FMO DATABASE

FMODB ID: 4JVLN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2063509.553442
FMO2-HF: Nuclear repulsion	1989804.079659
FMO2-HF: Total energy	-73705.473784
FMO2-MP2: Total energy	-73920.638512

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.
-6.274	-1.735	0.229	-1.963	-2.807	0.011

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 : -0.917 / q_NPA : -0.955

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	-0.031	-0.006	3.635	-5.800	-4.003	-0.012	-0.831	-0.955	0.004
4	A	4	ASP	-1	-0.755	-0.876	6.389	22.133	22.133	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.026	-0.004	9.856	-1.280	-1.280	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.000	0.000	12.717	-1.704	-1.704	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.023	0.018	15.281	0.555	0.555	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.032	-0.013	18.015	0.366	0.366	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.016	-0.013	19.042	-0.517	-0.517	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.021	-0.003	21.929	-0.224	-0.224	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.007	-0.004	25.099	0.086	0.086	0.000	0.000	0.000	0.000
12	A	12	PHE	0	-0.026	-0.013	26.005	-0.200	-0.200	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.035	0.020	28.125	0.368	0.368	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.964	0.996	30.226	-9.830	-9.830	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.054	0.014	31.797	-0.147	-0.147	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.026	-0.012	35.295	-0.039	-0.039	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.951	-0.965	32.036	9.488	9.488	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.076	-0.051	32.735	-0.080	-0.080	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.877	-0.934	32.108	9.039	9.039	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.077	-0.026	26.143	0.068	0.068	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.931	0.960	30.112	-8.744	-8.744	0.000	0.000	0.000	0.000
22	A	22	ILE	0	0.014	-0.003	26.008	0.153	0.153	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.060	-0.013	30.325	-0.229	-0.229	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.907	-0.952	29.960	10.079	10.079	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.903	0.941	32.726	-8.442	-8.442	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.971	0.985	33.967	-7.946	-7.946	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.014	-0.024	35.607	-0.283	-0.283	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.908	-0.954	36.202	8.205	8.205	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.008	0.008	35.978	0.087	0.087	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.011	0.007	30.659	0.349	0.349	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.011	-0.009	29.865	-0.313	-0.313	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.000	0.005	29.773	0.320	0.320	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.009	-0.027	28.201	-0.092	-0.092	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.952	-0.958	30.277	8.974	8.974	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.008	-0.011	24.987	0.020	0.020	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.011	0.016	29.251	-0.114	-0.114	0.000	0.000	0.000	0.000
37	A	37	MET	0	0.033	-0.002	23.903	0.206	0.206	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.052	0.037	29.586	-0.169	-0.169	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.040	-0.039	27.687	0.341	0.341	0.000	0.000	0.000	0.000
40	A	40	HIS	1	0.868	0.935	26.593	-10.203	-10.203	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.006	0.027	25.499	0.110	0.110	0.000	0.000	0.000	0.000
42	A	42	CYS	0	-0.020	0.015	21.867	0.482	0.482	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.020	0.025	17.387	-0.110	-0.110	0.000	0.000	0.000	0.000
44	A	44	HIS	1	0.827	0.918	20.623	-12.334	-12.334	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.020	-0.016	20.941	0.258	0.258	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.825	-0.924	23.088	11.120	11.120	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.034	-0.037	23.087	0.343	0.343	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.022	-0.005	28.453	-0.257	-0.257	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.897	0.960	31.830	-9.521	-9.521	0.000	0.000	0.000	0.000
50	A	50	HIS	0	-0.021	-0.013	30.951	-0.346	-0.346	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.053	-0.013	33.016	-0.194	-0.194	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.033	-0.019	35.649	-0.239	-0.239	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.073	-0.031	34.974	-0.239	-0.239	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.905	-0.946	35.174	8.833	8.833	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.017	-0.018	30.202	0.134	0.134	0.000	0.000	0.000	0.000
56	A	56	ARG	1	1.014	1.001	30.052	-10.257	-10.257	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.017	-0.015	25.821	0.282	0.282	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.014	0.010	24.838	0.090	0.090	0.000	0.000	0.000	0.000
