FMO DATABASE

FMODB ID: MNV7Z

Calculation Name: 3JV1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3JV1

Chain ID: A

ChEMBL ID:

UniProt ID: Q584R4

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	182
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1786761.427554
FMO2-HF: Nuclear repulsion	1714747.715195
FMO2-HF: Total energy	-72013.712359
FMO2-MP2: Total energy	-72224.629435

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:46:ALA)

Summations of interaction energy for fragment #1(A:46:ALA)

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.
-18.003	-15.39	8.312	-5.654	-5.272	-0.051

Interaction energy analysis for fragmet #1(A:46:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / q_NPA : -0.019

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	48	SER	0	-0.048	-0.025	2.791	-1.195	1.154	0.048	-1.133	-1.264	0.002
4	A	49	ASP	-1	-0.810	-0.906	1.906	-16.601	-16.660	8.265	-4.422	-3.784	-0.053
5	A	50	GLN	0	-0.037	-0.018	4.342	1.090	1.413	-0.001	-0.099	-0.224	0.000
6	A	51	ARG	1	0.940	0.960	6.055	0.763	0.763	0.000	0.000	0.000	0.000
7	A	52	LEU	0	0.002	0.014	7.542	0.275	0.275	0.000	0.000	0.000	0.000
8	A	53	SER	0	-0.015	0.002	8.384	0.336	0.336	0.000	0.000	0.000	0.000
9	A	54	GLU	-1	-0.872	-0.946	10.006	-0.435	-0.435	0.000	0.000	0.000	0.000
10	A	55	ALA	0	-0.041	-0.023	12.013	0.127	0.127	0.000	0.000	0.000	0.000
11	A	56	THR	0	0.004	-0.014	12.638	0.078	0.078	0.000	0.000	0.000	0.000
12	A	57	LEU	0	-0.031	0.003	14.440	0.061	0.061	0.000	0.000	0.000	0.000
13	A	58	ARG	1	0.879	0.926	16.113	0.274	0.274	0.000	0.000	0.000	0.000
14	A	59	GLU	-1	-0.766	-0.819	17.857	-0.195	-0.195	0.000	0.000	0.000	0.000
15	A	60	LEU	0	-0.021	-0.010	18.972	0.032	0.032	0.000	0.000	0.000	0.000
16	A	61	GLU	-1	-0.955	-0.990	19.489	-0.260	-0.260	0.000	0.000	0.000	0.000
17	A	62	ASP	-1	-0.865	-0.920	22.085	-0.172	-0.172	0.000	0.000	0.000	0.000
18	A	63	GLU	-1	-0.775	-0.873	23.531	-0.166	-0.166	0.000	0.000	0.000	0.000
19	A	64	ARG	1	0.815	0.893	23.594	0.257	0.257	0.000	0.000	0.000	0.000
20	A	65	GLN	0	-0.125	-0.071	25.332	0.026	0.026	0.000	0.000	0.000	0.000
21	A	66	ARG	1	0.712	0.829	22.935	0.207	0.207	0.000	0.000	0.000	0.000
22	A	67	ALA	0	-0.021	-0.013	30.229	0.000	0.000	0.000	0.000	0.000	0.000
23	A	68	GLY	0	0.006	-0.009	32.990	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	69	LEU	0	-0.023	0.003	29.438	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	70	PRO	0	0.007	0.011	32.673	0.006	0.006	0.000	0.000	0.000	0.000
26	A	71	GLU	-1	-0.936	-0.964	35.133	-0.095	-0.095	0.000	0.000	0.000	0.000
27	A	72	LYS	1	0.863	0.938	36.474	0.117	0.117	0.000	0.000	0.000	0.000
28	A	73	PRO	0	0.022	0.014	38.226	0.004	0.004	0.000	0.000	0.000	0.000
29	A	74	GLU	-1	-0.965	-0.976	41.387	-0.077	-0.077	0.000	0.000	0.000	0.000
30	A	75	ILE	0	-0.049	-0.032	42.630	0.001	0.001	0.000	0.000	0.000	0.000
31	A	76	PRO	0	-0.008	-0.001	44.579	0.003	0.003	0.000	0.000	0.000	0.000
