FMO DATABASE

FMODB ID: 9RL52

Calculation Name: 2HNK-A-Xray547

Preferred Name:

Target Type:

Ligand Name: s-adenosyl-l-homocysteine | sulfate ion | di(hydroxyethyl)ether

Ligand 3-letter code: SAH | SO4 | PEG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HNK

Chain ID: A

ChEMBL ID:

UniProt ID: Q8F8Y3

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	232
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2896747.879159
FMO2-HF: Nuclear repulsion	2806901.848018
FMO2-HF: Total energy	-89846.031141
FMO2-MP2: Total energy	-90112.134734

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:3:ARG)

Summations of interaction energy for fragment #1(A:3:ARG)

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.
-237.745	-234.363	6.259	-5.258	-4.383	-0.064

Interaction energy analysis for fragmet #1(A:3:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.796 / q_NPA : 1.889

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	5	ASN	0	0.098	0.067	3.430	11.546	13.451	0.001	-0.778	-1.128	-0.001
4	A	6	ILE	0	0.024	0.004	1.897	-50.169	-48.869	6.259	-4.450	-3.109	-0.063
5	A	7	SER	0	-0.026	-0.017	4.265	-6.531	-6.354	-0.001	-0.030	-0.146	0.000
6	A	8	LEU	0	0.026	0.023	5.510	4.022	4.022	0.000	0.000	0.000	0.000
7	A	9	THR	0	0.028	0.003	9.076	0.919	0.919	0.000	0.000	0.000	0.000
8	A	10	GLU	-1	-0.803	-0.898	12.337	-30.012	-30.012	0.000	0.000	0.000	0.000
9	A	11	SER	0	-0.046	-0.018	15.205	1.350	1.350	0.000	0.000	0.000	0.000
10	A	12	LEU	0	-0.046	-0.027	10.055	0.700	0.700	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.890	-0.951	13.129	-37.220	-37.220	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.843	-0.923	15.422	-23.881	-23.881	0.000	0.000	0.000	0.000
13	A	15	TYR	0	-0.072	-0.039	16.103	1.586	1.586	0.000	0.000	0.000	0.000
14	A	16	ILE	0	0.015	0.005	12.508	0.916	0.916	0.000	0.000	0.000	0.000
15	A	17	PHE	0	0.034	0.034	17.157	1.352	1.352	0.000	0.000	0.000	0.000
16	A	18	ARG	1	0.919	0.960	19.896	26.994	26.994	0.000	0.000	0.000	0.000
17	A	19	ASN	0	-0.119	-0.056	19.296	1.492	1.492	0.000	0.000	0.000	0.000
18	A	20	SER	0	-0.081	-0.053	19.775	0.044	0.044	0.000	0.000	0.000	0.000
19	A	21	VAL	0	-0.039	0.008	21.478	0.877	0.877	0.000	0.000	0.000	0.000
20	A	22	ARG	1	0.916	0.953	23.995	21.657	21.657	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.711	-0.811	26.991	-20.575	-20.575	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.010	0.010	28.762	0.341	0.341	0.000	0.000	0.000	0.000
23	A	25	ASP	-1	-0.869	-0.935	32.362	-16.861	-16.861	0.000	0.000	0.000	0.000
24	A	26	SER	0	-0.036	-0.043	34.473	-0.118	-0.118	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.028	0.001	29.617	-0.015	-0.015	0.000	0.000	0.000	0.000
