FMO DATABASE

FMODB ID: Z7MQN

Calculation Name: 2L2E-A-Other547

Preferred Name:

Target Type:

Ligand Name: myristic acid

Ligand 3-letter code: MYR

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2L2E

Chain ID: A

ChEMBL ID:

UniProt ID: Q09711

Base Structure: SolutionNMR

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	-2104425.885528
FMO2-HF: Nuclear repulsion	2027086.18741
FMO2-HF: Total energy	-77339.698118
FMO2-MP2: Total energy	-77563.043829

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:GLY)

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

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.
-143.274	-139.256	4.327	-4.27	-4.074	-0.03

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.915 / q_NPA : 0.946

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	SER	0	0.000	-0.005	3.862	4.988	7.374	-0.023	-1.235	-1.129	-0.006
5	A	6	SER	0	0.019	0.020	4.559	-8.457	-8.297	-0.001	-0.015	-0.144	0.000
135	A	136	VAL	0	-0.027	-0.020	2.382	-5.723	-6.123	3.934	-2.033	-1.501	-0.015
137	A	138	LEU	0	0.032	0.012	3.352	-21.996	-20.843	0.033	-0.610	-0.576	-0.005
138	A	139	PRO	0	-0.083	-0.048	2.491	-0.890	-0.257	0.385	-0.362	-0.655	-0.004
139	A	140	GLU	-1	-0.913	-0.956	4.647	-24.569	-24.483	-0.001	-0.015	-0.069	0.000
4	A	5	GLN	0	0.076	0.042	5.397	3.837	3.837	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.903	0.941	6.269	38.985	38.985	0.000	0.000	0.000	0.000
7	A	8	LEU	0	0.053	0.032	8.153	1.075	1.075	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.034	-0.026	11.521	0.021	0.021	0.000	0.000	0.000	0.000
9	A	10	GLN	0	0.024	0.001	14.326	-0.225	-0.225	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.840	-0.901	15.386	-15.716	-15.716	0.000	0.000	0.000	0.000
11	A	12	GLN	0	-0.004	-0.012	15.201	-0.660	-0.660	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.012	0.004	10.291	-0.616	-0.616	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.024	0.011	14.129	0.733	0.733	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.959	-0.975	17.281	-14.696	-14.696	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.029	0.018	13.643	0.494	0.494	0.000	0.000	0.000	0.000
16	A	17	VAL	0	0.019	0.004	14.472	0.467	0.467	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.859	0.928	16.966	13.907	13.907	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.030	0.016	19.657	0.922	0.922	0.000	0.000	0.000	0.000
19	A	20	THR	0	-0.037	-0.010	17.480	0.292	0.292	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.934	0.982	20.326	13.444	13.444	0.000	0.000	0.000	0.000
21	A	22	PHE	0	-0.011	-0.015	21.855	0.520	0.520	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.908	-0.939	24.303	-11.567	-11.567	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.871	0.935	22.665	12.977	12.977	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.985	0.967	25.401	10.811	10.811	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.932	-0.946	28.482	-9.676	-9.676	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.043	0.017	24.378	0.226	0.226	0.000	0.000	0.000	0.000
27	A	28	GLN	0	-0.011	-0.009	27.043	0.168	0.168	0.000	0.000	0.000	0.000
28	A	29	GLN	0	-0.039	-0.016	28.262	0.359	0.359	0.000	0.000	0.000	0.000
29	A	30	TRP	0	0.046	0.016	29.696	0.124	0.124	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.035	-0.027	25.903	0.195	0.195	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.984	0.992	29.589	9.590	9.590	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.003	0.000	31.703	0.247	0.247	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.005	0.001	31.451	0.186	0.186	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.004	-0.017	27.194	0.009	0.009	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.926	0.982	32.238	8.229	8.229	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.943	-0.978	35.497	-7.954	-7.954	0.000	0.000	0.000	0.000
37	A	38	CYS	0	-0.083	-0.042	35.201	0.273	0.273	0.000	0.000	0.000	0.000
