.807	-0.904	36.018	-0.045	-0.045	0.000	0.000	0.000	0.000
153	A	160	ARG	1	0.830	0.883	33.073	0.028	0.028	0.000	0.000	0.000	0.000
154	A	161	ASN	0	0.025	0.011	32.006	-0.008	-0.008	0.000	0.000	0.000	0.000
155	A	162	LEU	0	0.092	0.041	31.718	-0.007	-0.007	0.000	0.000	0.000	0.000
156	A	163	ARG	1	0.962	0.995	27.233	0.043	0.043	0.000	0.000	0.000	0.000
157	A	164	VAL	0	-0.022	-0.012	26.995	-0.004	-0.004	0.000	0.000	0.000	0.000
158	A	165	LYS	1	0.926	0.966	26.669	0.061	0.061	0.000	0.000	0.000	0.000
159	A	166	ALA	0	0.034	0.015	26.609	-0.009	-0.009	0.000	0.000	0.000	0.000
160	A	167	LEU	0	-0.045	-0.022	23.542	-0.003	-0.003	0.000	0.000	0.000	0.000
161	A	168	THR	0	-0.063	-0.037	22.159	-0.010	-0.010	0.000	0.000	0.000	0.000
162	A	169	ARG	1	0.916	0.971	21.868	0.085	0.085	0.000	0.000	0.000	0.000
163	A	170	ASN	0	0.010	0.014	18.463	0.009	0.009	0.000	0.000	0.000	0.000
164	A	171	VAL	0	0.022	0.010	21.902	0.010	0.010	0.000	0.000	0.000	0.000
165	A	172	PRO	0	0.010	0.007	23.587	0.000	0.000	0.000	0.000	0.000	0.000
166	A	173	VAL	0	-0.006	-0.002	25.596	0.000	0.000	0.000	0.000	0.000	0.000
167	A	174	ARG	1	0.859	0.934	28.394	0.009	0.009	0.000	0.000	0.000	0.000
168	A	175	ASP	-1	-0.788	-0.884	31.114	-0.011	-0.011	0.000	0.000	0.000	0.000
169	A	176	ILE	0	0.010	0.002	34.731	0.004	0.004	0.000	0.000	0.000	0.000
170	A	177	PRO	0	0.017	0.009	37.288	0.003	0.003	0.000	0.000	0.000	0.000
171	A	178	ALA	0	0.021	0.011	33.314	0.004	0.004	0.000	0.000	0.000	0.000
172	A	179	PHE	0	-0.001	0.000	30.788	0.004	0.004	0.000	0.000	0.000	0.000
173	A	180	LEU	0	-0.006	-0.006	34.215	0.003	0.003	0.000	0.000	0.000	0.000
174	A	181	THR	0	-0.020	-0.014	35.922	0.003	0.003	0.000	0.000	0.000	0.000
175	A	182	TRP	0	-0.050	-0.014	27.801	0.002	0.002	0.000	0.000	0.000	0.000
176	A	183	ALA	0	-0.004	0.006	33.433	0.004	0.004	0.000	0.000	0.000	0.000
177	A	184	GLN	0	-0.126	-0.053	34.912	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)