FMO DATABASE

FMODB ID: ZLZVN

Calculation Name: 4FOP-A-Xray547

Preferred Name:

Target Type:

Ligand Name: acetate ion | glycerol | di(hydroxyethyl)ether

Ligand 3-letter code: ACT | GOL | PEG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4FOP

Chain ID: A

ChEMBL ID:

UniProt ID: D0C9L6

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	193
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2117881.990878
FMO2-HF: Nuclear repulsion	2044585.334216
FMO2-HF: Total energy	-73296.656662
FMO2-MP2: Total energy	-73511.338971

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:1:MET)

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

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.
22.714	30.718	5.022	-4.308	-8.716	-0.027

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.835 / q_NPA : 0.909

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	3	ASN	0	0.002	-0.002	2.927	-11.842	-9.031	0.210	-1.486	-1.535	-0.009
4	A	4	ILE	0	-0.052	-0.014	5.374	1.745	1.838	-0.001	-0.004	-0.087	0.000
89	A	89	ALA	0	-0.015	0.002	4.988	-6.479	-6.452	-0.001	-0.002	-0.023	0.000
108	A	108	THR	0	0.030	-0.002	3.585	-0.618	-0.334	0.008	-0.063	-0.229	0.000
130	A	130	HIS	0	-0.006	-0.012	2.633	2.123	2.715	0.265	-0.138	-0.719	0.001
178	A	178	GLY	0	0.027	0.021	3.489	-2.090	-1.923	0.007	-0.049	-0.126	0.000
179	A	179	GLN	0	-0.040	0.001	2.634	-19.792	-17.788	0.930	-1.326	-1.607	-0.016
180	A	180	VAL	0	0.000	-0.007	2.071	4.723	5.534	3.189	-0.948	-3.053	-0.003
181	A	181	PRO	0	0.035	0.009	3.055	4.312	5.454	0.416	-0.291	-1.267	0.000
184	A	184	MET	0	-0.039	-0.015	4.651	3.112	3.185	-0.001	-0.001	-0.070	0.000
5	A	5	SER	0	0.036	0.010	7.788	1.772	1.772	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.019	0.000	11.129	2.289	2.289	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.008	0.000	11.774	-1.433	-1.433	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.005	-0.009	13.914	1.197	1.197	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.038	0.020	16.253	-0.558	-0.558	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.068	-0.051	17.966	0.498	0.498	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.030	0.001	20.689	0.030	0.030	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.042	-0.013	24.336	-0.161	-0.161	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.033	0.026	27.921	-0.083	-0.083	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.049	0.027	30.163	0.190	0.190	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.016	-0.020	32.394	-0.210	-0.210	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.868	-0.944	34.586	-8.508	-8.508	0.000	0.000	0.000	0.000
17	A	17	TYR	0	0.008	-0.004	30.165	-0.069	-0.069	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.012	0.027	29.316	-0.255	-0.255	0.000	0.000	0.000	0.000
19	A	19	GLN	0	0.041	0.027	29.081	-0.159	-0.159	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.068	-0.035	29.641	0.030	0.030	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.881	0.925	26.285	9.091	9.091	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.074	-0.074	24.545	-0.313	-0.313	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.018	0.007	23.966	-0.347	-0.347	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.041	0.029	21.606	-0.252	-0.252	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.032	-0.023	19.071	-0.530	-0.530	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.030	-0.018	19.988	-0.520	-0.520	0.000	0.000	0.000	0.000
27	A	27	TRP	0	0.030	0.020	22.409	-0.393	-0.393	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.033	0.009	14.152	-0.376	-0.376	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.011	-0.009	17.067	-0.439	-0.439	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.922	-0.971	19.503	-11.481	-11.481	0.000	0.000	0.000	0.000
31	A	31	GLN	0	0.025	0.006	21.872	0.259	0.259	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.043	-0.023	15.267	-0.248	-0.248	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.035	-0.028	19.633	-0.246	-0.246	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.920	-0.948	21.694	-11.217	-11.217	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.904	0.968	18.461	15.176	15.176	0.000	0.000	0.000	0.000
