FMO DATABASE

FMODB ID: 5GN8Z

Calculation Name: 4V8P-A-Xray547

Preferred Name:

Target Type:

Ligand Name: magnesium ion | zinc ion

Ligand 3-letter code: MG | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4V8P

Chain ID: A

ChEMBL ID:

UniProt ID: Q245F2

Base Structure: X-ray

Registration Date: 2025-10-06

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	212
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2303845.356975
FMO2-HF: Nuclear repulsion	2220525.056655
FMO2-HF: Total energy	-83320.300319
FMO2-MP2: Total energy	-83566.507319

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.
365.606	366.294	-0.003	-0.264	-0.421	0

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 : 0.929 / q_NPA : 0.955

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].
3	A	4	ARG	1	0.994	0.993	3.846	32.171	32.859	-0.003	-0.264	-0.421
4	A	5	PRO	0	0.044	0.014	6.661	2.624	2.624	0.000	0.000	0.000
5	A	6	ALA	0	0.072	0.030	8.812	1.397	1.397	0.000	0.000	0.000
6	A	7	ARG	1	1.005	0.995	11.949	24.666	24.666	0.000	0.000	0.000
7	A	8	CYS	0	-0.070	-0.027	10.880	0.799	0.799	0.000	0.000	0.000
8	A	9	TYR	0	-0.006	-0.033	10.408	-0.262	-0.262	0.000	0.000	0.000
9	A	10	ARG	1	0.816	0.929	15.359	16.177	16.177	0.000	0.000	0.000
10	A	11	GLN	0	0.112	0.044	17.537	0.775	0.775	0.000	0.000	0.000
11	A	12	PRO	0	-0.003	0.003	20.335	-0.606	-0.606	0.000	0.000	0.000
12	A	13	LYS	1	0.962	0.974	20.275	15.667	15.667	0.000	0.000	0.000
13	A	14	GLY	0	0.012	0.032	22.338	0.280	0.280	0.000	0.000	0.000
14	A	15	LYS	1	1.030	1.015	23.443	10.957	10.957	0.000	0.000	0.000
15	A	16	PRO	0	0.004	-0.014	23.978	-0.673	-0.673	0.000	0.000	0.000
16	A	17	TYR	0	0.018	0.006	19.260	0.434	0.434	0.000	0.000	0.000
17	A	18	PRO	0	0.082	0.047	21.352	-0.864	-0.864	0.000	0.000	0.000
18	A	19	LYS	1	0.955	0.977	20.240	14.881	14.881	0.000	0.000	0.000
19	A	20	SER	0	0.008	0.006	22.780	0.597	0.597	0.000	0.000	0.000
20	A	21	ARG	1	1.011	0.997	24.976	9.421	9.421	0.000	0.000	0.000
21	A	22	TYR	0	0.070	0.045	26.036	0.170	0.170	0.000	0.000	0.000
22	A	23	ASN	0	-0.097	-0.048	20.953	-0.812	-0.812	0.000	0.000	0.000
23	A	24	ARG	1	1.041	1.021	20.572	14.189	14.189	0.000	0.000	0.000
24	A	25	GLY	0	0.024	0.004	18.006	-0.594	-0.594	0.000	0.000	0.000
25	A	26	VAL	0	-0.045	-0.015	16.390	-1.261	-1.261	0.000	0.000	0.000
26	A	27	PRO	0	0.041	0.030	12.923	0.966	0.966	0.000	0.000	0.000
27	A	28	ASP	-1	-0.816	-0.902	15.431	-15.284	-15.284	0.000	0.000	0.000
28	A	29	ALA	0	-0.032	-0.019	14.916	-1.175	-1.175	0.000	0.000	0.000
