Header list of 1e0q.pdb file
Complete list - 12 20 Bytes
HEADER PROTEIN BINDING 05-APR-00 1E0Q
TITLE MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF
TITLE 2 UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYUBIQUITIN-B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-17;
COMPND 5 SYNONYM: UBIQUITIN;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 4 ORGANISM_COMMON: CATTLE;
SOURCE 5 ORGANISM_TAXID: 9913
KEYWDS PROTEIN BINDING, MUTANT PEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR R.ZERELLA,P.Y.CHEN,P.A.EVANS,A.RAINE,D.H.WILLIAMS
REVDAT 4 15-MAY-13 1E0Q 1 COMPND JRNL REMARK ATOM
REVDAT 4 2 TER MASTER
REVDAT 3 07-NOV-12 1E0Q 1 HEADER COMPND SOURCE KEYWDS
REVDAT 3 2 JRNL REMARK VERSN DBREF
REVDAT 3 3 SEQADV
REVDAT 2 24-FEB-09 1E0Q 1 VERSN
REVDAT 1 16-JAN-01 1E0Q 0
JRNL AUTH R.ZERELLA,P.Y.CHEN,P.A.EVANS,A.RAINE,D.H.WILLIAMS
JRNL TITL STRUCTURAL CHARACTERIZATION OF A MUTANT PEPTIDE DERIVED
JRNL TITL 2 FROM UBIQUITIN: IMPLICATIONS FOR PROTEIN FOLDING.
JRNL REF PROTEIN SCI. V. 9 2142 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 11152124
JRNL DOI 10.1110/PS.9.11.2142
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 1E0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-APR-00.
REMARK 100 THE PDBE ID CODE IS EBI-4820.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275
REMARK 210 PH : 3.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O AND 90%
REMARK 210 WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX500; DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.8
REMARK 210 METHOD USED : SIMULATED ANNEALING FROM
REMARK 210 RANDOM COORDINATES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D NMR
REMARK 210 SPECTROSCOPY ON A NON-LABELLED SAMPLE.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 PHE A 4 CD1 PHE A 4 CE1 0.124
REMARK 500 1 PHE A 4 CD2 PHE A 4 CE2 0.128
REMARK 500 1 PHE A 4 CE1 PHE A 4 CZ 0.148
REMARK 500 1 PHE A 4 CE2 PHE A 4 CZ 0.149
REMARK 500 1 PHE A 4 CG PHE A 4 CD1 0.163
REMARK 500 1 PHE A 4 CG PHE A 4 CD2 0.142
REMARK 500 2 PHE A 4 CD1 PHE A 4 CE1 0.124
REMARK 500 2 PHE A 4 CD2 PHE A 4 CE2 0.129
REMARK 500 2 PHE A 4 CE1 PHE A 4 CZ 0.147
REMARK 500 2 PHE A 4 CE2 PHE A 4 CZ 0.148
REMARK 500 2 PHE A 4 CG PHE A 4 CD1 0.163
REMARK 500 2 PHE A 4 CG PHE A 4 CD2 0.142
REMARK 500 3 PHE A 4 CD1 PHE A 4 CE1 0.123
REMARK 500 3 PHE A 4 CD2 PHE A 4 CE2 0.129
REMARK 500 3 PHE A 4 CE1 PHE A 4 CZ 0.147
REMARK 500 3 PHE A 4 CE2 PHE A 4 CZ 0.149
REMARK 500 3 PHE A 4 CG PHE A 4 CD1 0.164
REMARK 500 3 PHE A 4 CG PHE A 4 CD2 0.142
REMARK 500 4 PHE A 4 CD1 PHE A 4 CE1 0.123
REMARK 500 4 PHE A 4 CD2 PHE A 4 CE2 0.127
REMARK 500 4 PHE A 4 CE1 PHE A 4 CZ 0.148
REMARK 500 4 PHE A 4 CE2 PHE A 4 CZ 0.148
REMARK 500 4 PHE A 4 CG PHE A 4 CD1 0.162
REMARK 500 4 PHE A 4 CG PHE A 4 CD2 0.144
REMARK 500 5 PHE A 4 CD1 PHE A 4 CE1 0.125
REMARK 500 5 PHE A 4 CD2 PHE A 4 CE2 0.127
REMARK 500 5 PHE A 4 CE1 PHE A 4 CZ 0.149
REMARK 500 5 PHE A 4 CE2 PHE A 4 CZ 0.149
REMARK 500 5 PHE A 4 CG PHE A 4 CD1 0.160
REMARK 500 5 PHE A 4 CG PHE A 4 CD2 0.146
REMARK 500 6 PHE A 4 CD1 PHE A 4 CE1 0.125
REMARK 500 6 PHE A 4 CD2 PHE A 4 CE2 0.127
REMARK 500 6 PHE A 4 CE1 PHE A 4 CZ 0.147
REMARK 500 6 PHE A 4 CE2 PHE A 4 CZ 0.149
REMARK 500 6 PHE A 4 CG PHE A 4 CD1 0.159
REMARK 500 6 PHE A 4 CG PHE A 4 CD2 0.149
REMARK 500 7 PHE A 4 CD1 PHE A 4 CE1 0.123
REMARK 500 7 PHE A 4 CD2 PHE A 4 CE2 0.128
REMARK 500 7 PHE A 4 CE1 PHE A 4 CZ 0.148
REMARK 500 7 PHE A 4 CE2 PHE A 4 CZ 0.148
REMARK 500 7 PHE A 4 CG PHE A 4 CD1 0.164
REMARK 500 7 PHE A 4 CG PHE A 4 CD2 0.141
REMARK 500 8 PHE A 4 CD1 PHE A 4 CE1 0.125
REMARK 500 8 PHE A 4 CD2 PHE A 4 CE2 0.126
REMARK 500 8 PHE A 4 CE1 PHE A 4 CZ 0.147
REMARK 500 8 PHE A 4 CE2 PHE A 4 CZ 0.147
REMARK 500 8 PHE A 4 CG PHE A 4 CD1 0.159
REMARK 500 8 PHE A 4 CG PHE A 4 CD2 0.150
REMARK 500 9 PHE A 4 CD1 PHE A 4 CE1 0.124
REMARK 500 9 PHE A 4 CD2 PHE A 4 CE2 0.126
REMARK 500
REMARK 500 THIS ENTRY HAS 162 BOND DEVIATIONS.
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 2 LEU A 8 -18.70 79.09
REMARK 500 3 ASP A 9 -42.35 -140.35
REMARK 500 7 LEU A 8 -18.86 79.05
REMARK 500 21 LEU A 8 -9.34 75.78
REMARK 500 24 LEU A 8 -10.31 77.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AAR RELATED DB: PDB
REMARK 900 UBIQUITIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THR 9 HAS BEEN REPLACED BY ASP
DBREF 1E0Q A 1 17 UNP P0CG53 UBB_BOVIN 1 17
SEQADV 1E0Q ASP A 9 UNP P0CG53 THR 9 ENGINEERED MUTATION
SEQRES 1 A 17 MET GLN ILE PHE VAL LYS THR LEU ASP GLY LYS THR ILE
SEQRES 2 A 17 THR LEU GLU VAL
SHEET 1 A 2 GLN A 2 THR A 7 0
SHEET 2 A 2 LYS A 11 GLU A 16 -1 O LYS A 11 N THR A 7
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 - 12 20 Bytes