FMO DATABASE

FMODB ID: J3829

Calculation Name: 1MJS-A-Xray372

Preferred Name: Mothers against decapentaplegic homolog 3

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1MJS

Chain ID: A

ChEMBL ID: CHEMBL1293258

UniProt ID: P84022

Base Structure: X-ray

Registration Date: 2023-06-21

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	OptH
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	183
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1969211.853423
FMO2-HF: Nuclear repulsion	1895337.037813
FMO2-HF: Total energy	-73874.81561
FMO2-MP2: Total energy	-74084.64791

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:228:PRO)

Summations of interaction energy for fragment #1(A:228:PRO)

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.
-8.362	-1.617	6.443	-3.847	-9.342	-0.032

Interaction energy analysis for fragmet #1(A:228:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.009 / q_NPA : -0.009

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	230	PHE	0	0.042	0.012	3.169	-0.620	1.007	0.019	-0.667	-0.979	0.002
4	A	231	TRP	0	0.018	-0.008	2.629	-3.252	-0.886	0.801	-1.268	-1.899	-0.008
5	A	232	CYS	0	-0.036	-0.017	3.461	0.755	0.757	0.012	0.249	-0.263	0.000
6	A	233	SER	0	0.017	0.032	6.617	-0.098	-0.098	0.000	0.000	0.000	0.000
7	A	234	ILE	0	0.011	-0.012	9.349	0.111	0.111	0.000	0.000	0.000	0.000
8	A	235	SER	0	-0.006	0.009	12.882	0.021	0.021	0.000	0.000	0.000	0.000
9	A	236	TYR	0	-0.016	-0.038	16.093	0.018	0.018	0.000	0.000	0.000	0.000
10	A	237	TYR	0	0.027	0.004	17.992	0.015	0.015	0.000	0.000	0.000	0.000
11	A	238	GLU	-1	-0.712	-0.827	22.671	-0.180	-0.180	0.000	0.000	0.000	0.000
12	A	239	LEU	0	-0.008	0.004	26.367	0.011	0.011	0.000	0.000	0.000	0.000
13	A	240	ASN	0	-0.016	-0.011	26.234	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	241	GLN	0	0.022	0.021	26.424	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	242	ARG	1	0.886	0.952	16.640	0.316	0.316	0.000	0.000	0.000	0.000
16	A	243	VAL	0	-0.036	-0.024	22.214	0.012	0.012	0.000	0.000	0.000	0.000
17	A	244	GLY	0	0.020	0.005	21.303	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	245	GLU	-1	-0.930	-0.958	17.593	-0.319	-0.319	0.000	0.000	0.000	0.000
19	A	246	THR	0	-0.052	-0.029	12.153	0.027	0.027	0.000	0.000	0.000	0.000
20	A	247	PHE	0	-0.010	0.013	11.818	-0.023	-0.023	0.000	0.000	0.000	0.000
21	A	248	HIS	0	0.042	0.016	8.634	-0.174	-0.174	0.000	0.000	0.000	0.000
22	A	249	ALA	0	0.017	0.004	7.901	0.059	0.059	0.000	0.000	0.000	0.000
23	A	250	SER	0	0.011	-0.004	6.707	-0.503	-0.503	0.000	0.000	0.000	0.000
24	A	251	GLN	0	0.015	0.022	7.896	-0.053	-0.053	0.000	0.000	0.000	0.000
25	A	252	PRO	0	0.010	0.015	7.881	-0.072	-0.072	0.000	0.000	0.000	0.000
26	A	253	SER	0	0.009	0.000	8.868	0.149	0.149	0.000	0.000	0.000	0.000
27	A	254	MET	0	-0.014	0.012	11.246	-0.066	-0.066	0.000	0.000	0.000	0.000
28	A	255	THR	0	-0.007	-0.002	13.878	0.026	0.026	0.000	0.000	0.000	0.000
