FMO DATABASE

FMODB ID: RM5Z8

Calculation Name: 3BBD-A-Xray547

Preferred Name:

Target Type:

Ligand Name: s-adenosyl-l-homocysteine | glycerol

Ligand 3-letter code: SAH | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3BBD

Chain ID: A

ChEMBL ID:

UniProt ID: Q57977

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	204
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2564794.037757
FMO2-HF: Nuclear repulsion	2481280.601692
FMO2-HF: Total energy	-83513.436065
FMO2-MP2: Total energy	-83757.590478

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:THR)

Summations of interaction energy for fragment #1(A:2:THR)

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.
48.049	55.552	6.273	-6.108	-7.668	-0.06

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.802 / q_NPA : 0.897

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	ASN	0	0.012	-0.003	3.497	-3.937	-2.108	0.004	-0.831	-1.003	-0.002
73	A	74	LYS	1	0.816	0.900	5.247	23.294	23.395	-0.001	-0.014	-0.085	0.000
74	A	75	LYS	1	0.851	0.915	2.186	25.730	27.304	1.673	-1.388	-1.859	-0.010
75	A	76	LEU	0	-0.015	-0.001	2.304	-22.224	-19.835	4.455	-3.214	-3.630	-0.042
76	A	77	ASN	0	-0.037	-0.005	2.774	2.895	4.508	0.143	-0.659	-1.097	-0.006
77	A	78	ILE	0	0.018	0.005	4.831	1.634	1.631	-0.001	-0.002	0.006	0.000
4	A	5	ILE	0	0.000	0.000	5.864	3.333	3.333	0.000	0.000	0.000	0.000
5	A	6	ILE	0	0.022	0.006	8.831	0.562	0.562	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.033	-0.003	11.940	0.944	0.944	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.039	0.014	15.472	0.040	0.040	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.880	0.926	17.828	13.260	13.260	0.000	0.000	0.000	0.000
9	A	10	SER	0	-0.012	-0.011	18.583	0.457	0.457	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.014	0.008	21.241	0.358	0.358	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.072	-0.045	20.187	0.375	0.375	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.729	-0.853	23.519	-11.043	-11.043	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.019	-0.002	26.257	0.198	0.198	0.000	0.000	0.000	0.000
14	A	15	ILE	0	-0.072	-0.039	29.050	0.090	0.090	0.000	0.000	0.000	0.000
15	A	16	PRO	0	0.053	0.023	31.344	0.164	0.164	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.767	-0.883	33.544	-8.105	-8.105	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.875	-0.941	33.641	-8.848	-8.848	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.061	-0.046	34.977	0.267	0.267	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.899	0.947	34.885	8.761	8.761	0.000	0.000	0.000	0.000
20	A	21	ASN	0	0.008	0.001	39.275	0.018	0.018	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.900	0.961	40.691	7.775	7.775	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.048	-0.014	36.947	0.020	0.020	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.971	0.993	40.670	6.756	6.756	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.905	0.951	35.925	8.392	8.392	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.043	0.014	40.392	0.166	0.166	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.985	0.978	40.098	6.647	6.647	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.010	0.009	39.371	-0.086	-0.086	0.000	0.000	0.000	0.000
28	A	29	TYR	0	-0.032	-0.026	31.055	-0.203	-0.203	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.857	0.930	35.673	8.154	8.154	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.036	0.027	30.792	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.827	-0.902	31.909	-8.663	-8.663	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.006	0.018	25.577	-0.120	-0.120	0.000	0.000	0.000	0.000
33	A	34	LEU	0	-0.021	-0.001	29.174	0.382	0.382	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.775	-0.876	29.095	-10.377	-10.377	0.000	0.000	0.000	0.000
35	A	36	SER	0	0.033	-0.008	31.102	0.394	0.394	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.079	-0.051	31.251	0.449	0.449	0.000	0.000	0.000	0.000
37	A	38	TYR	0	-0.030	-0.020	32.893	0.390	0.390	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.020	-0.012	33.339	0.116	0.116	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.049	0.023	36.743	0.169	0.169	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.888	0.946	37.675	7.167	7.167	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.007	0.004	38.265	0.088	0.088	0.000	0.000	0.000	0.000
