FMO DATABASE

FMODB ID: 153YZ

Calculation Name: 1HK0-X-Xray547

Preferred Name: Gamma-crystallin D

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1HK0

Chain ID: X

ChEMBL ID: CHEMBL4296286

UniProt ID: P07320

Base Structure: X-ray

Registration Date: 2025-10-03

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	173
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1996567.675431
FMO2-HF: Nuclear repulsion	1922802.742005
FMO2-HF: Total energy	-73764.933425
FMO2-MP2: Total energy	-73975.946286

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:1:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-133.531	-129.767	12.214	-8.553	-7.423	-0.093

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.813 / q_NPA : 0.899

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	3	ILE	0	-0.014	0.006	3.819	-1.618	-1.008	-0.005	-0.265	-0.340	0.000
37	A	37	VAL	0	-0.018	0.004	4.358	-2.222	-2.178	-0.001	-0.016	-0.026	0.000
38	A	38	ASP	-1	-0.830	-0.918	3.529	-40.855	-40.676	0.007	-0.061	-0.125	0.000
39	A	39	SER	0	-0.019	-0.024	2.299	-12.030	-9.940	3.644	-3.020	-2.714	-0.027
40	A	40	GLY	0	-0.021	-0.005	1.904	-40.054	-40.233	8.212	-4.684	-3.348	-0.061
41	A	41	CYS	0	-0.043	-0.024	3.532	12.433	12.470	0.001	0.037	-0.075	0.000
42	A	42	TRP	0	0.014	0.004	3.265	2.530	2.856	0.001	-0.164	-0.163	0.000
80	A	80	LEU	0	0.003	0.013	2.535	-4.268	-3.611	0.355	-0.380	-0.632	-0.005
4	A	4	THR	0	0.016	0.003	6.787	3.289	3.289	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.018	-0.019	10.074	0.534	0.534	0.000	0.000	0.000	0.000
6	A	6	TYR	0	0.061	0.017	12.757	0.061	0.061	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.751	-0.855	16.739	-14.115	-14.115	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.833	-0.896	20.316	-12.855	-12.855	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.870	0.918	19.865	12.654	12.654	0.000	0.000	0.000	0.000
10	A	10	GLY	0	-0.019	-0.005	19.717	0.395	0.395	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.062	-0.037	14.586	0.127	0.127	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.043	-0.013	17.550	0.482	0.482	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.054	0.024	20.097	-0.312	-0.312	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.830	0.908	19.997	14.384	14.384	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.012	-0.009	14.916	-0.552	-0.552	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.015	-0.002	13.661	0.934	0.934	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.835	-0.913	9.188	-29.566	-29.566	0.000	0.000	0.000	0.000
18	A	18	CYS	0	-0.056	-0.001	8.598	2.658	2.658	0.000	0.000	0.000	0.000
19	A	19	SER	0	0.042	-0.002	5.149	-7.900	-7.900	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.008	-0.001	5.374	-3.451	-3.451	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.819	-0.909	7.389	-29.233	-29.233	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.014	-0.014	10.049	0.435	0.435	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.022	0.019	12.740	0.346	0.346	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.071	0.016	16.210	1.076	1.076	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.028	0.012	13.251	0.021	0.021	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.014	0.009	17.372	0.671	0.671	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.030	-0.009	20.072	0.416	0.416	0.000	0.000	0.000	0.000
28	A	28	TYR	0	-0.028	-0.010	17.271	0.476	0.476	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.037	-0.019	15.702	-0.223	-0.223	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.074	-0.056	19.306	0.264	0.264	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.813	0.909	21.152	14.002	14.002	0.000	0.000	0.000	0.000
