FMO DATABASE

FMODB ID: 37NKL

Calculation Name: 1IXV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1IXV

Chain ID: A

ChEMBL ID:

UniProt ID: P50086

Base Structure: X-ray

Registration Date: 2023-09-26

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	229
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2700968.754543
FMO2-HF: Nuclear repulsion	2611493.490385
FMO2-HF: Total energy	-89475.264158
FMO2-MP2: Total energy	-89738.846488

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:ASN)

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

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.
-17.518	-12.924	0.485	-2.309	-2.771	-0.014

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / 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	5	PRO	0	0.011	-0.002	3.459	-2.297	0.193	0.010	-1.118	-1.382	0.003
4	A	6	LEU	0	0.006	0.016	5.498	-1.006	-1.006	0.000	0.000	0.000	0.000
5	A	7	HIS	0	0.033	0.005	6.387	0.217	0.217	0.000	0.000	0.000	0.000
6	A	8	GLN	0	-0.024	-0.015	5.363	1.355	1.355	0.000	0.000	0.000	0.000
7	A	9	ALA	0	-0.011	-0.006	7.323	-0.694	-0.694	0.000	0.000	0.000	0.000
8	A	10	CYS	0	-0.068	-0.033	10.516	-0.422	-0.422	0.000	0.000	0.000	0.000
9	A	11	MET	0	-0.047	-0.010	6.579	-0.311	-0.311	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.872	-0.929	9.899	1.644	1.644	0.000	0.000	0.000	0.000
11	A	13	ASN	0	-0.029	-0.024	12.808	-0.112	-0.112	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.771	-0.856	12.179	1.877	1.877	0.000	0.000	0.000	0.000
13	A	15	PHE	0	0.002	-0.019	14.730	0.151	0.151	0.000	0.000	0.000	0.000
14	A	16	PHE	0	0.026	0.013	16.426	0.008	0.008	0.000	0.000	0.000	0.000
15	A	17	LYS	1	0.871	0.909	10.711	-2.254	-2.254	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.006	0.000	12.913	0.142	0.142	0.000	0.000	0.000	0.000
17	A	19	GLN	0	-0.058	-0.021	14.048	-0.054	-0.054	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.873	-0.940	14.186	1.133	1.133	0.000	0.000	0.000	0.000
19	A	21	LEU	0	-0.042	-0.013	8.923	0.093	0.093	0.000	0.000	0.000	0.000
20	A	22	LEU	0	-0.043	-0.012	12.427	-0.091	-0.091	0.000	0.000	0.000	0.000
21	A	23	HIS	0	-0.008	0.005	14.891	-0.169	-0.169	0.000	0.000	0.000	0.000
22	A	24	SER	0	-0.048	-0.042	13.372	0.013	0.013	0.000	0.000	0.000	0.000
23	A	25	LYS	1	0.902	0.947	8.126	-2.903	-2.903	0.000	0.000	0.000	0.000
24	A	26	PRO	0	0.067	0.034	12.723	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	27	SER	0	-0.028	-0.017	12.666	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	28	LEU	0	-0.009	-0.012	7.913	-0.126	-0.126	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.023	-0.002	11.141	-0.093	-0.093	0.000	0.000	0.000	0.000
28	A	30	LEU	0	0.008	-0.005	13.986	-0.060	-0.060	0.000	0.000	0.000	0.000
29	A	31	GLN	0	-0.018	0.000	6.596	0.171	0.171	0.000	0.000	0.000	0.000
30	A	32	LYS	1	0.920	0.966	10.227	0.801	0.801	0.000	0.000	0.000	0.000
31	A	33	ASP	-1	-0.780	-0.883	5.466	-3.576	-3.576	0.000	0.000	0.000	0.000
32	A	34	GLN	0	-0.057	-0.047	2.543	-8.912	-6.808	0.475	-1.191	-1.389	-0.017
