FMO DATABASE

FMODB ID: 9LZZ2

Calculation Name: 1OY2-A-Other547

Preferred Name: SHC-transforming protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1OY2

Chain ID: A

ChEMBL ID: CHEMBL5626

UniProt ID: P29353

Base Structure: SolutionNMR

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	191
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1899145.296711
FMO2-HF: Nuclear repulsion	1823895.630197
FMO2-HF: Total energy	-75249.666514
FMO2-MP2: Total energy	-75462.440715

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:17:GLY)

Summations of interaction energy for fragment #1(A:17:GLY)

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.
7.027	7.804	0.002	-0.474	-0.304	-0.002

Interaction energy analysis for fragmet #1(A:17:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.836 / q_NPA : 0.911

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	19	LEU	0	0.031	0.006	3.807	-8.591	-7.814	0.002	-0.474	-0.304	-0.002
4	A	20	GLY	0	0.000	0.018	6.492	4.780	4.780	0.000	0.000	0.000	0.000
5	A	21	GLY	0	-0.013	-0.017	7.803	-4.767	-4.767	0.000	0.000	0.000	0.000
6	A	22	GLU	-1	-0.958	-0.983	10.202	-17.346	-17.346	0.000	0.000	0.000	0.000
7	A	23	GLU	-1	-0.940	-0.950	11.000	-25.149	-25.149	0.000	0.000	0.000	0.000
8	A	24	TRP	0	-0.044	-0.029	13.215	0.163	0.163	0.000	0.000	0.000	0.000
9	A	25	THR	0	0.019	0.010	16.873	0.306	0.306	0.000	0.000	0.000	0.000
10	A	26	ARG	1	0.927	0.963	20.519	14.066	14.066	0.000	0.000	0.000	0.000
11	A	27	HIS	0	0.028	0.018	18.767	0.670	0.670	0.000	0.000	0.000	0.000
12	A	28	GLY	0	-0.003	0.004	23.679	0.410	0.410	0.000	0.000	0.000	0.000
13	A	29	SER	0	0.028	0.012	26.509	-0.211	-0.211	0.000	0.000	0.000	0.000
14	A	30	PHE	0	0.007	-0.006	27.924	-0.020	-0.020	0.000	0.000	0.000	0.000
15	A	31	VAL	0	-0.028	-0.006	30.858	0.210	0.210	0.000	0.000	0.000	0.000
16	A	32	ASN	0	0.029	0.001	33.274	0.007	0.007	0.000	0.000	0.000	0.000
17	A	33	LYS	1	0.937	0.969	35.560	8.687	8.687	0.000	0.000	0.000	0.000
18	A	34	PRO	0	0.023	0.031	35.533	-0.243	-0.243	0.000	0.000	0.000	0.000
19	A	35	THR	0	-0.003	-0.016	32.562	0.073	0.073	0.000	0.000	0.000	0.000
20	A	36	ARG	1	0.926	0.971	36.058	8.264	8.264	0.000	0.000	0.000	0.000
21	A	37	GLY	0	0.046	0.018	33.143	-0.061	-0.061	0.000	0.000	0.000	0.000
22	A	38	TRP	0	-0.058	-0.042	32.199	0.168	0.168	0.000	0.000	0.000	0.000
23	A	39	LEU	0	0.009	0.033	34.082	-0.186	-0.186	0.000	0.000	0.000	0.000
24	A	40	HIS	0	0.006	-0.017	35.636	0.237	0.237	0.000	0.000	0.000	0.000
