FMO DATABASE

FMODB ID: 9RZ32

Calculation Name: 3UMF-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3UMF

Chain ID: A

ChEMBL ID:

UniProt ID: G4V9S0

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	194
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2110277.757902
FMO2-HF: Nuclear repulsion	2032807.397731
FMO2-HF: Total energy	-77470.360171
FMO2-MP2: Total energy	-77694.187724

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:4:GLN)

Summations of interaction energy for fragment #1(A:4:GLN)

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.
-27.774	-25.177	18.838	-8.39	-13.048	-0.044

Interaction energy analysis for fragmet #1(A:4:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.833 / q_NPA : 0.900

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	6	LEU	0	0.006	0.001	1.730	2.291	3.690	7.853	-3.316	-5.936	-0.008
4	A	7	ALA	0	-0.009	0.001	3.280	-0.580	-0.285	-0.007	0.322	-0.611	-0.001
5	A	8	LYS	0	0.018	0.015	5.094	5.728	5.893	-0.001	-0.010	-0.153	0.000
75	A	78	LYS	1	0.886	0.941	2.219	21.103	21.008	3.548	-1.255	-2.199	0.019
79	A	82	ILE	0	-0.014	-0.011	3.754	-2.382	-1.902	0.007	-0.145	-0.342	0.001
107	A	110	VAL	0	-0.045	-0.016	3.255	-0.781	0.179	0.013	-0.391	-0.583	-0.002
108	A	111	CYS	0	0.001	-0.008	1.871	-25.533	-26.205	7.426	-3.572	-3.183	-0.053
109	A	112	PRO	0	0.015	0.007	4.507	4.278	4.343	-0.001	-0.023	-0.041	0.000
6	A	9	ALA	0	-0.037	-0.010	5.980	4.023	4.023	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.919	0.970	7.834	19.700	19.700	0.000	0.000	0.000	0.000
8	A	11	VAL	0	0.006	0.001	7.947	1.566	1.566	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.006	0.005	10.890	0.390	0.390	0.000	0.000	0.000	0.000
10	A	13	PHE	0	0.026	0.012	10.764	0.193	0.193	0.000	0.000	0.000	0.000
11	A	14	VAL	0	0.006	0.009	15.500	0.600	0.600	0.000	0.000	0.000	0.000
12	A	15	LEU	0	-0.009	-0.004	19.129	0.259	0.259	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.062	0.018	21.942	0.152	0.152	0.000	0.000	0.000	0.000
14	A	17	GLY	0	0.020	0.026	25.686	-0.061	-0.061	0.000	0.000	0.000	0.000
15	A	18	PRO	0	-0.027	-0.018	28.380	-0.014	-0.014	0.000	0.000	0.000	0.000
16	A	19	GLY	0	0.056	0.030	31.636	0.110	0.110	0.000	0.000	0.000	0.000
17	A	20	SER	0	-0.041	-0.020	28.160	0.011	0.011	0.000	0.000	0.000	0.000
18	A	21	GLY	0	0.035	0.012	29.750	-0.053	-0.053	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.893	0.932	22.741	11.492	11.492	0.000	0.000	0.000	0.000
20	A	23	GLY	0	0.024	0.025	25.089	-0.334	-0.334	0.000	0.000	0.000	0.000
21	A	24	THR	0	0.072	0.030	25.945	-0.190	-0.190	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.034	-0.020	25.898	-0.230	-0.230	0.000	0.000	0.000	0.000
23	A	26	CYS	0	-0.024	-0.006	21.729	-0.425	-0.425	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.900	-0.949	23.245	-10.473	-10.473	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.877	0.948	25.656	9.413	9.413	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.019	-0.006	21.328	-0.112	-0.112	0.000	0.000	0.000	0.000