29	A	256	VAL	0	0.005	0.019	15.725	-0.032	-0.032	0.000	0.000	0.000	0.000
30	A	257	ASP	-1	-0.822	-0.912	18.201	-0.276	-0.276	0.000	0.000	0.000	0.000
31	A	258	GLY	0	0.024	-0.003	21.946	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	259	PHE	0	-0.021	-0.005	24.439	0.024	0.024	0.000	0.000	0.000	0.000
33	A	260	THR	0	-0.043	-0.029	25.371	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	261	ASP	-1	-0.894	-0.936	24.311	-0.218	-0.218	0.000	0.000	0.000	0.000
35	A	262	PRO	0	-0.008	-0.006	23.145	-0.014	-0.014	0.000	0.000	0.000	0.000
36	A	263	SER	0	0.057	0.020	17.893	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	264	ASN	0	0.009	0.007	17.613	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	265	SER	0	0.036	-0.002	12.782	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	266	GLU	-1	-0.950	-0.978	12.837	-0.610	-0.610	0.000	0.000	0.000	0.000
40	A	267	ARG	1	0.855	0.938	15.106	0.360	0.360	0.000	0.000	0.000	0.000
41	A	268	PHE	0	0.024	0.013	15.639	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	269	CYS	0	-0.032	-0.019	17.609	0.016	0.016	0.000	0.000	0.000	0.000
43	A	270	LEU	0	-0.009	-0.021	19.652	0.009	0.009	0.000	0.000	0.000	0.000
44	A	271	GLY	0	0.011	0.010	23.035	0.020	0.020	0.000	0.000	0.000	0.000
45	A	272	LEU	0	-0.019	-0.017	24.736	0.016	0.016	0.000	0.000	0.000	0.000
46	A	273	LEU	0	-0.017	0.015	21.255	0.012	0.012	0.000	0.000	0.000	0.000
47	A	274	SER	0	0.000	0.003	25.689	0.010	0.010	0.000	0.000	0.000	0.000
48	A	275	ASN	0	0.002	-0.034	27.723	0.000	0.000	0.000	0.000	0.000	0.000
49	A	276	VAL	0	0.044	0.023	29.907	0.005	0.005	0.000	0.000	0.000	0.000
50	A	277	ASN	0	-0.030	-0.010	32.123	0.005	0.005	0.000	0.000	0.000	0.000
51	A	278	ARG	1	0.785	0.900	27.866	0.169	0.169	0.000	0.000	0.000	0.000
52	A	279	ASN	0	0.066	0.045	32.937	0.003	0.003	0.000	0.000	0.000	0.000
53	A	280	ALA	0	0.122	0.029	34.631	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	281	ALA	0	-0.015	-0.001	34.606	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	282	VAL	0	-0.010	-0.010	29.065	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	283	GLU	-1	-0.938	-0.973	30.900	-0.133	-0.133	0.000	0.000	0.000	0.000
57	A	284	LEU	0	-0.036	-0.007	32.912	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	285	THR	0	-0.012	-0.018	28.315	0.000	0.000	0.000	0.000	0.000	0.000
59	A	286	ARG	1	0.888	0.933	25.890	0.191	0.191	0.000	0.000	0.000	0.000
60	A	287	ARG	1	0.900	0.959	28.900	0.120	0.120	0.000	0.000	0.000	0.000
61	A	288	HIS	0	-0.037	-0.014	30.600	0.007	0.007	0.000	0.000	0.000	0.000
62	A	289	ILE	0	-0.030	0.009	23.898	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	290	GLY	0	0.057	0.031	26.074	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	291	ARG	1	0.985	0.969	23.939	0.194	0.194	0.000	0.000	0.000	0.000
65	A	292	GLY	0	0.005	0.014	22.046	-0.023	-0.023	0.000	0.000	0.000	0.000
66	A	293	VAL	0	-0.023	-0.006	17.182	0.021	0.021	0.000	0.000	0.000	0.000
67	A	294	ARG	1	0.938	0.981	15.920	0.382	0.382	0.000	0.000	0.000	0.000
