FMO DATABASE

FMODB ID: 97RJ2

Calculation Name: 4JRR-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | glycerol

Ligand 3-letter code: SO4 | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4JRR

Chain ID: A

ChEMBL ID:

UniProt ID: Q5ZZ88

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	188
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2101697.175901
FMO2-HF: Nuclear repulsion	2025548.952328
FMO2-HF: Total energy	-76148.223572
FMO2-MP2: Total energy	-76366.031101

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:29:GLY)

Summations of interaction energy for fragment #1(A:29: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.
-19.615	-15.909	2.998	-3.547	-3.158	-0.048

Interaction energy analysis for fragmet #1(A:29:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.832 / q_NPA : 0.904

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	31	HIS	0	0.020	0.007	2.123	-34.077	-30.452	2.999	-3.535	-3.090	-0.048
4	A	32	MET	0	-0.002	0.007	4.785	5.102	5.183	-0.001	-0.012	-0.068	0.000
5	A	33	GLN	0	0.043	0.022	8.296	0.109	0.109	0.000	0.000	0.000	0.000
6	A	34	PHE	0	0.005	0.012	10.902	1.955	1.955	0.000	0.000	0.000	0.000
7	A	35	ILE	0	-0.029	-0.020	11.955	-0.656	-0.656	0.000	0.000	0.000	0.000
8	A	36	GLU	-1	-0.868	-0.935	14.960	-15.776	-15.776	0.000	0.000	0.000	0.000
9	A	37	GLY	0	-0.024	-0.018	17.415	-0.274	-0.274	0.000	0.000	0.000	0.000
10	A	38	LYS	1	0.857	0.925	17.375	17.543	17.543	0.000	0.000	0.000	0.000
11	A	39	ASP	-1	-0.750	-0.861	16.507	-18.264	-18.264	0.000	0.000	0.000	0.000
12	A	40	TYR	0	0.015	0.000	15.055	1.025	1.025	0.000	0.000	0.000	0.000
13	A	41	GLN	0	-0.003	0.002	20.534	-0.070	-0.070	0.000	0.000	0.000	0.000
14	A	42	THR	0	0.033	0.020	20.885	0.348	0.348	0.000	0.000	0.000	0.000
15	A	43	VAL	0	-0.026	-0.007	23.484	0.405	0.405	0.000	0.000	0.000	0.000
16	A	44	ALA	0	0.038	0.023	27.288	-0.169	-0.169	0.000	0.000	0.000	0.000
17	A	45	SER	0	-0.013	-0.018	28.904	-0.019	-0.019	0.000	0.000	0.000	0.000
18	A	46	ALA	0	-0.002	0.008	30.987	0.252	0.252	0.000	0.000	0.000	0.000
19	A	47	GLN	0	0.026	0.013	34.406	-0.326	-0.326	0.000	0.000	0.000	0.000
20	A	48	LEU	0	-0.013	-0.004	33.352	0.175	0.175	0.000	0.000	0.000	0.000
21	A	49	SER	0	-0.007	-0.005	37.118	0.037	0.037	0.000	0.000	0.000	0.000
22	A	50	THR	0	-0.022	-0.014	33.452	0.240	0.240	0.000	0.000	0.000	0.000
23	A	51	ASN	0	-0.012	-0.013	36.370	-0.144	-0.144	0.000	0.000	0.000	0.000