33	A	35	ASP	-1	-0.878	-0.923	6.693	-2.086	-2.086	0.000	0.000	0.000	0.000
34	A	36	GLY	0	0.036	0.011	9.965	0.448	0.448	0.000	0.000	0.000	0.000
35	A	37	ARG	1	0.760	0.863	9.977	1.076	1.076	0.000	0.000	0.000	0.000
36	A	38	ILE	0	0.011	0.011	10.845	-0.148	-0.148	0.000	0.000	0.000	0.000
37	A	39	PRO	0	0.015	-0.013	10.793	0.002	0.002	0.000	0.000	0.000	0.000
38	A	40	LEU	0	0.061	0.028	12.402	0.037	0.037	0.000	0.000	0.000	0.000
39	A	41	HIS	0	0.009	0.006	13.083	0.042	0.042	0.000	0.000	0.000	0.000
40	A	42	TRP	0	-0.004	-0.019	7.962	0.221	0.221	0.000	0.000	0.000	0.000
41	A	43	SER	0	0.025	-0.007	12.884	0.026	0.026	0.000	0.000	0.000	0.000
42	A	44	VAL	0	-0.018	0.000	15.687	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.060	-0.036	14.329	-0.048	-0.048	0.000	0.000	0.000	0.000
44	A	46	PHE	0	-0.013	-0.004	11.940	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	47	GLN	0	-0.002	0.010	16.510	0.051	0.051	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.072	0.063	16.949	0.019	0.019	0.000	0.000	0.000	0.000
47	A	49	HIS	0	-0.019	-0.010	18.962	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.868	-0.926	21.487	0.377	0.377	0.000	0.000	0.000	0.000
49	A	51	ILE	0	-0.015	0.003	15.231	0.000	0.000	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.007	-0.012	18.688	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	53	SER	0	0.018	0.010	19.783	-0.045	-0.045	0.000	0.000	0.000	0.000
52	A	54	PHE	0	0.010	-0.004	17.712	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.015	0.001	15.085	0.003	0.003	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.048	0.013	19.170	-0.038	-0.038	0.000	0.000	0.000	0.000
55	A	57	SER	0	-0.058	-0.032	22.394	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.836	0.926	19.495	-0.443	-0.443	0.000	0.000	0.000	0.000
57	A	59	MET	0	-0.027	-0.012	18.763	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.898	-0.943	22.474	0.073	0.073	0.000	0.000	0.000	0.000
59	A	61	ASN	0	-0.061	-0.032	25.860	-0.023	-0.023	0.000	0.000	0.000	0.000
60	A	62	VAL	0	-0.011	0.004	20.639	-0.026	-0.026	0.000	0.000	0.000	0.000
61	A	63	ASN	0	0.055	0.014	24.101	0.034	0.034	0.000	0.000	0.000	0.000
62	A	64	LEU	0	0.014	-0.001	21.410	-0.027	-0.027	0.000	0.000	0.000	0.000
63	A	65	ASP	-1	-0.835	-0.922	21.698	-0.233	-0.233	0.000	0.000	0.000	0.000
64	A	66	ASP	-1	-0.868	-0.934	22.044	-0.252	-0.252	0.000	0.000	0.000	0.000
65	A	67	TYR	0	-0.064	-0.036	16.068	-0.070	-0.070	0.000	0.000	0.000	0.000
66	A	68	PRO	0	-0.054	-0.024	18.208	0.024	0.024	0.000	0.000	0.000	0.000
67	A	69	ASP	-1	-0.771	-0.864	14.575	-0.831	-0.831	0.000	0.000	0.000	0.000
68	A	70	ASP	-1	-0.850	-0.925	12.564	-1.365	-1.365	0.000	0.000	0.000	0.000
69	A	71	SER	0	-0.056	-0.040	15.587	0.076	0.076	0.000	0.000	0.000	0.000
70	A	72	GLY	0	-0.020	-0.032	18.089	0.092	0.092	0.000	0.000	0.000	0.000
71	A	73	TRP	0	-0.053	-0.036	17.901	0.084	0.084	0.000	0.000	0.000	0.000
72	A	74	THR	0	0.043	0.016	17.970	-0.038	-0.038	0.000	0.000	0.000	0.000
