FMO DATABASE

FMODB ID: VQVZ1

Calculation Name: 3F5D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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:

Apendix: None

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
Remarks

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	-2212191.101049
FMO2-HF: Nuclear repulsion	2135213.528785
FMO2-HF: Total energy	-76977.572263
FMO2-MP2: Total energy	-77202.574424

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.
-9.75	-2.21	4.966	-4.53	-7.976	-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 : -0.025 / q_NPA : -0.010

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	0.974	0.984	3.880	-1.410	0.289	-0.013	-0.686	-1.000	0.002
4	A	6	ALA	0	0.029	0.010	5.503	0.335	0.335	0.000	0.000	0.000	0.000
5	A	7	LEU	0	-0.027	-0.013	8.840	-0.094	-0.094	0.000	0.000	0.000	0.000
6	A	8	PHE	0	0.031	0.000	11.552	0.080	0.080	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.041	-0.025	14.619	-0.006	-0.006	0.000	0.000	0.000	0.000
8	A	10	ILE	0	0.018	0.012	17.597	0.018	0.018	0.000	0.000	0.000	0.000
9	A	11	LEU	0	0.000	0.011	20.189	0.004	0.004	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.731	-0.850	23.688	-0.114	-0.114	0.000	0.000	0.000	0.000
11	A	13	GLN	0	-0.040	-0.003	26.497	0.010	0.010	0.000	0.000	0.000	0.000
12	A	14	TYR	0	-0.038	-0.019	20.472	0.007	0.007	0.000	0.000	0.000	0.000
13	A	15	ALA	0	0.042	0.010	24.776	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.805	-0.875	22.631	-0.133	-0.133	0.000	0.000	0.000	0.000
15	A	17	TRP	0	-0.007	-0.024	21.729	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.793	-0.912	22.403	-0.065	-0.065	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.023	0.008	18.251	0.010	0.010	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.014	0.009	16.688	-0.023	-0.023	0.000	0.000	0.000	0.000
19	A	21	TYR	0	0.006	0.009	16.420	-0.032	-0.032	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.015	0.019	13.145	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	23	ALA	0	0.001	-0.001	12.269	-0.037	-0.037	0.000	0.000	0.000	0.000
22	A	24	SER	0	-0.017	-0.033	11.341	-0.093	-0.093	0.000	0.000	0.000	0.000
23	A	25	ALA	0	-0.007	0.011	12.017	-0.050	-0.050	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.011	-0.010	8.213	0.010	0.010	0.000	0.000	0.000	0.000
25	A	27	ASN	0	0.025	0.000	6.871	-0.353	-0.353	0.000	0.000	0.000	0.000
26	A	28	GLN	0	-0.049	-0.029	7.520	-0.137	-0.137	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.746	0.862	6.173	-0.400	-0.400	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.859	-0.927	4.400	-2.077	-1.890	-0.001	-0.028	-0.157	0.000
29	A	31	ASP	-1	-0.836	-0.895	2.672	-1.646	0.087	1.496	-1.124	-2.105	-0.012
30	A	32	TRP	0	-0.016	-0.019	2.703	-0.317	1.637	1.782	-1.576	-2.160	-0.017
31	A	33	SER	0	0.003	0.003	2.331	-4.096	-2.180	1.702	-1.082	-2.537	-0.014
32	A	34	VAL	0	-0.040	-0.013	4.415	0.437	0.488	0.000	-0.034	-0.017	0.000
33	A	35	HIS	0	-0.042	-0.023	6.490	-0.165	-0.165	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.010	-0.023	10.369	0.092	0.092	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.014	-0.018	13.971	0.000	0.000	0.000	0.000	0.000	0.000
36	A	38	SER	0	0.011	-0.019	16.138	0.023	0.023	0.000	0.000	0.000	0.000
37	A	39	LEU	0	-0.065	-0.036	19.968	0.006	0.006	0.000	0.000	0.000	0.000
38	A	40	ASP	-1	-0.885	-0.933	22.552	-0.101	-0.101	0.000	0.000	0.000	0.000
39	A	41	PRO	0	0.007	-0.016	20.551	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	42	ILE	0	-0.024	-0.021	20.505	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	43	VAL	0	-0.013	0.015	21.118	0.015	0.015	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.045	-0.052	23.400	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.075	-0.054	23.679	0.003	0.003	0.000	0.000	0.000	0.000
44	A	46	ILE	0	0.011	-0.002	25.548	0.006	0.006	0.000	0.000	0.000	0.000
