FMO DATABASE

FMODB ID: ZLL3N

Calculation Name: 4DOO-A-Xray547

Preferred Name:

Target Type:

Ligand Name: lauric acid | potassium ion

Ligand 3-letter code: DAO | K

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4DOO

Chain ID: A

ChEMBL ID:

UniProt ID: Q9M1X2

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	203
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2295995.56123
FMO2-HF: Nuclear repulsion	2217284.71592
FMO2-HF: Total energy	-78710.84531
FMO2-MP2: Total energy	-78941.811359

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:3:GLU)

Summations of interaction energy for fragment #1(A:3:GLU)

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.
5.841	8.01	0.015	-0.951	-1.233	-0.001

Interaction energy analysis for fragmet #1(A:3:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.091 / q_NPA : -0.048

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	5	VAL	0	0.059	0.048	3.570	3.949	5.837	0.011	-0.863	-1.036	-0.001
14	A	16	ALA	0	0.086	0.030	3.629	2.363	2.644	0.004	-0.088	-0.197	0.000
4	A	6	VAL	0	-0.016	-0.014	5.430	-0.791	-0.791	0.000	0.000	0.000	0.000
5	A	7	GLU	-1	-0.715	-0.837	8.332	1.040	1.040	0.000	0.000	0.000	0.000
6	A	8	PRO	0	-0.002	0.000	11.343	-0.004	-0.004	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.790	0.875	13.063	-0.225	-0.225	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.106	-0.102	15.497	-0.145	-0.145	0.000	0.000	0.000	0.000
9	A	11	GLY	0	0.015	0.018	12.715	-0.082	-0.082	0.000	0.000	0.000	0.000
10	A	12	PHE	0	-0.056	-0.030	12.096	-0.251	-0.251	0.000	0.000	0.000	0.000
11	A	13	SER	0	0.022	0.012	7.349	-0.395	-0.395	0.000	0.000	0.000	0.000
12	A	14	PHE	0	0.034	0.019	8.381	0.115	0.115	0.000	0.000	0.000	0.000
13	A	15	PRO	0	-0.006	0.013	5.665	-1.837	-1.837	0.000	0.000	0.000	0.000
15	A	17	SER	0	-0.032	-0.003	5.512	3.680	3.680	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.023	-0.015	7.740	-0.545	-0.545	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.029	0.016	10.728	0.622	0.622	0.000	0.000	0.000	0.000
18	A	20	ASP	-1	-0.883	-0.924	9.346	-6.318	-6.318	0.000	0.000	0.000	0.000
19	A	21	SER	0	-0.014	-0.006	10.563	0.037	0.037	0.000	0.000	0.000	0.000
20	A	22	ARG	1	0.917	0.962	12.695	3.245	3.245	0.000	0.000	0.000	0.000
21	A	23	ARG	1	0.938	0.950	8.550	4.228	4.228	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.070	-0.030	7.563	1.041	1.041	0.000	0.000	0.000	0.000
23	A	25	LEU	0	0.000	0.000	9.722	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	26	GLY	0	0.066	0.047	12.408	0.637	0.637	0.000	0.000	0.000	0.000
25	A	27	VAL	0	-0.035	-0.021	9.731	-0.532	-0.532	0.000	0.000	0.000	0.000
26	A	28	GLY	0	0.035	0.028	13.005	0.425	0.425	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.093	-0.045	16.304	-0.173	-0.173	0.000	0.000	0.000	0.000
28	A	30	ARG	1	0.915	0.985	18.981	0.633	0.633	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.950	0.971	21.323	-0.074	-0.074	0.000	0.000	0.000	0.000
30	A	32	LYS	1	0.935	0.972	24.812	0.197	0.197	0.000	0.000	0.000	0.000
31	A	33	SER	0	0.015	0.014	28.561	0.040	0.040	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.042	-0.041	30.804	-0.039	-0.039	0.000	0.000	0.000	0.000
33	A	35	LEU	0	0.042	0.022	33.896	0.017	0.017	0.000	0.000	0.000	0.000