38	A	39	PRO	0	0.000	0.014	32.929	-0.339	-0.339	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.004	0.004	31.500	0.129	0.129	0.000	0.000	0.000	0.000
40	A	41	GLY	0	-0.020	-0.004	27.698	-0.125	-0.125	0.000	0.000	0.000	0.000
41	A	42	HIS	1	0.856	0.908	25.682	11.333	11.333	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.012	0.002	26.212	0.382	0.382	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.034	0.016	27.288	-0.398	-0.398	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.941	0.991	25.759	11.642	11.642	0.000	0.000	0.000	0.000
45	A	46	SER	0	-0.001	-0.023	28.180	-0.128	-0.128	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.902	-0.947	30.930	-9.547	-9.547	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.053	0.019	23.116	0.131	0.131	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.005	-0.007	28.174	-0.190	-0.190	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.914	0.962	29.372	8.657	8.657	0.000	0.000	0.000	0.000
50	A	51	ILE	0	0.022	0.013	28.645	0.205	0.205	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.023	-0.015	23.393	0.342	0.342	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.931	0.953	28.393	8.983	8.983	0.000	0.000	0.000	0.000
53	A	54	GLN	0	-0.080	-0.026	31.815	0.479	0.479	0.000	0.000	0.000	0.000
54	A	55	PHE	0	0.004	-0.002	29.335	0.174	0.174	0.000	0.000	0.000	0.000
55	A	56	PHE	0	-0.009	-0.002	23.416	0.119	0.119	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.010	0.007	28.049	-0.378	-0.378	0.000	0.000	0.000	0.000
57	A	58	PHE	0	-0.046	-0.018	26.916	0.288	0.288	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.033	0.021	26.590	0.186	0.186	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.902	-0.953	27.049	-10.715	-10.715	0.000	0.000	0.000	0.000
60	A	61	PRO	0	-0.007	-0.013	26.303	-0.415	-0.415	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.040	-0.023	26.621	-0.265	-0.265	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.096	0.052	24.266	-0.240	-0.240	0.000	0.000	0.000	0.000
63	A	64	PHE	0	0.030	0.014	18.408	-0.535	-0.535	0.000	0.000	0.000	0.000
64	A	65	ALA	0	0.005	-0.005	21.637	-0.505	-0.505	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.951	-0.987	23.164	-12.069	-12.069	0.000	0.000	0.000	0.000
66	A	67	TYR	0	-0.005	0.013	14.305	-0.675	-0.675	0.000	0.000	0.000	0.000
67	A	68	VAL	0	-0.009	-0.013	18.305	-0.764	-0.764	0.000	0.000	0.000	0.000
68	A	69	PHE	0	-0.009	-0.008	19.262	-0.294	-0.294	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.021	0.008	17.791	0.267	0.267	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.040	0.008	13.681	-0.803	-0.803	0.000	0.000	0.000	0.000
71	A	72	PHE	0	-0.070	-0.079	15.536	-0.484	-0.484	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.878	-0.940	18.634	-12.418	-12.418	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.004	-0.001	18.863	0.222	0.222	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.945	-0.971	20.987	-11.829	-11.829	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.890	0.947	20.726	14.786	14.786	0.000	0.000	0.000	0.000
76	A	77	ASN	0	-0.009	-0.010	25.081	0.028	0.028	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.039	0.022	27.229	0.315	0.315	0.000	0.000	0.000	0.000
78	A	79	TYR	0	-0.088	-0.031	25.649	0.178	0.178	0.000	0.000	0.000	0.000
79	A	80	ILE	0	0.044	0.025	21.881	-0.501	-0.501	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.845	-0.922	21.913	-12.213	-12.213	0.000	0.000	0.000	0.000
81	A	82	PHE	0	-0.008	-0.007	21.606	-0.650	-0.650	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.987	1.001	22.400	11.771	11.771	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.760	-0.874	18.014	-16.528	-16.528	0.000	0.000	0.000	0.000
84	A	85	PHE	0	-0.005	0.001	17.645	-0.988	-0.988	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.006	0.002	18.165	-0.705	-0.705	0.000	0.000	0.000	0.000
