Header list of 2cvr.pdb file
Complete list - v 10 2 Bytes
HEADER DNA BINDING PROTEIN 13-JUN-05 2CVR TITLE NMR SOLUTION STRUCTURE OF SSO7D MUTANT, K12L, 12 CONFORMERS COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA-BINDING PROTEIN 7A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SSO7D, 7 KDA DNA-BINDING PROTEIN A, ENDORIBONUCLEASE P2, COMPND 5 P7SS; COMPND 6 EC: 3.1.27.-; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS; SOURCE 3 ORGANISM_TAXID: 2287; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSE; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7 KEYWDS DNA-BINDING PROTEIN, THERMOSTABLE PROTEIN, SULFOLOBUS SOLFATARICUS, KEYWDS 2 SINGLE POINT MUTATION, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 12 MDLTYP MINIMIZED AVERAGE AUTHOR I.AROSIO,T.RECCA,R.CONSONNI,E.ALBERTI,P.FUSI,L.ZETTA REVDAT 4 10-NOV-21 2CVR 1 REMARK SEQADV REVDAT 3 04-APR-12 2CVR 1 SPRSDE VERSN REVDAT 2 24-FEB-09 2CVR 1 VERSN REVDAT 1 29-AUG-06 2CVR 0 SPRSDE 04-APR-12 2CVR 1R83 JRNL AUTH I.AROSIO,T.RECCA,R.CONSONNI,E.ALBERTI,P.FUSI,L.ZETTA JRNL TITL STRUCTURAL DETERMINANTS RESPONSIBLE FOR THE THERMOSTABILITY JRNL TITL 2 OF SSO7D AND ITS SINGLE POINT MUTANTS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.CONSONNI,L.SANTOMO,P.FUSI,P.TORTORA,L.ZETTA REMARK 1 TITL A SINGLE-POINT MUTATION IN THE EXTREME HEAT- AND REMARK 1 TITL 2 PRESSURE-RESISTANT SSO7D PROTEIN FROM SULFOLOBUS REMARK 1 TITL 3 SOLFATARICUS LEADS TO A MAJOR REARRANGEMENT OF THE REMARK 1 TITL 4 HYDROPHOBIC CORE REMARK 1 REF BIOCHEMISTRY V. 38 12709 1999 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 10504241 REMARK 1 DOI 10.1021/BI9911280 REMARK 1 REFERENCE 2 REMARK 1 AUTH R.CONSONNI,I.AROSIO,B.BELLONI,F.FOGOLARI,P.FUSI,E.SHEHI, REMARK 1 AUTH 2 L.ZETTA REMARK 1 TITL INVESTIGATIONS OF SSO7D CATALYTIC RESIDUES BY NMR TITRATION REMARK 1 TITL 2 SHIFTS AND ELECTROSTATIC CALCULATIONS REMARK 1 REF BIOCHEMISTRY V. 42 1421 2003 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 12578354 REMARK 1 DOI 10.1021/BI0265168 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 3.0 REMARK 3 AUTHORS : DAUBER-OSGUTHORPE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 683 RESTRAINTS, 660 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 7 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 16 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS. REMARK 4 REMARK 4 2CVR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000024677. 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 : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM K12L; 90% H2O, 10% D2O; 2MM REMARK 210 K12L; 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D 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 : FELIX 98.0, DISCOVER 3.0, REMARK 210 XWINNMR 2.6 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12 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: 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HB2 LYS A 21 OG1 THR A 32 0.98 REMARK 500 HB2 LYS A 21 HG1 THR A 32 1.11 REMARK 500 CB LYS A 21 OG1 THR A 32 2.02 REMARK 500 REMARK 500 REMARK: NULL 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 1 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 2 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 3 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 4 GLU A 35 CD GLU A 35 OE2 0.119 REMARK 500 5 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 