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HEADER HYDROLASE 13-OCT-22 8H5J
TITLE CRYSTAL STRUCTURE OF PETASE
TITLE 2 S121E/A180V/P181V/D186H/N233C/S242T/N246D/S282C MUTANT FROM IDEONELLA
TITLE 3 SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE ; IDEONELLA SAKAIENSIS; MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.LEE,H.SEO,K.-J.KIM
REVDAT 1 25-OCT-23 8H5J 0
JRNL AUTH S.H.LEE,H.SEO,K.J.KIM
JRNL TITL A CASE OF BALANCE ENGINEERING EXHIBITS KINETIC RELATIONSHIP
JRNL TITL 2 BETWEEN MESOPHILIC AND THERMOPHILIC POLY(ETHYLENE
JRNL TITL 3 TEREPHTHALATE) DEPOLYMERASES.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0350
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 84386
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) : 0.157
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4424
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5928
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 292
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3856
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 523
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.060
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.148
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4276 ; 0.011 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 3679 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5858 ; 1.745 ; 1.635
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8633 ; 0.612 ; 1.548
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 586 ; 6.660 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 34 ;15.267 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 651 ;14.868 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 633 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5168 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 884 ; 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 8H5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1300031250.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-21
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 : 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 : NULL
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 : 88810
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 28.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 1.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 30.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG3350, 0.1 M BIS-TRIS PH6.5,
REMARK 280 AND 0.2 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 69.60900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.33250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 69.60900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.33250
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 626 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 760 LIES ON A SPECIAL POSITION.
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 MET A 13
REMARK 465 GLY A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 HIS A 22
REMARK 465 SER A 23
REMARK 465 SER A 24
REMARK 465 GLY A 25
REMARK 465 LEU A 26
REMARK 465 VAL A 27
REMARK 465 PRO A 28
REMARK 465 ARG A 29
REMARK 465 GLU A 292
REMARK 465 ASP A 293
REMARK 465 PRO A 294
REMARK 465 ALA A 295
REMARK 465 ALA A 296
REMARK 465 ASN A 297
REMARK 465 LYS A 298
REMARK 465 ALA A 299
REMARK 465 ARG A 300
REMARK 465 LYS A 301
REMARK 465 GLU A 302
REMARK 465 ALA A 303
REMARK 465 GLU A 304
REMARK 465 LEU A 305
REMARK 465 ALA A 306
REMARK 465 ALA A 307
REMARK 465 ALA A 308
REMARK 465 THR A 309
REMARK 465 ALA A 310
REMARK 465 GLU A 311
REMARK 465 GLN A 312
REMARK 465 MET B 13
REMARK 465 GLY B 14
REMARK 465 SER B 15
REMARK 465 SER B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 HIS B 20
REMARK 465 HIS B 21
REMARK 465 HIS B 22
REMARK 465 SER B 23
REMARK 465 SER B 24
REMARK 465 GLY B 25
REMARK 465 LEU B 26
REMARK 465 VAL B 27
REMARK 465 PRO B 28
REMARK 465 ARG B 29
REMARK 465 GLU B 292
REMARK 465 ASP B 293
REMARK 465 PRO B 294
REMARK 465 ALA B 295
REMARK 465 ALA B 296
REMARK 465 ASN B 297
REMARK 465 LYS B 298
REMARK 465 ALA B 299
REMARK 465 ARG B 300
REMARK 465 LYS B 301
REMARK 465 GLU B 302
REMARK 465 ALA B 303
REMARK 465 GLU B 304
REMARK 465 LEU B 305
REMARK 465 ALA B 306
REMARK 465 ALA B 307
REMARK 465 ALA B 308
REMARK 465 THR B 309
REMARK 465 ALA B 310
REMARK 465 GLU B 311
REMARK 465 GLN B 312
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 693 O HOH A 747 1.55
REMARK 500 O HOH A 672 O HOH A 730 1.63
REMARK 500 O HOH B 625 O HOH B 733 1.67
REMARK 500 O3 PO4 A 403 O HOH A 501 2.17
REMARK 500 O HOH A 647 O HOH A 717 2.18
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 123 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 MET A 262 CG - SD - CE ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 MET B 262 CG - SD - CE ANGL. DEV. = -15.3 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 88 -7.70 77.15
REMARK 500 SER A 160 -118.04 62.30
REMARK 500 SER A 214 -79.55 -124.07
REMARK 500 SER A 214 -80.72 -122.32
REMARK 500 ASN B 73 66.56 -155.34
REMARK 500 THR B 88 -6.66 77.21
REMARK 500 SER B 160 -122.38 60.91
REMARK 500 SER B 214 -81.69 -125.08
REMARK 500 SER B 214 -81.43 -123.13
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 34 0.14 SIDE CHAIN
REMARK 500 ARG A 123 0.12 SIDE CHAIN
REMARK 500 ARG A 132 0.09 SIDE CHAIN
REMARK 500 ARG B 123 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 160 OG
REMARK 620 2 HOH A 588 O 115.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 160 OG
REMARK 620 2 HOH B 604 O 65.0
REMARK 620 N 1
DBREF1 8H5J A 34 290 UNP PETH_IDESA
DBREF2 8H5J A A0A0K8P6T7 34 290
DBREF1 8H5J B 34 290 UNP PETH_IDESA
DBREF2 8H5J B A0A0K8P6T7 34 290
