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HEADER HYDROLASE 14-JUL-05 2CZQ
TITLE A NOVEL CUTINASE-LIKE PROTEIN FROM CRYPTOCOCCUS SP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOCOCCUS SP.;
SOURCE 3 ORGANISM_COMMON: FUNGI;
SOURCE 4 STRAIN: S-2
KEYWDS ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MASAKI,N.R.KAMINI,H.IKEDA,H.IEFUJI,H.KONDO,M.SUZUKI,
AUTHOR 2 S.TSUDA
REVDAT 1 14-JUL-06 2CZQ 0
JRNL AUTH K.MASAKI,N.R.KAMINI,H.IKEDA,H.IEFUJI
JRNL TITL A CUTINASE-LIKE PROTEIN FROM YEAST, CRYPTOCOCCUS
JRNL TITL 2 SP. S-2 HYDROLYSES POLY(LACTIC ACID) AND OTHER
JRNL TITL 3 BIODEGRADABLE PLASTICS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 142150
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) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 15686
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.05
REMARK 3 BIN RESOLUTION RANGE LOW : 1.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8719
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 972
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3451
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 5.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.02000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.029
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.027
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3095 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4216 ; 1.167 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 410 ; 5.603 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 484 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2372 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1562 ; 0.189 ; 0.200
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): 304 ; 0.076 ; 0.200
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): 91 ; 0.149 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 43 ; 0.093 ; 0.200
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): 2028 ; 0.524 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3249 ; 0.878 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1067 ; 1.157 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 964 ; 1.734 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3095 ; 0.502 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 410 ; 1.518 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3041 ; 1.321 ; 2.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CZQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-2005.
REMARK 100 THE RCSB ID CODE IS RCSB024807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-2002; 27-MAY-2002
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.90
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; PHOTON FACTORY
REMARK 200 BEAMLINE : BL6A; BL6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978; 1.0717, 1.0723, 0.9779
REMARK 200 MONOCHROMATOR : MIRROR-MONOCHROMATOR SI(111);
REMARK 200 MIRROR-MONOCHROMATOR SI(111)
REMARK 200 OPTICS : MIRROR-MONOCHROMATOR; MIRROR-
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 157936
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.06700
REMARK 200 FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : 0.33300
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3-1.6M SODIUM CITRATE, PH 5.9,
REMARK 280 VAPOR DIFFUSION, 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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 17.23900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.75700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.40350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.75700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.23900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.40350
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO B 20 CG PRO B 20 CD 0.060
REMARK 500 PRO B 20 CD PRO B 20 N -0.043
REMARK 500 PRO B 75 CG PRO B 75 CD 0.126
REMARK 500 PRO B 75 CD PRO B 75 N -0.043
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 220 DISTANCE = 7.63 ANGSTROMS
DBREF 2CZQ A 1 205 GB 29467703 BAC67242 35 239
