FMO DATABASE

FMODB ID: 89K6Y

Calculation Name: 4XW3-A-Xray372

Preferred Name: ATP-dependent RNA helicase DDX1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 4XW3

Chain ID: A

ChEMBL ID: CHEMBL2010634

UniProt ID: Q92499

Base Structure: X-ray

Registration Date: 2023-09-23

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	190
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2166531.667335
FMO2-HF: Nuclear repulsion	2090676.976613
FMO2-HF: Total energy	-75854.690722
FMO2-MP2: Total energy	-76070.374695

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:86:SER)

Summations of interaction energy for fragment #1(A:86:SER)

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.
-6.254	-2.634	0.372	-1.607	-2.385	-0.001

Interaction energy analysis for fragmet #1(A:86:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.024 / q_NPA : 0.003

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	88	LEU	0	0.031	0.000	3.825	-3.614	-1.712	-0.010	-0.897	-0.994	0.003
4	A	89	ASN	0	-0.001	0.003	2.834	-0.566	0.684	0.375	-0.596	-1.029	-0.004
5	A	90	LYS	1	0.869	0.945	4.646	-0.056	0.038	-0.001	-0.012	-0.082	0.000
6	A	91	TRP	0	0.045	0.031	7.014	0.457	0.457	0.000	0.000	0.000	0.000
7	A	92	GLN	0	-0.013	-0.011	8.176	-0.416	-0.416	0.000	0.000	0.000	0.000
8	A	93	MET	0	0.027	0.030	11.282	0.154	0.154	0.000	0.000	0.000	0.000
9	A	94	ASN	0	0.022	-0.004	9.676	0.307	0.307	0.000	0.000	0.000	0.000
10	A	95	PRO	0	0.007	0.005	8.648	-0.122	-0.122	0.000	0.000	0.000	0.000
11	A	96	TYR	0	-0.028	-0.036	5.685	0.211	0.211	0.000	0.000	0.000	0.000
12	A	97	ASP	-1	-0.765	-0.853	11.347	0.730	0.730	0.000	0.000	0.000	0.000
13	A	98	ARG	1	0.854	0.906	13.437	-0.642	-0.642	0.000	0.000	0.000	0.000
14	A	99	GLY	0	0.020	0.022	16.927	0.001	0.001	0.000	0.000	0.000	0.000
15	A	100	SER	0	0.008	-0.011	19.053	0.017	0.017	0.000	0.000	0.000	0.000
16	A	101	ALA	0	0.007	0.008	20.534	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	102	PHE	0	-0.017	-0.006	17.106	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	103	ALA	0	0.006	0.010	17.268	0.050	0.050	0.000	0.000	0.000	0.000
19	A	104	ILE	0	-0.007	-0.019	12.796	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	105	GLY	0	0.042	0.026	14.322	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	106	SER	0	0.011	-0.010	11.595	0.061	0.061	0.000	0.000	0.000	0.000
22	A	107	ASP	-1	-0.739	-0.862	10.871	-0.193	-0.193	0.000	0.000	0.000	0.000
23	A	108	GLY	0	-0.038	-0.003	10.887	-0.034	-0.034	0.000	0.000	0.000	0.000
24	A	109	LEU	0	-0.038	-0.032	11.808	0.110	0.110	0.000	0.000	0.000	0.000
25	A	110	CYS	0	0.012	0.017	15.146	0.025	0.025	0.000	0.000	0.000	0.000
26	A	111	CYS	0	-0.061	-0.018	17.241	0.044	0.044	0.000	0.000	0.000	0.000
27	A	112	GLN	0	0.015	-0.009	19.000	-0.022	-0.022	0.000	0.000	0.000	0.000
28	A	113	SER	0	0.009	0.019	21.144	0.030	0.030	0.000	0.000	0.000	0.000
29	A	114	ARG	1	0.852	0.912	23.778	-0.088	-0.088	0.000	0.000	0.000	0.000
30	A	115	GLU	-1	-0.855	-0.912	26.489	0.162	0.162	0.000	0.000	0.000	0.000
31	A	116	VAL	0	-0.008	-0.010	28.476	0.003	0.003	0.000	0.000	0.000	0.000
