FMO DATABASE

FMODB ID: 2MNJR

Calculation Name: 1WPN-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | manganese (ii) ion

Ligand 3-letter code: SO4 | MN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1WPN

Chain ID: A

ChEMBL ID:

UniProt ID: P37487

Base Structure: X-ray

Registration Date: 2025-10-05

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	187
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2072215.342035
FMO2-HF: Nuclear repulsion	1999263.432737
FMO2-HF: Total energy	-72951.909297
FMO2-MP2: Total energy	-73164.256039

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:GLU)

Summations of interaction energy for fragment #1(A:2: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.
-27.534	-27.657	14.611	-7.208	-7.281	0.046

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.071 / q_NPA : -0.038

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	ILE	0	0.038	0.019	2.523	4.421	7.283	1.081	-1.667	-2.277	-0.017
4	A	5	LEU	0	-0.011	-0.006	5.066	-1.659	-1.577	-0.001	-0.006	-0.075	0.000
32	A	33	ASN	0	-0.035	-0.025	3.838	4.375	4.789	0.000	-0.080	-0.334	0.000
67	A	68	VAL	0	-0.062	-0.032	4.412	0.291	0.462	-0.001	-0.026	-0.144	0.000
68	A	69	ASN	0	0.006	-0.005	1.737	-26.390	-30.323	13.532	-5.390	-4.209	0.063
69	A	70	GLY	0	-0.013	0.004	4.380	-4.552	-4.271	0.000	-0.039	-0.242	0.000
5	A	6	ILE	0	0.008	0.003	8.625	0.576	0.576	0.000	0.000	0.000	0.000
6	A	7	PHE	0	0.027	0.007	11.278	-0.165	-0.165	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.058	0.030	15.008	0.113	0.113	0.000	0.000	0.000	0.000
8	A	9	HIS	1	0.775	0.881	18.435	-0.146	-0.146	0.000	0.000	0.000	0.000
9	A	10	GLN	0	-0.035	-0.042	21.073	-0.222	-0.222	0.000	0.000	0.000	0.000
10	A	11	ASN	0	-0.080	-0.043	22.859	-0.078	-0.078	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.003	0.017	22.374	-0.024	-0.024	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.786	-0.895	24.439	0.029	0.029	0.000	0.000	0.000	0.000
13	A	14	THR	0	0.046	-0.016	24.628	-0.052	-0.052	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.654	-0.801	23.819	-0.473	-0.473	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.056	-0.034	20.674	-0.060	-0.060	0.000	0.000	0.000	0.000
16	A	17	ILE	0	-0.044	-0.015	19.768	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	18	CYS	0	-0.052	-0.022	19.958	-0.191	-0.191	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.013	-0.039	19.919	-0.282	-0.282	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.008	0.011	15.905	-0.200	-0.200	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.012	-0.015	15.643	-0.405	-0.405	0.000	0.000	0.000	0.000
21	A	22	ALA	0	0.006	0.003	16.618	-0.402	-0.402	0.000	0.000	0.000	0.000
22	A	23	TYR	0	-0.018	-0.040	13.177	-0.508	-0.508	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.008	0.008	11.995	-0.621	-0.621	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.796	-0.856	12.171	-4.025	-4.025	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.021	-0.004	13.838	-0.548	-0.548	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.836	0.894	8.949	3.284	3.284	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.009	-0.011	9.358	-2.715	-2.715	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.767	0.855	10.667	2.748	2.748	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.039	-0.008	11.309	0.335	0.335	0.000	0.000	0.000	0.000
30	A	31	GLY	0	-0.037	-0.006	9.060	-0.320	-0.320	0.000	0.000	0.000	0.000
31	A	32	PHE	0	-0.052	-0.022	5.131	-3.801	-3.801	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.040	0.015	5.847	-0.762	-0.762	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.774	-0.842	8.557	-1.103	-1.103	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.004	0.021	10.960	0.605	0.605	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.030	-0.022	12.224	0.056	0.056	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.858	0.908	14.889	0.136	0.136	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.059	0.034	16.156	0.104	0.104	0.000	0.000	0.000	0.000
