FMO DATABASE

FMODB ID: 1YJ3Z

Calculation Name: 2RPZ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2RPZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WV35

Base Structure: SolutionNMR

Registration Date: 2025-10-04

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	192
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2119879.024895
FMO2-HF: Nuclear repulsion	2043402.139937
FMO2-HF: Total energy	-76476.884958
FMO2-MP2: Total energy	-76700.358141

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:39:GLY)

Summations of interaction energy for fragment #1(A:39: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.
-161.349	-156.636	16.739	-10.966	-10.485	-0.119

Interaction energy analysis for fragmet #1(A:39:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.827 / q_NPA : 0.911

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	41	SER	0	0.029	0.023	3.709	8.799	10.731	-0.009	-0.913	-1.009	-0.003
34	A	72	TYR	0	0.064	0.014	4.433	5.132	5.228	-0.001	-0.006	-0.089	0.000
52	A	90	LEU	0	-0.054	-0.021	1.908	-15.137	-16.661	5.300	-1.778	-1.998	-0.022
53	A	91	GLU	-1	-0.819	-0.950	2.014	-104.329	-103.120	8.912	-5.473	-4.648	-0.071
54	A	92	ASP	-1	-0.872	-0.944	5.150	-32.941	-32.862	-0.001	-0.001	-0.077	0.000
64	A	102	ALA	0	0.001	0.003	2.594	-0.638	-0.277	0.280	-0.247	-0.393	-0.002
65	A	103	PHE	0	0.064	0.022	2.983	-15.150	-13.065	0.057	-1.224	-0.918	-0.012
68	A	106	THR	0	-0.058	-0.037	2.286	-4.937	-4.855	2.085	-1.131	-1.036	-0.007
69	A	107	ILE	0	-0.069	0.000	2.824	1.567	1.960	0.116	-0.193	-0.317	-0.002
4	A	42	GLY	0	0.054	0.020	5.629	1.493	1.493	0.000	0.000	0.000	0.000
5	A	43	SER	0	-0.033	-0.012	9.337	2.915	2.915	0.000	0.000	0.000	0.000
6	A	44	SER	0	-0.004	-0.011	10.922	2.162	2.162	0.000	0.000	0.000	0.000
7	A	45	GLY	0	0.006	0.019	8.425	-2.089	-2.089	0.000	0.000	0.000	0.000
8	A	46	ARG	1	0.879	0.924	9.384	19.561	19.561	0.000	0.000	0.000	0.000
9	A	47	LEU	0	0.010	0.002	10.609	-0.148	-0.148	0.000	0.000	0.000	0.000
10	A	48	PRO	0	0.065	0.044	13.763	1.018	1.018	0.000	0.000	0.000	0.000
11	A	49	VAL	0	0.022	0.004	17.482	-0.110	-0.110	0.000	0.000	0.000	0.000
12	A	50	ASN	0	-0.035	-0.020	20.034	-0.292	-0.292	0.000	0.000	0.000	0.000
13	A	51	PHE	0	0.043	0.031	12.945	0.247	0.247	0.000	0.000	0.000	0.000
14	A	52	PHE	0	0.041	0.011	15.325	0.132	0.132	0.000	0.000	0.000	0.000
15	A	53	LYS	1	0.950	0.963	17.466	13.043	13.043	0.000	0.000	0.000	0.000
16	A	54	PHE	0	-0.044	-0.019	19.956	0.745	0.745	0.000	0.000	0.000	0.000