32	A	32	CYS	0	-0.035	-0.016	14.967	-0.863	-0.863	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.032	-0.046	18.439	0.510	0.510	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.044	-0.013	16.657	0.095	0.095	0.000	0.000	0.000	0.000
35	A	35	ALA	0	0.006	-0.001	11.364	-0.421	-0.421	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.901	0.941	9.632	23.527	23.527	0.000	0.000	0.000	0.000
43	A	43	MET	0	-0.032	0.016	7.418	2.927	2.927	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.004	0.002	11.088	-0.768	-0.768	0.000	0.000	0.000	0.000
45	A	45	TYR	0	0.075	0.029	13.261	0.391	0.391	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.810	-0.897	16.886	-13.624	-13.624	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.030	0.009	20.060	0.771	0.771	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.025	0.008	19.001	-0.930	-0.930	0.000	0.000	0.000	0.000
49	A	49	ASN	0	-0.055	-0.040	18.441	-0.104	-0.104	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.018	-0.011	13.182	0.720	0.720	0.000	0.000	0.000	0.000
51	A	51	SER	0	0.008	0.008	17.455	0.072	0.072	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.016	-0.020	20.594	-0.238	-0.238	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.069	-0.044	21.163	-0.343	-0.343	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.047	0.024	16.523	-1.557	-1.557	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.022	-0.009	15.291	0.967	0.967	0.000	0.000	0.000	0.000
56	A	56	PHE	0	0.020	-0.001	9.529	-1.241	-1.241	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.036	-0.010	9.385	1.316	1.316	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.920	0.943	7.346	22.519	22.519	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.812	0.885	6.315	39.001	39.001	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.000	0.008	7.400	4.871	4.871	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.876	-0.924	9.994	-26.328	-26.328	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.004	-0.001	10.382	0.850	0.850	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.026	0.000	14.915	-0.033	-0.033	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.807	-0.904	18.127	-13.587	-13.587	0.000	0.000	0.000	0.000
65	A	65	HIS	0	0.030	0.005	18.237	-0.181	-0.181	0.000	0.000	0.000	0.000
66	A	66	GLN	0	0.010	0.015	19.093	-0.631	-0.631	0.000	0.000	0.000	0.000
67	A	67	GLN	0	-0.008	0.000	17.336	-0.820	-0.820	0.000	0.000	0.000	0.000
68	A	68	TRP	0	-0.008	0.009	14.564	-1.084	-1.084	0.000	0.000	0.000	0.000
69	A	69	MET	0	-0.042	-0.036	16.423	0.287	0.287	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.024	0.025	19.283	0.415	0.415	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.021	-0.019	20.204	0.563	0.563	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.032	-0.018	22.475	0.508	0.508	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.808	-0.888	20.631	-14.207	-14.207	0.000	0.000	0.000	0.000
74	A	74	SER	0	0.006	0.004	20.688	-0.370	-0.370	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.016	-0.010	14.781	-0.300	-0.300	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.862	0.912	18.118	13.919	13.919	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.033	-0.007	15.313	0.100	0.100	0.000	0.000	0.000	0.000
78	A	78	CYS	0	-0.027	0.000	10.314	0.048	0.048	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.925	0.965	9.783	23.926	23.926	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.039	-0.026	6.352	4.159	4.159	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.019	-0.008	6.764	-4.821	-4.821	0.000	0.000	0.000	0.000
