HEADER GENE REGULATION/DNA 19-MAY-05 1ZRD
TITLE 4 CRYSTAL STRUCTURES OF CAP-DNA WITH ALL BASE-PAIR SUBSTITUTIONS AT
TITLE 2 POSITION 6, CAP-[6A;17T]ICAP38 DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*AP*TP*TP*TP*CP*GP*AP*AP*AP*AP*AP*TP*GP*AP*GP*AP*T)-
COMPND 3 3';
COMPND 4 CHAIN: W, Y;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*CP*TP*AP*GP*AP*TP*CP*TP*CP*AP*TP*TP*TP*TP*TP*CP*GP*AP
COMPND 8 *AP*AP*T)-3';
COMPND 9 CHAIN: X, Z;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: CATABOLITE GENE ACTIVATOR;
COMPND 13 CHAIN: A, B;
COMPND 14 SYNONYM: CAMP RECEPTOR PROTEIN, CAMP-REGULATORY PROTEIN;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 562;
SOURCE 8 GENE: CRP, CAP, CSM;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PAKCRP1
KEYWDS PROTEIN-DNA COMPLEX, CAP, CAP-DNA, CATABOLITE GENE ACTIVATOR PROTEIN,
KEYWDS 2 CAMP RECEPTOR PROTEIN, CRP, GENE REGULATION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.BERMAN,A.A.NAPOLI
REVDAT 4 23-AUG-23 1ZRD 1 REMARK
REVDAT 3 11-OCT-17 1ZRD 1 REMARK
REVDAT 2 24-FEB-09 1ZRD 1 VERSN
REVDAT 1 21-MAR-06 1ZRD 0
JRNL AUTH A.A.NAPOLI,C.L.LAWSON,R.H.EBRIGHT,H.M.BERMAN
JRNL TITL INDIRECT READOUT OF DNA SEQUENCE AT THE PRIMARY-KINK SITE IN
JRNL TITL 2 THE CAP-DNA COMPLEX: RECOGNITION OF PYRIMIDINE-PURINE AND
JRNL TITL 3 PURINE-PURINE STEPS.
JRNL REF J.MOL.BIOL. V. 357 173 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16427082
JRNL DOI 10.1016/J.JMB.2005.12.051
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.63
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) (%) : 77.9
REMARK 3 NUMBER OF REFLECTIONS : 16375
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) : 0.224
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1599
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.93
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1563
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 174
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3160
REMARK 3 NUCLEIC ACID ATOMS : 1546
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -19.09000
REMARK 3 B22 (A**2) : -0.64000
REMARK 3 B33 (A**2) : 19.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.49
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.57
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.970
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 44.46
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : CMP.PAR
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : CMP_TOP.TOP
REMARK 3 TOPOLOGY FILE 4 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000033030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17903
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.79700
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 1ZRC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2MM CAMP, 0.1M MES, 0.2M NACL, 0.05M
REMARK 280 MGCL2, 5% PEG 8000, 15% DIOXANE, PH 6.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 30.64450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.03900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.67250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.03900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.64450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.67250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X, Y, Z, A, B
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 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 VAL A 1
REMARK 465 LEU A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 THR A 7
