FMO DATABASE

FMODB ID: GVQL1

Calculation Name: 1K3Y-A-Xray547

Preferred Name: Glutathione S-transferase A1

Target Type: SINGLE PROTEIN

Ligand Name: s-hexylglutathione

Ligand 3-letter code: GTX

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1K3Y

Chain ID: A

ChEMBL ID: CHEMBL3409

UniProt ID: P08263

Base Structure: X-ray

Registration Date: 2025-10-05

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	221
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2796844.019235
FMO2-HF: Nuclear repulsion	2707904.944939
FMO2-HF: Total energy	-88939.074296
FMO2-MP2: Total energy	-89199.341654

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:2:ALA)

Summations of interaction energy for fragment #1(A:2: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.
41.154	43.084	0	-1.088	-0.842	-0.005

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.825 / q_NPA : 0.904

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	4	LYS	1	0.856	0.938	3.289	23.161	25.012	0.001	-1.083	-0.770	-0.005
60	A	61	ASP	-1	-0.797	-0.858	4.434	-44.894	-44.815	-0.001	-0.005	-0.072	0.000
4	A	5	PRO	0	-0.004	-0.001	6.135	0.329	0.329	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.882	0.951	7.740	29.448	29.448	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.002	-0.004	10.825	0.636	0.636	0.000	0.000	0.000	0.000
7	A	8	HIS	0	-0.021	-0.033	12.436	2.085	2.085	0.000	0.000	0.000	0.000
8	A	9	TYR	0	0.039	-0.001	16.960	0.648	0.648	0.000	0.000	0.000	0.000
9	A	10	PHE	0	0.072	0.063	20.403	-0.215	-0.215	0.000	0.000	0.000	0.000
10	A	11	ASN	0	-0.034	-0.024	22.914	-0.670	-0.670	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.034	0.021	24.202	0.540	0.540	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.750	0.853	23.841	10.513	10.513	0.000	0.000	0.000	0.000
13	A	14	GLY	0	0.028	0.010	23.838	-0.552	-0.552	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.815	0.856	23.718	11.404	11.404	0.000	0.000	0.000	0.000
15	A	16	MET	0	0.011	0.017	16.944	-0.722	-0.722	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.729	-0.856	19.581	-14.736	-14.736	0.000	0.000	0.000	0.000
17	A	18	SER	0	0.046	0.034	20.851	-0.683	-0.683	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.027	-0.028	15.071	-0.238	-0.238	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.728	0.844	16.349	14.378	14.378	0.000	0.000	0.000	0.000
20	A	21	TRP	0	0.008	0.003	17.652	-0.478	-0.478	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.037	-0.013	16.435	-0.183	-0.183	0.000	0.000	0.000	0.000
22	A	23	LEU	0	-0.013	-0.007	11.098	-0.619	-0.619	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.029	0.022	14.525	-0.599	-0.599	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.002	-0.007	16.642	0.173	0.173	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.018	-0.004	14.182	0.519	0.519	0.000	0.000	0.000	0.000
26	A	27	GLY	0	-0.025	-0.012	14.263	-0.643	-0.643	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.064	-0.021	8.879	-1.359	-1.359	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.883	-0.942	9.647	-26.226	-26.226	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.036	-0.029	9.407	-2.984	-2.984	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.843	-0.924	10.195	-28.545	-28.545	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.769	-0.873	12.487	-16.848	-16.848	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.919	0.965	15.445	17.676	17.676	0.000	0.000	0.000	0.000
33	A	34	PHE	0	-0.037	-0.029	17.220	0.355	0.355	0.000	0.000	0.000	0.000
