Header list of 1p6r.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 30-APR-03 1P6R
TITLE SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE REPRESSOR BLAI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLINASE REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-82);
COMPND 5 SYNONYM: REGULATORY PROTEIN BLAI, BETA-LACTAMASE REPRESSOR PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 1402;
SOURCE 4 GENE: BLAI OR PENI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22
KEYWDS TRANSCRIPTION REGULATION, REPRESSOR, DNA-BINDING, WINGED HELIX
KEYWDS 2 PROTEIN, BACTERIAL RESISTANCE TO ANTIBIOTICS, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR H.V.MELCKEBEKE,C.VREULS,P.GANS,G.LLABRES,P.FILEE,B.JORIS,J.P.SIMORRE
REVDAT 3 23-FEB-22 1P6R 1 REMARK
REVDAT 2 24-FEB-09 1P6R 1 VERSN
REVDAT 1 09-DEC-03 1P6R 0
JRNL AUTH H.V.MELCKEBEKE,C.VREULS,P.GANS,G.LLABRES,B.JORIS,J.P.SIMORRE
JRNL TITL SOLUTION STRUCTURAL STUDY OF BLAI: IMPLICATIONS FOR THE
JRNL TITL 2 REPRESSION OF GENES INVOLVED IN BETA-LACTAM ANTIBIOTIC
JRNL TITL 3 RESISTANCE.
JRNL REF J.MOL.BIOL. V. 333 711 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14568532
JRNL DOI 10.1016/J.JMB.2003.09.005
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000, AMBER 1991
REMARK 3 AUTHORS : ACCELRYS (FELIX), PEARLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FOR STRUCTURE CALCULATION, A TOTAL OF
REMARK 3 1252 INTERPROTON AND 110 DIHEDRAL RESTRAINTS WERE USED. THE
REMARK 3 DISTANCE CONSTRAINTS CONTAIN 596 INTRARESIDUE, 205 SEQUENTIAL,
REMARK 3 87 MEDIUM-RANGE, 145 LONG-RANGE, AND 219 AMBIGUOUS CORRELATIONS.
REMARK 4
REMARK 4 1P6R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019077.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7.6; 7.6
REMARK 210 IONIC STRENGTH : 300 MM KCL, 75 MM PHOSPHATE
REMARK 210 SODIUM; 300 MM KCL, 75 MM
REMARK 210 PHOSPHATE SODIUM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N 0.75 MM, PHOSPHATE BUFFER
REMARK 210 75 MM PH 7.6, 300 MM KCL 90% H2O,
REMARK 210 10% D2O; U-15N-13C 0.50 MM,
REMARK 210 PHOSPHATE BUFFER 75 MM PH 7.6,
REMARK 210 300 MM KCL 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D-13C-
REMARK 210 SEPARATED NOESY OPTIMIZED FOR CH
REMARK 210 GROUPS; 4D 13C-SEPARATED-HSQC-
REMARK 210 NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER 2000, TALOS 1999
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
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: 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 THR A 38 70.98 -68.16
REMARK 500 1 ASP A 73 -55.36 -156.29
REMARK 500 1 ASP A 76 81.44 -68.32
REMARK 500 1 TYR A 77 75.52 62.73
REMARK 500 1 LYS A 81 76.00 -64.76
REMARK 500 2 SER A 23 -158.16 -131.93
REMARK 500 2 GLU A 62 77.78 -110.21
REMARK 500 2 SER A 75 -76.52 -65.38
REMARK 500 2 ASP A 76 40.76 -73.59
REMARK 500 3 LYS A 2 -67.71 60.54
REMARK 500 3 SER A 23 -158.17 -131.91
REMARK 500 3 THR A 38 60.41 -68.29
REMARK 500 3 GLU A 74 -78.59 56.61
REMARK 500 3 ASP A 76 -77.90 53.72
REMARK 500 4 ILE A 4 74.04 -152.40
REMARK 500 4 SER A 23 -157.90 -131.46