34	A	36	GLY	0	0.016	0.007	36.053	0.016	0.016	0.000	0.000	0.000	0.000
35	A	37	LEU	0	0.057	0.021	32.535	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	38	LYS	1	0.906	0.970	31.257	-0.043	-0.043	0.000	0.000	0.000	0.000
37	A	39	ASN	0	0.026	0.008	27.423	-0.058	-0.058	0.000	0.000	0.000	0.000
38	A	40	ILE	0	-0.019	-0.001	26.322	0.031	0.031	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.757	-0.866	21.127	0.003	0.003	0.000	0.000	0.000	0.000
40	A	42	VAL	0	-0.048	-0.030	23.261	-0.021	-0.021	0.000	0.000	0.000	0.000
41	A	43	TYR	0	0.047	0.011	19.786	-0.018	-0.018	0.000	0.000	0.000	0.000
42	A	44	ALA	0	0.034	0.045	15.187	0.121	0.121	0.000	0.000	0.000	0.000
43	A	45	PHE	0	-0.020	-0.029	16.309	-0.105	-0.105	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.044	0.038	12.971	0.144	0.144	0.000	0.000	0.000	0.000
45	A	47	VAL	0	-0.016	-0.016	13.729	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	48	TYR	0	-0.024	-0.041	9.069	0.430	0.430	0.000	0.000	0.000	0.000
47	A	49	ALA	0	0.022	0.007	14.018	0.457	0.457	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.840	-0.927	14.333	-3.043	-3.043	0.000	0.000	0.000	0.000
49	A	51	CYS	0	0.022	0.007	13.286	0.006	0.006	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.883	-0.930	15.800	-1.915	-1.915	0.000	0.000	0.000	0.000
51	A	53	ASP	-1	-0.814	-0.890	19.190	-1.583	-1.583	0.000	0.000	0.000	0.000
52	A	54	VAL	0	-0.016	-0.007	17.646	0.198	0.198	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.862	0.936	16.120	2.029	2.029	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.831	0.906	20.591	1.048	1.048	0.000	0.000	0.000	0.000
55	A	57	LEU	0	-0.036	-0.009	23.045	0.124	0.124	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.029	-0.001	21.388	0.115	0.115	0.000	0.000	0.000	0.000
57	A	59	GLY	0	-0.003	-0.001	24.247	0.100	0.100	0.000	0.000	0.000	0.000
58	A	60	ASP	-1	-0.889	-0.928	26.134	-0.707	-0.707	0.000	0.000	0.000	0.000
59	A	61	LYS	1	0.803	0.890	28.011	0.599	0.599	0.000	0.000	0.000	0.000
60	A	62	TYR	0	-0.051	-0.045	26.110	0.079	0.079	0.000	0.000	0.000	0.000
61	A	63	ALA	0	0.053	0.035	27.482	0.029	0.029	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.085	-0.058	27.768	0.042	0.042	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.003	0.031	27.334	0.061	0.061	0.000	0.000	0.000	0.000
64	A	66	PRO	0	0.029	0.020	24.153	-0.055	-0.055	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.071	0.029	19.708	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	68	SER	0	0.008	-0.002	21.766	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.930	-0.974	23.746	0.036	0.036	0.000	0.000	0.000	0.000
68	A	70	ILE	0	-0.032	0.002	22.589	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.745	0.842	19.905	-0.055	-0.055	0.000	0.000	0.000	0.000
70	A	72	GLY	0	-0.011	0.001	23.735	0.014	0.014	0.000	0.000	0.000	0.000
71	A	73	ASN	0	-0.084	-0.048	27.211	0.004	0.004	0.000	0.000	0.000	0.000
72	A	74	LYS	1	0.952	0.960	27.831	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	75	SER	0	0.014	0.012	29.402	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	76	PHE	0	0.023	0.026	20.739	-0.065	-0.065	0.000	0.000	0.000	0.000
75	A	77	MET	0	-0.007	-0.004	24.327	-0.083	-0.083	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.872	-0.917	25.408	-0.606	-0.606	0.000	0.000	0.000	0.000