24	A	52	LYS	1	0.989	0.992	31.813	9.640	9.640	0.000	0.000	0.000	0.000
25	A	53	ASP	-1	-0.856	-0.920	33.863	-8.772	-8.772	0.000	0.000	0.000	0.000
26	A	54	LYS	1	0.806	0.901	34.409	8.333	8.333	0.000	0.000	0.000	0.000
27	A	55	THR	0	-0.040	-0.018	28.869	-0.205	-0.205	0.000	0.000	0.000	0.000
28	A	56	PRO	0	0.015	0.014	25.786	0.136	0.136	0.000	0.000	0.000	0.000
29	A	57	LEU	0	-0.007	0.005	28.160	0.200	0.200	0.000	0.000	0.000	0.000
30	A	58	ILE	0	0.022	0.008	26.439	-0.417	-0.417	0.000	0.000	0.000	0.000
31	A	59	THR	0	-0.043	-0.019	29.774	0.496	0.496	0.000	0.000	0.000	0.000
32	A	60	GLU	-1	-0.829	-0.920	31.515	-9.687	-9.687	0.000	0.000	0.000	0.000
33	A	61	PHE	0	0.000	-0.007	32.554	0.375	0.375	0.000	0.000	0.000	0.000
34	A	62	PHE	0	0.056	-0.002	34.928	-0.146	-0.146	0.000	0.000	0.000	0.000
35	A	63	SER	0	0.058	0.006	37.504	0.260	0.260	0.000	0.000	0.000	0.000
36	A	64	TYR	0	0.025	-0.005	40.818	-0.050	-0.050	0.000	0.000	0.000	0.000
37	A	65	GLY	0	0.030	0.024	43.220	0.063	0.063	0.000	0.000	0.000	0.000
38	A	66	CYS	0	-0.090	-0.026	37.400	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	67	PRO	0	0.043	0.023	39.646	-0.106	-0.106	0.000	0.000	0.000	0.000
40	A	68	TRP	0	0.020	-0.015	33.880	0.021	0.021	0.000	0.000	0.000	0.000
41	A	69	CYS	0	-0.037	-0.001	34.927	-0.246	-0.246	0.000	0.000	0.000	0.000
42	A	70	TYR	0	0.013	0.008	36.532	-0.116	-0.116	0.000	0.000	0.000	0.000
43	A	71	LYS	1	0.905	0.958	34.977	8.849	8.849	0.000	0.000	0.000	0.000
44	A	72	ILE	0	0.080	0.045	31.103	-0.078	-0.078	0.000	0.000	0.000	0.000
45	A	73	ASP	-1	-0.844	-0.901	33.471	-8.709	-8.709	0.000	0.000	0.000	0.000
46	A	74	ALA	0	0.020	0.007	35.597	-0.045	-0.045	0.000	0.000	0.000	0.000
47	A	75	PRO	0	0.046	0.022	31.284	-0.086	-0.086	0.000	0.000	0.000	0.000
48	A	76	LEU	0	-0.001	0.003	30.197	-0.346	-0.346	0.000	0.000	0.000	0.000
49	A	77	ASN	0	-0.011	-0.001	32.063	-0.186	-0.186	0.000	0.000	0.000	0.000
50	A	78	ASP	-1	-0.884	-0.926	32.755	-9.297	-9.297	0.000	0.000	0.000	0.000
51	A	79	TRP	0	-0.093	-0.061	24.712	0.021	0.021	0.000	0.000	0.000	0.000
52	A	80	ALA	0	0.013	-0.001	29.570	-0.219	-0.219	0.000	0.000	0.000	0.000
53	A	81	THR	0	-0.044	-0.035	31.428	0.061	0.061	0.000	0.000	0.000	0.000
54	A	82	ARG	1	0.900	0.953	27.726	10.970	10.970	0.000	0.000	0.000	0.000
55	A	83	MET	0	-0.040	0.002	24.133	-0.445	-0.445	0.000	0.000	0.000	0.000
56	A	84	GLY	0	0.017	0.016	28.649	-0.083	-0.083	0.000	0.000	0.000	0.000
57	A	85	LYS	1	0.906	0.940	30.901	9.194	9.194	0.000	0.000	0.000	0.000