REMARK 500 4 LYS A 81 -119.40 -179.23
REMARK 500 6 SER A 22 -61.69 -98.83
REMARK 500 6 GLU A 74 -72.63 62.18
REMARK 500 6 TYR A 77 115.84 -162.78
REMARK 500 7 LYS A 2 -70.51 68.92
REMARK 500 7 SER A 23 -158.48 -132.68
REMARK 500 7 THR A 36 -62.12 -93.24
REMARK 500 7 THR A 38 66.43 -67.84
REMARK 500 7 ASP A 73 -62.07 -155.11
REMARK 500 7 ASP A 76 -105.82 48.82
REMARK 500 7 LYS A 81 55.86 -104.49
REMARK 500 8 ILE A 4 61.71 33.20
REMARK 500 8 GLN A 6 78.96 -69.26
REMARK 500 8 SER A 23 -157.57 -131.54
REMARK 500 8 THR A 36 -70.03 -98.48
REMARK 500 8 ALA A 56 -70.54 -97.97
REMARK 500 8 PRO A 70 88.51 -64.33
REMARK 500 8 GLU A 74 -70.83 -34.41
REMARK 500 8 SER A 75 31.39 -90.49
REMARK 500 8 LYS A 81 -131.37 60.79
REMARK 500 9 LYS A 3 -57.44 -150.25
REMARK 500 9 SER A 23 -157.26 -132.50
REMARK 500 9 THR A 38 81.74 -65.30
REMARK 500 10 ILE A 4 68.65 -155.36
REMARK 500 10 SER A 23 -159.66 -132.71
REMARK 500 10 THR A 38 70.40 -69.24
REMARK 500 10 TYR A 77 49.99 -72.99
REMARK 500 11 SER A 23 -158.25 -132.44
REMARK 500 11 THR A 38 78.76 -64.83
REMARK 500 11 ASP A 76 33.05 -94.87
REMARK 500 11 TYR A 77 -78.17 -64.17
REMARK 500 11 LYS A 81 -50.12 -158.94
REMARK 500 12 GLN A 6 48.29 -80.35
REMARK 500 12 SER A 23 -156.60 -130.65
REMARK 500
REMARK 500 THIS ENTRY HAS 82 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 TYR A 68 0.13 SIDE CHAIN
REMARK 500 1 TYR A 77 0.08 SIDE CHAIN
REMARK 500 2 PHE A 66 0.09 SIDE CHAIN
REMARK 500 2 TYR A 68 0.12 SIDE CHAIN
REMARK 500 3 TYR A 68 0.09 SIDE CHAIN
REMARK 500 3 TYR A 77 0.18 SIDE CHAIN
REMARK 500 4 TYR A 68 0.08 SIDE CHAIN
REMARK 500 6 PHE A 66 0.13 SIDE CHAIN
REMARK 500 7 TYR A 68 0.14 SIDE CHAIN
REMARK 500 8 TYR A 68 0.08 SIDE CHAIN
REMARK 500 9 TYR A 68 0.07 SIDE CHAIN
REMARK 500 10 PHE A 66 0.08 SIDE CHAIN
REMARK 500 10 TYR A 68 0.13 SIDE CHAIN
REMARK 500 11 TYR A 68 0.12 SIDE CHAIN
REMARK 500 12 PHE A 66 0.08 SIDE CHAIN
REMARK 500 13 ARG A 64 0.08 SIDE CHAIN
REMARK 500 13 TYR A 77 0.12 SIDE CHAIN
REMARK 500 14 TYR A 68 0.10 SIDE CHAIN
REMARK 500 15 TYR A 68 0.09 SIDE CHAIN
REMARK 500 16 PHE A 66 0.07 SIDE CHAIN
REMARK 500 16 TYR A 68 0.10 SIDE CHAIN
REMARK 500 17 TYR A 68 0.12 SIDE CHAIN
REMARK 500 18 PHE A 66 0.09 SIDE CHAIN
REMARK 500 18 TYR A 77 0.09 SIDE CHAIN
REMARK 500 19 TYR A 68 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P6R A 1 82 UNP P06555 BLAI_BACLI 1 82
SEQRES 1 A 82 MET LYS LYS ILE PRO GLN ILE SER ASP ALA GLU LEU GLU
SEQRES 2 A 82 VAL MET LYS VAL ILE TRP LYS HIS SER SER ILE ASN THR
SEQRES 3 A 82 ASN GLU VAL ILE LYS GLU LEU SER LYS THR SER THR TRP
SEQRES 4 A 82 SER PRO LYS THR ILE GLN THR MET LEU LEU ARG LEU ILE
SEQRES 5 A 82 LYS LYS GLY ALA LEU ASN HIS HIS LYS GLU GLY ARG VAL
SEQRES 6 A 82 PHE VAL TYR THR PRO ASN ILE ASP GLU SER ASP TYR ILE
SEQRES 7 A 82 GLU VAL LYS SER
HELIX 1 1 SER A 8 LYS A 20 1 13
HELIX 2 2 THR A 26 SER A 37 1 12
HELIX 3 3 SER A 40 LYS A 54 1 15
SHEET 1 A 3 ILE A 24 ASN A 25 0
SHEET 2 A 3 VAL A 65 PRO A 70 -1 O TYR A 68 N ILE A 24
SHEET 3 A 3 LEU A 57 GLU A 62 -1 N HIS A 60 O VAL A 67
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 - b 23 2 Bytes