FMO DATABASE

FMODB ID: R9QJ8

Calculation Name: 1O63-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O63

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X0D2

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptAll
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	202
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2267459.62175
FMO2-HF: Nuclear repulsion	2187261.335509
FMO2-HF: Total energy	-80198.286242
FMO2-MP2: Total energy	-80432.756293

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-38.511	-24.935	26.053	-14.678	-24.954	-0.096

Interaction energy analysis for fragmet #1(A:2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.035 / q_NPA : -0.023

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	4	LEU	0	0.053	0.009	2.499	-1.857	0.234	1.350	-1.122	-2.320	0.006
4	A	5	ALA	0	-0.032	-0.011	5.294	0.031	0.072	-0.001	-0.003	-0.037	0.000
5	A	6	ILE	0	0.030	-0.004	7.809	-0.033	-0.033	0.000	0.000	0.000	0.000
6	A	7	PRO	0	-0.018	-0.002	11.279	0.029	0.029	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.828	0.907	15.005	-0.067	-0.067	0.000	0.000	0.000	0.000
8	A	9	GLY	0	0.001	-0.009	17.245	0.018	0.018	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.820	0.865	19.712	0.036	0.036	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.061	0.037	16.545	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.844	-0.920	14.837	-0.080	-0.080	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.839	-0.924	15.323	-0.141	-0.141	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.871	0.930	16.053	0.119	0.119	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.005	0.006	10.486	-0.031	-0.031	0.000	0.000	0.000	0.000
15	A	16	MET	0	0.007	0.004	11.075	-0.067	-0.067	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.039	-0.027	12.594	-0.059	-0.059	0.000	0.000	0.000	0.000
17	A	18	TYR	0	-0.011	-0.006	10.650	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.029	0.013	6.144	-0.063	-0.063	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.988	1.001	9.155	0.181	0.181	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.855	0.917	11.890	0.223	0.223	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.042	-0.007	7.470	-0.061	-0.061	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.001	-0.008	8.969	-0.113	-0.113	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.063	-0.017	6.147	-0.093	-0.093	0.000	0.000	0.000	0.000
24	A	25	ILE	0	-0.008	-0.013	8.829	0.183	0.183	0.000	0.000	0.000	0.000
25	A	26	PHE	0	-0.027	-0.037	7.979	-0.112	-0.112	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.909	-0.941	11.765	-0.173	-0.173	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.781	0.846	13.008	-0.051	-0.051	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.837	-0.910	13.289	-0.238	-0.238	0.000	0.000	0.000	0.000
29	A	30	SER	0	0.004	-0.009	15.462	0.037	0.037	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.016	-0.002	16.468	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.011	0.005	15.994	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.008	0.013	10.475	0.040	0.040	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.840	0.920	10.435	0.105	0.105	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.786	-0.857	8.753	0.145	0.145	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.074	0.029	7.663	0.059	0.059	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.845	0.917	6.924	1.217	1.217	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.832	-0.894	4.198	-1.969	-1.670	-0.001	-0.076	-0.222	0.000
38	A	39	ILE	0	-0.024	-0.006	2.173	-9.685	-6.825	3.149	-2.632	-3.377	-0.030
39	A	40	VAL	0	0.001	0.001	3.820	0.918	1.428	0.003	-0.142	-0.372	0.000
40	A	41	CYS	0	-0.041	0.001	5.655	-0.070	-0.070	0.000	0.000	0.000	0.000
41	A	42	PHE	0	0.031	0.006	7.822	0.055	0.055	0.000	0.000	0.000	0.000
42	A	43	MET	0	-0.035	0.001	10.674	-0.049	-0.049	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.033	0.021	13.080	0.007	0.007	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.908	0.942	15.521	-0.088	-0.088	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.055	0.014	16.583	0.021	0.021	0.000	0.000	0.000	0.000