25	A	41	PRO	0	-0.006	0.011	32.771	0.018	0.018	0.000	0.000	0.000	0.000
26	A	42	ASN	0	0.042	-0.003	29.506	0.199	0.199	0.000	0.000	0.000	0.000
27	A	43	ASP	-1	-0.887	-0.943	27.859	-11.956	-11.956	0.000	0.000	0.000	0.000
28	A	44	LYS	1	0.942	0.976	28.032	9.256	9.256	0.000	0.000	0.000	0.000
29	A	45	VAL	0	-0.022	-0.021	27.922	0.013	0.013	0.000	0.000	0.000	0.000
30	A	46	MET	0	-0.029	-0.007	24.252	-0.354	-0.354	0.000	0.000	0.000	0.000
31	A	47	GLY	0	0.047	0.037	23.252	-0.621	-0.621	0.000	0.000	0.000	0.000
32	A	48	PRO	0	-0.105	-0.040	24.370	-0.283	-0.283	0.000	0.000	0.000	0.000
33	A	49	GLY	0	0.048	0.033	26.954	-0.161	-0.161	0.000	0.000	0.000	0.000
34	A	50	VAL	0	-0.093	-0.051	27.975	0.349	0.349	0.000	0.000	0.000	0.000
35	A	51	SER	0	0.017	0.006	29.948	-0.125	-0.125	0.000	0.000	0.000	0.000
36	A	52	TYR	0	0.026	0.000	31.895	0.264	0.264	0.000	0.000	0.000	0.000
37	A	53	LEU	0	-0.021	-0.009	34.794	-0.159	-0.159	0.000	0.000	0.000	0.000
38	A	54	VAL	0	-0.019	-0.008	34.970	0.238	0.238	0.000	0.000	0.000	0.000
39	A	55	ARG	1	0.935	0.974	36.861	7.477	7.477	0.000	0.000	0.000	0.000
40	A	56	TYR	0	-0.006	-0.006	32.856	0.028	0.028	0.000	0.000	0.000	0.000
41	A	57	MET	0	-0.035	-0.003	36.459	0.195	0.195	0.000	0.000	0.000	0.000
42	A	58	GLY	0	0.014	0.008	37.312	-0.166	-0.166	0.000	0.000	0.000	0.000
43	A	59	CYS	0	0.002	0.005	35.086	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	60	VAL	0	-0.029	-0.016	37.811	0.241	0.241	0.000	0.000	0.000	0.000
45	A	61	GLU	-1	-0.903	-0.944	37.911	-8.517	-8.517	0.000	0.000	0.000	0.000
46	A	62	VAL	0	-0.029	-0.024	40.044	0.309	0.309	0.000	0.000	0.000	0.000
47	A	63	LEU	0	0.053	0.019	41.020	-0.144	-0.144	0.000	0.000	0.000	0.000
48	A	64	GLN	0	0.008	0.026	42.508	0.187	0.187	0.000	0.000	0.000	0.000
49	A	65	SER	0	-0.022	-0.021	42.618	-0.146	-0.146	0.000	0.000	0.000	0.000
50	A	66	MET	0	0.021	0.013	43.796	0.009	0.009	0.000	0.000	0.000	0.000
51	A	67	ARG	1	0.946	0.980	46.779	6.221	6.221	0.000	0.000	0.000	0.000
52	A	68	ALA	0	0.040	0.021	47.741	0.016	0.016	0.000	0.000	0.000	0.000
53	A	69	LEU	0	-0.036	-0.006	49.834	0.129	0.129	0.000	0.000	0.000	0.000
54	A	70	ASP	-1	-0.886	-0.948	51.815	-5.804	-5.804	0.000	0.000	0.000	0.000
55	A	71	PHE	0	-0.026	-0.008	49.088	-0.077	-0.077	0.000	0.000	0.000	0.000
56	A	72	ASN	0	-0.050	-0.007	47.517	-0.164	-0.164	0.000	0.000	0.000	0.000
57	A	73	THR	0	0.076	-0.021	46.104	0.152	0.152	0.000	0.000	0.000	0.000
58	A	74	ARG	1	0.902	0.962	39.852	7.681	7.681	0.000	0.000	0.000	0.000
