HEADER HYDROLASE/HYDROLASE INHIBITOR 22-OCT-10 3PD0
TITLE CASPASE-3 E246A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 29-277;
COMPND 5 SYNONYM: CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, CPP-32, PROTEIN
COMPND 6 YAMA, SREBP CLEAVAGE ACTIVITY 1, SCA-1, CASPASE-3 SUBUNIT P17,
COMPND 7 CASPASE-3 SUBUNIT P12;
COMPND 8 EC: 3.4.22.56;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: INHIBITOR AC-DEVD-CMK;
COMPND 13 CHAIN: B;
COMPND 14 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: CASP3, CPP32;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) LYS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES
KEYWDS SALT BRIDGE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WALTERS,P.SWARTZ,C.MATTOS,A.C.CLARK
REVDAT 2 23-MAR-11 3PD0 1 JRNL KEYWDS REMARK SITE
REVDAT 1 16-FEB-11 3PD0 0
JRNL AUTH J.WALTERS,P.SWARTZ,C.MATTOS,A.C.CLARK
JRNL TITL THERMODYNAMIC, ENZYMATIC AND STRUCTURAL EFFECTS OF REMOVING
JRNL TITL 2 A SALT BRIDGE AT THE BASE OF LOOP 4 IN (PRO)CASPASE-3.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 508 31 2011
JRNL REFN ISSN 0003-9861
JRNL PMID 21266160
JRNL DOI 10.1016/J.ABB.2011.01.011
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.51
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) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 17891
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1755
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 : 1954
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.99500
REMARK 3 B22 (A**2) : -1.89900
REMARK 3 B33 (A**2) : 12.89500
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) : 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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : 1.234 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.845 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.088 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.000 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 37.92
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 3PD0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB062227.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18710
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
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) : 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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: INHIBITOR, AC-DEVD-CMK, RECONSTITUTED
REMARK 280 IN DMSO, WAS ADDED AT A 5:1 INHIBITOR:PROTEIN RATIO (W/W). FINAL
REMARK 280 BUFFER CONSISTED OF 10 MM TRIS-HCL, 10 MM DTT, 3 MM NAN3, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, PH 8.5, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 33.80650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.88900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.11400
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.80650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.88900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.11400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.80650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.88900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.11400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.80650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.88900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.11400
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 67.61300
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 67.61300
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 96.22800
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 96.22800
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 450 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE CL ATOM IS TOO FAR AWAY TO BE A PART OF THE RESIDUE 0QE. IT IS
REMARK 400 PRESENTED HERE AS A FREE ION
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 THR A 174
REMARK 465 ASP A 175
REMARK 465 SER A 176
REMARK 465 GLY A 177
REMARK 465 VAL A 178
REMARK 465 ASP A 179
REMARK 465 ASP A 180