86	A	87	CYS	0	-0.032	-0.005	16.909	-0.181	-0.181	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.025	0.012	13.897	-0.948	-0.948	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.003	0.007	14.288	-1.040	-1.040	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.024	-0.024	15.702	0.446	0.446	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.071	-0.030	9.966	-0.565	-0.565	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.009	0.005	13.043	-0.743	-0.743	0.000	0.000	0.000	0.000
92	A	93	SER	0	0.053	0.031	15.258	1.487	1.487	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.983	0.983	17.781	12.478	12.478	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.030	-0.010	19.786	0.975	0.975	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.883	-0.931	19.817	-13.730	-13.730	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.016	-0.003	15.564	-0.156	-0.156	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.010	-0.010	18.735	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.842	-0.929	21.909	-13.053	-13.053	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.875	0.938	12.991	22.730	22.730	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.006	-0.001	17.351	-0.238	-0.238	0.000	0.000	0.000	0.000
101	A	102	ILE	0	0.037	0.013	20.303	0.305	0.305	0.000	0.000	0.000	0.000
102	A	103	TRP	0	-0.050	-0.012	19.940	0.743	0.743	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.009	-0.009	18.757	0.303	0.303	0.000	0.000	0.000	0.000
104	A	105	PHE	0	0.009	0.019	20.816	0.169	0.169	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.009	-0.026	23.785	0.260	0.260	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.092	-0.023	20.482	0.456	0.456	0.000	0.000	0.000	0.000
107	A	108	TYR	0	0.021	-0.018	20.338	0.208	0.208	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.848	-0.901	25.244	-10.139	-10.139	0.000	0.000	0.000	0.000
109	A	110	LEU	0	-0.093	-0.061	27.872	0.383	0.383	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.945	-0.965	29.648	-10.342	-10.342	0.000	0.000	0.000	0.000
111	A	112	ASN	0	-0.130	-0.059	32.288	0.304	0.304	0.000	0.000	0.000	0.000
112	A	113	ASN	0	0.025	0.007	32.067	0.533	0.533	0.000	0.000	0.000	0.000
113	A	114	GLY	0	-0.010	0.009	30.896	0.139	0.139	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.065	-0.047	29.410	-0.142	-0.142	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.012	0.023	22.762	0.078	0.078	0.000	0.000	0.000	0.000
116	A	117	SER	0	0.021	-0.005	26.406	0.252	0.252	0.000	0.000	0.000	0.000
117	A	118	TYR	0	-0.033	-0.027	20.981	-0.676	-0.676	0.000	0.000	0.000	0.000
118	A	119	ASP	-1	-0.886	-0.960	21.998	-13.086	-13.086	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.781	-0.908	21.586	-15.324	-15.324	0.000	0.000	0.000	0.000
120	A	121	MET	0	-0.007	0.020	16.441	-0.948	-0.948	0.000	0.000	0.000	0.000
121	A	122	LEU	0	0.005	-0.008	15.996	-1.259	-1.259	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.866	0.928	16.606	13.982	13.982	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.008	0.004	16.484	-0.916	-0.916	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.052	-0.034	12.579	-1.236	-1.236	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.943	-0.955	12.250	-23.180	-23.180	0.000	0.000	0.000	0.000
126	A	127	ALA	0	0.034	0.018	13.064	-1.212	-1.212	0.000	0.000	0.000	0.000
127	A	128	ILE	0	-0.050	-0.025	9.882	-0.795	-0.795	0.000	0.000	0.000	0.000
128	A	129	TYR	0	-0.017	-0.015	7.723	-2.841	-2.841	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.885	0.944	8.885	17.376	17.376	0.000	0.000	0.000	0.000
130	A	131	MET	0	0.016	0.014	11.114	0.607	0.607	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.015	-0.005	4.875	-1.801	-1.801	0.000	0.000	0.000	0.000
132	A	133	GLY	0	0.014	0.009	6.579	-3.344	-3.344	0.000	0.000	0.000	0.000
133	A	134	SER	0	-0.032	-0.013	7.988	2.406	2.406	0.000	0.000	0.000	0.000
