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HEADER HYDROLASE 27-AUG-20 7CW1
TITLE CRYSTAL STRUCTURE OF A BIODEGRADABLE PLASTIC-DEGRADING CUTINASE-LIKE
TITLE 2 ENZYME FROM THE PHYLLOSPHERE YEAST, PSEUDOZYMA ANTARCTICA, SOLVED BY
TITLE 3 GETTING THE PHASE FROM ANOMALOUS SCATTERING OF UNCOVALENTLY
TITLE 4 COORDINATED ARSENIC (CACODYLATE).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE-LIKE ENZYME;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 84753
KEYWDS CUTINASE-LIKE ENZYME, BIODEGRADABLE PLASTIC DEGRADING ENZYME,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SUZUKI
REVDAT 1 16-SEP-20 7CW1 0
JRNL AUTH K.SUZUKI
JRNL TITL CRYSTAL STRUCTURE OF A BIODEGRADABLE PLASTIC-DEGRADING
JRNL TITL 2 CUTINASE-LIKE ENZYME FROM THE PHYLLOSPHERE YEAST, PSEUDOZYMA
JRNL TITL 3 ANTARCTICA, SOLVED BY GETTING THE PHASE FROM ANOMALOUS
JRNL TITL 4 SCATTERING OF UNCOVALENTLY COORDINATED ARSENIC (CACODYLATE).
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 31548
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1713
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2239
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.1740
REMARK 3 BIN FREE R VALUE SET COUNT : 119
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2846
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : -0.27000
REMARK 3 B33 (A**2) : 0.41000
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): 0.113
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.913
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2910 ; 0.012 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2586 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3962 ; 1.684 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6014 ; 1.594 ; 1.574
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 392 ; 6.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;31.162 ;23.692
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 422 ;11.061 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;19.603 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 400 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3376 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 580 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7CW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1300017284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
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 : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.6.2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33315
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 55.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.90
REMARK 200 R MERGE FOR SHELL (I) : 0.48700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CRANK2 2.0.229
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M SODIUM ACETATE TRIHYDRATE,
REMARK 280 0.085M SODIUM CACODYLATE TRIHYDRATE , 25.5%W/V POLYETHYLENE
REMARK 280 GLYCOL 8000, 15%W/V POLYETHYLENE GLYCOL 400, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 22.03250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.19350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.79350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.19350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.03250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.79350
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ALA A 1
REMARK 465 ALA B 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 134 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 30 CG - CD - NE ANGL. DEV. = -14.6 DEGREES
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 THR A 14 -124.83 45.02
REMARK 500 SER A 82 -128.39 60.88
REMARK 500 ASN B 71 106.48 -164.66
REMARK 500 SER B 82 -123.49 64.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7CC4 RELATED DB: PDB
REMARK 900 7CC4 CONTAINS THE SAME PROTEIN THAT WAS SOLVED BY THE MOLECULAR
REMARK 900 REPLACEMENT METHOD.
DBREF 7CW1 A 1 198 UNP S6BC01 S6BC01_PSEA2 27 224
DBREF 7CW1 B 1 198 UNP S6BC01 S6BC01_PSEA2 27 224
SEQRES 1 A 198 ALA GLY CYS SER SER TYR VAL ILE ILE ASN THR ARG GLY
SEQRES 2 A 198 THR SER GLU PRO GLN GLY PRO SER VAL GLY PHE ARG THR
