Header list of 2cyu.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 08-JUL-05 2CYU
TITLE NMR STRUCTURE OF A DOWNHILL FOLDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: E3-BINDING DOMAIN;
COMPND 5 SYNONYM: DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF
COMPND 6 2- OXOGLUTARATE DEHYDROGENASE COMPLEX;
COMPND 7 EC: 2.3.1.61;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN E COLI.
KEYWDS HELIX BUNDLE, DOWNHILL FOLDING PROTEIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.MUNOZ,M.SADQI
REVDAT 4 09-MAR-22 2CYU 1 REMARK
REVDAT 3 24-FEB-09 2CYU 1 VERSN
REVDAT 2 15-AUG-06 2CYU 1 JRNL
REVDAT 1 15-JUL-06 2CYU 0
JRNL AUTH M.SADQI,D.FUSHMAN,V.MUNOZ
JRNL TITL ATOM-BY-ATOM ANALYSIS OF GLOBAL DOWNHILL PROTEIN FOLDING.
JRNL REF NATURE V. 442 317 2006
JRNL REFN ISSN 0028-0836
JRNL PMID 16799571
JRNL DOI 10.1038/NATURE04859
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, XPLOR-NIH 2.11
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FIRST THREE RESIDUES OF OUR PROTEIN
REMARK 3 VARIANT ARE NOT STRUCTURED (NO DISTANCE RESTRAINTS). ACCORDINGLY,
REMARK 3 THE COORDINATES FOR THE N-TERMINAL NAPHTHYLALANINE ARE NOT SHOWN
REMARK 4
REMARK 4 2CYU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000024776.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 90% H2O, 10% D2O, TRACE AMOUNTS
REMARK 210 OF DSS FOR NMR CALIBRATION
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE SGI6X, NMRVIEW 5.0.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 NAL A 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO A 4 88.86 -65.45
REMARK 500 1 ALA A 17 -17.88 -44.68
REMARK 500 1 SER A 18 35.60 -87.89
REMARK 500 1 VAL A 25 113.84 54.46
REMARK 500 1 ASP A 33 -60.40 -92.56
REMARK 500 1 LEU A 38 -108.29 -67.35
REMARK 500 1 ALA A 39 29.73 49.95
REMARK 500 2 SER A 3 68.92 -166.47
REMARK 500 2 PRO A 4 0.51 -64.23
REMARK 500 2 ASN A 14 74.18 80.68
REMARK 500 2 ALA A 17 -15.94 -45.12
REMARK 500 2 ASP A 33 -65.66 -91.69
REMARK 500 2 VAL A 34 -28.19 -38.37
REMARK 500 2 HIS A 37 -79.23 -68.52
REMARK 500 2 LEU A 38 -88.03 -48.11
REMARK 500 2 ALA A 39 159.50 -45.15
REMARK 500 3 SER A 3 68.91 -171.54
REMARK 500 3 ASN A 14 75.31 84.76
REMARK 500 3 ALA A 17 -12.29 -47.88
REMARK 500 3 HIS A 37 -75.04 -67.32
REMARK 500 3 LEU A 38 -106.43 -62.41
REMARK 500 3 ALA A 39 17.29 49.60
REMARK 500 4 SER A 3 -52.26 -178.36
REMARK 500 4 PRO A 4 1.44 -63.53
REMARK 500 4 ASN A 14 71.48 80.05
REMARK 500 4 ALA A 17 -18.17 -45.21
REMARK 500 4 ALA A 19 20.65 -76.56
REMARK 500 4 ILE A 20 -136.10 -143.48
REMARK 500 4 LYS A 21 134.23 -170.84
REMARK 500 4 THR A 23 -23.26 61.69
REMARK 500 4 ASP A 33 -63.47 -90.68
REMARK 500 4 HIS A 37 -71.84 -67.99
REMARK 500 4 LEU A 38 -105.46 -62.09
REMARK 500 5 SER A 3 69.82 -166.65
REMARK 500 5 PRO A 4 85.98 -63.40
REMARK 500 5 ALA A 17 -14.27 -47.37
REMARK 500 5 SER A 18 32.51 -87.01
REMARK 500 5 LYS A 21 -138.16 -83.32
REMARK 500 5 THR A 23 -20.91 62.88
REMARK 500 5 ARG A 28 -108.31 -87.50
REMARK 500 5 ASP A 33 -60.72 -91.05
REMARK 500 5 LEU A 38 -105.40 -62.50
REMARK 500 6 SER A 3 -51.95 -178.37
REMARK 500 6 PRO A 4 2.74 -63.91
REMARK 500 6 ASN A 14 70.77 80.77
REMARK 500 6 ALA A 17 -15.32 -46.26
REMARK 500 6 LYS A 21 -139.14 -102.70
REMARK 500 6 THR A 23 -21.22 62.45
REMARK 500 6 LEU A 38 -109.13 -71.31
REMARK 500 7 SER A 3 70.03 -173.04
REMARK 500
REMARK 500 THIS ENTRY HAS 145 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BBL RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF E3 BINDING DOMAIN OF 2-OXOGLUTARATE
REMARK 900 DEHYDROGENASE COMPLEX OF E COLI
REMARK 900 RELATED ID: 1BAL RELATED DB: PDB
REMARK 900 FAMILY OF 56 STRUCTURES OF E3 BINDING DOMAIN OF 2-OXOGLUTARATE
REMARK 900 DEHYDROGENASE COMPLEX OF E COLI WITH 10 EXTRA UNSTRUCTURED RESIDUES
REMARK 900 IN N-TERMINUS
DBREF 2CYU A 2 40 UNP P0AFG7 ODO2_ECO57 113 151
SEQRES 1 A 40 NAL LEU SER PRO ALA ILE ARG ARG LEU LEU ALA GLU HIS
SEQRES 2 A 40 ASN LEU ASP ALA SER ALA ILE LYS GLY THR GLY VAL GLY
SEQRES 3 A 40 GLY ARG LEU THR ARG GLU ASP VAL GLU LYS HIS LEU ALA
SEQRES 4 A 40 LYS
HELIX 1 1 ALA A 5 ASN A 14 1 10
HELIX 2 2 ASP A 16 ILE A 20 5 5
HELIX 3 3 THR A 30 LEU A 38 1 9
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes