Header list of 1n0a.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 11-OCT-02 1N0A
TITLE TURN STABILITY IN BETA-HAIRPIN PEPTIDES: 3:5 TYPE I G1 BULGE TURNS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BHPW_PDG, BETA-HAIRPIN PEPTIDE;
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.
KEYWDS BETA HAIRPIN, BETA-TURN, BETA-BULGE, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR T.BLANDL,A.G.COCHRAN,N.J.SKELTON
REVDAT 3 23-FEB-22 1N0A 1 REMARK LINK
REVDAT 2 24-FEB-09 1N0A 1 VERSN
REVDAT 1 21-OCT-03 1N0A 0
JRNL AUTH T.BLANDL,A.G.COCHRAN,N.J.SKELTON
JRNL TITL TURN STABILITY IN BETA-HAIRPIN PEPTIDES: INVESTIGATION OF
JRNL TITL 2 PEPTIDES CONTAINING 3:5 TYPE I G1 BULGE TURNS
JRNL REF PROTEIN SCI. V. 12 237 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 12538887
JRNL DOI 10.1110/PS.0228603
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII 98.0, DISCOVER 3.0
REMARK 3 AUTHORS : TIM HAVEL (DGII), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 100 DISTANCE GEOMETRY STRUCTURES WERE CALCULATED. THE 80
REMARK 3 STRUCTURES OF LOWEST PENALTY FUNCTION WERE FURTHER REFINED USING
REMARK 3 RESTRAINED MOLECULAR DYNAMICS.
REMARK 3 THE 20 STRUCTURES OF LOWEST RESTRAINT VIOLATION ENERGY WERE USED
REMARK 3 TO DESCRIBE THE STRUCTURE.
REMARK 3 61 DISTANCE AND 21 DIHEDRAL ANGLE RESTRAINTS WERE USED.
REMARK 3 THE FINAL ENSEMBLE HAS NO DISTANCE VIOLATIONS GREATER THAN 0.1 A
REMARK 3 AND NO DIHEDRAL ANGLE VIOALTIONS GREATER THAN 1 DEGREE.
REMARK 3 95% OF THE RESIDUES ARE IN THE MOST FAVOURABLE REGION OF THE
REMARK 3 RAMACHANDRAN PLOT.
REMARK 3 THE MEAN BACKBONE ATOM RMSD TO THE MEAN STRUCTURE IS 0.29+/-0.05 A.
REMARK 4
REMARK 4 1N0A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017358.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 5.0; 5.0
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 8 MM PEPTIDE, NO BUFFER; 8 MM
REMARK 210 PEPTIDE, NO BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D ROESY; 2D TOCSY; DQF-COSY; 2D
REMARK 210 COSY-35; 2D 13C-HMQC
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 2001, FELIX 98.0,
REMARK 210 XWINNMR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AUGMENTED BY LOOSE PHI AND PSI RESTRAINTS
REMARK 210 GENERATED FROM TALOS. MODEL 21 IS THE AVERAGE MINIMIZED
REMARK 210 STRUCTURE.
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 800
REMARK 800 SITE
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: 1N09 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS NO SEQUENCE DATABASE REFERENCE SINCE
REMARK 999 THE PEPTIDE IS A DE NOVO DESIGNED SEQUENCE.
DBREF 1N0A A 0 12 PDB 1N0A 1N0A 0 12
SEQRES 1 A 13 ACE CYS THR TRP GLU PRO ASP GLY LYS LEU THR CYS NH2
HET ACE A 0 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 2 TRP A 3 0
SHEET 2 A 2 LEU A 9 THR A 10 -1 O THR A 10 N THR A 2
SSBOND 1 CYS A 1 CYS A 11 1555 1555 2.05
LINK C ACE A 0 N CYS A 1 1555 1555 1.34
LINK C CYS A 11 N NH2 A 12 1555 1555 1.34
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