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HEADER HYDROLASE 24-NOV-25 9XUE
TITLE CRYSTAL STRUCTURE OF THE DEEP-SEA HALOPHILIC PET HYDROLASE DSPETASE01
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PET HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AETOKTHONOS HYDRILLICOLA THURMOND2011;
SOURCE 3 ORGANISM_TAXID: 2712845;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, PET HYDROLASE, PET DEGRADATION ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI,M.Z.ZHANG,S.Q.HUANG,C.ZENG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO
REVDAT 1 23-SEP-26 9XUE 0
JRNL AUTH X.LI,M.Z.ZHANG,S.Q.HUANG,C.ZENG,J.-W.HUANG,C.-C.CHEN,
JRNL AUTH 2 R.-T.GUO
JRNL TITL CRYSTAL STRUCTURE OF THE DEEP-SEA HALOPHILIC PET HYDROLASE
JRNL TITL 2 DSPETASE01
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 54329
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2790
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) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3288
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.80000
REMARK 3 B22 (A**2) : -0.77000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.092
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.844
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4062 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3639 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5561 ; 1.752 ; 1.658
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8424 ; 1.522 ; 1.572
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 539 ; 6.796 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;24.841 ;19.680
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 585 ;12.168 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;21.014 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 550 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4750 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 956 ; 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): 2085 ; 1.518 ; 1.966
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2084 ; 1.514 ; 1.965
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2614 ; 1.980 ; 2.946
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2615 ; 1.980 ; 2.946
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1977 ; 2.323 ; 2.205
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1978 ; 2.322 ; 2.206
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2936 ; 3.346 ; 3.221
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4746 ; 4.504 ;24.760
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4580 ; 4.252 ;23.924
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 9XUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 28-NOV-25.
REMARK 100 THE DEPOSITION ID IS D_1300066358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : TPS 07A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57132
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM FLUORIDE,25% W/V
REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 22.45800
