FMO DATABASE

FMODB ID: 9Q7V2

Calculation Name: 6D90-Q-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6D90

Chain ID: Q

ChEMBL ID:

UniProt ID: P62495

Base Structure: ElectronMicroscopy

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1794764.330073
FMO2-HF: Nuclear repulsion	1720549.404937
FMO2-HF: Total energy	-74214.925136
FMO2-MP2: Total energy	-74434.170066

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.
261.168	262.052	-0.01	-0.32	-0.555	-0.001

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 : 0.854 / q_NPA : 0.914

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	ASP	-1	-0.858	-0.909	3.854	-34.486	-33.602	-0.010	-0.320	-0.555	-0.001
4	A	5	ILE	0	0.005	0.006	6.172	6.237	6.237	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.914	0.945	8.333	20.917	20.917	0.000	0.000	0.000	0.000
6	A	7	HIS	0	0.030	0.031	7.789	-0.988	-0.988	0.000	0.000	0.000	0.000
7	A	8	ASN	0	-0.008	-0.007	11.904	1.466	1.466	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.910	0.933	15.298	17.309	17.309	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.815	-0.896	13.067	-20.070	-20.070	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.975	0.997	16.826	14.879	14.879	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.961	0.970	19.011	14.944	14.944	0.000	0.000	0.000	0.000
12	A	13	VAL	0	0.001	0.002	22.137	0.324	0.324	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.945	0.982	23.802	12.555	12.555	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.859	0.918	27.982	8.838	8.838	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.988	0.994	23.984	12.284	12.284	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.778	-0.888	30.708	-9.745	-9.745	0.000	0.000	0.000	0.000
17	A	18	PRO	0	-0.048	-0.011	34.189	-0.102	-0.102	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.954	0.965	32.868	9.249	9.249	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.014	0.008	36.983	-0.021	-0.021	0.000	0.000	0.000	0.000
20	A	21	GLN	0	0.110	0.038	39.465	-0.250	-0.250	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.896	-0.925	42.028	-6.781	-6.781	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.116	0.038	44.355	-0.156	-0.156	0.000	0.000	0.000	0.000
23	A	24	TYR	0	0.069	0.044	46.141	-0.070	-0.070	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.058	-0.033	41.710	-0.058	-0.058	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.871	0.912	36.190	8.053	8.053	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.032	0.033	42.601	-0.148	-0.148	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.008	-0.001	44.614	-0.073	-0.073	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.029	-0.028	38.023	-0.115	-0.115	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.954	0.989	40.294	7.218	7.218	0.000	0.000	0.000	0.000
30	A	31	LEU	0	0.064	0.048	41.413	-0.104	-0.104	0.000	0.000	0.000	0.000
31	A	32	TYR	0	0.002	-0.037	41.245	-0.090	-0.090	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.825	0.898	33.530	8.976	8.976	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.014	0.013	37.966	-0.238	-0.238	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.044	0.016	40.414	-0.105	-0.105	0.000	0.000	0.000	0.000
35	A	36	ALA	0	-0.058	-0.027	37.142	0.009	0.009	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.967	0.987	35.063	8.477	8.477	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.985	1.009	37.365	7.491	7.491	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.049	-0.023	40.339	0.238	0.238	0.000	0.000	0.000	0.000
39	A	40	ASN	0	0.062	0.040	40.182	-0.267	-0.267	0.000	0.000	0.000	0.000
40	A	41	SER	0	0.031	0.009	41.512	0.183	0.183	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.043	0.016	38.448	-0.043	-0.043	0.000	0.000	0.000	0.000