32	A	117	LYS	1	0.882	0.908	31.930	-0.121	-0.121	0.000	0.000	0.000	0.000
33	A	118	GLU	-1	-0.860	-0.905	28.232	0.147	0.147	0.000	0.000	0.000	0.000
34	A	119	TRP	0	-0.017	-0.007	27.357	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	120	HIS	0	-0.018	-0.013	22.293	0.043	0.043	0.000	0.000	0.000	0.000
36	A	121	GLY	0	0.044	0.018	21.503	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	122	CYS	0	-0.094	-0.022	15.364	0.043	0.043	0.000	0.000	0.000	0.000
38	A	123	ARG	1	0.842	0.887	16.032	-0.650	-0.650	0.000	0.000	0.000	0.000
39	A	124	ALA	0	0.043	0.005	13.448	0.083	0.083	0.000	0.000	0.000	0.000
40	A	125	THR	0	-0.072	-0.049	7.892	0.052	0.052	0.000	0.000	0.000	0.000
41	A	126	LYS	1	0.855	0.929	8.108	-0.185	-0.185	0.000	0.000	0.000	0.000
42	A	127	GLY	0	0.021	0.013	12.189	-0.090	-0.090	0.000	0.000	0.000	0.000
43	A	128	LEU	0	-0.029	-0.013	15.832	0.006	0.006	0.000	0.000	0.000	0.000
44	A	129	MET	0	-0.002	-0.011	18.530	0.007	0.007	0.000	0.000	0.000	0.000
45	A	130	LYS	1	0.830	0.902	20.762	-0.194	-0.194	0.000	0.000	0.000	0.000
46	A	131	GLY	0	0.075	0.043	21.857	0.005	0.005	0.000	0.000	0.000	0.000
47	A	132	LYS	1	0.834	0.931	24.240	-0.065	-0.065	0.000	0.000	0.000	0.000
48	A	133	HIS	0	-0.018	-0.016	20.705	0.000	0.000	0.000	0.000	0.000	0.000
49	A	134	TYR	0	-0.014	-0.008	21.992	0.015	0.015	0.000	0.000	0.000	0.000
50	A	135	TYR	0	-0.052	-0.035	19.612	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	136	GLU	-1	-0.747	-0.859	21.327	0.008	0.008	0.000	0.000	0.000	0.000
52	A	137	VAL	0	-0.002	-0.012	21.352	0.010	0.010	0.000	0.000	0.000	0.000
53	A	138	SER	0	-0.012	0.010	23.180	-0.014	-0.014	0.000	0.000	0.000	0.000
54	A	139	CYS	0	-0.008	0.006	24.570	0.014	0.014	0.000	0.000	0.000	0.000
55	A	140	HIS	0	-0.030	-0.045	22.274	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	141	ASP	-1	-0.774	-0.884	27.302	0.063	0.063	0.000	0.000	0.000	0.000
57	A	142	GLN	0	-0.019	-0.022	30.158	0.003	0.003	0.000	0.000	0.000	0.000
58	A	143	GLY	0	0.007	0.031	30.289	0.002	0.002	0.000	0.000	0.000	0.000
59	A	144	LEU	0	-0.029	-0.012	30.975	0.001	0.001	0.000	0.000	0.000	0.000
60	A	145	CYS	0	-0.014	-0.010	26.401	0.011	0.011	0.000	0.000	0.000	0.000
61	A	146	ARG	1	0.797	0.879	26.706	-0.201	-0.201	0.000	0.000	0.000	0.000
62	A	147	VAL	0	0.034	0.023	23.716	0.023	0.023	0.000	0.000	0.000	0.000
63	A	148	GLY	0	0.048	0.015	23.336	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	149	TRP	0	0.022	0.017	19.377	0.028	0.028	0.000	0.000	0.000	0.000
65	A	150	SER	0	0.000	-0.002	21.121	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	151	THR	0	0.064	0.033	20.587	0.039	0.039	0.000	0.000	0.000	0.000
67	A	152	MET	0	0.014	0.016	15.477	0.049	0.049	0.000	0.000	0.000	0.000
68	A	153	GLN	0	-0.041	-0.017	19.375	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	154	ALA	0	-0.058	0.000	22.301	-0.026	-0.026	0.000	0.000	0.000	0.000
70	A	155	SER	0	0.044	0.016	22.298	0.047	0.047	0.000	0.000	0.000	0.000
71	A	156	LEU	0	-0.021	0.002	18.191	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	157	ASP	-1	-0.849	-0.900	22.312	0.196	0.196	0.000	0.000	0.000	0.000
