FMO DATABASE

FMODB ID: 82Q1Y

Calculation Name: 4UQF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4UQF

Chain ID: A

ChEMBL ID:

UniProt ID: Q8Y5X1

Base Structure: X-ray

Registration Date: 2023-03-14

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	185
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1896631.416165
FMO2-HF: Nuclear repulsion	1822016.218517
FMO2-HF: Total energy	-74615.197648
FMO2-MP2: Total energy	-74828.252328

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:3:GLN)

Summations of interaction energy for fragment #1(A:3:GLN)

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.
-5.694	-1.943	0.078	-1.436	-2.393	0.002

Interaction energy analysis for fragmet #1(A:3:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / q_NPA : -0.017

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	5	ASP	-1	-0.866	-0.938	3.144	-1.274	1.252	0.055	-1.123	-1.458	0.000
4	A	6	LYS	1	0.891	0.922	3.789	-11.564	-11.147	0.004	-0.101	-0.319	0.001
5	A	7	GLN	0	0.043	0.029	7.107	-0.118	-0.118	0.000	0.000	0.000	0.000
6	A	8	LYS	1	1.005	1.014	8.763	0.122	0.122	0.000	0.000	0.000	0.000
7	A	9	ILE	0	-0.030	-0.011	8.422	-0.005	-0.005	0.000	0.000	0.000	0.000
8	A	10	ALA	0	-0.004	-0.012	11.102	-0.078	-0.078	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.881	-0.940	13.089	0.314	0.314	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.017	-0.016	14.428	-0.059	-0.059	0.000	0.000	0.000	0.000
11	A	13	VAL	0	-0.034	-0.017	15.196	-0.031	-0.031	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.991	0.994	17.234	-0.383	-0.383	0.000	0.000	0.000	0.000
13	A	15	VAL	0	0.031	0.021	19.015	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	16	ILE	0	-0.043	-0.016	18.737	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	17	LEU	0	-0.019	-0.022	20.585	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.905	-0.958	23.423	0.238	0.238	0.000	0.000	0.000	0.000
17	A	19	ALA	0	-0.046	-0.017	24.784	-0.023	-0.023	0.000	0.000	0.000	0.000
18	A	20	VAL	0	-0.097	-0.043	25.624	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	21	GLY	0	-0.015	0.002	28.009	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	22	GLU	-1	-0.828	-0.900	26.010	0.316	0.316	0.000	0.000	0.000	0.000
21	A	23	ASN	0	0.022	-0.003	27.834	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	24	PRO	0	-0.018	-0.025	22.652	0.020	0.020	0.000	0.000	0.000	0.000
23	A	25	ASP	-1	-0.898	-0.942	23.207	0.322	0.322	0.000	0.000	0.000	0.000
24	A	26	ARG	1	0.780	0.895	25.427	-0.351	-0.351	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.866	-0.946	25.011	0.332	0.332	0.000	0.000	0.000	0.000
26	A	28	GLY	0	-0.064	-0.032	24.001	0.033	0.033	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.101	-0.060	22.014	0.050	0.050	0.000	0.000	0.000	0.000
28	A	30	ILE	0	0.070	0.061	20.015	0.059	0.059	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.879	-0.943	17.003	0.720	0.720	0.000	0.000	0.000	0.000
30	A	32	THR	0	-0.103	-0.055	16.270	0.146	0.146	0.000	0.000	0.000	0.000
