FMO DATABASE

FMODB ID: 5YJ1Z

Calculation Name: 3KEV-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | s-hydroxycysteine | acetate ion

Ligand 3-letter code: SO4 | CSO | ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3KEV

Chain ID: A

ChEMBL ID:

UniProt ID: D1MPT4

Base Structure: X-ray

Registration Date: 2025-10-04

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	189
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2117497.339654
FMO2-HF: Nuclear repulsion	2041548.720152
FMO2-HF: Total energy	-75948.619502
FMO2-MP2: Total energy	-76175.188255

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:4:ALA)

Summations of interaction energy for fragment #1(A:4: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.
-74.257	-67.952	11.947	-7.435	-10.816	-0.09

Interaction energy analysis for fragmet #1(A:4:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.790 / q_NPA : 0.902

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	6	LYS	1	0.910	0.939	3.856	35.431	36.512	-0.006	-0.416	-0.659	0.000
6	A	9	ILE	0	-0.032	-0.005	2.398	2.058	2.014	1.408	-0.485	-0.878	-0.004
67	A	70	ALA	0	-0.013	-0.005	2.226	-8.111	-7.625	1.234	-0.834	-0.887	-0.004
68	A	71	ASN	0	-0.057	-0.023	3.294	-7.753	-7.709	0.005	0.257	-0.306	-0.001
70	A	73	GLN	0	-0.014	-0.013	2.087	-27.337	-25.802	4.199	-2.726	-3.007	-0.037
71	A	74	VAL	0	-0.043	-0.028	2.753	-0.863	-0.886	0.876	0.268	-1.120	-0.006
72	A	75	ASP	-1	-0.760	-0.872	2.170	-78.285	-75.301	4.220	-3.432	-3.773	-0.038
73	A	76	SER	0	0.021	0.004	3.680	5.154	5.212	0.010	-0.030	-0.038	0.000
76	A	79	LYS	1	0.771	0.862	3.617	55.692	55.876	0.001	-0.037	-0.148	0.000
4	A	7	LYS	1	0.941	0.974	5.798	29.565	29.565	0.000	0.000	0.000	0.000
5	A	8	ALA	0	0.033	0.015	5.662	2.788	2.788	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.010	-0.010	6.372	3.187	3.187	0.000	0.000	0.000	0.000
8	A	11	GLU	-1	-0.922	-0.938	9.622	-19.535	-19.535	0.000	0.000	0.000	0.000
9	A	12	LEU	0	0.039	0.017	7.187	1.313	1.313	0.000	0.000	0.000	0.000
10	A	13	PHE	0	0.005	-0.001	10.420	1.389	1.389	0.000	0.000	0.000	0.000
11	A	14	GLN	0	-0.072	-0.053	12.247	2.196	2.196	0.000	0.000	0.000	0.000
12	A	15	THR	0	-0.011	-0.004	13.998	1.681	1.681	0.000	0.000	0.000	0.000
13	A	16	TYR	0	-0.102	-0.096	12.924	0.366	0.366	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.854	0.963	16.221	16.297	16.297	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.737	-0.866	17.745	-13.057	-13.057	0.000	0.000	0.000	0.000