27	A	30	VAL	0	-0.016	-0.004	20.256	-0.358	-0.358	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.040	-0.024	22.475	-0.028	-0.028	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.872	0.957	25.314	11.309	11.309	0.000	0.000	0.000	0.000
30	A	33	PHE	0	0.005	-0.003	20.703	0.128	0.128	0.000	0.000	0.000	0.000
31	A	34	HIS	0	-0.006	0.007	20.027	-1.174	-1.174	0.000	0.000	0.000	0.000
32	A	35	PHE	0	0.003	-0.001	16.951	-0.733	-0.733	0.000	0.000	0.000	0.000
33	A	36	ASN	0	-0.006	0.012	12.463	1.923	1.923	0.000	0.000	0.000	0.000
34	A	37	HIS	0	-0.056	-0.040	15.861	-0.187	-0.187	0.000	0.000	0.000	0.000
35	A	38	LEU	0	-0.002	0.002	11.842	0.068	0.068	0.000	0.000	0.000	0.000
36	A	39	SER	0	0.019	-0.008	15.984	0.092	0.092	0.000	0.000	0.000	0.000
37	A	40	SER	0	0.037	0.003	16.945	-0.191	-0.191	0.000	0.000	0.000	0.000
38	A	41	GLY	0	0.030	0.017	17.867	0.100	0.100	0.000	0.000	0.000	0.000
39	A	42	ASP	-1	-0.833	-0.904	19.583	-11.983	-11.983	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.026	-0.007	13.412	-0.023	-0.023	0.000	0.000	0.000	0.000
41	A	44	LEU	0	0.018	0.011	17.272	0.030	0.030	0.000	0.000	0.000	0.000
42	A	45	ARG	1	0.927	0.965	19.345	10.730	10.730	0.000	0.000	0.000	0.000
43	A	46	ALA	0	-0.031	-0.018	18.188	0.348	0.348	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.751	-0.859	16.774	-13.744	-13.744	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.017	0.004	19.320	0.331	0.331	0.000	0.000	0.000	0.000
46	A	49	GLN	0	-0.046	-0.026	22.908	0.678	0.678	0.000	0.000	0.000	0.000
47	A	50	SER	0	-0.006	0.000	20.274	0.211	0.211	0.000	0.000	0.000	0.000
48	A	51	GLY	0	-0.008	0.003	22.366	0.114	0.114	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.036	-0.034	19.988	0.389	0.389	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.008	-0.022	22.015	0.235	0.235	0.000	0.000	0.000	0.000
51	A	54	LYS	1	0.904	0.958	14.760	15.140	15.140	0.000	0.000	0.000	0.000
52	A	55	GLY	0	0.052	0.033	21.039	0.081	0.081	0.000	0.000	0.000	0.000
53	A	56	LYS	1	0.903	0.948	22.287	10.146	10.146	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.799	-0.876	23.643	-9.571	-9.571	0.000	0.000	0.000	0.000
55	A	58	LEU	0	0.000	-0.012	18.735	0.095	0.095	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.891	0.941	23.411	9.100	9.100	0.000	0.000	0.000	0.000
57	A	60	ALA	0	0.003	0.002	26.542	0.259	0.259	0.000	0.000	0.000	0.000
58	A	61	MET	0	-0.013	0.001	22.578	0.021	0.021	0.000	0.000	0.000	0.000
59	A	62	MET	0	-0.043	-0.025	22.433	0.184	0.184	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.950	-0.960	27.597	-8.267	-8.267	0.000	0.000	0.000	0.000
61	A	64	ARG	1	0.767	0.849	28.122	9.519	9.519	0.000	0.000	0.000	0.000
62	A	65	GLY	0	-0.022	0.004	30.342	0.153	0.153	0.000	0.000	0.000	0.000
63	A	66	GLU	-1	-0.880	-0.932	26.868	-9.541	-9.541	0.000	0.000	0.000	0.000
64	A	67	LEU	0	-0.026	-0.019	23.697	-0.192	-0.192	0.000	0.000	0.000	0.000
65	A	68	VAL	0	0.002	0.001	19.022	-0.134	-0.134	0.000	0.000	0.000	0.000
66	A	69	PRO	0	0.017	0.008	18.123	-0.275	-0.275	0.000	0.000	0.000	0.000
67	A	70	LEU	0	0.032	0.022	14.140	-0.346	-0.346	0.000	0.000	0.000	0.000