73	A	75	PRO	0	0.060	0.010	17.265	0.003	0.003	0.000	0.000	0.000	0.000
74	A	76	PHE	0	0.077	0.040	19.155	0.030	0.030	0.000	0.000	0.000	0.000
75	A	77	HIS	0	0.025	0.022	21.110	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	78	ILE	0	-0.028	0.001	15.695	0.010	0.010	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.037	0.020	19.996	0.022	0.022	0.000	0.000	0.000	0.000
78	A	80	CYS	0	-0.055	-0.024	22.478	0.020	0.020	0.000	0.000	0.000	0.000
79	A	81	SER	0	0.008	0.004	21.654	0.010	0.010	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.041	-0.017	19.644	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.015	0.010	22.752	0.019	0.019	0.000	0.000	0.000	0.000
82	A	84	ASN	0	-0.030	-0.028	24.387	0.006	0.006	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.039	0.003	26.315	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	86	GLU	-1	-0.900	-0.938	27.696	0.150	0.150	0.000	0.000	0.000	0.000
85	A	87	VAL	0	0.023	0.002	21.779	0.003	0.003	0.000	0.000	0.000	0.000
86	A	88	VAL	0	-0.027	-0.018	25.190	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.944	0.965	26.764	-0.034	-0.034	0.000	0.000	0.000	0.000
88	A	90	SER	0	-0.023	0.001	25.554	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	91	LEU	0	-0.019	-0.017	21.454	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	92	TYR	0	-0.002	-0.021	25.609	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	93	ASP	-1	-0.915	-0.955	29.071	0.010	0.010	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.861	0.948	25.232	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.007	-0.009	30.034	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	96	LEU	0	-0.035	-0.009	27.464	-0.015	-0.015	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.829	0.914	28.361	0.008	0.008	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.007	0.011	26.176	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.821	-0.917	28.294	-0.149	-0.149	0.000	0.000	0.000	0.000
98	A	100	LEU	0	-0.041	-0.021	28.965	-0.019	-0.019	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.067	-0.049	30.602	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.892	0.970	23.437	0.310	0.310	0.000	0.000	0.000	0.000
101	A	103	ILE	0	-0.032	-0.008	27.273	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	104	THR	0	-0.021	0.000	22.426	-0.026	-0.026	0.000	0.000	0.000	0.000
103	A	105	ASN	0	0.025	-0.002	19.831	0.073	0.073	0.000	0.000	0.000	0.000
104	A	106	GLN	0	-0.009	-0.007	22.253	0.017	0.017	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.011	0.001	25.636	0.027	0.027	0.000	0.000	0.000	0.000
106	A	108	VAL	0	-0.050	-0.018	25.126	0.026	0.026	0.000	0.000	0.000	0.000
107	A	109	THR	0	0.090	0.025	26.530	-0.016	-0.016	0.000	0.000	0.000	0.000
108	A	110	CYS	0	0.024	-0.002	26.254	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	111	LEU	0	0.055	0.042	27.390	0.009	0.009	0.000	0.000	0.000	0.000
110	A	112	HIS	0	-0.024	0.000	28.874	0.004	0.004	0.000	0.000	0.000	0.000
