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HEADER HYDROLASE 17-APR-25 9QYC
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R4M12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R4M12;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COMPOST METAGENOME;
SOURCE 3 ORGANISM_TAXID: 702656;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE, ENZYMATIC PLASTIC DEGRADATION, ENZYME ENGINEERING,
KEYWDS 2 POLYESTER HYDROLASE LEIPZIG 7, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.USEINI,N.STRATER,G.KUENZE,C.SONNENDECKER
REVDAT 1 27-MAY-26 9QYC 0
JRNL AUTH P.BLAZQUEZ-SANCHEZ,J.GUNKEL,A.USEINI,A.ZLOBIN,J.D.ZAKARY,
JRNL AUTH 2 A.SCHOLER,N.GRAEFE,F.ENGELBERGER,F.CANTANHEDE,R.FRANK,
JRNL AUTH 3 Z.ZHAO,A.ZAREI,E.BUTENSCHON,J.MATYSIK,W.ZIMMERMANN,
JRNL AUTH 4 N.STRATER,C.SONNENDECKER,G.KUNZE
JRNL TITL COMPUTATIONAL ENGINEERING OF THE POLYESTER HYDROLASE PHL7
JRNL TITL 2 FOR EFFICIENT POLY(ETHYLENE TEREPHTHALATE) DEGRADATION IN
JRNL TITL 3 BIOCATALYTIC RECYCLING PROCESSES.
JRNL REF NAT COMMUN V. 17 2026
JRNL REFN ESSN 2041-1723
JRNL PMID 42140896
JRNL DOI 10.1038/S41467-026-70868-4
REMARK 2
REMARK 2 RESOLUTION. 1.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21.2_5419)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 93155
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.121
REMARK 3 R VALUE (WORKING SET) : 0.121
REMARK 3 FREE R VALUE : 0.148
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1925
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.1500 - 2.8100 1.00 7739 145 0.1296 0.1518
REMARK 3 2 2.8100 - 2.2300 1.00 7397 148 0.1050 0.1242
REMARK 3 3 2.2300 - 1.9500 1.00 7336 134 0.0867 0.1183
REMARK 3 4 1.9500 - 1.7700 1.00 7277 156 0.0802 0.1049
REMARK 3 5 1.7700 - 1.6400 1.00 7249 157 0.0813 0.1254
REMARK 3 6 1.6400 - 1.5400 1.00 7221 175 0.0933 0.1250
REMARK 3 7 1.5400 - 1.4700 1.00 7168 174 0.1127 0.1479
REMARK 3 8 1.4700 - 1.4000 1.00 7202 151 0.1405 0.1737
REMARK 3 9 1.4000 - 1.3500 1.00 7192 151 0.1630 0.2176
REMARK 3 10 1.3500 - 1.3000 1.00 7144 163 0.1911 0.2144
REMARK 3 11 1.3000 - 1.2600 0.97 6953 128 0.2146 0.2401
REMARK 3 12 1.2600 - 1.2300 0.77 5484 122 0.2532 0.2993
REMARK 3 13 1.2300 - 1.1900 0.51 3635 80 0.2643 0.2887
REMARK 3 14 1.1900 - 1.1600 0.31 2233 41 0.2885 0.3416
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 NULL
REMARK 3 ANGLE : 1.469 NULL
REMARK 3 CHIRALITY : 0.103 326
REMARK 3 PLANARITY : 0.021 412
REMARK 3 DIHEDRAL : 12.093 814
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9QYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1292147210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93166
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.160
REMARK 200 RESOLUTION RANGE LOW (A) : 52.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 26.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
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: FOURIER SYNTHESIS
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 (%): 53.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 5.6, 20% PEG
REMARK 280 4000, 20% (V/V) ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 53.41150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.38600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.38600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.70575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.38600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.38600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.11725
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.38600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.38600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.70575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.38600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.38600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 80.11725
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.41150
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 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 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 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 THR A 64 -1.53 66.94
REMARK 500 SER A 131 -122.26 57.33
REMARK 500 HIS A 185 -101.22 -120.43
REMARK 500 HIS A 185 -101.22 -124.33
REMARK 500 PRO A 243 -176.01 -69.87
REMARK 500 THR A 256 30.84 -99.78
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 99 0.11 SIDE CHAIN
REMARK 500 ARG A 117 0.21 SIDE CHAIN
REMARK 500 ARG A 254 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9QYC A 1 262 PDB 9QYC 9QYC 1 262
SEQRES 1 A 262 MET ALA ASN PRO TYR GLN ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 262 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 262 GLN THR THR VAL SER ARG LEU ASP ALA SER GLY PHE GLY
SEQRES 4 A 262 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 262 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 262 GLY GLN SER SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 262 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE SER
SEQRES 8 A 262 ARG PHE ASP TYR PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 A 262 ALA ALA LEU ASP TYR LEU THR THR ASP SER THR VAL ARG
SEQRES 10 A 262 ASP ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 262 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 262 ASN PRO SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 262 HIS THR ARG LYS ASP TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 A 262 LEU ILE VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 262 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 262 SER LEU PRO LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 A 262 HIS THR VAL SER ASN THR PRO ASN THR THR THR ALA LYS
SEQRES 18 A 262 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP LYS ASP
SEQRES 19 A 262 THR ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 262 PRO ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE HIS
SEQRES 21 A 262 HIS HIS
HET CIT A 301 18
HETNAM CIT CITRIC ACID
FORMUL 2 CIT C6 H8 O7
FORMUL 3 HOH *389(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 GLY A 66 ALA A 71 5 6
HELIX 3 AA3 TRP A 72 SER A 79 1 8
HELIX 4 AA4 TYR A 95 ASP A 113 1 19
HELIX 5 AA5 VAL A 116 ASP A 118 5 3
HELIX 6 AA6 SER A 131 ASN A 144 1 14
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 THR A 210 THR A 214 5 5
HELIX 9 AA9 ASN A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 ARG A 236 5 3
HELIX 11 AB2 TYR A 237 CYS A 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O ILE A 43 N THR A 28
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O ILE A 85
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ASP A 121 N PHE A 54
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O ALA A 200 N ILE A 171
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O ARG A 254 N TYR A 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.06
CISPEP 1 CYS A 242 PRO A 243 0 -7.72
CISPEP 2 CYS A 257 PRO A 258 0 -1.94
CRYST1 74.772 74.772 106.823 90.00 90.00 90.00 P 41 21 2 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 0.013374 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009361 0.00000
TER 4190 HIS A 262
MASTER 266 0 1 11 9 0 0 6 2383 1 20 21
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