HEADER HYDROLASE 12-FEB-07 2OUR
TITLE CRYSTAL STRUCTURE OF PDE10A2 MUTANT D674A IN COMPLEX WITH CAMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE
COMPND 3 10A;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN;
COMPND 6 EC: 3.1.4.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: PDE10A2;
SOURCE 6 GENE: PDE10A;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PDE10, CAMP, SUBSTRATE SPECIFICITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.C.WANG,Y.D.LIU,J.HOU,M.Y.ZHENG,H.ROBINSON
REVDAT 6 03-APR-24 2OUR 1 REMARK
REVDAT 5 21-FEB-24 2OUR 1 REMARK
REVDAT 4 20-OCT-21 2OUR 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2OUR 1 VERSN
REVDAT 2 24-APR-07 2OUR 1 JRNL
REVDAT 1 20-MAR-07 2OUR 0
JRNL AUTH H.WANG,Y.LIU,J.HOU,M.ZHENG,H.ROBINSON,H.KE
JRNL TITL FROM THE COVER: STRUCTURAL INSIGHT INTO SUBSTRATE
JRNL TITL 2 SPECIFICITY OF PHOSPHODIESTERASE 10.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 5782 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17389385
JRNL DOI 10.1073/PNAS.0700279104
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 96206
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 9661
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 : 5174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 433
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.60
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101420
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
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: PDE10A2 NATIVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 0.1 M MGCL2, 100
REMARK 280 MM BME, AND 13% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 24.64800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.99950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.14250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.99950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.64800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.14250
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
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 446
REMARK 465 THR A 771
REMARK 465 ALA A 772
REMARK 465 THR A 773
REMARK 465 TRP A 774
REMARK 465 ILE A 775
REMARK 465 SER A 776
REMARK 465 SER B 571
REMARK 465 ASN B 572
REMARK 465 SER B 573
REMARK 465 TYR B 574
REMARK 465 LEU B 575
REMARK 465 GLN B 576
REMARK 465 LYS B 577
REMARK 465 PHE B 578
REMARK 465 ASP B 579
REMARK 465 HIS B 580
REMARK 465 PRO B 581
REMARK 465 LEU B 582
REMARK 465 ALA B 583
REMARK 465 ALA B 584
REMARK 465 LEU B 585
REMARK 465 TYR B 586
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 TYR A 524 -52.50 -124.65
REMARK 500 ASN A 526 -169.38 -120.96
REMARK 500 ASN A 544 31.38 -142.65
REMARK 500 CYS A 676 -9.22 -56.57
REMARK 500 VAL A 733 -63.43 -128.45
REMARK 500 GLU A 769 42.98 -107.00
REMARK 500 HIS B 525 35.82 -143.78
REMARK 500 ASN B 544 37.99 -142.26
REMARK 500 CYS B 676 -6.46 -58.80
REMARK 500 VAL B 733 -60.47 -120.29
REMARK 500 GLU B 770 110.65 69.49
REMARK 500 THR B 771 -106.92 -61.69
REMARK 500 ALA B 772 43.86 -79.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 777 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 1 O
REMARK 620 2 HOH A 2 O 90.4
REMARK 620 3 HOH A 3 O 171.5 96.5
REMARK 620 4 HOH A 4 O 88.7 87.7 86.5
REMARK 620 5 HOH A 5 O 80.6 170.9 92.4 90.9
REMARK 620 6 ASP A 564 OD1 100.1 91.8 84.8 171.2 91.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 777 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 11 O
REMARK 620 2 HOH B 12 O 83.1
REMARK 620 3 HOH B 13 O 87.8 91.1
REMARK 620 4 HOH B 14 O 88.3 170.2 84.0
REMARK 620 5 HOH B 15 O 81.2 92.0 168.2 91.2
REMARK 620 6 ASP B 564 OD1 166.3 92.9 105.4 96.5 85.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 778