42	A	43	MET	0	-0.036	-0.019	31.978	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.848	-0.907	37.228	-7.349	-7.349	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.914	0.961	39.955	7.490	7.490	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.038	-0.006	32.416	0.078	0.078	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.961	0.985	31.138	9.816	9.816	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.770	-0.867	30.005	-10.250	-10.250	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.881	0.949	30.779	7.857	7.857	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.892	-0.956	31.960	-9.133	-9.133	0.000	0.000	0.000	0.000
50	A	51	MET	0	-0.086	-0.051	26.665	-0.350	-0.350	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.806	0.891	26.622	9.640	9.640	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.019	0.015	28.167	0.187	0.187	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.802	0.858	26.578	11.140	11.140	0.000	0.000	0.000	0.000
54	A	55	PRO	0	0.078	0.039	24.071	-0.538	-0.538	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.782	-0.857	23.182	-11.989	-11.989	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.015	0.013	21.260	-0.420	-0.420	0.000	0.000	0.000	0.000
57	A	58	ILE	0	0.008	0.027	17.859	-0.742	-0.742	0.000	0.000	0.000	0.000
58	A	59	HIS	0	-0.072	-0.034	18.728	-0.513	-0.513	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.032	0.002	19.803	-0.590	-0.590	0.000	0.000	0.000	0.000
60	A	61	SER	0	-0.004	-0.032	16.524	-0.506	-0.506	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.001	-0.001	13.742	-1.055	-1.055	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.058	-0.024	15.459	-0.681	-0.681	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.025	-0.020	16.606	0.009	0.009	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.007	-0.002	10.385	-0.734	-0.734	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.061	-0.023	11.553	-1.504	-1.504	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.898	-0.922	12.914	-17.595	-17.595	0.000	0.000	0.000	0.000
67	A	68	SER	0	-0.021	-0.010	11.131	-0.455	-0.455	0.000	0.000	0.000	0.000
68	A	69	PRO	0	0.046	0.006	11.291	-1.232	-1.232	0.000	0.000	0.000	0.000
69	A	70	ILE	0	0.014	0.018	5.145	-1.769	-1.769	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.048	-0.051	6.367	-7.435	-7.435	0.000	0.000	0.000	0.000
71	A	72	HIS	0	-0.017	-0.011	7.941	-1.600	-1.600	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.894	-0.930	7.536	-30.307	-30.307	0.000	0.000	0.000	0.000
78	A	79	TYR	0	0.036	0.008	6.502	1.438	1.438	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.040	-0.021	11.407	0.427	0.427	0.000	0.000	0.000	0.000
80	A	81	HIS	0	0.061	0.036	15.174	-0.155	-0.155	0.000	0.000	0.000	0.000
81	A	82	THR	0	-0.014	-0.035	17.310	0.024	0.024	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.064	-0.074	21.003	0.007	0.007	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.851	-0.897	24.260	-11.942	-11.942	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.831	-0.896	21.674	-13.233	-13.233	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.904	0.962	20.722	11.655	11.655	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.006	-0.010	13.936	-0.586	-0.586	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.020	-0.012	15.779	0.353	0.353	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.899	0.947	6.388	32.436	32.436	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.043	-0.030	11.143	1.589	1.589	0.000	0.000	0.000	0.000
90	A	91	ASN	0	0.027	0.019	9.890	-3.331	-3.331	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.072	0.043	6.495	2.173	2.173	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.827	-0.894	9.592	-20.537	-20.537	0.000	0.000	0.000	0.000
93	A	94	THR	0	-0.066	-0.048	12.832	2.169	2.169	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.989	0.999	15.134	12.971	12.971	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.006	0.002	17.338	0.932	0.932	0.000	0.000	0.000	0.000
96	A	97	PRO	0	-0.022	-0.010	19.394	0.346	0.346	0.000	0.000	0.000	0.000