31	A	33	PRO	0	0.038	0.032	15.642	0.131	0.131	0.000	0.000	0.000	0.000
32	A	34	MET	0	0.042	0.014	10.237	0.353	0.353	0.000	0.000	0.000	0.000
33	A	35	ARG	1	0.881	0.937	11.552	-0.421	-0.421	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.030	0.018	13.245	0.142	0.142	0.000	0.000	0.000	0.000
35	A	37	ALA	0	0.004	0.007	9.292	0.138	0.138	0.000	0.000	0.000	0.000
36	A	38	ARG	1	0.943	0.960	8.211	-1.424	-1.424	0.000	0.000	0.000	0.000
37	A	39	MET	0	0.031	0.033	9.572	0.104	0.104	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.008	-0.018	10.744	-0.023	-0.023	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.910	-0.959	3.718	11.571	12.073	0.017	-0.119	-0.401	0.000
40	A	42	GLU	-1	-0.955	-0.965	7.808	1.614	1.614	0.000	0.000	0.000	0.000
41	A	43	VAL	0	-0.031	-0.034	10.291	-0.203	-0.203	0.000	0.000	0.000	0.000
42	A	44	PHE	0	-0.014	-0.019	10.010	-0.276	-0.276	0.000	0.000	0.000	0.000
43	A	45	ALA	0	0.046	0.024	7.952	0.130	0.130	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.031	0.008	8.684	0.092	0.092	0.000	0.000	0.000	0.000
45	A	47	LEU	0	-0.099	-0.043	8.790	-0.234	-0.234	0.000	0.000	0.000	0.000
46	A	48	LYS	1	0.887	0.942	4.164	-3.866	-3.560	0.002	-0.093	-0.215	0.001
47	A	49	LYS	1	0.938	0.979	7.730	-1.538	-1.538	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.801	-0.873	10.565	0.209	0.209	0.000	0.000	0.000	0.000
49	A	51	PRO	0	-0.007	-0.013	14.026	-0.023	-0.023	0.000	0.000	0.000	0.000
50	A	52	SER	0	-0.039	-0.044	16.299	-0.044	-0.044	0.000	0.000	0.000	0.000
51	A	53	VAL	0	0.059	0.028	14.657	-0.034	-0.034	0.000	0.000	0.000	0.000
52	A	54	HIS	0	-0.079	-0.054	15.563	-0.102	-0.102	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.047	-0.043	19.377	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.838	-0.883	19.865	0.005	0.005	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.067	-0.048	21.852	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	58	ILE	0	-0.032	0.004	24.158	0.001	0.001	0.000	0.000	0.000	0.000
57	A	59	PHE	0	-0.051	-0.033	26.367	0.012	0.012	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.944	-0.981	29.283	0.075	0.075	0.000	0.000	0.000	0.000
59	A	61	GLU	-1	-0.960	-0.972	32.165	0.037	0.037	0.000	0.000	0.000	0.000
60	A	62	GLN	0	-0.060	-0.032	35.852	0.006	0.006	0.000	0.000	0.000	0.000
61	A	63	HIS	0	0.052	0.028	37.198	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.945	-0.988	38.243	0.042	0.042	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.948	-0.958	40.314	0.064	0.064	0.000	0.000	0.000	0.000
64	A	66	LEU	0	-0.049	-0.032	38.088	0.005	0.005	0.000	0.000	0.000	0.000
65	A	67	VAL	0	0.012	0.017	33.444	0.001	0.001	0.000	0.000	0.000	0.000
66	A	68	LEU	0	-0.031	-0.026	33.835	0.005	0.005	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.029	-0.004	29.004	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	70	LYS	1	0.857	0.926	31.328	-0.157	-0.157	0.000	0.000	0.000	0.000
