FMO DATABASE

FMODB ID: MRZ9Z

Calculation Name: 1E6B-A-Xray547

Preferred Name:

Target Type:

Ligand Name: beta-mercaptoethanol

Ligand 3-letter code: BME

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1E6B

Chain ID: A

ChEMBL ID:

UniProt ID: Q9ZVQ3

Base Structure: X-ray

Registration Date: 2025-09-02

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	194
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2178104.974264
FMO2-HF: Nuclear repulsion	2101859.393052
FMO2-HF: Total energy	-76245.581212
FMO2-MP2: Total energy	-76468.109346

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:8:LYS)

Summations of interaction energy for fragment #1(A:8:LYS)

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.
-251.335	-248.261	20.516	-11.997	-11.591	-0.139

Interaction energy analysis for fragmet #1(A:8:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.700 / q_NPA : 1.832

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	10	LYS	1	0.864	0.927	2.834	95.376	99.237	0.568	-1.563	-2.866	-0.010
4	A	11	LEU	0	0.001	0.008	5.065	7.270	7.289	-0.001	-0.004	-0.014	0.000
26	A	33	ASP	-1	-0.886	-0.938	4.765	-66.786	-66.748	-0.001	-0.007	-0.030	0.000
27	A	34	TYR	0	-0.079	-0.060	4.065	-11.975	-11.615	0.001	-0.101	-0.259	0.000
28	A	35	GLU	-1	-0.801	-0.900	1.745	-169.628	-170.937	19.945	-10.267	-8.368	-0.129
29	A	36	TYR	0	-0.018	-0.033	4.021	6.078	6.183	0.004	-0.055	-0.054	0.000
5	A	12	TYR	0	0.023	0.028	8.784	-0.184	-0.184	0.000	0.000	0.000	0.000
6	A	13	SER	0	0.018	-0.023	10.895	3.594	3.594	0.000	0.000	0.000	0.000
7	A	14	TYR	0	0.038	0.017	13.373	0.744	0.744	0.000	0.000	0.000	0.000
8	A	15	TRP	0	0.062	0.030	16.510	1.425	1.425	0.000	0.000	0.000	0.000
9	A	16	ARG	1	0.940	0.980	17.978	23.467	23.467	0.000	0.000	0.000	0.000
10	A	17	SER	0	-0.024	-0.003	18.531	1.766	1.766	0.000	0.000	0.000	0.000
11	A	18	SER	0	0.031	0.007	19.948	-1.124	-1.124	0.000	0.000	0.000	0.000
12	A	19	CYS	0	0.019	0.003	20.235	-0.240	-0.240	0.000	0.000	0.000	0.000
13	A	20	ALA	0	0.049	0.010	15.499	-1.018	-1.018	0.000	0.000	0.000	0.000
14	A	21	HIS	0	0.005	0.004	16.286	-0.403	-0.403	0.000	0.000	0.000	0.000
15	A	22	ARG	1	0.864	0.919	18.210	26.054	26.054	0.000	0.000	0.000	0.000
16	A	23	VAL	0	0.027	0.014	12.770	-0.193	-0.193	0.000	0.000	0.000	0.000
17	A	24	ARG	1	0.762	0.893	13.245	34.379	34.379	0.000	0.000	0.000	0.000
18	A	25	ILE	0	-0.015	0.005	14.433	-0.817	-0.817	0.000	0.000	0.000	0.000
19	A	26	ALA	0	0.002	0.002	14.662	-0.043	-0.043	0.000	0.000	0.000	0.000
20	A	27	LEU	0	-0.007	-0.008	8.457	-0.494	-0.494	0.000	0.000	0.000	0.000
