FMO DATABASE

FMODB ID: 5JRQZ

Calculation Name: 3F5D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3F5D

Chain ID: A

ChEMBL ID:

UniProt ID: P96658

Base Structure: X-ray

Registration Date: 2023-09-22

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	193
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2209800.826496
FMO2-HF: Nuclear repulsion	2132824.906795
FMO2-HF: Total energy	-76975.919701
FMO2-MP2: Total energy	-77201.057023

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:LEU)

Summations of interaction energy for fragment #1(A:3: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.
-11.211	-3.019	4.489	-4.604	-8.079	-0.041

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.042 / 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	5	LYS	1	0.944	0.962	3.249	-1.891	0.605	0.071	-1.034	-1.534	0.000
4	A	6	ALA	0	0.031	0.010	5.095	0.236	0.299	-0.001	-0.004	-0.058	0.000
5	A	7	LEU	0	-0.016	-0.017	8.479	-0.059	-0.059	0.000	0.000	0.000	0.000
6	A	8	PHE	0	0.011	-0.009	11.165	0.066	0.066	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.030	-0.022	14.271	0.003	0.003	0.000	0.000	0.000	0.000
8	A	10	ILE	0	0.010	0.016	17.348	0.017	0.017	0.000	0.000	0.000	0.000
9	A	11	LEU	0	-0.004	0.015	20.005	0.001	0.001	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.794	-0.919	23.444	-0.118	-0.118	0.000	0.000	0.000	0.000
11	A	13	GLN	0	-0.019	0.027	26.120	0.010	0.010	0.000	0.000	0.000	0.000
12	A	14	TYR	0	-0.030	-0.022	20.754	0.006	0.006	0.000	0.000	0.000	0.000
13	A	15	ALA	0	0.024	0.005	24.462	0.000	0.000	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.787	-0.866	22.624	-0.144	-0.144	0.000	0.000	0.000	0.000
15	A	17	TRP	0	-0.012	-0.035	21.644	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.782	-0.907	21.968	-0.099	-0.099	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.035	0.010	17.695	0.007	0.007	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.008	0.006	16.235	-0.034	-0.034	0.000	0.000	0.000	0.000
19	A	21	TYR	0	0.021	0.012	16.432	-0.023	-0.023	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.010	0.014	13.168	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	23	ALA	0	0.010	0.003	11.921	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	24	SER	0	-0.004	-0.014	11.029	-0.089	-0.089	0.000	0.000	0.000	0.000
23	A	25	ALA	0	-0.015	-0.004	11.653	-0.046	-0.046	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.012	-0.016	8.243	0.005	0.005	0.000	0.000	0.000	0.000
25	A	27	ASN	0	0.029	0.000	6.718	-0.363	-0.363	0.000	0.000	0.000	0.000
26	A	28	GLN	0	-0.053	-0.017	7.008	-0.145	-0.145	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.775	0.891	5.878	-0.312	-0.312	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.895	-0.941	4.640	-1.762	-1.618	-0.001	-0.017	-0.126	0.000
29	A	31	ASP	-1	-0.829	-0.904	2.588	-1.859	-0.166	1.553	-1.106	-2.141	-0.011
30	A	32	TRP	0	-0.025	-0.026	2.616	-1.994	-0.289	2.606	-1.748	-2.562	-0.024
31	A	33	SER	0	0.050	0.033	2.841	-3.299	-1.251	0.261	-0.684	-1.625	-0.006
32	A	34	VAL	0	-0.039	-0.008	4.162	0.497	0.540	0.000	-0.011	-0.033	0.000