29	A	30	ARG	1	0.968	0.965	8.441	28.136	28.136	0.000	0.000	0.000
30	A	31	ILE	0	-0.006	0.020	15.245	0.461	0.461	0.000	0.000	0.000
31	A	32	ARG	1	0.903	0.928	18.658	15.832	15.832	0.000	0.000	0.000
32	A	33	ILE	0	-0.024	-0.008	20.903	0.675	0.675	0.000	0.000	0.000
33	A	34	TYR	0	0.039	0.011	21.418	-0.151	-0.151	0.000	0.000	0.000
34	A	35	ASP	-1	-0.818	-0.896	25.686	-10.092	-10.092	0.000	0.000	0.000
35	A	36	SER	0	-0.088	-0.062	26.931	-0.346	-0.346	0.000	0.000	0.000
36	A	37	GLY	0	0.090	0.054	29.052	0.167	0.167	0.000	0.000	0.000
37	A	38	ARG	1	0.851	0.921	32.023	7.571	7.571	0.000	0.000	0.000
38	A	39	LYS	1	0.868	0.916	28.550	10.684	10.684	0.000	0.000	0.000
39	A	40	LYS	1	0.961	0.974	35.071	8.184	8.184	0.000	0.000	0.000
40	A	41	ALA	0	0.031	0.050	38.423	0.184	0.184	0.000	0.000	0.000
41	A	42	THR	0	0.042	0.021	40.370	-0.102	-0.102	0.000	0.000	0.000
42	A	43	VAL	0	-0.014	-0.021	41.971	-0.110	-0.110	0.000	0.000	0.000
43	A	44	GLU	-1	-0.744	-0.816	43.322	-6.537	-6.537	0.000	0.000	0.000
44	A	45	GLU	-1	-0.821	-0.885	42.631	-7.236	-7.236	0.000	0.000	0.000
45	A	46	PHE	0	-0.059	-0.039	38.559	-0.043	-0.043	0.000	0.000	0.000
46	A	47	PRO	0	0.043	0.033	40.887	-0.127	-0.127	0.000	0.000	0.000
47	A	48	TYR	0	-0.033	-0.046	40.485	-0.050	-0.050	0.000	0.000	0.000
48	A	49	VAL	0	-0.022	-0.010	35.952	-0.210	-0.210	0.000	0.000	0.000
49	A	50	VAL	0	-0.022	-0.012	33.345	0.121	0.121	0.000	0.000	0.000
50	A	51	HIS	0	0.014	0.026	31.792	-0.418	-0.418	0.000	0.000	0.000
51	A	52	ILE	0	-0.001	0.011	25.383	0.031	0.031	0.000	0.000	0.000
52	A	53	VAL	0	0.005	-0.003	28.950	-0.036	-0.036	0.000	0.000	0.000
53	A	54	SER	0	0.035	0.019	25.544	-0.120	-0.120	0.000	0.000	0.000
54	A	55	ASP	-1	-0.812	-0.906	27.165	-9.733	-9.733	0.000	0.000	0.000
55	A	56	GLU	-1	-0.809	-0.889	23.475	-13.260	-13.260	0.000	0.000	0.000
56	A	57	LYS	1	0.843	0.915	25.809	11.153	11.153	0.000	0.000	0.000
57	A	58	GLU	-1	-0.821	-0.906	20.362	-15.446	-15.446	0.000	0.000	0.000
58	A	59	GLN	0	-0.058	-0.037	18.119	1.074	1.074	0.000	0.000	0.000
59	A	60	ILE	0	0.028	0.024	17.552	-1.187	-1.187	0.000	0.000	0.000
60	A	61	THR	0	0.010	-0.006	11.918	0.028	0.028	0.000	0.000	0.000
61	A	62	SER	0	0.002	-0.012	13.584	0.787	0.787	0.000	0.000	0.000
62	A	63	GLU	-1	-0.815	-0.906	10.147	-25.215	-25.215	0.000	0.000	0.000
63	A	64	ALA	0	0.009	0.020	13.366	0.303	0.303	0.000	0.000	0.000
64	A	65	LEU	0	0.020	0.018	15.367	0.953	0.953	0.000	0.000	0.000
65	A	66	GLU	-1	-0.769	-0.888	15.850	-14.637	-14.637	0.000	0.000	0.000