36	A	36	TYR	0	-0.101	-0.091	17.147	-0.435	-0.435	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.029	0.029	21.386	-0.028	-0.028	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.089	-0.035	18.601	0.183	0.183	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.024	-0.026	22.966	0.167	0.167	0.000	0.000	0.000	0.000
40	A	40	LEU	0	0.008	0.008	21.882	-0.276	-0.276	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.939	0.965	25.657	11.985	11.985	0.000	0.000	0.000	0.000
42	A	42	ASN	0	0.027	0.008	27.305	-0.454	-0.454	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.812	-0.890	24.810	-12.093	-12.093	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.030	0.008	27.724	-0.181	-0.181	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.895	0.968	26.209	11.522	11.522	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.053	-0.026	23.574	-0.195	-0.195	0.000	0.000	0.000	0.000
47	A	47	HIS	0	0.012	0.018	25.042	-0.252	-0.252	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.063	0.022	25.112	-0.096	-0.096	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.005	0.014	25.106	0.407	0.407	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.060	-0.056	22.116	-0.534	-0.534	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.063	0.029	21.487	0.644	0.644	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.763	0.850	18.819	15.013	15.013	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.056	0.035	18.586	0.910	0.910	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.018	-0.004	17.195	-1.207	-1.207	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.067	0.034	14.130	0.560	0.560	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.822	-0.884	13.236	-19.661	-19.661	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.014	0.016	13.824	-1.170	-1.170	0.000	0.000	0.000	0.000
58	A	58	HIS	0	-0.022	-0.010	10.383	-1.002	-1.002	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.825	-0.884	13.477	-16.113	-16.113	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.025	-0.011	12.130	-1.573	-1.573	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.910	0.956	14.688	17.947	17.947	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.030	0.020	15.811	-1.007	-1.007	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.040	-0.024	18.286	0.564	0.564	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.058	0.044	19.646	-0.478	-0.478	0.000	0.000	0.000	0.000
65	A	65	PRO	0	-0.009	-0.006	21.103	0.432	0.432	0.000	0.000	0.000	0.000
66	A	66	MET	0	-0.016	0.003	24.118	0.399	0.399	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.030	-0.027	25.545	0.290	0.290	0.000	0.000	0.000	0.000
68	A	68	TYR	0	0.006	0.002	28.060	0.292	0.292	0.000	0.000	0.000	0.000
69	A	69	MET	0	0.053	0.067	22.541	-0.498	-0.498	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.050	-0.038	24.070	-0.639	-0.639	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.944	0.992	25.769	9.565	9.565	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.036	0.006	20.883	-0.140	-0.140	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.003	0.006	20.619	-0.520	-0.520	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.027	-0.036	21.649	-0.087	-0.087	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.033	-0.008	22.811	0.051	0.051	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.034	-0.008	16.536	-0.334	-0.334	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.017	0.020	18.500	-0.791	-0.791	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.015	-0.001	19.852	-0.357	-0.357	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.055	0.021	17.832	-0.253	-0.253	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.040	-0.045	15.171	-0.349	-0.349	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.914	0.959	16.764	14.105	14.105	0.000	0.000	0.000	0.000
82	A	82	PHE	0	-0.010	-0.001	18.825	0.164	0.164	0.000	0.000	0.000	0.000