34	A	35	ILE	0	-0.011	-0.002	20.585	0.212	0.212	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.817	0.886	22.909	12.354	12.354	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.002	0.006	26.284	0.530	0.530	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.052	0.022	26.815	-0.410	-0.410	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.860	-0.940	27.444	-10.547	-10.547	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.825	-0.907	22.900	-13.237	-13.237	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.037	-0.019	22.522	-0.756	-0.756	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.777	-0.863	23.555	-11.232	-11.232	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.779	0.880	19.763	14.720	14.720	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.016	-0.013	17.332	-0.594	-0.594	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.815	0.893	20.093	11.271	11.271	0.000	0.000	0.000	0.000
45	A	46	ASN	0	-0.001	-0.004	22.642	0.021	0.021	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.842	-0.887	17.932	-15.407	-15.407	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.005	0.005	18.482	-0.638	-0.638	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.053	-0.038	14.331	-0.875	-0.875	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.011	0.002	16.952	-0.759	-0.759	0.000	0.000	0.000	0.000
50	A	51	MET	0	0.017	0.017	19.268	0.525	0.525	0.000	0.000	0.000	0.000
51	A	52	PHE	0	0.004	-0.019	21.052	0.494	0.494	0.000	0.000	0.000	0.000
52	A	53	GLN	0	0.022	0.016	23.289	0.381	0.381	0.000	0.000	0.000	0.000
53	A	54	GLN	0	0.003	0.006	23.075	0.135	0.135	0.000	0.000	0.000	0.000
54	A	55	VAL	0	0.027	0.025	19.413	-0.730	-0.730	0.000	0.000	0.000	0.000
55	A	56	PRO	0	-0.050	-0.045	18.868	0.673	0.673	0.000	0.000	0.000	0.000
56	A	57	MET	0	-0.026	0.010	14.222	-0.319	-0.319	0.000	0.000	0.000	0.000
57	A	58	VAL	0	-0.008	-0.010	10.961	0.041	0.041	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.801	-0.873	8.584	-26.668	-26.668	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.009	-0.014	6.607	-1.643	-1.643	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.032	0.025	5.012	2.514	2.514	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.045	-0.003	5.755	5.349	5.349	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.875	0.929	9.460	23.112	23.112	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.007	0.013	12.234	1.473	1.473	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.033	0.006	14.725	0.090	0.090	0.000	0.000	0.000	0.000
66	A	67	GLN	0	0.040	0.012	18.221	0.006	0.006	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.025	0.010	19.438	-0.466	-0.466	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.876	0.903	19.622	11.158	11.158	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.020	0.022	18.260	-0.277	-0.277	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.012	-0.002	14.444	-0.895	-0.895	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.007	-0.002	15.193	-1.066	-1.066	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.016	0.016	17.394	-0.112	-0.112	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.035	-0.040	8.821	1.374	1.374	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.023	0.005	11.712	-0.998	-0.998	0.000	0.000	0.000	0.000
75	A	76	ALA	0	0.007	-0.005	13.567	-0.302	-0.302	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.065	-0.027	15.490	0.502	0.502	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.842	0.916	6.433	40.766	40.766	0.000	0.000	0.000	0.000
78	A	79	TYR	0	0.008	-0.005	8.421	-2.222	-2.222	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.032	-0.010	14.127	1.376	1.376	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.002	0.014	16.881	1.083	1.083	0.000	0.000	0.000	0.000