21	A	28	ALA	0	-0.016	0.005	11.524	-1.297	-1.297	0.000	0.000	0.000	0.000
22	A	29	LEU	0	-0.045	-0.031	13.748	1.089	1.089	0.000	0.000	0.000	0.000
23	A	30	LYS	1	0.721	0.845	11.977	36.009	36.009	0.000	0.000	0.000	0.000
24	A	31	GLY	0	0.000	0.021	11.831	-0.941	-0.941	0.000	0.000	0.000	0.000
25	A	32	LEU	0	-0.044	-0.018	7.195	-3.320	-3.320	0.000	0.000	0.000	0.000
30	A	37	ILE	0	-0.010	-0.005	5.494	-1.375	-1.375	0.000	0.000	0.000	0.000
31	A	38	PRO	0	0.009	-0.004	8.766	3.397	3.397	0.000	0.000	0.000	0.000
32	A	39	VAL	0	0.021	0.021	12.319	-0.432	-0.432	0.000	0.000	0.000	0.000
33	A	40	ASN	0	-0.025	-0.033	15.135	2.207	2.207	0.000	0.000	0.000	0.000
34	A	41	LEU	0	-0.004	-0.010	18.353	1.141	1.141	0.000	0.000	0.000	0.000
35	A	42	LEU	0	-0.044	-0.017	20.869	1.152	1.152	0.000	0.000	0.000	0.000
36	A	43	LYS	1	0.935	0.969	19.984	28.143	28.143	0.000	0.000	0.000	0.000
37	A	44	GLY	0	0.017	0.027	22.100	0.692	0.692	0.000	0.000	0.000	0.000
38	A	45	ASP	-1	-0.814	-0.907	16.669	-31.914	-31.914	0.000	0.000	0.000	0.000
39	A	46	GLN	0	-0.020	-0.022	17.737	-1.806	-1.806	0.000	0.000	0.000	0.000
40	A	47	PHE	0	-0.079	-0.052	18.774	0.275	0.275	0.000	0.000	0.000	0.000
41	A	48	ASP	-1	-0.797	-0.886	16.722	-31.992	-31.992	0.000	0.000	0.000	0.000
42	A	49	SER	0	-0.003	-0.018	18.748	-0.611	-0.611	0.000	0.000	0.000	0.000
43	A	50	ASP	-1	-0.907	-0.944	14.744	-34.197	-34.197	0.000	0.000	0.000	0.000
44	A	51	PHE	0	-0.063	-0.027	13.104	-2.656	-2.656	0.000	0.000	0.000	0.000
45	A	52	LYS	1	0.905	0.953	14.806	26.850	26.850	0.000	0.000	0.000	0.000
46	A	53	LYS	1	0.933	0.985	14.684	38.746	38.746	0.000	0.000	0.000	0.000
47	A	54	ILE	0	-0.050	-0.022	9.733	-1.492	-1.492	0.000	0.000	0.000	0.000
48	A	55	ASN	0	-0.009	0.001	13.362	0.014	0.014	0.000	0.000	0.000	0.000
49	A	56	PRO	0	0.069	0.040	15.047	2.026	2.026	0.000	0.000	0.000	0.000
50	A	57	MET	0	-0.031	-0.027	18.373	2.247	2.247	0.000	0.000	0.000	0.000
51	A	58	GLY	0	-0.015	-0.001	18.084	1.428	1.428	0.000	0.000	0.000	0.000
52	A	59	THR	0	-0.022	-0.009	18.672	-0.361	-0.361	0.000	0.000	0.000	0.000
53	A	60	VAL	0	0.029	0.028	14.993	-2.145	-2.145	0.000	0.000	0.000	0.000
54	A	61	PRO	0	-0.075	-0.042	14.364	2.056	2.056	0.000	0.000	0.000	0.000
55	A	62	ALA	0	0.001	-0.004	12.923	1.923	1.923	0.000	0.000	0.000	0.000
56	A	63	LEU	0	-0.006	0.010	8.531	-3.159	-3.159	0.000	0.000	0.000	0.000
57	A	64	VAL	0	-0.009	-0.010	6.500	2.986	2.986	0.000	0.000	0.000	0.000
58	A	65	ASP	-1	-0.790	-0.873	5.369	-83.686	-83.686	0.000	0.000	0.000	0.000