16	A	19	PRO	0	-0.040	-0.037	21.513	-0.221	-0.221	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.011	-0.001	23.668	0.137	0.137	0.000	0.000	0.000	0.000
18	A	21	GLY	0	-0.062	-0.016	20.256	-0.068	-0.068	0.000	0.000	0.000	0.000
19	A	22	ASN	0	0.029	-0.004	18.209	-0.769	-0.769	0.000	0.000	0.000	0.000
20	A	23	TYR	0	-0.022	-0.022	17.252	-0.640	-0.640	0.000	0.000	0.000	0.000
21	A	24	ILE	0	-0.009	0.024	13.360	0.181	0.181	0.000	0.000	0.000	0.000
22	A	25	GLY	0	0.056	0.020	17.803	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	26	ALA	0	0.050	0.017	20.461	-0.383	-0.383	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.928	-0.952	22.987	-11.301	-11.301	0.000	0.000	0.000	0.000
25	A	28	GLY	0	-0.021	-0.024	18.822	-0.156	-0.156	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.042	-0.034	16.447	-0.708	-0.708	0.000	0.000	0.000	0.000
27	A	30	GLN	0	-0.031	-0.008	18.633	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	31	ARG	1	0.958	0.995	19.074	14.084	14.084	0.000	0.000	0.000	0.000
29	A	32	LEU	0	-0.016	0.005	12.277	-0.591	-0.591	0.000	0.000	0.000	0.000
30	A	33	PHE	0	-0.031	-0.041	15.637	-0.909	-0.909	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.894	-0.931	18.060	-12.321	-12.321	0.000	0.000	0.000	0.000
32	A	35	ASP	-1	-0.807	-0.883	16.356	-15.606	-15.606	0.000	0.000	0.000	0.000
33	A	36	ILE	0	-0.133	-0.070	12.999	-0.791	-0.791	0.000	0.000	0.000	0.000
34	A	37	GLN	0	-0.087	-0.057	16.357	-0.509	-0.509	0.000	0.000	0.000	0.000
35	A	38	VAL	0	-0.055	-0.025	16.892	0.085	0.085	0.000	0.000	0.000	0.000
36	A	39	ASP	-1	-0.787	-0.866	19.934	-11.443	-11.443	0.000	0.000	0.000	0.000
37	A	40	PRO	0	-0.001	-0.022	21.625	-0.426	-0.426	0.000	0.000	0.000	0.000
38	A	41	SER	0	-0.048	-0.034	22.690	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	42	ASP	-1	-0.767	-0.844	21.204	-13.662	-13.662	0.000	0.000	0.000	0.000
40	A	43	VAL	0	0.083	0.047	21.595	-0.569	-0.569	0.000	0.000	0.000	0.000
41	A	44	VAL	0	-0.047	-0.038	16.881	-0.539	-0.539	0.000	0.000	0.000	0.000
42	A	45	THR	0	-0.026	-0.010	16.872	-1.124	-1.124	0.000	0.000	0.000	0.000
43	A	46	LEU	0	0.040	0.024	17.889	-0.629	-0.629	0.000	0.000	0.000	0.000
44	A	47	VAL	0	-0.035	-0.017	15.801	-0.486	-0.486	0.000	0.000	0.000	0.000
45	A	48	LEU	0	-0.011	-0.008	11.217	-1.217	-1.217	0.000	0.000	0.000	0.000
46	A	49	ALA	0	0.038	0.023	14.101	-1.073	-1.073	0.000	0.000	0.000	0.000
47	A	50	TRP	0	-0.018	0.000	16.340	-0.668	-0.668	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.783	0.870	11.607	20.375	20.375	0.000	0.000	0.000	0.000