59	A	59	PHE	0	0.031	0.013	19.341	0.402	0.402	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.939	0.966	20.727	-14.485	-14.485	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.915	-0.969	20.178	15.294	15.294	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.001	-0.002	21.824	-0.034	-0.034	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.070	-0.020	15.378	0.368	0.368	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.013	0.015	17.088	-0.232	-0.232	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.928	0.961	14.040	-17.268	-17.268	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.047	0.023	13.991	-1.641	-1.641	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.841	0.932	13.361	-19.189	-19.189	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.050	0.029	12.887	-1.618	-1.618	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.013	-0.019	13.784	0.416	0.416	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.046	0.003	14.380	-0.923	-0.923	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.002	0.007	16.109	0.049	0.049	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.027	0.010	19.354	0.291	0.291	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.034	-0.027	21.067	-0.289	-0.289	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.880	-0.935	24.340	11.602	11.602	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.927	-0.966	22.488	12.299	12.299	0.000	0.000	0.000	0.000
76	A	76	PHE	0	-0.094	-0.048	23.204	-0.027	-0.027	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.001	0.015	25.757	-0.246	-0.246	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.010	0.002	29.567	-0.180	-0.180	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.018	-0.016	24.924	-0.390	-0.390	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.966	0.972	26.036	-11.459	-11.459	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.003	0.017	23.977	0.428	0.428	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.001	0.009	19.316	-0.108	-0.108	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.022	-0.002	20.569	-0.255	-0.255	0.000	0.000	0.000	0.000
84	A	84	CYS	0	-0.105	-0.055	17.218	0.977	0.977	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.827	-0.917	17.489	16.372	16.372	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.039	-0.018	15.838	-0.811	-0.811	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.050	0.019	16.905	0.824	0.824	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.042	-0.020	13.796	-0.273	-0.273	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.028	0.000	17.859	-0.072	-0.072	0.000	0.000	0.000	0.000
90	A	90	TYR	0	0.020	0.002	17.491	0.032	0.032	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.008	-0.032	19.505	-0.599	-0.599	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.014	0.014	20.862	-0.458	-0.458	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.006	-0.033	21.847	-0.288	-0.288	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.007	-0.020	19.110	-0.195	-0.195	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.897	0.963	21.134	-11.197	-11.197	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.106	-0.077	22.162	-0.309	-0.309	0.000	0.000	0.000	0.000
97	A	97	TRP	0	0.098	0.049	21.576	-0.419	-0.419	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.030	-0.009	23.753	0.044	0.044	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.861	0.944	26.093	-10.581	-10.581	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.809	-0.912	28.945	9.319	9.319	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.891	-0.966	30.379	9.352	9.352	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.093	-0.060	23.494	0.193	0.193	0.000	0.000	0.000	0.000
103	A	103	PHE	0	-0.035	-0.048	28.282	0.205	0.205	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.908	-0.945	30.736	8.592	8.592	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.837	0.935	28.253	-10.044	-10.044	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.025	-0.017	29.032	0.370	0.370	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.049	-0.018	26.490	-0.139	-0.139	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.910	-0.947	28.941	8.824	8.824	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.014	-0.019	26.266	0.223	0.223	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.009	0.014	28.991	-0.162	-0.162	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.055	0.020	24.747	-0.146	-0.146	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.033	0.007	28.832	0.245	0.245	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.852	-0.932	30.456	9.081	9.081	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.921	-0.965	29.219	10.091	10.091	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.047	-0.025	25.461	0.257	0.257	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.024	0.002	27.791	0.136	0.136	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.927	0.970	30.599	-9.096	-9.096	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.062	-0.016	25.869	0.210	0.210	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.018	-0.022	25.097	-0.439	-0.439	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.015	-0.008	21.608	0.523	0.523	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.943	0.972	21.202	-14.501	-14.501	0.000	0.000	0.000	0.000
