FMO DATABASE

FMODB ID: YV972

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	OptHSide
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
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2211137.913634
FMO2-HF: Nuclear repulsion	2134160.923253
FMO2-HF: Total energy	-76976.990381
FMO2-MP2: Total energy	-77202.063541

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.
-10.901	-3.279	5.942	-4.732	-8.831	-0.048

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 : -0.053 / 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	0.969	0.975	3.237	-2.030	0.446	0.064	-1.020	-1.519	0.000
4	A	6	ALA	0	0.030	0.009	5.110	0.310	0.372	-0.001	-0.004	-0.056	0.000
5	A	7	LEU	0	-0.015	-0.015	8.492	-0.092	-0.092	0.000	0.000	0.000	0.000
6	A	8	PHE	0	0.008	-0.012	11.195	0.085	0.085	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.031	-0.023	14.298	-0.002	-0.002	0.000	0.000	0.000	0.000
8	A	10	ILE	0	0.010	0.017	17.380	0.021	0.021	0.000	0.000	0.000	0.000
9	A	11	LEU	0	0.017	0.023	20.041	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.759	-0.886	23.483	-0.136	-0.136	0.000	0.000	0.000	0.000
11	A	13	GLN	0	-0.052	-0.011	26.074	0.011	0.011	0.000	0.000	0.000	0.000
12	A	14	TYR	0	-0.014	-0.012	21.000	0.006	0.006	0.000	0.000	0.000	0.000
13	A	15	ALA	0	0.026	0.002	24.524	0.000	0.000	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.794	-0.871	22.708	-0.160	-0.160	0.000	0.000	0.000	0.000
15	A	17	TRP	0	-0.007	-0.028	21.714	-0.020	-0.020	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.796	-0.914	22.048	-0.104	-0.104	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.037	0.010	17.761	0.009	0.009	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.011	0.006	16.293	-0.036	-0.036	0.000	0.000	0.000	0.000
19	A	21	TYR	0	0.016	0.013	16.474	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.005	0.012	13.220	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	23	ALA	0	0.011	0.004	11.976	-0.042	-0.042	0.000	0.000	0.000	0.000
22	A	24	SER	0	0.000	-0.012	11.072	-0.093	-0.093	0.000	0.000	0.000	0.000
23	A	25	ALA	0	-0.013	0.009	11.663	-0.047	-0.047	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.008	-0.014	8.264	0.010	0.010	0.000	0.000	0.000	0.000
25	A	27	ASN	0	0.031	0.002	6.748	-0.339	-0.339	0.000	0.000	0.000	0.000
26	A	28	GLN	0	-0.059	-0.031	7.019	-0.150	-0.150	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.774	0.891	6.067	-0.357	-0.357	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.883	-0.933	4.620	-1.607	-1.475	-0.001	-0.018	-0.112	0.000
29	A	31	ASP	-1	-0.834	-0.904	2.582	-1.574	-0.078	1.782	-1.051	-2.228	-0.011
30	A	32	TRP	0	0.005	-0.015	2.629	-1.381	-0.061	2.801	-1.542	-2.580	-0.023
31	A	33	SER	0	0.011	0.018	2.380	-3.846	-1.786	1.297	-1.058	-2.299	-0.014
32	A	34	VAL	0	-0.022	-0.007	4.251	0.464	0.540	0.000	-0.039	-0.037	0.000
33	A	35	HIS	0	-0.038	-0.013	5.909	-0.231	-0.231	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.018	-0.024	9.961	0.094	0.094	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.009	-0.016	13.677	0.002	0.002	0.000	0.000	0.000	0.000
36	A	38	SER	0	0.010	-0.024	15.772	0.027	0.027	0.000	0.000	0.000	0.000
37	A	39	LEU	0	-0.067	-0.036	19.534	0.003	0.003	0.000	0.000	0.000	0.000
38	A	40	ASP	-1	-0.889	-0.940	22.386	-0.128	-0.128	0.000	0.000	0.000	0.000
39	A	41	PRO	0	0.006	-0.021	20.199	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	42	ILE	0	-0.035	-0.024	20.358	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	43	VAL	0	-0.016	0.019	20.848	0.015	0.015	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.018	-0.025	23.149	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.050	-0.030	23.556	0.006	0.006	0.000	0.000	0.000	0.000
44	A	46	ILE	0	0.016	-0.010	25.313	0.006	0.006	0.000	0.000	0.000	0.000