49	A	52	LEU	0	-0.063	-0.030	10.149	-1.805	-1.805	0.000	0.000	0.000	0.000
50	A	53	LYS	1	0.844	0.929	12.722	21.288	21.288	0.000	0.000	0.000	0.000
51	A	54	ALA	0	-0.019	0.005	16.092	0.485	0.485	0.000	0.000	0.000	0.000
52	A	55	SER	0	-0.047	-0.061	17.495	0.907	0.907	0.000	0.000	0.000	0.000
53	A	56	SER	0	-0.003	0.004	20.612	0.901	0.901	0.000	0.000	0.000	0.000
54	A	57	THR	0	-0.007	-0.023	21.398	-0.452	-0.452	0.000	0.000	0.000	0.000
55	A	58	CYS	0	-0.060	-0.032	21.300	0.210	0.210	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.893	-0.944	19.802	-12.912	-12.912	0.000	0.000	0.000	0.000
57	A	60	PHE	0	-0.035	-0.026	14.232	-0.852	-0.852	0.000	0.000	0.000	0.000
58	A	61	SER	0	0.014	-0.014	16.310	-0.230	-0.230	0.000	0.000	0.000	0.000
59	A	62	GLU	-1	-0.907	-0.962	13.106	-20.827	-20.827	0.000	0.000	0.000	0.000
60	A	63	LYS	1	0.922	0.954	11.827	17.349	17.349	0.000	0.000	0.000	0.000
61	A	64	GLU	-1	-0.759	-0.835	11.291	-18.660	-18.660	0.000	0.000	0.000	0.000
62	A	65	PHE	0	0.053	0.022	9.543	-2.060	-2.060	0.000	0.000	0.000	0.000
63	A	66	VAL	0	0.015	-0.002	7.482	-3.238	-3.238	0.000	0.000	0.000	0.000
64	A	67	GLU	-1	-0.874	-0.937	6.196	-36.876	-36.876	0.000	0.000	0.000	0.000
65	A	68	GLY	0	0.020	0.020	7.020	-2.816	-2.816	0.000	0.000	0.000	0.000
66	A	69	LEU	0	0.006	-0.005	5.008	-1.580	-1.580	0.000	0.000	0.000	0.000
69	A	72	LEU	0	-0.039	-0.016	6.110	1.739	1.739	0.000	0.000	0.000	0.000
74	A	77	LEU	0	0.107	0.057	7.439	-0.988	-0.988	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.807	-0.890	10.656	-18.850	-18.850	0.000	0.000	0.000	0.000
77	A	80	LEU	0	0.045	0.030	8.711	-0.569	-0.569	0.000	0.000	0.000	0.000
78	A	81	LYS	1	0.910	0.972	9.698	18.141	18.141	0.000	0.000	0.000	0.000
79	A	82	ARG	1	0.922	0.957	11.203	21.647	21.647	0.000	0.000	0.000	0.000
80	A	83	LYS	1	0.921	0.975	8.169	29.799	29.799	0.000	0.000	0.000	0.000
81	A	84	LEU	0	0.059	0.027	10.673	0.827	0.827	0.000	0.000	0.000	0.000
82	A	85	SER	0	-0.011	-0.008	13.811	1.552	1.552	0.000	0.000	0.000	0.000
83	A	86	SER	0	-0.117	-0.048	12.343	0.431	0.431	0.000	0.000	0.000	0.000
84	A	87	LEU	0	0.027	-0.007	11.868	0.670	0.670	0.000	0.000	0.000	0.000
85	A	88	ARG	1	0.834	0.884	15.122	14.938	14.938	0.000	0.000	0.000	0.000
86	A	89	LYS	1	0.918	0.954	17.660	16.763	16.763	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.835	-0.886	14.300	-19.744	-19.744	0.000	0.000	0.000	0.000
88	A	91	ILE	0	-0.011	-0.010	18.050	0.235	0.235	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.839	-0.905	20.892	-11.576	-11.576	0.000	0.000	0.000	0.000