68	A	71	GLU	-1	-0.823	-0.929	13.019	-15.614	-15.614	0.000	0.000	0.000	0.000
69	A	72	VAL	0	-0.014	-0.001	12.553	-0.754	-0.754	0.000	0.000	0.000	0.000
70	A	73	VAL	0	0.010	-0.002	13.587	-0.423	-0.423	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.019	-0.009	8.927	-0.681	-0.681	0.000	0.000	0.000	0.000
72	A	75	ALA	0	-0.004	0.003	8.813	-1.408	-1.408	0.000	0.000	0.000	0.000
73	A	76	LEU	0	0.008	0.007	9.214	-0.830	-0.830	0.000	0.000	0.000	0.000
74	A	77	LEU	0	-0.008	-0.004	9.831	-0.423	-0.423	0.000	0.000	0.000	0.000
76	A	79	GLU	-1	-0.968	-0.979	6.522	-19.736	-19.736	0.000	0.000	0.000	0.000
77	A	80	ALA	0	0.010	-0.006	8.734	-0.709	-0.709	0.000	0.000	0.000	0.000
78	A	81	MET	0	-0.015	-0.010	6.197	0.072	0.072	0.000	0.000	0.000	0.000
80	A	83	LYS	1	0.933	0.971	6.963	16.821	16.821	0.000	0.000	0.000	0.000
81	A	84	LEU	0	0.008	0.002	10.091	1.449	1.449	0.000	0.000	0.000	0.000
82	A	85	VAL	0	-0.026	-0.009	6.373	0.749	0.749	0.000	0.000	0.000	0.000
83	A	86	ASP	-1	-0.830	-0.910	9.573	-28.508	-28.508	0.000	0.000	0.000	0.000
84	A	87	LYS	1	0.817	0.920	11.853	17.793	17.793	0.000	0.000	0.000	0.000
85	A	88	ASN	0	0.039	0.001	13.305	0.497	0.497	0.000	0.000	0.000	0.000
86	A	89	CYS	0	0.023	0.027	10.885	-0.432	-0.432	0.000	0.000	0.000	0.000
87	A	90	HIS	0	-0.023	-0.011	11.089	-1.605	-1.605	0.000	0.000	0.000	0.000
88	A	91	PHE	0	-0.012	-0.007	9.472	0.530	0.530	0.000	0.000	0.000	0.000
89	A	92	LEU	0	0.015	0.026	13.278	-0.145	-0.145	0.000	0.000	0.000	0.000
90	A	93	ILE	0	-0.007	-0.013	11.140	0.031	0.031	0.000	0.000	0.000	0.000
91	A	94	ASP	-1	-0.812	-0.892	15.044	-11.977	-11.977	0.000	0.000	0.000	0.000
92	A	95	GLY	0	-0.061	-0.026	18.719	0.254	0.254	0.000	0.000	0.000	0.000
93	A	96	TYR	0	-0.047	-0.024	12.259	0.478	0.478	0.000	0.000	0.000	0.000
94	A	97	PRO	0	-0.001	0.011	14.502	-0.271	-0.271	0.000	0.000	0.000	0.000
95	A	98	ARG	1	0.977	0.960	16.496	11.807	11.807	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.863	-0.934	18.786	-11.257	-11.257	0.000	0.000	0.000	0.000
97	A	100	LEU	0	0.034	-0.004	17.650	-0.640	-0.640	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.827	-0.920	16.202	-14.739	-14.739	0.000	0.000	0.000	0.000
99	A	102	GLN	0	0.014	0.006	14.263	-1.235	-1.235	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.032	0.022	12.733	-1.042	-1.042	0.000	0.000	0.000	0.000
101	A	104	ILE	0	0.026	0.014	11.500	-1.507	-1.507	0.000	0.000	0.000	0.000
102	A	105	LYS	1	0.849	0.922	10.861	13.678	13.678	0.000	0.000	0.000	0.000
103	A	106	PHE	0	0.036	0.012	7.459	-1.413	-1.413	0.000	0.000	0.000	0.000
104	A	107	GLU	-1	-0.773	-0.870	6.667	-23.858	-23.858	0.000	0.000	0.000	0.000
105	A	108	LYS	1	0.804	0.921	6.925	19.239	19.239	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.841	-0.915	5.859	-25.857	-25.857	0.000	0.000	0.000	0.000
110	A	113	CYS	0	-0.093	-0.022	8.266	-0.530	-0.530	0.000	0.000	0.000	0.000
111	A	114	LEU	0	-0.008	-0.001	10.883	0.055	0.055	0.000	0.000	0.000	0.000
112	A	115	CYS	0	-0.036	-0.018	13.318	0.863	0.863	0.000	0.000	0.000	0.000
113	A	116	VAL	0	0.013	0.001	15.537	-0.572	-0.572	0.000	0.000	0.000	0.000