69	A	71	ASP	-1	-0.880	-0.952	31.036	0.220	0.220	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.006	0.014	24.926	0.009	0.009	0.000	0.000	0.000	0.000
71	A	73	ARG	1	0.924	0.955	24.958	-0.313	-0.313	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.034	0.031	21.978	0.020	0.020	0.000	0.000	0.000	0.000
73	A	75	SER	0	-0.032	-0.031	19.976	0.005	0.005	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.003	-0.017	18.424	0.037	0.037	0.000	0.000	0.000	0.000
75	A	77	MET	0	0.001	0.011	16.330	-0.022	-0.022	0.000	0.000	0.000	0.000
76	A	78	CYS	0	-0.102	-0.009	19.370	-0.031	-0.031	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.759	-0.893	19.683	0.438	0.438	0.000	0.000	0.000	0.000
78	A	80	HIS	0	-0.026	-0.016	20.642	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	81	HIS	0	-0.022	-0.046	23.034	-0.037	-0.037	0.000	0.000	0.000	0.000
80	A	82	LEU	0	-0.001	0.013	17.005	0.023	0.023	0.000	0.000	0.000	0.000
81	A	83	VAL	0	0.011	0.003	19.879	0.036	0.036	0.000	0.000	0.000	0.000
82	A	84	PRO	0	0.044	0.005	20.231	-0.014	-0.014	0.000	0.000	0.000	0.000
83	A	85	PHE	0	-0.042	-0.008	21.893	-0.052	-0.052	0.000	0.000	0.000	0.000
84	A	86	PHE	0	0.014	-0.006	22.903	0.049	0.049	0.000	0.000	0.000	0.000
85	A	87	GLY	0	0.021	0.013	25.029	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	88	VAL	0	-0.036	-0.003	26.772	0.021	0.021	0.000	0.000	0.000	0.000
87	A	89	ALA	0	-0.006	-0.005	26.403	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	90	HIS	0	0.047	0.018	28.430	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	91	VAL	0	-0.018	-0.006	27.273	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	92	ALA	0	0.040	0.015	30.699	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	93	TYR	0	-0.030	-0.033	31.074	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.090	0.056	34.431	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.020	0.030	34.918	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	96	GLN	0	-0.015	-0.016	35.463	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	97	ASN	0	-0.073	-0.058	36.017	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	98	GLY	0	0.055	0.041	37.084	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	99	ARG	1	0.853	0.927	31.338	-0.041	-0.041	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.059	0.029	31.823	0.010	0.010	0.000	0.000	0.000	0.000
99	A	101	ALA	0	0.007	0.005	27.180	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.088	0.037	26.927	0.002	0.002	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.022	0.000	26.292	0.019	0.019	0.000	0.000	0.000	0.000
102	A	104	SER	0	-0.017	-0.026	23.428	0.021	0.021	0.000	0.000	0.000	0.000
103	A	105	LYS	1	0.954	0.991	21.701	-0.070	-0.070	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.063	0.030	21.850	0.026	0.026	0.000	0.000	0.000	0.000
105	A	107	ALA	0	-0.008	-0.007	22.901	0.026	0.026	0.000	0.000	0.000	0.000
106	A	108	ARG	1	0.964	0.990	17.279	-0.310	-0.310	0.000	0.000	0.000	0.000
107	A	109	VAL	0	0.025	0.030	17.983	0.066	0.066	0.000	0.000	0.000	0.000
