FMO DATABASE

FMODB ID: 7YK9K

Calculation Name: 1CJB-A-Xray547

Preferred Name: Hypoxanthine-guanine-xanthine phosphoribosyltransferase

Target Type: SINGLE PROTEIN

Ligand Name: (1s)-1(9-deazahypoxanthin-9yl)1,4-dideoxy-1,4-imino-d-ribitol-5-phosphate | pyrophosphate 2-

Ligand 3-letter code: IRP | POP

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1CJB

Chain ID: A

ChEMBL ID: CHEMBL3988608

UniProt ID: P20035

Base Structure: X-ray

Registration Date: 2025-09-02

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	227
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2900142.231441
FMO2-HF: Nuclear repulsion	2809566.15699
FMO2-HF: Total energy	-90576.074452
FMO2-MP2: Total energy	-90841.161655

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:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-37.517	-35.044	0.041	-1.012	-1.5	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / 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	4	PRO	0	0.022	0.016	3.236	-4.682	-2.721	0.044	-0.927	-1.077	-0.004
11	A	12	ASN	0	-0.057	-0.035	4.679	-1.246	-1.027	-0.001	-0.017	-0.201	0.000
63	A	64	VAL	0	-0.049	-0.010	4.048	-3.439	-3.212	-0.001	-0.053	-0.173	0.000
64	A	65	TYR	0	0.019	-0.002	4.426	-7.387	-7.321	-0.001	-0.015	-0.049	0.000
4	A	5	ASN	0	0.020	0.008	5.761	5.242	5.242	0.000	0.000	0.000	0.000
5	A	6	ASN	0	-0.017	-0.004	7.798	3.961	3.961	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.034	0.005	10.317	0.380	0.380	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.017	0.010	13.085	1.224	1.224	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.019	-0.009	10.907	1.056	1.056	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.009	0.007	10.455	0.602	0.602	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.906	-0.950	6.605	-36.459	-36.459	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.014	0.023	7.108	-1.706	-1.706	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.097	-0.042	7.742	0.812	0.812	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.856	-0.921	11.504	-18.563	-18.563	0.000	0.000	0.000	0.000
15	A	16	PRO	0	-0.075	-0.031	15.251	0.046	0.046	0.000	0.000	0.000	0.000
16	A	17	VAL	0	-0.012	-0.015	17.786	0.458	0.458	0.000	0.000	0.000	0.000
17	A	18	PHE	0	0.013	-0.006	20.984	0.033	0.033	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.007	0.016	23.275	0.360	0.360	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.011	-0.019	26.645	-0.348	-0.348	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.830	-0.925	29.236	-10.520	-10.520	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.907	-0.952	31.854	-8.692	-8.692	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.839	-0.894	29.469	-10.339	-10.339	0.000	0.000	0.000	0.000
23	A	24	GLY	0	-0.030	-0.022	32.607	0.005	0.005	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.036	-0.027	31.410	0.006	0.006	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.829	-0.905	36.647	-7.748	-7.748	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.049	-0.038	38.735	-0.104	-0.104	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.875	-0.928	40.787	-7.108	-7.108	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.026	-0.003	38.925	0.080	0.080	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.028	-0.023	34.636	-0.204	-0.204	0.000	0.000	0.000	0.000
30	A	31	MET	0	0.005	0.008	38.494	0.221	0.221	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.031	0.024	37.260	-0.259	-0.259	0.000	0.000	0.000	0.000
32	A	33	PRO	0	0.007	0.002	39.249	0.232	0.232	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.045	0.018	42.401	0.010	0.010	0.000	0.000	0.000	0.000
34	A	35	HIS	0	0.001	0.003	42.488	0.205	0.205	0.000	0.000	0.000	0.000
