FMO DATABASE

FMODB ID: 8GL6Y

Calculation Name: 1ZR3-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-(n-morpholino)-ethanesulfonic acid

Ligand 3-letter code: MES

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ZR3

Chain ID: A

ChEMBL ID:

UniProt ID: O75367

Base Structure: X-ray

Registration Date: 2025-10-03

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	186
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1966337.63876
FMO2-HF: Nuclear repulsion	1896900.096766
FMO2-HF: Total energy	-69437.541994
FMO2-MP2: Total energy	-69641.477237

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:182:GLY)

Summations of interaction energy for fragment #1(A:182: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.
-91.126	-86.228	2.214	-3.717	-3.395	-0.041

Interaction energy analysis for fragmet #1(A:182:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.851 / q_NPA : 0.920

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	184	THR	0	0.034	0.017	3.857	3.165	3.974	-0.013	-0.341	-0.455	0.000
26	A	207	ILE	0	-0.014	-0.004	3.986	-13.801	-13.658	-0.001	-0.063	-0.079	0.000
27	A	208	ASP	-1	-0.862	-0.938	2.465	-98.790	-94.882	2.229	-3.313	-2.825	-0.041
28	A	209	SER	0	-0.079	-0.044	5.247	4.000	4.038	-0.001	0.000	-0.036	0.000
4	A	185	VAL	0	-0.048	-0.019	7.006	0.870	0.870	0.000	0.000	0.000	0.000
5	A	186	LEU	0	-0.006	-0.007	9.454	1.357	1.357	0.000	0.000	0.000	0.000
6	A	187	SER	0	0.013	0.004	12.903	1.803	1.803	0.000	0.000	0.000	0.000
7	A	188	THR	0	-0.014	-0.017	13.643	-2.210	-2.210	0.000	0.000	0.000	0.000
8	A	189	LYS	1	0.838	0.927	15.753	14.078	14.078	0.000	0.000	0.000	0.000
9	A	190	SER	0	-0.029	-0.026	18.415	-1.039	-1.039	0.000	0.000	0.000	0.000
10	A	191	LEU	0	0.041	0.034	19.600	0.588	0.588	0.000	0.000	0.000	0.000
11	A	192	PHE	0	0.013	-0.002	22.516	-0.165	-0.165	0.000	0.000	0.000	0.000
12	A	193	LEU	0	-0.044	-0.008	24.403	0.255	0.255	0.000	0.000	0.000	0.000
13	A	194	GLY	0	-0.022	-0.008	21.378	-0.167	-0.167	0.000	0.000	0.000	0.000
14	A	195	GLN	0	-0.024	-0.008	18.045	-0.676	-0.676	0.000	0.000	0.000	0.000
15	A	196	LYS	1	0.909	0.958	11.835	22.813	22.813	0.000	0.000	0.000	0.000
16	A	197	LEU	0	0.032	0.029	15.442	-0.608	-0.608	0.000	0.000	0.000	0.000
17	A	198	GLN	0	-0.001	-0.037	10.582	-1.687	-1.687	0.000	0.000	0.000	0.000
18	A	199	VAL	0	0.019	0.020	12.875	-0.693	-0.693	0.000	0.000	0.000	0.000
19	A	200	VAL	0	0.009	-0.006	7.319	-1.184	-1.184	0.000	0.000	0.000	0.000