59	A	75	THR	0	0.066	0.043	45.899	-0.048	-0.048	0.000	0.000	0.000	0.000
60	A	76	GLN	0	0.018	0.009	48.393	-0.075	-0.075	0.000	0.000	0.000	0.000
61	A	77	VAL	0	0.033	0.006	43.911	0.043	0.043	0.000	0.000	0.000	0.000
62	A	78	THR	0	0.027	0.005	43.489	-0.097	-0.097	0.000	0.000	0.000	0.000
63	A	79	ARG	1	1.021	1.018	45.391	5.931	5.931	0.000	0.000	0.000	0.000
64	A	80	GLU	-1	-0.886	-0.928	48.571	-6.305	-6.305	0.000	0.000	0.000	0.000
65	A	81	ALA	0	0.014	-0.002	43.241	-0.026	-0.026	0.000	0.000	0.000	0.000
66	A	82	ILE	0	0.024	0.014	43.757	-0.080	-0.080	0.000	0.000	0.000	0.000
67	A	83	SER	0	-0.023	-0.029	45.484	0.055	0.055	0.000	0.000	0.000	0.000
68	A	84	LEU	0	-0.032	-0.013	45.781	0.043	0.043	0.000	0.000	0.000	0.000
69	A	85	VAL	0	0.002	-0.007	41.142	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	86	CYS	0	-0.030	0.005	44.277	0.052	0.052	0.000	0.000	0.000	0.000
71	A	87	GLU	-1	-0.826	-0.908	47.014	-6.010	-6.010	0.000	0.000	0.000	0.000
72	A	88	ALA	0	-0.058	-0.017	44.495	0.062	0.062	0.000	0.000	0.000	0.000
73	A	89	VAL	0	-0.035	-0.016	43.027	-0.015	-0.015	0.000	0.000	0.000	0.000
74	A	90	PRO	0	0.008	0.003	45.842	0.029	0.029	0.000	0.000	0.000	0.000
75	A	91	GLY	0	-0.044	-0.024	47.971	0.105	0.105	0.000	0.000	0.000	0.000
76	A	92	ALA	0	0.046	0.031	45.311	0.016	0.016	0.000	0.000	0.000	0.000
77	A	93	LYS	1	0.862	0.941	47.319	6.335	6.335	0.000	0.000	0.000	0.000
78	A	94	GLY	0	0.065	0.019	49.223	0.006	0.006	0.000	0.000	0.000	0.000
79	A	95	ALA	0	0.015	0.004	50.174	0.114	0.114	0.000	0.000	0.000	0.000
80	A	96	THR	0	-0.051	-0.030	50.715	0.198	0.198	0.000	0.000	0.000	0.000
81	A	97	ARG	1	0.993	0.974	52.446	5.426	5.426	0.000	0.000	0.000	0.000
82	A	98	ARG	1	0.895	0.951	53.108	5.841	5.841	0.000	0.000	0.000	0.000
83	A	99	ARG	1	1.007	0.994	52.612	5.886	5.886	0.000	0.000	0.000	0.000
84	A	100	LYS	1	0.857	0.940	54.056	5.521	5.521	0.000	0.000	0.000	0.000
85	A	101	PRO	0	0.088	0.059	53.861	-0.025	-0.025	0.000	0.000	0.000	0.000
86	A	102	CYS	0	-0.054	-0.031	54.426	0.161	0.161	0.000	0.000	0.000	0.000
87	A	103	SER	0	0.028	0.012	55.299	-0.064	-0.064	0.000	0.000	0.000	0.000
88	A	104	ARG	1	0.891	0.948	55.277	5.547	5.547	0.000	0.000	0.000	0.000
89	A	105	PRO	0	0.052	0.036	49.756	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	106	LEU	0	-0.015	-0.016	53.113	0.095	0.095	0.000	0.000	0.000	0.000
91	A	107	SER	0	0.004	-0.016	52.127	-0.087	-0.087	0.000	0.000	0.000	0.000
92	A	108	SER	0	-0.035	-0.010	51.056	0.011	0.011	0.000	0.000	0.000	0.000