35	A	36	TYR	0	-0.020	-0.063	38.947	0.132	0.132	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.896	0.954	42.496	7.042	7.042	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.925	0.955	43.598	6.743	6.743	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.022	0.003	42.399	0.091	0.091	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.021	0.018	37.260	-0.203	-0.203	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.016	-0.014	38.318	0.171	0.171	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.912	0.959	34.569	9.241	9.241	0.000	0.000	0.000	0.000
42	A	43	VAL	0	-0.010	-0.012	32.912	-0.188	-0.188	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.012	-0.005	28.866	0.040	0.040	0.000	0.000	0.000	0.000
44	A	45	VAL	0	0.028	-0.005	25.995	-0.191	-0.191	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.033	0.021	29.388	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	47	ASN	0	-0.021	-0.024	28.975	-0.643	-0.643	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.019	0.003	27.979	-0.386	-0.386	0.000	0.000	0.000	0.000
48	A	49	VAL	0	0.037	0.017	25.408	-0.419	-0.419	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.004	0.005	24.165	-0.684	-0.684	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.866	0.917	23.057	10.411	10.411	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.041	0.017	22.944	-0.476	-0.476	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.782	0.905	15.740	17.453	17.453	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.001	-0.003	18.422	-1.047	-1.047	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.863	-0.912	18.165	-14.756	-14.756	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.836	0.907	13.364	20.671	20.671	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.021	0.003	14.033	-1.449	-1.449	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.022	0.015	13.326	-1.749	-1.749	0.000	0.000	0.000	0.000
58	A	59	TYR	0	0.032	0.013	13.553	-1.814	-1.814	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.791	-0.887	10.182	-26.035	-26.035	0.000	0.000	0.000	0.000
60	A	61	ILE	0	0.019	0.015	8.951	-3.513	-3.513	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.838	0.903	9.221	19.522	19.522	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.786	0.890	7.827	27.708	27.708	0.000	0.000	0.000	0.000
65	A	66	ASN	0	-0.016	0.000	7.008	3.799	3.799	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.001	-0.012	8.683	3.353	3.353	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.952	-0.961	7.775	-26.660	-26.660	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.783	-0.856	10.048	-18.114	-18.114	0.000	0.000	0.000	0.000
69	A	70	PHE	0	-0.026	-0.020	10.938	-0.786	-0.786	0.000	0.000	0.000	0.000
70	A	71	HIS	0	-0.008	-0.022	13.047	2.058	2.058	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.009	-0.002	15.743	-0.600	-0.600	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.007	-0.010	17.363	1.118	1.118	0.000	0.000	0.000	0.000
73	A	74	CYS	0	-0.058	-0.009	19.530	-0.047	-0.047	0.000	0.000	0.000	0.000
74	A	75	LEU	0	0.057	0.034	20.863	0.534	0.534	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.028	0.017	24.016	0.339	0.339	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.836	0.877	27.689	9.382	9.382	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.055	0.033	27.509	0.033	0.033	0.000	0.000	0.000	0.000
78	A	79	SER	0	0.023	0.003	22.357	-0.040	-0.040	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.980	0.998	24.010	10.205	10.205	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.010	0.012	26.115	-0.040	-0.040	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.004	-0.006	16.871	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.079	0.022	20.752	-0.380	-0.380	0.000	0.000	0.000	0.000