81	A	82	TYR	0	-0.075	-0.084	18.949	0.500	0.500	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.030	0.016	21.152	0.545	0.545	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.848	0.912	22.519	10.422	10.422	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.839	-0.919	24.386	-11.060	-11.060	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.013	-0.007	26.366	-0.203	-0.203	0.000	0.000	0.000	0.000
86	A	87	LYS	1	0.949	0.977	28.015	9.307	9.307	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.799	-0.896	26.851	-11.549	-11.549	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.977	0.996	22.329	13.298	13.298	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.017	0.014	26.427	0.029	0.029	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.031	-0.013	29.832	0.202	0.202	0.000	0.000	0.000	0.000
91	A	92	ILE	0	0.001	-0.001	23.860	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.811	-0.895	24.926	-12.765	-12.765	0.000	0.000	0.000	0.000
93	A	94	MET	0	-0.029	-0.011	27.405	0.262	0.262	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.027	-0.026	29.165	0.333	0.333	0.000	0.000	0.000	0.000
95	A	96	ILE	0	0.008	-0.007	23.842	0.070	0.070	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.800	-0.856	26.660	-11.721	-11.721	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.013	0.018	29.537	0.211	0.211	0.000	0.000	0.000	0.000
98	A	99	ILE	0	-0.052	-0.036	27.921	0.211	0.211	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.007	0.000	27.484	0.009	0.009	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.891	-0.936	29.217	-9.395	-9.395	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.034	-0.025	32.905	0.177	0.177	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.027	0.006	29.930	0.109	0.109	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.762	-0.840	29.754	-10.706	-10.706	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.086	-0.049	31.827	0.240	0.240	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.017	-0.010	33.140	0.233	0.233	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.047	-0.019	28.120	0.053	0.053	0.000	0.000	0.000	0.000
107	A	108	LEU	0	0.010	-0.005	32.004	0.006	0.006	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.020	0.010	34.708	0.259	0.259	0.000	0.000	0.000	0.000
109	A	110	PRO	0	-0.047	-0.032	34.666	0.245	0.245	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.009	-0.003	34.897	0.014	0.014	0.000	0.000	0.000	0.000
111	A	112	CYS	0	-0.061	-0.009	37.795	0.120	0.120	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.054	0.027	40.851	0.005	0.005	0.000	0.000	0.000	0.000
113	A	114	PRO	0	0.001	-0.017	44.195	0.023	0.023	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.904	-0.954	45.897	-6.222	-6.222	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.930	-0.954	45.021	-7.054	-7.054	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.855	0.920	42.225	7.233	7.233	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.803	-0.893	43.951	-6.955	-6.955	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.027	0.009	46.305	-0.039	-0.039	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.900	0.945	40.519	7.687	7.687	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.029	0.015	40.810	-0.179	-0.179	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.003	-0.001	42.836	-0.075	-0.075	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.012	-0.015	43.085	-0.038	-0.038	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.008	0.007	38.006	-0.084	-0.084	0.000	0.000	0.000	0.000
124	A	125	LYS	1	0.859	0.912	40.811	7.263	7.263	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.839	-0.897	42.794	-7.137	-7.137	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.900	0.949	40.307	7.386	7.386	0.000	0.000	0.000	0.000