114	A	117	ILE	0	0.022	0.017	17.998	0.597	0.597	0.000	0.000	0.000	0.000
115	A	118	ASN	0	0.004	-0.005	21.062	-0.097	-0.097	0.000	0.000	0.000	0.000
116	A	119	PHE	0	-0.026	-0.023	23.222	0.328	0.328	0.000	0.000	0.000	0.000
117	A	120	ASP	-1	-0.905	-0.955	26.718	-9.378	-9.378	0.000	0.000	0.000	0.000
118	A	121	VAL	0	-0.034	-0.027	29.289	0.205	0.205	0.000	0.000	0.000	0.000
119	A	122	SER	0	0.040	0.009	32.866	-0.085	-0.085	0.000	0.000	0.000	0.000
120	A	123	GLU	-1	-0.730	-0.822	35.685	-7.389	-7.389	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.816	-0.908	37.510	-7.413	-7.413	0.000	0.000	0.000	0.000
122	A	125	VAL	0	-0.038	-0.010	35.793	0.116	0.116	0.000	0.000	0.000	0.000
123	A	126	MET	0	-0.007	0.012	34.813	0.060	0.060	0.000	0.000	0.000	0.000
124	A	127	ARG	1	0.848	0.890	36.846	7.063	7.063	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.923	0.967	40.162	7.390	7.390	0.000	0.000	0.000	0.000
126	A	129	ARG	1	0.783	0.889	33.601	8.442	8.442	0.000	0.000	0.000	0.000
127	A	130	LEU	0	-0.041	-0.026	34.488	-0.072	-0.072	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.023	0.016	39.000	0.059	0.059	0.000	0.000	0.000	0.000
129	A	132	LYS	1	0.867	0.933	42.317	6.383	6.383	0.000	0.000	0.000	0.000
130	A	133	ARG	1	0.798	0.871	46.054	6.014	6.014	0.000	0.000	0.000	0.000
131	A	134	ALA	0	0.020	0.028	44.577	0.080	0.080	0.000	0.000	0.000	0.000
132	A	135	GLU	-1	-0.839	-0.888	46.698	-5.653	-5.653	0.000	0.000	0.000	0.000
133	A	136	THR	0	0.006	-0.024	50.350	0.021	0.021	0.000	0.000	0.000	0.000
134	A	137	SER	0	-0.017	-0.007	52.827	0.087	0.087	0.000	0.000	0.000	0.000
135	A	138	ASN	0	-0.055	-0.018	47.110	0.101	0.101	0.000	0.000	0.000	0.000
136	A	139	ARG	1	0.953	0.970	48.979	5.881	5.881	0.000	0.000	0.000	0.000
137	A	140	VAL	0	-0.045	-0.024	45.359	-0.021	-0.021	0.000	0.000	0.000	0.000
138	A	141	ASP	-1	-0.800	-0.896	45.291	-6.363	-6.363	0.000	0.000	0.000	0.000
139	A	142	ASP	-1	-0.819	-0.896	44.870	-6.517	-6.517	0.000	0.000	0.000	0.000
140	A	143	ASN	0	-0.008	-0.016	41.647	-0.259	-0.259	0.000	0.000	0.000	0.000
141	A	144	GLU	-1	-0.782	-0.911	40.415	-6.746	-6.746	0.000	0.000	0.000	0.000
142	A	145	GLU	-1	-0.773	-0.886	40.369	-7.099	-7.099	0.000	0.000	0.000	0.000
143	A	146	THR	0	-0.050	-0.031	37.265	-0.193	-0.193	0.000	0.000	0.000	0.000
144	A	147	ILE	0	-0.047	-0.027	35.490	-0.297	-0.297	0.000	0.000	0.000	0.000
145	A	148	VAL	0	0.000	0.006	35.638	-0.250	-0.250	0.000	0.000	0.000	0.000
146	A	149	LYS	1	0.844	0.913	36.233	6.899	6.899	0.000	0.000	0.000	0.000
147	A	150	ARG	1	0.966	1.000	31.268	8.178	8.178	0.000	0.000	0.000	0.000
148	A	151	PHE	0	-0.015	-0.015	31.432	-0.304	-0.304	0.000	0.000	0.000	0.000
149	A	152	ARG	1	0.877	0.898	31.659	7.162	7.162	0.000	0.000	0.000	0.000
150	A	153	THR	0	-0.005	-0.010	29.604	-0.134	-0.134	0.000	0.000	0.000	0.000
151	A	154	PHE	0	-0.020	-0.004	24.158	-0.262	-0.262	0.000	0.000	0.000	0.000
152	A	155	ASN	0	0.003	0.007	27.083	-0.255	-0.255	0.000	0.000	0.000	0.000
153	A	156	GLU	-1	-0.832	-0.902	28.179	-9.114	-9.114	0.000	0.000	0.000	0.000
154	A	157	LEU	0	-0.025	-0.006	23.987	-0.165	-0.165	0.000	0.000	0.000	0.000