97	A	98	ARG	1	1.018	1.004	18.607	14.736	14.736	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.014	0.001	24.452	0.191	0.191	0.000	0.000	0.000	0.000
99	A	100	TYR	0	0.060	-0.002	25.764	-0.308	-0.308	0.000	0.000	0.000	0.000
100	A	101	PHE	0	0.045	0.019	27.114	-0.168	-0.168	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.933	0.963	26.792	10.295	10.295	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.016	0.013	19.640	-0.183	-0.183	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.009	0.012	24.202	-0.267	-0.267	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.030	0.012	26.597	-0.046	-0.046	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.069	-0.028	21.545	0.023	0.023	0.000	0.000	0.000	0.000
106	A	107	MET	0	0.023	0.004	17.919	-0.245	-0.245	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.784	-0.886	23.182	-9.866	-9.866	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.937	0.975	25.582	10.530	10.530	0.000	0.000	0.000	0.000
109	A	110	VAL	0	0.003	0.008	19.584	0.031	0.031	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.013	-0.013	21.893	-0.092	-0.092	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.775	0.861	24.397	9.900	9.900	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.030	0.037	24.554	0.299	0.299	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.947	-0.975	25.594	-10.415	-10.415	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.939	0.961	21.920	11.898	11.898	0.000	0.000	0.000	0.000
115	A	116	ASN	0	0.052	0.030	18.704	-0.283	-0.283	0.000	0.000	0.000	0.000
116	A	117	HIS	0	0.011	-0.009	17.703	-0.347	-0.347	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.012	-0.008	14.343	-0.922	-0.922	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.013	-0.006	14.000	-1.227	-1.227	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.875	0.950	14.276	17.917	17.917	0.000	0.000	0.000	0.000
120	A	121	MET	0	-0.002	0.000	16.006	-0.739	-0.739	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.871	-0.926	15.701	-17.043	-17.043	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.933	-0.970	19.031	-11.987	-11.987	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.769	0.864	14.987	17.068	17.068	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.007	-0.010	19.364	-0.366	-0.366	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.013	-0.021	15.594	-0.942	-0.942	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.799	-0.907	16.090	-15.468	-15.468	0.000	0.000	0.000	0.000
127	A	128	ASP	-1	-0.818	-0.877	16.641	-15.288	-15.288	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.006	-0.002	11.582	-0.972	-0.972	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.039	-0.031	12.096	-1.927	-1.927	0.000	0.000	0.000	0.000
130	A	131	ASN	0	0.001	-0.007	12.212	-1.810	-1.810	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.836	-0.901	12.732	-18.520	-18.520	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.101	-0.042	7.416	-1.326	-1.326	0.000	0.000	0.000	0.000
133	A	134	ASN	0	-0.060	-0.030	7.723	-2.668	-2.668	0.000	0.000	0.000	0.000
134	A	135	ALA	0	0.001	0.007	9.255	-2.526	-2.526	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.925	0.960	7.889	34.085	34.085	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.896	0.960	10.610	27.813	27.813	0.000	0.000	0.000	0.000
137	A	138	ILE	0	0.013	-0.001	11.298	-2.203	-2.203	0.000	0.000	0.000	0.000
138	A	139	ALA	0	-0.002	0.000	13.080	1.824	1.824	0.000	0.000	0.000	0.000
139	A	140	ILE	0	0.010	0.003	14.758	-0.459	-0.459	0.000	0.000	0.000	0.000
140	A	141	MET	0	-0.004	0.000	15.317	0.567	0.567	0.000	0.000	0.000	0.000
141	A	142	THR	0	-0.003	-0.016	18.191	0.870	0.870	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.983	0.989	22.017	10.856	10.856	0.000	0.000	0.000	0.000
143	A	144	THR	0	-0.057	-0.035	24.920	0.466	0.466	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.052	0.039	22.669	0.210	0.210	0.000	0.000	0.000	0.000
145	A	146	LYS	1	0.937	0.957	21.760	12.715	12.715	0.000	0.000	0.000	0.000
146	A	147	LEU	0	0.008	0.019	21.788	-0.747	-0.747	0.000	0.000	0.000	0.000
147	A	148	THR	0	-0.019	-0.008	17.335	0.064	0.064	0.000	0.000	0.000	0.000
148	A	149	HIS	0	0.041	0.008	20.007	-0.717	-0.717	0.000	0.000	0.000	0.000