77	A	79	ASP	-1	-0.753	-0.861	26.951	-0.574	-0.574	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.016	-0.011	20.618	-0.097	-0.097	0.000	0.000	0.000	0.000
79	A	81	MET	0	-0.090	-0.029	23.852	-0.102	-0.102	0.000	0.000	0.000	0.000
80	A	82	GLU	-1	-0.962	-0.983	25.604	-0.646	-0.646	0.000	0.000	0.000	0.000
81	A	83	ALA	0	0.053	0.026	25.443	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	84	ASP	-1	-0.897	-0.951	26.070	-1.247	-1.247	0.000	0.000	0.000	0.000
83	A	85	ILE	0	-0.018	-0.005	19.965	-0.070	-0.070	0.000	0.000	0.000	0.000
84	A	86	LYS	1	0.795	0.882	19.108	2.067	2.067	0.000	0.000	0.000	0.000
85	A	87	MET	0	-0.016	-0.015	17.809	-0.157	-0.157	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.015	-0.014	15.388	0.077	0.077	0.000	0.000	0.000	0.000
87	A	89	ILE	0	-0.014	0.019	16.433	-0.142	-0.142	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.853	0.894	12.032	4.227	4.227	0.000	0.000	0.000	0.000
89	A	91	LEU	0	-0.023	-0.018	16.251	0.092	0.092	0.000	0.000	0.000	0.000
90	A	92	GLN	0	-0.002	-0.010	12.272	0.135	0.135	0.000	0.000	0.000	0.000
91	A	93	ILE	0	-0.015	-0.008	18.000	0.230	0.230	0.000	0.000	0.000	0.000
92	A	94	VAL	0	0.012	0.018	18.635	0.023	0.023	0.000	0.000	0.000	0.000
93	A	95	TYR	0	-0.007	-0.011	21.262	0.126	0.126	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.000	-0.008	25.037	-0.054	-0.054	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.901	0.953	26.402	0.195	0.195	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.004	0.024	26.102	0.051	0.051	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.011	-0.013	30.090	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	100	ILE	0	0.077	0.030	31.173	0.011	0.011	0.000	0.000	0.000	0.000
99	A	101	ARG	1	0.972	0.997	33.156	0.372	0.372	0.000	0.000	0.000	0.000
100	A	102	SER	0	-0.019	-0.007	33.334	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.019	0.003	28.697	0.006	0.006	0.000	0.000	0.000	0.000
102	A	104	ARG	1	0.889	0.936	31.469	0.614	0.614	0.000	0.000	0.000	0.000
103	A	105	ASN	0	0.032	0.016	33.747	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	106	ALA	0	0.002	0.008	30.812	0.009	0.009	0.000	0.000	0.000	0.000
105	A	107	PHE	0	0.014	0.016	29.469	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	108	GLN	0	-0.017	-0.015	31.078	0.021	0.021	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.955	-0.972	34.228	-0.321	-0.321	0.000	0.000	0.000	0.000
108	A	110	SER	0	-0.070	-0.059	29.773	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	111	VAL	0	0.054	0.023	29.527	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.043	0.026	32.037	0.006	0.006	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.076	-0.039	33.648	0.009	0.009	0.000	0.000	0.000	0.000
112	A	114	ARG	1	0.781	0.880	28.958	0.496	0.496	0.000	0.000	0.000	0.000
113	A	115	LEU	0	0.040	0.020	33.613	0.010	0.010	0.000	0.000	0.000	0.000
114	A	116	LYS	1	0.950	0.970	35.719	0.309	0.309	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.837	0.930	33.766	0.365	0.365	0.000	0.000	0.000	0.000
116	A	118	PHE	0	-0.007	-0.004	30.877	0.009	0.009	0.000	0.000	0.000	0.000
117	A	119	GLY	0	0.036	0.016	36.253	-0.015	-0.015	0.000	0.000	0.000	0.000
