Header list of 1k43.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 05-OCT-01 1K43
TITLE 10 STRUCTURE ENSEMBLE OF THE 14-RESIDUE PEPTIDE RG-KWTY-NG-ITYE-GR
TITLE 2 (MBH12)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MBH12;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING FMOC
SOURCE 4 CHEMISTRY.
KEYWDS BETA-HAIRPIN, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.T.PASTOR,M.LOPEZ DE LA PAZ,E.LACROIX,L.SERRANO,E.PEREZ-PAYA
REVDAT 5 23-FEB-22 1K43 1 REMARK
REVDAT 4 24-FEB-09 1K43 1 VERSN
REVDAT 3 01-APR-03 1K43 1 JRNL
REVDAT 2 13-FEB-02 1K43 1 JRNL REMARK
REVDAT 1 17-OCT-01 1K43 0
JRNL AUTH M.T.PASTOR,M.LOPEZ DE LA PAZ,E.LACROIX,L.SERRANO,
JRNL AUTH 2 E.PEREZ-PAYA
JRNL TITL COMBINATORIAL APPROACHES: A NEW TOOL TO SEARCH FOR HIGHLY
JRNL TITL 2 STRUCTURED BETA-HAIRPIN PEPTIDES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 614 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11782528
JRNL DOI 10.1073/PNAS.012583999
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, GROMOS 96
REMARK 3 AUTHORS : BRUKER (XWINNMR), VAN GUNSTEREN (GROMOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 70 RESTRAINTS, 60 ARE NOE-DERIVED DISTANCE CONSTRAINTS AND 10
REMARK 3 DIHEDRAL ANGLE RESTRAINTS. THE PAIRWISE RMSD FOR RESIDUES 3-12
REMARK 3 WAS 0.38 +/- 0.21 A FOR THE BACKBONE AND 1.36 +/- 0.35 A FOR ALL
REMARK 3 HEAVY ATOMS. THE ESTIMATED BETA-HAIRPIN POPULATION OF THIS
REMARK 3 PEPTIDE IS 66 +/- 4%. THE FIRST AND LAST TWO RESIDUES (RG) ARE
REMARK 3 DISORDERED, BECAUSE THEY WERE ADDED JUST TO AVOID AGGREGATION.
REMARK 3 THE SIDE CHAINS OF TRP4, TYR6, ILE9 AND TYR11 ARE INTERACTING IN
REMARK 3 ONE SIDE OF THE BETA HAIRPIN, FORMING A HYDROPHOBIC CLUSTER.
REMARK 3 ASN7 AT POSITION L1 OF THE BETA-TURN IS DIRECTED OUTWARDS FROM
REMARK 3 THE BETA-HAIRPIN, AS EXPECTED FOR A TYPE I' BETA-TURN.
REMARK 4
REMARK 4 1K43 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014535.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PEPTIDE MBH12; 1 MM PEPTIDE
REMARK 210 MBH12; 1 MM PEPTIDE MBH12
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D ROESY; 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 : XWINNMR 2.6, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED
REMARK 210 WITH TORSION ANGLE DYNAMICS
REMARK 210 (DYANA)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
REMARK 210
REMARK 210 REMARK: NULL
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 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 TYR A 6 139.68 -172.03
REMARK 500 2 LYS A 3 136.62 -179.96
REMARK 500 2 GLU A 12 69.21 -102.80
REMARK 500 3 LYS A 3 137.05 -174.58
REMARK 500 3 GLU A 12 78.90 -117.42
REMARK 500 8 LYS A 3 132.65 -178.73
REMARK 500 8 GLU A 12 65.67 -68.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J4M RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1K43 A 1 14 PDB 1K43 1K43 1 14
SEQRES 1 A 14 ARG GLY LYS TRP THR TYR ASN GLY ILE THR TYR GLU GLY
SEQRES 2 A 14 ARG
SHEET 1 A 2 TRP A 4 TYR A 6 0
SHEET 2 A 2 ILE A 9 TYR A 11 -1 O TYR A 11 N TRP A 4
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 - 23 20 Bytes