83	A	83	HIS	0	0.014	0.002	6.682	1.229	1.229	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.009	-0.026	8.548	2.271	2.271	0.000	0.000	0.000	0.000
85	A	85	GLY	0	-0.023	-0.004	12.012	-0.672	-0.672	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.060	-0.039	13.966	0.622	0.622	0.000	0.000	0.000	0.000
87	A	88	HIS	0	0.013	0.006	12.960	0.235	0.235	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.801	0.871	17.942	14.041	14.041	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.016	0.009	20.432	-0.258	-0.258	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.897	0.944	22.678	11.807	11.807	0.000	0.000	0.000	0.000
91	A	92	LEU	0	0.016	0.000	23.992	-0.245	-0.245	0.000	0.000	0.000	0.000
92	A	93	TYR	0	0.012	0.001	27.777	0.237	0.237	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.773	-0.868	31.257	-8.451	-8.451	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.808	0.882	34.257	8.304	8.304	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.835	-0.909	32.868	-9.613	-9.613	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.872	-0.912	32.629	-9.130	-9.130	0.000	0.000	0.000	0.000
97	A	98	TYR	0	-0.112	-0.091	27.011	0.173	0.173	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.883	0.943	32.826	8.825	8.825	0.000	0.000	0.000	0.000
99	A	100	GLY	0	-0.024	-0.015	35.604	-0.101	-0.101	0.000	0.000	0.000	0.000
100	A	101	GLN	0	-0.009	-0.019	36.169	-0.191	-0.191	0.000	0.000	0.000	0.000
101	A	102	MET	0	-0.032	-0.006	30.302	-0.311	-0.311	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.009	0.006	28.632	0.223	0.223	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.784	-0.890	26.341	-12.011	-12.011	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.016	-0.013	23.376	0.295	0.295	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.056	0.012	21.564	-0.132	-0.132	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.993	-0.984	20.658	-13.668	-13.668	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.818	-0.877	18.033	-17.761	-17.761	0.000	0.000	0.000	0.000
108	A	109	CYS	0	-0.058	-0.015	20.890	0.880	0.880	0.000	0.000	0.000	0.000
109	A	110	SER	0	0.044	0.023	23.931	-0.131	-0.131	0.000	0.000	0.000	0.000
110	A	111	CYS	0	-0.027	-0.031	24.891	0.129	0.129	0.000	0.000	0.000	0.000
111	A	112	LEU	0	0.021	0.019	27.370	0.087	0.087	0.000	0.000	0.000	0.000
112	A	113	GLN	0	-0.014	-0.040	28.863	0.097	0.097	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.882	-0.935	31.278	-9.659	-9.659	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.880	0.941	27.595	11.231	11.231	0.000	0.000	0.000	0.000
115	A	116	PHE	0	0.029	0.007	31.418	0.206	0.206	0.000	0.000	0.000	0.000
116	A	117	ARG	1	0.925	0.972	33.261	8.486	8.486	0.000	0.000	0.000	0.000
117	A	118	PHE	0	0.028	0.015	33.674	0.281	0.281	0.000	0.000	0.000	0.000
118	A	119	ASN	0	-0.017	-0.004	32.953	-0.343	-0.343	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.896	-0.950	31.032	-9.615	-9.615	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.033	-0.005	27.117	0.109	0.109	0.000	0.000	0.000	0.000
121	A	122	HIS	0	-0.017	-0.024	29.235	-0.331	-0.331	0.000	0.000	0.000	0.000
122	A	123	SER	0	-0.046	-0.026	28.591	-0.035	-0.035	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.029	-0.012	22.468	0.047	0.047	0.000	0.000	0.000	0.000
124	A	125	ASN	0	-0.003	0.004	24.515	-0.446	-0.446	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.006	0.012	17.977	0.064	0.064	0.000	0.000	0.000	0.000