118	A	120	GLY	0	0.003	0.015	38.723	0.029	0.029	0.000	0.000	0.000	0.000
119	A	121	SER	0	-0.082	-0.062	41.586	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.892	-0.942	43.044	-0.362	-0.362	0.000	0.000	0.000	0.000
121	A	123	ASN	0	-0.025	-0.009	38.414	-0.036	-0.036	0.000	0.000	0.000	0.000
122	A	124	ASP	-1	-0.876	-0.937	39.230	-0.436	-0.436	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.899	-0.953	40.092	-0.481	-0.481	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.012	0.008	34.288	-0.040	-0.040	0.000	0.000	0.000	0.000
125	A	127	LEU	0	0.029	0.017	34.295	-0.053	-0.053	0.000	0.000	0.000	0.000
126	A	128	GLN	0	0.005	0.013	35.667	-0.051	-0.051	0.000	0.000	0.000	0.000
127	A	129	SER	0	-0.032	-0.023	35.207	-0.040	-0.040	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.043	0.008	27.607	-0.039	-0.039	0.000	0.000	0.000	0.000
129	A	131	THR	0	-0.031	-0.035	31.888	-0.029	-0.029	0.000	0.000	0.000	0.000
130	A	132	SER	0	-0.056	-0.037	33.890	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	LEU	0	-0.024	0.007	28.624	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	134	PHE	0	0.016	0.014	26.335	-0.046	-0.046	0.000	0.000	0.000	0.000
133	A	135	LYS	1	0.856	0.925	31.395	0.715	0.715	0.000	0.000	0.000	0.000
134	A	136	ASP	-1	-0.856	-0.913	33.241	-0.665	-0.665	0.000	0.000	0.000	0.000
135	A	137	GLU	-1	-0.892	-0.932	28.786	-0.968	-0.968	0.000	0.000	0.000	0.000
136	A	138	TYR	0	-0.015	-0.021	31.979	0.078	0.078	0.000	0.000	0.000	0.000
137	A	139	LYS	1	0.888	0.941	27.608	0.871	0.871	0.000	0.000	0.000	0.000
138	A	140	ILE	0	0.043	0.018	25.095	-0.041	-0.041	0.000	0.000	0.000	0.000
139	A	141	PRO	0	0.012	0.013	24.908	0.062	0.062	0.000	0.000	0.000	0.000
140	A	142	ARG	1	0.923	0.956	18.755	0.377	0.377	0.000	0.000	0.000	0.000
141	A	143	ASN	0	-0.020	-0.023	18.558	0.057	0.057	0.000	0.000	0.000	0.000
142	A	144	SER	0	-0.013	0.003	18.793	-0.163	-0.163	0.000	0.000	0.000	0.000
143	A	145	THR	0	0.003	-0.013	15.790	-0.076	-0.076	0.000	0.000	0.000	0.000
144	A	146	ILE	0	-0.049	-0.027	18.789	0.104	0.104	0.000	0.000	0.000	0.000
145	A	147	ASP	-1	-0.768	-0.829	16.274	-3.322	-3.322	0.000	0.000	0.000	0.000
146	A	148	LEU	0	-0.007	-0.006	19.211	0.203	0.203	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.055	-0.050	18.696	-0.136	-0.136	0.000	0.000	0.000	0.000
148	A	150	LYS	1	0.842	0.942	20.924	1.432	1.432	0.000	0.000	0.000	0.000
149	A	151	ASP	-1	-0.800	-0.883	21.591	-2.011	-2.011	0.000	0.000	0.000	0.000
150	A	152	PRO	0	0.031	-0.002	23.213	0.109	0.109	0.000	0.000	0.000	0.000
151	A	153	GLY	0	-0.023	-0.007	25.994	0.060	0.060	0.000	0.000	0.000	0.000
152	A	154	HIS	0	-0.040	-0.021	27.372	0.052	0.052	0.000	0.000	0.000	0.000
153	A	155	VAL	0	-0.034	-0.015	27.203	0.101	0.101	0.000	0.000	0.000	0.000
154	A	156	LEU	0	0.026	0.020	24.904	-0.097	-0.097	0.000	0.000	0.000	0.000
155	A	157	SER	0	-0.009	-0.018	23.608	0.156	0.156	0.000	0.000	0.000	0.000
156	A	158	VAL	0	-0.024	-0.002	23.557	-0.085	-0.085	0.000	0.000	0.000	0.000
157	A	159	ALA	0	0.021	0.008	20.647	0.040	0.040	0.000	0.000	0.000	0.000
158	A	160	ILE	0	-0.002	0.000	21.776	-0.079	-0.079	0.000	0.000	0.000	0.000
159	A	161	GLU	-1	-0.873	-0.942	20.291	-1.547	-1.547	0.000	0.000	0.000	0.000
160	A	162	GLY	0	-0.024	-0.006	19.349	-0.041	-0.041	0.000	0.000	0.000	0.000
