Header list of 1jy4.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 11-SEP-01 1JY4
TITLE B4DIMER: A DE NOVO DESIGNED EIGHT-STRANDED BETA-SHEET ASSEMBLED USING
TITLE 2 A DISULFIDE BOND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: B4DIMER;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS EIGHT-STRANDED BETA-SHEET, DISULFIDE BOND, DE NOVO PROTEIN DESIGN, DE
KEYWDS 2 NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.VENKATRAMAN,G.A.NAGANA GOWDA,P.BALARAM
REVDAT 3 23-FEB-22 1JY4 1 REMARK LINK
REVDAT 2 24-FEB-09 1JY4 1 VERSN
REVDAT 1 12-JUN-02 1JY4 0
JRNL AUTH J.VENKATRAMAN,G.A.NAGANA GOWDA,P.BALARAM
JRNL TITL DESIGN AND CONSTRUCTION OF AN OPEN MULTISTRANDED BETA-SHEET
JRNL TITL 2 POLYPEPTIDE STABILIZED BY A DISULFIDE BRIDGE.
JRNL REF J.AM.CHEM.SOC. V. 124 4987 2002
JRNL REFN ISSN 0002-7863
JRNL PMID 11982362
JRNL DOI 10.1021/JA0174276
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE TEN STRUCTURES WERE DETERMINED BY NMR AND TORSION ANGLE
REMARK 3 DYNAMICS/SIMULATED ANNEALING METHODS. THE PEPTIDE DIMER WAS
REMARK 3 TREATED AS A SINGLE ENTITY AND SYMMETRY ELEMENTS WERE NOT UTILIZED
REMARK 3 DURING STRUCTURE CALCULATIONS. THE STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 446 RESTRAINTS, 398 ARE NOE-DERIVED DISTANCE CONSTRAINTS,48
REMARK 3 DISTANCE RESTRAINTS ARE FROM HYDROGEN BONDS. THE LIST OF
REMARK 3 CONSTRAINTS IS AVAILABLE IN THE FILE DYANA_UPPERCONST.TXT.
REMARK 3 STRUCTURE CALCULATIONS WERE PERFORMED WITH THE PROGRAM DYANA-1.5
REMARK 3 (P. GUENTERT, C. MUMENTHALER, K. WUTHRICH, J. MOL. BIOL.(1997)
REMARK 3 VOL.273, 283-298). NO VIOLATION OF DISTANCE CONSTRAINTS FROM NOES
REMARK 3 EXCEEDED 0.3ANGSTROMS.
REMARK 3 THE ENSEMBLE OF STRUCTURES IS SUPERIMPOSED OVER THE BEST-
REMARK 3 STRUCTURED REGION ENCOMPASING RESIDUES E11-L34. THE AVERAGE RMSDS
REMARK 3 BETWEEN THE SUPERPOSED STRUCTURES AND THE AVERAGE STRUCTURE ARE AS
REMARK 3 FOLLOWS:
REMARK 3 0.75(CHAIN A, RESIDUES 11-34, BACKBONE ATOMS)
REMARK 3 0.72(CHAIN B, RESIDUES 11-34, BACKBONE ATOMS.
