HEADER GENE REGULATION/DNA 05-NOV-00 1EA4
TITLE TRANSCRIPTIONAL REPRESSOR COPG/22BP DSDNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REPRESSOR COPG;
COMPND 3 CHAIN: A, B, D, E, F, G, H, J, K, L;
COMPND 4 FRAGMENT: DNA-BINDING PROTEIN;
COMPND 5 SYNONYM: REPA PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*TP*AP*AP*CP*CP*GP*TP*GP
COMPND 9 *CP*AP*CP*TP*CP*AP*AP*TP*GP*CP*AP*AP*TP*C)-3');
COMPND 10 CHAIN: U, W, Y;
COMPND 11 FRAGMENT: 22BP SSDNA - FIRST STRAND;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA(5'-D(*AP*GP*AP*TP*TP*GP*CP*AP*TP
COMPND 15 *TP*GP*AP*GP*TP*GP*CP*AP*CP*GP*GP*TP*T)-3');
COMPND 16 CHAIN: V, X, Z;
COMPND 17 FRAGMENT: 22BP SSDNA - SECOND STRAND;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE;
SOURCE 3 ORGANISM_TAXID: 1311;
SOURCE 4 CELLULAR_LOCATION: PLASMID PMV158;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMV158;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES
KEYWDS TRANSCRIPTIONAL REPRESSOR, DNA-BINDING PROTEIN, PLASMID, PROTEIN-DNA
KEYWDS 2 COMPLEX, GENE REGULATION/DNA, GENE REGULATION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.X.GOMIS-RUETH,M.COSTA,M.SOLA,P.ACEBO,R.ERITJA,M.ESPINOSA,G.D.SOLAR,
AUTHOR 2 M.COLL
REVDAT 4 13-DEC-23 1EA4 1 DBREF
REVDAT 3 24-FEB-09 1EA4 1 VERSN
REVDAT 2 03-JUN-02 1EA4 1 SEQRES ATOM TER
REVDAT 1 05-JUL-01 1EA4 0
JRNL AUTH M.COSTA,M.SOLA,G.DEL,R.ERITJA,A.M.HERNAINDEZ-ARRIAGA,
JRNL AUTH 2 M.ESPINOSA,F.X.GOMIS-RUETH,M.COLL
JRNL TITL PLASMID TRANSCRIPTIONAL REPRESSOR COPG OLIGOMERISES TO
JRNL TITL 2 RENDER HELICAL SUPERSTRUCTURES UNBOUND AND IN COMPLEXES WITH
JRNL TITL 3 OLIGONUCLEOTIDES
JRNL REF J.MOL.BIOL. V. 310 403 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11428897
JRNL DOI 10.1006/JMBI.2001.4760
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.X.GOMIS-RUETH,M.SOLA,P.ACEBO,A.PARRAGA,A.GUASCH,R.ERITJA,
REMARK 1 AUTH 2 A.GONZALEZ,M.ESPINOSA,G.D.SOLAR,M.COLL
REMARK 1 TITL THE STRUCTURE OF PLASMID-ENCODED TRANSCRIPTIONAL REPRESSOR
REMARK 1 TITL 2 COPG UNLIGANDED AND BOUND TO ITS OPERATOR
REMARK 1 REF EMBO J. V. 17 7404 1998
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 9857196
REMARK 1 DOI 10.1093/EMBOJ/17.24.7404
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.X.GOMIS-RUETH,M.SOLA,R.PEREZ-LUQUE,P.ACEBO,M.T.ALDA,
REMARK 1 AUTH 2 A.GONZALEZ,M.ESPINOSA,G.D.SOLAR,M.COLL
REMARK 1 TITL OVEREXPRESSION, PURIFICATION, CRYSTALLIZATION AND
REMARK 1 TITL 2 PRELIMINARY X-RAY DIFFRACTION ANALYSIS OF THE PMV158-ENCODED
REMARK 1 TITL 3 PLASMID TRANSCRIPTIONAL REPRESSOR PROTEIN COPG
REMARK 1 REF FEBS LETT. V. 425 161 1998
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 9541028
REMARK 1 DOI 10.1016/S0014-5793(98)00219-1
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 17507
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3377
REMARK 3 NUCLEIC ACID ATOMS : 2535
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 101
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.340
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NOE RESTRAINTS FOR WATSON & CRICK BASE
REMARK 3 PAIRING. THE COMPLEX SET UP FOR CRYSTALLIZATION WAS MADE UP BY A
REMARK 3 COPG DIMER-OF-HOMODIMERS AND A 22-BP DSDNA. THERE ARE 2,5 OF
REMARK 3 THOSE COMPLEXES IN THE ASYMMETRIC UNIT, DEFG+WX (PROTEIN + DNA),
REMARK 3 HJKL+UV, AND ABA'B'+YZ. THE LATTER REPRESENTS THE "HALF"
REMARK 3 COMPLEX. THE OTHER HALF IS CREATED BY A CRYSTALLOGRAPHIC TWOFOLD
REMARK 3 (RENDERING A' AND B'). THE DNA PART HAS BEEN MODELLED WITH THE
REMARK 3 TWO OBSERVED ORIENTATIONS, EACH WITH OCCUPANCY 0.5. THERE ARE
REMARK 3 NCS RESTRAINTS, BUT SO MANY THAT THE MATRICES AND TRANSLATIONS
REMARK 3 HAVE NOT BEEN INCLUDED IN THIS ENTRY. ESSENTIALLY, ALL PROTEIN
REMARK 3 CHAINS AND ALL DNA STRANDS HAVE BEEN SUBJECTED TO RESTRAINTS.