REMARK 290 SMTRY3 2 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 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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 329 O HOH A 558 2.13
REMARK 500 OE1 GLU B 225 O HOH B 401 2.15
REMARK 500 O HOH A 500 O HOH A 584 2.17
REMARK 500 O HOH B 673 O HOH B 674 2.17
REMARK 500 O HOH A 424 O HOH A 540 2.17
REMARK 500 O HOH B 602 O HOH B 675 2.18
REMARK 500 O THR A 189 O HOH A 301 2.18
REMARK 500 O1 PEG B 301 O HOH B 402 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 624 O HOH B 660 2545 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 60 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 60 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 60 NE - CZ - NH2 ANGL. DEV. = -4.5 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 92 -17.32 78.17
REMARK 500 SER A 159 -119.44 59.77
REMARK 500 THR A 182 58.44 37.28
REMARK 500 HIS A 213 -88.43 -132.36
REMARK 500 LEU A 221 49.28 -85.13
REMARK 500 THR B 92 -1.20 69.28
REMARK 500 SER B 159 -122.26 65.74
REMARK 500 THR B 182 59.11 39.02
REMARK 500 HIS B 213 -90.17 -120.54
REMARK 500 SER B 243 121.51 -33.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 693 DISTANCE = 6.32 ANGSTROMS
DBREF 9XUE A 32 287 PDB 9XUE 9XUE 32 287
DBREF 9XUE B 32 287 PDB 9XUE 9XUE 32 287
SEQRES 1 A 256 ASP TYR GLU ARG GLY PRO ASP PRO THR SER SER SER ILE
SEQRES 2 A 256 GLU ALA SER ARG GLY PRO TYR ALA VAL SER THR LYS SER
SEQRES 3 A 256 ILE SER ARG PHE ALA ALA ARG GLY PHE GLY GLY GLY THR
SEQRES 4 A 256 ILE HIS TYR PRO THR THR THR ALA ASP GLY THR PHE GLY
SEQRES 5 A 256 VAL VAL ALA VAL SER PRO GLY TYR THR ALA SER GLU SER
SEQRES 6 A 256 THR ILE ARG TRP LEU GLY PRO ARG LEU ALA SER PHE GLY
SEQRES 7 A 256 PHE VAL VAL ILE THR PHE ASP THR ASN SER ARG TYR ASP
SEQRES 8 A 256 GLN PRO ARG ALA ARG GLY THR GLN LEU LEU ALA ALA ILE
SEQRES 9 A 256 ASP GLN ALA ILE GLY ASP SER THR VAL GLY SER ARG ILE
SEQRES 10 A 256 ASP PRO SER ARG GLN ALA VAL VAL GLY HIS SER MET GLY
SEQRES 11 A 256 GLY GLY GLY THR LEU GLU ALA ALA LYS THR ARG PRO SER
SEQRES 12 A 256 ILE GLU ALA ALA VAL GLY LEU THR PRO TRP ASN LEU ASP
SEQRES 13 A 256 LYS THR TRP PRO GLU VAL GLU ALA ALA ALA LEU GLN ILE
SEQRES 14 A 256 GLY ALA GLN ASN ASP SER VAL ALA PRO PRO ARG SER HIS
SEQRES 15 A 256 ALA VAL PRO PHE TYR GLY SER LEU THR ASN ALA GLU ARG
SEQRES 16 A 256 ARG ALA TYR LEU GLU LEU ARG GLY ALA SER HIS PHE ALA
SEQRES 17 A 256 PRO ASN THR SER ASN THR THR ILE ALA LYS TYR THR LEU
SEQRES 18 A 256 ALA TRP LEU LYS ARG TYR VAL ASP ASP ASP THR ARG TYR
SEQRES 19 A 256 GLU GLN PHE LEU ALA PRO GLY PRO SER THR GLY PHE GLY
SEQRES 20 A 256 SER ALA VAL SER ASP TYR ARG ILE GLN
SEQRES 1 B 256 ASP TYR GLU ARG GLY PRO ASP PRO THR SER SER SER ILE
SEQRES 2 B 256 GLU ALA SER ARG GLY PRO TYR ALA VAL SER THR LYS SER
SEQRES 3 B 256 ILE SER ARG PHE ALA ALA ARG GLY PHE GLY GLY GLY THR
SEQRES 4 B 256 ILE HIS TYR PRO THR THR THR ALA ASP GLY THR PHE GLY
SEQRES 5 B 256 VAL VAL ALA VAL SER PRO GLY TYR THR ALA SER GLU SER
SEQRES 6 B 256 THR ILE ARG TRP LEU GLY PRO ARG LEU ALA SER PHE GLY
SEQRES 7 B 256 PHE VAL VAL ILE THR PHE ASP THR ASN SER ARG TYR ASP
SEQRES 8 B 256 GLN PRO ARG ALA ARG GLY THR GLN LEU LEU ALA ALA ILE