122	A	122	CYS	0	-0.084	-0.032	19.876	-0.370	-0.370	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.040	0.029	20.780	0.523	0.523	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.028	0.013	18.999	-0.179	-0.179	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.016	-0.008	20.032	0.080	0.080	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.724	-0.815	18.359	14.462	14.462	0.000	0.000	0.000	0.000
127	A	127	ALA	0	0.020	0.009	20.234	-0.478	-0.478	0.000	0.000	0.000	0.000
128	A	128	CYS	0	-0.011	0.006	23.925	0.118	0.118	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.018	-0.009	26.543	-0.128	-0.128	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.026	0.014	25.344	0.216	0.216	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.030	0.017	27.827	-0.184	-0.184	0.000	0.000	0.000	0.000
132	A	132	GLY	0	0.032	0.014	31.602	0.073	0.073	0.000	0.000	0.000	0.000
133	A	133	PHE	0	0.021	0.004	33.912	0.263	0.263	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.874	-0.945	35.498	8.233	8.233	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.852	-0.925	31.708	9.152	9.152	0.000	0.000	0.000	0.000
136	A	136	HIS	1	0.764	0.867	28.793	-10.268	-10.268	0.000	0.000	0.000	0.000
137	A	137	LYS	1	1.003	1.006	31.791	-8.063	-8.063	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.890	0.970	33.645	-9.057	-9.057	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.032	0.026	26.988	0.045	0.045	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.011	-0.005	28.329	0.062	0.062	0.000	0.000	0.000	0.000
141	A	141	SER	0	-0.114	-0.084	31.000	-0.043	-0.043	0.000	0.000	0.000	0.000
142	A	142	ASN	0	-0.067	-0.038	31.804	-0.333	-0.333	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.100	-0.054	28.269	0.252	0.252	0.000	0.000	0.000	0.000
144	A	144	ILE	0	0.008	0.024	24.986	0.417	0.417	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.043	-0.028	23.204	-0.257	-0.257	0.000	0.000	0.000	0.000
146	A	146	ILE	0	0.057	0.023	23.903	0.275	0.275	0.000	0.000	0.000	0.000
147	A	147	ILE	0	0.001	-0.003	18.042	0.034	0.034	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.770	-0.868	21.711	11.746	11.746	0.000	0.000	0.000	0.000
149	A	149	ASN	0	-0.010	-0.018	21.594	0.210	0.210	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.006	0.011	15.627	0.559	0.559	0.000	0.000	0.000	0.000
151	A	151	ASN	0	0.014	-0.006	12.702	-0.493	-0.493	0.000	0.000	0.000	0.000
152	A	152	GLU	-1	-0.841	-0.940	14.499	17.334	17.334	0.000	0.000	0.000	0.000
153	A	153	ASN	0	-0.053	-0.035	10.242	-0.464	-0.464	0.000	0.000	0.000	0.000
154	A	154	LEU	0	-0.002	-0.010	11.575	1.326	1.326	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.990	1.012	13.965	-15.453	-15.453	0.000	0.000	0.000	0.000
156	A	156	ASN	0	-0.046	-0.025	9.052	-1.653	-1.653	0.000	0.000	0.000	0.000
157	A	157	LEU	0	0.013	-0.003	8.344	1.595	1.595	0.000	0.000	0.000	0.000
158	A	158	VAL	0	0.033	0.029	11.633	-0.178	-0.178	0.000	0.000	0.000	0.000
159	A	159	GLY	0	-0.036	-0.008	14.603	0.239	0.239	0.000	0.000	0.000	0.000
160	A	160	LYS	1	0.828	0.920	8.959	-24.652	-24.652	0.000	0.000	0.000	0.000
161	A	161	SER	0	0.011	-0.009	12.042	-1.439	-1.439	0.000	0.000	0.000	0.000
162	A	162	PHE	0	0.006	0.017	8.245	1.810	1.810	0.000	0.000	0.000	0.000
163	A	163	TYR	0	0.016	0.010	8.178	-4.399	-4.399	0.000	0.000	0.000	0.000
164	A	164	PHE	0	0.038	0.012	9.021	2.591	2.591	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.007	-0.016	8.990	-1.114	-1.114	0.000	0.000	0.000	0.000
166	A	166	GLY	0	0.047	0.015	12.322	0.358	0.358	0.000	0.000	0.000	0.000
167	A	167	LEU	0	-0.018	-0.020	12.710	-0.841	-0.841	0.000	0.000	0.000	0.000
168	A	168	PRO	0	0.001	0.003	16.073	0.014	0.014	0.000	0.000	0.000	0.000
169	A	169	LEU	0	0.028	0.013	19.512	0.188	0.188	0.000	0.000	0.000	0.000
170	A	170	LYS	1	0.937	0.986	21.893	-14.102	-14.102	0.000	0.000	0.000	0.000
171	A	171	ILE	0	-0.005	-0.009	23.388	-0.500	-0.500	0.000	0.000	0.000	0.000
172	A	172	PHE	0	-0.020	-0.021	24.676	0.307	0.307	0.000	0.000	0.000	0.000
173	A	173	ASP	-1	-0.883	-0.946	28.760	9.056	9.056	0.000	0.000	0.000	0.000
174	A	174	ILE	0	0.011	0.029	27.718	-0.339	-0.339	0.000	0.000	0.000	0.000
175	A	175	ASP	-1	-0.828	-0.919	30.039	10.305	10.305	0.000	0.000	0.000	0.000
176	A	176	ALA	0	0.055	0.017	26.817	0.179	0.179	0.000	0.000	0.000	0.000
177	A	177	SER	0	-0.012	-0.005	22.447	-0.316	-0.316	0.000	0.000	0.000	0.000
178	A	178	PRO	0	0.013	0.030	21.344	0.386	0.386	0.000	0.000	0.000	0.000
179	A	179	ILE	0	-0.025	-0.021	16.957	0.253	0.253	0.000	0.000	0.000	0.000
180	A	180	ARG	1	0.853	0.924	12.179	-21.339	-21.339	0.000	0.000	0.000	0.000
181	A	181	CYS	0	-0.034	-0.012	13.199	0.224	0.224	0.000	0.000	0.000	0.000
182	A	182	ILE	0	0.009	0.009	6.748	0.319	0.319	0.000	0.000	0.000	0.000
183	A	183	ALA	0	-0.010	-0.007	7.965	-1.661	-1.661	0.000	0.000	0.000	0.000
184	A	184	ILE	0	0.008	0.002	3.988	1.383	1.803	0.006	-0.166	-0.260	0.001
185	A	185	LEU	0	-0.048	-0.032	3.232	-10.791	-9.212	0.226	-0.744	-1.062	0.007
186	A	186	GLU	-1	-0.946	-0.961	3.565	36.651	37.394	0.009	-0.222	-0.530	-0.001

Top

Graph

Manual

About

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