26	A	28	LEU	0	0.011	0.010	28.813	-0.217	-0.217	0.000	0.000	0.000	0.000
27	A	29	LYS	1	0.748	0.850	30.998	15.488	15.488	0.000	0.000	0.000	0.000
28	A	30	LEU	0	0.042	0.034	31.763	0.055	0.055	0.000	0.000	0.000	0.000
29	A	31	ARG	1	0.841	0.894	25.086	21.820	21.820	0.000	0.000	0.000	0.000
30	A	32	LYS	1	0.922	0.961	29.951	17.626	17.626	0.000	0.000	0.000	0.000
31	A	33	GLU	-1	-0.772	-0.845	32.002	-15.544	-15.544	0.000	0.000	0.000	0.000
32	A	34	THR	0	0.007	0.011	30.385	0.311	0.311	0.000	0.000	0.000	0.000
33	A	35	GLY	0	-0.017	-0.015	30.134	-0.072	-0.072	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.126	-0.064	30.787	0.157	0.157	0.000	0.000	0.000	0.000
35	A	37	LEU	0	-0.025	-0.003	34.210	0.323	0.323	0.000	0.000	0.000	0.000
36	A	38	ALA	0	0.003	0.011	32.940	0.253	0.253	0.000	0.000	0.000	0.000
37	A	39	GLN	0	0.023	0.002	26.813	-0.666	-0.666	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.022	0.020	26.737	-0.168	-0.168	0.000	0.000	0.000	0.000
39	A	41	ASN	0	-0.039	-0.029	20.151	-0.632	-0.632	0.000	0.000	0.000	0.000
40	A	42	MET	0	-0.009	0.002	23.442	-0.735	-0.735	0.000	0.000	0.000	0.000
41	A	43	GLN	0	-0.005	-0.004	24.899	1.412	1.412	0.000	0.000	0.000	0.000
42	A	44	ILE	0	0.001	0.017	22.657	-0.751	-0.751	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.012	-0.023	19.649	0.565	0.565	0.000	0.000	0.000	0.000
44	A	46	PRO	0	0.023	0.010	22.061	0.181	0.181	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.805	-0.907	17.865	-27.180	-27.180	0.000	0.000	0.000	0.000
46	A	48	GLU	0	-0.036	-0.054	19.515	-0.306	-0.306	0.000	0.000	0.000	0.000
47	A	49	GLY	0	0.053	0.011	20.797	0.540	0.540	0.000	0.000	0.000	0.000
48	A	50	GLN	0	-0.035	-0.042	22.680	1.451	1.451	0.000	0.000	0.000	0.000
49	A	51	PHE	0	0.003	0.007	17.856	0.213	0.213	0.000	0.000	0.000	0.000
50	A	52	LEU	0	0.046	0.023	21.672	0.309	0.309	0.000	0.000	0.000	0.000
51	A	53	ASN	0	-0.022	0.016	24.657	0.679	0.679	0.000	0.000	0.000	0.000
52	A	54	ILE	0	0.004	-0.011	22.380	0.656	0.656	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.014	0.010	20.866	0.395	0.395	0.000	0.000	0.000	0.000
54	A	56	THR	0	0.000	-0.008	24.973	0.633	0.633	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.842	0.929	28.534	19.832	19.832	0.000	0.000	0.000	0.000
56	A	58	ILE	0	-0.045	-0.020	23.823	0.392	0.392	0.000	0.000	0.000	0.000
57	A	59	SER	0	-0.052	-0.035	27.918	0.334	0.334	0.000	0.000	0.000	0.000
58	A	60	GLY	0	-0.003	0.006	29.522	0.443	0.443	0.000	0.000	0.000	0.000
59	A	61	ALA	0	-0.043	-0.010	31.957	0.624	0.624	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.822	0.869	33.701	15.530	15.530	0.000	0.000	0.000	0.000
