SEQRES 1 A 153 GLY LEU SER ASP GLY GLU TRP GLN GLN VAL LEU ASN VAL The space group and related information are given.The protein and its crystalline form are provided, including: REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.įollowing the introductory material, some specific information regarding REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.1 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20 REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45 JRNL TITL 2 INTERMEDIATE IN WILDTYPE CARBONMONOXY MYOGLOBIN JRNL TITL CRYSTAL STRUCTURE OF A NEW LIGAND BINDING JRNL AUTH K.CHU,J.VOJTECHOVSKY,B.H.MCMAHON,R.M.SWEET, REVDAT 2 29-APR-05 1DWR 1 REMARK HET HETNAM FORMUL KEYWDS OXYGEN TRANSPORT, RESPIRATORY PROTEINĪUTHOR K.CHU,J.VOJTECHOVSKY,B.H.MCMAHON,R.M.SWEET,J.BERENDZEN, SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS TITLE MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO Structure matches the measured data (x-ray reflection intensities in (particularly the free-R factor), that contain information on how well the deposited Some basic information regarding the crystallographic dataĮspecially critical to check are the resolution and the R-factor.References to the literature that describe the structure in detail.List of authors who sent the entry to the PDB.The biological source of the marcomolecule.The protein, date of deposition, PDB ID code.The initial lines of a PDB entry contain information on: We will focus on PDB entry 1DWR (an x-ray structure of myogloblin complexedīe downloaded from the Protein Data bank. Learned about the background of the structure (experimental conditionsĮtc.) and the structural quality (the resolution, coordinate uncertainty). Us have a closer look at a typical PDB file, to see what can be Before we will turn to the structure determination itself, let Individual protein structures can be retrieved as so-called PDBįiles. (currently about 565,000, as available from the UniProtKB/Swiss-ProtĮxperimentally solved protein structures are stored at the Protein Data Bank, from which Known protein sequences is three times larger The number of solved proteins grows even faster, due to advancements As can also be seen on the PDB holdings list, About 88% of these are x-ray crystallographic structures, the restĪre NMR structures (7%) and cryoEM structures (5%). PDB holdings, more than 180,000 protein structures have been solved There are two main techniques for solving protein structures: x-rayĬrystallography and Nuclear Magnetic Resonance (NMR). Today, we'll focus on how computational techniques are employed to aid In the last lectures we learned how protein structures are determined experimentally.
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