33	A	35	HIS	0	0.002	0.005	5.768	-0.140	-0.140	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.008	0.001	10.010	0.068	0.068	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.007	-0.009	13.722	0.006	0.006	0.000	0.000	0.000	0.000
36	A	38	SER	0	0.010	-0.026	15.802	0.020	0.020	0.000	0.000	0.000	0.000
37	A	39	LEU	0	-0.064	-0.034	19.562	0.003	0.003	0.000	0.000	0.000	0.000
38	A	40	ASP	-1	-0.874	-0.932	22.385	-0.111	-0.111	0.000	0.000	0.000	0.000
39	A	41	PRO	0	-0.025	-0.027	20.205	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	42	ILE	0	-0.005	-0.017	20.374	-0.015	-0.015	0.000	0.000	0.000	0.000
41	A	43	VAL	0	-0.008	0.027	20.944	0.012	0.012	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.012	-0.020	23.193	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.039	-0.026	23.446	0.005	0.005	0.000	0.000	0.000	0.000
44	A	46	ILE	0	0.019	-0.006	25.217	0.006	0.006	0.000	0.000	0.000	0.000
45	A	47	GLY	0	-0.052	-0.030	26.962	0.007	0.007	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.037	-0.016	27.826	0.003	0.003	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.066	-0.030	22.162	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.935	0.973	24.052	0.124	0.124	0.000	0.000	0.000	0.000
49	A	51	THR	0	0.028	0.020	17.734	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	52	SER	0	-0.006	-0.007	17.863	0.022	0.022	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.042	-0.024	16.305	-0.030	-0.030	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.858	-0.903	11.563	-0.473	-0.473	0.000	0.000	0.000	0.000
53	A	55	TYR	0	-0.034	-0.028	7.967	0.046	0.046	0.000	0.000	0.000	0.000
54	A	56	ILE	0	0.026	0.033	14.790	0.005	0.005	0.000	0.000	0.000	0.000
55	A	57	ILE	0	-0.001	-0.021	17.815	0.005	0.005	0.000	0.000	0.000	0.000
56	A	58	GLY	0	-0.116	-0.067	18.192	0.016	0.016	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.070	-0.036	16.670	0.011	0.011	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.848	-0.899	13.175	-0.183	-0.183	0.000	0.000	0.000	0.000
59	A	61	PRO	0	-0.043	-0.015	8.805	0.025	0.025	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.047	0.016	11.324	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.078	-0.057	10.268	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	64	PHE	0	-0.020	-0.001	7.956	-0.052	-0.052	0.000	0.000	0.000	0.000
63	A	65	ASN	0	0.026	0.007	6.176	-0.442	-0.442	0.000	0.000	0.000	0.000
64	A	66	LEU	0	0.046	0.041	9.076	0.109	0.109	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.008	0.010	11.100	-0.077	-0.077	0.000	0.000	0.000	0.000
66	A	68	VAL	0	0.001	0.008	13.166	0.044	0.044	0.000	0.000	0.000	0.000
67	A	69	MET	0	-0.046	-0.013	15.648	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	70	ILE	0	0.024	0.011	18.107	0.015	0.015	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.003	0.007	20.676	0.006	0.006	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.001	-0.008	24.237	-0.013	-0.013	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.914	-0.943	26.956	-0.072	-0.072	0.000	0.000	0.000	0.000
72	A	74	SER	0	-0.028	-0.049	27.133	0.007	0.007	0.000	0.000	0.000	0.000