42	A	43	PHE	0	0.009	0.003	40.427	-0.112	-0.112	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.044	0.009	41.625	0.038	0.038	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.005	0.002	35.622	-0.196	-0.196	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.052	-0.025	37.804	-0.172	-0.172	0.000	0.000	0.000	0.000
46	A	47	VAL	0	0.000	0.004	39.630	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	48	LEU	0	0.017	0.017	36.261	-0.028	-0.028	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.952	0.975	33.487	8.858	8.858	0.000	0.000	0.000	0.000
49	A	50	ARG	1	0.820	0.888	36.865	7.223	7.223	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.027	0.022	39.875	0.035	0.035	0.000	0.000	0.000	0.000
51	A	52	PHE	0	0.070	0.038	33.649	0.026	0.026	0.000	0.000	0.000	0.000
52	A	53	MET	0	-0.052	-0.005	36.594	-0.126	-0.126	0.000	0.000	0.000	0.000
53	A	54	SER	0	0.046	0.017	37.546	0.154	0.154	0.000	0.000	0.000	0.000
54	A	55	ARG	1	1.026	1.003	39.560	6.703	6.703	0.000	0.000	0.000	0.000
55	A	56	THR	0	0.026	0.006	40.045	0.100	0.100	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.057	-0.028	36.679	0.110	0.110	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.884	0.946	40.781	7.324	7.324	0.000	0.000	0.000	0.000
58	A	59	PRO	0	0.003	0.013	43.787	0.100	0.100	0.000	0.000	0.000	0.000
59	A	60	PRO	0	-0.013	-0.010	46.863	-0.014	-0.014	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.007	-0.002	50.556	-0.032	-0.032	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.033	-0.017	52.191	0.013	0.013	0.000	0.000	0.000	0.000
62	A	63	LEU	0	0.073	0.030	55.896	-0.051	-0.051	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.013	-0.023	58.910	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.916	0.958	50.871	6.119	6.119	0.000	0.000	0.000	0.000
65	A	66	MET	0	-0.013	-0.009	55.606	-0.085	-0.085	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.029	0.017	56.487	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.974	0.990	57.575	5.416	5.416	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.900	0.939	52.190	5.947	5.947	0.000	0.000	0.000	0.000
69	A	70	MET	0	0.005	-0.004	55.795	-0.149	-0.149	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.981	1.009	58.240	5.057	5.057	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.024	0.001	55.069	0.011	0.011	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.102	0.049	58.790	0.014	0.014	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.074	0.046	58.681	-0.109	-0.109	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.804	0.911	51.595	5.945	5.945	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.869	-0.939	57.920	-5.071	-5.071	0.000	0.000	0.000	0.000
76	A	77	ASN	0	0.020	0.008	59.096	-0.051	-0.051	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.870	0.939	54.234	5.654	5.654	0.000	0.000	0.000	0.000
78	A	79	THR	0	0.026	0.024	53.327	0.101	0.101	0.000	0.000	0.000	0.000
79	A	80	ALA	0	-0.009	-0.011	53.111	-0.119	-0.119	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.024	-0.009	47.995	0.016	0.016	0.000	0.000	0.000	0.000
81	A	82	VAL	0	0.002	-0.009	48.579	-0.115	-0.115	0.000	0.000	0.000	0.000
82	A	83	VAL	0	0.006	0.003	43.248	0.039	0.039	0.000	0.000	0.000	0.000
83	A	84	GLY	0	-0.004	-0.022	45.334	-0.163	-0.163	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.092	-0.045	47.784	0.100	0.100	0.000	0.000	0.000	0.000
85	A	86	VAL	0	0.083	0.044	51.507	-0.054	-0.054	0.000	0.000	0.000	0.000
86	A	87	THR	0	-0.001	0.001	54.378	0.043	0.043	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.777	-0.886	56.967	-5.036	-5.036	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.816	-0.887	59.099	-5.553	-5.553	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.040	0.019	61.569	0.036	0.036	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.917	0.973	58.555	5.347	5.347	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.007	-0.012	62.612	-0.068	-0.068	0.000	0.000	0.000	0.000
