Header list of 2f52.pdb file
Complete list - r 9 2 Bytes
HEADER DNA BINDING PROTEIN/TRANSCRIPTION 25-NOV-05 2F52
TITLE SOLUTION STRUCTURE OF COLD SHOCK PROTEIN CSPB FROM BACILLUS SUBTILIS
TITLE 2 IN COMPLEX WITH HEPTATHYMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLD SHOCK PROTEIN CSPB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAJOR COLD SHOCK PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: CSPB, CSPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS BETA BARREL, OB-FOLD, DNA BINDING PROTEIN-TRANSCRIPTION COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR M.ZEEB,H.STICHT,J.BALBACH
REVDAT 4 09-MAR-22 2F52 1 REMARK
REVDAT 3 24-FEB-09 2F52 1 VERSN
REVDAT 2 24-OCT-06 2F52 1 JRNL
REVDAT 1 19-SEP-06 2F52 0
JRNL AUTH M.ZEEB,K.E.MAX,U.WEININGER,C.LOW,H.STICHT,J.BALBACH
JRNL TITL RECOGNITION OF T-RICH SINGLE-STRANDED DNA BY THE COLD SHOCK
JRNL TITL 2 PROTEIN BS-CSPB IN SOLUTION.
JRNL REF NUCLEIC ACIDS RES. V. 34 4561 2006
JRNL REFN ISSN 0305-1048
JRNL PMID 16956971
JRNL DOI 10.1093/NAR/GKL376
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2.3, X-PLOR 1.2.1
REMARK 3 AUTHORS : MSI (FELIX), NIH (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F52 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035462.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 53MM BUFFER SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM CSPB U-15N, 50MM NA
REMARK 210 -CACODYLATE, 3MM MGCL2, 1.2MM
REMARK 210 HEPTATHYMIDINE, 90% H2O, 10% D2O;
REMARK 210 0.8MM CSPB U-15N, 13C, 50MM NA-
REMARK 210 CACODYLATE, 3MM MGCL2, 1.2MM
REMARK 210 HEPTATHYMIDINE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; RDC WITH
REMARK 210 IPAP
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 1.2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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 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 H LYS A 7 O PHE A 17 1.52
REMARK 500 H ASN A 10 O PHE A 15 1.55
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 GLU A 21 108.87 -59.22
REMARK 500 1 ASP A 24 -174.19 -52.92
REMARK 500 1 PHE A 38 54.48 168.96
REMARK 500 1 PHE A 49 166.78 172.81
REMARK 500 2 ASP A 24 -176.44 -54.46
REMARK 500 2 PHE A 49 165.82 174.63
REMARK 500 3 ASP A 24 -177.38 -51.13
REMARK 500 3 PHE A 49 165.67 173.39
REMARK 500 4 ASP A 24 -176.60 -55.02
REMARK 500 4 PHE A 49 165.39 175.13
REMARK 500 5 ASP A 24 -175.02 -55.28
REMARK 500 5 PHE A 38 46.94 -175.42
REMARK 500 5 PHE A 49 167.66 171.29
REMARK 500 5 ASN A 62 78.23 43.63
REMARK 500 6 ASP A 24 -177.12 -53.52
REMARK 500 6 PHE A 49 164.70 176.28
REMARK 500 6 ASN A 62 73.91 43.19
REMARK 500 7 ASP A 24 -178.35 -55.31
REMARK 500 7 PHE A 38 40.38 -178.96
REMARK 500 7 PHE A 49 168.56 172.75
REMARK 500 7 ASN A 62 74.41 41.27
REMARK 500 8 ASP A 24 -177.40 -53.54