REMARK 465 ASP A 181
REMARK 465 MET A 182
REMARK 465 ALA A 183
REMARK 465 CYS A 184
REMARK 465 HIS A 185
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 ASP B 5 CL CL B 7 2.13
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 SER A 120 -176.86 -171.86
REMARK 500 LYS A 229 -44.96 -130.03
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 CL B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF INHIBITOR AC-DEVD-CMK
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PCX RELATED DB: PDB
REMARK 900 CASPASE-3 E246A K242A DOUBLE MUTANT
REMARK 900 RELATED ID: 3PD1 RELATED DB: PDB
REMARK 900 CASPASE-3 K242A
DBREF 3PD0 A 29 277 UNP P42574 CASP3_HUMAN 29 277
DBREF 3PD0 B 1 6 PDB 3PD0 3PD0 1 6
SEQADV 3PD0 SER A 170 UNP P42574 CYS 170 CONFLICT
SEQADV 3PD0 ALA A 246 UNP P42574 GLU 246 ENGINEERED MUTATION
SEQADV 3PD0 HIS A 278 UNP P42574 EXPRESSION TAG
SEQRES 1 A 250 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 A 250 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 A 250 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 A 250 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 A 250 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 A 250 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 A 250 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 A 250 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 A 250 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 A 250 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 A 250 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP SER GLY
SEQRES 12 A 250 ILE GLU THR ASP SER GLY VAL ASP ASP ASP MET ALA CYS
SEQRES 13 A 250 HIS LYS ILE PRO VAL GLU ALA ASP PHE LEU TYR ALA TYR
SEQRES 14 A 250 SER THR ALA PRO GLY TYR TYR SER TRP ARG ASN SER LYS
SEQRES 15 A 250 ASP GLY SER TRP PHE ILE GLN SER LEU CYS ALA MET LEU
SEQRES 16 A 250 LYS GLN TYR ALA ASP LYS LEU GLU PHE MET HIS ILE LEU
SEQRES 17 A 250 THR ARG VAL ASN ARG LYS VAL ALA THR ALA PHE GLU SER
SEQRES 18 A 250 PHE SER PHE ASP ALA THR PHE HIS ALA LYS LYS GLN ILE
SEQRES 19 A 250 PRO CYS ILE VAL SER MET LEU THR LYS GLU LEU TYR PHE
SEQRES 20 A 250 TYR HIS HIS
SEQRES 1 B 6 ACE ASP GLU VAL ASP 0QE
HET ACE B 1 3
HET 0QE B 6 1
HET CL B 7 1
HETNAM ACE ACETYL GROUP
HETNAM 0QE CHLOROMETHANE
HETNAM CL CHLORIDE ION
HETSYN 0QE CHLORO METHYL GROUP
FORMUL 2 ACE C2 H4 O
FORMUL 2 0QE C H3 CL
FORMUL 3 CL CL 1-
FORMUL 4 HOH *215(H2 O)
HELIX 1 1 HIS A 56 GLY A 60 5 5
HELIX 2 2 GLY A 66 LEU A 81 1 16
HELIX 3 3 THR A 92 LYS A 105 1 14
HELIX 4 4 LEU A 136 PHE A 142 1 7
HELIX 5 5 CYS A 148 THR A 152 5 5
HELIX 6 6 TRP A 214 ALA A 227 1 14
HELIX 7 7 GLU A 231 PHE A 247 1 17
SHEET 1 A 6 GLU A 84 ASN A 89 0
SHEET 2 A 6 GLU A 43 ASN A 51 1 N ILE A 49 O LYS A 88
SHEET 3 A 6 ARG A 111 LEU A 119 1 O VAL A 117 N ILE A 48
SHEET 4 A 6 LYS A 156 GLN A 161 1 O LEU A 157 N PHE A 114
SHEET 5 A 6 PHE A 193 TYR A 197 1 O LEU A 194 N PHE A 158
SHEET 6 A 6 CYS A 264 SER A 267 -1 O VAL A 266 N TYR A 195
SHEET 1 B 3 GLY A 122 GLU A 123 0
SHEET 2 B 3 ILE A 126 GLY A 129 -1 O ILE A 126 N GLU A 123
SHEET 3 B 3 GLY A 132 ASP A 135 -1 O GLY A 132 N GLY A 129
SHEET 1 C 3 GLY A 212 SER A 213 0
SHEET 2 C 3 TRP A 206 ASN A 208 -1 N ASN A 208 O GLY A 212
SHEET 3 C 3 GLU B 3 VAL B 4 -1 O GLU B 3 N ARG A 207
LINK C ACE B 1 N ASP B 2 1555 1555 1.33
LINK C ASP B 5 C1 0QE B 6 1555 1555 1.53
SITE 1 AC1 4 CYS A 163 HOH A 487 ASP B 5 0QE B 6
SITE 1 AC2 23 SER A 58 ARG A 64 HIS A 121 GLY A 122
SITE 2 AC2 23 GLN A 161 CYS A 163 SER A 205 TRP A 206
SITE 3 AC2 23 ARG A 207 ASN A 208 SER A 209 TRP A 214
SITE 4 AC2 23 SER A 249 PHE A 250 HOH A 367 HOH A 369
SITE 5 AC2 23 HOH A 384 HOH A 393 HOH A 408 CL B 7
SITE 6 AC2 23 HOH B 300 HOH B 301 HOH B 511
CRYST1 67.613 83.778 96.228 90.00 90.00 90.00 I 2 2 2 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 0.014790 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011936 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010392 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