126	A	127	LEU	0	0.004	0.001	20.653	-0.200	-0.200	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.792	-0.862	18.231	-15.195	-15.195	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.067	0.029	14.254	0.021	0.021	0.000	0.000	0.000	0.000
129	A	130	SER	0	0.001	0.004	11.584	1.571	1.571	0.000	0.000	0.000	0.000
130	A	131	TRP	0	-0.022	-0.027	13.900	-0.231	-0.231	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.026	-0.010	14.159	-0.541	-0.541	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.009	0.015	16.870	0.610	0.610	0.000	0.000	0.000	0.000
133	A	134	TYR	0	0.022	-0.006	16.771	-0.636	-0.636	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.823	-0.904	22.461	-11.240	-11.240	0.000	0.000	0.000	0.000
135	A	136	LEU	0	-0.021	-0.012	25.360	0.665	0.665	0.000	0.000	0.000	0.000
136	A	137	SER	0	0.043	0.036	25.361	-0.506	-0.506	0.000	0.000	0.000	0.000
137	A	138	ASN	0	-0.063	-0.049	24.277	-0.115	-0.115	0.000	0.000	0.000	0.000
138	A	139	TYR	0	-0.023	-0.006	19.607	-0.234	-0.234	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.887	0.945	21.157	11.237	11.237	0.000	0.000	0.000	0.000
140	A	141	GLY	0	0.024	0.010	23.682	0.213	0.213	0.000	0.000	0.000	0.000
141	A	142	ARG	1	0.920	0.951	22.622	11.327	11.327	0.000	0.000	0.000	0.000
142	A	143	GLN	0	0.050	0.024	16.621	-0.774	-0.774	0.000	0.000	0.000	0.000
143	A	144	TYR	0	-0.015	-0.009	19.257	0.179	0.179	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.004	-0.012	12.514	-0.278	-0.278	0.000	0.000	0.000	0.000
145	A	146	LEU	0	-0.033	0.002	16.119	0.919	0.919	0.000	0.000	0.000	0.000
146	A	147	MET	0	-0.015	-0.013	12.924	-2.258	-2.258	0.000	0.000	0.000	0.000
147	A	148	PRO	0	0.015	0.001	14.954	1.093	1.093	0.000	0.000	0.000	0.000
148	A	149	GLY	0	0.040	0.027	17.924	-0.100	-0.100	0.000	0.000	0.000	0.000
149	A	150	ASP	-1	-0.863	-0.902	21.331	-12.082	-12.082	0.000	0.000	0.000	0.000
150	A	151	TYR	0	-0.027	-0.022	18.747	-0.246	-0.246	0.000	0.000	0.000	0.000
151	A	152	ARG	1	0.903	0.917	25.490	10.216	10.216	0.000	0.000	0.000	0.000
152	A	153	ARG	1	0.958	0.976	28.542	10.668	10.668	0.000	0.000	0.000	0.000
153	A	154	TYR	0	0.032	0.013	27.467	-0.235	-0.235	0.000	0.000	0.000	0.000
154	A	155	GLN	0	-0.025	-0.016	26.618	-0.503	-0.503	0.000	0.000	0.000	0.000
155	A	156	ASP	-1	-0.857	-0.921	24.863	-11.943	-11.943	0.000	0.000	0.000	0.000
156	A	157	TRP	0	-0.016	0.002	21.491	-0.641	-0.641	0.000	0.000	0.000	0.000
157	A	158	GLY	0	-0.013	-0.012	22.074	-0.496	-0.496	0.000	0.000	0.000	0.000
158	A	159	ALA	0	-0.024	0.005	24.155	0.061	0.061	0.000	0.000	0.000	0.000
159	A	160	THR	0	-0.007	-0.026	26.317	0.252	0.252	0.000	0.000	0.000	0.000
160	A	161	ASN	0	-0.041	-0.028	29.454	0.412	0.412	0.000	0.000	0.000	0.000
161	A	162	ALA	0	0.096	0.047	29.119	-0.412	-0.412	0.000	0.000	0.000	0.000
162	A	163	ARG	1	0.908	0.977	29.397	9.782	9.782	0.000	0.000	0.000	0.000
163	A	164	VAL	0	0.002	0.004	25.002	-0.461	-0.461	0.000	0.000	0.000	0.000
164	A	165	GLY	0	0.024	0.023	26.543	0.459	0.459	0.000	0.000	0.000	0.000
165	A	166	SER	0	-0.076	-0.048	23.315	-0.080	-0.080	0.000	0.000	0.000	0.000
166	A	167	LEU	0	-0.010	0.006	20.894	-0.162	-0.162	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.918	0.974	15.751	19.031	19.031	0.000	0.000	0.000	0.000
168	A	169	ARG	1	0.901	0.933	15.161	17.513	17.513	0.000	0.000	0.000	0.000
169	A	170	VAL	0	-0.045	-0.023	9.253	-0.590	-0.590	0.000	0.000	0.000	0.000
170	A	171	ILE	0	-0.001	-0.007	10.386	-0.652	-0.652	0.000	0.000	0.000	0.000
171	A	172	ASP	-1	-0.774	-0.874	6.142	-45.466	-45.466	0.000	0.000	0.000	0.000
172	A	173	PHE	0	-0.034	-0.024	8.668	2.019	2.019	0.000	0.000	0.000	0.000
173	A	174	SER	-1	-0.888	-0.914	8.922	-31.222	-31.222	0.000	0.000	0.000	0.000

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