17	A	55	GLN	0	-0.011	-0.003	13.189	1.234	1.234	0.000	0.000	0.000	0.000
18	A	56	PHE	0	-0.039	-0.033	13.747	-0.475	-0.475	0.000	0.000	0.000	0.000
19	A	57	ARG	1	0.911	0.976	16.985	13.360	13.360	0.000	0.000	0.000	0.000
20	A	58	ASN	0	0.023	0.013	16.820	1.384	1.384	0.000	0.000	0.000	0.000
21	A	59	VAL	0	-0.041	-0.008	19.550	-0.356	-0.356	0.000	0.000	0.000	0.000
22	A	60	GLU	-1	-0.842	-0.929	22.511	-11.551	-11.551	0.000	0.000	0.000	0.000
23	A	61	TYR	0	0.044	0.028	25.140	0.001	0.001	0.000	0.000	0.000	0.000
24	A	62	SER	0	-0.020	-0.012	23.619	0.407	0.407	0.000	0.000	0.000	0.000
25	A	63	SER	0	-0.018	-0.009	24.426	-0.343	-0.343	0.000	0.000	0.000	0.000
26	A	64	GLY	0	0.015	-0.003	23.136	0.295	0.295	0.000	0.000	0.000	0.000
27	A	65	ARG	1	0.869	0.940	17.982	14.824	14.824	0.000	0.000	0.000	0.000
28	A	66	ASN	0	-0.015	-0.001	14.636	-0.873	-0.873	0.000	0.000	0.000	0.000
29	A	67	LYS	1	0.926	0.981	7.497	35.746	35.746	0.000	0.000	0.000	0.000
30	A	68	THR	0	0.007	0.009	11.562	0.434	0.434	0.000	0.000	0.000	0.000
31	A	69	PHE	0	0.008	0.007	6.955	-1.614	-1.614	0.000	0.000	0.000	0.000
32	A	70	LEU	0	-0.036	0.000	7.137	3.232	3.232	0.000	0.000	0.000	0.000
33	A	71	CYS	0	-0.014	0.006	7.179	-5.246	-5.246	0.000	0.000	0.000	0.000
35	A	73	VAL	0	0.029	0.010	9.760	-0.351	-0.351	0.000	0.000	0.000	0.000
36	A	74	VAL	0	-0.035	-0.022	10.486	0.398	0.398	0.000	0.000	0.000	0.000
37	A	75	GLU	-1	-0.866	-0.926	13.173	-15.590	-15.590	0.000	0.000	0.000	0.000
38	A	76	VAL	0	-0.036	-0.008	15.215	0.400	0.400	0.000	0.000	0.000	0.000
39	A	77	GLN	0	0.010	-0.003	17.851	0.873	0.873	0.000	0.000	0.000	0.000
40	A	78	SER	0	0.031	-0.004	21.638	0.179	0.179	0.000	0.000	0.000	0.000
41	A	79	LYS	0	-0.026	-0.031	24.255	0.102	0.102	0.000	0.000	0.000	0.000
42	A	80	GLY	0	-0.008	0.031	26.551	0.382	0.382	0.000	0.000	0.000	0.000
43	A	81	GLY	0	0.044	0.002	26.418	0.387	0.387	0.000	0.000	0.000	0.000
44	A	82	GLN	0	-0.003	0.015	19.576	0.206	0.206	0.000	0.000	0.000	0.000
45	A	83	ALA	0	0.009	-0.008	20.287	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	84	GLN	0	-0.035	-0.003	12.433	0.918	0.918	0.000	0.000	0.000	0.000
47	A	85	ALA	0	0.054	0.031	15.028	-0.355	-0.355	0.000	0.000	0.000	0.000
48	A	86	THR	0	-0.046	-0.023	8.803	-0.551	-0.551	0.000	0.000	0.000	0.000
49	A	87	GLN	0	0.002	-0.016	9.879	1.648	1.648	0.000	0.000	0.000	0.000
50	A	88	GLY	0	0.000	0.011	6.864	-0.854	-0.854	0.000	0.000	0.000	0.000
51	A	89	TYR	0	0.002	0.016	5.589	2.755	2.755	0.000	0.000	0.000	0.000
55	A	93	GLU	-1	-0.913	-0.951	6.027	-39.113	-39.113	0.000	0.000	0.000	0.000