93	A	109	ILE	0	-0.034	-0.027	47.503	-0.150	-0.150	0.000	0.000	0.000	0.000
94	A	110	LEU	0	0.003	0.009	44.897	0.023	0.023	0.000	0.000	0.000	0.000
95	A	111	GLY	0	0.015	0.023	44.598	0.067	0.067	0.000	0.000	0.000	0.000
96	A	112	ARG	1	0.907	0.947	42.226	7.450	7.450	0.000	0.000	0.000	0.000
97	A	113	SER	0	0.032	0.029	41.944	-0.173	-0.173	0.000	0.000	0.000	0.000
98	A	114	ASN	0	-0.067	-0.042	37.229	0.077	0.077	0.000	0.000	0.000	0.000
99	A	115	LEU	0	0.086	0.043	39.912	-0.117	-0.117	0.000	0.000	0.000	0.000
100	A	116	LYS	1	0.905	0.954	32.603	9.359	9.359	0.000	0.000	0.000	0.000
101	A	117	PHE	0	0.033	0.005	31.174	-0.240	-0.240	0.000	0.000	0.000	0.000
102	A	118	ALA	0	0.006	0.005	36.259	-0.081	-0.081	0.000	0.000	0.000	0.000
103	A	119	GLY	0	0.028	0.002	39.271	0.103	0.103	0.000	0.000	0.000	0.000
104	A	120	MET	0	-0.003	0.011	33.282	0.129	0.129	0.000	0.000	0.000	0.000
105	A	121	PRO	0	0.006	-0.007	37.169	-0.163	-0.163	0.000	0.000	0.000	0.000
106	A	122	ILE	0	-0.080	-0.030	31.784	-0.143	-0.143	0.000	0.000	0.000	0.000
107	A	123	THR	0	0.039	0.013	31.620	0.236	0.236	0.000	0.000	0.000	0.000
108	A	124	LEU	0	0.005	0.004	30.269	-0.412	-0.412	0.000	0.000	0.000	0.000
109	A	125	THR	0	0.017	-0.002	27.114	0.289	0.289	0.000	0.000	0.000	0.000
110	A	126	VAL	0	-0.041	-0.012	27.862	-0.296	-0.296	0.000	0.000	0.000	0.000
111	A	127	SER	0	0.059	0.022	24.248	0.087	0.087	0.000	0.000	0.000	0.000
112	A	128	THR	0	-0.009	-0.015	23.589	0.334	0.334	0.000	0.000	0.000	0.000
113	A	129	SER	0	-0.054	-0.031	22.935	-0.417	-0.417	0.000	0.000	0.000	0.000
114	A	130	SER	0	0.027	0.019	20.997	-0.444	-0.444	0.000	0.000	0.000	0.000
115	A	131	LEU	0	-0.006	-0.008	23.601	0.511	0.511	0.000	0.000	0.000	0.000
116	A	132	ASN	0	0.007	0.024	20.920	-0.159	-0.159	0.000	0.000	0.000	0.000
117	A	133	LEU	0	0.026	0.007	25.260	0.448	0.448	0.000	0.000	0.000	0.000
118	A	134	MET	0	-0.002	0.006	26.803	-0.467	-0.467	0.000	0.000	0.000	0.000
119	A	135	ALA	0	0.000	-0.003	29.116	0.425	0.425	0.000	0.000	0.000	0.000
120	A	136	ALA	0	0.029	0.019	31.782	0.016	0.016	0.000	0.000	0.000	0.000
121	A	137	ASP	-1	-0.914	-0.949	34.499	-8.173	-8.173	0.000	0.000	0.000	0.000
122	A	138	CYS	0	-0.009	-0.016	33.036	0.016	0.016	0.000	0.000	0.000	0.000
123	A	139	LYS	1	0.846	0.926	32.678	8.773	8.773	0.000	0.000	0.000	0.000
124	A	140	GLN	0	0.015	0.011	27.885	-0.262	-0.262	0.000	0.000	0.000	0.000
125	A	141	ILE	0	0.003	-0.004	23.614	0.181	0.181	0.000	0.000	0.000	0.000
