FMO DATABASE

FMODB ID: 98482

Calculation Name: 2OTP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2OTP

Chain ID: A

ChEMBL ID:

UniProt ID: Q8N149

Base Structure: X-ray

Registration Date: 2023-09-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	192
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1833685.748352
FMO2-HF: Nuclear repulsion	1757594.207562
FMO2-HF: Total energy	-76091.54079
FMO2-MP2: Total energy	-76313.557297

3D Structure Molmil

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.
-3.106	1.29	0.52	-1.394	-3.518	0

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 : -0.010 / q_NPA : -0.025

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	0.924	1.001	3.810	-1.486	-0.232	-0.011	-0.526	-0.717	0.003
4	A	6	PRO	0	-0.037	-0.025	6.481	0.433	0.433	0.000	0.000	0.000	0.000
5	A	7	THR	0	-0.030	-0.015	9.036	0.149	0.149	0.000	0.000	0.000	0.000
6	A	8	LEU	0	-0.010	-0.013	12.432	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	9	TRP	0	0.035	0.021	15.451	0.017	0.017	0.000	0.000	0.000	0.000
8	A	10	ALA	0	0.023	0.003	19.090	-0.017	-0.017	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.866	-0.914	21.746	-0.099	-0.099	0.000	0.000	0.000	0.000
10	A	12	PRO	0	-0.023	-0.003	23.594	0.008	0.008	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.098	0.041	26.210	0.010	0.010	0.000	0.000	0.000	0.000
12	A	14	SER	0	-0.034	-0.027	24.615	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	15	VAL	0	-0.019	-0.013	26.405	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	16	ILE	0	0.012	0.015	28.668	0.005	0.005	0.000	0.000	0.000	0.000
15	A	17	ILE	0	0.044	0.028	31.591	0.001	0.001	0.000	0.000	0.000	0.000
16	A	18	GLN	0	0.024	0.018	34.293	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.010	0.008	34.455	0.004	0.004	0.000	0.000	0.000	0.000
18	A	20	SER	0	-0.015	-0.022	32.884	0.005	0.005	0.000	0.000	0.000	0.000
19	A	21	PRO	0	-0.021	-0.012	30.905	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	22	VAL	0	-0.007	0.007	26.325	0.003	0.003	0.000	0.000	0.000	0.000
21	A	23	THR	0	0.001	-0.010	21.919	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	24	LEU	0	0.007	0.019	19.380	0.007	0.007	0.000	0.000	0.000	0.000
23	A	25	ARG	1	0.823	0.902	17.057	0.086	0.086	0.000	0.000	0.000	0.000
24	A	26	CYS	0	0.071	0.043	12.279	-0.036	-0.036	0.000	0.000	0.000	0.000
25	A	27	GLN	0	-0.001	-0.001	12.289	0.009	0.009	0.000	0.000	0.000	0.000
26	A	28	GLY	0	0.074	0.018	8.207	-0.058	-0.058	0.000	0.000	0.000	0.000
27	A	29	SER	0	-0.032	0.009	4.697	0.122	0.206	-0.001	-0.005	-0.077	0.000
28	A	30	LEU	0	0.031	-0.007	6.835	-0.042	-0.042	0.000	0.000	0.000	0.000
29	A	31	GLN	0	-0.055	-0.003	4.435	-0.183	-0.032	-0.001	-0.007	-0.143	0.000
30	A	32	ALA	0	-0.037	-0.017	7.671	-0.090	-0.090	0.000	0.000	0.000	0.000
31	A	33	GLU	-1	-0.774	-0.887	8.999	-0.275	-0.275	0.000	0.000	0.000	0.000
32	A	34	GLU	-1	-0.895	-0.954	10.101	-0.396	-0.396	0.000	0.000	0.000	0.000
33	A	35	TYR	0	-0.063	-0.041	10.974	-0.044	-0.044	0.000	0.000	0.000	0.000