90	A	93	ASP	-1	-0.867	-0.896	21.696	-12.964	-12.964	0.000	0.000	0.000	0.000
91	A	94	PRO	0	0.066	0.025	23.602	-0.201	-0.201	0.000	0.000	0.000	0.000
92	A	95	SER	0	-0.074	-0.053	23.900	0.109	0.109	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.840	0.899	16.814	16.906	16.906	0.000	0.000	0.000	0.000
94	A	97	PHE	0	0.010	0.011	21.945	-0.243	-0.243	0.000	0.000	0.000	0.000
95	A	98	ARG	1	0.815	0.885	24.075	10.152	10.152	0.000	0.000	0.000	0.000
96	A	99	ALA	0	-0.034	-0.025	21.957	0.091	0.091	0.000	0.000	0.000	0.000
97	A	100	PHE	0	-0.020	-0.011	20.423	-0.145	-0.145	0.000	0.000	0.000	0.000
98	A	101	TYR	0	0.038	-0.001	22.126	-0.016	-0.016	0.000	0.000	0.000	0.000
99	A	102	GLN	0	-0.001	-0.009	25.735	0.492	0.492	0.000	0.000	0.000	0.000
100	A	103	PHE	0	-0.049	-0.012	19.161	0.126	0.126	0.000	0.000	0.000	0.000
101	A	104	VAL	0	0.035	0.015	22.800	0.046	0.046	0.000	0.000	0.000	0.000
102	A	105	PHE	0	0.007	0.028	24.638	0.176	0.176	0.000	0.000	0.000	0.000
103	A	106	GLN	0	0.011	-0.002	24.735	0.601	0.601	0.000	0.000	0.000	0.000
104	A	107	TYR	0	0.012	0.013	20.116	-0.075	-0.075	0.000	0.000	0.000	0.000
105	A	108	SER	0	0.000	-0.002	23.892	-0.109	-0.109	0.000	0.000	0.000	0.000
106	A	109	LYS	1	0.817	0.915	26.672	10.675	10.675	0.000	0.000	0.000	0.000
107	A	110	GLU	-1	-0.846	-0.926	28.051	-10.114	-10.114	0.000	0.000	0.000	0.000
108	A	111	PRO	0	-0.010	-0.008	26.620	0.200	0.200	0.000	0.000	0.000	0.000
109	A	112	SER	0	-0.031	-0.022	29.122	0.064	0.064	0.000	0.000	0.000	0.000
110	A	113	GLN	0	0.032	0.031	32.470	0.396	0.396	0.000	0.000	0.000	0.000
111	A	114	ARG	1	0.943	0.964	32.955	7.811	7.811	0.000	0.000	0.000	0.000
112	A	115	SER	0	-0.022	-0.011	34.784	-0.078	-0.078	0.000	0.000	0.000	0.000
113	A	116	LEU	0	-0.011	0.021	30.033	-0.063	-0.063	0.000	0.000	0.000	0.000
114	A	117	PRO	0	0.031	0.007	32.894	0.250	0.250	0.000	0.000	0.000	0.000
115	A	118	ALA	0	0.054	0.031	35.068	-0.190	-0.190	0.000	0.000	0.000	0.000
116	A	119	GLU	-1	-0.900	-0.949	36.608	-8.125	-8.125	0.000	0.000	0.000	0.000
117	A	120	THR	0	-0.001	-0.006	30.370	-0.060	-0.060	0.000	0.000	0.000	0.000
118	A	121	ALA	0	-0.020	-0.011	31.764	-0.283	-0.283	0.000	0.000	0.000	0.000
119	A	122	MET	0	0.011	0.008	33.118	-0.090	-0.090	0.000	0.000	0.000	0.000
120	A	123	ALA	0	0.027	0.019	31.721	-0.072	-0.072	0.000	0.000	0.000	0.000
121	A	124	LEU	0	-0.019	-0.017	26.575	-0.265	-0.265	0.000	0.000	0.000	0.000
122	A	125	TRP	0	0.033	-0.009	29.443	-0.107	-0.107	0.000	0.000	0.000	0.000