134	A	135	MET	0	-0.067	-0.019	7.693	2.424	2.424	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.938	0.971	4.938	33.692	33.692	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.901	-0.945	7.549	-28.402	-28.402	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.941	-0.966	5.829	-43.337	-43.337	0.000	0.000	0.000	0.000
142	A	143	ASP	-1	-0.880	-0.933	8.924	-28.860	-28.860	0.000	0.000	0.000	0.000
143	A	144	THR	0	-0.048	-0.020	11.106	1.857	1.857	0.000	0.000	0.000	0.000
144	A	145	PRO	0	0.048	0.018	10.539	0.796	0.796	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.796	-0.887	12.502	-15.294	-15.294	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.949	0.970	15.134	20.296	20.296	0.000	0.000	0.000	0.000
147	A	148	ARG	1	0.767	0.864	6.978	35.525	35.525	0.000	0.000	0.000	0.000
148	A	149	VAL	0	0.047	0.027	14.698	0.754	0.754	0.000	0.000	0.000	0.000
149	A	150	ASN	0	-0.020	-0.016	16.911	1.184	1.184	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.883	0.937	15.292	19.896	19.896	0.000	0.000	0.000	0.000
151	A	152	ILE	0	-0.011	0.002	15.966	0.561	0.561	0.000	0.000	0.000	0.000
152	A	153	PHE	0	0.045	0.011	19.619	0.855	0.855	0.000	0.000	0.000	0.000
153	A	154	ASN	0	-0.067	-0.023	22.294	0.467	0.467	0.000	0.000	0.000	0.000
154	A	155	MET	0	-0.031	-0.009	18.925	0.552	0.552	0.000	0.000	0.000	0.000
155	A	156	MET	0	-0.067	-0.030	23.173	0.294	0.294	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.958	-0.960	25.586	-10.178	-10.178	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.851	0.949	24.977	12.371	12.371	0.000	0.000	0.000	0.000
158	A	159	ASN	0	-0.027	-0.025	28.257	0.152	0.152	0.000	0.000	0.000	0.000
159	A	160	LYS	1	0.898	0.943	26.154	11.417	11.417	0.000	0.000	0.000	0.000
160	A	161	ASP	-1	-0.869	-0.936	25.864	-11.699	-11.699	0.000	0.000	0.000	0.000
161	A	162	GLY	0	-0.044	-0.020	28.188	0.043	0.043	0.000	0.000	0.000	0.000
162	A	163	GLN	0	0.025	0.000	27.875	-0.279	-0.279	0.000	0.000	0.000	0.000
163	A	164	LEU	0	-0.040	-0.012	23.618	0.038	0.038	0.000	0.000	0.000	0.000
164	A	165	THR	0	0.078	0.042	27.429	-0.130	-0.130	0.000	0.000	0.000	0.000
165	A	166	LEU	0	0.016	0.012	24.473	-0.516	-0.516	0.000	0.000	0.000	0.000
166	A	167	GLU	-1	-0.858	-0.940	24.916	-11.557	-11.557	0.000	0.000	0.000	0.000
167	A	168	GLU	-1	-0.889	-0.953	25.644	-11.497	-11.497	0.000	0.000	0.000	0.000
168	A	169	PHE	0	-0.033	-0.007	18.143	-0.587	-0.587	0.000	0.000	0.000	0.000
169	A	170	CYS	0	-0.053	-0.018	20.994	-0.897	-0.897	0.000	0.000	0.000	0.000
170	A	171	GLU	-1	-0.805	-0.880	21.261	-13.326	-13.326	0.000	0.000	0.000	0.000
171	A	172	GLY	0	0.042	0.003	21.417	-0.306	-0.306	0.000	0.000	0.000	0.000
172	A	173	SER	0	-0.088	-0.060	16.850	-0.850	-0.850	0.000	0.000	0.000	0.000
173	A	174	LYS	1	0.806	0.886	17.353	11.967	11.967	0.000	0.000	0.000	0.000
174	A	175	ARG	1	0.912	0.952	19.828	12.819	12.819	0.000	0.000	0.000	0.000
175	A	176	ASP	-1	-0.786	-0.883	15.149	-19.466	-19.466	0.000	0.000	0.000	0.000
176	A	177	PRO	0	0.015	-0.003	14.977	-1.226	-1.226	0.000	0.000	0.000	0.000
177	A	178	THR	0	-0.032	0.004	9.454	-1.492	-1.492	0.000	0.000	0.000	0.000
178	A	179	ILE	0	0.048	0.021	10.422	-2.426	-2.426	0.000	0.000	0.000	0.000
179	A	180	VAL	0	-0.003	0.004	12.293	-0.505	-0.505	0.000	0.000	0.000	0.000
180	A	181	SER	0	-0.065	-0.050	10.115	-0.890	-0.890	0.000	0.000	0.000	0.000
181	A	182	ALA	0	-0.006	-0.009	7.737	-1.876	-1.876	0.000	0.000	0.000	0.000
182	A	183	LEU	0	-0.010	-0.002	8.148	-2.103	-2.103	0.000	0.000	0.000	0.000
183	A	184	SER	0	0.030	0.023	10.272	-0.332	-0.332	0.000	0.000	0.000	0.000
184	A	185	LEU	0	-0.073	-0.044	5.249	-0.043	-0.043	0.000	0.000	0.000	0.000
185	A	186	TYR	0	-0.020	-0.018	7.062	-2.787	-2.787	0.000	0.000	0.000	0.000
186	A	187	ASP	-1	-0.889	-0.940	9.405	-19.959	-19.959	0.000	0.000	0.000	0.000
187	A	188	GLY	0	-0.049	-0.039	12.863	1.096	1.096	0.000	0.000	0.000	0.000
188	A	189	LEU	0	-0.112	-0.049	9.458	0.034	0.034	0.000	0.000	0.000	0.000
189	A	190	VAL	-1	-0.927	-0.941	14.179	-16.505	-16.505	0.000	0.000	0.000	0.000

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