32	A	77	GLU	-1	-0.880	-0.951	47.975	-0.063	-0.063	0.000	0.000	0.000	0.000
33	A	78	GLY	0	-0.050	-0.020	50.710	0.001	0.001	0.000	0.000	0.000	0.000
34	A	79	TRP	0	-0.035	-0.023	46.087	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	80	THR	0	-0.037	-0.012	44.325	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	81	ILE	0	-0.003	-0.016	38.786	0.001	0.001	0.000	0.000	0.000	0.000
37	A	82	ASP	-1	-0.885	-0.915	37.299	-0.119	-0.119	0.000	0.000	0.000	0.000
38	A	83	ARG	1	0.905	0.948	29.577	0.164	0.164	0.000	0.000	0.000	0.000
39	A	84	LYS	1	0.825	0.895	30.992	0.134	0.134	0.000	0.000	0.000	0.000
40	A	85	PRO	0	-0.006	-0.014	27.451	0.001	0.001	0.000	0.000	0.000	0.000
41	A	86	GLY	0	0.018	0.010	26.083	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	87	VAL	0	-0.109	-0.048	26.721	0.000	0.000	0.000	0.000	0.000	0.000
43	A	88	THR	0	0.027	0.015	29.611	0.007	0.007	0.000	0.000	0.000	0.000
44	A	89	HIS	0	-0.045	-0.031	31.254	0.006	0.006	0.000	0.000	0.000	0.000
45	A	90	PHE	0	-0.013	0.001	34.378	0.001	0.001	0.000	0.000	0.000	0.000
46	A	91	THR	0	0.013	-0.012	36.429	0.008	0.008	0.000	0.000	0.000	0.000
47	A	92	MET	0	-0.016	-0.003	40.045	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	93	ARG	1	0.862	0.946	41.083	0.090	0.090	0.000	0.000	0.000	0.000
49	A	94	LYS	1	0.918	0.978	46.345	0.056	0.056	0.000	0.000	0.000	0.000
50	A	95	SER	0	0.000	0.011	49.832	0.001	0.001	0.000	0.000	0.000	0.000
51	A	96	HIS	0	0.013	-0.006	53.207	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	97	GLY	0	-0.019	-0.001	56.273	0.002	0.002	0.000	0.000	0.000	0.000
53	A	98	ASP	-1	-0.946	-0.984	57.640	-0.045	-0.045	0.000	0.000	0.000	0.000
54	A	99	GLU	-1	-0.869	-0.897	55.647	-0.048	-0.048	0.000	0.000	0.000	0.000
55	A	100	GLU	-1	-0.927	-0.964	48.501	-0.069	-0.069	0.000	0.000	0.000	0.000
56	A	101	ILE	0	-0.034	-0.027	49.555	0.001	0.001	0.000	0.000	0.000	0.000
57	A	102	ILE	0	-0.043	-0.030	44.464	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	103	LEU	0	0.022	0.020	43.475	0.002	0.002	0.000	0.000	0.000	0.000
59	A	104	GLN	0	-0.004	-0.010	40.476	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	105	LEU	0	0.025	0.026	36.998	0.004	0.004	0.000	0.000	0.000	0.000
61	A	106	THR	0	-0.035	-0.037	37.654	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	107	GLY	0	0.004	0.010	34.945	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	108	GLU	-1	-0.850	-0.896	32.941	-0.116	-0.116	0.000	0.000	0.000	0.000
64	A	109	ASP	-1	-0.855	-0.937	35.184	-0.070	-0.070	0.000	0.000	0.000	0.000
65	A	110	ARG	1	0.823	0.898	37.088	0.063	0.063	0.000	0.000	0.000	0.000
66	A	111	SER	0	-0.022	0.006	35.654	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	112	ASN	0	-0.050	-0.034	36.240	0.001	0.001	0.000	0.000	0.000	0.000
68	A	113	GLU	-1	-0.951	-0.959	36.651	-0.064	-0.064	0.000	0.000	0.000	0.000
69	A	114	GLU	-1	-0.983	-0.982	38.084	-0.064	-0.064	0.000	0.000	0.000	0.000