45	A	47	GLY	0	-0.045	-0.022	27.054	0.008	0.008	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.027	-0.009	27.918	0.004	0.004	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.056	-0.031	22.812	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.909	0.962	24.008	0.145	0.145	0.000	0.000	0.000	0.000
49	A	51	THR	0	0.035	0.019	17.724	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	52	SER	0	-0.009	-0.006	17.726	0.026	0.026	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.043	-0.025	16.355	-0.037	-0.037	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.821	-0.864	10.658	-0.621	-0.621	0.000	0.000	0.000	0.000
53	A	55	TYR	0	-0.017	-0.026	7.888	0.059	0.059	0.000	0.000	0.000	0.000
54	A	56	ILE	0	0.036	0.035	14.789	0.011	0.011	0.000	0.000	0.000	0.000
55	A	57	ILE	0	-0.008	-0.019	17.821	0.005	0.005	0.000	0.000	0.000	0.000
56	A	58	GLY	0	-0.107	-0.060	18.190	0.018	0.018	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.070	-0.038	16.695	0.014	0.014	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.841	-0.900	13.167	-0.213	-0.213	0.000	0.000	0.000	0.000
59	A	61	PRO	0	-0.031	-0.009	8.701	0.037	0.037	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.045	0.015	11.335	0.003	0.003	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.062	-0.043	10.553	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	64	PHE	0	-0.013	0.001	7.981	-0.062	-0.062	0.000	0.000	0.000	0.000
63	A	65	ASN	0	0.012	0.000	6.268	-0.296	-0.296	0.000	0.000	0.000	0.000
64	A	66	LEU	0	0.033	0.035	9.065	0.109	0.109	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.015	0.009	11.110	-0.094	-0.094	0.000	0.000	0.000	0.000
66	A	68	VAL	0	-0.001	0.006	13.080	0.049	0.049	0.000	0.000	0.000	0.000
67	A	69	MET	0	-0.042	-0.008	15.658	-0.024	-0.024	0.000	0.000	0.000	0.000
68	A	70	ILE	0	0.019	0.004	18.017	0.018	0.018	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.023	0.021	20.694	0.005	0.005	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.006	-0.006	24.261	-0.015	-0.015	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.922	-0.948	26.982	-0.077	-0.077	0.000	0.000	0.000	0.000
72	A	74	SER	0	-0.012	-0.024	27.203	0.008	0.008	0.000	0.000	0.000	0.000
73	A	75	TRP	0	-0.028	-0.033	21.429	0.005	0.005	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.038	0.007	28.212	0.007	0.007	0.000	0.000	0.000	0.000
75	A	77	ASN	0	-0.023	-0.034	27.823	0.002	0.002	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.853	-0.925	29.441	-0.050	-0.050	0.000	0.000	0.000	0.000
77	A	79	ASN	0	0.017	0.015	26.718	0.004	0.004	0.000	0.000	0.000	0.000
78	A	80	LYS	1	1.004	0.995	26.166	0.058	0.058	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.917	0.954	23.528	0.095	0.095	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.088	0.053	21.668	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.009	0.013	22.550	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	84	HIS	0	-0.019	-0.015	21.566	0.007	0.007	0.000	0.000	0.000	0.000
83	A	85	PHE	0	0.018	0.032	14.796	0.013	0.013	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.062	0.023	18.917	0.002	0.002	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.909	0.960	20.206	0.034	0.034	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.015	-0.033	18.641	0.015	0.015	0.000	0.000	0.000	0.000
87	A	89	ALA	0	-0.021	-0.009	16.332	0.014	0.014	0.000	0.000	0.000	0.000
88	A	90	PHE	0	0.062	0.014	17.679	0.018	0.018	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.050	-0.017	20.492	0.013	0.013	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.815	0.918	14.914	0.101	0.101	0.000	0.000	0.000	0.000
91	A	93	ASN	0	-0.029	-0.017	16.722	0.013	0.013	0.000	0.000	0.000	0.000
92	A	94	ILE	0	-0.020	0.008	12.748	0.033	0.033	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.009	0.000	12.979	-0.021	-0.021	0.000	0.000	0.000	0.000
94	A	96	ILE	0	0.004	-0.002	14.660	-0.052	-0.052	0.000	0.000	0.000	0.000