58	A	86	GLY	0	-0.015	-0.004	26.852	-0.112	-0.112	0.000	0.000	0.000	0.000
59	A	87	ALA	0	-0.004	-0.017	26.448	-0.464	-0.464	0.000	0.000	0.000	0.000
60	A	88	HIS	0	-0.007	0.026	28.880	0.353	0.353	0.000	0.000	0.000	0.000
61	A	89	LEU	0	0.005	0.003	31.562	-0.230	-0.230	0.000	0.000	0.000	0.000
62	A	90	GLU	-1	-0.916	-0.950	33.242	-8.143	-8.143	0.000	0.000	0.000	0.000
63	A	91	ARG	1	0.832	0.900	34.707	8.639	8.639	0.000	0.000	0.000	0.000
64	A	92	VAL	0	-0.014	0.006	37.073	0.280	0.280	0.000	0.000	0.000	0.000
65	A	93	PRO	0	-0.043	0.002	38.331	-0.145	-0.145	0.000	0.000	0.000	0.000
66	A	94	VAL	0	0.000	-0.008	37.911	0.032	0.032	0.000	0.000	0.000	0.000
67	A	95	VAL	0	-0.042	-0.059	41.232	0.129	0.129	0.000	0.000	0.000	0.000
68	A	96	PHE	0	0.018	0.008	37.722	0.024	0.024	0.000	0.000	0.000	0.000
69	A	97	LYS	1	0.935	0.975	43.688	7.332	7.332	0.000	0.000	0.000	0.000
70	A	98	PRO	0	0.064	0.018	46.802	0.013	0.013	0.000	0.000	0.000	0.000
71	A	99	ASN	0	0.021	0.005	49.159	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	100	TRP	0	-0.012	-0.004	40.903	-0.062	-0.062	0.000	0.000	0.000	0.000
73	A	101	ASP	-1	-0.786	-0.882	46.842	-6.488	-6.488	0.000	0.000	0.000	0.000
74	A	102	LEU	0	0.000	0.012	48.977	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	103	TYR	0	-0.035	-0.046	45.833	-0.070	-0.070	0.000	0.000	0.000	0.000
76	A	104	ALA	0	0.022	0.009	44.996	-0.091	-0.091	0.000	0.000	0.000	0.000
77	A	105	LYS	1	0.820	0.902	45.959	6.178	6.178	0.000	0.000	0.000	0.000
78	A	106	ALA	0	0.020	0.026	48.371	0.034	0.034	0.000	0.000	0.000	0.000
79	A	107	TYR	0	0.011	0.008	40.257	0.008	0.008	0.000	0.000	0.000	0.000
80	A	108	TYR	0	-0.001	-0.023	42.549	-0.095	-0.095	0.000	0.000	0.000	0.000
81	A	109	THR	0	0.017	0.009	46.481	0.066	0.066	0.000	0.000	0.000	0.000
82	A	110	ALA	0	0.024	0.006	46.717	0.050	0.050	0.000	0.000	0.000	0.000
83	A	111	LYS	1	0.919	0.966	41.112	7.610	7.610	0.000	0.000	0.000	0.000
84	A	112	THR	0	-0.086	-0.057	45.427	-0.065	-0.065	0.000	0.000	0.000	0.000
85	A	113	LEU	0	-0.032	-0.018	48.248	0.053	0.053	0.000	0.000	0.000	0.000
86	A	114	ALA	0	-0.028	-0.003	45.974	0.031	0.031	0.000	0.000	0.000	0.000
87	A	115	MET	0	0.024	0.011	46.587	0.007	0.007	0.000	0.000	0.000	0.000
88	A	116	SER	0	-0.022	-0.014	41.981	0.025	0.025	0.000	0.000	0.000	0.000
89	A	117	ASP	-1	-0.870	-0.932	40.804	-8.011	-8.011	0.000	0.000	0.000	0.000
90	A	118	LYS	1	0.875	0.942	42.490	6.310	6.310	0.000	0.000	0.000	0.000
91	A	119	MET	0	-0.010	-0.019	45.845	0.060	0.060	0.000	0.000	0.000	0.000