68	A	295	LEU	0	-0.040	-0.025	12.089	0.034	0.034	0.000	0.000	0.000	0.000
69	A	296	TYR	0	-0.034	-0.066	11.846	-0.063	-0.063	0.000	0.000	0.000	0.000
70	A	297	TYR	0	0.007	0.014	2.947	-0.616	0.264	0.061	-0.284	-0.657	-0.001
71	A	298	ILE	0	0.018	-0.013	8.816	-0.048	-0.048	0.000	0.000	0.000	0.000
72	A	299	GLY	0	0.028	0.018	8.295	0.074	0.074	0.000	0.000	0.000	0.000
73	A	300	GLY	0	-0.027	-0.007	6.242	0.134	0.134	0.000	0.000	0.000	0.000
74	A	301	GLU	-1	-0.791	-0.887	7.189	-0.070	-0.070	0.000	0.000	0.000	0.000
75	A	302	VAL	0	0.003	0.005	8.407	-0.123	-0.123	0.000	0.000	0.000	0.000
76	A	303	PHE	0	-0.016	-0.012	10.911	0.092	0.092	0.000	0.000	0.000	0.000
77	A	304	ALA	0	0.012	0.007	14.093	-0.061	-0.061	0.000	0.000	0.000	0.000
78	A	305	GLU	-1	-0.856	-0.906	16.648	-0.211	-0.211	0.000	0.000	0.000	0.000
79	A	306	CYS	0	-0.044	0.002	19.713	-0.022	-0.022	0.000	0.000	0.000	0.000
80	A	307	LEU	0	-0.044	-0.020	20.574	0.019	0.019	0.000	0.000	0.000	0.000
81	A	308	SER	0	-0.050	-0.020	23.871	0.018	0.018	0.000	0.000	0.000	0.000
82	A	309	ASP	-1	-0.871	-0.937	26.218	-0.139	-0.139	0.000	0.000	0.000	0.000
83	A	310	SER	0	0.003	-0.002	28.469	0.015	0.015	0.000	0.000	0.000	0.000
84	A	311	ALA	0	-0.047	-0.037	26.858	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	312	ILE	0	0.018	0.013	20.184	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	313	PHE	0	-0.058	-0.028	23.386	0.017	0.017	0.000	0.000	0.000	0.000
87	A	314	VAL	0	0.046	0.016	17.298	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	315	GLN	0	-0.004	0.009	19.353	0.015	0.015	0.000	0.000	0.000	0.000
89	A	316	SER	0	0.004	-0.027	15.090	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	317	PRO	0	0.037	0.017	16.022	0.018	0.018	0.000	0.000	0.000	0.000
91	A	318	ASN	0	0.007	0.001	13.586	0.001	0.001	0.000	0.000	0.000	0.000
92	A	319	CYS	0	-0.002	0.011	16.106	0.013	0.013	0.000	0.000	0.000	0.000
93	A	320	ASN	0	-0.013	-0.017	18.044	0.009	0.009	0.000	0.000	0.000	0.000
94	A	321	GLN	0	-0.004	0.042	18.736	0.009	0.009	0.000	0.000	0.000	0.000
95	A	322	ARG	1	0.976	1.011	20.569	0.025	0.025	0.000	0.000	0.000	0.000
96	A	323	TYR	0	-0.048	-0.072	21.802	0.002	0.002	0.000	0.000	0.000	0.000
97	A	324	GLY	0	0.035	0.043	25.634	0.001	0.001	0.000	0.000	0.000	0.000
98	A	325	TRP	0	-0.082	-0.050	23.938	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	326	HIS	0	0.012	-0.007	23.390	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	327	PRO	0	-0.038	-0.002	22.744	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	328	ALA	0	0.014	-0.006	22.728	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	329	THR	0	-0.012	-0.003	23.687	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	330	VAL	0	-0.003	-0.007	22.935	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	331	CYS	0	-0.015	0.000	21.441	0.013	0.013	0.000	0.000	0.000	0.000
105	A	332	LYS	1	0.969	0.990	23.402	0.098	0.098	0.000	0.000	0.000	0.000
106	A	333	ILE	0	-0.007	0.004	19.778	0.008	0.008	0.000	0.000	0.000	0.000