149	A	150	PRO	0	0.079	0.013	16.313	-0.710	-0.710	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.963	0.998	14.827	14.417	14.417	0.000	0.000	0.000	0.000
151	A	152	LEU	0	-0.020	-0.018	14.192	-0.777	-0.777	0.000	0.000	0.000	0.000
152	A	153	LEU	0	-0.011	-0.001	12.065	-0.481	-0.481	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.846	0.896	8.903	22.819	22.819	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.909	-0.944	8.303	-28.032	-28.032	0.000	0.000	0.000	0.000
155	A	156	TYR	0	-0.054	-0.035	9.981	1.602	1.602	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.744	-0.841	6.059	-36.359	-36.359	0.000	0.000	0.000	0.000
157	A	158	THR	0	0.009	-0.016	6.576	-5.253	-5.253	0.000	0.000	0.000	0.000
158	A	159	PHE	0	-0.014	-0.006	7.644	4.057	4.057	0.000	0.000	0.000	0.000
159	A	160	ILE	0	0.020	0.008	11.399	-0.223	-0.223	0.000	0.000	0.000	0.000
160	A	161	ILE	0	-0.014	-0.009	13.191	1.154	1.154	0.000	0.000	0.000	0.000
161	A	162	GLY	0	0.025	0.009	16.642	0.041	0.041	0.000	0.000	0.000	0.000
162	A	163	GLY	0	0.011	0.001	19.608	0.016	0.016	0.000	0.000	0.000	0.000
163	A	164	PHE	0	-0.048	-0.012	20.100	0.417	0.417	0.000	0.000	0.000	0.000
164	A	165	PRO	0	-0.032	-0.010	23.896	-0.197	-0.197	0.000	0.000	0.000	0.000
165	A	166	TYR	0	0.007	0.001	26.804	0.146	0.146	0.000	0.000	0.000	0.000
166	A	167	GLY	0	0.034	0.029	27.404	-0.143	-0.143	0.000	0.000	0.000	0.000
167	A	168	LYS	1	0.795	0.867	24.437	12.188	12.188	0.000	0.000	0.000	0.000
168	A	169	LEU	0	0.024	0.017	17.882	0.378	0.378	0.000	0.000	0.000	0.000
169	A	170	LYS	1	0.932	0.956	22.585	11.164	11.164	0.000	0.000	0.000	0.000
170	A	171	ILE	0	0.034	0.019	17.722	-0.091	-0.091	0.000	0.000	0.000	0.000
171	A	172	ASN	0	-0.116	-0.067	21.927	0.814	0.814	0.000	0.000	0.000	0.000
172	A	173	LYS	1	1.000	0.990	21.819	12.812	12.812	0.000	0.000	0.000	0.000
173	A	174	GLU	-1	-0.834	-0.931	22.150	-12.502	-12.502	0.000	0.000	0.000	0.000
174	A	175	LYS	1	0.882	0.958	21.952	12.133	12.133	0.000	0.000	0.000	0.000
175	A	176	VAL	0	-0.034	-0.003	16.117	-0.571	-0.571	0.000	0.000	0.000	0.000
176	A	177	PHE	0	0.012	0.009	15.581	0.435	0.435	0.000	0.000	0.000	0.000
177	A	178	GLY	0	0.015	0.023	14.513	-0.158	-0.158	0.000	0.000	0.000	0.000
178	A	179	ASP	-1	-0.924	-0.965	15.370	-16.407	-16.407	0.000	0.000	0.000	0.000
179	A	180	ILE	0	-0.033	-0.014	15.861	-1.011	-1.011	0.000	0.000	0.000	0.000
180	A	181	LYS	1	0.888	0.942	17.553	18.383	18.383	0.000	0.000	0.000	0.000
181	A	182	GLU	-1	-0.829	-0.880	18.308	-13.717	-13.717	0.000	0.000	0.000	0.000
182	A	183	ILE	0	-0.030	-0.020	16.518	0.472	0.472	0.000	0.000	0.000	0.000
183	A	184	SER	0	0.009	0.013	19.705	-0.106	-0.106	0.000	0.000	0.000	0.000
184	A	185	ILE	0	0.038	0.009	17.487	-0.240	-0.240	0.000	0.000	0.000	0.000
185	A	186	TYR	0	-0.003	-0.010	20.899	0.388	0.388	0.000	0.000	0.000	0.000
186	A	187	ASN	0	0.021	0.015	24.458	-0.329	-0.329	0.000	0.000	0.000	0.000
187	A	188	LYS	1	0.969	0.983	26.906	10.633	10.633	0.000	0.000	0.000	0.000
188	A	189	GLY	0	-0.026	-0.005	26.280	-0.439	-0.439	0.000	0.000	0.000	0.000
189	A	190	LEU	0	0.007	-0.001	22.511	0.257	0.257	0.000	0.000	0.000	0.000
190	A	191	MET	0	0.022	0.021	23.542	-0.070	-0.070	0.000	0.000	0.000	0.000
191	A	192	ALA	0	0.089	0.043	19.021	-0.473	-0.473	0.000	0.000	0.000	0.000
192	A	193	TRP	0	0.122	0.053	18.093	-0.918	-0.918	0.000	0.000	0.000	0.000
193	A	194	THR	0	-0.049	-0.013	18.277	-0.414	-0.414	0.000	0.000	0.000	0.000
194	A	195	VAL	0	-0.020	-0.005	16.647	-0.476	-0.476	0.000	0.000	0.000	0.000
195	A	196	CYS	0	0.002	-0.003	14.103	-1.088	-1.088	0.000	0.000	0.000	0.000
196	A	197	GLY	0	0.046	0.036	13.701	-1.479	-1.479	0.000	0.000	0.000	0.000
197	A	198	ILE	0	-0.012	-0.012	14.801	-0.663	-0.663	0.000	0.000	0.000	0.000
198	A	199	ILE	0	-0.001	0.009	10.343	-0.430	-0.430	0.000	0.000	0.000	0.000
199	A	200	CYS	0	0.012	0.008	10.021	-1.909	-1.909	0.000	0.000	0.000	0.000
200	A	201	TYR	0	0.006	0.004	10.727	-1.256	-1.256	0.000	0.000	0.000	0.000
201	A	202	SER	0	-0.056	-0.032	12.312	-0.223	-0.223	0.000	0.000	0.000	0.000
202	A	203	LEU	0	-0.029	-0.021	6.529	-0.209	-0.209	0.000	0.000	0.000	0.000
203	A	204	SER	0	-0.038	-0.028	8.757	-2.305	-2.305	0.000	0.000	0.000	0.000
204	A	205	PHE	-1	-0.873	-0.896	10.721	-21.300	-21.300	0.000	0.000	0.000	0.000

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