REMARK 4
REMARK 4 1JY4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014320.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : UNBUFFERED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM B4DIMER, CD3OH
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
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 : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS/
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 2 GLU A 3 35.09 -154.44
REMARK 500 2 LYS A 5 -140.11 -111.15
REMARK 500 2 VAL A 25 79.25 -116.65
REMARK 500 2 LEU A 34 67.22 -117.78
REMARK 500 3 GLU B 3 65.89 -116.09
REMARK 500 3 LYS B 5 -141.47 -119.48
REMARK 500 4 DPR A 9 -27.40 74.95
REMARK 500 4 LEU A 34 56.85 -115.94
REMARK 500 4 ALA B 18 17.60 91.54
REMARK 500 5 GLU A 3 73.72 -116.26
REMARK 500 5 CYS A 4 42.57 -150.03
REMARK 500 5 CYS B 4 63.93 -119.64
REMARK 500 5 DPR B 9 -23.08 74.85
REMARK 500 6 DPR A 9 -30.42 75.06
REMARK 500 6 ALA A 18 27.55 -160.65
REMARK 500 6 LEU A 26 89.34 -150.60
REMARK 500 6 CYS B 4 75.64 -115.70
REMARK 500 6 DPR B 17 -31.96 74.97
REMARK 500 6 ALA B 18 -27.97 162.30
REMARK 500 7 ALA A 18 21.68 91.14
REMARK 500 7 LEU A 34 53.96 -109.99
REMARK 500 7 LEU B 34 67.92 -114.41
REMARK 500 8 GLU A 3 67.94 -117.50
REMARK 500 9 THR A 7 65.88 -118.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JY6 RELATED DB: PDB
REMARK 900 B4DIMERA: A DE NOVO DESIGNED FOUR-STRANDED BETA-SHEET ASSEMBLED
REMARK 900 USING A DISULFIDE BOND
DBREF 1JY4 A 1 35 PDB 1JY4 1JY4 1 35
DBREF 1JY4 B 1 35 PDB 1JY4 1JY4 1 35
SEQRES 1 A 35 ARG GLY GLU CYS LYS PHE THR VAL DPR GLY ARG THR ALA
SEQRES 2 A 35 LEU ASN THR DPR ALA VAL GLN LYS TRP HIS PHE VAL LEU
SEQRES 3 A 35 DPR GLY TYR LYS CYS GLU ILE LEU ALA
SEQRES 1 B 35 ARG GLY GLU CYS LYS PHE THR VAL DPR GLY ARG THR ALA
SEQRES 2 B 35 LEU ASN THR DPR ALA VAL GLN LYS TRP HIS PHE VAL LEU
SEQRES 3 B 35 DPR GLY TYR LYS CYS GLU ILE LEU ALA
MODRES 1JY4 DPR A 9 PRO D-PROLINE
MODRES 1JY4 DPR A 17 PRO D-PROLINE
MODRES 1JY4 DPR A 27 PRO D-PROLINE
MODRES 1JY4 DPR B 9 PRO D-PROLINE
MODRES 1JY4 DPR B 17 PRO D-PROLINE
MODRES 1JY4 DPR B 27 PRO D-PROLINE
HET DPR A 9 14
HET DPR A 17 14
HET DPR A 27 14
HET DPR B 9 14
HET DPR B 17 14
HET DPR B 27 14
HETNAM DPR D-PROLINE
FORMUL 1 DPR 6(C5 H9 N O2)
SHEET 1 A 8 LYS A 5 VAL A 8 0
SHEET 2 A 8 ARG A 11 THR A 16 -1 O ALA A 13 N PHE A 6
SHEET 3 A 8 VAL A 19 LEU A 26 -1 O VAL A 19 N THR A 16
SHEET 4 A 8 TYR A 29 ALA A 35 -1 O CYS A 31 N PHE A 24
SHEET 5 A 8 TYR B 29 ALA B 35 -1 O GLU B 32 N LYS A 30
SHEET 6 A 8 VAL B 19 LEU B 26 -1 N GLN B 20 O ALA B 35
SHEET 7 A 8 ARG B 11 THR B 16 -1 N THR B 12 O HIS B 23
SHEET 8 A 8 LYS B 5 VAL B 8 -1 N VAL B 8 O ARG B 11
SSBOND 1 CYS A 31 CYS B 31 1555 1555 2.00
LINK C VAL A 8 N DPR A 9 1555 1555 1.36
LINK C DPR A 9 N GLY A 10 1555 1555 1.32
LINK C THR A 16 N DPR A 17 1555 1555 1.36
LINK C DPR A 17 N ALA A 18 1555 1555 1.33
LINK C LEU A 26 N DPR A 27 1555 1555 1.36
LINK C DPR A 27 N GLY A 28 1555 1555 1.33
LINK C VAL B 8 N DPR B 9 1555 1555 1.36
LINK C DPR B 9 N GLY B 10 1555 1555 1.32
LINK C THR B 16 N DPR B 17 1555 1555 1.36
LINK C DPR B 17 N ALA B 18 1555 1555 1.32
LINK C LEU B 26 N DPR B 27 1555 1555 1.36
LINK C DPR B 27 N GLY B 28 1555 1555 1.32
CRYST1 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