107	A	334	PRO	0	-0.027	-0.042	24.314	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	335	PRO	0	0.049	0.001	26.140	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	336	GLY	0	0.001	0.011	25.831	0.011	0.011	0.000	0.000	0.000	0.000
110	A	337	CYS	0	-0.050	0.009	24.804	0.007	0.007	0.000	0.000	0.000	0.000
111	A	338	ASN	0	-0.001	-0.012	19.735	-0.017	-0.017	0.000	0.000	0.000	0.000
112	A	339	LEU	0	0.027	0.009	18.949	0.023	0.023	0.000	0.000	0.000	0.000
113	A	340	LYS	1	0.839	0.927	14.500	0.064	0.064	0.000	0.000	0.000	0.000
114	A	341	ILE	0	-0.018	-0.021	12.922	0.026	0.026	0.000	0.000	0.000	0.000
115	A	342	PHE	0	0.017	0.022	8.714	-0.008	-0.008	0.000	0.000	0.000	0.000
116	A	343	ASN	0	0.041	0.008	12.116	0.005	0.005	0.000	0.000	0.000	0.000
117	A	344	ASN	0	0.074	0.015	8.365	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	345	GLN	0	-0.025	-0.004	11.322	0.055	0.055	0.000	0.000	0.000	0.000
119	A	346	GLU	-1	-0.875	-0.950	14.640	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	347	PHE	0	0.024	0.005	9.901	0.008	0.008	0.000	0.000	0.000	0.000
121	A	348	ALA	0	0.023	0.009	12.318	0.029	0.029	0.000	0.000	0.000	0.000
122	A	349	ALA	0	-0.025	-0.002	13.654	0.017	0.017	0.000	0.000	0.000	0.000
123	A	350	LEU	0	0.010	-0.002	16.383	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	351	LEU	0	0.014	0.028	11.866	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	352	ALA	0	-0.020	-0.015	15.889	0.008	0.008	0.000	0.000	0.000	0.000
126	A	353	GLN	0	-0.052	-0.026	17.819	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	354	SER	0	0.026	-0.019	18.238	-0.015	-0.015	0.000	0.000	0.000	0.000
128	A	355	VAL	0	0.009	0.005	17.656	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	356	ASN	0	-0.060	-0.025	20.136	0.002	0.002	0.000	0.000	0.000	0.000
130	A	357	GLN	0	-0.044	-0.020	22.983	-0.008	-0.008	0.000	0.000	0.000	0.000
131	A	358	GLY	0	0.022	0.026	23.000	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	359	PHE	0	0.028	-0.004	18.040	0.003	0.003	0.000	0.000	0.000	0.000
133	A	360	GLU	-1	-0.890	-0.955	19.591	0.052	0.052	0.000	0.000	0.000	0.000
134	A	361	ALA	0	-0.013	0.003	20.609	-0.012	-0.012	0.000	0.000	0.000	0.000
135	A	362	VAL	0	0.016	0.002	15.464	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	363	TYR	0	0.031	0.019	15.589	-0.010	-0.010	0.000	0.000	0.000	0.000
137	A	364	GLN	0	0.048	0.030	16.433	-0.024	-0.024	0.000	0.000	0.000	0.000
138	A	365	LEU	0	-0.016	-0.010	13.871	-0.031	-0.031	0.000	0.000	0.000	0.000
139	A	366	THR	0	-0.024	-0.016	12.591	-0.041	-0.041	0.000	0.000	0.000	0.000
140	A	367	ARG	1	0.952	0.974	13.278	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	368	MET	0	-0.082	-0.032	13.521	-0.021	-0.021	0.000	0.000	0.000	0.000
142	A	369	CYS	0	-0.063	-0.009	9.301	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	370	THR	0	0.016	0.020	10.504	-0.096	-0.096	0.000	0.000	0.000	0.000
144	A	371	ILE	0	-0.035	-0.012	12.091	0.049	0.049	0.000	0.000	0.000	0.000