66	A	67	ALA	0	-0.023	-0.010	14.903	0.641	0.641	0.000	0.000	0.000
67	A	68	ALA	0	0.021	0.011	16.988	0.724	0.724	0.000	0.000	0.000
68	A	69	ARG	1	0.868	0.929	20.305	14.351	14.351	0.000	0.000	0.000
69	A	70	ILE	0	-0.041	-0.026	17.389	0.720	0.720	0.000	0.000	0.000
70	A	71	ALA	0	-0.036	-0.012	20.738	0.479	0.479	0.000	0.000	0.000
71	A	72	ALA	0	0.084	0.039	22.362	0.513	0.513	0.000	0.000	0.000
72	A	73	ASN	0	0.002	-0.010	24.588	0.872	0.872	0.000	0.000	0.000
73	A	74	LYS	1	0.940	0.965	20.223	14.662	14.662	0.000	0.000	0.000
74	A	75	ASN	0	-0.006	-0.005	25.913	0.062	0.062	0.000	0.000	0.000
75	A	76	LEU	0	0.018	0.011	28.263	0.334	0.334	0.000	0.000	0.000
76	A	77	ILE	0	-0.078	-0.049	27.660	0.319	0.319	0.000	0.000	0.000
77	A	78	LYS	1	0.931	0.978	26.763	11.425	11.425	0.000	0.000	0.000
78	A	79	PHE	0	0.014	0.007	28.978	0.067	0.067	0.000	0.000	0.000
79	A	80	ILE	0	-0.004	0.012	33.932	0.223	0.223	0.000	0.000	0.000
80	A	81	SER	0	0.113	0.053	35.062	0.102	0.102	0.000	0.000	0.000
81	A	82	LYS	1	0.913	0.947	29.269	10.089	10.089	0.000	0.000	0.000
82	A	83	ASP	-1	-0.899	-0.939	34.082	-7.914	-7.914	0.000	0.000	0.000
83	A	84	ALA	0	0.049	0.009	37.115	0.045	0.045	0.000	0.000	0.000
84	A	85	PHE	0	0.033	0.016	29.930	-0.045	-0.045	0.000	0.000	0.000
85	A	86	HIS	0	-0.021	0.005	32.702	0.126	0.126	0.000	0.000	0.000
86	A	87	LEU	0	-0.016	0.000	26.180	0.093	0.093	0.000	0.000	0.000
87	A	88	ARG	1	0.912	0.950	28.732	9.445	9.445	0.000	0.000	0.000
88	A	89	CYS	0	-0.039	-0.007	23.918	-0.091	-0.091	0.000	0.000	0.000
89	A	90	ARG	1	0.903	0.937	26.383	9.736	9.736	0.000	0.000	0.000
90	A	91	VAL	0	0.001	0.021	22.997	0.040	0.040	0.000	0.000	0.000
91	A	92	HIS	0	0.038	0.017	23.034	-0.073	-0.073	0.000	0.000	0.000
92	A	93	PRO	0	-0.053	-0.034	18.107	0.011	0.011	0.000	0.000	0.000
93	A	94	TRP	0	0.055	0.013	19.840	-0.720	-0.720	0.000	0.000	0.000
94	A	95	HIS	0	-0.013	0.013	18.603	0.617	0.617	0.000	0.000	0.000
95	A	96	VAL	0	-0.007	-0.007	16.454	-1.104	-1.104	0.000	0.000	0.000
96	A	97	LEU	0	-0.040	-0.013	12.911	0.431	0.431	0.000	0.000	0.000
97	A	98	ARG	1	0.889	0.964	14.154	16.030	16.030	0.000	0.000	0.000
98	A	99	ILE	0	-0.017	-0.001	7.339	-1.082	-1.082	0.000	0.000	0.000
99	A	100	ASN	0	0.005	-0.012	11.706	0.115	0.115	0.000	0.000	0.000
100	A	101	LYS	1	0.882	0.916	7.816	28.801	28.801	0.000	0.000	0.000
101	A	102	MET	0	0.079	0.068	11.226	-1.403	-1.403	0.000	0.000	0.000
102	A	103	LEU	0	0.044	0.024	7.124	-1.176	-1.176	0.000	0.000	0.000
103	A	104	SER	0	-0.012	-0.023	9.204	-1.728	-1.728	0.000	0.000	0.000
