HEADER HYDROLASE 03-MAY-05 1ZKL
TITLE MULTIPLE DETERMINANTS FOR INHIBITOR SELECTIVITY OF CYCLIC NUCLEOTIDE
TITLE 2 PHOSPHODIESTERASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH-AFFINITY CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE
COMPND 3 7A;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN (130-482);
COMPND 6 SYNONYM: HCP1, TM22;
COMPND 7 EC: 3.1.4.17;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDE7A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS PDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WANG,Y.LIU,Y.CHEN,H.ROBINSON,H.KE
REVDAT 5 14-FEB-24 1ZKL 1 REMARK LINK
REVDAT 4 24-FEB-09 1ZKL 1 VERSN
REVDAT 3 13-SEP-05 1ZKL 1 JRNL
REVDAT 2 09-AUG-05 1ZKL 1 JRNL
REVDAT 1 05-JUL-05 1ZKL 0
JRNL AUTH H.WANG,Y.LIU,Y.CHEN,H.ROBINSON,H.KE
JRNL TITL MULTIPLE ELEMENTS JOINTLY DETERMINE INHIBITOR SELECTIVITY OF
JRNL TITL 2 CYCLIC NUCLEOTIDE PHOSPHODIESTERASES 4 AND 7
JRNL REF J.BIOL.CHEM. V. 280 30949 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15994308
JRNL DOI 10.1074/JBC.M504398200
REMARK 2
REMARK 2 RESOLUTION. 1.67 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.50
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) (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 55766
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) : 0.194
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5668
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 : 2584
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 289
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.10
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) : 1.100
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 1ZKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57579
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670
REMARK 200 RESOLUTION RANGE LOW (A) : 39.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6 - 0.8 M (NH4)2SO4, 2.5 - 5 MM
REMARK 280 MERCAPTOETHANOL, 10 MM EDTA, 0.1 M TRIS HCL, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.43000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.86000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 42.86000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.43000
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: 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 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 130
REMARK 465 ASN A 131
REMARK 465 SER A 132
REMARK 465 LEU A 133
REMARK 465 ASN A 134
REMARK 465 ILE A 135
REMARK 465 LEU A 136
REMARK 465 ASP A 137
REMARK 465 ASP A 138
REMARK 465 ARG A 456
REMARK 465 GLU A 457
REMARK 465 GLN A 458
REMARK 465 SER A 459
REMARK 465 SER A 460
REMARK 465 SER A 461
REMARK 465 GLU A 462
REMARK 465 ASP A 463
REMARK 465 THR A 464
REMARK 465 ASP A 465
REMARK 465 ALA A 466
REMARK 465 ALA A 467
REMARK 465 PHE A 468
REMARK 465 GLU A 469
REMARK 465 LEU A 470
REMARK 465 ASN A 471
REMARK 465 SER A 472
REMARK 465 GLN A 473
REMARK 465 LEU A 474
REMARK 465 LEU A 475
REMARK 465 PRO A 476
REMARK 465 GLN A 477
REMARK 465 GLU A 478
REMARK 465 ASN A 479
REMARK 465 ARG A 480
REMARK 465 LEU A 481
REMARK 465 SER A 482
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 ASN A 277 23.47 49.97
REMARK 500 LEU A 454 34.07 -74.91
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 216 NE2
REMARK 620 2 HIS A 252 NE2 95.4
REMARK 620 3 ASP A 253 OD2 90.2 86.9
REMARK 620 4 ASP A 362 OD1 95.6 88.0 172.6
REMARK 620 5 HOH A 504 O 87.3 176.3 95.5 89.3
REMARK 620 6 HOH A 509 O 163.7 100.7 93.0 82.7 76.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 253 OD1
REMARK 620 2 HOH A 505 O 99.9
REMARK 620 3 HOH A 506 O 91.6 84.6
REMARK 620 4 HOH A 507 O 170.3 88.2 83.8
REMARK 620 5 HOH A 508 O 85.8 174.3 94.5 86.1
REMARK 620 6 HOH A 509 O 96.9 85.8 168.2 88.9 94.3
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 ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IBM A 503