REMARK 4
REMARK 4 1EA4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1290005528.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0527
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17592
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.920
REMARK 200 RESOLUTION RANGE LOW (A) : 43.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1B01
REMARK 200
REMARK 200 REMARK: ONE COPG DIMER/ 9BP DSDNA MODEL WAS USED AS SEARCHING
REMARK 200 MODEL.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, NACL, NAACO, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 106.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.02000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 106.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.02000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: FUNCTIONAL TETRAMERS (EACH ONE CONTACTING A
REMARK 300 22BP DSDNA)ARE DEFG, HJKL, AND ABA'B' (A' AND
REMARK 300 B' ARE SYMMETRYEQUIVALENT MOLECULES).TETRAMER DEFG
REMARK 300 CONTACTS DSDNA WX, HJKL PAIRS UV, ANDABA'B'
REMARK 300 INTERACTS WITH YZ(DOUBLE OCCUPANCY DUE TO
REMARK 300 CRYSTALLOGRAPHIC TWOFOLD AXIS)THE BIOMOLECULE 1 IS
REMARK 300 THE SUPERHELICAL STRUCTURE AND THETETRAMERS CAN BE
REMARK 300 GENERATED USING THE MATRICES GIVENFOR BIOMOLECULES 2
REMARK 300 , 3 AND 4
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: 32-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 32-MERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E, F, G, H, J, K, L,
REMARK 350 AND CHAINS: U, V, W, X, Y, Z
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 213.40000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 76.04000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, W, X
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, J, K, L, U, V
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Y, Z
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 213.40000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 76.04000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 REGULATES THE PLASMID COPY NUMBER BY BINDING TO THE
REMARK 400 REPAB PROMOTER THUS CONTROLING THE SYNTHESIS OF THE PLASMID
REMARK 400 REPLICATION INITIATOR PROTEIN REPB AND ITS OWN ONE.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 44
REMARK 465 LYS A 45
REMARK 465 GLY B 42
REMARK 465 GLN B 43
REMARK 465 GLU B 44
REMARK 465 LYS B 45
REMARK 465 GLU D 44
REMARK 465 LYS D 45
REMARK 465 LYS E 45
REMARK 465 GLN G 43
REMARK 465 GLU G 44
REMARK 465 LYS G 45
REMARK 465 MET H 1
REMARK 465 LYS J 45
REMARK 465 GLU K 44
REMARK 465 LYS K 45
REMARK 465 LYS L 45
REMARK 465 DT U 201
REMARK 465 DC U 222
REMARK 465 DT V 222
REMARK 465 DT Y 201
REMARK 465 DT Z 222
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 DA U 202 P OP1 OP2
REMARK 470 DT U 221 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT U 221 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT U 221 C7 C6
REMARK 470 DT V 221 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT V 221 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT V 221 C7 C6
REMARK 470 DT X 222 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT X 222 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT X 222 C7 C6
REMARK 470 DA Y 202 P OP1 OP2
REMARK 470 DC Y 213 P OP1 OP2
REMARK 470 DA Z 212 P OP1 OP2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O TYR B 39 N LYS B 41 2.04
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 LYS F 45 CE LYS F 45 NZ -0.154
REMARK 500 LYS H 45 CE LYS H 45 NZ -0.153
REMARK 500 DG Z 211 N1 DG Z 211 C2 0.052
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 DT V 214 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG Z 211 O4' - C1' - N9 ANGL. DEV. = 2.5 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 LYS A 19 -71.16 -53.06
REMARK 500 LYS B 40 51.08 -64.46
REMARK 500 GLN E 43 -31.50 -143.29
REMARK 500 GLN F 43 26.42 -144.64
REMARK 500 GLU F 44 -114.96 -69.93
REMARK 500 LYS G 2 95.67 -178.21
REMARK 500 GLN H 43 42.64 -88.47
REMARK 500 GLU H 44 -163.12 -127.81
REMARK 500 LYS K 2 45.86 -105.94
REMARK 500 LYS K 3 143.83 -22.13
REMARK 500 LYS K 19 -70.23 -58.29
REMARK 500 LYS L 2 54.62 149.48
REMARK 500 LYS L 3 140.61 -11.12
REMARK 500 LYS L 19 -71.00 -51.95
REMARK 500 GLN L 43 -44.20 -25.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH H2002 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH Y2001 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH Y2002 DISTANCE = 6.55 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B01 RELATED DB: PDB
REMARK 900 TRANSCRIPTIONAL REPRESSOR COPG/DEOXYRIBONUCLEIC ACID COMPLEX
REMARK 900 RELATED ID: 2CPG RELATED DB: PDB
REMARK 900 TRANSCRIPTIONAL REPRESSOR COPG