126	A	142	ILE	0	-0.020	-0.005	25.873	-0.046	-0.046	0.000	0.000	0.000	0.000
127	A	143	ALA	0	0.035	0.021	21.388	-0.085	-0.085	0.000	0.000	0.000	0.000
128	A	144	ASN	0	-0.039	-0.041	23.105	0.480	0.480	0.000	0.000	0.000	0.000
129	A	145	HIS	0	0.032	0.011	18.946	-0.178	-0.178	0.000	0.000	0.000	0.000
130	A	146	HIS	0	0.011	0.031	21.640	-0.636	-0.636	0.000	0.000	0.000	0.000
131	A	147	MET	0	-0.038	-0.031	24.105	-0.088	-0.088	0.000	0.000	0.000	0.000
132	A	148	GLN	0	0.000	-0.001	21.155	-0.246	-0.246	0.000	0.000	0.000	0.000
133	A	149	SER	0	0.039	0.015	24.366	-0.045	-0.045	0.000	0.000	0.000	0.000
134	A	150	ILE	0	0.022	0.034	27.286	0.372	0.372	0.000	0.000	0.000	0.000
135	A	151	SER	0	-0.065	-0.044	29.877	-0.220	-0.220	0.000	0.000	0.000	0.000
136	A	152	PHE	0	-0.014	-0.013	32.507	0.109	0.109	0.000	0.000	0.000	0.000
137	A	153	ALA	0	0.082	0.060	36.324	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	154	SER	0	-0.037	-0.043	38.321	0.048	0.048	0.000	0.000	0.000	0.000
139	A	155	GLY	0	-0.033	0.004	41.670	0.139	0.139	0.000	0.000	0.000	0.000
140	A	156	GLY	0	0.015	-0.001	43.073	0.063	0.063	0.000	0.000	0.000	0.000
141	A	157	ASP	-1	-0.952	-0.955	46.639	-6.466	-6.466	0.000	0.000	0.000	0.000
142	A	158	PRO	0	0.009	0.014	48.341	0.146	0.146	0.000	0.000	0.000	0.000
143	A	159	ASP	-1	-0.885	-0.959	43.825	-7.252	-7.252	0.000	0.000	0.000	0.000
144	A	160	THR	0	-0.084	-0.081	46.988	0.055	0.055	0.000	0.000	0.000	0.000
145	A	161	ALA	0	-0.050	-0.013	49.148	0.008	0.008	0.000	0.000	0.000	0.000
146	A	162	GLU	-1	-0.896	-0.948	45.402	-7.135	-7.135	0.000	0.000	0.000	0.000
147	A	163	TYR	0	-0.029	-0.039	43.593	-0.062	-0.062	0.000	0.000	0.000	0.000
148	A	164	VAL	0	0.039	0.033	39.207	0.016	0.016	0.000	0.000	0.000	0.000
149	A	165	ALA	0	-0.015	-0.011	39.661	-0.060	-0.060	0.000	0.000	0.000	0.000
150	A	166	TYR	0	0.018	-0.002	31.573	-0.025	-0.025	0.000	0.000	0.000	0.000
151	A	167	VAL	0	-0.025	-0.014	33.299	0.040	0.040	0.000	0.000	0.000	0.000
152	A	168	ALA	0	0.001	0.006	31.959	-0.286	-0.286	0.000	0.000	0.000	0.000
153	A	169	LYS	1	0.855	0.921	30.142	10.038	10.038	0.000	0.000	0.000	0.000
154	A	170	ASP	-1	-0.853	-0.925	28.929	-10.609	-10.609	0.000	0.000	0.000	0.000
155	A	171	PRO	0	0.031	-0.003	30.780	0.202	0.202	0.000	0.000	0.000	0.000
156	A	172	VAL	0	0.025	0.006	28.667	0.177	0.177	0.000	0.000	0.000	0.000
157	A	173	ASN	0	-0.084	-0.045	31.707	0.329	0.329	0.000	0.000	0.000	0.000
158	A	174	GLN	0	-0.013	-0.014	34.945	0.258	0.258	0.000	0.000	0.000	0.000