92	A	120	ASN	0	0.045	0.040	39.806	0.213	0.213	0.000	0.000	0.000	0.000
93	A	121	PRO	0	0.040	0.022	42.016	0.013	0.013	0.000	0.000	0.000	0.000
94	A	122	ILE	0	-0.007	0.008	43.492	0.072	0.072	0.000	0.000	0.000	0.000
95	A	123	LEU	0	-0.002	-0.007	46.002	0.126	0.126	0.000	0.000	0.000	0.000
96	A	124	PHE	0	-0.005	-0.003	39.101	0.040	0.040	0.000	0.000	0.000	0.000
97	A	125	LYS	1	0.827	0.923	44.417	6.762	6.762	0.000	0.000	0.000	0.000
98	A	126	ALA	0	0.030	0.019	46.528	0.074	0.074	0.000	0.000	0.000	0.000
99	A	127	ILE	0	-0.024	-0.006	46.518	0.084	0.084	0.000	0.000	0.000	0.000
100	A	128	GLN	0	-0.070	-0.050	42.650	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	129	GLU	-1	-0.903	-0.932	45.799	-6.948	-6.948	0.000	0.000	0.000	0.000
102	A	130	ASP	-1	-0.863	-0.946	47.476	-6.372	-6.372	0.000	0.000	0.000	0.000
103	A	131	LYS	1	0.791	0.903	47.314	6.970	6.970	0.000	0.000	0.000	0.000
104	A	132	ASN	0	0.062	0.035	51.328	0.154	0.154	0.000	0.000	0.000	0.000
105	A	133	PRO	0	-0.005	-0.004	51.389	-0.113	-0.113	0.000	0.000	0.000	0.000
106	A	134	LEU	0	0.012	0.011	50.581	-0.074	-0.074	0.000	0.000	0.000	0.000
107	A	135	ALA	0	0.022	0.015	53.463	-0.034	-0.034	0.000	0.000	0.000	0.000
108	A	136	THR	0	0.005	0.007	54.786	0.029	0.029	0.000	0.000	0.000	0.000
109	A	137	LYS	1	0.960	0.967	56.397	5.676	5.676	0.000	0.000	0.000	0.000
110	A	138	GLN	0	-0.005	-0.008	57.734	-0.029	-0.029	0.000	0.000	0.000	0.000
111	A	139	SER	0	-0.015	-0.017	56.721	-0.039	-0.039	0.000	0.000	0.000	0.000
112	A	140	MET	0	0.016	0.025	50.671	-0.070	-0.070	0.000	0.000	0.000	0.000
113	A	141	VAL	0	0.001	0.003	55.311	-0.045	-0.045	0.000	0.000	0.000	0.000
114	A	142	ASP	-1	-0.789	-0.867	57.911	-5.272	-5.272	0.000	0.000	0.000	0.000
115	A	143	PHE	0	0.013	0.007	50.532	0.005	0.005	0.000	0.000	0.000	0.000
116	A	144	PHE	0	0.004	-0.007	49.606	-0.095	-0.095	0.000	0.000	0.000	0.000
117	A	145	VAL	0	-0.014	0.001	54.993	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	146	ALA	0	-0.030	-0.008	56.926	0.029	0.029	0.000	0.000	0.000	0.000
119	A	147	HIS	0	-0.055	-0.030	52.667	-0.078	-0.078	0.000	0.000	0.000	0.000
120	A	148	GLY	0	-0.014	-0.009	54.255	-0.105	-0.105	0.000	0.000	0.000	0.000
121	A	149	VAL	0	-0.056	-0.020	53.463	-0.024	-0.024	0.000	0.000	0.000	0.000
122	A	150	ASP	-1	-0.785	-0.904	56.453	-5.240	-5.240	0.000	0.000	0.000	0.000
123	A	151	ARG	1	0.865	0.901	58.669	5.137	5.137	0.000	0.000	0.000	0.000