20	A	201	GLN	0	-0.021	-0.014	10.662	1.391	1.391	0.000	0.000	0.000	0.000
21	A	202	ALA	0	-0.006	-0.010	7.371	-2.143	-2.143	0.000	0.000	0.000	0.000
22	A	203	ASP	-1	-0.762	-0.853	8.844	-27.135	-27.135	0.000	0.000	0.000	0.000
23	A	204	ILE	0	0.027	0.026	8.217	-4.786	-4.786	0.000	0.000	0.000	0.000
24	A	205	ALA	0	0.016	0.015	9.040	-1.711	-1.711	0.000	0.000	0.000	0.000
25	A	206	SER	0	-0.131	-0.089	4.987	-2.489	-2.489	0.000	0.000	0.000	0.000
29	A	210	ASP	-1	-0.763	-0.870	8.172	-23.246	-23.246	0.000	0.000	0.000	0.000
30	A	211	ALA	0	0.037	0.015	11.520	1.522	1.522	0.000	0.000	0.000	0.000
31	A	212	VAL	0	0.005	0.016	10.888	-1.919	-1.919	0.000	0.000	0.000	0.000
32	A	213	VAL	0	0.001	0.006	12.778	1.510	1.510	0.000	0.000	0.000	0.000
33	A	214	HIS	0	-0.013	-0.031	15.895	-0.708	-0.708	0.000	0.000	0.000	0.000
34	A	215	PRO	0	-0.019	-0.020	18.078	0.815	0.815	0.000	0.000	0.000	0.000
35	A	216	THR	0	-0.022	-0.007	21.283	0.184	0.184	0.000	0.000	0.000	0.000
36	A	217	ASN	0	0.019	0.001	24.045	0.137	0.137	0.000	0.000	0.000	0.000
37	A	218	THR	0	0.053	0.021	27.687	-0.198	-0.198	0.000	0.000	0.000	0.000
38	A	219	ASP	-1	-0.905	-0.944	29.911	-10.543	-10.543	0.000	0.000	0.000	0.000
39	A	220	PHE	0	0.034	0.015	23.970	-0.166	-0.166	0.000	0.000	0.000	0.000
40	A	221	TYR	0	-0.029	-0.004	25.451	-0.296	-0.296	0.000	0.000	0.000	0.000
41	A	222	ILE	0	0.032	0.030	20.297	-0.469	-0.469	0.000	0.000	0.000	0.000
42	A	223	GLY	0	0.058	0.022	21.818	0.429	0.429	0.000	0.000	0.000	0.000
43	A	224	GLY	0	-0.076	-0.041	21.870	-0.018	-0.018	0.000	0.000	0.000	0.000
44	A	225	GLU	-1	-0.928	-0.963	17.187	-17.958	-17.958	0.000	0.000	0.000	0.000
45	A	226	VAL	0	0.024	0.008	15.321	-0.883	-0.883	0.000	0.000	0.000	0.000
46	A	227	GLY	0	0.071	0.041	16.328	-0.896	-0.896	0.000	0.000	0.000	0.000
47	A	228	ASN	0	0.013	-0.001	18.132	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	229	THR	0	-0.111	-0.080	12.412	0.103	0.103	0.000	0.000	0.000	0.000
49	A	230	LEU	0	0.007	0.002	12.508	-1.325	-1.325	0.000	0.000	0.000	0.000
50	A	231	GLU	-1	-0.877	-0.950	14.505	-15.223	-15.223	0.000	0.000	0.000	0.000
51	A	232	LYS	1	0.856	0.931	14.079	21.140	21.140	0.000	0.000	0.000	0.000
52	A	233	LYS	1	0.800	0.915	8.039	33.026	33.026	0.000	0.000	0.000	0.000
53	A	234	GLY	0	0.075	0.037	12.790	-0.139	-0.139	0.000	0.000	0.000	0.000
54	A	235	GLY	0	-0.011	0.005	14.733	1.039	1.039	0.000	0.000	0.000	0.000
55	A	236	LYS	1	0.920	0.954	18.069	12.700	12.700	0.000	0.000	0.000	0.000