59	A	66	GLY	0	0.001	0.006	5.189	5.183	5.183	0.000	0.000	0.000	0.000
60	A	67	ASP	-1	-0.898	-0.958	6.363	-48.617	-48.617	0.000	0.000	0.000	0.000
61	A	68	VAL	0	-0.050	-0.014	9.231	4.201	4.201	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.006	0.000	9.853	-5.019	-5.019	0.000	0.000	0.000	0.000
63	A	70	ILE	0	-0.017	0.005	12.201	3.494	3.494	0.000	0.000	0.000	0.000
64	A	71	ASN	0	-0.030	-0.035	13.751	-1.800	-1.800	0.000	0.000	0.000	0.000
65	A	72	ASP	-1	-0.751	-0.896	16.513	-28.049	-28.049	0.000	0.000	0.000	0.000
66	A	73	SER	0	-0.038	0.003	17.742	-0.840	-0.840	0.000	0.000	0.000	0.000
67	A	74	PHE	0	0.024	-0.005	18.730	-0.620	-0.620	0.000	0.000	0.000	0.000
68	A	75	ALA	0	0.025	0.008	18.554	-0.444	-0.444	0.000	0.000	0.000	0.000
69	A	76	ILE	0	-0.023	-0.009	12.942	-1.301	-1.301	0.000	0.000	0.000	0.000
70	A	77	ILE	0	-0.009	-0.013	14.299	-1.581	-1.581	0.000	0.000	0.000	0.000
71	A	78	MET	0	-0.021	-0.001	16.297	0.447	0.447	0.000	0.000	0.000	0.000
72	A	79	TYR	0	-0.006	-0.021	8.966	1.167	1.167	0.000	0.000	0.000	0.000
73	A	80	LEU	0	-0.016	-0.023	9.770	-1.844	-1.844	0.000	0.000	0.000	0.000
74	A	81	ASP	-1	-0.835	-0.911	12.722	-30.776	-30.776	0.000	0.000	0.000	0.000
75	A	82	GLU	-1	-0.982	-0.989	15.754	-29.444	-29.444	0.000	0.000	0.000	0.000
76	A	83	LYS	1	0.814	0.901	6.807	61.457	61.457	0.000	0.000	0.000	0.000
77	A	84	TYR	0	-0.010	-0.014	6.218	-4.011	-4.011	0.000	0.000	0.000	0.000
78	A	85	PRO	0	0.050	0.032	12.359	1.107	1.107	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.989	-0.976	15.376	-27.876	-27.876	0.000	0.000	0.000	0.000
80	A	87	PRO	0	0.036	0.015	15.100	-1.785	-1.785	0.000	0.000	0.000	0.000
81	A	88	PRO	0	-0.001	0.012	18.006	-0.946	-0.946	0.000	0.000	0.000	0.000
82	A	89	LEU	0	0.028	0.001	16.595	1.060	1.060	0.000	0.000	0.000	0.000
83	A	90	LEU	0	-0.028	-0.022	20.613	1.205	1.205	0.000	0.000	0.000	0.000
84	A	91	PRO	0	0.007	0.025	23.705	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	92	ARG	1	0.979	0.972	26.713	19.885	19.885	0.000	0.000	0.000	0.000
86	A	93	ASP	-1	-0.830	-0.896	28.362	-17.371	-17.371	0.000	0.000	0.000	0.000
87	A	94	LEU	0	0.089	0.020	30.118	-0.399	-0.399	0.000	0.000	0.000	0.000
88	A	95	HIS	0	0.030	0.033	31.889	-0.402	-0.402	0.000	0.000	0.000	0.000
89	A	96	LYS	1	0.922	0.945	30.815	17.731	17.731	0.000	0.000	0.000	0.000
90	A	97	ARG	1	0.884	0.957	23.377	22.695	22.695	0.000	0.000	0.000	0.000
91	A	98	ALA	0	0.009	0.020	28.853	-0.488	-0.488	0.000	0.000	0.000	0.000
92	A	99	VAL	0	0.046	0.013	31.208	-0.277	-0.277	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.014	-0.028	26.389	-0.859	-0.859	0.000	0.000	0.000	0.000
