FMO DATABASE

FMODB ID: 5JVNZ

Calculation Name: 2B0A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2B0A

Chain ID: A

ChEMBL ID:

UniProt ID: Q58193

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	186
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2063732.713674
FMO2-HF: Nuclear repulsion	1990026.504736
FMO2-HF: Total energy	-73706.208938
FMO2-MP2: Total energy	-73921.417677

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:GLU)

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

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.
-3.832	0.49700000000001	0.414	-1.914	-2.827	0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.920 / q_NPA : -0.969

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	LEU	0	-0.023	-0.002	3.698	-4.517	-2.836	-0.012	-0.780	-0.889	0.003
4	A	4	ASP	-1	-0.748	-0.857	6.427	22.472	22.472	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.020	-0.005	9.341	-1.383	-1.383	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.009	-0.020	12.552	-1.788	-1.788	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.020	0.017	15.322	0.501	0.501	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.039	-0.015	18.180	0.387	0.387	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.020	-0.014	19.037	-0.554	-0.554	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.024	-0.001	21.939	-0.210	-0.210	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.002	-0.022	25.097	0.104	0.104	0.000	0.000	0.000	0.000
12	A	12	PHE	0	-0.014	-0.011	26.094	-0.211	-0.211	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.034	0.022	28.158	0.361	0.361	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.938	0.983	30.258	-9.812	-9.812	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.050	0.010	31.741	-0.148	-0.148	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.026	-0.011	35.291	-0.042	-0.042	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.940	-0.959	31.797	9.580	9.580	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.080	-0.054	32.832	-0.076	-0.076	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.863	-0.911	32.145	9.112	9.112	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.080	-0.030	26.058	0.065	0.065	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.925	0.957	30.131	-8.817	-8.817	0.000	0.000	0.000	0.000
22	A	22	ILE	0	0.015	-0.001	25.926	0.149	0.149	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.058	-0.016	30.325	-0.234	-0.234	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.910	-0.956	30.078	10.166	10.166	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.900	0.947	32.708	-8.613	-8.613	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.972	0.983	33.943	-8.156	-8.156	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.008	-0.021	35.578	-0.290	-0.290	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.900	-0.948	36.178	8.234	8.234	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.013	0.002	35.935	0.092	0.092	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.022	0.004	30.679	0.370	0.370	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.019	-0.011	29.760	-0.318	-0.318	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.001	0.004	29.750	0.323	0.323	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.010	-0.017	28.262	-0.085	-0.085	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.951	-0.960	30.289	9.030	9.030	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.012	-0.016	24.970	0.019	0.019	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.005	0.012	29.275	-0.121	-0.121	0.000	0.000	0.000	0.000
37	A	37	MET	0	0.037	0.002	24.000	0.222	0.222	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.052	0.038	29.630	-0.170	-0.170	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.055	-0.053	27.789	0.369	0.369	0.000	0.000	0.000	0.000
40	A	40	HIS	1	0.848	0.915	26.674	-10.296	-10.296	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.002	0.026	25.514	0.114	0.114	0.000	0.000	0.000	0.000
42	A	42	CYS	0	-0.024	0.014	21.934	0.481	0.481	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.021	0.021	17.431	-0.085	-0.085	0.000	0.000	0.000	0.000
44	A	44	HIS	1	0.831	0.922	20.685	-12.266	-12.266	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.012	-0.017	20.840	0.219	0.219	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.799	-0.914	23.197	10.911	10.911	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.045	-0.039	23.716	0.525	0.525	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.033	0.000	28.451	-0.253	-0.253	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.841	0.916	31.731	-9.511	-9.511	0.000	0.000	0.000	0.000
50	A	50	HIS	0	-0.031	-0.007	30.795	-0.384	-0.384	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.030	-0.003	33.128	-0.210	-0.210	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.017	-0.014	35.704	-0.264	-0.264	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.076	-0.031	34.876	-0.242	-0.242	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.904	-0.947	34.888	8.794	8.794	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.029	-0.021	29.878	0.130	0.130	0.000	0.000	0.000	0.000