SEQRES 9 B 256 ASP GLN ALA ILE GLY ASP SER THR VAL GLY SER ARG ILE
SEQRES 10 B 256 ASP PRO SER ARG GLN ALA VAL VAL GLY HIS SER MET GLY
SEQRES 11 B 256 GLY GLY GLY THR LEU GLU ALA ALA LYS THR ARG PRO SER
SEQRES 12 B 256 ILE GLU ALA ALA VAL GLY LEU THR PRO TRP ASN LEU ASP
SEQRES 13 B 256 LYS THR TRP PRO GLU VAL GLU ALA ALA ALA LEU GLN ILE
SEQRES 14 B 256 GLY ALA GLN ASN ASP SER VAL ALA PRO PRO ARG SER HIS
SEQRES 15 B 256 ALA VAL PRO PHE TYR GLY SER LEU THR ASN ALA GLU ARG
SEQRES 16 B 256 ARG ALA TYR LEU GLU LEU ARG GLY ALA SER HIS PHE ALA
SEQRES 17 B 256 PRO ASN THR SER ASN THR THR ILE ALA LYS TYR THR LEU
SEQRES 18 B 256 ALA TRP LEU LYS ARG TYR VAL ASP ASP ASP THR ARG TYR
SEQRES 19 B 256 GLU GLN PHE LEU ALA PRO GLY PRO SER THR GLY PHE GLY
SEQRES 20 B 256 SER ALA VAL SER ASP TYR ARG ILE GLN
HET PEG B 301 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 PEG C4 H10 O3
FORMUL 4 HOH *580(H2 O)
HELIX 1 AA1 SER A 42 ALA A 46 5 5
HELIX 2 AA2 SER A 59 ALA A 63 5 5
HELIX 3 AA3 SER A 94 ARG A 99 5 6
HELIX 4 AA4 TRP A 100 SER A 107 1 8
HELIX 5 AA5 GLN A 123 GLY A 140 1 18
HELIX 6 AA6 VAL A 144 SER A 146 5 3
HELIX 7 AA7 SER A 159 ARG A 172 1 14
HELIX 8 AA8 HIS A 213 LEU A 221 1 9
HELIX 9 AA9 PHE A 238 THR A 242 5 5
HELIX 10 AB1 ASN A 244 ASP A 260 1 17
HELIX 11 AB2 ASP A 262 LEU A 269 5 8
HELIX 12 AB3 THR B 40 ALA B 46 1 7
HELIX 13 AB4 SER B 94 ARG B 99 5 6
HELIX 14 AB5 TRP B 100 SER B 107 1 8
HELIX 15 AB6 GLN B 123 ASP B 141 1 19
HELIX 16 AB7 VAL B 144 SER B 146 5 3
HELIX 17 AB8 SER B 159 ARG B 172 1 14
HELIX 18 AB9 HIS B 213 LEU B 221 1 9
HELIX 19 AC1 PHE B 238 THR B 242 5 5
HELIX 20 AC2 ASN B 244 ASP B 260 1 17
HELIX 21 AC3 ASP B 262 LEU B 269 5 8
SHEET 1 AA1 9 VAL A 53 ILE A 58 0
SHEET 2 AA1 9 GLY A 69 PRO A 74 -1 O GLY A 69 N ILE A 58
SHEET 3 AA1 9 VAL A 111 PHE A 115 -1 O VAL A 112 N HIS A 72
SHEET 4 AA1 9 PHE A 82 SER A 88 1 N VAL A 87 O ILE A 113
SHEET 5 AA1 9 ILE A 148 HIS A 158 1 O VAL A 156 N SER A 88
SHEET 6 AA1 9 ALA A 177 LEU A 181 1 O LEU A 181 N GLY A 157
SHEET 7 AA1 9 ALA A 196 ALA A 202 1 O ILE A 200 N GLY A 180
SHEET 8 AA1 9 ARG A 227 LEU A 232 1 O LEU A 232 N GLY A 201
SHEET 9 AA1 9 VAL A 281 GLN A 287 -1 O ASP A 283 N GLU A 231
SHEET 1 AA2 9 VAL B 53 ILE B 58 0
SHEET 2 AA2 9 GLY B 69 PRO B 74 -1 O ILE B 71 N LYS B 56
SHEET 3 AA2 9 VAL B 111 PHE B 115 -1 O VAL B 112 N HIS B 72
SHEET 4 AA2 9 PHE B 82 SER B 88 1 N VAL B 85 O VAL B 111
SHEET 5 AA2 9 ILE B 148 HIS B 158 1 O VAL B 156 N ALA B 86
SHEET 6 AA2 9 ALA B 177 LEU B 181 1 O LEU B 181 N GLY B 157
SHEET 7 AA2 9 ALA B 196 ALA B 202 1 O ILE B 200 N GLY B 180
SHEET 8 AA2 9 ARG B 227 LEU B 232 1 O LEU B 232 N GLY B 201
SHEET 9 AA2 9 VAL B 281 GLN B 287 -1 O ASP B 283 N GLU B 231
CISPEP 1 ALA A 270 PRO A 271 0 10.09
CISPEP 2 ALA B 270 PRO B 271 0 -2.94
CRYST1 70.279 44.916 73.160 90.00 92.82 90.00 P 1 21 1 4
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 0.014229 0.000000 0.000700 0.00000
SCALE2 0.000000 0.022264 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013685 0.00000
TER 1983 GLN A 287
TER 3945 GLN B 287
MASTER 331 0 1 21 18 0 0 6 4451 2 7 40
END |