111	A	113	LEU	0	-0.052	-0.017	23.093	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	114	ALA	0	0.020	0.017	26.928	0.006	0.006	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.009	-0.010	28.778	0.011	0.011	0.000	0.000	0.000	0.000
114	A	116	GLY	0	-0.028	-0.015	29.276	0.007	0.007	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.862	0.937	22.181	0.198	0.198	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.864	0.929	28.641	0.104	0.104	0.000	0.000	0.000	0.000
117	A	119	TRP	0	0.012	0.022	25.461	0.024	0.024	0.000	0.000	0.000	0.000
118	A	120	PHE	0	0.010	0.001	31.177	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.789	-0.910	33.346	-0.024	-0.024	0.000	0.000	0.000	0.000
120	A	122	VAL	0	0.000	0.012	28.254	0.003	0.003	0.000	0.000	0.000	0.000
121	A	123	SER	0	-0.016	-0.031	31.570	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	124	GLN	0	-0.086	-0.053	33.428	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	125	PHE	0	0.032	0.026	31.481	0.000	0.000	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.002	-0.002	29.375	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.007	-0.002	33.585	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	128	GLU	-1	-0.910	-0.951	37.136	-0.019	-0.019	0.000	0.000	0.000	0.000
127	A	129	ASN	0	-0.044	-0.010	34.937	0.009	0.009	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.008	0.010	36.619	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	131	ALA	0	-0.035	-0.015	33.347	-0.009	-0.009	0.000	0.000	0.000	0.000
130	A	132	SER	0	-0.001	-0.008	35.126	0.006	0.006	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.014	0.002	35.687	-0.012	-0.012	0.000	0.000	0.000	0.000
132	A	134	ARG	1	0.827	0.911	37.602	0.100	0.100	0.000	0.000	0.000	0.000
133	A	135	ILE	0	0.042	0.034	32.624	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.889	0.955	34.985	0.164	0.164	0.000	0.000	0.000	0.000
135	A	137	ASP	-1	-0.751	-0.861	29.869	-0.262	-0.262	0.000	0.000	0.000	0.000
136	A	138	LYS	1	0.915	0.957	26.001	0.433	0.433	0.000	0.000	0.000	0.000
137	A	139	PHE	0	-0.003	-0.008	28.280	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	140	ASN	0	-0.039	-0.020	33.492	0.006	0.006	0.000	0.000	0.000	0.000
139	A	141	GLN	0	-0.024	-0.003	33.592	0.011	0.011	0.000	0.000	0.000	0.000
140	A	142	ILE	0	-0.001	0.013	34.382	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	143	PRO	0	0.004	-0.013	33.047	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	144	LEU	0	0.048	0.028	34.709	0.003	0.003	0.000	0.000	0.000	0.000
143	A	145	HIS	0	0.042	0.017	35.875	0.004	0.004	0.000	0.000	0.000	0.000
144	A	146	ARG	1	0.894	0.946	27.802	0.248	0.248	0.000	0.000	0.000	0.000
145	A	147	ALA	0	0.011	-0.001	34.151	0.004	0.004	0.000	0.000	0.000	0.000
146	A	148	ALA	0	-0.016	-0.002	36.307	0.008	0.008	0.000	0.000	0.000	0.000
147	A	149	SER	0	0.022	0.025	34.470	0.002	0.002	0.000	0.000	0.000	0.000
148	A	150	VAL	0	-0.008	-0.008	31.781	0.004	0.004	0.000	0.000	0.000	0.000
149	A	151	GLY	0	0.073	0.039	34.966	0.011	0.011	0.000	0.000	0.000	0.000
150	A	152	SER	0	-0.091	-0.049	36.232	0.014	0.014	0.000	0.000	0.000	0.000