73	A	75	TRP	0	-0.023	-0.030	21.459	0.004	0.004	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.063	-0.007	28.183	0.006	0.006	0.000	0.000	0.000	0.000
75	A	77	ASN	0	0.011	-0.015	27.793	0.003	0.003	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.893	-0.940	29.409	-0.049	-0.049	0.000	0.000	0.000	0.000
77	A	79	ASN	0	0.012	0.002	26.286	0.000	0.000	0.000	0.000	0.000	0.000
78	A	80	LYS	1	1.024	1.000	25.803	0.064	0.064	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.873	0.933	23.569	0.081	0.081	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.104	0.069	21.767	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.009	0.014	22.518	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	84	HIS	0	-0.027	-0.018	21.714	0.006	0.006	0.000	0.000	0.000	0.000
83	A	85	PHE	0	0.029	0.037	14.756	0.009	0.009	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.055	0.024	18.892	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.965	0.980	20.191	0.039	0.039	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.023	-0.034	18.268	0.013	0.013	0.000	0.000	0.000	0.000
87	A	89	ALA	0	-0.009	-0.009	16.377	0.008	0.008	0.000	0.000	0.000	0.000
88	A	90	PHE	0	0.055	0.011	17.668	0.013	0.013	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.062	-0.025	20.490	0.011	0.011	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.828	0.934	14.803	0.123	0.123	0.000	0.000	0.000	0.000
91	A	93	ASN	0	-0.026	-0.019	16.632	0.007	0.007	0.000	0.000	0.000	0.000
92	A	94	ILE	0	-0.033	0.009	12.965	0.025	0.025	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.018	0.005	12.956	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	96	ILE	0	0.010	-0.003	14.668	-0.049	-0.049	0.000	0.000	0.000	0.000
95	A	97	ALA	0	0.008	0.013	17.036	0.025	0.025	0.000	0.000	0.000	0.000
96	A	98	ALA	0	-0.032	-0.024	18.504	-0.023	-0.023	0.000	0.000	0.000	0.000
97	A	99	ILE	0	-0.001	0.004	21.334	0.014	0.014	0.000	0.000	0.000	0.000
98	A	100	CYS	0	-0.005	0.011	23.567	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.031	0.005	26.876	0.005	0.005	0.000	0.000	0.000	0.000
100	A	102	ALA	0	0.007	0.017	22.564	0.004	0.004	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.022	-0.016	24.579	0.006	0.006	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.797	-0.888	26.367	-0.043	-0.043	0.000	0.000	0.000	0.000
103	A	105	PHE	0	-0.025	-0.009	24.797	0.004	0.004	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.012	-0.006	22.655	0.005	0.005	0.000	0.000	0.000	0.000
105	A	107	ALA	0	0.026	0.015	26.664	0.006	0.006	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.935	0.966	30.263	0.045	0.045	0.000	0.000	0.000	0.000
107	A	109	ASN	0	-0.120	-0.085	27.901	0.003	0.003	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.004	0.008	29.191	0.001	0.001	0.000	0.000	0.000	0.000
109	A	111	LEU	0	-0.065	-0.028	23.795	0.004	0.004	0.000	0.000	0.000	0.000
110	A	112	LEU	0	0.000	0.011	26.333	0.002	0.002	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.011	-0.021	28.608	0.003	0.003	0.000	0.000	0.000	0.000
112	A	114	ASN	0	0.005	-0.006	28.429	0.005	0.005	0.000	0.000	0.000	0.000