92	A	93	GLN	0	0.055	0.049	65.740	-0.063	-0.063	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.868	-0.927	68.518	-4.548	-4.548	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.075	-0.045	64.259	-0.105	-0.105	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.023	-0.001	64.235	0.037	0.037	0.000	0.000	0.000	0.000
96	A	97	LYS	1	1.043	1.034	65.050	4.655	4.655	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.051	-0.024	59.503	-0.061	-0.061	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.904	0.950	57.019	5.589	5.589	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.002	-0.002	55.078	-0.093	-0.093	0.000	0.000	0.000	0.000
100	A	101	CYS	0	0.033	0.034	50.680	0.026	0.026	0.000	0.000	0.000	0.000
101	A	102	ALA	0	-0.030	-0.017	50.873	-0.133	-0.133	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.003	0.012	45.702	0.024	0.024	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.964	0.977	50.420	6.032	6.032	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.036	0.026	53.143	-0.039	-0.039	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.042	-0.043	56.033	0.074	0.074	0.000	0.000	0.000	0.000
106	A	107	SER	0	0.064	0.017	58.206	0.018	0.018	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.969	0.999	61.692	4.990	4.990	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.021	0.000	59.374	0.054	0.054	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.928	0.959	57.321	5.431	5.431	0.000	0.000	0.000	0.000
110	A	111	SER	0	0.044	0.021	62.525	0.056	0.056	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.821	0.900	63.776	4.988	4.988	0.000	0.000	0.000	0.000
112	A	113	ILE	0	0.015	-0.006	59.970	0.033	0.033	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.021	-0.011	62.237	0.017	0.017	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.910	0.962	65.604	4.650	4.650	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.019	0.027	66.503	0.061	0.061	0.000	0.000	0.000	0.000
116	A	117	GLY	0	0.064	0.043	68.172	0.019	0.019	0.000	0.000	0.000	0.000
117	A	118	GLY	0	-0.012	-0.008	63.822	-0.029	-0.029	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.939	0.967	60.762	5.065	5.065	0.000	0.000	0.000	0.000
119	A	120	ILE	0	-0.044	-0.041	56.782	-0.092	-0.092	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.017	0.025	54.871	0.044	0.044	0.000	0.000	0.000	0.000
121	A	122	THR	0	-0.005	-0.020	52.340	-0.079	-0.079	0.000	0.000	0.000	0.000
122	A	123	PHE	0	0.024	-0.019	46.208	-0.024	-0.024	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.858	-0.918	49.002	-6.189	-6.189	0.000	0.000	0.000	0.000
124	A	125	GLN	0	0.045	0.025	50.897	0.043	0.043	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.046	-0.038	49.104	0.048	0.048	0.000	0.000	0.000	0.000
126	A	127	ALA	0	-0.039	-0.015	48.457	-0.060	-0.060	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.050	0.018	49.731	-0.063	-0.063	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.817	-0.883	52.966	-5.568	-5.568	0.000	0.000	0.000	0.000
129	A	130	SER	0	-0.028	-0.022	51.081	0.054	0.054	0.000	0.000	0.000	0.000
130	A	131	PRO	0	0.040	0.031	48.784	-0.149	-0.149	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.978	0.987	45.773	6.724	6.724	0.000	0.000	0.000	0.000
132	A	133	GLY	0	-0.016	0.001	46.048	-0.152	-0.152	0.000	0.000	0.000	0.000
133	A	134	ARG	1	0.962	0.963	48.454	6.099	6.099	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.099	0.061	51.435	0.078	0.078	0.000	0.000	0.000	0.000
135	A	136	THR	0	-0.048	-0.024	48.950	0.082	0.082	0.000	0.000	0.000	0.000
136	A	137	VAL	0	0.037	0.022	50.649	-0.043	-0.043	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.018	-0.005	44.121	0.018	0.018	0.000	0.000	0.000	0.000