56	A	237	GLU	-1	-0.815	-0.913	17.104	-18.012	-18.012	0.000	0.000	0.000	0.000
57	A	238	PHE	0	0.019	0.009	16.308	0.233	0.233	0.000	0.000	0.000	0.000
58	A	239	VAL	0	0.004	-0.001	18.397	0.556	0.556	0.000	0.000	0.000	0.000
59	A	240	GLU	-1	-0.922	-0.975	21.706	-12.536	-12.536	0.000	0.000	0.000	0.000
60	A	241	ALA	0	0.042	0.026	20.111	0.537	0.537	0.000	0.000	0.000	0.000
61	A	242	VAL	0	-0.024	-0.014	20.651	0.278	0.278	0.000	0.000	0.000	0.000
62	A	243	LEU	0	-0.035	-0.013	23.137	0.665	0.665	0.000	0.000	0.000	0.000
63	A	244	GLU	-1	-0.947	-0.977	24.778	-12.251	-12.251	0.000	0.000	0.000	0.000
64	A	245	LEU	0	-0.108	-0.042	22.522	0.467	0.467	0.000	0.000	0.000	0.000
65	A	246	ARG	1	0.835	0.912	25.991	11.722	11.722	0.000	0.000	0.000	0.000
66	A	247	LYS	1	0.922	0.960	28.466	9.972	9.972	0.000	0.000	0.000	0.000
67	A	248	LYS	1	0.902	0.955	25.994	12.252	12.252	0.000	0.000	0.000	0.000
68	A	249	ASN	0	-0.060	-0.027	28.278	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	250	GLY	0	0.036	0.035	30.436	0.321	0.321	0.000	0.000	0.000	0.000
70	A	251	PRO	0	-0.032	-0.042	30.929	-0.360	-0.360	0.000	0.000	0.000	0.000
71	A	252	LEU	0	-0.032	0.016	25.384	0.110	0.110	0.000	0.000	0.000	0.000
72	A	253	GLU	-1	-0.812	-0.914	29.879	-10.496	-10.496	0.000	0.000	0.000	0.000
73	A	254	VAL	0	-0.002	-0.013	29.811	-0.365	-0.365	0.000	0.000	0.000	0.000
74	A	255	ALA	0	-0.043	-0.022	27.835	0.257	0.257	0.000	0.000	0.000	0.000
75	A	256	GLY	0	0.043	0.044	27.589	-0.207	-0.207	0.000	0.000	0.000	0.000
76	A	257	ALA	0	-0.049	-0.049	22.709	-0.466	-0.466	0.000	0.000	0.000	0.000
77	A	258	ALA	0	0.025	0.017	23.489	0.370	0.370	0.000	0.000	0.000	0.000
78	A	259	VAL	0	-0.005	-0.011	19.240	-0.633	-0.633	0.000	0.000	0.000	0.000
79	A	260	SER	0	0.009	0.012	18.692	0.691	0.691	0.000	0.000	0.000	0.000
80	A	261	ALA	0	0.017	0.009	17.704	-0.742	-0.742	0.000	0.000	0.000	0.000
81	A	262	GLY	0	-0.011	-0.009	13.990	0.524	0.524	0.000	0.000	0.000	0.000
82	A	263	HIS	0	0.013	0.007	13.981	-1.910	-1.910	0.000	0.000	0.000	0.000
83	A	264	GLY	0	0.055	0.031	14.191	-0.024	-0.024	0.000	0.000	0.000	0.000
84	A	265	LEU	0	-0.089	-0.042	10.813	-1.557	-1.557	0.000	0.000	0.000	0.000
85	A	266	PRO	0	-0.047	-0.018	5.788	0.066	0.066	0.000	0.000	0.000	0.000
86	A	267	ALA	0	0.002	0.014	7.971	-0.575	-0.575	0.000	0.000	0.000	0.000
87	A	268	LYS	1	0.861	0.916	9.752	27.866	27.866	0.000	0.000	0.000	0.000
88	A	269	PHE	0	-0.013	-0.007	12.817	1.982	1.982	0.000	0.000	0.000	0.000