56	A	94	HIS	0	-0.011	-0.016	8.567	1.205	1.205	0.000	0.000	0.000	0.000
57	A	95	ALA	0	-0.020	-0.017	11.952	1.881	1.881	0.000	0.000	0.000	0.000
58	A	96	GLY	0	0.010	0.002	10.366	0.519	0.519	0.000	0.000	0.000	0.000
59	A	97	ALA	0	-0.014	0.020	6.808	1.574	1.574	0.000	0.000	0.000	0.000
60	A	98	HIS	1	0.937	0.964	7.357	23.202	23.202	0.000	0.000	0.000	0.000
61	A	99	ALA	0	0.039	0.017	6.009	-3.404	-3.404	0.000	0.000	0.000	0.000
62	A	100	GLU	-1	-0.799	-0.916	6.120	-32.804	-32.804	0.000	0.000	0.000	0.000
63	A	101	GLU	-1	-0.857	-0.934	7.866	-27.312	-27.312	0.000	0.000	0.000	0.000
66	A	104	PHE	0	0.007	-0.013	5.526	0.807	0.807	0.000	0.000	0.000	0.000
67	A	105	ASN	0	-0.062	-0.033	4.956	4.014	4.014	0.000	0.000	0.000	0.000
70	A	108	LEU	0	-0.038	-0.023	6.134	4.846	4.846	0.000	0.000	0.000	0.000
71	A	109	PRO	0	0.016	0.022	8.456	0.881	0.881	0.000	0.000	0.000	0.000
72	A	110	ALA	0	-0.018	-0.017	10.583	2.022	2.022	0.000	0.000	0.000	0.000
73	A	111	PHE	0	0.001	-0.022	13.022	-0.839	-0.839	0.000	0.000	0.000	0.000
74	A	112	ASP	-1	-0.857	-0.908	16.596	-14.717	-14.717	0.000	0.000	0.000	0.000
75	A	113	PRO	0	-0.041	-0.049	20.027	0.038	0.038	0.000	0.000	0.000	0.000
76	A	114	ALA	0	-0.018	-0.001	22.962	0.411	0.411	0.000	0.000	0.000	0.000
77	A	115	LEU	0	-0.014	0.015	20.112	0.354	0.354	0.000	0.000	0.000	0.000
78	A	116	LYS	1	0.878	0.944	21.177	12.349	12.349	0.000	0.000	0.000	0.000
79	A	117	TYR	0	0.051	0.031	14.742	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	118	ASN	0	-0.011	-0.019	17.819	0.248	0.248	0.000	0.000	0.000	0.000
81	A	119	VAL	0	-0.006	-0.003	12.232	-0.847	-0.847	0.000	0.000	0.000	0.000
82	A	120	THR	0	0.009	-0.003	13.917	1.465	1.465	0.000	0.000	0.000	0.000
83	A	121	TRP	0	-0.006	-0.009	9.586	-1.569	-1.569	0.000	0.000	0.000	0.000
84	A	122	TYR	0	-0.003	-0.005	12.172	1.797	1.797	0.000	0.000	0.000	0.000
85	A	123	VAL	0	0.007	0.007	11.532	-1.737	-1.737	0.000	0.000	0.000	0.000
86	A	124	SER	0	0.058	0.025	14.141	1.577	1.577	0.000	0.000	0.000	0.000
87	A	125	SER	0	0.034	0.017	14.988	1.295	1.295	0.000	0.000	0.000	0.000
88	A	126	SER	0	0.004	-0.005	15.287	-0.893	-0.893	0.000	0.000	0.000	0.000
89	A	127	PRO	0	0.013	0.007	14.035	-0.401	-0.401	0.000	0.000	0.000	0.000
90	A	128	CYS	0	0.011	0.019	15.315	0.980	0.980	0.000	0.000	0.000	0.000
91	A	129	ALA	0	0.089	0.024	16.882	-0.625	-0.625	0.000	0.000	0.000	0.000
92	A	130	ALA	0	0.032	0.012	15.918	-0.051	-0.051	0.000	0.000	0.000	0.000
93	A	131	CYS	0	-0.066	-0.054	12.013	-0.739	-0.739	0.000	0.000	0.000	0.000
