FMO DATABASE

FMODB ID: 6NZQZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2262854.335298
FMO2-HF: Nuclear repulsion	2182658.03731
FMO2-HF: Total energy	-80196.297988
FMO2-MP2: Total energy	-80430.803632

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.
-39.444	-20.931	12.168	-11.705	-18.977	-0.094

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 : -0.039 / q_NPA : -0.011

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	0.047	0.015	3.044	-1.624	0.827	0.242	-1.021	-1.673	0.005
4	A	5	ALA	0	-0.028	-0.005	5.502	-0.050	-0.050	0.000	0.000	0.000	0.000
5	A	6	ILE	0	0.019	-0.021	8.136	-0.034	-0.034	0.000	0.000	0.000	0.000
6	A	7	PRO	0	-0.015	0.010	11.352	0.033	0.033	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.868	0.915	14.996	-0.133	-0.133	0.000	0.000	0.000	0.000
8	A	9	GLY	0	-0.051	-0.031	17.669	0.015	0.015	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.838	0.881	20.377	0.029	0.029	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.033	0.005	17.026	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.896	-0.931	15.776	-0.081	-0.081	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.894	-0.966	15.799	-0.179	-0.179	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.986	1.002	17.131	0.094	0.094	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.017	0.013	11.237	-0.035	-0.035	0.000	0.000	0.000	0.000
15	A	16	MET	0	-0.009	-0.002	11.506	-0.089	-0.089	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.006	-0.001	13.324	-0.085	-0.085	0.000	0.000	0.000	0.000
17	A	18	TYR	0	0.001	-0.005	11.770	-0.034	-0.034	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.022	0.004	7.264	-0.079	-0.079	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.983	1.001	9.972	0.214	0.214	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.835	0.906	12.795	0.275	0.275	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.049	0.000	8.152	-0.102	-0.102	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.000	-0.014	9.747	-0.120	-0.120	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.073	-0.023	6.656	-0.096	-0.096	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.004	0.000	9.396	0.245	0.245	0.000	0.000	0.000	0.000
25	A	26	PHE	0	-0.028	-0.043	8.255	-0.109	-0.109	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.954	-0.965	11.541	-0.198	-0.198	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.929	0.972	12.598	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.881	-0.945	12.906	-0.287	-0.287	0.000	0.000	0.000	0.000
29	A	30	SER	0	-0.007	0.008	15.157	0.035	0.035	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.006	-0.023	16.480	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.010	-0.023	15.788	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.027	0.004	10.237	0.057	0.057	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.900	0.949	10.589	0.151	0.151	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.878	-0.937	8.293	0.120	0.120	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.068	0.024	7.172	0.056	0.056	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.945	0.985	6.508	1.160	1.160	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.895	-0.946	3.922	-2.705	-2.295	0.001	-0.126	-0.285	0.000
38	A	39	ILE	0	-0.017	-0.004	2.146	-10.871	-8.554	3.957	-3.132	-3.143	-0.035
39	A	40	VAL	0	-0.010	0.007	3.527	1.432	1.907	0.004	-0.109	-0.370	0.000
40	A	41	CYS	0	-0.045	-0.017	5.860	-0.144	-0.144	0.000	0.000	0.000	0.000
41	A	42	PHE	0	0.022	0.003	7.947	0.075	0.075	0.000	0.000	0.000	0.000
42	A	43	MET	0	-0.012	0.015	10.752	-0.043	-0.043	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.019	0.013	13.194	0.013	0.013	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.969	0.979	15.530	-0.126	-0.126	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.082	0.039	16.877	0.032	0.032	0.000	0.000	0.000	0.000
46	A	47	PHE	0	0.056	0.023	17.150	0.022	0.022	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.949	-0.978	16.831	0.246	0.246	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.012	0.004	11.646	0.063	0.063	0.000	0.000	0.000	0.000