46	A	47	PHE	0	0.067	0.031	17.055	0.012	0.012	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.887	-0.916	17.103	0.184	0.184	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.011	0.012	11.251	0.050	0.050	0.000	0.000	0.000	0.000
49	A	50	PRO	0	0.050	0.019	12.577	0.062	0.062	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.024	-0.035	14.465	0.026	0.026	0.000	0.000	0.000	0.000
51	A	52	TYR	0	0.009	-0.005	11.099	0.029	0.029	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.044	-0.007	7.669	0.100	0.100	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.003	0.000	11.008	0.048	0.048	0.000	0.000	0.000	0.000
54	A	55	HIS	0	-0.081	-0.045	14.329	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.001	0.006	10.739	0.024	0.024	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.030	-0.002	9.526	0.215	0.215	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.020	-0.014	6.424	0.205	0.205	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.733	-0.829	2.436	2.587	4.894	2.791	-2.351	-2.747	-0.024
59	A	60	ILE	0	0.019	0.004	2.625	-1.377	-0.436	0.830	-0.229	-1.542	0.002
60	A	61	GLY	0	0.024	0.002	5.297	-0.061	-0.073	-0.001	-0.001	0.014	0.000
61	A	62	PHE	0	0.019	0.015	7.528	-0.023	-0.023	0.000	0.000	0.000	0.000
62	A	63	CYS	0	-0.035	-0.015	11.857	0.020	0.020	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.073	0.042	15.581	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	65	THR	0	0.032	-0.015	19.008	0.011	0.011	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.861	-0.941	21.171	0.036	0.036	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.051	-0.022	18.070	0.009	0.009	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.014	-0.021	16.008	0.013	0.013	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.021	-0.001	19.972	0.006	0.006	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.820	-0.890	23.461	0.061	0.061	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.808	0.895	19.210	-0.163	-0.163	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.726	-0.821	20.078	0.086	0.086	0.000	0.000	0.000	0.000
72	A	73	THR	0	-0.068	-0.037	16.589	0.024	0.024	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.006	-0.006	16.809	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.043	-0.010	11.379	0.015	0.015	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.025	0.017	10.987	-0.039	-0.039	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.043	0.017	11.265	0.006	0.006	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.061	-0.015	9.051	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.047	0.022	9.075	-0.023	-0.023	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.001	0.002	14.124	0.024	0.024	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.001	-0.004	12.483	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.037	0.015	16.574	0.017	0.017	0.000	0.000	0.000	0.000
82	A	83	THR	0	0.009	-0.002	18.391	0.009	0.009	0.000	0.000	0.000	0.000
83	A	84	ASN	0	0.009	0.010	20.872	0.011	0.011	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.046	-0.011	19.775	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.017	-0.014	23.486	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.827	0.894	26.441	0.017	0.017	0.000	0.000	0.000	0.000
87	A	88	MET	0	0.008	0.029	27.085	0.002	0.002	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.021	-0.016	29.748	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.040	0.025	33.600	0.004	0.004	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.007	-0.015	36.782	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.056	0.019	39.170	0.003	0.003	0.000	0.000	0.000	0.000