145	A	372	ARG	1	0.848	0.928	14.830	0.162	0.162	0.000	0.000	0.000	0.000
146	A	373	MET	0	-0.002	-0.012	16.956	0.008	0.008	0.000	0.000	0.000	0.000
147	A	374	SER	0	-0.029	-0.032	19.624	-0.009	-0.009	0.000	0.000	0.000	0.000
148	A	375	PHE	0	0.059	0.016	19.967	0.005	0.005	0.000	0.000	0.000	0.000
149	A	376	VAL	0	0.025	0.032	25.028	0.012	0.012	0.000	0.000	0.000	0.000
150	A	377	LYS	1	0.910	0.951	28.271	0.128	0.128	0.000	0.000	0.000	0.000
151	A	378	GLY	0	0.057	0.056	26.840	-0.012	-0.012	0.000	0.000	0.000	0.000
152	A	379	TRP	0	-0.032	-0.020	21.331	0.003	0.003	0.000	0.000	0.000	0.000
153	A	387	THR	0	0.051	0.022	27.354	0.000	0.000	0.000	0.000	0.000	0.000
154	A	388	VAL	0	0.016	0.003	22.100	0.001	0.001	0.000	0.000	0.000	0.000
155	A	389	THR	0	0.017	0.003	25.391	-0.007	-0.007	0.000	0.000	0.000	0.000
156	A	390	SER	0	-0.058	-0.021	26.884	0.003	0.003	0.000	0.000	0.000	0.000
157	A	391	THR	0	-0.028	0.006	25.190	0.005	0.005	0.000	0.000	0.000	0.000
158	A	392	PRO	0	0.003	-0.028	27.576	-0.006	-0.006	0.000	0.000	0.000	0.000
159	A	393	CYS	0	0.003	0.015	24.896	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	394	TRP	0	-0.021	-0.022	19.635	-0.003	-0.003	0.000	0.000	0.000	0.000
161	A	395	ILE	0	0.002	0.004	16.157	-0.007	-0.007	0.000	0.000	0.000	0.000
162	A	396	GLU	-1	-0.831	-0.912	15.060	-0.236	-0.236	0.000	0.000	0.000	0.000
163	A	397	LEU	0	-0.013	-0.011	11.051	-0.047	-0.047	0.000	0.000	0.000	0.000
164	A	398	HIS	0	-0.032	-0.010	9.636	0.061	0.061	0.000	0.000	0.000	0.000
165	A	399	LEU	0	0.012	-0.006	6.366	-0.228	-0.228	0.000	0.000	0.000	0.000
166	A	400	ASN	0	0.039	-0.008	3.000	0.422	0.899	0.119	-0.145	-0.452	0.000
167	A	401	GLY	0	-0.009	0.013	2.487	-1.617	-0.143	1.312	-1.350	-1.436	0.001
168	A	402	PRO	0	0.004	-0.015	2.834	1.966	0.466	0.190	1.674	-0.364	0.000
169	A	403	LEU	0	0.063	0.030	6.464	0.161	0.161	0.000	0.000	0.000	0.000
170	A	404	GLN	0	0.017	0.009	2.302	-4.099	-2.680	3.929	-2.056	-3.292	-0.026
171	A	405	TRP	0	-0.055	-0.015	5.942	0.242	0.242	0.000	0.000	0.000	0.000
172	A	406	LEU	0	0.043	0.000	7.901	-0.018	-0.018	0.000	0.000	0.000	0.000
173	A	407	ASP	-1	-0.920	-0.943	9.003	0.490	0.490	0.000	0.000	0.000	0.000
174	A	408	LYS	1	0.965	0.996	9.206	-1.024	-1.024	0.000	0.000	0.000	0.000
175	A	409	VAL	0	-0.042	-0.026	11.327	-0.053	-0.053	0.000	0.000	0.000	0.000
176	A	410	LEU	0	0.011	-0.008	13.806	-0.046	-0.046	0.000	0.000	0.000	0.000
177	A	411	THR	0	-0.016	-0.014	13.429	-0.045	-0.045	0.000	0.000	0.000	0.000
178	A	412	GLN	0	-0.070	-0.047	15.171	0.008	0.008	0.000	0.000	0.000	0.000
179	A	413	MET	0	-0.102	-0.020	17.634	-0.029	-0.029	0.000	0.000	0.000	0.000
180	A	414	GLY	0	0.018	0.025	19.758	-0.033	-0.033	0.000	0.000	0.000	0.000
181	A	415	SER	0	-0.037	-0.032	21.465	-0.005	-0.005	0.000	0.000	0.000	0.000
182	A	416	PRO	0	0.015	0.006	25.188	-0.003	-0.003	0.000	0.000	0.000	0.000
183	A	417	SER	0	-0.032	0.002	27.312	-0.012	-0.012	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:228:PRO)