Header list of 1kvg.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 25-JAN-02 1KVG
TITLE EPO-3 BETA HAIRPIN PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN: EPO-3 RECEPTOR AGONIST;
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. IT IS A NOVEL
SOURCE 4 SEQUENCE DERIVED FROM PHAGE-DISPLAY SELECTION.
KEYWDS BETA HAIRPIN PEPTIDE, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.J.SKELTON,S.RUSSELL,F.DE SAUVAGE,A.G.COCHRAN
REVDAT 3 23-FEB-22 1KVG 1 REMARK LINK
REVDAT 2 24-FEB-09 1KVG 1 VERSN
REVDAT 1 06-MAR-02 1KVG 0
JRNL AUTH N.J.SKELTON,S.RUSSELL,F.DE SAUVAGE,A.G.COCHRAN
JRNL TITL AMINO ACID DETERMINANTS OF BETA-HAIRPIN CONFORMATION IN
JRNL TITL 2 ERYTHROPOEITIN RECEPTOR AGONIST PEPTIDES DERIVED FROM A
JRNL TITL 3 PHAGE DISPLAY LIBRARY
JRNL REF J.MOL.BIOL. V. 316 1121 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11884148
JRNL DOI 10.1006/JMBI.2002.5410
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.L.JOHNSON,F.X.FARRELL,F.P.BARBONE,F.J.MCMAHON,J.TULLAI,
REMARK 1 AUTH 2 K.HOEY,O.LIVNAH,N.C.WRIGHTON,S.A.MIDDLETON,D.A.LOUGHNEY,
REMARK 1 AUTH 3 W.J.DOWER,L.S.MULCAHY,I.A.WILSON,L.K.JOLLIFFE
REMARK 1 TITL IDENTIFICATION OF A 13 AMINO ACID PEPTIDE MIMETIC OF
REMARK 1 TITL 2 ERYTHROPOIETIN AND DESCRIPTION OF AMINO ACIDS CRITICAL FOR
REMARK 1 TITL 3 THE MIMETIC ACTIVITY OF EMP1
REMARK 1 REF BIOCHEMISTRY V. 37 3699 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI971956Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII 98.0, DISCOVER 3.1
REMARK 3 AUTHORS : TIMOTHY HAVEL (DGII), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 70 NOE DISTANCE RESTRAINTS, 8 PHI AND
REMARK 3 3 CHI-1 DIHEDRAL ANGLE RESTRAINTS.
REMARK 3 NO HYDROGEN BOND RESTRAINTS WERE EMPLOYED.
REMARK 3 NOTE THAT THE HA-HB COUPLING CONSTANTS INDICATE ROTATIONAL
REMARK 3 AVERAGING ABOUT THE PHE4 CHI-1 ANGLE.
REMARK 3 SEVERAL NOES TO THE AROMATIC RING OF PHE4 WERE NOT USED TO
REMARK 3 GENERATE RESTRAINTS AS THEY COULD BE SATISFIED
REMARK 3 BY A -60 OR 180 DEGREE ROTAMER, BUT NOT BY BOTH.
REMARK 3 THE MEAN BACKBONE ATOM RMSD TO THE MEAN STRUCTURE WITHIN THE
REMARK 3 DISULFIDE CYCLE IS 0.31 +/- 0.06 ANGSTOMS.
REMARK 4
REMARK 4 1KVG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015381.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290; 290
REMARK 210 PH : 5.1; 5.1
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 8 MM PEPTIDE; 8 MM PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-ROESY; DQF-COSY; COSY-35
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
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 : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 LEU A 7 53.20 -99.45
REMARK 500 5 LEU A 7 59.22 -99.22
REMARK 500 7 LEU A 7 54.70 -99.43
REMARK 500 9 LEU A 7 52.44 -99.40
REMARK 500 12 LEU A 7 49.47 -99.51
REMARK 500 17 LEU A 7 54.32 -99.40
REMARK 500 18 LEU A 7 54.41 -99.38
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 NH2 A 13
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GJE RELATED DB: PDB
REMARK 900 ANTAGONIST OF IGFBP-1.
REMARK 900 RELATED ID: 1KVF RELATED DB: PDB
REMARK 900 EMP-18, ERYTHROPOEITIN RECEPTOR AGONIST PEPTIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AN APPROPRIATE DATABASE MATCH WAS
REMARK 999 NOT AVAILABLE AT THE TIME OF PROCESSING.
DBREF 1KVG A 1 13 PDB 1KVG 1KVG 1 13
SEQRES 1 A 13 SER CYS HIS PHE GLY PRO LEU GLY TRP VAL CYS LYS NH2
HET NH2 A 13 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SHEET 1 A 2 CYS A 2 GLY A 5 0
SHEET 2 A 2 GLY A 8 CYS A 11 -1 O GLY A 8 N GLY A 5
SSBOND 1 CYS A 2 CYS A 11 1555 1555 2.06
LINK C LYS A 12 N NH2 A 13 1555 1555 1.33
SITE 1 AC1 1 LYS A 12
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