REMARK 465 THR A 208
REMARK 465 ARG A 209
REMARK 465 VAL B 1
REMARK 465 LEU B 2
REMARK 465 GLY B 3
REMARK 465 LYS B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 THR B 7
REMARK 465 THR B 208
REMARK 465 ARG B 209
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 OH TYR A 63 OE2 GLU A 171 2.18
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 DG W 7 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG Z -4 O4' - C1' - N9 ANGL. DEV. = 1.8 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 THR A 10 -31.30 -38.19
REMARK 500 LYS A 26 -3.64 78.09
REMARK 500 GLU A 37 4.56 -161.57
REMARK 500 GLN A 66 129.35 -36.11
REMARK 500 LEU A 75 -7.47 -58.06
REMARK 500 VAL A 108 19.44 -140.30
REMARK 500 ASN A 109 82.97 154.85
REMARK 500 PRO A 110 1.80 -69.91
REMARK 500 CYS A 178 171.66 179.90
REMARK 500 PRO B 9 -100.78 -55.56
REMARK 500 HIS B 19 76.60 -112.55
REMARK 500 LYS B 26 6.62 86.21
REMARK 500 GLU B 37 20.46 -156.79
REMARK 500 GLU B 54 2.66 -65.76
REMARK 500 ASN B 65 -155.63 -101.53
REMARK 500 ASN B 109 86.94 -152.32
REMARK 500 PRO B 110 0.32 -62.93
REMARK 500 ASP B 155 21.50 -76.41
REMARK 500 ASN B 194 68.34 34.79
REMARK 500 HIS B 199 82.75 -168.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP B 210
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZRC RELATED DB: PDB
REMARK 900 4 CRYSTAL STRUCTURES OF CAP-DNA WITH ALL BASE-PAIR SUBSTITUTIONS AT
REMARK 900 POSITION 6, CAP-ICAP38 DNA
REMARK 900 RELATED ID: 1ZRE RELATED DB: PDB
REMARK 900 4 CRYSTAL STRUCTURES OF CAP-DNA WITH ALL BASE-PAIR SUBSTITUTIONS AT
REMARK 900 POSITION 6, CAP-[6G;17C]ICAP38 DNA
REMARK 900 RELATED ID: 1ZRF RELATED DB: PDB
REMARK 900 4 CRYSTAL STRUCTURES OF CAP-DNA WITH ALL BASE-PAIR SUBSTITUTIONS AT
REMARK 900 POSITION 6, CAP-[6C;17G]ICAP38 DNA
DBREF 1ZRD A 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
DBREF 1ZRD B 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
DBREF 1ZRD W -8 9 PDB 1ZRD 1ZRD -8 9
DBREF 1ZRD X 13 -8 PDB 1ZRD 1ZRD 13 -8
DBREF 1ZRD Y -8 9 PDB 1ZRD 1ZRD -8 9
DBREF 1ZRD Z 13 -8 PDB 1ZRD 1ZRD 13 -8
SEQRES 1 W 17 DA DT DT DT DC DG DA DA DA DA DA DT DG
SEQRES 2 W 17 DA DG DA DT
SEQRES 1 X 21 DC DT DA DG DA DT DC DT DC DA DT DT DT
SEQRES 2 X 21 DT DT DC DG DA DA DA DT
SEQRES 1 Y 17 DA DT DT DT DC DG DA DA DA DA DA DT DG
SEQRES 2 Y 17 DA DG DA DT
SEQRES 1 Z 21 DC DT DA DG DA DT DC DT DC DA DT DT DT
SEQRES 2 Z 21 DT DT DC DG DA DA DA DT
SEQRES 1 A 209 VAL LEU GLY LYS PRO GLN THR ASP PRO THR LEU GLU TRP
SEQRES 2 A 209 PHE LEU SER HIS CYS HIS ILE HIS LYS TYR PRO SER LYS
SEQRES 3 A 209 SER THR LEU ILE HIS GLN GLY GLU LYS ALA GLU THR LEU
SEQRES 4 A 209 TYR TYR ILE VAL LYS GLY SER VAL ALA VAL LEU ILE LYS
SEQRES 5 A 209 ASP GLU GLU GLY LYS GLU MET ILE LEU SER TYR LEU ASN
SEQRES 6 A 209 GLN GLY ASP PHE ILE GLY GLU LEU GLY LEU PHE GLU GLU
SEQRES 7 A 209 GLY GLN GLU ARG SER ALA TRP VAL ARG ALA LYS THR ALA
SEQRES 8 A 209 CYS GLU VAL ALA GLU ILE SER TYR LYS LYS PHE ARG GLN
SEQRES 9 A 209 LEU ILE GLN VAL ASN PRO ASP ILE LEU MET ARG LEU SER
SEQRES 10 A 209 ALA GLN MET ALA ARG ARG LEU GLN VAL THR SER GLU LYS
SEQRES 11 A 209 VAL GLY ASN LEU ALA PHE LEU ASP VAL THR GLY ARG ILE
SEQRES 12 A 209 ALA GLN THR LEU LEU ASN LEU ALA LYS GLN PRO ASP ALA
SEQRES 13 A 209 MET THR HIS PRO ASP GLY MET GLN ILE LYS ILE THR ARG
SEQRES 14 A 209 GLN GLU ILE GLY GLN ILE VAL GLY CYS SER ARG GLU THR
SEQRES 15 A 209 VAL GLY ARG ILE LEU LYS MET LEU GLU ASP GLN ASN LEU
SEQRES 16 A 209 ILE SER ALA HIS GLY LYS THR ILE VAL VAL TYR GLY THR
SEQRES 17 A 209 ARG
SEQRES 1 B 209 VAL LEU GLY LYS PRO GLN THR ASP PRO THR LEU GLU TRP