SEQADV 8H5J MET A 13 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8H5J GLY A 14 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER A 15 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER A 16 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 17 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 18 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 19 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 20 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 21 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 22 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER A 23 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER A 24 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLY A 25 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LEU A 26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J VAL A 27 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J PRO A 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ARG A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLY A 30 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER A 31 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS A 32 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J MET A 33 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU A 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 8H5J VAL A 180 UNP A0A0K8P6T ALA 180 ENGINEERED MUTATION
SEQADV 8H5J VAL A 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 8H5J HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8H5J CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8H5J THR A 242 UNP A0A0K8P6T SER 242 ENGINEERED MUTATION
SEQADV 8H5J ASP A 246 UNP A0A0K8P6T ASN 246 ENGINEERED MUTATION
SEQADV 8H5J CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 8H5J LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ASP A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J PRO A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ASN A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LYS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 299 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ARG A 300 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LYS A 301 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU A 302 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 303 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU A 304 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LEU A 305 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 306 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 307 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 308 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J THR A 309 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA A 310 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU A 311 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLN A 312 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J MET B 13 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8H5J GLY B 14 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER B 15 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER B 16 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 17 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 18 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 19 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 20 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 21 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 22 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER B 23 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER B 24 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLY B 25 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LEU B 26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J VAL B 27 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J PRO B 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ARG B 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLY B 30 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J SER B 31 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J HIS B 32 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J MET B 33 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU B 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 8H5J VAL B 180 UNP A0A0K8P6T ALA 180 ENGINEERED MUTATION
SEQADV 8H5J VAL B 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 8H5J HIS B 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8H5J CYS B 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8H5J THR B 242 UNP A0A0K8P6T SER 242 ENGINEERED MUTATION
SEQADV 8H5J ASP B 246 UNP A0A0K8P6T ASN 246 ENGINEERED MUTATION
SEQADV 8H5J CYS B 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 8H5J LEU B 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU B 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ASP B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J PRO B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ASN B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LYS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 299 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ARG B 300 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LYS B 301 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU B 302 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 303 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU B 304 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J LEU B 305 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 306 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 307 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 308 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J THR B 309 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J ALA B 310 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLU B 311 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5J GLN B 312 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 300 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 300 LEU VAL PRO ARG GLY SER HIS MET ARG GLY PRO ASN PRO
