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HEADER HYDROLASE 16-JUN-20 7CC4
TITLE A BIODEGRADABLE PLASTIC-DEGRADING CUTINASE-LIKE ENZYME FROM THE
TITLE 2 PHYLLOSPHERE YEAST PSEUDOZYMA ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE-LIKE ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOESZIOMYCES ANTARCTICUS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 84753;
SOURCE 5 GENE: PACLE1, CLE1, PSANT_00437;
SOURCE 6 EXPRESSION_SYSTEM: MOESZIOMYCES ANTARCTICUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 84753;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GB-4(0)-X14
KEYWDS CUTINASE-LIKE ENZYME, BIODEGRADABLE PLASTIC DEGRADING ENZYME,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SUZUKI,T.WATANABE,H.KITAMOTO
REVDAT 1 15-JUL-20 7CC4 0
JRNL AUTH T.WATANABE,H.KITAMOTO
JRNL TITL A BIODEGRADABLE PLASTIC-DEGRADING CUTINASE-LIKE ENZYME FROM
JRNL TITL 2 THE PHYLLOSPHERE YEAST PSEUDOZYMA ANTARCTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19938
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1000
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1440
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.2230
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 : 1
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.73000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : 1.01000
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): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.976
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2902 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2574 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3950 ; 1.528 ; 1.640
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5990 ; 1.446 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 392 ; 6.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;31.701 ;23.692
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 422 ;11.959 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;19.049 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 398 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3376 ; 0.007 ; 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 7CC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1300016872.
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 : 8.5
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 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 : 20991
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 31.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 12.80
REMARK 200 R MERGE FOR SHELL (I) : 0.41900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 2.0.229
REMARK 200 STARTING MODEL: 2CZQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS HYDROCHLORIDE, SODIUM
REMARK 280 ACETATE TRIHYDRATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 22.07500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.96850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.79800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.96850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.07500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.79800
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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: 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 15 -3.70 78.21
REMARK 500 ASN A 71 104.83 -161.73
REMARK 500 SER A 82 -132.83 60.04
REMARK 500 ASN B 52 -179.93 -174.87
REMARK 500 SER B 82 -127.92 60.26
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 NA B 201
DBREF 7CC4 A 1 198 UNP S6BC01 S6BC01_PSEA2 27 224
DBREF 7CC4 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 NA B 201 1
HETNAM NA SODIUM ION
FORMUL 3 NA NA 1+
FORMUL 4 HOH *203(H2 O)
HELIX 1 AA1 PHE A 24 VAL A 35 1 12
HELIX 2 AA2 SER A 53 ASN A 71 1 19
HELIX 3 AA3 SER A 82 LEU A 92 1 11
HELIX 4 AA4 PRO A 93 LEU A 95 5 3
HELIX 5 AA5 THR A 96 ALA A 102 1 7
HELIX 6 AA6 SER A 137 THR A 141 5 5
HELIX 7 AA7 PRO A 145 SER A 150 5 6
HELIX 8 AA8 THR A 172 TYR A 180 5 9
HELIX 9 AA9 ASN A 181 GLY A 198 1 18
HELIX 10 AB1 SER B 21 GLY B 23 5 3
HELIX 11 AB2 PHE B 24 VAL B 35 1 12
HELIX 12 AB3 SER B 53 ASN B 71 1 19
HELIX 13 AB4 SER B 82 LEU B 92 1 11
HELIX 14 AB5 PRO B 93 LEU B 95 5 3
HELIX 15 AB6 GLY B 97 ALA B 102 1 6
HELIX 16 AB7 SER B 137 THR B 141 5 5
HELIX 17 AB8 PRO B 145 SER B 150 5 6
HELIX 18 AB9 THR B 172 TYR B 180 5 9
HELIX 19 AC1 ASN B 181 GLY B 198 1 18
SHEET 1 AA1 6 GLY A 38 ASP A 42 0
SHEET 2 AA1 6 TYR A 6 THR A 11 1 N ASN A 10 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 GLU B 79 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 ILE B 155 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 2.04
SSBOND 2 CYS A 156 CYS A 163 1555 1555 2.05
SSBOND 3 CYS B 3 CYS B 75 1555 1555 2.04
SSBOND 4 CYS B 156 CYS B 163 1555 1555 2.09
LINK NA NA B 201 O HOH B 363 1555 1555 3.04
SITE 1 AC1 5 ASN A 117 ASP B 123 GLY B 124 TYR B 158
SITE 2 AC1 5 HOH B 363
CRYST1 44.150 61.596 109.937 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 0.022650 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009096 0.00000
TER 1424 GLY A 198
TER 2848 GLY B 198
MASTER 288 0 1 19 12 0 2 6 3050 2 10 32
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