94	A	132	ALA	0	0.027	0.009	13.687	-0.724	-0.724	0.000	0.000	0.000	0.000
95	A	133	ASP	-1	-0.874	-0.939	16.284	-16.095	-16.095	0.000	0.000	0.000	0.000
96	A	134	ARG	1	0.856	0.903	11.312	24.261	24.261	0.000	0.000	0.000	0.000
97	A	135	ILE	0	0.017	0.029	12.343	-0.264	-0.264	0.000	0.000	0.000	0.000
98	A	136	LEU	0	0.035	0.024	14.622	0.815	0.815	0.000	0.000	0.000	0.000
99	A	137	LYS	1	0.894	0.954	16.546	16.228	16.228	0.000	0.000	0.000	0.000
100	A	138	THR	0	-0.010	0.011	13.813	0.447	0.447	0.000	0.000	0.000	0.000
101	A	139	LEU	0	0.038	0.010	16.629	0.493	0.493	0.000	0.000	0.000	0.000
102	A	140	SER	0	0.025	0.012	19.201	0.845	0.845	0.000	0.000	0.000	0.000
103	A	141	LYS	1	0.787	0.902	17.105	17.811	17.811	0.000	0.000	0.000	0.000
104	A	142	THR	0	-0.001	-0.003	17.964	0.698	0.698	0.000	0.000	0.000	0.000
105	A	143	LYS	1	0.931	0.968	20.556	12.638	12.638	0.000	0.000	0.000	0.000
106	A	144	ASN	0	-0.024	-0.014	20.925	0.389	0.389	0.000	0.000	0.000	0.000
107	A	145	LEU	0	0.001	0.020	15.082	-0.264	-0.264	0.000	0.000	0.000	0.000
108	A	146	ARG	1	0.828	0.897	18.676	14.324	14.324	0.000	0.000	0.000	0.000
109	A	147	LEU	0	0.035	0.034	13.480	-0.312	-0.312	0.000	0.000	0.000	0.000
110	A	148	LEU	0	-0.071	-0.022	16.390	1.303	1.303	0.000	0.000	0.000	0.000
111	A	149	ILE	0	0.028	0.003	14.208	-1.456	-1.456	0.000	0.000	0.000	0.000
112	A	150	LEU	0	-0.060	-0.012	15.983	1.396	1.396	0.000	0.000	0.000	0.000
113	A	151	VAL	0	0.010	0.003	16.314	-1.165	-1.165	0.000	0.000	0.000	0.000
114	A	152	SER	0	-0.022	0.000	18.439	0.547	0.547	0.000	0.000	0.000	0.000
115	A	153	ARG	1	0.854	0.916	19.953	13.821	13.821	0.000	0.000	0.000	0.000
116	A	154	LEU	0	-0.045	-0.005	20.262	-0.787	-0.787	0.000	0.000	0.000	0.000
117	A	155	PHE	0	-0.005	-0.015	17.839	0.304	0.304	0.000	0.000	0.000	0.000
118	A	156	MET	0	-0.029	-0.008	19.491	-0.403	-0.403	0.000	0.000	0.000	0.000
119	A	157	TRP	0	0.047	0.001	22.951	-0.143	-0.143	0.000	0.000	0.000	0.000
120	A	158	GLU	-1	-0.886	-0.943	24.916	-10.969	-10.969	0.000	0.000	0.000	0.000
121	A	159	GLU	-1	-0.884	-0.943	24.293	-12.049	-12.049	0.000	0.000	0.000	0.000
122	A	160	PRO	0	0.012	-0.008	26.928	-0.190	-0.190	0.000	0.000	0.000	0.000
123	A	161	GLU	-1	-0.961	-0.982	22.537	-14.009	-14.009	0.000	0.000	0.000	0.000
124	A	162	VAL	0	0.016	-0.004	21.116	-0.412	-0.412	0.000	0.000	0.000	0.000
125	A	163	GLN	0	0.011	0.021	23.424	-0.077	-0.077	0.000	0.000	0.000	0.000
126	A	164	ALA	0	-0.011	-0.007	25.785	-0.050	-0.050	0.000	0.000	0.000	0.000