56	A	56	ARG	1	1.010	1.001	29.750	-10.092	-10.092	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.025	-0.018	25.501	0.303	0.303	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.004	0.013	24.447	0.067	0.067	0.000	0.000	0.000	0.000
59	A	59	PHE	0	0.036	0.019	18.980	0.387	0.387	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.897	0.923	20.675	-14.530	-14.530	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.891	-0.937	19.938	15.231	15.231	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.037	0.010	21.483	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.075	-0.020	15.104	0.349	0.349	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.004	0.014	16.856	-0.241	-0.241	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.944	0.967	13.728	-17.344	-17.344	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.030	0.016	13.675	-1.624	-1.624	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.872	0.951	13.425	-18.260	-18.260	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.043	0.023	12.811	-1.498	-1.498	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.043	-0.045	13.287	0.191	0.191	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.057	0.000	13.393	-0.782	-0.782	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.006	0.005	15.176	0.007	0.007	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.031	-0.008	18.417	0.387	0.387	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.059	-0.034	20.191	-0.311	-0.311	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.864	-0.916	23.119	11.565	11.565	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.925	-0.959	21.235	12.126	12.126	0.000	0.000	0.000	0.000
76	A	76	PHE	0	-0.072	-0.045	22.155	-0.065	-0.065	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.002	0.015	24.808	-0.230	-0.230	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.006	-0.002	28.612	-0.157	-0.157	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.026	-0.014	23.909	-0.363	-0.363	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.952	0.970	25.339	-11.294	-11.294	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.013	0.020	23.066	0.382	0.382	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.016	0.014	18.544	-0.123	-0.123	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.021	0.000	20.126	-0.228	-0.228	0.000	0.000	0.000	0.000
84	A	84	CYS	0	-0.091	-0.053	17.018	0.864	0.864	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.792	-0.879	17.523	16.171	16.171	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.022	-0.011	15.640	-0.776	-0.776	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.034	0.018	16.442	0.728	0.728	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.029	-0.013	12.925	-0.254	-0.254	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.020	-0.004	17.034	-0.122	-0.122	0.000	0.000	0.000	0.000
90	A	90	TYR	0	0.021	0.000	16.701	0.089	0.089	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.007	-0.042	18.736	-0.595	-0.595	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.012	0.017	20.373	-0.458	-0.458	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.016	-0.037	21.393	-0.253	-0.253	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.005	-0.021	18.932	-0.199	-0.199	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.868	0.942	20.987	-11.206	-11.206	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.078	-0.061	22.179	-0.250	-0.250	0.000	0.000	0.000	0.000
97	A	97	TRP	0	0.091	0.048	21.754	-0.455	-0.455	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.028	-0.008	23.909	0.056	0.056	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.807	0.901	26.436	-10.479	-10.479	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.819	-0.915	29.208	9.324	9.324	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.831	-0.920	30.365	9.581	9.581	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.083	-0.053	23.316	0.137	0.137	0.000	0.000	0.000	0.000
103	A	103	PHE	0	-0.027	-0.037	27.916	0.172	0.172	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.900	-0.950	30.546	8.620	8.620	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.837	0.937	27.766	-9.857	-9.857	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.011	-0.014	28.563	0.361	0.361	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.047	-0.020	25.654	-0.156	-0.156	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.913	-0.943	28.224	8.695	8.695	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.013	-0.018	25.355	0.212	0.212	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.017	0.015	28.187	-0.154	-0.154	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.042	0.013	23.854	-0.152	-0.152	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.029	0.010	28.028	0.236	0.236	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.827	-0.912	29.576	8.938	8.938	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.858	-0.926	28.677	9.714	9.714	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.019	-0.008	24.578	0.236	0.236	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.018	0.005	27.156	0.167	0.167	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.843	0.926	30.135	-9.318	-9.318	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.074	-0.029	25.496	0.212	0.212	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.014	-0.018	25.109	-0.346	-0.346	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.017	-0.011	21.294	0.532	0.532	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.870	0.923	20.897	-15.007	-15.007	0.000	0.000	0.000	0.000