83	A	83	TYR	0	-0.045	-0.034	17.812	0.332	0.332	0.000	0.000	0.000	0.000
84	A	84	GLN	0	-0.024	-0.004	16.601	-1.074	-1.074	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.018	0.004	11.480	-1.139	-1.139	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.054	0.021	9.670	0.953	0.953	0.000	0.000	0.000	0.000
87	A	87	PRO	0	0.042	0.010	9.492	-1.391	-1.391	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.843	-0.925	4.862	-29.541	-29.541	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.022	-0.007	7.461	2.105	2.105	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.027	-0.013	8.899	-1.484	-1.484	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.016	-0.008	10.550	1.473	1.473	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.002	0.011	13.508	-0.177	-0.177	0.000	0.000	0.000	0.000
94	A	94	HIS	1	0.855	0.911	14.878	15.919	15.919	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.689	-0.801	17.940	-12.540	-12.540	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.830	-0.902	17.172	-14.598	-14.598	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.039	0.016	20.138	0.314	0.314	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.938	-0.959	19.914	-11.806	-11.806	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.071	-0.032	15.249	-0.515	-0.515	0.000	0.000	0.000	0.000
100	A	100	ASN	0	0.030	0.018	21.241	0.208	0.208	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.040	0.018	22.762	-0.471	-0.471	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.023	0.032	22.997	0.284	0.284	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.049	-0.025	18.491	-0.336	-0.336	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.021	0.005	14.988	-0.071	-0.071	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.867	0.936	12.475	15.605	15.605	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.034	0.034	6.116	0.105	0.105	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.867	0.917	8.120	19.264	19.264	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.039	0.037	6.419	1.285	1.285	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.001	0.001	8.830	1.224	1.224	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.038	0.014	12.409	-0.070	-0.070	0.000	0.000	0.000	0.000
112	A	112	HIS	0	0.066	0.036	15.005	-0.793	-0.793	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.020	0.017	17.477	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	114	GLY	0	-0.014	-0.005	18.990	0.385	0.385	0.000	0.000	0.000	0.000
115	A	115	HIS	0	-0.010	-0.021	19.237	0.166	0.166	0.000	0.000	0.000	0.000
116	A	116	ASN	0	0.046	0.002	20.924	-0.447	-0.447	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.064	0.046	21.112	0.143	0.143	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.009	-0.013	14.997	-0.366	-0.366	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.835	0.901	18.112	10.804	10.804	0.000	0.000	0.000	0.000
120	A	120	ASP	-1	-0.840	-0.909	20.731	-11.856	-11.856	0.000	0.000	0.000	0.000
121	A	121	ILE	0	0.010	0.003	15.403	-0.152	-0.152	0.000	0.000	0.000	0.000
122	A	122	VAL	0	-0.025	-0.020	14.392	-0.350	-0.350	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.041	-0.018	16.336	-0.380	-0.380	0.000	0.000	0.000	0.000
124	A	124	HIS	0	-0.007	0.010	18.565	-0.036	-0.036	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.034	-0.020	13.203	0.094	0.094	0.000	0.000	0.000	0.000
126	A	126	GLY	0	0.059	0.051	13.506	-1.140	-1.140	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.002	-0.021	11.301	-0.190	-0.190	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.044	-0.015	7.132	0.752	0.752	0.000	0.000	0.000	0.000
129	A	129	PHE	0	0.053	0.046	6.721	-2.482	-2.482	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.780	0.870	7.773	21.960	21.960	0.000	0.000	0.000	0.000
132	A	132	LEU	0	0.020	0.016	10.464	-0.763	-0.763	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.773	0.853	12.650	16.326	16.326	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.068	0.023	15.179	-0.147	-0.147	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.005	0.000	18.217	0.402	0.402	0.000	0.000	0.000	0.000