89	A	270	VAL	0	0.006	0.004	14.115	-1.484	-1.484	0.000	0.000	0.000	0.000
90	A	271	ILE	0	-0.014	-0.006	16.261	1.187	1.187	0.000	0.000	0.000	0.000
91	A	272	HIS	0	0.027	0.019	18.616	-0.060	-0.060	0.000	0.000	0.000	0.000
92	A	273	CYS	0	-0.015	-0.014	21.037	0.476	0.476	0.000	0.000	0.000	0.000
93	A	274	ASN	0	-0.017	0.000	23.243	-0.279	-0.279	0.000	0.000	0.000	0.000
94	A	275	SER	0	0.030	0.004	24.702	0.173	0.173	0.000	0.000	0.000	0.000
95	A	276	PRO	0	-0.006	0.009	26.590	0.329	0.329	0.000	0.000	0.000	0.000
96	A	277	VAL	0	-0.005	0.004	28.846	-0.461	-0.461	0.000	0.000	0.000	0.000
97	A	278	TRP	0	0.029	-0.003	30.522	0.151	0.151	0.000	0.000	0.000	0.000
98	A	279	GLY	0	0.037	0.003	32.147	0.173	0.173	0.000	0.000	0.000	0.000
99	A	280	ALA	0	-0.035	-0.013	34.488	0.284	0.284	0.000	0.000	0.000	0.000
100	A	281	ASP	-1	-0.907	-0.969	36.096	-8.116	-8.116	0.000	0.000	0.000	0.000
101	A	282	LYS	1	0.952	0.996	35.675	8.202	8.202	0.000	0.000	0.000	0.000
102	A	283	CYS	0	-0.078	-0.013	31.925	-0.367	-0.367	0.000	0.000	0.000	0.000
103	A	284	GLU	-1	-0.775	-0.909	30.600	-9.845	-9.845	0.000	0.000	0.000	0.000
104	A	285	GLU	-1	-0.866	-0.947	30.030	-9.256	-9.256	0.000	0.000	0.000	0.000
105	A	286	LEU	0	-0.013	-0.009	30.606	-0.260	-0.260	0.000	0.000	0.000	0.000
106	A	287	LEU	0	0.012	0.046	24.101	-0.398	-0.398	0.000	0.000	0.000	0.000
107	A	288	GLU	-1	-0.816	-0.899	25.755	-11.180	-11.180	0.000	0.000	0.000	0.000
108	A	289	LYS	1	0.873	0.933	26.460	9.196	9.196	0.000	0.000	0.000	0.000
109	A	290	THR	0	0.043	-0.003	23.398	-0.187	-0.187	0.000	0.000	0.000	0.000
110	A	291	VAL	0	-0.032	-0.002	21.074	-0.535	-0.535	0.000	0.000	0.000	0.000
111	A	292	LYS	1	0.865	0.929	22.285	11.131	11.131	0.000	0.000	0.000	0.000
112	A	293	ASN	0	-0.005	-0.006	24.341	-0.092	-0.092	0.000	0.000	0.000	0.000
113	A	294	CYS	0	-0.054	-0.034	19.333	-0.356	-0.356	0.000	0.000	0.000	0.000
114	A	295	LEU	0	-0.027	-0.008	18.608	-0.724	-0.724	0.000	0.000	0.000	0.000
115	A	296	ALA	0	0.049	0.029	20.786	-0.264	-0.264	0.000	0.000	0.000	0.000
116	A	297	LEU	0	0.006	-0.001	20.976	0.011	0.011	0.000	0.000	0.000	0.000
117	A	298	ALA	0	-0.009	-0.001	17.179	-0.479	-0.479	0.000	0.000	0.000	0.000
118	A	299	ASP	-1	-0.730	-0.829	18.863	-15.118	-15.118	0.000	0.000	0.000	0.000
119	A	300	ASP	-1	-0.910	-0.936	21.366	-12.754	-12.754	0.000	0.000	0.000	0.000
120	A	301	LYS	1	0.832	0.915	19.082	14.485	14.485	0.000	0.000	0.000	0.000
121	A	302	LYS	1	0.914	0.958	19.276	12.239	12.239	0.000	0.000	0.000	0.000
