| content |
HEADER HYDROLASE 26-JAN-21 7DZV
TITLE CYRSTAL STRUCTURE OF PETASE E186A MUTANT FROM RHIZOBACTER GUMMIPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DLH DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PET HYDROLASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBACTER GUMMIPHILUS;
SOURCE 3 ORGANISM_COMMON: METHYLIBIUM SP. NS21;
SOURCE 4 ORGANISM_TAXID: 946333;
SOURCE 5 STRAIN: NS21;
SOURCE 6 GENE: A4W93_05950;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI-B
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-Y.SAGONG,K.-J.KIM
REVDAT 1 07-JUL-21 7DZV 0
JRNL AUTH H.-Y.SAGONG,H.F.SON,H.SEO,H.HONG,D.LEE,K.-J.KIM
JRNL TITL IMPLICATIONS FOR THE PET DECOMPOSITION MECHANISM THROUGH
JRNL TITL 2 SIMILARITY AND DISSIMILARITY BETWEEN PETASES FROM
JRNL TITL 3 RHIZOBACTER GUMMIPHILUS AND IDEONELLA SAKAIENSIS.
JRNL REF J HAZARD MATER 2021
JRNL REFN ISSN 1873-3336
JRNL DOI 10.1016/J.JHAZMAT.2021.126075
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 38676
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) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2057
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2680
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.1500
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.1720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 307
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : 1.56000
REMARK 3 B33 (A**2) : -0.74000
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): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.063
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.939
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2061 ; 0.015 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1822 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2802 ; 2.006 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4242 ; 1.685 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 267 ; 6.460 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;31.362 ;21.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 307 ;11.302 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;13.572 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 270 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2350 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 437 ; 0.002 ; 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 7DZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300020516.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40798
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 12.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36500
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
REMARK 200 STARTING MODEL: 7DZT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE TRIBASIC, TRIS, NACL,
REMARK 280 PH 7.0, EVAPORATION, TEMPERATURE 298K
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 25.49400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.44350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.31350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.44350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.49400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.31350
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 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 MET A 259 CG - SD - CE ANGL. DEV. = -26.2 DEGREES
REMARK 500 GLU A 294 CA - C - O ANGL. DEV. = -15.7 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 ASN A 71 44.34 -143.41
REMARK 500 THR A 86 -12.09 74.44
REMARK 500 SER A 158 -123.12 64.54
REMARK 500 GLN A 185 66.81 -117.79
REMARK 500 HIS A 211 -88.38 -122.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 121 0.08 SIDE CHAIN
REMARK 500 ARG A 130 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7DZV A 27 292 UNP A0A1W6L588_9BURK
DBREF2 7DZV A A0A1W6L588 27 292
SEQADV 7DZV ALA A 186 UNP A0A1W6L58 GLU 186 ENGINEERED MUTATION
SEQADV 7DZV LEU A 293 UNP A0A1W6L58 EXPRESSION TAG
SEQADV 7DZV GLU A 294 UNP A0A1W6L58 EXPRESSION TAG
SEQRES 1 A 268 THR ASN PRO TYR GLN ARG GLY PRO ASP PRO THR VAL SER
SEQRES 2 A 268 SER LEU GLU ALA THR ARG GLY PRO PHE SER THR SER SER
SEQRES 3 A 268 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 A 268 VAL TYR TYR PRO THR ASN ALA GLY GLY LYS VAL GLY ALA
SEQRES 5 A 268 ILE ALA VAL VAL PRO GLY TYR THR ALA ARG GLN SER SER
SEQRES 6 A 268 ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 A 268 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 A 268 PRO SER SER ARG SER SER GLN GLN MET ALA ALA LEU ARG
SEQRES 9 A 268 GLN VAL VAL SER LEU ALA GLY THR SER SER SER PRO ILE
SEQRES 10 A 268 TYR ASN LYS VAL ASP THR ALA ARG LEU GLY VAL MET GLY
SEQRES 11 A 268 TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA LYS
SEQRES 12 A 268 ASN ASN PRO SER LEU ARG ALA ALA ALA PRO GLN ALA PRO
SEQRES 13 A 268 TRP ALA GLN ALA SER PHE SER SER VAL THR VAL PRO THR
SEQRES 14 A 268 LEU ILE VAL SER CYS GLU ASN ASP SER ILE ALA PRO ASN
SEQRES 15 A 268 SER SER HIS SER PHE PRO PHE TYR ASN GLN MET THR ARG
SEQRES 16 A 268 ASN LYS LYS ALA ASN LEU VAL ILE ASN GLY GLY SER HIS
SEQRES 17 A 268 SER CYS ALA ASN SER GLY ASN SER ASP ALA GLY LEU ILE
SEQRES 18 A 268 GLY LYS TYR GLY VAL ALA TRP MET LYS ARG PHE MET ASP
SEQRES 19 A 268 ASP ASP THR ARG TYR SER LYS PHE LEU CYS GLY ALA GLU
SEQRES 20 A 268 HIS GLN ALA ASP LEU SER LYS ARG ALA VAL GLU ALA TYR
SEQRES 21 A 268 LYS GLU ASN CYS PRO TYR LEU GLU
HET GOL A 401 6
HET GOL A 402 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 HOH *307(H2 O)
HELIX 1 AA1 THR A 37 ALA A 43 1 7
HELIX 2 AA2 ARG A 88 ASN A 93 5 6
HELIX 3 AA3 TRP A 94 PHE A 104 1 11
HELIX 4 AA4 GLN A 117 GLY A 137 1 21
HELIX 5 AA5 SER A 158 ASN A 171 1 14
HELIX 6 AA6 HIS A 211 MET A 219 1 9
HELIX 7 AA7 ASP A 243 ASP A 260 1 18
HELIX 8 AA8 ASP A 262 TYR A 265 5 4
HELIX 9 AA9 SER A 266 GLY A 271 1 6
HELIX 10 AB1 GLY A 271 LEU A 278 1 8
SHEET 1 AA1 6 THR A 50 THR A 54 0
SHEET 2 AA1 6 ALA A 63 PRO A 69 -1 O VAL A 66 N PHE A 53
SHEET 3 AA1 6 VAL A 105 ASP A 110 -1 O VAL A 106 N TYR A 67
SHEET 4 AA1 6 VAL A 76 VAL A 82 1 N VAL A 81 O ILE A 107
SHEET 5 AA1 6 VAL A 147 GLY A 156 1 O ASP A 148 N VAL A 76
SHEET 6 AA1 6 ALA A 176 ALA A 177 1 O ALA A 176 N VAL A 154
SHEET 1 AA2 3 THR A 195 CYS A 200 0
SHEET 2 AA2 3 LYS A 224 ILE A 229 1 O LEU A 227 N SER A 199
SHEET 3 AA2 3 VAL A 283 GLU A 288 -1 O ALA A 285 N VAL A 228
SSBOND 1 CYS A 200 CYS A 236 1555 1555 2.09
SSBOND 2 CYS A 270 CYS A 290 1555 1555 2.12
CISPEP 1 CYS A 290 PRO A 291 0 -1.31
CRYST1 50.988 54.627 108.887 90.00 90.00 90.00 P 21 21 21 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 0.019612 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009184 0.00000
TER 2001 GLU A 294
MASTER 298 0 2 10 9 0 0 6 2319 1 16 21
END |