DBREF 1ZKL A 130 482 UNP Q13946 PDE7A_HUMAN 130 482
SEQRES 1 A 353 SER ASN SER LEU ASN ILE LEU ASP ASP ASP TYR ASN GLY
SEQRES 2 A 353 GLN ALA LYS CYS MET LEU GLU LYS VAL GLY ASN TRP ASN
SEQRES 3 A 353 PHE ASP ILE PHE LEU PHE ASP ARG LEU THR ASN GLY ASN
SEQRES 4 A 353 SER LEU VAL SER LEU THR PHE HIS LEU PHE SER LEU HIS
SEQRES 5 A 353 GLY LEU ILE GLU TYR PHE HIS LEU ASP MET MET LYS LEU
SEQRES 6 A 353 ARG ARG PHE LEU VAL MET ILE GLN GLU ASP TYR HIS SER
SEQRES 7 A 353 GLN ASN PRO TYR HIS ASN ALA VAL HIS ALA ALA ASP VAL
SEQRES 8 A 353 THR GLN ALA MET HIS CYS TYR LEU LYS GLU PRO LYS LEU
SEQRES 9 A 353 ALA ASN SER VAL THR PRO TRP ASP ILE LEU LEU SER LEU
SEQRES 10 A 353 ILE ALA ALA ALA THR HIS ASP LEU ASP HIS PRO GLY VAL
SEQRES 11 A 353 ASN GLN PRO PHE LEU ILE LYS THR ASN HIS TYR LEU ALA
SEQRES 12 A 353 THR LEU TYR LYS ASN THR SER VAL LEU GLU ASN HIS HIS
SEQRES 13 A 353 TRP ARG SER ALA VAL GLY LEU LEU ARG GLU SER GLY LEU
SEQRES 14 A 353 PHE SER HIS LEU PRO LEU GLU SER ARG GLN GLN MET GLU
SEQRES 15 A 353 THR GLN ILE GLY ALA LEU ILE LEU ALA THR ASP ILE SER
SEQRES 16 A 353 ARG GLN ASN GLU TYR LEU SER LEU PHE ARG SER HIS LEU
SEQRES 17 A 353 ASP ARG GLY ASP LEU CYS LEU GLU ASP THR ARG HIS ARG
SEQRES 18 A 353 HIS LEU VAL LEU GLN MET ALA LEU LYS CYS ALA ASP ILE
SEQRES 19 A 353 CYS ASN PRO CYS ARG THR TRP GLU LEU SER LYS GLN TRP
SEQRES 20 A 353 SER GLU LYS VAL THR GLU GLU PHE PHE HIS GLN GLY ASP
SEQRES 21 A 353 ILE GLU LYS LYS TYR HIS LEU GLY VAL SER PRO LEU CYS
SEQRES 22 A 353 ASP ARG HIS THR GLU SER ILE ALA ASN ILE GLN ILE GLY
SEQRES 23 A 353 PHE MET THR TYR LEU VAL GLU PRO LEU PHE THR GLU TRP
SEQRES 24 A 353 ALA ARG PHE SER ASN THR ARG LEU SER GLN THR MET LEU
SEQRES 25 A 353 GLY HIS VAL GLY LEU ASN LYS ALA SER TRP LYS GLY LEU
SEQRES 26 A 353 GLN ARG GLU GLN SER SER SER GLU ASP THR ASP ALA ALA
SEQRES 27 A 353 PHE GLU LEU ASN SER GLN LEU LEU PRO GLN GLU ASN ARG
SEQRES 28 A 353 LEU SER
HET ZN A 501 1
HET MG A 502 1
HET IBM A 503 16
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM IBM 3-ISOBUTYL-1-METHYLXANTHINE
FORMUL 2 ZN ZN 2+
FORMUL 3 MG MG 2+
FORMUL 4 IBM C10 H14 N4 O2
FORMUL 5 HOH *289(H2 O)
HELIX 1 1 ASP A 139 GLU A 149 1 11
HELIX 2 2 ASP A 157 THR A 165 1 9
HELIX 3 3 ASN A 168 HIS A 181 1 14
HELIX 4 4 GLY A 182 PHE A 187 1 6
HELIX 5 5 ASP A 190 ASP A 204 1 15
HELIX 6 6 ASN A 213 LYS A 229 1 17
HELIX 7 7 GLU A 230 ASN A 235 1 6
HELIX 8 8 THR A 238 HIS A 252 1 15
HELIX 9 9 ASN A 260 THR A 267 1 8
HELIX 10 10 HIS A 269 TYR A 275 1 7
HELIX 11 11 SER A 279 GLY A 297 1 19
HELIX 12 12 PRO A 303 ALA A 320 1 18
HELIX 13 13 THR A 321 SER A 324 5 4
HELIX 14 14 ARG A 325 GLY A 340 1 16
HELIX 15 15 ASP A 346 ILE A 363 1 18
HELIX 16 16 CYS A 364 ARG A 368 5 5
HELIX 17 17 THR A 369 TYR A 394 1 26
HELIX 18 18 SER A 408 LEU A 420 1 13
HELIX 19 19 LEU A 420 SER A 432 1 13
HELIX 20 20 THR A 434 LEU A 454 1 21
LINK NE2 HIS A 216 ZN ZN A 501 1555 1555 2.11
LINK NE2 HIS A 252 ZN ZN A 501 1555 1555 2.11
LINK OD2 ASP A 253 ZN ZN A 501 1555 1555 2.05
LINK OD1 ASP A 253 MG MG A 502 1555 1555 2.09
LINK OD1 ASP A 362 ZN ZN A 501 1555 1555 2.06
LINK ZN ZN A 501 O HOH A 504 1555 1555 2.33
LINK ZN ZN A 501 O HOH A 509 1555 1555 2.22
LINK MG MG A 502 O HOH A 505 1555 1555 2.24
LINK MG MG A 502 O HOH A 506 1555 1555 2.21
LINK MG MG A 502 O HOH A 507 1555 1555 2.23
LINK MG MG A 502 O HOH A 508 1555 1555 2.20
LINK MG MG A 502 O HOH A 509 1555 1555 2.22
SITE 1 AC1 6 HIS A 216 HIS A 252 ASP A 253 ASP A 362
SITE 2 AC1 6 HOH A 504 HOH A 509
SITE 1 AC2 6 ASP A 253 HOH A 505 HOH A 506 HOH A 507
SITE 2 AC2 6 HOH A 508 HOH A 509
SITE 1 AC3 9 TYR A 211 VAL A 380 PHE A 384 ILE A 412
SITE 2 AC3 9 GLN A 413 PHE A 416 HOH A 542 HOH A 552
SITE 3 AC3 9 HOH A 573
CRYST1 115.751 115.751 64.290 90.00 90.00 120.00 P 31 2 1 6
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 0.008639 0.004988 0.000000 0.00000
SCALE2 0.000000 0.009976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
