HEADER TRANSCRIPTION 28-DEC-03 1RZS
TITLE SOLUTION STRUCTURE OF P22 CRO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATORY PROTEIN CRO;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANTIREPRESSOR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22;
SOURCE 3 ORGANISM_TAXID: 10754;
SOURCE 4 GENE: CRO;
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: PET21B
KEYWDS HELIX-TURN-HELIX, DNA-BINDING PROTEIN, STRUCTURAL EVOLUTION,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR T.NEWLOVE,J.H.KONIECZKA,M.H.CORDES
REVDAT 3 02-MAR-22 1RZS 1 REMARK
REVDAT 2 24-FEB-09 1RZS 1 VERSN
REVDAT 1 01-JUN-04 1RZS 0
JRNL AUTH T.NEWLOVE,J.H.KONIECZKA,M.H.CORDES
JRNL TITL SECONDARY STRUCTURE SWITCHING IN CRO PROTEIN EVOLUTION.
JRNL REF STRUCTURE V. 12 569 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15062080
JRNL DOI 10.1016/J.STR.2004.02.024
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), A. BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 30 STRUCTURES WERE CALCULATED USING 916
REMARK 3 NOE-DERIVED DISTANCE RESTRAINTS, 10 HYDROGEN BOND DISTANCE
REMARK 3 RESTRAINTS, 41 PHI ANGLE RESTRAINTS AND 5 CHI1 ANGLE RESTRAINTS.
REMARK 3 23 OF 30 CALCULATED STRUCTURES WERE INITIALLY ACCEPTED BASED ON
REMARK 3 NO DISTANCE RESTRAINT VIOLATIONS GREATER THAN 0.4 ANGSTROMS AND
REMARK 3 NO ANGLE RESTRAINT VIOLATIONS GREATER THAN 5 DEGREES. OF THE 23,
REMARK 3 2 WERE ELIMINATED FOR HAVING SIGNIFICANTLY HIGHER ENERGY THAN
REMARK 3 THE OTHERS, LEAVING 21 STRUCTURES IN THE FINAL ENSEMBLE. THE
REMARK 3 ORDERED REGION OF THE STRUCTURE INCLUDES RESIDUES 1-57. PAIRWISE
REMARK 3 RMSDS FOR THE ORDERED REGION WERE 0.53 A (BACKBONE ATOMS) AND
REMARK 3 1.29 A (ALL HEAVY ATOMS). NONE OF THE BACKBONE ANGLES IN THE
REMARK 3 ORDERED REGION OF ANY ENSEMBLE MEMBER FELL OUTSIDE THE MOST
REMARK 3 FAVORABLE AND ADDITIONALLY ALLOWED REGIONS OF A RAMACHANDRAN
REMARK 3 PLOT.
REMARK 4
REMARK 4 1RZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021188.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 300
REMARK 210 PH : 6.4; 6.4
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE; 50 MM
REMARK 210 SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 6 MM P22 CRO, 50 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10%
REMARK 210 D2O; 3.5 MM P22 CRO U-15N, 50 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 90% H2O,
REMARK 210 10% D2O; 2.75 MM P22 CRO U-15N,
REMARK 210 13C, 50 MM SODIUM PHOSPHATE
REMARK 210 BUFFER, 90% H2O, 10% D2O; 3.5 MM
REMARK 210 P22 CRO U-15N, 50 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA; HNHB; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HYDROGEN
REMARK 210 EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 4.1.3, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : AGREEMENT WITH DISTANCE AND