108	A	110	VAL	0	-0.008	-0.003	19.282	0.038	0.038	0.000	0.000	0.000	0.000
109	A	111	ASP	-1	-0.906	-0.955	17.039	0.616	0.616	0.000	0.000	0.000	0.000
110	A	112	ASP	-1	-0.884	-0.938	14.418	0.797	0.797	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.060	-0.029	15.088	0.088	0.088	0.000	0.000	0.000	0.000
112	A	114	SER	0	0.007	0.006	17.420	0.003	0.003	0.000	0.000	0.000	0.000
113	A	115	ARG	1	0.885	0.995	12.746	-0.940	-0.940	0.000	0.000	0.000	0.000
114	A	116	ARG	1	0.924	0.945	12.752	-0.538	-0.538	0.000	0.000	0.000	0.000
115	A	117	PRO	0	-0.003	0.015	13.730	-0.085	-0.085	0.000	0.000	0.000	0.000
116	A	118	GLN	0	0.012	-0.013	16.965	-0.095	-0.095	0.000	0.000	0.000	0.000
117	A	119	LEU	0	0.007	0.017	20.058	-0.016	-0.016	0.000	0.000	0.000	0.000
118	A	120	GLN	0	0.044	0.007	23.535	0.024	0.024	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.842	-0.933	25.552	0.267	0.267	0.000	0.000	0.000	0.000
120	A	122	ARG	1	0.815	0.897	20.232	-0.396	-0.396	0.000	0.000	0.000	0.000
121	A	123	ILE	0	0.012	0.021	20.712	-0.007	-0.007	0.000	0.000	0.000	0.000
122	A	124	THR	0	0.017	0.018	23.005	-0.017	-0.017	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.033	-0.028	26.551	-0.014	-0.014	0.000	0.000	0.000	0.000
124	A	126	THR	0	0.000	0.002	20.190	-0.017	-0.017	0.000	0.000	0.000	0.000
125	A	127	VAL	0	0.023	0.014	22.616	-0.012	-0.012	0.000	0.000	0.000	0.000
126	A	128	ALA	0	-0.002	-0.008	24.268	-0.021	-0.021	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.792	-0.873	24.987	0.123	0.123	0.000	0.000	0.000	0.000
128	A	130	ILE	0	0.033	0.021	20.015	-0.017	-0.017	0.000	0.000	0.000	0.000
129	A	131	MET	0	-0.018	-0.002	24.151	-0.016	-0.016	0.000	0.000	0.000	0.000
130	A	132	MET	0	-0.037	-0.018	26.974	-0.018	-0.018	0.000	0.000	0.000	0.000
131	A	133	GLU	-1	-0.953	-0.978	23.969	0.115	0.115	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.774	0.857	21.902	-0.072	-0.072	0.000	0.000	0.000	0.000
133	A	135	LEU	0	0.012	0.008	26.257	-0.010	-0.010	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.946	1.000	29.260	-0.045	-0.045	0.000	0.000	0.000	0.000
135	A	137	PRO	0	0.005	0.032	30.972	-0.009	-0.009	0.000	0.000	0.000	0.000
136	A	138	LEU	0	0.026	0.004	34.092	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	139	GLY	0	0.002	-0.011	35.359	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	140	VAL	0	-0.020	-0.005	29.914	0.001	0.001	0.000	0.000	0.000	0.000
139	A	141	MET	0	-0.019	-0.005	33.331	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	142	VAL	0	0.011	0.015	27.589	0.005	0.005	0.000	0.000	0.000	0.000
141	A	143	ILE	0	0.000	-0.007	30.962	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	144	MET	0	-0.037	-0.006	24.181	0.010	0.010	0.000	0.000	0.000	0.000
143	A	145	GLU	-1	-0.870	-0.931	29.734	0.206	0.206	0.000	0.000	0.000	0.000
144	A	146	ALA	0	-0.033	-0.023	27.179	0.020	0.020	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.846	-0.916	28.609	0.270	0.270	0.000	0.000	0.000	0.000