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OUN RELATED DB: PDB
REMARK 900 RELATED ID: 2OUP RELATED DB: PDB
REMARK 900 RELATED ID: 2OUQ RELATED DB: PDB
REMARK 900 RELATED ID: 2OUS RELATED DB: PDB
REMARK 900 RELATED ID: 2OUU RELATED DB: PDB
REMARK 900 RELATED ID: 2OUV RELATED DB: PDB
REMARK 900 RELATED ID: 2OUY RELATED DB: PDB
DBREF 2OUR A 449 776 UNP Q9Y233 PDE10_HUMAN 439 766
DBREF 2OUR B 449 776 UNP Q9Y233 PDE10_HUMAN 439 766
SEQADV 2OUR SER A 446 UNP Q9Y233 CLONING ARTIFACT
SEQADV 2OUR HIS A 447 UNP Q9Y233 CLONING ARTIFACT
SEQADV 2OUR MET A 448 UNP Q9Y233 CLONING ARTIFACT
SEQADV 2OUR ALA A 674 UNP Q9Y233 ASP 664 ENGINEERED MUTATION
SEQADV 2OUR SER B 446 UNP Q9Y233 CLONING ARTIFACT
SEQADV 2OUR HIS B 447 UNP Q9Y233 CLONING ARTIFACT
SEQADV 2OUR MET B 448 UNP Q9Y233 CLONING ARTIFACT
SEQADV 2OUR ALA B 674 UNP Q9Y233 ASP 664 ENGINEERED MUTATION
SEQRES 1 A 331 SER HIS MET SER ILE CYS THR SER GLU GLU TRP GLN GLY
SEQRES 2 A 331 LEU MET GLN PHE THR LEU PRO VAL ARG LEU CYS LYS GLU
SEQRES 3 A 331 ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU ASN
SEQRES 4 A 331 MET TRP PRO GLY ILE PHE VAL TYR MET VAL HIS ARG SER
SEQRES 5 A 331 CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS ARG
SEQRES 6 A 331 PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL PRO
SEQRES 7 A 331 TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS CYS
SEQRES 8 A 331 MET TYR ALA ILE LEU GLN ASN ASN HIS THR LEU PHE THR
SEQRES 9 A 331 ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU CYS
SEQRES 10 A 331 HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR LEU
SEQRES 11 A 331 GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER THR
SEQRES 12 A 331 SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL SER
SEQRES 13 A 331 ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR LEU
SEQRES 14 A 331 SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE ARG
SEQRES 15 A 331 LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE GLY
SEQRES 16 A 331 ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY SER
SEQRES 17 A 331 LEU ASN LEU ASN ASN GLN SER HIS ARG ASP ARG VAL ILE
SEQRES 18 A 331 GLY LEU MET MET THR ALA CYS ALA LEU CYS SER VAL THR
SEQRES 19 A 331 LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP ILE
SEQRES 20 A 331 TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS LYS
SEQRES 21 A 331 LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP LYS
SEQRES 22 A 331 LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR ASN
SEQRES 23 A 331 ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN ILE
SEQRES 24 A 331 LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG ASP
SEQRES 25 A 331 ASN LEU SER GLN TRP GLU LYS VAL ILE ARG GLY GLU GLU
SEQRES 26 A 331 THR ALA THR TRP ILE SER
SEQRES 1 B 331 SER HIS MET SER ILE CYS THR SER GLU GLU TRP GLN GLY
SEQRES 2 B 331 LEU MET GLN PHE THR LEU PRO VAL ARG LEU CYS LYS GLU
SEQRES 3 B 331 ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU ASN
SEQRES 4 B 331 MET TRP PRO GLY ILE PHE VAL TYR MET VAL HIS ARG SER
SEQRES 5 B 331 CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS ARG
SEQRES 6 B 331 PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL PRO
SEQRES 7 B 331 TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS CYS
SEQRES 8 B 331 MET TYR ALA ILE LEU GLN ASN ASN HIS THR LEU PHE THR
SEQRES 9 B 331 ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU CYS
SEQRES 10 B 331 HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR LEU
SEQRES 11 B 331 GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER THR
SEQRES 12 B 331 SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL SER
SEQRES 13 B 331 ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR LEU