113	A	115	HIS	0	0.003	0.010	23.358	0.004	0.004	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.031	0.005	28.176	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	117	HIS	0	-0.039	-0.025	27.589	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	118	THR	0	0.029	0.017	27.745	0.001	0.001	0.000	0.000	0.000	0.000
117	A	119	GLY	0	0.042	-0.002	28.483	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	120	ASN	0	0.038	0.018	29.584	0.003	0.003	0.000	0.000	0.000	0.000
119	A	121	PHE	0	0.040	0.003	31.855	0.003	0.003	0.000	0.000	0.000	0.000
120	A	122	VAL	0	0.071	0.049	35.086	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	123	TYR	0	0.001	-0.007	35.992	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.040	-0.005	33.736	0.001	0.001	0.000	0.000	0.000	0.000
123	A	125	TRP	0	-0.022	-0.054	30.443	0.001	0.001	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.845	0.920	36.400	0.021	0.021	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.836	-0.891	39.613	-0.017	-0.017	0.000	0.000	0.000	0.000
126	A	128	TYR	0	-0.038	-0.009	32.566	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	LYS	1	0.974	0.973	37.122	0.021	0.021	0.000	0.000	0.000	0.000
128	A	130	GLN	0	-0.080	-0.058	32.280	0.005	0.005	0.000	0.000	0.000	0.000
129	A	131	TYR	0	0.026	0.021	32.276	0.001	0.001	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.847	0.918	34.506	0.009	0.009	0.000	0.000	0.000	0.000
131	A	133	PRO	0	-0.016	0.020	33.288	0.002	0.002	0.000	0.000	0.000	0.000
132	A	134	ILE	0	-0.035	0.009	31.662	0.001	0.001	0.000	0.000	0.000	0.000
133	A	135	SER	0	-0.042	-0.019	31.841	0.003	0.003	0.000	0.000	0.000	0.000
134	A	136	SER	0	0.011	-0.004	33.738	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	137	PHE	0	-0.020	0.011	32.105	0.002	0.002	0.000	0.000	0.000	0.000
136	A	138	VAL	0	-0.003	-0.017	31.599	0.002	0.002	0.000	0.000	0.000	0.000
137	A	139	GLU	-1	-0.932	-0.962	32.674	-0.011	-0.011	0.000	0.000	0.000	0.000
138	A	140	LYS	1	0.909	0.948	30.868	-0.009	-0.009	0.000	0.000	0.000	0.000
139	A	141	GLN	0	-0.007	0.018	28.080	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	ALA	0	0.023	0.002	24.442	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	143	VAL	0	-0.040	-0.009	25.744	0.009	0.009	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.975	0.986	19.024	-0.126	-0.126	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.787	-0.861	23.505	0.051	0.051	0.000	0.000	0.000	0.000
144	A	146	LYS	1	0.857	0.913	21.972	-0.060	-0.060	0.000	0.000	0.000	0.000
145	A	147	ASN	0	0.032	0.011	16.790	0.019	0.019	0.000	0.000	0.000	0.000
146	A	148	LEU	0	0.023	0.022	19.032	-0.020	-0.020	0.000	0.000	0.000	0.000
147	A	149	VAL	0	0.013	0.003	19.336	0.011	0.011	0.000	0.000	0.000	0.000
148	A	150	THR	0	-0.014	-0.002	21.535	-0.015	-0.015	0.000	0.000	0.000	0.000
149	A	151	ALA	0	0.053	0.003	24.169	0.008	0.008	0.000	0.000	0.000	0.000
150	A	152	ASN	0	0.046	0.078	25.880	-0.011	-0.011	0.000	0.000	0.000	0.000
151	A	153	GLY	0	0.073	0.000	26.714	-0.003	-0.003	0.000	0.000	0.000	0.000
152	A	154	THR	0	-0.082	-0.056	27.312	-0.004	-0.004	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.002	0.003	26.001	0.003	0.003	0.000	0.000	0.000	0.000