159	A	175	ARG	1	0.920	0.994	34.899	8.509	8.509	0.000	0.000	0.000	0.000
160	A	176	ALA	0	0.095	0.051	34.908	0.252	0.252	0.000	0.000	0.000	0.000
161	A	177	CYS	0	-0.045	-0.020	36.154	-0.133	-0.133	0.000	0.000	0.000	0.000
162	A	178	HIS	0	0.064	0.041	30.453	0.132	0.132	0.000	0.000	0.000	0.000
163	A	179	ILE	0	-0.014	-0.009	36.156	0.152	0.152	0.000	0.000	0.000	0.000
164	A	180	LEU	0	-0.014	-0.011	35.271	-0.245	-0.245	0.000	0.000	0.000	0.000
165	A	181	GLU	-1	-0.844	-0.907	38.968	-7.021	-7.021	0.000	0.000	0.000	0.000
166	A	182	CYS	0	-0.089	-0.036	39.612	-0.209	-0.209	0.000	0.000	0.000	0.000
167	A	183	PRO	0	0.072	0.056	41.634	0.039	0.039	0.000	0.000	0.000	0.000
168	A	184	GLU	-1	-0.936	-0.976	42.793	-7.105	-7.105	0.000	0.000	0.000	0.000
169	A	185	GLY	0	0.016	0.005	39.745	-0.193	-0.193	0.000	0.000	0.000	0.000
170	A	186	LEU	0	-0.005	-0.016	33.888	0.013	0.013	0.000	0.000	0.000	0.000
171	A	187	ALA	0	0.037	0.003	37.820	-0.072	-0.072	0.000	0.000	0.000	0.000
172	A	188	GLN	0	0.024	0.011	40.875	0.099	0.099	0.000	0.000	0.000	0.000
173	A	189	ASP	-1	-0.767	-0.900	36.185	-8.810	-8.810	0.000	0.000	0.000	0.000
174	A	190	VAL	0	-0.061	-0.035	35.388	-0.029	-0.029	0.000	0.000	0.000	0.000
175	A	191	ILE	0	-0.010	0.017	37.909	-0.014	-0.014	0.000	0.000	0.000	0.000
176	A	192	SER	0	-0.066	-0.031	39.320	0.036	0.036	0.000	0.000	0.000	0.000
177	A	193	THR	0	-0.009	-0.008	40.460	0.242	0.242	0.000	0.000	0.000	0.000
178	A	194	ILE	0	-0.029	0.001	39.533	0.056	0.056	0.000	0.000	0.000	0.000
179	A	195	GLY	0	-0.040	-0.014	38.050	-0.222	-0.222	0.000	0.000	0.000	0.000
180	A	196	GLN	0	-0.013	-0.030	34.636	-0.067	-0.067	0.000	0.000	0.000	0.000
181	A	197	ALA	0	-0.003	0.012	29.337	-0.054	-0.054	0.000	0.000	0.000	0.000
182	A	198	PHE	0	-0.016	-0.009	31.156	0.074	0.074	0.000	0.000	0.000	0.000
183	A	199	GLU	-1	-0.881	-0.949	26.088	-11.547	-11.547	0.000	0.000	0.000	0.000
184	A	200	LEU	0	-0.023	-0.003	25.530	-0.444	-0.444	0.000	0.000	0.000	0.000
185	A	201	ARG	1	0.968	0.972	28.599	9.630	9.630	0.000	0.000	0.000	0.000
186	A	202	PHE	0	-0.029	-0.016	29.976	0.097	0.097	0.000	0.000	0.000	0.000
187	A	203	LYS	1	0.837	0.922	26.900	11.291	11.291	0.000	0.000	0.000	0.000
188	A	204	GLN	0	-0.012	-0.017	23.211	-0.080	-0.080	0.000	0.000	0.000	0.000
189	A	205	TYR	0	0.040	0.008	16.299	-0.090	-0.090	0.000	0.000	0.000	0.000
190	A	206	LEU	0	0.020	0.036	21.094	-0.352	-0.352	0.000	0.000	0.000	0.000
191	A	207	ARG	0	0.090	0.067	20.468	2.874	2.874	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:17:GLY)