61	A	63	ARG	1	0.784	0.889	36.365	15.421	15.421	0.000	0.000	0.000	0.000
62	A	64	ILE	0	0.043	0.025	31.177	-0.299	-0.299	0.000	0.000	0.000	0.000
63	A	65	ILE	0	0.001	-0.001	33.272	0.611	0.611	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.746	-0.835	30.386	-19.913	-19.913	0.000	0.000	0.000	0.000
65	A	67	ILE	0	-0.029	-0.014	30.565	0.734	0.734	0.000	0.000	0.000	0.000
66	A	68	GLY	0	0.018	0.010	29.988	-0.700	-0.700	0.000	0.000	0.000	0.000
67	A	69	THR	0	-0.052	-0.055	30.474	-0.181	-0.181	0.000	0.000	0.000	0.000
68	A	70	PHE	0	0.016	-0.001	29.760	-0.072	-0.072	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.013	-0.029	32.193	0.400	0.400	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.041	0.008	32.720	0.296	0.296	0.000	0.000	0.000	0.000
71	A	73	TYR	0	-0.052	-0.041	25.998	-0.205	-0.205	0.000	0.000	0.000	0.000
72	A	74	SER	0	0.034	-0.006	27.168	-0.109	-0.109	0.000	0.000	0.000	0.000
73	A	75	SER	0	0.008	-0.003	28.762	0.319	0.319	0.000	0.000	0.000	0.000
74	A	76	LEU	0	-0.016	0.006	31.924	0.381	0.381	0.000	0.000	0.000	0.000
75	A	77	CYS	0	-0.028	0.015	27.856	0.016	0.016	0.000	0.000	0.000	0.000
76	A	78	PHE	0	0.028	0.009	27.055	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.007	0.002	31.304	0.273	0.273	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.042	-0.035	32.399	0.279	0.279	0.000	0.000	0.000	0.000
79	A	81	ALA	0	-0.087	-0.030	30.064	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	82	LEU	0	-0.017	0.003	31.987	0.117	0.117	0.000	0.000	0.000	0.000
81	A	83	PRO	0	0.021	0.020	34.780	0.274	0.274	0.000	0.000	0.000	0.000
82	A	84	GLU	-1	-0.935	-0.975	37.733	-13.782	-13.782	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.805	-0.884	40.921	-14.782	-14.782	0.000	0.000	0.000	0.000
84	A	86	GLY	0	-0.041	-0.013	37.882	0.004	0.004	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.824	0.907	38.484	13.925	13.925	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.010	-0.004	32.855	-0.361	-0.361	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.023	0.004	36.710	0.450	0.450	0.000	0.000	0.000	0.000
88	A	90	CYS	0	-0.001	0.006	35.372	-0.581	-0.581	0.000	0.000	0.000	0.000
89	A	91	CYS	0	-0.020	-0.008	35.162	0.685	0.685	0.000	0.000	0.000	0.000
90	A	92	ASP	-1	-0.735	-0.861	34.194	-17.911	-17.911	0.000	0.000	0.000	0.000
91	A	93	VAL	0	0.023	-0.002	35.572	0.495	0.495	0.000	0.000	0.000	0.000
92	A	94	SER	0	-0.011	0.003	37.104	0.567	0.567	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.860	-0.909	38.930	-13.721	-13.721	0.000	0.000	0.000	0.000
