Header list of 1jic.pdb file
Complete list - 29 201 Bytes
HEADER DNA BINDING PROTEIN 20-JUL-98 1JIC
TITLE SOLUTION NMR STRUCTURE OF RECOMBINANT SSO7D WITH RNASE ACTIVITY,
TITLE 2 MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SSO7D;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 CELL_LINE: BL21;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSE;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS THERMOSTABLE RIBONUCLEASE, DNA-BINDING, SULFOLOBUS SOLFATARICUS,
KEYWDS 2 RNASE AND DNA-BINDING PROTEIN, DNA-BINDING PROTEIN, DNA BINDING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
AUTHOR R.CONSONNI,L.SANTOMO,L.ZETTA
REVDAT 4 29-NOV-17 1JIC 1 KEYWDS REMARK HELIX
REVDAT 3 24-FEB-09 1JIC 1 VERSN
REVDAT 2 01-APR-03 1JIC 1 JRNL
REVDAT 1 14-OCT-98 1JIC 0
JRNL AUTH R.CONSONNI,L.SANTOMO,P.FUSI,L.ZETTA
JRNL TITL A SINGLE-POINT MUTATION IN THE EXTREME HEAT- AND
JRNL TITL 2 PRESSURE-RESISTANT SSO7D PROTEIN FROM SULFOLOBUS
JRNL TITL 3 SOLFATARICUS LEADS TO A MAJOR REARRANGEMENT OF THE
JRNL TITL 4 HYDROPHOBIC CORE.
JRNL REF BIOCHEMISTRY V. 38 12709 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10504241
JRNL DOI 10.1021/BI9911280
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.FUSI,K.GOOSSENS,R.CONSONNI,M.GRISA,P.PURICELLI,G.VECCHIO,
REMARK 1 AUTH 2 M.VANONI,L.ZETTA,K.HEREMANS,P.TORTORA
REMARK 1 TITL EXTREME HEAT-AND PRESSURE-RESISTANT 7-KDA PROTEIN P2 FROM
REMARK 1 TITL 2 THE ARCHAEON SULFOLOBUS SOLFATARICUS IS DRAMATICALLY
REMARK 1 TITL 3 DESTABILIZED BY A SINGLE-POINT AMINO ACID SUBSTITUTION
REMARK 1 REF PROTEINS V. 29 381 1997
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.CONSONNI,R.LIMIROLI,H.MOLINARI,P.FUSI,M.GRISA,M.VANONI,
REMARK 1 AUTH 2 P.TORTORA
REMARK 1 TITL 1H-NMR AND PHOTO-CIDNP SPECTROSCOPIES SHOW A POSSIBLE ROLE
REMARK 1 TITL 2 FOR TRP23 AND PHE31 IN NUCLEIC ACID BINDING BY P2
REMARK 1 TITL 3 RIBONUCLEASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS
REMARK 1 REF FEBS LETT. V. 372 135 1995
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 2.9
REMARK 3 AUTHORS : DAUBER-OSGUTHORPE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JIC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174332.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CLEAN TOCSY; DQF COSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER, FELIX
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY TERM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE MINIMIZED AVERAGE STRUCTURE WAS DETERMINED USING 15
REMARK 210 SELECTED CONFORMERS
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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 10 CD GLU A 10 OE2 0.118
REMARK 500 GLU A 11 CD GLU A 11 OE2 0.118
REMARK 500 GLU A 35 CD GLU A 35 OE2 0.119
REMARK 500 GLU A 47 CD GLU A 47 OE2 0.118
REMARK 500 GLU A 53 CD GLU A 53 OE2 0.119
REMARK 500 GLU A 59 CD GLU A 59 OE2 0.120
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.8 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 TYR A 7 -81.22 -114.03
REMARK 500 LYS A 8 -100.38 -113.05
REMARK 500 GLU A 35 -12.00 -140.21
REMARK 500 LYS A 52 -49.91 -152.28
REMARK 500 LYS A 60 -58.33 -163.60
REMARK 500 GLN A 61 -84.64 -73.78
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JIC A 1 62 UNP P39476 DN72_SULSO 1 62
SEQRES 1 A 62 ALA THR VAL LYS PHE LYS TYR LYS GLY GLU GLU LYS GLN
SEQRES 2 A 62 VAL ASP ILE SER LYS ILE LYS LYS VAL TRP ARG VAL GLY
SEQRES 3 A 62 LYS MET ILE SER PHE THR TYR ASP GLU GLY GLY GLY LYS
SEQRES 4 A 62 THR GLY ARG GLY ALA VAL SER GLU LYS ASP ALA PRO LYS
SEQRES 5 A 62 GLU LEU LEU GLN MET LEU GLU LYS GLN LYS
HELIX 1 1 ILE A 16 ILE A 19 5 4
HELIX 2 2 GLU A 47 ALA A 50 5 4
HELIX 3 3 LYS A 52 MET A 57 5 6
SHEET 1 A 2 THR A 2 TYR A 7 0
SHEET 2 A 2 GLU A 10 ILE A 16 -1 N VAL A 14 O VAL A 3
SHEET 1 B 3 LYS A 20 VAL A 25 0
SHEET 2 B 3 MET A 28 TYR A 33 -1 O THR A 32 N LYS A 21
SHEET 3 B 3 GLY A 41 GLU A 47 -1 O VAL A 45 N ILE A 29
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
Complete list - 29 201 Bytes