146	A	148	HIS	0	-0.022	-0.029	26.432	0.046	0.046	0.000	0.000	0.000	0.000
147	A	149	MET	0	0.057	0.024	25.240	-0.022	-0.022	0.000	0.000	0.000	0.000
148	A	151	MET	0	-0.012	-0.015	27.489	-0.021	-0.021	0.000	0.000	0.000	0.000
149	A	152	THR	0	-0.018	0.011	30.362	-0.019	-0.019	0.000	0.000	0.000	0.000
150	A	153	ILE	0	0.028	0.015	26.727	-0.011	-0.011	0.000	0.000	0.000	0.000
151	A	154	ARG	1	0.921	0.967	28.795	-0.284	-0.284	0.000	0.000	0.000	0.000
152	A	155	GLY	0	0.009	0.001	31.973	-0.009	-0.009	0.000	0.000	0.000	0.000
153	A	156	VAL	0	-0.045	-0.022	33.475	-0.009	-0.009	0.000	0.000	0.000	0.000
154	A	157	ASN	0	-0.021	0.002	34.856	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	158	LYS	1	0.941	0.966	34.986	-0.189	-0.189	0.000	0.000	0.000	0.000
156	A	159	PRO	0	0.051	0.029	34.339	0.010	0.010	0.000	0.000	0.000	0.000
157	A	160	GLY	0	0.005	0.005	34.462	-0.014	-0.014	0.000	0.000	0.000	0.000
158	A	161	THR	0	-0.056	-0.025	34.276	-0.013	-0.013	0.000	0.000	0.000	0.000
159	A	162	LYS	1	0.913	0.960	32.890	-0.231	-0.231	0.000	0.000	0.000	0.000
160	A	163	THR	0	0.002	0.004	30.553	-0.017	-0.017	0.000	0.000	0.000	0.000
161	A	164	ILE	0	0.006	0.002	31.682	0.014	0.014	0.000	0.000	0.000	0.000
162	A	165	THR	0	-0.018	-0.016	28.892	-0.008	-0.008	0.000	0.000	0.000	0.000
163	A	166	SER	0	-0.022	-0.026	31.844	-0.003	-0.003	0.000	0.000	0.000	0.000
164	A	167	ALA	0	0.008	0.014	30.235	-0.003	-0.003	0.000	0.000	0.000	0.000
165	A	168	VAL	0	-0.006	0.007	32.204	0.000	0.000	0.000	0.000	0.000	0.000
166	A	169	ARG	1	0.765	0.837	29.551	-0.146	-0.146	0.000	0.000	0.000	0.000
167	A	170	GLY	0	0.022	0.012	34.589	0.000	0.000	0.000	0.000	0.000	0.000
168	A	171	ALA	0	0.096	0.025	37.103	0.001	0.001	0.000	0.000	0.000	0.000
169	A	172	PHE	0	0.031	0.023	36.406	0.000	0.000	0.000	0.000	0.000	0.000
170	A	173	LYS	1	0.874	0.938	35.224	-0.095	-0.095	0.000	0.000	0.000	0.000
171	A	174	ASN	0	-0.049	-0.036	39.528	-0.001	-0.001	0.000	0.000	0.000	0.000
172	A	175	ASP	-1	-0.805	-0.881	42.521	0.072	0.072	0.000	0.000	0.000	0.000
173	A	176	ASP	-1	-0.912	-0.982	43.213	0.084	0.084	0.000	0.000	0.000	0.000
174	A	177	LYS	1	0.939	0.971	44.813	-0.066	-0.066	0.000	0.000	0.000	0.000
175	A	178	LEU	0	0.083	0.060	40.555	0.005	0.005	0.000	0.000	0.000	0.000
176	A	179	ARG	1	0.854	0.909	39.456	-0.094	-0.094	0.000	0.000	0.000	0.000
177	A	180	SER	0	-0.023	-0.014	41.132	0.009	0.009	0.000	0.000	0.000	0.000
178	A	181	GLU	-1	-0.918	-0.952	43.381	0.088	0.088	0.000	0.000	0.000	0.000
179	A	182	VAL	0	-0.012	-0.002	36.743	0.005	0.005	0.000	0.000	0.000	0.000
180	A	183	LEU	0	-0.021	-0.019	38.411	0.008	0.008	0.000	0.000	0.000	0.000
181	A	184	ALA	0	-0.041	-0.008	40.619	0.004	0.004	0.000	0.000	0.000	0.000
182	A	185	LEU	0	-0.022	-0.019	40.031	0.003	0.003	0.000	0.000	0.000	0.000
183	A	186	ILE	0	-0.004	-0.012	35.409	0.006	0.006	0.000	0.000	0.000	0.000
184	A	187	LYS	1	0.932	0.995	38.367	-0.111	-0.111	0.000	0.000	0.000	0.000
185	A	188	HIS	0	0.007	0.001	39.673	0.008	0.008	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:3:GLN)