94	A	96	GLU	-1	-0.903	-0.945	39.442	-15.071	-15.071	0.000	0.000	0.000	0.000
95	A	97	TRP	0	0.006	-0.009	35.369	-0.132	-0.132	0.000	0.000	0.000	0.000
96	A	98	THR	0	0.016	-0.024	36.942	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.048	-0.024	38.636	0.136	0.136	0.000	0.000	0.000	0.000
98	A	100	VAL	0	-0.032	-0.011	36.269	0.129	0.129	0.000	0.000	0.000	0.000
99	A	101	ALA	0	0.022	0.020	36.059	-0.047	-0.047	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.897	0.925	37.134	14.148	14.148	0.000	0.000	0.000	0.000
101	A	103	LYS	1	0.818	0.901	39.521	15.243	15.243	0.000	0.000	0.000	0.000
102	A	104	TYR	0	0.005	-0.012	36.112	0.156	0.156	0.000	0.000	0.000	0.000
103	A	105	TRP	0	-0.010	-0.012	35.517	0.328	0.328	0.000	0.000	0.000	0.000
104	A	106	LYS	1	0.821	0.898	39.269	13.433	13.433	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.823	-0.862	38.744	-15.166	-15.166	0.000	0.000	0.000	0.000
106	A	108	ASN	0	-0.058	-0.055	36.727	-0.150	-0.150	0.000	0.000	0.000	0.000
107	A	109	GLY	0	0.001	0.012	39.620	-0.022	-0.022	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.004	-0.008	36.199	0.085	0.085	0.000	0.000	0.000	0.000
109	A	111	GLU	-1	-0.766	-0.867	40.420	-13.690	-13.690	0.000	0.000	0.000	0.000
110	A	112	ASN	0	-0.019	-0.001	42.456	-0.120	-0.120	0.000	0.000	0.000	0.000
111	A	113	LYS	1	0.798	0.907	37.297	16.056	16.056	0.000	0.000	0.000	0.000
112	A	114	ILE	0	-0.033	-0.010	37.336	-0.364	-0.364	0.000	0.000	0.000	0.000
113	A	115	PHE	0	-0.019	-0.004	39.907	0.372	0.372	0.000	0.000	0.000	0.000
114	A	116	LEU	0	0.000	-0.011	38.734	-0.397	-0.397	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.840	0.932	40.048	14.622	14.622	0.000	0.000	0.000	0.000
116	A	118	LEU	0	0.025	0.024	39.718	-0.333	-0.333	0.000	0.000	0.000	0.000
117	A	119	GLY	0	0.004	-0.002	40.296	0.425	0.425	0.000	0.000	0.000	0.000
118	A	120	SER	0	0.043	0.024	38.732	-0.558	-0.558	0.000	0.000	0.000	0.000
119	A	121	ALA	0	0.079	0.038	35.042	0.272	0.272	0.000	0.000	0.000	0.000
120	A	122	LEU	0	0.015	0.013	33.934	0.080	0.080	0.000	0.000	0.000	0.000
121	A	123	GLU	-1	-0.951	-0.973	37.326	-13.815	-13.815	0.000	0.000	0.000	0.000
122	A	124	THR	0	-0.040	-0.029	39.105	0.345	0.345	0.000	0.000	0.000	0.000
123	A	125	LEU	0	0.017	0.000	34.150	0.190	0.190	0.000	0.000	0.000	0.000
124	A	126	GLN	0	-0.028	-0.026	38.859	-0.235	-0.235	0.000	0.000	0.000	0.000
125	A	127	VAL	0	0.012	0.002	41.295	0.294	0.294	0.000	0.000	0.000	0.000
126	A	128	LEU	0	-0.035	0.006	39.408	0.321	0.321	0.000	0.000	0.000	0.000
127	A	129	ILE	0	-0.037	-0.010	38.053	0.048	0.048	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.846	-0.916	42.405	-13.837	-13.837	0.000	0.000	0.000	0.000