73	A	158	LEU	0	0.027	0.015	23.588	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	159	GLY	0	0.014	0.018	25.918	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	160	THR	0	-0.100	-0.068	28.439	-0.017	-0.017	0.000	0.000	0.000	0.000
76	A	161	ASP	-1	-0.728	-0.862	26.871	0.281	0.281	0.000	0.000	0.000	0.000
77	A	162	LYS	1	0.967	0.979	29.934	-0.215	-0.215	0.000	0.000	0.000	0.000
78	A	163	PHE	0	-0.003	-0.004	25.016	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	164	GLY	0	0.033	0.014	25.006	0.029	0.029	0.000	0.000	0.000	0.000
80	A	165	PHE	0	-0.026	-0.005	26.022	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	166	GLY	0	0.007	0.000	26.375	0.015	0.015	0.000	0.000	0.000	0.000
82	A	167	PHE	0	0.013	0.008	28.091	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	168	GLY	0	0.026	0.002	28.991	0.008	0.008	0.000	0.000	0.000	0.000
84	A	169	GLY	0	0.065	0.031	31.249	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	170	THR	0	0.012	0.007	32.826	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	171	GLY	0	-0.007	0.022	35.024	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	172	LYS	1	0.883	0.923	34.830	-0.090	-0.090	0.000	0.000	0.000	0.000
88	A	173	LYS	1	0.904	0.972	32.720	-0.107	-0.107	0.000	0.000	0.000	0.000
89	A	174	SER	0	-0.030	-0.017	30.241	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	175	HIS	0	-0.016	-0.033	29.930	0.005	0.005	0.000	0.000	0.000	0.000
91	A	176	ASN	0	-0.021	-0.003	31.419	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	177	LYS	1	0.928	0.959	32.346	-0.189	-0.189	0.000	0.000	0.000	0.000
93	A	178	GLN	0	-0.044	0.010	34.411	-0.015	-0.015	0.000	0.000	0.000	0.000
94	A	179	PHE	0	-0.009	-0.022	32.459	0.008	0.008	0.000	0.000	0.000	0.000
95	A	180	ASP	-1	-0.864	-0.922	36.681	0.105	0.105	0.000	0.000	0.000	0.000
96	A	181	ASN	0	-0.030	-0.026	37.489	0.005	0.005	0.000	0.000	0.000	0.000
97	A	182	TYR	0	-0.022	-0.040	32.840	0.002	0.002	0.000	0.000	0.000	0.000
98	A	183	GLY	0	0.003	0.017	36.077	0.001	0.001	0.000	0.000	0.000	0.000
99	A	184	GLU	-1	-0.840	-0.908	36.062	0.038	0.038	0.000	0.000	0.000	0.000
100	A	185	GLU	-1	-0.887	-0.946	35.770	0.068	0.068	0.000	0.000	0.000	0.000
101	A	186	PHE	0	-0.076	-0.047	28.982	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	187	THR	0	0.020	0.000	32.306	0.004	0.004	0.000	0.000	0.000	0.000
103	A	188	MET	0	0.006	0.008	30.633	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	189	HIS	0	-0.016	-0.012	30.079	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	190	ASP	-1	-0.781	-0.857	31.025	0.035	0.035	0.000	0.000	0.000	0.000
106	A	191	THR	0	-0.056	-0.043	25.896	0.000	0.000	0.000	0.000	0.000	0.000
107	A	192	ILE	0	-0.018	-0.004	26.990	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	193	GLY	0	0.042	0.027	25.928	0.002	0.002	0.000	0.000	0.000	0.000
109	A	194	CYS	0	-0.046	-0.027	23.578	0.002	0.002	0.000	0.000	0.000	0.000
110	A	195	TYR	0	0.023	0.002	24.363	0.000	0.000	0.000	0.000	0.000	0.000