127	A	165	ALA	0	-0.057	-0.023	20.481	-0.129	-0.129	0.000	0.000	0.000	0.000
128	A	166	LEU	0	0.036	0.005	18.930	-0.616	-0.616	0.000	0.000	0.000	0.000
129	A	167	LYS	1	0.885	0.944	21.765	11.073	11.073	0.000	0.000	0.000	0.000
130	A	168	LYS	1	0.944	0.970	21.951	13.798	13.798	0.000	0.000	0.000	0.000
131	A	169	LEU	0	-0.029	-0.001	17.247	-0.040	-0.040	0.000	0.000	0.000	0.000
132	A	170	LYS	1	0.932	0.970	21.234	11.101	11.101	0.000	0.000	0.000	0.000
133	A	171	GLU	-1	-0.903	-0.947	24.526	-10.865	-10.865	0.000	0.000	0.000	0.000
134	A	172	ALA	0	-0.015	0.003	21.734	0.301	0.301	0.000	0.000	0.000	0.000
135	A	173	GLY	0	-0.001	0.006	23.109	-0.149	-0.149	0.000	0.000	0.000	0.000
136	A	174	CYS	0	-0.068	-0.023	18.041	-0.437	-0.437	0.000	0.000	0.000	0.000
137	A	175	LYS	1	0.871	0.944	19.864	14.279	14.279	0.000	0.000	0.000	0.000
138	A	176	LEU	0	0.076	0.040	18.881	-0.915	-0.915	0.000	0.000	0.000	0.000
139	A	177	ARG	1	0.919	0.944	20.719	15.350	15.350	0.000	0.000	0.000	0.000
140	A	178	ILE	0	0.055	0.042	20.928	-0.836	-0.836	0.000	0.000	0.000	0.000
141	A	179	MET	0	-0.091	-0.048	17.049	0.510	0.510	0.000	0.000	0.000	0.000
142	A	180	LYS	1	0.937	0.987	20.823	13.047	13.047	0.000	0.000	0.000	0.000
143	A	181	PRO	0	0.044	0.013	22.815	-0.545	-0.545	0.000	0.000	0.000	0.000
144	A	182	GLN	0	0.033	0.007	24.734	-0.061	-0.061	0.000	0.000	0.000	0.000
145	A	183	ASP	-1	-0.824	-0.928	19.902	-15.244	-15.244	0.000	0.000	0.000	0.000
146	A	184	PHE	0	-0.001	-0.021	17.995	-0.856	-0.856	0.000	0.000	0.000	0.000
147	A	185	GLU	-1	-0.947	-0.952	20.045	-12.845	-12.845	0.000	0.000	0.000	0.000
148	A	186	TYR	0	0.056	0.027	16.214	-0.446	-0.446	0.000	0.000	0.000	0.000
149	A	187	ILE	0	-0.056	-0.046	14.324	-0.975	-0.975	0.000	0.000	0.000	0.000
150	A	188	TRP	0	-0.052	-0.037	16.588	-0.937	-0.937	0.000	0.000	0.000	0.000
151	A	189	GLN	0	-0.037	-0.012	19.369	0.214	0.214	0.000	0.000	0.000	0.000
152	A	190	ASN	0	-0.016	0.004	16.664	0.575	0.575	0.000	0.000	0.000	0.000
153	A	191	PHE	0	-0.043	-0.033	10.239	-0.860	-0.860	0.000	0.000	0.000	0.000
154	A	192	VAL	0	-0.036	-0.009	13.695	-1.411	-1.411	0.000	0.000	0.000	0.000
155	A	193	GLU	-1	-0.856	-0.904	16.488	-17.393	-17.393	0.000	0.000	0.000	0.000
156	A	194	GLN	0	0.037	-0.001	18.831	0.421	0.421	0.000	0.000	0.000	0.000
157	A	195	GLU	-1	-0.914	-0.959	22.504	-12.983	-12.983	0.000	0.000	0.000	0.000
158	A	196	GLU	-1	-0.932	-0.957	25.113	-11.389	-11.389	0.000	0.000	0.000	0.000
159	A	197	GLY	0	-0.030	-0.009	27.034	0.360	0.360	0.000	0.000	0.000	0.000