124	A	152	GLU	-1	-0.865	-0.936	60.725	-5.208	-5.208	0.000	0.000	0.000	0.000
125	A	153	ILE	0	-0.014	0.009	55.354	-0.065	-0.065	0.000	0.000	0.000	0.000
126	A	154	ALA	0	0.002	-0.002	55.740	-0.091	-0.091	0.000	0.000	0.000	0.000
127	A	155	LYS	1	0.850	0.908	56.780	5.062	5.062	0.000	0.000	0.000	0.000
128	A	156	SER	0	-0.015	-0.024	58.798	-0.065	-0.065	0.000	0.000	0.000	0.000
129	A	157	ALA	0	-0.005	0.000	53.383	-0.041	-0.041	0.000	0.000	0.000	0.000
130	A	158	PHE	0	-0.013	-0.016	51.790	-0.099	-0.099	0.000	0.000	0.000	0.000
131	A	159	GLU	-1	-0.932	-0.946	55.718	-5.232	-5.232	0.000	0.000	0.000	0.000
132	A	160	ASN	0	-0.042	-0.018	58.345	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	161	SER	0	0.069	0.038	54.104	0.004	0.004	0.000	0.000	0.000	0.000
134	A	162	PRO	0	0.078	0.038	53.667	-0.144	-0.144	0.000	0.000	0.000	0.000
135	A	163	THR	0	-0.009	-0.007	50.236	-0.102	-0.102	0.000	0.000	0.000	0.000
136	A	164	ILE	0	-0.009	0.000	48.928	-0.187	-0.187	0.000	0.000	0.000	0.000
137	A	165	ASP	-1	-0.813	-0.911	48.821	-6.247	-6.247	0.000	0.000	0.000	0.000
138	A	166	MET	0	-0.004	-0.001	48.799	-0.173	-0.173	0.000	0.000	0.000	0.000
139	A	167	ARG	1	0.929	0.988	41.623	7.295	7.295	0.000	0.000	0.000	0.000
140	A	168	VAL	0	0.009	0.006	44.200	-0.239	-0.239	0.000	0.000	0.000	0.000
141	A	169	ASN	0	0.011	-0.001	44.291	-0.208	-0.208	0.000	0.000	0.000	0.000
142	A	170	SER	0	-0.017	-0.014	42.693	-0.146	-0.146	0.000	0.000	0.000	0.000
143	A	171	GLY	0	-0.002	-0.008	40.147	-0.217	-0.217	0.000	0.000	0.000	0.000
144	A	172	MET	0	0.057	0.048	39.328	-0.299	-0.299	0.000	0.000	0.000	0.000
145	A	173	SER	0	-0.015	-0.017	40.003	-0.108	-0.108	0.000	0.000	0.000	0.000
146	A	174	LEU	0	-0.025	-0.005	35.192	-0.154	-0.154	0.000	0.000	0.000	0.000
147	A	175	MET	0	-0.028	-0.005	35.361	-0.245	-0.245	0.000	0.000	0.000	0.000
148	A	176	ALA	0	0.012	0.002	35.153	-0.240	-0.240	0.000	0.000	0.000	0.000
149	A	177	HIS	0	-0.027	-0.010	32.819	0.060	0.060	0.000	0.000	0.000	0.000
150	A	178	TYR	0	-0.022	-0.036	31.012	-0.191	-0.191	0.000	0.000	0.000	0.000
151	A	179	GLN	0	-0.049	-0.024	30.912	-0.369	-0.369	0.000	0.000	0.000	0.000
152	A	180	ILE	0	-0.043	-0.014	30.421	-0.322	-0.322	0.000	0.000	0.000	0.000
153	A	181	ASN	0	0.010	-0.008	33.457	0.114	0.114	0.000	0.000	0.000	0.000
154	A	182	ALA	0	0.014	0.010	33.151	0.215	0.215	0.000	0.000	0.000	0.000
155	A	183	VAL	0	-0.020	0.001	34.113	-0.100	-0.100	0.000	0.000	0.000	0.000
156	A	184	PRO	0	0.006	-0.012	32.012	0.188	0.188	0.000	0.000	0.000	0.000