151	A	153	LEU	0	0.089	0.037	38.364	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	154	LYS	1	0.870	0.953	37.707	0.026	0.026	0.000	0.000	0.000	0.000
153	A	155	LEU	0	0.011	-0.002	34.852	0.002	0.002	0.000	0.000	0.000	0.000
154	A	156	ILE	0	0.029	0.024	38.476	-0.004	-0.004	0.000	0.000	0.000	0.000
155	A	157	GLU	-1	-0.765	-0.837	41.353	-0.050	-0.050	0.000	0.000	0.000	0.000
156	A	158	LEU	0	-0.049	-0.003	37.138	0.001	0.001	0.000	0.000	0.000	0.000
157	A	159	LEU	0	0.003	-0.007	36.328	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	160	CYS	0	-0.023	-0.005	40.459	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	161	GLY	0	0.051	0.039	44.110	0.002	0.002	0.000	0.000	0.000	0.000
160	A	162	LEU	0	-0.024	-0.005	40.670	0.002	0.002	0.000	0.000	0.000	0.000
161	A	163	GLY	0	-0.008	-0.021	41.052	0.001	0.001	0.000	0.000	0.000	0.000
162	A	164	LYS	1	0.835	0.924	41.903	0.052	0.052	0.000	0.000	0.000	0.000
163	A	165	SER	0	0.020	-0.009	41.224	-0.007	-0.007	0.000	0.000	0.000	0.000
164	A	166	ALA	0	-0.063	-0.015	42.513	0.005	0.005	0.000	0.000	0.000	0.000
165	A	167	VAL	0	0.045	0.020	42.962	-0.005	-0.005	0.000	0.000	0.000	0.000
166	A	168	ASN	0	0.016	-0.003	44.713	-0.007	-0.007	0.000	0.000	0.000	0.000
167	A	169	TRP	0	-0.045	-0.038	40.175	-0.005	-0.005	0.000	0.000	0.000	0.000
168	A	170	GLN	0	0.009	0.003	42.089	-0.002	-0.002	0.000	0.000	0.000	0.000
169	A	171	ASP	-1	-0.805	-0.894	37.149	-0.189	-0.189	0.000	0.000	0.000	0.000
170	A	172	LYS	1	0.850	0.898	33.749	0.263	0.263	0.000	0.000	0.000	0.000
171	A	173	GLN	0	-0.043	-0.011	36.066	-0.013	-0.013	0.000	0.000	0.000	0.000
172	A	174	GLY	0	0.060	0.039	40.226	0.007	0.007	0.000	0.000	0.000	0.000
173	A	175	TRP	0	-0.028	-0.020	39.359	0.008	0.008	0.000	0.000	0.000	0.000
174	A	176	THR	0	0.018	0.018	41.017	-0.006	-0.006	0.000	0.000	0.000	0.000
175	A	177	PRO	0	-0.017	-0.025	39.934	-0.002	-0.002	0.000	0.000	0.000	0.000
176	A	178	LEU	0	0.023	0.033	41.171	0.000	0.000	0.000	0.000	0.000	0.000
177	A	179	PHE	0	0.030	0.021	42.288	0.003	0.003	0.000	0.000	0.000	0.000
178	A	180	HIS	0	-0.041	-0.031	36.598	0.000	0.000	0.000	0.000	0.000	0.000
179	A	181	ALA	0	-0.022	-0.004	39.723	0.000	0.000	0.000	0.000	0.000	0.000
180	A	182	LEU	0	0.009	0.006	41.592	0.003	0.003	0.000	0.000	0.000	0.000
181	A	183	ALA	0	-0.018	0.002	40.163	0.003	0.003	0.000	0.000	0.000	0.000
182	A	184	GLU	-1	-0.957	-0.981	35.774	-0.161	-0.161	0.000	0.000	0.000	0.000
183	A	185	GLY	0	0.002	0.000	39.172	0.005	0.005	0.000	0.000	0.000	0.000
184	A	186	HIS	0	-0.028	0.007	37.366	0.018	0.018	0.000	0.000	0.000	0.000
185	A	187	GLY	0	0.039	0.005	42.777	0.000	0.000	0.000	0.000	0.000	0.000
186	A	188	ASP	-1	-0.882	-0.948	45.610	-0.058	-0.058	0.000	0.000	0.000	0.000
187	A	189	ALA	0	-0.032	-0.020	42.356	0.002	0.002	0.000	0.000	0.000	0.000
188	A	190	ALA	0	0.012	0.000	44.353	-0.002	-0.002	0.000	0.000	0.000	0.000
189	A	191	VAL	0	0.031	0.017	46.314	0.000	0.000	0.000	0.000	0.000	0.000
190	A	192	LEU	0	-0.059	-0.020	44.464	0.001	0.001	0.000	0.000	0.000	0.000