94	A	101	TYR	0	0.033	0.010	24.019	-0.190	-0.190	0.000	0.000	0.000	0.000
95	A	102	GLN	0	-0.023	-0.012	28.158	-0.104	-0.104	0.000	0.000	0.000	0.000
96	A	103	ALA	0	0.027	0.003	29.437	0.087	0.087	0.000	0.000	0.000	0.000
97	A	104	MET	0	-0.030	0.011	24.283	-0.155	-0.155	0.000	0.000	0.000	0.000
98	A	105	SER	0	0.041	0.014	27.269	-0.227	-0.227	0.000	0.000	0.000	0.000
99	A	106	ILE	0	-0.009	0.004	29.483	0.201	0.201	0.000	0.000	0.000	0.000
100	A	107	VAL	0	-0.020	-0.009	26.409	0.186	0.186	0.000	0.000	0.000	0.000
101	A	108	LEU	0	-0.039	-0.020	23.863	-0.093	-0.093	0.000	0.000	0.000	0.000
102	A	109	SER	0	-0.083	-0.059	27.315	0.148	0.148	0.000	0.000	0.000	0.000
103	A	110	GLY	0	-0.014	0.000	30.589	0.470	0.470	0.000	0.000	0.000	0.000
104	A	111	ILE	0	-0.076	-0.032	30.953	0.535	0.535	0.000	0.000	0.000	0.000
105	A	112	GLN	0	0.043	0.039	24.986	-0.522	-0.522	0.000	0.000	0.000	0.000
106	A	113	PRO	0	-0.018	0.007	29.333	0.089	0.089	0.000	0.000	0.000	0.000
107	A	133	THR	0	0.014	0.002	44.492	0.063	0.063	0.000	0.000	0.000	0.000
108	A	134	ALA	0	0.000	-0.005	41.741	-0.260	-0.260	0.000	0.000	0.000	0.000
109	A	135	TRP	0	-0.006	0.001	37.566	0.306	0.306	0.000	0.000	0.000	0.000
110	A	136	VAL	0	0.040	0.019	39.869	-0.242	-0.242	0.000	0.000	0.000	0.000
111	A	137	ASN	0	0.008	0.006	34.308	0.336	0.336	0.000	0.000	0.000	0.000
112	A	138	ASN	0	0.062	0.015	38.487	-0.269	-0.269	0.000	0.000	0.000	0.000
113	A	139	ALA	0	0.001	0.012	36.331	0.161	0.161	0.000	0.000	0.000	0.000
114	A	140	ILE	0	0.026	0.016	32.660	-0.176	-0.176	0.000	0.000	0.000	0.000
115	A	141	THR	0	0.020	0.021	36.011	-0.169	-0.169	0.000	0.000	0.000	0.000
116	A	142	LYS	1	0.944	0.986	38.923	15.779	15.779	0.000	0.000	0.000	0.000
117	A	143	GLY	0	0.022	0.002	35.298	0.077	0.077	0.000	0.000	0.000	0.000
118	A	144	PHE	0	0.001	-0.012	31.929	-0.248	-0.248	0.000	0.000	0.000	0.000
119	A	145	THR	0	0.028	0.002	36.568	0.232	0.232	0.000	0.000	0.000	0.000
120	A	146	ALA	0	-0.089	-0.039	36.902	0.349	0.349	0.000	0.000	0.000	0.000
121	A	147	LEU	0	0.009	0.003	31.628	0.065	0.065	0.000	0.000	0.000	0.000
122	A	148	GLU	-1	-0.722	-0.840	35.272	-16.620	-16.620	0.000	0.000	0.000	0.000
123	A	149	LYS	1	0.865	0.931	37.667	15.219	15.219	0.000	0.000	0.000	0.000
124	A	150	LEU	0	-0.066	-0.019	33.187	0.227	0.227	0.000	0.000	0.000	0.000
125	A	151	LEU	0	0.010	-0.008	31.625	-0.105	-0.105	0.000	0.000	0.000	0.000
126	A	152	VAL	0	0.013	0.022	35.763	-0.022	-0.022	0.000	0.000	0.000	0.000
127	A	153	ASN	0	-0.055	-0.024	38.958	0.427	0.427	0.000	0.000	0.000	0.000