SEQRES 3 A 300 THR ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR
SEQRES 4 A 300 VAL ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY
SEQRES 5 A 300 ALA GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR
SEQRES 6 A 300 VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG
SEQRES 7 A 300 GLN SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 8 A 300 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR
SEQRES 9 A 300 LEU ASP GLN PRO GLU SER ARG SER SER GLN GLN MET ALA
SEQRES 10 A 300 ALA LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER
SEQRES 11 A 300 SER PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY
SEQRES 12 A 300 VAL MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE
SEQRES 13 A 300 SER ALA ALA ASN ASN PRO SER LEU LYS ALA ALA VAL VAL
SEQRES 14 A 300 GLN ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL
SEQRES 15 A 300 THR VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER
SEQRES 16 A 300 ILE ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP
SEQRES 17 A 300 SER MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE CYS
SEQRES 18 A 300 GLY GLY SER HIS SER CYS ALA ASN THR GLY ASN SER ASP
SEQRES 19 A 300 GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS
SEQRES 20 A 300 ARG PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA
SEQRES 21 A 300 CYS GLU ASN PRO ASN SER THR ARG VAL CYS ASP PHE ARG
SEQRES 22 A 300 THR ALA ASN CYS SER LEU GLU ASP PRO ALA ALA ASN LYS
SEQRES 23 A 300 ALA ARG LYS GLU ALA GLU LEU ALA ALA ALA THR ALA GLU
SEQRES 24 A 300 GLN
SEQRES 1 B 300 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 300 LEU VAL PRO ARG GLY SER HIS MET ARG GLY PRO ASN PRO
SEQRES 3 B 300 THR ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR
SEQRES 4 B 300 VAL ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY
SEQRES 5 B 300 ALA GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR
SEQRES 6 B 300 VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG
SEQRES 7 B 300 GLN SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 8 B 300 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR
SEQRES 9 B 300 LEU ASP GLN PRO GLU SER ARG SER SER GLN GLN MET ALA
SEQRES 10 B 300 ALA LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER
SEQRES 11 B 300 SER PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY
SEQRES 12 B 300 VAL MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE
SEQRES 13 B 300 SER ALA ALA ASN ASN PRO SER LEU LYS ALA ALA VAL VAL
SEQRES 14 B 300 GLN ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL
SEQRES 15 B 300 THR VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER
SEQRES 16 B 300 ILE ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP
SEQRES 17 B 300 SER MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE CYS
SEQRES 18 B 300 GLY GLY SER HIS SER CYS ALA ASN THR GLY ASN SER ASP
SEQRES 19 B 300 GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS
SEQRES 20 B 300 ARG PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA
SEQRES 21 B 300 CYS GLU ASN PRO ASN SER THR ARG VAL CYS ASP PHE ARG
SEQRES 22 B 300 THR ALA ASN CYS SER LEU GLU ASP PRO ALA ALA ASN LYS
SEQRES 23 B 300 ALA ARG LYS GLU ALA GLU LEU ALA ALA ALA THR ALA GLU
SEQRES 24 B 300 GLN
HET K A 401 1
HET PO4 A 402 5
HET PO4 A 403 5
HET K B 401 1
HET PO4 B 402 5
HET GOL B 403 6
HET K B 404 1
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 K 3(K 1+)
FORMUL 4 PO4 3(O4 P 3-)
FORMUL 8 GOL C3 H8 O3
FORMUL 10 HOH *523(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASP A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
HELIX 10 AB1 THR B 39 GLU B 44 1 6
HELIX 11 AB2 ARG B 90 LYS B 95 5 6
HELIX 12 AB3 TRP B 96 SER B 103 1 8
HELIX 13 AB4 GLN B 119 GLY B 139 1 21
HELIX 14 AB5 SER B 160 ASN B 173 1 14
HELIX 15 AB6 SER B 214 SER B 221 1 8
HELIX 16 AB7 ASP B 246 ASP B 263 1 18
HELIX 17 AB8 ASP B 265 ARG B 267 5 3
HELIX 18 AB9 TYR B 268 GLU B 274 1 7
SHEET 1 AA1 9 VAL A 52 THR A 56 0
SHEET 2 AA1 9 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 9 PHE A 106 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 9 VAL A 78 VAL A 84 1 N ILE A 83 O ILE A 109
SHEET 5 AA1 9 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 9 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 7 AA1 9 THR A 198 CYS A 203 1 O PHE A 201 N VAL A 181
SHEET 8 AA1 9 LYS A 227 ILE A 232 1 O LEU A 230 N ALA A 202
SHEET 9 AA1 9 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SHEET 1 AA2 9 VAL B 52 THR B 56 0
SHEET 2 AA2 9 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA2 9 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA2 9 VAL B 78 VAL B 84 1 N ILE B 81 O ILE B 109
SHEET 5 AA2 9 VAL B 149 TRP B 159 1 O ASP B 150 N VAL B 78
SHEET 6 AA2 9 ALA B 178 GLN B 182 1 O GLN B 182 N GLY B 158
SHEET 7 AA2 9 THR B 198 CYS B 203 1 O PHE B 201 N VAL B 181
SHEET 8 AA2 9 LYS B 227 ILE B 232 1 O ILE B 232 N ALA B 202
SHEET 9 AA2 9 VAL B 281 ALA B 287 -1 O ARG B 285 N PHE B 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.07
SSBOND 2 CYS A 233 CYS A 282 1555 1555 2.00
SSBOND 3 CYS A 273 CYS A 289 1555 1555 2.17
SSBOND 4 CYS B 203 CYS B 239 1555 1555 2.12
SSBOND 5 CYS B 233 CYS B 282 1555 1555 2.05
SSBOND 6 CYS B 273 CYS B 289 1555 1555 2.32
LINK OG SER A 160 K K A 401 1555 4556 3.03
LINK K K A 401 O HOH A 588 1555 4546 3.13
LINK OG SER B 160 K K B 401 1555 1555 2.91
LINK K K B 401 O HOH B 604 1555 1555 2.82
LINK K K B 404 O HOH B 659 1555 1555 2.82
CRYST1 139.218 50.665 80.854 90.00 124.64 90.00 C 1 2 1 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 0.007183 0.000000 0.004963 0.00000
SCALE2 0.000000 0.019737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015033 0.00000
TER 2076 LEU A 291
TER 4143 LEU B 291
MASTER 433 0 7 18 18 0 0 6 4403 2 39 48
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