127	A	128	ILE	0	0.009	0.013	37.616	-0.111	-0.111	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.970	0.986	39.906	6.847	6.847	0.000	0.000	0.000	0.000
129	A	130	ASN	0	-0.021	-0.033	43.077	0.077	0.077	0.000	0.000	0.000	0.000
130	A	131	ARG	1	0.903	0.958	39.433	7.806	7.806	0.000	0.000	0.000	0.000
131	A	132	TYR	0	0.000	-0.010	35.528	0.062	0.062	0.000	0.000	0.000	0.000
132	A	133	PHE	0	0.009	0.003	35.200	-0.190	-0.190	0.000	0.000	0.000	0.000
133	A	134	PRO	0	0.019	0.008	38.651	-0.060	-0.060	0.000	0.000	0.000	0.000
134	A	135	ALA	0	-0.024	0.002	37.528	0.030	0.030	0.000	0.000	0.000	0.000
135	A	136	PHE	0	0.019	0.003	32.655	-0.060	-0.060	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.759	-0.876	36.111	-8.203	-8.203	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.940	0.967	38.815	7.600	7.600	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.014	0.004	33.481	0.070	0.070	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.008	0.020	33.018	0.004	0.004	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.947	0.965	36.734	7.191	7.191	0.000	0.000	0.000	0.000
141	A	142	SER	0	-0.128	-0.064	37.876	0.141	0.141	0.000	0.000	0.000	0.000
142	A	143	HIS	0	-0.008	-0.012	33.354	0.306	0.306	0.000	0.000	0.000	0.000
143	A	144	GLY	0	0.006	0.014	38.296	0.047	0.047	0.000	0.000	0.000	0.000
144	A	145	GLN	0	-0.031	-0.014	33.009	-0.271	-0.271	0.000	0.000	0.000	0.000
145	A	146	ASP	-1	-0.863	-0.946	31.260	-9.533	-9.533	0.000	0.000	0.000	0.000
146	A	147	TYR	0	-0.026	-0.014	26.301	-0.253	-0.253	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.001	-0.010	28.642	0.336	0.336	0.000	0.000	0.000	0.000
148	A	149	VAL	0	-0.001	-0.006	27.789	0.343	0.343	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.032	0.016	28.124	-0.250	-0.250	0.000	0.000	0.000	0.000
150	A	151	ASN	0	-0.026	-0.005	28.760	-0.102	-0.102	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.908	0.952	23.019	13.191	13.191	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.014	0.014	20.931	0.102	0.102	0.000	0.000	0.000	0.000
153	A	154	SER	0	-0.021	-0.023	22.330	-0.476	-0.476	0.000	0.000	0.000	0.000
154	A	155	ARG	1	0.896	0.923	20.355	14.819	14.819	0.000	0.000	0.000	0.000
155	A	156	ALA	0	0.010	0.015	22.043	0.221	0.221	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.770	-0.871	25.446	-11.451	-11.451	0.000	0.000	0.000	0.000
157	A	158	ILE	0	-0.017	-0.001	20.933	0.275	0.275	0.000	0.000	0.000	0.000
158	A	159	HIS	0	0.049	0.011	20.556	-0.018	-0.018	0.000	0.000	0.000	0.000
159	A	160	LEU	0	0.016	0.022	25.315	0.388	0.388	0.000	0.000	0.000	0.000
160	A	161	VAL	0	-0.012	-0.018	27.423	0.375	0.375	0.000	0.000	0.000	0.000
161	A	162	GLU	-1	-0.800	-0.886	24.006	-13.024	-13.024	0.000	0.000	0.000	0.000
162	A	163	LEU	0	0.001	0.001	27.234	0.326	0.326	0.000	0.000	0.000	0.000
163	A	164	LEU	0	-0.036	-0.024	30.249	0.413	0.413	0.000	0.000	0.000	0.000
164	A	165	TYR	0	-0.043	-0.039	29.021	0.379	0.379	0.000	0.000	0.000	0.000
165	A	166	TYR	0	-0.041	-0.048	25.444	0.259	0.259	0.000	0.000	0.000	0.000
166	A	167	VAL	0	-0.003	-0.007	32.372	0.301	0.301	0.000	0.000	0.000	0.000
167	A	168	GLU	-1	-0.891	-0.939	34.544	-8.941	-8.941	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.799	-0.870	31.744	-10.030	-10.030	0.000	0.000	0.000	0.000
169	A	170	LEU	0	-0.037	0.005	36.190	0.220	0.220	0.000	0.000	0.000	0.000
170	A	171	ASP	-1	-0.779	-0.876	38.365	-7.086	-7.086	0.000	0.000	0.000	0.000
171	A	172	SER	0	0.037	0.031	39.637	0.015	0.015	0.000	0.000	0.000	0.000
172	A	173	SER	0	-0.053	-0.044	40.608	0.047	0.047	0.000	0.000	0.000	0.000
