Header list of 1zk6.pdb file
Complete list - r 2 2 Bytes
HEADER ISOMERASE 02-MAY-05 1ZK6
TITLE NMR SOLUTION STRUCTURE OF B. SUBTILIS PRSA PPIASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOLDASE PROTEIN PRSA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PPIASE DOMAIN;
COMPND 5 EC: 5.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: PRSA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-2T;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKTH 3678
KEYWDS ALPHA/BETA STRUCTURE, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR H.TOSSAVAINEN,P.PERMI,S.L.PURHONEN,M.SARVAS,I.KILPELAINEN,R.SEPPALA
REVDAT 3 02-MAR-22 1ZK6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZK6 1 VERSN
REVDAT 1 28-MAR-06 1ZK6 0
JRNL AUTH H.TOSSAVAINEN,P.PERMI,S.L.PURHONEN,M.SARVAS,I.KILPELAINEN,
JRNL AUTH 2 R.SEPPALA
JRNL TITL NMR SOLUTION STRUCTURE AND CHARACTERIZATION OF SUBSTRATE
JRNL TITL 2 BINDING SITE OF THE PPIASE DOMAIN OF PRSA PROTEIN FROM
JRNL TITL 3 BACILLUS SUBTILIS
JRNL REF FEBS LETT. V. 580 1822 2006
JRNL REFN ISSN 0014-5793
JRNL PMID 16516208
JRNL DOI 10.1016/J.FEBSLET.2006.02.042
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, AMBER 8.0
REMARK 3 AUTHORS : VARIAN INC. (VNMR),
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZK6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032810.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM PRSA PPIASE DOMAIN
REMARK 210 U15N,13C; 20 MM BIS-TRIS BUFFER;
REMARK 210 92% H2O, 8% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, SPARKY 3.106, CYANA
REMARK 210 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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 : 1
REMARK 210
REMARK 210 REMARK: NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 114
REMARK 465 SER A 115
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 9 ARG A 119 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 3 TYR A 151 -31.02 -130.16
REMARK 500 5 TYR A 151 -34.99 -134.09
REMARK 500 6 TYR A 151 -31.75 -131.38
REMARK 500 6 PRO A 191 103.00 -54.51
REMARK 500 10 THR A 185 0.15 -64.26
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZK6 A 116 206 UNP P24327 PRSA_BACSU 135 225
SEQADV 1ZK6 GLY A 114 UNP P24327 CLONING ARTIFACT
SEQADV 1ZK6 SER A 115 UNP P24327 CLONING ARTIFACT
SEQRES 1 A 93 GLY SER GLY LYS ILE ARG ALA SER HIS ILE LEU VAL ALA
SEQRES 2 A 93 ASP LYS LYS THR ALA GLU GLU VAL GLU LYS LYS LEU LYS
SEQRES 3 A 93 LYS GLY GLU LYS PHE GLU ASP LEU ALA LYS GLU TYR SER
SEQRES 4 A 93 THR ASP SER SER ALA SER LYS GLY GLY ASP LEU GLY TRP
SEQRES 5 A 93 PHE ALA LYS GLU GLY GLN MET ASP GLU THR PHE SER LYS
SEQRES 6 A 93 ALA ALA PHE LYS LEU LYS THR GLY GLU VAL SER ASP PRO
SEQRES 7 A 93 VAL LYS THR GLN TYR GLY TYR HIS ILE ILE LYS LYS THR
SEQRES 8 A 93 GLU GLU
HELIX 1 1 ASP A 127 GLY A 141 1 15
HELIX 2 2 LYS A 143 SER A 152 1 10
HELIX 3 3 ASP A 154 GLY A 160 5 7
HELIX 4 4 THR A 175 LEU A 183 1 9
SHEET 1 A 4 ASP A 162 PHE A 166 0
SHEET 2 A 4 ILE A 118 VAL A 125 -1 N ILE A 118 O PHE A 166
SHEET 3 A 4 TYR A 198 GLU A 205 -1 O LYS A 202 N SER A 121
SHEET 4 A 4 VAL A 192 LYS A 193 -1 N VAL A 192 O HIS A 199
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 - r 2 2 Bytes