92	A	93	PRO	0	-0.026	-0.012	42.639	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.874	0.912	45.037	0.006	0.006	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.011	0.000	46.718	0.000	0.000	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.863	0.949	46.717	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.023	0.025	47.235	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.018	-0.023	43.106	0.001	0.001	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.012	0.012	45.777	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.879	-0.931	47.760	0.011	0.011	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.005	0.001	49.174	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.806	-0.862	45.015	0.028	0.028	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.794	0.896	42.803	-0.018	-0.018	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.799	0.881	42.693	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	105	ILE	0	0.006	0.002	37.268	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.036	0.025	37.694	0.003	0.003	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.010	-0.035	32.380	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.789	0.877	28.120	-0.022	-0.022	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.065	-0.028	25.199	0.006	0.006	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.029	0.008	29.237	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	111	ASN	0	0.000	-0.016	26.574	-0.006	-0.006	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.001	-0.004	27.017	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.004	-0.013	29.665	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	114	GLN	0	-0.050	-0.035	32.649	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.834	0.888	25.476	-0.060	-0.060	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.051	-0.053	32.718	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	117	CYS	0	-0.011	-0.017	34.656	-0.006	-0.006	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.837	-0.902	33.739	0.042	0.042	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.118	-0.071	34.827	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.856	0.917	36.907	-0.013	-0.013	0.000	0.000	0.000	0.000
120	A	121	GLY	0	-0.022	0.006	40.182	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	122	TRP	0	-0.042	-0.034	40.740	0.000	0.000	0.000	0.000	0.000	0.000
122	A	123	HIS	0	0.052	0.029	41.444	0.003	0.003	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.827	0.890	40.826	-0.028	-0.028	0.000	0.000	0.000	0.000
124	A	126	ILE	0	0.024	0.014	34.895	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	127	ILE	0	-0.034	-0.018	37.790	0.002	0.002	0.000	0.000	0.000	0.000
126	A	128	PRO	0	0.001	-0.002	32.997	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	129	LEU	0	0.006	0.016	33.555	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.920	0.934	28.069	-0.062	-0.062	0.000	0.000	0.000	0.000
129	A	131	GLY	0	-0.006	-0.009	30.178	0.000	0.000	0.000	0.000	0.000	0.000
130	A	132	SER	0	-0.019	-0.027	32.535	0.002	0.002	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.023	0.024	33.423	0.001	0.001	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.855	-0.916	35.678	0.012	0.012	0.000	0.000	0.000	0.000
133	A	135	LEU	0	0.028	0.014	38.397	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	136	ALA	0	-0.001	0.003	39.758	0.000	0.000	0.000	0.000	0.000	0.000
135	A	137	PRO	0	-0.019	-0.012	40.844	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.028	-0.006	43.668	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	139	ALA	0	-0.027	-0.015	44.236	0.000	0.000	0.000	0.000	0.000	0.000
138	A	140	GLY	0	0.010	0.017	46.206	0.001	0.001	0.000	0.000	0.000	0.000
139	A	141	LEU	0	-0.015	0.010	40.714	0.001	0.001	0.000	0.000	0.000	0.000
140	A	142	SER	0	-0.057	-0.057	41.240	0.002	0.002	0.000	0.000	0.000	0.000
141	A	143	ASP	-1	-0.831	-0.900	43.651	0.016	0.016	0.000	0.000	0.000	0.000
142	A	144	LEU	0	-0.003	-0.008	40.883	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	145	ILE	0	-0.022	-0.003	36.406	0.002	0.002	0.000	0.000	0.000	0.000
144	A	146	VAL	0	0.042	0.027	32.022	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	147	ASP	-1	-0.778	-0.849	30.608	0.025	0.025	0.000	0.000	0.000	0.000
146	A	148	ILE	0	0.024	0.010	25.452	-0.003	-0.003	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.036	-0.019	29.710	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.771	-0.858	26.321	-0.035	-0.035	0.000	0.000	0.000	0.000