DBREF 1EA4 A 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 B 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 D 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 E 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 F 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 G 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 H 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 J 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 K 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 L 1 45 UNP P13920 REPA_STRPN 1 45
DBREF 1EA4 U 201 222 PDB 1EA4 1EA4 201 222
DBREF 1EA4 V 201 222 PDB 1EA4 1EA4 201 222
DBREF 1EA4 W 201 222 PDB 1EA4 1EA4 201 222
DBREF 1EA4 X 201 222 PDB 1EA4 1EA4 201 222
DBREF 1EA4 Y 202 222 PDB 1EA4 1EA4 202 222
DBREF 1EA4 Z 201 222 PDB 1EA4 1EA4 201 222
SEQRES 1 A 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 A 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 A 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 A 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 B 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 B 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 B 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 B 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 D 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 D 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 D 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 D 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 E 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 E 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 E 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 E 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 F 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 F 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 F 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 F 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 G 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 G 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 G 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 G 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 H 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 H 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 H 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 H 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 J 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 J 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 J 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 J 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 K 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 K 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 K 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 K 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 L 45 MET LYS LYS ARG LEU THR ILE THR LEU SER GLU SER VAL
SEQRES 2 L 45 LEU GLU ASN LEU GLU LYS MET ALA ARG GLU MET GLY LEU
SEQRES 3 L 45 SER LYS SER ALA MET ILE SER VAL ALA LEU GLU ASN TYR
SEQRES 4 L 45 LYS LYS GLY GLN GLU LYS
SEQRES 1 U 22 DT DA DA DC DC DG DT DG DC DA DC DT DC
SEQRES 2 U 22 DA DA DT DG DC DA DA DT DC
SEQRES 1 V 22 DA DG DA DT DT DG DC DA DT DT DG DA DG
SEQRES 2 V 22 DT DG DC DA DC DG DG DT DT
SEQRES 1 W 22 DT DA DA DC DC DG DT DG DC DA DC DT DC
SEQRES 2 W 22 DA DA DT DG DC DA DA DT DC
SEQRES 1 X 22 DA DG DA DT DT DG DC DA DT DT DG DA DG
SEQRES 2 X 22 DT DG DC DA DC DG DG DT DT
SEQRES 1 Y 22 DT DA DA DC DC DG DT DG DC DA DC DT DC
SEQRES 2 Y 22 DA DA DT DG DC DA DA DT DC
SEQRES 1 Z 22 DA DG DA DT DT DG DC DA DT DT DG DA DG
SEQRES 2 Z 22 DT DG DC DA DC DG DG DT DT
FORMUL 17 HOH *101(H2 O)
HELIX 1 1 GLU A 11 GLY A 25 1 15
HELIX 2 2 SER A 27 LYS A 40 1 14
HELIX 3 3 SER B 10 MET B 24 1 15
HELIX 4 4 SER B 27 LYS B 40 1 14
HELIX 5 5 GLU D 11 GLY D 25 1 15
HELIX 6 6 SER D 27 LYS D 41 1 15
HELIX 7 7 SER E 10 GLY E 25 1 16
HELIX 8 8 SER E 27 GLY E 42 1 16
HELIX 9 9 SER F 10 GLY F 25 1 16
HELIX 10 10 SER F 27 GLY F 42 1 16
HELIX 11 11 GLU G 11 GLY G 25 1 15
HELIX 12 12 SER G 27 LYS G 41 1 15
HELIX 13 13 GLU H 11 GLY H 25 1 15
HELIX 14 14 SER H 27 GLN H 43 1 17
HELIX 15 15 SER J 10 GLY J 25 1 16
HELIX 16 16 SER J 27 GLY J 42 1 16
HELIX 17 17 SER K 10 GLY K 25 1 16
HELIX 18 18 SER K 27 GLY K 42 1 16
HELIX 19 19 SER L 10 GLY L 25 1 16
HELIX 20 20 SER L 27 GLU L 44 1 18
SHEET 1 A 2 LYS A 3 SER A 10 0
SHEET 2 A 2 LYS B 2 LEU B 9 -1 O LEU B 9 N LYS A 3
SHEET 1 B 2 LYS D 3 SER D 10 0
SHEET 2 B 2 LYS E 2 LEU E 9 -1 O LEU E 9 N LYS D 3
SHEET 1 C 2 LYS F 2 LEU F 9 0
SHEET 2 C 2 LYS G 3 SER G 10 -1 O LEU G 9 N LYS F 3
SHEET 1 D 2 LYS H 3 SER H 10 0
SHEET 2 D 2 LYS J 2 LEU J 9 -1 O LEU J 9 N LYS H 3
SHEET 1 E 2 ARG K 4 THR K 8 0
SHEET 2 E 2 ARG L 4 THR L 8 -1 O LEU L 5 N ILE K 7
CRYST1 213.400 76.040 50.520 90.00 90.00 90.00 P 21 21 2 40
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 0.004686 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019794 0.00000
(ATOM LINES ARE NOT SHOWN.)
END