128	A	154	CYS	0	-0.075	-0.021	34.264	-0.087	-0.087	0.000	0.000	0.000	0.000
129	A	155	ALA	0	0.006	0.002	35.972	-0.127	-0.127	0.000	0.000	0.000	0.000
130	A	156	GLY	0	0.038	0.019	33.801	-0.390	-0.390	0.000	0.000	0.000	0.000
131	A	157	LYS	1	0.928	0.949	30.761	19.599	19.599	0.000	0.000	0.000	0.000
132	A	158	HIS	1	0.842	0.930	27.762	21.716	21.716	0.000	0.000	0.000	0.000
133	A	159	ALA	0	0.003	-0.010	28.672	0.749	0.749	0.000	0.000	0.000	0.000
134	A	160	THR	0	-0.005	-0.022	29.379	0.383	0.383	0.000	0.000	0.000	0.000
135	A	161	GLY	0	0.034	0.017	31.000	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	162	ASP	-1	-0.846	-0.917	30.652	-18.466	-18.466	0.000	0.000	0.000	0.000
137	A	163	GLU	-1	-0.954	-0.967	25.552	-22.957	-22.957	0.000	0.000	0.000	0.000
138	A	164	ILE	0	-0.059	-0.023	21.971	0.477	0.477	0.000	0.000	0.000	0.000
139	A	165	TYR	0	0.003	-0.003	23.321	-0.068	-0.068	0.000	0.000	0.000	0.000
140	A	166	LEU	0	0.031	0.004	21.171	-0.053	-0.053	0.000	0.000	0.000	0.000
141	A	167	ALA	0	0.008	-0.005	23.316	-0.262	-0.262	0.000	0.000	0.000	0.000
142	A	168	ASP	-1	-0.730	-0.849	24.467	-22.238	-22.238	0.000	0.000	0.000	0.000
143	A	169	LEU	0	-0.003	0.007	18.361	-0.151	-0.151	0.000	0.000	0.000	0.000
144	A	170	PHE	0	-0.003	-0.018	21.214	-0.662	-0.662	0.000	0.000	0.000	0.000
145	A	171	LEU	0	0.008	0.002	24.507	0.415	0.415	0.000	0.000	0.000	0.000
146	A	172	ALA	0	0.036	0.031	23.708	0.396	0.396	0.000	0.000	0.000	0.000
147	A	173	PRO	0	0.005	-0.002	21.973	0.505	0.505	0.000	0.000	0.000	0.000
148	A	174	GLN	0	-0.033	-0.010	24.529	0.339	0.339	0.000	0.000	0.000	0.000
149	A	175	ILE	0	-0.001	-0.005	27.836	0.675	0.675	0.000	0.000	0.000	0.000
150	A	176	HIS	0	-0.014	0.005	24.767	0.729	0.729	0.000	0.000	0.000	0.000
151	A	177	GLY	0	-0.032	-0.031	27.388	0.316	0.316	0.000	0.000	0.000	0.000
152	A	178	ALA	0	-0.007	-0.008	28.354	0.541	0.541	0.000	0.000	0.000	0.000
153	A	179	ILE	0	0.024	0.018	31.168	0.572	0.572	0.000	0.000	0.000	0.000
154	A	180	ASN	0	0.000	-0.013	27.398	1.050	1.050	0.000	0.000	0.000	0.000
155	A	181	ARG	1	0.806	0.902	24.666	23.459	23.459	0.000	0.000	0.000	0.000
156	A	182	PHE	0	-0.025	-0.023	31.416	0.349	0.349	0.000	0.000	0.000	0.000
157	A	183	GLN	0	0.005	0.023	34.449	0.842	0.842	0.000	0.000	0.000	0.000
158	A	184	ILE	0	-0.042	-0.015	34.902	0.457	0.457	0.000	0.000	0.000	0.000
159	A	185	ASN	0	-0.018	-0.029	36.509	-0.626	-0.626	0.000	0.000	0.000	0.000
160	A	186	MET	0	0.016	-0.002	34.004	-0.028	-0.028	0.000	0.000	0.000	0.000
161	A	187	GLU	-1	-0.858	-0.901	38.073	-14.370	-14.370	0.000	0.000	0.000	0.000
