HEADER DNA BINDING PROTEIN 06-MAR-01 1I6X
TITLE STRUCTURE OF A STAR MUTANT CRP-CAMP AT 2.2 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATABOLITE GENE ACTIVATOR PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CAMP RECEPTOR PROTEIN, CRP, CAP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CAMP RECEPTOR PROTEIN (CRP), ALLOSTERY, DNA BINDING CYCLIC AMP,
KEYWDS 2 TRANSCRIPTION REGULATION, CATABOLITE ACTIVATOR PROTEIN (CAP), DNA
KEYWDS 3 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.WHITE,J.C.LEE,R.O.FOX
REVDAT 4 09-AUG-23 1I6X 1 REMARK
REVDAT 3 27-OCT-21 1I6X 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1I6X 1 VERSN
REVDAT 1 17-JUN-03 1I6X 0
JRNL AUTH M.A.WHITE,D.LIU,S.-H.LIN,R.O.FOX,J.C.LEE
JRNL TITL THE EFFECT OF THE D53H POINT MUTATION ON THE MACROSCOPIC
JRNL TITL 2 MOTIONS OF E. COLI CYCLIC AMP RECEPTOR PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.T.WEBER,T.A.STEITZ
REMARK 1 TITL STRUCTURE OF A COMPLEX OF CATABOLITE GENE ACTIVATOR PROTEIN
REMARK 1 TITL 2 AND CYCLIC AMP AT 2.5 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 198 311 1987
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1693252.270
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 22833
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2243
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 815
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 85
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.55000
REMARK 3 B22 (A**2) : 0.56000
REMARK 3 B33 (A**2) : -0.01000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.22
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
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) : 21.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.570 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.640 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.310 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 55.90
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE DATA WERE MERGED FROM THREE INDEPENDENT DATA SETS
REMARK 3 COLLECTED ON THREE DIFFERENT DETECTOR TYPES, WITH
REMARK 3 INCOMPATIBLE PROCESSING SOFTWARE. THE PROCESSED DATA
REMARK 3 SETS WERE COMBINED IN SCALEPACK AND THEREFORE SOME
REMARK 3 OVERALL STATISTICS ARE NOT AVAILABLE. THE THREE SETS
REMARK 3 WERE COLLECTED ON (1) A BRUKER SMART 2K CCD
REMARK 3 (2) A MACSCIENCE DIP2030 AND (3) X4A (A RIGAKU
REMARK 3 R-AXIS IV)
REMARK 3 THE DATA REDUNDANCY FOR EACH SET IS: 8.2, 1.5, 2.7.
REMARK 3 THE HIGHEST RESOLUTION SHELLS OF EACH SET IS:
REMARK 3 2.6, 2.4, 2.2.
REMARK 3 THE RMERGE IN THE HIGHEST RESOLUTION SHELL IS:
REMARK 3 30.9, 31.7, 31.1%.
REMARK 3 THE OVERALL RMERGE FOR EACH SET IS: 10.5, 7.4, 3.7%.
REMARK 3 THE NUMBER OF UNIQUE REFLECTIONS IS: 14899, 9570, 20183.
REMARK 3 THE OVERALL PERCENT COMPLETENESS IS: 99.9, 45.2, 81.7%.
REMARK 4
REMARK 4 1I6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012980.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-98; 21-MAY-98; 01-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 95; 95; 95
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; N; Y
REMARK 200 RADIATION SOURCE : ROTATING ANODE; ROTATING ANODE;
REMARK 200 NSLS
REMARK 200 BEAMLINE : NULL; NULL; X4A
REMARK 200 X-RAY GENERATOR MODEL : MACSCIENCE; MACSCIENCE; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.5418; 0.97950
REMARK 200 MONOCHROMATOR : NULL; NULL; NULL
REMARK 200 OPTICS : MULTILAYER; MULTILAYER; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE; BRUKER SMART 2000;
REMARK 200 RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23757
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 70.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
REMARK 200 R SYM FOR SHELL (I) : 0.31100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; SINGLE
REMARK 200 WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1I5Z CRP DIMER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM KCL, 1MM EDTA, 50MM TRIS, 35%
REMARK 280 GLYCEROL, 20:1 CAMP:CRP, PH 7.8, LIQUID DIFFUSION, TEMPERATURE
REMARK 280 298K