161	A	163	ASN	0	-0.041	-0.014	20.065	-0.014	-0.014	0.000	0.000	0.000	0.000
162	A	164	HIS	0	-0.018	-0.015	23.769	0.025	0.025	0.000	0.000	0.000	0.000
163	A	165	VAL	0	0.001	-0.003	24.930	0.076	0.076	0.000	0.000	0.000	0.000
164	A	166	GLY	0	0.009	0.004	27.461	0.108	0.108	0.000	0.000	0.000	0.000
165	A	167	SER	0	-0.023	-0.034	26.926	-0.090	-0.090	0.000	0.000	0.000	0.000
166	A	168	VAL	0	-0.014	-0.003	29.192	0.081	0.081	0.000	0.000	0.000	0.000
167	A	169	LYS	1	0.913	0.961	30.217	0.868	0.868	0.000	0.000	0.000	0.000
168	A	170	SER	0	0.031	0.010	31.120	0.070	0.070	0.000	0.000	0.000	0.000
169	A	171	HIS	0	0.063	0.046	30.614	-0.018	-0.018	0.000	0.000	0.000	0.000
170	A	172	LEU	0	0.026	0.033	30.865	-0.026	-0.026	0.000	0.000	0.000	0.000
171	A	173	LEU	0	0.028	0.018	29.836	0.014	0.014	0.000	0.000	0.000	0.000
172	A	174	CYS	0	-0.026	-0.011	26.703	-0.051	-0.051	0.000	0.000	0.000	0.000
173	A	175	ARG	1	0.878	0.923	26.879	0.592	0.592	0.000	0.000	0.000	0.000
174	A	176	SER	0	-0.002	-0.025	28.556	0.042	0.042	0.000	0.000	0.000	0.000
175	A	177	ILE	0	-0.024	-0.020	24.568	0.026	0.026	0.000	0.000	0.000	0.000
176	A	178	LEU	0	0.021	0.004	21.669	-0.026	-0.026	0.000	0.000	0.000	0.000
177	A	179	ASP	-1	-0.776	-0.875	24.067	-0.521	-0.521	0.000	0.000	0.000	0.000
178	A	180	LEU	0	-0.034	-0.016	25.573	0.068	0.068	0.000	0.000	0.000	0.000
179	A	181	TYR	0	-0.084	-0.051	20.148	0.013	0.013	0.000	0.000	0.000	0.000
180	A	182	ILE	0	-0.011	-0.010	18.492	0.050	0.050	0.000	0.000	0.000	0.000
181	A	183	GLY	0	0.113	0.066	22.533	0.053	0.053	0.000	0.000	0.000	0.000
182	A	184	GLU	-1	-0.864	-0.933	25.755	-0.143	-0.143	0.000	0.000	0.000	0.000
183	A	185	GLU	-1	-0.951	-0.987	27.978	-0.199	-0.199	0.000	0.000	0.000	0.000
184	A	186	PRO	0	-0.006	0.023	22.916	-0.028	-0.028	0.000	0.000	0.000	0.000
185	A	187	PHE	0	-0.054	-0.056	22.630	0.090	0.090	0.000	0.000	0.000	0.000
186	A	188	ASP	-1	-0.857	-0.935	18.776	-0.051	-0.051	0.000	0.000	0.000	0.000
187	A	189	LYS	1	0.934	0.960	20.700	0.050	0.050	0.000	0.000	0.000	0.000
188	A	190	ASN	0	-0.020	0.008	15.181	0.124	0.124	0.000	0.000	0.000	0.000
189	A	191	ALA	0	0.021	0.007	15.836	-0.015	-0.015	0.000	0.000	0.000	0.000
190	A	192	ARG	1	0.751	0.875	16.822	0.065	0.065	0.000	0.000	0.000	0.000
191	A	193	GLU	-1	-0.818	-0.886	19.086	-0.112	-0.112	0.000	0.000	0.000	0.000
192	A	194	ASP	-1	-0.833	-0.916	13.455	0.423	0.423	0.000	0.000	0.000	0.000
193	A	195	PHE	0	-0.014	-0.023	15.053	-0.195	-0.195	0.000	0.000	0.000	0.000
194	A	196	LEU	0	-0.005	-0.007	16.293	-0.133	-0.133	0.000	0.000	0.000	0.000
195	A	197	ASP	-1	-0.791	-0.879	16.320	0.205	0.205	0.000	0.000	0.000	0.000
196	A	198	ASN	0	-0.033	-0.018	11.783	0.158	0.158	0.000	0.000	0.000	0.000
197	A	199	ALA	0	-0.017	-0.009	14.536	-0.213	-0.213	0.000	0.000	0.000	0.000
198	A	200	ALA	0	-0.031	-0.017	17.077	-0.028	-0.028	0.000	0.000	0.000	0.000
199	A	201	SER	0	-0.047	-0.033	14.579	0.197	0.197	0.000	0.000	0.000	0.000
200	A	202	LEU	0	-0.006	-0.007	12.459	-0.088	-0.088	0.000	0.000	0.000	0.000
201	A	203	ALA	0	-0.050	-0.035	15.146	-0.183	-0.183	0.000	0.000	0.000	0.000
202	A	204	PHE	0	-0.097	-0.054	17.108	0.063	0.063	0.000	0.000	0.000	0.000
203	A	205	ASP	-2	-1.790	-1.865	12.548	-3.149	-3.149	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:GLU)