129	A	131	SER	0	-0.097	-0.063	45.622	0.451	0.451	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.939	0.956	47.519	11.728	11.728	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.007	-0.006	50.167	0.211	0.211	0.000	0.000	0.000	0.000
132	A	134	ALA	0	0.010	0.019	47.381	-0.099	-0.099	0.000	0.000	0.000	0.000
133	A	135	PRO	0	0.027	0.031	45.662	0.316	0.316	0.000	0.000	0.000	0.000
134	A	136	SER	0	0.014	-0.012	47.725	-0.211	-0.211	0.000	0.000	0.000	0.000
135	A	137	TRP	0	0.025	-0.003	41.858	-0.019	-0.019	0.000	0.000	0.000	0.000
136	A	138	ALA	0	0.023	0.005	43.244	-0.357	-0.357	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.014	0.001	44.661	-0.019	-0.019	0.000	0.000	0.000	0.000
138	A	140	ASP	-1	-0.895	-0.962	46.807	-13.011	-13.011	0.000	0.000	0.000	0.000
139	A	141	PHE	0	-0.017	0.015	37.527	-0.160	-0.160	0.000	0.000	0.000	0.000
140	A	142	ALA	0	-0.023	-0.011	40.608	-0.016	-0.016	0.000	0.000	0.000	0.000
141	A	143	PHE	0	-0.001	-0.014	42.680	0.038	0.038	0.000	0.000	0.000	0.000
142	A	144	GLY	0	0.066	0.053	43.378	0.083	0.083	0.000	0.000	0.000	0.000
143	A	145	PRO	0	-0.038	-0.029	40.221	-0.373	-0.373	0.000	0.000	0.000	0.000
144	A	146	SER	0	-0.032	-0.012	38.060	0.141	0.141	0.000	0.000	0.000	0.000
145	A	147	SER	0	-0.035	-0.016	39.143	0.033	0.033	0.000	0.000	0.000	0.000
146	A	148	ILE	0	-0.044	-0.025	34.182	0.110	0.110	0.000	0.000	0.000	0.000
147	A	149	ASP	-1	-0.760	-0.851	33.548	-17.159	-17.159	0.000	0.000	0.000	0.000
148	A	150	LEU	0	-0.006	-0.011	27.461	-0.553	-0.553	0.000	0.000	0.000	0.000
149	A	151	PHE	0	0.051	0.000	29.319	0.715	0.715	0.000	0.000	0.000	0.000
150	A	152	PHE	0	0.009	-0.001	23.579	-0.804	-0.804	0.000	0.000	0.000	0.000
151	A	153	LEU	0	-0.035	-0.015	26.074	0.891	0.891	0.000	0.000	0.000	0.000
152	A	154	ASP	-1	-0.809	-0.915	25.249	-24.016	-24.016	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.022	0.003	26.715	0.385	0.385	0.000	0.000	0.000	0.000
154	A	156	ASP	-1	-0.784	-0.870	27.999	-19.230	-19.230	0.000	0.000	0.000	0.000
155	A	157	LYS	1	0.828	0.930	24.145	23.270	23.270	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.874	-0.955	26.900	-20.535	-20.535	0.000	0.000	0.000	0.000
157	A	159	ASN	0	-0.031	-0.019	29.028	0.262	0.262	0.000	0.000	0.000	0.000
158	A	160	TYR	0	0.000	-0.004	22.896	0.744	0.744	0.000	0.000	0.000	0.000
159	A	161	PRO	0	-0.051	-0.031	27.258	0.110	0.110	0.000	0.000	0.000	0.000
160	A	162	ASN	0	-0.041	-0.031	29.194	0.331	0.331	0.000	0.000	0.000	0.000
161	A	163	TYR	0	-0.024	-0.055	29.998	0.708	0.708	0.000	0.000	0.000	0.000
162	A	164	TYR	0	-0.041	-0.040	26.843	0.105	0.105	0.000	0.000	0.000	0.000