111	A	196	LEU	0	-0.029	-0.015	22.168	0.009	0.009	0.000	0.000	0.000	0.000
112	A	197	ASP	-1	-0.835	-0.928	25.206	0.106	0.106	0.000	0.000	0.000	0.000
113	A	198	ILE	0	0.000	-0.002	22.959	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	199	ASP	-1	-0.856	-0.922	26.407	0.147	0.147	0.000	0.000	0.000	0.000
115	A	200	LYS	1	0.835	0.912	28.964	-0.096	-0.096	0.000	0.000	0.000	0.000
116	A	201	GLY	0	-0.038	-0.002	29.502	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	202	HIS	0	0.015	0.009	29.797	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	203	VAL	0	0.023	0.013	27.053	0.007	0.007	0.000	0.000	0.000	0.000
119	A	204	LYS	1	0.853	0.945	28.968	-0.083	-0.083	0.000	0.000	0.000	0.000
120	A	205	PHE	0	0.057	0.018	26.458	0.009	0.009	0.000	0.000	0.000	0.000
121	A	206	SER	0	-0.006	0.002	29.843	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	207	LYS	1	0.831	0.909	30.601	-0.040	-0.040	0.000	0.000	0.000	0.000
123	A	208	ASN	0	-0.018	-0.027	31.442	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	209	GLY	0	0.027	0.017	31.788	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	210	LYS	1	0.855	0.934	33.086	-0.042	-0.042	0.000	0.000	0.000	0.000
126	A	211	ASP	-1	-0.840	-0.949	34.351	0.069	0.069	0.000	0.000	0.000	0.000
127	A	212	LEU	0	-0.039	-0.007	33.020	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	213	GLY	0	0.021	0.026	35.499	0.001	0.001	0.000	0.000	0.000	0.000
129	A	214	LEU	0	-0.045	-0.020	33.275	0.006	0.006	0.000	0.000	0.000	0.000
130	A	215	ALA	0	-0.005	0.014	31.876	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	216	PHE	0	-0.015	-0.032	30.634	0.002	0.002	0.000	0.000	0.000	0.000
132	A	217	GLU	-1	-0.807	-0.885	32.349	0.110	0.110	0.000	0.000	0.000	0.000
133	A	218	ILE	0	-0.048	-0.036	26.770	0.007	0.007	0.000	0.000	0.000	0.000
134	A	219	PRO	0	0.040	0.022	30.366	-0.010	-0.010	0.000	0.000	0.000	0.000
135	A	220	PRO	0	0.043	-0.009	31.574	0.012	0.012	0.000	0.000	0.000	0.000
136	A	221	HIS	0	-0.050	-0.032	29.857	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	222	MET	0	-0.009	0.021	26.026	0.011	0.011	0.000	0.000	0.000	0.000
138	A	223	LYS	1	0.900	0.970	26.891	-0.150	-0.150	0.000	0.000	0.000	0.000
139	A	224	ASN	0	-0.030	-0.022	25.458	0.002	0.002	0.000	0.000	0.000	0.000
140	A	225	GLN	0	-0.015	-0.007	22.903	0.033	0.033	0.000	0.000	0.000	0.000
141	A	226	ALA	0	0.020	0.010	18.186	-0.018	-0.018	0.000	0.000	0.000	0.000
142	A	227	LEU	0	-0.019	-0.010	20.287	0.018	0.018	0.000	0.000	0.000	0.000
143	A	228	PHE	0	-0.004	0.000	13.508	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	229	PRO	0	-0.005	0.012	16.320	-0.029	-0.029	0.000	0.000	0.000	0.000
145	A	230	ALA	0	-0.005	0.004	17.767	0.070	0.070	0.000	0.000	0.000	0.000
146	A	231	CYS	0	-0.047	-0.005	19.760	-0.049	-0.049	0.000	0.000	0.000	0.000
147	A	232	VAL	0	-0.005	-0.004	21.892	0.034	0.034	0.000	0.000	0.000	0.000
148	A	233	LEU	0	-0.003	0.000	22.070	-0.025	-0.025	0.000	0.000	0.000	0.000
149	A	234	LYS	1	0.897	0.949	25.812	-0.123	-0.123	0.000	0.000	0.000	0.000
150	A	235	ASN	0	-0.016	-0.016	27.913	-0.013	-0.013	0.000	0.000	0.000	0.000