83	A	84	THR	0	-0.018	-0.021	22.103	-0.146	-0.146	0.000	0.000	0.000	0.000
84	A	85	ALA	0	-0.040	-0.015	23.312	0.036	0.036	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.016	0.007	15.857	-0.212	-0.212	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.060	0.033	19.182	-0.617	-0.617	0.000	0.000	0.000	0.000
87	A	88	LYS	1	0.912	0.982	20.860	11.803	11.803	0.000	0.000	0.000	0.000
88	A	89	HIS	0	-0.047	-0.019	19.599	0.092	0.092	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.011	0.005	14.081	-0.314	-0.314	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.012	-0.017	17.561	-0.291	-0.291	0.000	0.000	0.000	0.000
91	A	92	ARG	1	0.835	0.921	20.132	13.358	13.358	0.000	0.000	0.000	0.000
92	A	93	ILE	0	0.007	-0.004	15.880	0.116	0.116	0.000	0.000	0.000	0.000
93	A	94	HIS	0	0.004	0.023	14.935	-1.239	-1.239	0.000	0.000	0.000	0.000
94	A	95	ASN	0	0.020	-0.013	17.228	-0.159	-0.159	0.000	0.000	0.000	0.000
95	A	96	TYR	0	-0.050	-0.032	20.749	0.685	0.685	0.000	0.000	0.000	0.000
96	A	97	SER	0	-0.060	-0.030	16.765	-0.115	-0.115	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.041	0.007	18.395	-0.433	-0.433	0.000	0.000	0.000	0.000
98	A	99	VAL	0	0.026	0.001	19.733	0.666	0.666	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.943	-0.973	21.829	-11.779	-11.779	0.000	0.000	0.000	0.000
100	A	101	THR	0	0.039	0.021	21.411	-0.232	-0.232	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.058	-0.021	18.042	-0.624	-0.624	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.953	0.971	16.922	16.084	16.084	0.000	0.000	0.000	0.000
103	A	104	PRO	0	0.033	0.010	17.720	-0.520	-0.520	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.008	0.015	11.529	-0.447	-0.447	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.000	-0.014	14.053	-1.277	-1.277	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.020	0.027	16.320	1.106	1.106	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.922	-0.957	18.395	-14.013	-14.013	0.000	0.000	0.000	0.000
108	A	109	HIS	1	0.837	0.888	19.605	14.947	14.947	0.000	0.000	0.000	0.000
109	A	110	TYR	0	-0.037	-0.024	22.623	-0.291	-0.291	0.000	0.000	0.000	0.000
110	A	111	VAL	0	0.028	0.008	22.893	0.321	0.321	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.862	0.944	25.723	10.009	10.009	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.045	0.021	24.702	0.159	0.159	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.875	0.951	28.132	9.407	9.407	0.000	0.000	0.000	0.000
114	A	115	SER	0	0.110	0.049	28.657	-0.080	-0.080	0.000	0.000	0.000	0.000
115	A	116	TYR	0	0.012	0.022	28.703	0.089	0.089	0.000	0.000	0.000	0.000
116	A	117	CYS	0	-0.044	-0.021	33.201	0.184	0.184	0.000	0.000	0.000	0.000
117	A	118	ASN	0	0.036	0.021	36.966	0.151	0.151	0.000	0.000	0.000	0.000
118	A	119	ASP	-1	-0.830	-0.909	34.999	-8.763	-8.763	0.000	0.000	0.000	0.000
119	A	120	GLN	0	-0.003	0.001	33.658	-0.392	-0.392	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.013	0.003	30.397	0.043	0.043	0.000	0.000	0.000	0.000
121	A	122	THR	0	0.012	-0.009	32.508	0.101	0.101	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.042	-0.015	31.791	0.161	0.161	0.000	0.000	0.000	0.000
123	A	124	THR	0	-0.029	-0.020	31.745	-0.270	-0.270	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.036	-0.047	25.863	-0.359	-0.359	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.929	-0.941	30.435	-9.189	-9.189	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.006	-0.020	25.388	-0.362	-0.362	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.005	0.001	29.134	0.312	0.312	0.000	0.000	0.000	0.000
128	A	129	SER	0	-0.051	-0.044	26.149	-0.319	-0.319	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.808	-0.875	24.820	-12.135	-12.135	0.000	0.000	0.000	0.000