39	A	40	GLY	0	0.031	0.010	19.637	0.060	0.060	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.054	-0.016	22.821	-0.060	-0.060	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.036	0.017	23.875	0.022	0.022	0.000	0.000	0.000	0.000
42	A	43	ASN	0	0.001	0.015	26.362	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.068	0.021	29.725	-0.055	-0.055	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.757	-0.814	30.785	-0.250	-0.250	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.010	-0.050	25.286	-0.041	-0.041	0.000	0.000	0.000	0.000
46	A	47	GLN	0	-0.071	-0.041	27.698	-0.048	-0.048	0.000	0.000	0.000	0.000
47	A	48	TYR	0	0.010	0.010	29.137	-0.063	-0.063	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.014	0.002	28.103	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.048	-0.022	23.105	-0.093	-0.093	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.843	-0.916	26.911	-0.612	-0.612	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.083	-0.033	29.904	-0.030	-0.030	0.000	0.000	0.000	0.000
52	A	53	PHE	0	-0.051	-0.015	26.896	-0.046	-0.046	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.906	0.953	26.569	0.722	0.722	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.029	-0.007	21.678	-0.257	-0.257	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.917	-0.957	20.993	-1.182	-1.182	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.019	-0.015	21.298	0.006	0.006	0.000	0.000	0.000	0.000
57	A	58	PRO	0	0.017	0.008	17.075	-0.028	-0.028	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.743	0.810	11.147	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.064	-0.023	16.772	0.107	0.107	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.011	-0.010	13.363	0.015	0.015	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.892	-0.947	16.604	1.328	1.328	0.000	0.000	0.000	0.000
62	A	63	THR	0	-0.054	-0.053	13.986	-0.203	-0.203	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.007	-0.011	9.624	-0.446	-0.446	0.000	0.000	0.000	0.000
64	A	65	ALA	0	0.068	0.030	8.800	1.291	1.291	0.000	0.000	0.000	0.000
65	A	66	ASN	0	-0.064	-0.014	9.088	0.924	0.924	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.873	-0.900	8.175	0.634	0.634	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.012	-0.013	5.833	-2.727	-2.727	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.048	-0.021	8.573	-0.202	-0.202	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.003	0.016	11.352	-0.192	-0.192	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.015	-0.006	14.957	-0.312	-0.312	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.770	-0.875	17.647	0.285	0.285	0.000	0.000	0.000	0.000
75	A	76	HIS	0	-0.057	-0.015	17.123	0.299	0.299	0.000	0.000	0.000	0.000
76	A	77	ASN	0	0.004	-0.022	19.488	0.126	0.126	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.806	-0.858	20.478	1.027	1.027	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.929	0.943	20.355	-2.164	-2.164	0.000	0.000	0.000	0.000
79	A	80	GLN	0	-0.046	-0.037	21.309	0.150	0.150	0.000	0.000	0.000	0.000
80	A	81	GLN	0	-0.045	-0.023	22.511	-0.140	-0.140	0.000	0.000	0.000	0.000
81	A	82	SER	0	0.049	0.013	17.298	0.008	0.008	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.011	0.017	13.490	-0.197	-0.197	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.838	0.912	17.253	-1.696	-1.696	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.716	-0.851	13.003	4.255	4.255	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.026	-0.012	13.683	0.648	0.648	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.854	-0.916	13.946	3.126	3.126	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-1.002	-0.994	12.475	4.625	4.625	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.040	-0.008	8.400	1.518	1.518	0.000	0.000	0.000	0.000