104	A	105	CYS	0	0.058	0.021	11.642	0.705	0.705	0.000	0.000	0.000
105	A	106	ALA	0	0.041	0.044	14.731	0.978	0.978	0.000	0.000	0.000
106	A	107	GLY	0	-0.076	-0.042	15.601	0.745	0.745	0.000	0.000	0.000
107	A	108	ALA	0	0.070	0.027	17.079	-0.306	-0.306	0.000	0.000	0.000
108	A	109	ASP	-1	-0.804	-0.897	19.081	-15.312	-15.312	0.000	0.000	0.000
109	A	110	ARG	1	0.937	0.942	19.767	12.289	12.289	0.000	0.000	0.000
110	A	111	LEU	0	-0.070	-0.026	17.855	0.187	0.187	0.000	0.000	0.000
111	A	112	GLN	0	-0.007	0.008	13.656	-2.613	-2.613	0.000	0.000	0.000
112	A	113	SER	0	0.052	0.018	16.153	-0.604	-0.604	0.000	0.000	0.000
113	A	114	GLY	0	-0.019	-0.002	17.331	0.273	0.273	0.000	0.000	0.000
114	A	115	MET	0	-0.008	0.000	17.965	0.478	0.478	0.000	0.000	0.000
115	A	116	ARG	1	0.985	0.996	21.326	13.181	13.181	0.000	0.000	0.000
116	A	117	GLY	0	0.057	0.025	21.148	0.751	0.751	0.000	0.000	0.000
117	A	118	ALA	0	0.019	0.020	18.401	-0.756	-0.756	0.000	0.000	0.000
118	A	119	PHE	0	0.026	0.002	17.746	-0.974	-0.974	0.000	0.000	0.000
119	A	120	GLY	0	-0.019	-0.004	15.053	-0.227	-0.227	0.000	0.000	0.000
120	A	121	LYS	1	0.905	0.965	12.159	24.989	24.989	0.000	0.000	0.000
121	A	122	ALA	0	0.017	0.002	13.684	-0.833	-0.833	0.000	0.000	0.000
122	A	123	LEU	0	-0.050	-0.019	7.544	-1.608	-1.608	0.000	0.000	0.000
123	A	124	GLY	0	0.035	0.004	10.491	-1.947	-1.947	0.000	0.000	0.000
124	A	125	LYS	1	0.839	0.928	12.585	18.141	18.141	0.000	0.000	0.000
125	A	126	ALA	0	0.013	-0.001	15.023	-1.050	-1.050	0.000	0.000	0.000
126	A	127	ALA	0	0.006	0.018	17.390	0.702	0.702	0.000	0.000	0.000
127	A	128	ARG	1	0.783	0.881	20.801	13.444	13.444	0.000	0.000	0.000
128	A	129	VAL	0	0.000	0.006	23.146	0.408	0.408	0.000	0.000	0.000
129	A	130	ASP	-1	-0.757	-0.864	24.946	-11.023	-11.023	0.000	0.000	0.000
130	A	131	ILE	0	0.018	0.010	28.057	-0.067	-0.067	0.000	0.000	0.000
131	A	132	GLY	0	0.030	0.019	30.217	0.299	0.299	0.000	0.000	0.000
132	A	133	SER	0	-0.056	-0.030	28.090	0.061	0.061	0.000	0.000	0.000
133	A	134	ILE	0	-0.014	-0.016	28.900	-0.233	-0.233	0.000	0.000	0.000
134	A	135	LEU	0	0.003	-0.004	23.308	-0.167	-0.167	0.000	0.000	0.000
135	A	136	PHE	0	0.005	-0.012	22.294	-0.204	-0.204	0.000	0.000	0.000
136	A	137	SER	0	-0.016	-0.015	27.902	0.296	0.296	0.000	0.000	0.000
137	A	138	VAL	0	0.008	0.006	30.587	-0.169	-0.169	0.000	0.000	0.000
138	A	139	ARG	1	0.773	0.909	33.004	8.449	8.449	0.000	0.000	0.000
139	A	140	VAL	0	0.055	0.009	35.667	-0.141	-0.141	0.000	0.000	0.000
140	A	141	LYS	1	0.942	0.974	38.472	7.204	7.204	0.000	0.000	0.000