70	A	115	ILE	0	-0.012	-0.021	34.075	0.000	0.000	0.000	0.000	0.000	0.000
71	A	116	THR	0	0.066	0.051	37.793	0.001	0.001	0.000	0.000	0.000	0.000
72	A	117	ARG	1	0.878	0.923	34.661	0.098	0.098	0.000	0.000	0.000	0.000
73	A	118	THR	0	0.017	0.000	38.837	0.005	0.005	0.000	0.000	0.000	0.000
74	A	119	LEU	0	-0.045	-0.022	39.730	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	120	ASP	-1	-0.879	-0.921	42.106	-0.068	-0.068	0.000	0.000	0.000	0.000
76	A	121	VAL	0	-0.005	-0.015	44.758	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	122	LEU	0	-0.046	-0.022	45.349	0.004	0.004	0.000	0.000	0.000	0.000
78	A	123	VAL	0	0.012	0.012	49.364	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	124	VAL	0	-0.012	-0.014	50.320	0.002	0.002	0.000	0.000	0.000	0.000
80	A	125	ASN	0	0.081	0.016	53.519	0.000	0.000	0.000	0.000	0.000	0.000
81	A	126	GLY	0	0.008	0.016	56.958	0.001	0.001	0.000	0.000	0.000	0.000
82	A	127	GLY	0	-0.047	-0.026	55.449	0.001	0.001	0.000	0.000	0.000	0.000
83	A	128	LYS	1	0.805	0.910	55.446	0.041	0.041	0.000	0.000	0.000	0.000
84	A	129	ALA	0	0.040	0.012	51.680	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	130	LEU	0	-0.039	0.006	53.754	0.002	0.002	0.000	0.000	0.000	0.000
86	A	131	VAL	0	-0.016	-0.024	47.773	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	132	PHE	0	0.031	0.009	49.876	0.003	0.003	0.000	0.000	0.000	0.000
88	A	133	GLY	0	0.038	0.037	46.426	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	134	MET	0	-0.059	-0.041	45.662	0.004	0.004	0.000	0.000	0.000	0.000
90	A	135	SER	0	0.056	0.001	43.282	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	136	VAL	0	-0.082	-0.027	42.261	0.003	0.003	0.000	0.000	0.000	0.000
92	A	137	GLU	-1	-0.828	-0.909	42.715	-0.061	-0.061	0.000	0.000	0.000	0.000
93	A	138	ASP	-1	-0.929	-0.960	43.883	-0.057	-0.057	0.000	0.000	0.000	0.000
94	A	139	GLY	0	-0.042	-0.017	44.565	0.002	0.002	0.000	0.000	0.000	0.000
95	A	140	GLU	-1	-0.925	-0.955	46.290	-0.048	-0.048	0.000	0.000	0.000	0.000
96	A	141	PHE	0	-0.054	-0.044	45.384	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	142	VAL	0	0.047	0.044	47.705	0.003	0.003	0.000	0.000	0.000	0.000
98	A	143	ILE	0	-0.048	-0.047	48.415	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	144	ASN	0	0.000	-0.005	45.808	0.004	0.004	0.000	0.000	0.000	0.000
100	A	145	ASN	0	-0.039	-0.032	48.156	0.000	0.000	0.000	0.000	0.000	0.000
101	A	146	VAL	0	0.033	0.026	50.836	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	147	CYS	0	-0.036	0.008	50.944	0.002	0.002	0.000	0.000	0.000	0.000
103	A	148	PHE	0	0.021	0.000	53.107	0.000	0.000	0.000	0.000	0.000	0.000
104	A	149	ARG	1	0.850	0.909	49.674	0.051	0.051	0.000	0.000	0.000	0.000
105	A	150	HIS	0	0.068	0.027	53.880	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	151	ASP	-1	-0.847	-0.924	52.424	-0.051	-0.051	0.000	0.000	0.000	0.000
107	A	152	GLY	0	0.069	0.021	51.756	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	153	LYS	1	0.931	0.970	49.026	0.052	0.052	0.000	0.000	0.000	0.000