89	A	90	GLN	0	-0.011	-0.005	6.340	-3.077	-3.077	0.000	0.000	0.000	0.000
90	A	91	VAL	0	0.018	0.003	8.769	0.275	0.275	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.010	0.002	5.299	-0.220	-0.220	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.794	-0.871	9.826	-3.032	-3.032	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.009	0.005	12.876	0.265	0.265	0.000	0.000	0.000	0.000
94	A	95	ILE	0	0.009	0.016	15.628	-0.176	-0.176	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.745	-0.874	18.383	0.451	0.451	0.000	0.000	0.000	0.000
96	A	97	HIS	1	0.806	0.909	21.793	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	98	HIS	1	0.799	0.908	24.163	-0.286	-0.286	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.861	0.912	26.392	-0.700	-0.700	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.032	0.030	22.895	0.024	0.024	0.000	0.000	0.000	0.000
100	A	101	ALA	0	-0.048	-0.028	24.774	-0.052	-0.052	0.000	0.000	0.000	0.000
101	A	102	ASN	0	-0.073	-0.048	24.223	0.085	0.085	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.058	0.025	16.054	0.088	0.088	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.961	-0.980	19.366	1.635	1.635	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.021	-0.024	14.741	0.141	0.141	0.000	0.000	0.000	0.000
105	A	106	ALA	0	-0.022	0.002	14.638	-0.274	-0.274	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.899	-0.945	11.477	3.909	3.909	0.000	0.000	0.000	0.000
107	A	108	PRO	0	-0.052	-0.029	14.278	-0.291	-0.291	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.019	0.022	12.981	0.378	0.378	0.000	0.000	0.000	0.000
109	A	110	TYR	0	-0.018	-0.007	13.410	-0.460	-0.460	0.000	0.000	0.000	0.000
110	A	111	TYR	0	0.019	0.003	15.174	-0.042	-0.042	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.695	0.811	18.102	0.614	0.614	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.032	0.013	20.238	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.771	-0.871	23.336	-0.490	-0.490	0.000	0.000	0.000	0.000
114	A	115	PRO	0	-0.044	-0.016	26.394	0.021	0.021	0.000	0.000	0.000	0.000
115	A	116	VAL	0	-0.061	-0.032	27.130	-0.035	-0.035	0.000	0.000	0.000	0.000
116	A	117	GLY	0	0.063	0.014	29.482	0.055	0.055	0.000	0.000	0.000	0.000
117	A	118	CYS	0	-0.119	-0.033	27.026	0.003	0.003	0.000	0.000	0.000	0.000
118	A	119	THR	0	-0.020	-0.029	20.698	0.006	0.006	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.049	0.022	22.964	-0.127	-0.127	0.000	0.000	0.000	0.000
120	A	121	THR	0	-0.043	-0.054	24.014	-0.140	-0.140	0.000	0.000	0.000	0.000
121	A	122	ILE	0	-0.039	-0.007	21.334	-0.059	-0.059	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.007	0.007	17.881	-0.136	-0.136	0.000	0.000	0.000	0.000
123	A	124	ASN	0	-0.018	-0.023	20.989	-0.275	-0.275	0.000	0.000	0.000	0.000
124	A	125	LYS	1	0.773	0.882	23.380	0.456	0.456	0.000	0.000	0.000	0.000
125	A	126	MET	0	0.021	0.020	16.170	-0.031	-0.031	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.005	-0.040	17.980	-0.178	-0.178	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.818	0.896	20.181	0.831	0.831	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.832	-0.890	20.401	-1.101	-1.101	0.000	0.000	0.000	0.000
129	A	130	ASN	0	-0.066	-0.037	15.974	-0.280	-0.280	0.000	0.000	0.000	0.000
130	A	131	ASN	0	-0.069	-0.029	18.836	-0.077	-0.077	0.000	0.000	0.000	0.000
131	A	132	VAL	0	0.002	0.010	16.405	-0.088	-0.088	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.894	0.946	19.817	1.955	1.955	0.000	0.000	0.000	0.000
133	A	134	ILE	0	0.051	0.031	21.031	-0.173	-0.173	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.924	-0.962	20.234	-2.290	-2.290	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.952	0.993	23.664	1.031	1.031	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.880	-0.948	24.195	-1.288	-1.288	0.000	0.000	0.000	0.000