141	A	142	GLU	-1	-0.797	-0.882	41.006	-6.984	-6.984	0.000	0.000	0.000
142	A	143	PRO	0	0.008	0.013	42.055	-0.131	-0.131	0.000	0.000	0.000
143	A	144	HIS	0	0.055	0.016	37.807	-0.146	-0.146	0.000	0.000	0.000
144	A	145	VAL	0	-0.007	0.003	37.145	-0.312	-0.312	0.000	0.000	0.000
145	A	146	LYS	1	0.982	0.979	36.455	7.760	7.760	0.000	0.000	0.000
146	A	147	TYR	0	0.087	0.049	34.377	-0.323	-0.323	0.000	0.000	0.000
147	A	148	ALA	0	-0.010	-0.006	32.534	-0.370	-0.370	0.000	0.000	0.000
148	A	149	ILE	0	-0.001	-0.009	31.506	-0.350	-0.350	0.000	0.000	0.000
149	A	150	ASP	-1	-0.796	-0.841	30.798	-10.381	-10.381	0.000	0.000	0.000
150	A	151	ALA	0	0.022	0.011	28.202	-0.434	-0.434	0.000	0.000	0.000
151	A	152	LEU	0	-0.048	-0.028	26.730	-0.602	-0.602	0.000	0.000	0.000
152	A	153	THR	0	-0.021	-0.028	26.500	-0.429	-0.429	0.000	0.000	0.000
153	A	154	ARG	1	0.837	0.894	24.839	10.176	10.176	0.000	0.000	0.000
154	A	155	ALA	0	-0.029	-0.016	22.425	-0.670	-0.670	0.000	0.000	0.000
155	A	156	LYS	1	0.901	0.941	21.664	10.666	10.666	0.000	0.000	0.000
156	A	157	ALA	0	0.024	0.018	21.317	-0.312	-0.312	0.000	0.000	0.000
157	A	158	LYS	1	0.861	0.940	16.986	15.884	15.884	0.000	0.000	0.000
158	A	159	PHE	0	-0.033	-0.016	16.900	-1.045	-1.045	0.000	0.000	0.000
159	A	160	PRO	0	-0.050	-0.026	16.240	-0.260	-0.260	0.000	0.000	0.000
160	A	161	GLY	0	0.083	0.036	18.422	0.597	0.597	0.000	0.000	0.000
161	A	162	ARG	1	0.861	0.945	21.699	10.998	10.998	0.000	0.000	0.000
162	A	163	GLN	0	0.023	-0.003	21.926	-0.092	-0.092	0.000	0.000	0.000
163	A	164	LYS	1	0.868	0.921	26.344	9.810	9.810	0.000	0.000	0.000
164	A	165	VAL	0	0.013	0.005	29.183	-0.230	-0.230	0.000	0.000	0.000
165	A	166	VAL	0	0.012	0.012	31.519	0.243	0.243	0.000	0.000	0.000
166	A	167	THR	0	0.033	0.024	34.997	-0.109	-0.109	0.000	0.000	0.000
167	A	168	SER	0	-0.020	-0.012	37.873	0.208	0.208	0.000	0.000	0.000
168	A	169	GLN	0	0.048	0.021	39.857	0.126	0.126	0.000	0.000	0.000
169	A	170	LYS	1	0.866	0.934	41.081	7.679	7.679	0.000	0.000	0.000
170	A	171	TRP	0	0.067	0.036	42.418	-0.059	-0.059	0.000	0.000	0.000
171	A	172	GLY	0	0.048	0.023	39.550	-0.028	-0.028	0.000	0.000	0.000
172	A	173	PHE	0	-0.082	-0.064	32.996	-0.142	-0.142	0.000	0.000	0.000
173	A	174	THR	0	0.000	0.008	38.272	-0.054	-0.054	0.000	0.000	0.000
174	A	175	LYS	1	0.953	0.964	40.355	7.727	7.727	0.000	0.000	0.000
175	A	176	LEU	0	0.067	0.053	42.859	0.022	0.022	0.000	0.000	0.000
176	A	177	THR	0	0.025	0.002	44.830	-0.135	-0.135	0.000	0.000	0.000