34	A	36	HIS	0	0.020	0.003	12.197	0.037	0.037	0.000	0.000	0.000	0.000
35	A	37	LEU	0	-0.014	0.026	13.820	0.007	0.007	0.000	0.000	0.000	0.000
36	A	38	TYR	0	-0.045	-0.043	16.746	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	39	ARG	1	0.956	1.011	17.871	0.160	0.160	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.884	-0.941	20.084	-0.105	-0.105	0.000	0.000	0.000	0.000
39	A	41	ASN	0	-0.018	-0.022	23.003	0.008	0.008	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.962	0.977	20.419	0.148	0.148	0.000	0.000	0.000	0.000
41	A	43	SER	0	0.092	0.097	20.044	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	44	ALA	0	0.121	0.077	20.562	0.001	0.001	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.094	-0.117	17.357	-0.015	-0.015	0.000	0.000	0.000	0.000
44	A	46	TRP	0	-0.100	-0.020	19.090	0.010	0.010	0.000	0.000	0.000	0.000
45	A	47	VAL	0	0.041	0.016	15.190	-0.022	-0.022	0.000	0.000	0.000	0.000
46	A	48	ARG	1	0.907	0.971	16.664	0.252	0.252	0.000	0.000	0.000	0.000
47	A	49	ARG	1	0.775	0.862	13.782	0.333	0.333	0.000	0.000	0.000	0.000
48	A	50	ILE	0	-0.077	-0.035	13.994	0.038	0.038	0.000	0.000	0.000	0.000
49	A	51	GLN	0	0.045	0.010	15.398	-0.016	-0.016	0.000	0.000	0.000	0.000
50	A	52	GLU	-1	-0.881	-0.923	14.759	-0.221	-0.221	0.000	0.000	0.000	0.000
51	A	53	PRO	0	-0.054	-0.016	15.940	0.027	0.027	0.000	0.000	0.000	0.000
52	A	54	GLY	0	0.053	0.017	15.403	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.874	0.934	16.702	0.134	0.134	0.000	0.000	0.000	0.000
54	A	56	ASN	0	0.014	-0.006	13.711	-0.038	-0.038	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.055	0.026	15.014	0.015	0.015	0.000	0.000	0.000	0.000
56	A	58	GLN	0	-0.116	-0.067	16.483	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	59	PHE	0	0.016	0.002	15.736	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	60	PRO	0	-0.017	-0.016	21.203	0.006	0.006	0.000	0.000	0.000	0.000
59	A	61	ILE	0	0.018	0.005	24.904	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	62	PRO	0	-0.014	0.002	27.754	0.006	0.006	0.000	0.000	0.000	0.000
61	A	63	SER	0	0.042	0.021	31.363	0.005	0.005	0.000	0.000	0.000	0.000
62	A	64	ILE	0	-0.026	0.005	27.625	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	65	THR	0	0.010	-0.035	30.828	0.007	0.007	0.000	0.000	0.000	0.000
64	A	66	TRP	0	0.056	-0.010	31.286	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.932	-0.947	29.479	-0.097	-0.097	0.000	0.000	0.000	0.000
66	A	68	HIS	0	0.003	0.032	26.433	0.000	0.000	0.000	0.000	0.000	0.000
67	A	69	ALA	0	0.013	0.030	26.106	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.065	0.028	24.777	0.002	0.002	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.857	0.929	16.868	0.168	0.168	0.000	0.000	0.000	0.000
70	A	72	TYR	0	-0.054	-0.052	18.814	-0.024	-0.024	0.000	0.000	0.000	0.000
71	A	73	HIS	0	0.088	0.046	13.305	0.061	0.061	0.000	0.000	0.000	0.000
72	A	75	GLN	0	-0.032	-0.054	7.852	0.207	0.207	0.000	0.000	0.000	0.000
73	A	76	TYR	0	-0.024	-0.020	3.452	-0.178	0.473	0.038	-0.204	-0.484	-0.001