130	A	131	ASP	-1	-0.808	-0.865	26.310	-11.736	-11.736	0.000	0.000	0.000	0.000
131	A	132	LEU	0	0.029	0.006	21.583	-0.352	-0.352	0.000	0.000	0.000	0.000
132	A	133	SER	0	-0.044	-0.044	21.340	-0.730	-0.730	0.000	0.000	0.000	0.000
133	A	134	CYS	0	-0.060	-0.032	21.896	-0.504	-0.504	0.000	0.000	0.000	0.000
134	A	135	LEU	0	-0.011	-0.014	17.368	-0.474	-0.474	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.874	0.945	16.746	12.779	12.779	0.000	0.000	0.000	0.000
136	A	137	GLY	0	-0.020	-0.014	15.167	0.178	0.178	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.790	0.883	14.141	15.949	15.949	0.000	0.000	0.000	0.000
138	A	139	HIS	0	0.034	0.009	7.557	-0.622	-0.622	0.000	0.000	0.000	0.000
139	A	140	VAL	0	-0.001	-0.012	11.387	1.554	1.554	0.000	0.000	0.000	0.000
140	A	141	LEU	0	-0.025	-0.010	11.475	-1.906	-1.906	0.000	0.000	0.000	0.000
141	A	142	ILE	0	-0.007	0.000	13.634	1.782	1.782	0.000	0.000	0.000	0.000
142	A	143	VAL	0	-0.023	-0.010	15.936	-0.837	-0.837	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.833	-0.941	18.484	-12.996	-12.996	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-0.827	-0.930	20.511	-12.891	-12.891	0.000	0.000	0.000	0.000
145	A	146	ILE	0	-0.030	-0.036	22.544	-0.274	-0.274	0.000	0.000	0.000	0.000
146	A	147	ILE	0	-0.015	0.005	17.824	0.164	0.164	0.000	0.000	0.000	0.000
147	A	148	ASP	-1	-0.786	-0.896	22.314	-10.981	-10.981	0.000	0.000	0.000	0.000
148	A	149	THR	0	0.029	-0.003	24.897	-0.366	-0.366	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.031	0.028	22.536	-0.152	-0.152	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.926	0.954	22.647	10.108	10.108	0.000	0.000	0.000	0.000
151	A	152	THR	0	0.020	0.008	24.040	0.178	0.178	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.071	0.036	17.984	-0.050	-0.050	0.000	0.000	0.000	0.000
153	A	154	VAL	0	0.017	0.028	19.761	-0.421	-0.421	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.894	0.952	20.814	11.014	11.014	0.000	0.000	0.000	0.000
155	A	156	PHE	0	0.030	0.012	19.562	0.142	0.142	0.000	0.000	0.000	0.000
156	A	157	CYS	0	0.000	-0.003	16.864	-0.526	-0.526	0.000	0.000	0.000	0.000
157	A	158	GLU	-1	-0.819	-0.897	18.577	-14.934	-14.934	0.000	0.000	0.000	0.000
158	A	159	TYR	0	-0.065	-0.039	20.943	0.471	0.471	0.000	0.000	0.000	0.000
159	A	160	LEU	0	0.043	0.008	16.786	0.146	0.146	0.000	0.000	0.000	0.000
160	A	161	LYS	1	0.821	0.909	16.827	15.686	15.686	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.903	0.963	18.436	12.734	12.734	0.000	0.000	0.000	0.000
162	A	163	PHE	0	-0.008	0.000	19.820	0.567	0.567	0.000	0.000	0.000	0.000
163	A	164	GLU	-1	-0.917	-0.952	17.482	-14.005	-14.005	0.000	0.000	0.000	0.000
164	A	165	ILE	0	0.005	0.012	13.263	-0.145	-0.145	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.925	0.983	9.291	24.498	24.498	0.000	0.000	0.000	0.000
166	A	167	THR	0	-0.037	-0.028	7.030	-2.008	-2.008	0.000	0.000	0.000	0.000
167	A	168	VAL	0	-0.002	-0.003	9.600	1.847	1.847	0.000	0.000	0.000	0.000
168	A	169	ALA	0	0.020	0.028	8.767	-1.637	-1.637	0.000	0.000	0.000	0.000
169	A	170	ILE	0	-0.047	-0.029	10.736	2.679	2.679	0.000	0.000	0.000	0.000
170	A	171	ALA	0	0.026	0.012	12.620	-1.357	-1.357	0.000	0.000	0.000	0.000
171	A	172	CYS	0	-0.050	-0.024	14.650	1.366	1.366	0.000	0.000	0.000	0.000
172	A	173	LEU	0	-0.019	0.013	17.868	-0.356	-0.356	0.000	0.000	0.000	0.000
173	A	174	PHE	0	0.009	-0.017	20.370	0.130	0.130	0.000	0.000	0.000	0.000
174	A	175	ILE	0	0.023	0.016	19.226	-0.413	-0.413	0.000	0.000	0.000	0.000
175	A	176	LYS	1	0.824	0.920	21.612	11.030	11.030	0.000	0.000	0.000	0.000
176	A	177	ARG	1	0.761	0.862	24.647	11.654	11.654	0.000	0.000	0.000	0.000
177	A	178	THR	0	-0.032	-0.023	26.319	0.463	0.463	0.000	0.000	0.000	0.000