45	A	47	GLY	0	-0.031	-0.014	27.238	0.007	0.007	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.020	-0.005	28.205	0.000	0.000	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.017	-0.006	23.237	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.874	0.927	23.926	0.130	0.130	0.000	0.000	0.000	0.000
49	A	51	THR	0	0.012	0.022	18.065	-0.016	-0.016	0.000	0.000	0.000	0.000
50	A	52	SER	0	0.019	0.005	18.026	0.022	0.022	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.042	-0.013	16.468	-0.031	-0.031	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.823	-0.867	10.753	-0.544	-0.544	0.000	0.000	0.000	0.000
53	A	55	TYR	0	-0.002	-0.020	8.386	0.052	0.052	0.000	0.000	0.000	0.000
54	A	56	ILE	0	0.032	0.027	15.334	0.011	0.011	0.000	0.000	0.000	0.000
55	A	57	ILE	0	-0.009	-0.012	18.349	0.007	0.007	0.000	0.000	0.000	0.000
56	A	58	GLY	0	-0.129	-0.089	18.883	0.016	0.016	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.035	-0.003	17.150	0.011	0.011	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.816	-0.889	13.557	-0.137	-0.137	0.000	0.000	0.000	0.000
59	A	61	PRO	0	-0.032	-0.006	9.208	0.033	0.033	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.046	0.007	11.821	0.003	0.003	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.060	-0.033	11.071	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	64	PHE	0	-0.006	-0.002	8.253	-0.059	-0.059	0.000	0.000	0.000	0.000
63	A	65	ASN	0	-0.001	-0.004	6.558	-0.235	-0.235	0.000	0.000	0.000	0.000
64	A	66	LEU	0	0.040	0.033	9.426	0.099	0.099	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.055	-0.008	11.335	-0.094	-0.094	0.000	0.000	0.000	0.000
66	A	68	VAL	0	0.010	0.005	13.420	0.041	0.041	0.000	0.000	0.000	0.000
67	A	69	MET	0	-0.039	-0.011	16.041	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	70	ILE	0	0.036	0.013	18.660	0.015	0.015	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.009	0.014	21.405	0.001	0.001	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.061	0.020	24.722	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.899	-0.948	27.371	-0.057	-0.057	0.000	0.000	0.000	0.000
72	A	74	SER	0	-0.051	-0.045	27.345	0.008	0.008	0.000	0.000	0.000	0.000
73	A	75	TRP	0	-0.019	-0.027	21.952	0.006	0.006	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.039	-0.006	28.442	0.008	0.008	0.000	0.000	0.000	0.000
75	A	77	ASN	0	-0.013	-0.009	28.380	0.001	0.001	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.812	-0.902	30.525	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	79	ASN	0	0.014	0.024	27.202	0.005	0.005	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.908	0.938	26.778	0.025	0.025	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.907	0.949	23.178	0.080	0.080	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.077	0.046	22.098	0.001	0.001	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.013	0.011	22.992	0.003	0.003	0.000	0.000	0.000	0.000
82	A	84	HIS	0	0.031	0.021	22.142	0.005	0.005	0.000	0.000	0.000	0.000
83	A	85	PHE	0	0.026	0.032	14.974	0.015	0.015	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.065	0.028	19.455	0.008	0.008	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.888	0.945	20.842	0.003	0.003	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.001	-0.023	19.091	0.014	0.014	0.000	0.000	0.000	0.000
87	A	89	ALA	0	-0.024	-0.012	17.004	0.015	0.015	0.000	0.000	0.000	0.000
88	A	90	PHE	0	0.056	0.010	18.279	0.021	0.021	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.059	-0.026	21.070	0.011	0.011	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.833	0.922	15.203	0.011	0.011	0.000	0.000	0.000	0.000
91	A	93	ASN	0	-0.033	-0.009	17.020	0.017	0.017	0.000	0.000	0.000	0.000
92	A	94	ILE	0	-0.004	0.018	13.182	0.035	0.035	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.019	0.007	12.743	-0.033	-0.033	0.000	0.000	0.000	0.000