138	A	139	LEU	0	0.009	0.020	47.691	-0.062	-0.062	0.000	0.000	0.000	0.000
139	A	140	SER	0	0.024	-0.007	45.552	-0.209	-0.209	0.000	0.000	0.000	0.000
140	A	141	GLY	0	0.040	0.045	47.548	0.132	0.132	0.000	0.000	0.000	0.000
141	A	142	PRO	0	-0.028	-0.012	46.723	-0.168	-0.168	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.914	0.940	37.343	8.023	8.023	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.930	0.964	39.984	7.581	7.581	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.028	0.028	45.485	0.077	0.077	0.000	0.000	0.000	0.000
145	A	146	ARG	1	0.942	0.971	41.306	7.452	7.452	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.763	-0.883	46.708	-6.335	-6.335	0.000	0.000	0.000	0.000
147	A	148	VAL	0	-0.004	0.002	41.960	-0.026	-0.026	0.000	0.000	0.000	0.000
148	A	149	TYR	0	0.041	0.010	39.421	-0.151	-0.151	0.000	0.000	0.000	0.000
149	A	150	ARG	1	0.956	0.984	44.114	6.121	6.121	0.000	0.000	0.000	0.000
150	A	151	HIS	1	0.804	0.895	44.759	6.800	6.800	0.000	0.000	0.000	0.000
151	A	152	PHE	0	-0.022	-0.012	39.573	-0.142	-0.142	0.000	0.000	0.000	0.000
152	A	153	GLY	0	0.051	0.031	40.796	0.158	0.158	0.000	0.000	0.000	0.000
153	A	154	LYS	1	1.014	1.009	40.697	7.383	7.383	0.000	0.000	0.000	0.000
154	A	155	ALA	0	0.077	0.043	41.578	0.154	0.154	0.000	0.000	0.000	0.000
155	A	156	PRO	0	-0.018	0.002	43.392	0.068	0.068	0.000	0.000	0.000	0.000
156	A	157	GLY	0	-0.019	-0.029	46.486	0.153	0.153	0.000	0.000	0.000	0.000
157	A	158	THR	0	-0.030	-0.014	43.056	-0.113	-0.113	0.000	0.000	0.000	0.000
158	A	159	PRO	0	0.092	0.040	45.968	0.082	0.082	0.000	0.000	0.000	0.000
159	A	160	HIS	0	-0.001	0.006	46.786	-0.141	-0.141	0.000	0.000	0.000	0.000
160	A	161	SER	0	-0.045	-0.013	45.826	-0.159	-0.159	0.000	0.000	0.000	0.000
161	A	162	HIS	0	0.021	0.005	47.779	0.046	0.046	0.000	0.000	0.000	0.000
162	A	163	THR	0	-0.050	-0.019	44.881	0.056	0.056	0.000	0.000	0.000	0.000
163	A	164	LYS	1	0.867	0.942	47.909	6.193	6.193	0.000	0.000	0.000	0.000
164	A	165	PRO	0	0.073	0.034	47.997	-0.151	-0.151	0.000	0.000	0.000	0.000
165	A	166	TYR	0	-0.017	-0.028	43.115	0.107	0.107	0.000	0.000	0.000	0.000
166	A	167	VAL	0	-0.015	0.005	49.107	0.023	0.023	0.000	0.000	0.000	0.000
167	A	168	ARG	1	1.007	0.999	52.730	5.614	5.614	0.000	0.000	0.000	0.000
168	A	169	SER	0	0.077	0.040	54.516	0.065	0.065	0.000	0.000	0.000	0.000
169	A	170	LYS	1	0.895	0.949	57.685	5.365	5.365	0.000	0.000	0.000	0.000
170	A	171	GLY	0	0.074	0.022	59.284	0.051	0.051	0.000	0.000	0.000	0.000
171	A	172	ARG	1	1.001	1.003	62.879	4.762	4.762	0.000	0.000	0.000	0.000
172	A	173	LYS	1	0.969	0.983	62.282	4.993	4.993	0.000	0.000	0.000	0.000
173	A	174	PHE	0	0.050	0.023	57.626	-0.046	-0.046	0.000	0.000	0.000	0.000
174	A	175	GLU	-1	-0.789	-0.884	52.113	-6.119	-6.119	0.000	0.000	0.000	0.000
175	A	176	ARG	1	0.795	0.891	56.589	5.408	5.408	0.000	0.000	0.000	0.000
176	A	177	ALA	0	0.085	0.011	58.084	0.093	0.093	0.000	0.000	0.000	0.000
177	A	178	ARG	1	1.021	1.025	52.363	5.882	5.882	0.000	0.000	0.000	0.000
178	A	179	GLY	0	0.073	0.050	53.806	-0.098	-0.098	0.000	0.000	0.000	0.000
179	A	180	ARG	1	0.757	0.875	51.947	5.907	5.907	0.000	0.000	0.000	0.000
180	A	181	ARG	1	0.918	0.947	56.893	5.294	5.294	0.000	0.000	0.000	0.000
181	A	182	ALA	0	0.091	0.055	59.431	-0.036	-0.036	0.000	0.000	0.000	0.000
182	A	183	SER	0	0.054	0.035	60.446	-0.038	-0.038	0.000	0.000	0.000	0.000
183	A	184	ARG	1	0.880	0.951	59.925	5.075	5.075	0.000	0.000	0.000	0.000
184	A	185	GLY	0	0.057	0.025	57.719	-0.099	-0.099	0.000	0.000	0.000	0.000
185	A	186	TYR	0	0.032	0.021	51.379	-0.054	-0.054	0.000	0.000	0.000	0.000
186	A	187	LYS	1	0.807	0.894	54.807	5.763	5.763	0.000	0.000	0.000	0.000
187	A	188	ASN	-1	-0.800	-0.885	49.504	-6.008	-6.008	0.000	0.000	0.000	0.000

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