163	A	165	PRO	0	0.019	0.010	30.169	0.149	0.149	0.000	0.000	0.000	0.000
164	A	166	LEU	0	-0.026	-0.010	33.478	0.447	0.447	0.000	0.000	0.000	0.000
165	A	167	ILE	0	0.026	0.009	29.045	0.318	0.318	0.000	0.000	0.000	0.000
166	A	168	LEU	0	0.015	0.009	29.239	0.288	0.288	0.000	0.000	0.000	0.000
167	A	169	LYS	1	0.895	0.968	33.073	16.055	16.055	0.000	0.000	0.000	0.000
168	A	170	LEU	0	0.024	0.005	35.730	0.402	0.402	0.000	0.000	0.000	0.000
169	A	171	LEU	0	-0.041	0.000	29.859	0.263	0.263	0.000	0.000	0.000	0.000
170	A	172	LYS	1	0.846	0.918	34.476	16.578	16.578	0.000	0.000	0.000	0.000
171	A	173	PRO	0	0.022	0.010	33.782	-0.659	-0.659	0.000	0.000	0.000	0.000
172	A	174	GLY	0	-0.055	-0.018	31.101	0.270	0.270	0.000	0.000	0.000	0.000
173	A	175	GLY	0	0.022	0.017	30.376	-0.455	-0.455	0.000	0.000	0.000	0.000
174	A	176	LEU	0	-0.043	-0.028	23.925	-0.608	-0.608	0.000	0.000	0.000	0.000
175	A	177	LEU	0	0.021	0.013	25.311	0.680	0.680	0.000	0.000	0.000	0.000
176	A	178	ILE	0	-0.022	-0.008	22.214	-1.140	-1.140	0.000	0.000	0.000	0.000
177	A	179	ALA	0	0.008	-0.001	22.332	0.954	0.954	0.000	0.000	0.000	0.000
178	A	180	ASP	-1	-0.773	-0.859	20.754	-28.714	-28.714	0.000	0.000	0.000	0.000
179	A	181	ASN	0	-0.028	-0.034	19.230	1.404	1.404	0.000	0.000	0.000	0.000
180	A	182	VAL	0	-0.037	-0.008	16.537	-0.193	-0.193	0.000	0.000	0.000	0.000
181	A	183	LEU	0	-0.026	-0.029	11.619	-1.608	-1.608	0.000	0.000	0.000	0.000
182	A	184	TRP	0	0.000	0.006	15.678	-0.156	-0.156	0.000	0.000	0.000	0.000
183	A	185	ASP	-1	-0.898	-0.937	16.051	-31.657	-31.657	0.000	0.000	0.000	0.000
184	A	186	GLY	0	-0.022	0.000	13.853	-1.146	-1.146	0.000	0.000	0.000	0.000
185	A	187	SER	0	-0.056	-0.049	14.457	-0.200	-0.200	0.000	0.000	0.000	0.000
186	A	188	VAL	0	0.011	-0.002	15.457	0.892	0.892	0.000	0.000	0.000	0.000
187	A	189	ALA	0	-0.030	-0.006	13.726	0.390	0.390	0.000	0.000	0.000	0.000
188	A	190	ASP	-1	-0.848	-0.914	15.733	-30.715	-30.715	0.000	0.000	0.000	0.000
189	A	191	LEU	0	0.011	-0.013	17.838	1.587	1.587	0.000	0.000	0.000	0.000
190	A	192	SER	0	-0.023	-0.007	21.020	1.784	1.784	0.000	0.000	0.000	0.000
191	A	193	HIS	1	0.778	0.902	19.815	28.941	28.941	0.000	0.000	0.000	0.000
192	A	194	GLN	0	0.000	-0.016	23.010	-0.165	-0.165	0.000	0.000	0.000	0.000
193	A	195	GLU	-1	-0.768	-0.841	24.067	-24.009	-24.009	0.000	0.000	0.000	0.000
194	A	196	PRO	0	0.023	-0.004	26.389	-0.571	-0.571	0.000	0.000	0.000	0.000
195	A	197	SER	0	0.057	0.030	25.393	-0.290	-0.290	0.000	0.000	0.000	0.000
196	A	198	THR	0	0.017	-0.014	20.879	-0.545	-0.545	0.000	0.000	0.000	0.000
197	A	199	VAL	0	-0.034	-0.010	22.870	-0.822	-0.822	0.000	0.000	0.000	0.000