49	A	50	PRO	0	0.047	0.009	12.920	0.086	0.086	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.006	0.019	14.654	0.034	0.034	0.000	0.000	0.000	0.000
51	A	52	TYR	0	0.024	0.008	11.145	0.039	0.039	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.033	-0.006	8.232	0.128	0.128	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.004	-0.003	11.174	0.067	0.067	0.000	0.000	0.000	0.000
54	A	55	HIS	0	-0.075	-0.036	14.174	-0.030	-0.030	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.019	-0.001	10.514	0.010	0.010	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.045	-0.018	9.447	0.218	0.218	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.025	-0.019	6.455	0.232	0.232	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.738	-0.788	2.626	3.356	5.685	1.378	-1.469	-2.238	-0.013
59	A	60	ILE	0	0.020	0.003	2.640	-1.191	-0.442	0.302	-0.149	-0.901	0.000
60	A	61	GLY	0	0.014	0.009	6.089	-0.088	-0.088	0.000	0.000	0.000	0.000
61	A	62	PHE	0	0.022	0.012	7.827	-0.044	-0.044	0.000	0.000	0.000	0.000
62	A	63	CYS	0	-0.064	-0.026	12.096	0.018	0.018	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.103	0.042	15.742	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	65	THR	0	0.025	-0.012	19.242	0.013	0.013	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.881	-0.939	21.477	0.072	0.072	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.051	-0.031	17.964	0.012	0.012	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.010	-0.023	16.453	0.018	0.018	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.039	0.027	20.298	0.005	0.005	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.837	-0.897	23.723	0.096	0.096	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.831	0.916	18.932	-0.255	-0.255	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.874	-0.924	20.954	0.145	0.145	0.000	0.000	0.000	0.000
72	A	73	THR	0	-0.077	-0.042	16.739	0.035	0.035	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.021	0.004	16.894	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.055	-0.031	11.750	0.019	0.019	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.041	0.030	11.349	-0.054	-0.054	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.050	0.022	11.986	0.019	0.019	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.087	-0.023	9.090	-0.024	-0.024	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.063	0.022	9.416	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.005	0.015	14.258	0.030	0.030	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.004	-0.004	12.527	-0.026	-0.026	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.043	0.016	16.786	0.024	0.024	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.015	-0.017	19.762	0.011	0.011	0.000	0.000	0.000	0.000
83	A	84	ASN	0	0.003	0.005	21.772	0.013	0.013	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.061	-0.028	20.388	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.014	-0.006	24.322	0.001	0.001	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.848	0.923	27.056	0.009	0.009	0.000	0.000	0.000	0.000
87	A	88	MET	0	0.016	0.029	27.335	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.032	-0.014	30.194	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.058	0.034	34.040	0.005	0.005	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.019	-0.026	37.132	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.061	0.026	39.491	0.004	0.004	0.000	0.000	0.000	0.000
92	A	93	PRO	0	-0.006	0.010	42.872	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.984	0.981	45.963	0.002	0.002	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.010	0.011	47.103	0.000	0.000	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.904	0.960	48.370	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.052	0.035	47.284	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.027	-0.024	43.439	0.002	0.002	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.010	0.005	46.302	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.890	-0.953	48.321	0.020	0.020	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.037	-0.008	50.106	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.955	-0.985	45.608	0.042	0.042	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.873	0.954	43.267	-0.031	-0.031	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.869	0.945	42.903	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	105	ILE	0	0.013	0.004	37.369	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.024	0.024	37.778	0.004	0.004	0.000	0.000	0.000	0.000