95	A	97	ALA	0	0.007	0.011	16.965	0.025	0.025	0.000	0.000	0.000	0.000
96	A	98	ALA	0	-0.030	-0.023	18.499	-0.026	-0.026	0.000	0.000	0.000	0.000
97	A	99	ILE	0	-0.003	0.004	21.093	0.015	0.015	0.000	0.000	0.000	0.000
98	A	100	CYS	0	-0.001	0.006	23.571	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.024	0.008	26.885	0.006	0.006	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.009	0.009	22.565	0.005	0.005	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.006	-0.011	24.595	0.008	0.008	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.799	-0.888	26.375	-0.042	-0.042	0.000	0.000	0.000	0.000
103	A	105	PHE	0	-0.013	-0.007	25.161	0.006	0.006	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.009	-0.012	22.594	0.006	0.006	0.000	0.000	0.000	0.000
105	A	107	ALA	0	0.024	0.015	26.675	0.007	0.007	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.892	0.944	30.270	0.052	0.052	0.000	0.000	0.000	0.000
107	A	109	ASN	0	-0.109	-0.064	27.952	0.005	0.005	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.028	-0.002	29.203	0.002	0.002	0.000	0.000	0.000	0.000
109	A	111	LEU	0	-0.090	-0.038	23.903	0.005	0.005	0.000	0.000	0.000	0.000
110	A	112	LEU	0	0.014	0.017	26.210	0.004	0.004	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.022	-0.026	28.605	0.003	0.003	0.000	0.000	0.000	0.000
112	A	114	ASN	0	0.010	0.000	28.392	0.004	0.004	0.000	0.000	0.000	0.000
113	A	115	HIS	0	-0.019	-0.005	23.081	0.008	0.008	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.006	0.001	28.160	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	117	HIS	0	-0.017	-0.007	27.572	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	118	THR	0	0.027	0.018	27.715	0.000	0.000	0.000	0.000	0.000	0.000
117	A	119	GLY	0	0.043	-0.003	28.477	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	120	ASN	0	0.021	0.011	29.551	0.002	0.002	0.000	0.000	0.000	0.000
119	A	121	PHE	0	0.046	0.006	31.857	0.003	0.003	0.000	0.000	0.000	0.000
120	A	122	VAL	0	0.066	0.046	35.088	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	123	TYR	0	0.001	-0.008	35.993	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.034	0.000	33.827	0.001	0.001	0.000	0.000	0.000	0.000
123	A	125	TRP	0	-0.025	-0.058	30.107	0.001	0.001	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.839	0.913	36.409	0.019	0.019	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.834	-0.884	39.644	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	128	TYR	0	-0.021	0.000	32.557	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	LYS	1	0.979	0.979	37.273	0.019	0.019	0.000	0.000	0.000	0.000
128	A	130	GLN	0	-0.062	-0.035	32.240	0.006	0.006	0.000	0.000	0.000	0.000
129	A	131	TYR	0	0.024	0.019	32.177	0.002	0.002	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.827	0.895	34.517	0.004	0.004	0.000	0.000	0.000	0.000
131	A	133	PRO	0	-0.042	0.008	33.085	0.003	0.003	0.000	0.000	0.000	0.000
132	A	134	ILE	0	-0.007	0.018	31.931	0.000	0.000	0.000	0.000	0.000	0.000
133	A	135	SER	0	-0.030	-0.009	31.438	0.002	0.002	0.000	0.000	0.000	0.000
134	A	136	SER	0	0.003	-0.008	33.725	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	137	PHE	0	-0.016	0.009	32.190	0.003	0.003	0.000	0.000	0.000	0.000
136	A	138	VAL	0	-0.014	-0.024	31.600	0.002	0.002	0.000	0.000	0.000	0.000
137	A	139	GLU	-1	-0.920	-0.952	32.661	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	140	LYS	1	0.900	0.943	30.913	-0.015	-0.015	0.000	0.000	0.000	0.000
139	A	141	GLN	0	-0.003	0.013	28.181	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	ALA	0	0.025	0.002	24.416	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	143	VAL	0	-0.047	-0.013	25.727	0.009	0.009	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.984	1.005	18.752	-0.164	-0.164	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.772	-0.862	23.500	0.071	0.071	0.000	0.000	0.000	0.000