137	A	138	ILE	0	0.007	0.005	19.665	0.110	0.110	0.000	0.000	0.000	0.000
138	A	139	ALA	0	0.055	0.010	22.938	0.098	0.098	0.000	0.000	0.000	0.000
139	A	140	GLY	0	0.052	0.016	25.687	0.111	0.111	0.000	0.000	0.000	0.000
140	A	141	LEU	0	-0.023	0.006	22.161	0.117	0.117	0.000	0.000	0.000	0.000
141	A	142	MET	0	-0.034	-0.019	22.420	0.048	0.048	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.007	-0.002	25.251	0.105	0.105	0.000	0.000	0.000	0.000
143	A	144	SER	0	0.001	-0.025	27.813	0.101	0.101	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.014	0.000	25.335	0.085	0.085	0.000	0.000	0.000	0.000
145	A	146	ILE	0	0.029	0.010	27.426	0.084	0.084	0.000	0.000	0.000	0.000
146	A	147	ILE	0	-0.020	0.006	30.007	0.067	0.067	0.000	0.000	0.000	0.000
147	A	148	SER	0	-0.027	-0.029	29.554	0.063	0.063	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.765	-0.882	27.785	-0.068	-0.068	0.000	0.000	0.000	0.000
149	A	150	SER	0	-0.098	-0.075	31.149	0.045	0.045	0.000	0.000	0.000	0.000
150	A	151	LEU	0	-0.026	-0.018	34.306	0.021	0.021	0.000	0.000	0.000	0.000
151	A	152	LEU	0	-0.061	-0.023	35.737	0.011	0.011	0.000	0.000	0.000	0.000
152	A	153	PHE	0	0.005	-0.022	34.426	0.008	0.008	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.915	0.974	38.247	0.164	0.164	0.000	0.000	0.000	0.000
154	A	155	SER	0	-0.012	0.016	34.547	0.041	0.041	0.000	0.000	0.000	0.000
155	A	156	PRO	0	-0.023	-0.021	37.551	-0.019	-0.019	0.000	0.000	0.000	0.000
156	A	157	THR	0	-0.039	-0.023	32.826	0.005	0.005	0.000	0.000	0.000	0.000
157	A	158	CYS	0	-0.024	0.005	33.665	-0.036	-0.036	0.000	0.000	0.000	0.000
158	A	159	THR	0	-0.029	-0.035	32.673	0.003	0.003	0.000	0.000	0.000	0.000
159	A	160	ASP	-1	-0.859	-0.943	34.862	-0.277	-0.277	0.000	0.000	0.000	0.000
160	A	161	GLN	0	0.000	0.002	30.384	-0.092	-0.092	0.000	0.000	0.000	0.000
161	A	162	ASP	-1	-0.704	-0.799	30.193	-0.349	-0.349	0.000	0.000	0.000	0.000
162	A	163	VAL	0	0.028	0.015	31.871	-0.042	-0.042	0.000	0.000	0.000	0.000
163	A	164	ALA	0	-0.038	-0.018	33.083	-0.031	-0.031	0.000	0.000	0.000	0.000
164	A	165	ALA	0	-0.003	0.000	28.384	-0.048	-0.048	0.000	0.000	0.000	0.000
165	A	166	ALA	0	0.052	0.022	30.238	-0.060	-0.060	0.000	0.000	0.000	0.000
166	A	167	LYS	1	0.955	0.974	31.973	0.464	0.464	0.000	0.000	0.000	0.000
167	A	168	GLU	-1	-0.832	-0.889	29.474	-0.844	-0.844	0.000	0.000	0.000	0.000
168	A	169	LEU	0	-0.022	-0.012	25.749	-0.063	-0.063	0.000	0.000	0.000	0.000
169	A	170	ALA	0	0.005	0.009	29.491	-0.040	-0.040	0.000	0.000	0.000	0.000
170	A	171	GLU	-1	-0.963	-0.969	32.641	-0.708	-0.708	0.000	0.000	0.000	0.000
171	A	172	ILE	0	-0.058	-0.035	26.713	-0.036	-0.036	0.000	0.000	0.000	0.000
172	A	173	ALA	0	0.005	-0.001	29.381	-0.064	-0.064	0.000	0.000	0.000	0.000
173	A	174	GLY	0	-0.083	-0.034	30.372	0.003	0.003	0.000	0.000	0.000	0.000
174	A	175	VAL	0	-0.058	-0.036	33.202	0.033	0.033	0.000	0.000	0.000	0.000
175	A	176	ASP	-1	-0.798	-0.903	35.791	-0.437	-0.437	0.000	0.000	0.000	0.000
176	A	177	ALA	0	0.015	-0.009	35.658	-0.003	-0.003	0.000	0.000	0.000	0.000
177	A	178	GLU	-1	-0.885	-0.953	36.590	-0.284	-0.284	0.000	0.000	0.000	0.000
178	A	179	GLU	-1	-1.001	-0.995	39.744	-0.403	-0.403	0.000	0.000	0.000	0.000
179	A	180	TYR	0	-0.012	-0.019	30.811	0.012	0.012	0.000	0.000	0.000	0.000
180	A	181	GLY	0	0.041	0.013	35.690	0.014	0.014	0.000	0.000	0.000	0.000
181	A	182	LEU	0	-0.026	-0.019	36.734	0.037	0.037	0.000	0.000	0.000	0.000
182	A	183	ASN	0	-0.122	-0.062	38.289	0.050	0.050	0.000	0.000	0.000	0.000
183	A	184	MET	0	-0.008	0.018	31.824	-0.005	-0.005	0.000	0.000	0.000	0.000
184	A	185	LEU	0	-0.005	-0.012	34.496	0.029	0.029	0.000	0.000	0.000	0.000
185	A	186	LYS	1	0.871	0.948	36.539	0.259	0.259	0.000	0.000	0.000	0.000
186	A	187	ALA	0	-0.042	-0.019	34.825	0.013	0.013	0.000	0.000	0.000	0.000
187	A	188	GLY	-1	-0.954	-0.959	34.599	-0.050	-0.050	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:2:GLU)