157	A	185	ALA	0	0.001	-0.003	30.171	-0.296	-0.296	0.000	0.000	0.000	0.000
158	A	186	PHE	0	0.006	0.000	27.380	0.279	0.279	0.000	0.000	0.000	0.000
159	A	187	VAL	0	-0.004	-0.004	27.728	-0.337	-0.337	0.000	0.000	0.000	0.000
160	A	188	VAL	0	0.006	0.003	24.273	0.283	0.283	0.000	0.000	0.000	0.000
161	A	189	ASN	0	0.020	-0.011	23.687	0.309	0.309	0.000	0.000	0.000	0.000
162	A	190	ASN	0	-0.011	0.015	27.019	0.003	0.003	0.000	0.000	0.000	0.000
163	A	191	LYS	1	0.848	0.943	23.200	12.245	12.245	0.000	0.000	0.000	0.000
164	A	192	TYR	0	0.051	-0.002	19.971	-0.731	-0.731	0.000	0.000	0.000	0.000
165	A	193	LYS	1	0.866	0.948	24.034	11.739	11.739	0.000	0.000	0.000	0.000
166	A	194	THR	0	0.020	-0.012	22.791	-0.536	-0.536	0.000	0.000	0.000	0.000
167	A	195	ASP	-1	-0.805	-0.901	25.024	-11.034	-11.034	0.000	0.000	0.000	0.000
168	A	196	LEU	0	0.030	0.006	26.076	-0.395	-0.395	0.000	0.000	0.000	0.000
169	A	197	GLN	0	-0.058	-0.015	27.544	-0.158	-0.158	0.000	0.000	0.000	0.000
170	A	198	MET	0	-0.068	-0.026	22.243	-0.231	-0.231	0.000	0.000	0.000	0.000
171	A	199	ALA	0	-0.008	0.002	22.242	-0.695	-0.695	0.000	0.000	0.000	0.000
172	A	200	GLY	0	-0.008	0.005	23.010	-0.417	-0.417	0.000	0.000	0.000	0.000
173	A	201	SER	0	-0.025	-0.027	23.844	0.296	0.296	0.000	0.000	0.000	0.000
174	A	202	GLU	-1	-0.856	-0.956	25.541	-10.562	-10.562	0.000	0.000	0.000	0.000
175	A	203	GLU	-1	-0.947	-0.959	22.623	-13.795	-13.795	0.000	0.000	0.000	0.000
176	A	204	ARG	1	0.823	0.903	15.019	18.618	18.618	0.000	0.000	0.000	0.000
177	A	205	LEU	0	0.018	0.004	21.510	-0.455	-0.455	0.000	0.000	0.000	0.000
178	A	206	PHE	0	0.014	0.000	23.683	-0.134	-0.134	0.000	0.000	0.000	0.000
179	A	207	GLU	-1	-0.897	-0.931	18.514	-17.610	-17.610	0.000	0.000	0.000	0.000
180	A	208	ILE	0	-0.047	-0.028	18.957	-0.732	-0.732	0.000	0.000	0.000	0.000
181	A	209	LEU	0	-0.009	-0.001	20.248	-0.172	-0.172	0.000	0.000	0.000	0.000
182	A	210	ASN	0	0.012	0.000	20.400	0.585	0.585	0.000	0.000	0.000	0.000
183	A	211	TYR	0	-0.018	-0.007	13.459	-0.046	-0.046	0.000	0.000	0.000	0.000
184	A	212	LEU	0	-0.015	-0.021	18.428	-0.121	-0.121	0.000	0.000	0.000	0.000
185	A	213	VAL	0	0.008	0.007	20.741	0.206	0.206	0.000	0.000	0.000	0.000
186	A	214	ARG	1	0.912	0.957	18.849	15.542	15.542	0.000	0.000	0.000	0.000
187	A	215	LYS	1	0.831	0.944	15.779	18.122	18.122	0.000	0.000	0.000	0.000
188	A	216	SER	-1	-0.869	-0.911	19.974	-12.685	-12.685	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:29:GLY)