109	A	154	LEU	0	0.018	0.016	46.725	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	155	ALA	0	-0.038	-0.026	46.887	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	156	LEU	0	-0.002	-0.002	46.240	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	157	ASP	-1	-0.881	-0.904	42.676	-0.080	-0.080	0.000	0.000	0.000	0.000
113	A	158	THR	0	0.070	0.031	38.788	0.002	0.002	0.000	0.000	0.000	0.000
114	A	159	SER	0	-0.073	-0.033	38.406	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	160	ALA	0	0.036	0.001	36.144	0.003	0.003	0.000	0.000	0.000	0.000
116	A	161	GLU	-1	-0.875	-0.924	38.279	-0.060	-0.060	0.000	0.000	0.000	0.000
117	A	162	ALA	0	0.015	0.012	41.405	0.004	0.004	0.000	0.000	0.000	0.000
118	A	163	GLN	0	0.010	-0.028	38.386	0.007	0.007	0.000	0.000	0.000	0.000
119	A	164	PHE	0	-0.022	0.002	41.585	0.004	0.004	0.000	0.000	0.000	0.000
120	A	165	GLN	0	-0.043	-0.026	43.215	0.005	0.005	0.000	0.000	0.000	0.000
121	A	166	LYS	1	0.845	0.910	44.056	0.072	0.072	0.000	0.000	0.000	0.000
122	A	167	SER	0	-0.074	-0.037	44.145	0.002	0.002	0.000	0.000	0.000	0.000
123	A	168	GLN	0	-0.043	-0.017	46.299	0.002	0.002	0.000	0.000	0.000	0.000
124	A	169	LEU	0	-0.073	-0.022	49.384	0.003	0.003	0.000	0.000	0.000	0.000
125	A	170	TYR	0	0.005	0.002	51.370	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	171	MET	0	0.039	0.004	47.425	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	172	GLY	0	0.021	0.024	52.046	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	173	PRO	0	-0.072	-0.042	54.840	0.000	0.000	0.000	0.000	0.000	0.000
129	A	174	ASP	-1	-0.821	-0.897	54.094	-0.040	-0.040	0.000	0.000	0.000	0.000
130	A	175	LEU	0	0.004	-0.009	53.341	0.002	0.002	0.000	0.000	0.000	0.000
131	A	176	ALA	0	-0.016	0.001	55.881	0.001	0.001	0.000	0.000	0.000	0.000
132	A	177	ASP	-1	-0.995	-0.994	57.544	-0.030	-0.030	0.000	0.000	0.000	0.000
133	A	178	LEU	0	-0.117	-0.063	58.334	0.001	0.001	0.000	0.000	0.000	0.000
134	A	179	GLU	-1	-0.901	-0.950	61.386	-0.027	-0.027	0.000	0.000	0.000	0.000
135	A	180	ASP	-1	-0.838	-0.930	62.130	-0.033	-0.033	0.000	0.000	0.000	0.000
136	A	181	HIS	0	-0.074	-0.032	62.907	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	182	LEU	0	-0.038	-0.001	60.885	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	183	VAL	0	0.060	0.021	57.128	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	184	ASP	-1	-0.843	-0.927	58.761	-0.037	-0.037	0.000	0.000	0.000	0.000
140	A	185	SER	0	-0.084	-0.048	60.592	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	186	PHE	0	-0.028	-0.022	56.566	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	187	THR	0	0.060	0.033	55.679	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	188	SER	0	-0.020	-0.018	56.792	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	189	TYR	0	-0.066	-0.035	55.940	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	190	LEU	0	0.023	0.008	51.983	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	191	SER	0	0.041	0.028	54.490	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	192	ALA	0	-0.057	-0.022	56.051	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	193	ARG	1	0.720	0.827	54.159	0.047	0.047	0.000	0.000	0.000	0.000