94	A	96	ILE	0	-0.003	0.001	14.801	-0.048	-0.048	0.000	0.000	0.000	0.000
95	A	97	ALA	0	0.016	0.014	17.388	0.019	0.019	0.000	0.000	0.000	0.000
96	A	98	ALA	0	-0.034	-0.013	18.979	-0.023	-0.023	0.000	0.000	0.000	0.000
97	A	99	ILE	0	-0.015	0.003	21.536	0.013	0.013	0.000	0.000	0.000	0.000
98	A	100	CYS	0	-0.010	0.012	23.979	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.027	-0.003	27.274	0.005	0.005	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.003	0.014	22.880	0.004	0.004	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.004	-0.010	24.922	0.008	0.008	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.764	-0.870	26.508	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	105	PHE	0	-0.006	-0.006	25.327	0.004	0.004	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.012	-0.018	22.871	0.005	0.005	0.000	0.000	0.000	0.000
105	A	107	ALA	0	0.019	0.016	27.090	0.007	0.007	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.807	0.887	30.729	0.028	0.028	0.000	0.000	0.000	0.000
107	A	109	ASN	0	-0.067	-0.046	28.263	0.003	0.003	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.029	0.011	29.679	0.003	0.003	0.000	0.000	0.000	0.000
109	A	111	LEU	0	-0.068	-0.029	24.153	0.006	0.006	0.000	0.000	0.000	0.000
110	A	112	LEU	0	0.014	0.015	26.488	0.008	0.008	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.028	-0.013	28.686	0.002	0.002	0.000	0.000	0.000	0.000
112	A	114	ASN	0	0.019	0.006	28.404	0.001	0.001	0.000	0.000	0.000	0.000
113	A	115	HIS	0	-0.055	-0.029	23.036	0.010	0.010	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.017	-0.010	28.164	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	117	HIS	0	-0.009	0.006	27.719	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	118	THR	0	0.015	-0.007	27.985	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	119	GLY	0	0.033	-0.004	28.859	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	120	ASN	0	-0.023	-0.017	29.834	0.001	0.001	0.000	0.000	0.000	0.000
119	A	121	PHE	0	0.040	0.006	32.305	0.002	0.002	0.000	0.000	0.000	0.000
120	A	122	VAL	0	0.056	0.043	35.575	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	123	TYR	0	0.003	-0.011	36.431	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.030	-0.005	34.228	0.000	0.000	0.000	0.000	0.000	0.000
123	A	125	TRP	0	-0.031	-0.056	30.319	0.002	0.002	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.838	0.910	36.650	0.006	0.006	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.821	-0.879	39.936	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	128	TYR	0	-0.022	-0.001	32.994	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	LYS	1	0.974	0.982	37.415	0.002	0.002	0.000	0.000	0.000	0.000
128	A	130	GLN	0	-0.047	-0.016	32.205	0.006	0.006	0.000	0.000	0.000	0.000
129	A	131	TYR	0	-0.008	-0.001	32.583	0.003	0.003	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.822	0.882	34.681	-0.017	-0.017	0.000	0.000	0.000	0.000
131	A	133	PRO	0	-0.013	0.018	33.148	0.003	0.003	0.000	0.000	0.000	0.000
132	A	134	ILE	0	-0.006	0.003	31.837	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	135	SER	0	-0.038	-0.006	31.642	0.001	0.001	0.000	0.000	0.000	0.000
134	A	136	SER	0	-0.031	-0.034	34.036	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	137	PHE	0	0.022	0.027	32.451	0.004	0.004	0.000	0.000	0.000	0.000
136	A	138	VAL	0	-0.016	-0.007	31.881	0.001	0.001	0.000	0.000	0.000	0.000
137	A	139	GLU	-1	-0.912	-0.948	32.738	0.010	0.010	0.000	0.000	0.000	0.000
138	A	140	LYS	1	0.897	0.941	30.988	-0.033	-0.033	0.000	0.000	0.000	0.000
139	A	141	GLN	0	0.005	0.011	28.194	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	ALA	0	0.016	-0.004	24.545	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	143	VAL	0	-0.040	-0.010	25.841	0.006	0.006	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.917	0.967	18.674	-0.218	-0.218	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.751	-0.841	23.689	0.099	0.099	0.000	0.000	0.000	0.000