74	A	77	TYR	0	-0.032	0.008	6.593	-0.390	-0.390	0.000	0.000	0.000	0.000
75	A	78	SER	0	0.021	0.003	5.069	0.186	0.186	0.000	0.000	0.000	0.000
76	A	79	HIS	0	0.016	0.016	6.983	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	80	ASN	0	-0.044	-0.024	7.540	0.059	0.059	0.000	0.000	0.000	0.000
78	A	81	HIS	0	0.006	0.015	2.614	-1.555	-0.461	0.439	-0.362	-1.172	-0.002
79	A	82	SER	0	0.004	0.001	4.742	0.087	0.167	-0.001	-0.005	-0.073	0.000
80	A	83	SER	0	-0.017	-0.019	3.069	-1.160	-0.469	0.056	-0.217	-0.529	0.000
81	A	84	GLU	-1	-0.930	-0.961	3.504	0.792	1.197	0.002	-0.066	-0.341	0.000
82	A	85	TYR	0	-0.035	-0.035	5.278	0.059	0.045	-0.001	-0.002	0.018	0.000
83	A	86	SER	0	0.028	0.009	7.935	-0.058	-0.058	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.869	-0.929	10.374	-0.063	-0.063	0.000	0.000	0.000	0.000
85	A	88	PRO	0	-0.070	-0.041	13.696	-0.027	-0.027	0.000	0.000	0.000	0.000
86	A	89	LEU	0	-0.020	0.003	16.583	0.027	0.027	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.921	-0.970	19.345	-0.048	-0.048	0.000	0.000	0.000	0.000
88	A	91	LEU	0	-0.044	-0.004	22.954	0.009	0.009	0.000	0.000	0.000	0.000
89	A	92	VAL	0	0.007	-0.004	25.210	0.003	0.003	0.000	0.000	0.000	0.000
90	A	93	VAL	0	0.010	0.026	28.838	0.002	0.002	0.000	0.000	0.000	0.000
91	A	94	THR	0	-0.032	-0.034	31.992	0.005	0.005	0.000	0.000	0.000	0.000
92	A	95	GLY	0	-0.003	-0.011	35.294	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	96	ALA	0	-0.008	0.007	37.152	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	97	TYR	0	0.006	-0.009	36.910	0.001	0.001	0.000	0.000	0.000	0.000
95	A	98	SER	0	-0.003	-0.005	41.594	0.000	0.000	0.000	0.000	0.000	0.000
96	A	99	LYS	1	0.868	0.945	43.011	0.015	0.015	0.000	0.000	0.000	0.000
97	A	100	PRO	0	0.083	0.026	40.983	0.001	0.001	0.000	0.000	0.000	0.000
98	A	101	THR	0	-0.066	-0.038	44.333	0.000	0.000	0.000	0.000	0.000	0.000
99	A	102	LEU	0	0.037	0.038	42.250	0.001	0.001	0.000	0.000	0.000	0.000
100	A	103	SER	0	-0.008	-0.012	45.695	0.000	0.000	0.000	0.000	0.000	0.000
101	A	104	ALA	0	-0.009	0.001	48.020	0.001	0.001	0.000	0.000	0.000	0.000
102	A	105	LEU	0	-0.022	0.041	48.793	0.000	0.000	0.000	0.000	0.000	0.000
103	A	106	PRO	0	-0.004	-0.021	49.833	0.001	0.001	0.000	0.000	0.000	0.000
104	A	107	SER	0	0.028	-0.029	53.100	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	108	PRO	0	0.022	-0.003	50.510	0.001	0.001	0.000	0.000	0.000	0.000
106	A	109	VAL	0	-0.015	0.013	50.639	0.001	0.001	0.000	0.000	0.000	0.000
107	A	110	VAL	0	0.029	0.019	48.186	0.000	0.000	0.000	0.000	0.000	0.000
108	A	111	THR	0	0.007	0.005	51.323	0.000	0.000	0.000	0.000	0.000	0.000
109	A	112	LEU	0	0.003	-0.015	49.617	0.000	0.000	0.000	0.000	0.000	0.000
110	A	113	GLY	0	-0.009	0.005	46.568	0.001	0.001	0.000	0.000	0.000	0.000
111	A	114	GLY	0	-0.003	0.019	47.610	0.001	0.001	0.000	0.000	0.000	0.000
112	A	115	ASN	0	-0.011	-0.014	46.517	0.001	0.001	0.000	0.000	0.000	0.000
113	A	116	VAL	0	-0.013	-0.010	45.669	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	117	THR	0	-0.023	-0.018	45.637	0.001	0.001	0.000	0.000	0.000	0.000