REMARK 210 ANGLE RESTRAINTS; TWO STRUCTURES
REMARK 210 WERE ALSO ELIMINATED DUE TO HIGH
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: 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 LYS A 31 -163.64 -121.39
REMARK 500 1 GLU A 54 45.12 -86.06
REMARK 500 1 ASN A 55 -62.00 -90.34
REMARK 500 1 ALA A 60 63.86 -155.06
REMARK 500 2 GLN A 59 35.15 -150.32
REMARK 500 3 PRO A 35 -175.96 -51.78
REMARK 500 3 ASN A 55 -70.44 -53.28
REMARK 500 3 ALA A 60 -66.86 -92.70
REMARK 500 4 ILE A 22 -96.41 -111.73
REMARK 500 4 ALA A 60 98.41 -160.03
REMARK 500 5 PRO A 35 176.44 -49.38
REMARK 500 6 LYS A 31 -163.52 -110.25
REMARK 500 6 PRO A 35 168.74 -48.54
REMARK 500 6 ASN A 55 -75.00 -46.48
REMARK 500 7 PRO A 35 -179.90 -53.33
REMARK 500 7 THR A 46 39.06 -83.43
REMARK 500 7 ALA A 47 27.22 49.26
REMARK 500 7 ALA A 60 -81.14 63.04
REMARK 500 8 TYR A 57 29.59 -146.45
REMARK 500 9 TRP A 30 170.98 -55.17
REMARK 500 9 PRO A 35 179.56 -49.27
REMARK 500 9 TYR A 57 28.74 -153.07
REMARK 500 10 LYS A 31 -163.50 -110.54
REMARK 500 10 TYR A 57 23.11 -142.07
REMARK 500 10 ALA A 60 -70.97 -100.71
REMARK 500 11 LYS A 31 -164.27 -127.71
REMARK 500 11 TYR A 40 -70.29 -66.48
REMARK 500 11 THR A 46 32.60 -83.16
REMARK 500 12 LYS A 31 -169.81 -105.39
REMARK 500 12 TYR A 40 -70.42 -67.37
REMARK 500 13 LYS A 31 -163.25 -119.32
REMARK 500 13 THR A 46 37.78 -88.26
REMARK 500 13 ALA A 47 28.83 46.89
REMARK 500 13 GLU A 54 44.69 -90.10
REMARK 500 13 ASN A 55 -74.79 -90.28
REMARK 500 14 PRO A 35 158.34 -49.24
REMARK 500 14 GLU A 54 37.42 -90.12
REMARK 500 14 ARG A 58 45.92 -98.20
REMARK 500 14 ALA A 60 33.10 -145.39
REMARK 500 15 TRP A 30 -178.18 -53.17
REMARK 500 15 ASN A 55 -74.96 -72.76
REMARK 500 15 ALA A 60 -78.48 64.89
REMARK 500 16 GLU A 54 38.09 -90.25
REMARK 500 16 ASN A 55 -76.90 -90.40
REMARK 500 17 ALA A 19 -46.29 -132.07
REMARK 500 17 PRO A 35 -175.05 -53.55
REMARK 500 17 ALA A 60 -47.37 -139.16
REMARK 500 18 LYS A 31 -166.61 -126.71
REMARK 500 18 PRO A 35 171.35 -51.00
REMARK 500 18 GLU A 54 46.33 -89.16
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RZS A 1 61 UNP P09964 RCRO_BPP22 1 61
SEQRES 1 A 61 MET TYR LYS LYS ASP VAL ILE ASP HIS PHE GLY THR GLN
SEQRES 2 A 61 ARG ALA VAL ALA LYS ALA LEU GLY ILE SER ASP ALA ALA
SEQRES 3 A 61 VAL SER GLN TRP LYS GLU VAL ILE PRO GLU LYS ASP ALA
SEQRES 4 A 61 TYR ARG LEU GLU ILE VAL THR ALA GLY ALA LEU LYS TYR
SEQRES 5 A 61 GLN GLU ASN ALA TYR ARG GLN ALA ALA
HELIX 1 1 TYR A 2 GLY A 11 1 10
HELIX 2 2 THR A 12 GLY A 21 1 10
HELIX 3 3 SER A 23 TRP A 30 1 8
HELIX 4 4 PRO A 35 THR A 46 1 12
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
(ATOM LINES ARE NOT SHOWN.)
END