136	A	136	ILE	0	-0.003	-0.008	20.816	0.285	0.285	0.000	0.000	0.000	0.000
137	A	137	GLY	0	0.023	0.023	23.919	0.502	0.502	0.000	0.000	0.000	0.000
138	A	138	HIS	0	0.045	0.013	25.831	0.142	0.142	0.000	0.000	0.000	0.000
139	A	139	PRO	0	-0.020	0.008	27.762	0.174	0.174	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.040	0.020	30.763	0.324	0.324	0.000	0.000	0.000	0.000
141	A	141	SER	0	-0.043	-0.050	32.525	0.200	0.200	0.000	0.000	0.000	0.000
142	A	142	LYS	1	0.956	0.971	30.986	8.011	8.011	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.834	-0.903	32.479	-8.114	-8.114	0.000	0.000	0.000	0.000
144	A	144	ARG	1	0.901	0.943	34.261	7.907	7.907	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.011	0.013	27.975	-0.097	-0.097	0.000	0.000	0.000	0.000
146	A	146	SER	0	-0.002	0.001	30.202	-0.228	-0.228	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.051	0.015	31.915	-0.084	-0.084	0.000	0.000	0.000	0.000
148	A	148	HIS	0	-0.039	-0.018	27.710	0.319	0.319	0.000	0.000	0.000	0.000
149	A	149	VAL	0	0.005	-0.007	26.165	-0.120	-0.120	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.015	-0.007	28.532	-0.182	-0.182	0.000	0.000	0.000	0.000
151	A	151	GLY	0	0.049	0.043	31.293	0.264	0.264	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.894	0.940	30.971	8.235	8.235	0.000	0.000	0.000	0.000
153	A	153	ALA	0	0.001	0.007	29.398	0.152	0.152	0.000	0.000	0.000	0.000
154	A	154	PRO	0	-0.013	0.008	31.538	0.149	0.149	0.000	0.000	0.000	0.000
155	A	155	SER	0	0.062	0.004	32.161	-0.263	-0.263	0.000	0.000	0.000	0.000
156	A	156	ASN	0	0.024	0.029	32.012	-0.112	-0.112	0.000	0.000	0.000	0.000
157	A	157	GLU	-1	-0.817	-0.910	28.800	-9.501	-9.501	0.000	0.000	0.000	0.000
158	A	158	GLN	0	-0.055	-0.053	27.050	-0.155	-0.155	0.000	0.000	0.000	0.000
159	A	159	SER	0	0.048	0.010	27.216	-0.309	-0.309	0.000	0.000	0.000	0.000
160	A	160	LEU	0	-0.051	-0.017	25.844	-0.313	-0.313	0.000	0.000	0.000	0.000
161	A	161	MET	0	-0.068	-0.027	23.075	-0.554	-0.554	0.000	0.000	0.000	0.000
162	A	162	ASP	-1	-0.812	-0.893	22.483	-11.328	-11.328	0.000	0.000	0.000	0.000
163	A	163	GLY	0	0.060	0.032	23.136	-0.451	-0.451	0.000	0.000	0.000	0.000
164	A	164	ALA	0	-0.027	-0.015	19.534	-0.545	-0.545	0.000	0.000	0.000	0.000
165	A	165	ILE	0	-0.041	-0.019	18.532	-1.117	-1.117	0.000	0.000	0.000	0.000
166	A	166	ASP	-1	-0.837	-0.927	18.785	-13.322	-13.322	0.000	0.000	0.000	0.000
167	A	167	HIS	0	-0.058	-0.029	15.828	-0.228	-0.228	0.000	0.000	0.000	0.000
168	A	168	ALA	0	0.000	0.005	14.590	-1.006	-1.006	0.000	0.000	0.000	0.000
169	A	169	LEU	0	-0.030	-0.010	14.587	-1.425	-1.425	0.000	0.000	0.000	0.000
170	A	170	SER	0	-0.090	-0.050	16.732	-0.439	-0.439	0.000	0.000	0.000	0.000
171	A	171	LYS	1	0.855	0.918	11.856	17.428	17.428	0.000	0.000	0.000	0.000
172	A	172	VAL	0	0.028	0.012	11.125	-2.428	-2.428	0.000	0.000	0.000	0.000
173	A	173	LYS	1	0.911	0.952	10.795	18.672	18.672	0.000	0.000	0.000	0.000
174	A	174	LEU	0	-0.015	-0.010	8.578	-1.774	-1.774	0.000	0.000	0.000	0.000
175	A	175	LEU	0	-0.012	-0.002	6.313	-4.837	-4.837	0.000	0.000	0.000	0.000
176	A	176	VAL	0	0.027	0.013	6.323	-4.680	-4.680	0.000	0.000	0.000	0.000
177	A	177	GLN	0	-0.037	-0.011	7.813	-0.766	-0.766	0.000	0.000	0.000	0.000
182	A	182	GLN	0	0.047	0.022	5.654	1.637	1.637	0.000	0.000	0.000	0.000
183	A	183	ALA	0	0.031	0.011	7.061	3.198	3.198	0.000	0.000	0.000	0.000
185	A	185	ASN	0	-0.015	-0.011	8.085	2.420	2.420	0.000	0.000	0.000	0.000
186	A	186	GLN	0	0.041	0.019	10.969	2.460	2.460	0.000	0.000	0.000	0.000
187	A	187	ILE	0	-0.002	0.016	10.077	1.369	1.369	0.000	0.000	0.000	0.000
188	A	188	ASN	0	-0.005	-0.021	9.985	1.581	1.581	0.000	0.000	0.000	0.000
189	A	189	ALA	0	-0.027	-0.011	13.493	0.915	0.915	0.000	0.000	0.000	0.000
190	A	190	TYR	0	-0.030	-0.003	16.236	0.684	0.684	0.000	0.000	0.000	0.000
191	A	191	LYS	1	0.918	0.946	18.273	12.346	12.346	0.000	0.000	0.000	0.000
192	A	192	PRO	0	-0.042	-0.018	21.920	-0.127	-0.127	0.000	0.000	0.000	0.000
193	A	193	ALA	-1	-0.901	-0.924	24.696	-10.346	-10.346	0.000	0.000	0.000	0.000

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