123	A	126	ASP	-1	-0.824	-0.870	32.084	-9.029	-9.029	0.000	0.000	0.000	0.000
124	A	127	VAL	0	-0.011	-0.009	25.725	-0.146	-0.146	0.000	0.000	0.000	0.000
125	A	128	LEU	0	-0.085	-0.040	24.682	-0.392	-0.392	0.000	0.000	0.000	0.000
126	A	129	LEU	0	0.012	-0.009	27.936	-0.137	-0.137	0.000	0.000	0.000	0.000
127	A	130	ARG	1	0.788	0.852	31.234	8.943	8.943	0.000	0.000	0.000	0.000
128	A	131	GLY	0	-0.048	-0.023	31.114	-0.277	-0.277	0.000	0.000	0.000	0.000
129	A	132	ARG	1	0.844	0.916	25.216	11.412	11.412	0.000	0.000	0.000	0.000
130	A	133	PHE	0	0.055	0.030	32.457	0.110	0.110	0.000	0.000	0.000	0.000
131	A	134	SER	0	0.010	-0.004	35.599	-0.018	-0.018	0.000	0.000	0.000	0.000
132	A	135	LEU	0	0.030	0.028	38.810	0.137	0.137	0.000	0.000	0.000	0.000
133	A	136	LEU	0	0.003	0.018	34.207	0.092	0.092	0.000	0.000	0.000	0.000
134	A	137	ASP	-1	-0.824	-0.897	38.158	-7.985	-7.985	0.000	0.000	0.000	0.000
135	A	138	SER	0	0.027	0.007	40.580	0.088	0.088	0.000	0.000	0.000	0.000
136	A	139	TRP	0	0.021	0.015	37.095	0.162	0.162	0.000	0.000	0.000	0.000
137	A	140	LEU	0	-0.015	-0.022	36.425	0.060	0.060	0.000	0.000	0.000	0.000
138	A	141	GLU	-1	-1.018	-1.006	40.584	-6.605	-6.605	0.000	0.000	0.000	0.000
139	A	142	PHE	0	0.042	0.021	43.257	0.101	0.101	0.000	0.000	0.000	0.000
140	A	143	LEU	0	0.018	-0.006	39.062	0.089	0.089	0.000	0.000	0.000	0.000
141	A	144	LYS	1	0.868	0.952	43.239	7.088	7.088	0.000	0.000	0.000	0.000
142	A	145	ASN	0	-0.048	-0.020	45.410	0.174	0.174	0.000	0.000	0.000	0.000
143	A	146	ASN	0	-0.058	-0.027	44.652	0.150	0.150	0.000	0.000	0.000	0.000
144	A	147	THR	0	0.013	0.012	42.665	-0.159	-0.159	0.000	0.000	0.000	0.000
145	A	148	HIS	0	0.014	0.011	42.280	-0.179	-0.179	0.000	0.000	0.000	0.000
146	A	149	SER	0	-0.026	-0.016	37.382	-0.206	-0.206	0.000	0.000	0.000	0.000
147	A	150	ILE	0	0.014	0.015	35.420	0.112	0.112	0.000	0.000	0.000	0.000
148	A	151	SER	0	0.042	0.023	35.615	-0.260	-0.260	0.000	0.000	0.000	0.000
149	A	152	ARG	1	0.916	0.938	28.671	10.212	10.212	0.000	0.000	0.000	0.000
150	A	153	ASP	-1	-0.894	-0.950	33.776	-8.785	-8.785	0.000	0.000	0.000	0.000
151	A	154	THR	0	0.004	-0.004	36.201	0.075	0.075	0.000	0.000	0.000	0.000
152	A	155	TRP	0	-0.016	-0.008	28.405	0.108	0.108	0.000	0.000	0.000	0.000
153	A	156	ASN	0	-0.042	-0.025	30.948	-0.328	-0.328	0.000	0.000	0.000	0.000
154	A	157	LEU	0	0.036	0.016	32.816	-0.127	-0.127	0.000	0.000	0.000	0.000
155	A	158	LEU	0	0.059	0.045	34.860	0.151	0.151	0.000	0.000	0.000	0.000
156	A	159	TYR	0	-0.035	-0.004	28.732	-0.062	-0.062	0.000	0.000	0.000	0.000