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 23.13100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.66950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.67150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.66950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.13100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.67150
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 300 REMARK: THE DIMER IS THE BIOLOGICAL UNIT
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 207
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: 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 26 -1.67 79.96
REMARK 500 GLU A 54 138.35 -35.51
REMARK 500 GLU A 55 120.73 61.65
REMARK 500 LYS A 57 -163.91 67.45
REMARK 500 GLU A 58 137.59 -25.88
REMARK 500 PRO A 160 27.84 -68.36
REMARK 500 ASP A 161 37.25 -179.66
REMARK 500 GLN A 193 5.00 -61.47
REMARK 500 GLU B 54 32.48 36.22
REMARK 500 ASN B 109 102.80 -160.22
REMARK 500 PHE B 136 36.51 -94.72
REMARK 500 LYS B 201 22.73 -148.28
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 TRS A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I5Z RELATED DB: PDB
REMARK 900 WT STRUCTURE AT 1.9A
REMARK 900 RELATED ID: 3GAP RELATED DB: PDB
REMARK 900 RELATED ID: 1G6N RELATED DB: PDB
DBREF 1I6X A 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
DBREF 1I6X B 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
SEQADV 1I6X HIS A 53 UNP P0ACJ8 ASP 54 ENGINEERED MUTATION
SEQADV 1I6X HIS B 53 UNP P0ACJ8 ASP 54 ENGINEERED MUTATION
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 HIS 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 HIS 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 TRS A 351 8
HET CMP A 301 22
HET CMP A 302 22
HET CMP B 401 22
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETSYN TRS TRIS BUFFER
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 3 TRS C4 H12 N O3 1+
FORMUL 4 CMP 3(C10 H12 N5 O6 P)
FORMUL 7 HOH *83(H2 O)
HELIX 1 1 ASP A 8 SER A 16 1 9
HELIX 2 2 TYR A 99 ASN A 109 1 11
HELIX 3 3 PRO A 110 LEU A 137 1 28
HELIX 4 4 ASP A 138 LEU A 150 1 13
HELIX 5 5 ALA A 151 GLN A 153 5 3
HELIX 6 6 THR A 168 GLY A 177 1 10
HELIX 7 7 SER A 179 GLN A 193 1 15
HELIX 8 8 ASP B 8 HIS B 17 1 10
HELIX 9 9 TYR B 99 ASN B 109 1 11
HELIX 10 10 PRO B 110 PHE B 136 1 27
HELIX 11 11 ASP B 138 LYS B 152 1 15
HELIX 12 12 THR B 168 GLY B 177 1 10
HELIX 13 13 SER B 179 GLN B 193 1 15
SHEET 1 A 4 HIS A 19 TYR A 23 0
SHEET 2 A 4 CYS A 92 SER A 98 -1 N CYS A 92 O TYR A 23
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 ILE A 51 -1 N ALA A 48 O ARG A 87
SHEET 4 B 4 MET A 59 ASN A 65 -1 O MET A 59 N ILE A 51
SHEET 1 C 4 MET A 157 HIS A 159 0
SHEET 2 C 4 GLY A 162 LYS A 166 -1 N GLY A 162 O HIS A 159
SHEET 3 C 4 THR A 202 VAL A 205 -1 O ILE A 203 N ILE A 165
SHEET 4 C 4 ILE A 196 HIS A 199 -1 O SER A 197 N VAL A 204
SHEET 1 D 4 HIS B 19 TYR B 23 0
SHEET 2 D 4 CYS B 92 SER B 98 -1 N CYS B 92 O TYR B 23
SHEET 3 D 4 THR B 38 LYS B 44 -1 N LEU B 39 O ILE B 97
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 SER B 46 LYS B 52 -1 N ALA B 48 O ARG B 87
SHEET 4 E 4 GLU B 58 ASN B 65 -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 N GLY B 162 O HIS B 159
SHEET 3 F 4 THR B 202 TYR B 206 -1 N ILE B 203 O ILE B 165
SHEET 4 F 4 ILE B 196 HIS B 199 -1 O SER B 197 N VAL B 204
SITE 1 AC1 9 LYS A 130 ASN A 133 LEU A 134 ARG A 142
SITE 2 AC1 9 GLN A 145 THR A 146 ILE A 175 VAL A 176
SITE 3 AC1 9 HOH A 511
SITE 1 AC2 15 VAL A 49 LEU A 61 ILE A 70 GLY A 71
SITE 2 AC2 15 GLU A 72 LEU A 73 ARG A 82 SER A 83
SITE 3 AC2 15 VAL A 86 ARG A 123 THR A 127 HOH A 501
SITE 4 AC2 15 HOH A 502 SER B 128 HOH B 517
SITE 1 AC3 11 GLY A 56 GLU A 58 GLN A 170 GLY A 173
SITE 2 AC3 11 GLN A 174 GLY A 177 CYS A 178 SER A 179
SITE 3 AC3 11 ARG A 180 ALA B 135 PHE B 136
SITE 1 AC4 14 LEU A 124 SER A 128 VAL B 49 ILE B 70
SITE 2 AC4 14 GLY B 71 GLU B 72 LEU B 73 ARG B 82
SITE 3 AC4 14 SER B 83 ALA B 84 ARG B 123 THR B 127
SITE 4 AC4 14 HOH B 506 HOH B 508
CRYST1 46.262 93.343 105.339 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 0.021616 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009493 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