122	A	303	LEU	0	-0.046	-0.003	14.939	-0.916	-0.916	0.000	0.000	0.000	0.000
123	A	304	LYS	1	0.880	0.931	13.396	21.232	21.232	0.000	0.000	0.000	0.000
124	A	305	SER	0	-0.007	0.002	9.386	0.393	0.393	0.000	0.000	0.000	0.000
125	A	306	ILE	0	0.037	0.028	12.173	0.361	0.361	0.000	0.000	0.000	0.000
126	A	307	ALA	0	0.011	0.006	9.529	-0.172	-0.172	0.000	0.000	0.000	0.000
127	A	308	PHE	0	0.043	0.011	11.661	1.197	1.197	0.000	0.000	0.000	0.000
128	A	309	PRO	0	0.026	0.028	14.248	-0.811	-0.811	0.000	0.000	0.000	0.000
129	A	310	SER	0	-0.003	-0.023	15.823	0.759	0.759	0.000	0.000	0.000	0.000
130	A	311	ILE	0	0.012	-0.001	19.309	0.493	0.493	0.000	0.000	0.000	0.000
131	A	312	GLY	0	0.069	0.037	21.458	0.341	0.341	0.000	0.000	0.000	0.000
132	A	313	SER	0	-0.034	0.003	22.525	0.262	0.262	0.000	0.000	0.000	0.000
133	A	314	GLY	0	0.020	0.027	23.469	-0.251	-0.251	0.000	0.000	0.000	0.000
134	A	315	ARG	1	0.926	0.939	24.054	12.690	12.690	0.000	0.000	0.000	0.000
135	A	316	ASN	0	-0.061	-0.028	26.594	0.289	0.289	0.000	0.000	0.000	0.000
136	A	317	GLY	0	0.052	0.030	27.919	0.345	0.345	0.000	0.000	0.000	0.000
137	A	318	PHE	0	-0.011	-0.010	26.585	0.255	0.255	0.000	0.000	0.000	0.000
138	A	319	PRO	0	0.031	0.015	27.158	-0.446	-0.446	0.000	0.000	0.000	0.000
139	A	320	LYS	1	0.848	0.903	22.080	14.206	14.206	0.000	0.000	0.000	0.000
140	A	321	GLN	0	-0.027	-0.030	24.076	-0.177	-0.177	0.000	0.000	0.000	0.000
141	A	322	THR	0	0.039	0.022	26.189	-0.060	-0.060	0.000	0.000	0.000	0.000
142	A	323	ALA	0	0.034	0.010	23.502	0.058	0.058	0.000	0.000	0.000	0.000
143	A	324	ALA	0	0.003	0.009	22.032	-0.168	-0.168	0.000	0.000	0.000	0.000
144	A	325	GLN	0	0.007	0.003	22.968	-0.051	-0.051	0.000	0.000	0.000	0.000
145	A	326	LEU	0	-0.016	0.002	26.064	0.083	0.083	0.000	0.000	0.000	0.000
146	A	327	ILE	0	0.001	-0.002	19.722	-0.037	-0.037	0.000	0.000	0.000	0.000
147	A	328	LEU	0	-0.003	-0.003	19.756	-0.297	-0.297	0.000	0.000	0.000	0.000
148	A	329	LYS	1	0.847	0.907	22.781	10.517	10.517	0.000	0.000	0.000	0.000
149	A	330	ALA	0	-0.037	-0.013	24.230	0.251	0.251	0.000	0.000	0.000	0.000
150	A	331	ILE	0	0.032	0.011	18.792	0.105	0.105	0.000	0.000	0.000	0.000
151	A	332	SER	0	-0.006	0.017	22.676	0.233	0.233	0.000	0.000	0.000	0.000
152	A	333	SER	0	0.000	0.000	24.927	0.235	0.235	0.000	0.000	0.000	0.000
153	A	334	TYR	0	-0.033	-0.043	22.464	0.546	0.546	0.000	0.000	0.000	0.000
154	A	335	PHE	0	0.043	0.010	18.589	0.098	0.098	0.000	0.000	0.000	0.000