157	A	160	ASP	-1	-0.773	-0.853	33.228	-9.293	-9.293	0.000	0.000	0.000	0.000
158	A	161	PHE	0	0.033	0.019	35.568	0.105	0.105	0.000	0.000	0.000	0.000
159	A	162	SER	0	-0.089	-0.056	34.107	0.021	0.021	0.000	0.000	0.000	0.000
160	A	163	GLN	0	-0.072	-0.050	32.451	-0.047	-0.047	0.000	0.000	0.000	0.000
161	A	164	LEU	0	-0.012	0.017	35.917	-0.014	-0.014	0.000	0.000	0.000	0.000
162	A	165	SER	0	-0.052	-0.048	38.683	0.162	0.162	0.000	0.000	0.000	0.000
163	A	166	GLU	-1	-0.939	-0.942	40.421	-7.045	-7.045	0.000	0.000	0.000	0.000
164	A	167	LYS	1	0.835	0.892	43.465	6.641	6.641	0.000	0.000	0.000	0.000
165	A	168	ASP	-1	-0.906	-0.967	42.555	-7.194	-7.194	0.000	0.000	0.000	0.000
166	A	169	LEU	0	-0.009	0.006	42.754	-0.018	-0.018	0.000	0.000	0.000	0.000
167	A	170	SER	0	-0.050	-0.028	45.029	0.152	0.152	0.000	0.000	0.000	0.000
168	A	171	ASP	-1	-0.925	-0.949	48.007	-6.239	-6.239	0.000	0.000	0.000	0.000
169	A	172	TYR	0	-0.021	-0.023	44.087	-0.105	-0.105	0.000	0.000	0.000	0.000
170	A	173	ASP	-1	-0.907	-0.945	45.577	-6.830	-6.830	0.000	0.000	0.000	0.000
171	A	174	GLU	-1	-0.805	-0.920	46.898	-6.251	-6.251	0.000	0.000	0.000	0.000
172	A	175	ASN	0	-0.109	-0.068	46.175	-0.014	-0.014	0.000	0.000	0.000	0.000
173	A	176	GLY	0	-0.052	-0.015	47.867	0.013	0.013	0.000	0.000	0.000	0.000
174	A	177	ALA	0	-0.027	-0.011	43.476	-0.051	-0.051	0.000	0.000	0.000	0.000
175	A	178	TRP	0	-0.026	-0.007	39.052	-0.375	-0.375	0.000	0.000	0.000	0.000
176	A	179	PRO	0	-0.021	-0.020	39.318	0.158	0.158	0.000	0.000	0.000	0.000
177	A	180	VAL	0	0.032	0.014	42.622	-0.019	-0.019	0.000	0.000	0.000	0.000
178	A	181	LEU	0	-0.007	0.007	40.379	0.043	0.043	0.000	0.000	0.000	0.000
179	A	182	ILE	0	-0.009	-0.007	38.664	-0.010	-0.010	0.000	0.000	0.000	0.000
180	A	183	ASP	-1	-0.750	-0.851	43.146	-6.438	-6.438	0.000	0.000	0.000	0.000
181	A	184	ASP	-1	-0.893	-0.952	46.741	-6.416	-6.416	0.000	0.000	0.000	0.000
182	A	185	PHE	0	-0.071	-0.029	41.968	0.067	0.067	0.000	0.000	0.000	0.000
183	A	186	VAL	0	0.009	0.000	45.200	0.073	0.073	0.000	0.000	0.000	0.000
184	A	187	LYS	1	0.814	0.910	47.631	6.336	6.336	0.000	0.000	0.000	0.000
185	A	188	TRP	0	0.040	0.009	46.531	0.036	0.036	0.000	0.000	0.000	0.000
186	A	189	LEU	0	-0.042	-0.030	44.846	0.058	0.058	0.000	0.000	0.000	0.000
187	A	190	LYS	1	0.788	0.907	49.465	6.059	6.059	0.000	0.000	0.000	0.000
188	A	191	HIS	0	-0.121	-0.054	52.828	0.063	0.063	0.000	0.000	0.000	0.000
189	A	192	GLU	-2	-1.818	-1.896	54.413	-11.397	-11.397	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ALA)