177	A	178	ARG	1	0.935	0.960	43.252	7.263	7.263	0.000	0.000	0.000
178	A	179	ALA	0	0.051	0.044	47.745	0.096	0.096	0.000	0.000	0.000
179	A	180	GLN	0	0.035	0.017	48.797	0.003	0.003	0.000	0.000	0.000
180	A	181	TYR	0	-0.006	-0.043	47.109	0.045	0.045	0.000	0.000	0.000
181	A	182	SER	0	-0.039	-0.026	49.989	0.110	0.110	0.000	0.000	0.000
182	A	183	ARG	1	0.996	0.992	52.683	5.714	5.714	0.000	0.000	0.000
183	A	184	LEU	0	0.015	-0.001	51.096	0.077	0.077	0.000	0.000	0.000
184	A	185	ARG	1	0.837	0.898	50.425	6.301	6.301	0.000	0.000	0.000
185	A	186	ASN	0	0.001	0.004	54.144	0.035	0.035	0.000	0.000	0.000
186	A	187	GLN	0	-0.024	-0.016	57.413	0.014	0.014	0.000	0.000	0.000
187	A	188	LYS	1	0.995	1.012	56.439	5.306	5.306	0.000	0.000	0.000
188	A	189	LYS	1	0.949	0.991	54.340	5.724	5.724	0.000	0.000	0.000
189	A	190	LEU	0	-0.055	-0.030	49.508	-0.127	-0.127	0.000	0.000	0.000
190	A	191	VAL	0	0.075	0.044	49.844	0.051	0.051	0.000	0.000	0.000
191	A	192	THR	0	-0.015	-0.018	45.825	-0.152	-0.152	0.000	0.000	0.000
192	A	193	ASP	-1	-0.800	-0.895	43.260	-7.207	-7.207	0.000	0.000	0.000
193	A	194	GLY	0	0.041	0.031	40.883	-0.193	-0.193	0.000	0.000	0.000
194	A	195	SER	0	-0.039	-0.037	36.746	0.114	0.114	0.000	0.000	0.000
195	A	196	ASN	0	-0.076	-0.033	39.599	-0.218	-0.218	0.000	0.000	0.000
196	A	197	VAL	0	-0.008	-0.017	41.972	0.109	0.109	0.000	0.000	0.000
197	A	198	LYS	1	0.863	0.940	45.625	6.829	6.829	0.000	0.000	0.000
198	A	199	VAL	0	0.015	0.000	48.181	0.084	0.084	0.000	0.000	0.000
199	A	200	ILE	0	0.012	0.008	51.079	-0.034	-0.034	0.000	0.000	0.000
200	A	201	GLY	0	-0.005	0.001	54.334	0.064	0.064	0.000	0.000	0.000
201	A	202	GLU	-1	-0.830	-0.931	55.916	-5.542	-5.542	0.000	0.000	0.000
202	A	203	ARG	1	0.937	0.962	56.737	5.421	5.421	0.000	0.000	0.000
203	A	204	GLY	0	-0.021	0.003	57.119	-0.006	-0.006	0.000	0.000	0.000
204	A	205	PRO	0	0.059	0.011	57.741	0.065	0.065	0.000	0.000	0.000
205	A	206	LEU	0	0.075	0.026	60.255	-0.075	-0.075	0.000	0.000	0.000
206	A	207	SER	0	0.034	0.017	61.064	-0.004	-0.004	0.000	0.000	0.000
207	A	208	ARG	1	0.784	0.919	55.409	5.581	5.581	0.000	0.000	0.000
208	A	209	LEU	0	-0.072	-0.032	58.460	-0.077	-0.077	0.000	0.000	0.000
209	A	210	GLU	-1	-0.928	-0.980	57.818	-5.441	-5.441	0.000	0.000	0.000
210	A	211	LEU	0	-0.029	-0.016	61.108	0.038	0.038	0.000	0.000	0.000
211	A	212	PHE	0	-0.043	-0.016	63.953	0.076	0.076	0.000	0.000	0.000
212	A	213	ARG	0	0.055	0.051	60.667	0.253	0.253	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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