155	A	336	VAL	0	-0.014	-0.007	24.654	0.216	0.216	0.000	0.000	0.000	0.000
156	A	337	SER	0	-0.042	-0.028	27.921	0.574	0.574	0.000	0.000	0.000	0.000
157	A	338	THR	0	-0.087	-0.040	25.164	0.371	0.371	0.000	0.000	0.000	0.000
158	A	339	MET	0	0.005	-0.006	25.717	-0.453	-0.453	0.000	0.000	0.000	0.000
159	A	340	SER	0	-0.045	-0.015	26.500	-0.006	-0.006	0.000	0.000	0.000	0.000
160	A	341	SER	0	-0.057	-0.038	21.430	-0.448	-0.448	0.000	0.000	0.000	0.000
161	A	342	SER	0	-0.021	-0.026	18.642	0.239	0.239	0.000	0.000	0.000	0.000
162	A	343	ILE	0	-0.063	-0.016	15.558	-1.121	-1.121	0.000	0.000	0.000	0.000
163	A	344	LYS	1	0.905	0.944	14.696	16.862	16.862	0.000	0.000	0.000	0.000
164	A	345	THR	0	-0.044	-0.017	10.748	0.102	0.102	0.000	0.000	0.000	0.000
165	A	346	VAL	0	0.023	0.014	13.388	-0.328	-0.328	0.000	0.000	0.000	0.000
166	A	347	TYR	0	-0.007	-0.006	8.023	-1.024	-1.024	0.000	0.000	0.000	0.000
167	A	348	PHE	0	0.035	0.009	11.704	0.890	0.890	0.000	0.000	0.000	0.000
168	A	349	VAL	0	-0.014	-0.012	9.064	-1.073	-1.073	0.000	0.000	0.000	0.000
169	A	350	LEU	0	-0.013	0.001	11.920	1.558	1.558	0.000	0.000	0.000	0.000
170	A	351	PHE	0	0.053	0.006	12.652	-1.192	-1.192	0.000	0.000	0.000	0.000
171	A	352	ASP	-1	-0.752	-0.824	15.132	-16.022	-16.022	0.000	0.000	0.000	0.000
172	A	353	SER	0	0.061	0.000	17.726	-0.181	-0.181	0.000	0.000	0.000	0.000
173	A	354	GLU	-1	-0.866	-0.900	19.141	-12.812	-12.812	0.000	0.000	0.000	0.000
174	A	355	SER	0	-0.029	-0.061	18.562	0.521	0.521	0.000	0.000	0.000	0.000
175	A	356	ILE	0	-0.026	-0.001	14.040	-0.067	-0.067	0.000	0.000	0.000	0.000
176	A	357	GLY	0	0.007	0.009	17.860	0.033	0.033	0.000	0.000	0.000	0.000
177	A	358	ILE	0	0.023	0.012	21.154	0.247	0.247	0.000	0.000	0.000	0.000
178	A	359	TYR	0	0.029	-0.013	17.860	0.211	0.211	0.000	0.000	0.000	0.000
179	A	360	VAL	0	-0.033	-0.010	18.232	-0.050	-0.050	0.000	0.000	0.000	0.000
180	A	361	GLN	0	-0.039	-0.021	19.876	0.243	0.243	0.000	0.000	0.000	0.000
181	A	362	GLU	-1	-0.783	-0.882	22.816	-11.404	-11.404	0.000	0.000	0.000	0.000
182	A	363	MET	0	-0.034	-0.007	16.488	-0.123	-0.123	0.000	0.000	0.000	0.000
183	A	364	ALA	0	-0.040	-0.022	21.323	0.101	0.101	0.000	0.000	0.000	0.000
184	A	365	LYS	1	0.783	0.879	23.332	11.928	11.928	0.000	0.000	0.000	0.000
185	A	366	LEU	0	-0.037	0.001	21.999	0.406	0.406	0.000	0.000	0.000	0.000
186	A	367	ASP	-2	-1.701	-1.834	24.742	-25.058	-25.058	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:182:GLY)