106	A	107	THR	0	0.025	-0.004	32.530	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.928	0.974	27.854	-0.047	-0.047	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.073	-0.031	25.377	0.008	0.008	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.051	0.008	29.338	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	111	ASN	0	0.003	-0.030	27.104	-0.009	-0.009	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.011	-0.002	27.392	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.065	-0.010	30.045	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	114	GLN	0	-0.027	-0.042	33.323	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.928	0.965	27.242	-0.092	-0.092	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.076	-0.084	33.318	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	117	CYS	0	-0.020	-0.015	35.240	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.828	-0.887	35.011	0.065	0.065	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.116	-0.056	35.666	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.933	0.950	37.770	-0.028	-0.028	0.000	0.000	0.000	0.000
120	A	121	GLY	0	-0.030	0.003	40.861	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	122	TRP	0	-0.047	-0.031	40.563	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	123	HIS	0	0.047	0.031	42.264	0.004	0.004	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.964	0.983	41.636	-0.045	-0.045	0.000	0.000	0.000	0.000
124	A	126	ILE	0	0.008	0.001	35.134	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	127	ILE	0	-0.038	-0.018	38.183	0.004	0.004	0.000	0.000	0.000	0.000
126	A	128	PRO	0	0.015	0.001	33.073	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	129	LEU	0	0.005	0.009	33.594	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.937	0.948	28.227	-0.094	-0.094	0.000	0.000	0.000	0.000
129	A	131	GLY	0	-0.019	-0.020	30.300	0.001	0.001	0.000	0.000	0.000	0.000
130	A	132	SER	0	0.021	0.020	32.378	0.000	0.000	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.018	0.008	33.229	0.000	0.000	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.871	-0.939	35.936	0.021	0.021	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.005	0.000	38.458	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	136	ALA	0	-0.011	-0.006	39.752	0.000	0.000	0.000	0.000	0.000	0.000
135	A	137	PRO	0	0.018	0.003	40.741	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.004	0.004	44.074	0.000	0.000	0.000	0.000	0.000	0.000
137	A	139	ALA	0	-0.024	-0.001	44.467	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	140	GLY	0	-0.006	0.002	46.300	0.001	0.001	0.000	0.000	0.000	0.000
139	A	141	LEU	0	-0.056	-0.019	40.313	0.002	0.002	0.000	0.000	0.000	0.000
140	A	142	SER	0	-0.073	-0.064	41.020	0.002	0.002	0.000	0.000	0.000	0.000
141	A	143	ASP	-1	-0.874	-0.939	43.486	0.027	0.027	0.000	0.000	0.000	0.000
142	A	144	LEU	0	-0.016	-0.015	40.688	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	145	ILE	0	-0.026	0.001	36.379	0.003	0.003	0.000	0.000	0.000	0.000
144	A	146	VAL	0	0.024	0.013	32.173	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	147	ASP	-1	-0.866	-0.939	31.216	0.040	0.040	0.000	0.000	0.000	0.000
146	A	148	ILE	0	-0.020	-0.008	25.851	-0.004	-0.004	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.026	0.002	30.167	-0.003	-0.003	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.774	-0.872	27.069	-0.029	-0.029	0.000	0.000	0.000	0.000
149	A	151	THR	0	0.012	-0.010	30.806	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	152	GLY	0	0.019	0.011	34.185	0.000	0.000	0.000	0.000	0.000	0.000