149	A	151	THR	0	0.021	0.001	30.132	0.000	0.000	0.000	0.000	0.000	0.000
150	A	152	GLY	0	0.034	0.030	33.522	0.000	0.000	0.000	0.000	0.000	0.000
151	A	153	ARG	1	0.812	0.902	35.737	0.017	0.017	0.000	0.000	0.000	0.000
152	A	154	THR	0	0.084	0.035	34.869	0.000	0.000	0.000	0.000	0.000	0.000
153	A	155	LEU	0	0.010	0.016	35.831	0.002	0.002	0.000	0.000	0.000	0.000
154	A	156	LYS	1	0.967	0.983	38.858	0.009	0.009	0.000	0.000	0.000	0.000
155	A	157	GLU	-1	-0.884	-0.938	38.415	-0.008	-0.008	0.000	0.000	0.000	0.000
156	A	158	ASN	0	-0.023	-0.009	39.575	0.002	0.002	0.000	0.000	0.000	0.000
157	A	159	ASN	0	-0.052	-0.032	42.917	0.000	0.000	0.000	0.000	0.000	0.000
158	A	160	LEU	0	0.006	0.017	39.551	0.001	0.001	0.000	0.000	0.000	0.000
159	A	161	GLU	-1	-0.842	-0.912	41.716	-0.006	-0.006	0.000	0.000	0.000	0.000
160	A	162	ILE	0	-0.019	-0.014	35.657	0.002	0.002	0.000	0.000	0.000	0.000
161	A	163	LEU	0	-0.032	-0.022	39.140	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	164	ASP	-1	-0.753	-0.844	37.198	0.004	0.004	0.000	0.000	0.000	0.000
163	A	165	GLU	-1	-0.838	-0.907	32.648	-0.011	-0.011	0.000	0.000	0.000	0.000
164	A	166	ILE	0	-0.055	-0.013	30.469	0.000	0.000	0.000	0.000	0.000	0.000
165	A	167	PHE	0	0.040	0.000	25.269	0.003	0.003	0.000	0.000	0.000	0.000
166	A	168	VAL	0	-0.022	-0.001	25.169	0.000	0.000	0.000	0.000	0.000	0.000
167	A	169	ILE	0	-0.031	-0.010	22.295	0.004	0.004	0.000	0.000	0.000	0.000
168	A	170	ARG	1	0.911	0.954	19.506	0.037	0.037	0.000	0.000	0.000	0.000
169	A	171	THR	0	-0.007	-0.008	13.978	0.010	0.010	0.000	0.000	0.000	0.000
170	A	172	HIS	0	0.020	0.031	15.010	-0.014	-0.014	0.000	0.000	0.000	0.000
171	A	173	VAL	0	0.040	0.022	8.557	0.020	0.020	0.000	0.000	0.000	0.000
172	A	174	VAL	0	-0.018	-0.017	10.031	0.005	0.005	0.000	0.000	0.000	0.000
173	A	175	VAL	0	0.014	-0.003	5.903	0.048	0.048	0.000	0.000	0.000	0.000
174	A	176	ASN	0	0.027	0.026	7.302	-0.246	-0.246	0.000	0.000	0.000	0.000
175	A	177	PRO	0	0.035	0.009	8.535	0.046	0.046	0.000	0.000	0.000	0.000
176	A	178	VAL	0	-0.046	-0.021	10.431	-0.058	-0.058	0.000	0.000	0.000	0.000
177	A	179	SER	0	0.030	-0.017	4.907	-0.199	-0.199	0.000	0.000	0.000	0.000
178	A	180	TYR	0	0.008	0.000	6.636	-0.116	-0.116	0.000	0.000	0.000	0.000
179	A	181	ARG	1	0.934	0.972	8.096	-0.497	-0.497	0.000	0.000	0.000	0.000
180	A	182	THR	0	-0.057	-0.047	8.215	-0.095	-0.095	0.000	0.000	0.000	0.000
181	A	183	LYS	1	0.808	0.901	2.137	-12.141	-10.982	3.825	-2.065	-2.920	0.016
182	A	184	ARG	1	0.851	0.935	5.242	-0.350	-0.350	0.000	0.000	0.000	0.000
183	A	185	GLU	-1	-0.769	-0.890	6.807	-0.372	-0.372	0.000	0.000	0.000	0.000
184	A	186	GLU	-1	-0.795	-0.877	1.985	-11.305	-10.465	8.982	-4.043	-5.779	-0.058
185	A	187	VAL	0	-0.025	-0.029	2.512	-2.849	-0.964	0.969	-1.020	-1.834	-0.003
186	A	188	VAL	0	-0.025	-0.014	3.361	0.315	0.223	0.013	0.250	-0.171	0.000
187	A	189	SER	0	0.038	0.034	6.149	0.028	0.028	0.000	0.000	0.000	0.000
188	A	190	PHE	0	-0.017	-0.017	2.351	-1.289	-0.706	4.144	-1.192	-3.535	-0.005
189	A	191	LEU	0	-0.026	-0.027	4.180	0.117	0.281	0.000	-0.052	-0.112	0.000
190	A	192	GLU	-1	-0.893	-0.947	6.676	-0.454	-0.454	0.000	0.000	0.000	0.000
191	A	193	LYS	1	0.938	0.970	7.489	1.096	1.096	0.000	0.000	0.000	0.000
192	A	194	LEU	0	-0.063	-0.036	6.301	0.082	0.082	0.000	0.000	0.000	0.000
193	A	195	GLN	0	0.008	0.003	8.804	0.095	0.095	0.000	0.000	0.000	0.000
194	A	196	GLU	-1	-0.885	-0.941	11.899	-0.409	-0.409	0.000	0.000	0.000	0.000
195	A	197	VAL	0	-0.050	-0.023	11.373	0.043	0.043	0.000	0.000	0.000	0.000
196	A	198	ILE	0	-0.037	-0.028	10.702	0.041	0.041	0.000	0.000	0.000	0.000
197	A	199	GLU	-1	-0.949	-0.945	14.114	-0.145	-0.145	0.000	0.000	0.000	0.000
198	A	200	HIS	0	0.069	0.044	16.777	0.015	0.015	0.000	0.000	0.000	0.000
199	A	201	ASP	-1	-0.850	-0.894	16.416	-0.169	-0.169	0.000	0.000	0.000	0.000
200	A	202	SER	0	-0.091	-0.069	17.773	0.021	0.021	0.000	0.000	0.000	0.000
201	A	203	ASN	0	-0.080	-0.047	19.629	0.028	0.028	0.000	0.000	0.000	0.000
202	A	204	GLU	-1	-1.034	-1.012	21.315	-0.121	-0.121	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)