162	A	188	PRO	0	-0.045	-0.024	40.700	0.188	0.188	0.000	0.000	0.000	0.000
163	A	189	TYR	0	-0.031	-0.022	37.351	0.121	0.121	0.000	0.000	0.000	0.000
164	A	190	PRO	0	0.071	0.043	37.521	-0.495	-0.495	0.000	0.000	0.000	0.000
165	A	191	THR	0	-0.009	-0.039	35.080	-0.242	-0.242	0.000	0.000	0.000	0.000
166	A	192	LEU	0	-0.020	-0.024	32.764	-0.612	-0.612	0.000	0.000	0.000	0.000
167	A	193	ALA	0	-0.013	-0.002	32.911	-0.642	-0.642	0.000	0.000	0.000	0.000
168	A	194	LYS	1	0.832	0.927	33.417	17.790	17.790	0.000	0.000	0.000	0.000
169	A	195	CYS	0	-0.057	-0.013	30.057	-0.299	-0.299	0.000	0.000	0.000	0.000
170	A	196	TYR	0	0.023	0.016	27.634	-0.958	-0.958	0.000	0.000	0.000	0.000
171	A	197	GLU	-1	-0.845	-0.918	29.391	-19.855	-19.855	0.000	0.000	0.000	0.000
172	A	198	SER	0	-0.064	-0.041	29.472	-0.577	-0.577	0.000	0.000	0.000	0.000
173	A	199	TYR	0	-0.023	-0.063	25.073	-0.619	-0.619	0.000	0.000	0.000	0.000
174	A	200	ASN	0	-0.041	-0.006	25.380	-1.633	-1.633	0.000	0.000	0.000	0.000
175	A	201	GLU	-1	-0.939	-0.960	26.674	-21.234	-21.234	0.000	0.000	0.000	0.000
176	A	202	LEU	0	-0.008	0.003	22.550	-0.646	-0.646	0.000	0.000	0.000	0.000
177	A	203	PRO	0	0.029	0.002	19.570	-0.774	-0.774	0.000	0.000	0.000	0.000
178	A	204	ALA	0	0.001	0.002	17.381	-1.022	-1.022	0.000	0.000	0.000	0.000
179	A	205	PHE	0	0.017	-0.001	18.110	-1.068	-1.068	0.000	0.000	0.000	0.000
180	A	206	GLN	0	-0.014	-0.021	20.531	-1.027	-1.027	0.000	0.000	0.000	0.000
181	A	207	ASN	0	-0.004	-0.012	15.780	1.124	1.124	0.000	0.000	0.000	0.000
182	A	208	ALA	0	-0.002	0.018	16.212	-1.749	-1.749	0.000	0.000	0.000	0.000
183	A	209	LEU	0	0.023	0.024	17.407	-0.064	-0.064	0.000	0.000	0.000	0.000
184	A	210	PRO	0	-0.051	-0.019	18.864	-1.300	-1.300	0.000	0.000	0.000	0.000
185	A	211	GLU	-1	-0.796	-0.916	19.206	-26.775	-26.775	0.000	0.000	0.000	0.000
186	A	212	LYS	1	0.911	0.969	17.547	27.911	27.911	0.000	0.000	0.000	0.000
187	A	213	GLN	0	-0.036	-0.022	14.119	-4.228	-4.228	0.000	0.000	0.000	0.000
188	A	214	PRO	0	0.010	-0.006	10.724	1.488	1.488	0.000	0.000	0.000	0.000
189	A	215	ASP	-1	-0.769	-0.863	13.700	-35.929	-35.929	0.000	0.000	0.000	0.000
190	A	216	ALA	0	-0.029	-0.004	15.756	1.652	1.652	0.000	0.000	0.000	0.000
191	A	217	PRO	0	-0.061	-0.042	19.064	0.117	0.117	0.000	0.000	0.000	0.000
192	A	218	SER	0	0.000	0.009	20.773	-0.165	-0.165	0.000	0.000	0.000	0.000
193	A	219	SER	0	-0.038	-0.024	22.684	0.894	0.894	0.000	0.000	0.000	0.000
194	A	220	THR	-1	-0.924	-0.947	22.984	-22.449	-22.449	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:LYS)