144	A	146	LYS	1	0.847	0.905	21.966	-0.078	-0.078	0.000	0.000	0.000	0.000
145	A	147	ASN	0	0.018	0.008	16.871	0.022	0.022	0.000	0.000	0.000	0.000
146	A	148	LEU	0	0.022	0.018	19.016	-0.021	-0.021	0.000	0.000	0.000	0.000
147	A	149	VAL	0	0.007	0.000	19.375	0.010	0.010	0.000	0.000	0.000	0.000
148	A	150	THR	0	-0.009	-0.003	21.527	-0.017	-0.017	0.000	0.000	0.000	0.000
149	A	151	ALA	0	0.053	0.008	24.136	0.009	0.009	0.000	0.000	0.000	0.000
150	A	152	ASN	0	0.031	0.051	25.873	-0.013	-0.013	0.000	0.000	0.000	0.000
151	A	153	GLY	0	0.075	0.011	26.754	-0.003	-0.003	0.000	0.000	0.000	0.000
152	A	154	THR	0	-0.063	-0.035	27.370	-0.006	-0.006	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.006	0.004	26.243	0.003	0.003	0.000	0.000	0.000	0.000
154	A	156	PRO	0	0.045	0.037	22.396	0.003	0.003	0.000	0.000	0.000	0.000
155	A	157	ILE	0	0.015	0.010	21.343	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.766	-0.871	21.824	-0.023	-0.023	0.000	0.000	0.000	0.000
157	A	159	PHE	0	0.009	0.000	18.926	0.015	0.015	0.000	0.000	0.000	0.000
158	A	160	THR	0	-0.014	-0.032	16.347	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	161	ASN	0	-0.021	-0.014	17.580	0.014	0.014	0.000	0.000	0.000	0.000
160	A	162	LEU	0	-0.003	-0.007	18.964	0.024	0.024	0.000	0.000	0.000	0.000
161	A	163	ILE	0	-0.006	-0.001	14.329	0.025	0.025	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.002	-0.008	13.001	0.029	0.029	0.000	0.000	0.000	0.000
163	A	165	GLU	-1	-0.906	-0.941	14.807	0.166	0.166	0.000	0.000	0.000	0.000
164	A	166	MET	0	-0.126	-0.055	15.873	0.042	0.042	0.000	0.000	0.000	0.000
165	A	167	ILE	0	-0.093	-0.040	10.575	0.002	0.002	0.000	0.000	0.000	0.000
166	A	168	ASP	-1	-0.935	-0.950	11.479	0.533	0.533	0.000	0.000	0.000	0.000
167	A	169	PHE	0	-0.038	-0.021	9.114	0.128	0.128	0.000	0.000	0.000	0.000
168	A	170	ASP	-1	-0.831	-0.916	11.767	0.355	0.355	0.000	0.000	0.000	0.000
169	A	171	THR	0	-0.024	-0.019	14.473	-0.013	-0.013	0.000	0.000	0.000	0.000
170	A	172	PRO	0	0.121	0.039	18.043	-0.028	-0.028	0.000	0.000	0.000	0.000
171	A	173	GLU	-1	-0.880	-0.913	20.673	0.150	0.150	0.000	0.000	0.000	0.000
172	A	174	ASN	0	-0.068	-0.055	16.863	-0.040	-0.040	0.000	0.000	0.000	0.000
173	A	175	ILE	0	0.017	0.021	15.835	-0.035	-0.035	0.000	0.000	0.000	0.000
174	A	176	GLU	-1	-0.840	-0.890	18.822	0.020	0.020	0.000	0.000	0.000	0.000
175	A	177	LYS	1	0.913	0.948	21.362	-0.110	-0.110	0.000	0.000	0.000	0.000
176	A	178	MET	0	-0.001	0.004	14.168	-0.007	-0.007	0.000	0.000	0.000	0.000
177	A	179	MET	0	-0.021	-0.011	17.838	-0.029	-0.029	0.000	0.000	0.000	0.000
178	A	180	TYR	0	0.004	0.007	21.889	-0.008	-0.008	0.000	0.000	0.000	0.000
179	A	181	MET	0	0.001	0.003	22.061	-0.009	-0.009	0.000	0.000	0.000	0.000
180	A	182	ASN	0	-0.051	-0.032	18.689	-0.017	-0.017	0.000	0.000	0.000	0.000
181	A	183	ARG	1	0.826	0.896	23.106	0.019	0.019	0.000	0.000	0.000	0.000
182	A	184	TYR	0	-0.050	-0.027	26.368	0.000	0.000	0.000	0.000	0.000	0.000
183	A	185	GLY	0	0.042	0.037	26.975	0.000	0.000	0.000	0.000	0.000	0.000
184	A	186	PHE	0	0.042	-0.008	26.343	0.008	0.008	0.000	0.000	0.000	0.000
185	A	187	TYR	0	0.017	0.005	28.162	0.004	0.004	0.000	0.000	0.000	0.000
186	A	188	HIS	0	0.064	0.046	30.867	0.006	0.006	0.000	0.000	0.000	0.000
187	A	189	PHE	0	-0.058	-0.027	23.810	0.007	0.007	0.000	0.000	0.000	0.000
188	A	190	CYS	0	-0.016	-0.036	28.801	0.005	0.005	0.000	0.000	0.000	0.000
189	A	191	ASP	-1	-0.918	-0.927	30.457	-0.002	-0.002	0.000	0.000	0.000	0.000
190	A	192	LYS	1	0.764	0.888	28.149	-0.025	-0.025	0.000	0.000	0.000	0.000
191	A	193	TYR	0	-0.050	-0.063	26.173	0.006	0.006	0.000	0.000	0.000	0.000
192	A	194	GLY	0	-0.024	0.031	29.571	0.005	0.005	0.000	0.000	0.000	0.000
193	A	195	ASN	0	-0.043	-0.045	25.613	-0.008	-0.008	0.000	0.000	0.000	0.000

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