HEADER TRANSFERASE 07-SEP-05 2AYP
TITLE CRYSTAL STRUCTURE OF CHK1 WITH AN INDOL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-269;
COMPND 5 EC: 2.7.1.37;
COMPND 6 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: CHEK1, CHK1
KEYWDS PROTEIN-INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.-H.LIN,P.XIA,P.KOVAR,Z.CHEN,H.ZHANG,S.H.ROSENBERG,H.L.SHAM
REVDAT 3 14-FEB-24 2AYP 1 REMARK
REVDAT 2 24-FEB-09 2AYP 1 VERSN
REVDAT 1 12-SEP-06 2AYP 0
JRNL AUTH N.-H.LIN,P.XIA,P.KOVAR,C.PARK,Z.CHEN,H.ZHANG,S.H.ROSENBERG,
JRNL AUTH 2 H.L.SHAM
JRNL TITL SYNTHESIS AND BIOLOGICAL EVALUATION OF
JRNL TITL 2 3-ETHYLIDENE-1,3-DIHYDRO-INDOL-2-ONES AS NOVEL CHECKPOINT 1
JRNL TITL 3 INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 421 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16242328
JRNL DOI 10.1016/J.BMCL.2005.09.064
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 311412.330
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 6649
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 + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.600
REMARK 3 FREE R VALUE TEST SET COUNT : 703
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 7550
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.00
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 455
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 46
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.052
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.05000
REMARK 3 B22 (A**2) : 4.50000
REMARK 3 B33 (A**2) : 1.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.89000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.000
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) : 0.700 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.670 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.100 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 27.09
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : A43.PAR
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : A43.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AYP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034461.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6649
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : NULL
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) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
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: CNX 2000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, ISOPROPANOL, HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.84900
REMARK 290 SMTRY3 2 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: 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 MET A 1
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 GLU A 7 71.62 37.34
REMARK 500 ASP A 8 -4.22 80.03
REMARK 500 VAL A 12 -78.78 -63.04
REMARK 500 GLU A 17 -124.36 -133.10
REMARK 500 ALA A 19 -7.38 -51.88
REMARK 500 GLU A 22 145.22 176.80
REMARK 500 MET A 42 154.83 -49.44
REMARK 500 ARG A 44 -150.02 53.89
REMARK 500 ALA A 45 48.71 -140.93
REMARK 500 VAL A 46 -9.61 -141.75
REMARK 500 ASP A 47 -75.73 -137.63
REMARK 500 PRO A 49 12.65 -60.48
REMARK 500 GLU A 50 -34.77 -150.50
REMARK 500 ASN A 51 6.62 -65.69
REMARK 500 ASN A 63 93.79 -160.34
REMARK 500 GLU A 65 4.56 -60.49
REMARK 500 VAL A 68 118.18 -36.62
REMARK 500 ARG A 75 99.94 -177.05
REMARK 500 ILE A 100 -52.33 -126.57
REMARK 500 ILE A 124 31.25 -96.25
REMARK 500 ARG A 129 -2.61 66.73
REMARK 500 ASP A 130 42.46 -151.74
REMARK 500 ASP A 139 -164.94 -101.75
REMARK 500 ASP A 142 52.24 73.62
REMARK 500 ASP A 148 90.63 49.32
REMARK 500 ASN A 165 -16.80 -145.29
REMARK 500 CYS A 168 157.28 176.43
REMARK 500 PRO A 211 31.78 -74.67
REMARK 500 ASP A 213 -9.94 -55.62
REMARK 500 LYS A 224 41.34 28.69
REMARK 500 LYS A 225 45.65 -90.03
REMARK 500 THR A 226 -0.80 -58.93
REMARK 500 TYR A 227 25.87 -79.32
REMARK 500 ALA A 237 -71.56 -58.93
REMARK 500 PRO A 250 -1.19 -58.32
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 43A A 270
DBREF 2AYP A 1 269 UNP O14757 CHK1_HUMAN 1 269
SEQRES 1 A 269 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 A 269 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 A 269 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 A 269 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 A 269 LYS LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU
SEQRES 6 A 269 ASN VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 A 269 ILE GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU
SEQRES 8 A 269 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 A 269 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 A 269 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 A 269 ILE LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 A 269 LEU LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG
SEQRES 13 A 269 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 A 269 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 A 269 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 A 269 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 A 269 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 A 269 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 A 269 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 A 269 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 A 269 LYS ASP ARG TRP TYR ASN LYS PRO LEU
HET 43A A 270 25
HETNAM 43A (3Z)-6-(4-HYDROXY-3-METHOXYPHENYL)-3-(1H-PYRROL-2-
HETNAM 2 43A YLMETHYLENE)-1,3-DIHYDRO-2H-INDOL-2-ONE
FORMUL 2 43A C20 H16 N2 O3
HELIX 1 1 ILE A 52 LEU A 62 1 11
HELIX 2 2 PHE A 93 ILE A 96 5 4
HELIX 3 3 PRO A 103 ILE A 124 1 22
HELIX 4 4 LYS A 132 GLU A 134 5 3
HELIX 5 5 PRO A 176 ARG A 181 1 6
HELIX 6 6 ALA A 186 GLY A 204 1 19
HELIX 7 7 CYS A 215 LYS A 222 1 8
HELIX 8 8 PRO A 230 ILE A 234 5 5
HELIX 9 9 ASP A 235 LEU A 246 1 12
HELIX 10 10 THR A 255 LYS A 260 1 6
SHEET 1 A 6 PHE A 5 VAL A 6 0
SHEET 2 A 6 TRP A 9 GLY A 16 -1 O TRP A 9 N VAL A 6
SHEET 3 A 6 VAL A 23 VAL A 27 -1 O LEU A 25 N GLN A 13
SHEET 4 A 6 ALA A 34 ASP A 41 -1 O VAL A 35 N ALA A 26
SHEET 5 A 6 ILE A 79 GLU A 85 -1 O LEU A 84 N ALA A 36
SHEET 6 A 6 PHE A 70 ARG A 75 -1 N GLY A 72 O PHE A 83
SHEET 1 B 3 GLY A 90 GLU A 91 0
SHEET 2 B 3 LEU A 136 LEU A 138 -1 O LEU A 138 N GLY A 90
SHEET 3 B 3 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 C 2 ILE A 126 THR A 127 0
SHEET 2 C 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
CISPEP 1 ASN A 229 PRO A 230 0 0.19
SITE 1 AC1 15 LEU A 15 ALA A 36 LYS A 38 GLU A 55
SITE 2 AC1 15 ASN A 59 VAL A 68 LEU A 84 GLU A 85
SITE 3 AC1 15 TYR A 86 CYS A 87 GLY A 90 LEU A 137
SITE 4 AC1 15 SER A 147 ASP A 148 PHE A 149
CRYST1 45.043 65.698 57.860 90.00 94.39 90.00 P 1 21 1 2
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 0.022201 0.000000 0.001702 0.00000
SCALE2 0.000000 0.015221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017334 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