191	A	193	LEU	0	-0.030	-0.033	42.645	0.000	0.000	0.000	0.000	0.000	0.000
192	A	194	VAL	0	-0.005	0.007	47.058	-0.001	-0.001	0.000	0.000	0.000	0.000
193	A	195	GLU	-1	-0.821	-0.914	50.644	-0.056	-0.056	0.000	0.000	0.000	0.000
194	A	196	LYS	1	0.768	0.880	48.284	0.051	0.051	0.000	0.000	0.000	0.000
195	A	197	TYR	0	-0.092	-0.094	46.497	0.002	0.002	0.000	0.000	0.000	0.000
196	A	198	GLY	0	0.051	0.041	49.444	-0.004	-0.004	0.000	0.000	0.000	0.000
197	A	199	ALA	0	-0.020	-0.024	47.555	-0.004	-0.004	0.000	0.000	0.000	0.000
198	A	200	GLU	-1	-0.883	-0.937	49.334	-0.087	-0.087	0.000	0.000	0.000	0.000
199	A	201	TYR	0	-0.050	-0.058	50.169	-0.007	-0.007	0.000	0.000	0.000	0.000
200	A	202	ASP	-1	-0.837	-0.920	51.249	-0.083	-0.083	0.000	0.000	0.000	0.000
201	A	203	LEU	0	-0.026	-0.001	47.580	-0.002	-0.002	0.000	0.000	0.000	0.000
202	A	204	VAL	0	-0.036	-0.020	48.998	0.001	0.001	0.000	0.000	0.000	0.000
203	A	205	ASP	-1	-0.839	-0.908	43.805	-0.159	-0.159	0.000	0.000	0.000	0.000
204	A	206	ASN	0	-0.035	-0.026	41.719	0.009	0.009	0.000	0.000	0.000	0.000
205	A	207	LYS	1	0.861	0.926	41.126	0.171	0.171	0.000	0.000	0.000	0.000
206	A	208	GLY	0	-0.005	-0.005	47.486	0.004	0.004	0.000	0.000	0.000	0.000
207	A	209	ALA	0	-0.018	0.003	47.191	0.005	0.005	0.000	0.000	0.000	0.000
208	A	210	LYS	1	0.837	0.899	48.469	0.084	0.084	0.000	0.000	0.000	0.000
209	A	211	ALA	0	0.036	0.015	46.559	-0.003	-0.003	0.000	0.000	0.000	0.000
210	A	212	GLU	-1	-0.779	-0.873	47.013	-0.084	-0.084	0.000	0.000	0.000	0.000
211	A	213	ASP	-1	-0.883	-0.932	48.989	-0.095	-0.095	0.000	0.000	0.000	0.000
212	A	214	VAL	0	-0.060	-0.022	43.369	-0.002	-0.002	0.000	0.000	0.000	0.000
213	A	215	ALA	0	-0.010	-0.007	43.840	-0.004	-0.004	0.000	0.000	0.000	0.000
214	A	216	LEU	0	-0.026	0.008	40.669	0.001	0.001	0.000	0.000	0.000	0.000
215	A	217	ASN	0	-0.044	-0.033	43.990	0.000	0.000	0.000	0.000	0.000	0.000
216	A	218	GLU	-1	-0.754	-0.863	47.385	-0.078	-0.078	0.000	0.000	0.000	0.000
217	A	219	GLN	0	-0.104	-0.074	49.738	0.007	0.007	0.000	0.000	0.000	0.000
218	A	220	VAL	0	0.019	0.025	45.417	0.004	0.004	0.000	0.000	0.000	0.000
219	A	221	LYS	1	0.815	0.875	48.751	0.090	0.090	0.000	0.000	0.000	0.000
220	A	222	LYS	1	0.939	0.971	50.921	0.059	0.059	0.000	0.000	0.000	0.000
221	A	223	PHE	0	-0.014	-0.003	49.547	0.002	0.002	0.000	0.000	0.000	0.000
222	A	224	PHE	0	0.054	0.018	49.705	0.002	0.002	0.000	0.000	0.000	0.000
223	A	225	LEU	0	0.005	-0.005	51.742	0.002	0.002	0.000	0.000	0.000	0.000
224	A	226	ASN	0	-0.128	-0.060	55.158	0.005	0.005	0.000	0.000	0.000	0.000
225	A	227	ASN	0	-0.109	-0.062	53.273	0.006	0.006	0.000	0.000	0.000	0.000
226	A	228	VAL	0	-0.009	0.000	52.168	-0.001	-0.001	0.000	0.000	0.000	0.000
227	A	229	VAL	0	-0.026	0.002	55.384	0.002	0.002	0.000	0.000	0.000	0.000
228	A	230	ASP	-1	-0.934	-0.938	57.440	-0.057	-0.057	0.000	0.000	0.000	0.000
229	A	231	ALA	0	-0.025	-0.019	57.916	0.001	0.001	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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