198	A	200	GLY	0	0.023	0.018	25.364	-0.158	-0.158	0.000	0.000	0.000	0.000
199	A	201	ILE	0	0.016	0.014	20.008	-0.128	-0.128	0.000	0.000	0.000	0.000
200	A	202	ARG	1	0.763	0.864	19.778	27.558	27.558	0.000	0.000	0.000	0.000
201	A	203	LYS	1	0.872	0.938	21.871	22.022	22.022	0.000	0.000	0.000	0.000
202	A	204	PHE	0	0.003	-0.005	22.062	0.359	0.359	0.000	0.000	0.000	0.000
203	A	205	ASN	0	0.008	-0.010	18.206	0.504	0.504	0.000	0.000	0.000	0.000
204	A	206	GLU	-1	-0.898	-0.941	21.201	-24.586	-24.586	0.000	0.000	0.000	0.000
205	A	207	LEU	0	-0.036	-0.018	22.785	0.307	0.307	0.000	0.000	0.000	0.000
206	A	208	VAL	0	0.018	0.002	21.662	0.187	0.187	0.000	0.000	0.000	0.000
207	A	209	TYR	0	-0.076	-0.028	17.609	-1.030	-1.030	0.000	0.000	0.000	0.000
208	A	210	ASN	0	-0.076	-0.052	21.784	-0.232	-0.232	0.000	0.000	0.000	0.000
209	A	211	ASP	-1	-0.795	-0.856	24.937	-20.319	-20.319	0.000	0.000	0.000	0.000
210	A	212	SER	0	-0.005	-0.006	26.898	-0.317	-0.317	0.000	0.000	0.000	0.000
211	A	213	LEU	0	-0.016	-0.005	28.575	0.364	0.364	0.000	0.000	0.000	0.000
212	A	214	VAL	0	-0.031	-0.015	25.148	0.344	0.344	0.000	0.000	0.000	0.000
213	A	215	ASP	-1	-0.871	-0.904	23.210	-24.986	-24.986	0.000	0.000	0.000	0.000
214	A	216	VAL	0	-0.010	-0.018	18.618	0.280	0.280	0.000	0.000	0.000	0.000
215	A	217	SER	0	-0.053	-0.022	16.194	-2.115	-2.115	0.000	0.000	0.000	0.000
216	A	218	LEU	0	0.024	0.019	13.186	1.129	1.129	0.000	0.000	0.000	0.000
217	A	219	VAL	0	0.003	-0.001	13.134	-3.447	-3.447	0.000	0.000	0.000	0.000
218	A	220	PRO	0	-0.043	-0.016	9.074	1.268	1.268	0.000	0.000	0.000	0.000
219	A	221	ILE	0	-0.008	-0.011	11.401	-1.576	-1.576	0.000	0.000	0.000	0.000
220	A	222	ALA	0	0.059	0.022	14.234	1.091	1.091	0.000	0.000	0.000	0.000
221	A	223	ASP	-1	-0.764	-0.859	14.570	-33.359	-33.359	0.000	0.000	0.000	0.000
222	A	224	GLY	0	-0.013	-0.005	14.513	-0.149	-0.149	0.000	0.000	0.000	0.000
223	A	225	VAL	0	0.001	-0.002	15.301	2.044	2.044	0.000	0.000	0.000	0.000
224	A	226	SER	0	-0.017	-0.009	17.205	-2.140	-2.140	0.000	0.000	0.000	0.000
225	A	227	LEU	0	-0.038	-0.008	19.046	1.645	1.645	0.000	0.000	0.000	0.000
226	A	228	VAL	0	0.036	0.001	20.917	-0.961	-0.961	0.000	0.000	0.000	0.000
227	A	229	ARG	1	0.894	0.960	23.548	22.849	22.849	0.000	0.000	0.000	0.000
228	A	230	LYS	1	0.897	0.964	26.259	17.626	17.626	0.000	0.000	0.000	0.000
229	A	231	ARG	1	0.822	0.903	26.400	22.786	22.786	0.000	0.000	0.000	0.000
230	A	232	LEU	0	-0.043	-0.038	30.447	0.518	0.518	0.000	0.000	0.000	0.000
231	A	233	GLU	-1	-0.912	-0.974	33.576	-17.380	-17.380	0.000	0.000	0.000	0.000
232	A	234	HIS	-1	-0.966	-0.965	32.844	-17.268	-17.268	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ARG)