DBREF 2CZQ B 1 205 GB 29467703 BAC67242 35 239
SEQRES 1 A 205 ALA THR SER SER ALA CYS PRO GLN TYR VAL LEU ILE ASN
SEQRES 2 A 205 THR ARG GLY THR GLY GLU PRO GLN GLY GLN SER ALA GLY
SEQRES 3 A 205 PHE ARG THR MET ASN SER GLN ILE THR ALA ALA LEU SER
SEQRES 4 A 205 GLY GLY THR ILE TYR ASN THR VAL TYR THR ALA ASP PHE
SEQRES 5 A 205 SER GLN ASN SER ALA ALA GLY THR ALA ASP ILE ILE ARG
SEQRES 6 A 205 ARG ILE ASN SER GLY LEU ALA ALA ASN PRO ASN VAL CYS
SEQRES 7 A 205 TYR ILE LEU GLN GLY TYR SER GLN GLY ALA ALA ALA THR
SEQRES 8 A 205 VAL VAL ALA LEU GLN GLN LEU GLY THR SER GLY ALA ALA
SEQRES 9 A 205 PHE ASN ALA VAL LYS GLY VAL PHE LEU ILE GLY ASN PRO
SEQRES 10 A 205 ASP HIS LYS SER GLY LEU THR CYS ASN VAL ASP SER ASN
SEQRES 11 A 205 GLY GLY THR THR THR ARG ASN VAL ASN GLY LEU SER VAL
SEQRES 12 A 205 ALA TYR GLN GLY SER VAL PRO SER GLY TRP VAL SER LYS
SEQRES 13 A 205 THR LEU ASP VAL CYS ALA TYR GLY ASP GLY VAL CYS ASP
SEQRES 14 A 205 THR ALA HIS GLY PHE GLY ILE ASN ALA GLN HIS LEU SER
SEQRES 15 A 205 TYR PRO SER ASP GLN GLY VAL GLN THR MET GLY TYR LYS
SEQRES 16 A 205 PHE ALA VAL ASN LYS LEU GLY GLY SER ALA
SEQRES 1 B 205 ALA THR SER SER ALA CYS PRO GLN TYR VAL LEU ILE ASN
SEQRES 2 B 205 THR ARG GLY THR GLY GLU PRO GLN GLY GLN SER ALA GLY
SEQRES 3 B 205 PHE ARG THR MET ASN SER GLN ILE THR ALA ALA LEU SER
SEQRES 4 B 205 GLY GLY THR ILE TYR ASN THR VAL TYR THR ALA ASP PHE
SEQRES 5 B 205 SER GLN ASN SER ALA ALA GLY THR ALA ASP ILE ILE ARG
SEQRES 6 B 205 ARG ILE ASN SER GLY LEU ALA ALA ASN PRO ASN VAL CYS
SEQRES 7 B 205 TYR ILE LEU GLN GLY TYR SER GLN GLY ALA ALA ALA THR
SEQRES 8 B 205 VAL VAL ALA LEU GLN GLN LEU GLY THR SER GLY ALA ALA
SEQRES 9 B 205 PHE ASN ALA VAL LYS GLY VAL PHE LEU ILE GLY ASN PRO
SEQRES 10 B 205 ASP HIS LYS SER GLY LEU THR CYS ASN VAL ASP SER ASN
SEQRES 11 B 205 GLY GLY THR THR THR ARG ASN VAL ASN GLY LEU SER VAL
SEQRES 12 B 205 ALA TYR GLN GLY SER VAL PRO SER GLY TRP VAL SER LYS
SEQRES 13 B 205 THR LEU ASP VAL CYS ALA TYR GLY ASP GLY VAL CYS ASP
SEQRES 14 B 205 THR ALA HIS GLY PHE GLY ILE ASN ALA GLN HIS LEU SER
SEQRES 15 B 205 TYR PRO SER ASP GLN GLY VAL GLN THR MET GLY TYR LYS
SEQRES 16 B 205 PHE ALA VAL ASN LYS LEU GLY GLY SER ALA
HET CIT 501 13
HET CIT 502 13
HET EDO 601 4
HET EDO 602 4
HETNAM CIT CITRIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CIT 2(C6 H8 O7)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 7 HOH *410(H2 O1)
HELIX 1 1 PHE A 27 LEU A 38 1 12
HELIX 2 2 SER A 56 ASN A 74 1 19
HELIX 3 3 SER A 85 GLY A 99 1 15
HELIX 4 4 GLY A 102 ALA A 107 1 6
HELIX 5 5 SER A 142 GLY A 147 1 6
HELIX 6 6 PRO A 150 SER A 155 5 6
HELIX 7 7 ASN A 177 SER A 182 1 6
HELIX 8 8 TYR A 183 SER A 185 5 3
HELIX 9 9 ASP A 186 LEU A 201 1 16
HELIX 10 10 SER B 24 GLY B 26 5 3
HELIX 11 11 PHE B 27 LEU B 38 1 12
HELIX 12 12 SER B 56 ASN B 74 1 19
HELIX 13 13 SER B 85 GLY B 99 1 15
HELIX 14 14 GLY B 102 ALA B 107 1 6
HELIX 15 15 SER B 142 GLY B 147 1 6
HELIX 16 16 PRO B 150 SER B 155 5 6
HELIX 17 17 ASN B 177 SER B 185 5 9
HELIX 18 18 ASP B 186 LEU B 201 1 16
SHEET 1 A 6 GLY A 41 ASN A 45 0
SHEET 2 A 6 TYR A 9 THR A 14 1 N LEU A 11 O THR A 42
SHEET 3 A 6 CYS A 78 TYR A 84 1 O GLN A 82 N ILE A 12
SHEET 4 A 6 VAL A 108 ILE A 114 1 O PHE A 112 N LEU A 81
SHEET 5 A 6 THR A 157 VAL A 160 1 O VAL A 160 N LEU A 113
SHEET 6 A 6 ASN A 126 VAL A 127 1 N VAL A 127 O ASP A 159
SHEET 1 B 6 GLY B 41 ASN B 45 0
SHEET 2 B 6 TYR B 9 THR B 14 1 N ASN B 13 O TYR B 44
SHEET 3 B 6 CYS B 78 TYR B 84 1 O GLN B 82 N ILE B 12
SHEET 4 B 6 VAL B 108 ILE B 114 1 O PHE B 112 N LEU B 81
SHEET 5 B 6 THR B 157 VAL B 160 1 O VAL B 160 N LEU B 113
SHEET 6 B 6 ASN B 126 VAL B 127 1 N VAL B 127 O ASP B 159
SSBOND 1 CYS A 6 CYS A 78
SSBOND 2 CYS A 161 CYS A 168
SSBOND 3 CYS B 6 CYS B 78
SSBOND 4 CYS B 161 CYS B 168
CRYST1 34.478 82.807 123.514 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 0.029004 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012076 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008096 0.00000
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