151	A	236	ALA	0	0.025	0.024	26.722	-0.013	-0.013	0.000	0.000	0.000	0.000
152	A	237	GLU	-1	-0.792	-0.888	22.627	0.048	0.048	0.000	0.000	0.000	0.000
153	A	238	LEU	0	-0.018	-0.013	22.094	-0.007	-0.007	0.000	0.000	0.000	0.000
154	A	239	LYS	1	0.851	0.925	16.984	0.116	0.116	0.000	0.000	0.000	0.000
155	A	240	PHE	0	-0.013	-0.016	16.951	0.007	0.007	0.000	0.000	0.000	0.000
156	A	241	ASN	0	0.056	0.006	17.713	-0.041	-0.041	0.000	0.000	0.000	0.000
157	A	242	PHE	0	-0.019	-0.027	14.094	0.031	0.031	0.000	0.000	0.000	0.000
158	A	243	GLY	0	0.049	0.017	17.235	0.017	0.017	0.000	0.000	0.000	0.000
159	A	244	GLU	-1	-0.882	-0.893	12.822	-0.228	-0.228	0.000	0.000	0.000	0.000
160	A	245	GLU	-1	-0.877	-0.919	16.243	-0.189	-0.189	0.000	0.000	0.000	0.000
161	A	246	GLU	-1	-0.923	-0.953	19.096	-0.068	-0.068	0.000	0.000	0.000	0.000
162	A	247	PHE	0	-0.084	-0.044	21.028	0.009	0.009	0.000	0.000	0.000	0.000
163	A	248	LYS	1	0.914	0.945	24.362	0.011	0.011	0.000	0.000	0.000	0.000
164	A	249	PHE	0	-0.009	-0.015	27.345	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	250	PRO	0	0.006	0.008	26.976	0.011	0.011	0.000	0.000	0.000	0.000
166	A	251	PRO	0	-0.033	0.006	25.151	0.005	0.005	0.000	0.000	0.000	0.000
167	A	252	LYS	1	0.871	0.922	28.306	-0.055	-0.055	0.000	0.000	0.000	0.000
168	A	253	ASP	-1	-0.818	-0.926	30.275	0.058	0.058	0.000	0.000	0.000	0.000
169	A	254	GLY	0	0.013	0.001	29.726	0.008	0.008	0.000	0.000	0.000	0.000
170	A	255	PHE	0	-0.068	-0.017	26.057	0.007	0.007	0.000	0.000	0.000	0.000
171	A	256	VAL	0	0.030	0.015	21.917	-0.015	-0.015	0.000	0.000	0.000	0.000
172	A	257	ALA	0	0.073	0.025	19.208	0.021	0.021	0.000	0.000	0.000	0.000
173	A	258	LEU	0	-0.023	-0.004	16.433	0.003	0.003	0.000	0.000	0.000	0.000
174	A	259	SER	0	-0.081	-0.086	14.123	0.041	0.041	0.000	0.000	0.000	0.000
175	A	260	LYS	1	0.822	0.900	14.833	0.137	0.137	0.000	0.000	0.000	0.000
176	A	261	ALA	0	-0.013	0.006	16.635	-0.004	-0.004	0.000	0.000	0.000	0.000
177	A	262	PRO	0	0.012	0.000	16.100	0.000	0.000	0.000	0.000	0.000	0.000
178	A	263	ASP	-1	-0.857	-0.935	12.564	0.164	0.164	0.000	0.000	0.000	0.000
179	A	264	GLY	0	-0.045	-0.018	15.000	0.068	0.068	0.000	0.000	0.000	0.000
180	A	265	TYR	0	-0.051	-0.027	17.666	0.009	0.009	0.000	0.000	0.000	0.000
181	A	266	ILE	0	-0.019	-0.003	12.589	0.019	0.019	0.000	0.000	0.000	0.000
182	A	267	VAL	0	0.010	0.014	14.157	0.023	0.023	0.000	0.000	0.000	0.000
183	A	268	LYS	1	0.896	0.942	6.133	-2.122	-2.122	0.000	0.000	0.000	0.000
184	A	269	SER	0	0.028	0.011	10.655	-0.108	-0.108	0.000	0.000	0.000	0.000
185	A	270	GLN	0	-0.016	-0.030	11.216	0.149	0.149	0.000	0.000	0.000	0.000
186	A	271	HIS	0	-0.058	-0.019	12.141	-0.034	-0.034	0.000	0.000	0.000	0.000
187	A	272	SER	0	-0.005	-0.013	7.265	0.311	0.311	0.000	0.000	0.000	0.000
188	A	273	GLY	0	0.041	0.015	6.825	-0.611	-0.611	0.000	0.000	0.000	0.000
189	A	274	ASN	0	-0.008	0.007	5.657	1.172	1.172	0.000	0.000	0.000	0.000
190	A	275	ALA	0	0.023	0.028	3.699	-0.828	-0.454	0.008	-0.102	-0.280	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:86:SER)