154	A	156	PRO	0	0.042	0.039	22.362	0.001	0.001	0.000	0.000	0.000	0.000
155	A	157	ILE	0	0.021	0.015	21.339	-0.003	-0.003	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.827	-0.931	21.833	-0.026	-0.026	0.000	0.000	0.000	0.000
157	A	159	PHE	0	-0.001	-0.006	18.879	0.012	0.012	0.000	0.000	0.000	0.000
158	A	160	THR	0	-0.013	-0.036	16.322	-0.006	-0.006	0.000	0.000	0.000	0.000
159	A	161	ASN	0	0.014	0.006	17.597	0.013	0.013	0.000	0.000	0.000	0.000
160	A	162	LEU	0	-0.015	-0.011	18.993	0.021	0.021	0.000	0.000	0.000	0.000
161	A	163	ILE	0	-0.016	-0.001	14.316	0.020	0.020	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.004	-0.010	13.087	0.021	0.021	0.000	0.000	0.000	0.000
163	A	165	GLU	-1	-0.916	-0.958	14.799	0.147	0.147	0.000	0.000	0.000	0.000
164	A	166	MET	0	-0.129	-0.043	15.841	0.037	0.037	0.000	0.000	0.000	0.000
165	A	167	ILE	0	-0.094	-0.042	10.141	-0.002	-0.002	0.000	0.000	0.000	0.000
166	A	168	ASP	-1	-0.934	-0.948	11.474	0.479	0.479	0.000	0.000	0.000	0.000
167	A	169	PHE	0	-0.051	-0.027	8.896	0.124	0.124	0.000	0.000	0.000	0.000
168	A	170	ASP	-1	-0.867	-0.921	11.766	0.324	0.324	0.000	0.000	0.000	0.000
169	A	171	THR	0	-0.018	-0.017	14.473	-0.014	-0.014	0.000	0.000	0.000	0.000
170	A	172	PRO	0	0.100	0.028	18.045	-0.026	-0.026	0.000	0.000	0.000	0.000
171	A	173	GLU	-1	-0.888	-0.943	20.672	0.140	0.140	0.000	0.000	0.000	0.000
172	A	174	ASN	0	-0.083	-0.034	17.806	-0.032	-0.032	0.000	0.000	0.000	0.000
173	A	175	ILE	0	0.023	0.010	15.979	-0.034	-0.034	0.000	0.000	0.000	0.000
174	A	176	GLU	-1	-0.932	-0.967	18.859	0.026	0.026	0.000	0.000	0.000	0.000
175	A	177	LYS	1	0.932	0.970	21.421	-0.077	-0.077	0.000	0.000	0.000	0.000
176	A	178	MET	0	0.013	0.008	14.224	-0.009	-0.009	0.000	0.000	0.000	0.000
177	A	179	MET	0	-0.015	-0.005	17.860	-0.027	-0.027	0.000	0.000	0.000	0.000
178	A	180	TYR	0	-0.024	-0.005	21.920	-0.007	-0.007	0.000	0.000	0.000	0.000
179	A	181	MET	0	-0.001	-0.001	22.052	-0.007	-0.007	0.000	0.000	0.000	0.000
180	A	182	ASN	0	-0.037	-0.022	18.811	-0.013	-0.013	0.000	0.000	0.000	0.000
181	A	183	ARG	1	0.889	0.956	23.105	0.023	0.023	0.000	0.000	0.000	0.000
182	A	184	TYR	0	-0.057	-0.037	26.369	0.001	0.001	0.000	0.000	0.000	0.000
183	A	185	GLY	0	0.043	0.043	26.976	0.000	0.000	0.000	0.000	0.000	0.000
184	A	186	PHE	0	0.036	-0.008	26.576	0.007	0.007	0.000	0.000	0.000	0.000
185	A	187	TYR	0	0.016	0.003	28.162	0.004	0.004	0.000	0.000	0.000	0.000
186	A	188	HIS	0	0.088	0.059	30.925	0.005	0.005	0.000	0.000	0.000	0.000
187	A	189	PHE	0	-0.053	-0.027	23.992	0.007	0.007	0.000	0.000	0.000	0.000
188	A	190	CYS	0	-0.016	-0.038	28.815	0.005	0.005	0.000	0.000	0.000	0.000
189	A	191	ASP	-1	-0.917	-0.921	30.472	-0.002	-0.002	0.000	0.000	0.000	0.000
190	A	192	LYS	1	0.866	0.944	29.864	-0.017	-0.017	0.000	0.000	0.000	0.000
191	A	193	TYR	0	-0.048	-0.042	26.522	0.007	0.007	0.000	0.000	0.000	0.000
192	A	194	GLY	0	-0.025	0.027	29.601	0.005	0.005	0.000	0.000	0.000	0.000
193	A	195	ASN	0	-0.033	-0.041	25.243	-0.006	-0.006	0.000	0.000	0.000	0.000

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