Header list of 1n09.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 11-OCT-02 1N09
TITLE A MINIMAL BETA-HAIRPIN PEPTIDE SCAFFOLD FOR BETA-TURN DISPLAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BHPW, DISULFIDE CYCLIZED BETA-HAIRPIN PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: THE STRUCTURE HAS A TRYPTOPHAN AND LEUCINE NON-
COMPND 6 HYDROGEN-BONDED CROSS-STRAND PAIR.
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS BETA HAIRPIN, BETA TURN, CYCLIC DISULFIDE, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.J.RUSSELL,T.BLANDL,N.J.SKELTON,A.G.COCHRAN
REVDAT 3 23-FEB-22 1N09 1 REMARK LINK
REVDAT 2 24-FEB-09 1N09 1 VERSN
REVDAT 1 04-FEB-03 1N09 0
JRNL AUTH S.J.RUSSELL,T.BLANDL,N.J.SKELTON,A.G.COCHRAN
JRNL TITL STABILITY OF CYCLIC BETA-HAIRPINS: ASYMMETRIC CONTRIBUTIONS
JRNL TITL 2 FROM SIDE CHAINS OF A HYDROGEN-BONDED CROSS-STRAND RESIDUE
JRNL TITL 3 PAIR
JRNL REF J.AM.CHEM.SOC. V. 125 388 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 12517150
JRNL DOI 10.1021/JA028075L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.G.COCHRAN,R.T.TONG,M.A.STAROVASNIK,E.J.PARK,R.S.MCDOWELL,
REMARK 1 AUTH 2 J.E.THEAKER,N.J.SKELTON
REMARK 1 TITL A MINIMAL PEPTIDE SCAFFOLD FOR BETA-TURN DISPLAY: OPTIMIZING
REMARK 1 TITL 2 A STRAND POSITION IN DISULFIDE-CYCLIZED BETA-HAIRPINS
REMARK 1 REF J.AM.CHEM.SOC. V. 123 625 2001
REMARK 1 REFN ISSN 0002-7863
REMARK 1 DOI 10.1021/JA003369X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, AMBER 6.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE, KOLLMAN, ET. AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 100 STRUCTURES WERE CALCULATED USING DISTANCE GEOMETRY.
REMARK 3 THE 80 STRUCTURES OF LOWEST PENALTY FUNCTION WERE REFINED USING
REMARK 3 THE SANDER MODULE OF AMBER (V6.0).
REMARK 3 THE CALCULATION EMPLOYED 79 DISTANCE RESTRAINTS, 12 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS AND 13 CHEMICAL SHIFT RESTRAINTS.
REMARK 3 THE 20 STRUCTURES OF LOWEST VIOLATION ENERGY WERE CHOSEN TO
REMARK 3 REPRESENT THE STRUCTURE.
REMARK 3 THERE ARE NO VIOLATIONS OF THE INPUT RESTRAINTS > 0.1 A OR 2
REMARK 3 DEGREES.
REMARK 3 THE RMS. DIFFERENCE BETWEEN CALCULATION AND OBSERVED CHEMICAL
REMARK 3 SHIFTS IS 0.09 PPM.
REMARK 3 79% OF THE BACKBONE GEOMETRIES ARE IN THE MOST FAVOURABLE REGION
REMARK 3 OF THE RAMACHANDRAN PLOT.
REMARK 3 THE BACKBONE HEAVY ATOM RMSD FROM THE MEAN STRUCTURE IS 0.39+/-
REMARK 3 0.08 A.
REMARK 4
REMARK 4 1N09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017357.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 288
REMARK 210 PH : 5.0; 5.0
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 5 MM PEPTIDE, UNBUFFERED AT PH
REMARK 210 5.0; 5 MM PEPTIDE, UNBUFFERED AT
REMARK 210 PH 5.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D ROESY; 2D
REMARK 210 COSY-35
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 : FELIX 980, DGII 980, AMBER 6.O
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND RESTRAINED
REMARK 210 MOLECULAR DYNAMICS WITH CHEMICAL
REMARK 210 SHIFT RESTRAINTS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: CHEMICAL SHIFT ASSIGNMENTS WERE DETERMINED USING STANDARD
REMARK 210 2D 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 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 ASN A 7 17.17 -149.46
REMARK 500 4 GLU A 5 75.67 -118.95
REMARK 500 4 ASN A 7 11.27 -143.74
REMARK 500 5 ASN A 7 17.87 -148.15
REMARK 500 6 GLU A 5 71.70 -105.40
REMARK 500 9 ASN A 7 27.21 -142.64
REMARK 500 14 GLU A 5 77.53 -103.68
REMARK 500 16 ASN A 7 13.20 -147.69
REMARK 500 18 ASN A 7 -19.70 -142.45
REMARK 500 20 ASN A 7 -1.82 -145.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N0C RELATED DB: PDB
REMARK 900 STABILITY OF CYCLIC BETA-HAIRPINS: ASYMMETRIC CONTIBUTIONS FROM
REMARK 900 SIDE CHAINS OF HYDROGEN BONDED CROSS-STRAND RESIDUE PAIR
REMARK 900 RELATED ID: 1N0D RELATED DB: PDB
REMARK 900 STABILITY OF CYCLIC BETA-HAIRPINS: ASYMMETRIC CONTIBUTIONS FROM
REMARK 900 SIDE CHAINS OF HYDROGEN BONDED CROSS-STRAND RESIDUE PAIR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS NO SEQUENCE DATABASE
REMARK 999 REFERENCE SINCE THE PEPTIDE IS A
REMARK 999 DE NOVO DESIGNED SEQUENCE.
DBREF 1N09 A 1 12 PDB 1N09 1N09 1 12
SEQRES 1 A 12 ACE CYS THR TRP GLU GLY ASN LYS LEU THR CYS NH2
HET ACE A 1 6
HET NH2 A 12 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
SHEET 1 A 2 THR A 3 GLU A 5 0
SHEET 2 A 2 LYS A 8 THR A 10 -1 O LYS A 8 N GLU A 5
SSBOND 1 CYS A 2 CYS A 11 1555 1555 2.05
LINK C ACE A 1 N CYS A 2 1555 1555 1.33
LINK C CYS A 11 N NH2 A 12 1555 1555 1.33
SITE 1 AC1 1 CYS A 11
SITE 1 AC2 1 CYS A 11
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