115	A	118	LEU	0	0.020	0.016	42.691	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	119	GLN	0	0.014	0.007	44.012	0.000	0.000	0.000	0.000	0.000	0.000
117	A	120	CYS	0	-0.001	0.004	41.918	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	121	VAL	0	0.009	-0.001	44.077	0.000	0.000	0.000	0.000	0.000	0.000
119	A	122	SER	0	0.044	0.003	44.319	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	GLN	0	-0.009	0.003	46.519	0.000	0.000	0.000	0.000	0.000	0.000
121	A	124	VAL	0	-0.031	-0.005	44.698	0.000	0.000	0.000	0.000	0.000	0.000
122	A	125	ALA	0	-0.004	0.004	44.942	0.001	0.001	0.000	0.000	0.000	0.000
123	A	126	PHE	0	0.001	-0.017	39.636	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	127	ASP	-1	-0.934	-0.959	37.848	-0.014	-0.014	0.000	0.000	0.000	0.000
125	A	128	GLY	0	0.032	0.012	35.770	0.000	0.000	0.000	0.000	0.000	0.000
126	A	129	PHE	0	-0.062	-0.027	36.012	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	130	ILE	0	-0.013	-0.009	32.148	0.001	0.001	0.000	0.000	0.000	0.000
128	A	131	LEU	0	0.001	0.019	35.251	0.000	0.000	0.000	0.000	0.000	0.000
129	A	132	CYS	0	-0.078	-0.071	31.129	0.001	0.001	0.000	0.000	0.000	0.000
130	A	133	LYS	1	0.936	0.965	35.440	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	134	GLU	-1	-0.837	-0.927	35.944	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	135	GLY	0	-0.053	-0.028	36.196	0.003	0.003	0.000	0.000	0.000	0.000
133	A	136	GLU	-1	-0.973	-0.991	36.643	0.011	0.011	0.000	0.000	0.000	0.000
134	A	137	ASP	-1	-0.920	-0.953	34.402	0.002	0.002	0.000	0.000	0.000	0.000
135	A	138	GLU	-1	-0.940	-0.943	29.276	0.000	0.000	0.000	0.000	0.000	0.000
136	A	139	HIS	0	-0.016	-0.012	32.163	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	140	PRO	0	-0.020	0.004	32.547	0.001	0.001	0.000	0.000	0.000	0.000
138	A	141	GLN	0	0.000	0.030	30.319	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	143	LEU	0	-0.034	-0.023	30.539	0.002	0.002	0.000	0.000	0.000	0.000
140	A	144	ASN	0	-0.003	-0.026	28.759	0.001	0.001	0.000	0.000	0.000	0.000
141	A	145	SER	0	-0.017	-0.001	30.228	0.006	0.006	0.000	0.000	0.000	0.000
142	A	146	HIS	0	0.036	0.027	27.736	-0.010	-0.010	0.000	0.000	0.000	0.000
143	A	147	SER	0	0.036	0.004	30.444	0.008	0.008	0.000	0.000	0.000	0.000
144	A	148	HIS	0	-0.083	-0.045	25.131	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	149	ALA	0	0.061	0.035	29.336	0.004	0.004	0.000	0.000	0.000	0.000
146	A	150	ARG	1	0.937	0.972	29.346	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	151	GLY	0	-0.011	-0.002	29.728	0.004	0.004	0.000	0.000	0.000	0.000
148	A	152	TRP	0	-0.004	-0.016	30.178	0.001	0.001	0.000	0.000	0.000	0.000
149	A	153	SER	0	0.007	0.028	30.513	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	154	TRP	0	0.050	0.000	25.863	0.006	0.006	0.000	0.000	0.000	0.000
151	A	155	ALA	0	-0.026	0.004	30.292	-0.003	-0.003	0.000	0.000	0.000	0.000
152	A	156	ILE	0	0.001	0.010	25.993	0.007	0.007	0.000	0.000	0.000	0.000