6 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 7 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 8 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 9 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 10 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 11 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 12 GLU A 35 CD GLU A 35 OE2 0.117 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 1 LYS A 27 CA - CB - CG ANGL. DEV. = 20.1 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 1 PHE A 5 76.75 -160.91 REMARK 500 1 LYS A 8 -98.28 -136.62 REMARK 500 1 GLU A 35 81.00 -162.27 REMARK 500 1 THR A 40 96.78 59.23 REMARK 500 1 ASP A 49 74.18 -159.41 REMARK 500 2 TYR A 7 -87.88 -91.81 REMARK 500 2 LYS A 8 -70.70 -115.04 REMARK 500 2 LYS A 21 93.25 67.25 REMARK 500 2 LYS A 27 -69.01 -94.41 REMARK 500 2 GLU A 35 67.30 -163.64 REMARK 500 2 LYS A 39 63.25 168.18 REMARK 500 2 GLU A 47 43.69 -97.78 REMARK 500 2 ASP A 49 57.14 -160.30 REMARK 500 2 GLU A 59 38.90 -160.39 REMARK 500 3 LYS A 20 -76.89 -76.80 REMARK 500 3 VAL A 22 95.21 56.61 REMARK 500 3 GLU A 35 84.20 -166.19 REMARK 500 3 GLU A 59 -91.29 -154.16 REMARK 500 3 LYS A 60 148.89 146.35 REMARK 500 3 GLN A 61 -100.75 -125.28 REMARK 500 4 GLU A 10 136.33 174.61 REMARK 500 4 LYS A 20 -74.99 -91.24 REMARK 500 4 LYS A 27 -50.05 102.86 REMARK 500 4 GLU A 35 78.58 -164.37 REMARK 500 4 LYS A 39 77.60 -153.68 REMARK 500 4 GLU A 59 66.72 -152.20 REMARK 500 5 PHE A 5 86.03 -164.63 REMARK 500 5 TYR A 7 -80.86 -85.39 REMARK 500 5 LYS A 20 -89.17 -93.88 REMARK 500 5 ASP A 49 47.34 -159.28 REMARK 500 5 GLU A 59 64.89 -101.04 REMARK 500 6 TYR A 7 -89.44 -143.94 REMARK 500 6 LYS A 8 -76.68 -103.42 REMARK 500 6 LYS A 20 -102.95 -92.88 REMARK 500 6 VAL A 25 35.74 -159.01 REMARK 500 6 LYS A 27 -73.91 -84.07 REMARK 500 6 GLU A 35 89.08 -164.10 REMARK 500 6 THR A 40 98.38 57.79 REMARK 500 6 ASP A 49 61.31 -151.03 REMARK 500 6 GLN A 61 -108.73 -115.75 REMARK 500 7 TYR A 7 -81.28 -144.92 REMARK 500 7 LYS A 8 -78.08 -111.61 REMARK 500 7 LYS A 21 93.32 57.27 REMARK 500 7 LYS A 27 73.56 154.00 REMARK 500 7 MET A 28 -177.29 60.08 REMARK 500 7 GLU A 35 76.46 -165.51 REMARK 500 7 LYS A 39 -40.06 -147.06 REMARK 500 7 THR A 40 -168.60 53.00 REMARK 500 7 ASP A 49 47.46 -106.53 REMARK 500 8 LYS A 21 116.52 73.47 REMARK 500 REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JIC RELATED DB: PDB REMARK 900 SSO7D RECOMBINANT WILD TYPE PROTEIN REMARK 900 RELATED ID: 1B4O RELATED DB: PDB REMARK 900 F31A MUTANT OF THE RECOMBINANT SSO7D DBREF 2CVR A 1 62 UNP P61991 DN71_SULSO 1 62 SEQADV 2CVR LEU A 12 UNP P61991 LYS 12 ENGINEERED MUTATION SEQRES 1 A 62 ALA THR VAL LYS PHE LYS TYR LYS GLY GLU GLU LEU 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 LYS A 52 LEU A 58 1 7 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 VAL A 22 VAL A 25 0 SHEET 2 B 3 MET A 28 GLU A 35 -1 O THR A 32 N LYS A 21 SHEET 3 B 3 THR A 40 GLU A 47 -1 N GLY A 41 O TYR A 33 CISPEP 1 LYS A 21 VAL A 22 3 7.27 CISPEP 2 LEU A 58 GLU A 59 3 -1.02 CISPEP 3 LYS A 39 THR A 40 8 4.52 CISPEP 4 GLU A 35 GLY A 36 9 -0.81 CISPEP 5 LEU A 58 GLU A 59 9 1.93 CISPEP 6 TYR A 7 LYS A 8 10 0.34 CISPEP 7 LYS A 8 GLY A 9 10 -8.35 CISPEP 8 LYS A 21 VAL A 22 11 3.12 CISPEP 9 GLU A 35 GLY A 36 11 0.78 CISPEP 10 LEU A 58 GLU A 59 12 -0.80 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 - v 10 2 Bytes