155	A	158	THR	0	0.000	-0.018	22.697	-0.350	-0.350	0.000	0.000	0.000	0.000
156	A	159	LYS	1	0.826	0.912	23.531	8.558	8.558	0.000	0.000	0.000	0.000
157	A	160	PRO	0	0.023	0.011	23.049	-0.226	-0.226	0.000	0.000	0.000	0.000
158	A	161	VAL	0	-0.018	-0.006	17.755	-0.397	-0.397	0.000	0.000	0.000	0.000
159	A	162	ILE	0	0.005	-0.004	19.838	-0.503	-0.503	0.000	0.000	0.000	0.000
160	A	163	GLU	-1	-0.870	-0.933	22.151	-11.065	-11.065	0.000	0.000	0.000	0.000
161	A	164	HIS	0	-0.006	0.003	15.314	-0.227	-0.227	0.000	0.000	0.000	0.000
162	A	165	TYR	0	-0.040	-0.064	13.096	-0.061	-0.061	0.000	0.000	0.000	0.000
163	A	166	LYS	1	0.925	0.969	19.026	10.541	10.541	0.000	0.000	0.000	0.000
164	A	167	GLN	0	-0.037	-0.023	22.049	-0.201	-0.201	0.000	0.000	0.000	0.000
165	A	168	GLN	0	-0.056	-0.025	15.111	-0.758	-0.758	0.000	0.000	0.000	0.000
166	A	169	ASN	0	-0.036	-0.013	19.465	-0.065	-0.065	0.000	0.000	0.000	0.000
167	A	170	LYS	1	0.888	0.944	12.721	20.131	20.131	0.000	0.000	0.000	0.000
168	A	171	VAL	0	-0.062	-0.021	18.954	-0.235	-0.235	0.000	0.000	0.000	0.000
169	A	172	ILE	0	0.005	0.011	20.778	0.536	0.536	0.000	0.000	0.000	0.000
170	A	173	THR	0	-0.017	-0.016	23.130	0.040	0.040	0.000	0.000	0.000	0.000
171	A	174	ILE	0	-0.060	-0.028	25.582	0.190	0.190	0.000	0.000	0.000	0.000
172	A	175	ASP	-1	-0.784	-0.857	28.136	-8.481	-8.481	0.000	0.000	0.000	0.000
173	A	176	ALA	0	0.018	-0.001	29.753	0.011	0.011	0.000	0.000	0.000	0.000
174	A	177	SER	0	-0.059	-0.055	31.817	0.244	0.244	0.000	0.000	0.000	0.000
175	A	178	GLY	0	-0.003	0.005	35.149	0.245	0.245	0.000	0.000	0.000	0.000
176	A	179	THR	0	0.022	-0.007	36.187	-0.080	-0.080	0.000	0.000	0.000	0.000
177	A	180	VAL	0	0.049	0.010	31.866	-0.194	-0.194	0.000	0.000	0.000	0.000
178	A	181	ASP	-1	-0.863	-0.927	32.160	-8.947	-8.947	0.000	0.000	0.000	0.000
179	A	182	ALA	0	0.048	0.026	32.965	-0.222	-0.222	0.000	0.000	0.000	0.000
180	A	183	ILE	0	-0.034	-0.010	29.160	-0.228	-0.228	0.000	0.000	0.000	0.000
181	A	184	PHE	0	0.012	0.007	26.209	-0.309	-0.309	0.000	0.000	0.000	0.000
182	A	185	ASP	-1	-0.891	-0.948	28.441	-9.738	-9.738	0.000	0.000	0.000	0.000
183	A	186	LYS	1	0.840	0.915	29.239	9.730	9.730	0.000	0.000	0.000	0.000
184	A	187	VAL	0	0.024	-0.006	23.720	-0.310	-0.310	0.000	0.000	0.000	0.000
185	A	188	ASN	0	0.009	-0.006	24.865	-0.854	-0.854	0.000	0.000	0.000	0.000
186	A	189	HIS	0	-0.069	-0.037	25.574	-0.170	-0.170	0.000	0.000	0.000	0.000
187	A	190	GLU	-1	-0.790	-0.862	24.785	-10.939	-10.939	0.000	0.000	0.000	0.000
188	A	191	LEU	0	0.041	0.008	19.343	-0.481	-0.481	0.000	0.000	0.000	0.000
189	A	192	GLN	0	0.013	0.016	21.145	-0.466	-0.466	0.000	0.000	0.000	0.000
190	A	193	LYS	1	0.798	0.882	23.130	10.952	10.952	0.000	0.000	0.000	0.000
191	A	194	PHE	0	0.001	0.006	17.235	-0.266	-0.266	0.000	0.000	0.000	0.000
192	A	195	GLY	0	0.006	0.010	17.647	-1.032	-1.032	0.000	0.000	0.000	0.000
193	A	196	VAL	0	-0.087	-0.056	17.270	-0.975	-0.975	0.000	0.000	0.000	0.000
194	A	197	LYS	0	0.059	0.036	19.999	-1.100	-1.100	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:4:GLN)