122	A	122	CYS	0	-0.054	-0.023	19.891	-0.245	-0.245	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.013	0.018	20.414	0.492	0.492	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.020	0.013	18.404	-0.144	-0.144	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.009	-0.007	19.333	0.035	0.035	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.726	-0.804	17.796	14.318	14.318	0.000	0.000	0.000	0.000
127	A	127	ALA	0	0.025	0.014	19.719	-0.457	-0.457	0.000	0.000	0.000	0.000
128	A	128	CYS	0	-0.020	0.001	23.459	0.122	0.122	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.002	0.000	26.153	-0.105	-0.105	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.015	0.007	24.581	0.213	0.213	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.026	0.016	27.134	-0.186	-0.186	0.000	0.000	0.000	0.000
132	A	132	GLY	0	0.023	0.013	30.914	0.082	0.082	0.000	0.000	0.000	0.000
133	A	133	PHE	0	0.000	-0.009	33.285	0.258	0.258	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.848	-0.932	34.978	8.219	8.219	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.856	-0.927	30.987	9.038	9.038	0.000	0.000	0.000	0.000
136	A	136	HIS	1	0.789	0.894	28.352	-10.232	-10.232	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.955	0.977	31.365	-8.144	-8.144	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.872	0.946	33.060	-8.902	-8.902	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.033	0.028	26.373	0.049	0.049	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.006	-0.003	28.206	0.068	0.068	0.000	0.000	0.000	0.000
141	A	141	SER	0	-0.104	-0.074	30.772	-0.044	-0.044	0.000	0.000	0.000	0.000
142	A	142	ASN	0	-0.083	-0.052	31.566	-0.307	-0.307	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.090	-0.048	27.524	0.068	0.068	0.000	0.000	0.000	0.000
144	A	144	ILE	0	0.011	0.021	24.765	0.428	0.428	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.036	-0.022	22.970	-0.251	-0.251	0.000	0.000	0.000	0.000
146	A	146	ILE	0	0.050	0.016	23.485	0.250	0.250	0.000	0.000	0.000	0.000
147	A	147	ILE	0	-0.004	-0.003	18.166	0.037	0.037	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.783	-0.884	21.215	11.577	11.577	0.000	0.000	0.000	0.000
149	A	149	ASN	0	-0.005	-0.009	21.310	0.198	0.198	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.002	0.012	15.185	0.606	0.606	0.000	0.000	0.000	0.000
151	A	151	ASN	0	-0.007	-0.019	13.023	-0.492	-0.492	0.000	0.000	0.000	0.000
152	A	152	GLU	-1	-0.827	-0.931	14.909	17.360	17.360	0.000	0.000	0.000	0.000
153	A	153	ASN	0	-0.045	-0.035	10.039	0.020	0.020	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.008	-0.004	11.037	1.112	1.112	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.992	1.015	13.282	-15.489	-15.489	0.000	0.000	0.000	0.000
156	A	156	ASN	0	-0.063	-0.031	9.143	-1.410	-1.410	0.000	0.000	0.000	0.000
157	A	157	LEU	0	0.009	0.003	7.482	1.265	1.265	0.000	0.000	0.000	0.000
158	A	158	VAL	0	0.031	0.028	10.748	-0.197	-0.197	0.000	0.000	0.000	0.000
159	A	159	GLY	0	-0.024	-0.005	13.675	0.209	0.209	0.000	0.000	0.000	0.000
160	A	160	LYS	1	0.834	0.921	8.566	-22.856	-22.856	0.000	0.000	0.000	0.000
161	A	161	SER	0	0.015	-0.001	11.113	-1.256	-1.256	0.000	0.000	0.000	0.000
162	A	162	PHE	0	0.010	0.010	7.790	1.510	1.510	0.000	0.000	0.000	0.000
163	A	163	TYR	0	0.014	0.009	8.248	-3.476	-3.476	0.000	0.000	0.000	0.000
164	A	164	PHE	0	0.033	0.012	9.081	2.463	2.463	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.004	-0.009	8.473	-1.068	-1.068	0.000	0.000	0.000	0.000
166	A	166	GLY	0	0.047	0.013	11.952	0.383	0.383	0.000	0.000	0.000	0.000
167	A	167	LEU	0	-0.026	-0.023	12.169	-0.865	-0.865	0.000	0.000	0.000	0.000
168	A	168	PRO	0	0.007	0.007	16.038	0.026	0.026	0.000	0.000	0.000	0.000
169	A	169	LEU	0	0.031	0.017	19.618	0.179	0.179	0.000	0.000	0.000	0.000
170	A	170	LYS	1	0.929	0.977	21.380	-14.465	-14.465	0.000	0.000	0.000	0.000
171	A	171	ILE	0	0.007	-0.002	23.236	-0.476	-0.476	0.000	0.000	0.000	0.000
172	A	172	PHE	0	-0.033	-0.027	24.146	0.316	0.316	0.000	0.000	0.000	0.000
173	A	173	ASP	-1	-0.849	-0.918	28.486	9.051	9.051	0.000	0.000	0.000	0.000
174	A	174	ILE	0	0.028	0.035	27.860	-0.324	-0.324	0.000	0.000	0.000	0.000
175	A	175	ASP	-1	-0.793	-0.888	30.065	10.384	10.384	0.000	0.000	0.000	0.000
176	A	176	ALA	0	0.045	0.008	26.923	0.164	0.164	0.000	0.000	0.000	0.000
177	A	177	SER	0	-0.037	-0.010	23.576	-0.168	-0.168	0.000	0.000	0.000	0.000
178	A	178	PRO	0	0.050	0.034	21.395	0.371	0.371	0.000	0.000	0.000	0.000
179	A	179	ILE	0	-0.032	-0.017	17.124	0.279	0.279	0.000	0.000	0.000	0.000
180	A	180	ARG	1	0.850	0.925	11.939	-22.072	-22.072	0.000	0.000	0.000	0.000
181	A	181	CYS	0	-0.037	-0.015	13.306	0.174	0.174	0.000	0.000	0.000	0.000
182	A	182	ILE	0	0.013	0.009	6.776	0.353	0.353	0.000	0.000	0.000	0.000
183	A	183	ALA	0	-0.010	-0.004	7.419	-1.695	-1.695	0.000	0.000	0.000	0.000
184	A	184	ILE	0	0.012	0.002	3.568	0.968	1.692	0.017	-0.378	-0.362	0.002
185	A	185	LEU	0	-0.050	-0.032	2.403	-7.708	-6.413	0.399	-0.568	-1.126	0.001
186	A	186	GLU	-1	-0.942	-0.961	3.631	34.033	34.662	0.010	-0.188	-0.450	-0.001

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