151	A	153	ARG	1	0.909	0.968	36.139	0.015	0.015	0.000	0.000	0.000	0.000
152	A	154	THR	0	0.064	0.032	34.823	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	155	LEU	0	0.030	0.040	35.947	0.002	0.002	0.000	0.000	0.000	0.000
154	A	156	LYS	1	0.984	0.990	39.033	0.008	0.008	0.000	0.000	0.000	0.000
155	A	157	GLU	-1	-0.966	-0.994	39.361	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	158	ASN	0	-0.021	-0.026	39.942	0.002	0.002	0.000	0.000	0.000	0.000
157	A	159	ASN	0	-0.057	-0.024	43.069	0.000	0.000	0.000	0.000	0.000	0.000
158	A	160	LEU	0	-0.025	-0.006	39.691	0.002	0.002	0.000	0.000	0.000	0.000
159	A	161	GLU	-1	-0.950	-0.994	42.183	0.001	0.001	0.000	0.000	0.000	0.000
160	A	162	ILE	0	-0.045	-0.035	36.346	0.002	0.002	0.000	0.000	0.000	0.000
161	A	163	LEU	0	-0.017	-0.012	39.784	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	164	ASP	-1	-0.796	-0.859	37.759	0.016	0.016	0.000	0.000	0.000	0.000
163	A	165	GLU	-1	-0.854	-0.911	33.422	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	166	ILE	0	-0.048	-0.019	31.001	0.002	0.002	0.000	0.000	0.000	0.000
165	A	167	PHE	0	0.018	-0.011	25.527	0.004	0.004	0.000	0.000	0.000	0.000
166	A	168	VAL	0	-0.032	0.000	25.277	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	169	ILE	0	-0.027	-0.015	22.612	0.007	0.007	0.000	0.000	0.000	0.000
168	A	170	ARG	1	0.945	0.971	20.186	0.014	0.014	0.000	0.000	0.000	0.000
169	A	171	THR	0	0.002	-0.003	14.639	0.015	0.015	0.000	0.000	0.000	0.000
170	A	172	HIS	0	0.035	0.052	15.232	-0.019	-0.019	0.000	0.000	0.000	0.000
171	A	173	VAL	0	0.057	0.022	8.539	0.016	0.016	0.000	0.000	0.000	0.000
172	A	174	VAL	0	-0.023	-0.016	10.500	-0.002	-0.002	0.000	0.000	0.000	0.000
173	A	175	VAL	0	0.021	-0.001	6.421	0.087	0.087	0.000	0.000	0.000	0.000
174	A	176	ASN	0	0.016	0.014	7.368	-0.327	-0.327	0.000	0.000	0.000	0.000
175	A	177	PRO	0	0.076	0.020	8.328	0.102	0.102	0.000	0.000	0.000	0.000
176	A	178	VAL	0	-0.026	-0.011	9.914	-0.069	-0.069	0.000	0.000	0.000	0.000
177	A	179	SER	0	-0.025	-0.071	4.665	-0.293	-0.230	-0.001	-0.002	-0.060	0.000
178	A	180	TYR	0	0.022	0.024	6.145	-0.051	-0.051	0.000	0.000	0.000	0.000
179	A	181	ARG	1	0.943	0.971	8.079	-0.726	-0.726	0.000	0.000	0.000	0.000
180	A	182	THR	0	-0.077	-0.068	7.674	0.018	0.018	0.000	0.000	0.000	0.000
181	A	183	LYS	1	0.894	0.932	2.552	-8.660	-7.490	0.978	-0.540	-1.608	0.002
182	A	184	ARG	1	0.942	0.998	4.583	-0.637	-0.533	-0.001	-0.006	-0.097	0.000
183	A	185	GLU	-1	-0.873	-0.953	6.586	-0.603	-0.603	0.000	0.000	0.000	0.000
184	A	186	GLU	-1	-0.892	-0.941	2.269	-14.594	-9.718	3.734	-3.702	-4.908	-0.045
185	A	187	VAL	0	-0.034	-0.032	2.755	-2.857	-0.817	0.595	-0.919	-1.716	-0.006
186	A	188	VAL	0	-0.006	-0.009	3.893	0.012	0.116	0.005	0.017	-0.126	0.000
187	A	189	SER	0	0.050	0.044	5.657	-0.020	-0.020	0.000	0.000	0.000	0.000
188	A	190	PHE	0	0.002	-0.009	2.732	-1.225	0.121	0.975	-0.535	-1.786	-0.002
189	A	191	LEU	0	-0.052	-0.052	4.587	0.234	0.313	-0.001	-0.012	-0.066	0.000
190	A	192	GLU	-1	-0.940	-0.957	7.019	-0.478	-0.478	0.000	0.000	0.000	0.000
191	A	193	LYS	1	0.972	0.989	7.270	1.388	1.388	0.000	0.000	0.000	0.000
192	A	194	LEU	0	-0.044	-0.019	6.949	0.105	0.105	0.000	0.000	0.000	0.000
193	A	195	GLN	0	0.012	-0.001	9.497	0.116	0.116	0.000	0.000	0.000	0.000
194	A	196	GLU	-1	-0.893	-0.936	12.279	-0.471	-0.471	0.000	0.000	0.000	0.000
195	A	197	VAL	0	-0.056	-0.025	11.944	0.044	0.044	0.000	0.000	0.000	0.000
196	A	198	ILE	0	-0.062	-0.051	11.092	0.056	0.056	0.000	0.000	0.000	0.000
197	A	199	GLU	-1	-0.946	-0.965	14.773	-0.164	-0.164	0.000	0.000	0.000	0.000
198	A	200	HIS	0	0.000	0.001	17.490	0.024	0.024	0.000	0.000	0.000	0.000
199	A	201	ASP	-1	-0.924	-0.961	17.417	-0.212	-0.212	0.000	0.000	0.000	0.000
200	A	202	SER	0	-0.031	-0.038	18.644	0.020	0.020	0.000	0.000	0.000	0.000
201	A	203	ASN	0	-0.090	-0.032	20.402	0.032	0.032	0.000	0.000	0.000	0.000
202	A	204	GLU	-1	-1.007	-0.981	22.246	-0.141	-0.141	0.000	0.000	0.000	0.000

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