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HEADER HYDROLASE 07-SEP-23 8U33
TITLE CRYSTAL STRUCTURE OF KAI2 S95C MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ESTERASE KAI2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN DWARF-14-LIKE,PROTEIN D14-LIKE,PROTEIN HYPOSENSITIVE
COMPND 5 TO LIGHT,PROTEIN KARRIKIN INSENSITIVE 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: KAI2, D14L, HTL, AT4G37470, F6G17.120;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSUMO
KEYWDS A B HYDROLASE, KARRIKIN SIGNALLING, PLANT HORMONE RECEPTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.F.DAVIES,M.T.WATERS,C.S.BOND
REVDAT 1 18-SEP-24 8U33 0
JRNL AUTH S.F.DAVIES,C.S.BOND,M.T.WATERS
JRNL TITL CRYSTAL STRUCTURE OF KAI2 S95C MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0405
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 39292
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2136
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) : 1.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2624
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2077
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 237
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52000
REMARK 3 B22 (A**2) : -0.59000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.578
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2220 ; 0.010 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2090 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3025 ; 1.683 ; 1.631
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4822 ; 0.560 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 283 ; 6.506 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 10 ; 5.221 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;13.613 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2567 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 489 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1091 ; 1.847 ; 1.815
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1091 ; 1.839 ; 1.814
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1365 ; 2.813 ; 3.258
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1366 ; 2.818 ; 3.260
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1129 ; 3.648 ; 2.222
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1130 ; 3.646 ; 2.223
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1653 ; 5.371 ; 3.888
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2548 ; 6.349 ;20.800
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2498 ; 6.222 ;18.770
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 8U33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-23.
REMARK 100 THE DEPOSITION ID IS D_1000277243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9464
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41446
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 47.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 1.35300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M AMMONIUM SULFATE, 1 M HEPES PH
REMARK 280 7.2; KAI2 PROTEIN AT 14 MG/ML, 1MM DGR24^(ENT-5DS) LIGAND IN
REMARK 280 DMSO, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 27.93450
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 465 ALA A 269
REMARK 465 MET A 270
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 ALA A 18 107.79 -51.36
REMARK 500 THR A 28 -163.77 -119.75
REMARK 500 OCS A 95 -128.38 60.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8U2L RELATED DB: PDB
REMARK 900 8U2L CONTAINS THE SAME PROTEIN WITH AN EXTRA L48I MUTATION
DBREF 8U33 A 1 270 UNP Q9SZU7 KAI2_ARATH 1 270
SEQADV 8U33 OCS A 95 UNP Q9SZU7 SER 95 ENGINEERED MUTATION
SEQRES 1 A 270 MET GLY VAL VAL GLU GLU ALA HIS ASN VAL LYS VAL ILE
SEQRES 2 A 270 GLY SER GLY GLU ALA THR ILE VAL LEU GLY HIS GLY PHE
SEQRES 3 A 270 GLY THR ASP GLN SER VAL TRP LYS HIS LEU VAL PRO HIS
SEQRES 4 A 270 LEU VAL ASP ASP TYR ARG VAL VAL LEU TYR ASP ASN MET
SEQRES 5 A 270 GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE ASP
SEQRES 6 A 270 ARG TYR SER ASN LEU GLU GLY TYR SER PHE ASP LEU ILE
SEQRES 7 A 270 ALA ILE LEU GLU ASP LEU LYS ILE GLU SER CYS ILE PHE
SEQRES 8 A 270 VAL GLY HIS OCS VAL SER ALA MET ILE GLY VAL LEU ALA
SEQRES 9 A 270 SER LEU ASN ARG PRO ASP LEU PHE SER LYS ILE VAL MET
SEQRES 10 A 270 ILE SER ALA SER PRO ARG TYR VAL ASN ASP VAL ASP TYR
SEQRES 11 A 270 GLN GLY GLY PHE GLU GLN GLU ASP LEU ASN GLN LEU PHE
SEQRES 12 A 270 GLU ALA ILE ARG SER ASN TYR LYS ALA TRP CYS LEU GLY
SEQRES 13 A 270 PHE ALA PRO LEU ALA VAL GLY GLY ASP MET ASP SER ILE
SEQRES 14 A 270 ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 270 PRO ASP ILE ALA LEU SER VAL GLY GLN THR ILE PHE GLN
SEQRES 16 A 270 SER ASP MET ARG GLN ILE LEU PRO PHE VAL THR VAL PRO
SEQRES 17 A 270 CYS HIS ILE LEU GLN SER VAL LYS ASP LEU ALA VAL PRO
SEQRES 18 A 270 VAL VAL VAL SER GLU TYR LEU HIS ALA ASN LEU GLY CYS
SEQRES 19 A 270 GLU SER VAL VAL GLU VAL ILE PRO SER ASP GLY HIS LEU
SEQRES 20 A 270 PRO GLN LEU SER SER PRO ASP SER VAL ILE PRO VAL ILE
SEQRES 21 A 270 LEU ARG HIS ILE ARG ASN ASP ILE ALA MET
HET OCS A 95 9
HET SO4 A 301 5
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET DMS A 308 4
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 OCS C3 H7 N O5 S
FORMUL 2 SO4 O4 S 2-
FORMUL 3 GOL 6(C3 H8 O3)
FORMUL 9 DMS C2 H6 O S
FORMUL 10 HOH *237(H2 O)
HELIX 1 AA1 GLY A 2 HIS A 8 1 7
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 ASN A 58 PHE A 62 5 5
HELIX 5 AA5 ASP A 65 SER A 68 5 4
HELIX 6 AA6 ASN A 69 LEU A 84 1 16
HELIX 7 AA7 OCS A 95 ARG A 108 1 14
HELIX 8 AA8 GLU A 135 ASN A 149 1 15
HELIX 9 AA9 ASN A 149 GLY A 163 1 15
HELIX 10 AB1 SER A 168 MET A 181 1 14
HELIX 11 AB2 ARG A 182 GLN A 195 1 14
HELIX 12 AB3 MET A 198 VAL A 205 5 8
HELIX 13 AB4 PRO A 221 LEU A 232 1 12
HELIX 14 AB5 LEU A 247 SER A 252 1 6
HELIX 15 AB6 SER A 252 ASN A 266 1 15
SHEET 1 AA1 7 LYS A 11 GLY A 14 0
SHEET 2 AA1 7 ARG A 45 TYR A 49 -1 O VAL A 46 N ILE A 13
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N ILE A 20 O ARG A 45
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O HIS A 94 N GLY A 23
SHEET 5 AA1 7 PHE A 112 ILE A 118 1 O VAL A 116 N PHE A 91
SHEET 6 AA1 7 CYS A 209 LYS A 216 1 O HIS A 210 N MET A 117
SHEET 7 AA1 7 SER A 236 ASP A 244 1 O ILE A 241 N GLN A 213
LINK C HIS A 94 N OCS A 95 1555 1555 1.45
LINK C OCS A 95 N VAL A 96 1555 1555 1.39
CRYST1 50.798 55.869 53.147 90.00 116.02 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 0.019686 0.000000 0.009610 0.00000
SCALE2 0.000000 0.017899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020938 0.00000
TER 2129 ILE A 268
MASTER 261 0 9 15 7 0 0 6 2359 1 56 21
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