Header list of 1uao.pdb file
Complete list - 26 20 Bytes
HEADER DE NOVO PROTEIN 13-MAR-03 1UAO
TITLE NMR STRUCTURE OF DESIGNED PROTEIN, CHIGNOLIN, CONSISTING OF ONLY TEN
TITLE 2 AMINO ACIDS (ENSEMBLES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIGNOLIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE WAS DESIGNED ON THE BASIS OF STATISTICS
SOURCE 4 DERIVED FROM NUMEROUS PROTEIN SEGMENTS.
KEYWDS DE NOVO PROTEIN, BETA-HAIRPIN, MINI-PROTEIN, G-PEPTIDE, AUTONOMOUS
KEYWDS 2 ELEMENT
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.HONDA,K.YAMASAKI
REVDAT 4 26-AUG-15 1UAO 1 JRNL VERSN
REVDAT 3 24-FEB-09 1UAO 1 VERSN
REVDAT 2 17-AUG-04 1UAO 1 JRNL
REVDAT 1 13-APR-04 1UAO 0
JRNL AUTH S.HONDA,K.YAMASAKI,Y.SAWADA,H.MORII
JRNL TITL 10 RESIDUE FOLDED PEPTIDE DESIGNED BY SEGMENT STATISTICS
JRNL REF STRUCTURE V. 12 1507 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15296744
JRNL DOI 10.1016/J.STR.2004.05.022
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 185 RESTRAINTS, 172 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 12
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,1 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1UAO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-03.
REMARK 100 THE RCSB ID CODE IS RCSB005623.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSOHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM CHIGNOLIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D ROESY; DQF-COSY; 2D
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, FELIX 2000, X-PLOR
REMARK 210 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 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 4 TRP A 9 -167.59 -69.03
REMARK 500 7 THR A 6 -53.23 -121.01
REMARK 500 8 TRP A 9 38.27 -87.59
REMARK 500 11 TRP A 9 -72.89 -84.72
REMARK 500 12 TRP A 9 57.70 -93.27
REMARK 500 13 TRP A 9 42.80 -90.88
REMARK 500 18 TRP A 9 79.66 -101.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5694 RELATED DB: BMRB
REMARK 900 NMR STRUCTURE OF DESIGNED PROTEIN, CHIGNOLIN, ONSISTING OF
REMARK 900 ONLY TEN AMINO ACIDS
REMARK 900 RELATED ID: 2RVD RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025
REMARK 900 RELATED ID: 5AWL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025
DBREF 1UAO A 1 10 PDB 1UAO 1UAO 1 10
SEQRES 1 A 10 GLY TYR ASP PRO GLU THR GLY THR TRP GLY
SHEET 1 A 2 TYR A 2 ASP A 3 0
SHEET 2 A 2 THR A 8 TRP A 9 -1 O THR A 8 N ASP A 3
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 - 26 20 Bytes