144	A	146	LYS	1	0.853	0.908	22.476	-0.107	-0.107	0.000	0.000	0.000	0.000
145	A	147	ASN	0	0.002	0.006	17.303	0.024	0.024	0.000	0.000	0.000	0.000
146	A	148	LEU	0	0.003	0.005	19.113	-0.015	-0.015	0.000	0.000	0.000	0.000
147	A	149	VAL	0	0.011	-0.001	19.281	0.006	0.006	0.000	0.000	0.000	0.000
148	A	150	THR	0	-0.022	-0.013	21.723	-0.016	-0.016	0.000	0.000	0.000	0.000
149	A	151	ALA	0	0.053	0.014	24.300	0.007	0.007	0.000	0.000	0.000	0.000
150	A	152	ASN	0	0.037	0.052	26.107	-0.012	-0.012	0.000	0.000	0.000	0.000
151	A	153	GLY	0	0.087	0.019	27.065	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	154	THR	0	-0.054	-0.032	27.808	-0.006	-0.006	0.000	0.000	0.000	0.000
153	A	155	ALA	0	0.002	0.016	26.314	0.000	0.000	0.000	0.000	0.000	0.000
154	A	156	PRO	0	0.037	0.024	22.000	0.008	0.008	0.000	0.000	0.000	0.000
155	A	157	ILE	0	-0.005	0.015	20.987	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.767	-0.875	21.619	0.004	0.004	0.000	0.000	0.000	0.000
157	A	159	PHE	0	0.017	0.002	19.148	0.019	0.019	0.000	0.000	0.000	0.000
158	A	160	THR	0	-0.013	-0.029	16.176	0.004	0.004	0.000	0.000	0.000	0.000
159	A	161	ASN	0	-0.024	-0.018	17.463	0.017	0.017	0.000	0.000	0.000	0.000
160	A	162	LEU	0	-0.019	-0.007	18.720	0.028	0.028	0.000	0.000	0.000	0.000
161	A	163	ILE	0	-0.001	-0.005	14.323	0.028	0.028	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.013	-0.010	12.854	0.043	0.043	0.000	0.000	0.000	0.000
163	A	165	GLU	-1	-0.856	-0.933	14.610	0.215	0.215	0.000	0.000	0.000	0.000
164	A	166	MET	0	-0.137	-0.048	15.645	0.019	0.019	0.000	0.000	0.000	0.000
165	A	167	ILE	0	-0.082	-0.042	10.535	0.011	0.011	0.000	0.000	0.000	0.000
166	A	168	ASP	-1	-0.927	-0.954	11.137	0.657	0.657	0.000	0.000	0.000	0.000
167	A	169	PHE	0	-0.012	0.006	8.978	0.124	0.124	0.000	0.000	0.000	0.000
168	A	170	ASP	-1	-0.811	-0.894	11.185	0.363	0.363	0.000	0.000	0.000	0.000
169	A	171	THR	0	-0.014	-0.023	14.063	-0.007	-0.007	0.000	0.000	0.000	0.000
170	A	172	PRO	0	0.083	0.036	17.702	-0.032	-0.032	0.000	0.000	0.000	0.000
171	A	173	GLU	-1	-0.849	-0.906	20.344	0.172	0.172	0.000	0.000	0.000	0.000
172	A	174	ASN	0	-0.036	-0.015	16.999	-0.060	-0.060	0.000	0.000	0.000	0.000
173	A	175	ILE	0	0.020	0.011	15.752	-0.039	-0.039	0.000	0.000	0.000	0.000
174	A	176	GLU	-1	-0.809	-0.862	18.846	0.026	0.026	0.000	0.000	0.000	0.000
175	A	177	LYS	1	0.885	0.927	21.097	-0.118	-0.118	0.000	0.000	0.000	0.000
176	A	178	MET	0	-0.019	-0.008	14.031	-0.008	-0.008	0.000	0.000	0.000	0.000
177	A	179	MET	0	-0.029	-0.015	17.604	-0.030	-0.030	0.000	0.000	0.000	0.000
178	A	180	TYR	0	0.006	0.003	21.772	-0.009	-0.009	0.000	0.000	0.000	0.000
179	A	181	MET	0	0.001	0.000	21.863	-0.010	-0.010	0.000	0.000	0.000	0.000
180	A	182	ASN	0	-0.031	-0.025	18.517	-0.020	-0.020	0.000	0.000	0.000	0.000
181	A	183	ARG	1	0.827	0.904	22.883	-0.005	-0.005	0.000	0.000	0.000	0.000
182	A	184	TYR	0	-0.041	-0.018	26.368	0.002	0.002	0.000	0.000	0.000	0.000
183	A	185	GLY	0	0.032	0.024	26.355	-0.002	-0.002	0.000	0.000	0.000	0.000
184	A	186	PHE	0	0.029	-0.011	25.978	0.008	0.008	0.000	0.000	0.000	0.000
185	A	187	TYR	0	0.017	0.008	27.861	0.004	0.004	0.000	0.000	0.000	0.000
186	A	188	HIS	0	0.081	0.040	30.670	0.006	0.006	0.000	0.000	0.000	0.000
187	A	189	PHE	0	-0.042	-0.011	23.440	0.007	0.007	0.000	0.000	0.000	0.000
188	A	190	CYS	0	-0.027	-0.019	28.539	0.005	0.005	0.000	0.000	0.000	0.000
189	A	191	ASP	-1	-0.918	-0.953	30.420	-0.002	-0.002	0.000	0.000	0.000	0.000
190	A	192	LYS	1	0.756	0.889	27.782	-0.032	-0.032	0.000	0.000	0.000	0.000
191	A	193	TYR	0	-0.064	-0.074	25.877	0.006	0.006	0.000	0.000	0.000	0.000
192	A	194	GLY	0	-0.017	0.020	29.150	0.004	0.004	0.000	0.000	0.000	0.000
193	A	195	ASN	0	-0.044	-0.035	25.638	-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)