SEQRES 14 B 331 SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE ARG
SEQRES 15 B 331 LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE GLY
SEQRES 16 B 331 ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY SER
SEQRES 17 B 331 LEU ASN LEU ASN ASN GLN SER HIS ARG ASP ARG VAL ILE
SEQRES 18 B 331 GLY LEU MET MET THR ALA CYS ALA LEU CYS SER VAL THR
SEQRES 19 B 331 LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP ILE
SEQRES 20 B 331 TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS LYS
SEQRES 21 B 331 LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP LYS
SEQRES 22 B 331 LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR ASN
SEQRES 23 B 331 ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN ILE
SEQRES 24 B 331 LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG ASP
SEQRES 25 B 331 ASN LEU SER GLN TRP GLU LYS VAL ILE ARG GLY GLU GLU
SEQRES 26 B 331 THR ALA THR TRP ILE SER
HET MG A 777 1
HET CMP A 778 22
HET MG B 777 1
HETNAM MG MAGNESIUM ION
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 3 MG 2(MG 2+)
FORMUL 4 CMP C10 H12 N5 O6 P
FORMUL 6 HOH *433(H2 O)
HELIX 1 1 THR A 452 MET A 460 1 9
HELIX 2 2 PRO A 465 ILE A 472 1 8
HELIX 3 3 ILE A 479 ASN A 484 5 6
HELIX 4 4 MET A 485 GLY A 499 1 15
HELIX 5 5 GLU A 504 ASN A 518 1 15
HELIX 6 6 ASN A 526 ASN A 543 1 18
HELIX 7 7 ASN A 544 PHE A 548 5 5
HELIX 8 8 THR A 549 HIS A 563 1 15
HELIX 9 9 SER A 571 PHE A 578 1 8
HELIX 10 10 HIS A 580 TYR A 586 1 7
HELIX 11 11 SER A 589 GLN A 604 1 16
HELIX 12 12 SER A 615 THR A 633 1 19
HELIX 13 13 ASP A 634 THR A 651 1 18
HELIX 14 14 ASN A 658 LEU A 675 1 18
HELIX 15 15 CYS A 676 LYS A 680 5 5
HELIX 16 16 LEU A 681 LEU A 706 1 26
HELIX 17 17 ILE A 711 ASP A 720 5 10
HELIX 18 18 GLU A 721 VAL A 733 1 13
HELIX 19 19 VAL A 733 LEU A 745 1 13
HELIX 20 20 THR A 748 GLY A 768 1 21
HELIX 21 21 THR B 452 GLN B 461 1 10
HELIX 22 22 PRO B 465 ARG B 467 5 3
HELIX 23 23 LEU B 468 GLU B 473 1 6
HELIX 24 24 ILE B 479 ASN B 484 5 6
HELIX 25 25 MET B 485 GLY B 499 1 15
HELIX 26 26 GLU B 504 LYS B 517 1 14
HELIX 27 27 ASN B 526 ASN B 543 1 18
HELIX 28 28 ASN B 544 PHE B 548 5 5
HELIX 29 29 THR B 549 HIS B 563 1 15
HELIX 30 30 SER B 589 GLN B 604 1 16
HELIX 31 31 SER B 615 THR B 633 1 19
HELIX 32 32 ASP B 634 THR B 651 1 18
HELIX 33 33 ASN B 658 LEU B 675 1 18
HELIX 34 34 CYS B 676 LYS B 680 5 5
HELIX 35 35 LEU B 681 LYS B 686 1 6
HELIX 36 36 TYR B 693 LEU B 706 1 14
HELIX 37 37 ILE B 711 ASP B 715 5 5
HELIX 38 38 GLU B 721 VAL B 733 1 13
HELIX 39 39 VAL B 733 LEU B 745 1 13
HELIX 40 40 THR B 748 ARG B 767 1 20
LINK O HOH A 1 MG MG A 777 1555 1555 2.24
LINK O HOH A 2 MG MG A 777 1555 1555 2.23
LINK O HOH A 3 MG MG A 777 1555 1555 2.19
LINK O HOH A 4 MG MG A 777 1555 1555 2.23
LINK O HOH A 5 MG MG A 777 1555 1555 2.17
LINK OD1 ASP A 564 MG MG A 777 1555 1555 2.08
LINK O HOH B 11 MG MG B 777 1555 1555 2.30
LINK O HOH B 12 MG MG B 777 1555 1555 2.29
LINK O HOH B 13 MG MG B 777 1555 1555 2.31
LINK O HOH B 14 MG MG B 777 1555 1555 2.39
LINK O HOH B 15 MG MG B 777 1555 1555 2.27
LINK OD1 ASP B 564 MG MG B 777 1555 1555 2.09
SITE 1 AC1 6 HOH A 1 HOH A 2 HOH A 3 HOH A 4
SITE 2 AC1 6 HOH A 5 ASP A 564
SITE 1 AC2 6 HOH B 11 HOH B 12 HOH B 13 HOH B 14
SITE 2 AC2 6 HOH B 15 ASP B 564
SITE 1 AC3 14 HOH A 1 HOH A 7 HOH A 8 HOH A 9
SITE 2 AC3 14 HOH A 10 HOH A 301 HIS A 525 LEU A 635
SITE 3 AC3 14 LEU A 675 ILE A 692 PHE A 696 GLN A 726
SITE 4 AC3 14 PHE A 729 LEU B 706
CRYST1 49.296 82.285 153.999 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 0.020286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012153 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006494 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