153	A	157	PHE	0	0.008	-0.010	27.946	-0.006	-0.006	0.000	0.000	0.000	0.000
154	A	158	SER	0	0.025	0.016	25.604	0.008	0.008	0.000	0.000	0.000	0.000
155	A	159	VAL	0	-0.014	-0.001	26.332	-0.005	-0.005	0.000	0.000	0.000	0.000
156	A	160	GLY	0	0.025	0.023	25.535	-0.003	-0.003	0.000	0.000	0.000	0.000
157	A	161	PRO	0	0.000	-0.025	25.929	0.007	0.007	0.000	0.000	0.000	0.000
158	A	162	VAL	0	-0.023	0.002	25.210	0.002	0.002	0.000	0.000	0.000	0.000
159	A	163	SER	0	0.010	-0.022	27.881	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	164	PRO	0	-0.048	-0.006	28.195	0.001	0.001	0.000	0.000	0.000	0.000
161	A	165	SER	0	0.052	0.015	31.327	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	166	ARG	1	0.936	0.958	34.158	-0.029	-0.029	0.000	0.000	0.000	0.000
163	A	167	ARG	1	0.871	0.922	31.123	-0.070	-0.070	0.000	0.000	0.000	0.000
164	A	168	TRP	0	0.039	0.017	27.399	-0.005	-0.005	0.000	0.000	0.000	0.000
165	A	169	SER	0	-0.021	-0.006	29.069	0.007	0.007	0.000	0.000	0.000	0.000
166	A	170	TYR	0	0.013	0.013	28.603	-0.009	-0.009	0.000	0.000	0.000	0.000
167	A	171	ARG	1	0.917	0.946	30.380	-0.071	-0.071	0.000	0.000	0.000	0.000
168	A	172	CYS	0	0.001	0.002	31.117	-0.004	-0.004	0.000	0.000	0.000	0.000
169	A	173	TYR	0	0.022	-0.002	33.552	0.004	0.004	0.000	0.000	0.000	0.000
170	A	174	ALA	0	0.019	0.007	35.432	-0.001	-0.001	0.000	0.000	0.000	0.000
171	A	175	TYR	0	-0.026	-0.013	37.344	0.000	0.000	0.000	0.000	0.000	0.000
172	A	176	ASP	-1	-0.773	-0.868	39.763	0.025	0.025	0.000	0.000	0.000	0.000
173	A	177	SER	0	0.011	-0.006	42.365	-0.001	-0.001	0.000	0.000	0.000	0.000
174	A	178	ASN	0	-0.107	-0.063	44.721	-0.002	-0.002	0.000	0.000	0.000	0.000
175	A	179	SER	0	-0.035	-0.026	46.200	-0.001	-0.001	0.000	0.000	0.000	0.000
176	A	180	PRO	0	0.013	0.018	44.686	0.002	0.002	0.000	0.000	0.000	0.000
177	A	181	TYR	0	0.004	0.004	45.159	0.000	0.000	0.000	0.000	0.000	0.000
178	A	182	VAL	0	-0.032	-0.004	46.287	0.001	0.001	0.000	0.000	0.000	0.000
179	A	183	TRP	0	-0.049	-0.028	40.958	0.001	0.001	0.000	0.000	0.000	0.000
180	A	184	SER	0	0.003	-0.001	37.646	0.000	0.000	0.000	0.000	0.000	0.000
181	A	185	LEU	0	-0.011	-0.012	38.121	-0.002	-0.002	0.000	0.000	0.000	0.000
182	A	186	PRO	0	-0.010	0.004	35.894	0.002	0.002	0.000	0.000	0.000	0.000
183	A	187	SER	0	0.000	0.005	30.829	0.004	0.004	0.000	0.000	0.000	0.000
184	A	188	ASP	-1	-0.914	-0.962	28.794	0.116	0.116	0.000	0.000	0.000	0.000
185	A	189	LEU	0	-0.077	-0.030	29.074	0.000	0.000	0.000	0.000	0.000	0.000
186	A	190	LEU	0	0.065	0.044	23.316	0.010	0.010	0.000	0.000	0.000	0.000
187	A	191	GLU	-1	-0.911	-0.957	25.764	0.086	0.086	0.000	0.000	0.000	0.000
188	A	192	LEU	0	-0.012	0.002	23.367	0.013	0.013	0.000	0.000	0.000	0.000
189	A	193	LEU	0	-0.012	-0.004	19.073	0.000	0.000	0.000	0.000	0.000	0.000
190	A	194	VAL	0	0.002	-0.007	21.222	-0.006	-0.006	0.000	0.000	0.000	0.000
191	A	195	PRO	0	-0.019	0.009	19.327	0.008	0.008	0.000	0.000	0.000	0.000
192	A	196	GLY	0	0.030	0.011	21.735	-0.013	-0.013	0.000	0.000	0.000	0.000

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