SEQRES 2 B 209 PHE LEU SER HIS CYS HIS ILE HIS LYS TYR PRO SER LYS
SEQRES 3 B 209 SER THR LEU ILE HIS GLN GLY GLU LYS ALA GLU THR LEU
SEQRES 4 B 209 TYR TYR ILE VAL LYS GLY SER VAL ALA VAL LEU ILE LYS
SEQRES 5 B 209 ASP GLU GLU GLY LYS GLU MET ILE LEU SER TYR LEU ASN
SEQRES 6 B 209 GLN GLY ASP PHE ILE GLY GLU LEU GLY LEU PHE GLU GLU
SEQRES 7 B 209 GLY GLN GLU ARG SER ALA TRP VAL ARG ALA LYS THR ALA
SEQRES 8 B 209 CYS GLU VAL ALA GLU ILE SER TYR LYS LYS PHE ARG GLN
SEQRES 9 B 209 LEU ILE GLN VAL ASN PRO ASP ILE LEU MET ARG LEU SER
SEQRES 10 B 209 ALA GLN MET ALA ARG ARG LEU GLN VAL THR SER GLU LYS
SEQRES 11 B 209 VAL GLY ASN LEU ALA PHE LEU ASP VAL THR GLY ARG ILE
SEQRES 12 B 209 ALA GLN THR LEU LEU ASN LEU ALA LYS GLN PRO ASP ALA
SEQRES 13 B 209 MET THR HIS PRO ASP GLY MET GLN ILE LYS ILE THR ARG
SEQRES 14 B 209 GLN GLU ILE GLY GLN ILE VAL GLY CYS SER ARG GLU THR
SEQRES 15 B 209 VAL GLY ARG ILE LEU LYS MET LEU GLU ASP GLN ASN LEU
SEQRES 16 B 209 ILE SER ALA HIS GLY LYS THR ILE VAL VAL TYR GLY THR
SEQRES 17 B 209 ARG
HET CMP A 210 22
HET CMP B 210 22
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 7 CMP 2(C10 H12 N5 O6 P)
FORMUL 9 HOH *31(H2 O)
HELIX 1 1 ASP A 8 SER A 16 1 9
HELIX 2 2 GLU A 72 GLU A 77 5 6
HELIX 3 3 TYR A 99 ILE A 106 1 8
HELIX 4 4 GLN A 107 ASN A 109 5 3
HELIX 5 5 PRO A 110 LEU A 137 1 28
HELIX 6 6 ASP A 138 ALA A 151 1 14
HELIX 7 7 THR A 168 GLY A 177 1 10
HELIX 8 8 SER A 179 GLN A 193 1 15
HELIX 9 9 ASP B 8 HIS B 17 1 10
HELIX 10 10 GLU B 72 PHE B 76 5 5
HELIX 11 11 TYR B 99 ASN B 109 1 11
HELIX 12 12 PRO B 110 LEU B 137 1 28
HELIX 13 13 ASP B 138 ALA B 151 1 14
HELIX 14 14 THR B 168 GLY B 177 1 10
HELIX 15 15 SER B 179 ASP B 192 1 14
SHEET 1 A 4 HIS A 19 TYR A 23 0
SHEET 2 A 4 CYS A 92 SER A 98 -1 O VAL A 94 N HIS A 21
SHEET 3 A 4 THR A 38 LYS A 44 -1 N LEU A 39 O ILE A 97
SHEET 4 A 4 PHE A 69 ILE A 70 -1 O ILE A 70 N TYR A 40
SHEET 1 B 4 THR A 28 ILE A 30 0
SHEET 2 B 4 TRP A 85 ALA A 88 -1 O VAL A 86 N LEU A 29
SHEET 3 B 4 SER A 46 LYS A 52 -1 N LEU A 50 O TRP A 85
SHEET 4 B 4 GLU A 58 ASN A 65 -1 O SER A 62 N VAL A 49
SHEET 1 C 4 MET A 157 HIS A 159 0
SHEET 2 C 4 GLY A 162 LYS A 166 -1 O GLN A 164 N MET A 157
SHEET 3 C 4 THR A 202 TYR A 206 -1 O ILE A 203 N ILE A 165
SHEET 4 C 4 ILE A 196 HIS A 199 -1 N SER A 197 O VAL A 204
SHEET 1 D 4 HIS B 21 TYR B 23 0
SHEET 2 D 4 CYS B 92 SER B 98 -1 O CYS B 92 N TYR B 23
SHEET 3 D 4 THR B 38 LYS B 44 -1 N LYS B 44 O GLU B 93
SHEET 4 D 4 PHE B 69 ILE B 70 -1 O ILE B 70 N TYR B 40
SHEET 1 E 4 THR B 28 ILE B 30 0
SHEET 2 E 4 TRP B 85 ALA B 88 -1 O VAL B 86 N LEU B 29
SHEET 3 E 4 VAL B 47 LYS B 52 -1 N LEU B 50 O TRP B 85
SHEET 4 E 4 GLU B 58 LEU B 64 -1 O MET B 59 N ILE B 51
SHEET 1 F 4 MET B 157 HIS B 159 0
SHEET 2 F 4 GLY B 162 LYS B 166 -1 O GLY B 162 N HIS B 159
SHEET 3 F 4 THR B 202 TYR B 206 -1 O ILE B 203 N ILE B 165
SHEET 4 F 4 ILE B 196 ALA B 198 -1 N SER B 197 O VAL B 204
SITE 1 AC1 10 VAL A 49 ILE A 70 GLY A 71 GLU A 72
SITE 2 AC1 10 LEU A 73 ARG A 82 SER A 83 ALA A 84
SITE 3 AC1 10 THR A 127 SER B 128
SITE 1 AC2 12 SER A 128 VAL B 49 LEU B 61 ILE B 70
SITE 2 AC2 12 GLY B 71 GLU B 72 LEU B 73 ARG B 82
SITE 3 AC2 12 SER B 83 ALA B 84 ARG B 123 THR B 127
CRYST1 61.289 75.345 178.078 90.00 90.00 90.00 P 21 21 21 8
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 0.016316 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013272 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005616 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