REMARK 500 8 LEU A 41 174.68 -59.69
REMARK 500 8 PHE A 49 164.42 175.83
REMARK 500 8 ASN A 62 73.91 38.62
REMARK 500 9 ASP A 24 -175.74 -54.79
REMARK 500 9 PHE A 49 166.48 171.69
REMARK 500 9 ASN A 62 74.56 38.68
REMARK 500 10 ASP A 24 -179.21 -54.75
REMARK 500 10 PHE A 49 166.14 172.26
REMARK 500 10 ASN A 62 71.90 42.82
REMARK 500 11 GLU A 21 99.93 -59.08
REMARK 500 11 ASP A 24 -163.41 -60.24
REMARK 500 11 GLN A 34 151.37 -43.79
REMARK 500 11 PHE A 49 168.59 172.15
REMARK 500 11 ASN A 62 79.41 43.86
REMARK 500 12 ASP A 24 -171.24 -54.81
REMARK 500 12 PHE A 38 38.33 -152.52
REMARK 500 12 PHE A 49 166.03 172.79
REMARK 500 12 ASN A 62 66.72 37.58
REMARK 500 13 ASP A 24 -173.70 -55.19
REMARK 500 13 PHE A 38 30.13 -144.15
REMARK 500 13 PHE A 49 169.30 169.25
REMARK 500 13 ASN A 62 72.74 41.13
REMARK 500 14 ASP A 24 -176.83 -52.53
REMARK 500 14 PHE A 38 44.85 -169.57
REMARK 500 14 THR A 40 99.70 -67.50
REMARK 500 14 PHE A 49 165.88 173.38
REMARK 500 14 ASN A 62 73.73 38.17
REMARK 500 15 ASP A 24 -178.96 -52.84
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 56 0.25 SIDE CHAIN
REMARK 500 2 ARG A 56 0.32 SIDE CHAIN
REMARK 500 3 ARG A 56 0.17 SIDE CHAIN
REMARK 500 4 ARG A 56 0.20 SIDE CHAIN
REMARK 500 5 ARG A 56 0.31 SIDE CHAIN
REMARK 500 6 ARG A 56 0.24 SIDE CHAIN
REMARK 500 7 ARG A 56 0.32 SIDE CHAIN
REMARK 500 8 ARG A 56 0.27 SIDE CHAIN
REMARK 500 9 ARG A 56 0.27 SIDE CHAIN
REMARK 500 10 ARG A 56 0.29 SIDE CHAIN
REMARK 500 11 ARG A 56 0.23 SIDE CHAIN
REMARK 500 12 ARG A 56 0.31 SIDE CHAIN
REMARK 500 13 ARG A 56 0.32 SIDE CHAIN
REMARK 500 14 ARG A 56 0.16 SIDE CHAIN
REMARK 500 15 ARG A 56 0.20 SIDE CHAIN
REMARK 500 16 ARG A 56 0.29 SIDE CHAIN
REMARK 500 17 ARG A 56 0.23 SIDE CHAIN
REMARK 500 18 ARG A 56 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CSP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE B. SUBTILIS MAJOR COLD-SHOCK PROTEIN
REMARK 900 RELATED ID: 1NMF RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF MAJOR COLD-SHOCK PROTEIN
DBREF 2F52 A 1 67 UNP P32081 CSPB_BACSU 1 67
SEQRES 1 A 67 MET LEU GLU GLY LYS VAL LYS TRP PHE ASN SER GLU LYS
SEQRES 2 A 67 GLY PHE GLY PHE ILE GLU VAL GLU GLY GLN ASP ASP VAL
SEQRES 3 A 67 PHE VAL HIS PHE SER ALA ILE GLN GLY GLU GLY PHE LYS
SEQRES 4 A 67 THR LEU GLU GLU GLY GLN ALA VAL SER PHE GLU ILE VAL
SEQRES 5 A 67 GLU GLY ASN ARG GLY PRO GLN ALA ALA ASN VAL THR LYS
SEQRES 6 A 67 GLU ALA
HELIX 1 1 HIS A 29 ILE A 33 5 5
SHEET 1 A 6 LEU A 2 ASN A 10 0
SHEET 2 A 6 PHE A 15 GLU A 19 -1 O PHE A 17 N LYS A 7
SHEET 3 A 6 ASP A 25 VAL A 28 -1 O VAL A 26 N ILE A 18
SHEET 4 A 6 PRO A 58 LYS A 65 1 O ALA A 60 N PHE A 27
SHEET 5 A 6 ALA A 46 GLU A 53 -1 N GLU A 50 O ALA A 61
SHEET 6 A 6 LEU A 2 ASN A 10 -1 N LEU A 2 O PHE A 49
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 9 2 Bytes