178	A	179	PRO	0	-0.014	-0.010	27.257	-0.398	-0.398	0.000	0.000	0.000	0.000
179	A	180	LEU	0	-0.017	-0.014	29.160	0.053	0.053	0.000	0.000	0.000	0.000
180	A	181	TRP	0	-0.055	-0.011	18.658	-0.131	-0.131	0.000	0.000	0.000	0.000
181	A	182	ASN	0	-0.035	-0.025	22.077	-0.417	-0.417	0.000	0.000	0.000	0.000
182	A	183	GLY	0	0.042	0.026	20.699	-0.211	-0.211	0.000	0.000	0.000	0.000
183	A	184	PHE	0	-0.024	0.007	16.303	-1.059	-1.059	0.000	0.000	0.000	0.000
184	A	185	LYS	1	0.896	0.939	14.207	19.325	19.325	0.000	0.000	0.000	0.000
185	A	186	ALA	0	-0.017	-0.013	14.116	-0.339	-0.339	0.000	0.000	0.000	0.000
186	A	187	ASP	-1	-0.797	-0.909	8.500	-31.235	-31.235	0.000	0.000	0.000	0.000
187	A	188	PHE	0	-0.010	-0.015	7.727	-1.447	-1.447	0.000	0.000	0.000	0.000
188	A	189	VAL	0	0.054	0.024	12.138	1.490	1.490	0.000	0.000	0.000	0.000
189	A	190	GLY	0	0.023	0.018	15.666	-0.053	-0.053	0.000	0.000	0.000	0.000
190	A	191	PHE	0	-0.016	-0.013	18.616	-0.045	-0.045	0.000	0.000	0.000	0.000
191	A	192	SER	0	0.014	0.024	21.004	0.028	0.028	0.000	0.000	0.000	0.000
192	A	193	ILE	0	-0.006	-0.009	22.420	0.393	0.393	0.000	0.000	0.000	0.000
193	A	194	PRO	0	0.056	0.030	26.074	-0.181	-0.181	0.000	0.000	0.000	0.000
194	A	195	ASP	-1	-0.846	-0.922	29.176	-10.318	-10.318	0.000	0.000	0.000	0.000
195	A	196	HIS	0	0.040	0.022	30.938	0.495	0.495	0.000	0.000	0.000	0.000
196	A	197	PHE	0	-0.058	-0.035	31.428	-0.310	-0.310	0.000	0.000	0.000	0.000
197	A	198	VAL	0	0.025	0.013	28.228	0.236	0.236	0.000	0.000	0.000	0.000
198	A	199	VAL	0	-0.017	-0.013	31.696	-0.032	-0.032	0.000	0.000	0.000	0.000
199	A	200	GLY	0	0.060	0.033	32.404	0.014	0.014	0.000	0.000	0.000	0.000
200	A	201	TYR	0	-0.029	-0.029	24.790	-0.331	-0.331	0.000	0.000	0.000	0.000
201	A	202	SER	0	-0.070	-0.036	28.034	-0.376	-0.376	0.000	0.000	0.000	0.000
202	A	203	LEU	0	0.023	0.033	26.344	0.057	0.057	0.000	0.000	0.000	0.000
203	A	204	ASP	-1	-0.840	-0.909	30.220	-9.460	-9.460	0.000	0.000	0.000	0.000
204	A	205	TYR	0	0.024	0.007	33.599	-0.181	-0.181	0.000	0.000	0.000	0.000
205	A	206	ASN	0	-0.032	-0.031	36.427	0.010	0.010	0.000	0.000	0.000	0.000
206	A	207	GLU	-1	-0.811	-0.918	35.420	-9.115	-9.115	0.000	0.000	0.000	0.000
207	A	208	ILE	0	-0.021	0.007	37.162	0.007	0.007	0.000	0.000	0.000	0.000
208	A	209	PHE	0	0.034	-0.004	36.015	-0.201	-0.201	0.000	0.000	0.000	0.000
209	A	210	ARG	1	0.757	0.872	31.496	9.578	9.578	0.000	0.000	0.000	0.000
210	A	211	ASP	-1	-0.848	-0.907	33.231	-8.697	-8.697	0.000	0.000	0.000	0.000
211	A	212	LEU	0	-0.031	-0.005	35.092	0.122	0.122	0.000	0.000	0.000	0.000
212	A	213	ASP	-1	-0.827	-0.918	33.141	-9.884	-9.884	0.000	0.000	0.000	0.000
213	A	214	HIS	0	-0.021	0.006	31.375	-0.666	-0.666	0.000	0.000	0.000	0.000
214	A	215	CYS	0	0.005	0.034	27.711	0.213	0.213	0.000	0.000	0.000	0.000
215	A	216	CYS	0	-0.039	-0.009	30.640	0.160	0.160	0.000	0.000	0.000	0.000
216	A	217	LEU	0	0.040	0.032	32.461	-0.168	-0.168	0.000	0.000	0.000	0.000
217	A	218	VAL	0	0.007	0.005	35.299	0.263	0.263	0.000	0.000	0.000	0.000
218	A	219	ASN	0	-0.034	-0.029	38.057	0.011	0.011	0.000	0.000	0.000	0.000
219	A	220	ASP	-1	-0.833	-0.938	41.296	-7.690	-7.690	0.000	0.000	0.000	0.000
220	A	221	GLU	-1	-0.921	-0.969	43.334	-6.580	-6.580	0.000	0.000	0.000	0.000
221	A	222	GLY	0	0.009	-0.006	42.181	0.062	0.062	0.000	0.000	0.000	0.000
222	A	223	LYS	1	0.858	0.931	37.615	8.402	8.402	0.000	0.000	0.000	0.000
223	A	224	LYS	1	0.945	0.980	41.996	6.472	6.472	0.000	0.000	0.000	0.000
224	A	225	LYS	1	0.895	0.959	45.378	6.828	6.828	0.000	0.000	0.000	0.000
225	A	226	TYR	0	-0.047	-0.030	42.143	0.168	0.168	0.000	0.000	0.000	0.000
226	A	227	LYS	1	0.866	0.949	42.556	7.100	7.100	0.000	0.000	0.000	0.000
227	A	228	ALA	-1	-0.880	-0.923	41.945	-7.100	-7.100	0.000	0.000	0.000	0.000

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