160	A	198	GLU	-1	-0.950	-0.970	27.998	-9.937	-9.937	0.000	0.000	0.000	0.000
161	A	199	SER	0	-0.031	-0.013	27.005	-0.378	-0.378	0.000	0.000	0.000	0.000
162	A	200	LYS	1	0.841	0.900	26.160	11.340	11.340	0.000	0.000	0.000	0.000
163	A	201	ALA	0	0.101	0.049	25.604	-0.370	-0.370	0.000	0.000	0.000	0.000
164	A	202	PHE	0	-0.045	-0.018	23.005	0.102	0.102	0.000	0.000	0.000	0.000
165	A	203	GLU	-1	-0.896	-0.945	25.113	-10.173	-10.173	0.000	0.000	0.000	0.000
166	A	204	PRO	0	-0.054	-0.028	26.472	0.167	0.167	0.000	0.000	0.000	0.000
167	A	205	TRP	0	-0.042	-0.040	28.542	0.317	0.317	0.000	0.000	0.000	0.000
168	A	206	GLU	-1	-0.995	-0.970	29.248	-10.510	-10.510	0.000	0.000	0.000	0.000
169	A	207	ASP	-1	-0.796	-0.914	30.584	-9.288	-9.288	0.000	0.000	0.000	0.000
170	A	208	ILE	0	-0.064	-0.029	29.047	-0.504	-0.504	0.000	0.000	0.000	0.000
171	A	209	GLN	0	-0.021	-0.017	29.272	-0.437	-0.437	0.000	0.000	0.000	0.000
172	A	210	GLU	-1	-0.841	-0.911	31.334	-9.400	-9.400	0.000	0.000	0.000	0.000
173	A	211	ASN	0	-0.032	-0.033	26.415	-0.446	-0.446	0.000	0.000	0.000	0.000
174	A	212	PHE	0	0.003	0.009	25.607	-0.447	-0.447	0.000	0.000	0.000	0.000
175	A	213	LEU	0	0.046	0.003	28.070	-0.191	-0.191	0.000	0.000	0.000	0.000
176	A	214	TYR	0	0.007	0.019	27.811	-0.048	-0.048	0.000	0.000	0.000	0.000
177	A	215	TYR	0	0.084	0.033	24.927	-0.145	-0.145	0.000	0.000	0.000	0.000
178	A	216	GLU	-1	-0.950	-0.977	26.591	-10.889	-10.889	0.000	0.000	0.000	0.000
179	A	217	GLU	-1	-0.880	-0.925	28.027	-9.716	-9.716	0.000	0.000	0.000	0.000
180	A	218	LYS	1	0.781	0.886	26.449	10.371	10.371	0.000	0.000	0.000	0.000
181	A	219	LEU	0	-0.022	-0.008	22.541	-0.299	-0.299	0.000	0.000	0.000	0.000
182	A	220	ALA	0	-0.040	-0.033	25.578	-0.003	-0.003	0.000	0.000	0.000	0.000
183	A	221	ASP	-1	-0.872	-0.943	28.847	-10.368	-10.368	0.000	0.000	0.000	0.000
184	A	222	ILE	0	-0.005	0.020	24.598	0.104	0.104	0.000	0.000	0.000	0.000
185	A	223	LEU	0	-0.118	-0.069	25.165	0.037	0.037	0.000	0.000	0.000	0.000
186	A	224	LYS	1	0.828	0.919	29.041	9.854	9.854	0.000	0.000	0.000	0.000
187	A	225	SER	0	0.075	0.052	32.289	0.049	0.049	0.000	0.000	0.000	0.000
188	A	226	GLY	0	0.017	0.006	33.847	0.193	0.193	0.000	0.000	0.000	0.000
189	A	227	PRO	0	-0.033	-0.015	37.582	-0.083	-0.083	0.000	0.000	0.000	0.000
190	A	228	SER	0	-0.008	-0.013	38.800	0.038	0.038	0.000	0.000	0.000	0.000
191	A	229	SER	0	-0.074	-0.057	41.213	0.103	0.103	0.000	0.000	0.000	0.000
192	A	230	GLY	-1	-0.907	-0.921	44.217	-6.877	-6.877	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:39:GLY)