SEQRES 3 A 198 MET ASN THR ARG ILE ARG SER ALA VAL SER GLY GLY SER
SEQRES 4 A 198 GLU TYR ASP THR VAL TYR PRO ALA GLY ILE ASP GLN ASN
SEQRES 5 A 198 SER ALA GLN GLY THR ALA ASN ILE VAL ALA GLN VAL LYS
SEQRES 6 A 198 ALA GLY LEU ALA ARG ASN PRO ASN THR CYS PHE LEU LEU
SEQRES 7 A 198 GLU GLY TYR SER GLN GLY ALA ALA ALA THR CYS ASN ALA
SEQRES 8 A 198 LEU PRO GLN LEU THR GLY ALA ALA PHE ASP ALA VAL LYS
SEQRES 9 A 198 GLY VAL ILE LEU ILE GLY ASN PRO GLU HIS LYS PRO ASN
SEQRES 10 A 198 LEU ALA CYS ASN VAL ASP GLY ASN GLY GLY LYS THR THR
SEQRES 11 A 198 PHE SER ALA ARG GLY ILE SER ALA ALA PHE THR GLN GLY
SEQRES 12 A 198 VAL PRO SER ASN TRP VAL SER LYS THR LEU ASP ILE CYS
SEQRES 13 A 198 ILE TYR GLY ASP GLY VAL CYS ASP VAL SER SER GLY PHE
SEQRES 14 A 198 GLY ILE THR PRO GLN HIS LEU THR TYR GLY TYR ASN THR
SEQRES 15 A 198 ASN VAL GLN THR MET GLY ALA ASN PHE GLY ILE LYS ALA
SEQRES 16 A 198 LEU GLN GLY
SEQRES 1 B 198 ALA GLY CYS SER SER TYR VAL ILE ILE ASN THR ARG GLY
SEQRES 2 B 198 THR SER GLU PRO GLN GLY PRO SER VAL GLY PHE ARG THR
SEQRES 3 B 198 MET ASN THR ARG ILE ARG SER ALA VAL SER GLY GLY SER
SEQRES 4 B 198 GLU TYR ASP THR VAL TYR PRO ALA GLY ILE ASP GLN ASN
SEQRES 5 B 198 SER ALA GLN GLY THR ALA ASN ILE VAL ALA GLN VAL LYS
SEQRES 6 B 198 ALA GLY LEU ALA ARG ASN PRO ASN THR CYS PHE LEU LEU
SEQRES 7 B 198 GLU GLY TYR SER GLN GLY ALA ALA ALA THR CYS ASN ALA
SEQRES 8 B 198 LEU PRO GLN LEU THR GLY ALA ALA PHE ASP ALA VAL LYS
SEQRES 9 B 198 GLY VAL ILE LEU ILE GLY ASN PRO GLU HIS LYS PRO ASN
SEQRES 10 B 198 LEU ALA CYS ASN VAL ASP GLY ASN GLY GLY LYS THR THR
SEQRES 11 B 198 PHE SER ALA ARG GLY ILE SER ALA ALA PHE THR GLN GLY
SEQRES 12 B 198 VAL PRO SER ASN TRP VAL SER LYS THR LEU ASP ILE CYS
SEQRES 13 B 198 ILE TYR GLY ASP GLY VAL CYS ASP VAL SER SER GLY PHE
SEQRES 14 B 198 GLY ILE THR PRO GLN HIS LEU THR TYR GLY TYR ASN THR
SEQRES 15 B 198 ASN VAL GLN THR MET GLY ALA ASN PHE GLY ILE LYS ALA
SEQRES 16 B 198 LEU GLN GLY
HET CAD A 201 5
HET NA A 202 1
HET CAD B 201 5
HETNAM CAD CACODYLIC ACID
HETNAM NA SODIUM ION
HETSYN CAD HYDROXYDIMETHYLARSINE OXIDE
FORMUL 3 CAD 2(C2 H7 AS O2)
FORMUL 4 NA NA 1+
FORMUL 6 HOH *361(H2 O)
HELIX 1 AA1 SER A 21 GLY A 23 5 3
HELIX 2 AA2 PHE A 24 VAL A 35 1 12
HELIX 3 AA3 SER A 53 ASN A 71 1 19
HELIX 4 AA4 SER A 82 LEU A 92 1 11
HELIX 5 AA5 PRO A 93 LEU A 95 5 3
HELIX 6 AA6 THR A 96 ALA A 102 1 7
HELIX 7 AA7 SER A 137 THR A 141 5 5
HELIX 8 AA8 PRO A 145 SER A 150 5 6
HELIX 9 AA9 THR A 172 TYR A 180 5 9
HELIX 10 AB1 ASN A 181 GLY A 198 1 18
HELIX 11 AB2 SER B 21 GLY B 23 5 3
HELIX 12 AB3 PHE B 24 VAL B 35 1 12
HELIX 13 AB4 SER B 53 ASN B 71 1 19
HELIX 14 AB5 SER B 82 LEU B 92 1 11
HELIX 15 AB6 PRO B 93 THR B 96 5 4
HELIX 16 AB7 GLY B 97 ALA B 102 1 6
HELIX 17 AB8 SER B 137 THR B 141 5 5
HELIX 18 AB9 PRO B 145 SER B 150 5 6
HELIX 19 AC1 ASP B 164 GLY B 168 5 5
HELIX 20 AC2 THR B 172 TYR B 180 5 9
HELIX 21 AC3 ASN B 181 GLY B 198 1 18
SHEET 1 AA1 6 GLU A 40 ASP A 42 0
SHEET 2 AA1 6 TYR A 6 THR A 11 1 N ILE A 8 O TYR A 41
SHEET 3 AA1 6 CYS A 75 TYR A 81 1 O LEU A 77 N ILE A 9
SHEET 4 AA1 6 VAL A 103 ILE A 109 1 O ILE A 107 N LEU A 78
SHEET 5 AA1 6 THR A 152 ILE A 155 1 O ILE A 155 N LEU A 108
SHEET 6 AA1 6 ASN A 121 VAL A 122 1 N VAL A 122 O ASP A 154
SHEET 1 AA2 6 GLY B 38 ASP B 42 0
SHEET 2 AA2 6 TYR B 6 THR B 11 1 N ILE B 8 O SER B 39
SHEET 3 AA2 6 CYS B 75 TYR B 81 1 O LEU B 77 N ILE B 9
SHEET 4 AA2 6 VAL B 103 ILE B 109 1 O ILE B 107 N LEU B 78
SHEET 5 AA2 6 THR B 152 ILE B 155 1 O LEU B 153 N LEU B 108
SHEET 6 AA2 6 ASN B 121 VAL B 122 1 N VAL B 122 O ASP B 154
SSBOND 1 CYS A 3 CYS A 75 1555 1555 2.09
SSBOND 2 CYS A 156 CYS A 163 1555 1555 2.05
SSBOND 3 CYS B 3 CYS B 75 1555 1555 2.14
SSBOND 4 CYS B 156 CYS B 163 1555 1555 2.09
LINK NA NA A 202 O HOH A 366 1555 1555 3.11
CRYST1 44.065 61.587 110.387 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 0.022694 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016237 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009059 0.00000
TER 1424 GLY A 198
TER 2848 GLY B 198
MASTER 309 0 3 21 12 0 0 6 3218 2 20 32
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