149	A	194	GLY	0	-0.011	-0.007	52.763	-0.002	-0.002	0.000	0.000	0.000	0.000
150	A	195	VAL	0	-0.030	-0.003	49.114	-0.002	-0.002	0.000	0.000	0.000	0.000
151	A	196	ASN	0	0.024	-0.001	50.942	0.000	0.000	0.000	0.000	0.000	0.000
152	A	197	ASP	-1	-0.737	-0.886	49.725	-0.055	-0.055	0.000	0.000	0.000	0.000
153	A	198	THR	0	-0.067	-0.023	48.612	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	199	LEU	0	-0.032	-0.008	45.885	-0.003	-0.003	0.000	0.000	0.000	0.000
155	A	200	ALA	0	0.028	0.027	45.225	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	201	ASN	0	0.035	0.015	43.988	-0.005	-0.005	0.000	0.000	0.000	0.000
157	A	202	PHE	0	-0.008	-0.016	41.221	-0.004	-0.004	0.000	0.000	0.000	0.000
158	A	203	ILE	0	0.019	0.004	40.050	-0.006	-0.006	0.000	0.000	0.000	0.000
159	A	204	ASP	-1	-0.810	-0.868	39.128	-0.089	-0.089	0.000	0.000	0.000	0.000
160	A	205	GLN	0	-0.045	-0.035	38.072	-0.009	-0.009	0.000	0.000	0.000	0.000
161	A	206	PHE	0	-0.045	-0.040	36.172	-0.009	-0.009	0.000	0.000	0.000	0.000
162	A	207	SER	0	-0.011	-0.027	35.068	-0.009	-0.009	0.000	0.000	0.000	0.000
163	A	208	LEU	0	0.040	0.029	33.421	-0.009	-0.009	0.000	0.000	0.000	0.000
164	A	209	TRP	0	-0.005	-0.003	32.605	-0.011	-0.011	0.000	0.000	0.000	0.000
165	A	210	SER	0	-0.060	-0.040	31.791	-0.008	-0.008	0.000	0.000	0.000	0.000
166	A	211	GLU	-1	-0.926	-0.951	29.006	-0.154	-0.154	0.000	0.000	0.000	0.000
167	A	212	GLN	0	-0.022	-0.026	27.370	-0.007	-0.007	0.000	0.000	0.000	0.000
168	A	213	ALA	0	-0.021	-0.020	27.188	-0.016	-0.016	0.000	0.000	0.000	0.000
169	A	214	ASP	-1	-0.778	-0.890	25.929	-0.215	-0.215	0.000	0.000	0.000	0.000
170	A	215	TYR	0	-0.053	-0.033	21.267	-0.041	-0.041	0.000	0.000	0.000	0.000
171	A	216	GLU	-1	-0.789	-0.893	22.144	-0.252	-0.252	0.000	0.000	0.000	0.000
172	A	217	GLU	-1	-0.991	-1.003	21.631	-0.367	-0.367	0.000	0.000	0.000	0.000
173	A	218	TRP	0	0.018	0.017	17.789	-0.055	-0.055	0.000	0.000	0.000	0.000
174	A	219	LEU	0	-0.007	0.005	17.610	-0.065	-0.065	0.000	0.000	0.000	0.000
175	A	220	SER	0	0.016	0.013	16.534	-0.088	-0.088	0.000	0.000	0.000	0.000
176	A	221	SER	0	-0.035	-0.020	16.484	-0.076	-0.076	0.000	0.000	0.000	0.000
177	A	222	ILE	0	0.003	0.004	12.667	-0.090	-0.090	0.000	0.000	0.000	0.000
178	A	223	ASN	0	-0.039	-0.008	12.327	-0.113	-0.113	0.000	0.000	0.000	0.000
179	A	224	LYS	1	0.867	0.921	11.564	0.360	0.360	0.000	0.000	0.000	0.000
180	A	225	PHE	0	-0.071	-0.015	10.847	-0.062	-0.062	0.000	0.000	0.000	0.000
181	A	226	VAL	0	-0.051	-0.022	6.829	-0.134	-0.134	0.000	0.000	0.000	0.000
182	A	227	SER	0	-0.043	-0.014	6.943	-0.499	-0.499	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:46:ALA)