173	A	174	LEU	0	-0.007	0.006	40.323	0.104	0.104	0.000	0.000	0.000	0.000
174	A	175	ILE	0	0.026	0.007	36.197	0.024	0.024	0.000	0.000	0.000	0.000
175	A	176	SER	0	-0.040	-0.032	40.245	0.058	0.058	0.000	0.000	0.000	0.000
176	A	177	SER	0	-0.020	-0.024	43.473	0.055	0.055	0.000	0.000	0.000	0.000
177	A	178	PHE	0	-0.006	0.012	39.758	0.083	0.083	0.000	0.000	0.000	0.000
178	A	179	PRO	0	0.009	0.004	39.800	-0.204	-0.204	0.000	0.000	0.000	0.000
179	A	180	LEU	0	0.011	0.000	37.603	-0.171	-0.171	0.000	0.000	0.000	0.000
180	A	181	LEU	0	0.004	0.007	34.561	-0.316	-0.316	0.000	0.000	0.000	0.000
181	A	182	LYS	1	0.864	0.940	34.891	7.409	7.409	0.000	0.000	0.000	0.000
182	A	183	ALA	0	0.009	0.016	35.661	-0.183	-0.183	0.000	0.000	0.000	0.000
183	A	184	LEU	0	0.008	0.009	29.708	-0.227	-0.227	0.000	0.000	0.000	0.000
184	A	185	LYS	1	0.856	0.924	30.902	9.167	9.167	0.000	0.000	0.000	0.000
185	A	186	THR	0	-0.021	-0.003	30.844	-0.298	-0.298	0.000	0.000	0.000	0.000
186	A	187	ARG	1	0.834	0.927	30.227	9.490	9.490	0.000	0.000	0.000	0.000
187	A	188	ILE	0	0.014	0.003	25.332	-0.364	-0.364	0.000	0.000	0.000	0.000
188	A	189	SER	0	0.008	-0.012	26.109	-0.530	-0.530	0.000	0.000	0.000	0.000
189	A	190	ASN	0	-0.042	-0.023	27.715	-0.131	-0.131	0.000	0.000	0.000	0.000
190	A	191	LEU	0	0.019	0.036	23.169	-0.055	-0.055	0.000	0.000	0.000	0.000
191	A	192	PRO	0	0.011	-0.005	21.639	-0.176	-0.176	0.000	0.000	0.000	0.000
192	A	193	THR	0	-0.033	-0.011	17.642	0.334	0.334	0.000	0.000	0.000	0.000
193	A	194	VAL	0	0.036	0.021	20.003	-0.250	-0.250	0.000	0.000	0.000	0.000
194	A	195	LYS	1	0.875	0.937	22.573	11.359	11.359	0.000	0.000	0.000	0.000
195	A	196	LYS	1	0.970	0.982	17.645	16.645	16.645	0.000	0.000	0.000	0.000
196	A	197	PHE	0	0.037	0.013	19.501	-0.095	-0.095	0.000	0.000	0.000	0.000
197	A	198	LEU	0	-0.014	0.005	21.990	0.298	0.298	0.000	0.000	0.000	0.000
198	A	199	GLN	0	-0.019	0.004	24.724	0.105	0.105	0.000	0.000	0.000	0.000
199	A	200	PRO	0	0.023	0.001	25.081	-0.361	-0.361	0.000	0.000	0.000	0.000
200	A	201	GLY	0	0.006	0.007	24.008	-0.144	-0.144	0.000	0.000	0.000	0.000
201	A	202	SER	0	-0.043	-0.008	20.554	-0.853	-0.853	0.000	0.000	0.000	0.000
202	A	203	PRO	0	0.006	-0.011	16.860	0.429	0.429	0.000	0.000	0.000	0.000
203	A	204	ARG	1	0.848	0.941	19.884	12.142	12.142	0.000	0.000	0.000	0.000
204	A	205	LYS	1	0.794	0.887	20.296	15.364	15.364	0.000	0.000	0.000	0.000
205	A	206	PRO	0	0.019	0.009	25.309	0.210	0.210	0.000	0.000	0.000	0.000
206	A	207	PRO	0	-0.004	-0.016	28.704	-0.245	-0.245	0.000	0.000	0.000	0.000
207	A	208	MET	0	-0.040	0.001	30.134	-0.168	-0.168	0.000	0.000	0.000	0.000
208	A	209	ASP	-1	-0.833	-0.911	31.593	-9.135	-9.135	0.000	0.000	0.000	0.000
209	A	210	GLU	-1	-0.836	-0.948	34.372	-8.351	-8.351	0.000	0.000	0.000	0.000
210	A	211	LYS	1	0.919	0.962	35.060	8.405	8.405	0.000	0.000	0.000	0.000
211	A	212	SER	0	-0.018	0.000	29.361	-0.203	-0.203	0.000	0.000	0.000	0.000
212	A	213	LEU	0	0.030	0.000	31.212	-0.294	-0.294	0.000	0.000	0.000	0.000
213	A	214	GLU	-1	-0.790	-0.872	33.289	-8.718	-8.718	0.000	0.000	0.000	0.000
214	A	215	GLU	-1	-0.904	-0.951	27.720	-11.497	-11.497	0.000	0.000	0.000	0.000
215	A	216	ALA	0	-0.014	-0.015	29.607	-0.174	-0.174	0.000	0.000	0.000	0.000
216	A	217	ARG	1	0.923	0.961	30.588	8.414	8.414	0.000	0.000	0.000	0.000
217	A	218	LYS	1	0.855	0.920	32.511	9.115	9.115	0.000	0.000	0.000	0.000
218	A	219	ILE	0	-0.053	-0.022	26.223	-0.062	-0.062	0.000	0.000	0.000	0.000
219	A	220	PHE	0	-0.080	-0.066	24.724	-0.369	-0.369	0.000	0.000	0.000	0.000
220	A	221	ARG	1	0.791	0.885	29.956	10.186	10.186	0.000	0.000	0.000	0.000
221	A	222	PHE	-1	-0.900	-0.934	31.225	-8.749	-8.749	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)